data_5IBL
# 
_entry.id   5IBL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5IBL         
WWPDB D_1000218582 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 5IBT unspecified 
PDB . 5IBU unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5IBL 
_pdbx_database_status.recvd_initial_deposition_date   2016-02-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Raymond, D.D.'  1 
'Harrison, S.C.' 2 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat. Med.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1546-170X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            22 
_citation.language                  ? 
_citation.page_first                1465 
_citation.page_last                 1469 
_citation.title                     'Influenza immunization elicits antibodies specific for an egg-adapted vaccine strain.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/nm.4223 
_citation.pdbx_database_id_PubMed   27820604 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Raymond, D.D.'    1  
primary 'Stewart, S.M.'    2  
primary 'Lee, J.'          3  
primary 'Ferdman, J.'      4  
primary 'Bajic, G.'        5  
primary 'Do, K.T.'         6  
primary 'Ernandes, M.J.'   7  
primary 'Suphaphiphat, P.' 8  
primary 'Settembre, E.C.'  9  
primary 'Dormitzer, P.R.'  10 
primary 'Del Giudice, G.'  11 
primary 'Finco, O.'        12 
primary 'Kang, T.H.'       13 
primary 'Ippolito, G.C.'   14 
primary 'Georgiou, G.'     15 
primary 'Kepler, T.B.'     16 
primary 'Haynes, B.F.'     17 
primary 'Moody, M.A.'      18 
primary 'Liao, H.X.'       19 
primary 'Schmidt, A.G.'    20 
primary 'Harrison, S.C.'   21 
# 
_cell.entry_id           5IBL 
_cell.length_a           54.130 
_cell.length_b           104.720 
_cell.length_c           116.660 
_cell.angle_alpha        101.95 
_cell.angle_beta         95.33 
_cell.angle_gamma        98.36 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5IBL 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
# 
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 Hemagglutinin          20133.242 2 ? ? 'UNP residues 345-520' ? 
2 polymer     man Hemagglutinin          36432.102 2 ? ? 'UNP residues 17-344'  ? 
3 polymer     man '6639 Heavy Chain'     24664.660 2 ? ? ?                      ? 
4 polymer     man '6639 Light Chain'     23335.873 2 ? ? ?                      ? 
5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   7 ? ? ?                      ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGV
;
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGV
;
A,E ? 
2 'polypeptide(L)' no no 
;ADTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTASSWSYI
VETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSDKGVTAACPHAGAKSFYKNLIWLVKKGNSYP
KLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKTFKPEIAIRPKVRDREGRMNYYWTLVEPGDK
ITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLR
NIPSIQSR
;
;ADTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTASSWSYI
VETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSDKGVTAACPHAGAKSFYKNLIWLVKKGNSYP
KLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKTFKPEIAIRPKVRDREGRMNYYWTLVEPGDK
ITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLR
NIPSIQSR
;
B,F ? 
3 'polypeptide(L)' no no 
;EVQLVQSGAEVKKPGESLTISCKGSGYSFSSYWIGWVRRMPGKGLEWMGIINPRDSDTRYSPSFQGQVTISADKSISTAY
LQWSSLKASDTAMYYCARVVADREGFGYYYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPE
PVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDK
;
;EVQLVQSGAEVKKPGESLTISCKGSGYSFSSYWIGWVRRMPGKGLEWMGIINPRDSDTRYSPSFQGQVTISADKSISTAY
LQWSSLKASDTAMYYCARVVADREGFGYYYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPE
PVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDK
;
C,H ? 
4 'polypeptide(L)' no no 
;EIVLTQSPGTLSLSPGEGATLSCRASQSVDSSSLAWYQQKPGQAPRLLIFAGSSRATGIPDRFSGKTSGTDFTLTISRLE
PEDFAVYYCQQCGNSPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;EIVLTQSPGTLSLSPGEGATLSCRASQSVDSSSLAWYQQKPGQAPRLLIFAGSSRATGIPDRFSGKTSGTDFTLTISRLE
PEDFAVYYCQQCGNSPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
D,L ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   LEU n 
1 3   PHE n 
1 4   GLY n 
1 5   ALA n 
1 6   ILE n 
1 7   ALA n 
1 8   GLY n 
1 9   PHE n 
1 10  ILE n 
1 11  GLU n 
1 12  GLY n 
1 13  GLY n 
1 14  TRP n 
1 15  THR n 
1 16  GLY n 
1 17  MET n 
1 18  VAL n 
1 19  ASP n 
1 20  GLY n 
1 21  TRP n 
1 22  TYR n 
1 23  GLY n 
1 24  TYR n 
1 25  HIS n 
1 26  HIS n 
1 27  GLN n 
1 28  ASN n 
1 29  GLU n 
1 30  GLN n 
1 31  GLY n 
1 32  SER n 
1 33  GLY n 
1 34  TYR n 
1 35  ALA n 
1 36  ALA n 
1 37  ASP n 
1 38  LEU n 
1 39  LYS n 
1 40  SER n 
1 41  THR n 
1 42  GLN n 
1 43  ASN n 
1 44  ALA n 
1 45  ILE n 
1 46  ASP n 
1 47  GLU n 
1 48  ILE n 
1 49  THR n 
1 50  ASN n 
1 51  LYS n 
1 52  VAL n 
1 53  ASN n 
1 54  SER n 
1 55  VAL n 
1 56  ILE n 
1 57  GLU n 
1 58  LYS n 
1 59  MET n 
1 60  ASN n 
1 61  THR n 
1 62  GLN n 
1 63  PHE n 
1 64  THR n 
1 65  ALA n 
1 66  VAL n 
1 67  GLY n 
1 68  LYS n 
1 69  GLU n 
1 70  PHE n 
1 71  ASN n 
1 72  HIS n 
1 73  LEU n 
1 74  GLU n 
1 75  LYS n 
1 76  ARG n 
1 77  ILE n 
1 78  GLU n 
1 79  ASN n 
1 80  LEU n 
1 81  ASN n 
1 82  LYS n 
1 83  LYS n 
1 84  VAL n 
1 85  ASP n 
1 86  ASP n 
1 87  GLY n 
1 88  PHE n 
1 89  LEU n 
1 90  ASP n 
1 91  ILE n 
1 92  TRP n 
1 93  THR n 
1 94  TYR n 
1 95  ASN n 
1 96  ALA n 
1 97  GLU n 
1 98  LEU n 
1 99  LEU n 
1 100 VAL n 
1 101 LEU n 
1 102 LEU n 
1 103 GLU n 
1 104 ASN n 
1 105 GLU n 
1 106 ARG n 
1 107 THR n 
1 108 LEU n 
1 109 ASP n 
1 110 TYR n 
1 111 HIS n 
1 112 ASP n 
1 113 SER n 
1 114 ASN n 
1 115 VAL n 
1 116 LYS n 
1 117 ASN n 
1 118 LEU n 
1 119 TYR n 
1 120 GLU n 
1 121 LYS n 
1 122 VAL n 
1 123 ARG n 
1 124 SER n 
1 125 GLN n 
1 126 LEU n 
1 127 LYS n 
1 128 ASN n 
1 129 ASN n 
1 130 ALA n 
1 131 LYS n 
1 132 GLU n 
1 133 ILE n 
1 134 GLY n 
1 135 ASN n 
1 136 GLY n 
1 137 CYS n 
1 138 PHE n 
1 139 GLU n 
1 140 PHE n 
1 141 TYR n 
1 142 HIS n 
1 143 LYS n 
1 144 CYS n 
1 145 ASP n 
1 146 ASN n 
1 147 THR n 
1 148 CYS n 
1 149 MET n 
1 150 GLU n 
1 151 SER n 
1 152 VAL n 
1 153 LYS n 
1 154 ASN n 
1 155 GLY n 
1 156 THR n 
1 157 TYR n 
1 158 ASP n 
1 159 TYR n 
1 160 PRO n 
1 161 LYS n 
1 162 TYR n 
1 163 SER n 
1 164 GLU n 
1 165 GLU n 
1 166 ALA n 
1 167 LYS n 
1 168 LEU n 
1 169 ASN n 
1 170 ARG n 
1 171 GLU n 
1 172 GLU n 
1 173 ILE n 
1 174 ASP n 
1 175 GLY n 
1 176 VAL n 
2 1   ALA n 
2 2   ASP n 
2 3   THR n 
2 4   LEU n 
2 5   CYS n 
2 6   ILE n 
2 7   GLY n 
2 8   TYR n 
2 9   HIS n 
2 10  ALA n 
2 11  ASN n 
2 12  ASN n 
2 13  SER n 
2 14  THR n 
2 15  ASP n 
2 16  THR n 
2 17  VAL n 
2 18  ASP n 
2 19  THR n 
2 20  VAL n 
2 21  LEU n 
2 22  GLU n 
2 23  LYS n 
2 24  ASN n 
2 25  VAL n 
2 26  THR n 
2 27  VAL n 
2 28  THR n 
2 29  HIS n 
2 30  SER n 
2 31  VAL n 
2 32  ASN n 
2 33  LEU n 
2 34  LEU n 
2 35  GLU n 
2 36  ASP n 
2 37  LYS n 
2 38  HIS n 
2 39  ASN n 
2 40  GLY n 
2 41  LYS n 
2 42  LEU n 
2 43  CYS n 
2 44  LYS n 
2 45  LEU n 
2 46  ARG n 
2 47  GLY n 
2 48  VAL n 
2 49  ALA n 
2 50  PRO n 
2 51  LEU n 
2 52  HIS n 
2 53  LEU n 
2 54  GLY n 
2 55  LYS n 
2 56  CYS n 
2 57  ASN n 
2 58  ILE n 
2 59  ALA n 
2 60  GLY n 
2 61  TRP n 
2 62  ILE n 
2 63  LEU n 
2 64  GLY n 
2 65  ASN n 
2 66  PRO n 
2 67  GLU n 
2 68  CYS n 
2 69  GLU n 
2 70  SER n 
2 71  LEU n 
2 72  SER n 
2 73  THR n 
2 74  ALA n 
2 75  SER n 
2 76  SER n 
2 77  TRP n 
2 78  SER n 
2 79  TYR n 
2 80  ILE n 
2 81  VAL n 
2 82  GLU n 
2 83  THR n 
2 84  PRO n 
2 85  SER n 
2 86  SER n 
2 87  ASP n 
2 88  ASN n 
2 89  GLY n 
2 90  THR n 
2 91  CYS n 
2 92  TYR n 
2 93  PRO n 
2 94  GLY n 
2 95  ASP n 
2 96  PHE n 
2 97  ILE n 
2 98  ASP n 
2 99  TYR n 
2 100 GLU n 
2 101 GLU n 
2 102 LEU n 
2 103 ARG n 
2 104 GLU n 
2 105 GLN n 
2 106 LEU n 
2 107 SER n 
2 108 SER n 
2 109 VAL n 
2 110 SER n 
2 111 SER n 
2 112 PHE n 
2 113 GLU n 
2 114 ARG n 
2 115 PHE n 
2 116 GLU n 
2 117 ILE n 
2 118 PHE n 
2 119 PRO n 
2 120 LYS n 
2 121 THR n 
2 122 SER n 
2 123 SER n 
2 124 TRP n 
2 125 PRO n 
2 126 ASN n 
2 127 HIS n 
2 128 ASP n 
2 129 SER n 
2 130 ASP n 
2 131 LYS n 
2 132 GLY n 
2 133 VAL n 
2 134 THR n 
2 135 ALA n 
2 136 ALA n 
2 137 CYS n 
2 138 PRO n 
2 139 HIS n 
2 140 ALA n 
2 141 GLY n 
2 142 ALA n 
2 143 LYS n 
2 144 SER n 
2 145 PHE n 
2 146 TYR n 
2 147 LYS n 
2 148 ASN n 
2 149 LEU n 
2 150 ILE n 
2 151 TRP n 
2 152 LEU n 
2 153 VAL n 
2 154 LYS n 
2 155 LYS n 
2 156 GLY n 
2 157 ASN n 
2 158 SER n 
2 159 TYR n 
2 160 PRO n 
2 161 LYS n 
2 162 LEU n 
2 163 SER n 
2 164 LYS n 
2 165 SER n 
2 166 TYR n 
2 167 ILE n 
2 168 ASN n 
2 169 ASP n 
2 170 LYS n 
2 171 GLY n 
2 172 LYS n 
2 173 GLU n 
2 174 VAL n 
2 175 LEU n 
2 176 VAL n 
2 177 LEU n 
2 178 TRP n 
2 179 GLY n 
2 180 ILE n 
2 181 HIS n 
2 182 HIS n 
2 183 PRO n 
2 184 SER n 
2 185 THR n 
2 186 SER n 
2 187 ALA n 
2 188 ASP n 
2 189 GLN n 
2 190 GLN n 
2 191 SER n 
2 192 LEU n 
2 193 TYR n 
2 194 GLN n 
2 195 ASN n 
2 196 ALA n 
2 197 ASP n 
2 198 ALA n 
2 199 TYR n 
2 200 VAL n 
2 201 PHE n 
2 202 VAL n 
2 203 GLY n 
2 204 SER n 
2 205 SER n 
2 206 ARG n 
2 207 TYR n 
2 208 SER n 
2 209 LYS n 
2 210 THR n 
2 211 PHE n 
2 212 LYS n 
2 213 PRO n 
2 214 GLU n 
2 215 ILE n 
2 216 ALA n 
2 217 ILE n 
2 218 ARG n 
2 219 PRO n 
2 220 LYS n 
2 221 VAL n 
2 222 ARG n 
2 223 ASP n 
2 224 ARG n 
2 225 GLU n 
2 226 GLY n 
2 227 ARG n 
2 228 MET n 
2 229 ASN n 
2 230 TYR n 
2 231 TYR n 
2 232 TRP n 
2 233 THR n 
2 234 LEU n 
2 235 VAL n 
2 236 GLU n 
2 237 PRO n 
2 238 GLY n 
2 239 ASP n 
2 240 LYS n 
2 241 ILE n 
2 242 THR n 
2 243 PHE n 
2 244 GLU n 
2 245 ALA n 
2 246 THR n 
2 247 GLY n 
2 248 ASN n 
2 249 LEU n 
2 250 VAL n 
2 251 VAL n 
2 252 PRO n 
2 253 ARG n 
2 254 TYR n 
2 255 ALA n 
2 256 PHE n 
2 257 ALA n 
2 258 MET n 
2 259 GLU n 
2 260 ARG n 
2 261 ASN n 
2 262 ALA n 
2 263 GLY n 
2 264 SER n 
2 265 GLY n 
2 266 ILE n 
2 267 ILE n 
2 268 ILE n 
2 269 SER n 
2 270 ASP n 
2 271 THR n 
2 272 PRO n 
2 273 VAL n 
2 274 HIS n 
2 275 ASP n 
2 276 CYS n 
2 277 ASN n 
2 278 THR n 
2 279 THR n 
2 280 CYS n 
2 281 GLN n 
2 282 THR n 
2 283 PRO n 
2 284 LYS n 
2 285 GLY n 
2 286 ALA n 
2 287 ILE n 
2 288 ASN n 
2 289 THR n 
2 290 SER n 
2 291 LEU n 
2 292 PRO n 
2 293 PHE n 
2 294 GLN n 
2 295 ASN n 
2 296 ILE n 
2 297 HIS n 
2 298 PRO n 
2 299 ILE n 
2 300 THR n 
2 301 ILE n 
2 302 GLY n 
2 303 LYS n 
2 304 CYS n 
2 305 PRO n 
2 306 LYS n 
2 307 TYR n 
2 308 VAL n 
2 309 LYS n 
2 310 SER n 
2 311 THR n 
2 312 LYS n 
2 313 LEU n 
2 314 ARG n 
2 315 LEU n 
2 316 ALA n 
2 317 THR n 
2 318 GLY n 
2 319 LEU n 
2 320 ARG n 
2 321 ASN n 
2 322 ILE n 
2 323 PRO n 
2 324 SER n 
2 325 ILE n 
2 326 GLN n 
2 327 SER n 
2 328 ARG n 
3 1   GLU n 
3 2   VAL n 
3 3   GLN n 
3 4   LEU n 
3 5   VAL n 
3 6   GLN n 
3 7   SER n 
3 8   GLY n 
3 9   ALA n 
3 10  GLU n 
3 11  VAL n 
3 12  LYS n 
3 13  LYS n 
3 14  PRO n 
3 15  GLY n 
3 16  GLU n 
3 17  SER n 
3 18  LEU n 
3 19  THR n 
3 20  ILE n 
3 21  SER n 
3 22  CYS n 
3 23  LYS n 
3 24  GLY n 
3 25  SER n 
3 26  GLY n 
3 27  TYR n 
3 28  SER n 
3 29  PHE n 
3 30  SER n 
3 31  SER n 
3 32  TYR n 
3 33  TRP n 
3 34  ILE n 
3 35  GLY n 
3 36  TRP n 
3 37  VAL n 
3 38  ARG n 
3 39  ARG n 
3 40  MET n 
3 41  PRO n 
3 42  GLY n 
3 43  LYS n 
3 44  GLY n 
3 45  LEU n 
3 46  GLU n 
3 47  TRP n 
3 48  MET n 
3 49  GLY n 
3 50  ILE n 
3 51  ILE n 
3 52  ASN n 
3 53  PRO n 
3 54  ARG n 
3 55  ASP n 
3 56  SER n 
3 57  ASP n 
3 58  THR n 
3 59  ARG n 
3 60  TYR n 
3 61  SER n 
3 62  PRO n 
3 63  SER n 
3 64  PHE n 
3 65  GLN n 
3 66  GLY n 
3 67  GLN n 
3 68  VAL n 
3 69  THR n 
3 70  ILE n 
3 71  SER n 
3 72  ALA n 
3 73  ASP n 
3 74  LYS n 
3 75  SER n 
3 76  ILE n 
3 77  SER n 
3 78  THR n 
3 79  ALA n 
3 80  TYR n 
3 81  LEU n 
3 82  GLN n 
3 83  TRP n 
3 84  SER n 
3 85  SER n 
3 86  LEU n 
3 87  LYS n 
3 88  ALA n 
3 89  SER n 
3 90  ASP n 
3 91  THR n 
3 92  ALA n 
3 93  MET n 
3 94  TYR n 
3 95  TYR n 
3 96  CYS n 
3 97  ALA n 
3 98  ARG n 
3 99  VAL n 
3 100 VAL n 
3 101 ALA n 
3 102 ASP n 
3 103 ARG n 
3 104 GLU n 
3 105 GLY n 
3 106 PHE n 
3 107 GLY n 
3 108 TYR n 
3 109 TYR n 
3 110 TYR n 
3 111 GLY n 
3 112 MET n 
3 113 ASP n 
3 114 VAL n 
3 115 TRP n 
3 116 GLY n 
3 117 GLN n 
3 118 GLY n 
3 119 THR n 
3 120 THR n 
3 121 VAL n 
3 122 THR n 
3 123 VAL n 
3 124 SER n 
3 125 SER n 
3 126 ALA n 
3 127 SER n 
3 128 THR n 
3 129 LYS n 
3 130 GLY n 
3 131 PRO n 
3 132 SER n 
3 133 VAL n 
3 134 PHE n 
3 135 PRO n 
3 136 LEU n 
3 137 ALA n 
3 138 PRO n 
3 139 SER n 
3 140 SER n 
3 141 LYS n 
3 142 SER n 
3 143 THR n 
3 144 SER n 
3 145 GLY n 
3 146 GLY n 
3 147 THR n 
3 148 ALA n 
3 149 ALA n 
3 150 LEU n 
3 151 GLY n 
3 152 CYS n 
3 153 LEU n 
3 154 VAL n 
3 155 LYS n 
3 156 ASP n 
3 157 TYR n 
3 158 PHE n 
3 159 PRO n 
3 160 GLU n 
3 161 PRO n 
3 162 VAL n 
3 163 THR n 
3 164 VAL n 
3 165 SER n 
3 166 TRP n 
3 167 ASN n 
3 168 SER n 
3 169 GLY n 
3 170 ALA n 
3 171 LEU n 
3 172 THR n 
3 173 SER n 
3 174 GLY n 
3 175 VAL n 
3 176 HIS n 
3 177 THR n 
3 178 PHE n 
3 179 PRO n 
3 180 ALA n 
3 181 VAL n 
3 182 LEU n 
3 183 GLN n 
3 184 SER n 
3 185 SER n 
3 186 GLY n 
3 187 LEU n 
3 188 TYR n 
3 189 SER n 
3 190 LEU n 
3 191 SER n 
3 192 SER n 
3 193 VAL n 
3 194 VAL n 
3 195 THR n 
3 196 VAL n 
3 197 PRO n 
3 198 SER n 
3 199 SER n 
3 200 SER n 
3 201 LEU n 
3 202 GLY n 
3 203 THR n 
3 204 GLN n 
3 205 THR n 
3 206 TYR n 
3 207 ILE n 
3 208 CYS n 
3 209 ASN n 
3 210 VAL n 
3 211 ASN n 
3 212 HIS n 
3 213 LYS n 
3 214 PRO n 
3 215 SER n 
3 216 ASN n 
3 217 THR n 
3 218 LYS n 
3 219 VAL n 
3 220 ASP n 
3 221 LYS n 
3 222 ARG n 
3 223 VAL n 
3 224 GLU n 
3 225 PRO n 
3 226 LYS n 
3 227 SER n 
3 228 CYS n 
3 229 ASP n 
3 230 LYS n 
4 1   GLU n 
4 2   ILE n 
4 3   VAL n 
4 4   LEU n 
4 5   THR n 
4 6   GLN n 
4 7   SER n 
4 8   PRO n 
4 9   GLY n 
4 10  THR n 
4 11  LEU n 
4 12  SER n 
4 13  LEU n 
4 14  SER n 
4 15  PRO n 
4 16  GLY n 
4 17  GLU n 
4 18  GLY n 
4 19  ALA n 
4 20  THR n 
4 21  LEU n 
4 22  SER n 
4 23  CYS n 
4 24  ARG n 
4 25  ALA n 
4 26  SER n 
4 27  GLN n 
4 28  SER n 
4 29  VAL n 
4 30  ASP n 
4 31  SER n 
4 32  SER n 
4 33  SER n 
4 34  LEU n 
4 35  ALA n 
4 36  TRP n 
4 37  TYR n 
4 38  GLN n 
4 39  GLN n 
4 40  LYS n 
4 41  PRO n 
4 42  GLY n 
4 43  GLN n 
4 44  ALA n 
4 45  PRO n 
4 46  ARG n 
4 47  LEU n 
4 48  LEU n 
4 49  ILE n 
4 50  PHE n 
4 51  ALA n 
4 52  GLY n 
4 53  SER n 
4 54  SER n 
4 55  ARG n 
4 56  ALA n 
4 57  THR n 
4 58  GLY n 
4 59  ILE n 
4 60  PRO n 
4 61  ASP n 
4 62  ARG n 
4 63  PHE n 
4 64  SER n 
4 65  GLY n 
4 66  LYS n 
4 67  THR n 
4 68  SER n 
4 69  GLY n 
4 70  THR n 
4 71  ASP n 
4 72  PHE n 
4 73  THR n 
4 74  LEU n 
4 75  THR n 
4 76  ILE n 
4 77  SER n 
4 78  ARG n 
4 79  LEU n 
4 80  GLU n 
4 81  PRO n 
4 82  GLU n 
4 83  ASP n 
4 84  PHE n 
4 85  ALA n 
4 86  VAL n 
4 87  TYR n 
4 88  TYR n 
4 89  CYS n 
4 90  GLN n 
4 91  GLN n 
4 92  CYS n 
4 93  GLY n 
4 94  ASN n 
4 95  SER n 
4 96  PRO n 
4 97  TRP n 
4 98  THR n 
4 99  PHE n 
4 100 GLY n 
4 101 GLN n 
4 102 GLY n 
4 103 THR n 
4 104 LYS n 
4 105 VAL n 
4 106 GLU n 
4 107 ILE n 
4 108 LYS n 
4 109 ARG n 
4 110 THR n 
4 111 VAL n 
4 112 ALA n 
4 113 ALA n 
4 114 PRO n 
4 115 SER n 
4 116 VAL n 
4 117 PHE n 
4 118 ILE n 
4 119 PHE n 
4 120 PRO n 
4 121 PRO n 
4 122 SER n 
4 123 ASP n 
4 124 GLU n 
4 125 GLN n 
4 126 LEU n 
4 127 LYS n 
4 128 SER n 
4 129 GLY n 
4 130 THR n 
4 131 ALA n 
4 132 SER n 
4 133 VAL n 
4 134 VAL n 
4 135 CYS n 
4 136 LEU n 
4 137 LEU n 
4 138 ASN n 
4 139 ASN n 
4 140 PHE n 
4 141 TYR n 
4 142 PRO n 
4 143 ARG n 
4 144 GLU n 
4 145 ALA n 
4 146 LYS n 
4 147 VAL n 
4 148 GLN n 
4 149 TRP n 
4 150 LYS n 
4 151 VAL n 
4 152 ASP n 
4 153 ASN n 
4 154 ALA n 
4 155 LEU n 
4 156 GLN n 
4 157 SER n 
4 158 GLY n 
4 159 ASN n 
4 160 SER n 
4 161 GLN n 
4 162 GLU n 
4 163 SER n 
4 164 VAL n 
4 165 THR n 
4 166 GLU n 
4 167 GLN n 
4 168 ASP n 
4 169 SER n 
4 170 LYS n 
4 171 ASP n 
4 172 SER n 
4 173 THR n 
4 174 TYR n 
4 175 SER n 
4 176 LEU n 
4 177 SER n 
4 178 SER n 
4 179 THR n 
4 180 LEU n 
4 181 THR n 
4 182 LEU n 
4 183 SER n 
4 184 LYS n 
4 185 ALA n 
4 186 ASP n 
4 187 TYR n 
4 188 GLU n 
4 189 LYS n 
4 190 HIS n 
4 191 LYS n 
4 192 VAL n 
4 193 TYR n 
4 194 ALA n 
4 195 CYS n 
4 196 GLU n 
4 197 VAL n 
4 198 THR n 
4 199 HIS n 
4 200 GLN n 
4 201 GLY n 
4 202 LEU n 
4 203 SER n 
4 204 SER n 
4 205 PRO n 
4 206 VAL n 
4 207 THR n 
4 208 LYS n 
4 209 SER n 
4 210 PHE n 
4 211 ASN n 
4 212 ARG n 
4 213 GLY n 
4 214 GLU n 
4 215 CYS 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' 1 176 ?     ? HA ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'cabbage looper' 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 328 ?     ? HA ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'cabbage looper' 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 230 Human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? Human            
'Homo sapiens'    9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 215 Human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? Human            
'Homo sapiens'    9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
# 
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 C9EL84_9INFA C9EL84 ? 1 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGV
;
345 
2 UNP C9EL84_9INFA C9EL84 ? 2 
;ADTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTASSWSYI
VETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSDKGVTAACPHAGAKSFYKNLIWLVKKGNSYP
KLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKTFKPEIAIRPKVRDREGRMNYYWTLVEPGDK
ITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLR
NIPSIQSR
;
17  
3 PDB 5IBL         5IBL   ? 3 ? 1   
4 PDB 5IBL         5IBL   ? 4 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5IBL A 1 ? 176 ? C9EL84 345 ? 520 ? 1  176 
2 2 5IBL B 1 ? 328 ? C9EL84 17  ? 344 ? 10 329 
3 3 5IBL C 1 ? 230 ? 5IBL   1   ? 230 ? 1  230 
4 4 5IBL D 1 ? 215 ? 5IBL   1   ? 215 ? 1  215 
5 1 5IBL E 1 ? 176 ? C9EL84 345 ? 520 ? 1  176 
6 2 5IBL F 1 ? 328 ? C9EL84 17  ? 344 ? 10 329 
7 3 5IBL H 1 ? 230 ? 5IBL   1   ? 230 ? 1  230 
8 4 5IBL L 1 ? 215 ? 5IBL   1   ? 215 ? 1  215 
# 
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 
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_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                   5IBL 
_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            3.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         59.48 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '12% (w/v) PEG 8000, 10% (w/v) MPD and 25 mM KH2PO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           173.15 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-08-15 
# 
_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   0.979200 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate            125.71 
_reflns.entry_id                         5IBL 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.39 
_reflns.d_resolution_low                 44.81 
_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                       32602 
_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             95.5 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  1.9 
_reflns.pdbx_Rmerge_I_obs                0.178 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            4.3 
_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                  ? 
_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                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.39 
_reflns_shell.d_res_low                   3.59 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         0.48 
_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_all        94 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                1.73 
_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             1.8 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5IBL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     32597 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             44.81 
_refine.ls_d_res_high                            3.39 
_refine.ls_percent_reflns_obs                    95.4 
_refine.ls_R_factor_obs                          0.216 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.214 
_refine.ls_R_factor_R_free                       0.257 
_refine.ls_R_factor_R_free_error                 0.000 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_number_reflns_R_free                  1635 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.902 
_refine.correlation_coeff_Fo_to_Fc_free          0.867 
_refine.B_iso_mean                               140.46 
_refine.aniso_B[1][1]                            -3.09700 
_refine.aniso_B[2][2]                            -6.67890 
_refine.aniso_B[3][3]                            9.77600 
_refine.aniso_B[1][2]                            -14.12280 
_refine.aniso_B[1][3]                            -2.96140 
_refine.aniso_B[2][3]                            -10.45600 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      5IBU 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.533 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        5IBL 
_refine_analyze.Luzzati_coordinate_error_obs    0.56 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         98 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               13174 
_refine_hist.d_res_high                       3.39 
_refine_hist.d_res_low                        44.81 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.008 ? 2.00  13499 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  18342 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  4582  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? 2.00  317   'X-RAY DIFFRACTION' HARMONIC     
t_gen_planes              ?     ? 5.00  1940  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 20.00 13499 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_omega_torsion           2.04  ? ?     ?     'X-RAY DIFFRACTION' ?            
t_other_torsion           21.22 ? ?     ?     'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  1800  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  14864 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.d_res_high                       3.39 
_refine_ls_shell.d_res_low                        3.50 
_refine_ls_shell.number_reflns_R_work             2779 
_refine_ls_shell.R_factor_R_work                  0.220 
_refine_ls_shell.percent_reflns_obs               90.42 
_refine_ls_shell.R_factor_R_free                  0.247 
_refine_ls_shell.R_factor_R_free_error            0.000 
_refine_ls_shell.percent_reflns_R_free            4.99 
_refine_ls_shell.number_reflns_R_free             146 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                2925 
# 
_struct.entry_id                     5IBL 
_struct.title                        'Human antibody 6639 in complex with influenza hemagglutinin H1 X-181' 
_struct.pdbx_descriptor              'Hemagglutinin, 6639 Heavy Chain, 6639 Light Chain' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5IBL 
_struct_keywords.text            'Hemagglutinin, complex, antibody, vaccine, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 1 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 37  ? VAL A 66  ? ASP A 37  VAL A 66  1 ? 30 
HELX_P HELX_P2  AA2 VAL A 84  ? LEU A 126 ? VAL A 84  LEU A 126 1 ? 43 
HELX_P HELX_P3  AA3 MET A 149 ? ASN A 154 ? MET A 149 ASN A 154 1 ? 6  
HELX_P HELX_P4  AA4 TYR A 162 ? ASP A 174 ? TYR A 162 ASP A 174 1 ? 13 
HELX_P HELX_P5  AA5 ASN B 57  ? GLY B 64  ? ASN B 65  GLY B 72  1 ? 8  
HELX_P HELX_P6  AA6 ASP B 98  ? SER B 108 ? ASP B 104 SER B 114 1 ? 11 
HELX_P HELX_P7  AA7 THR B 185 ? TYR B 193 ? THR B 187 TYR B 195 1 ? 9  
HELX_P HELX_P8  AA8 LYS B 220 ? ARG B 224 ? LYS B 222 ARG B 226 5 ? 5  
HELX_P HELX_P9  AA9 LYS C 87  ? THR C 91  ? LYS C 87  THR C 91  5 ? 5  
HELX_P HELX_P10 AB1 SER C 200 ? GLN C 204 ? SER C 200 GLN C 204 5 ? 5  
HELX_P HELX_P11 AB2 ASP D 30  ? SER D 32  ? ASP D 30  SER D 32  5 ? 3  
HELX_P HELX_P12 AB3 GLU D 80  ? PHE D 84  ? GLU D 80  PHE D 84  5 ? 5  
HELX_P HELX_P13 AB4 SER D 122 ? LYS D 127 ? SER D 122 LYS D 127 1 ? 6  
HELX_P HELX_P14 AB5 LYS D 184 ? GLU D 188 ? LYS D 184 GLU D 188 1 ? 5  
HELX_P HELX_P15 AB6 ASP E 37  ? GLY E 67  ? ASP E 37  GLY E 67  1 ? 31 
HELX_P HELX_P16 AB7 VAL E 84  ? LEU E 126 ? VAL E 84  LEU E 126 1 ? 43 
HELX_P HELX_P17 AB8 MET E 149 ? ASN E 154 ? MET E 149 ASN E 154 1 ? 6  
HELX_P HELX_P18 AB9 TYR E 162 ? ASP E 174 ? TYR E 162 ASP E 174 1 ? 13 
HELX_P HELX_P19 AC1 ASN F 57  ? GLY F 64  ? ASN F 65  GLY F 72  1 ? 8  
HELX_P HELX_P20 AC2 ASP F 98  ? LEU F 106 ? ASP F 104 LEU F 112 1 ? 9  
HELX_P HELX_P21 AC3 THR F 185 ? TYR F 193 ? THR F 187 TYR F 195 1 ? 9  
HELX_P HELX_P22 AC4 LYS F 220 ? ARG F 224 ? LYS F 222 ARG F 226 5 ? 5  
HELX_P HELX_P23 AC5 LYS G 87  ? THR G 91  ? LYS H 87  THR H 91  5 ? 5  
HELX_P HELX_P24 AC6 PRO G 197 ? LEU G 201 ? PRO H 197 LEU H 201 5 ? 5  
HELX_P HELX_P25 AC7 ASP H 30  ? SER H 32  ? ASP L 30  SER L 32  5 ? 3  
HELX_P HELX_P26 AC8 GLU H 80  ? PHE H 84  ? GLU L 80  PHE L 84  5 ? 5  
HELX_P HELX_P27 AC9 SER H 122 ? LYS H 127 ? SER L 122 LYS L 127 1 ? 6  
HELX_P HELX_P28 AD1 LYS H 184 ? GLU H 188 ? LYS L 184 GLU L 188 1 ? 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 
disulf1  disulf ?   ? B CYS 43  SG  ? ? ? 1_555 B CYS 276 SG ? ? B CYS 52  B CYS 277 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf2  disulf ?   ? B CYS 56  SG  ? ? ? 1_555 B CYS 68  SG ? ? B CYS 64  B CYS 76  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf3  disulf ?   ? B CYS 91  SG  ? ? ? 1_555 B CYS 137 SG ? ? B CYS 97  B CYS 139 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf4  disulf ?   ? B CYS 280 SG  ? ? ? 1_555 B CYS 304 SG ? ? B CYS 281 B CYS 305 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf5  disulf ?   ? C CYS 22  SG  ? ? ? 1_555 C CYS 96  SG ? ? C CYS 22  C CYS 96  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf6  disulf ?   ? C CYS 152 SG  ? ? ? 1_555 C CYS 208 SG ? ? C CYS 152 C CYS 208 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf7  disulf ?   ? D CYS 23  SG  ? ? ? 1_555 D CYS 89  SG ? ? D CYS 23  D CYS 89  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf8  disulf ?   ? D CYS 135 SG  ? ? ? 1_555 D CYS 195 SG ? ? D CYS 135 D CYS 195 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf9  disulf ?   ? F CYS 43  SG  ? ? ? 1_555 F CYS 276 SG ? ? F CYS 52  F CYS 277 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf10 disulf ?   ? F CYS 56  SG  ? ? ? 1_555 F CYS 68  SG ? ? F CYS 64  F CYS 76  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf11 disulf ?   ? F CYS 91  SG  ? ? ? 1_555 F CYS 137 SG ? ? F CYS 97  F CYS 139 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf12 disulf ?   ? F CYS 280 SG  ? ? ? 1_555 F CYS 304 SG ? ? F CYS 281 F CYS 305 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf13 disulf ?   ? G CYS 22  SG  ? ? ? 1_555 G CYS 96  SG ? ? H CYS 22  H CYS 96  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf14 disulf ?   ? G CYS 152 SG  ? ? ? 1_555 G CYS 208 SG ? ? H CYS 152 H CYS 208 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf15 disulf ?   ? H CYS 23  SG  ? ? ? 1_555 H CYS 89  SG ? ? L CYS 23  L CYS 89  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf16 disulf ?   ? H CYS 135 SG  ? ? ? 1_555 H CYS 195 SG ? ? L CYS 135 L CYS 195 1_555 ? ? ? ? ? ? ? 2.039 ? 
covale1  covale one ? B ASN 11  ND2 ? ? ? 1_555 J NAG .   C1 ? ? B ASN 20  B NAG 402 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale2  covale one ? B ASN 277 ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 278 B NAG 401 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale3  covale one ? F ASN 11  ND2 ? ? ? 1_555 N NAG .   C1 ? ? F ASN 20  F NAG 404 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale4  covale one ? F ASN 24  ND2 ? ? ? 1_555 O NAG .   C1 ? ? F ASN 33  F NAG 405 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale5  covale one ? F ASN 88  ND2 ? ? ? 1_555 M NAG .   C1 ? ? F ASN 94  F NAG 403 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale6  covale one ? F ASN 277 ND2 ? ? ? 1_555 L NAG .   C1 ? ? F ASN 278 F NAG 402 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale7  covale one ? F ASN 288 ND2 ? ? ? 1_555 K NAG .   C1 ? ? F ASN 289 F NAG 401 1_555 ? ? ? ? ? ? ? 1.433 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 PHE 158 C . ? PHE 158 C PRO 159 C ? PRO 159 C 1 -0.21 
2 GLU 160 C . ? GLU 160 C PRO 161 C ? PRO 161 C 1 5.49  
3 SER 7   D . ? SER 7   D PRO 8   D ? PRO 8   D 1 1.18  
4 SER 95  D . ? SER 95  D PRO 96  D ? PRO 96  D 1 1.75  
5 TYR 141 D . ? TYR 141 D PRO 142 D ? PRO 142 D 1 -0.20 
6 PHE 158 G . ? PHE 158 H PRO 159 G ? PRO 159 H 1 4.49  
7 SER 7   H . ? SER 7   L PRO 8   H ? PRO 8   L 1 2.00  
8 SER 95  H . ? SER 95  L PRO 96  H ? PRO 96  L 1 5.32  
9 TYR 141 H . ? TYR 141 L PRO 142 H ? PRO 142 L 1 0.26  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
AB1 ? 3 ? 
AB2 ? 4 ? 
AB3 ? 6 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 3 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 2 ? 
AC5 ? 2 ? 
AC6 ? 3 ? 
AC7 ? 2 ? 
AC8 ? 3 ? 
AC9 ? 5 ? 
AD1 ? 5 ? 
AD2 ? 2 ? 
AD3 ? 2 ? 
AD4 ? 4 ? 
AD5 ? 3 ? 
AD6 ? 4 ? 
AD7 ? 6 ? 
AD8 ? 4 ? 
AD9 ? 4 ? 
AE1 ? 4 ? 
AE2 ? 3 ? 
AE3 ? 4 ? 
AE4 ? 6 ? 
AE5 ? 4 ? 
AE6 ? 4 ? 
AE7 ? 4 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB3 5 6 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? parallel      
AC6 2 3 ? parallel      
AC7 1 2 ? parallel      
AC8 1 2 ? parallel      
AC8 2 3 ? parallel      
AC9 1 2 ? parallel      
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AC9 4 5 ? anti-parallel 
AD1 1 2 ? parallel      
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD1 4 5 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? parallel      
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
AD7 4 5 ? anti-parallel 
AD7 5 6 ? anti-parallel 
AD8 1 2 ? parallel      
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE4 1 2 ? parallel      
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE4 4 5 ? anti-parallel 
AE4 5 6 ? anti-parallel 
AE5 1 2 ? parallel      
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? 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 THR B 16  ? VAL B 17  ? THR B 25  VAL B 26  
AA1 2 VAL B 25  ? THR B 26  ? VAL B 34  THR B 35  
AA2 1 LEU B 34  ? GLU B 35  ? LEU B 43  GLU B 44  
AA2 2 PHE B 293 ? GLN B 294 ? PHE B 294 GLN B 295 
AA2 3 LYS B 306 ? TYR B 307 ? LYS B 307 TYR B 308 
AA3 1 LYS B 44  ? LEU B 45  ? LYS B 53  LEU B 54  
AA3 2 ASN B 277 ? THR B 278 ? ASN B 278 THR B 279 
AA4 1 LEU B 51  ? LEU B 53  ? LEU B 59  LEU B 61  
AA4 2 ILE B 80  ? GLU B 82  ? ILE B 87  GLU B 89  
AA4 3 ILE B 266 ? ILE B 268 ? ILE B 267 ILE B 269 
AA5 1 GLY B 94  ? PHE B 96  ? GLY B 100 PHE B 102 
AA5 2 ARG B 227 ? VAL B 235 ? ARG B 229 VAL B 237 
AA5 3 GLU B 173 ? HIS B 182 ? GLU B 175 HIS B 184 
AA5 4 TYR B 254 ? MET B 258 ? TYR B 256 MET B 260 
AA5 5 PHE B 112 B GLU B 116 ? PHE B 116 GLU B 119 
AA6 1 GLY B 94  ? PHE B 96  ? GLY B 100 PHE B 102 
AA6 2 ARG B 227 ? VAL B 235 ? ARG B 229 VAL B 237 
AA6 3 GLU B 173 ? HIS B 182 ? GLU B 175 HIS B 184 
AA6 4 LEU B 249 ? PRO B 252 ? LEU B 251 PRO B 254 
AA6 5 LEU B 149 ? TRP B 151 ? LEU B 151 TRP B 153 
AA7 1 HIS B 127 ? ASP B 128 ? HIS B 130 ASP B 131 
AA7 2 VAL B 153 ? LYS B 154 ? VAL B 155 LYS B 156 
AA8 1 THR B 134 ? HIS B 139 ? THR B 136 HIS B 141 
AA8 2 ALA B 142 ? SER B 144 ? ALA B 144 SER B 146 
AA9 1 LEU B 162 ? ILE B 167 ? LEU B 164 ILE B 169 
AA9 2 LYS B 240 ? ALA B 245 ? LYS B 242 ALA B 247 
AA9 3 VAL B 200 ? GLY B 203 ? VAL B 202 GLY B 205 
AA9 4 SER B 208 ? PHE B 211 ? SER B 210 PHE B 213 
AB1 1 GLY B 285 ? ILE B 287 ? GLY B 286 ILE B 288 
AB1 2 CYS B 280 ? THR B 282 ? CYS B 281 THR B 283 
AB1 3 ILE B 301 ? GLY B 302 ? ILE B 302 GLY B 303 
AB2 1 LEU C 4   ? GLN C 6   ? LEU C 4   GLN C 6   
AB2 2 THR C 19  ? GLY C 24  ? THR C 19  GLY C 24  
AB2 3 THR C 78  ? TRP C 83  ? THR C 78  TRP C 83  
AB2 4 VAL C 68  ? ASP C 73  ? VAL C 68  ASP C 73  
AB3 1 GLU C 10  ? VAL C 11  ? GLU C 10  VAL C 11  
AB3 2 THR C 119 ? THR C 122 ? THR C 119 THR C 122 
AB3 3 ALA C 92  ? ALA C 101 ? ALA C 92  ALA C 101 
AB3 4 ILE C 34  ? ARG C 39  ? ILE C 34  ARG C 39  
AB3 5 LEU C 45  ? ILE C 51  ? LEU C 45  ILE C 51  
AB3 6 THR C 58  ? TYR C 60  ? THR C 58  TYR C 60  
AB4 1 GLU C 10  ? VAL C 11  ? GLU C 10  VAL C 11  
AB4 2 THR C 119 ? THR C 122 ? THR C 119 THR C 122 
AB4 3 ALA C 92  ? ALA C 101 ? ALA C 92  ALA C 101 
AB4 4 TYR C 109 ? TRP C 115 ? TYR C 109 TRP C 115 
AB5 1 SER C 132 ? LEU C 136 ? SER C 132 LEU C 136 
AB5 2 GLY C 151 ? TYR C 157 ? GLY C 151 TYR C 157 
AB5 3 TYR C 188 ? VAL C 194 ? TYR C 188 VAL C 194 
AB5 4 VAL C 175 ? THR C 177 ? VAL C 175 THR C 177 
AB6 1 SER C 132 ? LEU C 136 ? SER C 132 LEU C 136 
AB6 2 GLY C 151 ? TYR C 157 ? GLY C 151 TYR C 157 
AB6 3 TYR C 188 ? VAL C 194 ? TYR C 188 VAL C 194 
AB6 4 VAL C 181 ? LEU C 182 ? VAL C 181 LEU C 182 
AB7 1 VAL C 162 ? TRP C 166 ? VAL C 162 TRP C 166 
AB7 2 ILE C 207 ? HIS C 212 ? ILE C 207 HIS C 212 
AB7 3 ASP C 220 ? ARG C 222 ? ASP C 220 ARG C 222 
AB8 1 LEU D 4   ? SER D 7   ? LEU D 4   SER D 7   
AB8 2 ALA D 19  ? ALA D 25  ? ALA D 19  ALA D 25  
AB8 3 THR D 73  ? ILE D 76  ? THR D 73  ILE D 76  
AB8 4 SER D 64  ? LYS D 66  ? SER D 64  LYS D 66  
AB9 1 THR D 10  ? LEU D 13  ? THR D 10  LEU D 13  
AB9 2 THR D 103 ? ILE D 107 ? THR D 103 ILE D 107 
AB9 3 VAL D 86  ? GLN D 91  ? VAL D 86  GLN D 91  
AB9 4 LEU D 34  ? GLN D 39  ? LEU D 34  GLN D 39  
AB9 5 ARG D 46  ? PHE D 50  ? ARG D 46  PHE D 50  
AB9 6 SER D 54  ? ARG D 55  ? SER D 54  ARG D 55  
AC1 1 THR D 10  ? LEU D 13  ? THR D 10  LEU D 13  
AC1 2 THR D 103 ? ILE D 107 ? THR D 103 ILE D 107 
AC1 3 VAL D 86  ? GLN D 91  ? VAL D 86  GLN D 91  
AC1 4 THR D 98  ? PHE D 99  ? THR D 98  PHE D 99  
AC2 1 SER D 115 ? PHE D 119 ? SER D 115 PHE D 119 
AC2 2 THR D 130 ? PHE D 140 ? THR D 130 PHE D 140 
AC2 3 TYR D 174 ? SER D 183 ? TYR D 174 SER D 183 
AC2 4 SER D 160 ? THR D 165 ? SER D 160 THR D 165 
AC3 1 ALA D 154 ? GLN D 156 ? ALA D 154 GLN D 156 
AC3 2 LYS D 146 ? VAL D 151 ? LYS D 146 VAL D 151 
AC3 3 VAL D 192 ? THR D 198 ? VAL D 192 THR D 198 
AC3 4 THR D 207 ? ASN D 211 ? THR D 207 ASN D 211 
AC4 1 THR F 16  ? VAL F 17  ? THR F 25  VAL F 26  
AC4 2 VAL F 25  ? THR F 26  ? VAL F 34  THR F 35  
AC5 1 SER F 30  ? ASN F 32  ? SER F 39  ASN F 41  
AC5 2 ARG F 314 ? ALA F 316 ? ARG F 315 ALA F 317 
AC6 1 LEU F 34  ? GLU F 35  ? LEU F 43  GLU F 44  
AC6 2 PHE F 293 ? GLN F 294 ? PHE F 294 GLN F 295 
AC6 3 LYS F 306 ? TYR F 307 ? LYS F 307 TYR F 308 
AC7 1 LYS F 44  ? LEU F 45  ? LYS F 53  LEU F 54  
AC7 2 ASN F 277 ? THR F 278 ? ASN F 278 THR F 279 
AC8 1 LEU F 51  ? LEU F 53  ? LEU F 59  LEU F 61  
AC8 2 ILE F 80  ? GLU F 82  ? ILE F 87  GLU F 89  
AC8 3 ILE F 266 ? ILE F 267 ? ILE F 267 ILE F 268 
AC9 1 GLY F 94  ? PHE F 96  ? GLY F 100 PHE F 102 
AC9 2 ARG F 227 ? VAL F 235 ? ARG F 229 VAL F 237 
AC9 3 GLU F 173 ? HIS F 182 ? GLU F 175 HIS F 184 
AC9 4 TYR F 254 ? ARG F 260 ? TYR F 256 ARG F 262 
AC9 5 VAL F 109 ? GLU F 116 ? VAL F 115 GLU F 119 
AD1 1 GLY F 94  ? PHE F 96  ? GLY F 100 PHE F 102 
AD1 2 ARG F 227 ? VAL F 235 ? ARG F 229 VAL F 237 
AD1 3 GLU F 173 ? HIS F 182 ? GLU F 175 HIS F 184 
AD1 4 LEU F 249 ? PRO F 252 ? LEU F 251 PRO F 254 
AD1 5 LEU F 149 ? TRP F 151 ? LEU F 151 TRP F 153 
AD2 1 HIS F 127 ? ASP F 128 ? HIS F 130 ASP F 131 
AD2 2 VAL F 153 ? LYS F 154 ? VAL F 155 LYS F 156 
AD3 1 THR F 134 ? HIS F 139 ? THR F 136 HIS F 141 
AD3 2 ALA F 142 ? SER F 144 ? ALA F 144 SER F 146 
AD4 1 LEU F 162 ? ILE F 167 ? LEU F 164 ILE F 169 
AD4 2 LYS F 240 ? ALA F 245 ? LYS F 242 ALA F 247 
AD4 3 VAL F 200 ? GLY F 203 ? VAL F 202 GLY F 205 
AD4 4 SER F 208 ? PHE F 211 ? SER F 210 PHE F 213 
AD5 1 GLY F 285 ? ILE F 287 ? GLY F 286 ILE F 288 
AD5 2 CYS F 280 ? THR F 282 ? CYS F 281 THR F 283 
AD5 3 ILE F 301 ? GLY F 302 ? ILE F 302 GLY F 303 
AD6 1 GLN G 3   ? GLN G 6   ? GLN H 3   GLN H 6   
AD6 2 THR G 19  ? SER G 25  ? THR H 19  SER H 25  
AD6 3 THR G 78  ? TRP G 83  ? THR H 78  TRP H 83  
AD6 4 VAL G 68  ? ASP G 73  ? VAL H 68  ASP H 73  
AD7 1 GLU G 10  ? VAL G 11  ? GLU H 10  VAL H 11  
AD7 2 THR G 119 ? THR G 122 ? THR H 119 THR H 122 
AD7 3 ALA G 92  ? ALA G 101 ? ALA H 92  ALA H 101 
AD7 4 ILE G 34  ? ARG G 39  ? ILE H 34  ARG H 39  
AD7 5 LEU G 45  ? ASN G 52  ? LEU H 45  ASN H 52  
AD7 6 ASP G 57  ? TYR G 60  ? ASP H 57  TYR H 60  
AD8 1 GLU G 10  ? VAL G 11  ? GLU H 10  VAL H 11  
AD8 2 THR G 119 ? THR G 122 ? THR H 119 THR H 122 
AD8 3 ALA G 92  ? ALA G 101 ? ALA H 92  ALA H 101 
AD8 4 TYR G 109 ? TRP G 115 ? TYR H 109 TRP H 115 
AD9 1 SER G 132 ? LEU G 136 ? SER H 132 LEU H 136 
AD9 2 GLY G 151 ? TYR G 157 ? GLY H 151 TYR H 157 
AD9 3 TYR G 188 ? VAL G 194 ? TYR H 188 VAL H 194 
AD9 4 VAL G 175 ? THR G 177 ? VAL H 175 THR H 177 
AE1 1 SER G 132 ? LEU G 136 ? SER H 132 LEU H 136 
AE1 2 GLY G 151 ? TYR G 157 ? GLY H 151 TYR H 157 
AE1 3 TYR G 188 ? VAL G 194 ? TYR H 188 VAL H 194 
AE1 4 VAL G 181 ? LEU G 182 ? VAL H 181 LEU H 182 
AE2 1 VAL G 162 ? TRP G 166 ? VAL H 162 TRP H 166 
AE2 2 ILE G 207 ? HIS G 212 ? ILE H 207 HIS H 212 
AE2 3 ASP G 220 ? ARG G 222 ? ASP H 220 ARG H 222 
AE3 1 LEU H 4   ? SER H 7   ? LEU L 4   SER L 7   
AE3 2 ALA H 19  ? ALA H 25  ? ALA L 19  ALA L 25  
AE3 3 THR H 73  ? ILE H 76  ? THR L 73  ILE L 76  
AE3 4 PHE H 63  ? LYS H 66  ? PHE L 63  LYS L 66  
AE4 1 THR H 10  ? LEU H 13  ? THR L 10  LEU L 13  
AE4 2 THR H 103 ? ILE H 107 ? THR L 103 ILE L 107 
AE4 3 VAL H 86  ? GLN H 91  ? VAL L 86  GLN L 91  
AE4 4 LEU H 34  ? GLN H 39  ? LEU L 34  GLN L 39  
AE4 5 ARG H 46  ? PHE H 50  ? ARG L 46  PHE L 50  
AE4 6 SER H 54  ? ARG H 55  ? SER L 54  ARG L 55  
AE5 1 THR H 10  ? LEU H 13  ? THR L 10  LEU L 13  
AE5 2 THR H 103 ? ILE H 107 ? THR L 103 ILE L 107 
AE5 3 VAL H 86  ? GLN H 91  ? VAL L 86  GLN L 91  
AE5 4 THR H 98  ? PHE H 99  ? THR L 98  PHE L 99  
AE6 1 SER H 115 ? PHE H 119 ? SER L 115 PHE L 119 
AE6 2 THR H 130 ? PHE H 140 ? THR L 130 PHE L 140 
AE6 3 TYR H 174 ? SER H 183 ? TYR L 174 SER L 183 
AE6 4 SER H 160 ? THR H 165 ? SER L 160 THR L 165 
AE7 1 ALA H 154 ? GLN H 156 ? ALA L 154 GLN L 156 
AE7 2 LYS H 146 ? VAL H 151 ? LYS L 146 VAL L 151 
AE7 3 VAL H 192 ? THR H 198 ? VAL L 192 THR L 198 
AE7 4 THR H 207 ? ASN H 211 ? THR L 207 ASN L 211 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL B 17  ? N VAL B 26  O VAL B 25  ? O VAL B 34  
AA2 1 2 N GLU B 35  ? N GLU B 44  O PHE B 293 ? O PHE B 294 
AA2 2 3 N GLN B 294 ? N GLN B 295 O LYS B 306 ? O LYS B 307 
AA3 1 2 N LYS B 44  ? N LYS B 53  O THR B 278 ? O THR B 279 
AA4 1 2 N LEU B 51  ? N LEU B 59  O VAL B 81  ? O VAL B 88  
AA4 2 3 N ILE B 80  ? N ILE B 87  O ILE B 267 ? O ILE B 268 
AA5 1 2 N ASP B 95  ? N ASP B 101 O TYR B 230 ? O TYR B 232 
AA5 2 3 O ARG B 227 ? O ARG B 229 N HIS B 182 ? N HIS B 184 
AA5 3 4 N LEU B 175 ? N LEU B 177 O PHE B 256 ? O PHE B 258 
AA5 4 5 O ALA B 257 ? O ALA B 259 N GLU B 113 C N GLU B 116 
AA6 1 2 N ASP B 95  ? N ASP B 101 O TYR B 230 ? O TYR B 232 
AA6 2 3 O ARG B 227 ? O ARG B 229 N HIS B 182 ? N HIS B 184 
AA6 3 4 N GLY B 179 ? N GLY B 181 O VAL B 250 ? O VAL B 252 
AA6 4 5 O VAL B 251 ? O VAL B 253 N ILE B 150 ? N ILE B 152 
AA7 1 2 N ASP B 128 ? N ASP B 131 O VAL B 153 ? O VAL B 155 
AA8 1 2 N CYS B 137 ? N CYS B 139 O SER B 144 ? O SER B 146 
AA9 1 2 N TYR B 166 ? N TYR B 168 O ILE B 241 ? O ILE B 243 
AA9 2 3 O THR B 242 ? O THR B 244 N GLY B 203 ? N GLY B 205 
AA9 3 4 N VAL B 200 ? N VAL B 202 O PHE B 211 ? O PHE B 213 
AB1 1 2 O ILE B 287 ? O ILE B 288 N CYS B 280 ? N CYS B 281 
AB1 2 3 N GLN B 281 ? N GLN B 282 O ILE B 301 ? O ILE B 302 
AB2 1 2 N VAL C 5   ? N VAL C 5   O LYS C 23  ? O LYS C 23  
AB2 2 3 N CYS C 22  ? N CYS C 22  O ALA C 79  ? O ALA C 79  
AB2 3 4 O GLN C 82  ? O GLN C 82  N THR C 69  ? N THR C 69  
AB3 1 2 N GLU C 10  ? N GLU C 10  O THR C 122 ? O THR C 122 
AB3 2 3 O THR C 119 ? O THR C 119 N TYR C 94  ? N TYR C 94  
AB3 3 4 O MET C 93  ? O MET C 93  N ARG C 39  ? N ARG C 39  
AB3 4 5 N TRP C 36  ? N TRP C 36  O MET C 48  ? O MET C 48  
AB3 5 6 N ILE C 50  ? N ILE C 50  O ARG C 59  ? O ARG C 59  
AB4 1 2 N GLU C 10  ? N GLU C 10  O THR C 122 ? O THR C 122 
AB4 2 3 O THR C 119 ? O THR C 119 N TYR C 94  ? N TYR C 94  
AB4 3 4 N VAL C 100 ? N VAL C 100 O GLY C 111 ? O GLY C 111 
AB5 1 2 N SER C 132 ? N SER C 132 O LYS C 155 ? O LYS C 155 
AB5 2 3 N VAL C 154 ? N VAL C 154 O LEU C 190 ? O LEU C 190 
AB5 3 4 O VAL C 193 ? O VAL C 193 N HIS C 176 ? N HIS C 176 
AB6 1 2 N SER C 132 ? N SER C 132 O LYS C 155 ? O LYS C 155 
AB6 2 3 N VAL C 154 ? N VAL C 154 O LEU C 190 ? O LEU C 190 
AB6 3 4 O SER C 189 ? O SER C 189 N VAL C 181 ? N VAL C 181 
AB7 1 2 N SER C 165 ? N SER C 165 O ASN C 209 ? O ASN C 209 
AB7 2 3 N CYS C 208 ? N CYS C 208 O LYS C 221 ? O LYS C 221 
AB8 1 2 N SER D 7   ? N SER D 7   O SER D 22  ? O SER D 22  
AB8 2 3 N LEU D 21  ? N LEU D 21  O LEU D 74  ? O LEU D 74  
AB8 3 4 O THR D 73  ? O THR D 73  N LYS D 66  ? N LYS D 66  
AB9 1 2 N LEU D 11  ? N LEU D 11  O GLU D 106 ? O GLU D 106 
AB9 2 3 O THR D 103 ? O THR D 103 N TYR D 87  ? N TYR D 87  
AB9 3 4 O TYR D 88  ? O TYR D 88  N TYR D 37  ? N TYR D 37  
AB9 4 5 N TRP D 36  ? N TRP D 36  O LEU D 48  ? O LEU D 48  
AB9 5 6 N PHE D 50  ? N PHE D 50  O SER D 54  ? O SER D 54  
AC1 1 2 N LEU D 11  ? N LEU D 11  O GLU D 106 ? O GLU D 106 
AC1 2 3 O THR D 103 ? O THR D 103 N TYR D 87  ? N TYR D 87  
AC1 3 4 N GLN D 91  ? N GLN D 91  O THR D 98  ? O THR D 98  
AC2 1 2 N SER D 115 ? N SER D 115 O ASN D 138 ? O ASN D 138 
AC2 2 3 N VAL D 133 ? N VAL D 133 O LEU D 180 ? O LEU D 180 
AC2 3 4 O THR D 179 ? O THR D 179 N GLN D 161 ? N GLN D 161 
AC3 1 2 O GLN D 156 ? O GLN D 156 N TRP D 149 ? N TRP D 149 
AC3 2 3 N GLN D 148 ? N GLN D 148 O GLU D 196 ? O GLU D 196 
AC3 3 4 N TYR D 193 ? N TYR D 193 O PHE D 210 ? O PHE D 210 
AC4 1 2 N VAL F 17  ? N VAL F 26  O VAL F 25  ? O VAL F 34  
AC5 1 2 N VAL F 31  ? N VAL F 40  O LEU F 315 ? O LEU F 316 
AC6 1 2 N GLU F 35  ? N GLU F 44  O PHE F 293 ? O PHE F 294 
AC6 2 3 N GLN F 294 ? N GLN F 295 O LYS F 306 ? O LYS F 307 
AC7 1 2 N LYS F 44  ? N LYS F 53  O THR F 278 ? O THR F 279 
AC8 1 2 N LEU F 53  ? N LEU F 61  O VAL F 81  ? O VAL F 88  
AC8 2 3 N GLU F 82  ? N GLU F 89  O ILE F 267 ? O ILE F 268 
AC9 1 2 N ASP F 95  ? N ASP F 101 O TYR F 230 ? O TYR F 232 
AC9 2 3 O ARG F 227 ? O ARG F 229 N HIS F 182 ? N HIS F 184 
AC9 3 4 N GLU F 173 ? N GLU F 175 O MET F 258 ? O MET F 260 
AC9 4 5 O GLU F 259 ? O GLU F 261 N SER F 110 ? N SER F 116 
AD1 1 2 N ASP F 95  ? N ASP F 101 O TYR F 230 ? O TYR F 232 
AD1 2 3 O ARG F 227 ? O ARG F 229 N HIS F 182 ? N HIS F 184 
AD1 3 4 N GLY F 179 ? N GLY F 181 O VAL F 250 ? O VAL F 252 
AD1 4 5 O VAL F 251 ? O VAL F 253 N ILE F 150 ? N ILE F 152 
AD2 1 2 N ASP F 128 ? N ASP F 131 O VAL F 153 ? O VAL F 155 
AD3 1 2 N CYS F 137 ? N CYS F 139 O SER F 144 ? O SER F 146 
AD4 1 2 N TYR F 166 ? N TYR F 168 O ILE F 241 ? O ILE F 243 
AD4 2 3 O THR F 242 ? O THR F 244 N GLY F 203 ? N GLY F 205 
AD4 3 4 N VAL F 200 ? N VAL F 202 O PHE F 211 ? O PHE F 213 
AD5 1 2 O ILE F 287 ? O ILE F 288 N CYS F 280 ? N CYS F 281 
AD5 2 3 N GLN F 281 ? N GLN F 282 O ILE F 301 ? O ILE F 302 
AD6 1 2 N VAL G 5   ? N VAL H 5   O LYS G 23  ? O LYS H 23  
AD6 2 3 N CYS G 22  ? N CYS H 22  O ALA G 79  ? O ALA H 79  
AD6 3 4 O GLN G 82  ? O GLN H 82  N THR G 69  ? N THR H 69  
AD7 1 2 N GLU G 10  ? N GLU H 10  O THR G 122 ? O THR H 122 
AD7 2 3 O THR G 119 ? O THR H 119 N TYR G 94  ? N TYR H 94  
AD7 3 4 O MET G 93  ? O MET H 93  N ARG G 39  ? N ARG H 39  
AD7 4 5 N TRP G 36  ? N TRP H 36  O MET G 48  ? O MET H 48  
AD7 5 6 N ILE G 50  ? N ILE H 50  O ARG G 59  ? O ARG H 59  
AD8 1 2 N GLU G 10  ? N GLU H 10  O THR G 122 ? O THR H 122 
AD8 2 3 O THR G 119 ? O THR H 119 N TYR G 94  ? N TYR H 94  
AD8 3 4 N VAL G 100 ? N VAL H 100 O GLY G 111 ? O GLY H 111 
AD9 1 2 N SER G 132 ? N SER H 132 O LYS G 155 ? O LYS H 155 
AD9 2 3 N VAL G 154 ? N VAL H 154 O LEU G 190 ? O LEU H 190 
AD9 3 4 O VAL G 193 ? O VAL H 193 N HIS G 176 ? N HIS H 176 
AE1 1 2 N SER G 132 ? N SER H 132 O LYS G 155 ? O LYS H 155 
AE1 2 3 N VAL G 154 ? N VAL H 154 O LEU G 190 ? O LEU H 190 
AE1 3 4 O SER G 189 ? O SER H 189 N VAL G 181 ? N VAL H 181 
AE2 1 2 N SER G 165 ? N SER H 165 O ASN G 209 ? O ASN H 209 
AE2 2 3 N CYS G 208 ? N CYS H 208 O LYS G 221 ? O LYS H 221 
AE3 1 2 N SER H 7   ? N SER L 7   O SER H 22  ? O SER L 22  
AE3 2 3 N ALA H 19  ? N ALA L 19  O ILE H 76  ? O ILE L 76  
AE3 3 4 O THR H 73  ? O THR L 73  N LYS H 66  ? N LYS L 66  
AE4 1 2 N LEU H 11  ? N LEU L 11  O GLU H 106 ? O GLU L 106 
AE4 2 3 O THR H 103 ? O THR L 103 N TYR H 87  ? N TYR L 87  
AE4 3 4 O TYR H 88  ? O TYR L 88  N TYR H 37  ? N TYR L 37  
AE4 4 5 N TRP H 36  ? N TRP L 36  O LEU H 48  ? O LEU L 48  
AE4 5 6 N PHE H 50  ? N PHE L 50  O SER H 54  ? O SER L 54  
AE5 1 2 N LEU H 11  ? N LEU L 11  O GLU H 106 ? O GLU L 106 
AE5 2 3 O THR H 103 ? O THR L 103 N TYR H 87  ? N TYR L 87  
AE5 3 4 N GLN H 91  ? N GLN L 91  O THR H 98  ? O THR L 98  
AE6 1 2 N PHE H 119 ? N PHE L 119 O VAL H 134 ? O VAL L 134 
AE6 2 3 N VAL H 133 ? N VAL L 133 O LEU H 180 ? O LEU L 180 
AE6 3 4 O THR H 179 ? O THR L 179 N GLN H 161 ? N GLN L 161 
AE7 1 2 O GLN H 156 ? O GLN L 156 N TRP H 149 ? N TRP L 149 
AE7 2 3 N GLN H 148 ? N GLN L 148 O GLU H 196 ? O GLU L 196 
AE7 3 4 N TYR H 193 ? N TYR L 193 O PHE H 210 ? O PHE L 210 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software B NAG 402 ? 4  'binding site for Mono-Saccharide NAG B 402 bound to ASN B 20'  
AC2 Software B NAG 401 ? 4  'binding site for Mono-Saccharide NAG B 401 bound to ASN B 278' 
AC3 Software F NAG 404 ? 10 'binding site for Mono-Saccharide NAG F 404 bound to ASN F 20'  
AC4 Software F NAG 405 ? 2  'binding site for Mono-Saccharide NAG F 405 bound to ASN F 33'  
AC5 Software F NAG 403 ? 4  'binding site for Mono-Saccharide NAG F 403 bound to ASN F 94'  
AC6 Software F NAG 402 ? 4  'binding site for Mono-Saccharide NAG F 402 bound to ASN F 278' 
AC7 Software F NAG 401 ? 1  'binding site for Mono-Saccharide NAG F 401 bound to ASN F 289' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  THR A 15  ? THR A 15  . ? 1_555 ? 
2  AC1 4  MET A 17  ? MET A 17  . ? 1_555 ? 
3  AC1 4  ASN B 11  ? ASN B 20  . ? 1_555 ? 
4  AC1 4  HIS B 29  ? HIS B 38  . ? 1_555 ? 
5  AC2 4  ARG B 46  ? ARG B 55  . ? 1_555 ? 
6  AC2 4  GLY B 47  A GLY B 55  . ? 1_555 ? 
7  AC2 4  ASP B 275 ? ASP B 276 . ? 1_555 ? 
8  AC2 4  ASN B 277 ? ASN B 278 . ? 1_555 ? 
9  AC3 10 ILE E 10  ? ILE E 10  . ? 1_555 ? 
10 AC3 10 GLY E 13  ? GLY E 13  . ? 1_555 ? 
11 AC3 10 TRP E 14  ? TRP E 14  . ? 1_555 ? 
12 AC3 10 MET E 17  ? MET E 17  . ? 1_555 ? 
13 AC3 10 GLY E 20  ? GLY E 20  . ? 1_555 ? 
14 AC3 10 TRP E 21  ? TRP E 21  . ? 1_555 ? 
15 AC3 10 ASN F 11  ? ASN F 20  . ? 1_555 ? 
16 AC3 10 HIS F 29  ? HIS F 38  . ? 1_555 ? 
17 AC3 10 ARG F 320 ? ARG F 321 . ? 1_555 ? 
18 AC3 10 ASN F 321 ? ASN F 322 . ? 1_555 ? 
19 AC4 2  SER B 205 ? SER B 207 . ? 1_455 ? 
20 AC4 2  ASN F 24  ? ASN F 33  . ? 1_555 ? 
21 AC5 4  GLU F 67  ? GLU F 75  . ? 1_555 ? 
22 AC5 4  ASN F 88  ? ASN F 94  . ? 1_555 ? 
23 AC5 4  PRO F 138 ? PRO F 140 . ? 1_555 ? 
24 AC5 4  ARG F 222 ? ARG F 224 . ? 1_555 ? 
25 AC6 4  ARG F 46  ? ARG F 55  . ? 1_555 ? 
26 AC6 4  GLY F 47  A GLY F 55  . ? 1_555 ? 
27 AC6 4  ASP F 275 ? ASP F 276 . ? 1_555 ? 
28 AC6 4  ASN F 277 ? ASN F 278 . ? 1_555 ? 
29 AC7 1  ASN F 288 ? ASN F 289 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5IBL 
_atom_sites.fract_transf_matrix[1][1]   0.018474 
_atom_sites.fract_transf_matrix[1][2]   0.002715 
_atom_sites.fract_transf_matrix[1][3]   0.002392 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009652 
_atom_sites.fract_transf_matrix[2][3]   0.002217 
_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]   0.008833 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . THR A 1 15  ? -47.213  -27.230  -37.497 1.00 177.09 ? 15  THR A N   1 
ATOM   2     C CA  . THR A 1 15  ? -46.903  -28.661  -37.523 1.00 177.00 ? 15  THR A CA  1 
ATOM   3     C C   . THR A 1 15  ? -45.936  -29.046  -38.655 1.00 181.60 ? 15  THR A C   1 
ATOM   4     O O   . THR A 1 15  ? -44.995  -29.809  -38.436 1.00 180.47 ? 15  THR A O   1 
ATOM   5     C CB  . THR A 1 15  ? -48.183  -29.511  -37.560 1.00 183.62 ? 15  THR A CB  1 
ATOM   6     O OG1 . THR A 1 15  ? -48.991  -29.103  -38.665 1.00 183.41 ? 15  THR A OG1 1 
ATOM   7     C CG2 . THR A 1 15  ? -48.982  -29.442  -36.260 1.00 180.89 ? 15  THR A CG2 1 
ATOM   8     N N   . GLY A 1 16  ? -46.188  -28.521  -39.849 1.00 179.90 ? 16  GLY A N   1 
ATOM   9     C CA  . GLY A 1 16  ? -45.388  -28.798  -41.036 1.00 180.85 ? 16  GLY A CA  1 
ATOM   10    C C   . GLY A 1 16  ? -43.963  -28.268  -41.035 1.00 186.86 ? 16  GLY A C   1 
ATOM   11    O O   . GLY A 1 16  ? -43.119  -28.796  -41.765 1.00 187.16 ? 16  GLY A O   1 
ATOM   12    N N   . MET A 1 17  ? -43.680  -27.218  -40.236 1.00 183.95 ? 17  MET A N   1 
ATOM   13    C CA  . MET A 1 17  ? -42.354  -26.594  -40.160 1.00 184.11 ? 17  MET A CA  1 
ATOM   14    C C   . MET A 1 17  ? -41.313  -27.498  -39.504 1.00 188.25 ? 17  MET A C   1 
ATOM   15    O O   . MET A 1 17  ? -41.596  -28.133  -38.487 1.00 187.66 ? 17  MET A O   1 
ATOM   16    C CB  . MET A 1 17  ? -42.426  -25.216  -39.474 1.00 186.52 ? 17  MET A CB  1 
ATOM   17    C CG  . MET A 1 17  ? -41.170  -24.377  -39.634 1.00 190.56 ? 17  MET A CG  1 
ATOM   18    S SD  . MET A 1 17  ? -41.398  -22.685  -39.034 1.00 195.14 ? 17  MET A SD  1 
ATOM   19    C CE  . MET A 1 17  ? -41.970  -21.887  -40.509 1.00 191.83 ? 17  MET A CE  1 
ATOM   20    N N   . VAL A 1 18  ? -40.116  -27.567  -40.117 1.00 185.32 ? 18  VAL A N   1 
ATOM   21    C CA  . VAL A 1 18  ? -38.970  -28.369  -39.660 1.00 185.31 ? 18  VAL A CA  1 
ATOM   22    C C   . VAL A 1 18  ? -37.666  -27.533  -39.616 1.00 189.16 ? 18  VAL A C   1 
ATOM   23    O O   . VAL A 1 18  ? -36.582  -28.079  -39.387 1.00 188.94 ? 18  VAL A O   1 
ATOM   24    C CB  . VAL A 1 18  ? -38.796  -29.707  -40.446 1.00 189.35 ? 18  VAL A CB  1 
ATOM   25    C CG1 . VAL A 1 18  ? -39.803  -30.758  -39.984 1.00 189.12 ? 18  VAL A CG1 1 
ATOM   26    C CG2 . VAL A 1 18  ? -38.866  -29.499  -41.960 1.00 189.24 ? 18  VAL A CG2 1 
ATOM   27    N N   . ASP A 1 19  ? -37.790  -26.203  -39.796 1.00 185.46 ? 19  ASP A N   1 
ATOM   28    C CA  . ASP A 1 19  ? -36.667  -25.264  -39.777 1.00 213.25 ? 19  ASP A CA  1 
ATOM   29    C C   . ASP A 1 19  ? -36.829  -24.231  -38.667 1.00 228.63 ? 19  ASP A C   1 
ATOM   30    O O   . ASP A 1 19  ? -36.913  -24.596  -37.496 1.00 185.56 ? 19  ASP A O   1 
ATOM   31    C CB  . ASP A 1 19  ? -36.495  -24.581  -41.146 1.00 215.16 ? 19  ASP A CB  1 
ATOM   32    C CG  . ASP A 1 19  ? -37.750  -23.916  -41.677 1.00 225.80 ? 19  ASP A CG  1 
ATOM   33    O OD1 . ASP A 1 19  ? -38.476  -24.561  -42.465 1.00 226.09 ? 19  ASP A OD1 1 
ATOM   34    O OD2 . ASP A 1 19  ? -38.001  -22.748  -41.312 1.00 232.46 ? 19  ASP A OD2 1 
ATOM   35    N N   . ALA A 1 36  ? -39.311  -19.602  -38.874 1.00 203.13 ? 36  ALA A N   1 
ATOM   36    C CA  . ALA A 1 36  ? -38.932  -19.850  -37.483 1.00 200.78 ? 36  ALA A CA  1 
ATOM   37    C C   . ALA A 1 36  ? -37.765  -18.957  -37.060 1.00 202.39 ? 36  ALA A C   1 
ATOM   38    O O   . ALA A 1 36  ? -36.776  -18.853  -37.793 1.00 201.24 ? 36  ALA A O   1 
ATOM   39    C CB  . ALA A 1 36  ? -38.560  -21.311  -37.288 1.00 201.55 ? 36  ALA A CB  1 
ATOM   40    N N   . ASP A 1 37  ? -37.879  -18.314  -35.878 1.00 197.89 ? 37  ASP A N   1 
ATOM   41    C CA  . ASP A 1 37  ? -36.837  -17.431  -35.346 1.00 195.43 ? 37  ASP A CA  1 
ATOM   42    C C   . ASP A 1 37  ? -35.709  -18.268  -34.773 1.00 198.79 ? 37  ASP A C   1 
ATOM   43    O O   . ASP A 1 37  ? -35.951  -19.091  -33.887 1.00 198.57 ? 37  ASP A O   1 
ATOM   44    C CB  . ASP A 1 37  ? -37.405  -16.441  -34.301 1.00 196.25 ? 37  ASP A CB  1 
ATOM   45    C CG  . ASP A 1 37  ? -36.406  -15.417  -33.780 1.00 200.91 ? 37  ASP A CG  1 
ATOM   46    O OD1 . ASP A 1 37  ? -35.856  -14.645  -34.602 1.00 199.99 ? 37  ASP A OD1 1 
ATOM   47    O OD2 . ASP A 1 37  ? -36.209  -15.356  -32.548 1.00 204.86 ? 37  ASP A OD2 1 
ATOM   48    N N   . LEU A 1 38  ? -34.481  -18.076  -35.304 1.00 194.55 ? 38  LEU A N   1 
ATOM   49    C CA  . LEU A 1 38  ? -33.281  -18.819  -34.905 1.00 193.04 ? 38  LEU A CA  1 
ATOM   50    C C   . LEU A 1 38  ? -32.811  -18.514  -33.481 1.00 196.03 ? 38  LEU A C   1 
ATOM   51    O O   . LEU A 1 38  ? -32.481  -19.457  -32.773 1.00 195.20 ? 38  LEU A O   1 
ATOM   52    C CB  . LEU A 1 38  ? -32.128  -18.640  -35.911 1.00 191.81 ? 38  LEU A CB  1 
ATOM   53    C CG  . LEU A 1 38  ? -31.197  -19.847  -36.081 1.00 195.63 ? 38  LEU A CG  1 
ATOM   54    C CD1 . LEU A 1 38  ? -30.839  -20.059  -37.534 1.00 196.17 ? 38  LEU A CD1 1 
ATOM   55    C CD2 . LEU A 1 38  ? -29.937  -19.701  -35.245 1.00 195.47 ? 38  LEU A CD2 1 
ATOM   56    N N   . LYS A 1 39  ? -32.782  -17.224  -33.060 1.00 191.94 ? 39  LYS A N   1 
ATOM   57    C CA  . LYS A 1 39  ? -32.349  -16.811  -31.713 1.00 190.17 ? 39  LYS A CA  1 
ATOM   58    C C   . LYS A 1 39  ? -33.211  -17.418  -30.600 1.00 194.36 ? 39  LYS A C   1 
ATOM   59    O O   . LYS A 1 39  ? -32.673  -17.771  -29.550 1.00 192.96 ? 39  LYS A O   1 
ATOM   60    C CB  . LYS A 1 39  ? -32.290  -15.280  -31.579 1.00 191.61 ? 39  LYS A CB  1 
ATOM   61    C CG  . LYS A 1 39  ? -31.388  -14.802  -30.440 1.00 203.83 ? 39  LYS A CG  1 
ATOM   62    C CD  . LYS A 1 39  ? -31.670  -13.353  -30.049 1.00 212.80 ? 39  LYS A CD  1 
ATOM   63    C CE  . LYS A 1 39  ? -30.932  -12.926  -28.801 1.00 219.30 ? 39  LYS A CE  1 
ATOM   64    N NZ  . LYS A 1 39  ? -31.546  -13.483  -27.565 1.00 227.05 ? 39  LYS A NZ  1 
ATOM   65    N N   . SER A 1 40  ? -34.534  -17.541  -30.832 1.00 192.18 ? 40  SER A N   1 
ATOM   66    C CA  . SER A 1 40  ? -35.477  -18.124  -29.878 1.00 192.36 ? 40  SER A CA  1 
ATOM   67    C C   . SER A 1 40  ? -35.266  -19.636  -29.708 1.00 195.39 ? 40  SER A C   1 
ATOM   68    O O   . SER A 1 40  ? -35.091  -20.093  -28.577 1.00 193.95 ? 40  SER A O   1 
ATOM   69    C CB  . SER A 1 40  ? -36.917  -17.802  -30.269 1.00 197.83 ? 40  SER A CB  1 
ATOM   70    O OG  . SER A 1 40  ? -37.248  -18.319  -31.547 1.00 209.26 ? 40  SER A OG  1 
ATOM   71    N N   . THR A 1 41  ? -35.248  -20.396  -30.822 1.00 192.41 ? 41  THR A N   1 
ATOM   72    C CA  . THR A 1 41  ? -35.035  -21.842  -30.793 1.00 192.45 ? 41  THR A CA  1 
ATOM   73    C C   . THR A 1 41  ? -33.601  -22.196  -30.371 1.00 196.14 ? 41  THR A C   1 
ATOM   74    O O   . THR A 1 41  ? -33.421  -23.190  -29.672 1.00 195.76 ? 41  THR A O   1 
ATOM   75    C CB  . THR A 1 41  ? -35.466  -22.516  -32.101 1.00 198.55 ? 41  THR A CB  1 
ATOM   76    O OG1 . THR A 1 41  ? -35.358  -23.925  -31.944 1.00 196.86 ? 41  THR A OG1 1 
ATOM   77    C CG2 . THR A 1 41  ? -34.671  -22.053  -33.294 1.00 196.84 ? 41  THR A CG2 1 
ATOM   78    N N   . GLN A 1 42  ? -32.595  -21.380  -30.780 1.00 192.36 ? 42  GLN A N   1 
ATOM   79    C CA  . GLN A 1 42  ? -31.177  -21.569  -30.436 1.00 190.95 ? 42  GLN A CA  1 
ATOM   80    C C   . GLN A 1 42  ? -30.981  -21.479  -28.917 1.00 193.94 ? 42  GLN A C   1 
ATOM   81    O O   . GLN A 1 42  ? -30.327  -22.349  -28.349 1.00 193.20 ? 42  GLN A O   1 
ATOM   82    C CB  . GLN A 1 42  ? -30.277  -20.561  -31.188 1.00 191.15 ? 42  GLN A CB  1 
ATOM   83    C CG  . GLN A 1 42  ? -28.777  -20.698  -30.937 1.00 205.91 ? 42  GLN A CG  1 
ATOM   84    C CD  . GLN A 1 42  ? -28.264  -19.593  -30.047 1.00 224.46 ? 42  GLN A CD  1 
ATOM   85    O OE1 . GLN A 1 42  ? -28.088  -18.447  -30.473 1.00 219.40 ? 42  GLN A OE1 1 
ATOM   86    N NE2 . GLN A 1 42  ? -28.012  -19.910  -28.786 1.00 216.09 ? 42  GLN A NE2 1 
ATOM   87    N N   . ASN A 1 43  ? -31.589  -20.460  -28.265 1.00 189.85 ? 43  ASN A N   1 
ATOM   88    C CA  . ASN A 1 43  ? -31.526  -20.269  -26.812 1.00 188.57 ? 43  ASN A CA  1 
ATOM   89    C C   . ASN A 1 43  ? -32.353  -21.312  -26.064 1.00 191.53 ? 43  ASN A C   1 
ATOM   90    O O   . ASN A 1 43  ? -32.068  -21.581  -24.898 1.00 190.56 ? 43  ASN A O   1 
ATOM   91    C CB  . ASN A 1 43  ? -31.931  -18.849  -26.414 1.00 190.49 ? 43  ASN A CB  1 
ATOM   92    C CG  . ASN A 1 43  ? -30.883  -17.804  -26.724 1.00 218.49 ? 43  ASN A CG  1 
ATOM   93    O OD1 . ASN A 1 43  ? -29.692  -17.953  -26.407 1.00 213.49 ? 43  ASN A OD1 1 
ATOM   94    N ND2 . ASN A 1 43  ? -31.311  -16.702  -27.324 1.00 210.96 ? 43  ASN A ND2 1 
ATOM   95    N N   . ALA A 1 44  ? -33.362  -21.907  -26.739 1.00 188.11 ? 44  ALA A N   1 
ATOM   96    C CA  . ALA A 1 44  ? -34.205  -22.968  -26.184 1.00 187.84 ? 44  ALA A CA  1 
ATOM   97    C C   . ALA A 1 44  ? -33.442  -24.306  -26.204 1.00 189.73 ? 44  ALA A C   1 
ATOM   98    O O   . ALA A 1 44  ? -33.328  -24.937  -25.154 1.00 189.15 ? 44  ALA A O   1 
ATOM   99    C CB  . ALA A 1 44  ? -35.513  -23.074  -26.956 1.00 189.95 ? 44  ALA A CB  1 
ATOM   100   N N   . ILE A 1 45  ? -32.869  -24.698  -27.378 1.00 184.64 ? 45  ILE A N   1 
ATOM   101   C CA  . ILE A 1 45  ? -32.052  -25.910  -27.580 1.00 183.52 ? 45  ILE A CA  1 
ATOM   102   C C   . ILE A 1 45  ? -30.912  -25.940  -26.545 1.00 184.30 ? 45  ILE A C   1 
ATOM   103   O O   . ILE A 1 45  ? -30.714  -26.960  -25.880 1.00 183.52 ? 45  ILE A O   1 
ATOM   104   C CB  . ILE A 1 45  ? -31.526  -25.985  -29.053 1.00 187.12 ? 45  ILE A CB  1 
ATOM   105   C CG1 . ILE A 1 45  ? -32.651  -26.403  -30.023 1.00 189.16 ? 45  ILE A CG1 1 
ATOM   106   C CG2 . ILE A 1 45  ? -30.302  -26.914  -29.196 1.00 187.33 ? 45  ILE A CG2 1 
ATOM   107   C CD1 . ILE A 1 45  ? -32.453  -25.950  -31.473 1.00 195.55 ? 45  ILE A CD1 1 
ATOM   108   N N   . ASP A 1 46  ? -30.202  -24.797  -26.393 1.00 178.71 ? 46  ASP A N   1 
ATOM   109   C CA  . ASP A 1 46  ? -29.103  -24.590  -25.449 1.00 176.70 ? 46  ASP A CA  1 
ATOM   110   C C   . ASP A 1 46  ? -29.562  -24.779  -24.000 1.00 178.17 ? 46  ASP A C   1 
ATOM   111   O O   . ASP A 1 46  ? -28.930  -25.545  -23.272 1.00 177.32 ? 46  ASP A O   1 
ATOM   112   C CB  . ASP A 1 46  ? -28.472  -23.196  -25.639 1.00 177.73 ? 46  ASP A CB  1 
ATOM   113   C CG  . ASP A 1 46  ? -27.712  -22.971  -26.940 1.00 187.68 ? 46  ASP A CG  1 
ATOM   114   O OD1 . ASP A 1 46  ? -27.814  -23.829  -27.854 1.00 188.37 ? 46  ASP A OD1 1 
ATOM   115   O OD2 . ASP A 1 46  ? -27.058  -21.914  -27.066 1.00 193.49 ? 46  ASP A OD2 1 
ATOM   116   N N   . GLU A 1 47  ? -30.672  -24.109  -23.597 1.00 173.34 ? 47  GLU A N   1 
ATOM   117   C CA  . GLU A 1 47  ? -31.256  -24.207  -22.252 1.00 172.24 ? 47  GLU A CA  1 
ATOM   118   C C   . GLU A 1 47  ? -31.758  -25.616  -21.935 1.00 174.18 ? 47  GLU A C   1 
ATOM   119   O O   . GLU A 1 47  ? -31.684  -26.026  -20.777 1.00 173.77 ? 47  GLU A O   1 
ATOM   120   C CB  . GLU A 1 47  ? -32.375  -23.172  -22.031 1.00 173.79 ? 47  GLU A CB  1 
ATOM   121   C CG  . GLU A 1 47  ? -31.887  -21.854  -21.448 1.00 185.45 ? 47  GLU A CG  1 
ATOM   122   C CD  . GLU A 1 47  ? -32.953  -20.806  -21.175 1.00 204.65 ? 47  GLU A CD  1 
ATOM   123   O OE1 . GLU A 1 47  ? -33.456  -20.199  -22.149 1.00 194.69 ? 47  GLU A OE1 1 
ATOM   124   O OE2 . GLU A 1 47  ? -33.240  -20.547  -19.984 1.00 196.85 ? 47  GLU A OE2 1 
ATOM   125   N N   . ILE A 1 48  ? -32.251  -26.356  -22.957 1.00 169.12 ? 48  ILE A N   1 
ATOM   126   C CA  . ILE A 1 48  ? -32.735  -27.732  -22.813 1.00 168.11 ? 48  ILE A CA  1 
ATOM   127   C C   . ILE A 1 48  ? -31.545  -28.671  -22.573 1.00 170.27 ? 48  ILE A C   1 
ATOM   128   O O   . ILE A 1 48  ? -31.504  -29.337  -21.540 1.00 169.27 ? 48  ILE A O   1 
ATOM   129   C CB  . ILE A 1 48  ? -33.636  -28.188  -24.010 1.00 171.96 ? 48  ILE A CB  1 
ATOM   130   C CG1 . ILE A 1 48  ? -34.955  -27.365  -24.125 1.00 172.40 ? 48  ILE A CG1 1 
ATOM   131   C CG2 . ILE A 1 48  ? -33.918  -29.703  -23.982 1.00 172.92 ? 48  ILE A CG2 1 
ATOM   132   C CD1 . ILE A 1 48  ? -35.906  -27.323  -22.904 1.00 176.83 ? 48  ILE A CD1 1 
ATOM   133   N N   . THR A 1 49  ? -30.567  -28.689  -23.511 1.00 166.02 ? 49  THR A N   1 
ATOM   134   C CA  . THR A 1 49  ? -29.357  -29.528  -23.461 1.00 165.03 ? 49  THR A CA  1 
ATOM   135   C C   . THR A 1 49  ? -28.550  -29.332  -22.172 1.00 166.62 ? 49  THR A C   1 
ATOM   136   O O   . THR A 1 49  ? -27.956  -30.291  -21.675 1.00 166.06 ? 49  THR A O   1 
ATOM   137   C CB  . THR A 1 49  ? -28.495  -29.342  -24.720 1.00 172.58 ? 49  THR A CB  1 
ATOM   138   O OG1 . THR A 1 49  ? -28.238  -27.952  -24.919 1.00 172.66 ? 49  THR A OG1 1 
ATOM   139   C CG2 . THR A 1 49  ? -29.135  -29.948  -25.970 1.00 170.81 ? 49  THR A CG2 1 
ATOM   140   N N   . ASN A 1 50  ? -28.560  -28.105  -21.620 1.00 161.63 ? 50  ASN A N   1 
ATOM   141   C CA  . ASN A 1 50  ? -27.886  -27.787  -20.364 1.00 160.62 ? 50  ASN A CA  1 
ATOM   142   C C   . ASN A 1 50  ? -28.693  -28.283  -19.162 1.00 163.79 ? 50  ASN A C   1 
ATOM   143   O O   . ASN A 1 50  ? -28.095  -28.728  -18.185 1.00 163.27 ? 50  ASN A O   1 
ATOM   144   C CB  . ASN A 1 50  ? -27.563  -26.301  -20.268 1.00 160.18 ? 50  ASN A CB  1 
ATOM   145   C CG  . ASN A 1 50  ? -26.305  -25.913  -21.018 1.00 179.09 ? 50  ASN A CG  1 
ATOM   146   O OD1 . ASN A 1 50  ? -25.293  -25.522  -20.424 1.00 171.49 ? 50  ASN A OD1 1 
ATOM   147   N ND2 . ASN A 1 50  ? -26.323  -26.035  -22.339 1.00 169.78 ? 50  ASN A ND2 1 
ATOM   148   N N   . LYS A 1 51  ? -30.047  -28.238  -19.255 1.00 159.89 ? 51  LYS A N   1 
ATOM   149   C CA  . LYS A 1 51  ? -30.999  -28.713  -18.236 1.00 159.17 ? 51  LYS A CA  1 
ATOM   150   C C   . LYS A 1 51  ? -30.967  -30.250  -18.163 1.00 163.08 ? 51  LYS A C   1 
ATOM   151   O O   . LYS A 1 51  ? -31.217  -30.813  -17.095 1.00 162.46 ? 51  LYS A O   1 
ATOM   152   C CB  . LYS A 1 51  ? -32.420  -28.238  -18.582 1.00 161.56 ? 51  LYS A CB  1 
ATOM   153   C CG  . LYS A 1 51  ? -33.421  -28.248  -17.434 1.00 178.16 ? 51  LYS A CG  1 
ATOM   154   C CD  . LYS A 1 51  ? -34.762  -27.673  -17.899 1.00 188.71 ? 51  LYS A CD  1 
ATOM   155   C CE  . LYS A 1 51  ? -35.742  -27.440  -16.773 1.00 196.93 ? 51  LYS A CE  1 
ATOM   156   N NZ  . LYS A 1 51  ? -36.973  -26.749  -17.241 1.00 203.67 ? 51  LYS A NZ  1 
ATOM   157   N N   . VAL A 1 52  ? -30.666  -30.913  -19.306 1.00 159.61 ? 52  VAL A N   1 
ATOM   158   C CA  . VAL A 1 52  ? -30.551  -32.367  -19.476 1.00 159.09 ? 52  VAL A CA  1 
ATOM   159   C C   . VAL A 1 52  ? -29.273  -32.882  -18.792 1.00 161.76 ? 52  VAL A C   1 
ATOM   160   O O   . VAL A 1 52  ? -29.353  -33.806  -17.981 1.00 161.09 ? 52  VAL A O   1 
ATOM   161   C CB  . VAL A 1 52  ? -30.639  -32.764  -20.978 1.00 163.70 ? 52  VAL A CB  1 
ATOM   162   C CG1 . VAL A 1 52  ? -30.132  -34.185  -21.227 1.00 163.60 ? 52  VAL A CG1 1 
ATOM   163   C CG2 . VAL A 1 52  ? -32.064  -32.599  -21.503 1.00 163.86 ? 52  VAL A CG2 1 
ATOM   164   N N   . ASN A 1 53  ? -28.107  -32.272  -19.105 1.00 157.33 ? 53  ASN A N   1 
ATOM   165   C CA  . ASN A 1 53  ? -26.807  -32.627  -18.518 1.00 156.35 ? 53  ASN A CA  1 
ATOM   166   C C   . ASN A 1 53  ? -26.765  -32.367  -17.009 1.00 157.75 ? 53  ASN A C   1 
ATOM   167   O O   . ASN A 1 53  ? -26.055  -33.072  -16.285 1.00 157.14 ? 53  ASN A O   1 
ATOM   168   C CB  . ASN A 1 53  ? -25.676  -31.880  -19.215 1.00 157.04 ? 53  ASN A CB  1 
ATOM   169   C CG  . ASN A 1 53  ? -25.242  -32.522  -20.502 1.00 179.08 ? 53  ASN A CG  1 
ATOM   170   O OD1 . ASN A 1 53  ? -25.917  -32.429  -21.537 1.00 172.56 ? 53  ASN A OD1 1 
ATOM   171   N ND2 . ASN A 1 53  ? -24.091  -33.176  -20.462 1.00 171.14 ? 53  ASN A ND2 1 
ATOM   172   N N   . SER A 1 54  ? -27.537  -31.365  -16.546 1.00 152.57 ? 54  SER A N   1 
ATOM   173   C CA  . SER A 1 54  ? -27.630  -30.988  -15.141 1.00 151.47 ? 54  SER A CA  1 
ATOM   174   C C   . SER A 1 54  ? -28.534  -31.918  -14.352 1.00 152.32 ? 54  SER A C   1 
ATOM   175   O O   . SER A 1 54  ? -28.242  -32.164  -13.186 1.00 152.14 ? 54  SER A O   1 
ATOM   176   C CB  . SER A 1 54  ? -28.096  -29.546  -14.997 1.00 155.43 ? 54  SER A CB  1 
ATOM   177   O OG  . SER A 1 54  ? -27.177  -28.664  -15.620 1.00 165.91 ? 54  SER A OG  1 
ATOM   178   N N   . VAL A 1 55  ? -29.623  -32.431  -14.967 1.00 146.45 ? 55  VAL A N   1 
ATOM   179   C CA  . VAL A 1 55  ? -30.542  -33.352  -14.290 1.00 144.71 ? 55  VAL A CA  1 
ATOM   180   C C   . VAL A 1 55  ? -29.915  -34.753  -14.162 1.00 147.84 ? 55  VAL A C   1 
ATOM   181   O O   . VAL A 1 55  ? -30.188  -35.454  -13.187 1.00 146.38 ? 55  VAL A O   1 
ATOM   182   C CB  . VAL A 1 55  ? -31.970  -33.367  -14.888 1.00 147.77 ? 55  VAL A CB  1 
ATOM   183   C CG1 . VAL A 1 55  ? -32.008  -34.018  -16.266 1.00 148.07 ? 55  VAL A CG1 1 
ATOM   184   C CG2 . VAL A 1 55  ? -32.957  -34.038  -13.941 1.00 146.31 ? 55  VAL A CG2 1 
ATOM   185   N N   . ILE A 1 56  ? -29.054  -35.137  -15.123 1.00 145.10 ? 56  ILE A N   1 
ATOM   186   C CA  . ILE A 1 56  ? -28.322  -36.405  -15.085 1.00 145.07 ? 56  ILE A CA  1 
ATOM   187   C C   . ILE A 1 56  ? -27.329  -36.295  -13.926 1.00 148.14 ? 56  ILE A C   1 
ATOM   188   O O   . ILE A 1 56  ? -27.229  -37.220  -13.118 1.00 147.10 ? 56  ILE A O   1 
ATOM   189   C CB  . ILE A 1 56  ? -27.648  -36.710  -16.457 1.00 149.20 ? 56  ILE A CB  1 
ATOM   190   C CG1 . ILE A 1 56  ? -28.711  -37.143  -17.488 1.00 149.60 ? 56  ILE A CG1 1 
ATOM   191   C CG2 . ILE A 1 56  ? -26.530  -37.767  -16.335 1.00 150.52 ? 56  ILE A CG2 1 
ATOM   192   C CD1 . ILE A 1 56  ? -28.333  -36.925  -18.933 1.00 157.95 ? 56  ILE A CD1 1 
ATOM   193   N N   . GLU A 1 57  ? -26.658  -35.125  -13.817 1.00 144.83 ? 57  GLU A N   1 
ATOM   194   C CA  . GLU A 1 57  ? -25.713  -34.785  -12.753 1.00 144.83 ? 57  GLU A CA  1 
ATOM   195   C C   . GLU A 1 57  ? -26.442  -34.799  -11.401 1.00 146.78 ? 57  GLU A C   1 
ATOM   196   O O   . GLU A 1 57  ? -25.927  -35.376  -10.443 1.00 146.62 ? 57  GLU A O   1 
ATOM   197   C CB  . GLU A 1 57  ? -25.074  -33.403  -13.026 1.00 146.74 ? 57  GLU A CB  1 
ATOM   198   C CG  . GLU A 1 57  ? -23.961  -33.007  -12.064 1.00 158.71 ? 57  GLU A CG  1 
ATOM   199   C CD  . GLU A 1 57  ? -24.391  -32.409  -10.736 1.00 185.02 ? 57  GLU A CD  1 
ATOM   200   O OE1 . GLU A 1 57  ? -25.131  -31.398  -10.746 1.00 177.34 ? 57  GLU A OE1 1 
ATOM   201   O OE2 . GLU A 1 57  ? -23.981  -32.949  -9.683  1.00 181.88 ? 57  GLU A OE2 1 
ATOM   202   N N   . LYS A 1 58  ? -27.645  -34.182  -11.343 1.00 141.32 ? 58  LYS A N   1 
ATOM   203   C CA  . LYS A 1 58  ? -28.479  -34.090  -10.142 1.00 139.51 ? 58  LYS A CA  1 
ATOM   204   C C   . LYS A 1 58  ? -28.962  -35.452  -9.661  1.00 139.70 ? 58  LYS A C   1 
ATOM   205   O O   . LYS A 1 58  ? -29.170  -35.617  -8.463  1.00 139.42 ? 58  LYS A O   1 
ATOM   206   C CB  . LYS A 1 58  ? -29.655  -33.120  -10.340 1.00 141.43 ? 58  LYS A CB  1 
ATOM   207   C CG  . LYS A 1 58  ? -30.011  -32.337  -9.079  1.00 151.54 ? 58  LYS A CG  1 
ATOM   208   C CD  . LYS A 1 58  ? -30.865  -31.114  -9.391  1.00 157.95 ? 58  LYS A CD  1 
ATOM   209   C CE  . LYS A 1 58  ? -30.903  -30.136  -8.244  1.00 165.83 ? 58  LYS A CE  1 
ATOM   210   N NZ  . LYS A 1 58  ? -31.508  -28.835  -8.644  1.00 174.49 ? 58  LYS A NZ  1 
ATOM   211   N N   . MET A 1 59  ? -29.121  -36.423  -10.577 1.00 133.00 ? 59  MET A N   1 
ATOM   212   C CA  . MET A 1 59  ? -29.524  -37.783  -10.228 1.00 130.73 ? 59  MET A CA  1 
ATOM   213   C C   . MET A 1 59  ? -28.305  -38.578  -9.754  1.00 135.21 ? 59  MET A C   1 
ATOM   214   O O   . MET A 1 59  ? -28.390  -39.280  -8.747  1.00 133.31 ? 59  MET A O   1 
ATOM   215   C CB  . MET A 1 59  ? -30.176  -38.478  -11.418 1.00 132.14 ? 59  MET A CB  1 
ATOM   216   C CG  . MET A 1 59  ? -31.568  -38.016  -11.695 1.00 134.30 ? 59  MET A CG  1 
ATOM   217   S SD  . MET A 1 59  ? -32.037  -38.432  -13.379 1.00 138.47 ? 59  MET A SD  1 
ATOM   218   C CE  . MET A 1 59  ? -32.756  -40.036  -13.128 1.00 133.64 ? 59  MET A CE  1 
ATOM   219   N N   . ASN A 1 60  ? -27.170  -38.451  -10.479 1.00 133.95 ? 60  ASN A N   1 
ATOM   220   C CA  . ASN A 1 60  ? -25.893  -39.102  -10.169 1.00 134.86 ? 60  ASN A CA  1 
ATOM   221   C C   . ASN A 1 60  ? -25.372  -38.653  -8.803  1.00 139.16 ? 60  ASN A C   1 
ATOM   222   O O   . ASN A 1 60  ? -24.869  -39.482  -8.044  1.00 139.10 ? 60  ASN A O   1 
ATOM   223   C CB  . ASN A 1 60  ? -24.852  -38.817  -11.264 1.00 137.15 ? 60  ASN A CB  1 
ATOM   224   C CG  . ASN A 1 60  ? -24.973  -39.671  -12.507 1.00 157.77 ? 60  ASN A CG  1 
ATOM   225   O OD1 . ASN A 1 60  ? -26.067  -40.034  -12.959 1.00 151.34 ? 60  ASN A OD1 1 
ATOM   226   N ND2 . ASN A 1 60  ? -23.838  -39.967  -13.119 1.00 149.06 ? 60  ASN A ND2 1 
ATOM   227   N N   . THR A 1 61  ? -25.520  -37.352  -8.479  1.00 135.85 ? 61  THR A N   1 
ATOM   228   C CA  . THR A 1 61  ? -25.101  -36.821  -7.185  1.00 136.44 ? 61  THR A CA  1 
ATOM   229   C C   . THR A 1 61  ? -26.090  -37.258  -6.100  1.00 139.03 ? 61  THR A C   1 
ATOM   230   O O   . THR A 1 61  ? -25.683  -37.413  -4.951  1.00 138.98 ? 61  THR A O   1 
ATOM   231   C CB  . THR A 1 61  ? -24.819  -35.305  -7.236  1.00 145.88 ? 61  THR A CB  1 
ATOM   232   O OG1 . THR A 1 61  ? -24.010  -34.958  -6.114  1.00 147.43 ? 61  THR A OG1 1 
ATOM   233   C CG2 . THR A 1 61  ? -26.085  -34.444  -7.261  1.00 143.30 ? 61  THR A CG2 1 
ATOM   234   N N   . GLN A 1 62  ? -27.369  -37.492  -6.476  1.00 134.22 ? 62  GLN A N   1 
ATOM   235   C CA  . GLN A 1 62  ? -28.412  -37.945  -5.557  1.00 132.79 ? 62  GLN A CA  1 
ATOM   236   C C   . GLN A 1 62  ? -28.247  -39.415  -5.224  1.00 138.15 ? 62  GLN A C   1 
ATOM   237   O O   . GLN A 1 62  ? -28.549  -39.804  -4.102  1.00 137.77 ? 62  GLN A O   1 
ATOM   238   C CB  . GLN A 1 62  ? -29.822  -37.661  -6.096  1.00 132.33 ? 62  GLN A CB  1 
ATOM   239   C CG  . GLN A 1 62  ? -30.945  -37.764  -5.053  1.00 139.30 ? 62  GLN A CG  1 
ATOM   240   C CD  . GLN A 1 62  ? -30.723  -36.911  -3.823  1.00 160.11 ? 62  GLN A CD  1 
ATOM   241   O OE1 . GLN A 1 62  ? -30.451  -35.708  -3.904  1.00 158.44 ? 62  GLN A OE1 1 
ATOM   242   N NE2 . GLN A 1 62  ? -30.845  -37.522  -2.653  1.00 151.66 ? 62  GLN A NE2 1 
ATOM   243   N N   . PHE A 1 63  ? -27.765  -40.230  -6.177  1.00 135.63 ? 63  PHE A N   1 
ATOM   244   C CA  . PHE A 1 63  ? -27.512  -41.650  -5.927  1.00 135.23 ? 63  PHE A CA  1 
ATOM   245   C C   . PHE A 1 63  ? -26.377  -41.781  -4.910  1.00 140.86 ? 63  PHE A C   1 
ATOM   246   O O   . PHE A 1 63  ? -26.446  -42.620  -4.010  1.00 139.25 ? 63  PHE A O   1 
ATOM   247   C CB  . PHE A 1 63  ? -27.195  -42.394  -7.238  1.00 137.27 ? 63  PHE A CB  1 
ATOM   248   C CG  . PHE A 1 63  ? -26.692  -43.810  -7.077  1.00 138.48 ? 63  PHE A CG  1 
ATOM   249   C CD1 . PHE A 1 63  ? -27.568  -44.850  -6.790  1.00 139.42 ? 63  PHE A CD1 1 
ATOM   250   C CD2 . PHE A 1 63  ? -25.346  -44.105  -7.229  1.00 142.31 ? 63  PHE A CD2 1 
ATOM   251   C CE1 . PHE A 1 63  ? -27.099  -46.156  -6.636  1.00 140.18 ? 63  PHE A CE1 1 
ATOM   252   C CE2 . PHE A 1 63  ? -24.878  -45.411  -7.075  1.00 145.04 ? 63  PHE A CE2 1 
ATOM   253   C CZ  . PHE A 1 63  ? -25.756  -46.428  -6.774  1.00 141.14 ? 63  PHE A CZ  1 
ATOM   254   N N   . THR A 1 64  ? -25.348  -40.913  -5.053  1.00 140.29 ? 64  THR A N   1 
ATOM   255   C CA  . THR A 1 64  ? -24.177  -40.815  -4.177  1.00 142.23 ? 64  THR A CA  1 
ATOM   256   C C   . THR A 1 64  ? -24.637  -40.312  -2.800  1.00 145.64 ? 64  THR A C   1 
ATOM   257   O O   . THR A 1 64  ? -24.152  -40.807  -1.779  1.00 146.00 ? 64  THR A O   1 
ATOM   258   C CB  . THR A 1 64  ? -23.101  -39.908  -4.817  1.00 153.96 ? 64  THR A CB  1 
ATOM   259   O OG1 . THR A 1 64  ? -22.935  -40.251  -6.197  1.00 151.56 ? 64  THR A OG1 1 
ATOM   260   C CG2 . THR A 1 64  ? -21.755  -39.996  -4.102  1.00 156.00 ? 64  THR A CG2 1 
ATOM   261   N N   . ALA A 1 65  ? -25.592  -39.350  -2.789  1.00 140.93 ? 65  ALA A N   1 
ATOM   262   C CA  . ALA A 1 65  ? -26.194  -38.783  -1.579  1.00 140.40 ? 65  ALA A CA  1 
ATOM   263   C C   . ALA A 1 65  ? -26.994  -39.863  -0.844  1.00 141.95 ? 65  ALA A C   1 
ATOM   264   O O   . ALA A 1 65  ? -26.901  -39.943  0.383   1.00 142.68 ? 65  ALA A O   1 
ATOM   265   C CB  . ALA A 1 65  ? -27.083  -37.600  -1.925  1.00 140.51 ? 65  ALA A CB  1 
ATOM   266   N N   . VAL A 1 66  ? -27.677  -40.768  -1.607  1.00 134.73 ? 66  VAL A N   1 
ATOM   267   C CA  . VAL A 1 66  ? -28.401  -41.923  -1.052  1.00 131.09 ? 66  VAL A CA  1 
ATOM   268   C C   . VAL A 1 66  ? -27.354  -43.050  -0.756  1.00 132.62 ? 66  VAL A C   1 
ATOM   269   O O   . VAL A 1 66  ? -27.424  -44.171  -1.266  1.00 130.58 ? 66  VAL A O   1 
ATOM   270   C CB  . VAL A 1 66  ? -29.665  -42.369  -1.869  1.00 132.17 ? 66  VAL A CB  1 
ATOM   271   C CG1 . VAL A 1 66  ? -30.469  -43.424  -1.116  1.00 129.44 ? 66  VAL A CG1 1 
ATOM   272   C CG2 . VAL A 1 66  ? -30.570  -41.182  -2.187  1.00 131.27 ? 66  VAL A CG2 1 
ATOM   273   N N   . GLY A 1 67  ? -26.357  -42.669  0.038   1.00 129.32 ? 67  GLY A N   1 
ATOM   274   C CA  . GLY A 1 67  ? -25.291  -43.521  0.534   1.00 129.73 ? 67  GLY A CA  1 
ATOM   275   C C   . GLY A 1 67  ? -25.585  -43.785  1.992   1.00 132.17 ? 67  GLY A C   1 
ATOM   276   O O   . GLY A 1 67  ? -24.678  -43.788  2.832   1.00 133.52 ? 67  GLY A O   1 
ATOM   277   N N   . LYS A 1 68  ? -26.895  -43.953  2.290   1.00 125.51 ? 68  LYS A N   1 
ATOM   278   C CA  . LYS A 1 68  ? -27.461  -44.217  3.609   1.00 123.70 ? 68  LYS A CA  1 
ATOM   279   C C   . LYS A 1 68  ? -27.444  -45.723  3.898   1.00 126.87 ? 68  LYS A C   1 
ATOM   280   O O   . LYS A 1 68  ? -28.457  -46.418  3.733   1.00 123.16 ? 68  LYS A O   1 
ATOM   281   C CB  . LYS A 1 68  ? -28.872  -43.615  3.728   1.00 122.62 ? 68  LYS A CB  1 
ATOM   282   C CG  . LYS A 1 68  ? -28.894  -42.091  3.810   1.00 131.36 ? 68  LYS A CG  1 
ATOM   283   C CD  . LYS A 1 68  ? -28.831  -41.583  5.247   1.00 139.68 ? 68  LYS A CD  1 
ATOM   284   C CE  . LYS A 1 68  ? -28.962  -40.082  5.336   1.00 148.01 ? 68  LYS A CE  1 
ATOM   285   N NZ  . LYS A 1 68  ? -29.216  -39.639  6.732   1.00 156.66 ? 68  LYS A NZ  1 
ATOM   286   N N   . GLU A 1 69  ? -26.244  -46.215  4.289   1.00 139.40 ? 69  GLU A N   1 
ATOM   287   C CA  . GLU A 1 69  ? -25.928  -47.605  4.631   1.00 158.47 ? 69  GLU A CA  1 
ATOM   288   C C   . GLU A 1 69  ? -25.140  -47.650  5.942   1.00 187.62 ? 69  GLU A C   1 
ATOM   289   O O   . GLU A 1 69  ? -24.235  -46.841  6.154   1.00 148.39 ? 69  GLU A O   1 
ATOM   290   C CB  . GLU A 1 69  ? -25.110  -48.271  3.513   1.00 159.43 ? 69  GLU A CB  1 
ATOM   291   C CG  . GLU A 1 69  ? -25.899  -48.547  2.245   1.00 168.46 ? 69  GLU A CG  1 
ATOM   292   C CD  . GLU A 1 69  ? -25.076  -49.022  1.064   1.00 185.42 ? 69  GLU A CD  1 
ATOM   293   O OE1 . GLU A 1 69  ? -25.519  -49.972  0.379   1.00 167.67 ? 69  GLU A OE1 1 
ATOM   294   O OE2 . GLU A 1 69  ? -23.998  -48.436  0.810   1.00 182.98 ? 69  GLU A OE2 1 
ATOM   295   N N   . LYS A 1 83  ? -32.766  -58.000  0.766   1.00 162.43 ? 83  LYS A N   1 
ATOM   296   C CA  . LYS A 1 83  ? -33.650  -57.192  1.608   1.00 162.37 ? 83  LYS A CA  1 
ATOM   297   C C   . LYS A 1 83  ? -32.904  -56.020  2.247   1.00 168.04 ? 83  LYS A C   1 
ATOM   298   O O   . LYS A 1 83  ? -33.482  -54.939  2.408   1.00 167.15 ? 83  LYS A O   1 
ATOM   299   C CB  . LYS A 1 83  ? -34.322  -58.055  2.688   1.00 163.72 ? 83  LYS A CB  1 
ATOM   300   C CG  . LYS A 1 83  ? -35.717  -57.575  3.076   1.00 161.89 ? 83  LYS A CG  1 
ATOM   301   C CD  . LYS A 1 83  ? -36.300  -58.388  4.232   1.00 159.91 ? 83  LYS A CD  1 
ATOM   302   C CE  . LYS A 1 83  ? -37.731  -58.028  4.546   1.00 153.14 ? 83  LYS A CE  1 
ATOM   303   N NZ  . LYS A 1 83  ? -38.669  -58.544  3.515   1.00 153.64 ? 83  LYS A NZ  1 
ATOM   304   N N   . VAL A 1 84  ? -31.624  -56.248  2.616   1.00 166.43 ? 84  VAL A N   1 
ATOM   305   C CA  . VAL A 1 84  ? -30.726  -55.266  3.236   1.00 167.10 ? 84  VAL A CA  1 
ATOM   306   C C   . VAL A 1 84  ? -30.467  -54.136  2.220   1.00 173.11 ? 84  VAL A C   1 
ATOM   307   O O   . VAL A 1 84  ? -30.993  -53.033  2.396   1.00 172.52 ? 84  VAL A O   1 
ATOM   308   C CB  . VAL A 1 84  ? -29.407  -55.924  3.757   1.00 170.80 ? 84  VAL A CB  1 
ATOM   309   C CG1 . VAL A 1 84  ? -28.497  -54.900  4.432   1.00 170.74 ? 84  VAL A CG1 1 
ATOM   310   C CG2 . VAL A 1 84  ? -29.695  -57.088  4.703   1.00 170.35 ? 84  VAL A CG2 1 
ATOM   311   N N   . ASP A 1 85  ? -29.713  -54.440  1.135   1.00 171.33 ? 85  ASP A N   1 
ATOM   312   C CA  . ASP A 1 85  ? -29.402  -53.504  0.048   1.00 171.88 ? 85  ASP A CA  1 
ATOM   313   C C   . ASP A 1 85  ? -30.661  -53.157  -0.764  1.00 177.66 ? 85  ASP A C   1 
ATOM   314   O O   . ASP A 1 85  ? -30.709  -52.081  -1.369  1.00 177.24 ? 85  ASP A O   1 
ATOM   315   C CB  . ASP A 1 85  ? -28.298  -54.064  -0.875  1.00 173.58 ? 85  ASP A CB  1 
ATOM   316   C CG  . ASP A 1 85  ? -26.871  -53.801  -0.417  1.00 181.19 ? 85  ASP A CG  1 
ATOM   317   O OD1 . ASP A 1 85  ? -26.144  -54.783  -0.143  1.00 181.76 ? 85  ASP A OD1 1 
ATOM   318   O OD2 . ASP A 1 85  ? -26.464  -52.620  -0.392  1.00 184.12 ? 85  ASP A OD2 1 
ATOM   319   N N   . ASP A 1 86  ? -31.682  -54.060  -0.758  1.00 175.61 ? 86  ASP A N   1 
ATOM   320   C CA  . ASP A 1 86  ? -32.969  -53.885  -1.448  1.00 176.05 ? 86  ASP A CA  1 
ATOM   321   C C   . ASP A 1 86  ? -33.793  -52.744  -0.840  1.00 180.12 ? 86  ASP A C   1 
ATOM   322   O O   . ASP A 1 86  ? -34.562  -52.106  -1.564  1.00 179.81 ? 86  ASP A O   1 
ATOM   323   C CB  . ASP A 1 86  ? -33.776  -55.192  -1.470  1.00 178.21 ? 86  ASP A CB  1 
ATOM   324   C CG  . ASP A 1 86  ? -34.983  -55.150  -2.386  1.00 190.45 ? 86  ASP A CG  1 
ATOM   325   O OD1 . ASP A 1 86  ? -36.074  -54.763  -1.912  1.00 191.18 ? 86  ASP A OD1 1 
ATOM   326   O OD2 . ASP A 1 86  ? -34.835  -55.494  -3.578  1.00 197.35 ? 86  ASP A OD2 1 
ATOM   327   N N   . GLY A 1 87  ? -33.619  -52.505  0.467   1.00 176.45 ? 87  GLY A N   1 
ATOM   328   C CA  . GLY A 1 87  ? -34.262  -51.417  1.200   1.00 176.04 ? 87  GLY A CA  1 
ATOM   329   C C   . GLY A 1 87  ? -33.932  -50.070  0.583   1.00 179.44 ? 87  GLY A C   1 
ATOM   330   O O   . GLY A 1 87  ? -34.841  -49.329  0.199   1.00 178.91 ? 87  GLY A O   1 
ATOM   331   N N   . PHE A 1 88  ? -32.615  -49.785  0.417   1.00 152.30 ? 88  PHE A N   1 
ATOM   332   C CA  . PHE A 1 88  ? -32.075  -48.577  -0.219  1.00 151.82 ? 88  PHE A CA  1 
ATOM   333   C C   . PHE A 1 88  ? -32.478  -48.512  -1.702  1.00 153.59 ? 88  PHE A C   1 
ATOM   334   O O   . PHE A 1 88  ? -32.810  -47.435  -2.200  1.00 153.24 ? 88  PHE A O   1 
ATOM   335   C CB  . PHE A 1 88  ? -30.529  -48.517  -0.061  1.00 153.63 ? 88  PHE A CB  1 
ATOM   336   C CG  . PHE A 1 88  ? -29.724  -48.149  -1.298  1.00 155.45 ? 88  PHE A CG  1 
ATOM   337   C CD1 . PHE A 1 88  ? -29.077  -49.127  -2.045  1.00 158.56 ? 88  PHE A CD1 1 
ATOM   338   C CD2 . PHE A 1 88  ? -29.613  -46.823  -1.710  1.00 157.61 ? 88  PHE A CD2 1 
ATOM   339   C CE1 . PHE A 1 88  ? -28.347  -48.786  -3.188  1.00 159.64 ? 88  PHE A CE1 1 
ATOM   340   C CE2 . PHE A 1 88  ? -28.898  -46.488  -2.862  1.00 160.30 ? 88  PHE A CE2 1 
ATOM   341   C CZ  . PHE A 1 88  ? -28.260  -47.469  -3.584  1.00 158.57 ? 88  PHE A CZ  1 
ATOM   342   N N   . LEU A 1 89  ? -32.386  -49.656  -2.405  1.00 148.42 ? 89  LEU A N   1 
ATOM   343   C CA  . LEU A 1 89  ? -32.682  -49.789  -3.828  1.00 147.80 ? 89  LEU A CA  1 
ATOM   344   C C   . LEU A 1 89  ? -34.025  -49.184  -4.199  1.00 150.20 ? 89  LEU A C   1 
ATOM   345   O O   . LEU A 1 89  ? -34.062  -48.325  -5.070  1.00 149.71 ? 89  LEU A O   1 
ATOM   346   C CB  . LEU A 1 89  ? -32.572  -51.256  -4.276  1.00 147.84 ? 89  LEU A CB  1 
ATOM   347   C CG  . LEU A 1 89  ? -31.541  -51.555  -5.374  1.00 152.88 ? 89  LEU A CG  1 
ATOM   348   C CD1 . LEU A 1 89  ? -30.120  -51.607  -4.816  1.00 153.04 ? 89  LEU A CD1 1 
ATOM   349   C CD2 . LEU A 1 89  ? -31.846  -52.868  -6.057  1.00 155.51 ? 89  LEU A CD2 1 
ATOM   350   N N   . ASP A 1 90  ? -35.097  -49.551  -3.474  1.00 146.26 ? 90  ASP A N   1 
ATOM   351   C CA  . ASP A 1 90  ? -36.458  -49.039  -3.677  1.00 146.27 ? 90  ASP A CA  1 
ATOM   352   C C   . ASP A 1 90  ? -36.554  -47.515  -3.504  1.00 149.90 ? 90  ASP A C   1 
ATOM   353   O O   . ASP A 1 90  ? -37.311  -46.866  -4.233  1.00 148.97 ? 90  ASP A O   1 
ATOM   354   C CB  . ASP A 1 90  ? -37.441  -49.737  -2.721  1.00 148.16 ? 90  ASP A CB  1 
ATOM   355   C CG  . ASP A 1 90  ? -37.628  -51.221  -2.974  1.00 160.10 ? 90  ASP A CG  1 
ATOM   356   O OD1 . ASP A 1 90  ? -38.006  -51.588  -4.108  1.00 161.16 ? 90  ASP A OD1 1 
ATOM   357   O OD2 . ASP A 1 90  ? -37.475  -52.009  -2.015  1.00 166.05 ? 90  ASP A OD2 1 
ATOM   358   N N   . ILE A 1 91  ? -35.776  -46.955  -2.545  1.00 146.83 ? 91  ILE A N   1 
ATOM   359   C CA  . ILE A 1 91  ? -35.724  -45.526  -2.207  1.00 146.75 ? 91  ILE A CA  1 
ATOM   360   C C   . ILE A 1 91  ? -35.200  -44.689  -3.382  1.00 151.08 ? 91  ILE A C   1 
ATOM   361   O O   . ILE A 1 91  ? -35.921  -43.814  -3.864  1.00 150.99 ? 91  ILE A O   1 
ATOM   362   C CB  . ILE A 1 91  ? -34.920  -45.271  -0.898  1.00 149.40 ? 91  ILE A CB  1 
ATOM   363   C CG1 . ILE A 1 91  ? -35.500  -46.058  0.302   1.00 149.35 ? 91  ILE A CG1 1 
ATOM   364   C CG2 . ILE A 1 91  ? -34.822  -43.771  -0.600  1.00 150.47 ? 91  ILE A CG2 1 
ATOM   365   C CD1 . ILE A 1 91  ? -34.513  -46.303  1.472   1.00 153.64 ? 91  ILE A CD1 1 
ATOM   366   N N   . TRP A 1 92  ? -33.945  -44.957  -3.817  1.00 147.51 ? 92  TRP A N   1 
ATOM   367   C CA  . TRP A 1 92  ? -33.252  -44.287  -4.926  1.00 147.20 ? 92  TRP A CA  1 
ATOM   368   C C   . TRP A 1 92  ? -34.021  -44.346  -6.249  1.00 151.39 ? 92  TRP A C   1 
ATOM   369   O O   . TRP A 1 92  ? -34.115  -43.331  -6.933  1.00 150.58 ? 92  TRP A O   1 
ATOM   370   C CB  . TRP A 1 92  ? -31.817  -44.839  -5.087  1.00 145.65 ? 92  TRP A CB  1 
ATOM   371   C CG  . TRP A 1 92  ? -31.289  -44.837  -6.497  1.00 146.59 ? 92  TRP A CG  1 
ATOM   372   C CD1 . TRP A 1 92  ? -31.072  -45.924  -7.291  1.00 149.66 ? 92  TRP A CD1 1 
ATOM   373   C CD2 . TRP A 1 92  ? -30.947  -43.689  -7.286  1.00 146.07 ? 92  TRP A CD2 1 
ATOM   374   N NE1 . TRP A 1 92  ? -30.593  -45.528  -8.517  1.00 149.15 ? 92  TRP A NE1 1 
ATOM   375   C CE2 . TRP A 1 92  ? -30.529  -44.160  -8.550  1.00 150.20 ? 92  TRP A CE2 1 
ATOM   376   C CE3 . TRP A 1 92  ? -30.972  -42.303  -7.055  1.00 146.88 ? 92  TRP A CE3 1 
ATOM   377   C CZ2 . TRP A 1 92  ? -30.119  -43.297  -9.572  1.00 149.25 ? 92  TRP A CZ2 1 
ATOM   378   C CZ3 . TRP A 1 92  ? -30.583  -41.450  -8.075  1.00 147.98 ? 92  TRP A CZ3 1 
ATOM   379   C CH2 . TRP A 1 92  ? -30.152  -41.947  -9.312  1.00 148.72 ? 92  TRP A CH2 1 
ATOM   380   N N   . THR A 1 93  ? -34.552  -45.530  -6.605  1.00 148.81 ? 93  THR A N   1 
ATOM   381   C CA  . THR A 1 93  ? -35.311  -45.771  -7.840  1.00 149.06 ? 93  THR A CA  1 
ATOM   382   C C   . THR A 1 93  ? -36.546  -44.874  -7.951  1.00 153.11 ? 93  THR A C   1 
ATOM   383   O O   . THR A 1 93  ? -36.906  -44.491  -9.064  1.00 152.78 ? 93  THR A O   1 
ATOM   384   C CB  . THR A 1 93  ? -35.644  -47.249  -7.996  1.00 158.63 ? 93  THR A CB  1 
ATOM   385   O OG1 . THR A 1 93  ? -36.380  -47.676  -6.849  1.00 161.45 ? 93  THR A OG1 1 
ATOM   386   C CG2 . THR A 1 93  ? -34.403  -48.104  -8.163  1.00 156.09 ? 93  THR A CG2 1 
ATOM   387   N N   . TYR A 1 94  ? -37.176  -44.519  -6.810  1.00 149.60 ? 94  TYR A N   1 
ATOM   388   C CA  . TYR A 1 94  ? -38.317  -43.606  -6.812  1.00 149.68 ? 94  TYR A CA  1 
ATOM   389   C C   . TYR A 1 94  ? -37.830  -42.162  -6.867  1.00 151.75 ? 94  TYR A C   1 
ATOM   390   O O   . TYR A 1 94  ? -38.466  -41.347  -7.530  1.00 151.09 ? 94  TYR A O   1 
ATOM   391   C CB  . TYR A 1 94  ? -39.244  -43.829  -5.610  1.00 151.86 ? 94  TYR A CB  1 
ATOM   392   C CG  . TYR A 1 94  ? -40.497  -42.974  -5.640  1.00 155.24 ? 94  TYR A CG  1 
ATOM   393   C CD1 . TYR A 1 94  ? -41.516  -43.224  -6.558  1.00 157.73 ? 94  TYR A CD1 1 
ATOM   394   C CD2 . TYR A 1 94  ? -40.673  -41.927  -4.739  1.00 156.64 ? 94  TYR A CD2 1 
ATOM   395   C CE1 . TYR A 1 94  ? -42.673  -42.445  -6.585  1.00 159.85 ? 94  TYR A CE1 1 
ATOM   396   C CE2 . TYR A 1 94  ? -41.831  -41.148  -4.749  1.00 158.47 ? 94  TYR A CE2 1 
ATOM   397   C CZ  . TYR A 1 94  ? -42.829  -41.410  -5.675  1.00 167.84 ? 94  TYR A CZ  1 
ATOM   398   O OH  . TYR A 1 94  ? -43.974  -40.643  -5.680  1.00 170.55 ? 94  TYR A OH  1 
ATOM   399   N N   . ASN A 1 95  ? -36.701  -41.854  -6.186  1.00 147.22 ? 95  ASN A N   1 
ATOM   400   C CA  . ASN A 1 95  ? -36.086  -40.521  -6.159  1.00 146.27 ? 95  ASN A CA  1 
ATOM   401   C C   . ASN A 1 95  ? -35.553  -40.129  -7.546  1.00 148.02 ? 95  ASN A C   1 
ATOM   402   O O   . ASN A 1 95  ? -35.627  -38.958  -7.926  1.00 147.38 ? 95  ASN A O   1 
ATOM   403   C CB  . ASN A 1 95  ? -34.970  -40.460  -5.109  1.00 146.92 ? 95  ASN A CB  1 
ATOM   404   C CG  . ASN A 1 95  ? -34.768  -39.109  -4.444  1.00 168.35 ? 95  ASN A CG  1 
ATOM   405   O OD1 . ASN A 1 95  ? -35.533  -38.151  -4.626  1.00 161.86 ? 95  ASN A OD1 1 
ATOM   406   N ND2 . ASN A 1 95  ? -33.742  -39.015  -3.617  1.00 160.31 ? 95  ASN A ND2 1 
ATOM   407   N N   . ALA A 1 96  ? -35.039  -41.117  -8.303  1.00 143.02 ? 96  ALA A N   1 
ATOM   408   C CA  . ALA A 1 96  ? -34.528  -40.933  -9.659  1.00 142.03 ? 96  ALA A CA  1 
ATOM   409   C C   . ALA A 1 96  ? -35.698  -40.704  -10.606 1.00 144.73 ? 96  ALA A C   1 
ATOM   410   O O   . ALA A 1 96  ? -35.611  -39.836  -11.473 1.00 144.34 ? 96  ALA A O   1 
ATOM   411   C CB  . ALA A 1 96  ? -33.734  -42.153  -10.091 1.00 142.87 ? 96  ALA A CB  1 
ATOM   412   N N   . GLU A 1 97  ? -36.806  -41.455  -10.416 1.00 140.47 ? 97  GLU A N   1 
ATOM   413   C CA  . GLU A 1 97  ? -38.028  -41.318  -11.209 1.00 140.24 ? 97  GLU A CA  1 
ATOM   414   C C   . GLU A 1 97  ? -38.670  -39.962  -10.929 1.00 143.93 ? 97  GLU A C   1 
ATOM   415   O O   . GLU A 1 97  ? -39.100  -39.293  -11.866 1.00 143.00 ? 97  GLU A O   1 
ATOM   416   C CB  . GLU A 1 97  ? -39.007  -42.472  -10.928 1.00 141.88 ? 97  GLU A CB  1 
ATOM   417   C CG  . GLU A 1 97  ? -38.752  -43.691  -11.805 1.00 151.22 ? 97  GLU A CG  1 
ATOM   418   C CD  . GLU A 1 97  ? -39.552  -44.944  -11.510 1.00 165.22 ? 97  GLU A CD  1 
ATOM   419   O OE1 . GLU A 1 97  ? -40.280  -45.405  -12.420 1.00 144.02 ? 97  GLU A OE1 1 
ATOM   420   O OE2 . GLU A 1 97  ? -39.377  -45.522  -10.413 1.00 162.79 ? 97  GLU A OE2 1 
ATOM   421   N N   . LEU A 1 98  ? -38.657  -39.534  -9.649  1.00 140.98 ? 98  LEU A N   1 
ATOM   422   C CA  . LEU A 1 98  ? -39.193  -38.259  -9.157  1.00 141.00 ? 98  LEU A CA  1 
ATOM   423   C C   . LEU A 1 98  ? -38.575  -37.057  -9.882  1.00 143.96 ? 98  LEU A C   1 
ATOM   424   O O   . LEU A 1 98  ? -39.317  -36.177  -10.317 1.00 143.78 ? 98  LEU A O   1 
ATOM   425   C CB  . LEU A 1 98  ? -38.956  -38.146  -7.640  1.00 141.20 ? 98  LEU A CB  1 
ATOM   426   C CG  . LEU A 1 98  ? -39.865  -37.204  -6.858  1.00 146.46 ? 98  LEU A CG  1 
ATOM   427   C CD1 . LEU A 1 98  ? -40.326  -37.859  -5.579  1.00 147.09 ? 98  LEU A CD1 1 
ATOM   428   C CD2 . LEU A 1 98  ? -39.163  -35.884  -6.551  1.00 148.63 ? 98  LEU A CD2 1 
ATOM   429   N N   . LEU A 1 99  ? -37.227  -37.031  -10.017 1.00 139.24 ? 99  LEU A N   1 
ATOM   430   C CA  . LEU A 1 99  ? -36.489  -35.956  -10.685 1.00 138.11 ? 99  LEU A CA  1 
ATOM   431   C C   . LEU A 1 99  ? -36.843  -35.827  -12.162 1.00 143.65 ? 99  LEU A C   1 
ATOM   432   O O   . LEU A 1 99  ? -36.893  -34.708  -12.675 1.00 143.61 ? 99  LEU A O   1 
ATOM   433   C CB  . LEU A 1 99  ? -34.977  -36.121  -10.505 1.00 137.11 ? 99  LEU A CB  1 
ATOM   434   C CG  . LEU A 1 99  ? -34.315  -35.176  -9.503  1.00 140.69 ? 99  LEU A CG  1 
ATOM   435   C CD1 . LEU A 1 99  ? -33.003  -35.745  -9.006  1.00 140.29 ? 99  LEU A CD1 1 
ATOM   436   C CD2 . LEU A 1 99  ? -34.099  -33.779  -10.097 1.00 141.92 ? 99  LEU A CD2 1 
ATOM   437   N N   . VAL A 1 100 ? -37.110  -36.967  -12.834 1.00 140.74 ? 100 VAL A N   1 
ATOM   438   C CA  . VAL A 1 100 ? -37.506  -37.029  -14.245 1.00 140.58 ? 100 VAL A CA  1 
ATOM   439   C C   . VAL A 1 100 ? -38.918  -36.437  -14.413 1.00 144.13 ? 100 VAL A C   1 
ATOM   440   O O   . VAL A 1 100 ? -39.096  -35.542  -15.240 1.00 143.18 ? 100 VAL A O   1 
ATOM   441   C CB  . VAL A 1 100 ? -37.352  -38.465  -14.832 1.00 145.04 ? 100 VAL A CB  1 
ATOM   442   C CG1 . VAL A 1 100 ? -38.064  -38.617  -16.178 1.00 145.24 ? 100 VAL A CG1 1 
ATOM   443   C CG2 . VAL A 1 100 ? -35.880  -38.847  -14.962 1.00 144.51 ? 100 VAL A CG2 1 
ATOM   444   N N   . LEU A 1 101 ? -39.896  -36.900  -13.593 1.00 141.15 ? 101 LEU A N   1 
ATOM   445   C CA  . LEU A 1 101 ? -41.293  -36.424  -13.597 1.00 141.46 ? 101 LEU A CA  1 
ATOM   446   C C   . LEU A 1 101 ? -41.357  -34.929  -13.259 1.00 144.95 ? 101 LEU A C   1 
ATOM   447   O O   . LEU A 1 101 ? -42.218  -34.217  -13.777 1.00 144.37 ? 101 LEU A O   1 
ATOM   448   C CB  . LEU A 1 101 ? -42.164  -37.216  -12.589 1.00 142.20 ? 101 LEU A CB  1 
ATOM   449   C CG  . LEU A 1 101 ? -42.208  -38.750  -12.704 1.00 146.89 ? 101 LEU A CG  1 
ATOM   450   C CD1 . LEU A 1 101 ? -42.436  -39.387  -11.351 1.00 147.24 ? 101 LEU A CD1 1 
ATOM   451   C CD2 . LEU A 1 101 ? -43.275  -39.217  -13.674 1.00 149.51 ? 101 LEU A CD2 1 
ATOM   452   N N   . LEU A 1 102 ? -40.431  -34.469  -12.396 1.00 141.66 ? 102 LEU A N   1 
ATOM   453   C CA  . LEU A 1 102 ? -40.317  -33.086  -11.951 1.00 141.64 ? 102 LEU A CA  1 
ATOM   454   C C   . LEU A 1 102 ? -39.664  -32.187  -13.000 1.00 145.95 ? 102 LEU A C   1 
ATOM   455   O O   . LEU A 1 102 ? -40.163  -31.083  -13.231 1.00 146.26 ? 102 LEU A O   1 
ATOM   456   C CB  . LEU A 1 102 ? -39.532  -33.015  -10.643 1.00 141.55 ? 102 LEU A CB  1 
ATOM   457   C CG  . LEU A 1 102 ? -40.041  -32.017  -9.641  1.00 146.85 ? 102 LEU A CG  1 
ATOM   458   C CD1 . LEU A 1 102 ? -40.338  -32.695  -8.333  1.00 147.77 ? 102 LEU A CD1 1 
ATOM   459   C CD2 . LEU A 1 102 ? -39.046  -30.882  -9.456  1.00 148.91 ? 102 LEU A CD2 1 
ATOM   460   N N   . GLU A 1 103 ? -38.545  -32.629  -13.615 1.00 141.85 ? 103 GLU A N   1 
ATOM   461   C CA  . GLU A 1 103 ? -37.870  -31.813  -14.628 1.00 140.87 ? 103 GLU A CA  1 
ATOM   462   C C   . GLU A 1 103 ? -38.635  -31.779  -15.962 1.00 145.53 ? 103 GLU A C   1 
ATOM   463   O O   . GLU A 1 103 ? -38.505  -30.793  -16.690 1.00 144.11 ? 103 GLU A O   1 
ATOM   464   C CB  . GLU A 1 103 ? -36.401  -32.203  -14.802 1.00 141.49 ? 103 GLU A CB  1 
ATOM   465   C CG  . GLU A 1 103 ? -35.505  -31.576  -13.745 1.00 151.46 ? 103 GLU A CG  1 
ATOM   466   C CD  . GLU A 1 103 ? -34.986  -30.190  -14.074 1.00 173.00 ? 103 GLU A CD  1 
ATOM   467   O OE1 . GLU A 1 103 ? -33.795  -30.068  -14.444 1.00 162.91 ? 103 GLU A OE1 1 
ATOM   468   O OE2 . GLU A 1 103 ? -35.767  -29.220  -13.945 1.00 170.40 ? 103 GLU A OE2 1 
ATOM   469   N N   . ASN A 1 104 ? -39.479  -32.811  -16.246 1.00 168.48 ? 104 ASN A N   1 
ATOM   470   C CA  . ASN A 1 104 ? -40.347  -32.870  -17.433 1.00 168.55 ? 104 ASN A CA  1 
ATOM   471   C C   . ASN A 1 104 ? -41.503  -31.868  -17.281 1.00 173.80 ? 104 ASN A C   1 
ATOM   472   O O   . ASN A 1 104 ? -41.898  -31.228  -18.259 1.00 173.45 ? 104 ASN A O   1 
ATOM   473   C CB  . ASN A 1 104 ? -40.896  -34.285  -17.664 1.00 167.16 ? 104 ASN A CB  1 
ATOM   474   C CG  . ASN A 1 104 ? -39.942  -35.242  -18.342 1.00 181.46 ? 104 ASN A CG  1 
ATOM   475   O OD1 . ASN A 1 104 ? -39.029  -34.856  -19.081 1.00 173.58 ? 104 ASN A OD1 1 
ATOM   476   N ND2 . ASN A 1 104 ? -40.166  -36.528  -18.140 1.00 172.62 ? 104 ASN A ND2 1 
ATOM   477   N N   . GLU A 1 105 ? -42.024  -31.722  -16.043 1.00 171.22 ? 105 GLU A N   1 
ATOM   478   C CA  . GLU A 1 105 ? -43.079  -30.768  -15.698 1.00 171.49 ? 105 GLU A CA  1 
ATOM   479   C C   . GLU A 1 105 ? -42.536  -29.349  -15.922 1.00 176.48 ? 105 GLU A C   1 
ATOM   480   O O   . GLU A 1 105 ? -43.242  -28.509  -16.473 1.00 175.55 ? 105 GLU A O   1 
ATOM   481   C CB  . GLU A 1 105 ? -43.505  -30.960  -14.232 1.00 173.01 ? 105 GLU A CB  1 
ATOM   482   C CG  . GLU A 1 105 ? -44.893  -30.436  -13.909 1.00 182.27 ? 105 GLU A CG  1 
ATOM   483   C CD  . GLU A 1 105 ? -46.009  -31.433  -14.153 1.00 197.49 ? 105 GLU A CD  1 
ATOM   484   O OE1 . GLU A 1 105 ? -46.213  -32.318  -13.291 1.00 184.26 ? 105 GLU A OE1 1 
ATOM   485   O OE2 . GLU A 1 105 ? -46.671  -31.336  -15.211 1.00 191.20 ? 105 GLU A OE2 1 
ATOM   486   N N   . ARG A 1 106 ? -41.256  -29.117  -15.542 1.00 174.62 ? 106 ARG A N   1 
ATOM   487   C CA  . ARG A 1 106 ? -40.545  -27.845  -15.693 1.00 175.14 ? 106 ARG A CA  1 
ATOM   488   C C   . ARG A 1 106 ? -40.155  -27.531  -17.139 1.00 180.90 ? 106 ARG A C   1 
ATOM   489   O O   . ARG A 1 106 ? -40.085  -26.355  -17.487 1.00 180.27 ? 106 ARG A O   1 
ATOM   490   C CB  . ARG A 1 106 ? -39.313  -27.781  -14.775 1.00 175.34 ? 106 ARG A CB  1 
ATOM   491   C CG  . ARG A 1 106 ? -39.638  -27.324  -13.361 1.00 187.61 ? 106 ARG A CG  1 
ATOM   492   C CD  . ARG A 1 106 ? -38.408  -26.840  -12.615 1.00 200.45 ? 106 ARG A CD  1 
ATOM   493   N NE  . ARG A 1 106 ? -37.693  -27.936  -11.959 1.00 213.58 ? 106 ARG A NE  1 
ATOM   494   C CZ  . ARG A 1 106 ? -36.646  -27.778  -11.154 1.00 232.84 ? 106 ARG A CZ  1 
ATOM   495   N NH1 . ARG A 1 106 ? -36.173  -26.563  -10.897 1.00 221.52 ? 106 ARG A NH1 1 
ATOM   496   N NH2 . ARG A 1 106 ? -36.063  -28.832  -10.599 1.00 222.96 ? 106 ARG A NH2 1 
ATOM   497   N N   . THR A 1 107 ? -39.886  -28.565  -17.969 1.00 179.36 ? 107 THR A N   1 
ATOM   498   C CA  . THR A 1 107 ? -39.511  -28.414  -19.385 1.00 180.14 ? 107 THR A CA  1 
ATOM   499   C C   . THR A 1 107 ? -40.713  -27.952  -20.221 1.00 185.47 ? 107 THR A C   1 
ATOM   500   O O   . THR A 1 107 ? -40.597  -26.976  -20.965 1.00 185.12 ? 107 THR A O   1 
ATOM   501   C CB  . THR A 1 107 ? -38.878  -29.716  -19.923 1.00 190.15 ? 107 THR A CB  1 
ATOM   502   O OG1 . THR A 1 107 ? -37.720  -30.034  -19.149 1.00 190.99 ? 107 THR A OG1 1 
ATOM   503   C CG2 . THR A 1 107 ? -38.493  -29.627  -21.400 1.00 189.00 ? 107 THR A CG2 1 
ATOM   504   N N   . LEU A 1 108 ? -41.858  -28.657  -20.092 1.00 183.11 ? 108 LEU A N   1 
ATOM   505   C CA  . LEU A 1 108 ? -43.103  -28.362  -20.812 1.00 183.38 ? 108 LEU A CA  1 
ATOM   506   C C   . LEU A 1 108 ? -43.705  -27.013  -20.414 1.00 187.48 ? 108 LEU A C   1 
ATOM   507   O O   . LEU A 1 108 ? -44.324  -26.348  -21.247 1.00 186.73 ? 108 LEU A O   1 
ATOM   508   C CB  . LEU A 1 108 ? -44.122  -29.500  -20.632 1.00 183.54 ? 108 LEU A CB  1 
ATOM   509   C CG  . LEU A 1 108 ? -43.781  -30.809  -21.344 1.00 188.28 ? 108 LEU A CG  1 
ATOM   510   C CD1 . LEU A 1 108 ? -44.313  -31.996  -20.577 1.00 188.36 ? 108 LEU A CD1 1 
ATOM   511   C CD2 . LEU A 1 108 ? -44.300  -30.814  -22.775 1.00 191.15 ? 108 LEU A CD2 1 
ATOM   512   N N   . ASP A 1 109 ? -43.503  -26.607  -19.149 1.00 184.52 ? 109 ASP A N   1 
ATOM   513   C CA  . ASP A 1 109 ? -43.958  -25.316  -18.643 1.00 184.62 ? 109 ASP A CA  1 
ATOM   514   C C   . ASP A 1 109 ? -43.010  -24.206  -19.122 1.00 187.59 ? 109 ASP A C   1 
ATOM   515   O O   . ASP A 1 109 ? -43.444  -23.060  -19.247 1.00 187.41 ? 109 ASP A O   1 
ATOM   516   C CB  . ASP A 1 109 ? -44.071  -25.336  -17.105 1.00 187.06 ? 109 ASP A CB  1 
ATOM   517   C CG  . ASP A 1 109 ? -45.294  -26.054  -16.547 1.00 199.52 ? 109 ASP A CG  1 
ATOM   518   O OD1 . ASP A 1 109 ? -45.714  -27.077  -17.143 1.00 200.69 ? 109 ASP A OD1 1 
ATOM   519   O OD2 . ASP A 1 109 ? -45.800  -25.625  -15.485 1.00 205.12 ? 109 ASP A OD2 1 
ATOM   520   N N   . TYR A 1 110 ? -41.724  -24.552  -19.407 1.00 183.19 ? 110 TYR A N   1 
ATOM   521   C CA  . TYR A 1 110 ? -40.708  -23.623  -19.917 1.00 182.60 ? 110 TYR A CA  1 
ATOM   522   C C   . TYR A 1 110 ? -40.977  -23.282  -21.384 1.00 187.49 ? 110 TYR A C   1 
ATOM   523   O O   . TYR A 1 110 ? -40.855  -22.115  -21.761 1.00 187.56 ? 110 TYR A O   1 
ATOM   524   C CB  . TYR A 1 110 ? -39.280  -24.176  -19.716 1.00 183.02 ? 110 TYR A CB  1 
ATOM   525   C CG  . TYR A 1 110 ? -38.228  -23.574  -20.623 1.00 184.18 ? 110 TYR A CG  1 
ATOM   526   C CD1 . TYR A 1 110 ? -37.713  -22.304  -20.381 1.00 186.19 ? 110 TYR A CD1 1 
ATOM   527   C CD2 . TYR A 1 110 ? -37.732  -24.282  -21.714 1.00 184.90 ? 110 TYR A CD2 1 
ATOM   528   C CE1 . TYR A 1 110 ? -36.745  -21.744  -21.214 1.00 187.32 ? 110 TYR A CE1 1 
ATOM   529   C CE2 . TYR A 1 110 ? -36.767  -23.732  -22.558 1.00 185.99 ? 110 TYR A CE2 1 
ATOM   530   C CZ  . TYR A 1 110 ? -36.267  -22.467  -22.296 1.00 193.03 ? 110 TYR A CZ  1 
ATOM   531   O OH  . TYR A 1 110 ? -35.319  -21.920  -23.126 1.00 193.02 ? 110 TYR A OH  1 
ATOM   532   N N   . HIS A 1 111 ? -41.318  -24.304  -22.207 1.00 184.14 ? 111 HIS A N   1 
ATOM   533   C CA  . HIS A 1 111 ? -41.639  -24.158  -23.634 1.00 184.03 ? 111 HIS A CA  1 
ATOM   534   C C   . HIS A 1 111 ? -42.886  -23.288  -23.809 1.00 187.07 ? 111 HIS A C   1 
ATOM   535   O O   . HIS A 1 111 ? -42.891  -22.375  -24.637 1.00 186.33 ? 111 HIS A O   1 
ATOM   536   C CB  . HIS A 1 111 ? -41.869  -25.535  -24.279 1.00 184.95 ? 111 HIS A CB  1 
ATOM   537   C CG  . HIS A 1 111 ? -40.615  -26.255  -24.659 1.00 188.54 ? 111 HIS A CG  1 
ATOM   538   N ND1 . HIS A 1 111 ? -39.907  -25.916  -25.798 1.00 190.62 ? 111 HIS A ND1 1 
ATOM   539   C CD2 . HIS A 1 111 ? -40.005  -27.304  -24.061 1.00 190.27 ? 111 HIS A CD2 1 
ATOM   540   C CE1 . HIS A 1 111 ? -38.883  -26.753  -25.846 1.00 190.27 ? 111 HIS A CE1 1 
ATOM   541   N NE2 . HIS A 1 111 ? -38.900  -27.607  -24.822 1.00 190.38 ? 111 HIS A NE2 1 
ATOM   542   N N   . ASP A 1 112 ? -43.925  -23.568  -22.994 1.00 183.41 ? 112 ASP A N   1 
ATOM   543   C CA  . ASP A 1 112 ? -45.207  -22.867  -22.929 1.00 183.18 ? 112 ASP A CA  1 
ATOM   544   C C   . ASP A 1 112 ? -44.988  -21.372  -22.666 1.00 186.27 ? 112 ASP A C   1 
ATOM   545   O O   . ASP A 1 112 ? -45.620  -20.541  -23.320 1.00 185.84 ? 112 ASP A O   1 
ATOM   546   C CB  . ASP A 1 112 ? -46.078  -23.507  -21.823 1.00 185.26 ? 112 ASP A CB  1 
ATOM   547   C CG  . ASP A 1 112 ? -47.336  -22.748  -21.452 1.00 196.71 ? 112 ASP A CG  1 
ATOM   548   O OD1 . ASP A 1 112 ? -47.454  -22.337  -20.276 1.00 196.98 ? 112 ASP A OD1 1 
ATOM   549   O OD2 . ASP A 1 112 ? -48.210  -22.584  -22.330 1.00 204.33 ? 112 ASP A OD2 1 
ATOM   550   N N   . SER A 1 113 ? -44.070  -21.044  -21.731 1.00 182.37 ? 113 SER A N   1 
ATOM   551   C CA  . SER A 1 113 ? -43.702  -19.679  -21.356 1.00 182.13 ? 113 SER A CA  1 
ATOM   552   C C   . SER A 1 113 ? -42.966  -18.941  -22.475 1.00 186.52 ? 113 SER A C   1 
ATOM   553   O O   . SER A 1 113 ? -43.074  -17.720  -22.556 1.00 186.50 ? 113 SER A O   1 
ATOM   554   C CB  . SER A 1 113 ? -42.866  -19.675  -20.080 1.00 185.20 ? 113 SER A CB  1 
ATOM   555   O OG  . SER A 1 113 ? -43.662  -19.948  -18.938 1.00 193.30 ? 113 SER A OG  1 
ATOM   556   N N   . ASN A 1 114 ? -42.228  -19.671  -23.332 1.00 174.20 ? 114 ASN A N   1 
ATOM   557   C CA  . ASN A 1 114 ? -41.498  -19.074  -24.454 1.00 174.54 ? 114 ASN A CA  1 
ATOM   558   C C   . ASN A 1 114 ? -42.420  -18.734  -25.622 1.00 179.41 ? 114 ASN A C   1 
ATOM   559   O O   . ASN A 1 114 ? -42.182  -17.740  -26.316 1.00 179.23 ? 114 ASN A O   1 
ATOM   560   C CB  . ASN A 1 114 ? -40.370  -19.988  -24.923 1.00 175.73 ? 114 ASN A CB  1 
ATOM   561   C CG  . ASN A 1 114 ? -39.304  -20.259  -23.894 1.00 202.12 ? 114 ASN A CG  1 
ATOM   562   O OD1 . ASN A 1 114 ? -38.777  -21.373  -23.815 1.00 199.92 ? 114 ASN A OD1 1 
ATOM   563   N ND2 . ASN A 1 114 ? -38.946  -19.257  -23.092 1.00 192.31 ? 114 ASN A ND2 1 
ATOM   564   N N   . VAL A 1 115 ? -43.463  -19.568  -25.841 1.00 176.25 ? 115 VAL A N   1 
ATOM   565   C CA  . VAL A 1 115 ? -44.469  -19.408  -26.899 1.00 176.22 ? 115 VAL A CA  1 
ATOM   566   C C   . VAL A 1 115 ? -45.239  -18.090  -26.682 1.00 178.97 ? 115 VAL A C   1 
ATOM   567   O O   . VAL A 1 115 ? -45.321  -17.267  -27.599 1.00 178.04 ? 115 VAL A O   1 
ATOM   568   C CB  . VAL A 1 115 ? -45.409  -20.652  -26.988 1.00 180.55 ? 115 VAL A CB  1 
ATOM   569   C CG1 . VAL A 1 115 ? -46.593  -20.403  -27.921 1.00 180.69 ? 115 VAL A CG1 1 
ATOM   570   C CG2 . VAL A 1 115 ? -44.642  -21.896  -27.427 1.00 180.67 ? 115 VAL A CG2 1 
ATOM   571   N N   . LYS A 1 116 ? -45.762  -17.895  -25.451 1.00 175.38 ? 116 LYS A N   1 
ATOM   572   C CA  . LYS A 1 116 ? -46.513  -16.711  -25.030 1.00 175.20 ? 116 LYS A CA  1 
ATOM   573   C C   . LYS A 1 116 ? -45.661  -15.445  -25.114 1.00 179.21 ? 116 LYS A C   1 
ATOM   574   O O   . LYS A 1 116 ? -46.160  -14.411  -25.560 1.00 179.12 ? 116 LYS A O   1 
ATOM   575   C CB  . LYS A 1 116 ? -47.076  -16.897  -23.611 1.00 177.48 ? 116 LYS A CB  1 
ATOM   576   C CG  . LYS A 1 116 ? -48.190  -17.936  -23.524 1.00 190.64 ? 116 LYS A CG  1 
ATOM   577   C CD  . LYS A 1 116 ? -48.859  -17.946  -22.154 1.00 200.83 ? 116 LYS A CD  1 
ATOM   578   C CE  . LYS A 1 116 ? -48.366  -19.054  -21.251 1.00 211.90 ? 116 LYS A CE  1 
ATOM   579   N NZ  . LYS A 1 116 ? -47.033  -18.755  -20.666 1.00 220.73 ? 116 LYS A NZ  1 
ATOM   580   N N   . ASN A 1 117 ? -44.374  -15.538  -24.721 1.00 175.43 ? 117 ASN A N   1 
ATOM   581   C CA  . ASN A 1 117 ? -43.430  -14.423  -24.759 1.00 175.19 ? 117 ASN A CA  1 
ATOM   582   C C   . ASN A 1 117 ? -43.010  -14.044  -26.175 1.00 179.00 ? 117 ASN A C   1 
ATOM   583   O O   . ASN A 1 117 ? -42.651  -12.887  -26.400 1.00 178.05 ? 117 ASN A O   1 
ATOM   584   C CB  . ASN A 1 117 ? -42.224  -14.690  -23.862 1.00 176.68 ? 117 ASN A CB  1 
ATOM   585   C CG  . ASN A 1 117 ? -42.524  -14.541  -22.386 1.00 203.53 ? 117 ASN A CG  1 
ATOM   586   O OD1 . ASN A 1 117 ? -43.614  -14.870  -21.896 1.00 197.55 ? 117 ASN A OD1 1 
ATOM   587   N ND2 . ASN A 1 117 ? -41.551  -14.048  -21.637 1.00 196.96 ? 117 ASN A ND2 1 
ATOM   588   N N   . LEU A 1 118 ? -43.073  -14.998  -27.131 1.00 176.63 ? 118 LEU A N   1 
ATOM   589   C CA  . LEU A 1 118 ? -42.752  -14.720  -28.533 1.00 177.31 ? 118 LEU A CA  1 
ATOM   590   C C   . LEU A 1 118 ? -43.926  -13.973  -29.180 1.00 182.61 ? 118 LEU A C   1 
ATOM   591   O O   . LEU A 1 118 ? -43.699  -13.063  -29.983 1.00 182.53 ? 118 LEU A O   1 
ATOM   592   C CB  . LEU A 1 118 ? -42.403  -15.998  -29.313 1.00 177.62 ? 118 LEU A CB  1 
ATOM   593   C CG  . LEU A 1 118 ? -41.636  -15.770  -30.625 1.00 182.64 ? 118 LEU A CG  1 
ATOM   594   C CD1 . LEU A 1 118 ? -40.423  -16.663  -30.722 1.00 182.95 ? 118 LEU A CD1 1 
ATOM   595   C CD2 . LEU A 1 118 ? -42.539  -15.951  -31.832 1.00 185.55 ? 118 LEU A CD2 1 
ATOM   596   N N   . TYR A 1 119 ? -45.174  -14.346  -28.811 1.00 179.79 ? 119 TYR A N   1 
ATOM   597   C CA  . TYR A 1 119 ? -46.396  -13.688  -29.282 1.00 180.03 ? 119 TYR A CA  1 
ATOM   598   C C   . TYR A 1 119 ? -46.478  -12.282  -28.685 1.00 184.09 ? 119 TYR A C   1 
ATOM   599   O O   . TYR A 1 119 ? -46.913  -11.353  -29.359 1.00 183.51 ? 119 TYR A O   1 
ATOM   600   C CB  . TYR A 1 119 ? -47.652  -14.535  -28.963 1.00 181.58 ? 119 TYR A CB  1 
ATOM   601   C CG  . TYR A 1 119 ? -48.967  -13.778  -29.015 1.00 183.97 ? 119 TYR A CG  1 
ATOM   602   C CD1 . TYR A 1 119 ? -49.560  -13.295  -27.855 1.00 186.41 ? 119 TYR A CD1 1 
ATOM   603   C CD2 . TYR A 1 119 ? -49.622  -13.556  -30.224 1.00 184.78 ? 119 TYR A CD2 1 
ATOM   604   C CE1 . TYR A 1 119 ? -50.763  -12.590  -27.896 1.00 188.13 ? 119 TYR A CE1 1 
ATOM   605   C CE2 . TYR A 1 119 ? -50.826  -12.850  -30.278 1.00 185.86 ? 119 TYR A CE2 1 
ATOM   606   C CZ  . TYR A 1 119 ? -51.393  -12.368  -29.110 1.00 194.19 ? 119 TYR A CZ  1 
ATOM   607   O OH  . TYR A 1 119 ? -52.577  -11.672  -29.158 1.00 195.19 ? 119 TYR A OH  1 
ATOM   608   N N   . GLU A 1 120 ? -46.038  -12.133  -27.420 1.00 181.11 ? 120 GLU A N   1 
ATOM   609   C CA  . GLU A 1 120 ? -46.015  -10.857  -26.703 1.00 181.07 ? 120 GLU A CA  1 
ATOM   610   C C   . GLU A 1 120 ? -44.955  -9.887   -27.239 1.00 185.37 ? 120 GLU A C   1 
ATOM   611   O O   . GLU A 1 120 ? -45.054  -8.691   -26.972 1.00 185.29 ? 120 GLU A O   1 
ATOM   612   C CB  . GLU A 1 120 ? -45.879  -11.073  -25.186 1.00 182.25 ? 120 GLU A CB  1 
ATOM   613   C CG  . GLU A 1 120 ? -47.137  -10.733  -24.401 1.00 191.11 ? 120 GLU A CG  1 
ATOM   614   C CD  . GLU A 1 120 ? -48.372  -11.549  -24.735 1.00 204.40 ? 120 GLU A CD  1 
ATOM   615   O OE1 . GLU A 1 120 ? -48.492  -12.685  -24.222 1.00 192.12 ? 120 GLU A OE1 1 
ATOM   616   O OE2 . GLU A 1 120 ? -49.225  -11.048  -25.502 1.00 196.43 ? 120 GLU A OE2 1 
ATOM   617   N N   . LYS A 1 121 ? -43.956  -10.392  -28.000 1.00 181.80 ? 121 LYS A N   1 
ATOM   618   C CA  . LYS A 1 121 ? -42.919  -9.566   -28.627 1.00 181.57 ? 121 LYS A CA  1 
ATOM   619   C C   . LYS A 1 121 ? -43.515  -8.896   -29.875 1.00 185.67 ? 121 LYS A C   1 
ATOM   620   O O   . LYS A 1 121 ? -43.319  -7.695   -30.075 1.00 185.43 ? 121 LYS A O   1 
ATOM   621   C CB  . LYS A 1 121 ? -41.678  -10.403  -28.994 1.00 183.68 ? 121 LYS A CB  1 
ATOM   622   C CG  . LYS A 1 121 ? -40.447  -9.557   -29.331 1.00 191.21 ? 121 LYS A CG  1 
ATOM   623   C CD  . LYS A 1 121 ? -39.395  -10.351  -30.083 1.00 197.21 ? 121 LYS A CD  1 
ATOM   624   C CE  . LYS A 1 121 ? -38.293  -9.467   -30.607 1.00 201.82 ? 121 LYS A CE  1 
ATOM   625   N NZ  . LYS A 1 121 ? -37.382  -10.219  -31.508 1.00 205.81 ? 121 LYS A NZ  1 
ATOM   626   N N   . VAL A 1 122 ? -44.266  -9.679   -30.689 1.00 182.06 ? 122 VAL A N   1 
ATOM   627   C CA  . VAL A 1 122 ? -44.950  -9.254   -31.923 1.00 181.71 ? 122 VAL A CA  1 
ATOM   628   C C   . VAL A 1 122 ? -46.121  -8.302   -31.592 1.00 184.90 ? 122 VAL A C   1 
ATOM   629   O O   . VAL A 1 122 ? -46.271  -7.267   -32.246 1.00 184.35 ? 122 VAL A O   1 
ATOM   630   C CB  . VAL A 1 122 ? -45.409  -10.489  -32.756 1.00 185.44 ? 122 VAL A CB  1 
ATOM   631   C CG1 . VAL A 1 122 ? -46.181  -10.076  -34.006 1.00 185.14 ? 122 VAL A CG1 1 
ATOM   632   C CG2 . VAL A 1 122 ? -44.224  -11.373  -33.130 1.00 185.45 ? 122 VAL A CG2 1 
ATOM   633   N N   . ARG A 1 123 ? -46.934  -8.661   -30.574 1.00 180.86 ? 123 ARG A N   1 
ATOM   634   C CA  . ARG A 1 123 ? -48.091  -7.896   -30.096 1.00 180.26 ? 123 ARG A CA  1 
ATOM   635   C C   . ARG A 1 123 ? -47.689  -6.528   -29.501 1.00 184.55 ? 123 ARG A C   1 
ATOM   636   O O   . ARG A 1 123 ? -48.456  -5.572   -29.627 1.00 184.33 ? 123 ARG A O   1 
ATOM   637   C CB  . ARG A 1 123 ? -48.892  -8.727   -29.080 1.00 178.29 ? 123 ARG A CB  1 
ATOM   638   C CG  . ARG A 1 123 ? -50.374  -8.380   -29.010 1.00 181.37 ? 123 ARG A CG  1 
ATOM   639   C CD  . ARG A 1 123 ? -50.839  -8.197   -27.576 1.00 182.73 ? 123 ARG A CD  1 
ATOM   640   N NE  . ARG A 1 123 ? -50.167  -7.068   -26.929 1.00 184.80 ? 123 ARG A NE  1 
ATOM   641   C CZ  . ARG A 1 123 ? -49.513  -7.141   -25.775 1.00 195.50 ? 123 ARG A CZ  1 
ATOM   642   N NH1 . ARG A 1 123 ? -49.460  -8.284   -25.105 1.00 182.58 ? 123 ARG A NH1 1 
ATOM   643   N NH2 . ARG A 1 123 ? -48.923  -6.065   -25.273 1.00 180.39 ? 123 ARG A NH2 1 
ATOM   644   N N   . SER A 1 124 ? -46.493  -6.436   -28.871 1.00 181.08 ? 124 SER A N   1 
ATOM   645   C CA  . SER A 1 124 ? -45.971  -5.193   -28.286 1.00 180.99 ? 124 SER A CA  1 
ATOM   646   C C   . SER A 1 124 ? -45.416  -4.233   -29.347 1.00 184.83 ? 124 SER A C   1 
ATOM   647   O O   . SER A 1 124 ? -45.327  -3.030   -29.091 1.00 184.72 ? 124 SER A O   1 
ATOM   648   C CB  . SER A 1 124 ? -44.907  -5.488   -27.234 1.00 184.42 ? 124 SER A CB  1 
ATOM   649   O OG  . SER A 1 124 ? -45.475  -6.136   -26.107 1.00 193.06 ? 124 SER A OG  1 
ATOM   650   N N   . GLN A 1 125 ? -45.043  -4.766   -30.530 1.00 181.07 ? 125 GLN A N   1 
ATOM   651   C CA  . GLN A 1 125 ? -44.520  -3.990   -31.664 1.00 180.79 ? 125 GLN A CA  1 
ATOM   652   C C   . GLN A 1 125 ? -45.657  -3.411   -32.534 1.00 183.55 ? 125 GLN A C   1 
ATOM   653   O O   . GLN A 1 125 ? -45.422  -2.481   -33.312 1.00 183.05 ? 125 GLN A O   1 
ATOM   654   C CB  . GLN A 1 125 ? -43.581  -4.856   -32.526 1.00 182.13 ? 125 GLN A CB  1 
ATOM   655   C CG  . GLN A 1 125 ? -42.207  -5.109   -31.909 1.00 196.20 ? 125 GLN A CG  1 
ATOM   656   C CD  . GLN A 1 125 ? -41.464  -6.219   -32.616 1.00 215.12 ? 125 GLN A CD  1 
ATOM   657   O OE1 . GLN A 1 125 ? -41.951  -7.350   -32.734 1.00 210.55 ? 125 GLN A OE1 1 
ATOM   658   N NE2 . GLN A 1 125 ? -40.250  -5.933   -33.072 1.00 207.51 ? 125 GLN A NE2 1 
ATOM   659   N N   . LEU A 1 126 ? -46.879  -3.962   -32.398 1.00 179.03 ? 126 LEU A N   1 
ATOM   660   C CA  . LEU A 1 126 ? -48.058  -3.555   -33.161 1.00 191.76 ? 126 LEU A CA  1 
ATOM   661   C C   . LEU A 1 126 ? -49.139  -3.019   -32.230 1.00 207.80 ? 126 LEU A C   1 
ATOM   662   O O   . LEU A 1 126 ? -49.955  -2.199   -32.640 1.00 168.02 ? 126 LEU A O   1 
ATOM   663   C CB  . LEU A 1 126 ? -48.604  -4.747   -33.976 1.00 191.50 ? 126 LEU A CB  1 
ATOM   664   C CG  . LEU A 1 126 ? -47.614  -5.479   -34.896 1.00 195.85 ? 126 LEU A CG  1 
ATOM   665   C CD1 . LEU A 1 126 ? -48.040  -6.911   -35.126 1.00 195.66 ? 126 LEU A CD1 1 
ATOM   666   C CD2 . LEU A 1 126 ? -47.439  -4.755   -36.221 1.00 198.60 ? 126 LEU A CD2 1 
ATOM   667   N N   . CYS A 1 148 ? -40.069  -6.133   -45.204 1.00 210.83 ? 148 CYS A N   1 
ATOM   668   C CA  . CYS A 1 148 ? -41.477  -5.946   -44.877 1.00 211.08 ? 148 CYS A CA  1 
ATOM   669   C C   . CYS A 1 148 ? -41.853  -6.632   -43.559 1.00 216.14 ? 148 CYS A C   1 
ATOM   670   O O   . CYS A 1 148 ? -42.334  -5.969   -42.635 1.00 215.52 ? 148 CYS A O   1 
ATOM   671   C CB  . CYS A 1 148 ? -42.368  -6.407   -46.029 1.00 211.58 ? 148 CYS A CB  1 
ATOM   672   S SG  . CYS A 1 148 ? -44.141  -6.429   -45.643 1.00 215.60 ? 148 CYS A SG  1 
ATOM   673   N N   . MET A 1 149 ? -41.644  -7.960   -43.489 1.00 214.02 ? 149 MET A N   1 
ATOM   674   C CA  . MET A 1 149 ? -41.948  -8.809   -42.334 1.00 214.47 ? 149 MET A CA  1 
ATOM   675   C C   . MET A 1 149 ? -40.783  -8.867   -41.342 1.00 219.06 ? 149 MET A C   1 
ATOM   676   O O   . MET A 1 149 ? -41.007  -9.063   -40.146 1.00 218.67 ? 149 MET A O   1 
ATOM   677   C CB  . MET A 1 149 ? -42.281  -10.231  -42.816 1.00 217.08 ? 149 MET A CB  1 
ATOM   678   C CG  . MET A 1 149 ? -43.270  -10.960  -41.934 1.00 220.98 ? 149 MET A CG  1 
ATOM   679   S SD  . MET A 1 149 ? -44.899  -11.126  -42.716 1.00 225.60 ? 149 MET A SD  1 
ATOM   680   C CE  . MET A 1 149 ? -45.769  -12.052  -41.459 1.00 222.17 ? 149 MET A CE  1 
ATOM   681   N N   . GLU A 1 150 ? -39.542  -8.705   -41.850 1.00 216.26 ? 150 GLU A N   1 
ATOM   682   C CA  . GLU A 1 150 ? -38.278  -8.751   -41.103 1.00 216.25 ? 150 GLU A CA  1 
ATOM   683   C C   . GLU A 1 150 ? -38.137  -7.663   -40.020 1.00 220.18 ? 150 GLU A C   1 
ATOM   684   O O   . GLU A 1 150 ? -37.335  -7.840   -39.101 1.00 219.91 ? 150 GLU A O   1 
ATOM   685   C CB  . GLU A 1 150 ? -37.072  -8.726   -42.066 1.00 217.79 ? 150 GLU A CB  1 
ATOM   686   C CG  . GLU A 1 150 ? -36.812  -10.042  -42.792 1.00 228.86 ? 150 GLU A CG  1 
ATOM   687   C CD  . GLU A 1 150 ? -37.781  -10.407  -43.902 1.00 251.57 ? 150 GLU A CD  1 
ATOM   688   O OE1 . GLU A 1 150 ? -37.817  -9.685   -44.924 1.00 254.47 ? 150 GLU A OE1 1 
ATOM   689   O OE2 . GLU A 1 150 ? -38.500  -11.421  -43.753 1.00 243.80 ? 150 GLU A OE2 1 
ATOM   690   N N   . SER A 1 151 ? -38.910  -6.554   -40.122 1.00 216.46 ? 151 SER A N   1 
ATOM   691   C CA  . SER A 1 151 ? -38.915  -5.444   -39.155 1.00 216.04 ? 151 SER A CA  1 
ATOM   692   C C   . SER A 1 151 ? -39.508  -5.866   -37.797 1.00 218.62 ? 151 SER A C   1 
ATOM   693   O O   . SER A 1 151 ? -39.014  -5.435   -36.749 1.00 218.07 ? 151 SER A O   1 
ATOM   694   C CB  . SER A 1 151 ? -39.665  -4.239   -39.718 1.00 219.96 ? 151 SER A CB  1 
ATOM   695   O OG  . SER A 1 151 ? -40.984  -4.575   -40.118 1.00 229.49 ? 151 SER A OG  1 
ATOM   696   N N   . VAL A 1 152 ? -40.558  -6.717   -37.827 1.00 214.16 ? 152 VAL A N   1 
ATOM   697   C CA  . VAL A 1 152 ? -41.240  -7.266   -36.646 1.00 213.45 ? 152 VAL A CA  1 
ATOM   698   C C   . VAL A 1 152 ? -40.320  -8.315   -35.997 1.00 214.73 ? 152 VAL A C   1 
ATOM   699   O O   . VAL A 1 152 ? -40.180  -8.339   -34.773 1.00 213.97 ? 152 VAL A O   1 
ATOM   700   C CB  . VAL A 1 152 ? -42.638  -7.861   -36.994 1.00 217.62 ? 152 VAL A CB  1 
ATOM   701   C CG1 . VAL A 1 152 ? -43.422  -8.217   -35.730 1.00 217.67 ? 152 VAL A CG1 1 
ATOM   702   C CG2 . VAL A 1 152 ? -43.447  -6.913   -37.880 1.00 217.63 ? 152 VAL A CG2 1 
ATOM   703   N N   . LYS A 1 153 ? -39.686  -9.167   -36.831 1.00 209.79 ? 153 LYS A N   1 
ATOM   704   C CA  . LYS A 1 153 ? -38.749  -10.219  -36.425 1.00 208.82 ? 153 LYS A CA  1 
ATOM   705   C C   . LYS A 1 153 ? -37.527  -9.613   -35.715 1.00 212.38 ? 153 LYS A C   1 
ATOM   706   O O   . LYS A 1 153 ? -37.108  -10.127  -34.678 1.00 211.89 ? 153 LYS A O   1 
ATOM   707   C CB  . LYS A 1 153 ? -38.311  -11.054  -37.644 1.00 210.52 ? 153 LYS A CB  1 
ATOM   708   C CG  . LYS A 1 153 ? -39.440  -11.845  -38.308 1.00 215.79 ? 153 LYS A CG  1 
ATOM   709   C CD  . LYS A 1 153 ? -39.046  -12.342  -39.688 1.00 221.16 ? 153 LYS A CD  1 
ATOM   710   C CE  . LYS A 1 153 ? -40.215  -12.947  -40.428 1.00 225.60 ? 153 LYS A CE  1 
ATOM   711   N NZ  . LYS A 1 153 ? -39.883  -13.222  -41.851 1.00 231.30 ? 153 LYS A NZ  1 
ATOM   712   N N   . ASN A 1 154 ? -36.986  -8.502   -36.260 1.00 208.77 ? 154 ASN A N   1 
ATOM   713   C CA  . ASN A 1 154 ? -35.834  -7.783   -35.711 1.00 237.42 ? 154 ASN A CA  1 
ATOM   714   C C   . ASN A 1 154 ? -36.297  -6.686   -34.746 1.00 268.90 ? 154 ASN A C   1 
ATOM   715   O O   . ASN A 1 154 ? -37.130  -6.935   -33.874 1.00 230.83 ? 154 ASN A O   1 
ATOM   716   C CB  . ASN A 1 154 ? -34.996  -7.177   -36.843 1.00 237.38 ? 154 ASN A CB  1 
ATOM   717   C CG  . ASN A 1 154 ? -33.534  -6.988   -36.516 1.00 256.10 ? 154 ASN A CG  1 
ATOM   718   O OD1 . ASN A 1 154 ? -33.158  -6.198   -35.643 1.00 249.31 ? 154 ASN A OD1 1 
ATOM   719   N ND2 . ASN A 1 154 ? -32.672  -7.679   -37.248 1.00 247.19 ? 154 ASN A ND2 1 
ATOM   720   N N   . TYR A 1 159 ? -44.291  0.023    -36.052 1.00 201.47 ? 159 TYR A N   1 
ATOM   721   C CA  . TYR A 1 159 ? -45.646  0.568    -36.092 1.00 201.26 ? 159 TYR A CA  1 
ATOM   722   C C   . TYR A 1 159 ? -45.746  1.987    -36.712 1.00 205.75 ? 159 TYR A C   1 
ATOM   723   O O   . TYR A 1 159 ? -46.697  2.181    -37.468 1.00 205.65 ? 159 TYR A O   1 
ATOM   724   C CB  . TYR A 1 159 ? -46.323  0.521    -34.705 1.00 202.07 ? 159 TYR A CB  1 
ATOM   725   C CG  . TYR A 1 159 ? -47.816  0.790    -34.734 1.00 203.65 ? 159 TYR A CG  1 
ATOM   726   C CD1 . TYR A 1 159 ? -48.718  -0.208   -35.094 1.00 205.18 ? 159 TYR A CD1 1 
ATOM   727   C CD2 . TYR A 1 159 ? -48.328  2.033    -34.373 1.00 204.78 ? 159 TYR A CD2 1 
ATOM   728   C CE1 . TYR A 1 159 ? -50.091  0.032    -35.118 1.00 205.74 ? 159 TYR A CE1 1 
ATOM   729   C CE2 . TYR A 1 159 ? -49.699  2.283    -34.390 1.00 205.67 ? 159 TYR A CE2 1 
ATOM   730   C CZ  . TYR A 1 159 ? -50.577  1.279    -34.764 1.00 212.45 ? 159 TYR A CZ  1 
ATOM   731   O OH  . TYR A 1 159 ? -51.928  1.514    -34.785 1.00 213.27 ? 159 TYR A OH  1 
ATOM   732   N N   . PRO A 1 160 ? -44.841  2.983    -36.459 1.00 202.29 ? 160 PRO A N   1 
ATOM   733   C CA  . PRO A 1 160 ? -45.027  4.318    -37.072 1.00 202.22 ? 160 PRO A CA  1 
ATOM   734   C C   . PRO A 1 160 ? -44.985  4.382    -38.604 1.00 205.44 ? 160 PRO A C   1 
ATOM   735   O O   . PRO A 1 160 ? -45.520  5.334    -39.173 1.00 204.84 ? 160 PRO A O   1 
ATOM   736   C CB  . PRO A 1 160 ? -43.908  5.159    -36.448 1.00 204.45 ? 160 PRO A CB  1 
ATOM   737   C CG  . PRO A 1 160 ? -43.519  4.429    -35.213 1.00 208.75 ? 160 PRO A CG  1 
ATOM   738   C CD  . PRO A 1 160 ? -43.662  2.986    -35.571 1.00 203.89 ? 160 PRO A CD  1 
ATOM   739   N N   . LYS A 1 161 ? -44.366  3.385    -39.269 1.00 201.81 ? 161 LYS A N   1 
ATOM   740   C CA  . LYS A 1 161 ? -44.281  3.313    -40.732 1.00 201.80 ? 161 LYS A CA  1 
ATOM   741   C C   . LYS A 1 161 ? -45.648  2.973    -41.355 1.00 205.44 ? 161 LYS A C   1 
ATOM   742   O O   . LYS A 1 161 ? -45.949  3.445    -42.453 1.00 205.12 ? 161 LYS A O   1 
ATOM   743   C CB  . LYS A 1 161 ? -43.221  2.280    -41.166 1.00 204.39 ? 161 LYS A CB  1 
ATOM   744   C CG  . LYS A 1 161 ? -42.800  2.400    -42.629 1.00 214.66 ? 161 LYS A CG  1 
ATOM   745   C CD  . LYS A 1 161 ? -42.002  1.194    -43.102 1.00 221.15 ? 161 LYS A CD  1 
ATOM   746   C CE  . LYS A 1 161 ? -41.766  1.214    -44.594 1.00 228.31 ? 161 LYS A CE  1 
ATOM   747   N NZ  . LYS A 1 161 ? -42.989  0.855    -45.362 1.00 234.64 ? 161 LYS A NZ  1 
ATOM   748   N N   . TYR A 1 162 ? -46.462  2.158    -40.651 1.00 201.64 ? 162 TYR A N   1 
ATOM   749   C CA  . TYR A 1 162 ? -47.786  1.706    -41.098 1.00 201.12 ? 162 TYR A CA  1 
ATOM   750   C C   . TYR A 1 162 ? -48.958  2.211    -40.215 1.00 204.34 ? 162 TYR A C   1 
ATOM   751   O O   . TYR A 1 162 ? -50.098  1.789    -40.435 1.00 203.51 ? 162 TYR A O   1 
ATOM   752   C CB  . TYR A 1 162 ? -47.810  0.161    -41.221 1.00 202.23 ? 162 TYR A CB  1 
ATOM   753   C CG  . TYR A 1 162 ? -46.966  -0.401   -42.348 1.00 204.52 ? 162 TYR A CG  1 
ATOM   754   C CD1 . TYR A 1 162 ? -45.603  -0.635   -42.178 1.00 206.67 ? 162 TYR A CD1 1 
ATOM   755   C CD2 . TYR A 1 162 ? -47.540  -0.747   -43.568 1.00 205.59 ? 162 TYR A CD2 1 
ATOM   756   C CE1 . TYR A 1 162 ? -44.824  -1.159   -43.209 1.00 207.75 ? 162 TYR A CE1 1 
ATOM   757   C CE2 . TYR A 1 162 ? -46.771  -1.276   -44.605 1.00 207.11 ? 162 TYR A CE2 1 
ATOM   758   C CZ  . TYR A 1 162 ? -45.414  -1.481   -44.420 1.00 214.12 ? 162 TYR A CZ  1 
ATOM   759   O OH  . TYR A 1 162 ? -44.654  -1.997   -45.440 1.00 215.25 ? 162 TYR A OH  1 
ATOM   760   N N   . SER A 1 163 ? -48.682  3.120    -39.238 1.00 200.93 ? 163 SER A N   1 
ATOM   761   C CA  . SER A 1 163 ? -49.675  3.686    -38.307 1.00 200.48 ? 163 SER A CA  1 
ATOM   762   C C   . SER A 1 163 ? -50.774  4.485    -39.005 1.00 204.14 ? 163 SER A C   1 
ATOM   763   O O   . SER A 1 163 ? -51.939  4.379    -38.614 1.00 203.57 ? 163 SER A O   1 
ATOM   764   C CB  . SER A 1 163 ? -49.000  4.546    -37.241 1.00 204.12 ? 163 SER A CB  1 
ATOM   765   O OG  . SER A 1 163 ? -49.927  4.981    -36.259 1.00 212.47 ? 163 SER A OG  1 
ATOM   766   N N   . GLU A 1 164 ? -50.402  5.287    -40.024 1.00 200.66 ? 164 GLU A N   1 
ATOM   767   C CA  . GLU A 1 164 ? -51.328  6.114    -40.805 1.00 200.09 ? 164 GLU A CA  1 
ATOM   768   C C   . GLU A 1 164 ? -52.230  5.266    -41.721 1.00 203.03 ? 164 GLU A C   1 
ATOM   769   O O   . GLU A 1 164 ? -53.387  5.627    -41.948 1.00 202.25 ? 164 GLU A O   1 
ATOM   770   C CB  . GLU A 1 164 ? -50.579  7.235    -41.571 1.00 201.63 ? 164 GLU A CB  1 
ATOM   771   C CG  . GLU A 1 164 ? -49.770  6.819    -42.797 1.00 212.83 ? 164 GLU A CG  1 
ATOM   772   C CD  . GLU A 1 164 ? -48.531  5.977    -42.560 1.00 231.62 ? 164 GLU A CD  1 
ATOM   773   O OE1 . GLU A 1 164 ? -47.564  6.490    -41.952 1.00 223.84 ? 164 GLU A OE1 1 
ATOM   774   O OE2 . GLU A 1 164 ? -48.515  4.812    -43.017 1.00 225.60 ? 164 GLU A OE2 1 
ATOM   775   N N   . GLU A 1 165 ? -51.692  4.133    -42.221 1.00 199.20 ? 165 GLU A N   1 
ATOM   776   C CA  . GLU A 1 165 ? -52.369  3.173    -43.095 1.00 198.58 ? 165 GLU A CA  1 
ATOM   777   C C   . GLU A 1 165 ? -53.475  2.441    -42.323 1.00 200.75 ? 165 GLU A C   1 
ATOM   778   O O   . GLU A 1 165 ? -54.551  2.204    -42.875 1.00 199.98 ? 165 GLU A O   1 
ATOM   779   C CB  . GLU A 1 165 ? -51.339  2.169    -43.649 1.00 200.48 ? 165 GLU A CB  1 
ATOM   780   C CG  . GLU A 1 165 ? -51.849  1.275    -44.765 1.00 210.94 ? 165 GLU A CG  1 
ATOM   781   C CD  . GLU A 1 165 ? -50.906  0.137    -45.097 1.00 229.01 ? 165 GLU A CD  1 
ATOM   782   O OE1 . GLU A 1 165 ? -49.930  0.376    -45.844 1.00 222.58 ? 165 GLU A OE1 1 
ATOM   783   O OE2 . GLU A 1 165 ? -51.127  -0.987   -44.591 1.00 220.54 ? 165 GLU A OE2 1 
ATOM   784   N N   . ALA A 1 166 ? -53.199  2.095    -41.049 1.00 196.16 ? 166 ALA A N   1 
ATOM   785   C CA  . ALA A 1 166 ? -54.107  1.384    -40.149 1.00 195.10 ? 166 ALA A CA  1 
ATOM   786   C C   . ALA A 1 166 ? -55.363  2.183    -39.803 1.00 196.06 ? 166 ALA A C   1 
ATOM   787   O O   . ALA A 1 166 ? -56.441  1.594    -39.751 1.00 195.21 ? 166 ALA A O   1 
ATOM   788   C CB  . ALA A 1 166 ? -53.374  0.979    -38.879 1.00 196.05 ? 166 ALA A CB  1 
ATOM   789   N N   . LYS A 1 167 ? -55.230  3.510    -39.576 1.00 190.69 ? 167 LYS A N   1 
ATOM   790   C CA  . LYS A 1 167 ? -56.350  4.394    -39.236 1.00 189.26 ? 167 LYS A CA  1 
ATOM   791   C C   . LYS A 1 167 ? -57.379  4.498    -40.364 1.00 191.60 ? 167 LYS A C   1 
ATOM   792   O O   . LYS A 1 167 ? -58.574  4.576    -40.081 1.00 190.68 ? 167 LYS A O   1 
ATOM   793   C CB  . LYS A 1 167 ? -55.858  5.779    -38.789 1.00 191.03 ? 167 LYS A CB  1 
ATOM   794   C CG  . LYS A 1 167 ? -56.820  6.479    -37.833 1.00 194.77 ? 167 LYS A CG  1 
ATOM   795   C CD  . LYS A 1 167 ? -56.383  7.904    -37.523 1.00 197.42 ? 167 LYS A CD  1 
ATOM   796   C CE  . LYS A 1 167 ? -57.344  8.614    -36.600 1.00 197.90 ? 167 LYS A CE  1 
ATOM   797   N NZ  . LYS A 1 167 ? -57.187  8.174    -35.189 1.00 201.52 ? 167 LYS A NZ  1 
ATOM   798   N N   . LEU A 1 168 ? -56.916  4.469    -41.632 1.00 187.57 ? 168 LEU A N   1 
ATOM   799   C CA  . LEU A 1 168 ? -57.766  4.513    -42.826 1.00 186.84 ? 168 LEU A CA  1 
ATOM   800   C C   . LEU A 1 168 ? -58.590  3.216    -42.927 1.00 190.35 ? 168 LEU A C   1 
ATOM   801   O O   . LEU A 1 168 ? -59.752  3.259    -43.340 1.00 189.52 ? 168 LEU A O   1 
ATOM   802   C CB  . LEU A 1 168 ? -56.899  4.708    -44.088 1.00 186.95 ? 168 LEU A CB  1 
ATOM   803   C CG  . LEU A 1 168 ? -57.612  5.223    -45.346 1.00 191.08 ? 168 LEU A CG  1 
ATOM   804   C CD1 . LEU A 1 168 ? -57.448  6.731    -45.498 1.00 190.62 ? 168 LEU A CD1 1 
ATOM   805   C CD2 . LEU A 1 168 ? -57.088  4.530    -46.585 1.00 193.80 ? 168 LEU A CD2 1 
ATOM   806   N N   . ASN A 1 169 ? -57.986  2.075    -42.521 1.00 186.97 ? 169 ASN A N   1 
ATOM   807   C CA  . ASN A 1 169 ? -58.610  0.749    -42.527 1.00 186.67 ? 169 ASN A CA  1 
ATOM   808   C C   . ASN A 1 169 ? -59.455  0.475    -41.276 1.00 189.94 ? 169 ASN A C   1 
ATOM   809   O O   . ASN A 1 169 ? -60.367  -0.349   -41.335 1.00 189.00 ? 169 ASN A O   1 
ATOM   810   C CB  . ASN A 1 169 ? -57.565  -0.340   -42.746 1.00 187.98 ? 169 ASN A CB  1 
ATOM   811   C CG  . ASN A 1 169 ? -57.038  -0.379   -44.160 1.00 212.69 ? 169 ASN A CG  1 
ATOM   812   O OD1 . ASN A 1 169 ? -57.621  -1.010   -45.049 1.00 207.58 ? 169 ASN A OD1 1 
ATOM   813   N ND2 . ASN A 1 169 ? -55.925  0.297    -44.404 1.00 204.51 ? 169 ASN A ND2 1 
ATOM   814   N N   . ARG A 1 170 ? -59.162  1.170    -40.157 1.00 186.79 ? 170 ARG A N   1 
ATOM   815   C CA  . ARG A 1 170 ? -59.913  1.049    -38.902 1.00 186.66 ? 170 ARG A CA  1 
ATOM   816   C C   . ARG A 1 170 ? -61.218  1.847    -38.972 1.00 191.73 ? 170 ARG A C   1 
ATOM   817   O O   . ARG A 1 170 ? -62.249  1.358    -38.514 1.00 191.13 ? 170 ARG A O   1 
ATOM   818   C CB  . ARG A 1 170 ? -59.066  1.485    -37.696 1.00 184.88 ? 170 ARG A CB  1 
ATOM   819   C CG  . ARG A 1 170 ? -58.177  0.373    -37.161 1.00 186.94 ? 170 ARG A CG  1 
ATOM   820   C CD  . ARG A 1 170 ? -57.450  0.780    -35.898 1.00 183.31 ? 170 ARG A CD  1 
ATOM   821   N NE  . ARG A 1 170 ? -56.142  1.373    -36.175 1.00 177.94 ? 170 ARG A NE  1 
ATOM   822   C CZ  . ARG A 1 170 ? -55.888  2.678    -36.167 1.00 184.98 ? 170 ARG A CZ  1 
ATOM   823   N NH1 . ARG A 1 170 ? -56.856  3.549    -35.910 1.00 171.04 ? 170 ARG A NH1 1 
ATOM   824   N NH2 . ARG A 1 170 ? -54.665  3.123    -36.423 1.00 168.59 ? 170 ARG A NH2 1 
ATOM   825   N N   . GLU A 1 171 ? -61.171  3.061    -39.568 1.00 189.29 ? 171 GLU A N   1 
ATOM   826   C CA  . GLU A 1 171 ? -62.320  3.956    -39.748 1.00 189.30 ? 171 GLU A CA  1 
ATOM   827   C C   . GLU A 1 171 ? -63.362  3.395    -40.737 1.00 193.32 ? 171 GLU A C   1 
ATOM   828   O O   . GLU A 1 171 ? -64.561  3.486    -40.462 1.00 192.93 ? 171 GLU A O   1 
ATOM   829   C CB  . GLU A 1 171 ? -61.865  5.372    -40.161 1.00 190.50 ? 171 GLU A CB  1 
ATOM   830   C CG  . GLU A 1 171 ? -61.343  6.219    -39.007 1.00 202.72 ? 171 GLU A CG  1 
ATOM   831   C CD  . GLU A 1 171 ? -60.948  7.650    -39.337 1.00 225.79 ? 171 GLU A CD  1 
ATOM   832   O OE1 . GLU A 1 171 ? -61.788  8.401    -39.886 1.00 224.75 ? 171 GLU A OE1 1 
ATOM   833   O OE2 . GLU A 1 171 ? -59.808  8.036    -38.992 1.00 218.60 ? 171 GLU A OE2 1 
ATOM   834   N N   . GLU A 1 172 ? -62.907  2.810    -41.873 1.00 189.79 ? 172 GLU A N   1 
ATOM   835   C CA  . GLU A 1 172 ? -63.780  2.216    -42.899 1.00 189.33 ? 172 GLU A CA  1 
ATOM   836   C C   . GLU A 1 172 ? -64.448  0.904    -42.443 1.00 193.22 ? 172 GLU A C   1 
ATOM   837   O O   . GLU A 1 172 ? -65.483  0.524    -42.997 1.00 192.30 ? 172 GLU A O   1 
ATOM   838   C CB  . GLU A 1 172 ? -63.025  2.020    -44.228 1.00 190.65 ? 172 GLU A CB  1 
ATOM   839   C CG  . GLU A 1 172 ? -63.044  3.240    -45.139 1.00 199.72 ? 172 GLU A CG  1 
ATOM   840   C CD  . GLU A 1 172 ? -64.054  3.205    -46.273 1.00 216.35 ? 172 GLU A CD  1 
ATOM   841   O OE1 . GLU A 1 172 ? -65.272  3.263    -45.989 1.00 209.77 ? 172 GLU A OE1 1 
ATOM   842   O OE2 . GLU A 1 172 ? -63.626  3.158    -47.450 1.00 206.90 ? 172 GLU A OE2 1 
ATOM   843   N N   . ILE A 1 173 ? -63.863  0.226    -41.432 1.00 190.33 ? 173 ILE A N   1 
ATOM   844   C CA  . ILE A 1 173 ? -64.372  -1.028   -40.871 1.00 190.44 ? 173 ILE A CA  1 
ATOM   845   C C   . ILE A 1 173 ? -65.316  -0.753   -39.675 1.00 194.75 ? 173 ILE A C   1 
ATOM   846   O O   . ILE A 1 173 ? -66.387  -1.363   -39.606 1.00 194.51 ? 173 ILE A O   1 
ATOM   847   C CB  . ILE A 1 173 ? -63.194  -2.017   -40.566 1.00 193.61 ? 173 ILE A CB  1 
ATOM   848   C CG1 . ILE A 1 173 ? -62.979  -3.009   -41.734 1.00 194.11 ? 173 ILE A CG1 1 
ATOM   849   C CG2 . ILE A 1 173 ? -63.345  -2.782   -39.241 1.00 194.27 ? 173 ILE A CG2 1 
ATOM   850   C CD1 . ILE A 1 173 ? -62.280  -2.460   -42.998 1.00 201.45 ? 173 ILE A CD1 1 
ATOM   851   N N   . ASP A 1 174 ? -64.938  0.173    -38.766 1.00 191.35 ? 174 ASP A N   1 
ATOM   852   C CA  . ASP A 1 174 ? -65.750  0.522    -37.594 1.00 217.18 ? 174 ASP A CA  1 
ATOM   853   C C   . ASP A 1 174 ? -66.898  1.467    -37.955 1.00 242.34 ? 174 ASP A C   1 
ATOM   854   O O   . ASP A 1 174 ? -66.691  2.476    -38.626 1.00 199.90 ? 174 ASP A O   1 
ATOM   855   C CB  . ASP A 1 174 ? -64.883  1.117    -36.465 1.00 219.08 ? 174 ASP A CB  1 
ATOM   856   C CG  . ASP A 1 174 ? -63.751  0.227    -35.980 1.00 226.05 ? 174 ASP A CG  1 
ATOM   857   O OD1 . ASP A 1 174 ? -63.943  -1.007   -35.926 1.00 226.26 ? 174 ASP A OD1 1 
ATOM   858   O OD2 . ASP A 1 174 ? -62.680  0.767    -35.635 1.00 230.21 ? 174 ASP A OD2 1 
ATOM   859   N N   . ASN B 2 11  ? -42.805  -33.000  -35.729 1.00 180.19 ? 20  ASN B N   1 
ATOM   860   C CA  . ASN B 2 11  ? -43.755  -33.389  -34.682 1.00 177.86 ? 20  ASN B CA  1 
ATOM   861   C C   . ASN B 2 11  ? -44.135  -34.875  -34.756 1.00 181.82 ? 20  ASN B C   1 
ATOM   862   O O   . ASN B 2 11  ? -44.774  -35.397  -33.838 1.00 179.70 ? 20  ASN B O   1 
ATOM   863   C CB  . ASN B 2 11  ? -45.032  -32.533  -34.744 1.00 176.55 ? 20  ASN B CB  1 
ATOM   864   C CG  . ASN B 2 11  ? -44.820  -31.040  -34.730 1.00 197.91 ? 20  ASN B CG  1 
ATOM   865   O OD1 . ASN B 2 11  ? -44.699  -30.428  -35.791 1.00 193.64 ? 20  ASN B OD1 1 
ATOM   866   N ND2 . ASN B 2 11  ? -44.785  -30.461  -33.506 1.00 187.31 ? 20  ASN B ND2 1 
ATOM   867   N N   . ASN B 2 12  ? -43.720  -35.543  -35.854 1.00 180.97 ? 21  ASN B N   1 
ATOM   868   C CA  . ASN B 2 12  ? -43.989  -36.931  -36.267 1.00 181.92 ? 21  ASN B CA  1 
ATOM   869   C C   . ASN B 2 12  ? -43.810  -38.021  -35.200 1.00 186.18 ? 21  ASN B C   1 
ATOM   870   O O   . ASN B 2 12  ? -44.509  -39.032  -35.279 1.00 185.66 ? 21  ASN B O   1 
ATOM   871   C CB  . ASN B 2 12  ? -43.162  -37.303  -37.523 1.00 185.84 ? 21  ASN B CB  1 
ATOM   872   C CG  . ASN B 2 12  ? -41.746  -37.825  -37.301 1.00 209.90 ? 21  ASN B CG  1 
ATOM   873   O OD1 . ASN B 2 12  ? -41.466  -39.032  -37.410 1.00 203.49 ? 21  ASN B OD1 1 
ATOM   874   N ND2 . ASN B 2 12  ? -40.824  -36.924  -36.986 1.00 202.63 ? 21  ASN B ND2 1 
ATOM   875   N N   . SER B 2 13  ? -42.861  -37.858  -34.260 1.00 183.39 ? 22  SER B N   1 
ATOM   876   C CA  . SER B 2 13  ? -42.555  -38.879  -33.253 1.00 182.99 ? 22  SER B CA  1 
ATOM   877   C C   . SER B 2 13  ? -43.663  -39.125  -32.228 1.00 184.95 ? 22  SER B C   1 
ATOM   878   O O   . SER B 2 13  ? -44.223  -38.180  -31.667 1.00 183.10 ? 22  SER B O   1 
ATOM   879   C CB  . SER B 2 13  ? -41.237  -38.573  -32.550 1.00 187.01 ? 22  SER B CB  1 
ATOM   880   O OG  . SER B 2 13  ? -40.335  -39.658  -32.695 1.00 196.09 ? 22  SER B OG  1 
ATOM   881   N N   . THR B 2 14  ? -43.958  -40.419  -31.988 1.00 181.99 ? 23  THR B N   1 
ATOM   882   C CA  . THR B 2 14  ? -44.976  -40.901  -31.048 1.00 181.05 ? 23  THR B CA  1 
ATOM   883   C C   . THR B 2 14  ? -44.423  -41.049  -29.608 1.00 184.67 ? 23  THR B C   1 
ATOM   884   O O   . THR B 2 14  ? -45.150  -41.531  -28.730 1.00 184.07 ? 23  THR B O   1 
ATOM   885   C CB  . THR B 2 14  ? -45.645  -42.194  -31.581 1.00 190.32 ? 23  THR B CB  1 
ATOM   886   O OG1 . THR B 2 14  ? -46.762  -42.521  -30.752 1.00 190.04 ? 23  THR B OG1 1 
ATOM   887   C CG2 . THR B 2 14  ? -44.684  -43.391  -31.662 1.00 189.20 ? 23  THR B CG2 1 
ATOM   888   N N   . ASP B 2 15  ? -43.149  -40.618  -29.375 1.00 181.00 ? 24  ASP B N   1 
ATOM   889   C CA  . ASP B 2 15  ? -42.420  -40.650  -28.094 1.00 179.85 ? 24  ASP B CA  1 
ATOM   890   C C   . ASP B 2 15  ? -43.306  -40.215  -26.925 1.00 182.63 ? 24  ASP B C   1 
ATOM   891   O O   . ASP B 2 15  ? -44.064  -39.254  -27.071 1.00 182.40 ? 24  ASP B O   1 
ATOM   892   C CB  . ASP B 2 15  ? -41.192  -39.720  -28.161 1.00 181.81 ? 24  ASP B CB  1 
ATOM   893   C CG  . ASP B 2 15  ? -40.060  -40.150  -29.075 1.00 191.63 ? 24  ASP B CG  1 
ATOM   894   O OD1 . ASP B 2 15  ? -40.346  -40.677  -30.171 1.00 193.41 ? 24  ASP B OD1 1 
ATOM   895   O OD2 . ASP B 2 15  ? -38.888  -39.905  -28.720 1.00 196.42 ? 24  ASP B OD2 1 
ATOM   896   N N   . THR B 2 16  ? -43.224  -40.910  -25.775 1.00 178.37 ? 25  THR B N   1 
ATOM   897   C CA  . THR B 2 16  ? -44.075  -40.543  -24.638 1.00 177.85 ? 25  THR B CA  1 
ATOM   898   C C   . THR B 2 16  ? -43.279  -40.296  -23.343 1.00 181.19 ? 25  THR B C   1 
ATOM   899   O O   . THR B 2 16  ? -42.379  -41.067  -23.001 1.00 180.87 ? 25  THR B O   1 
ATOM   900   C CB  . THR B 2 16  ? -45.232  -41.549  -24.455 1.00 186.43 ? 25  THR B CB  1 
ATOM   901   O OG1 . THR B 2 16  ? -46.106  -41.084  -23.428 1.00 186.50 ? 25  THR B OG1 1 
ATOM   902   C CG2 . THR B 2 16  ? -44.767  -42.984  -24.165 1.00 185.25 ? 25  THR B CG2 1 
ATOM   903   N N   . VAL B 2 17  ? -43.623  -39.199  -22.640 1.00 177.65 ? 26  VAL B N   1 
ATOM   904   C CA  . VAL B 2 17  ? -43.013  -38.783  -21.369 1.00 177.68 ? 26  VAL B CA  1 
ATOM   905   C C   . VAL B 2 17  ? -44.063  -38.783  -20.254 1.00 182.15 ? 26  VAL B C   1 
ATOM   906   O O   . VAL B 2 17  ? -45.261  -38.715  -20.538 1.00 182.00 ? 26  VAL B O   1 
ATOM   907   C CB  . VAL B 2 17  ? -42.255  -37.421  -21.442 1.00 181.95 ? 26  VAL B CB  1 
ATOM   908   C CG1 . VAL B 2 17  ? -41.149  -37.438  -22.497 1.00 181.30 ? 26  VAL B CG1 1 
ATOM   909   C CG2 . VAL B 2 17  ? -43.208  -36.250  -21.665 1.00 182.54 ? 26  VAL B CG2 1 
ATOM   910   N N   . ASP B 2 18  ? -43.615  -38.835  -18.993 1.00 179.41 ? 27  ASP B N   1 
ATOM   911   C CA  . ASP B 2 18  ? -44.517  -38.830  -17.845 1.00 181.07 ? 27  ASP B CA  1 
ATOM   912   C C   . ASP B 2 18  ? -44.168  -37.730  -16.835 1.00 185.87 ? 27  ASP B C   1 
ATOM   913   O O   . ASP B 2 18  ? -42.996  -37.376  -16.679 1.00 184.77 ? 27  ASP B O   1 
ATOM   914   C CB  . ASP B 2 18  ? -44.564  -40.218  -17.183 1.00 183.14 ? 27  ASP B CB  1 
ATOM   915   C CG  . ASP B 2 18  ? -45.061  -41.321  -18.102 1.00 192.09 ? 27  ASP B CG  1 
ATOM   916   O OD1 . ASP B 2 18  ? -44.315  -41.704  -19.031 1.00 191.15 ? 27  ASP B OD1 1 
ATOM   917   O OD2 . ASP B 2 18  ? -46.180  -41.820  -17.877 1.00 198.69 ? 27  ASP B OD2 1 
ATOM   918   N N   . THR B 2 19  ? -45.200  -37.180  -16.170 1.00 184.15 ? 28  THR B N   1 
ATOM   919   C CA  . THR B 2 19  ? -45.071  -36.131  -15.151 1.00 185.71 ? 28  THR B CA  1 
ATOM   920   C C   . THR B 2 19  ? -45.692  -36.568  -13.821 1.00 191.94 ? 28  THR B C   1 
ATOM   921   O O   . THR B 2 19  ? -46.292  -37.643  -13.741 1.00 191.89 ? 28  THR B O   1 
ATOM   922   C CB  . THR B 2 19  ? -45.637  -34.790  -15.642 1.00 192.61 ? 28  THR B CB  1 
ATOM   923   O OG1 . THR B 2 19  ? -46.938  -34.987  -16.201 1.00 191.20 ? 28  THR B OG1 1 
ATOM   924   C CG2 . THR B 2 19  ? -44.720  -34.096  -16.630 1.00 189.23 ? 28  THR B CG2 1 
ATOM   925   N N   . VAL B 2 20  ? -45.532  -35.732  -12.778 1.00 190.18 ? 29  VAL B N   1 
ATOM   926   C CA  . VAL B 2 20  ? -46.039  -35.973  -11.423 1.00 192.84 ? 29  VAL B CA  1 
ATOM   927   C C   . VAL B 2 20  ? -47.574  -36.061  -11.400 1.00 197.95 ? 29  VAL B C   1 
ATOM   928   O O   . VAL B 2 20  ? -48.123  -36.916  -10.703 1.00 199.22 ? 29  VAL B O   1 
ATOM   929   C CB  . VAL B 2 20  ? -45.517  -34.919  -10.407 1.00 199.26 ? 29  VAL B CB  1 
ATOM   930   C CG1 . VAL B 2 20  ? -45.625  -35.437  -8.973  1.00 202.03 ? 29  VAL B CG1 1 
ATOM   931   C CG2 . VAL B 2 20  ? -44.080  -34.497  -10.719 1.00 196.54 ? 29  VAL B CG2 1 
ATOM   932   N N   . LEU B 2 21  ? -48.251  -35.183  -12.164 1.00 193.90 ? 30  LEU B N   1 
ATOM   933   C CA  . LEU B 2 21  ? -49.712  -35.109  -12.234 1.00 195.73 ? 30  LEU B CA  1 
ATOM   934   C C   . LEU B 2 21  ? -50.335  -36.166  -13.161 1.00 196.96 ? 30  LEU B C   1 
ATOM   935   O O   . LEU B 2 21  ? -51.025  -37.063  -12.669 1.00 198.09 ? 30  LEU B O   1 
ATOM   936   C CB  . LEU B 2 21  ? -50.171  -33.686  -12.612 1.00 196.82 ? 30  LEU B CB  1 
ATOM   937   C CG  . LEU B 2 21  ? -49.870  -32.590  -11.590 1.00 204.58 ? 30  LEU B CG  1 
ATOM   938   C CD1 . LEU B 2 21  ? -49.252  -31.386  -12.253 1.00 203.23 ? 30  LEU B CD1 1 
ATOM   939   C CD2 . LEU B 2 21  ? -51.119  -32.192  -10.828 1.00 211.78 ? 30  LEU B CD2 1 
ATOM   940   N N   . GLU B 2 22  ? -50.092  -36.061  -14.492 1.00 189.91 ? 31  GLU B N   1 
ATOM   941   C CA  . GLU B 2 22  ? -50.629  -36.976  -15.511 1.00 187.64 ? 31  GLU B CA  1 
ATOM   942   C C   . GLU B 2 22  ? -49.562  -37.882  -16.138 1.00 187.17 ? 31  GLU B C   1 
ATOM   943   O O   . GLU B 2 22  ? -48.411  -37.469  -16.294 1.00 185.00 ? 31  GLU B O   1 
ATOM   944   C CB  . GLU B 2 22  ? -51.430  -36.219  -16.594 1.00 188.42 ? 31  GLU B CB  1 
ATOM   945   C CG  . GLU B 2 22  ? -50.623  -35.243  -17.443 1.00 197.13 ? 31  GLU B CG  1 
ATOM   946   C CD  . GLU B 2 22  ? -51.330  -34.644  -18.647 1.00 214.40 ? 31  GLU B CD  1 
ATOM   947   O OE1 . GLU B 2 22  ? -52.090  -35.371  -19.328 1.00 205.67 ? 31  GLU B OE1 1 
ATOM   948   O OE2 . GLU B 2 22  ? -51.077  -33.453  -18.941 1.00 206.87 ? 31  GLU B OE2 1 
ATOM   949   N N   . LYS B 2 23  ? -49.962  -39.111  -16.508 1.00 182.49 ? 32  LYS B N   1 
ATOM   950   C CA  . LYS B 2 23  ? -49.079  -40.115  -17.107 1.00 179.52 ? 32  LYS B CA  1 
ATOM   951   C C   . LYS B 2 23  ? -49.351  -40.316  -18.603 1.00 181.82 ? 32  LYS B C   1 
ATOM   952   O O   . LYS B 2 23  ? -50.474  -40.097  -19.059 1.00 181.97 ? 32  LYS B O   1 
ATOM   953   C CB  . LYS B 2 23  ? -49.175  -41.458  -16.346 1.00 182.39 ? 32  LYS B CB  1 
ATOM   954   C CG  . LYS B 2 23  ? -48.705  -41.415  -14.886 1.00 190.72 ? 32  LYS B CG  1 
ATOM   955   C CD  . LYS B 2 23  ? -47.181  -41.474  -14.736 1.00 194.47 ? 32  LYS B CD  1 
ATOM   956   C CE  . LYS B 2 23  ? -46.720  -41.456  -13.298 1.00 203.23 ? 32  LYS B CE  1 
ATOM   957   N NZ  . LYS B 2 23  ? -46.918  -40.130  -12.657 1.00 212.93 ? 32  LYS B NZ  1 
ATOM   958   N N   . ASN B 2 24  ? -48.306  -40.744  -19.353 1.00 176.76 ? 33  ASN B N   1 
ATOM   959   C CA  . ASN B 2 24  ? -48.282  -41.031  -20.799 1.00 175.27 ? 33  ASN B CA  1 
ATOM   960   C C   . ASN B 2 24  ? -48.738  -39.842  -21.673 1.00 177.08 ? 33  ASN B C   1 
ATOM   961   O O   . ASN B 2 24  ? -49.863  -39.826  -22.182 1.00 176.59 ? 33  ASN B O   1 
ATOM   962   C CB  . ASN B 2 24  ? -49.047  -42.323  -21.151 1.00 179.58 ? 33  ASN B CB  1 
ATOM   963   C CG  . ASN B 2 24  ? -48.257  -43.588  -20.906 1.00 211.03 ? 33  ASN B CG  1 
ATOM   964   O OD1 . ASN B 2 24  ? -48.443  -44.282  -19.900 1.00 209.25 ? 33  ASN B OD1 1 
ATOM   965   N ND2 . ASN B 2 24  ? -47.363  -43.926  -21.827 1.00 202.23 ? 33  ASN B ND2 1 
ATOM   966   N N   . VAL B 2 25  ? -47.833  -38.855  -21.848 1.00 172.03 ? 34  VAL B N   1 
ATOM   967   C CA  . VAL B 2 25  ? -48.056  -37.645  -22.651 1.00 170.95 ? 34  VAL B CA  1 
ATOM   968   C C   . VAL B 2 25  ? -47.112  -37.670  -23.861 1.00 172.18 ? 34  VAL B C   1 
ATOM   969   O O   . VAL B 2 25  ? -45.894  -37.746  -23.680 1.00 171.45 ? 34  VAL B O   1 
ATOM   970   C CB  . VAL B 2 25  ? -47.891  -36.334  -21.826 1.00 175.81 ? 34  VAL B CB  1 
ATOM   971   C CG1 . VAL B 2 25  ? -48.398  -35.124  -22.609 1.00 175.52 ? 34  VAL B CG1 1 
ATOM   972   C CG2 . VAL B 2 25  ? -48.592  -36.426  -20.470 1.00 177.61 ? 34  VAL B CG2 1 
ATOM   973   N N   . THR B 2 26  ? -47.677  -37.602  -25.086 1.00 167.17 ? 35  THR B N   1 
ATOM   974   C CA  . THR B 2 26  ? -46.912  -37.617  -26.340 1.00 165.80 ? 35  THR B CA  1 
ATOM   975   C C   . THR B 2 26  ? -46.035  -36.363  -26.451 1.00 169.00 ? 35  THR B C   1 
ATOM   976   O O   . THR B 2 26  ? -46.509  -35.265  -26.158 1.00 169.60 ? 35  THR B O   1 
ATOM   977   C CB  . THR B 2 26  ? -47.829  -37.820  -27.558 1.00 171.17 ? 35  THR B CB  1 
ATOM   978   O OG1 . THR B 2 26  ? -48.868  -38.746  -27.238 1.00 169.64 ? 35  THR B OG1 1 
ATOM   979   C CG2 . THR B 2 26  ? -47.067  -38.310  -28.784 1.00 169.33 ? 35  THR B CG2 1 
ATOM   980   N N   . VAL B 2 27  ? -44.757  -36.536  -26.843 1.00 163.99 ? 36  VAL B N   1 
ATOM   981   C CA  . VAL B 2 27  ? -43.789  -35.446  -26.964 1.00 163.29 ? 36  VAL B CA  1 
ATOM   982   C C   . VAL B 2 27  ? -42.922  -35.590  -28.236 1.00 166.50 ? 36  VAL B C   1 
ATOM   983   O O   . VAL B 2 27  ? -42.530  -36.695  -28.616 1.00 166.28 ? 36  VAL B O   1 
ATOM   984   C CB  . VAL B 2 27  ? -42.971  -35.289  -25.646 1.00 166.94 ? 36  VAL B CB  1 
ATOM   985   C CG1 . VAL B 2 27  ? -41.511  -34.905  -25.884 1.00 167.08 ? 36  VAL B CG1 1 
ATOM   986   C CG2 . VAL B 2 27  ? -43.642  -34.284  -24.719 1.00 167.10 ? 36  VAL B CG2 1 
ATOM   987   N N   . THR B 2 28  ? -42.634  -34.443  -28.873 1.00 162.55 ? 37  THR B N   1 
ATOM   988   C CA  . THR B 2 28  ? -41.837  -34.303  -30.090 1.00 162.69 ? 37  THR B CA  1 
ATOM   989   C C   . THR B 2 28  ? -40.353  -34.631  -29.840 1.00 165.90 ? 37  THR B C   1 
ATOM   990   O O   . THR B 2 28  ? -39.903  -35.706  -30.235 1.00 165.34 ? 37  THR B O   1 
ATOM   991   C CB  . THR B 2 28  ? -42.065  -32.906  -30.703 1.00 169.57 ? 37  THR B CB  1 
ATOM   992   O OG1 . THR B 2 28  ? -41.673  -31.908  -29.756 1.00 168.18 ? 37  THR B OG1 1 
ATOM   993   C CG2 . THR B 2 28  ? -43.514  -32.675  -31.099 1.00 166.85 ? 37  THR B CG2 1 
ATOM   994   N N   . HIS B 2 29  ? -39.612  -33.721  -29.166 1.00 162.67 ? 38  HIS B N   1 
ATOM   995   C CA  . HIS B 2 29  ? -38.184  -33.869  -28.859 1.00 163.32 ? 38  HIS B CA  1 
ATOM   996   C C   . HIS B 2 29  ? -37.944  -34.421  -27.445 1.00 165.83 ? 38  HIS B C   1 
ATOM   997   O O   . HIS B 2 29  ? -38.131  -33.708  -26.451 1.00 164.89 ? 38  HIS B O   1 
ATOM   998   C CB  . HIS B 2 29  ? -37.427  -32.537  -29.051 1.00 165.44 ? 38  HIS B CB  1 
ATOM   999   C CG  . HIS B 2 29  ? -37.628  -31.858  -30.374 1.00 169.80 ? 38  HIS B CG  1 
ATOM   1000  N ND1 . HIS B 2 29  ? -37.965  -30.515  -30.449 1.00 171.70 ? 38  HIS B ND1 1 
ATOM   1001  C CD2 . HIS B 2 29  ? -37.497  -32.345  -31.630 1.00 172.51 ? 38  HIS B CD2 1 
ATOM   1002  C CE1 . HIS B 2 29  ? -38.039  -30.236  -31.738 1.00 172.15 ? 38  HIS B CE1 1 
ATOM   1003  N NE2 . HIS B 2 29  ? -37.762  -31.304  -32.486 1.00 173.20 ? 38  HIS B NE2 1 
ATOM   1004  N N   . SER B 2 30  ? -37.515  -35.694  -27.366 1.00 161.91 ? 39  SER B N   1 
ATOM   1005  C CA  . SER B 2 30  ? -37.259  -36.377  -26.098 1.00 160.50 ? 39  SER B CA  1 
ATOM   1006  C C   . SER B 2 30  ? -36.133  -37.412  -26.201 1.00 162.69 ? 39  SER B C   1 
ATOM   1007  O O   . SER B 2 30  ? -36.015  -38.100  -27.216 1.00 163.33 ? 39  SER B O   1 
ATOM   1008  C CB  . SER B 2 30  ? -38.532  -37.042  -25.585 1.00 163.98 ? 39  SER B CB  1 
ATOM   1009  O OG  . SER B 2 30  ? -39.054  -37.949  -26.543 1.00 174.81 ? 39  SER B OG  1 
ATOM   1010  N N   . VAL B 2 31  ? -35.331  -37.539  -25.129 1.00 156.77 ? 40  VAL B N   1 
ATOM   1011  C CA  . VAL B 2 31  ? -34.208  -38.474  -25.060 1.00 155.80 ? 40  VAL B CA  1 
ATOM   1012  C C   . VAL B 2 31  ? -34.386  -39.494  -23.918 1.00 155.95 ? 40  VAL B C   1 
ATOM   1013  O O   . VAL B 2 31  ? -34.890  -39.140  -22.852 1.00 154.58 ? 40  VAL B O   1 
ATOM   1014  C CB  . VAL B 2 31  ? -32.847  -37.715  -25.009 1.00 160.76 ? 40  VAL B CB  1 
ATOM   1015  C CG1 . VAL B 2 31  ? -32.549  -37.127  -23.628 1.00 159.63 ? 40  VAL B CG1 1 
ATOM   1016  C CG2 . VAL B 2 31  ? -31.698  -38.589  -25.494 1.00 161.52 ? 40  VAL B CG2 1 
ATOM   1017  N N   . ASN B 2 32  ? -33.976  -40.754  -24.157 1.00 150.97 ? 41  ASN B N   1 
ATOM   1018  C CA  . ASN B 2 32  ? -34.024  -41.851  -23.183 1.00 148.99 ? 41  ASN B CA  1 
ATOM   1019  C C   . ASN B 2 32  ? -32.849  -41.716  -22.195 1.00 152.43 ? 41  ASN B C   1 
ATOM   1020  O O   . ASN B 2 32  ? -31.933  -40.927  -22.440 1.00 153.11 ? 41  ASN B O   1 
ATOM   1021  C CB  . ASN B 2 32  ? -33.970  -43.208  -23.917 1.00 149.44 ? 41  ASN B CB  1 
ATOM   1022  C CG  . ASN B 2 32  ? -34.327  -44.441  -23.101 1.00 173.60 ? 41  ASN B CG  1 
ATOM   1023  O OD1 . ASN B 2 32  ? -34.986  -44.381  -22.057 1.00 166.34 ? 41  ASN B OD1 1 
ATOM   1024  N ND2 . ASN B 2 32  ? -33.926  -45.608  -23.591 1.00 167.02 ? 41  ASN B ND2 1 
ATOM   1025  N N   . LEU B 2 33  ? -32.889  -42.460  -21.071 1.00 147.61 ? 42  LEU B N   1 
ATOM   1026  C CA  . LEU B 2 33  ? -31.842  -42.461  -20.038 1.00 146.41 ? 42  LEU B CA  1 
ATOM   1027  C C   . LEU B 2 33  ? -31.511  -43.885  -19.613 1.00 148.69 ? 42  LEU B C   1 
ATOM   1028  O O   . LEU B 2 33  ? -30.415  -44.148  -19.122 1.00 147.49 ? 42  LEU B O   1 
ATOM   1029  C CB  . LEU B 2 33  ? -32.295  -41.677  -18.791 1.00 145.98 ? 42  LEU B CB  1 
ATOM   1030  C CG  . LEU B 2 33  ? -32.647  -40.209  -18.962 1.00 151.95 ? 42  LEU B CG  1 
ATOM   1031  C CD1 . LEU B 2 33  ? -33.470  -39.725  -17.800 1.00 152.28 ? 42  LEU B CD1 1 
ATOM   1032  C CD2 . LEU B 2 33  ? -31.405  -39.356  -19.128 1.00 155.26 ? 42  LEU B CD2 1 
ATOM   1033  N N   . LEU B 2 34  ? -32.482  -44.790  -19.782 1.00 144.76 ? 43  LEU B N   1 
ATOM   1034  C CA  . LEU B 2 34  ? -32.424  -46.183  -19.367 1.00 143.42 ? 43  LEU B CA  1 
ATOM   1035  C C   . LEU B 2 34  ? -32.028  -47.137  -20.491 1.00 147.45 ? 43  LEU B C   1 
ATOM   1036  O O   . LEU B 2 34  ? -32.526  -47.014  -21.615 1.00 148.65 ? 43  LEU B O   1 
ATOM   1037  C CB  . LEU B 2 34  ? -33.805  -46.559  -18.801 1.00 143.38 ? 43  LEU B CB  1 
ATOM   1038  C CG  . LEU B 2 34  ? -33.913  -47.820  -17.954 1.00 147.07 ? 43  LEU B CG  1 
ATOM   1039  C CD1 . LEU B 2 34  ? -34.668  -47.538  -16.677 1.00 146.77 ? 43  LEU B CD1 1 
ATOM   1040  C CD2 . LEU B 2 34  ? -34.628  -48.912  -18.720 1.00 150.93 ? 43  LEU B CD2 1 
ATOM   1041  N N   . GLU B 2 35  ? -31.149  -48.111  -20.163 1.00 142.45 ? 44  GLU B N   1 
ATOM   1042  C CA  . GLU B 2 35  ? -30.725  -49.181  -21.062 1.00 142.98 ? 44  GLU B CA  1 
ATOM   1043  C C   . GLU B 2 35  ? -31.198  -50.514  -20.492 1.00 144.98 ? 44  GLU B C   1 
ATOM   1044  O O   . GLU B 2 35  ? -30.794  -50.908  -19.398 1.00 142.83 ? 44  GLU B O   1 
ATOM   1045  C CB  . GLU B 2 35  ? -29.208  -49.181  -21.321 1.00 144.79 ? 44  GLU B CB  1 
ATOM   1046  C CG  . GLU B 2 35  ? -28.773  -50.190  -22.382 1.00 158.59 ? 44  GLU B CG  1 
ATOM   1047  C CD  . GLU B 2 35  ? -29.027  -49.851  -23.843 1.00 186.83 ? 44  GLU B CD  1 
ATOM   1048  O OE1 . GLU B 2 35  ? -28.093  -50.040  -24.655 1.00 182.21 ? 44  GLU B OE1 1 
ATOM   1049  O OE2 . GLU B 2 35  ? -30.160  -49.444  -24.188 1.00 183.95 ? 44  GLU B OE2 1 
ATOM   1050  N N   . ASP B 2 36  ? -32.088  -51.178  -21.230 1.00 142.24 ? 45  ASP B N   1 
ATOM   1051  C CA  . ASP B 2 36  ? -32.707  -52.454  -20.877 1.00 141.62 ? 45  ASP B CA  1 
ATOM   1052  C C   . ASP B 2 36  ? -32.120  -53.626  -21.655 1.00 144.87 ? 45  ASP B C   1 
ATOM   1053  O O   . ASP B 2 36  ? -32.287  -54.776  -21.242 1.00 143.39 ? 45  ASP B O   1 
ATOM   1054  C CB  . ASP B 2 36  ? -34.228  -52.381  -21.102 1.00 145.00 ? 45  ASP B CB  1 
ATOM   1055  C CG  . ASP B 2 36  ? -34.634  -51.585  -22.332 1.00 161.88 ? 45  ASP B CG  1 
ATOM   1056  O OD1 . ASP B 2 36  ? -34.783  -50.349  -22.216 1.00 162.38 ? 45  ASP B OD1 1 
ATOM   1057  O OD2 . ASP B 2 36  ? -34.764  -52.195  -23.419 1.00 171.55 ? 45  ASP B OD2 1 
ATOM   1058  N N   . LYS B 2 37  ? -31.491  -53.344  -22.809 1.00 149.32 ? 46  LYS B N   1 
ATOM   1059  C CA  . LYS B 2 37  ? -30.898  -54.355  -23.689 1.00 148.02 ? 46  LYS B CA  1 
ATOM   1060  C C   . LYS B 2 37  ? -29.469  -54.744  -23.270 1.00 149.27 ? 46  LYS B C   1 
ATOM   1061  O O   . LYS B 2 37  ? -28.679  -53.882  -22.872 1.00 148.34 ? 46  LYS B O   1 
ATOM   1062  C CB  . LYS B 2 37  ? -30.973  -53.954  -25.188 1.00 152.00 ? 46  LYS B CB  1 
ATOM   1063  C CG  . LYS B 2 37  ? -31.064  -52.448  -25.490 1.00 157.43 ? 46  LYS B CG  1 
ATOM   1064  C CD  . LYS B 2 37  ? -32.467  -52.035  -25.944 1.00 162.28 ? 46  LYS B CD  1 
ATOM   1065  C CE  . LYS B 2 37  ? -32.618  -50.546  -26.176 1.00 166.24 ? 46  LYS B CE  1 
ATOM   1066  N NZ  . LYS B 2 37  ? -32.844  -49.796  -24.910 1.00 168.71 ? 46  LYS B NZ  1 
ATOM   1067  N N   . HIS B 2 38  ? -29.159  -56.060  -23.346 1.00 144.24 ? 47  HIS B N   1 
ATOM   1068  C CA  . HIS B 2 38  ? -27.863  -56.663  -23.001 1.00 141.80 ? 47  HIS B CA  1 
ATOM   1069  C C   . HIS B 2 38  ? -27.734  -58.081  -23.598 1.00 145.37 ? 47  HIS B C   1 
ATOM   1070  O O   . HIS B 2 38  ? -28.747  -58.729  -23.885 1.00 145.89 ? 47  HIS B O   1 
ATOM   1071  C CB  . HIS B 2 38  ? -27.695  -56.733  -21.470 1.00 140.61 ? 47  HIS B CB  1 
ATOM   1072  C CG  . HIS B 2 38  ? -28.557  -57.773  -20.831 1.00 143.50 ? 47  HIS B CG  1 
ATOM   1073  N ND1 . HIS B 2 38  ? -28.040  -58.994  -20.441 1.00 143.92 ? 47  HIS B ND1 1 
ATOM   1074  C CD2 . HIS B 2 38  ? -29.890  -57.768  -20.600 1.00 146.38 ? 47  HIS B CD2 1 
ATOM   1075  C CE1 . HIS B 2 38  ? -29.063  -59.676  -19.953 1.00 143.81 ? 47  HIS B CE1 1 
ATOM   1076  N NE2 . HIS B 2 38  ? -30.198  -58.978  -20.028 1.00 145.56 ? 47  HIS B NE2 1 
ATOM   1077  N N   . ASN B 2 39  ? -26.485  -58.566  -23.746 1.00 140.72 ? 48  ASN B N   1 
ATOM   1078  C CA  . ASN B 2 39  ? -26.182  -59.913  -24.236 1.00 140.45 ? 48  ASN B CA  1 
ATOM   1079  C C   . ASN B 2 39  ? -26.017  -60.826  -23.026 1.00 144.61 ? 48  ASN B C   1 
ATOM   1080  O O   . ASN B 2 39  ? -25.608  -60.356  -21.967 1.00 143.26 ? 48  ASN B O   1 
ATOM   1081  C CB  . ASN B 2 39  ? -24.887  -59.913  -25.075 1.00 137.14 ? 48  ASN B CB  1 
ATOM   1082  C CG  . ASN B 2 39  ? -23.636  -59.412  -24.375 1.00 138.68 ? 48  ASN B CG  1 
ATOM   1083  O OD1 . ASN B 2 39  ? -23.682  -58.669  -23.398 1.00 125.53 ? 48  ASN B OD1 1 
ATOM   1084  N ND2 . ASN B 2 39  ? -22.482  -59.751  -24.911 1.00 127.66 ? 48  ASN B ND2 1 
ATOM   1085  N N   . GLY B 2 40  ? -26.295  -62.114  -23.189 1.00 142.22 ? 49  GLY B N   1 
ATOM   1086  C CA  . GLY B 2 40  ? -26.140  -63.084  -22.107 1.00 141.06 ? 49  GLY B CA  1 
ATOM   1087  C C   . GLY B 2 40  ? -24.696  -63.446  -21.808 1.00 143.99 ? 49  GLY B C   1 
ATOM   1088  O O   . GLY B 2 40  ? -24.428  -64.201  -20.870 1.00 142.76 ? 49  GLY B O   1 
ATOM   1089  N N   . LYS B 2 41  ? -23.757  -62.903  -22.600 1.00 140.96 ? 50  LYS B N   1 
ATOM   1090  C CA  . LYS B 2 41  ? -22.322  -63.162  -22.509 1.00 140.24 ? 50  LYS B CA  1 
ATOM   1091  C C   . LYS B 2 41  ? -21.637  -62.337  -21.428 1.00 143.53 ? 50  LYS B C   1 
ATOM   1092  O O   . LYS B 2 41  ? -22.038  -61.197  -21.178 1.00 143.21 ? 50  LYS B O   1 
ATOM   1093  C CB  . LYS B 2 41  ? -21.645  -62.882  -23.866 1.00 143.94 ? 50  LYS B CB  1 
ATOM   1094  C CG  . LYS B 2 41  ? -22.179  -63.705  -25.047 1.00 157.12 ? 50  LYS B CG  1 
ATOM   1095  C CD  . LYS B 2 41  ? -21.620  -63.231  -26.396 1.00 161.98 ? 50  LYS B CD  1 
ATOM   1096  C CE  . LYS B 2 41  ? -22.598  -62.363  -27.159 1.00 163.69 ? 50  LYS B CE  1 
ATOM   1097  N NZ  . LYS B 2 41  ? -21.930  -61.551  -28.211 1.00 166.51 ? 50  LYS B NZ  1 
ATOM   1098  N N   . LEU B 2 42  ? -20.588  -62.918  -20.802 1.00 139.58 ? 51  LEU B N   1 
ATOM   1099  C CA  . LEU B 2 42  ? -19.724  -62.266  -19.809 1.00 137.70 ? 51  LEU B CA  1 
ATOM   1100  C C   . LEU B 2 42  ? -18.412  -61.926  -20.537 1.00 141.66 ? 51  LEU B C   1 
ATOM   1101  O O   . LEU B 2 42  ? -17.443  -62.684  -20.499 1.00 140.95 ? 51  LEU B O   1 
ATOM   1102  C CB  . LEU B 2 42  ? -19.454  -63.158  -18.576 1.00 136.51 ? 51  LEU B CB  1 
ATOM   1103  C CG  . LEU B 2 42  ? -20.625  -63.495  -17.657 1.00 140.66 ? 51  LEU B CG  1 
ATOM   1104  C CD1 . LEU B 2 42  ? -20.227  -64.567  -16.673 1.00 140.46 ? 51  LEU B CD1 1 
ATOM   1105  C CD2 . LEU B 2 42  ? -21.110  -62.279  -16.893 1.00 141.80 ? 51  LEU B CD2 1 
ATOM   1106  N N   . CYS B 2 43  ? -18.423  -60.805  -21.254 1.00 138.79 ? 52  CYS B N   1 
ATOM   1107  C CA  . CYS B 2 43  ? -17.305  -60.327  -22.061 1.00 139.42 ? 52  CYS B CA  1 
ATOM   1108  C C   . CYS B 2 43  ? -16.113  -59.871  -21.221 1.00 138.96 ? 52  CYS B C   1 
ATOM   1109  O O   . CYS B 2 43  ? -16.282  -59.521  -20.055 1.00 137.89 ? 52  CYS B O   1 
ATOM   1110  C CB  . CYS B 2 43  ? -17.777  -59.226  -23.005 1.00 142.27 ? 52  CYS B CB  1 
ATOM   1111  S SG  . CYS B 2 43  ? -19.207  -59.678  -24.029 1.00 148.27 ? 52  CYS B SG  1 
ATOM   1112  N N   . LYS B 2 44  ? -14.907  -59.887  -21.821 1.00 133.36 ? 53  LYS B N   1 
ATOM   1113  C CA  . LYS B 2 44  ? -13.657  -59.452  -21.192 1.00 131.59 ? 53  LYS B CA  1 
ATOM   1114  C C   . LYS B 2 44  ? -13.733  -57.943  -21.009 1.00 134.63 ? 53  LYS B C   1 
ATOM   1115  O O   . LYS B 2 44  ? -14.135  -57.242  -21.938 1.00 135.67 ? 53  LYS B O   1 
ATOM   1116  C CB  . LYS B 2 44  ? -12.450  -59.794  -22.087 1.00 134.91 ? 53  LYS B CB  1 
ATOM   1117  C CG  . LYS B 2 44  ? -12.305  -61.268  -22.431 1.00 146.82 ? 53  LYS B CG  1 
ATOM   1118  C CD  . LYS B 2 44  ? -11.202  -61.491  -23.453 1.00 157.46 ? 53  LYS B CD  1 
ATOM   1119  C CE  . LYS B 2 44  ? -11.144  -62.924  -23.922 1.00 165.18 ? 53  LYS B CE  1 
ATOM   1120  N NZ  . LYS B 2 44  ? -10.010  -63.151  -24.852 1.00 171.64 ? 53  LYS B NZ  1 
ATOM   1121  N N   . LEU B 2 45  ? -13.386  -57.439  -19.820 1.00 129.94 ? 54  LEU B N   1 
ATOM   1122  C CA  . LEU B 2 45  ? -13.426  -55.996  -19.574 1.00 130.86 ? 54  LEU B CA  1 
ATOM   1123  C C   . LEU B 2 45  ? -12.197  -55.330  -20.181 1.00 137.14 ? 54  LEU B C   1 
ATOM   1124  O O   . LEU B 2 45  ? -11.078  -55.767  -19.923 1.00 136.25 ? 54  LEU B O   1 
ATOM   1125  C CB  . LEU B 2 45  ? -13.550  -55.676  -18.070 1.00 129.82 ? 54  LEU B CB  1 
ATOM   1126  C CG  . LEU B 2 45  ? -13.564  -54.191  -17.665 1.00 135.75 ? 54  LEU B CG  1 
ATOM   1127  C CD1 . LEU B 2 45  ? -14.984  -53.645  -17.598 1.00 136.17 ? 54  LEU B CD1 1 
ATOM   1128  C CD2 . LEU B 2 45  ? -12.859  -53.981  -16.334 1.00 137.71 ? 54  LEU B CD2 1 
ATOM   1129  N N   . ARG B 2 46  ? -12.421  -54.272  -20.991 1.00 136.50 ? 55  ARG B N   1 
ATOM   1130  C CA  . ARG B 2 46  ? -11.420  -53.445  -21.684 1.00 138.94 ? 55  ARG B CA  1 
ATOM   1131  C C   . ARG B 2 46  ? -10.211  -54.252  -22.212 1.00 142.69 ? 55  ARG B C   1 
ATOM   1132  O O   . ARG B 2 46  ? -9.061   -53.823  -22.074 1.00 143.77 ? 55  ARG B O   1 
ATOM   1133  C CB  . ARG B 2 46  ? -10.977  -52.216  -20.833 1.00 141.95 ? 55  ARG B CB  1 
ATOM   1134  C CG  . ARG B 2 46  ? -10.502  -52.471  -19.388 1.00 153.88 ? 55  ARG B CG  1 
ATOM   1135  C CD  . ARG B 2 46  ? -10.329  -51.166  -18.615 1.00 168.47 ? 55  ARG B CD  1 
ATOM   1136  N NE  . ARG B 2 46  ? -10.248  -51.371  -17.163 1.00 178.18 ? 55  ARG B NE  1 
ATOM   1137  C CZ  . ARG B 2 46  ? -10.106  -50.395  -16.266 1.00 195.06 ? 55  ARG B CZ  1 
ATOM   1138  N NH1 . ARG B 2 46  ? -10.026  -49.127  -16.658 1.00 186.18 ? 55  ARG B NH1 1 
ATOM   1139  N NH2 . ARG B 2 46  ? -10.042  -50.680  -14.972 1.00 180.04 ? 55  ARG B NH2 1 
ATOM   1140  N N   . GLY B 2 47  A -10.496  -55.399  -22.829 1.00 137.78 ? 55  GLY B N   1 
ATOM   1141  C CA  . GLY B 2 47  A -9.466   -56.268  -23.384 1.00 137.80 ? 55  GLY B CA  1 
ATOM   1142  C C   . GLY B 2 47  A -9.035   -57.410  -22.486 1.00 139.51 ? 55  GLY B C   1 
ATOM   1143  O O   . GLY B 2 47  A -8.966   -58.551  -22.953 1.00 139.56 ? 55  GLY B O   1 
ATOM   1144  N N   . VAL B 2 48  ? -8.725   -57.109  -21.194 1.00 133.60 ? 56  VAL B N   1 
ATOM   1145  C CA  . VAL B 2 48  ? -8.263   -58.089  -20.190 1.00 130.93 ? 56  VAL B CA  1 
ATOM   1146  C C   . VAL B 2 48  ? -9.354   -59.118  -19.840 1.00 130.41 ? 56  VAL B C   1 
ATOM   1147  O O   . VAL B 2 48  ? -10.503  -58.749  -19.583 1.00 130.02 ? 56  VAL B O   1 
ATOM   1148  C CB  . VAL B 2 48  ? -7.618   -57.471  -18.913 1.00 134.47 ? 56  VAL B CB  1 
ATOM   1149  C CG1 . VAL B 2 48  ? -6.114   -57.304  -19.089 1.00 135.88 ? 56  VAL B CG1 1 
ATOM   1150  C CG2 . VAL B 2 48  ? -8.268   -56.151  -18.502 1.00 134.52 ? 56  VAL B CG2 1 
ATOM   1151  N N   . ALA B 2 49  ? -8.981   -60.412  -19.861 1.00 123.37 ? 57  ALA B N   1 
ATOM   1152  C CA  . ALA B 2 49  ? -9.873   -61.544  -19.605 1.00 120.71 ? 57  ALA B CA  1 
ATOM   1153  C C   . ALA B 2 49  ? -10.188  -61.775  -18.115 1.00 119.16 ? 57  ALA B C   1 
ATOM   1154  O O   . ALA B 2 49  ? -9.309   -61.570  -17.279 1.00 118.50 ? 57  ALA B O   1 
ATOM   1155  C CB  . ALA B 2 49  ? -9.295   -62.804  -20.227 1.00 122.45 ? 57  ALA B CB  1 
ATOM   1156  N N   . PRO B 2 50  ? -11.418  -62.220  -17.755 1.00 112.01 ? 58  PRO B N   1 
ATOM   1157  C CA  . PRO B 2 50  ? -11.722  -62.452  -16.334 1.00 109.33 ? 58  PRO B CA  1 
ATOM   1158  C C   . PRO B 2 50  ? -11.191  -63.784  -15.813 1.00 109.85 ? 58  PRO B C   1 
ATOM   1159  O O   . PRO B 2 50  ? -10.819  -64.651  -16.606 1.00 110.73 ? 58  PRO B O   1 
ATOM   1160  C CB  . PRO B 2 50  ? -13.250  -62.404  -16.291 1.00 110.77 ? 58  PRO B CB  1 
ATOM   1161  C CG  . PRO B 2 50  ? -13.675  -62.869  -17.616 1.00 116.74 ? 58  PRO B CG  1 
ATOM   1162  C CD  . PRO B 2 50  ? -12.590  -62.521  -18.604 1.00 113.76 ? 58  PRO B CD  1 
ATOM   1163  N N   . LEU B 2 51  ? -11.171  -63.945  -14.477 1.00 102.55 ? 59  LEU B N   1 
ATOM   1164  C CA  . LEU B 2 51  ? -10.709  -65.157  -13.808 1.00 101.27 ? 59  LEU B CA  1 
ATOM   1165  C C   . LEU B 2 51  ? -11.916  -66.006  -13.407 1.00 105.34 ? 59  LEU B C   1 
ATOM   1166  O O   . LEU B 2 51  ? -12.569  -65.705  -12.407 1.00 105.03 ? 59  LEU B O   1 
ATOM   1167  C CB  . LEU B 2 51  ? -9.845   -64.787  -12.587 1.00 100.22 ? 59  LEU B CB  1 
ATOM   1168  C CG  . LEU B 2 51  ? -9.169   -65.941  -11.860 1.00 104.81 ? 59  LEU B CG  1 
ATOM   1169  C CD1 . LEU B 2 51  ? -7.680   -65.958  -12.119 1.00 104.99 ? 59  LEU B CD1 1 
ATOM   1170  C CD2 . LEU B 2 51  ? -9.426   -65.861  -10.372 1.00 108.67 ? 59  LEU B CD2 1 
ATOM   1171  N N   . HIS B 2 52  ? -12.229  -67.048  -14.201 1.00 102.67 ? 60  HIS B N   1 
ATOM   1172  C CA  . HIS B 2 52  ? -13.355  -67.942  -13.926 1.00 102.91 ? 60  HIS B CA  1 
ATOM   1173  C C   . HIS B 2 52  ? -12.900  -69.176  -13.162 1.00 108.78 ? 60  HIS B C   1 
ATOM   1174  O O   . HIS B 2 52  ? -11.991  -69.888  -13.598 1.00 109.47 ? 60  HIS B O   1 
ATOM   1175  C CB  . HIS B 2 52  ? -14.098  -68.334  -15.210 1.00 104.73 ? 60  HIS B CB  1 
ATOM   1176  C CG  . HIS B 2 52  ? -15.335  -69.152  -14.977 1.00 108.89 ? 60  HIS B CG  1 
ATOM   1177  N ND1 . HIS B 2 52  ? -16.575  -68.558  -14.821 1.00 110.03 ? 60  HIS B ND1 1 
ATOM   1178  C CD2 . HIS B 2 52  ? -15.483  -70.496  -14.892 1.00 112.41 ? 60  HIS B CD2 1 
ATOM   1179  C CE1 . HIS B 2 52  ? -17.434  -69.552  -14.653 1.00 110.72 ? 60  HIS B CE1 1 
ATOM   1180  N NE2 . HIS B 2 52  ? -16.823  -70.736  -14.688 1.00 112.61 ? 60  HIS B NE2 1 
ATOM   1181  N N   . LEU B 2 53  ? -13.557  -69.426  -12.025 1.00 106.08 ? 61  LEU B N   1 
ATOM   1182  C CA  . LEU B 2 53  ? -13.279  -70.552  -11.144 1.00 107.47 ? 61  LEU B CA  1 
ATOM   1183  C C   . LEU B 2 53  ? -14.473  -71.515  -11.146 1.00 115.40 ? 61  LEU B C   1 
ATOM   1184  O O   . LEU B 2 53  ? -15.345  -71.449  -10.276 1.00 114.78 ? 61  LEU B O   1 
ATOM   1185  C CB  . LEU B 2 53  ? -12.952  -70.066  -9.709  1.00 106.06 ? 61  LEU B CB  1 
ATOM   1186  C CG  . LEU B 2 53  ? -11.912  -68.951  -9.543  1.00 108.85 ? 61  LEU B CG  1 
ATOM   1187  C CD1 . LEU B 2 53  ? -12.064  -68.260  -8.207  1.00 107.47 ? 61  LEU B CD1 1 
ATOM   1188  C CD2 . LEU B 2 53  ? -10.510  -69.486  -9.688  1.00 112.31 ? 61  LEU B CD2 1 
ATOM   1189  N N   . GLY B 2 54  ? -14.528  -72.365  -12.162 1.00 115.74 ? 62  GLY B N   1 
ATOM   1190  C CA  . GLY B 2 54  ? -15.570  -73.380  -12.276 1.00 118.48 ? 62  GLY B CA  1 
ATOM   1191  C C   . GLY B 2 54  ? -15.251  -74.536  -11.350 1.00 126.00 ? 62  GLY B C   1 
ATOM   1192  O O   . GLY B 2 54  ? -14.075  -74.879  -11.185 1.00 126.56 ? 62  GLY B O   1 
ATOM   1193  N N   . LYS B 2 55  ? -16.285  -75.127  -10.710 1.00 124.57 ? 63  LYS B N   1 
ATOM   1194  C CA  . LYS B 2 55  ? -16.133  -76.242  -9.756  1.00 127.31 ? 63  LYS B CA  1 
ATOM   1195  C C   . LYS B 2 55  ? -15.072  -75.919  -8.686  1.00 131.56 ? 63  LYS B C   1 
ATOM   1196  O O   . LYS B 2 55  ? -14.279  -76.782  -8.302  1.00 132.94 ? 63  LYS B O   1 
ATOM   1197  C CB  . LYS B 2 55  ? -15.849  -77.589  -10.477 1.00 133.55 ? 63  LYS B CB  1 
ATOM   1198  C CG  . LYS B 2 55  ? -17.106  -78.319  -10.964 1.00 150.23 ? 63  LYS B CG  1 
ATOM   1199  C CD  . LYS B 2 55  ? -16.789  -79.536  -11.846 1.00 157.91 ? 63  LYS B CD  1 
ATOM   1200  C CE  . LYS B 2 55  ? -18.020  -80.044  -12.562 1.00 158.71 ? 63  LYS B CE  1 
ATOM   1201  N NZ  . LYS B 2 55  ? -17.703  -81.154  -13.497 1.00 162.97 ? 63  LYS B NZ  1 
ATOM   1202  N N   . CYS B 2 56  ? -15.052  -74.642  -8.250  1.00 126.45 ? 64  CYS B N   1 
ATOM   1203  C CA  . CYS B 2 56  ? -14.141  -74.064  -7.260  1.00 124.99 ? 64  CYS B CA  1 
ATOM   1204  C C   . CYS B 2 56  ? -14.671  -72.691  -6.813  1.00 123.79 ? 64  CYS B C   1 
ATOM   1205  O O   . CYS B 2 56  ? -15.292  -71.983  -7.609  1.00 123.06 ? 64  CYS B O   1 
ATOM   1206  C CB  . CYS B 2 56  ? -12.731  -73.945  -7.840  1.00 125.67 ? 64  CYS B CB  1 
ATOM   1207  S SG  . CYS B 2 56  ? -11.413  -73.872  -6.595  1.00 129.51 ? 64  CYS B SG  1 
ATOM   1208  N N   . ASN B 2 57  ? -14.413  -72.307  -5.556  1.00 115.75 ? 65  ASN B N   1 
ATOM   1209  C CA  . ASN B 2 57  ? -14.793  -70.987  -5.044  1.00 111.70 ? 65  ASN B CA  1 
ATOM   1210  C C   . ASN B 2 57  ? -13.503  -70.196  -4.776  1.00 110.72 ? 65  ASN B C   1 
ATOM   1211  O O   . ASN B 2 57  ? -12.419  -70.779  -4.873  1.00 111.67 ? 65  ASN B O   1 
ATOM   1212  C CB  . ASN B 2 57  ? -15.654  -71.116  -3.785  1.00 111.29 ? 65  ASN B CB  1 
ATOM   1213  C CG  . ASN B 2 57  ? -15.107  -72.073  -2.757  1.00 133.11 ? 65  ASN B CG  1 
ATOM   1214  O OD1 . ASN B 2 57  ? -13.971  -71.950  -2.297  1.00 127.07 ? 65  ASN B OD1 1 
ATOM   1215  N ND2 . ASN B 2 57  ? -15.908  -73.052  -2.374  1.00 125.55 ? 65  ASN B ND2 1 
ATOM   1216  N N   . ILE B 2 58  ? -13.601  -68.891  -4.445  1.00 101.95 ? 66  ILE B N   1 
ATOM   1217  C CA  . ILE B 2 58  ? -12.423  -68.063  -4.149  1.00 99.39  ? 66  ILE B CA  1 
ATOM   1218  C C   . ILE B 2 58  ? -11.544  -68.719  -3.073  1.00 102.86 ? 66  ILE B C   1 
ATOM   1219  O O   . ILE B 2 58  ? -10.340  -68.836  -3.286  1.00 102.87 ? 66  ILE B O   1 
ATOM   1220  C CB  . ILE B 2 58  ? -12.804  -66.599  -3.804  1.00 100.90 ? 66  ILE B CB  1 
ATOM   1221  C CG1 . ILE B 2 58  ? -13.470  -65.913  -5.010  1.00 101.14 ? 66  ILE B CG1 1 
ATOM   1222  C CG2 . ILE B 2 58  ? -11.587  -65.797  -3.326  1.00 100.43 ? 66  ILE B CG2 1 
ATOM   1223  C CD1 . ILE B 2 58  ? -14.258  -64.638  -4.696  1.00 108.57 ? 66  ILE B CD1 1 
ATOM   1224  N N   . ALA B 2 59  ? -12.156  -69.200  -1.963  1.00 99.43  ? 67  ALA B N   1 
ATOM   1225  C CA  . ALA B 2 59  ? -11.474  -69.857  -0.834  1.00 100.07 ? 67  ALA B CA  1 
ATOM   1226  C C   . ALA B 2 59  ? -10.570  -71.013  -1.234  1.00 104.00 ? 67  ALA B C   1 
ATOM   1227  O O   . ALA B 2 59  ? -9.455   -71.095  -0.730  1.00 105.08 ? 67  ALA B O   1 
ATOM   1228  C CB  . ALA B 2 59  ? -12.476  -70.317  0.219   1.00 101.71 ? 67  ALA B CB  1 
ATOM   1229  N N   . GLY B 2 60  ? -11.051  -71.880  -2.125  1.00 107.98 ? 68  GLY B N   1 
ATOM   1230  C CA  . GLY B 2 60  ? -10.296  -73.029  -2.610  1.00 106.75 ? 68  GLY B CA  1 
ATOM   1231  C C   . GLY B 2 60  ? -9.115   -72.612  -3.452  1.00 107.39 ? 68  GLY B C   1 
ATOM   1232  O O   . GLY B 2 60  ? -8.019   -73.157  -3.312  1.00 105.98 ? 68  GLY B O   1 
ATOM   1233  N N   . TRP B 2 61  ? -9.342   -71.608  -4.299  1.00 103.40 ? 69  TRP B N   1 
ATOM   1234  C CA  . TRP B 2 61  ? -8.364   -71.025  -5.203  1.00 103.55 ? 69  TRP B CA  1 
ATOM   1235  C C   . TRP B 2 61  ? -7.276   -70.263  -4.456  1.00 103.74 ? 69  TRP B C   1 
ATOM   1236  O O   . TRP B 2 61  ? -6.109   -70.354  -4.821  1.00 103.27 ? 69  TRP B O   1 
ATOM   1237  C CB  . TRP B 2 61  ? -9.097   -70.107  -6.190  1.00 103.80 ? 69  TRP B CB  1 
ATOM   1238  C CG  . TRP B 2 61  ? -8.241   -69.080  -6.867  1.00 105.93 ? 69  TRP B CG  1 
ATOM   1239  C CD1 . TRP B 2 61  ? -7.378   -69.287  -7.901  1.00 109.78 ? 69  TRP B CD1 1 
ATOM   1240  C CD2 . TRP B 2 61  ? -8.215   -67.675  -6.595  1.00 106.10 ? 69  TRP B CD2 1 
ATOM   1241  N NE1 . TRP B 2 61  ? -6.796   -68.099  -8.275  1.00 110.06 ? 69  TRP B NE1 1 
ATOM   1242  C CE2 . TRP B 2 61  ? -7.300   -67.090  -7.496  1.00 110.94 ? 69  TRP B CE2 1 
ATOM   1243  C CE3 . TRP B 2 61  ? -8.856   -66.853  -5.656  1.00 107.44 ? 69  TRP B CE3 1 
ATOM   1244  C CZ2 . TRP B 2 61  ? -7.012   -65.722  -7.491  1.00 110.87 ? 69  TRP B CZ2 1 
ATOM   1245  C CZ3 . TRP B 2 61  ? -8.575   -65.497  -5.658  1.00 109.67 ? 69  TRP B CZ3 1 
ATOM   1246  C CH2 . TRP B 2 61  ? -7.658   -64.946  -6.565  1.00 111.10 ? 69  TRP B CH2 1 
ATOM   1247  N N   . ILE B 2 62  ? -7.654   -69.513  -3.426  1.00 98.48  ? 70  ILE B N   1 
ATOM   1248  C CA  . ILE B 2 62  ? -6.717   -68.705  -2.665  1.00 97.99  ? 70  ILE B CA  1 
ATOM   1249  C C   . ILE B 2 62  ? -5.916   -69.547  -1.646  1.00 100.39 ? 70  ILE B C   1 
ATOM   1250  O O   . ILE B 2 62  ? -4.761   -69.210  -1.396  1.00 100.39 ? 70  ILE B O   1 
ATOM   1251  C CB  . ILE B 2 62  ? -7.421   -67.460  -2.048  1.00 101.92 ? 70  ILE B CB  1 
ATOM   1252  C CG1 . ILE B 2 62  ? -6.435   -66.299  -1.811  1.00 103.15 ? 70  ILE B CG1 1 
ATOM   1253  C CG2 . ILE B 2 62  ? -8.241   -67.776  -0.797  1.00 102.85 ? 70  ILE B CG2 1 
ATOM   1254  C CD1 . ILE B 2 62  ? -6.017   -65.532  -3.081  1.00 111.30 ? 70  ILE B CD1 1 
ATOM   1255  N N   . LEU B 2 63  ? -6.500   -70.631  -1.082  1.00 95.35  ? 71  LEU B N   1 
ATOM   1256  C CA  . LEU B 2 63  ? -5.812   -71.522  -0.131  1.00 93.79  ? 71  LEU B CA  1 
ATOM   1257  C C   . LEU B 2 63  ? -4.890   -72.503  -0.859  1.00 97.23  ? 71  LEU B C   1 
ATOM   1258  O O   . LEU B 2 63  ? -3.870   -72.915  -0.306  1.00 97.26  ? 71  LEU B O   1 
ATOM   1259  C CB  . LEU B 2 63  ? -6.806   -72.319  0.726   1.00 93.94  ? 71  LEU B CB  1 
ATOM   1260  C CG  . LEU B 2 63  ? -7.539   -71.585  1.828   1.00 98.85  ? 71  LEU B CG  1 
ATOM   1261  C CD1 . LEU B 2 63  ? -8.724   -72.390  2.300   1.00 100.04 ? 71  LEU B CD1 1 
ATOM   1262  C CD2 . LEU B 2 63  ? -6.627   -71.290  2.996   1.00 101.75 ? 71  LEU B CD2 1 
ATOM   1263  N N   . GLY B 2 64  ? -5.274   -72.880  -2.076  1.00 92.35  ? 72  GLY B N   1 
ATOM   1264  C CA  . GLY B 2 64  ? -4.528   -73.824  -2.890  1.00 91.58  ? 72  GLY B CA  1 
ATOM   1265  C C   . GLY B 2 64  ? -5.063   -75.233  -2.790  1.00 95.61  ? 72  GLY B C   1 
ATOM   1266  O O   . GLY B 2 64  ? -4.275   -76.179  -2.781  1.00 95.01  ? 72  GLY B O   1 
ATOM   1267  N N   . ASN B 2 65  ? -6.406   -75.381  -2.713  1.00 93.63  ? 73  ASN B N   1 
ATOM   1268  C CA  . ASN B 2 65  ? -7.103   -76.671  -2.659  1.00 95.34  ? 73  ASN B CA  1 
ATOM   1269  C C   . ASN B 2 65  ? -6.675   -77.509  -3.883  1.00 100.87 ? 73  ASN B C   1 
ATOM   1270  O O   . ASN B 2 65  ? -6.745   -77.010  -5.006  1.00 100.74 ? 73  ASN B O   1 
ATOM   1271  C CB  . ASN B 2 65  ? -8.629   -76.460  -2.619  1.00 99.75  ? 73  ASN B CB  1 
ATOM   1272  C CG  . ASN B 2 65  ? -9.486   -77.718  -2.591  1.00 135.98 ? 73  ASN B CG  1 
ATOM   1273  O OD1 . ASN B 2 65  ? -9.126   -78.755  -2.021  1.00 132.63 ? 73  ASN B OD1 1 
ATOM   1274  N ND2 . ASN B 2 65  ? -10.678  -77.633  -3.173  1.00 133.34 ? 73  ASN B ND2 1 
ATOM   1275  N N   . PRO B 2 66  ? -6.143   -78.735  -3.684  1.00 98.97  ? 74  PRO B N   1 
ATOM   1276  C CA  . PRO B 2 66  ? -5.633   -79.521  -4.818  1.00 100.81 ? 74  PRO B CA  1 
ATOM   1277  C C   . PRO B 2 66  ? -6.627   -79.824  -5.945  1.00 109.99 ? 74  PRO B C   1 
ATOM   1278  O O   . PRO B 2 66  ? -6.196   -80.076  -7.078  1.00 110.57 ? 74  PRO B O   1 
ATOM   1279  C CB  . PRO B 2 66  ? -5.130   -80.797  -4.146  1.00 102.72 ? 74  PRO B CB  1 
ATOM   1280  C CG  . PRO B 2 66  ? -5.867   -80.874  -2.859  1.00 106.35 ? 74  PRO B CG  1 
ATOM   1281  C CD  . PRO B 2 66  ? -5.933   -79.458  -2.420  1.00 100.20 ? 74  PRO B CD  1 
ATOM   1282  N N   . GLU B 2 67  ? -7.947   -79.762  -5.648  1.00 109.10 ? 75  GLU B N   1 
ATOM   1283  C CA  . GLU B 2 67  ? -9.038   -79.985  -6.611  1.00 110.85 ? 75  GLU B CA  1 
ATOM   1284  C C   . GLU B 2 67  ? -9.078   -78.851  -7.670  1.00 113.40 ? 75  GLU B C   1 
ATOM   1285  O O   . GLU B 2 67  ? -9.744   -79.003  -8.696  1.00 114.11 ? 75  GLU B O   1 
ATOM   1286  C CB  . GLU B 2 67  ? -10.399  -80.095  -5.881  1.00 113.35 ? 75  GLU B CB  1 
ATOM   1287  C CG  . GLU B 2 67  ? -10.434  -81.063  -4.702  1.00 128.41 ? 75  GLU B CG  1 
ATOM   1288  C CD  . GLU B 2 67  ? -11.660  -80.946  -3.811  1.00 156.53 ? 75  GLU B CD  1 
ATOM   1289  O OE1 . GLU B 2 67  ? -11.539  -80.382  -2.699  1.00 136.72 ? 75  GLU B OE1 1 
ATOM   1290  O OE2 . GLU B 2 67  ? -12.742  -81.428  -4.221  1.00 161.96 ? 75  GLU B OE2 1 
ATOM   1291  N N   . CYS B 2 68  ? -8.361   -77.721  -7.405  1.00 107.90 ? 76  CYS B N   1 
ATOM   1292  C CA  . CYS B 2 68  ? -8.240   -76.526  -8.253  1.00 133.93 ? 76  CYS B CA  1 
ATOM   1293  C C   . CYS B 2 68  ? -6.761   -76.264  -8.557  1.00 146.90 ? 76  CYS B C   1 
ATOM   1294  O O   . CYS B 2 68  ? -6.354   -76.206  -9.716  1.00 111.09 ? 76  CYS B O   1 
ATOM   1295  C CB  . CYS B 2 68  ? -8.885   -75.316  -7.580  1.00 133.32 ? 76  CYS B CB  1 
ATOM   1296  S SG  . CYS B 2 68  ? -10.463  -75.667  -6.754  1.00 138.00 ? 76  CYS B SG  1 
ATOM   1297  N N   . ALA B 2 74  ? -3.468   -68.212  -13.083 1.00 129.44 ? 82  ALA B N   1 
ATOM   1298  C CA  . ALA B 2 74  ? -3.489   -66.984  -13.877 1.00 130.92 ? 82  ALA B CA  1 
ATOM   1299  C C   . ALA B 2 74  ? -3.217   -65.745  -13.015 1.00 135.38 ? 82  ALA B C   1 
ATOM   1300  O O   . ALA B 2 74  ? -3.814   -65.590  -11.946 1.00 132.92 ? 82  ALA B O   1 
ATOM   1301  C CB  . ALA B 2 74  ? -4.814   -66.849  -14.622 1.00 131.28 ? 82  ALA B CB  1 
ATOM   1302  N N   . SER B 2 75  ? -2.295   -64.875  -13.490 1.00 135.01 ? 83  SER B N   1 
ATOM   1303  C CA  . SER B 2 75  ? -1.837   -63.649  -12.818 1.00 135.86 ? 83  SER B CA  1 
ATOM   1304  C C   . SER B 2 75  ? -2.704   -62.411  -13.086 1.00 141.04 ? 83  SER B C   1 
ATOM   1305  O O   . SER B 2 75  ? -3.021   -61.681  -12.144 1.00 139.70 ? 83  SER B O   1 
ATOM   1306  C CB  . SER B 2 75  ? -0.376   -63.361  -13.174 1.00 141.53 ? 83  SER B CB  1 
ATOM   1307  O OG  . SER B 2 75  ? 0.108    -62.138  -12.638 1.00 150.35 ? 83  SER B OG  1 
ATOM   1308  N N   . SER B 2 76  A -3.042   -62.150  -14.363 1.00 139.80 ? 83  SER B N   1 
ATOM   1309  C CA  . SER B 2 76  A -3.808   -60.968  -14.761 1.00 140.51 ? 83  SER B CA  1 
ATOM   1310  C C   . SER B 2 76  A -5.272   -61.258  -15.072 1.00 142.00 ? 83  SER B C   1 
ATOM   1311  O O   . SER B 2 76  A -5.583   -62.213  -15.794 1.00 140.83 ? 83  SER B O   1 
ATOM   1312  C CB  . SER B 2 76  A -3.140   -60.263  -15.939 1.00 147.66 ? 83  SER B CB  1 
ATOM   1313  O OG  . SER B 2 76  A -1.793   -59.917  -15.658 1.00 158.86 ? 83  SER B OG  1 
ATOM   1314  N N   . TRP B 2 77  ? -6.167   -60.415  -14.517 1.00 137.31 ? 84  TRP B N   1 
ATOM   1315  C CA  . TRP B 2 77  ? -7.613   -60.491  -14.721 1.00 134.84 ? 84  TRP B CA  1 
ATOM   1316  C C   . TRP B 2 77  ? -8.306   -59.151  -14.536 1.00 134.74 ? 84  TRP B C   1 
ATOM   1317  O O   . TRP B 2 77  ? -7.777   -58.254  -13.872 1.00 134.95 ? 84  TRP B O   1 
ATOM   1318  C CB  . TRP B 2 77  ? -8.272   -61.588  -13.869 1.00 131.92 ? 84  TRP B CB  1 
ATOM   1319  C CG  . TRP B 2 77  ? -8.217   -61.358  -12.388 1.00 132.65 ? 84  TRP B CG  1 
ATOM   1320  C CD1 . TRP B 2 77  ? -9.110   -60.658  -11.634 1.00 135.04 ? 84  TRP B CD1 1 
ATOM   1321  C CD2 . TRP B 2 77  ? -7.265   -61.909  -11.474 1.00 132.66 ? 84  TRP B CD2 1 
ATOM   1322  N NE1 . TRP B 2 77  ? -8.741   -60.690  -10.311 1.00 134.34 ? 84  TRP B NE1 1 
ATOM   1323  C CE2 . TRP B 2 77  ? -7.625   -61.472  -10.180 1.00 136.03 ? 84  TRP B CE2 1 
ATOM   1324  C CE3 . TRP B 2 77  ? -6.124   -62.713  -11.622 1.00 134.63 ? 84  TRP B CE3 1 
ATOM   1325  C CZ2 . TRP B 2 77  ? -6.896   -61.825  -9.041  1.00 135.18 ? 84  TRP B CZ2 1 
ATOM   1326  C CZ3 . TRP B 2 77  ? -5.404   -63.064  -10.493 1.00 135.80 ? 84  TRP B CZ3 1 
ATOM   1327  C CH2 . TRP B 2 77  ? -5.787   -62.616  -9.221  1.00 135.64 ? 84  TRP B CH2 1 
ATOM   1328  N N   . SER B 2 78  ? -9.506   -59.040  -15.123 1.00 127.76 ? 85  SER B N   1 
ATOM   1329  C CA  . SER B 2 78  ? -10.368  -57.860  -15.097 1.00 126.49 ? 85  SER B CA  1 
ATOM   1330  C C   . SER B 2 78  ? -11.405  -57.917  -13.974 1.00 125.29 ? 85  SER B C   1 
ATOM   1331  O O   . SER B 2 78  ? -11.787  -56.866  -13.449 1.00 124.96 ? 85  SER B O   1 
ATOM   1332  C CB  . SER B 2 78  ? -11.069  -57.703  -16.440 1.00 130.36 ? 85  SER B CB  1 
ATOM   1333  O OG  . SER B 2 78  ? -11.630  -58.927  -16.887 1.00 138.51 ? 85  SER B OG  1 
ATOM   1334  N N   . TYR B 2 79  ? -11.875  -59.147  -13.633 1.00 117.91 ? 86  TYR B N   1 
ATOM   1335  C CA  . TYR B 2 79  ? -12.862  -59.466  -12.585 1.00 114.83 ? 86  TYR B CA  1 
ATOM   1336  C C   . TYR B 2 79  ? -12.912  -60.969  -12.276 1.00 114.96 ? 86  TYR B C   1 
ATOM   1337  O O   . TYR B 2 79  ? -12.567  -61.778  -13.136 1.00 115.16 ? 86  TYR B O   1 
ATOM   1338  C CB  . TYR B 2 79  ? -14.265  -58.928  -12.933 1.00 114.68 ? 86  TYR B CB  1 
ATOM   1339  C CG  . TYR B 2 79  ? -14.896  -59.464  -14.204 1.00 114.95 ? 86  TYR B CG  1 
ATOM   1340  C CD1 . TYR B 2 79  ? -14.622  -58.885  -15.440 1.00 117.56 ? 86  TYR B CD1 1 
ATOM   1341  C CD2 . TYR B 2 79  ? -15.864  -60.463  -14.156 1.00 113.94 ? 86  TYR B CD2 1 
ATOM   1342  C CE1 . TYR B 2 79  ? -15.244  -59.334  -16.606 1.00 116.55 ? 86  TYR B CE1 1 
ATOM   1343  C CE2 . TYR B 2 79  ? -16.498  -60.915  -15.314 1.00 113.85 ? 86  TYR B CE2 1 
ATOM   1344  C CZ  . TYR B 2 79  ? -16.185  -60.347  -16.537 1.00 119.42 ? 86  TYR B CZ  1 
ATOM   1345  O OH  . TYR B 2 79  ? -16.817  -60.787  -17.675 1.00 117.18 ? 86  TYR B OH  1 
ATOM   1346  N N   . ILE B 2 80  ? -13.331  -61.347  -11.059 1.00 126.94 ? 87  ILE B N   1 
ATOM   1347  C CA  . ILE B 2 80  ? -13.391  -62.762  -10.687 1.00 123.52 ? 87  ILE B CA  1 
ATOM   1348  C C   . ILE B 2 80  ? -14.790  -63.302  -10.839 1.00 131.23 ? 87  ILE B C   1 
ATOM   1349  O O   . ILE B 2 80  ? -15.736  -62.720  -10.316 1.00 132.40 ? 87  ILE B O   1 
ATOM   1350  C CB  . ILE B 2 80  ? -12.799  -63.066  -9.283  1.00 121.00 ? 87  ILE B CB  1 
ATOM   1351  C CG1 . ILE B 2 80  ? -11.387  -62.473  -9.115  1.00 118.97 ? 87  ILE B CG1 1 
ATOM   1352  C CG2 . ILE B 2 80  ? -12.798  -64.574  -8.987  1.00 118.43 ? 87  ILE B CG2 1 
ATOM   1353  C CD1 . ILE B 2 80  ? -11.333  -61.169  -8.323  1.00 126.34 ? 87  ILE B CD1 1 
ATOM   1354  N N   . VAL B 2 81  ? -14.913  -64.425  -11.551 1.00 130.39 ? 88  VAL B N   1 
ATOM   1355  C CA  . VAL B 2 81  ? -16.178  -65.124  -11.756 1.00 134.72 ? 88  VAL B CA  1 
ATOM   1356  C C   . VAL B 2 81  ? -16.157  -66.385  -10.894 1.00 137.02 ? 88  VAL B C   1 
ATOM   1357  O O   . VAL B 2 81  ? -15.101  -66.998  -10.705 1.00 133.28 ? 88  VAL B O   1 
ATOM   1358  C CB  . VAL B 2 81  ? -16.498  -65.449  -13.244 1.00 143.97 ? 88  VAL B CB  1 
ATOM   1359  C CG1 . VAL B 2 81  ? -17.997  -65.658  -13.451 1.00 149.42 ? 88  VAL B CG1 1 
ATOM   1360  C CG2 . VAL B 2 81  ? -15.986  -64.359  -14.179 1.00 145.93 ? 88  VAL B CG2 1 
ATOM   1361  N N   . GLU B 2 82  ? -17.322  -66.735  -10.342 1.00 136.38 ? 89  GLU B N   1 
ATOM   1362  C CA  . GLU B 2 82  ? -17.536  -67.919  -9.521  1.00 135.10 ? 89  GLU B CA  1 
ATOM   1363  C C   . GLU B 2 82  ? -18.912  -68.498  -9.857  1.00 145.54 ? 89  GLU B C   1 
ATOM   1364  O O   . GLU B 2 82  ? -19.899  -67.762  -9.971  1.00 149.06 ? 89  GLU B O   1 
ATOM   1365  C CB  . GLU B 2 82  ? -17.419  -67.592  -8.016  1.00 132.49 ? 89  GLU B CB  1 
ATOM   1366  C CG  . GLU B 2 82  ? -17.413  -68.820  -7.117  1.00 142.60 ? 89  GLU B CG  1 
ATOM   1367  C CD  . GLU B 2 82  ? -18.022  -68.614  -5.745  1.00 161.33 ? 89  GLU B CD  1 
ATOM   1368  O OE1 . GLU B 2 82  ? -19.227  -68.912  -5.564  1.00 147.88 ? 89  GLU B OE1 1 
ATOM   1369  O OE2 . GLU B 2 82  ? -17.280  -68.172  -4.839  1.00 157.76 ? 89  GLU B OE2 1 
ATOM   1370  N N   . THR B 2 83  ? -18.962  -69.817  -10.043 1.00 143.68 ? 90  THR B N   1 
ATOM   1371  C CA  . THR B 2 83  ? -20.209  -70.521  -10.303 1.00 150.01 ? 90  THR B CA  1 
ATOM   1372  C C   . THR B 2 83  ? -20.940  -70.593  -8.948  1.00 154.61 ? 90  THR B C   1 
ATOM   1373  O O   . THR B 2 83  ? -20.289  -70.890  -7.940  1.00 149.62 ? 90  THR B O   1 
ATOM   1374  C CB  . THR B 2 83  ? -19.908  -71.925  -10.864 1.00 157.62 ? 90  THR B CB  1 
ATOM   1375  O OG1 . THR B 2 83  ? -18.987  -71.814  -11.947 1.00 156.32 ? 90  THR B OG1 1 
ATOM   1376  C CG2 . THR B 2 83  ? -21.160  -72.664  -11.329 1.00 163.79 ? 90  THR B CG2 1 
ATOM   1377  N N   . PRO B 2 84  A -22.263  -70.304  -8.872  1.00 156.99 ? 90  PRO B N   1 
ATOM   1378  C CA  . PRO B 2 84  A -22.955  -70.418  -7.572  1.00 157.19 ? 90  PRO B CA  1 
ATOM   1379  C C   . PRO B 2 84  A -22.955  -71.859  -7.044  1.00 161.55 ? 90  PRO B C   1 
ATOM   1380  O O   . PRO B 2 84  A -22.825  -72.088  -5.838  1.00 157.67 ? 90  PRO B O   1 
ATOM   1381  C CB  . PRO B 2 84  A -24.370  -69.919  -7.878  1.00 166.36 ? 90  PRO B CB  1 
ATOM   1382  C CG  . PRO B 2 84  A -24.542  -70.102  -9.343  1.00 175.25 ? 90  PRO B CG  1 
ATOM   1383  C CD  . PRO B 2 84  A -23.192  -69.911  -9.952  1.00 165.52 ? 90  PRO B CD  1 
ATOM   1384  N N   . SER B 2 85  ? -23.029  -72.824  -7.984  1.00 162.59 ? 91  SER B N   1 
ATOM   1385  C CA  . SER B 2 85  ? -23.026  -74.272  -7.782  1.00 164.17 ? 91  SER B CA  1 
ATOM   1386  C C   . SER B 2 85  ? -21.682  -74.802  -7.236  1.00 161.78 ? 91  SER B C   1 
ATOM   1387  O O   . SER B 2 85  ? -21.651  -75.891  -6.656  1.00 161.07 ? 91  SER B O   1 
ATOM   1388  C CB  . SER B 2 85  ? -23.373  -74.973  -9.093  1.00 173.67 ? 91  SER B CB  1 
ATOM   1389  O OG  . SER B 2 85  ? -24.507  -74.395  -9.722  1.00 186.18 ? 91  SER B OG  1 
ATOM   1390  N N   . SER B 2 86  ? -20.580  -74.038  -7.427  1.00 153.81 ? 92  SER B N   1 
ATOM   1391  C CA  . SER B 2 86  ? -19.231  -74.394  -6.975  1.00 147.57 ? 92  SER B CA  1 
ATOM   1392  C C   . SER B 2 86  ? -19.102  -74.316  -5.457  1.00 149.36 ? 92  SER B C   1 
ATOM   1393  O O   . SER B 2 86  ? -19.278  -73.243  -4.865  1.00 147.14 ? 92  SER B O   1 
ATOM   1394  C CB  . SER B 2 86  ? -18.179  -73.524  -7.656  1.00 146.79 ? 92  SER B CB  1 
ATOM   1395  O OG  . SER B 2 86  ? -18.074  -72.234  -7.073  1.00 152.86 ? 92  SER B OG  1 
ATOM   1396  N N   . ASP B 2 87  ? -18.815  -75.473  -4.837  1.00 147.25 ? 93  ASP B N   1 
ATOM   1397  C CA  . ASP B 2 87  ? -18.669  -75.623  -3.386  1.00 145.23 ? 93  ASP B CA  1 
ATOM   1398  C C   . ASP B 2 87  ? -17.249  -76.064  -2.991  1.00 144.31 ? 93  ASP B C   1 
ATOM   1399  O O   . ASP B 2 87  ? -16.955  -76.166  -1.790  1.00 140.84 ? 93  ASP B O   1 
ATOM   1400  C CB  . ASP B 2 87  ? -19.719  -76.618  -2.841  1.00 152.55 ? 93  ASP B CB  1 
ATOM   1401  C CG  . ASP B 2 87  ? -21.166  -76.168  -2.975  1.00 167.55 ? 93  ASP B CG  1 
ATOM   1402  O OD1 . ASP B 2 87  ? -21.579  -75.257  -2.221  1.00 167.21 ? 93  ASP B OD1 1 
ATOM   1403  O OD2 . ASP B 2 87  ? -21.902  -76.771  -3.786  1.00 178.32 ? 93  ASP B OD2 1 
ATOM   1404  N N   . ASN B 2 88  ? -16.374  -76.312  -4.005  1.00 140.22 ? 94  ASN B N   1 
ATOM   1405  C CA  . ASN B 2 88  ? -14.986  -76.771  -3.834  1.00 135.78 ? 94  ASN B CA  1 
ATOM   1406  C C   . ASN B 2 88  ? -14.049  -75.675  -3.272  1.00 133.60 ? 94  ASN B C   1 
ATOM   1407  O O   . ASN B 2 88  ? -13.530  -74.834  -4.019  1.00 131.32 ? 94  ASN B O   1 
ATOM   1408  C CB  . ASN B 2 88  ? -14.444  -77.392  -5.130  1.00 137.07 ? 94  ASN B CB  1 
ATOM   1409  C CG  . ASN B 2 88  ? -15.268  -78.554  -5.638  1.00 165.00 ? 94  ASN B CG  1 
ATOM   1410  O OD1 . ASN B 2 88  ? -16.468  -78.430  -5.923  1.00 160.27 ? 94  ASN B OD1 1 
ATOM   1411  N ND2 . ASN B 2 88  ? -14.639  -79.711  -5.768  1.00 158.53 ? 94  ASN B ND2 1 
ATOM   1412  N N   . GLY B 2 89  ? -13.869  -75.712  -1.946  1.00 126.78 ? 95  GLY B N   1 
ATOM   1413  C CA  . GLY B 2 89  ? -13.052  -74.772  -1.192  1.00 121.25 ? 95  GLY B CA  1 
ATOM   1414  C C   . GLY B 2 89  ? -12.199  -75.408  -0.118  1.00 120.59 ? 95  GLY B C   1 
ATOM   1415  O O   . GLY B 2 89  ? -11.056  -75.792  -0.382  1.00 117.93 ? 95  GLY B O   1 
ATOM   1416  N N   . THR B 2 90  ? -12.744  -75.502  1.110   1.00 116.85 ? 96  THR B N   1 
ATOM   1417  C CA  . THR B 2 90  ? -12.034  -76.074  2.259   1.00 114.47 ? 96  THR B CA  1 
ATOM   1418  C C   . THR B 2 90  ? -12.199  -77.595  2.297   1.00 120.22 ? 96  THR B C   1 
ATOM   1419  O O   . THR B 2 90  ? -13.222  -78.104  2.762   1.00 123.54 ? 96  THR B O   1 
ATOM   1420  C CB  . THR B 2 90  ? -12.391  -75.372  3.596   1.00 118.14 ? 96  THR B CB  1 
ATOM   1421  O OG1 . THR B 2 90  ? -13.671  -75.795  4.082   1.00 117.78 ? 96  THR B OG1 1 
ATOM   1422  C CG2 . THR B 2 90  ? -12.315  -73.846  3.503   1.00 114.98 ? 96  THR B CG2 1 
ATOM   1423  N N   . CYS B 2 91  ? -11.192  -78.311  1.765   1.00 114.35 ? 97  CYS B N   1 
ATOM   1424  C CA  . CYS B 2 91  ? -11.146  -79.776  1.724   1.00 115.72 ? 97  CYS B CA  1 
ATOM   1425  C C   . CYS B 2 91  ? -11.065  -80.289  3.157   1.00 118.79 ? 97  CYS B C   1 
ATOM   1426  O O   . CYS B 2 91  ? -11.742  -81.253  3.502   1.00 122.49 ? 97  CYS B O   1 
ATOM   1427  C CB  . CYS B 2 91  ? -9.957   -80.249  0.898   1.00 114.14 ? 97  CYS B CB  1 
ATOM   1428  S SG  . CYS B 2 91  ? -8.380   -79.556  1.448   1.00 112.81 ? 97  CYS B SG  1 
ATOM   1429  N N   . TYR B 2 92  ? -10.249  -79.633  3.994   1.00 110.64 ? 98  TYR B N   1 
ATOM   1430  C CA  . TYR B 2 92  ? -10.157  -79.963  5.406   1.00 110.75 ? 98  TYR B CA  1 
ATOM   1431  C C   . TYR B 2 92  ? -11.258  -79.128  6.075   1.00 112.62 ? 98  TYR B C   1 
ATOM   1432  O O   . TYR B 2 92  ? -11.357  -77.932  5.775   1.00 110.47 ? 98  TYR B O   1 
ATOM   1433  C CB  . TYR B 2 92  ? -8.766   -79.629  5.980   1.00 109.69 ? 98  TYR B CB  1 
ATOM   1434  C CG  . TYR B 2 92  ? -8.541   -80.229  7.348   1.00 114.33 ? 98  TYR B CG  1 
ATOM   1435  C CD1 . TYR B 2 92  ? -9.066   -79.630  8.487   1.00 117.93 ? 98  TYR B CD1 1 
ATOM   1436  C CD2 . TYR B 2 92  ? -7.843   -81.422  7.502   1.00 116.58 ? 98  TYR B CD2 1 
ATOM   1437  C CE1 . TYR B 2 92  ? -8.910   -80.204  9.745   1.00 122.74 ? 98  TYR B CE1 1 
ATOM   1438  C CE2 . TYR B 2 92  ? -7.668   -82.002  8.759   1.00 119.94 ? 98  TYR B CE2 1 
ATOM   1439  C CZ  . TYR B 2 92  ? -8.206   -81.388  9.878   1.00 131.65 ? 98  TYR B CZ  1 
ATOM   1440  O OH  . TYR B 2 92  ? -8.050   -81.934  11.127  1.00 137.58 ? 98  TYR B OH  1 
ATOM   1441  N N   . PRO B 2 93  ? -12.136  -79.731  6.914   1.00 110.04 ? 99  PRO B N   1 
ATOM   1442  C CA  . PRO B 2 93  ? -13.227  -78.948  7.522   1.00 110.94 ? 99  PRO B CA  1 
ATOM   1443  C C   . PRO B 2 93  ? -12.746  -77.844  8.453   1.00 111.97 ? 99  PRO B C   1 
ATOM   1444  O O   . PRO B 2 93  ? -11.727  -78.000  9.122   1.00 109.65 ? 99  PRO B O   1 
ATOM   1445  C CB  . PRO B 2 93  ? -14.029  -80.004  8.283   1.00 117.53 ? 99  PRO B CB  1 
ATOM   1446  C CG  . PRO B 2 93  ? -13.041  -81.072  8.583   1.00 121.73 ? 99  PRO B CG  1 
ATOM   1447  C CD  . PRO B 2 93  ? -12.188  -81.138  7.355   1.00 114.30 ? 99  PRO B CD  1 
ATOM   1448  N N   . GLY B 2 94  ? -13.477  -76.737  8.480   1.00 109.39 ? 100 GLY B N   1 
ATOM   1449  C CA  . GLY B 2 94  ? -13.140  -75.619  9.350   1.00 108.57 ? 100 GLY B CA  1 
ATOM   1450  C C   . GLY B 2 94  ? -13.915  -74.347  9.109   1.00 115.03 ? 100 GLY B C   1 
ATOM   1451  O O   . GLY B 2 94  ? -15.003  -74.372  8.527   1.00 116.72 ? 100 GLY B O   1 
ATOM   1452  N N   . ASP B 2 95  ? -13.361  -73.226  9.578   1.00 112.42 ? 101 ASP B N   1 
ATOM   1453  C CA  . ASP B 2 95  ? -13.991  -71.925  9.408   1.00 114.40 ? 101 ASP B CA  1 
ATOM   1454  C C   . ASP B 2 95  ? -13.017  -70.915  8.821   1.00 114.07 ? 101 ASP B C   1 
ATOM   1455  O O   . ASP B 2 95  ? -11.942  -70.689  9.383   1.00 112.48 ? 101 ASP B O   1 
ATOM   1456  C CB  . ASP B 2 95  ? -14.585  -71.422  10.733  1.00 121.12 ? 101 ASP B CB  1 
ATOM   1457  C CG  . ASP B 2 95  ? -15.664  -72.313  11.333  1.00 149.58 ? 101 ASP B CG  1 
ATOM   1458  O OD1 . ASP B 2 95  ? -16.627  -72.664  10.601  1.00 155.24 ? 101 ASP B OD1 1 
ATOM   1459  O OD2 . ASP B 2 95  ? -15.578  -72.612  12.551  1.00 160.22 ? 101 ASP B OD2 1 
ATOM   1460  N N   . PHE B 2 96  ? -13.382  -70.332  7.665   1.00 108.19 ? 102 PHE B N   1 
ATOM   1461  C CA  . PHE B 2 96  ? -12.571  -69.310  7.017   1.00 103.99 ? 102 PHE B CA  1 
ATOM   1462  C C   . PHE B 2 96  ? -12.978  -67.992  7.641   1.00 109.87 ? 102 PHE B C   1 
ATOM   1463  O O   . PHE B 2 96  ? -14.108  -67.520  7.450   1.00 113.30 ? 102 PHE B O   1 
ATOM   1464  C CB  . PHE B 2 96  ? -12.777  -69.284  5.497   1.00 104.28 ? 102 PHE B CB  1 
ATOM   1465  C CG  . PHE B 2 96  ? -11.588  -68.750  4.733   1.00 101.70 ? 102 PHE B CG  1 
ATOM   1466  C CD1 . PHE B 2 96  ? -11.162  -67.436  4.902   1.00 103.49 ? 102 PHE B CD1 1 
ATOM   1467  C CD2 . PHE B 2 96  ? -10.899  -69.558  3.838   1.00 100.75 ? 102 PHE B CD2 1 
ATOM   1468  C CE1 . PHE B 2 96  ? -10.062  -66.947  4.203   1.00 101.58 ? 102 PHE B CE1 1 
ATOM   1469  C CE2 . PHE B 2 96  ? -9.805   -69.064  3.135   1.00 100.66 ? 102 PHE B CE2 1 
ATOM   1470  C CZ  . PHE B 2 96  ? -9.396   -67.763  3.322   1.00 98.36  ? 102 PHE B CZ  1 
ATOM   1471  N N   . ILE B 2 97  ? -12.064  -67.432  8.434   1.00 104.13 ? 103 ILE B N   1 
ATOM   1472  C CA  . ILE B 2 97  ? -12.265  -66.198  9.182   1.00 105.60 ? 103 ILE B CA  1 
ATOM   1473  C C   . ILE B 2 97  ? -12.155  -65.007  8.252   1.00 109.90 ? 103 ILE B C   1 
ATOM   1474  O O   . ILE B 2 97  ? -11.216  -64.935  7.454   1.00 107.18 ? 103 ILE B O   1 
ATOM   1475  C CB  . ILE B 2 97  ? -11.280  -66.132  10.376  1.00 107.97 ? 103 ILE B CB  1 
ATOM   1476  C CG1 . ILE B 2 97  ? -11.145  -67.511  11.106  1.00 108.02 ? 103 ILE B CG1 1 
ATOM   1477  C CG2 . ILE B 2 97  ? -11.613  -64.989  11.340  1.00 112.02 ? 103 ILE B CG2 1 
ATOM   1478  C CD1 . ILE B 2 97  ? -12.402  -68.142  11.801  1.00 119.21 ? 103 ILE B CD1 1 
ATOM   1479  N N   . ASP B 2 98  ? -13.126  -64.075  8.357   1.00 109.87 ? 104 ASP B N   1 
ATOM   1480  C CA  . ASP B 2 98  ? -13.222  -62.864  7.539   1.00 110.84 ? 104 ASP B CA  1 
ATOM   1481  C C   . ASP B 2 98  ? -13.171  -63.224  6.045   1.00 112.30 ? 104 ASP B C   1 
ATOM   1482  O O   . ASP B 2 98  ? -12.522  -62.526  5.260   1.00 110.89 ? 104 ASP B O   1 
ATOM   1483  C CB  . ASP B 2 98  ? -12.122  -61.836  7.916   1.00 112.81 ? 104 ASP B CB  1 
ATOM   1484  C CG  . ASP B 2 98  ? -12.044  -61.434  9.380   1.00 128.59 ? 104 ASP B CG  1 
ATOM   1485  O OD1 . ASP B 2 98  ? -13.116  -61.338  10.035  1.00 132.97 ? 104 ASP B OD1 1 
ATOM   1486  O OD2 . ASP B 2 98  ? -10.920  -61.152  9.857   1.00 134.42 ? 104 ASP B OD2 1 
ATOM   1487  N N   . TYR B 2 99  ? -13.825  -64.342  5.663   1.00 108.54 ? 105 TYR B N   1 
ATOM   1488  C CA  . TYR B 2 99  ? -13.837  -64.786  4.272   1.00 107.64 ? 105 TYR B CA  1 
ATOM   1489  C C   . TYR B 2 99  ? -14.570  -63.781  3.404   1.00 115.42 ? 105 TYR B C   1 
ATOM   1490  O O   . TYR B 2 99  ? -14.061  -63.409  2.346   1.00 114.13 ? 105 TYR B O   1 
ATOM   1491  C CB  . TYR B 2 99  ? -14.420  -66.202  4.120   1.00 109.27 ? 105 TYR B CB  1 
ATOM   1492  C CG  . TYR B 2 99  ? -14.519  -66.685  2.684   1.00 110.89 ? 105 TYR B CG  1 
ATOM   1493  C CD1 . TYR B 2 99  ? -13.460  -66.519  1.793   1.00 110.05 ? 105 TYR B CD1 1 
ATOM   1494  C CD2 . TYR B 2 99  ? -15.655  -67.343  2.227   1.00 115.10 ? 105 TYR B CD2 1 
ATOM   1495  C CE1 . TYR B 2 99  ? -13.562  -66.922  0.464   1.00 112.09 ? 105 TYR B CE1 1 
ATOM   1496  C CE2 . TYR B 2 99  ? -15.754  -67.787  0.909   1.00 116.85 ? 105 TYR B CE2 1 
ATOM   1497  C CZ  . TYR B 2 99  ? -14.705  -67.574  0.029   1.00 123.56 ? 105 TYR B CZ  1 
ATOM   1498  O OH  . TYR B 2 99  ? -14.802  -68.016  -1.273  1.00 127.13 ? 105 TYR B OH  1 
ATOM   1499  N N   . GLU B 2 100 ? -15.744  -63.317  3.872   1.00 116.64 ? 106 GLU B N   1 
ATOM   1500  C CA  . GLU B 2 100 ? -16.562  -62.309  3.195   1.00 120.36 ? 106 GLU B CA  1 
ATOM   1501  C C   . GLU B 2 100 ? -15.726  -61.032  3.065   1.00 124.11 ? 106 GLU B C   1 
ATOM   1502  O O   . GLU B 2 100 ? -15.674  -60.440  1.987   1.00 124.74 ? 106 GLU B O   1 
ATOM   1503  C CB  . GLU B 2 100 ? -17.884  -62.023  3.944   1.00 126.67 ? 106 GLU B CB  1 
ATOM   1504  C CG  . GLU B 2 100 ? -18.304  -63.043  4.993   1.00 141.67 ? 106 GLU B CG  1 
ATOM   1505  C CD  . GLU B 2 100 ? -17.615  -62.903  6.340   1.00 170.17 ? 106 GLU B CD  1 
ATOM   1506  O OE1 . GLU B 2 100 ? -18.120  -62.138  7.195   1.00 158.80 ? 106 GLU B OE1 1 
ATOM   1507  O OE2 . GLU B 2 100 ? -16.568  -63.562  6.538   1.00 170.69 ? 106 GLU B OE2 1 
ATOM   1508  N N   . GLU B 2 101 ? -15.003  -60.672  4.144   1.00 119.84 ? 107 GLU B N   1 
ATOM   1509  C CA  . GLU B 2 101 ? -14.109  -59.518  4.201   1.00 119.98 ? 107 GLU B CA  1 
ATOM   1510  C C   . GLU B 2 101 ? -12.920  -59.674  3.238   1.00 120.90 ? 107 GLU B C   1 
ATOM   1511  O O   . GLU B 2 101 ? -12.427  -58.664  2.734   1.00 121.98 ? 107 GLU B O   1 
ATOM   1512  C CB  . GLU B 2 101 ? -13.642  -59.261  5.642   1.00 121.96 ? 107 GLU B CB  1 
ATOM   1513  C CG  . GLU B 2 101 ? -14.679  -58.567  6.521   1.00 139.49 ? 107 GLU B CG  1 
ATOM   1514  C CD  . GLU B 2 101 ? -15.799  -59.402  7.123   1.00 156.88 ? 107 GLU B CD  1 
ATOM   1515  O OE1 . GLU B 2 101 ? -16.980  -59.105  6.830   1.00 149.40 ? 107 GLU B OE1 1 
ATOM   1516  O OE2 . GLU B 2 101 ? -15.504  -60.297  7.949   1.00 143.74 ? 107 GLU B OE2 1 
ATOM   1517  N N   . LEU B 2 102 ? -12.492  -60.936  2.953   1.00 113.76 ? 108 LEU B N   1 
ATOM   1518  C CA  . LEU B 2 102 ? -11.410  -61.246  2.004   1.00 110.78 ? 108 LEU B CA  1 
ATOM   1519  C C   . LEU B 2 102 ? -11.883  -61.029  0.571   1.00 117.01 ? 108 LEU B C   1 
ATOM   1520  O O   . LEU B 2 102 ? -11.109  -60.536  -0.252  1.00 115.98 ? 108 LEU B O   1 
ATOM   1521  C CB  . LEU B 2 102 ? -10.840  -62.676  2.202   1.00 107.13 ? 108 LEU B CB  1 
ATOM   1522  C CG  . LEU B 2 102 ? -9.728   -63.161  1.235   1.00 108.21 ? 108 LEU B CG  1 
ATOM   1523  C CD1 . LEU B 2 102 ? -8.474   -62.321  1.340   1.00 107.72 ? 108 LEU B CD1 1 
ATOM   1524  C CD2 . LEU B 2 102 ? -9.375   -64.591  1.493   1.00 106.60 ? 108 LEU B CD2 1 
ATOM   1525  N N   . ARG B 2 103 ? -13.156  -61.385  0.282   1.00 116.37 ? 109 ARG B N   1 
ATOM   1526  C CA  . ARG B 2 103 ? -13.770  -61.187  -1.031  1.00 118.80 ? 109 ARG B CA  1 
ATOM   1527  C C   . ARG B 2 103 ? -13.794  -59.694  -1.321  1.00 128.76 ? 109 ARG B C   1 
ATOM   1528  O O   . ARG B 2 103 ? -13.383  -59.283  -2.406  1.00 129.54 ? 109 ARG B O   1 
ATOM   1529  C CB  . ARG B 2 103 ? -15.190  -61.759  -1.078  1.00 118.41 ? 109 ARG B CB  1 
ATOM   1530  C CG  . ARG B 2 103 ? -15.249  -63.270  -1.030  1.00 118.81 ? 109 ARG B CG  1 
ATOM   1531  C CD  . ARG B 2 103 ? -16.688  -63.726  -1.034  1.00 124.55 ? 109 ARG B CD  1 
ATOM   1532  N NE  . ARG B 2 103 ? -17.146  -64.046  -2.382  1.00 126.81 ? 109 ARG B NE  1 
ATOM   1533  C CZ  . ARG B 2 103 ? -17.220  -65.279  -2.871  1.00 136.83 ? 109 ARG B CZ  1 
ATOM   1534  N NH1 . ARG B 2 103 ? -16.873  -66.319  -2.123  1.00 110.68 ? 109 ARG B NH1 1 
ATOM   1535  N NH2 . ARG B 2 103 ? -17.638  -65.481  -4.114  1.00 134.60 ? 109 ARG B NH2 1 
ATOM   1536  N N   . GLU B 2 104 ? -14.193  -58.880  -0.311  1.00 129.00 ? 110 GLU B N   1 
ATOM   1537  C CA  . GLU B 2 104 ? -14.239  -57.414  -0.385  1.00 133.10 ? 110 GLU B CA  1 
ATOM   1538  C C   . GLU B 2 104 ? -12.864  -56.840  -0.760  1.00 135.95 ? 110 GLU B C   1 
ATOM   1539  O O   . GLU B 2 104 ? -12.790  -55.936  -1.597  1.00 138.87 ? 110 GLU B O   1 
ATOM   1540  C CB  . GLU B 2 104 ? -14.745  -56.801  0.939   1.00 137.17 ? 110 GLU B CB  1 
ATOM   1541  C CG  . GLU B 2 104 ? -16.222  -57.044  1.247   1.00 155.07 ? 110 GLU B CG  1 
ATOM   1542  C CD  . GLU B 2 104 ? -17.265  -56.229  0.494   1.00 189.33 ? 110 GLU B CD  1 
ATOM   1543  O OE1 . GLU B 2 104 ? -17.074  -55.001  0.332   1.00 196.04 ? 110 GLU B OE1 1 
ATOM   1544  O OE2 . GLU B 2 104 ? -18.314  -56.810  0.131   1.00 183.94 ? 110 GLU B OE2 1 
ATOM   1545  N N   . GLN B 2 105 ? -11.784  -57.407  -0.182  1.00 128.00 ? 111 GLN B N   1 
ATOM   1546  C CA  . GLN B 2 105 ? -10.408  -56.991  -0.453  1.00 126.31 ? 111 GLN B CA  1 
ATOM   1547  C C   . GLN B 2 105 ? -9.911   -57.491  -1.803  1.00 128.39 ? 111 GLN B C   1 
ATOM   1548  O O   . GLN B 2 105 ? -9.176   -56.777  -2.488  1.00 128.93 ? 111 GLN B O   1 
ATOM   1549  C CB  . GLN B 2 105 ? -9.463   -57.423  0.679   1.00 124.82 ? 111 GLN B CB  1 
ATOM   1550  C CG  . GLN B 2 105 ? -9.726   -56.726  2.014   1.00 144.88 ? 111 GLN B CG  1 
ATOM   1551  C CD  . GLN B 2 105 ? -9.474   -55.239  1.961   1.00 171.96 ? 111 GLN B CD  1 
ATOM   1552  O OE1 . GLN B 2 105 ? -8.328   -54.775  1.970   1.00 168.20 ? 111 GLN B OE1 1 
ATOM   1553  N NE2 . GLN B 2 105 ? -10.545  -54.458  1.903   1.00 168.94 ? 111 GLN B NE2 1 
ATOM   1554  N N   . LEU B 2 106 ? -10.318  -58.707  -2.190  1.00 123.56 ? 112 LEU B N   1 
ATOM   1555  C CA  . LEU B 2 106 ? -9.924   -59.297  -3.462  1.00 123.35 ? 112 LEU B CA  1 
ATOM   1556  C C   . LEU B 2 106 ? -10.796  -58.819  -4.634  1.00 133.72 ? 112 LEU B C   1 
ATOM   1557  O O   . LEU B 2 106 ? -10.484  -59.151  -5.781  1.00 134.60 ? 112 LEU B O   1 
ATOM   1558  C CB  . LEU B 2 106 ? -9.852   -60.838  -3.388  1.00 120.04 ? 112 LEU B CB  1 
ATOM   1559  C CG  . LEU B 2 106 ? -8.497   -61.458  -2.990  1.00 121.07 ? 112 LEU B CG  1 
ATOM   1560  C CD1 . LEU B 2 106 ? -8.683   -62.837  -2.415  1.00 118.73 ? 112 LEU B CD1 1 
ATOM   1561  C CD2 . LEU B 2 106 ? -7.539   -61.553  -4.178  1.00 123.22 ? 112 LEU B CD2 1 
ATOM   1562  N N   . SER B 2 107 ? -11.853  -58.011  -4.357  1.00 134.77 ? 113 SER B N   1 
ATOM   1563  C CA  . SER B 2 107 ? -12.751  -57.455  -5.377  1.00 140.07 ? 113 SER B CA  1 
ATOM   1564  C C   . SER B 2 107 ? -11.931  -56.704  -6.414  1.00 149.98 ? 113 SER B C   1 
ATOM   1565  O O   . SER B 2 107 ? -11.886  -57.109  -7.579  1.00 150.69 ? 113 SER B O   1 
ATOM   1566  C CB  . SER B 2 107 ? -13.760  -56.498  -4.748  1.00 146.33 ? 113 SER B CB  1 
ATOM   1567  O OG  . SER B 2 107 ? -14.507  -57.129  -3.724  1.00 153.56 ? 113 SER B OG  1 
ATOM   1568  N N   . SER B 2 108 ? -11.212  -55.666  -5.950  1.00 150.25 ? 114 SER B N   1 
ATOM   1569  C CA  . SER B 2 108 ? -10.345  -54.806  -6.746  1.00 153.44 ? 114 SER B CA  1 
ATOM   1570  C C   . SER B 2 108 ? -8.889   -55.327  -6.777  1.00 156.13 ? 114 SER B C   1 
ATOM   1571  O O   . SER B 2 108 ? -8.103   -54.984  -5.889  1.00 154.06 ? 114 SER B O   1 
ATOM   1572  C CB  . SER B 2 108 ? -10.418  -53.374  -6.220  1.00 159.75 ? 114 SER B CB  1 
ATOM   1573  O OG  . SER B 2 108 ? -10.102  -53.307  -4.838  1.00 162.85 ? 114 SER B OG  1 
ATOM   1574  N N   . VAL B 2 109 ? -8.544   -56.190  -7.778  1.00 153.27 ? 115 VAL B N   1 
ATOM   1575  C CA  . VAL B 2 109 ? -7.193   -56.760  -7.949  1.00 150.99 ? 115 VAL B CA  1 
ATOM   1576  C C   . VAL B 2 109 ? -6.746   -56.749  -9.425  1.00 158.63 ? 115 VAL B C   1 
ATOM   1577  O O   . VAL B 2 109 ? -7.347   -57.432  -10.260 1.00 158.76 ? 115 VAL B O   1 
ATOM   1578  C CB  . VAL B 2 109 ? -7.004   -58.162  -7.299  1.00 149.92 ? 115 VAL B CB  1 
ATOM   1579  C CG1 . VAL B 2 109 ? -5.622   -58.731  -7.607  1.00 148.11 ? 115 VAL B CG1 1 
ATOM   1580  C CG2 . VAL B 2 109 ? -7.214   -58.113  -5.791  1.00 147.37 ? 115 VAL B CG2 1 
ATOM   1581  N N   . SER B 2 110 ? -5.669   -55.992  -9.721  1.00 158.02 ? 116 SER B N   1 
ATOM   1582  C CA  . SER B 2 110 ? -5.076   -55.883  -11.057 1.00 161.43 ? 116 SER B CA  1 
ATOM   1583  C C   . SER B 2 110 ? -4.022   -56.995  -11.223 1.00 163.18 ? 116 SER B C   1 
ATOM   1584  O O   . SER B 2 110 ? -4.373   -58.085  -11.687 1.00 161.82 ? 116 SER B O   1 
ATOM   1585  C CB  . SER B 2 110 ? -4.477   -54.491  -11.274 1.00 169.03 ? 116 SER B CB  1 
ATOM   1586  O OG  . SER B 2 110 ? -3.964   -54.325  -12.586 1.00 180.74 ? 116 SER B OG  1 
ATOM   1587  N N   . SER B 2 111 A -2.756   -56.736  -10.793 1.00 158.73 ? 116 SER B N   1 
ATOM   1588  C CA  . SER B 2 111 A -1.619   -57.672  -10.838 1.00 155.80 ? 116 SER B CA  1 
ATOM   1589  C C   . SER B 2 111 A -1.720   -58.722  -9.714  1.00 151.57 ? 116 SER B C   1 
ATOM   1590  O O   . SER B 2 111 A -2.582   -58.604  -8.837  1.00 149.28 ? 116 SER B O   1 
ATOM   1591  C CB  . SER B 2 111 A -0.293   -56.908  -10.762 1.00 162.45 ? 116 SER B CB  1 
ATOM   1592  O OG  . SER B 2 111 A 0.845    -57.758  -10.748 1.00 169.85 ? 116 SER B OG  1 
ATOM   1593  N N   . PHE B 2 112 B -0.848   -59.751  -9.757  1.00 144.14 ? 116 PHE B N   1 
ATOM   1594  C CA  . PHE B 2 112 B -0.820   -60.834  -8.777  1.00 138.73 ? 116 PHE B CA  1 
ATOM   1595  C C   . PHE B 2 112 B 0.459    -61.667  -8.910  1.00 138.36 ? 116 PHE B C   1 
ATOM   1596  O O   . PHE B 2 112 B 0.708    -62.249  -9.970  1.00 139.77 ? 116 PHE B O   1 
ATOM   1597  C CB  . PHE B 2 112 B -2.053   -61.736  -8.974  1.00 139.32 ? 116 PHE B CB  1 
ATOM   1598  C CG  . PHE B 2 112 B -2.627   -62.395  -7.748  1.00 137.48 ? 116 PHE B CG  1 
ATOM   1599  C CD1 . PHE B 2 112 B -3.376   -61.665  -6.832  1.00 140.47 ? 116 PHE B CD1 1 
ATOM   1600  C CD2 . PHE B 2 112 B -2.522   -63.767  -7.566  1.00 137.53 ? 116 PHE B CD2 1 
ATOM   1601  C CE1 . PHE B 2 112 B -3.967   -62.288  -5.732  1.00 138.88 ? 116 PHE B CE1 1 
ATOM   1602  C CE2 . PHE B 2 112 B -3.112   -64.390  -6.465  1.00 137.97 ? 116 PHE B CE2 1 
ATOM   1603  C CZ  . PHE B 2 112 B -3.829   -63.646  -5.554  1.00 135.88 ? 116 PHE B CZ  1 
ATOM   1604  N N   . GLU B 2 113 C 1.272    -61.712  -7.839  1.00 129.77 ? 116 GLU B N   1 
ATOM   1605  C CA  . GLU B 2 113 C 2.485    -62.528  -7.782  1.00 127.16 ? 116 GLU B CA  1 
ATOM   1606  C C   . GLU B 2 113 C 2.362    -63.518  -6.637  1.00 122.08 ? 116 GLU B C   1 
ATOM   1607  O O   . GLU B 2 113 C 2.247    -63.115  -5.477  1.00 120.35 ? 116 GLU B O   1 
ATOM   1608  C CB  . GLU B 2 113 C 3.771    -61.679  -7.627  1.00 131.36 ? 116 GLU B CB  1 
ATOM   1609  C CG  . GLU B 2 113 C 5.065    -62.494  -7.677  1.00 138.81 ? 116 GLU B CG  1 
ATOM   1610  C CD  . GLU B 2 113 C 6.318    -61.909  -7.041  1.00 156.52 ? 116 GLU B CD  1 
ATOM   1611  O OE1 . GLU B 2 113 C 6.307    -60.717  -6.655  1.00 154.20 ? 116 GLU B OE1 1 
ATOM   1612  O OE2 . GLU B 2 113 C 7.321    -62.652  -6.935  1.00 142.83 ? 116 GLU B OE2 1 
ATOM   1613  N N   . ARG B 2 114 ? 2.374    -64.812  -6.970  1.00 113.31 ? 117 ARG B N   1 
ATOM   1614  C CA  . ARG B 2 114 ? 2.360    -65.887  -5.987  1.00 108.12 ? 117 ARG B CA  1 
ATOM   1615  C C   . ARG B 2 114 ? 3.834    -66.232  -5.790  1.00 109.03 ? 117 ARG B C   1 
ATOM   1616  O O   . ARG B 2 114 ? 4.544    -66.463  -6.775  1.00 111.75 ? 117 ARG B O   1 
ATOM   1617  C CB  . ARG B 2 114 ? 1.551    -67.087  -6.507  1.00 106.67 ? 117 ARG B CB  1 
ATOM   1618  C CG  . ARG B 2 114 ? 1.616    -68.336  -5.637  1.00 112.19 ? 117 ARG B CG  1 
ATOM   1619  C CD  . ARG B 2 114 ? 0.778    -69.433  -6.259  1.00 122.70 ? 117 ARG B CD  1 
ATOM   1620  N NE  . ARG B 2 114 ? 1.238    -70.781  -5.912  1.00 128.17 ? 117 ARG B NE  1 
ATOM   1621  C CZ  . ARG B 2 114 ? 2.131    -71.480  -6.611  1.00 137.52 ? 117 ARG B CZ  1 
ATOM   1622  N NH1 . ARG B 2 114 ? 2.703    -70.954  -7.688  1.00 125.12 ? 117 ARG B NH1 1 
ATOM   1623  N NH2 . ARG B 2 114 ? 2.469    -72.704  -6.228  1.00 118.55 ? 117 ARG B NH2 1 
ATOM   1624  N N   . PHE B 2 115 ? 4.312    -66.193  -4.537  1.00 100.78 ? 118 PHE B N   1 
ATOM   1625  C CA  . PHE B 2 115 ? 5.716    -66.467  -4.229  1.00 100.51 ? 118 PHE B CA  1 
ATOM   1626  C C   . PHE B 2 115 ? 5.891    -67.336  -3.005  1.00 100.85 ? 118 PHE B C   1 
ATOM   1627  O O   . PHE B 2 115 ? 5.075    -67.258  -2.091  1.00 99.02  ? 118 PHE B O   1 
ATOM   1628  C CB  . PHE B 2 115 ? 6.510    -65.154  -4.085  1.00 104.89 ? 118 PHE B CB  1 
ATOM   1629  C CG  . PHE B 2 115 ? 6.179    -64.286  -2.890  1.00 105.41 ? 118 PHE B CG  1 
ATOM   1630  C CD1 . PHE B 2 115 ? 5.114    -63.394  -2.931  1.00 107.68 ? 118 PHE B CD1 1 
ATOM   1631  C CD2 . PHE B 2 115 ? 6.969    -64.317  -1.748  1.00 107.99 ? 118 PHE B CD2 1 
ATOM   1632  C CE1 . PHE B 2 115 ? 4.819    -62.580  -1.833  1.00 108.67 ? 118 PHE B CE1 1 
ATOM   1633  C CE2 . PHE B 2 115 ? 6.669    -63.505  -0.648  1.00 110.98 ? 118 PHE B CE2 1 
ATOM   1634  C CZ  . PHE B 2 115 ? 5.598    -62.642  -0.699  1.00 108.51 ? 118 PHE B CZ  1 
ATOM   1635  N N   . GLU B 2 116 ? 6.970    -68.140  -2.969  1.00 97.26  ? 119 GLU B N   1 
ATOM   1636  C CA  . GLU B 2 116 ? 7.282    -68.985  -1.817  1.00 95.83  ? 119 GLU B CA  1 
ATOM   1637  C C   . GLU B 2 116 ? 7.785    -68.068  -0.697  1.00 100.52 ? 119 GLU B C   1 
ATOM   1638  O O   . GLU B 2 116 ? 8.957    -67.686  -0.681  1.00 103.64 ? 119 GLU B O   1 
ATOM   1639  C CB  . GLU B 2 116 ? 8.304    -70.087  -2.176  1.00 98.82  ? 119 GLU B CB  1 
ATOM   1640  C CG  . GLU B 2 116 ? 7.812    -71.502  -1.894  1.00 108.46 ? 119 GLU B CG  1 
ATOM   1641  C CD  . GLU B 2 116 ? 8.709    -72.652  -2.324  1.00 136.82 ? 119 GLU B CD  1 
ATOM   1642  O OE1 . GLU B 2 116 ? 9.373    -72.543  -3.381  1.00 130.68 ? 119 GLU B OE1 1 
ATOM   1643  O OE2 . GLU B 2 116 ? 8.695    -73.695  -1.629  1.00 136.17 ? 119 GLU B OE2 1 
ATOM   1644  N N   . ILE B 2 117 ? 6.856    -67.629  0.171   1.00 94.94  ? 120 ILE B N   1 
ATOM   1645  C CA  . ILE B 2 117 ? 7.135    -66.732  1.297   1.00 96.38  ? 120 ILE B CA  1 
ATOM   1646  C C   . ILE B 2 117 ? 8.081    -67.414  2.294   1.00 103.86 ? 120 ILE B C   1 
ATOM   1647  O O   . ILE B 2 117 ? 9.096    -66.831  2.686   1.00 106.95 ? 120 ILE B O   1 
ATOM   1648  C CB  . ILE B 2 117 ? 5.830    -66.160  1.937   1.00 97.37  ? 120 ILE B CB  1 
ATOM   1649  C CG1 . ILE B 2 117 ? 6.143    -65.162  3.075   1.00 100.01 ? 120 ILE B CG1 1 
ATOM   1650  C CG2 . ILE B 2 117 ? 4.845    -67.258  2.381   1.00 94.47  ? 120 ILE B CG2 1 
ATOM   1651  C CD1 . ILE B 2 117 ? 5.015    -64.263  3.484   1.00 105.34 ? 120 ILE B CD1 1 
ATOM   1652  N N   . PHE B 2 118 ? 7.759    -68.665  2.648   1.00 99.92  ? 121 PHE B N   1 
ATOM   1653  C CA  . PHE B 2 118 ? 8.531    -69.520  3.536   1.00 101.26 ? 121 PHE B CA  1 
ATOM   1654  C C   . PHE B 2 118 ? 8.669    -70.871  2.821   1.00 104.79 ? 121 PHE B C   1 
ATOM   1655  O O   . PHE B 2 118 ? 7.818    -71.750  3.011   1.00 102.45 ? 121 PHE B O   1 
ATOM   1656  C CB  . PHE B 2 118 ? 7.837    -69.689  4.898   1.00 102.30 ? 121 PHE B CB  1 
ATOM   1657  C CG  . PHE B 2 118 ? 7.476    -68.436  5.665   1.00 104.95 ? 121 PHE B CG  1 
ATOM   1658  C CD1 . PHE B 2 118 ? 8.458    -67.671  6.279   1.00 111.55 ? 121 PHE B CD1 1 
ATOM   1659  C CD2 . PHE B 2 118 ? 6.147    -68.078  5.857   1.00 105.22 ? 121 PHE B CD2 1 
ATOM   1660  C CE1 . PHE B 2 118 ? 8.120    -66.539  7.026   1.00 113.98 ? 121 PHE B CE1 1 
ATOM   1661  C CE2 . PHE B 2 118 ? 5.811    -66.947  6.608   1.00 109.38 ? 121 PHE B CE2 1 
ATOM   1662  C CZ  . PHE B 2 118 ? 6.799    -66.187  7.188   1.00 110.78 ? 121 PHE B CZ  1 
ATOM   1663  N N   . PRO B 2 119 ? 9.699    -71.022  1.945   1.00 103.84 ? 122 PRO B N   1 
ATOM   1664  C CA  . PRO B 2 119 ? 9.856    -72.276  1.180   1.00 103.63 ? 122 PRO B CA  1 
ATOM   1665  C C   . PRO B 2 119 ? 9.985    -73.559  2.005   1.00 106.60 ? 122 PRO B C   1 
ATOM   1666  O O   . PRO B 2 119 ? 10.746   -73.602  2.974   1.00 107.79 ? 122 PRO B O   1 
ATOM   1667  C CB  . PRO B 2 119 ? 11.107   -72.020  0.327   1.00 108.94 ? 122 PRO B CB  1 
ATOM   1668  C CG  . PRO B 2 119 ? 11.831   -70.923  1.022   1.00 115.97 ? 122 PRO B CG  1 
ATOM   1669  C CD  . PRO B 2 119 ? 10.750   -70.053  1.579   1.00 108.96 ? 122 PRO B CD  1 
ATOM   1670  N N   . LYS B 2 120 ? 9.250    -74.618  1.584   1.00 101.12 ? 123 LYS B N   1 
ATOM   1671  C CA  . LYS B 2 120 ? 9.186    -75.943  2.223   1.00 101.04 ? 123 LYS B CA  1 
ATOM   1672  C C   . LYS B 2 120 ? 10.574   -76.565  2.488   1.00 108.05 ? 123 LYS B C   1 
ATOM   1673  O O   . LYS B 2 120 ? 10.774   -77.214  3.520   1.00 107.97 ? 123 LYS B O   1 
ATOM   1674  C CB  . LYS B 2 120 ? 8.281    -76.888  1.404   1.00 102.26 ? 123 LYS B CB  1 
ATOM   1675  C CG  . LYS B 2 120 ? 7.417    -77.843  2.241   1.00 107.66 ? 123 LYS B CG  1 
ATOM   1676  C CD  . LYS B 2 120 ? 7.892    -79.307  2.166   1.00 114.13 ? 123 LYS B CD  1 
ATOM   1677  C CE  . LYS B 2 120 ? 7.348    -80.073  0.976   1.00 111.13 ? 123 LYS B CE  1 
ATOM   1678  N NZ  . LYS B 2 120 ? 8.022    -81.389  0.791   1.00 113.52 ? 123 LYS B NZ  1 
ATOM   1679  N N   . THR B 2 121 ? 11.530   -76.331  1.567   1.00 108.02 ? 124 THR B N   1 
ATOM   1680  C CA  . THR B 2 121 ? 12.911   -76.819  1.664   1.00 112.21 ? 124 THR B CA  1 
ATOM   1681  C C   . THR B 2 121 ? 13.608   -76.326  2.941   1.00 118.74 ? 124 THR B C   1 
ATOM   1682  O O   . THR B 2 121 ? 13.730   -77.093  3.898   1.00 119.71 ? 124 THR B O   1 
ATOM   1683  C CB  . THR B 2 121 ? 13.726   -76.482  0.393   1.00 118.20 ? 124 THR B CB  1 
ATOM   1684  O OG1 . THR B 2 121 ? 13.705   -75.072  0.179   1.00 114.29 ? 124 THR B OG1 1 
ATOM   1685  C CG2 . THR B 2 121 ? 13.215   -77.201  -0.844  1.00 115.12 ? 124 THR B CG2 1 
ATOM   1686  N N   . SER B 2 122 ? 14.010   -75.041  2.966   1.00 115.78 ? 125 SER B N   1 
ATOM   1687  C CA  . SER B 2 122 ? 14.742   -74.410  4.058   1.00 118.15 ? 125 SER B CA  1 
ATOM   1688  C C   . SER B 2 122 ? 13.902   -74.050  5.298   1.00 120.96 ? 125 SER B C   1 
ATOM   1689  O O   . SER B 2 122 ? 14.037   -74.724  6.318   1.00 122.94 ? 125 SER B O   1 
ATOM   1690  C CB  . SER B 2 122 ? 15.487   -73.181  3.549   1.00 123.08 ? 125 SER B CB  1 
ATOM   1691  O OG  . SER B 2 122 ? 14.579   -72.259  2.970   1.00 125.38 ? 125 SER B OG  1 
ATOM   1692  N N   . SER B 2 123 ? 13.068   -72.987  5.208   1.00 113.92 ? 126 SER B N   1 
ATOM   1693  C CA  . SER B 2 123 ? 12.238   -72.348  6.242   1.00 111.85 ? 126 SER B CA  1 
ATOM   1694  C C   . SER B 2 123 ? 11.899   -73.152  7.501   1.00 116.42 ? 126 SER B C   1 
ATOM   1695  O O   . SER B 2 123 ? 11.982   -72.586  8.592   1.00 117.98 ? 126 SER B O   1 
ATOM   1696  C CB  . SER B 2 123 ? 10.940   -71.836  5.643   1.00 110.32 ? 126 SER B CB  1 
ATOM   1697  O OG  . SER B 2 123 ? 11.231   -70.770  4.760   1.00 118.08 ? 126 SER B OG  1 
ATOM   1698  N N   . TRP B 2 124 ? 11.483   -74.425  7.368   1.00 111.49 ? 127 TRP B N   1 
ATOM   1699  C CA  . TRP B 2 124 ? 11.094   -75.238  8.522   1.00 111.56 ? 127 TRP B CA  1 
ATOM   1700  C C   . TRP B 2 124 ? 12.046   -76.433  8.697   1.00 120.65 ? 127 TRP B C   1 
ATOM   1701  O O   . TRP B 2 124 ? 11.772   -77.516  8.169   1.00 119.86 ? 127 TRP B O   1 
ATOM   1702  C CB  . TRP B 2 124 ? 9.616    -75.647  8.406   1.00 106.05 ? 127 TRP B CB  1 
ATOM   1703  C CG  . TRP B 2 124 ? 8.759    -74.561  7.820   1.00 103.96 ? 127 TRP B CG  1 
ATOM   1704  C CD1 . TRP B 2 124 ? 8.289    -74.490  6.542   1.00 104.62 ? 127 TRP B CD1 1 
ATOM   1705  C CD2 . TRP B 2 124 ? 8.410    -73.318  8.443   1.00 103.83 ? 127 TRP B CD2 1 
ATOM   1706  N NE1 . TRP B 2 124 ? 7.616    -73.305  6.348   1.00 102.50 ? 127 TRP B NE1 1 
ATOM   1707  C CE2 . TRP B 2 124 ? 7.681    -72.563  7.498   1.00 105.19 ? 127 TRP B CE2 1 
ATOM   1708  C CE3 . TRP B 2 124 ? 8.616    -72.777  9.721   1.00 107.33 ? 127 TRP B CE3 1 
ATOM   1709  C CZ2 . TRP B 2 124 ? 7.147    -71.309  7.796   1.00 104.08 ? 127 TRP B CZ2 1 
ATOM   1710  C CZ3 . TRP B 2 124 ? 8.084    -71.533  10.013  1.00 108.40 ? 127 TRP B CZ3 1 
ATOM   1711  C CH2 . TRP B 2 124 ? 7.361    -70.813  9.057   1.00 106.38 ? 127 TRP B CH2 1 
ATOM   1712  N N   . PRO B 2 125 ? 13.194   -76.247  9.405   1.00 122.01 ? 128 PRO B N   1 
ATOM   1713  C CA  . PRO B 2 125 ? 14.174   -77.342  9.532   1.00 125.27 ? 128 PRO B CA  1 
ATOM   1714  C C   . PRO B 2 125 ? 14.046   -78.225  10.770  1.00 130.95 ? 128 PRO B C   1 
ATOM   1715  O O   . PRO B 2 125 ? 14.462   -79.381  10.716  1.00 132.40 ? 128 PRO B O   1 
ATOM   1716  C CB  . PRO B 2 125 ? 15.515   -76.608  9.511   1.00 131.33 ? 128 PRO B CB  1 
ATOM   1717  C CG  . PRO B 2 125 ? 15.205   -75.216  10.011  1.00 135.69 ? 128 PRO B CG  1 
ATOM   1718  C CD  . PRO B 2 125 ? 13.705   -75.017  10.042  1.00 126.27 ? 128 PRO B CD  1 
ATOM   1719  N N   . ASN B 2 126 ? 13.514   -77.689  11.883  1.00 128.19 ? 129 ASN B N   1 
ATOM   1720  C CA  . ASN B 2 126 ? 13.338   -78.454  13.116  1.00 130.86 ? 129 ASN B CA  1 
ATOM   1721  C C   . ASN B 2 126 ? 11.912   -79.006  13.239  1.00 131.11 ? 129 ASN B C   1 
ATOM   1722  O O   . ASN B 2 126 ? 11.447   -79.309  14.346  1.00 132.41 ? 129 ASN B O   1 
ATOM   1723  C CB  . ASN B 2 126 ? 13.754   -77.624  14.330  1.00 136.48 ? 129 ASN B CB  1 
ATOM   1724  C CG  . ASN B 2 126 ? 15.229   -77.323  14.373  1.00 174.11 ? 129 ASN B CG  1 
ATOM   1725  O OD1 . ASN B 2 126 ? 16.083   -78.186  14.112  1.00 175.74 ? 129 ASN B OD1 1 
ATOM   1726  N ND2 . ASN B 2 126 ? 15.560   -76.089  14.721  1.00 168.02 ? 129 ASN B ND2 1 
ATOM   1727  N N   . HIS B 2 127 ? 11.229   -79.159  12.078  1.00 123.42 ? 130 HIS B N   1 
ATOM   1728  C CA  . HIS B 2 127 ? 9.853    -79.649  11.968  1.00 120.06 ? 130 HIS B CA  1 
ATOM   1729  C C   . HIS B 2 127 ? 9.625    -80.538  10.740  1.00 120.74 ? 130 HIS B C   1 
ATOM   1730  O O   . HIS B 2 127 ? 10.359   -80.444  9.751   1.00 120.38 ? 130 HIS B O   1 
ATOM   1731  C CB  . HIS B 2 127 ? 8.864    -78.473  11.983  1.00 117.98 ? 130 HIS B CB  1 
ATOM   1732  C CG  . HIS B 2 127 ? 9.026    -77.589  13.179  1.00 123.96 ? 130 HIS B CG  1 
ATOM   1733  N ND1 . HIS B 2 127 ? 9.801    -76.446  13.125  1.00 127.02 ? 130 HIS B ND1 1 
ATOM   1734  C CD2 . HIS B 2 127 ? 8.584    -77.762  14.446  1.00 128.05 ? 130 HIS B CD2 1 
ATOM   1735  C CE1 . HIS B 2 127 ? 9.766    -75.935  14.345  1.00 129.27 ? 130 HIS B CE1 1 
ATOM   1736  N NE2 . HIS B 2 127 ? 9.044    -76.691  15.174  1.00 130.25 ? 130 HIS B NE2 1 
ATOM   1737  N N   . ASP B 2 128 ? 8.602    -81.406  10.823  1.00 115.19 ? 131 ASP B N   1 
ATOM   1738  C CA  . ASP B 2 128 ? 8.208    -82.319  9.758   1.00 113.71 ? 131 ASP B CA  1 
ATOM   1739  C C   . ASP B 2 128 ? 7.159    -81.622  8.904   1.00 111.95 ? 131 ASP B C   1 
ATOM   1740  O O   . ASP B 2 128 ? 6.056    -81.329  9.368   1.00 109.53 ? 131 ASP B O   1 
ATOM   1741  C CB  . ASP B 2 128 ? 7.675    -83.640  10.346  1.00 118.44 ? 131 ASP B CB  1 
ATOM   1742  C CG  . ASP B 2 128 ? 7.386    -84.754  9.352   1.00 132.39 ? 131 ASP B CG  1 
ATOM   1743  O OD1 . ASP B 2 128 ? 6.822    -84.462  8.278   1.00 131.17 ? 131 ASP B OD1 1 
ATOM   1744  O OD2 . ASP B 2 128 ? 7.637    -85.932  9.693   1.00 143.45 ? 131 ASP B OD2 1 
ATOM   1745  N N   . SER B 2 129 ? 7.526    -81.341  7.658   1.00 117.49 ? 132 SER B N   1 
ATOM   1746  C CA  . SER B 2 129 ? 6.670    -80.670  6.685   1.00 116.06 ? 132 SER B CA  1 
ATOM   1747  C C   . SER B 2 129 ? 6.010    -81.666  5.715   1.00 120.49 ? 132 SER B C   1 
ATOM   1748  O O   . SER B 2 129 ? 4.922    -81.400  5.189   1.00 118.75 ? 132 SER B O   1 
ATOM   1749  C CB  . SER B 2 129 ? 7.470    -79.619  5.919   1.00 120.30 ? 132 SER B CB  1 
ATOM   1750  O OG  . SER B 2 129 ? 8.818    -80.008  5.715   1.00 128.53 ? 132 SER B OG  1 
ATOM   1751  N N   . ASP B 2 130 ? 6.671    -82.814  5.497   1.00 118.59 ? 133 ASP B N   1 
ATOM   1752  C CA  . ASP B 2 130 ? 6.248    -83.862  4.568   1.00 117.71 ? 133 ASP B CA  1 
ATOM   1753  C C   . ASP B 2 130 ? 5.072    -84.722  5.048   1.00 118.24 ? 133 ASP B C   1 
ATOM   1754  O O   . ASP B 2 130 ? 4.363    -85.261  4.196   1.00 117.55 ? 133 ASP B O   1 
ATOM   1755  C CB  . ASP B 2 130 ? 7.436    -84.757  4.175   1.00 122.27 ? 133 ASP B CB  1 
ATOM   1756  C CG  . ASP B 2 130 ? 8.698    -84.005  3.788   1.00 140.52 ? 133 ASP B CG  1 
ATOM   1757  O OD1 . ASP B 2 130 ? 8.656    -83.233  2.800   1.00 141.70 ? 133 ASP B OD1 1 
ATOM   1758  O OD2 . ASP B 2 130 ? 9.736    -84.216  4.448   1.00 151.48 ? 133 ASP B OD2 1 
ATOM   1759  N N   . LYS B 2 131 A 4.862    -84.875  6.383   1.00 112.57 ? 133 LYS B N   1 
ATOM   1760  C CA  . LYS B 2 131 A 3.756    -85.694  6.902   1.00 110.11 ? 133 LYS B CA  1 
ATOM   1761  C C   . LYS B 2 131 A 2.445    -84.907  7.076   1.00 111.40 ? 133 LYS B C   1 
ATOM   1762  O O   . LYS B 2 131 A 1.414    -85.500  7.394   1.00 109.90 ? 133 LYS B O   1 
ATOM   1763  C CB  . LYS B 2 131 A 4.134    -86.452  8.189   1.00 112.72 ? 133 LYS B CB  1 
ATOM   1764  C CG  . LYS B 2 131 A 4.032    -87.985  8.054   1.00 125.92 ? 133 LYS B CG  1 
ATOM   1765  C CD  . LYS B 2 131 A 2.576    -88.532  8.040   1.00 129.57 ? 133 LYS B CD  1 
ATOM   1766  C CE  . LYS B 2 131 A 2.427    -89.853  7.320   1.00 127.72 ? 133 LYS B CE  1 
ATOM   1767  N NZ  . LYS B 2 131 A 1.034    -90.062  6.853   1.00 123.76 ? 133 LYS B NZ  1 
ATOM   1768  N N   . GLY B 2 132 ? 2.474    -83.607  6.785   1.00 107.49 ? 134 GLY B N   1 
ATOM   1769  C CA  . GLY B 2 132 ? 1.300    -82.744  6.874   1.00 105.71 ? 134 GLY B CA  1 
ATOM   1770  C C   . GLY B 2 132 ? 0.273    -82.899  5.762   1.00 107.11 ? 134 GLY B C   1 
ATOM   1771  O O   . GLY B 2 132 ? -0.156   -81.894  5.177   1.00 106.57 ? 134 GLY B O   1 
ATOM   1772  N N   . VAL B 2 133 ? -0.141   -84.162  5.471   1.00 101.01 ? 135 VAL B N   1 
ATOM   1773  C CA  . VAL B 2 133 ? -1.129   -84.514  4.440   1.00 98.95  ? 135 VAL B CA  1 
ATOM   1774  C C   . VAL B 2 133 ? -2.242   -85.391  4.995   1.00 103.16 ? 135 VAL B C   1 
ATOM   1775  O O   . VAL B 2 133 ? -1.999   -86.238  5.858   1.00 103.40 ? 135 VAL B O   1 
ATOM   1776  C CB  . VAL B 2 133 ? -0.535   -85.108  3.143   1.00 101.72 ? 135 VAL B CB  1 
ATOM   1777  C CG1 . VAL B 2 133 ? 0.064    -84.017  2.275   1.00 101.76 ? 135 VAL B CG1 1 
ATOM   1778  C CG2 . VAL B 2 133 ? 0.477    -86.215  3.427   1.00 101.78 ? 135 VAL B CG2 1 
ATOM   1779  N N   . THR B 2 134 ? -3.464   -85.190  4.484   1.00 99.38  ? 136 THR B N   1 
ATOM   1780  C CA  . THR B 2 134 ? -4.643   -85.911  4.945   1.00 99.35  ? 136 THR B CA  1 
ATOM   1781  C C   . THR B 2 134 ? -5.533   -86.391  3.789   1.00 103.97 ? 136 THR B C   1 
ATOM   1782  O O   . THR B 2 134 ? -5.433   -85.877  2.677   1.00 103.65 ? 136 THR B O   1 
ATOM   1783  C CB  . THR B 2 134 ? -5.383   -85.047  5.973   1.00 107.40 ? 136 THR B CB  1 
ATOM   1784  O OG1 . THR B 2 134 ? -6.219   -85.869  6.787   1.00 108.48 ? 136 THR B OG1 1 
ATOM   1785  C CG2 . THR B 2 134 ? -6.158   -83.885  5.335   1.00 106.01 ? 136 THR B CG2 1 
ATOM   1786  N N   . ALA B 2 135 ? -6.404   -87.373  4.070   1.00 101.95 ? 137 ALA B N   1 
ATOM   1787  C CA  . ALA B 2 135 ? -7.345   -87.945  3.112   1.00 103.77 ? 137 ALA B CA  1 
ATOM   1788  C C   . ALA B 2 135 ? -8.525   -87.016  2.839   1.00 110.66 ? 137 ALA B C   1 
ATOM   1789  O O   . ALA B 2 135 ? -9.158   -87.136  1.790   1.00 111.81 ? 137 ALA B O   1 
ATOM   1790  C CB  . ALA B 2 135 ? -7.836   -89.290  3.608   1.00 105.66 ? 137 ALA B CB  1 
ATOM   1791  N N   . ALA B 2 136 ? -8.809   -86.077  3.765   1.00 108.70 ? 138 ALA B N   1 
ATOM   1792  C CA  . ALA B 2 136 ? -9.882   -85.084  3.628   1.00 110.53 ? 138 ALA B CA  1 
ATOM   1793  C C   . ALA B 2 136 ? -9.578   -84.131  2.479   1.00 116.92 ? 138 ALA B C   1 
ATOM   1794  O O   . ALA B 2 136 ? -10.479  -83.491  1.938   1.00 118.69 ? 138 ALA B O   1 
ATOM   1795  C CB  . ALA B 2 136 ? -10.025  -84.292  4.915   1.00 110.48 ? 138 ALA B CB  1 
ATOM   1796  N N   . CYS B 2 137 ? -8.305   -84.054  2.109   1.00 113.45 ? 139 CYS B N   1 
ATOM   1797  C CA  . CYS B 2 137 ? -7.836   -83.215  1.038   1.00 114.24 ? 139 CYS B CA  1 
ATOM   1798  C C   . CYS B 2 137 ? -7.179   -84.082  -0.053  1.00 118.47 ? 139 CYS B C   1 
ATOM   1799  O O   . CYS B 2 137 ? -5.956   -84.165  -0.104  1.00 117.01 ? 139 CYS B O   1 
ATOM   1800  C CB  . CYS B 2 137 ? -6.877   -82.174  1.596   1.00 114.01 ? 139 CYS B CB  1 
ATOM   1801  S SG  . CYS B 2 137 ? -6.859   -80.639  0.659   1.00 119.34 ? 139 CYS B SG  1 
ATOM   1802  N N   . PRO B 2 138 ? -7.957   -84.781  -0.914  1.00 116.94 ? 140 PRO B N   1 
ATOM   1803  C CA  . PRO B 2 138 ? -7.325   -85.651  -1.916  1.00 117.23 ? 140 PRO B CA  1 
ATOM   1804  C C   . PRO B 2 138 ? -6.962   -84.959  -3.225  1.00 120.55 ? 140 PRO B C   1 
ATOM   1805  O O   . PRO B 2 138 ? -7.440   -83.855  -3.507  1.00 121.19 ? 140 PRO B O   1 
ATOM   1806  C CB  . PRO B 2 138 ? -8.353   -86.772  -2.112  1.00 120.86 ? 140 PRO B CB  1 
ATOM   1807  C CG  . PRO B 2 138 ? -9.668   -86.211  -1.598  1.00 126.47 ? 140 PRO B CG  1 
ATOM   1808  C CD  . PRO B 2 138 ? -9.428   -84.850  -1.009  1.00 120.55 ? 140 PRO B CD  1 
ATOM   1809  N N   . HIS B 2 139 ? -6.102   -85.627  -4.015  1.00 115.00 ? 141 HIS B N   1 
ATOM   1810  C CA  . HIS B 2 139 ? -5.620   -85.208  -5.327  1.00 114.47 ? 141 HIS B CA  1 
ATOM   1811  C C   . HIS B 2 139 ? -5.043   -86.430  -6.012  1.00 115.40 ? 141 HIS B C   1 
ATOM   1812  O O   . HIS B 2 139 ? -4.001   -86.937  -5.593  1.00 112.95 ? 141 HIS B O   1 
ATOM   1813  C CB  . HIS B 2 139 ? -4.601   -84.067  -5.199  1.00 114.30 ? 141 HIS B CB  1 
ATOM   1814  C CG  . HIS B 2 139 ? -3.812   -83.797  -6.428  1.00 119.47 ? 141 HIS B CG  1 
ATOM   1815  N ND1 . HIS B 2 139 ? -2.704   -84.542  -6.728  1.00 121.97 ? 141 HIS B ND1 1 
ATOM   1816  C CD2 . HIS B 2 139 ? -3.976   -82.846  -7.377  1.00 123.22 ? 141 HIS B CD2 1 
ATOM   1817  C CE1 . HIS B 2 139 ? -2.233   -84.048  -7.861  1.00 123.39 ? 141 HIS B CE1 1 
ATOM   1818  N NE2 . HIS B 2 139 ? -2.969   -83.025  -8.290  1.00 124.49 ? 141 HIS B NE2 1 
ATOM   1819  N N   . ALA B 2 140 ? -5.746   -86.917  -7.048  1.00 113.00 ? 142 ALA B N   1 
ATOM   1820  C CA  . ALA B 2 140 ? -5.413   -88.103  -7.843  1.00 113.97 ? 142 ALA B CA  1 
ATOM   1821  C C   . ALA B 2 140 ? -5.360   -89.373  -6.989  1.00 116.11 ? 142 ALA B C   1 
ATOM   1822  O O   . ALA B 2 140 ? -4.545   -90.264  -7.236  1.00 116.11 ? 142 ALA B O   1 
ATOM   1823  C CB  . ALA B 2 140 ? -4.113   -87.899  -8.624  1.00 115.14 ? 142 ALA B CB  1 
ATOM   1824  N N   . GLY B 2 141 ? -6.237   -89.434  -5.990  1.00 111.73 ? 143 GLY B N   1 
ATOM   1825  C CA  . GLY B 2 141 ? -6.336   -90.555  -5.059  1.00 111.23 ? 143 GLY B CA  1 
ATOM   1826  C C   . GLY B 2 141 ? -5.467   -90.407  -3.825  1.00 112.15 ? 143 GLY B C   1 
ATOM   1827  O O   . GLY B 2 141 ? -5.846   -90.865  -2.740  1.00 111.65 ? 143 GLY B O   1 
ATOM   1828  N N   . ALA B 2 142 ? -4.300   -89.747  -3.997  1.00 106.37 ? 144 ALA B N   1 
ATOM   1829  C CA  . ALA B 2 142 ? -3.290   -89.499  -2.971  1.00 103.84 ? 144 ALA B CA  1 
ATOM   1830  C C   . ALA B 2 142 ? -3.756   -88.556  -1.878  1.00 104.11 ? 144 ALA B C   1 
ATOM   1831  O O   . ALA B 2 142 ? -4.524   -87.632  -2.145  1.00 103.79 ? 144 ALA B O   1 
ATOM   1832  C CB  . ALA B 2 142 ? -2.031   -88.944  -3.617  1.00 104.76 ? 144 ALA B CB  1 
ATOM   1833  N N   . LYS B 2 143 ? -3.268   -88.777  -0.650  1.00 98.57  ? 145 LYS B N   1 
ATOM   1834  C CA  . LYS B 2 143 ? -3.547   -87.893  0.475   1.00 97.46  ? 145 LYS B CA  1 
ATOM   1835  C C   . LYS B 2 143 ? -2.737   -86.623  0.185   1.00 101.11 ? 145 LYS B C   1 
ATOM   1836  O O   . LYS B 2 143 ? -1.502   -86.670  0.136   1.00 101.00 ? 145 LYS B O   1 
ATOM   1837  C CB  . LYS B 2 143 ? -3.081   -88.522  1.807   1.00 99.99  ? 145 LYS B CB  1 
ATOM   1838  C CG  . LYS B 2 143 ? -4.086   -89.438  2.502   1.00 114.04 ? 145 LYS B CG  1 
ATOM   1839  C CD  . LYS B 2 143 ? -3.477   -90.104  3.751   1.00 121.34 ? 145 LYS B CD  1 
ATOM   1840  C CE  . LYS B 2 143 ? -3.804   -89.476  5.091   1.00 124.36 ? 145 LYS B CE  1 
ATOM   1841  N NZ  . LYS B 2 143 ? -5.091   -89.963  5.643   1.00 130.28 ? 145 LYS B NZ  1 
ATOM   1842  N N   . SER B 2 144 ? -3.429   -85.521  -0.112  1.00 97.23  ? 146 SER B N   1 
ATOM   1843  C CA  . SER B 2 144 ? -2.770   -84.258  -0.432  1.00 96.71  ? 146 SER B CA  1 
ATOM   1844  C C   . SER B 2 144 ? -3.081   -83.205  0.637   1.00 98.92  ? 146 SER B C   1 
ATOM   1845  O O   . SER B 2 144 ? -3.463   -83.559  1.760   1.00 98.64  ? 146 SER B O   1 
ATOM   1846  C CB  . SER B 2 144 ? -3.193   -83.783  -1.819  1.00 102.24 ? 146 SER B CB  1 
ATOM   1847  O OG  . SER B 2 144 ? -2.357   -82.746  -2.306  1.00 112.04 ? 146 SER B OG  1 
ATOM   1848  N N   . PHE B 2 145 ? -2.896   -81.918  0.295   1.00 93.94  ? 147 PHE B N   1 
ATOM   1849  C CA  . PHE B 2 145 ? -3.125   -80.769  1.164   1.00 92.16  ? 147 PHE B CA  1 
ATOM   1850  C C   . PHE B 2 145 ? -3.153   -79.496  0.306   1.00 94.03  ? 147 PHE B C   1 
ATOM   1851  O O   . PHE B 2 145 ? -2.990   -79.590  -0.911  1.00 93.57  ? 147 PHE B O   1 
ATOM   1852  C CB  . PHE B 2 145 ? -2.020   -80.714  2.244   1.00 93.37  ? 147 PHE B CB  1 
ATOM   1853  C CG  . PHE B 2 145 ? -2.361   -79.870  3.441   1.00 94.30  ? 147 PHE B CG  1 
ATOM   1854  C CD1 . PHE B 2 145 ? -3.439   -80.193  4.256   1.00 96.99  ? 147 PHE B CD1 1 
ATOM   1855  C CD2 . PHE B 2 145 ? -1.610   -78.746  3.751   1.00 96.64  ? 147 PHE B CD2 1 
ATOM   1856  C CE1 . PHE B 2 145 ? -3.771   -79.390  5.345   1.00 97.76  ? 147 PHE B CE1 1 
ATOM   1857  C CE2 . PHE B 2 145 ? -1.941   -77.947  4.842   1.00 99.23  ? 147 PHE B CE2 1 
ATOM   1858  C CZ  . PHE B 2 145 ? -3.020   -78.272  5.630   1.00 96.90  ? 147 PHE B CZ  1 
ATOM   1859  N N   . TYR B 2 146 ? -3.389   -78.322  0.923   1.00 89.88  ? 148 TYR B N   1 
ATOM   1860  C CA  . TYR B 2 146 ? -3.401   -77.028  0.234   1.00 90.25  ? 148 TYR B CA  1 
ATOM   1861  C C   . TYR B 2 146 ? -1.968   -76.668  -0.183  1.00 95.86  ? 148 TYR B C   1 
ATOM   1862  O O   . TYR B 2 146 ? -1.055   -76.702  0.650   1.00 94.88  ? 148 TYR B O   1 
ATOM   1863  C CB  . TYR B 2 146 ? -3.966   -75.915  1.126   1.00 89.70  ? 148 TYR B CB  1 
ATOM   1864  C CG  . TYR B 2 146 ? -5.314   -76.193  1.744   1.00 88.45  ? 148 TYR B CG  1 
ATOM   1865  C CD1 . TYR B 2 146 ? -6.488   -75.898  1.061   1.00 90.95  ? 148 TYR B CD1 1 
ATOM   1866  C CD2 . TYR B 2 146 ? -5.419   -76.659  3.050   1.00 87.59  ? 148 TYR B CD2 1 
ATOM   1867  C CE1 . TYR B 2 146 ? -7.735   -76.079  1.654   1.00 90.75  ? 148 TYR B CE1 1 
ATOM   1868  C CE2 . TYR B 2 146 ? -6.660   -76.853  3.650   1.00 88.30  ? 148 TYR B CE2 1 
ATOM   1869  C CZ  . TYR B 2 146 ? -7.816   -76.555  2.949   1.00 94.74  ? 148 TYR B CZ  1 
ATOM   1870  O OH  . TYR B 2 146 ? -9.044   -76.773  3.518   1.00 94.44  ? 148 TYR B OH  1 
ATOM   1871  N N   . LYS B 2 147 ? -1.774   -76.345  -1.472  1.00 94.37  ? 149 LYS B N   1 
ATOM   1872  C CA  . LYS B 2 147 ? -0.456   -76.041  -2.027  1.00 95.65  ? 149 LYS B CA  1 
ATOM   1873  C C   . LYS B 2 147 ? 0.214    -74.819  -1.416  1.00 101.63 ? 149 LYS B C   1 
ATOM   1874  O O   . LYS B 2 147 ? 1.432    -74.826  -1.230  1.00 102.80 ? 149 LYS B O   1 
ATOM   1875  C CB  . LYS B 2 147 ? -0.518   -75.912  -3.555  1.00 99.45  ? 149 LYS B CB  1 
ATOM   1876  C CG  . LYS B 2 147 ? 0.615    -76.648  -4.270  1.00 113.42 ? 149 LYS B CG  1 
ATOM   1877  C CD  . LYS B 2 147 ? 1.816    -75.750  -4.596  1.00 120.72 ? 149 LYS B CD  1 
ATOM   1878  C CE  . LYS B 2 147 ? 2.957    -76.548  -5.190  1.00 121.77 ? 149 LYS B CE  1 
ATOM   1879  N NZ  . LYS B 2 147 ? 4.080    -75.680  -5.631  1.00 123.85 ? 149 LYS B NZ  1 
ATOM   1880  N N   . ASN B 2 148 ? -0.575   -73.794  -1.079  1.00 97.99  ? 150 ASN B N   1 
ATOM   1881  C CA  . ASN B 2 148 ? -0.055   -72.534  -0.563  1.00 98.66  ? 150 ASN B CA  1 
ATOM   1882  C C   . ASN B 2 148 ? 0.315    -72.521  0.944   1.00 102.93 ? 150 ASN B C   1 
ATOM   1883  O O   . ASN B 2 148 ? 0.945    -71.551  1.375   1.00 103.77 ? 150 ASN B O   1 
ATOM   1884  C CB  . ASN B 2 148 ? -1.014   -71.398  -0.901  1.00 97.75  ? 150 ASN B CB  1 
ATOM   1885  C CG  . ASN B 2 148 ? -1.371   -71.329  -2.364  1.00 117.69 ? 150 ASN B CG  1 
ATOM   1886  O OD1 . ASN B 2 148 ? -0.588   -71.702  -3.252  1.00 109.68 ? 150 ASN B OD1 1 
ATOM   1887  N ND2 . ASN B 2 148 ? -2.576   -70.870  -2.648  1.00 112.03 ? 150 ASN B ND2 1 
ATOM   1888  N N   . LEU B 2 149 ? -0.039   -73.567  1.733   1.00 98.24  ? 151 LEU B N   1 
ATOM   1889  C CA  . LEU B 2 149 ? 0.332    -73.607  3.160   1.00 97.64  ? 151 LEU B CA  1 
ATOM   1890  C C   . LEU B 2 149 ? 0.718    -75.016  3.642   1.00 101.59 ? 151 LEU B C   1 
ATOM   1891  O O   . LEU B 2 149 ? 0.089    -75.995  3.253   1.00 101.35 ? 151 LEU B O   1 
ATOM   1892  C CB  . LEU B 2 149 ? -0.707   -72.951  4.103   1.00 96.95  ? 151 LEU B CB  1 
ATOM   1893  C CG  . LEU B 2 149 ? -2.192   -73.043  3.772   1.00 100.98 ? 151 LEU B CG  1 
ATOM   1894  C CD1 . LEU B 2 149 ? -2.770   -74.347  4.244   1.00 100.10 ? 151 LEU B CD1 1 
ATOM   1895  C CD2 . LEU B 2 149 ? -2.957   -71.928  4.453   1.00 102.77 ? 151 LEU B CD2 1 
ATOM   1896  N N   . ILE B 2 150 ? 1.776    -75.101  4.471   1.00 98.22  ? 152 ILE B N   1 
ATOM   1897  C CA  . ILE B 2 150 ? 2.336    -76.342  5.017   1.00 98.11  ? 152 ILE B CA  1 
ATOM   1898  C C   . ILE B 2 150 ? 1.752    -76.673  6.405   1.00 103.81 ? 152 ILE B C   1 
ATOM   1899  O O   . ILE B 2 150 ? 1.766    -75.820  7.296   1.00 104.78 ? 152 ILE B O   1 
ATOM   1900  C CB  . ILE B 2 150 ? 3.894    -76.259  5.090   1.00 102.79 ? 152 ILE B CB  1 
ATOM   1901  C CG1 . ILE B 2 150 ? 4.535    -75.814  3.769   1.00 104.85 ? 152 ILE B CG1 1 
ATOM   1902  C CG2 . ILE B 2 150 ? 4.513    -77.560  5.583   1.00 103.49 ? 152 ILE B CG2 1 
ATOM   1903  C CD1 . ILE B 2 150 ? 5.736    -74.853  3.950   1.00 112.17 ? 152 ILE B CD1 1 
ATOM   1904  N N   . TRP B 2 151 ? 1.298    -77.932  6.599   1.00 99.47  ? 153 TRP B N   1 
ATOM   1905  C CA  . TRP B 2 151 ? 0.805    -78.422  7.887   1.00 97.99  ? 153 TRP B CA  1 
ATOM   1906  C C   . TRP B 2 151 ? 2.036    -78.900  8.664   1.00 102.44 ? 153 TRP B C   1 
ATOM   1907  O O   . TRP B 2 151 ? 2.569    -79.983  8.386   1.00 102.28 ? 153 TRP B O   1 
ATOM   1908  C CB  . TRP B 2 151 ? -0.200   -79.567  7.677   1.00 95.72  ? 153 TRP B CB  1 
ATOM   1909  C CG  . TRP B 2 151 ? -0.905   -80.085  8.906   1.00 96.21  ? 153 TRP B CG  1 
ATOM   1910  C CD1 . TRP B 2 151 ? -0.691   -79.722  10.206  1.00 99.48  ? 153 TRP B CD1 1 
ATOM   1911  C CD2 . TRP B 2 151 ? -1.945   -81.073  8.933   1.00 95.58  ? 153 TRP B CD2 1 
ATOM   1912  N NE1 . TRP B 2 151 ? -1.531   -80.423  11.038  1.00 98.63  ? 153 TRP B NE1 1 
ATOM   1913  C CE2 . TRP B 2 151 ? -2.318   -81.254  10.282  1.00 99.74  ? 153 TRP B CE2 1 
ATOM   1914  C CE3 . TRP B 2 151 ? -2.610   -81.817  7.942   1.00 96.66  ? 153 TRP B CE3 1 
ATOM   1915  C CZ2 . TRP B 2 151 ? -3.324   -82.149  10.666  1.00 99.40  ? 153 TRP B CZ2 1 
ATOM   1916  C CZ3 . TRP B 2 151 ? -3.602   -82.706  8.323   1.00 98.34  ? 153 TRP B CZ3 1 
ATOM   1917  C CH2 . TRP B 2 151 ? -3.953   -82.865  9.669   1.00 99.21  ? 153 TRP B CH2 1 
ATOM   1918  N N   . LEU B 2 152 ? 2.519    -78.063  9.601   1.00 99.39  ? 154 LEU B N   1 
ATOM   1919  C CA  . LEU B 2 152 ? 3.710    -78.382  10.384  1.00 100.16 ? 154 LEU B CA  1 
ATOM   1920  C C   . LEU B 2 152 ? 3.440    -79.250  11.608  1.00 102.89 ? 154 LEU B C   1 
ATOM   1921  O O   . LEU B 2 152 ? 2.683    -78.859  12.505  1.00 101.71 ? 154 LEU B O   1 
ATOM   1922  C CB  . LEU B 2 152 ? 4.496    -77.125  10.779  1.00 101.71 ? 154 LEU B CB  1 
ATOM   1923  C CG  . LEU B 2 152 ? 5.515    -76.596  9.779   1.00 108.03 ? 154 LEU B CG  1 
ATOM   1924  C CD1 . LEU B 2 152 ? 6.440    -75.642  10.454  1.00 110.44 ? 154 LEU B CD1 1 
ATOM   1925  C CD2 . LEU B 2 152 ? 6.359    -77.707  9.176   1.00 112.95 ? 154 LEU B CD2 1 
ATOM   1926  N N   . VAL B 2 153 ? 4.104    -80.420  11.639  1.00 99.41  ? 155 VAL B N   1 
ATOM   1927  C CA  . VAL B 2 153 ? 4.040    -81.412  12.715  1.00 99.24  ? 155 VAL B CA  1 
ATOM   1928  C C   . VAL B 2 153 ? 5.446    -81.665  13.323  1.00 106.30 ? 155 VAL B C   1 
ATOM   1929  O O   . VAL B 2 153 ? 6.450    -81.278  12.717  1.00 106.84 ? 155 VAL B O   1 
ATOM   1930  C CB  . VAL B 2 153 ? 3.308    -82.701  12.271  1.00 101.63 ? 155 VAL B CB  1 
ATOM   1931  C CG1 . VAL B 2 153 ? 1.806    -82.467  12.188  1.00 99.66  ? 155 VAL B CG1 1 
ATOM   1932  C CG2 . VAL B 2 153 ? 3.842    -83.220  10.939  1.00 101.67 ? 155 VAL B CG2 1 
ATOM   1933  N N   . LYS B 2 154 ? 5.508    -82.269  14.533  1.00 105.21 ? 156 LYS B N   1 
ATOM   1934  C CA  . LYS B 2 154 ? 6.751    -82.529  15.284  1.00 108.55 ? 156 LYS B CA  1 
ATOM   1935  C C   . LYS B 2 154 ? 7.771    -83.418  14.551  1.00 116.81 ? 156 LYS B C   1 
ATOM   1936  O O   . LYS B 2 154 ? 7.409    -84.448  13.974  1.00 115.66 ? 156 LYS B O   1 
ATOM   1937  C CB  . LYS B 2 154 ? 6.461    -83.085  16.699  1.00 111.14 ? 156 LYS B CB  1 
ATOM   1938  C CG  . LYS B 2 154 ? 5.789    -84.458  16.753  1.00 112.95 ? 156 LYS B CG  1 
ATOM   1939  C CD  . LYS B 2 154 ? 5.586    -84.930  18.176  1.00 115.39 ? 156 LYS B CD  1 
ATOM   1940  C CE  . LYS B 2 154 ? 5.257    -86.397  18.227  1.00 119.33 ? 156 LYS B CE  1 
ATOM   1941  N NZ  . LYS B 2 154 ? 4.903    -86.834  19.598  1.00 126.46 ? 156 LYS B NZ  1 
ATOM   1942  N N   . LYS B 2 155 ? 9.054    -83.008  14.594  1.00 118.04 ? 157 LYS B N   1 
ATOM   1943  C CA  . LYS B 2 155 ? 10.169   -83.723  13.970  1.00 120.94 ? 157 LYS B CA  1 
ATOM   1944  C C   . LYS B 2 155 ? 10.694   -84.789  14.945  1.00 128.87 ? 157 LYS B C   1 
ATOM   1945  O O   . LYS B 2 155 ? 11.652   -84.541  15.686  1.00 131.67 ? 157 LYS B O   1 
ATOM   1946  C CB  . LYS B 2 155 ? 11.278   -82.732  13.553  1.00 125.92 ? 157 LYS B CB  1 
ATOM   1947  C CG  . LYS B 2 155 ? 12.294   -83.283  12.550  1.00 143.11 ? 157 LYS B CG  1 
ATOM   1948  C CD  . LYS B 2 155 ? 13.415   -82.275  12.292  1.00 155.90 ? 157 LYS B CD  1 
ATOM   1949  C CE  . LYS B 2 155 ? 14.523   -82.830  11.427  1.00 168.26 ? 157 LYS B CE  1 
ATOM   1950  N NZ  . LYS B 2 155 ? 15.650   -81.866  11.296  1.00 181.57 ? 157 LYS B NZ  1 
ATOM   1951  N N   . GLY B 2 156 ? 10.025   -85.944  14.950  1.00 124.94 ? 158 GLY B N   1 
ATOM   1952  C CA  . GLY B 2 156 ? 10.353   -87.086  15.799  1.00 126.97 ? 158 GLY B CA  1 
ATOM   1953  C C   . GLY B 2 156 ? 10.377   -86.772  17.282  1.00 132.74 ? 158 GLY B C   1 
ATOM   1954  O O   . GLY B 2 156 ? 11.457   -86.644  17.861  1.00 135.01 ? 158 GLY B O   1 
ATOM   1955  N N   . ASN B 2 157 ? 9.178    -86.648  17.896  1.00 129.10 ? 159 ASN B N   1 
ATOM   1956  C CA  . ASN B 2 157 ? 8.901    -86.339  19.310  1.00 131.19 ? 159 ASN B CA  1 
ATOM   1957  C C   . ASN B 2 157 ? 9.723    -85.127  19.861  1.00 139.11 ? 159 ASN B C   1 
ATOM   1958  O O   . ASN B 2 157 ? 10.296   -85.197  20.956  1.00 142.05 ? 159 ASN B O   1 
ATOM   1959  C CB  . ASN B 2 157 ? 9.005    -87.590  20.226  1.00 136.18 ? 159 ASN B CB  1 
ATOM   1960  C CG  . ASN B 2 157 ? 10.315   -88.344  20.214  1.00 172.11 ? 159 ASN B CG  1 
ATOM   1961  O OD1 . ASN B 2 157 ? 10.419   -89.431  19.634  1.00 166.28 ? 159 ASN B OD1 1 
ATOM   1962  N ND2 . ASN B 2 157 ? 11.329   -87.812  20.894  1.00 170.11 ? 159 ASN B ND2 1 
ATOM   1963  N N   . SER B 2 158 ? 9.730    -84.002  19.095  1.00 134.64 ? 160 SER B N   1 
ATOM   1964  C CA  . SER B 2 158 ? 10.411   -82.740  19.430  1.00 136.14 ? 160 SER B CA  1 
ATOM   1965  C C   . SER B 2 158 ? 9.946    -81.580  18.535  1.00 134.32 ? 160 SER B C   1 
ATOM   1966  O O   . SER B 2 158 ? 10.428   -81.422  17.409  1.00 133.15 ? 160 SER B O   1 
ATOM   1967  C CB  . SER B 2 158 ? 11.932   -82.895  19.365  1.00 145.92 ? 160 SER B CB  1 
ATOM   1968  O OG  . SER B 2 158 ? 12.599   -81.753  19.880  1.00 161.01 ? 160 SER B OG  1 
ATOM   1969  N N   . TYR B 2 159 ? 8.995    -80.782  19.048  1.00 121.09 ? 161 TYR B N   1 
ATOM   1970  C CA  . TYR B 2 159 ? 8.437    -79.598  18.381  1.00 117.38 ? 161 TYR B CA  1 
ATOM   1971  C C   . TYR B 2 159 ? 8.924    -78.333  19.125  1.00 121.90 ? 161 TYR B C   1 
ATOM   1972  O O   . TYR B 2 159 ? 8.247    -77.869  20.048  1.00 121.58 ? 161 TYR B O   1 
ATOM   1973  C CB  . TYR B 2 159 ? 6.893    -79.646  18.382  1.00 115.89 ? 161 TYR B CB  1 
ATOM   1974  C CG  . TYR B 2 159 ? 6.195    -78.685  17.437  1.00 113.68 ? 161 TYR B CG  1 
ATOM   1975  C CD1 . TYR B 2 159 ? 6.341    -77.305  17.574  1.00 114.36 ? 161 TYR B CD1 1 
ATOM   1976  C CD2 . TYR B 2 159 ? 5.313    -79.149  16.472  1.00 113.00 ? 161 TYR B CD2 1 
ATOM   1977  C CE1 . TYR B 2 159 ? 5.680    -76.417  16.720  1.00 112.32 ? 161 TYR B CE1 1 
ATOM   1978  C CE2 . TYR B 2 159 ? 4.652    -78.273  15.612  1.00 111.49 ? 161 TYR B CE2 1 
ATOM   1979  C CZ  . TYR B 2 159 ? 4.829    -76.907  15.744  1.00 114.17 ? 161 TYR B CZ  1 
ATOM   1980  O OH  . TYR B 2 159 ? 4.139    -76.051  14.918  1.00 108.16 ? 161 TYR B OH  1 
ATOM   1981  N N   . PRO B 2 160 ? 10.081   -77.748  18.754  1.00 119.35 ? 162 PRO B N   1 
ATOM   1982  C CA  . PRO B 2 160 ? 10.534   -76.534  19.455  1.00 119.54 ? 162 PRO B CA  1 
ATOM   1983  C C   . PRO B 2 160 ? 9.796    -75.288  18.967  1.00 120.10 ? 162 PRO B C   1 
ATOM   1984  O O   . PRO B 2 160 ? 9.201    -75.316  17.890  1.00 117.60 ? 162 PRO B O   1 
ATOM   1985  C CB  . PRO B 2 160 ? 12.038   -76.474  19.141  1.00 123.60 ? 162 PRO B CB  1 
ATOM   1986  C CG  . PRO B 2 160 ? 12.334   -77.678  18.255  1.00 129.02 ? 162 PRO B CG  1 
ATOM   1987  C CD  . PRO B 2 160 ? 11.029   -78.134  17.695  1.00 122.06 ? 162 PRO B CD  1 
ATOM   1988  N N   . LYS B 2 161 ? 9.829    -74.200  19.760  1.00 116.86 ? 163 LYS B N   1 
ATOM   1989  C CA  . LYS B 2 161 ? 9.175    -72.934  19.421  1.00 115.13 ? 163 LYS B CA  1 
ATOM   1990  C C   . LYS B 2 161 ? 9.749    -72.350  18.121  1.00 118.87 ? 163 LYS B C   1 
ATOM   1991  O O   . LYS B 2 161 ? 10.909   -71.932  18.093  1.00 120.04 ? 163 LYS B O   1 
ATOM   1992  C CB  . LYS B 2 161 ? 9.303    -71.924  20.579  1.00 118.60 ? 163 LYS B CB  1 
ATOM   1993  C CG  . LYS B 2 161 ? 8.518    -70.624  20.375  1.00 127.70 ? 163 LYS B CG  1 
ATOM   1994  C CD  . LYS B 2 161 ? 9.049    -69.486  21.247  1.00 137.58 ? 163 LYS B CD  1 
ATOM   1995  C CE  . LYS B 2 161 ? 10.065   -68.615  20.534  1.00 145.05 ? 163 LYS B CE  1 
ATOM   1996  N NZ  . LYS B 2 161 ? 10.727   -67.656  21.459  1.00 152.78 ? 163 LYS B NZ  1 
ATOM   1997  N N   . LEU B 2 162 ? 8.940    -72.364  17.041  1.00 113.75 ? 164 LEU B N   1 
ATOM   1998  C CA  . LEU B 2 162 ? 9.316    -71.800  15.736  1.00 112.88 ? 164 LEU B CA  1 
ATOM   1999  C C   . LEU B 2 162 ? 8.993    -70.310  15.710  1.00 114.85 ? 164 LEU B C   1 
ATOM   2000  O O   . LEU B 2 162 ? 8.014    -69.890  16.334  1.00 114.46 ? 164 LEU B O   1 
ATOM   2001  C CB  . LEU B 2 162 ? 8.639    -72.530  14.551  1.00 111.44 ? 164 LEU B CB  1 
ATOM   2002  C CG  . LEU B 2 162 ? 7.104    -72.549  14.474  1.00 115.08 ? 164 LEU B CG  1 
ATOM   2003  C CD1 . LEU B 2 162 ? 6.597    -71.655  13.359  1.00 114.26 ? 164 LEU B CD1 1 
ATOM   2004  C CD2 . LEU B 2 162 ? 6.603    -73.940  14.234  1.00 117.67 ? 164 LEU B CD2 1 
ATOM   2005  N N   . SER B 2 163 ? 9.813    -69.510  15.010  1.00 110.50 ? 165 SER B N   1 
ATOM   2006  C CA  . SER B 2 163 ? 9.583    -68.068  14.930  1.00 110.66 ? 165 SER B CA  1 
ATOM   2007  C C   . SER B 2 163 ? 10.110   -67.462  13.628  1.00 113.21 ? 165 SER B C   1 
ATOM   2008  O O   . SER B 2 163 ? 11.036   -66.646  13.643  1.00 115.16 ? 165 SER B O   1 
ATOM   2009  C CB  . SER B 2 163 ? 10.127   -67.348  16.168  1.00 117.33 ? 165 SER B CB  1 
ATOM   2010  O OG  . SER B 2 163 ? 9.467    -66.111  16.402  1.00 127.69 ? 165 SER B OG  1 
ATOM   2011  N N   . LYS B 2 164 ? 9.524    -67.870  12.494  1.00 106.56 ? 166 LYS B N   1 
ATOM   2012  C CA  . LYS B 2 164 ? 9.924    -67.313  11.207  1.00 105.94 ? 166 LYS B CA  1 
ATOM   2013  C C   . LYS B 2 164 ? 9.231    -65.956  10.997  1.00 110.50 ? 166 LYS B C   1 
ATOM   2014  O O   . LYS B 2 164 ? 8.122    -65.732  11.501  1.00 109.68 ? 166 LYS B O   1 
ATOM   2015  C CB  . LYS B 2 164 ? 9.671    -68.299  10.057  1.00 105.95 ? 166 LYS B CB  1 
ATOM   2016  C CG  . LYS B 2 164 ? 10.852   -68.468  9.106   1.00 118.54 ? 166 LYS B CG  1 
ATOM   2017  C CD  . LYS B 2 164 ? 11.989   -69.313  9.693   1.00 133.00 ? 166 LYS B CD  1 
ATOM   2018  C CE  . LYS B 2 164 ? 13.293   -69.105  8.950   1.00 147.87 ? 166 LYS B CE  1 
ATOM   2019  N NZ  . LYS B 2 164 ? 14.459   -69.699  9.665   1.00 157.09 ? 166 LYS B NZ  1 
ATOM   2020  N N   . SER B 2 165 ? 9.926    -65.027  10.325  1.00 108.27 ? 167 SER B N   1 
ATOM   2021  C CA  . SER B 2 165 ? 9.432    -63.674  10.081  1.00 109.02 ? 167 SER B CA  1 
ATOM   2022  C C   . SER B 2 165 ? 9.714    -63.207  8.652   1.00 111.92 ? 167 SER B C   1 
ATOM   2023  O O   . SER B 2 165 ? 10.856   -63.298  8.185   1.00 112.52 ? 167 SER B O   1 
ATOM   2024  C CB  . SER B 2 165 ? 10.047   -62.698  11.080  1.00 115.50 ? 167 SER B CB  1 
ATOM   2025  O OG  . SER B 2 165 ? 9.858    -63.119  12.420  1.00 124.73 ? 167 SER B OG  1 
ATOM   2026  N N   . TYR B 2 166 ? 8.675    -62.705  7.962   1.00 106.93 ? 168 TYR B N   1 
ATOM   2027  C CA  . TYR B 2 166 ? 8.815    -62.190  6.600   1.00 106.92 ? 168 TYR B CA  1 
ATOM   2028  C C   . TYR B 2 166 ? 8.756    -60.673  6.590   1.00 114.06 ? 168 TYR B C   1 
ATOM   2029  O O   . TYR B 2 166 ? 7.855    -60.088  7.186   1.00 115.46 ? 168 TYR B O   1 
ATOM   2030  C CB  . TYR B 2 166 ? 7.759    -62.777  5.642   1.00 105.45 ? 168 TYR B CB  1 
ATOM   2031  C CG  . TYR B 2 166 ? 7.799    -62.161  4.255   1.00 107.39 ? 168 TYR B CG  1 
ATOM   2032  C CD1 . TYR B 2 166 ? 8.783    -62.519  3.339   1.00 109.43 ? 168 TYR B CD1 1 
ATOM   2033  C CD2 . TYR B 2 166 ? 6.866    -61.203  3.869   1.00 108.98 ? 168 TYR B CD2 1 
ATOM   2034  C CE1 . TYR B 2 166 ? 8.838    -61.940  2.071   1.00 111.37 ? 168 TYR B CE1 1 
ATOM   2035  C CE2 . TYR B 2 166 ? 6.902    -60.628  2.599   1.00 110.68 ? 168 TYR B CE2 1 
ATOM   2036  C CZ  . TYR B 2 166 ? 7.895    -60.995  1.705   1.00 117.92 ? 168 TYR B CZ  1 
ATOM   2037  O OH  . TYR B 2 166 ? 7.949    -60.431  0.453   1.00 119.67 ? 168 TYR B OH  1 
ATOM   2038  N N   . ILE B 2 167 ? 9.685    -60.047  5.860   1.00 110.71 ? 169 ILE B N   1 
ATOM   2039  C CA  . ILE B 2 167 ? 9.770    -58.600  5.715   1.00 112.92 ? 169 ILE B CA  1 
ATOM   2040  C C   . ILE B 2 167 ? 9.357    -58.291  4.287   1.00 115.89 ? 169 ILE B C   1 
ATOM   2041  O O   . ILE B 2 167 ? 9.936    -58.848  3.355   1.00 113.67 ? 169 ILE B O   1 
ATOM   2042  C CB  . ILE B 2 167 ? 11.193   -58.091  6.063   1.00 118.55 ? 169 ILE B CB  1 
ATOM   2043  C CG1 . ILE B 2 167 ? 11.653   -58.592  7.463   1.00 119.38 ? 169 ILE B CG1 1 
ATOM   2044  C CG2 . ILE B 2 167 ? 11.274   -56.561  5.979   1.00 122.36 ? 169 ILE B CG2 1 
ATOM   2045  C CD1 . ILE B 2 167 ? 12.459   -59.972  7.505   1.00 125.53 ? 169 ILE B CD1 1 
ATOM   2046  N N   . ASN B 2 168 ? 8.328    -57.445  4.115   1.00 114.44 ? 170 ASN B N   1 
ATOM   2047  C CA  . ASN B 2 168 ? 7.792    -57.097  2.798   1.00 114.82 ? 170 ASN B CA  1 
ATOM   2048  C C   . ASN B 2 168 ? 8.739    -56.243  1.956   1.00 123.73 ? 170 ASN B C   1 
ATOM   2049  O O   . ASN B 2 168 ? 8.894    -55.046  2.198   1.00 127.23 ? 170 ASN B O   1 
ATOM   2050  C CB  . ASN B 2 168 ? 6.410    -56.452  2.901   1.00 114.18 ? 170 ASN B CB  1 
ATOM   2051  C CG  . ASN B 2 168 ? 5.630    -56.451  1.607   1.00 130.47 ? 170 ASN B CG  1 
ATOM   2052  O OD1 . ASN B 2 168 ? 6.130    -56.790  0.527   1.00 118.71 ? 170 ASN B OD1 1 
ATOM   2053  N ND2 . ASN B 2 168 ? 4.373    -56.071  1.690   1.00 126.47 ? 170 ASN B ND2 1 
ATOM   2054  N N   . ASP B 2 169 ? 9.341    -56.874  0.938   1.00 120.58 ? 171 ASP B N   1 
ATOM   2055  C CA  . ASP B 2 169 ? 10.272   -56.239  0.002   1.00 123.65 ? 171 ASP B CA  1 
ATOM   2056  C C   . ASP B 2 169 ? 9.636    -56.040  -1.388  1.00 128.54 ? 171 ASP B C   1 
ATOM   2057  O O   . ASP B 2 169 ? 10.183   -55.299  -2.211  1.00 130.39 ? 171 ASP B O   1 
ATOM   2058  C CB  . ASP B 2 169 ? 11.570   -57.068  -0.105  1.00 124.62 ? 171 ASP B CB  1 
ATOM   2059  C CG  . ASP B 2 169 ? 11.376   -58.476  -0.647  1.00 132.65 ? 171 ASP B CG  1 
ATOM   2060  O OD1 . ASP B 2 169 ? 11.804   -58.735  -1.795  1.00 134.29 ? 171 ASP B OD1 1 
ATOM   2061  O OD2 . ASP B 2 169 ? 10.788   -59.314  0.071   1.00 134.26 ? 171 ASP B OD2 1 
ATOM   2062  N N   . LYS B 2 170 ? 8.475    -56.694  -1.629  1.00 123.23 ? 172 LYS B N   1 
ATOM   2063  C CA  . LYS B 2 170 ? 7.726    -56.689  -2.894  1.00 122.89 ? 172 LYS B CA  1 
ATOM   2064  C C   . LYS B 2 170 ? 7.184    -55.313  -3.325  1.00 133.08 ? 172 LYS B C   1 
ATOM   2065  O O   . LYS B 2 170 ? 6.904    -55.123  -4.513  1.00 133.87 ? 172 LYS B O   1 
ATOM   2066  C CB  . LYS B 2 170 ? 6.586    -57.733  -2.869  1.00 120.81 ? 172 LYS B CB  1 
ATOM   2067  C CG  . LYS B 2 170 ? 7.022    -59.165  -2.542  1.00 121.95 ? 172 LYS B CG  1 
ATOM   2068  C CD  . LYS B 2 170 ? 7.870    -59.827  -3.632  1.00 126.92 ? 172 LYS B CD  1 
ATOM   2069  C CE  . LYS B 2 170 ? 8.658    -60.996  -3.091  1.00 129.33 ? 172 LYS B CE  1 
ATOM   2070  N NZ  . LYS B 2 170 ? 9.525    -61.607  -4.132  1.00 136.66 ? 172 LYS B NZ  1 
ATOM   2071  N N   . GLY B 2 171 ? 7.023    -54.386  -2.375  1.00 133.30 ? 173 GLY B N   1 
ATOM   2072  C CA  . GLY B 2 171 ? 6.504    -53.045  -2.640  1.00 137.83 ? 173 GLY B CA  1 
ATOM   2073  C C   . GLY B 2 171 ? 4.989    -52.998  -2.741  1.00 142.26 ? 173 GLY B C   1 
ATOM   2074  O O   . GLY B 2 171 ? 4.385    -51.930  -2.604  1.00 146.66 ? 173 GLY B O   1 
ATOM   2075  N N   . LYS B 2 172 ? 4.376    -54.170  -2.997  1.00 133.80 ? 174 LYS B N   1 
ATOM   2076  C CA  . LYS B 2 172 ? 2.939    -54.388  -3.137  1.00 132.43 ? 174 LYS B CA  1 
ATOM   2077  C C   . LYS B 2 172 ? 2.376    -54.926  -1.815  1.00 133.71 ? 174 LYS B C   1 
ATOM   2078  O O   . LYS B 2 172 ? 3.149    -55.302  -0.930  1.00 131.88 ? 174 LYS B O   1 
ATOM   2079  C CB  . LYS B 2 172 ? 2.674    -55.385  -4.289  1.00 131.17 ? 174 LYS B CB  1 
ATOM   2080  C CG  . LYS B 2 172 ? 3.047    -54.852  -5.671  1.00 142.02 ? 174 LYS B CG  1 
ATOM   2081  C CD  . LYS B 2 172 ? 2.784    -55.857  -6.782  1.00 145.91 ? 174 LYS B CD  1 
ATOM   2082  C CE  . LYS B 2 172 ? 3.003    -55.240  -8.144  1.00 154.94 ? 174 LYS B CE  1 
ATOM   2083  N NZ  . LYS B 2 172 ? 2.731    -56.202  -9.244  1.00 158.55 ? 174 LYS B NZ  1 
ATOM   2084  N N   . GLU B 2 173 ? 1.036    -54.945  -1.675  1.00 129.90 ? 175 GLU B N   1 
ATOM   2085  C CA  . GLU B 2 173 ? 0.359    -55.473  -0.486  1.00 127.75 ? 175 GLU B CA  1 
ATOM   2086  C C   . GLU B 2 173 ? 0.481    -56.993  -0.531  1.00 125.89 ? 175 GLU B C   1 
ATOM   2087  O O   . GLU B 2 173 ? 0.086    -57.614  -1.521  1.00 123.81 ? 175 GLU B O   1 
ATOM   2088  C CB  . GLU B 2 173 ? -1.118   -55.059  -0.456  1.00 131.34 ? 175 GLU B CB  1 
ATOM   2089  C CG  . GLU B 2 173 ? -1.337   -53.564  -0.345  1.00 147.50 ? 175 GLU B CG  1 
ATOM   2090  C CD  . GLU B 2 173 ? -2.783   -53.158  -0.527  1.00 175.03 ? 175 GLU B CD  1 
ATOM   2091  O OE1 . GLU B 2 173 ? -3.303   -53.296  -1.658  1.00 159.98 ? 175 GLU B OE1 1 
ATOM   2092  O OE2 . GLU B 2 173 ? -3.394   -52.690  0.460   1.00 180.39 ? 175 GLU B OE2 1 
ATOM   2093  N N   . VAL B 2 174 ? 1.071    -57.586  0.507   1.00 120.08 ? 176 VAL B N   1 
ATOM   2094  C CA  . VAL B 2 174 ? 1.286    -59.027  0.515   1.00 115.87 ? 176 VAL B CA  1 
ATOM   2095  C C   . VAL B 2 174 ? 0.212    -59.746  1.357   1.00 117.97 ? 176 VAL B C   1 
ATOM   2096  O O   . VAL B 2 174 ? 0.139    -59.545  2.570   1.00 118.94 ? 176 VAL B O   1 
ATOM   2097  C CB  . VAL B 2 174 ? 2.751    -59.380  0.909   1.00 118.79 ? 176 VAL B CB  1 
ATOM   2098  C CG1 . VAL B 2 174 ? 2.924    -60.870  1.208   1.00 115.16 ? 176 VAL B CG1 1 
ATOM   2099  C CG2 . VAL B 2 174 ? 3.723    -58.943  -0.187  1.00 119.49 ? 176 VAL B CG2 1 
ATOM   2100  N N   . LEU B 2 175 ? -0.630   -60.567  0.689   1.00 110.98 ? 177 LEU B N   1 
ATOM   2101  C CA  . LEU B 2 175 ? -1.671   -61.369  1.334   1.00 108.37 ? 177 LEU B CA  1 
ATOM   2102  C C   . LEU B 2 175 ? -1.030   -62.659  1.852   1.00 108.18 ? 177 LEU B C   1 
ATOM   2103  O O   . LEU B 2 175 ? -0.413   -63.395  1.081   1.00 105.99 ? 177 LEU B O   1 
ATOM   2104  C CB  . LEU B 2 175 ? -2.824   -61.675  0.356   1.00 107.85 ? 177 LEU B CB  1 
ATOM   2105  C CG  . LEU B 2 175 ? -3.797   -62.794  0.742   1.00 110.09 ? 177 LEU B CG  1 
ATOM   2106  C CD1 . LEU B 2 175 ? -4.595   -62.445  1.989   1.00 111.58 ? 177 LEU B CD1 1 
ATOM   2107  C CD2 . LEU B 2 175 ? -4.729   -63.113  -0.392  1.00 112.45 ? 177 LEU B CD2 1 
ATOM   2108  N N   . VAL B 2 176 ? -1.165   -62.913  3.158   1.00 103.78 ? 178 VAL B N   1 
ATOM   2109  C CA  . VAL B 2 176 ? -0.597   -64.090  3.819   1.00 100.92 ? 178 VAL B CA  1 
ATOM   2110  C C   . VAL B 2 176 ? -1.721   -64.898  4.462   1.00 103.46 ? 178 VAL B C   1 
ATOM   2111  O O   . VAL B 2 176 ? -2.483   -64.357  5.266   1.00 104.61 ? 178 VAL B O   1 
ATOM   2112  C CB  . VAL B 2 176 ? 0.492    -63.694  4.853   1.00 105.29 ? 178 VAL B CB  1 
ATOM   2113  C CG1 . VAL B 2 176 ? 1.018    -64.912  5.603   1.00 103.01 ? 178 VAL B CG1 1 
ATOM   2114  C CG2 . VAL B 2 176 ? 1.637    -62.938  4.191   1.00 106.06 ? 178 VAL B CG2 1 
ATOM   2115  N N   . LEU B 2 177 ? -1.821   -66.186  4.111   1.00 97.44  ? 179 LEU B N   1 
ATOM   2116  C CA  . LEU B 2 177 ? -2.839   -67.075  4.674   1.00 96.85  ? 179 LEU B CA  1 
ATOM   2117  C C   . LEU B 2 177 ? -2.169   -68.164  5.496   1.00 100.89 ? 179 LEU B C   1 
ATOM   2118  O O   . LEU B 2 177 ? -1.084   -68.631  5.133   1.00 100.51 ? 179 LEU B O   1 
ATOM   2119  C CB  . LEU B 2 177 ? -3.697   -67.719  3.579   1.00 95.93  ? 179 LEU B CB  1 
ATOM   2120  C CG  . LEU B 2 177 ? -4.596   -66.802  2.780   1.00 101.97 ? 179 LEU B CG  1 
ATOM   2121  C CD1 . LEU B 2 177 ? -3.975   -66.475  1.443   1.00 101.91 ? 179 LEU B CD1 1 
ATOM   2122  C CD2 . LEU B 2 177 ? -5.904   -67.458  2.524   1.00 104.39 ? 179 LEU B CD2 1 
ATOM   2123  N N   . TRP B 2 178 ? -2.816   -68.564  6.604   1.00 96.80  ? 180 TRP B N   1 
ATOM   2124  C CA  . TRP B 2 178 ? -2.327   -69.606  7.508   1.00 95.27  ? 180 TRP B CA  1 
ATOM   2125  C C   . TRP B 2 178 ? -3.492   -70.267  8.205   1.00 99.60  ? 180 TRP B C   1 
ATOM   2126  O O   . TRP B 2 178 ? -4.555   -69.658  8.343   1.00 101.69 ? 180 TRP B O   1 
ATOM   2127  C CB  . TRP B 2 178 ? -1.351   -69.027  8.551   1.00 94.48  ? 180 TRP B CB  1 
ATOM   2128  C CG  . TRP B 2 178 ? -1.983   -68.093  9.545   1.00 96.97  ? 180 TRP B CG  1 
ATOM   2129  C CD1 . TRP B 2 178 ? -2.487   -68.416  10.771  1.00 100.30 ? 180 TRP B CD1 1 
ATOM   2130  C CD2 . TRP B 2 178 ? -2.159   -66.678  9.399   1.00 98.42  ? 180 TRP B CD2 1 
ATOM   2131  N NE1 . TRP B 2 178 ? -2.980   -67.293  11.392  1.00 101.68 ? 180 TRP B NE1 1 
ATOM   2132  C CE2 . TRP B 2 178 ? -2.788   -66.210  10.573  1.00 103.87 ? 180 TRP B CE2 1 
ATOM   2133  C CE3 . TRP B 2 178 ? -1.854   -65.756  8.383   1.00 100.49 ? 180 TRP B CE3 1 
ATOM   2134  C CZ2 . TRP B 2 178 ? -3.116   -64.862  10.759  1.00 105.59 ? 180 TRP B CZ2 1 
ATOM   2135  C CZ3 . TRP B 2 178 ? -2.179   -64.422  8.569   1.00 104.32 ? 180 TRP B CZ3 1 
ATOM   2136  C CH2 . TRP B 2 178 ? -2.813   -63.988  9.740   1.00 106.62 ? 180 TRP B CH2 1 
ATOM   2137  N N   . GLY B 2 179 ? -3.269   -71.481  8.683   1.00 94.19  ? 181 GLY B N   1 
ATOM   2138  C CA  . GLY B 2 179 ? -4.286   -72.238  9.392   1.00 94.22  ? 181 GLY B CA  1 
ATOM   2139  C C   . GLY B 2 179 ? -3.932   -72.519  10.831  1.00 99.00  ? 181 GLY B C   1 
ATOM   2140  O O   . GLY B 2 179 ? -2.767   -72.409  11.219  1.00 98.41  ? 181 GLY B O   1 
ATOM   2141  N N   . ILE B 2 180 ? -4.951   -72.864  11.631  1.00 97.39  ? 182 ILE B N   1 
ATOM   2142  C CA  . ILE B 2 180 ? -4.826   -73.253  13.036  1.00 98.67  ? 182 ILE B CA  1 
ATOM   2143  C C   . ILE B 2 180 ? -5.579   -74.569  13.153  1.00 105.32 ? 182 ILE B C   1 
ATOM   2144  O O   . ILE B 2 180 ? -6.797   -74.595  12.973  1.00 106.45 ? 182 ILE B O   1 
ATOM   2145  C CB  . ILE B 2 180 ? -5.353   -72.175  14.033  1.00 103.29 ? 182 ILE B CB  1 
ATOM   2146  C CG1 . ILE B 2 180 ? -4.666   -70.789  13.850  1.00 104.60 ? 182 ILE B CG1 1 
ATOM   2147  C CG2 . ILE B 2 180 ? -5.277   -72.655  15.484  1.00 104.01 ? 182 ILE B CG2 1 
ATOM   2148  C CD1 . ILE B 2 180 ? -3.150   -70.688  14.038  1.00 114.34 ? 182 ILE B CD1 1 
ATOM   2149  N N   . HIS B 2 181 ? -4.849   -75.666  13.389  1.00 102.53 ? 183 HIS B N   1 
ATOM   2150  C CA  . HIS B 2 181 ? -5.418   -77.007  13.515  1.00 103.51 ? 183 HIS B CA  1 
ATOM   2151  C C   . HIS B 2 181 ? -5.923   -77.254  14.942  1.00 110.00 ? 183 HIS B C   1 
ATOM   2152  O O   . HIS B 2 181 ? -5.176   -77.053  15.900  1.00 110.85 ? 183 HIS B O   1 
ATOM   2153  C CB  . HIS B 2 181 ? -4.381   -78.071  13.096  1.00 103.64 ? 183 HIS B CB  1 
ATOM   2154  C CG  . HIS B 2 181 ? -4.865   -79.487  13.213  1.00 107.83 ? 183 HIS B CG  1 
ATOM   2155  N ND1 . HIS B 2 181 ? -4.390   -80.334  14.199  1.00 110.66 ? 183 HIS B ND1 1 
ATOM   2156  C CD2 . HIS B 2 181 ? -5.776   -80.155  12.468  1.00 109.30 ? 183 HIS B CD2 1 
ATOM   2157  C CE1 . HIS B 2 181 ? -5.017   -81.483  14.016  1.00 110.92 ? 183 HIS B CE1 1 
ATOM   2158  N NE2 . HIS B 2 181 ? -5.859   -81.424  12.987  1.00 110.55 ? 183 HIS B NE2 1 
ATOM   2159  N N   . HIS B 2 182 ? -7.186   -77.683  15.079  1.00 106.38 ? 184 HIS B N   1 
ATOM   2160  C CA  . HIS B 2 182 ? -7.794   -77.985  16.374  1.00 107.30 ? 184 HIS B CA  1 
ATOM   2161  C C   . HIS B 2 182 ? -8.017   -79.517  16.461  1.00 110.05 ? 184 HIS B C   1 
ATOM   2162  O O   . HIS B 2 182 ? -8.981   -80.034  15.885  1.00 109.96 ? 184 HIS B O   1 
ATOM   2163  C CB  . HIS B 2 182 ? -9.088   -77.165  16.593  1.00 109.37 ? 184 HIS B CB  1 
ATOM   2164  C CG  . HIS B 2 182 ? -8.903   -75.679  16.454  1.00 112.26 ? 184 HIS B CG  1 
ATOM   2165  N ND1 . HIS B 2 182 ? -8.730   -74.864  17.556  1.00 114.90 ? 184 HIS B ND1 1 
ATOM   2166  C CD2 . HIS B 2 182 ? -8.875   -74.910  15.341  1.00 112.94 ? 184 HIS B CD2 1 
ATOM   2167  C CE1 . HIS B 2 182 ? -8.597   -73.635  17.084  1.00 113.94 ? 184 HIS B CE1 1 
ATOM   2168  N NE2 . HIS B 2 182 ? -8.674   -73.612  15.757  1.00 113.10 ? 184 HIS B NE2 1 
ATOM   2169  N N   . PRO B 2 183 ? -7.081   -80.265  17.099  1.00 106.88 ? 185 PRO B N   1 
ATOM   2170  C CA  . PRO B 2 183 ? -7.219   -81.731  17.171  1.00 108.93 ? 185 PRO B CA  1 
ATOM   2171  C C   . PRO B 2 183 ? -8.411   -82.179  18.003  1.00 117.63 ? 185 PRO B C   1 
ATOM   2172  O O   . PRO B 2 183 ? -8.681   -81.588  19.046  1.00 118.87 ? 185 PRO B O   1 
ATOM   2173  C CB  . PRO B 2 183 ? -5.905   -82.184  17.821  1.00 110.98 ? 185 PRO B CB  1 
ATOM   2174  C CG  . PRO B 2 183 ? -4.998   -81.011  17.759  1.00 113.38 ? 185 PRO B CG  1 
ATOM   2175  C CD  . PRO B 2 183 ? -5.873   -79.816  17.811  1.00 108.06 ? 185 PRO B CD  1 
ATOM   2176  N N   . SER B 2 184 ? -9.115   -83.226  17.546  1.00 115.69 ? 186 SER B N   1 
ATOM   2177  C CA  . SER B 2 184 ? -10.299  -83.777  18.217  1.00 117.82 ? 186 SER B CA  1 
ATOM   2178  C C   . SER B 2 184 ? -10.033  -84.305  19.645  1.00 121.64 ? 186 SER B C   1 
ATOM   2179  O O   . SER B 2 184 ? -10.729  -83.901  20.578  1.00 122.35 ? 186 SER B O   1 
ATOM   2180  C CB  . SER B 2 184 ? -10.954  -84.846  17.351  1.00 123.71 ? 186 SER B CB  1 
ATOM   2181  O OG  . SER B 2 184 ? -9.989   -85.768  16.876  1.00 134.99 ? 186 SER B OG  1 
ATOM   2182  N N   . THR B 2 185 ? -9.026   -85.187  19.814  1.00 117.19 ? 187 THR B N   1 
ATOM   2183  C CA  . THR B 2 185 ? -8.650   -85.754  21.117  1.00 118.06 ? 187 THR B CA  1 
ATOM   2184  C C   . THR B 2 185 ? -7.393   -85.080  21.654  1.00 120.11 ? 187 THR B C   1 
ATOM   2185  O O   . THR B 2 185 ? -6.598   -84.535  20.878  1.00 117.58 ? 187 THR B O   1 
ATOM   2186  C CB  . THR B 2 185 ? -8.456   -87.280  21.033  1.00 122.48 ? 187 THR B CB  1 
ATOM   2187  O OG1 . THR B 2 185 ? -7.318   -87.593  20.229  1.00 116.38 ? 187 THR B OG1 1 
ATOM   2188  C CG2 . THR B 2 185 ? -9.679   -88.006  20.506  1.00 123.05 ? 187 THR B CG2 1 
ATOM   2189  N N   . SER B 2 186 ? -7.214   -85.114  22.984  1.00 117.97 ? 188 SER B N   1 
ATOM   2190  C CA  . SER B 2 186 ? -6.032   -84.553  23.643  1.00 117.01 ? 188 SER B CA  1 
ATOM   2191  C C   . SER B 2 186 ? -4.774   -85.295  23.183  1.00 120.76 ? 188 SER B C   1 
ATOM   2192  O O   . SER B 2 186 ? -3.725   -84.677  23.012  1.00 118.72 ? 188 SER B O   1 
ATOM   2193  C CB  . SER B 2 186 ? -6.173   -84.595  25.166  1.00 122.80 ? 188 SER B CB  1 
ATOM   2194  O OG  . SER B 2 186 ? -6.680   -85.801  25.723  1.00 135.06 ? 188 SER B OG  1 
ATOM   2195  N N   . ALA B 2 187 ? -4.917   -86.613  22.929  1.00 119.40 ? 189 ALA B N   1 
ATOM   2196  C CA  . ALA B 2 187 ? -3.889   -87.536  22.460  1.00 120.20 ? 189 ALA B CA  1 
ATOM   2197  C C   . ALA B 2 187 ? -3.381   -87.144  21.084  1.00 121.42 ? 189 ALA B C   1 
ATOM   2198  O O   . ALA B 2 187 ? -2.190   -87.304  20.809  1.00 121.42 ? 189 ALA B O   1 
ATOM   2199  C CB  . ALA B 2 187 ? -4.451   -88.942  22.414  1.00 124.17 ? 189 ALA B CB  1 
ATOM   2200  N N   . ASP B 2 188 ? -4.282   -86.641  20.217  1.00 115.89 ? 190 ASP B N   1 
ATOM   2201  C CA  . ASP B 2 188 ? -3.943   -86.199  18.865  1.00 113.33 ? 190 ASP B CA  1 
ATOM   2202  C C   . ASP B 2 188 ? -2.981   -85.000  18.913  1.00 115.72 ? 190 ASP B C   1 
ATOM   2203  O O   . ASP B 2 188 ? -2.022   -84.958  18.142  1.00 114.90 ? 190 ASP B O   1 
ATOM   2204  C CB  . ASP B 2 188 ? -5.211   -85.889  18.042  1.00 113.45 ? 190 ASP B CB  1 
ATOM   2205  C CG  . ASP B 2 188 ? -5.819   -87.073  17.300  1.00 118.84 ? 190 ASP B CG  1 
ATOM   2206  O OD1 . ASP B 2 188 ? -5.700   -88.216  17.798  1.00 121.61 ? 190 ASP B OD1 1 
ATOM   2207  O OD2 . ASP B 2 188 ? -6.464   -86.848  16.253  1.00 120.22 ? 190 ASP B OD2 1 
ATOM   2208  N N   . GLN B 2 189 ? -3.204   -84.068  19.862  1.00 106.18 ? 191 GLN B N   1 
ATOM   2209  C CA  . GLN B 2 189 ? -2.353   -82.900  20.077  1.00 104.88 ? 191 GLN B CA  1 
ATOM   2210  C C   . GLN B 2 189 ? -0.955   -83.366  20.483  1.00 110.10 ? 191 GLN B C   1 
ATOM   2211  O O   . GLN B 2 189 ? 0.046    -82.872  19.963  1.00 108.59 ? 191 GLN B O   1 
ATOM   2212  C CB  . GLN B 2 189 ? -2.966   -82.016  21.179  1.00 107.04 ? 191 GLN B CB  1 
ATOM   2213  C CG  . GLN B 2 189 ? -2.121   -80.810  21.602  1.00 120.45 ? 191 GLN B CG  1 
ATOM   2214  C CD  . GLN B 2 189 ? -2.102   -79.718  20.561  1.00 136.23 ? 191 GLN B CD  1 
ATOM   2215  O OE1 . GLN B 2 189 ? -3.139   -79.315  20.030  1.00 128.85 ? 191 GLN B OE1 1 
ATOM   2216  N NE2 . GLN B 2 189 ? -0.921   -79.190  20.278  1.00 130.15 ? 191 GLN B NE2 1 
ATOM   2217  N N   . GLN B 2 190 ? -0.913   -84.354  21.382  1.00 110.01 ? 192 GLN B N   1 
ATOM   2218  C CA  . GLN B 2 190 ? 0.296    -84.953  21.932  1.00 112.52 ? 192 GLN B CA  1 
ATOM   2219  C C   . GLN B 2 190 ? 1.065    -85.812  20.914  1.00 116.42 ? 192 GLN B C   1 
ATOM   2220  O O   . GLN B 2 190 ? 2.249    -86.077  21.121  1.00 118.11 ? 192 GLN B O   1 
ATOM   2221  C CB  . GLN B 2 190 ? -0.052   -85.762  23.194  1.00 117.58 ? 192 GLN B CB  1 
ATOM   2222  C CG  . GLN B 2 190 ? 1.020    -85.742  24.279  1.00 134.11 ? 192 GLN B CG  1 
ATOM   2223  C CD  . GLN B 2 190 ? 1.413    -87.135  24.706  1.00 160.58 ? 192 GLN B CD  1 
ATOM   2224  O OE1 . GLN B 2 190 ? 2.564    -87.549  24.546  1.00 159.08 ? 192 GLN B OE1 1 
ATOM   2225  N NE2 . GLN B 2 190 ? 0.469    -87.896  25.250  1.00 155.83 ? 192 GLN B NE2 1 
ATOM   2226  N N   . SER B 2 191 ? 0.402    -86.257  19.833  1.00 110.54 ? 193 SER B N   1 
ATOM   2227  C CA  . SER B 2 191 ? 1.025    -87.071  18.785  1.00 109.14 ? 193 SER B CA  1 
ATOM   2228  C C   . SER B 2 191 ? 1.467    -86.248  17.555  1.00 108.08 ? 193 SER B C   1 
ATOM   2229  O O   . SER B 2 191 ? 2.366    -86.674  16.819  1.00 106.82 ? 193 SER B O   1 
ATOM   2230  C CB  . SER B 2 191 ? 0.094    -88.203  18.369  1.00 113.72 ? 193 SER B CB  1 
ATOM   2231  O OG  . SER B 2 191 ? -1.147   -87.703  17.899  1.00 122.26 ? 193 SER B OG  1 
ATOM   2232  N N   . LEU B 2 192 ? 0.834    -85.079  17.337  1.00 101.11 ? 194 LEU B N   1 
ATOM   2233  C CA  . LEU B 2 192 ? 1.142    -84.206  16.205  1.00 97.59  ? 194 LEU B CA  1 
ATOM   2234  C C   . LEU B 2 192 ? 2.103    -83.089  16.581  1.00 102.38 ? 194 LEU B C   1 
ATOM   2235  O O   . LEU B 2 192 ? 2.950    -82.705  15.770  1.00 101.05 ? 194 LEU B O   1 
ATOM   2236  C CB  . LEU B 2 192 ? -0.144   -83.581  15.641  1.00 95.98  ? 194 LEU B CB  1 
ATOM   2237  C CG  . LEU B 2 192 ? -1.170   -84.495  14.997  1.00 99.66  ? 194 LEU B CG  1 
ATOM   2238  C CD1 . LEU B 2 192 ? -2.511   -83.809  14.929  1.00 98.61  ? 194 LEU B CD1 1 
ATOM   2239  C CD2 . LEU B 2 192 ? -0.720   -84.950  13.614  1.00 101.41 ? 194 LEU B CD2 1 
ATOM   2240  N N   . TYR B 2 193 ? 1.946    -82.537  17.790  1.00 100.62 ? 195 TYR B N   1 
ATOM   2241  C CA  . TYR B 2 193 ? 2.747    -81.405  18.235  1.00 100.82 ? 195 TYR B CA  1 
ATOM   2242  C C   . TYR B 2 193 ? 3.433    -81.644  19.597  1.00 110.02 ? 195 TYR B C   1 
ATOM   2243  O O   . TYR B 2 193 ? 4.354    -80.907  19.952  1.00 110.14 ? 195 TYR B O   1 
ATOM   2244  C CB  . TYR B 2 193 ? 1.876    -80.125  18.226  1.00 100.47 ? 195 TYR B CB  1 
ATOM   2245  C CG  . TYR B 2 193 ? 0.908    -80.031  17.054  1.00 99.30  ? 195 TYR B CG  1 
ATOM   2246  C CD1 . TYR B 2 193 ? -0.453   -80.278  17.223  1.00 101.20 ? 195 TYR B CD1 1 
ATOM   2247  C CD2 . TYR B 2 193 ? 1.360    -79.733  15.770  1.00 97.98  ? 195 TYR B CD2 1 
ATOM   2248  C CE1 . TYR B 2 193 ? -1.342   -80.211  16.147  1.00 99.66  ? 195 TYR B CE1 1 
ATOM   2249  C CE2 . TYR B 2 193 ? 0.480    -79.667  14.688  1.00 97.30  ? 195 TYR B CE2 1 
ATOM   2250  C CZ  . TYR B 2 193 ? -0.868   -79.917  14.879  1.00 100.44 ? 195 TYR B CZ  1 
ATOM   2251  O OH  . TYR B 2 193 ? -1.723   -79.858  13.810  1.00 93.73  ? 195 TYR B OH  1 
ATOM   2252  N N   . GLN B 2 194 ? 2.990    -82.697  20.334  1.00 110.65 ? 196 GLN B N   1 
ATOM   2253  C CA  . GLN B 2 194 ? 3.430    -83.178  21.660  1.00 114.62 ? 196 GLN B CA  1 
ATOM   2254  C C   . GLN B 2 194 ? 3.210    -82.174  22.801  1.00 120.94 ? 196 GLN B C   1 
ATOM   2255  O O   . GLN B 2 194 ? 2.877    -82.588  23.916  1.00 122.96 ? 196 GLN B O   1 
ATOM   2256  C CB  . GLN B 2 194 ? 4.869    -83.718  21.679  1.00 117.79 ? 196 GLN B CB  1 
ATOM   2257  C CG  . GLN B 2 194 ? 5.035    -84.836  22.723  1.00 143.26 ? 196 GLN B CG  1 
ATOM   2258  C CD  . GLN B 2 194 ? 6.198    -85.763  22.475  1.00 169.55 ? 196 GLN B CD  1 
ATOM   2259  O OE1 . GLN B 2 194 ? 7.296    -85.340  22.105  1.00 168.33 ? 196 GLN B OE1 1 
ATOM   2260  N NE2 . GLN B 2 194 ? 6.001    -87.050  22.740  1.00 161.63 ? 196 GLN B NE2 1 
ATOM   2261  N N   . ASN B 2 195 ? 3.386    -80.879  22.525  1.00 116.84 ? 197 ASN B N   1 
ATOM   2262  C CA  . ASN B 2 195 ? 3.198    -79.797  23.480  1.00 118.02 ? 197 ASN B CA  1 
ATOM   2263  C C   . ASN B 2 195 ? 1.700    -79.640  23.749  1.00 121.41 ? 197 ASN B C   1 
ATOM   2264  O O   . ASN B 2 195 ? 0.969    -79.133  22.895  1.00 118.51 ? 197 ASN B O   1 
ATOM   2265  C CB  . ASN B 2 195 ? 3.830    -78.503  22.943  1.00 118.64 ? 197 ASN B CB  1 
ATOM   2266  C CG  . ASN B 2 195 ? 5.334    -78.569  22.798  1.00 133.39 ? 197 ASN B CG  1 
ATOM   2267  O OD1 . ASN B 2 195 ? 6.082    -77.952  23.569  1.00 126.08 ? 197 ASN B OD1 1 
ATOM   2268  N ND2 . ASN B 2 195 ? 5.814    -79.305  21.799  1.00 121.02 ? 197 ASN B ND2 1 
ATOM   2269  N N   . ALA B 2 196 ? 1.245    -80.148  24.914  1.00 120.63 ? 198 ALA B N   1 
ATOM   2270  C CA  . ALA B 2 196 ? -0.153   -80.136  25.348  1.00 120.89 ? 198 ALA B CA  1 
ATOM   2271  C C   . ALA B 2 196 ? -0.699   -78.722  25.446  1.00 125.37 ? 198 ALA B C   1 
ATOM   2272  O O   . ALA B 2 196 ? -1.816   -78.481  24.987  1.00 124.00 ? 198 ALA B O   1 
ATOM   2273  C CB  . ALA B 2 196 ? -0.297   -80.854  26.676  1.00 124.77 ? 198 ALA B CB  1 
ATOM   2274  N N   . ASP B 2 197 ? 0.093    -77.786  26.012  1.00 124.10 ? 199 ASP B N   1 
ATOM   2275  C CA  . ASP B 2 197 ? -0.287   -76.379  26.104  1.00 123.78 ? 199 ASP B CA  1 
ATOM   2276  C C   . ASP B 2 197 ? 0.482    -75.605  25.039  1.00 125.65 ? 199 ASP B C   1 
ATOM   2277  O O   . ASP B 2 197 ? 1.482    -74.931  25.323  1.00 125.68 ? 199 ASP B O   1 
ATOM   2278  C CB  . ASP B 2 197 ? -0.084   -75.803  27.517  1.00 128.59 ? 199 ASP B CB  1 
ATOM   2279  C CG  . ASP B 2 197 ? -0.862   -74.516  27.736  1.00 144.73 ? 199 ASP B CG  1 
ATOM   2280  O OD1 . ASP B 2 197 ? -2.049   -74.598  28.124  1.00 146.21 ? 199 ASP B OD1 1 
ATOM   2281  O OD2 . ASP B 2 197 ? -0.291   -73.425  27.495  1.00 152.48 ? 199 ASP B OD2 1 
ATOM   2282  N N   . ALA B 2 198 ? 0.030    -75.773  23.790  1.00 120.14 ? 200 ALA B N   1 
ATOM   2283  C CA  . ALA B 2 198 ? 0.612    -75.136  22.617  1.00 118.21 ? 200 ALA B CA  1 
ATOM   2284  C C   . ALA B 2 198 ? -0.138   -73.862  22.291  1.00 120.14 ? 200 ALA B C   1 
ATOM   2285  O O   . ALA B 2 198 ? -1.347   -73.776  22.510  1.00 119.23 ? 200 ALA B O   1 
ATOM   2286  C CB  . ALA B 2 198 ? 0.576    -76.087  21.430  1.00 117.69 ? 200 ALA B CB  1 
ATOM   2287  N N   . TYR B 2 199 ? 0.591    -72.869  21.781  1.00 115.84 ? 201 TYR B N   1 
ATOM   2288  C CA  . TYR B 2 199 ? 0.040    -71.581  21.394  1.00 115.09 ? 201 TYR B CA  1 
ATOM   2289  C C   . TYR B 2 199 ? 0.509    -71.206  19.995  1.00 114.73 ? 201 TYR B C   1 
ATOM   2290  O O   . TYR B 2 199 ? 1.467    -71.793  19.478  1.00 113.99 ? 201 TYR B O   1 
ATOM   2291  C CB  . TYR B 2 199 ? 0.446    -70.490  22.409  1.00 119.12 ? 201 TYR B CB  1 
ATOM   2292  C CG  . TYR B 2 199 ? 1.881    -70.008  22.280  1.00 124.04 ? 201 TYR B CG  1 
ATOM   2293  C CD1 . TYR B 2 199 ? 2.916    -70.646  22.958  1.00 127.98 ? 201 TYR B CD1 1 
ATOM   2294  C CD2 . TYR B 2 199 ? 2.199    -68.892  21.505  1.00 125.07 ? 201 TYR B CD2 1 
ATOM   2295  C CE1 . TYR B 2 199 ? 4.236    -70.201  22.849  1.00 130.55 ? 201 TYR B CE1 1 
ATOM   2296  C CE2 . TYR B 2 199 ? 3.518    -68.451  21.374  1.00 126.97 ? 201 TYR B CE2 1 
ATOM   2297  C CZ  . TYR B 2 199 ? 4.533    -69.105  22.054  1.00 135.93 ? 201 TYR B CZ  1 
ATOM   2298  O OH  . TYR B 2 199 ? 5.832    -68.671  21.944  1.00 138.10 ? 201 TYR B OH  1 
ATOM   2299  N N   . VAL B 2 200 ? -0.154   -70.209  19.394  1.00 108.45 ? 202 VAL B N   1 
ATOM   2300  C CA  . VAL B 2 200 ? 0.203    -69.644  18.094  1.00 106.50 ? 202 VAL B CA  1 
ATOM   2301  C C   . VAL B 2 200 ? 0.113    -68.118  18.225  1.00 108.89 ? 202 VAL B C   1 
ATOM   2302  O O   . VAL B 2 200 ? -0.667   -67.626  19.033  1.00 108.56 ? 202 VAL B O   1 
ATOM   2303  C CB  . VAL B 2 200 ? -0.630   -70.168  16.884  1.00 109.33 ? 202 VAL B CB  1 
ATOM   2304  C CG1 . VAL B 2 200 ? 0.103    -69.893  15.579  1.00 108.71 ? 202 VAL B CG1 1 
ATOM   2305  C CG2 . VAL B 2 200 ? -0.955   -71.658  16.993  1.00 108.44 ? 202 VAL B CG2 1 
ATOM   2306  N N   . PHE B 2 201 ? 0.940    -67.380  17.473  1.00 104.53 ? 203 PHE B N   1 
ATOM   2307  C CA  . PHE B 2 201 ? 0.930    -65.922  17.452  1.00 105.10 ? 203 PHE B CA  1 
ATOM   2308  C C   . PHE B 2 201 ? 1.337    -65.393  16.083  1.00 108.49 ? 203 PHE B C   1 
ATOM   2309  O O   . PHE B 2 201 ? 2.392    -65.774  15.571  1.00 108.52 ? 203 PHE B O   1 
ATOM   2310  C CB  . PHE B 2 201 ? 1.805    -65.310  18.562  1.00 108.13 ? 203 PHE B CB  1 
ATOM   2311  C CG  . PHE B 2 201 ? 1.884    -63.803  18.446  1.00 111.27 ? 203 PHE B CG  1 
ATOM   2312  C CD1 . PHE B 2 201 ? 3.026    -63.187  17.945  1.00 115.14 ? 203 PHE B CD1 1 
ATOM   2313  C CD2 . PHE B 2 201 ? 0.783    -63.006  18.746  1.00 114.03 ? 203 PHE B CD2 1 
ATOM   2314  C CE1 . PHE B 2 201 ? 3.081    -61.799  17.788  1.00 117.49 ? 203 PHE B CE1 1 
ATOM   2315  C CE2 . PHE B 2 201 ? 0.841    -61.617  18.593  1.00 118.22 ? 203 PHE B CE2 1 
ATOM   2316  C CZ  . PHE B 2 201 ? 1.990    -61.024  18.118  1.00 117.14 ? 203 PHE B CZ  1 
ATOM   2317  N N   . VAL B 2 202 ? 0.509    -64.499  15.504  1.00 104.18 ? 204 VAL B N   1 
ATOM   2318  C CA  . VAL B 2 202 ? 0.784    -63.867  14.214  1.00 103.87 ? 204 VAL B CA  1 
ATOM   2319  C C   . VAL B 2 202 ? 0.853    -62.349  14.400  1.00 110.94 ? 204 VAL B C   1 
ATOM   2320  O O   . VAL B 2 202 ? -0.169   -61.710  14.666  1.00 111.42 ? 204 VAL B O   1 
ATOM   2321  C CB  . VAL B 2 202 ? -0.193   -64.297  13.097  1.00 106.46 ? 204 VAL B CB  1 
ATOM   2322  C CG1 . VAL B 2 202 ? 0.210    -63.681  11.764  1.00 107.26 ? 204 VAL B CG1 1 
ATOM   2323  C CG2 . VAL B 2 202 ? -0.249   -65.813  12.977  1.00 104.06 ? 204 VAL B CG2 1 
ATOM   2324  N N   . GLY B 2 203 ? 2.065    -61.803  14.280  1.00 109.26 ? 205 GLY B N   1 
ATOM   2325  C CA  . GLY B 2 203 ? 2.336    -60.381  14.469  1.00 111.51 ? 205 GLY B CA  1 
ATOM   2326  C C   . GLY B 2 203 ? 2.781    -59.607  13.242  1.00 116.78 ? 205 GLY B C   1 
ATOM   2327  O O   . GLY B 2 203 ? 3.845    -59.867  12.679  1.00 115.52 ? 205 GLY B O   1 
ATOM   2328  N N   . SER B 2 204 ? 1.964    -58.621  12.857  1.00 115.75 ? 206 SER B N   1 
ATOM   2329  C CA  . SER B 2 204 ? 2.144    -57.669  11.758  1.00 118.08 ? 206 SER B CA  1 
ATOM   2330  C C   . SER B 2 204 ? 1.921    -56.288  12.387  1.00 125.18 ? 206 SER B C   1 
ATOM   2331  O O   . SER B 2 204 ? 1.562    -56.221  13.567  1.00 124.26 ? 206 SER B O   1 
ATOM   2332  C CB  . SER B 2 204 ? 1.101    -57.934  10.670  1.00 121.95 ? 206 SER B CB  1 
ATOM   2333  O OG  . SER B 2 204 ? 0.988    -56.890  9.714   1.00 134.37 ? 206 SER B OG  1 
ATOM   2334  N N   . SER B 2 205 ? 2.138    -55.194  11.640  1.00 125.31 ? 207 SER B N   1 
ATOM   2335  C CA  . SER B 2 205 ? 1.878    -53.869  12.205  1.00 128.53 ? 207 SER B CA  1 
ATOM   2336  C C   . SER B 2 205 ? 0.368    -53.644  12.324  1.00 133.19 ? 207 SER B C   1 
ATOM   2337  O O   . SER B 2 205 ? -0.083   -53.092  13.329  1.00 134.29 ? 207 SER B O   1 
ATOM   2338  C CB  . SER B 2 205 ? 2.531    -52.771  11.375  1.00 136.67 ? 207 SER B CB  1 
ATOM   2339  O OG  . SER B 2 205 ? 3.941    -52.784  11.532  1.00 147.50 ? 207 SER B OG  1 
ATOM   2340  N N   . ARG B 2 206 ? -0.413   -54.129  11.333  1.00 128.55 ? 208 ARG B N   1 
ATOM   2341  C CA  . ARG B 2 206 ? -1.871   -54.014  11.337  1.00 128.92 ? 208 ARG B CA  1 
ATOM   2342  C C   . ARG B 2 206 ? -2.565   -55.212  12.023  1.00 128.29 ? 208 ARG B C   1 
ATOM   2343  O O   . ARG B 2 206 ? -3.578   -55.012  12.695  1.00 128.13 ? 208 ARG B O   1 
ATOM   2344  C CB  . ARG B 2 206 ? -2.442   -53.736  9.926   1.00 132.90 ? 208 ARG B CB  1 
ATOM   2345  C CG  . ARG B 2 206 ? -2.116   -54.754  8.821   1.00 143.78 ? 208 ARG B CG  1 
ATOM   2346  C CD  . ARG B 2 206 ? -3.111   -54.670  7.661   1.00 156.38 ? 208 ARG B CD  1 
ATOM   2347  N NE  . ARG B 2 206 ? -2.844   -53.554  6.744   1.00 165.64 ? 208 ARG B NE  1 
ATOM   2348  C CZ  . ARG B 2 206 ? -3.652   -53.174  5.754   1.00 178.62 ? 208 ARG B CZ  1 
ATOM   2349  N NH1 . ARG B 2 206 ? -4.805   -53.799  5.549   1.00 164.57 ? 208 ARG B NH1 1 
ATOM   2350  N NH2 . ARG B 2 206 ? -3.319   -52.156  4.973   1.00 165.90 ? 208 ARG B NH2 1 
ATOM   2351  N N   . TYR B 2 207 ? -2.005   -56.435  11.889  1.00 121.45 ? 209 TYR B N   1 
ATOM   2352  C CA  . TYR B 2 207 ? -2.565   -57.654  12.486  1.00 118.61 ? 209 TYR B CA  1 
ATOM   2353  C C   . TYR B 2 207 ? -1.813   -58.103  13.738  1.00 120.96 ? 209 TYR B C   1 
ATOM   2354  O O   . TYR B 2 207 ? -0.588   -58.094  13.746  1.00 120.36 ? 209 TYR B O   1 
ATOM   2355  C CB  . TYR B 2 207 ? -2.574   -58.803  11.455  1.00 118.11 ? 209 TYR B CB  1 
ATOM   2356  C CG  . TYR B 2 207 ? -3.341   -60.031  11.902  1.00 117.63 ? 209 TYR B CG  1 
ATOM   2357  C CD1 . TYR B 2 207 ? -2.722   -61.035  12.644  1.00 117.10 ? 209 TYR B CD1 1 
ATOM   2358  C CD2 . TYR B 2 207 ? -4.679   -60.202  11.565  1.00 119.35 ? 209 TYR B CD2 1 
ATOM   2359  C CE1 . TYR B 2 207 ? -3.432   -62.149  13.088  1.00 116.18 ? 209 TYR B CE1 1 
ATOM   2360  C CE2 . TYR B 2 207 ? -5.394   -61.325  11.984  1.00 118.58 ? 209 TYR B CE2 1 
ATOM   2361  C CZ  . TYR B 2 207 ? -4.766   -62.295  12.748  1.00 121.49 ? 209 TYR B CZ  1 
ATOM   2362  O OH  . TYR B 2 207 ? -5.471   -63.397  13.167  1.00 118.41 ? 209 TYR B OH  1 
ATOM   2363  N N   . SER B 2 208 ? -2.549   -58.562  14.766  1.00 117.03 ? 210 SER B N   1 
ATOM   2364  C CA  . SER B 2 208 ? -1.983   -59.113  16.000  1.00 116.06 ? 210 SER B CA  1 
ATOM   2365  C C   . SER B 2 208 ? -2.993   -59.972  16.746  1.00 120.32 ? 210 SER B C   1 
ATOM   2366  O O   . SER B 2 208 ? -3.957   -59.449  17.313  1.00 120.91 ? 210 SER B O   1 
ATOM   2367  C CB  . SER B 2 208 ? -1.407   -58.025  16.901  1.00 121.97 ? 210 SER B CB  1 
ATOM   2368  O OG  . SER B 2 208 ? -0.040   -57.807  16.591  1.00 133.24 ? 210 SER B OG  1 
ATOM   2369  N N   . LYS B 2 209 ? -2.782   -61.304  16.719  1.00 116.20 ? 211 LYS B N   1 
ATOM   2370  C CA  . LYS B 2 209 ? -3.658   -62.276  17.384  1.00 115.35 ? 211 LYS B CA  1 
ATOM   2371  C C   . LYS B 2 209 ? -2.931   -63.521  17.888  1.00 117.61 ? 211 LYS B C   1 
ATOM   2372  O O   . LYS B 2 209 ? -2.031   -64.038  17.221  1.00 116.13 ? 211 LYS B O   1 
ATOM   2373  C CB  . LYS B 2 209 ? -4.851   -62.667  16.495  1.00 118.30 ? 211 LYS B CB  1 
ATOM   2374  C CG  . LYS B 2 209 ? -6.193   -62.591  17.218  1.00 136.76 ? 211 LYS B CG  1 
ATOM   2375  C CD  . LYS B 2 209 ? -6.652   -63.944  17.744  1.00 145.65 ? 211 LYS B CD  1 
ATOM   2376  C CE  . LYS B 2 209 ? -7.834   -63.823  18.675  1.00 155.30 ? 211 LYS B CE  1 
ATOM   2377  N NZ  . LYS B 2 209 ? -8.224   -65.139  19.251  1.00 159.75 ? 211 LYS B NZ  1 
ATOM   2378  N N   . THR B 2 210 ? -3.334   -63.989  19.079  1.00 113.96 ? 212 THR B N   1 
ATOM   2379  C CA  . THR B 2 210 ? -2.795   -65.177  19.740  1.00 112.74 ? 212 THR B CA  1 
ATOM   2380  C C   . THR B 2 210 ? -3.820   -66.299  19.590  1.00 116.04 ? 212 THR B C   1 
ATOM   2381  O O   . THR B 2 210 ? -5.017   -66.038  19.681  1.00 116.41 ? 212 THR B O   1 
ATOM   2382  C CB  . THR B 2 210 ? -2.469   -64.878  21.222  1.00 120.69 ? 212 THR B CB  1 
ATOM   2383  O OG1 . THR B 2 210 ? -1.892   -63.575  21.347  1.00 120.07 ? 212 THR B OG1 1 
ATOM   2384  C CG2 . THR B 2 210 ? -1.536   -65.914  21.843  1.00 118.76 ? 212 THR B CG2 1 
ATOM   2385  N N   . PHE B 2 211 ? -3.361   -67.535  19.365  1.00 112.28 ? 213 PHE B N   1 
ATOM   2386  C CA  . PHE B 2 211 ? -4.238   -68.691  19.185  1.00 112.43 ? 213 PHE B CA  1 
ATOM   2387  C C   . PHE B 2 211 ? -3.894   -69.857  20.113  1.00 116.75 ? 213 PHE B C   1 
ATOM   2388  O O   . PHE B 2 211 ? -2.732   -70.051  20.473  1.00 116.58 ? 213 PHE B O   1 
ATOM   2389  C CB  . PHE B 2 211 ? -4.208   -69.175  17.725  1.00 113.80 ? 213 PHE B CB  1 
ATOM   2390  C CG  . PHE B 2 211 ? -4.365   -68.104  16.675  1.00 116.06 ? 213 PHE B CG  1 
ATOM   2391  C CD1 . PHE B 2 211 ? -5.622   -67.645  16.308  1.00 120.49 ? 213 PHE B CD1 1 
ATOM   2392  C CD2 . PHE B 2 211 ? -3.256   -67.577  16.027  1.00 118.09 ? 213 PHE B CD2 1 
ATOM   2393  C CE1 . PHE B 2 211 ? -5.765   -66.655  15.334  1.00 122.52 ? 213 PHE B CE1 1 
ATOM   2394  C CE2 . PHE B 2 211 ? -3.402   -66.596  15.043  1.00 121.88 ? 213 PHE B CE2 1 
ATOM   2395  C CZ  . PHE B 2 211 ? -4.655   -66.141  14.705  1.00 121.32 ? 213 PHE B CZ  1 
ATOM   2396  N N   . LYS B 2 212 ? -4.915   -70.648  20.466  1.00 113.13 ? 214 LYS B N   1 
ATOM   2397  C CA  . LYS B 2 212 ? -4.801   -71.851  21.285  1.00 113.00 ? 214 LYS B CA  1 
ATOM   2398  C C   . LYS B 2 212 ? -5.772   -72.892  20.718  1.00 115.16 ? 214 LYS B C   1 
ATOM   2399  O O   . LYS B 2 212 ? -6.834   -72.507  20.219  1.00 114.21 ? 214 LYS B O   1 
ATOM   2400  C CB  . LYS B 2 212 ? -5.080   -71.555  22.768  1.00 117.38 ? 214 LYS B CB  1 
ATOM   2401  C CG  . LYS B 2 212 ? -3.901   -71.898  23.673  1.00 135.17 ? 214 LYS B CG  1 
ATOM   2402  C CD  . LYS B 2 212 ? -4.161   -71.566  25.140  1.00 148.00 ? 214 LYS B CD  1 
ATOM   2403  C CE  . LYS B 2 212 ? -2.949   -71.855  25.999  1.00 161.25 ? 214 LYS B CE  1 
ATOM   2404  N NZ  . LYS B 2 212 ? -3.093   -71.335  27.382  1.00 171.06 ? 214 LYS B NZ  1 
ATOM   2405  N N   . PRO B 2 213 ? -5.424   -74.199  20.728  1.00 104.39 ? 215 PRO B N   1 
ATOM   2406  C CA  . PRO B 2 213 ? -6.321   -75.196  20.118  1.00 104.95 ? 215 PRO B CA  1 
ATOM   2407  C C   . PRO B 2 213 ? -7.560   -75.547  20.927  1.00 107.63 ? 215 PRO B C   1 
ATOM   2408  O O   . PRO B 2 213 ? -7.486   -75.760  22.139  1.00 106.90 ? 215 PRO B O   1 
ATOM   2409  C CB  . PRO B 2 213 ? -5.417   -76.411  19.909  1.00 107.31 ? 215 PRO B CB  1 
ATOM   2410  C CG  . PRO B 2 213 ? -4.394   -76.301  20.989  1.00 111.44 ? 215 PRO B CG  1 
ATOM   2411  C CD  . PRO B 2 213 ? -4.190   -74.829  21.248  1.00 106.10 ? 215 PRO B CD  1 
ATOM   2412  N N   . GLU B 2 214 ? -8.696   -75.619  20.232  1.00 103.89 ? 216 GLU B N   1 
ATOM   2413  C CA  . GLU B 2 214 ? -9.985   -75.981  20.795  1.00 103.80 ? 216 GLU B CA  1 
ATOM   2414  C C   . GLU B 2 214 ? -10.125  -77.495  20.622  1.00 106.57 ? 216 GLU B C   1 
ATOM   2415  O O   . GLU B 2 214 ? -10.716  -77.959  19.645  1.00 107.18 ? 216 GLU B O   1 
ATOM   2416  C CB  . GLU B 2 214 ? -11.123  -75.221  20.086  1.00 106.29 ? 216 GLU B CB  1 
ATOM   2417  C CG  . GLU B 2 214 ? -11.193  -73.723  20.356  1.00 120.57 ? 216 GLU B CG  1 
ATOM   2418  C CD  . GLU B 2 214 ? -12.459  -73.042  19.856  1.00 149.27 ? 216 GLU B CD  1 
ATOM   2419  O OE1 . GLU B 2 214 ? -12.769  -73.166  18.648  1.00 152.03 ? 216 GLU B OE1 1 
ATOM   2420  O OE2 . GLU B 2 214 ? -13.142  -72.382  20.675  1.00 141.44 ? 216 GLU B OE2 1 
ATOM   2421  N N   . ILE B 2 215 ? -9.523   -78.266  21.548  1.00 101.80 ? 217 ILE B N   1 
ATOM   2422  C CA  . ILE B 2 215 ? -9.532   -79.729  21.503  1.00 102.42 ? 217 ILE B CA  1 
ATOM   2423  C C   . ILE B 2 215 ? -10.902  -80.274  21.912  1.00 107.91 ? 217 ILE B C   1 
ATOM   2424  O O   . ILE B 2 215 ? -11.277  -80.197  23.087  1.00 107.21 ? 217 ILE B O   1 
ATOM   2425  C CB  . ILE B 2 215 ? -8.343   -80.364  22.282  1.00 105.56 ? 217 ILE B CB  1 
ATOM   2426  C CG1 . ILE B 2 215 ? -7.003   -80.038  21.591  1.00 106.10 ? 217 ILE B CG1 1 
ATOM   2427  C CG2 . ILE B 2 215 ? -8.505   -81.879  22.416  1.00 107.33 ? 217 ILE B CG2 1 
ATOM   2428  C CD1 . ILE B 2 215 ? -5.822   -79.905  22.527  1.00 115.76 ? 217 ILE B CD1 1 
ATOM   2429  N N   . ALA B 2 216 ? -11.648  -80.807  20.911  1.00 106.15 ? 218 ALA B N   1 
ATOM   2430  C CA  . ALA B 2 216 ? -12.994  -81.386  21.037  1.00 106.90 ? 218 ALA B CA  1 
ATOM   2431  C C   . ALA B 2 216 ? -13.356  -82.247  19.829  1.00 111.82 ? 218 ALA B C   1 
ATOM   2432  O O   . ALA B 2 216 ? -13.047  -81.876  18.693  1.00 111.33 ? 218 ALA B O   1 
ATOM   2433  C CB  . ALA B 2 216 ? -14.030  -80.280  21.190  1.00 107.34 ? 218 ALA B CB  1 
ATOM   2434  N N   . ILE B 2 217 ? -14.035  -83.382  20.071  1.00 109.91 ? 219 ILE B N   1 
ATOM   2435  C CA  . ILE B 2 217 ? -14.506  -84.274  19.003  1.00 110.99 ? 219 ILE B CA  1 
ATOM   2436  C C   . ILE B 2 217 ? -15.768  -83.635  18.380  1.00 115.22 ? 219 ILE B C   1 
ATOM   2437  O O   . ILE B 2 217 ? -16.768  -83.438  19.078  1.00 115.77 ? 219 ILE B O   1 
ATOM   2438  C CB  . ILE B 2 217 ? -14.728  -85.743  19.508  1.00 115.64 ? 219 ILE B CB  1 
ATOM   2439  C CG1 . ILE B 2 217 ? -13.381  -86.490  19.668  1.00 116.95 ? 219 ILE B CG1 1 
ATOM   2440  C CG2 . ILE B 2 217 ? -15.691  -86.535  18.598  1.00 116.84 ? 219 ILE B CG2 1 
ATOM   2441  C CD1 . ILE B 2 217 ? -13.438  -87.808  20.482  1.00 126.87 ? 219 ILE B CD1 1 
ATOM   2442  N N   . ARG B 2 218 ? -15.699  -83.281  17.081  1.00 110.85 ? 220 ARG B N   1 
ATOM   2443  C CA  . ARG B 2 218 ? -16.813  -82.683  16.328  1.00 110.50 ? 220 ARG B CA  1 
ATOM   2444  C C   . ARG B 2 218 ? -17.407  -83.716  15.336  1.00 114.79 ? 220 ARG B C   1 
ATOM   2445  O O   . ARG B 2 218 ? -16.783  -84.762  15.134  1.00 114.75 ? 220 ARG B O   1 
ATOM   2446  C CB  . ARG B 2 218 ? -16.333  -81.436  15.558  1.00 108.63 ? 220 ARG B CB  1 
ATOM   2447  C CG  . ARG B 2 218 ? -16.060  -80.223  16.411  1.00 113.16 ? 220 ARG B CG  1 
ATOM   2448  C CD  . ARG B 2 218 ? -14.572  -80.017  16.517  1.00 116.83 ? 220 ARG B CD  1 
ATOM   2449  N NE  . ARG B 2 218 ? -14.249  -78.722  17.104  1.00 117.70 ? 220 ARG B NE  1 
ATOM   2450  C CZ  . ARG B 2 218 ? -13.033  -78.356  17.485  1.00 123.96 ? 220 ARG B CZ  1 
ATOM   2451  N NH1 . ARG B 2 218 ? -12.009  -79.194  17.363  1.00 103.20 ? 220 ARG B NH1 1 
ATOM   2452  N NH2 . ARG B 2 218 ? -12.830  -77.152  17.998  1.00 111.82 ? 220 ARG B NH2 1 
ATOM   2453  N N   . PRO B 2 219 ? -18.569  -83.461  14.677  1.00 111.13 ? 221 PRO B N   1 
ATOM   2454  C CA  . PRO B 2 219 ? -19.082  -84.442  13.701  1.00 111.21 ? 221 PRO B CA  1 
ATOM   2455  C C   . PRO B 2 219 ? -18.131  -84.647  12.517  1.00 114.98 ? 221 PRO B C   1 
ATOM   2456  O O   . PRO B 2 219 ? -17.438  -83.706  12.123  1.00 114.60 ? 221 PRO B O   1 
ATOM   2457  C CB  . PRO B 2 219 ? -20.406  -83.823  13.244  1.00 113.54 ? 221 PRO B CB  1 
ATOM   2458  C CG  . PRO B 2 219 ? -20.259  -82.362  13.509  1.00 117.94 ? 221 PRO B CG  1 
ATOM   2459  C CD  . PRO B 2 219 ? -19.463  -82.287  14.769  1.00 112.93 ? 221 PRO B CD  1 
ATOM   2460  N N   . LYS B 2 220 ? -18.084  -85.875  11.964  1.00 111.24 ? 222 LYS B N   1 
ATOM   2461  C CA  . LYS B 2 220 ? -17.209  -86.207  10.841  1.00 110.10 ? 222 LYS B CA  1 
ATOM   2462  C C   . LYS B 2 220 ? -17.622  -85.513  9.537   1.00 113.91 ? 222 LYS B C   1 
ATOM   2463  O O   . LYS B 2 220 ? -18.361  -86.072  8.717   1.00 113.72 ? 222 LYS B O   1 
ATOM   2464  C CB  . LYS B 2 220 ? -17.063  -87.726  10.665  1.00 112.33 ? 222 LYS B CB  1 
ATOM   2465  C CG  . LYS B 2 220 ? -15.803  -88.285  11.302  1.00 129.83 ? 222 LYS B CG  1 
ATOM   2466  C CD  . LYS B 2 220 ? -15.488  -89.691  10.797  1.00 142.31 ? 222 LYS B CD  1 
ATOM   2467  C CE  . LYS B 2 220 ? -14.287  -90.314  11.476  1.00 158.47 ? 222 LYS B CE  1 
ATOM   2468  N NZ  . LYS B 2 220 ? -13.001  -89.687  11.059  1.00 168.41 ? 222 LYS B NZ  1 
ATOM   2469  N N   . VAL B 2 221 ? -17.156  -84.264  9.379   1.00 110.27 ? 223 VAL B N   1 
ATOM   2470  C CA  . VAL B 2 221 ? -17.369  -83.437  8.187   1.00 109.98 ? 223 VAL B CA  1 
ATOM   2471  C C   . VAL B 2 221 ? -16.145  -83.725  7.323   1.00 110.91 ? 223 VAL B C   1 
ATOM   2472  O O   . VAL B 2 221 ? -15.017  -83.473  7.760   1.00 110.83 ? 223 VAL B O   1 
ATOM   2473  C CB  . VAL B 2 221 ? -17.538  -81.931  8.534   1.00 115.21 ? 223 VAL B CB  1 
ATOM   2474  C CG1 . VAL B 2 221 ? -17.547  -81.071  7.274   1.00 115.68 ? 223 VAL B CG1 1 
ATOM   2475  C CG2 . VAL B 2 221 ? -18.810  -81.694  9.348   1.00 115.89 ? 223 VAL B CG2 1 
ATOM   2476  N N   . ARG B 2 222 ? -16.364  -84.338  6.141   1.00 104.60 ? 224 ARG B N   1 
ATOM   2477  C CA  . ARG B 2 222 ? -15.310  -84.817  5.233   1.00 102.46 ? 224 ARG B CA  1 
ATOM   2478  C C   . ARG B 2 222 ? -14.437  -85.850  5.986   1.00 104.17 ? 224 ARG B C   1 
ATOM   2479  O O   . ARG B 2 222 ? -13.207  -85.849  5.926   1.00 101.92 ? 224 ARG B O   1 
ATOM   2480  C CB  . ARG B 2 222 ? -14.529  -83.667  4.551   1.00 102.00 ? 224 ARG B CB  1 
ATOM   2481  C CG  . ARG B 2 222 ? -15.352  -82.981  3.451   1.00 109.03 ? 224 ARG B CG  1 
ATOM   2482  C CD  . ARG B 2 222 ? -14.579  -82.024  2.558   1.00 108.50 ? 224 ARG B CD  1 
ATOM   2483  N NE  . ARG B 2 222 ? -13.499  -82.685  1.816   1.00 112.60 ? 224 ARG B NE  1 
ATOM   2484  C CZ  . ARG B 2 222 ? -13.647  -83.301  0.646   1.00 127.77 ? 224 ARG B CZ  1 
ATOM   2485  N NH1 . ARG B 2 222 ? -14.837  -83.358  0.062   1.00 117.88 ? 224 ARG B NH1 1 
ATOM   2486  N NH2 . ARG B 2 222 ? -12.608  -83.875  0.056   1.00 114.47 ? 224 ARG B NH2 1 
ATOM   2487  N N   . ASP B 2 223 ? -15.152  -86.712  6.738   1.00 102.15 ? 225 ASP B N   1 
ATOM   2488  C CA  . ASP B 2 223 ? -14.710  -87.793  7.621   1.00 102.46 ? 225 ASP B CA  1 
ATOM   2489  C C   . ASP B 2 223 ? -13.503  -87.398  8.491   1.00 106.74 ? 225 ASP B C   1 
ATOM   2490  O O   . ASP B 2 223 ? -12.586  -88.197  8.696   1.00 106.55 ? 225 ASP B O   1 
ATOM   2491  C CB  . ASP B 2 223 ? -14.499  -89.115  6.856   1.00 103.36 ? 225 ASP B CB  1 
ATOM   2492  C CG  . ASP B 2 223 ? -15.706  -90.048  6.945   1.00 107.28 ? 225 ASP B CG  1 
ATOM   2493  O OD1 . ASP B 2 223 ? -16.740  -89.746  6.306   1.00 104.28 ? 225 ASP B OD1 1 
ATOM   2494  O OD2 . ASP B 2 223 ? -15.619  -91.071  7.665   1.00 114.12 ? 225 ASP B OD2 1 
ATOM   2495  N N   . ARG B 2 224 ? -13.551  -86.162  9.032   1.00 103.23 ? 226 ARG B N   1 
ATOM   2496  C CA  . ARG B 2 224 ? -12.552  -85.593  9.936   1.00 102.63 ? 226 ARG B CA  1 
ATOM   2497  C C   . ARG B 2 224 ? -13.228  -85.093  11.202  1.00 107.03 ? 226 ARG B C   1 
ATOM   2498  O O   . ARG B 2 224 ? -14.169  -84.294  11.128  1.00 106.47 ? 226 ARG B O   1 
ATOM   2499  C CB  . ARG B 2 224 ? -11.744  -84.467  9.267   1.00 99.07  ? 226 ARG B CB  1 
ATOM   2500  C CG  . ARG B 2 224 ? -10.618  -84.963  8.381   1.00 100.32 ? 226 ARG B CG  1 
ATOM   2501  C CD  . ARG B 2 224 ? -9.432   -85.499  9.157   1.00 103.95 ? 226 ARG B CD  1 
ATOM   2502  N NE  . ARG B 2 224 ? -8.782   -86.596  8.438   1.00 108.44 ? 226 ARG B NE  1 
ATOM   2503  C CZ  . ARG B 2 224 ? -9.039   -87.888  8.635   1.00 123.01 ? 226 ARG B CZ  1 
ATOM   2504  N NH1 . ARG B 2 224 ? -9.927   -88.265  9.548   1.00 114.54 ? 226 ARG B NH1 1 
ATOM   2505  N NH2 . ARG B 2 224 ? -8.405   -88.812  7.929   1.00 107.86 ? 226 ARG B NH2 1 
ATOM   2506  N N   . GLU B 2 225 ? -12.767  -85.591  12.363  1.00 118.46 ? 227 GLU B N   1 
ATOM   2507  C CA  . GLU B 2 225 ? -13.311  -85.208  13.665  1.00 119.75 ? 227 GLU B CA  1 
ATOM   2508  C C   . GLU B 2 225 ? -12.811  -83.819  14.102  1.00 120.70 ? 227 GLU B C   1 
ATOM   2509  O O   . GLU B 2 225 ? -13.563  -83.068  14.729  1.00 122.33 ? 227 GLU B O   1 
ATOM   2510  C CB  . GLU B 2 225 ? -13.025  -86.279  14.725  1.00 123.00 ? 227 GLU B CB  1 
ATOM   2511  C CG  . GLU B 2 225 ? -13.766  -87.585  14.488  1.00 139.24 ? 227 GLU B CG  1 
ATOM   2512  C CD  . GLU B 2 225 ? -14.395  -88.215  15.717  1.00 175.99 ? 227 GLU B CD  1 
ATOM   2513  O OE1 . GLU B 2 225 ? -13.656  -88.540  16.676  1.00 175.85 ? 227 GLU B OE1 1 
ATOM   2514  O OE2 . GLU B 2 225 ? -15.633  -88.403  15.713  1.00 177.28 ? 227 GLU B OE2 1 
ATOM   2515  N N   . GLY B 2 226 ? -11.567  -83.490  13.747  1.00 112.34 ? 228 GLY B N   1 
ATOM   2516  C CA  . GLY B 2 226 ? -10.957  -82.201  14.054  1.00 108.94 ? 228 GLY B CA  1 
ATOM   2517  C C   . GLY B 2 226 ? -11.299  -81.130  13.035  1.00 110.18 ? 228 GLY B C   1 
ATOM   2518  O O   . GLY B 2 226 ? -11.955  -81.411  12.027  1.00 111.31 ? 228 GLY B O   1 
ATOM   2519  N N   . ARG B 2 227 ? -10.871  -79.883  13.296  1.00 102.78 ? 229 ARG B N   1 
ATOM   2520  C CA  . ARG B 2 227 ? -11.126  -78.747  12.402  1.00 99.86  ? 229 ARG B CA  1 
ATOM   2521  C C   . ARG B 2 227 ? -9.884   -77.878  12.203  1.00 99.33  ? 229 ARG B C   1 
ATOM   2522  O O   . ARG B 2 227 ? -8.923   -77.972  12.965  1.00 96.47  ? 229 ARG B O   1 
ATOM   2523  C CB  . ARG B 2 227 ? -12.298  -77.884  12.914  1.00 98.66  ? 229 ARG B CB  1 
ATOM   2524  C CG  . ARG B 2 227 ? -13.630  -78.609  13.081  1.00 103.70 ? 229 ARG B CG  1 
ATOM   2525  C CD  . ARG B 2 227 ? -14.451  -78.693  11.811  1.00 105.75 ? 229 ARG B CD  1 
ATOM   2526  N NE  . ARG B 2 227 ? -15.791  -79.201  12.090  1.00 112.47 ? 229 ARG B NE  1 
ATOM   2527  C CZ  . ARG B 2 227 ? -16.121  -80.486  12.080  1.00 129.83 ? 229 ARG B CZ  1 
ATOM   2528  N NH1 . ARG B 2 227 ? -15.214  -81.411  11.788  1.00 110.97 ? 229 ARG B NH1 1 
ATOM   2529  N NH2 . ARG B 2 227 ? -17.360  -80.859  12.363  1.00 128.62 ? 229 ARG B NH2 1 
ATOM   2530  N N   . MET B 2 228 ? -9.913   -77.035  11.169  1.00 95.98  ? 230 MET B N   1 
ATOM   2531  C CA  . MET B 2 228 ? -8.832   -76.116  10.852  1.00 94.24  ? 230 MET B CA  1 
ATOM   2532  C C   . MET B 2 228 ? -9.421   -74.748  10.573  1.00 98.36  ? 230 MET B C   1 
ATOM   2533  O O   . MET B 2 228 ? -10.190  -74.600  9.624   1.00 99.18  ? 230 MET B O   1 
ATOM   2534  C CB  . MET B 2 228 ? -8.060   -76.588  9.609   1.00 95.56  ? 230 MET B CB  1 
ATOM   2535  C CG  . MET B 2 228 ? -6.686   -77.130  9.901   1.00 98.24  ? 230 MET B CG  1 
ATOM   2536  S SD  . MET B 2 228 ? -5.737   -77.421  8.381   1.00 101.67 ? 230 MET B SD  1 
ATOM   2537  C CE  . MET B 2 228 ? -4.778   -78.816  8.881   1.00 98.04  ? 230 MET B CE  1 
ATOM   2538  N N   . ASN B 2 229 ? -9.070   -73.744  11.375  1.00 94.38  ? 231 ASN B N   1 
ATOM   2539  C CA  . ASN B 2 229 ? -9.543   -72.394  11.101  1.00 95.49  ? 231 ASN B CA  1 
ATOM   2540  C C   . ASN B 2 229 ? -8.550   -71.710  10.153  1.00 97.32  ? 231 ASN B C   1 
ATOM   2541  O O   . ASN B 2 229 ? -7.339   -71.857  10.339  1.00 96.28  ? 231 ASN B O   1 
ATOM   2542  C CB  . ASN B 2 229 ? -9.751   -71.602  12.384  1.00 98.78  ? 231 ASN B CB  1 
ATOM   2543  C CG  . ASN B 2 229 ? -11.005  -71.964  13.139  1.00 140.06 ? 231 ASN B CG  1 
ATOM   2544  O OD1 . ASN B 2 229 ? -11.970  -72.518  12.590  1.00 136.21 ? 231 ASN B OD1 1 
ATOM   2545  N ND2 . ASN B 2 229 ? -11.024  -71.636  14.422  1.00 139.40 ? 231 ASN B ND2 1 
ATOM   2546  N N   . TYR B 2 230 ? -9.055   -71.023  9.107   1.00 91.89  ? 232 TYR B N   1 
ATOM   2547  C CA  . TYR B 2 230 ? -8.209   -70.357  8.120   1.00 89.10  ? 232 TYR B CA  1 
ATOM   2548  C C   . TYR B 2 230 ? -8.229   -68.858  8.322   1.00 94.99  ? 232 TYR B C   1 
ATOM   2549  O O   . TYR B 2 230 ? -9.284   -68.233  8.183   1.00 97.53  ? 232 TYR B O   1 
ATOM   2550  C CB  . TYR B 2 230 ? -8.623   -70.751  6.692   1.00 90.08  ? 232 TYR B CB  1 
ATOM   2551  C CG  . TYR B 2 230 ? -8.757   -72.245  6.516   1.00 90.40  ? 232 TYR B CG  1 
ATOM   2552  C CD1 . TYR B 2 230 ? -7.634   -73.059  6.433   1.00 90.10  ? 232 TYR B CD1 1 
ATOM   2553  C CD2 . TYR B 2 230 ? -10.004  -72.850  6.483   1.00 93.28  ? 232 TYR B CD2 1 
ATOM   2554  C CE1 . TYR B 2 230 ? -7.748   -74.440  6.309   1.00 90.19  ? 232 TYR B CE1 1 
ATOM   2555  C CE2 . TYR B 2 230 ? -10.131  -74.230  6.355   1.00 94.65  ? 232 TYR B CE2 1 
ATOM   2556  C CZ  . TYR B 2 230 ? -8.999   -75.021  6.264   1.00 99.30  ? 232 TYR B CZ  1 
ATOM   2557  O OH  . TYR B 2 230 ? -9.106   -76.384  6.157   1.00 101.54 ? 232 TYR B OH  1 
ATOM   2558  N N   . TYR B 2 231 ? -7.067   -68.284  8.680   1.00 91.21  ? 233 TYR B N   1 
ATOM   2559  C CA  . TYR B 2 231 ? -6.898   -66.847  8.939   1.00 93.05  ? 233 TYR B CA  1 
ATOM   2560  C C   . TYR B 2 231 ? -6.054   -66.165  7.858   1.00 98.91  ? 233 TYR B C   1 
ATOM   2561  O O   . TYR B 2 231 ? -5.182   -66.801  7.255   1.00 95.98  ? 233 TYR B O   1 
ATOM   2562  C CB  . TYR B 2 231 ? -6.283   -66.597  10.329  1.00 93.95  ? 233 TYR B CB  1 
ATOM   2563  C CG  . TYR B 2 231 ? -7.077   -67.152  11.492  1.00 96.27  ? 233 TYR B CG  1 
ATOM   2564  C CD1 . TYR B 2 231 ? -6.928   -68.475  11.894  1.00 96.58  ? 233 TYR B CD1 1 
ATOM   2565  C CD2 . TYR B 2 231 ? -7.919   -66.337  12.238  1.00 100.16 ? 233 TYR B CD2 1 
ATOM   2566  C CE1 . TYR B 2 231 ? -7.639   -68.988  12.975  1.00 98.06  ? 233 TYR B CE1 1 
ATOM   2567  C CE2 . TYR B 2 231 ? -8.629   -66.838  13.329  1.00 102.91 ? 233 TYR B CE2 1 
ATOM   2568  C CZ  . TYR B 2 231 ? -8.497   -68.171  13.684  1.00 107.91 ? 233 TYR B CZ  1 
ATOM   2569  O OH  . TYR B 2 231 ? -9.190   -68.692  14.748  1.00 112.14 ? 233 TYR B OH  1 
ATOM   2570  N N   . TRP B 2 232 ? -6.309   -64.864  7.626   1.00 100.30 ? 234 TRP B N   1 
ATOM   2571  C CA  . TRP B 2 232 ? -5.598   -64.090  6.610   1.00 101.71 ? 234 TRP B CA  1 
ATOM   2572  C C   . TRP B 2 232 ? -5.363   -62.632  7.005   1.00 108.48 ? 234 TRP B C   1 
ATOM   2573  O O   . TRP B 2 232 ? -6.175   -62.040  7.722   1.00 109.71 ? 234 TRP B O   1 
ATOM   2574  C CB  . TRP B 2 232 ? -6.351   -64.156  5.263   1.00 102.23 ? 234 TRP B CB  1 
ATOM   2575  C CG  . TRP B 2 232 ? -7.615   -63.336  5.234   1.00 106.77 ? 234 TRP B CG  1 
ATOM   2576  C CD1 . TRP B 2 232 ? -8.860   -63.731  5.628   1.00 111.19 ? 234 TRP B CD1 1 
ATOM   2577  C CD2 . TRP B 2 232 ? -7.737   -61.960  4.843   1.00 109.49 ? 234 TRP B CD2 1 
ATOM   2578  N NE1 . TRP B 2 232 ? -9.752   -62.691  5.497   1.00 114.05 ? 234 TRP B NE1 1 
ATOM   2579  C CE2 . TRP B 2 232 ? -9.087   -61.589  5.025   1.00 116.48 ? 234 TRP B CE2 1 
ATOM   2580  C CE3 . TRP B 2 232 ? -6.831   -60.999  4.358   1.00 111.39 ? 234 TRP B CE3 1 
ATOM   2581  C CZ2 . TRP B 2 232 ? -9.555   -60.300  4.738   1.00 119.48 ? 234 TRP B CZ2 1 
ATOM   2582  C CZ3 . TRP B 2 232 ? -7.298   -59.730  4.056   1.00 116.37 ? 234 TRP B CZ3 1 
ATOM   2583  C CH2 . TRP B 2 232 ? -8.646   -59.393  4.237   1.00 119.96 ? 234 TRP B CH2 1 
ATOM   2584  N N   . THR B 2 233 ? -4.279   -62.042  6.463   1.00 106.45 ? 235 THR B N   1 
ATOM   2585  C CA  . THR B 2 233 ? -3.921   -60.632  6.631   1.00 109.35 ? 235 THR B CA  1 
ATOM   2586  C C   . THR B 2 233 ? -3.117   -60.107  5.443   1.00 114.58 ? 235 THR B C   1 
ATOM   2587  O O   . THR B 2 233 ? -2.538   -60.876  4.675   1.00 111.42 ? 235 THR B O   1 
ATOM   2588  C CB  . THR B 2 233 ? -3.238   -60.334  7.982   1.00 117.80 ? 235 THR B CB  1 
ATOM   2589  O OG1 . THR B 2 233 ? -3.238   -58.919  8.179   1.00 120.25 ? 235 THR B OG1 1 
ATOM   2590  C CG2 . THR B 2 233 ? -1.812   -60.848  8.052   1.00 113.37 ? 235 THR B CG2 1 
ATOM   2591  N N   . LEU B 2 234 ? -3.108   -58.786  5.301   1.00 116.11 ? 236 LEU B N   1 
ATOM   2592  C CA  . LEU B 2 234 ? -2.344   -58.074  4.295   1.00 118.08 ? 236 LEU B CA  1 
ATOM   2593  C C   . LEU B 2 234 ? -1.163   -57.453  5.028   1.00 125.12 ? 236 LEU B C   1 
ATOM   2594  O O   . LEU B 2 234 ? -1.298   -57.040  6.187   1.00 126.45 ? 236 LEU B O   1 
ATOM   2595  C CB  . LEU B 2 234 ? -3.192   -56.970  3.643   1.00 121.68 ? 236 LEU B CB  1 
ATOM   2596  C CG  . LEU B 2 234 ? -4.325   -57.425  2.734   1.00 126.79 ? 236 LEU B CG  1 
ATOM   2597  C CD1 . LEU B 2 234 ? -5.489   -56.467  2.812   1.00 130.72 ? 236 LEU B CD1 1 
ATOM   2598  C CD2 . LEU B 2 234 ? -3.851   -57.578  1.293   1.00 130.10 ? 236 LEU B CD2 1 
ATOM   2599  N N   . VAL B 2 235 ? 0.005    -57.437  4.380   1.00 122.01 ? 237 VAL B N   1 
ATOM   2600  C CA  . VAL B 2 235 ? 1.205    -56.834  4.943   1.00 123.36 ? 237 VAL B CA  1 
ATOM   2601  C C   . VAL B 2 235 ? 1.618    -55.715  4.006   1.00 130.88 ? 237 VAL B C   1 
ATOM   2602  O O   . VAL B 2 235 ? 1.834    -55.941  2.817   1.00 130.52 ? 237 VAL B O   1 
ATOM   2603  C CB  . VAL B 2 235 ? 2.337    -57.855  5.231   1.00 124.64 ? 237 VAL B CB  1 
ATOM   2604  C CG1 . VAL B 2 235 ? 3.617    -57.155  5.672   1.00 126.79 ? 237 VAL B CG1 1 
ATOM   2605  C CG2 . VAL B 2 235 ? 1.902    -58.864  6.288   1.00 122.03 ? 237 VAL B CG2 1 
ATOM   2606  N N   . GLU B 2 236 ? 1.662    -54.499  4.541   1.00 130.97 ? 238 GLU B N   1 
ATOM   2607  C CA  . GLU B 2 236 ? 2.042    -53.294  3.811   1.00 134.64 ? 238 GLU B CA  1 
ATOM   2608  C C   . GLU B 2 236 ? 3.540    -53.389  3.459   1.00 137.72 ? 238 GLU B C   1 
ATOM   2609  O O   . GLU B 2 236 ? 4.280    -54.032  4.209   1.00 136.38 ? 238 GLU B O   1 
ATOM   2610  C CB  . GLU B 2 236 ? 1.777    -52.047  4.685   1.00 140.50 ? 238 GLU B CB  1 
ATOM   2611  C CG  . GLU B 2 236 ? 0.358    -51.931  5.238   1.00 155.40 ? 238 GLU B CG  1 
ATOM   2612  C CD  . GLU B 2 236 ? 0.224    -52.050  6.748   1.00 181.84 ? 238 GLU B CD  1 
ATOM   2613  O OE1 . GLU B 2 236 ? -0.293   -51.094  7.371   1.00 179.12 ? 238 GLU B OE1 1 
ATOM   2614  O OE2 . GLU B 2 236 ? 0.627    -53.095  7.309   1.00 175.30 ? 238 GLU B OE2 1 
ATOM   2615  N N   . PRO B 2 237 ? 4.019    -52.792  2.338   1.00 135.32 ? 239 PRO B N   1 
ATOM   2616  C CA  . PRO B 2 237 ? 5.461    -52.868  2.023   1.00 135.64 ? 239 PRO B CA  1 
ATOM   2617  C C   . PRO B 2 237 ? 6.352    -52.301  3.130   1.00 140.82 ? 239 PRO B C   1 
ATOM   2618  O O   . PRO B 2 237 ? 6.056    -51.231  3.671   1.00 144.28 ? 239 PRO B O   1 
ATOM   2619  C CB  . PRO B 2 237 ? 5.588    -52.058  0.731   1.00 140.93 ? 239 PRO B CB  1 
ATOM   2620  C CG  . PRO B 2 237 ? 4.383    -51.188  0.701   1.00 147.77 ? 239 PRO B CG  1 
ATOM   2621  C CD  . PRO B 2 237 ? 3.299    -52.007  1.318   1.00 139.55 ? 239 PRO B CD  1 
ATOM   2622  N N   . GLY B 2 238 ? 7.398    -53.051  3.481   1.00 134.14 ? 240 GLY B N   1 
ATOM   2623  C CA  . GLY B 2 238 ? 8.356    -52.684  4.522   1.00 135.42 ? 240 GLY B CA  1 
ATOM   2624  C C   . GLY B 2 238 ? 8.095    -53.333  5.869   1.00 134.02 ? 240 GLY B C   1 
ATOM   2625  O O   . GLY B 2 238 ? 9.032    -53.550  6.644   1.00 134.34 ? 240 GLY B O   1 
ATOM   2626  N N   . ASP B 2 239 ? 6.811    -53.636  6.152   1.00 126.05 ? 241 ASP B N   1 
ATOM   2627  C CA  . ASP B 2 239 ? 6.332    -54.258  7.386   1.00 123.45 ? 241 ASP B CA  1 
ATOM   2628  C C   . ASP B 2 239 ? 6.716    -55.747  7.470   1.00 124.56 ? 241 ASP B C   1 
ATOM   2629  O O   . ASP B 2 239 ? 6.824    -56.422  6.442   1.00 121.79 ? 241 ASP B O   1 
ATOM   2630  C CB  . ASP B 2 239 ? 4.812    -54.050  7.516   1.00 123.73 ? 241 ASP B CB  1 
ATOM   2631  C CG  . ASP B 2 239 ? 4.160    -54.530  8.800   1.00 125.17 ? 241 ASP B CG  1 
ATOM   2632  O OD1 . ASP B 2 239 ? 4.871    -54.652  9.821   1.00 125.14 ? 241 ASP B OD1 1 
ATOM   2633  O OD2 . ASP B 2 239 ? 2.931    -54.739  8.795   1.00 128.99 ? 241 ASP B OD2 1 
ATOM   2634  N N   . LYS B 2 240 ? 6.937    -56.240  8.707   1.00 121.49 ? 242 LYS B N   1 
ATOM   2635  C CA  . LYS B 2 240 ? 7.337    -57.618  9.012   1.00 117.84 ? 242 LYS B CA  1 
ATOM   2636  C C   . LYS B 2 240 ? 6.230    -58.423  9.702   1.00 117.71 ? 242 LYS B C   1 
ATOM   2637  O O   . LYS B 2 240 ? 5.676    -57.986  10.716  1.00 119.45 ? 242 LYS B O   1 
ATOM   2638  C CB  . LYS B 2 240 ? 8.633    -57.638  9.856   1.00 122.93 ? 242 LYS B CB  1 
ATOM   2639  C CG  . LYS B 2 240 ? 9.123    -59.030  10.267  1.00 130.35 ? 242 LYS B CG  1 
ATOM   2640  C CD  . LYS B 2 240 ? 9.756    -59.016  11.650  1.00 142.18 ? 242 LYS B CD  1 
ATOM   2641  C CE  . LYS B 2 240 ? 11.259   -59.144  11.588  1.00 160.44 ? 242 LYS B CE  1 
ATOM   2642  N NZ  . LYS B 2 240 ? 11.886   -59.027  12.933  1.00 176.71 ? 242 LYS B NZ  1 
ATOM   2643  N N   . ILE B 2 241 ? 5.946    -59.617  9.169   1.00 108.81 ? 243 ILE B N   1 
ATOM   2644  C CA  . ILE B 2 241 ? 4.966    -60.532  9.741   1.00 105.54 ? 243 ILE B CA  1 
ATOM   2645  C C   . ILE B 2 241 ? 5.703    -61.703  10.411  1.00 108.97 ? 243 ILE B C   1 
ATOM   2646  O O   . ILE B 2 241 ? 6.441    -62.429  9.746   1.00 107.86 ? 243 ILE B O   1 
ATOM   2647  C CB  . ILE B 2 241 ? 3.849    -60.937  8.734   1.00 105.36 ? 243 ILE B CB  1 
ATOM   2648  C CG1 . ILE B 2 241 ? 2.812    -61.883  9.396   1.00 102.87 ? 243 ILE B CG1 1 
ATOM   2649  C CG2 . ILE B 2 241 ? 4.415    -61.495  7.407   1.00 104.52 ? 243 ILE B CG2 1 
ATOM   2650  C CD1 . ILE B 2 241 ? 1.549    -62.122  8.604   1.00 101.29 ? 243 ILE B CD1 1 
ATOM   2651  N N   . THR B 2 242 ? 5.549    -61.830  11.741  1.00 106.38 ? 244 THR B N   1 
ATOM   2652  C CA  . THR B 2 242 ? 6.185    -62.860  12.568  1.00 105.64 ? 244 THR B CA  1 
ATOM   2653  C C   . THR B 2 242 ? 5.201    -63.990  12.843  1.00 105.57 ? 244 THR B C   1 
ATOM   2654  O O   . THR B 2 242 ? 3.998    -63.748  12.931  1.00 104.86 ? 244 THR B O   1 
ATOM   2655  C CB  . THR B 2 242 ? 6.765    -62.218  13.844  1.00 120.73 ? 244 THR B CB  1 
ATOM   2656  O OG1 . THR B 2 242 ? 7.675    -61.183  13.461  1.00 125.18 ? 244 THR B OG1 1 
ATOM   2657  C CG2 . THR B 2 242 ? 7.485    -63.217  14.755  1.00 120.21 ? 244 THR B CG2 1 
ATOM   2658  N N   . PHE B 2 243 ? 5.714    -65.221  12.951  1.00 100.00 ? 245 PHE B N   1 
ATOM   2659  C CA  . PHE B 2 243 ? 4.917    -66.417  13.207  1.00 97.56  ? 245 PHE B CA  1 
ATOM   2660  C C   . PHE B 2 243 ? 5.483    -67.252  14.362  1.00 104.06 ? 245 PHE B C   1 
ATOM   2661  O O   . PHE B 2 243 ? 6.331    -68.122  14.141  1.00 103.67 ? 245 PHE B O   1 
ATOM   2662  C CB  . PHE B 2 243 ? 4.807    -67.260  11.928  1.00 95.83  ? 245 PHE B CB  1 
ATOM   2663  C CG  . PHE B 2 243 ? 3.678    -66.878  11.009  1.00 95.68  ? 245 PHE B CG  1 
ATOM   2664  C CD1 . PHE B 2 243 ? 3.787    -65.783  10.165  1.00 99.26  ? 245 PHE B CD1 1 
ATOM   2665  C CD2 . PHE B 2 243 ? 2.525    -67.646  10.946  1.00 96.20  ? 245 PHE B CD2 1 
ATOM   2666  C CE1 . PHE B 2 243 ? 2.749    -65.446  9.299   1.00 99.50  ? 245 PHE B CE1 1 
ATOM   2667  C CE2 . PHE B 2 243 ? 1.491    -67.313  10.074  1.00 98.25  ? 245 PHE B CE2 1 
ATOM   2668  C CZ  . PHE B 2 243 ? 1.605    -66.210  9.263   1.00 97.17  ? 245 PHE B CZ  1 
ATOM   2669  N N   . GLU B 2 244 ? 5.017    -66.990  15.592  1.00 102.72 ? 246 GLU B N   1 
ATOM   2670  C CA  . GLU B 2 244 ? 5.462    -67.727  16.773  1.00 104.41 ? 246 GLU B CA  1 
ATOM   2671  C C   . GLU B 2 244 ? 4.519    -68.906  17.012  1.00 105.92 ? 246 GLU B C   1 
ATOM   2672  O O   . GLU B 2 244 ? 3.305    -68.711  17.002  1.00 105.04 ? 246 GLU B O   1 
ATOM   2673  C CB  . GLU B 2 244 ? 5.502    -66.796  17.990  1.00 110.30 ? 246 GLU B CB  1 
ATOM   2674  C CG  . GLU B 2 244 ? 6.495    -67.222  19.054  1.00 127.41 ? 246 GLU B CG  1 
ATOM   2675  C CD  . GLU B 2 244 ? 6.749    -66.184  20.132  1.00 171.00 ? 246 GLU B CD  1 
ATOM   2676  O OE1 . GLU B 2 244 ? 7.936    -65.939  20.446  1.00 182.56 ? 246 GLU B OE1 1 
ATOM   2677  O OE2 . GLU B 2 244 ? 5.768    -65.617  20.668  1.00 170.99 ? 246 GLU B OE2 1 
ATOM   2678  N N   . ALA B 2 245 ? 5.064    -70.132  17.189  1.00 101.30 ? 247 ALA B N   1 
ATOM   2679  C CA  . ALA B 2 245 ? 4.264    -71.345  17.423  1.00 99.44  ? 247 ALA B CA  1 
ATOM   2680  C C   . ALA B 2 245 ? 5.000    -72.468  18.138  1.00 103.74 ? 247 ALA B C   1 
ATOM   2681  O O   . ALA B 2 245 ? 6.196    -72.669  17.928  1.00 103.23 ? 247 ALA B O   1 
ATOM   2682  C CB  . ALA B 2 245 ? 3.695    -71.870  16.116  1.00 96.59  ? 247 ALA B CB  1 
ATOM   2683  N N   . THR B 2 246 ? 4.253    -73.216  18.965  1.00 101.52 ? 248 THR B N   1 
ATOM   2684  C CA  . THR B 2 246 ? 4.715    -74.392  19.712  1.00 103.30 ? 248 THR B CA  1 
ATOM   2685  C C   . THR B 2 246 ? 3.824    -75.598  19.368  1.00 105.72 ? 248 THR B C   1 
ATOM   2686  O O   . THR B 2 246 ? 3.924    -76.657  19.995  1.00 106.78 ? 248 THR B O   1 
ATOM   2687  C CB  . THR B 2 246 ? 4.779    -74.116  21.220  1.00 114.57 ? 248 THR B CB  1 
ATOM   2688  O OG1 . THR B 2 246 ? 3.525    -73.596  21.666  1.00 114.46 ? 248 THR B OG1 1 
ATOM   2689  C CG2 . THR B 2 246 ? 5.925    -73.191  21.604  1.00 115.00 ? 248 THR B CG2 1 
ATOM   2690  N N   . GLY B 2 247 ? 3.002    -75.423  18.334  1.00 99.59  ? 249 GLY B N   1 
ATOM   2691  C CA  . GLY B 2 247 ? 2.087    -76.431  17.819  1.00 97.90  ? 249 GLY B CA  1 
ATOM   2692  C C   . GLY B 2 247 ? 0.850    -75.841  17.178  1.00 100.48 ? 249 GLY B C   1 
ATOM   2693  O O   . GLY B 2 247 ? 0.588    -74.637  17.296  1.00 100.54 ? 249 GLY B O   1 
ATOM   2694  N N   . ASN B 2 248 ? 0.103    -76.701  16.454  1.00 95.14  ? 250 ASN B N   1 
ATOM   2695  C CA  . ASN B 2 248 ? -1.178   -76.440  15.786  1.00 93.31  ? 250 ASN B CA  1 
ATOM   2696  C C   . ASN B 2 248 ? -1.129   -75.485  14.593  1.00 94.37  ? 250 ASN B C   1 
ATOM   2697  O O   . ASN B 2 248 ? -2.122   -75.407  13.868  1.00 93.73  ? 250 ASN B O   1 
ATOM   2698  C CB  . ASN B 2 248 ? -2.224   -75.968  16.789  1.00 95.04  ? 250 ASN B CB  1 
ATOM   2699  C CG  . ASN B 2 248 ? -2.412   -76.959  17.902  1.00 123.52 ? 250 ASN B CG  1 
ATOM   2700  O OD1 . ASN B 2 248 ? -1.766   -76.885  18.953  1.00 120.60 ? 250 ASN B OD1 1 
ATOM   2701  N ND2 . ASN B 2 248 ? -3.225   -77.961  17.653  1.00 115.31 ? 250 ASN B ND2 1 
ATOM   2702  N N   . LEU B 2 249 ? -0.007   -74.785  14.362  1.00 89.02  ? 251 LEU B N   1 
ATOM   2703  C CA  . LEU B 2 249 ? 0.079    -73.853  13.236  1.00 86.75  ? 251 LEU B CA  1 
ATOM   2704  C C   . LEU B 2 249 ? 0.285    -74.576  11.922  1.00 89.61  ? 251 LEU B C   1 
ATOM   2705  O O   . LEU B 2 249 ? 1.047    -75.546  11.863  1.00 90.15  ? 251 LEU B O   1 
ATOM   2706  C CB  . LEU B 2 249 ? 1.159    -72.760  13.459  1.00 86.70  ? 251 LEU B CB  1 
ATOM   2707  C CG  . LEU B 2 249 ? 1.417    -71.704  12.353  1.00 88.25  ? 251 LEU B CG  1 
ATOM   2708  C CD1 . LEU B 2 249 ? 0.179    -70.874  12.042  1.00 88.08  ? 251 LEU B CD1 1 
ATOM   2709  C CD2 . LEU B 2 249 ? 2.536    -70.792  12.739  1.00 89.08  ? 251 LEU B CD2 1 
ATOM   2710  N N   . VAL B 2 250 ? -0.448   -74.110  10.887  1.00 84.45  ? 252 VAL B N   1 
ATOM   2711  C CA  . VAL B 2 250 ? -0.384   -74.544  9.493   1.00 83.15  ? 252 VAL B CA  1 
ATOM   2712  C C   . VAL B 2 250 ? 0.237    -73.326  8.769   1.00 86.66  ? 252 VAL B C   1 
ATOM   2713  O O   . VAL B 2 250 ? -0.466   -72.423  8.298   1.00 87.09  ? 252 VAL B O   1 
ATOM   2714  C CB  . VAL B 2 250 ? -1.759   -74.979  8.905   1.00 87.30  ? 252 VAL B CB  1 
ATOM   2715  C CG1 . VAL B 2 250 ? -1.593   -75.548  7.506   1.00 86.65  ? 252 VAL B CG1 1 
ATOM   2716  C CG2 . VAL B 2 250 ? -2.459   -75.992  9.803   1.00 88.02  ? 252 VAL B CG2 1 
ATOM   2717  N N   . VAL B 2 251 ? 1.577    -73.282  8.792   1.00 82.21  ? 253 VAL B N   1 
ATOM   2718  C CA  . VAL B 2 251 ? 2.443    -72.216  8.275   1.00 81.80  ? 253 VAL B CA  1 
ATOM   2719  C C   . VAL B 2 251 ? 2.219    -71.873  6.790   1.00 87.37  ? 253 VAL B C   1 
ATOM   2720  O O   . VAL B 2 251 ? 1.926    -72.780  6.013   1.00 87.41  ? 253 VAL B O   1 
ATOM   2721  C CB  . VAL B 2 251 ? 3.944    -72.528  8.543   1.00 85.25  ? 253 VAL B CB  1 
ATOM   2722  C CG1 . VAL B 2 251 ? 4.251    -72.592  10.032  1.00 85.96  ? 253 VAL B CG1 1 
ATOM   2723  C CG2 . VAL B 2 251 ? 4.401    -73.801  7.840   1.00 84.51  ? 253 VAL B CG2 1 
ATOM   2724  N N   . PRO B 2 252 ? 2.424    -70.609  6.345   1.00 85.29  ? 254 PRO B N   1 
ATOM   2725  C CA  . PRO B 2 252 ? 2.295    -70.317  4.907   1.00 85.78  ? 254 PRO B CA  1 
ATOM   2726  C C   . PRO B 2 252 ? 3.511    -70.792  4.095   1.00 89.63  ? 254 PRO B C   1 
ATOM   2727  O O   . PRO B 2 252 ? 4.639    -70.789  4.590   1.00 88.65  ? 254 PRO B O   1 
ATOM   2728  C CB  . PRO B 2 252 ? 2.176    -68.785  4.861   1.00 88.45  ? 254 PRO B CB  1 
ATOM   2729  C CG  . PRO B 2 252 ? 2.112    -68.331  6.298   1.00 92.51  ? 254 PRO B CG  1 
ATOM   2730  C CD  . PRO B 2 252 ? 2.772    -69.389  7.095   1.00 87.36  ? 254 PRO B CD  1 
ATOM   2731  N N   . ARG B 2 253 ? 3.266    -71.231  2.854   1.00 87.32  ? 255 ARG B N   1 
ATOM   2732  C CA  . ARG B 2 253 ? 4.302    -71.632  1.905   1.00 88.61  ? 255 ARG B CA  1 
ATOM   2733  C C   . ARG B 2 253 ? 4.323    -70.548  0.846   1.00 94.54  ? 255 ARG B C   1 
ATOM   2734  O O   . ARG B 2 253 ? 5.369    -69.949  0.620   1.00 95.52  ? 255 ARG B O   1 
ATOM   2735  C CB  . ARG B 2 253 ? 4.012    -73.000  1.261   1.00 90.23  ? 255 ARG B CB  1 
ATOM   2736  C CG  . ARG B 2 253 ? 5.158    -73.503  0.373   1.00 100.96 ? 255 ARG B CG  1 
ATOM   2737  C CD  . ARG B 2 253 ? 4.962    -74.935  -0.073  1.00 110.06 ? 255 ARG B CD  1 
ATOM   2738  N NE  . ARG B 2 253 ? 5.934    -75.320  -1.093  1.00 120.55 ? 255 ARG B NE  1 
ATOM   2739  C CZ  . ARG B 2 253 ? 5.799    -76.372  -1.895  1.00 143.81 ? 255 ARG B CZ  1 
ATOM   2740  N NH1 . ARG B 2 253 ? 4.729    -77.155  -1.803  1.00 127.84 ? 255 ARG B NH1 1 
ATOM   2741  N NH2 . ARG B 2 253 ? 6.728    -76.644  -2.804  1.00 141.72 ? 255 ARG B NH2 1 
ATOM   2742  N N   . TYR B 2 254 ? 3.158    -70.275  0.225   1.00 91.73  ? 256 TYR B N   1 
ATOM   2743  C CA  . TYR B 2 254 ? 3.010    -69.242  -0.791  1.00 93.86  ? 256 TYR B CA  1 
ATOM   2744  C C   . TYR B 2 254 ? 2.145    -68.085  -0.308  1.00 97.24  ? 256 TYR B C   1 
ATOM   2745  O O   . TYR B 2 254 ? 1.112    -68.308  0.325   1.00 95.74  ? 256 TYR B O   1 
ATOM   2746  C CB  . TYR B 2 254 ? 2.436    -69.816  -2.093  1.00 97.55  ? 256 TYR B CB  1 
ATOM   2747  C CG  . TYR B 2 254 ? 3.335    -70.820  -2.778  1.00 101.74 ? 256 TYR B CG  1 
ATOM   2748  C CD1 . TYR B 2 254 ? 3.178    -72.185  -2.563  1.00 103.49 ? 256 TYR B CD1 1 
ATOM   2749  C CD2 . TYR B 2 254 ? 4.308    -70.411  -3.684  1.00 105.16 ? 256 TYR B CD2 1 
ATOM   2750  C CE1 . TYR B 2 254 ? 3.986    -73.119  -3.213  1.00 106.43 ? 256 TYR B CE1 1 
ATOM   2751  C CE2 . TYR B 2 254 ? 5.118    -71.335  -4.345  1.00 107.81 ? 256 TYR B CE2 1 
ATOM   2752  C CZ  . TYR B 2 254 ? 4.959    -72.690  -4.100  1.00 115.12 ? 256 TYR B CZ  1 
ATOM   2753  O OH  . TYR B 2 254 ? 5.754    -73.611  -4.742  1.00 118.18 ? 256 TYR B OH  1 
ATOM   2754  N N   . ALA B 2 255 ? 2.578    -66.853  -0.607  1.00 95.68  ? 257 ALA B N   1 
ATOM   2755  C CA  . ALA B 2 255 ? 1.865    -65.611  -0.296  1.00 97.13  ? 257 ALA B CA  1 
ATOM   2756  C C   . ALA B 2 255 ? 1.592    -64.862  -1.601  1.00 105.74 ? 257 ALA B C   1 
ATOM   2757  O O   . ALA B 2 255 ? 2.105    -65.261  -2.651  1.00 106.61 ? 257 ALA B O   1 
ATOM   2758  C CB  . ALA B 2 255 ? 2.682    -64.749  0.649   1.00 97.96  ? 257 ALA B CB  1 
ATOM   2759  N N   . PHE B 2 256 ? 0.777    -63.793  -1.552  1.00 105.32 ? 258 PHE B N   1 
ATOM   2760  C CA  . PHE B 2 256 ? 0.431    -63.078  -2.772  1.00 108.90 ? 258 PHE B CA  1 
ATOM   2761  C C   . PHE B 2 256 ? 0.664    -61.580  -2.715  1.00 116.21 ? 258 PHE B C   1 
ATOM   2762  O O   . PHE B 2 256 ? -0.078   -60.848  -2.058  1.00 115.29 ? 258 PHE B O   1 
ATOM   2763  C CB  . PHE B 2 256 ? -1.011   -63.387  -3.197  1.00 111.81 ? 258 PHE B CB  1 
ATOM   2764  C CG  . PHE B 2 256 ? -1.392   -64.842  -3.084  1.00 111.64 ? 258 PHE B CG  1 
ATOM   2765  C CD1 . PHE B 2 256 ? -0.953   -65.769  -4.025  1.00 115.52 ? 258 PHE B CD1 1 
ATOM   2766  C CD2 . PHE B 2 256 ? -2.166   -65.291  -2.021  1.00 112.36 ? 258 PHE B CD2 1 
ATOM   2767  C CE1 . PHE B 2 256 ? -1.296   -67.115  -3.914  1.00 115.54 ? 258 PHE B CE1 1 
ATOM   2768  C CE2 . PHE B 2 256 ? -2.507   -66.636  -1.908  1.00 114.39 ? 258 PHE B CE2 1 
ATOM   2769  C CZ  . PHE B 2 256 ? -2.070   -67.540  -2.856  1.00 113.29 ? 258 PHE B CZ  1 
ATOM   2770  N N   . ALA B 2 257 ? 1.687    -61.126  -3.439  1.00 117.44 ? 259 ALA B N   1 
ATOM   2771  C CA  . ALA B 2 257 ? 2.002    -59.712  -3.572  1.00 121.83 ? 259 ALA B CA  1 
ATOM   2772  C C   . ALA B 2 257 ? 1.106    -59.219  -4.715  1.00 132.23 ? 259 ALA B C   1 
ATOM   2773  O O   . ALA B 2 257 ? 1.224    -59.687  -5.851  1.00 133.53 ? 259 ALA B O   1 
ATOM   2774  C CB  . ALA B 2 257 ? 3.474    -59.533  -3.912  1.00 123.82 ? 259 ALA B CB  1 
ATOM   2775  N N   . MET B 2 258 ? 0.149    -58.348  -4.390  1.00 132.28 ? 260 MET B N   1 
ATOM   2776  C CA  . MET B 2 258 ? -0.834   -57.867  -5.356  1.00 136.51 ? 260 MET B CA  1 
ATOM   2777  C C   . MET B 2 258 ? -0.897   -56.354  -5.510  1.00 146.63 ? 260 MET B C   1 
ATOM   2778  O O   . MET B 2 258 ? -0.634   -55.611  -4.563  1.00 146.09 ? 260 MET B O   1 
ATOM   2779  C CB  . MET B 2 258 ? -2.230   -58.427  -5.013  1.00 137.84 ? 260 MET B CB  1 
ATOM   2780  C CG  . MET B 2 258 ? -2.716   -58.053  -3.617  1.00 139.97 ? 260 MET B CG  1 
ATOM   2781  S SD  . MET B 2 258 ? -4.440   -58.472  -3.312  1.00 144.50 ? 260 MET B SD  1 
ATOM   2782  C CE  . MET B 2 258 ? -4.271   -60.153  -2.798  1.00 136.60 ? 260 MET B CE  1 
ATOM   2783  N N   . GLU B 2 259 ? -1.289   -55.908  -6.709  1.00 122.56 ? 261 GLU B N   1 
ATOM   2784  C CA  . GLU B 2 259 ? -1.503   -54.503  -7.017  1.00 123.51 ? 261 GLU B CA  1 
ATOM   2785  C C   . GLU B 2 259 ? -3.001   -54.340  -7.229  1.00 129.46 ? 261 GLU B C   1 
ATOM   2786  O O   . GLU B 2 259 ? -3.591   -55.017  -8.074  1.00 128.13 ? 261 GLU B O   1 
ATOM   2787  C CB  . GLU B 2 259 ? -0.706   -54.051  -8.248  1.00 125.25 ? 261 GLU B CB  1 
ATOM   2788  C CG  . GLU B 2 259 ? -0.398   -52.565  -8.212  1.00 137.96 ? 261 GLU B CG  1 
ATOM   2789  C CD  . GLU B 2 259 ? -0.343   -51.879  -9.561  1.00 164.71 ? 261 GLU B CD  1 
ATOM   2790  O OE1 . GLU B 2 259 ? 0.568    -52.205  -10.356 1.00 170.38 ? 261 GLU B OE1 1 
ATOM   2791  O OE2 . GLU B 2 259 ? -1.190   -50.989  -9.808  1.00 153.54 ? 261 GLU B OE2 1 
ATOM   2792  N N   . ARG B 2 260 ? -3.622   -53.496  -6.409  1.00 129.05 ? 262 ARG B N   1 
ATOM   2793  C CA  . ARG B 2 260 ? -5.059   -53.273  -6.460  1.00 130.41 ? 262 ARG B CA  1 
ATOM   2794  C C   . ARG B 2 260 ? -5.474   -52.338  -7.587  1.00 136.30 ? 262 ARG B C   1 
ATOM   2795  O O   . ARG B 2 260 ? -4.815   -51.327  -7.842  1.00 136.46 ? 262 ARG B O   1 
ATOM   2796  C CB  . ARG B 2 260 ? -5.600   -52.787  -5.102  1.00 131.53 ? 262 ARG B CB  1 
ATOM   2797  C CG  . ARG B 2 260 ? -5.552   -53.848  -3.998  1.00 141.36 ? 262 ARG B CG  1 
ATOM   2798  C CD  . ARG B 2 260 ? -6.781   -53.806  -3.108  1.00 147.46 ? 262 ARG B CD  1 
ATOM   2799  N NE  . ARG B 2 260 ? -6.466   -53.440  -1.727  1.00 152.09 ? 262 ARG B NE  1 
ATOM   2800  C CZ  . ARG B 2 260 ? -6.161   -54.309  -0.769  1.00 165.95 ? 262 ARG B CZ  1 
ATOM   2801  N NH1 . ARG B 2 260 ? -6.092   -55.607  -1.037  1.00 156.01 ? 262 ARG B NH1 1 
ATOM   2802  N NH2 . ARG B 2 260 ? -5.905   -53.885  0.462   1.00 151.11 ? 262 ARG B NH2 1 
ATOM   2803  N N   . ASN B 2 261 ? -6.567   -52.704  -8.268  1.00 133.36 ? 263 ASN B N   1 
ATOM   2804  C CA  . ASN B 2 261 ? -7.202   -51.941  -9.338  1.00 133.75 ? 263 ASN B CA  1 
ATOM   2805  C C   . ASN B 2 261 ? -8.352   -51.173  -8.679  1.00 137.67 ? 263 ASN B C   1 
ATOM   2806  O O   . ASN B 2 261 ? -8.486   -51.213  -7.456  1.00 136.37 ? 263 ASN B O   1 
ATOM   2807  C CB  . ASN B 2 261 ? -7.739   -52.901  -10.410 1.00 135.48 ? 263 ASN B CB  1 
ATOM   2808  C CG  . ASN B 2 261 ? -8.071   -52.248  -11.729 1.00 166.16 ? 263 ASN B CG  1 
ATOM   2809  O OD1 . ASN B 2 261 ? -7.192   -51.801  -12.475 1.00 163.33 ? 263 ASN B OD1 1 
ATOM   2810  N ND2 . ASN B 2 261 ? -9.354   -52.190  -12.052 1.00 159.34 ? 263 ASN B ND2 1 
ATOM   2811  N N   . ALA B 2 262 ? -9.160   -50.464  -9.464  1.00 135.83 ? 264 ALA B N   1 
ATOM   2812  C CA  . ALA B 2 262 ? -10.302  -49.738  -8.939  1.00 136.60 ? 264 ALA B CA  1 
ATOM   2813  C C   . ALA B 2 262 ? -11.576  -50.448  -9.402  1.00 142.11 ? 264 ALA B C   1 
ATOM   2814  O O   . ALA B 2 262 ? -12.256  -51.075  -8.584  1.00 140.83 ? 264 ALA B O   1 
ATOM   2815  C CB  . ALA B 2 262 ? -10.272  -48.290  -9.413  1.00 138.06 ? 264 ALA B CB  1 
ATOM   2816  N N   . GLY B 2 263 ? -11.825  -50.412  -10.715 1.00 141.11 ? 265 GLY B N   1 
ATOM   2817  C CA  . GLY B 2 263 ? -12.987  -51.010  -11.365 1.00 142.17 ? 265 GLY B CA  1 
ATOM   2818  C C   . GLY B 2 263 ? -12.914  -52.510  -11.567 1.00 146.80 ? 265 GLY B C   1 
ATOM   2819  O O   . GLY B 2 263 ? -12.928  -52.987  -12.706 1.00 147.34 ? 265 GLY B O   1 
ATOM   2820  N N   . SER B 2 264 ? -12.844  -53.261  -10.454 1.00 142.56 ? 266 SER B N   1 
ATOM   2821  C CA  . SER B 2 264 ? -12.811  -54.725  -10.428 1.00 141.78 ? 266 SER B CA  1 
ATOM   2822  C C   . SER B 2 264 ? -13.718  -55.211  -9.294  1.00 144.23 ? 266 SER B C   1 
ATOM   2823  O O   . SER B 2 264 ? -13.851  -54.531  -8.267  1.00 143.76 ? 266 SER B O   1 
ATOM   2824  C CB  . SER B 2 264 ? -11.388  -55.245  -10.230 1.00 144.59 ? 266 SER B CB  1 
ATOM   2825  O OG  . SER B 2 264 ? -10.469  -54.722  -11.174 1.00 153.82 ? 266 SER B OG  1 
ATOM   2826  N N   . GLY B 2 265 A -14.332  -56.372  -9.500  1.00 139.44 ? 266 GLY B N   1 
ATOM   2827  C CA  . GLY B 2 265 A -15.237  -56.981  -8.531  1.00 138.17 ? 266 GLY B CA  1 
ATOM   2828  C C   . GLY B 2 265 A -15.364  -58.483  -8.671  1.00 139.48 ? 266 GLY B C   1 
ATOM   2829  O O   . GLY B 2 265 A -14.521  -59.129  -9.304  1.00 139.03 ? 266 GLY B O   1 
ATOM   2830  N N   . ILE B 2 266 ? -16.416  -59.046  -8.053  1.00 134.13 ? 267 ILE B N   1 
ATOM   2831  C CA  . ILE B 2 266 ? -16.699  -60.480  -8.073  1.00 133.28 ? 267 ILE B CA  1 
ATOM   2832  C C   . ILE B 2 266 ? -18.133  -60.743  -8.528  1.00 138.26 ? 267 ILE B C   1 
ATOM   2833  O O   . ILE B 2 266 ? -19.086  -60.296  -7.890  1.00 138.13 ? 267 ILE B O   1 
ATOM   2834  C CB  . ILE B 2 266 ? -16.358  -61.174  -6.722  1.00 135.16 ? 267 ILE B CB  1 
ATOM   2835  C CG1 . ILE B 2 266 ? -14.855  -61.064  -6.399  1.00 134.61 ? 267 ILE B CG1 1 
ATOM   2836  C CG2 . ILE B 2 266 ? -16.807  -62.643  -6.715  1.00 135.96 ? 267 ILE B CG2 1 
ATOM   2837  C CD1 . ILE B 2 266 ? -14.556  -60.817  -4.984  1.00 137.33 ? 267 ILE B CD1 1 
ATOM   2838  N N   . ILE B 2 267 ? -18.270  -61.481  -9.630  1.00 135.79 ? 268 ILE B N   1 
ATOM   2839  C CA  . ILE B 2 267 ? -19.556  -61.863  -10.201 1.00 136.56 ? 268 ILE B CA  1 
ATOM   2840  C C   . ILE B 2 267 ? -19.840  -63.329  -9.849  1.00 141.68 ? 268 ILE B C   1 
ATOM   2841  O O   . ILE B 2 267 ? -18.987  -64.186  -10.087 1.00 141.81 ? 268 ILE B O   1 
ATOM   2842  C CB  . ILE B 2 267 ? -19.552  -61.595  -11.739 1.00 140.45 ? 268 ILE B CB  1 
ATOM   2843  C CG1 . ILE B 2 267 ? -19.737  -60.088  -12.029 1.00 140.78 ? 268 ILE B CG1 1 
ATOM   2844  C CG2 . ILE B 2 267 ? -20.601  -62.449  -12.486 1.00 142.21 ? 268 ILE B CG2 1 
ATOM   2845  C CD1 . ILE B 2 267 ? -19.543  -59.651  -13.492 1.00 149.25 ? 268 ILE B CD1 1 
ATOM   2846  N N   . ILE B 2 268 ? -21.023  -63.618  -9.276  1.00 138.72 ? 269 ILE B N   1 
ATOM   2847  C CA  . ILE B 2 268 ? -21.417  -64.998  -8.980  1.00 138.99 ? 269 ILE B CA  1 
ATOM   2848  C C   . ILE B 2 268 ? -22.579  -65.333  -9.930  1.00 144.80 ? 269 ILE B C   1 
ATOM   2849  O O   . ILE B 2 268 ? -23.742  -65.073  -9.603  1.00 144.98 ? 269 ILE B O   1 
ATOM   2850  C CB  . ILE B 2 268 ? -21.709  -65.301  -7.473  1.00 141.32 ? 269 ILE B CB  1 
ATOM   2851  C CG1 . ILE B 2 268 ? -20.689  -64.636  -6.528  1.00 141.09 ? 269 ILE B CG1 1 
ATOM   2852  C CG2 . ILE B 2 268 ? -21.759  -66.808  -7.218  1.00 141.90 ? 269 ILE B CG2 1 
ATOM   2853  C CD1 . ILE B 2 268 ? -21.230  -63.447  -5.777  1.00 149.52 ? 269 ILE B CD1 1 
ATOM   2854  N N   . SER B 2 269 ? -22.248  -65.828  -11.145 1.00 142.18 ? 270 SER B N   1 
ATOM   2855  C CA  . SER B 2 269 ? -23.235  -66.140  -12.185 1.00 143.16 ? 270 SER B CA  1 
ATOM   2856  C C   . SER B 2 269 ? -22.851  -67.342  -13.032 1.00 148.10 ? 270 SER B C   1 
ATOM   2857  O O   . SER B 2 269 ? -21.669  -67.551  -13.324 1.00 147.04 ? 270 SER B O   1 
ATOM   2858  C CB  . SER B 2 269 ? -23.475  -64.927  -13.088 1.00 147.01 ? 270 SER B CB  1 
ATOM   2859  O OG  . SER B 2 269 ? -24.552  -65.147  -13.985 1.00 156.60 ? 270 SER B OG  1 
ATOM   2860  N N   . ASP B 2 270 ? -23.873  -68.111  -13.452 1.00 146.62 ? 271 ASP B N   1 
ATOM   2861  C CA  . ASP B 2 270 ? -23.735  -69.296  -14.298 1.00 148.17 ? 271 ASP B CA  1 
ATOM   2862  C C   . ASP B 2 270 ? -23.777  -68.955  -15.811 1.00 154.23 ? 271 ASP B C   1 
ATOM   2863  O O   . ASP B 2 270 ? -23.637  -69.864  -16.636 1.00 155.53 ? 271 ASP B O   1 
ATOM   2864  C CB  . ASP B 2 270 ? -24.785  -70.369  -13.922 1.00 150.35 ? 271 ASP B CB  1 
ATOM   2865  C CG  . ASP B 2 270 ? -24.225  -71.624  -13.253 1.00 160.39 ? 271 ASP B CG  1 
ATOM   2866  O OD1 . ASP B 2 270 ? -23.403  -72.327  -13.890 1.00 161.63 ? 271 ASP B OD1 1 
ATOM   2867  O OD2 . ASP B 2 270 ? -24.670  -71.949  -12.129 1.00 165.07 ? 271 ASP B OD2 1 
ATOM   2868  N N   . THR B 2 271 ? -23.932  -67.647  -16.170 1.00 150.24 ? 272 THR B N   1 
ATOM   2869  C CA  . THR B 2 271 ? -23.964  -67.157  -17.563 1.00 150.97 ? 272 THR B CA  1 
ATOM   2870  C C   . THR B 2 271 ? -22.620  -67.438  -18.296 1.00 155.86 ? 272 THR B C   1 
ATOM   2871  O O   . THR B 2 271 ? -21.581  -67.481  -17.634 1.00 154.18 ? 272 THR B O   1 
ATOM   2872  C CB  . THR B 2 271 ? -24.412  -65.678  -17.640 1.00 150.66 ? 272 THR B CB  1 
ATOM   2873  O OG1 . THR B 2 271 ? -23.598  -64.866  -16.798 1.00 144.29 ? 272 THR B OG1 1 
ATOM   2874  C CG2 . THR B 2 271 ? -25.878  -65.488  -17.285 1.00 147.54 ? 272 THR B CG2 1 
ATOM   2875  N N   . PRO B 2 272 ? -22.604  -67.689  -19.632 1.00 154.72 ? 273 PRO B N   1 
ATOM   2876  C CA  . PRO B 2 272 ? -21.327  -68.009  -20.298 1.00 155.09 ? 273 PRO B CA  1 
ATOM   2877  C C   . PRO B 2 272 ? -20.373  -66.826  -20.461 1.00 157.27 ? 273 PRO B C   1 
ATOM   2878  O O   . PRO B 2 272 ? -20.769  -65.682  -20.255 1.00 156.92 ? 273 PRO B O   1 
ATOM   2879  C CB  . PRO B 2 272 ? -21.772  -68.561  -21.653 1.00 159.44 ? 273 PRO B CB  1 
ATOM   2880  C CG  . PRO B 2 272 ? -23.055  -67.861  -21.928 1.00 164.62 ? 273 PRO B CG  1 
ATOM   2881  C CD  . PRO B 2 272 ? -23.730  -67.722  -20.593 1.00 158.29 ? 273 PRO B CD  1 
ATOM   2882  N N   . VAL B 2 273 ? -19.123  -67.113  -20.850 1.00 152.33 ? 274 VAL B N   1 
ATOM   2883  C CA  . VAL B 2 273 ? -18.079  -66.114  -21.074 1.00 151.10 ? 274 VAL B CA  1 
ATOM   2884  C C   . VAL B 2 273 ? -17.503  -66.294  -22.482 1.00 159.04 ? 274 VAL B C   1 
ATOM   2885  O O   . VAL B 2 273 ? -17.055  -67.390  -22.824 1.00 159.61 ? 274 VAL B O   1 
ATOM   2886  C CB  . VAL B 2 273 ? -17.014  -66.105  -19.938 1.00 151.85 ? 274 VAL B CB  1 
ATOM   2887  C CG1 . VAL B 2 273 ? -16.666  -67.516  -19.477 1.00 151.25 ? 274 VAL B CG1 1 
ATOM   2888  C CG2 . VAL B 2 273 ? -15.757  -65.334  -20.330 1.00 151.34 ? 274 VAL B CG2 1 
ATOM   2889  N N   . HIS B 2 274 ? -17.555  -65.225  -23.303 1.00 158.18 ? 275 HIS B N   1 
ATOM   2890  C CA  . HIS B 2 274 ? -17.077  -65.230  -24.691 1.00 161.03 ? 275 HIS B CA  1 
ATOM   2891  C C   . HIS B 2 274 ? -15.915  -64.260  -24.946 1.00 166.73 ? 275 HIS B C   1 
ATOM   2892  O O   . HIS B 2 274 ? -15.565  -63.470  -24.067 1.00 164.58 ? 275 HIS B O   1 
ATOM   2893  C CB  . HIS B 2 274 ? -18.244  -64.986  -25.662 1.00 163.79 ? 275 HIS B CB  1 
ATOM   2894  C CG  . HIS B 2 274 ? -19.195  -66.139  -25.727 1.00 168.14 ? 275 HIS B CG  1 
ATOM   2895  N ND1 . HIS B 2 274 ? -20.119  -66.367  -24.722 1.00 168.56 ? 275 HIS B ND1 1 
ATOM   2896  C CD2 . HIS B 2 274 ? -19.305  -67.118  -26.655 1.00 172.00 ? 275 HIS B CD2 1 
ATOM   2897  C CE1 . HIS B 2 274 ? -20.772  -67.461  -25.079 1.00 169.27 ? 275 HIS B CE1 1 
ATOM   2898  N NE2 . HIS B 2 274 ? -20.315  -67.951  -26.233 1.00 171.73 ? 275 HIS B NE2 1 
ATOM   2899  N N   . ASP B 2 275 ? -15.318  -64.326  -26.154 1.00 166.92 ? 276 ASP B N   1 
ATOM   2900  C CA  . ASP B 2 275 ? -14.166  -63.512  -26.558 1.00 167.61 ? 276 ASP B CA  1 
ATOM   2901  C C   . ASP B 2 275 ? -14.474  -62.014  -26.778 1.00 172.85 ? 276 ASP B C   1 
ATOM   2902  O O   . ASP B 2 275 ? -13.540  -61.242  -27.014 1.00 172.49 ? 276 ASP B O   1 
ATOM   2903  C CB  . ASP B 2 275 ? -13.482  -64.117  -27.798 1.00 171.79 ? 276 ASP B CB  1 
ATOM   2904  C CG  . ASP B 2 275 ? -11.986  -63.876  -27.850 1.00 181.93 ? 276 ASP B CG  1 
ATOM   2905  O OD1 . ASP B 2 275 ? -11.536  -63.133  -28.754 1.00 183.73 ? 276 ASP B OD1 1 
ATOM   2906  O OD2 . ASP B 2 275 ? -11.263  -64.435  -26.991 1.00 185.53 ? 276 ASP B OD2 1 
ATOM   2907  N N   . CYS B 2 276 ? -15.759  -61.598  -26.669 1.00 169.80 ? 277 CYS B N   1 
ATOM   2908  C CA  . CYS B 2 276 ? -16.207  -60.202  -26.819 1.00 169.37 ? 277 CYS B CA  1 
ATOM   2909  C C   . CYS B 2 276 ? -15.543  -59.243  -25.805 1.00 167.53 ? 277 CYS B C   1 
ATOM   2910  O O   . CYS B 2 276 ? -15.018  -59.684  -24.780 1.00 165.26 ? 277 CYS B O   1 
ATOM   2911  C CB  . CYS B 2 276 ? -17.733  -60.107  -26.757 1.00 170.74 ? 277 CYS B CB  1 
ATOM   2912  S SG  . CYS B 2 276 ? -18.488  -61.029  -25.383 1.00 173.19 ? 277 CYS B SG  1 
ATOM   2913  N N   . ASN B 2 277 ? -15.566  -57.933  -26.107 1.00 161.47 ? 278 ASN B N   1 
ATOM   2914  C CA  . ASN B 2 277 ? -15.049  -56.878  -25.235 1.00 158.21 ? 278 ASN B CA  1 
ATOM   2915  C C   . ASN B 2 277 ? -16.237  -56.074  -24.714 1.00 158.28 ? 278 ASN B C   1 
ATOM   2916  O O   . ASN B 2 277 ? -17.274  -56.016  -25.382 1.00 159.39 ? 278 ASN B O   1 
ATOM   2917  C CB  . ASN B 2 277 ? -14.115  -55.934  -26.003 1.00 160.81 ? 278 ASN B CB  1 
ATOM   2918  C CG  . ASN B 2 277 ? -12.858  -56.543  -26.574 1.00 194.31 ? 278 ASN B CG  1 
ATOM   2919  O OD1 . ASN B 2 277 ? -12.237  -57.436  -25.971 1.00 189.45 ? 278 ASN B OD1 1 
ATOM   2920  N ND2 . ASN B 2 277 ? -12.472  -55.998  -27.753 1.00 192.22 ? 278 ASN B ND2 1 
ATOM   2921  N N   . THR B 2 278 ? -16.091  -55.438  -23.542 1.00 150.68 ? 279 THR B N   1 
ATOM   2922  C CA  . THR B 2 278 ? -17.156  -54.610  -22.969 1.00 149.12 ? 279 THR B CA  1 
ATOM   2923  C C   . THR B 2 278 ? -16.606  -53.509  -22.051 1.00 150.29 ? 279 THR B C   1 
ATOM   2924  O O   . THR B 2 278 ? -15.545  -53.676  -21.447 1.00 148.99 ? 279 THR B O   1 
ATOM   2925  C CB  . THR B 2 278 ? -18.242  -55.470  -22.292 1.00 153.84 ? 279 THR B CB  1 
ATOM   2926  O OG1 . THR B 2 278 ? -19.393  -54.662  -22.055 1.00 153.39 ? 279 THR B OG1 1 
ATOM   2927  C CG2 . THR B 2 278 ? -17.774  -56.138  -20.996 1.00 149.97 ? 279 THR B CG2 1 
ATOM   2928  N N   . THR B 2 279 ? -17.337  -52.385  -21.960 1.00 145.83 ? 280 THR B N   1 
ATOM   2929  C CA  . THR B 2 279 ? -17.002  -51.243  -21.104 1.00 144.23 ? 280 THR B CA  1 
ATOM   2930  C C   . THR B 2 279 ? -17.664  -51.453  -19.748 1.00 145.38 ? 280 THR B C   1 
ATOM   2931  O O   . THR B 2 279 ? -17.097  -51.094  -18.713 1.00 143.47 ? 280 THR B O   1 
ATOM   2932  C CB  . THR B 2 279 ? -17.497  -49.925  -21.724 1.00 156.64 ? 280 THR B CB  1 
ATOM   2933  O OG1 . THR B 2 279 ? -18.908  -49.995  -21.951 1.00 158.58 ? 280 THR B OG1 1 
ATOM   2934  C CG2 . THR B 2 279 ? -16.766  -49.561  -23.008 1.00 157.71 ? 280 THR B CG2 1 
ATOM   2935  N N   . CYS B 2 280 ? -18.876  -52.036  -19.773 1.00 141.52 ? 281 CYS B N   1 
ATOM   2936  C CA  . CYS B 2 280 ? -19.705  -52.321  -18.612 1.00 139.99 ? 281 CYS B CA  1 
ATOM   2937  C C   . CYS B 2 280 ? -20.101  -53.801  -18.568 1.00 138.85 ? 281 CYS B C   1 
ATOM   2938  O O   . CYS B 2 280 ? -20.540  -54.351  -19.580 1.00 139.40 ? 281 CYS B O   1 
ATOM   2939  C CB  . CYS B 2 280 ? -20.930  -51.412  -18.607 1.00 142.14 ? 281 CYS B CB  1 
ATOM   2940  S SG  . CYS B 2 280 ? -21.958  -51.558  -17.124 1.00 145.23 ? 281 CYS B SG  1 
ATOM   2941  N N   . GLN B 2 281 ? -19.952  -54.434  -17.392 1.00 130.30 ? 282 GLN B N   1 
ATOM   2942  C CA  . GLN B 2 281 ? -20.257  -55.846  -17.201 1.00 128.41 ? 282 GLN B CA  1 
ATOM   2943  C C   . GLN B 2 281 ? -21.117  -56.093  -15.962 1.00 130.42 ? 282 GLN B C   1 
ATOM   2944  O O   . GLN B 2 281 ? -20.807  -55.583  -14.887 1.00 128.65 ? 282 GLN B O   1 
ATOM   2945  C CB  . GLN B 2 281 ? -18.947  -56.653  -17.146 1.00 128.68 ? 282 GLN B CB  1 
ATOM   2946  C CG  . GLN B 2 281 ? -19.112  -58.169  -17.050 1.00 141.27 ? 282 GLN B CG  1 
ATOM   2947  C CD  . GLN B 2 281 ? -19.770  -58.760  -18.266 1.00 167.20 ? 282 GLN B CD  1 
ATOM   2948  O OE1 . GLN B 2 281 ? -19.159  -58.905  -19.327 1.00 165.99 ? 282 GLN B OE1 1 
ATOM   2949  N NE2 . GLN B 2 281 ? -21.040  -59.105  -18.136 1.00 161.88 ? 282 GLN B NE2 1 
ATOM   2950  N N   . THR B 2 282 ? -22.207  -56.872  -16.124 1.00 127.78 ? 283 THR B N   1 
ATOM   2951  C CA  . THR B 2 282 ? -23.136  -57.256  -15.045 1.00 127.16 ? 283 THR B CA  1 
ATOM   2952  C C   . THR B 2 282 ? -23.313  -58.785  -15.016 1.00 132.84 ? 283 THR B C   1 
ATOM   2953  O O   . THR B 2 282 ? -23.213  -59.392  -16.086 1.00 134.13 ? 283 THR B O   1 
ATOM   2954  C CB  . THR B 2 282 ? -24.521  -56.576  -15.184 1.00 132.75 ? 283 THR B CB  1 
ATOM   2955  O OG1 . THR B 2 282 ? -25.336  -57.267  -16.131 1.00 130.24 ? 283 THR B OG1 1 
ATOM   2956  C CG2 . THR B 2 282 ? -24.442  -55.098  -15.493 1.00 132.76 ? 283 THR B CG2 1 
ATOM   2957  N N   . PRO B 2 283 ? -23.651  -59.423  -13.854 1.00 128.99 ? 284 PRO B N   1 
ATOM   2958  C CA  . PRO B 2 283 ? -23.852  -60.892  -13.835 1.00 129.09 ? 284 PRO B CA  1 
ATOM   2959  C C   . PRO B 2 283 ? -24.907  -61.430  -14.812 1.00 134.67 ? 284 PRO B C   1 
ATOM   2960  O O   . PRO B 2 283 ? -24.816  -62.585  -15.240 1.00 135.23 ? 284 PRO B O   1 
ATOM   2961  C CB  . PRO B 2 283 ? -24.223  -61.179  -12.376 1.00 129.59 ? 284 PRO B CB  1 
ATOM   2962  C CG  . PRO B 2 283 ? -23.628  -60.056  -11.612 1.00 133.08 ? 284 PRO B CG  1 
ATOM   2963  C CD  . PRO B 2 283 ? -23.804  -58.861  -12.498 1.00 129.38 ? 284 PRO B CD  1 
ATOM   2964  N N   . LYS B 2 284 ? -25.890  -60.586  -15.176 1.00 131.23 ? 285 LYS B N   1 
ATOM   2965  C CA  . LYS B 2 284 ? -26.947  -60.883  -16.141 1.00 132.36 ? 285 LYS B CA  1 
ATOM   2966  C C   . LYS B 2 284 ? -26.365  -60.890  -17.570 1.00 138.73 ? 285 LYS B C   1 
ATOM   2967  O O   . LYS B 2 284 ? -26.812  -61.676  -18.408 1.00 139.72 ? 285 LYS B O   1 
ATOM   2968  C CB  . LYS B 2 284 ? -28.070  -59.834  -16.021 1.00 134.83 ? 285 LYS B CB  1 
ATOM   2969  C CG  . LYS B 2 284 ? -29.461  -60.380  -16.288 1.00 147.47 ? 285 LYS B CG  1 
ATOM   2970  C CD  . LYS B 2 284 ? -30.524  -59.360  -15.938 1.00 153.73 ? 285 LYS B CD  1 
ATOM   2971  C CE  . LYS B 2 284 ? -31.911  -59.876  -16.206 1.00 162.45 ? 285 LYS B CE  1 
ATOM   2972  N NZ  . LYS B 2 284 ? -32.953  -58.930  -15.733 1.00 170.36 ? 285 LYS B NZ  1 
ATOM   2973  N N   . GLY B 2 285 ? -25.376  -60.023  -17.817 1.00 135.78 ? 286 GLY B N   1 
ATOM   2974  C CA  . GLY B 2 285 ? -24.690  -59.877  -19.100 1.00 136.87 ? 286 GLY B CA  1 
ATOM   2975  C C   . GLY B 2 285 ? -24.036  -58.523  -19.315 1.00 140.84 ? 286 GLY B C   1 
ATOM   2976  O O   . GLY B 2 285 ? -24.275  -57.586  -18.551 1.00 139.72 ? 286 GLY B O   1 
ATOM   2977  N N   . ALA B 2 286 ? -23.204  -58.407  -20.363 1.00 138.73 ? 287 ALA B N   1 
ATOM   2978  C CA  . ALA B 2 286 ? -22.466  -57.178  -20.683 1.00 139.22 ? 287 ALA B CA  1 
ATOM   2979  C C   . ALA B 2 286 ? -23.331  -56.061  -21.276 1.00 146.25 ? 287 ALA B C   1 
ATOM   2980  O O   . ALA B 2 286 ? -24.370  -56.338  -21.875 1.00 147.31 ? 287 ALA B O   1 
ATOM   2981  C CB  . ALA B 2 286 ? -21.314  -57.500  -21.620 1.00 140.73 ? 287 ALA B CB  1 
ATOM   2982  N N   . ILE B 2 287 ? -22.903  -54.789  -21.093 1.00 143.66 ? 288 ILE B N   1 
ATOM   2983  C CA  . ILE B 2 287 ? -23.598  -53.607  -21.629 1.00 144.89 ? 288 ILE B CA  1 
ATOM   2984  C C   . ILE B 2 287 ? -22.643  -52.667  -22.368 1.00 150.17 ? 288 ILE B C   1 
ATOM   2985  O O   . ILE B 2 287 ? -21.571  -52.347  -21.853 1.00 148.77 ? 288 ILE B O   1 
ATOM   2986  C CB  . ILE B 2 287 ? -24.439  -52.795  -20.600 1.00 147.07 ? 288 ILE B CB  1 
ATOM   2987  C CG1 . ILE B 2 287 ? -24.814  -53.603  -19.331 1.00 145.35 ? 288 ILE B CG1 1 
ATOM   2988  C CG2 . ILE B 2 287 ? -25.675  -52.205  -21.291 1.00 150.00 ? 288 ILE B CG2 1 
ATOM   2989  C CD1 . ILE B 2 287 ? -25.191  -52.752  -18.163 1.00 146.91 ? 288 ILE B CD1 1 
ATOM   2990  N N   . ASN B 2 288 ? -23.057  -52.195  -23.553 1.00 148.99 ? 289 ASN B N   1 
ATOM   2991  C CA  . ASN B 2 288 ? -22.310  -51.232  -24.364 1.00 149.99 ? 289 ASN B CA  1 
ATOM   2992  C C   . ASN B 2 288 ? -23.277  -50.093  -24.677 1.00 155.95 ? 289 ASN B C   1 
ATOM   2993  O O   . ASN B 2 288 ? -23.962  -50.119  -25.709 1.00 157.62 ? 289 ASN B O   1 
ATOM   2994  C CB  . ASN B 2 288 ? -21.752  -51.884  -25.645 1.00 152.25 ? 289 ASN B CB  1 
ATOM   2995  C CG  . ASN B 2 288 ? -20.900  -50.971  -26.511 1.00 173.96 ? 289 ASN B CG  1 
ATOM   2996  O OD1 . ASN B 2 288 ? -20.094  -50.168  -26.024 1.00 167.50 ? 289 ASN B OD1 1 
ATOM   2997  N ND2 . ASN B 2 288 ? -21.037  -51.095  -27.826 1.00 166.09 ? 289 ASN B ND2 1 
ATOM   2998  N N   . THR B 2 289 ? -23.381  -49.125  -23.741 1.00 151.77 ? 290 THR B N   1 
ATOM   2999  C CA  . THR B 2 289 ? -24.302  -47.989  -23.862 1.00 152.43 ? 290 THR B CA  1 
ATOM   3000  C C   . THR B 2 289 ? -23.710  -46.639  -23.415 1.00 156.04 ? 290 THR B C   1 
ATOM   3001  O O   . THR B 2 289 ? -22.809  -46.584  -22.571 1.00 154.42 ? 290 THR B O   1 
ATOM   3002  C CB  . THR B 2 289 ? -25.630  -48.287  -23.142 1.00 156.98 ? 290 THR B CB  1 
ATOM   3003  O OG1 . THR B 2 289 ? -26.566  -47.260  -23.460 1.00 155.92 ? 290 THR B OG1 1 
ATOM   3004  C CG2 . THR B 2 289 ? -25.483  -48.413  -21.624 1.00 153.50 ? 290 THR B CG2 1 
ATOM   3005  N N   . SER B 2 290 ? -24.261  -45.555  -23.984 1.00 153.58 ? 291 SER B N   1 
ATOM   3006  C CA  . SER B 2 290 ? -23.908  -44.166  -23.696 1.00 153.14 ? 291 SER B CA  1 
ATOM   3007  C C   . SER B 2 290 ? -24.899  -43.579  -22.682 1.00 156.97 ? 291 SER B C   1 
ATOM   3008  O O   . SER B 2 290 ? -24.670  -42.492  -22.142 1.00 156.51 ? 291 SER B O   1 
ATOM   3009  C CB  . SER B 2 290 ? -23.907  -43.342  -24.983 1.00 158.14 ? 291 SER B CB  1 
ATOM   3010  O OG  . SER B 2 290 ? -25.050  -43.587  -25.786 1.00 167.05 ? 291 SER B OG  1 
ATOM   3011  N N   . LEU B 2 291 ? -25.991  -44.323  -22.418 1.00 153.37 ? 292 LEU B N   1 
ATOM   3012  C CA  . LEU B 2 291 ? -27.070  -43.957  -21.500 1.00 152.48 ? 292 LEU B CA  1 
ATOM   3013  C C   . LEU B 2 291 ? -26.603  -43.866  -20.037 1.00 152.12 ? 292 LEU B C   1 
ATOM   3014  O O   . LEU B 2 291 ? -25.771  -44.673  -19.614 1.00 150.30 ? 292 LEU B O   1 
ATOM   3015  C CB  . LEU B 2 291 ? -28.267  -44.923  -21.654 1.00 153.12 ? 292 LEU B CB  1 
ATOM   3016  C CG  . LEU B 2 291 ? -29.008  -44.862  -22.999 1.00 160.18 ? 292 LEU B CG  1 
ATOM   3017  C CD1 . LEU B 2 291 ? -29.783  -46.129  -23.260 1.00 162.68 ? 292 LEU B CD1 1 
ATOM   3018  C CD2 . LEU B 2 291 ? -29.945  -43.674  -23.063 1.00 161.77 ? 292 LEU B CD2 1 
ATOM   3019  N N   . PRO B 2 292 ? -27.110  -42.880  -19.259 1.00 146.69 ? 293 PRO B N   1 
ATOM   3020  C CA  . PRO B 2 292 ? -26.652  -42.734  -17.869 1.00 144.37 ? 293 PRO B CA  1 
ATOM   3021  C C   . PRO B 2 292 ? -27.266  -43.696  -16.850 1.00 145.78 ? 293 PRO B C   1 
ATOM   3022  O O   . PRO B 2 292 ? -26.765  -43.777  -15.726 1.00 143.91 ? 293 PRO B O   1 
ATOM   3023  C CB  . PRO B 2 292 ? -26.993  -41.284  -17.548 1.00 146.96 ? 293 PRO B CB  1 
ATOM   3024  C CG  . PRO B 2 292 ? -28.182  -40.995  -18.378 1.00 153.10 ? 293 PRO B CG  1 
ATOM   3025  C CD  . PRO B 2 292 ? -28.068  -41.816  -19.624 1.00 149.39 ? 293 PRO B CD  1 
ATOM   3026  N N   . PHE B 2 293 ? -28.349  -44.405  -17.216 1.00 142.45 ? 294 PHE B N   1 
ATOM   3027  C CA  . PHE B 2 293 ? -29.014  -45.340  -16.304 1.00 141.33 ? 294 PHE B CA  1 
ATOM   3028  C C   . PHE B 2 293 ? -29.295  -46.681  -16.939 1.00 144.84 ? 294 PHE B C   1 
ATOM   3029  O O   . PHE B 2 293 ? -29.384  -46.778  -18.163 1.00 145.93 ? 294 PHE B O   1 
ATOM   3030  C CB  . PHE B 2 293 ? -30.276  -44.724  -15.694 1.00 143.92 ? 294 PHE B CB  1 
ATOM   3031  C CG  . PHE B 2 293 ? -29.938  -43.493  -14.894 1.00 146.00 ? 294 PHE B CG  1 
ATOM   3032  C CD1 . PHE B 2 293 ? -29.344  -43.600  -13.641 1.00 148.41 ? 294 PHE B CD1 1 
ATOM   3033  C CD2 . PHE B 2 293 ? -30.129  -42.226  -15.428 1.00 150.10 ? 294 PHE B CD2 1 
ATOM   3034  C CE1 . PHE B 2 293 ? -28.979  -42.459  -12.923 1.00 149.76 ? 294 PHE B CE1 1 
ATOM   3035  C CE2 . PHE B 2 293 ? -29.762  -41.086  -14.711 1.00 153.28 ? 294 PHE B CE2 1 
ATOM   3036  C CZ  . PHE B 2 293 ? -29.197  -41.211  -13.461 1.00 150.23 ? 294 PHE B CZ  1 
ATOM   3037  N N   . GLN B 2 294 ? -29.389  -47.726  -16.111 1.00 139.59 ? 295 GLN B N   1 
ATOM   3038  C CA  . GLN B 2 294 ? -29.614  -49.085  -16.584 1.00 139.22 ? 295 GLN B CA  1 
ATOM   3039  C C   . GLN B 2 294 ? -30.498  -49.867  -15.627 1.00 141.83 ? 295 GLN B C   1 
ATOM   3040  O O   . GLN B 2 294 ? -30.312  -49.777  -14.418 1.00 140.20 ? 295 GLN B O   1 
ATOM   3041  C CB  . GLN B 2 294 ? -28.254  -49.768  -16.860 1.00 139.98 ? 295 GLN B CB  1 
ATOM   3042  C CG  . GLN B 2 294 ? -28.100  -51.226  -16.433 1.00 153.79 ? 295 GLN B CG  1 
ATOM   3043  C CD  . GLN B 2 294 ? -27.405  -51.358  -15.103 1.00 169.42 ? 295 GLN B CD  1 
ATOM   3044  O OE1 . GLN B 2 294 ? -27.986  -51.809  -14.124 1.00 162.42 ? 295 GLN B OE1 1 
ATOM   3045  N NE2 . GLN B 2 294 ? -26.134  -50.986  -15.039 1.00 161.89 ? 295 GLN B NE2 1 
ATOM   3046  N N   . ASN B 2 295 ? -31.460  -50.626  -16.170 1.00 139.42 ? 296 ASN B N   1 
ATOM   3047  C CA  . ASN B 2 295 ? -32.364  -51.440  -15.363 1.00 139.13 ? 296 ASN B CA  1 
ATOM   3048  C C   . ASN B 2 295 ? -32.036  -52.952  -15.419 1.00 144.19 ? 296 ASN B C   1 
ATOM   3049  O O   . ASN B 2 295 ? -32.844  -53.770  -14.965 1.00 143.34 ? 296 ASN B O   1 
ATOM   3050  C CB  . ASN B 2 295 ? -33.827  -51.149  -15.738 1.00 140.98 ? 296 ASN B CB  1 
ATOM   3051  C CG  . ASN B 2 295 ? -34.381  -51.923  -16.916 1.00 170.40 ? 296 ASN B CG  1 
ATOM   3052  O OD1 . ASN B 2 295 ? -33.665  -52.330  -17.836 1.00 164.53 ? 296 ASN B OD1 1 
ATOM   3053  N ND2 . ASN B 2 295 ? -35.686  -52.134  -16.912 1.00 166.10 ? 296 ASN B ND2 1 
ATOM   3054  N N   . ILE B 2 296 ? -30.838  -53.310  -15.937 1.00 141.67 ? 297 ILE B N   1 
ATOM   3055  C CA  . ILE B 2 296 ? -30.388  -54.699  -16.127 1.00 141.02 ? 297 ILE B CA  1 
ATOM   3056  C C   . ILE B 2 296 ? -30.051  -55.427  -14.793 1.00 141.95 ? 297 ILE B C   1 
ATOM   3057  O O   . ILE B 2 296 ? -30.742  -56.392  -14.457 1.00 141.22 ? 297 ILE B O   1 
ATOM   3058  C CB  . ILE B 2 296 ? -29.228  -54.779  -17.169 1.00 144.61 ? 297 ILE B CB  1 
ATOM   3059  C CG1 . ILE B 2 296 ? -29.696  -54.225  -18.531 1.00 146.55 ? 297 ILE B CG1 1 
ATOM   3060  C CG2 . ILE B 2 296 ? -28.693  -56.221  -17.323 1.00 145.52 ? 297 ILE B CG2 1 
ATOM   3061  C CD1 . ILE B 2 296 ? -28.632  -53.624  -19.365 1.00 155.19 ? 297 ILE B CD1 1 
ATOM   3062  N N   . HIS B 2 297 ? -28.989  -55.007  -14.070 1.00 136.20 ? 298 HIS B N   1 
ATOM   3063  C CA  . HIS B 2 297 ? -28.572  -55.670  -12.832 1.00 134.18 ? 298 HIS B CA  1 
ATOM   3064  C C   . HIS B 2 297 ? -27.842  -54.721  -11.871 1.00 136.86 ? 298 HIS B C   1 
ATOM   3065  O O   . HIS B 2 297 ? -26.988  -53.956  -12.325 1.00 137.25 ? 298 HIS B O   1 
ATOM   3066  C CB  . HIS B 2 297 ? -27.680  -56.878  -13.156 1.00 134.41 ? 298 HIS B CB  1 
ATOM   3067  C CG  . HIS B 2 297 ? -27.521  -57.821  -12.013 1.00 136.50 ? 298 HIS B CG  1 
ATOM   3068  N ND1 . HIS B 2 297 ? -26.592  -57.595  -11.020 1.00 137.14 ? 298 HIS B ND1 1 
ATOM   3069  C CD2 . HIS B 2 297 ? -28.199  -58.957  -11.731 1.00 137.90 ? 298 HIS B CD2 1 
ATOM   3070  C CE1 . HIS B 2 297 ? -26.724  -58.602  -10.173 1.00 135.72 ? 298 HIS B CE1 1 
ATOM   3071  N NE2 . HIS B 2 297 ? -27.677  -59.448  -10.562 1.00 136.50 ? 298 HIS B NE2 1 
ATOM   3072  N N   . PRO B 2 298 ? -28.132  -54.777  -10.544 1.00 131.32 ? 299 PRO B N   1 
ATOM   3073  C CA  . PRO B 2 298 ? -27.453  -53.872  -9.596  1.00 130.06 ? 299 PRO B CA  1 
ATOM   3074  C C   . PRO B 2 298 ? -25.931  -54.015  -9.513  1.00 132.05 ? 299 PRO B C   1 
ATOM   3075  O O   . PRO B 2 298 ? -25.256  -53.000  -9.331  1.00 131.98 ? 299 PRO B O   1 
ATOM   3076  C CB  . PRO B 2 298 ? -28.135  -54.172  -8.262  1.00 131.41 ? 299 PRO B CB  1 
ATOM   3077  C CG  . PRO B 2 298 ? -28.705  -55.530  -8.424  1.00 135.95 ? 299 PRO B CG  1 
ATOM   3078  C CD  . PRO B 2 298 ? -29.134  -55.609  -9.850  1.00 132.50 ? 299 PRO B CD  1 
ATOM   3079  N N   . ILE B 2 299 ? -25.388  -55.248  -9.663  1.00 126.56 ? 300 ILE B N   1 
ATOM   3080  C CA  . ILE B 2 299 ? -23.939  -55.494  -9.646  1.00 125.01 ? 300 ILE B CA  1 
ATOM   3081  C C   . ILE B 2 299 ? -23.372  -55.071  -11.006 1.00 129.60 ? 300 ILE B C   1 
ATOM   3082  O O   . ILE B 2 299 ? -23.847  -55.545  -12.037 1.00 129.47 ? 300 ILE B O   1 
ATOM   3083  C CB  . ILE B 2 299 ? -23.586  -56.969  -9.291  1.00 127.17 ? 300 ILE B CB  1 
ATOM   3084  C CG1 . ILE B 2 299 ? -24.160  -57.389  -7.915  1.00 126.82 ? 300 ILE B CG1 1 
ATOM   3085  C CG2 . ILE B 2 299 ? -22.071  -57.206  -9.356  1.00 127.42 ? 300 ILE B CG2 1 
ATOM   3086  C CD1 . ILE B 2 299 ? -24.203  -58.955  -7.634  1.00 132.30 ? 300 ILE B CD1 1 
ATOM   3087  N N   . THR B 2 300 ? -22.386  -54.152  -11.006 1.00 126.96 ? 301 THR B N   1 
ATOM   3088  C CA  . THR B 2 300 ? -21.751  -53.616  -12.222 1.00 127.92 ? 301 THR B CA  1 
ATOM   3089  C C   . THR B 2 300 ? -20.225  -53.496  -12.073 1.00 132.14 ? 301 THR B C   1 
ATOM   3090  O O   . THR B 2 300 ? -19.739  -53.198  -10.981 1.00 130.76 ? 301 THR B O   1 
ATOM   3091  C CB  . THR B 2 300 ? -22.341  -52.240  -12.587 1.00 137.35 ? 301 THR B CB  1 
ATOM   3092  O OG1 . THR B 2 300 ? -22.180  -51.331  -11.498 1.00 140.51 ? 301 THR B OG1 1 
ATOM   3093  C CG2 . THR B 2 300 ? -23.795  -52.296  -13.020 1.00 135.21 ? 301 THR B CG2 1 
ATOM   3094  N N   . ILE B 2 301 ? -19.477  -53.714  -13.174 1.00 130.11 ? 302 ILE B N   1 
ATOM   3095  C CA  . ILE B 2 301 ? -18.010  -53.603  -13.228 1.00 129.82 ? 302 ILE B CA  1 
ATOM   3096  C C   . ILE B 2 301 ? -17.606  -52.721  -14.425 1.00 136.73 ? 302 ILE B C   1 
ATOM   3097  O O   . ILE B 2 301 ? -18.014  -52.989  -15.562 1.00 137.70 ? 302 ILE B O   1 
ATOM   3098  C CB  . ILE B 2 301 ? -17.298  -54.993  -13.231 1.00 132.24 ? 302 ILE B CB  1 
ATOM   3099  C CG1 . ILE B 2 301 ? -17.644  -55.793  -11.964 1.00 131.85 ? 302 ILE B CG1 1 
ATOM   3100  C CG2 . ILE B 2 301 ? -15.767  -54.855  -13.389 1.00 132.39 ? 302 ILE B CG2 1 
ATOM   3101  C CD1 . ILE B 2 301 ? -17.338  -57.250  -12.012 1.00 139.95 ? 302 ILE B CD1 1 
ATOM   3102  N N   . GLY B 2 302 ? -16.809  -51.689  -14.145 1.00 134.04 ? 303 GLY B N   1 
ATOM   3103  C CA  . GLY B 2 302 ? -16.325  -50.738  -15.143 1.00 134.99 ? 303 GLY B CA  1 
ATOM   3104  C C   . GLY B 2 302 ? -17.195  -49.500  -15.232 1.00 140.35 ? 303 GLY B C   1 
ATOM   3105  O O   . GLY B 2 302 ? -18.064  -49.301  -14.373 1.00 140.72 ? 303 GLY B O   1 
ATOM   3106  N N   . LYS B 2 303 ? -16.965  -48.644  -16.267 1.00 137.32 ? 304 LYS B N   1 
ATOM   3107  C CA  . LYS B 2 303 ? -17.759  -47.421  -16.484 1.00 137.97 ? 304 LYS B CA  1 
ATOM   3108  C C   . LYS B 2 303 ? -19.183  -47.862  -16.775 1.00 142.76 ? 304 LYS B C   1 
ATOM   3109  O O   . LYS B 2 303 ? -19.478  -48.355  -17.866 1.00 142.97 ? 304 LYS B O   1 
ATOM   3110  C CB  . LYS B 2 303 ? -17.173  -46.525  -17.591 1.00 141.44 ? 304 LYS B CB  1 
ATOM   3111  C CG  . LYS B 2 303 ? -16.158  -45.516  -17.058 1.00 155.06 ? 304 LYS B CG  1 
ATOM   3112  C CD  . LYS B 2 303 ? -15.549  -44.634  -18.148 1.00 165.25 ? 304 LYS B CD  1 
ATOM   3113  C CE  . LYS B 2 303 ? -14.375  -43.832  -17.619 1.00 170.61 ? 304 LYS B CE  1 
ATOM   3114  N NZ  . LYS B 2 303 ? -13.741  -42.986  -18.669 1.00 176.63 ? 304 LYS B NZ  1 
ATOM   3115  N N   . CYS B 2 304 ? -20.030  -47.804  -15.731 1.00 139.48 ? 305 CYS B N   1 
ATOM   3116  C CA  . CYS B 2 304 ? -21.389  -48.326  -15.764 1.00 139.87 ? 305 CYS B CA  1 
ATOM   3117  C C   . CYS B 2 304 ? -22.486  -47.332  -15.423 1.00 142.23 ? 305 CYS B C   1 
ATOM   3118  O O   . CYS B 2 304 ? -22.338  -46.539  -14.490 1.00 141.04 ? 305 CYS B O   1 
ATOM   3119  C CB  . CYS B 2 304 ? -21.489  -49.557  -14.872 1.00 139.55 ? 305 CYS B CB  1 
ATOM   3120  S SG  . CYS B 2 304 ? -20.732  -51.040  -15.580 1.00 144.09 ? 305 CYS B SG  1 
ATOM   3121  N N   . PRO B 2 305 ? -23.646  -47.455  -16.116 1.00 138.84 ? 306 PRO B N   1 
ATOM   3122  C CA  . PRO B 2 305 ? -24.790  -46.597  -15.796 1.00 139.01 ? 306 PRO B CA  1 
ATOM   3123  C C   . PRO B 2 305 ? -25.432  -47.098  -14.508 1.00 140.70 ? 306 PRO B C   1 
ATOM   3124  O O   . PRO B 2 305 ? -25.783  -48.276  -14.417 1.00 139.20 ? 306 PRO B O   1 
ATOM   3125  C CB  . PRO B 2 305 ? -25.726  -46.787  -17.001 1.00 142.30 ? 306 PRO B CB  1 
ATOM   3126  C CG  . PRO B 2 305 ? -24.960  -47.577  -18.008 1.00 147.09 ? 306 PRO B CG  1 
ATOM   3127  C CD  . PRO B 2 305 ? -23.979  -48.369  -17.227 1.00 141.13 ? 306 PRO B CD  1 
ATOM   3128  N N   . LYS B 2 306 ? -25.532  -46.215  -13.500 1.00 136.76 ? 307 LYS B N   1 
ATOM   3129  C CA  . LYS B 2 306 ? -26.092  -46.504  -12.175 1.00 135.70 ? 307 LYS B CA  1 
ATOM   3130  C C   . LYS B 2 306 ? -27.438  -47.223  -12.269 1.00 140.54 ? 307 LYS B C   1 
ATOM   3131  O O   . LYS B 2 306 ? -28.303  -46.795  -13.036 1.00 140.76 ? 307 LYS B O   1 
ATOM   3132  C CB  . LYS B 2 306 ? -26.185  -45.217  -11.337 1.00 138.16 ? 307 LYS B CB  1 
ATOM   3133  C CG  . LYS B 2 306 ? -24.821  -44.719  -10.875 1.00 149.39 ? 307 LYS B CG  1 
ATOM   3134  C CD  . LYS B 2 306 ? -24.733  -43.208  -10.763 1.00 160.09 ? 307 LYS B CD  1 
ATOM   3135  C CE  . LYS B 2 306 ? -23.339  -42.833  -10.305 1.00 169.44 ? 307 LYS B CE  1 
ATOM   3136  N NZ  . LYS B 2 306 ? -23.247  -41.427  -9.848  1.00 177.84 ? 307 LYS B NZ  1 
ATOM   3137  N N   . TYR B 2 307 ? -27.577  -48.357  -11.548 1.00 137.46 ? 308 TYR B N   1 
ATOM   3138  C CA  . TYR B 2 307 ? -28.778  -49.195  -11.571 1.00 137.99 ? 308 TYR B CA  1 
ATOM   3139  C C   . TYR B 2 307 ? -30.030  -48.508  -11.029 1.00 143.90 ? 308 TYR B C   1 
ATOM   3140  O O   . TYR B 2 307 ? -29.975  -47.766  -10.048 1.00 142.53 ? 308 TYR B O   1 
ATOM   3141  C CB  . TYR B 2 307 ? -28.550  -50.549  -10.865 1.00 137.86 ? 308 TYR B CB  1 
ATOM   3142  C CG  . TYR B 2 307 ? -29.735  -51.500  -10.925 1.00 139.92 ? 308 TYR B CG  1 
ATOM   3143  C CD1 . TYR B 2 307 ? -30.075  -52.151  -12.107 1.00 142.66 ? 308 TYR B CD1 1 
ATOM   3144  C CD2 . TYR B 2 307 ? -30.512  -51.751  -9.799  1.00 140.41 ? 308 TYR B CD2 1 
ATOM   3145  C CE1 . TYR B 2 307 ? -31.155  -53.031  -12.168 1.00 143.69 ? 308 TYR B CE1 1 
ATOM   3146  C CE2 . TYR B 2 307 ? -31.605  -52.619  -9.851  1.00 141.62 ? 308 TYR B CE2 1 
ATOM   3147  C CZ  . TYR B 2 307 ? -31.924  -53.256  -11.039 1.00 150.06 ? 308 TYR B CZ  1 
ATOM   3148  O OH  . TYR B 2 307 ? -32.995  -54.115  -11.107 1.00 151.41 ? 308 TYR B OH  1 
ATOM   3149  N N   . VAL B 2 308 ? -31.160  -48.784  -11.700 1.00 143.30 ? 309 VAL B N   1 
ATOM   3150  C CA  . VAL B 2 308 ? -32.523  -48.341  -11.392 1.00 144.76 ? 309 VAL B CA  1 
ATOM   3151  C C   . VAL B 2 308 ? -33.489  -49.521  -11.637 1.00 150.06 ? 309 VAL B C   1 
ATOM   3152  O O   . VAL B 2 308 ? -33.179  -50.401  -12.440 1.00 149.60 ? 309 VAL B O   1 
ATOM   3153  C CB  . VAL B 2 308 ? -32.955  -47.047  -12.143 1.00 150.42 ? 309 VAL B CB  1 
ATOM   3154  C CG1 . VAL B 2 308 ? -32.426  -45.798  -11.447 1.00 150.28 ? 309 VAL B CG1 1 
ATOM   3155  C CG2 . VAL B 2 308 ? -32.536  -47.071  -13.611 1.00 151.18 ? 309 VAL B CG2 1 
ATOM   3156  N N   . LYS B 2 309 ? -34.628  -49.563  -10.931 1.00 147.75 ? 310 LYS B N   1 
ATOM   3157  C CA  . LYS B 2 309 ? -35.610  -50.643  -11.072 1.00 147.84 ? 310 LYS B CA  1 
ATOM   3158  C C   . LYS B 2 309 ? -36.723  -50.295  -12.074 1.00 152.43 ? 310 LYS B C   1 
ATOM   3159  O O   . LYS B 2 309 ? -37.497  -51.174  -12.461 1.00 152.33 ? 310 LYS B O   1 
ATOM   3160  C CB  . LYS B 2 309 ? -36.187  -51.056  -9.706  1.00 149.97 ? 310 LYS B CB  1 
ATOM   3161  C CG  . LYS B 2 309 ? -35.237  -51.924  -8.894  1.00 168.85 ? 310 LYS B CG  1 
ATOM   3162  C CD  . LYS B 2 309 ? -35.912  -52.532  -7.666  1.00 181.81 ? 310 LYS B CD  1 
ATOM   3163  C CE  . LYS B 2 309 ? -35.562  -51.808  -6.394  1.00 194.04 ? 310 LYS B CE  1 
ATOM   3164  N NZ  . LYS B 2 309 ? -35.677  -52.699  -5.212  1.00 200.97 ? 310 LYS B NZ  1 
ATOM   3165  N N   . SER B 2 310 ? -36.768  -49.020  -12.511 1.00 149.36 ? 311 SER B N   1 
ATOM   3166  C CA  . SER B 2 310 ? -37.742  -48.444  -13.444 1.00 150.65 ? 311 SER B CA  1 
ATOM   3167  C C   . SER B 2 310 ? -37.855  -49.163  -14.799 1.00 154.04 ? 311 SER B C   1 
ATOM   3168  O O   . SER B 2 310 ? -36.876  -49.738  -15.284 1.00 153.00 ? 311 SER B O   1 
ATOM   3169  C CB  . SER B 2 310 ? -37.467  -46.955  -13.656 1.00 155.75 ? 311 SER B CB  1 
ATOM   3170  O OG  . SER B 2 310 ? -36.079  -46.663  -13.669 1.00 165.35 ? 311 SER B OG  1 
ATOM   3171  N N   . THR B 2 311 ? -39.073  -49.121  -15.396 1.00 150.65 ? 312 THR B N   1 
ATOM   3172  C CA  . THR B 2 311 ? -39.421  -49.713  -16.696 1.00 150.73 ? 312 THR B CA  1 
ATOM   3173  C C   . THR B 2 311 ? -38.689  -48.954  -17.811 1.00 153.20 ? 312 THR B C   1 
ATOM   3174  O O   . THR B 2 311 ? -38.106  -49.578  -18.704 1.00 153.12 ? 312 THR B O   1 
ATOM   3175  C CB  . THR B 2 311 ? -40.949  -49.682  -16.910 1.00 159.61 ? 312 THR B CB  1 
ATOM   3176  O OG1 . THR B 2 311 ? -41.633  -49.888  -15.668 1.00 158.38 ? 312 THR B OG1 1 
ATOM   3177  C CG2 . THR B 2 311 ? -41.415  -50.692  -17.954 1.00 158.68 ? 312 THR B CG2 1 
ATOM   3178  N N   . LYS B 2 312 ? -38.734  -47.603  -17.743 1.00 148.18 ? 313 LYS B N   1 
ATOM   3179  C CA  . LYS B 2 312 ? -38.082  -46.669  -18.661 1.00 148.04 ? 313 LYS B CA  1 
ATOM   3180  C C   . LYS B 2 312 ? -38.021  -45.264  -18.056 1.00 151.11 ? 313 LYS B C   1 
ATOM   3181  O O   . LYS B 2 312 ? -38.881  -44.902  -17.247 1.00 150.32 ? 313 LYS B O   1 
ATOM   3182  C CB  . LYS B 2 312 ? -38.789  -46.638  -20.026 1.00 151.79 ? 313 LYS B CB  1 
ATOM   3183  C CG  . LYS B 2 312 ? -37.825  -46.630  -21.209 1.00 160.83 ? 313 LYS B CG  1 
ATOM   3184  C CD  . LYS B 2 312 ? -37.553  -48.033  -21.751 1.00 167.45 ? 313 LYS B CD  1 
ATOM   3185  C CE  . LYS B 2 312 ? -36.934  -47.980  -23.126 1.00 177.10 ? 313 LYS B CE  1 
ATOM   3186  N NZ  . LYS B 2 312 ? -36.863  -49.327  -23.751 1.00 185.07 ? 313 LYS B NZ  1 
ATOM   3187  N N   . LEU B 2 313 ? -36.965  -44.501  -18.403 1.00 120.07 ? 314 LEU B N   1 
ATOM   3188  C CA  . LEU B 2 313 ? -36.754  -43.127  -17.931 1.00 136.79 ? 314 LEU B CA  1 
ATOM   3189  C C   . LEU B 2 313 ? -36.337  -42.180  -19.056 1.00 157.78 ? 314 LEU B C   1 
ATOM   3190  O O   . LEU B 2 313 ? -35.488  -42.521  -19.877 1.00 112.90 ? 314 LEU B O   1 
ATOM   3191  C CB  . LEU B 2 313 ? -35.750  -43.058  -16.765 1.00 136.61 ? 314 LEU B CB  1 
ATOM   3192  C CG  . LEU B 2 313 ? -36.287  -43.372  -15.370 1.00 141.05 ? 314 LEU B CG  1 
ATOM   3193  C CD1 . LEU B 2 313 ? -35.178  -43.312  -14.348 1.00 141.15 ? 314 LEU B CD1 1 
ATOM   3194  C CD2 . LEU B 2 313 ? -37.370  -42.393  -14.959 1.00 143.68 ? 314 LEU B CD2 1 
ATOM   3195  N N   . GLN C 3 3   ? -79.243  8.283    -34.639 1.00 145.73 ? 3   GLN C N   1 
ATOM   3196  C CA  . GLN C 3 3   ? -80.251  8.688    -35.615 1.00 143.63 ? 3   GLN C CA  1 
ATOM   3197  C C   . GLN C 3 3   ? -81.482  9.184    -34.872 1.00 146.63 ? 3   GLN C C   1 
ATOM   3198  O O   . GLN C 3 3   ? -82.093  8.424    -34.119 1.00 146.62 ? 3   GLN C O   1 
ATOM   3199  C CB  . GLN C 3 3   ? -80.620  7.527    -36.562 1.00 145.86 ? 3   GLN C CB  1 
ATOM   3200  C CG  . GLN C 3 3   ? -79.431  6.838    -37.233 1.00 156.48 ? 3   GLN C CG  1 
ATOM   3201  C CD  . GLN C 3 3   ? -78.854  5.725    -36.387 1.00 174.05 ? 3   GLN C CD  1 
ATOM   3202  O OE1 . GLN C 3 3   ? -79.495  4.697    -36.136 1.00 170.67 ? 3   GLN C OE1 1 
ATOM   3203  N NE2 . GLN C 3 3   ? -77.624  5.908    -35.930 1.00 164.95 ? 3   GLN C NE2 1 
ATOM   3204  N N   . LEU C 3 4   ? -81.817  10.470   -35.041 1.00 142.30 ? 4   LEU C N   1 
ATOM   3205  C CA  . LEU C 3 4   ? -82.979  11.062   -34.386 1.00 141.40 ? 4   LEU C CA  1 
ATOM   3206  C C   . LEU C 3 4   ? -84.025  11.443   -35.420 1.00 145.83 ? 4   LEU C C   1 
ATOM   3207  O O   . LEU C 3 4   ? -83.730  12.166   -36.376 1.00 144.58 ? 4   LEU C O   1 
ATOM   3208  C CB  . LEU C 3 4   ? -82.592  12.272   -33.517 1.00 140.67 ? 4   LEU C CB  1 
ATOM   3209  C CG  . LEU C 3 4   ? -81.918  11.978   -32.172 1.00 146.17 ? 4   LEU C CG  1 
ATOM   3210  C CD1 . LEU C 3 4   ? -81.188  13.189   -31.664 1.00 146.22 ? 4   LEU C CD1 1 
ATOM   3211  C CD2 . LEU C 3 4   ? -82.922  11.547   -31.129 1.00 147.88 ? 4   LEU C CD2 1 
ATOM   3212  N N   . VAL C 3 5   ? -85.241  10.922   -35.244 1.00 143.93 ? 5   VAL C N   1 
ATOM   3213  C CA  . VAL C 3 5   ? -86.354  11.158   -36.154 1.00 144.22 ? 5   VAL C CA  1 
ATOM   3214  C C   . VAL C 3 5   ? -87.399  11.998   -35.426 1.00 148.21 ? 5   VAL C C   1 
ATOM   3215  O O   . VAL C 3 5   ? -88.135  11.475   -34.590 1.00 148.16 ? 5   VAL C O   1 
ATOM   3216  C CB  . VAL C 3 5   ? -86.944  9.822    -36.695 1.00 150.05 ? 5   VAL C CB  1 
ATOM   3217  C CG1 . VAL C 3 5   ? -88.030  10.077   -37.739 1.00 150.14 ? 5   VAL C CG1 1 
ATOM   3218  C CG2 . VAL C 3 5   ? -85.854  8.913    -37.265 1.00 151.20 ? 5   VAL C CG2 1 
ATOM   3219  N N   . GLN C 3 6   ? -87.458  13.298   -35.740 1.00 144.63 ? 6   GLN C N   1 
ATOM   3220  C CA  . GLN C 3 6   ? -88.412  14.224   -35.126 1.00 144.33 ? 6   GLN C CA  1 
ATOM   3221  C C   . GLN C 3 6   ? -89.817  14.130   -35.737 1.00 148.92 ? 6   GLN C C   1 
ATOM   3222  O O   . GLN C 3 6   ? -90.013  13.447   -36.748 1.00 149.12 ? 6   GLN C O   1 
ATOM   3223  C CB  . GLN C 3 6   ? -87.894  15.660   -35.219 1.00 144.93 ? 6   GLN C CB  1 
ATOM   3224  C CG  . GLN C 3 6   ? -86.937  16.038   -34.114 1.00 154.57 ? 6   GLN C CG  1 
ATOM   3225  C CD  . GLN C 3 6   ? -86.564  17.481   -34.243 1.00 170.05 ? 6   GLN C CD  1 
ATOM   3226  O OE1 . GLN C 3 6   ? -85.632  17.838   -34.963 1.00 166.15 ? 6   GLN C OE1 1 
ATOM   3227  N NE2 . GLN C 3 6   ? -87.319  18.348   -33.590 1.00 159.82 ? 6   GLN C NE2 1 
ATOM   3228  N N   . SER C 3 7   ? -90.794  14.824   -35.111 1.00 145.37 ? 7   SER C N   1 
ATOM   3229  C CA  . SER C 3 7   ? -92.187  14.903   -35.563 1.00 145.77 ? 7   SER C CA  1 
ATOM   3230  C C   . SER C 3 7   ? -92.270  15.724   -36.863 1.00 150.91 ? 7   SER C C   1 
ATOM   3231  O O   . SER C 3 7   ? -91.387  16.547   -37.142 1.00 150.86 ? 7   SER C O   1 
ATOM   3232  C CB  . SER C 3 7   ? -93.050  15.557   -34.487 1.00 148.30 ? 7   SER C CB  1 
ATOM   3233  O OG  . SER C 3 7   ? -94.379  15.787   -34.923 1.00 155.50 ? 7   SER C OG  1 
ATOM   3234  N N   . GLY C 3 8   ? -93.336  15.502   -37.629 1.00 147.95 ? 8   GLY C N   1 
ATOM   3235  C CA  . GLY C 3 8   ? -93.587  16.216   -38.879 1.00 148.45 ? 8   GLY C CA  1 
ATOM   3236  C C   . GLY C 3 8   ? -94.003  17.662   -38.678 1.00 151.63 ? 8   GLY C C   1 
ATOM   3237  O O   . GLY C 3 8   ? -94.312  18.070   -37.551 1.00 151.14 ? 8   GLY C O   1 
ATOM   3238  N N   . ALA C 3 9   ? -94.017  18.444   -39.782 1.00 147.86 ? 9   ALA C N   1 
ATOM   3239  C CA  . ALA C 3 9   ? -94.389  19.865   -39.806 1.00 147.99 ? 9   ALA C CA  1 
ATOM   3240  C C   . ALA C 3 9   ? -95.767  20.106   -39.193 1.00 152.35 ? 9   ALA C C   1 
ATOM   3241  O O   . ALA C 3 9   ? -96.709  19.357   -39.472 1.00 153.03 ? 9   ALA C O   1 
ATOM   3242  C CB  . ALA C 3 9   ? -94.347  20.396   -41.229 1.00 149.99 ? 9   ALA C CB  1 
ATOM   3243  N N   . GLU C 3 10  ? -95.869  21.123   -38.322 1.00 148.50 ? 10  GLU C N   1 
ATOM   3244  C CA  . GLU C 3 10  ? -97.112  21.443   -37.623 1.00 149.89 ? 10  GLU C CA  1 
ATOM   3245  C C   . GLU C 3 10  ? -97.524  22.909   -37.786 1.00 154.68 ? 10  GLU C C   1 
ATOM   3246  O O   . GLU C 3 10  ? -96.716  23.810   -37.556 1.00 153.77 ? 10  GLU C O   1 
ATOM   3247  C CB  . GLU C 3 10  ? -97.010  21.060   -36.132 1.00 150.18 ? 10  GLU C CB  1 
ATOM   3248  C CG  . GLU C 3 10  ? -96.888  19.564   -35.845 1.00 159.24 ? 10  GLU C CG  1 
ATOM   3249  C CD  . GLU C 3 10  ? -98.089  18.696   -36.181 1.00 175.07 ? 10  GLU C CD  1 
ATOM   3250  O OE1 . GLU C 3 10  ? -99.226  19.075   -35.812 1.00 165.64 ? 10  GLU C OE1 1 
ATOM   3251  O OE2 . GLU C 3 10  ? -97.888  17.620   -36.790 1.00 162.72 ? 10  GLU C OE2 1 
ATOM   3252  N N   . VAL C 3 11  ? -98.782  23.140   -38.204 1.00 152.93 ? 11  VAL C N   1 
ATOM   3253  C CA  . VAL C 3 11  ? -99.350  24.478   -38.392 1.00 155.13 ? 11  VAL C CA  1 
ATOM   3254  C C   . VAL C 3 11  ? -100.629 24.571   -37.563 1.00 160.89 ? 11  VAL C C   1 
ATOM   3255  O O   . VAL C 3 11  ? -101.576 23.819   -37.807 1.00 161.62 ? 11  VAL C O   1 
ATOM   3256  C CB  . VAL C 3 11  ? -99.608  24.844   -39.884 1.00 161.32 ? 11  VAL C CB  1 
ATOM   3257  C CG1 . VAL C 3 11  ? -100.137 26.270   -40.019 1.00 164.10 ? 11  VAL C CG1 1 
ATOM   3258  C CG2 . VAL C 3 11  ? -98.357  24.658   -40.739 1.00 159.22 ? 11  VAL C CG2 1 
ATOM   3259  N N   . LYS C 3 12  ? -100.644 25.485   -36.581 1.00 158.24 ? 12  LYS C N   1 
ATOM   3260  C CA  . LYS C 3 12  ? -101.786 25.719   -35.692 1.00 160.45 ? 12  LYS C CA  1 
ATOM   3261  C C   . LYS C 3 12  ? -101.925 27.200   -35.368 1.00 167.32 ? 12  LYS C C   1 
ATOM   3262  O O   . LYS C 3 12  ? -100.921 27.899   -35.247 1.00 165.93 ? 12  LYS C O   1 
ATOM   3263  C CB  . LYS C 3 12  ? -101.664 24.896   -34.392 1.00 160.68 ? 12  LYS C CB  1 
ATOM   3264  C CG  . LYS C 3 12  ? -102.222 23.476   -34.496 1.00 171.61 ? 12  LYS C CG  1 
ATOM   3265  C CD  . LYS C 3 12  ? -102.375 22.808   -33.134 1.00 177.61 ? 12  LYS C CD  1 
ATOM   3266  C CE  . LYS C 3 12  ? -102.873 21.386   -33.246 1.00 184.34 ? 12  LYS C CE  1 
ATOM   3267  N NZ  . LYS C 3 12  ? -103.257 20.828   -31.923 1.00 191.45 ? 12  LYS C NZ  1 
ATOM   3268  N N   . LYS C 3 13  ? -103.172 27.673   -35.223 1.00 167.59 ? 13  LYS C N   1 
ATOM   3269  C CA  . LYS C 3 13  ? -103.484 29.064   -34.887 1.00 170.34 ? 13  LYS C CA  1 
ATOM   3270  C C   . LYS C 3 13  ? -103.133 29.336   -33.410 1.00 173.51 ? 13  LYS C C   1 
ATOM   3271  O O   . LYS C 3 13  ? -103.203 28.402   -32.603 1.00 171.26 ? 13  LYS C O   1 
ATOM   3272  C CB  . LYS C 3 13  ? -104.958 29.373   -35.182 1.00 177.12 ? 13  LYS C CB  1 
ATOM   3273  C CG  . LYS C 3 13  ? -105.294 29.316   -36.666 1.00 190.50 ? 13  LYS C CG  1 
ATOM   3274  C CD  . LYS C 3 13  ? -106.789 29.422   -36.905 1.00 202.86 ? 13  LYS C CD  1 
ATOM   3275  C CE  . LYS C 3 13  ? -107.153 29.057   -38.321 1.00 211.92 ? 13  LYS C CE  1 
ATOM   3276  N NZ  . LYS C 3 13  ? -108.552 29.439   -38.642 1.00 218.22 ? 13  LYS C NZ  1 
ATOM   3277  N N   . PRO C 3 14  ? -102.718 30.578   -33.038 1.00 171.75 ? 14  PRO C N   1 
ATOM   3278  C CA  . PRO C 3 14  ? -102.308 30.835   -31.643 1.00 171.31 ? 14  PRO C CA  1 
ATOM   3279  C C   . PRO C 3 14  ? -103.355 30.547   -30.572 1.00 177.82 ? 14  PRO C C   1 
ATOM   3280  O O   . PRO C 3 14  ? -104.557 30.664   -30.816 1.00 180.70 ? 14  PRO C O   1 
ATOM   3281  C CB  . PRO C 3 14  ? -101.894 32.307   -31.659 1.00 175.11 ? 14  PRO C CB  1 
ATOM   3282  C CG  . PRO C 3 14  ? -101.544 32.582   -33.082 1.00 179.21 ? 14  PRO C CG  1 
ATOM   3283  C CD  . PRO C 3 14  ? -102.530 31.784   -33.870 1.00 175.47 ? 14  PRO C CD  1 
ATOM   3284  N N   . GLY C 3 15  ? -102.862 30.153   -29.401 1.00 172.86 ? 15  GLY C N   1 
ATOM   3285  C CA  . GLY C 3 15  ? -103.664 29.791   -28.239 1.00 174.03 ? 15  GLY C CA  1 
ATOM   3286  C C   . GLY C 3 15  ? -103.761 28.290   -28.058 1.00 175.02 ? 15  GLY C C   1 
ATOM   3287  O O   . GLY C 3 15  ? -103.836 27.806   -26.926 1.00 174.50 ? 15  GLY C O   1 
ATOM   3288  N N   . GLU C 3 16  ? -103.737 27.548   -29.186 1.00 169.63 ? 16  GLU C N   1 
ATOM   3289  C CA  . GLU C 3 16  ? -103.841 26.088   -29.270 1.00 167.27 ? 16  GLU C CA  1 
ATOM   3290  C C   . GLU C 3 16  ? -102.734 25.326   -28.534 1.00 168.71 ? 16  GLU C C   1 
ATOM   3291  O O   . GLU C 3 16  ? -101.699 25.902   -28.194 1.00 167.19 ? 16  GLU C O   1 
ATOM   3292  C CB  . GLU C 3 16  ? -103.903 25.641   -30.740 1.00 167.84 ? 16  GLU C CB  1 
ATOM   3293  C CG  . GLU C 3 16  ? -105.267 25.805   -31.385 1.00 181.59 ? 16  GLU C CG  1 
ATOM   3294  C CD  . GLU C 3 16  ? -105.357 25.218   -32.779 1.00 201.69 ? 16  GLU C CD  1 
ATOM   3295  O OE1 . GLU C 3 16  ? -105.179 25.979   -33.757 1.00 199.84 ? 16  GLU C OE1 1 
ATOM   3296  O OE2 . GLU C 3 16  ? -105.591 23.993   -32.894 1.00 191.64 ? 16  GLU C OE2 1 
ATOM   3297  N N   . SER C 3 17  ? -102.969 24.021   -28.293 1.00 164.76 ? 17  SER C N   1 
ATOM   3298  C CA  . SER C 3 17  ? -102.031 23.117   -27.631 1.00 162.42 ? 17  SER C CA  1 
ATOM   3299  C C   . SER C 3 17  ? -101.427 22.156   -28.655 1.00 163.05 ? 17  SER C C   1 
ATOM   3300  O O   . SER C 3 17  ? -102.160 21.461   -29.367 1.00 162.14 ? 17  SER C O   1 
ATOM   3301  C CB  . SER C 3 17  ? -102.721 22.348   -26.507 1.00 168.13 ? 17  SER C CB  1 
ATOM   3302  O OG  . SER C 3 17  ? -101.810 21.525   -25.794 1.00 177.93 ? 17  SER C OG  1 
ATOM   3303  N N   . LEU C 3 18  ? -100.087 22.143   -28.735 1.00 158.00 ? 18  LEU C N   1 
ATOM   3304  C CA  . LEU C 3 18  ? -99.313  21.310   -29.658 1.00 155.69 ? 18  LEU C CA  1 
ATOM   3305  C C   . LEU C 3 18  ? -98.184  20.595   -28.912 1.00 158.53 ? 18  LEU C C   1 
ATOM   3306  O O   . LEU C 3 18  ? -97.570  21.186   -28.028 1.00 158.26 ? 18  LEU C O   1 
ATOM   3307  C CB  . LEU C 3 18  ? -98.725  22.198   -30.777 1.00 155.34 ? 18  LEU C CB  1 
ATOM   3308  C CG  . LEU C 3 18  ? -98.011  21.492   -31.932 1.00 157.63 ? 18  LEU C CG  1 
ATOM   3309  C CD1 . LEU C 3 18  ? -98.988  21.102   -33.023 1.00 158.91 ? 18  LEU C CD1 1 
ATOM   3310  C CD2 . LEU C 3 18  ? -96.921  22.367   -32.499 1.00 158.35 ? 18  LEU C CD2 1 
ATOM   3311  N N   . THR C 3 19  ? -97.909  19.333   -29.278 1.00 153.87 ? 19  THR C N   1 
ATOM   3312  C CA  . THR C 3 19  ? -96.817  18.533   -28.703 1.00 152.04 ? 19  THR C CA  1 
ATOM   3313  C C   . THR C 3 19  ? -96.054  17.846   -29.843 1.00 152.30 ? 19  THR C C   1 
ATOM   3314  O O   . THR C 3 19  ? -96.668  17.134   -30.645 1.00 152.41 ? 19  THR C O   1 
ATOM   3315  C CB  . THR C 3 19  ? -97.293  17.601   -27.555 1.00 162.88 ? 19  THR C CB  1 
ATOM   3316  O OG1 . THR C 3 19  ? -96.212  16.759   -27.137 1.00 161.07 ? 19  THR C OG1 1 
ATOM   3317  C CG2 . THR C 3 19  ? -98.518  16.753   -27.918 1.00 163.10 ? 19  THR C CG2 1 
ATOM   3318  N N   . ILE C 3 20  ? -94.730  18.110   -29.947 1.00 145.00 ? 20  ILE C N   1 
ATOM   3319  C CA  . ILE C 3 20  ? -93.887  17.555   -31.014 1.00 142.13 ? 20  ILE C CA  1 
ATOM   3320  C C   . ILE C 3 20  ? -92.894  16.534   -30.478 1.00 142.95 ? 20  ILE C C   1 
ATOM   3321  O O   . ILE C 3 20  ? -92.224  16.782   -29.476 1.00 142.30 ? 20  ILE C O   1 
ATOM   3322  C CB  . ILE C 3 20  ? -93.211  18.637   -31.903 1.00 144.54 ? 20  ILE C CB  1 
ATOM   3323  C CG1 . ILE C 3 20  ? -92.448  19.695   -31.066 1.00 144.74 ? 20  ILE C CG1 1 
ATOM   3324  C CG2 . ILE C 3 20  ? -94.251  19.283   -32.831 1.00 146.37 ? 20  ILE C CG2 1 
ATOM   3325  C CD1 . ILE C 3 20  ? -91.363  20.454   -31.808 1.00 150.77 ? 20  ILE C CD1 1 
ATOM   3326  N N   . SER C 3 21  ? -92.832  15.373   -31.151 1.00 138.10 ? 21  SER C N   1 
ATOM   3327  C CA  . SER C 3 21  ? -91.971  14.241   -30.812 1.00 137.30 ? 21  SER C CA  1 
ATOM   3328  C C   . SER C 3 21  ? -90.569  14.332   -31.419 1.00 140.25 ? 21  SER C C   1 
ATOM   3329  O O   . SER C 3 21  ? -90.299  15.208   -32.243 1.00 139.38 ? 21  SER C O   1 
ATOM   3330  C CB  . SER C 3 21  ? -92.645  12.922   -31.181 1.00 140.85 ? 21  SER C CB  1 
ATOM   3331  O OG  . SER C 3 21  ? -93.081  12.909   -32.530 1.00 148.79 ? 21  SER C OG  1 
ATOM   3332  N N   . CYS C 3 22  ? -89.676  13.429   -30.976 1.00 136.88 ? 22  CYS C N   1 
ATOM   3333  C CA  . CYS C 3 22  ? -88.270  13.303   -31.361 1.00 136.38 ? 22  CYS C CA  1 
ATOM   3334  C C   . CYS C 3 22  ? -87.903  11.875   -30.935 1.00 139.96 ? 22  CYS C C   1 
ATOM   3335  O O   . CYS C 3 22  ? -87.815  11.601   -29.741 1.00 139.99 ? 22  CYS C O   1 
ATOM   3336  C CB  . CYS C 3 22  ? -87.438  14.371   -30.641 1.00 136.65 ? 22  CYS C CB  1 
ATOM   3337  S SG  . CYS C 3 22  ? -85.683  13.965   -30.413 1.00 141.92 ? 22  CYS C SG  1 
ATOM   3338  N N   . LYS C 3 23  ? -87.805  10.950   -31.909 1.00 136.19 ? 23  LYS C N   1 
ATOM   3339  C CA  . LYS C 3 23  ? -87.571  9.519    -31.685 1.00 136.97 ? 23  LYS C CA  1 
ATOM   3340  C C   . LYS C 3 23  ? -86.122  9.059    -31.890 1.00 141.47 ? 23  LYS C C   1 
ATOM   3341  O O   . LYS C 3 23  ? -85.620  9.047    -33.017 1.00 139.94 ? 23  LYS C O   1 
ATOM   3342  C CB  . LYS C 3 23  ? -88.529  8.687    -32.561 1.00 139.62 ? 23  LYS C CB  1 
ATOM   3343  C CG  . LYS C 3 23  ? -89.060  7.430    -31.889 1.00 150.92 ? 23  LYS C CG  1 
ATOM   3344  C CD  . LYS C 3 23  ? -88.282  6.191    -32.286 1.00 160.48 ? 23  LYS C CD  1 
ATOM   3345  C CE  . LYS C 3 23  ? -88.859  4.957    -31.645 1.00 169.63 ? 23  LYS C CE  1 
ATOM   3346  N NZ  . LYS C 3 23  ? -87.955  3.788    -31.797 1.00 180.27 ? 23  LYS C NZ  1 
ATOM   3347  N N   . GLY C 3 24  ? -85.490  8.650    -30.789 1.00 140.54 ? 24  GLY C N   1 
ATOM   3348  C CA  . GLY C 3 24  ? -84.122  8.142    -30.766 1.00 142.28 ? 24  GLY C CA  1 
ATOM   3349  C C   . GLY C 3 24  ? -84.050  6.750    -31.351 1.00 148.29 ? 24  GLY C C   1 
ATOM   3350  O O   . GLY C 3 24  ? -84.805  5.869    -30.930 1.00 148.95 ? 24  GLY C O   1 
ATOM   3351  N N   . SER C 3 25  ? -83.157  6.548    -32.337 1.00 145.32 ? 25  SER C N   1 
ATOM   3352  C CA  . SER C 3 25  ? -83.025  5.270    -33.042 1.00 146.64 ? 25  SER C CA  1 
ATOM   3353  C C   . SER C 3 25  ? -81.593  4.717    -33.122 1.00 152.03 ? 25  SER C C   1 
ATOM   3354  O O   . SER C 3 25  ? -80.641  5.463    -33.358 1.00 151.08 ? 25  SER C O   1 
ATOM   3355  C CB  . SER C 3 25  ? -83.620  5.369    -34.447 1.00 149.19 ? 25  SER C CB  1 
ATOM   3356  O OG  . SER C 3 25  ? -84.776  6.192    -34.514 1.00 154.20 ? 25  SER C OG  1 
ATOM   3357  N N   . GLY C 3 26  ? -81.480  3.399    -32.958 1.00 150.83 ? 26  GLY C N   1 
ATOM   3358  C CA  . GLY C 3 26  ? -80.228  2.654    -33.047 1.00 153.30 ? 26  GLY C CA  1 
ATOM   3359  C C   . GLY C 3 26  ? -79.220  2.864    -31.934 1.00 158.14 ? 26  GLY C C   1 
ATOM   3360  O O   . GLY C 3 26  ? -78.036  2.567    -32.125 1.00 160.14 ? 26  GLY C O   1 
ATOM   3361  N N   . TYR C 3 27  ? -79.674  3.359    -30.760 1.00 152.94 ? 27  TYR C N   1 
ATOM   3362  C CA  . TYR C 3 27  ? -78.818  3.602    -29.591 1.00 154.00 ? 27  TYR C CA  1 
ATOM   3363  C C   . TYR C 3 27  ? -79.598  3.542    -28.256 1.00 157.80 ? 27  TYR C C   1 
ATOM   3364  O O   . TYR C 3 27  ? -80.832  3.616    -28.256 1.00 155.31 ? 27  TYR C O   1 
ATOM   3365  C CB  . TYR C 3 27  ? -78.047  4.935    -29.747 1.00 153.45 ? 27  TYR C CB  1 
ATOM   3366  C CG  . TYR C 3 27  ? -78.809  6.160    -29.292 1.00 152.06 ? 27  TYR C CG  1 
ATOM   3367  C CD1 . TYR C 3 27  ? -79.798  6.729    -30.091 1.00 151.12 ? 27  TYR C CD1 1 
ATOM   3368  C CD2 . TYR C 3 27  ? -78.538  6.756    -28.065 1.00 153.37 ? 27  TYR C CD2 1 
ATOM   3369  C CE1 . TYR C 3 27  ? -80.506  7.854    -29.672 1.00 149.43 ? 27  TYR C CE1 1 
ATOM   3370  C CE2 . TYR C 3 27  ? -79.241  7.878    -27.635 1.00 151.88 ? 27  TYR C CE2 1 
ATOM   3371  C CZ  . TYR C 3 27  ? -80.219  8.427    -28.444 1.00 154.12 ? 27  TYR C CZ  1 
ATOM   3372  O OH  . TYR C 3 27  ? -80.906  9.530    -28.011 1.00 150.76 ? 27  TYR C OH  1 
ATOM   3373  N N   . SER C 3 28  ? -78.866  3.435    -27.121 1.00 156.84 ? 28  SER C N   1 
ATOM   3374  C CA  . SER C 3 28  ? -79.448  3.409    -25.777 1.00 157.39 ? 28  SER C CA  1 
ATOM   3375  C C   . SER C 3 28  ? -79.891  4.824    -25.413 1.00 159.16 ? 28  SER C C   1 
ATOM   3376  O O   . SER C 3 28  ? -79.136  5.586    -24.803 1.00 159.49 ? 28  SER C O   1 
ATOM   3377  C CB  . SER C 3 28  ? -78.450  2.862    -24.760 1.00 164.91 ? 28  SER C CB  1 
ATOM   3378  O OG  . SER C 3 28  ? -78.997  2.882    -23.450 1.00 174.41 ? 28  SER C OG  1 
ATOM   3379  N N   . PHE C 3 29  ? -81.116  5.173    -25.843 1.00 153.67 ? 29  PHE C N   1 
ATOM   3380  C CA  . PHE C 3 29  ? -81.777  6.473    -25.678 1.00 151.51 ? 29  PHE C CA  1 
ATOM   3381  C C   . PHE C 3 29  ? -81.683  7.051    -24.271 1.00 157.04 ? 29  PHE C C   1 
ATOM   3382  O O   . PHE C 3 29  ? -81.465  8.256    -24.116 1.00 155.89 ? 29  PHE C O   1 
ATOM   3383  C CB  . PHE C 3 29  ? -83.241  6.365    -26.126 1.00 151.18 ? 29  PHE C CB  1 
ATOM   3384  C CG  . PHE C 3 29  ? -84.059  7.634    -26.093 1.00 150.33 ? 29  PHE C CG  1 
ATOM   3385  C CD1 . PHE C 3 29  ? -83.983  8.554    -27.128 1.00 151.28 ? 29  PHE C CD1 1 
ATOM   3386  C CD2 . PHE C 3 29  ? -84.944  7.882    -25.052 1.00 152.49 ? 29  PHE C CD2 1 
ATOM   3387  C CE1 . PHE C 3 29  ? -84.762  9.712    -27.111 1.00 150.49 ? 29  PHE C CE1 1 
ATOM   3388  C CE2 . PHE C 3 29  ? -85.736  9.031    -25.046 1.00 153.57 ? 29  PHE C CE2 1 
ATOM   3389  C CZ  . PHE C 3 29  ? -85.635  9.941    -26.073 1.00 149.77 ? 29  PHE C CZ  1 
ATOM   3390  N N   . SER C 3 30  ? -81.833  6.176    -23.261 1.00 157.58 ? 30  SER C N   1 
ATOM   3391  C CA  . SER C 3 30  ? -81.809  6.495    -21.837 1.00 158.41 ? 30  SER C CA  1 
ATOM   3392  C C   . SER C 3 30  ? -80.432  6.932    -21.319 1.00 162.34 ? 30  SER C C   1 
ATOM   3393  O O   . SER C 3 30  ? -80.367  7.738    -20.388 1.00 161.13 ? 30  SER C O   1 
ATOM   3394  C CB  . SER C 3 30  ? -82.334  5.315    -21.028 1.00 167.17 ? 30  SER C CB  1 
ATOM   3395  O OG  . SER C 3 30  ? -83.664  4.962    -21.375 1.00 175.27 ? 30  SER C OG  1 
ATOM   3396  N N   . SER C 3 31  ? -79.342  6.413    -21.918 1.00 160.18 ? 31  SER C N   1 
ATOM   3397  C CA  . SER C 3 31  ? -77.966  6.723    -21.514 1.00 161.70 ? 31  SER C CA  1 
ATOM   3398  C C   . SER C 3 31  ? -77.579  8.193    -21.740 1.00 159.01 ? 31  SER C C   1 
ATOM   3399  O O   . SER C 3 31  ? -77.076  8.843    -20.818 1.00 158.97 ? 31  SER C O   1 
ATOM   3400  C CB  . SER C 3 31  ? -76.975  5.795    -22.213 1.00 169.66 ? 31  SER C CB  1 
ATOM   3401  O OG  . SER C 3 31  ? -77.025  4.477    -21.690 1.00 184.72 ? 31  SER C OG  1 
ATOM   3402  N N   . TYR C 3 32  ? -77.838  8.711    -22.954 1.00 149.83 ? 32  TYR C N   1 
ATOM   3403  C CA  . TYR C 3 32  ? -77.499  10.072   -23.362 1.00 144.84 ? 32  TYR C CA  1 
ATOM   3404  C C   . TYR C 3 32  ? -78.634  11.050   -23.129 1.00 141.94 ? 32  TYR C C   1 
ATOM   3405  O O   . TYR C 3 32  ? -79.801  10.705   -23.328 1.00 139.67 ? 32  TYR C O   1 
ATOM   3406  C CB  . TYR C 3 32  ? -77.125  10.098   -24.846 1.00 145.31 ? 32  TYR C CB  1 
ATOM   3407  C CG  . TYR C 3 32  ? -76.001  9.168    -25.247 1.00 152.82 ? 32  TYR C CG  1 
ATOM   3408  C CD1 . TYR C 3 32  ? -74.689  9.628    -25.339 1.00 156.99 ? 32  TYR C CD1 1 
ATOM   3409  C CD2 . TYR C 3 32  ? -76.258  7.849    -25.620 1.00 156.82 ? 32  TYR C CD2 1 
ATOM   3410  C CE1 . TYR C 3 32  ? -73.652  8.787    -25.749 1.00 163.06 ? 32  TYR C CE1 1 
ATOM   3411  C CE2 . TYR C 3 32  ? -75.231  6.999    -26.035 1.00 162.74 ? 32  TYR C CE2 1 
ATOM   3412  C CZ  . TYR C 3 32  ? -73.928  7.473    -26.096 1.00 171.91 ? 32  TYR C CZ  1 
ATOM   3413  O OH  . TYR C 3 32  ? -72.896  6.651    -26.487 1.00 177.83 ? 32  TYR C OH  1 
ATOM   3414  N N   . TRP C 3 33  ? -78.283  12.289   -22.765 1.00 136.08 ? 33  TRP C N   1 
ATOM   3415  C CA  . TRP C 3 33  ? -79.239  13.372   -22.547 1.00 132.64 ? 33  TRP C CA  1 
ATOM   3416  C C   . TRP C 3 33  ? -79.807  13.842   -23.888 1.00 132.08 ? 33  TRP C C   1 
ATOM   3417  O O   . TRP C 3 33  ? -79.123  13.738   -24.910 1.00 132.56 ? 33  TRP C O   1 
ATOM   3418  C CB  . TRP C 3 33  ? -78.542  14.557   -21.866 1.00 131.55 ? 33  TRP C CB  1 
ATOM   3419  C CG  . TRP C 3 33  ? -78.204  14.345   -20.421 1.00 136.52 ? 33  TRP C CG  1 
ATOM   3420  C CD1 . TRP C 3 33  ? -77.199  13.571   -19.918 1.00 143.97 ? 33  TRP C CD1 1 
ATOM   3421  C CD2 . TRP C 3 33  ? -78.813  14.993   -19.296 1.00 136.25 ? 33  TRP C CD2 1 
ATOM   3422  N NE1 . TRP C 3 33  ? -77.176  13.659   -18.544 1.00 145.92 ? 33  TRP C NE1 1 
ATOM   3423  C CE2 . TRP C 3 33  ? -78.149  14.534   -18.136 1.00 144.40 ? 33  TRP C CE2 1 
ATOM   3424  C CE3 . TRP C 3 33  ? -79.873  15.904   -19.152 1.00 134.87 ? 33  TRP C CE3 1 
ATOM   3425  C CZ2 . TRP C 3 33  ? -78.510  14.952   -16.851 1.00 145.06 ? 33  TRP C CZ2 1 
ATOM   3426  C CZ3 . TRP C 3 33  ? -80.232  16.316   -17.877 1.00 137.72 ? 33  TRP C CZ3 1 
ATOM   3427  C CH2 . TRP C 3 33  ? -79.557  15.839   -16.745 1.00 142.39 ? 33  TRP C CH2 1 
ATOM   3428  N N   . ILE C 3 34  ? -81.049  14.361   -23.887 1.00 124.14 ? 34  ILE C N   1 
ATOM   3429  C CA  . ILE C 3 34  ? -81.692  14.904   -25.092 1.00 120.21 ? 34  ILE C CA  1 
ATOM   3430  C C   . ILE C 3 34  ? -82.083  16.358   -24.850 1.00 120.75 ? 34  ILE C C   1 
ATOM   3431  O O   . ILE C 3 34  ? -82.807  16.654   -23.908 1.00 119.78 ? 34  ILE C O   1 
ATOM   3432  C CB  . ILE C 3 34  ? -82.890  14.043   -25.599 1.00 123.28 ? 34  ILE C CB  1 
ATOM   3433  C CG1 . ILE C 3 34  ? -82.450  12.622   -26.037 1.00 126.24 ? 34  ILE C CG1 1 
ATOM   3434  C CG2 . ILE C 3 34  ? -83.702  14.758   -26.703 1.00 121.41 ? 34  ILE C CG2 1 
ATOM   3435  C CD1 . ILE C 3 34  ? -81.537  12.527   -27.275 1.00 131.66 ? 34  ILE C CD1 1 
ATOM   3436  N N   . GLY C 3 35  ? -81.600  17.241   -25.708 1.00 116.49 ? 35  GLY C N   1 
ATOM   3437  C CA  . GLY C 3 35  ? -81.888  18.665   -25.628 1.00 115.01 ? 35  GLY C CA  1 
ATOM   3438  C C   . GLY C 3 35  ? -82.867  19.141   -26.677 1.00 118.58 ? 35  GLY C C   1 
ATOM   3439  O O   . GLY C 3 35  ? -83.391  18.336   -27.450 1.00 118.50 ? 35  GLY C O   1 
ATOM   3440  N N   . TRP C 3 36  ? -83.120  20.459   -26.704 1.00 114.83 ? 36  TRP C N   1 
ATOM   3441  C CA  . TRP C 3 36  ? -84.026  21.081   -27.663 1.00 114.86 ? 36  TRP C CA  1 
ATOM   3442  C C   . TRP C 3 36  ? -83.528  22.466   -28.063 1.00 116.80 ? 36  TRP C C   1 
ATOM   3443  O O   . TRP C 3 36  ? -83.265  23.296   -27.193 1.00 116.84 ? 36  TRP C O   1 
ATOM   3444  C CB  . TRP C 3 36  ? -85.449  21.149   -27.101 1.00 115.20 ? 36  TRP C CB  1 
ATOM   3445  C CG  . TRP C 3 36  ? -86.211  19.859   -27.197 1.00 117.83 ? 36  TRP C CG  1 
ATOM   3446  C CD1 . TRP C 3 36  ? -86.300  18.891   -26.241 1.00 121.94 ? 36  TRP C CD1 1 
ATOM   3447  C CD2 . TRP C 3 36  ? -87.023  19.413   -28.296 1.00 118.77 ? 36  TRP C CD2 1 
ATOM   3448  N NE1 . TRP C 3 36  ? -87.110  17.866   -26.676 1.00 122.68 ? 36  TRP C NE1 1 
ATOM   3449  C CE2 . TRP C 3 36  ? -87.569  18.160   -27.934 1.00 123.93 ? 36  TRP C CE2 1 
ATOM   3450  C CE3 . TRP C 3 36  ? -87.340  19.947   -29.557 1.00 120.52 ? 36  TRP C CE3 1 
ATOM   3451  C CZ2 . TRP C 3 36  ? -88.413  17.434   -28.786 1.00 124.48 ? 36  TRP C CZ2 1 
ATOM   3452  C CZ3 . TRP C 3 36  ? -88.167  19.222   -30.404 1.00 123.45 ? 36  TRP C CZ3 1 
ATOM   3453  C CH2 . TRP C 3 36  ? -88.697  17.983   -30.016 1.00 124.99 ? 36  TRP C CH2 1 
ATOM   3454  N N   . VAL C 3 37  ? -83.373  22.706   -29.380 1.00 111.42 ? 37  VAL C N   1 
ATOM   3455  C CA  . VAL C 3 37  ? -82.883  23.969   -29.936 1.00 110.59 ? 37  VAL C CA  1 
ATOM   3456  C C   . VAL C 3 37  ? -83.886  24.573   -30.944 1.00 115.10 ? 37  VAL C C   1 
ATOM   3457  O O   . VAL C 3 37  ? -84.221  23.940   -31.947 1.00 115.10 ? 37  VAL C O   1 
ATOM   3458  C CB  . VAL C 3 37  ? -81.450  23.816   -30.521 1.00 114.24 ? 37  VAL C CB  1 
ATOM   3459  C CG1 . VAL C 3 37  ? -80.988  25.092   -31.210 1.00 114.93 ? 37  VAL C CG1 1 
ATOM   3460  C CG2 . VAL C 3 37  ? -80.447  23.410   -29.444 1.00 113.77 ? 37  VAL C CG2 1 
ATOM   3461  N N   . ARG C 3 38  ? -84.363  25.801   -30.655 1.00 112.47 ? 38  ARG C N   1 
ATOM   3462  C CA  . ARG C 3 38  ? -85.292  26.578   -31.481 1.00 114.23 ? 38  ARG C CA  1 
ATOM   3463  C C   . ARG C 3 38  ? -84.497  27.475   -32.434 1.00 120.54 ? 38  ARG C C   1 
ATOM   3464  O O   . ARG C 3 38  ? -83.385  27.885   -32.117 1.00 120.45 ? 38  ARG C O   1 
ATOM   3465  C CB  . ARG C 3 38  ? -86.222  27.428   -30.582 1.00 115.21 ? 38  ARG C CB  1 
ATOM   3466  C CG  . ARG C 3 38  ? -86.982  28.556   -31.294 1.00 127.49 ? 38  ARG C CG  1 
ATOM   3467  C CD  . ARG C 3 38  ? -88.139  29.102   -30.489 1.00 138.31 ? 38  ARG C CD  1 
ATOM   3468  N NE  . ARG C 3 38  ? -87.910  30.478   -30.055 1.00 147.71 ? 38  ARG C NE  1 
ATOM   3469  C CZ  . ARG C 3 38  ? -88.822  31.233   -29.452 1.00 164.65 ? 38  ARG C CZ  1 
ATOM   3470  N NH1 . ARG C 3 38  ? -90.038  30.756   -29.213 1.00 147.78 ? 38  ARG C NH1 1 
ATOM   3471  N NH2 . ARG C 3 38  ? -88.527  32.473   -29.085 1.00 158.08 ? 38  ARG C NH2 1 
ATOM   3472  N N   . ARG C 3 39  ? -85.078  27.779   -33.591 1.00 119.61 ? 39  ARG C N   1 
ATOM   3473  C CA  . ARG C 3 39  ? -84.511  28.656   -34.602 1.00 121.72 ? 39  ARG C CA  1 
ATOM   3474  C C   . ARG C 3 39  ? -85.678  29.470   -35.153 1.00 131.18 ? 39  ARG C C   1 
ATOM   3475  O O   . ARG C 3 39  ? -86.579  28.918   -35.792 1.00 132.80 ? 39  ARG C O   1 
ATOM   3476  C CB  . ARG C 3 39  ? -83.780  27.830   -35.694 1.00 121.12 ? 39  ARG C CB  1 
ATOM   3477  C CG  . ARG C 3 39  ? -83.636  28.486   -37.081 1.00 127.80 ? 39  ARG C CG  1 
ATOM   3478  C CD  . ARG C 3 39  ? -82.448  29.409   -37.190 1.00 123.93 ? 39  ARG C CD  1 
ATOM   3479  N NE  . ARG C 3 39  ? -81.214  28.666   -37.429 1.00 120.70 ? 39  ARG C NE  1 
ATOM   3480  C CZ  . ARG C 3 39  ? -80.004  29.214   -37.455 1.00 136.14 ? 39  ARG C CZ  1 
ATOM   3481  N NH1 . ARG C 3 39  ? -79.851  30.517   -37.251 1.00 126.27 ? 39  ARG C NH1 1 
ATOM   3482  N NH2 . ARG C 3 39  ? -78.935  28.463   -37.677 1.00 122.52 ? 39  ARG C NH2 1 
ATOM   3483  N N   . MET C 3 40  ? -85.695  30.767   -34.853 1.00 130.15 ? 40  MET C N   1 
ATOM   3484  C CA  . MET C 3 40  ? -86.760  31.629   -35.348 1.00 134.26 ? 40  MET C CA  1 
ATOM   3485  C C   . MET C 3 40  ? -86.447  32.143   -36.763 1.00 141.28 ? 40  MET C C   1 
ATOM   3486  O O   . MET C 3 40  ? -85.268  32.309   -37.084 1.00 140.05 ? 40  MET C O   1 
ATOM   3487  C CB  . MET C 3 40  ? -87.051  32.764   -34.362 1.00 138.11 ? 40  MET C CB  1 
ATOM   3488  C CG  . MET C 3 40  ? -88.162  32.416   -33.400 1.00 141.58 ? 40  MET C CG  1 
ATOM   3489  S SD  . MET C 3 40  ? -89.169  33.835   -32.913 1.00 150.80 ? 40  MET C SD  1 
ATOM   3490  C CE  . MET C 3 40  ? -90.106  34.121   -34.403 1.00 152.76 ? 40  MET C CE  1 
ATOM   3491  N N   . PRO C 3 41  ? -87.464  32.367   -37.636 1.00 142.30 ? 41  PRO C N   1 
ATOM   3492  C CA  . PRO C 3 41  ? -87.172  32.834   -39.003 1.00 145.87 ? 41  PRO C CA  1 
ATOM   3493  C C   . PRO C 3 41  ? -86.351  34.119   -39.070 1.00 151.07 ? 41  PRO C C   1 
ATOM   3494  O O   . PRO C 3 41  ? -86.791  35.176   -38.609 1.00 153.37 ? 41  PRO C O   1 
ATOM   3495  C CB  . PRO C 3 41  ? -88.562  32.991   -39.640 1.00 152.66 ? 41  PRO C CB  1 
ATOM   3496  C CG  . PRO C 3 41  ? -89.506  33.072   -38.495 1.00 156.94 ? 41  PRO C CG  1 
ATOM   3497  C CD  . PRO C 3 41  ? -88.916  32.188   -37.444 1.00 146.38 ? 41  PRO C CD  1 
ATOM   3498  N N   . GLY C 3 42  ? -85.145  33.988   -39.617 1.00 145.75 ? 42  GLY C N   1 
ATOM   3499  C CA  . GLY C 3 42  ? -84.197  35.083   -39.770 1.00 147.07 ? 42  GLY C CA  1 
ATOM   3500  C C   . GLY C 3 42  ? -83.551  35.495   -38.466 1.00 147.29 ? 42  GLY C C   1 
ATOM   3501  O O   . GLY C 3 42  ? -83.268  36.678   -38.266 1.00 149.59 ? 42  GLY C O   1 
ATOM   3502  N N   . LYS C 3 43  ? -83.325  34.519   -37.569 1.00 138.66 ? 43  LYS C N   1 
ATOM   3503  C CA  . LYS C 3 43  ? -82.705  34.719   -36.257 1.00 135.77 ? 43  LYS C CA  1 
ATOM   3504  C C   . LYS C 3 43  ? -81.704  33.597   -35.946 1.00 135.53 ? 43  LYS C C   1 
ATOM   3505  O O   . LYS C 3 43  ? -81.561  32.669   -36.742 1.00 134.87 ? 43  LYS C O   1 
ATOM   3506  C CB  . LYS C 3 43  ? -83.780  34.848   -35.158 1.00 137.98 ? 43  LYS C CB  1 
ATOM   3507  C CG  . LYS C 3 43  ? -84.353  36.258   -35.026 1.00 154.80 ? 43  LYS C CG  1 
ATOM   3508  C CD  . LYS C 3 43  ? -85.721  36.397   -35.691 1.00 166.81 ? 43  LYS C CD  1 
ATOM   3509  C CE  . LYS C 3 43  ? -86.033  37.821   -36.108 1.00 180.59 ? 43  LYS C CE  1 
ATOM   3510  N NZ  . LYS C 3 43  ? -86.344  38.712   -34.957 1.00 189.88 ? 43  LYS C NZ  1 
ATOM   3511  N N   . GLY C 3 44  ? -81.001  33.713   -34.820 1.00 129.58 ? 44  GLY C N   1 
ATOM   3512  C CA  . GLY C 3 44  ? -80.012  32.731   -34.389 1.00 126.10 ? 44  GLY C CA  1 
ATOM   3513  C C   . GLY C 3 44  ? -80.609  31.534   -33.674 1.00 126.32 ? 44  GLY C C   1 
ATOM   3514  O O   . GLY C 3 44  ? -81.820  31.491   -33.420 1.00 126.68 ? 44  GLY C O   1 
ATOM   3515  N N   . LEU C 3 45  ? -79.754  30.547   -33.344 1.00 119.05 ? 45  LEU C N   1 
ATOM   3516  C CA  . LEU C 3 45  ? -80.166  29.336   -32.636 1.00 115.78 ? 45  LEU C CA  1 
ATOM   3517  C C   . LEU C 3 45  ? -80.319  29.604   -31.143 1.00 119.93 ? 45  LEU C C   1 
ATOM   3518  O O   . LEU C 3 45  ? -79.394  30.093   -30.491 1.00 119.33 ? 45  LEU C O   1 
ATOM   3519  C CB  . LEU C 3 45  ? -79.199  28.169   -32.884 1.00 114.29 ? 45  LEU C CB  1 
ATOM   3520  C CG  . LEU C 3 45  ? -79.170  27.618   -34.298 1.00 119.17 ? 45  LEU C CG  1 
ATOM   3521  C CD1 . LEU C 3 45  ? -77.880  26.902   -34.566 1.00 119.94 ? 45  LEU C CD1 1 
ATOM   3522  C CD2 . LEU C 3 45  ? -80.342  26.709   -34.569 1.00 119.16 ? 45  LEU C CD2 1 
ATOM   3523  N N   . GLU C 3 46  ? -81.505  29.298   -30.617 1.00 117.25 ? 46  GLU C N   1 
ATOM   3524  C CA  . GLU C 3 46  ? -81.869  29.481   -29.219 1.00 117.08 ? 46  GLU C CA  1 
ATOM   3525  C C   . GLU C 3 46  ? -81.934  28.120   -28.550 1.00 119.87 ? 46  GLU C C   1 
ATOM   3526  O O   . GLU C 3 46  ? -82.591  27.219   -29.064 1.00 118.58 ? 46  GLU C O   1 
ATOM   3527  C CB  . GLU C 3 46  ? -83.239  30.182   -29.113 1.00 120.42 ? 46  GLU C CB  1 
ATOM   3528  C CG  . GLU C 3 46  ? -83.293  31.564   -29.748 1.00 138.57 ? 46  GLU C CG  1 
ATOM   3529  C CD  . GLU C 3 46  ? -84.678  32.061   -30.119 1.00 173.11 ? 46  GLU C CD  1 
ATOM   3530  O OE1 . GLU C 3 46  ? -84.938  32.231   -31.333 1.00 179.38 ? 46  GLU C OE1 1 
ATOM   3531  O OE2 . GLU C 3 46  ? -85.496  32.302   -29.200 1.00 167.60 ? 46  GLU C OE2 1 
ATOM   3532  N N   . TRP C 3 47  ? -81.252  27.958   -27.416 1.00 117.58 ? 47  TRP C N   1 
ATOM   3533  C CA  . TRP C 3 47  ? -81.291  26.702   -26.673 1.00 117.32 ? 47  TRP C CA  1 
ATOM   3534  C C   . TRP C 3 47  ? -82.481  26.734   -25.700 1.00 122.05 ? 47  TRP C C   1 
ATOM   3535  O O   . TRP C 3 47  ? -82.685  27.733   -25.004 1.00 122.18 ? 47  TRP C O   1 
ATOM   3536  C CB  . TRP C 3 47  ? -79.965  26.469   -25.954 1.00 116.57 ? 47  TRP C CB  1 
ATOM   3537  C CG  . TRP C 3 47  ? -79.896  25.220   -25.132 1.00 117.81 ? 47  TRP C CG  1 
ATOM   3538  C CD1 . TRP C 3 47  ? -79.503  23.985   -25.554 1.00 120.96 ? 47  TRP C CD1 1 
ATOM   3539  C CD2 . TRP C 3 47  ? -80.145  25.103   -23.720 1.00 118.82 ? 47  TRP C CD2 1 
ATOM   3540  N NE1 . TRP C 3 47  ? -79.534  23.094   -24.504 1.00 121.29 ? 47  TRP C NE1 1 
ATOM   3541  C CE2 . TRP C 3 47  ? -79.905  23.758   -23.362 1.00 123.18 ? 47  TRP C CE2 1 
ATOM   3542  C CE3 . TRP C 3 47  ? -80.554  26.007   -22.720 1.00 120.77 ? 47  TRP C CE3 1 
ATOM   3543  C CZ2 . TRP C 3 47  ? -80.045  23.297   -22.044 1.00 123.56 ? 47  TRP C CZ2 1 
ATOM   3544  C CZ3 . TRP C 3 47  ? -80.708  25.546   -21.420 1.00 123.17 ? 47  TRP C CZ3 1 
ATOM   3545  C CH2 . TRP C 3 47  ? -80.459  24.206   -21.094 1.00 124.23 ? 47  TRP C CH2 1 
ATOM   3546  N N   . MET C 3 48  ? -83.276  25.654   -25.680 1.00 118.81 ? 48  MET C N   1 
ATOM   3547  C CA  . MET C 3 48  ? -84.474  25.559   -24.849 1.00 119.71 ? 48  MET C CA  1 
ATOM   3548  C C   . MET C 3 48  ? -84.284  24.810   -23.540 1.00 126.03 ? 48  MET C C   1 
ATOM   3549  O O   . MET C 3 48  ? -84.696  25.316   -22.503 1.00 126.58 ? 48  MET C O   1 
ATOM   3550  C CB  . MET C 3 48  ? -85.638  24.957   -25.638 1.00 122.09 ? 48  MET C CB  1 
ATOM   3551  C CG  . MET C 3 48  ? -86.117  25.837   -26.749 1.00 126.24 ? 48  MET C CG  1 
ATOM   3552  S SD  . MET C 3 48  ? -87.538  25.129   -27.590 1.00 131.46 ? 48  MET C SD  1 
ATOM   3553  C CE  . MET C 3 48  ? -86.712  24.072   -28.715 1.00 127.07 ? 48  MET C CE  1 
ATOM   3554  N N   . GLY C 3 49  ? -83.721  23.604   -23.599 1.00 123.90 ? 49  GLY C N   1 
ATOM   3555  C CA  . GLY C 3 49  ? -83.506  22.769   -22.420 1.00 125.04 ? 49  GLY C CA  1 
ATOM   3556  C C   . GLY C 3 49  ? -82.926  21.403   -22.721 1.00 129.14 ? 49  GLY C C   1 
ATOM   3557  O O   . GLY C 3 49  ? -82.649  21.087   -23.881 1.00 128.36 ? 49  GLY C O   1 
ATOM   3558  N N   . ILE C 3 50  ? -82.672  20.622   -21.673 1.00 126.57 ? 50  ILE C N   1 
ATOM   3559  C CA  . ILE C 3 50  ? -82.134  19.268   -21.782 1.00 127.87 ? 50  ILE C CA  1 
ATOM   3560  C C   . ILE C 3 50  ? -82.914  18.340   -20.853 1.00 135.26 ? 50  ILE C C   1 
ATOM   3561  O O   . ILE C 3 50  ? -83.484  18.801   -19.860 1.00 135.71 ? 50  ILE C O   1 
ATOM   3562  C CB  . ILE C 3 50  ? -80.599  19.189   -21.548 1.00 132.36 ? 50  ILE C CB  1 
ATOM   3563  C CG1 . ILE C 3 50  ? -80.168  19.923   -20.263 1.00 134.73 ? 50  ILE C CG1 1 
ATOM   3564  C CG2 . ILE C 3 50  ? -79.816  19.678   -22.762 1.00 131.68 ? 50  ILE C CG2 1 
ATOM   3565  C CD1 . ILE C 3 50  ? -78.901  19.371   -19.586 1.00 149.25 ? 50  ILE C CD1 1 
ATOM   3566  N N   . ILE C 3 51  ? -82.958  17.041   -21.185 1.00 134.21 ? 51  ILE C N   1 
ATOM   3567  C CA  . ILE C 3 51  ? -83.666  16.032   -20.396 1.00 136.85 ? 51  ILE C CA  1 
ATOM   3568  C C   . ILE C 3 51  ? -82.916  14.686   -20.446 1.00 143.88 ? 51  ILE C C   1 
ATOM   3569  O O   . ILE C 3 51  ? -82.515  14.238   -21.523 1.00 142.53 ? 51  ILE C O   1 
ATOM   3570  C CB  . ILE C 3 51  ? -85.193  15.938   -20.767 1.00 139.47 ? 51  ILE C CB  1 
ATOM   3571  C CG1 . ILE C 3 51  ? -85.994  15.108   -19.729 1.00 142.98 ? 51  ILE C CG1 1 
ATOM   3572  C CG2 . ILE C 3 51  ? -85.457  15.454   -22.205 1.00 138.73 ? 51  ILE C CG2 1 
ATOM   3573  C CD1 . ILE C 3 51  ? -87.477  15.524   -19.564 1.00 150.99 ? 51  ILE C CD1 1 
ATOM   3574  N N   . ASN C 3 52  ? -82.672  14.090   -19.265 1.00 144.65 ? 52  ASN C N   1 
ATOM   3575  C CA  . ASN C 3 52  ? -82.019  12.790   -19.141 1.00 148.51 ? 52  ASN C CA  1 
ATOM   3576  C C   . ASN C 3 52  ? -83.154  11.779   -19.138 1.00 155.34 ? 52  ASN C C   1 
ATOM   3577  O O   . ASN C 3 52  ? -83.908  11.758   -18.166 1.00 156.12 ? 52  ASN C O   1 
ATOM   3578  C CB  . ASN C 3 52  ? -81.203  12.698   -17.847 1.00 152.51 ? 52  ASN C CB  1 
ATOM   3579  C CG  . ASN C 3 52  ? -80.660  11.321   -17.549 1.00 175.58 ? 52  ASN C CG  1 
ATOM   3580  O OD1 . ASN C 3 52  ? -79.821  10.770   -18.275 1.00 172.26 ? 52  ASN C OD1 1 
ATOM   3581  N ND2 . ASN C 3 52  ? -81.119  10.741   -16.460 1.00 167.66 ? 52  ASN C ND2 1 
ATOM   3582  N N   . PRO C 3 53  ? -83.323  10.956   -20.205 1.00 153.52 ? 53  PRO C N   1 
ATOM   3583  C CA  . PRO C 3 53  ? -84.472  10.029   -20.248 1.00 155.56 ? 53  PRO C CA  1 
ATOM   3584  C C   . PRO C 3 53  ? -84.599  9.032    -19.078 1.00 165.38 ? 53  PRO C C   1 
ATOM   3585  O O   . PRO C 3 53  ? -85.722  8.611    -18.795 1.00 166.35 ? 53  PRO C O   1 
ATOM   3586  C CB  . PRO C 3 53  ? -84.310  9.330    -21.599 1.00 156.92 ? 53  PRO C CB  1 
ATOM   3587  C CG  . PRO C 3 53  ? -83.531  10.302   -22.422 1.00 157.79 ? 53  PRO C CG  1 
ATOM   3588  C CD  . PRO C 3 53  ? -82.551  10.892   -21.462 1.00 153.93 ? 53  PRO C CD  1 
ATOM   3589  N N   . ARG C 3 54  ? -83.489  8.722    -18.357 1.00 165.14 ? 54  ARG C N   1 
ATOM   3590  C CA  . ARG C 3 54  ? -83.508  7.831    -17.186 1.00 170.21 ? 54  ARG C CA  1 
ATOM   3591  C C   . ARG C 3 54  ? -84.274  8.482    -16.015 1.00 174.63 ? 54  ARG C C   1 
ATOM   3592  O O   . ARG C 3 54  ? -85.367  8.026    -15.676 1.00 175.59 ? 54  ARG C O   1 
ATOM   3593  C CB  . ARG C 3 54  ? -82.079  7.434    -16.749 1.00 173.58 ? 54  ARG C CB  1 
ATOM   3594  C CG  . ARG C 3 54  ? -81.389  6.424    -17.652 1.00 184.69 ? 54  ARG C CG  1 
ATOM   3595  C CD  . ARG C 3 54  ? -81.474  5.001    -17.139 1.00 202.02 ? 54  ARG C CD  1 
ATOM   3596  N NE  . ARG C 3 54  ? -80.743  4.080    -18.012 1.00 212.54 ? 54  ARG C NE  1 
ATOM   3597  C CZ  . ARG C 3 54  ? -81.301  3.092    -18.705 1.00 228.80 ? 54  ARG C CZ  1 
ATOM   3598  N NH1 . ARG C 3 54  ? -82.611  2.880    -18.639 1.00 214.42 ? 54  ARG C NH1 1 
ATOM   3599  N NH2 . ARG C 3 54  ? -80.557  2.317    -19.483 1.00 218.34 ? 54  ARG C NH2 1 
ATOM   3600  N N   . ASP C 3 55  ? -83.711  9.565    -15.432 1.00 169.97 ? 55  ASP C N   1 
ATOM   3601  C CA  . ASP C 3 55  ? -84.281  10.315   -14.307 1.00 169.93 ? 55  ASP C CA  1 
ATOM   3602  C C   . ASP C 3 55  ? -85.514  11.110   -14.705 1.00 168.77 ? 55  ASP C C   1 
ATOM   3603  O O   . ASP C 3 55  ? -86.301  11.488   -13.832 1.00 169.75 ? 55  ASP C O   1 
ATOM   3604  C CB  . ASP C 3 55  ? -83.243  11.301   -13.738 1.00 171.49 ? 55  ASP C CB  1 
ATOM   3605  C CG  . ASP C 3 55  ? -81.990  10.671   -13.173 1.00 188.82 ? 55  ASP C CG  1 
ATOM   3606  O OD1 . ASP C 3 55  ? -82.093  9.954    -12.151 1.00 195.34 ? 55  ASP C OD1 1 
ATOM   3607  O OD2 . ASP C 3 55  ? -80.894  10.958   -13.703 1.00 192.95 ? 55  ASP C OD2 1 
ATOM   3608  N N   . SER C 3 56  ? -85.643  11.414   -16.020 1.00 159.93 ? 56  SER C N   1 
ATOM   3609  C CA  . SER C 3 56  ? -86.681  12.243   -16.645 1.00 155.81 ? 56  SER C CA  1 
ATOM   3610  C C   . SER C 3 56  ? -86.584  13.700   -16.143 1.00 157.10 ? 56  SER C C   1 
ATOM   3611  O O   . SER C 3 56  ? -87.500  14.497   -16.367 1.00 155.52 ? 56  SER C O   1 
ATOM   3612  C CB  . SER C 3 56  ? -88.076  11.642   -16.466 1.00 160.97 ? 56  SER C CB  1 
ATOM   3613  O OG  . SER C 3 56  ? -88.137  10.335   -17.014 1.00 171.48 ? 56  SER C OG  1 
ATOM   3614  N N   . ASP C 3 57  ? -85.443  14.042   -15.486 1.00 153.09 ? 57  ASP C N   1 
ATOM   3615  C CA  . ASP C 3 57  ? -85.166  15.366   -14.934 1.00 151.12 ? 57  ASP C CA  1 
ATOM   3616  C C   . ASP C 3 57  ? -84.866  16.373   -16.039 1.00 149.65 ? 57  ASP C C   1 
ATOM   3617  O O   . ASP C 3 57  ? -84.098  16.084   -16.959 1.00 148.19 ? 57  ASP C O   1 
ATOM   3618  C CB  . ASP C 3 57  ? -84.060  15.321   -13.852 1.00 155.74 ? 57  ASP C CB  1 
ATOM   3619  C CG  . ASP C 3 57  ? -82.634  15.109   -14.341 1.00 162.17 ? 57  ASP C CG  1 
ATOM   3620  O OD1 . ASP C 3 57  ? -81.746  15.902   -13.946 1.00 161.15 ? 57  ASP C OD1 1 
ATOM   3621  O OD2 . ASP C 3 57  ? -82.401  14.140   -15.098 1.00 168.58 ? 57  ASP C OD2 1 
ATOM   3622  N N   . THR C 3 58  ? -85.518  17.536   -15.966 1.00 143.36 ? 58  THR C N   1 
ATOM   3623  C CA  . THR C 3 58  ? -85.379  18.609   -16.946 1.00 139.26 ? 58  THR C CA  1 
ATOM   3624  C C   . THR C 3 58  ? -84.461  19.722   -16.404 1.00 141.09 ? 58  THR C C   1 
ATOM   3625  O O   . THR C 3 58  ? -84.012  19.661   -15.256 1.00 142.39 ? 58  THR C O   1 
ATOM   3626  C CB  . THR C 3 58  ? -86.780  19.105   -17.400 1.00 147.16 ? 58  THR C CB  1 
ATOM   3627  O OG1 . THR C 3 58  ? -87.751  18.057   -17.279 1.00 147.81 ? 58  THR C OG1 1 
ATOM   3628  C CG2 . THR C 3 58  ? -86.783  19.649   -18.829 1.00 142.59 ? 58  THR C CG2 1 
ATOM   3629  N N   . ARG C 3 59  ? -84.162  20.711   -17.256 1.00 131.54 ? 59  ARG C N   1 
ATOM   3630  C CA  . ARG C 3 59  ? -83.329  21.875   -16.989 1.00 132.20 ? 59  ARG C CA  1 
ATOM   3631  C C   . ARG C 3 59  ? -83.680  22.878   -18.106 1.00 137.76 ? 59  ARG C C   1 
ATOM   3632  O O   . ARG C 3 59  ? -83.029  22.894   -19.152 1.00 135.81 ? 59  ARG C O   1 
ATOM   3633  C CB  . ARG C 3 59  ? -81.833  21.468   -17.006 1.00 130.74 ? 59  ARG C CB  1 
ATOM   3634  C CG  . ARG C 3 59  ? -80.852  22.472   -16.392 1.00 140.31 ? 59  ARG C CG  1 
ATOM   3635  C CD  . ARG C 3 59  ? -79.411  21.997   -16.578 1.00 142.90 ? 59  ARG C CD  1 
ATOM   3636  N NE  . ARG C 3 59  ? -78.417  23.056   -16.363 1.00 141.92 ? 59  ARG C NE  1 
ATOM   3637  C CZ  . ARG C 3 59  ? -77.201  23.081   -16.911 1.00 142.65 ? 59  ARG C CZ  1 
ATOM   3638  N NH1 . ARG C 3 59  ? -76.812  22.112   -17.732 1.00 120.61 ? 59  ARG C NH1 1 
ATOM   3639  N NH2 . ARG C 3 59  ? -76.372  24.080   -16.651 1.00 122.76 ? 59  ARG C NH2 1 
ATOM   3640  N N   . TYR C 3 60  ? -84.769  23.655   -17.911 1.00 137.70 ? 60  TYR C N   1 
ATOM   3641  C CA  . TYR C 3 60  ? -85.248  24.648   -18.885 1.00 138.39 ? 60  TYR C CA  1 
ATOM   3642  C C   . TYR C 3 60  ? -84.379  25.915   -18.920 1.00 143.68 ? 60  TYR C C   1 
ATOM   3643  O O   . TYR C 3 60  ? -83.765  26.285   -17.918 1.00 144.68 ? 60  TYR C O   1 
ATOM   3644  C CB  . TYR C 3 60  ? -86.695  25.084   -18.587 1.00 142.02 ? 60  TYR C CB  1 
ATOM   3645  C CG  . TYR C 3 60  ? -87.737  23.990   -18.563 1.00 146.07 ? 60  TYR C CG  1 
ATOM   3646  C CD1 . TYR C 3 60  ? -88.033  23.312   -17.385 1.00 150.56 ? 60  TYR C CD1 1 
ATOM   3647  C CD2 . TYR C 3 60  ? -88.527  23.728   -19.679 1.00 146.14 ? 60  TYR C CD2 1 
ATOM   3648  C CE1 . TYR C 3 60  ? -89.033  22.341   -17.338 1.00 153.18 ? 60  TYR C CE1 1 
ATOM   3649  C CE2 . TYR C 3 60  ? -89.530  22.756   -19.646 1.00 147.59 ? 60  TYR C CE2 1 
ATOM   3650  C CZ  . TYR C 3 60  ? -89.780  22.065   -18.470 1.00 158.94 ? 60  TYR C CZ  1 
ATOM   3651  O OH  . TYR C 3 60  ? -90.764  21.105   -18.411 1.00 161.21 ? 60  TYR C OH  1 
ATOM   3652  N N   . SER C 3 61  ? -84.387  26.606   -20.069 1.00 139.71 ? 61  SER C N   1 
ATOM   3653  C CA  . SER C 3 61  ? -83.703  27.879   -20.283 1.00 139.73 ? 61  SER C CA  1 
ATOM   3654  C C   . SER C 3 61  ? -84.612  28.976   -19.698 1.00 146.44 ? 61  SER C C   1 
ATOM   3655  O O   . SER C 3 61  ? -85.834  28.826   -19.779 1.00 146.29 ? 61  SER C O   1 
ATOM   3656  C CB  . SER C 3 61  ? -83.497  28.113   -21.780 1.00 141.06 ? 61  SER C CB  1 
ATOM   3657  O OG  . SER C 3 61  ? -83.021  29.409   -22.103 1.00 149.35 ? 61  SER C OG  1 
ATOM   3658  N N   . PRO C 3 62  ? -84.065  30.082   -19.129 1.00 145.21 ? 62  PRO C N   1 
ATOM   3659  C CA  . PRO C 3 62  ? -84.935  31.150   -18.591 1.00 147.47 ? 62  PRO C CA  1 
ATOM   3660  C C   . PRO C 3 62  ? -85.971  31.692   -19.583 1.00 150.89 ? 62  PRO C C   1 
ATOM   3661  O O   . PRO C 3 62  ? -87.101  31.982   -19.189 1.00 151.96 ? 62  PRO C O   1 
ATOM   3662  C CB  . PRO C 3 62  ? -83.938  32.241   -18.193 1.00 150.27 ? 62  PRO C CB  1 
ATOM   3663  C CG  . PRO C 3 62  ? -82.676  31.524   -17.939 1.00 153.70 ? 62  PRO C CG  1 
ATOM   3664  C CD  . PRO C 3 62  ? -82.639  30.420   -18.942 1.00 146.58 ? 62  PRO C CD  1 
ATOM   3665  N N   . SER C 3 63  ? -85.586  31.803   -20.870 1.00 145.48 ? 63  SER C N   1 
ATOM   3666  C CA  . SER C 3 63  ? -86.432  32.286   -21.965 1.00 144.64 ? 63  SER C CA  1 
ATOM   3667  C C   . SER C 3 63  ? -87.584  31.321   -22.326 1.00 149.01 ? 63  SER C C   1 
ATOM   3668  O O   . SER C 3 63  ? -88.542  31.752   -22.973 1.00 148.47 ? 63  SER C O   1 
ATOM   3669  C CB  . SER C 3 63  ? -85.582  32.559   -23.205 1.00 145.59 ? 63  SER C CB  1 
ATOM   3670  O OG  . SER C 3 63  ? -84.574  33.526   -22.960 1.00 152.43 ? 63  SER C OG  1 
ATOM   3671  N N   . PHE C 3 64  ? -87.490  30.029   -21.924 1.00 146.14 ? 64  PHE C N   1 
ATOM   3672  C CA  . PHE C 3 64  ? -88.484  28.993   -22.247 1.00 146.03 ? 64  PHE C CA  1 
ATOM   3673  C C   . PHE C 3 64  ? -89.122  28.299   -21.030 1.00 152.28 ? 64  PHE C C   1 
ATOM   3674  O O   . PHE C 3 64  ? -90.060  27.512   -21.205 1.00 151.44 ? 64  PHE C O   1 
ATOM   3675  C CB  . PHE C 3 64  ? -87.877  27.945   -23.199 1.00 146.04 ? 64  PHE C CB  1 
ATOM   3676  C CG  . PHE C 3 64  ? -87.459  28.475   -24.550 1.00 146.18 ? 64  PHE C CG  1 
ATOM   3677  C CD1 . PHE C 3 64  ? -86.159  28.917   -24.771 1.00 148.68 ? 64  PHE C CD1 1 
ATOM   3678  C CD2 . PHE C 3 64  ? -88.360  28.516   -25.608 1.00 147.63 ? 64  PHE C CD2 1 
ATOM   3679  C CE1 . PHE C 3 64  ? -85.773  29.409   -26.020 1.00 148.35 ? 64  PHE C CE1 1 
ATOM   3680  C CE2 . PHE C 3 64  ? -87.971  29.000   -26.859 1.00 149.42 ? 64  PHE C CE2 1 
ATOM   3681  C CZ  . PHE C 3 64  ? -86.681  29.443   -27.057 1.00 146.91 ? 64  PHE C CZ  1 
ATOM   3682  N N   . GLN C 3 65  ? -88.618  28.585   -19.811 1.00 151.42 ? 65  GLN C N   1 
ATOM   3683  C CA  . GLN C 3 65  ? -89.117  28.021   -18.554 1.00 153.50 ? 65  GLN C CA  1 
ATOM   3684  C C   . GLN C 3 65  ? -90.548  28.493   -18.291 1.00 159.32 ? 65  GLN C C   1 
ATOM   3685  O O   . GLN C 3 65  ? -90.825  29.693   -18.358 1.00 159.81 ? 65  GLN C O   1 
ATOM   3686  C CB  . GLN C 3 65  ? -88.174  28.389   -17.384 1.00 156.78 ? 65  GLN C CB  1 
ATOM   3687  C CG  . GLN C 3 65  ? -88.679  28.030   -15.979 1.00 181.14 ? 65  GLN C CG  1 
ATOM   3688  C CD  . GLN C 3 65  ? -88.523  26.569   -15.629 1.00 206.22 ? 65  GLN C CD  1 
ATOM   3689  O OE1 . GLN C 3 65  ? -87.413  26.074   -15.408 1.00 202.87 ? 65  GLN C OE1 1 
ATOM   3690  N NE2 . GLN C 3 65  ? -89.641  25.863   -15.506 1.00 199.48 ? 65  GLN C NE2 1 
ATOM   3691  N N   . GLY C 3 66  ? -91.435  27.534   -18.029 1.00 156.55 ? 66  GLY C N   1 
ATOM   3692  C CA  . GLY C 3 66  ? -92.845  27.785   -17.754 1.00 158.04 ? 66  GLY C CA  1 
ATOM   3693  C C   . GLY C 3 66  ? -93.717  27.792   -18.993 1.00 160.81 ? 66  GLY C C   1 
ATOM   3694  O O   . GLY C 3 66  ? -94.776  27.156   -19.006 1.00 160.79 ? 66  GLY C O   1 
ATOM   3695  N N   . GLN C 3 67  ? -93.267  28.511   -20.043 1.00 155.88 ? 67  GLN C N   1 
ATOM   3696  C CA  . GLN C 3 67  ? -93.946  28.661   -21.335 1.00 154.43 ? 67  GLN C CA  1 
ATOM   3697  C C   . GLN C 3 67  ? -94.157  27.297   -22.023 1.00 158.17 ? 67  GLN C C   1 
ATOM   3698  O O   . GLN C 3 67  ? -95.303  26.855   -22.179 1.00 158.48 ? 67  GLN C O   1 
ATOM   3699  C CB  . GLN C 3 67  ? -93.159  29.630   -22.250 1.00 154.43 ? 67  GLN C CB  1 
ATOM   3700  C CG  . GLN C 3 67  ? -92.740  30.950   -21.596 1.00 166.32 ? 67  GLN C CG  1 
ATOM   3701  C CD  . GLN C 3 67  ? -93.923  31.807   -21.239 1.00 186.99 ? 67  GLN C CD  1 
ATOM   3702  O OE1 . GLN C 3 67  ? -94.540  32.440   -22.099 1.00 184.41 ? 67  GLN C OE1 1 
ATOM   3703  N NE2 . GLN C 3 67  ? -94.277  31.826   -19.964 1.00 179.39 ? 67  GLN C NE2 1 
ATOM   3704  N N   . VAL C 3 68  ? -93.044  26.628   -22.394 1.00 153.29 ? 68  VAL C N   1 
ATOM   3705  C CA  . VAL C 3 68  ? -93.026  25.311   -23.032 1.00 151.76 ? 68  VAL C CA  1 
ATOM   3706  C C   . VAL C 3 68  ? -92.640  24.236   -21.997 1.00 156.53 ? 68  VAL C C   1 
ATOM   3707  O O   . VAL C 3 68  ? -91.922  24.533   -21.032 1.00 157.55 ? 68  VAL C O   1 
ATOM   3708  C CB  . VAL C 3 68  ? -92.124  25.303   -24.296 1.00 153.79 ? 68  VAL C CB  1 
ATOM   3709  C CG1 . VAL C 3 68  ? -90.640  25.360   -23.939 1.00 153.09 ? 68  VAL C CG1 1 
ATOM   3710  C CG2 . VAL C 3 68  ? -92.426  24.110   -25.194 1.00 152.86 ? 68  VAL C CG2 1 
ATOM   3711  N N   . THR C 3 69  ? -93.140  23.004   -22.190 1.00 151.85 ? 69  THR C N   1 
ATOM   3712  C CA  . THR C 3 69  ? -92.881  21.873   -21.302 1.00 151.48 ? 69  THR C CA  1 
ATOM   3713  C C   . THR C 3 69  ? -92.163  20.757   -22.079 1.00 152.82 ? 69  THR C C   1 
ATOM   3714  O O   . THR C 3 69  ? -92.654  20.326   -23.122 1.00 151.80 ? 69  THR C O   1 
ATOM   3715  C CB  . THR C 3 69  ? -94.189  21.436   -20.600 1.00 161.12 ? 69  THR C CB  1 
ATOM   3716  O OG1 . THR C 3 69  ? -94.905  22.593   -20.148 1.00 161.85 ? 69  THR C OG1 1 
ATOM   3717  C CG2 . THR C 3 69  ? -93.944  20.498   -19.423 1.00 160.57 ? 69  THR C CG2 1 
ATOM   3718  N N   . ILE C 3 70  ? -90.982  20.328   -21.587 1.00 148.18 ? 70  ILE C N   1 
ATOM   3719  C CA  . ILE C 3 70  ? -90.187  19.269   -22.215 1.00 146.67 ? 70  ILE C CA  1 
ATOM   3720  C C   . ILE C 3 70  ? -90.508  17.951   -21.527 1.00 151.68 ? 70  ILE C C   1 
ATOM   3721  O O   . ILE C 3 70  ? -90.244  17.792   -20.334 1.00 151.90 ? 70  ILE C O   1 
ATOM   3722  C CB  . ILE C 3 70  ? -88.657  19.556   -22.244 1.00 148.73 ? 70  ILE C CB  1 
ATOM   3723  C CG1 . ILE C 3 70  ? -88.343  21.005   -22.678 1.00 148.81 ? 70  ILE C CG1 1 
ATOM   3724  C CG2 . ILE C 3 70  ? -87.940  18.545   -23.148 1.00 148.15 ? 70  ILE C CG2 1 
ATOM   3725  C CD1 . ILE C 3 70  ? -86.980  21.534   -22.249 1.00 155.21 ? 70  ILE C CD1 1 
ATOM   3726  N N   . SER C 3 71  ? -91.096  17.021   -22.284 1.00 148.80 ? 71  SER C N   1 
ATOM   3727  C CA  . SER C 3 71  ? -91.494  15.694   -21.810 1.00 149.30 ? 71  SER C CA  1 
ATOM   3728  C C   . SER C 3 71  ? -90.536  14.628   -22.366 1.00 152.78 ? 71  SER C C   1 
ATOM   3729  O O   . SER C 3 71  ? -89.884  14.863   -23.385 1.00 152.17 ? 71  SER C O   1 
ATOM   3730  C CB  . SER C 3 71  ? -92.927  15.385   -22.247 1.00 153.32 ? 71  SER C CB  1 
ATOM   3731  O OG  . SER C 3 71  ? -93.796  16.505   -22.158 1.00 162.03 ? 71  SER C OG  1 
ATOM   3732  N N   . ALA C 3 72  ? -90.441  13.466   -21.696 1.00 148.93 ? 72  ALA C N   1 
ATOM   3733  C CA  . ALA C 3 72  ? -89.589  12.366   -22.151 1.00 147.99 ? 72  ALA C CA  1 
ATOM   3734  C C   . ALA C 3 72  ? -90.164  11.000   -21.794 1.00 151.07 ? 72  ALA C C   1 
ATOM   3735  O O   . ALA C 3 72  ? -90.600  10.782   -20.660 1.00 150.42 ? 72  ALA C O   1 
ATOM   3736  C CB  . ALA C 3 72  ? -88.181  12.509   -21.595 1.00 148.27 ? 72  ALA C CB  1 
ATOM   3737  N N   . ASP C 3 73  ? -90.171  10.086   -22.776 1.00 147.43 ? 73  ASP C N   1 
ATOM   3738  C CA  . ASP C 3 73  ? -90.646  8.718    -22.603 1.00 147.74 ? 73  ASP C CA  1 
ATOM   3739  C C   . ASP C 3 73  ? -89.570  7.730    -23.041 1.00 151.05 ? 73  ASP C C   1 
ATOM   3740  O O   . ASP C 3 73  ? -89.476  7.382    -24.223 1.00 150.83 ? 73  ASP C O   1 
ATOM   3741  C CB  . ASP C 3 73  ? -91.972  8.477    -23.340 1.00 150.30 ? 73  ASP C CB  1 
ATOM   3742  C CG  . ASP C 3 73  ? -92.785  7.345    -22.745 1.00 162.39 ? 73  ASP C CG  1 
ATOM   3743  O OD1 . ASP C 3 73  ? -92.233  6.233    -22.585 1.00 163.09 ? 73  ASP C OD1 1 
ATOM   3744  O OD2 . ASP C 3 73  ? -93.989  7.553    -22.486 1.00 170.10 ? 73  ASP C OD2 1 
ATOM   3745  N N   . LYS C 3 74  ? -88.748  7.297    -22.065 1.00 146.86 ? 74  LYS C N   1 
ATOM   3746  C CA  . LYS C 3 74  ? -87.639  6.348    -22.221 1.00 146.27 ? 74  LYS C CA  1 
ATOM   3747  C C   . LYS C 3 74  ? -88.084  4.983    -22.755 1.00 151.28 ? 74  LYS C C   1 
ATOM   3748  O O   . LYS C 3 74  ? -87.308  4.333    -23.455 1.00 151.35 ? 74  LYS C O   1 
ATOM   3749  C CB  . LYS C 3 74  ? -86.847  6.189    -20.904 1.00 147.69 ? 74  LYS C CB  1 
ATOM   3750  C CG  . LYS C 3 74  ? -87.712  6.028    -19.652 1.00 158.05 ? 74  LYS C CG  1 
ATOM   3751  C CD  . LYS C 3 74  ? -86.902  5.627    -18.431 1.00 166.75 ? 74  LYS C CD  1 
ATOM   3752  C CE  . LYS C 3 74  ? -87.622  5.984    -17.150 1.00 176.95 ? 74  LYS C CE  1 
ATOM   3753  N NZ  . LYS C 3 74  ? -86.838  5.612    -15.944 1.00 183.15 ? 74  LYS C NZ  1 
ATOM   3754  N N   . SER C 3 75  ? -89.332  4.563    -22.433 1.00 148.40 ? 75  SER C N   1 
ATOM   3755  C CA  . SER C 3 75  ? -89.935  3.289    -22.849 1.00 149.37 ? 75  SER C CA  1 
ATOM   3756  C C   . SER C 3 75  ? -90.139  3.219    -24.367 1.00 154.02 ? 75  SER C C   1 
ATOM   3757  O O   . SER C 3 75  ? -89.803  2.203    -24.979 1.00 154.28 ? 75  SER C O   1 
ATOM   3758  C CB  . SER C 3 75  ? -91.259  3.055    -22.122 1.00 153.24 ? 75  SER C CB  1 
ATOM   3759  O OG  . SER C 3 75  ? -91.130  3.181    -20.715 1.00 161.29 ? 75  SER C OG  1 
ATOM   3760  N N   . ILE C 3 76  ? -90.681  4.305    -24.964 1.00 150.66 ? 76  ILE C N   1 
ATOM   3761  C CA  . ILE C 3 76  ? -90.921  4.441    -26.408 1.00 151.34 ? 76  ILE C CA  1 
ATOM   3762  C C   . ILE C 3 76  ? -89.658  5.018    -27.085 1.00 154.41 ? 76  ILE C C   1 
ATOM   3763  O O   . ILE C 3 76  ? -89.584  5.052    -28.320 1.00 155.63 ? 76  ILE C O   1 
ATOM   3764  C CB  . ILE C 3 76  ? -92.178  5.319    -26.731 1.00 154.44 ? 76  ILE C CB  1 
ATOM   3765  C CG1 . ILE C 3 76  ? -93.275  5.239    -25.641 1.00 154.96 ? 76  ILE C CG1 1 
ATOM   3766  C CG2 . ILE C 3 76  ? -92.743  4.982    -28.123 1.00 156.45 ? 76  ILE C CG2 1 
ATOM   3767  C CD1 . ILE C 3 76  ? -94.327  6.383    -25.683 1.00 164.72 ? 76  ILE C CD1 1 
ATOM   3768  N N   . SER C 3 77  ? -88.662  5.454    -26.266 1.00 148.03 ? 77  SER C N   1 
ATOM   3769  C CA  . SER C 3 77  ? -87.406  6.101    -26.674 1.00 145.91 ? 77  SER C CA  1 
ATOM   3770  C C   . SER C 3 77  ? -87.711  7.377    -27.481 1.00 146.82 ? 77  SER C C   1 
ATOM   3771  O O   . SER C 3 77  ? -87.178  7.580    -28.574 1.00 146.60 ? 77  SER C O   1 
ATOM   3772  C CB  . SER C 3 77  ? -86.463  5.132    -27.393 1.00 149.58 ? 77  SER C CB  1 
ATOM   3773  O OG  . SER C 3 77  ? -86.887  4.818    -28.709 1.00 157.51 ? 77  SER C OG  1 
ATOM   3774  N N   . THR C 3 78  ? -88.617  8.217    -26.928 1.00 141.04 ? 78  THR C N   1 
ATOM   3775  C CA  . THR C 3 78  ? -89.092  9.450    -27.553 1.00 139.62 ? 78  THR C CA  1 
ATOM   3776  C C   . THR C 3 78  ? -89.112  10.624   -26.597 1.00 140.25 ? 78  THR C C   1 
ATOM   3777  O O   . THR C 3 78  ? -89.584  10.497   -25.468 1.00 139.68 ? 78  THR C O   1 
ATOM   3778  C CB  . THR C 3 78  ? -90.514  9.277    -28.104 1.00 149.34 ? 78  THR C CB  1 
ATOM   3779  O OG1 . THR C 3 78  ? -90.813  7.897    -28.313 1.00 150.99 ? 78  THR C OG1 1 
ATOM   3780  C CG2 . THR C 3 78  ? -90.744  10.076   -29.373 1.00 148.34 ? 78  THR C CG2 1 
ATOM   3781  N N   . ALA C 3 79  ? -88.653  11.781   -27.078 1.00 134.70 ? 79  ALA C N   1 
ATOM   3782  C CA  . ALA C 3 79  ? -88.651  13.043   -26.342 1.00 133.13 ? 79  ALA C CA  1 
ATOM   3783  C C   . ALA C 3 79  ? -89.764  13.906   -26.909 1.00 136.62 ? 79  ALA C C   1 
ATOM   3784  O O   . ALA C 3 79  ? -90.114  13.748   -28.077 1.00 136.72 ? 79  ALA C O   1 
ATOM   3785  C CB  . ALA C 3 79  ? -87.317  13.744   -26.519 1.00 132.99 ? 79  ALA C CB  1 
ATOM   3786  N N   . TYR C 3 80  ? -90.324  14.810   -26.097 1.00 133.14 ? 80  TYR C N   1 
ATOM   3787  C CA  . TYR C 3 80  ? -91.407  15.697   -26.526 1.00 133.52 ? 80  TYR C CA  1 
ATOM   3788  C C   . TYR C 3 80  ? -91.157  17.152   -26.150 1.00 138.08 ? 80  TYR C C   1 
ATOM   3789  O O   . TYR C 3 80  ? -90.381  17.432   -25.237 1.00 137.78 ? 80  TYR C O   1 
ATOM   3790  C CB  . TYR C 3 80  ? -92.772  15.229   -25.970 1.00 135.33 ? 80  TYR C CB  1 
ATOM   3791  C CG  . TYR C 3 80  ? -93.067  13.765   -26.208 1.00 137.74 ? 80  TYR C CG  1 
ATOM   3792  C CD1 . TYR C 3 80  ? -93.301  13.280   -27.491 1.00 140.65 ? 80  TYR C CD1 1 
ATOM   3793  C CD2 . TYR C 3 80  ? -93.105  12.860   -25.152 1.00 138.49 ? 80  TYR C CD2 1 
ATOM   3794  C CE1 . TYR C 3 80  ? -93.542  11.927   -27.723 1.00 142.68 ? 80  TYR C CE1 1 
ATOM   3795  C CE2 . TYR C 3 80  ? -93.353  11.503   -25.370 1.00 140.02 ? 80  TYR C CE2 1 
ATOM   3796  C CZ  . TYR C 3 80  ? -93.569  11.040   -26.660 1.00 147.95 ? 80  TYR C CZ  1 
ATOM   3797  O OH  . TYR C 3 80  ? -93.814  9.708    -26.906 1.00 149.11 ? 80  TYR C OH  1 
ATOM   3798  N N   . LEU C 3 81  ? -91.827  18.076   -26.851 1.00 134.99 ? 81  LEU C N   1 
ATOM   3799  C CA  . LEU C 3 81  ? -91.769  19.508   -26.580 1.00 134.70 ? 81  LEU C CA  1 
ATOM   3800  C C   . LEU C 3 81  ? -93.218  20.013   -26.571 1.00 140.77 ? 81  LEU C C   1 
ATOM   3801  O O   . LEU C 3 81  ? -93.692  20.625   -27.532 1.00 140.65 ? 81  LEU C O   1 
ATOM   3802  C CB  . LEU C 3 81  ? -90.894  20.231   -27.619 1.00 133.96 ? 81  LEU C CB  1 
ATOM   3803  C CG  . LEU C 3 81  ? -90.461  21.658   -27.276 1.00 138.15 ? 81  LEU C CG  1 
ATOM   3804  C CD1 . LEU C 3 81  ? -89.292  21.670   -26.311 1.00 137.88 ? 81  LEU C CD1 1 
ATOM   3805  C CD2 . LEU C 3 81  ? -90.073  22.404   -28.517 1.00 140.35 ? 81  LEU C CD2 1 
ATOM   3806  N N   . GLN C 3 82  ? -93.935  19.676   -25.487 1.00 138.93 ? 82  GLN C N   1 
ATOM   3807  C CA  . GLN C 3 82  ? -95.342  19.995   -25.250 1.00 139.81 ? 82  GLN C CA  1 
ATOM   3808  C C   . GLN C 3 82  ? -95.564  21.492   -24.984 1.00 143.33 ? 82  GLN C C   1 
ATOM   3809  O O   . GLN C 3 82  ? -94.849  22.086   -24.174 1.00 142.99 ? 82  GLN C O   1 
ATOM   3810  C CB  . GLN C 3 82  ? -95.873  19.133   -24.083 1.00 142.29 ? 82  GLN C CB  1 
ATOM   3811  C CG  . GLN C 3 82  ? -97.401  19.013   -24.015 1.00 163.66 ? 82  GLN C CG  1 
ATOM   3812  C CD  . GLN C 3 82  ? -97.891  17.646   -23.576 1.00 178.43 ? 82  GLN C CD  1 
ATOM   3813  O OE1 . GLN C 3 82  ? -97.273  16.949   -22.758 1.00 170.20 ? 82  GLN C OE1 1 
ATOM   3814  N NE2 . GLN C 3 82  ? -99.045  17.246   -24.090 1.00 170.95 ? 82  GLN C NE2 1 
ATOM   3815  N N   . TRP C 3 83  ? -96.568  22.088   -25.664 1.00 147.85 ? 83  TRP C N   1 
ATOM   3816  C CA  . TRP C 3 83  ? -96.954  23.496   -25.522 1.00 148.58 ? 83  TRP C CA  1 
ATOM   3817  C C   . TRP C 3 83  ? -98.267  23.648   -24.778 1.00 156.59 ? 83  TRP C C   1 
ATOM   3818  O O   . TRP C 3 83  ? -99.284  23.071   -25.181 1.00 157.62 ? 83  TRP C O   1 
ATOM   3819  C CB  . TRP C 3 83  ? -97.041  24.211   -26.875 1.00 145.74 ? 83  TRP C CB  1 
ATOM   3820  C CG  . TRP C 3 83  ? -95.736  24.770   -27.339 1.00 143.87 ? 83  TRP C CG  1 
ATOM   3821  C CD1 . TRP C 3 83  ? -95.104  25.885   -26.870 1.00 146.60 ? 83  TRP C CD1 1 
ATOM   3822  C CD2 . TRP C 3 83  ? -94.912  24.250   -28.385 1.00 141.30 ? 83  TRP C CD2 1 
ATOM   3823  N NE1 . TRP C 3 83  ? -93.929  26.085   -27.553 1.00 143.59 ? 83  TRP C NE1 1 
ATOM   3824  C CE2 . TRP C 3 83  ? -93.782  25.090   -28.485 1.00 143.74 ? 83  TRP C CE2 1 
ATOM   3825  C CE3 . TRP C 3 83  ? -95.016  23.146   -29.252 1.00 141.70 ? 83  TRP C CE3 1 
ATOM   3826  C CZ2 . TRP C 3 83  ? -92.762  24.861   -29.413 1.00 141.28 ? 83  TRP C CZ2 1 
ATOM   3827  C CZ3 . TRP C 3 83  ? -94.004  22.920   -30.171 1.00 141.15 ? 83  TRP C CZ3 1 
ATOM   3828  C CH2 . TRP C 3 83  ? -92.900  23.778   -30.256 1.00 140.75 ? 83  TRP C CH2 1 
ATOM   3829  N N   . SER C 3 84  ? -98.234  24.442   -23.692 1.00 154.94 ? 84  SER C N   1 
ATOM   3830  C CA  . SER C 3 84  ? -99.376  24.747   -22.832 1.00 158.63 ? 84  SER C CA  1 
ATOM   3831  C C   . SER C 3 84  ? -100.413 25.535   -23.662 1.00 163.38 ? 84  SER C C   1 
ATOM   3832  O O   . SER C 3 84  ? -101.535 25.063   -23.864 1.00 165.73 ? 84  SER C O   1 
ATOM   3833  C CB  . SER C 3 84  ? -98.917  25.543   -21.609 1.00 162.93 ? 84  SER C CB  1 
ATOM   3834  O OG  . SER C 3 84  ? -97.677  25.080   -21.092 1.00 166.97 ? 84  SER C OG  1 
ATOM   3835  N N   . SER C 3 85  ? -99.995  26.698   -24.193 1.00 157.20 ? 85  SER C N   1 
ATOM   3836  C CA  . SER C 3 85  ? -100.776 27.574   -25.065 1.00 157.19 ? 85  SER C CA  1 
ATOM   3837  C C   . SER C 3 85  ? -99.791  28.228   -26.024 1.00 156.56 ? 85  SER C C   1 
ATOM   3838  O O   . SER C 3 85  ? -98.742  28.722   -25.590 1.00 155.06 ? 85  SER C O   1 
ATOM   3839  C CB  . SER C 3 85  ? -101.529 28.630   -24.260 1.00 164.01 ? 85  SER C CB  1 
ATOM   3840  O OG  . SER C 3 85  ? -102.387 29.395   -25.090 1.00 172.30 ? 85  SER C OG  1 
ATOM   3841  N N   . LEU C 3 86  ? -100.102 28.181   -27.328 1.00 150.50 ? 86  LEU C N   1 
ATOM   3842  C CA  . LEU C 3 86  ? -99.235  28.719   -28.370 1.00 146.91 ? 86  LEU C CA  1 
ATOM   3843  C C   . LEU C 3 86  ? -99.305  30.230   -28.522 1.00 149.94 ? 86  LEU C C   1 
ATOM   3844  O O   . LEU C 3 86  ? -100.375 30.826   -28.401 1.00 151.82 ? 86  LEU C O   1 
ATOM   3845  C CB  . LEU C 3 86  ? -99.495  28.030   -29.715 1.00 145.61 ? 86  LEU C CB  1 
ATOM   3846  C CG  . LEU C 3 86  ? -98.876  26.645   -29.904 1.00 148.50 ? 86  LEU C CG  1 
ATOM   3847  C CD1 . LEU C 3 86  ? -99.554  25.909   -31.029 1.00 148.74 ? 86  LEU C CD1 1 
ATOM   3848  C CD2 . LEU C 3 86  ? -97.386  26.730   -30.175 1.00 148.29 ? 86  LEU C CD2 1 
ATOM   3849  N N   . LYS C 3 87  ? -98.143  30.843   -28.778 1.00 143.72 ? 87  LYS C N   1 
ATOM   3850  C CA  . LYS C 3 87  ? -97.984  32.280   -29.004 1.00 143.74 ? 87  LYS C CA  1 
ATOM   3851  C C   . LYS C 3 87  ? -97.575  32.458   -30.460 1.00 145.10 ? 87  LYS C C   1 
ATOM   3852  O O   . LYS C 3 87  ? -97.011  31.531   -31.045 1.00 142.79 ? 87  LYS C O   1 
ATOM   3853  C CB  . LYS C 3 87  ? -96.876  32.870   -28.104 1.00 145.70 ? 87  LYS C CB  1 
ATOM   3854  C CG  . LYS C 3 87  ? -97.093  32.736   -26.594 1.00 160.71 ? 87  LYS C CG  1 
ATOM   3855  C CD  . LYS C 3 87  ? -96.236  31.625   -25.964 1.00 166.36 ? 87  LYS C CD  1 
ATOM   3856  C CE  . LYS C 3 87  ? -94.869  32.085   -25.502 1.00 171.36 ? 87  LYS C CE  1 
ATOM   3857  N NZ  . LYS C 3 87  ? -93.868  32.075   -26.602 1.00 173.82 ? 87  LYS C NZ  1 
ATOM   3858  N N   . ALA C 3 88  ? -97.806  33.653   -31.034 1.00 141.92 ? 88  ALA C N   1 
ATOM   3859  C CA  . ALA C 3 88  ? -97.400  33.959   -32.409 1.00 140.31 ? 88  ALA C CA  1 
ATOM   3860  C C   . ALA C 3 88  ? -95.865  33.957   -32.515 1.00 141.83 ? 88  ALA C C   1 
ATOM   3861  O O   . ALA C 3 88  ? -95.322  33.764   -33.604 1.00 139.93 ? 88  ALA C O   1 
ATOM   3862  C CB  . ALA C 3 88  ? -97.956  35.307   -32.831 1.00 142.93 ? 88  ALA C CB  1 
ATOM   3863  N N   . SER C 3 89  ? -95.179  34.132   -31.363 1.00 138.57 ? 89  SER C N   1 
ATOM   3864  C CA  . SER C 3 89  ? -93.724  34.111   -31.224 1.00 137.01 ? 89  SER C CA  1 
ATOM   3865  C C   . SER C 3 89  ? -93.167  32.682   -31.330 1.00 139.11 ? 89  SER C C   1 
ATOM   3866  O O   . SER C 3 89  ? -91.981  32.519   -31.619 1.00 138.18 ? 89  SER C O   1 
ATOM   3867  C CB  . SER C 3 89  ? -93.308  34.736   -29.894 1.00 141.38 ? 89  SER C CB  1 
ATOM   3868  O OG  . SER C 3 89  ? -93.763  33.965   -28.793 1.00 150.79 ? 89  SER C OG  1 
ATOM   3869  N N   . ASP C 3 90  ? -94.020  31.654   -31.103 1.00 134.63 ? 90  ASP C N   1 
ATOM   3870  C CA  . ASP C 3 90  ? -93.642  30.239   -31.179 1.00 132.34 ? 90  ASP C CA  1 
ATOM   3871  C C   . ASP C 3 90  ? -93.458  29.734   -32.628 1.00 134.19 ? 90  ASP C C   1 
ATOM   3872  O O   . ASP C 3 90  ? -93.048  28.587   -32.827 1.00 131.78 ? 90  ASP C O   1 
ATOM   3873  C CB  . ASP C 3 90  ? -94.622  29.354   -30.378 1.00 135.03 ? 90  ASP C CB  1 
ATOM   3874  C CG  . ASP C 3 90  ? -94.472  29.413   -28.859 1.00 146.77 ? 90  ASP C CG  1 
ATOM   3875  O OD1 . ASP C 3 90  ? -93.435  29.929   -28.378 1.00 146.42 ? 90  ASP C OD1 1 
ATOM   3876  O OD2 . ASP C 3 90  ? -95.374  28.913   -28.154 1.00 154.90 ? 90  ASP C OD2 1 
ATOM   3877  N N   . THR C 3 91  ? -93.729  30.599   -33.633 1.00 132.01 ? 91  THR C N   1 
ATOM   3878  C CA  . THR C 3 91  ? -93.556  30.298   -35.059 1.00 131.51 ? 91  THR C CA  1 
ATOM   3879  C C   . THR C 3 91  ? -92.052  30.164   -35.287 1.00 133.88 ? 91  THR C C   1 
ATOM   3880  O O   . THR C 3 91  ? -91.355  31.174   -35.401 1.00 133.61 ? 91  THR C O   1 
ATOM   3881  C CB  . THR C 3 91  ? -94.175  31.413   -35.935 1.00 142.99 ? 91  THR C CB  1 
ATOM   3882  O OG1 . THR C 3 91  ? -95.473  31.755   -35.446 1.00 145.15 ? 91  THR C OG1 1 
ATOM   3883  C CG2 . THR C 3 91  ? -94.249  31.030   -37.412 1.00 141.26 ? 91  THR C CG2 1 
ATOM   3884  N N   . ALA C 3 92  ? -91.547  28.918   -35.263 1.00 129.27 ? 92  ALA C N   1 
ATOM   3885  C CA  . ALA C 3 92  ? -90.116  28.642   -35.401 1.00 128.33 ? 92  ALA C CA  1 
ATOM   3886  C C   . ALA C 3 92  ? -89.809  27.211   -35.855 1.00 130.96 ? 92  ALA C C   1 
ATOM   3887  O O   . ALA C 3 92  ? -90.711  26.376   -35.963 1.00 130.05 ? 92  ALA C O   1 
ATOM   3888  C CB  . ALA C 3 92  ? -89.416  28.915   -34.072 1.00 128.76 ? 92  ALA C CB  1 
ATOM   3889  N N   . MET C 3 93  ? -88.514  26.944   -36.105 1.00 127.53 ? 93  MET C N   1 
ATOM   3890  C CA  . MET C 3 93  ? -87.942  25.649   -36.475 1.00 127.11 ? 93  MET C CA  1 
ATOM   3891  C C   . MET C 3 93  ? -87.384  25.021   -35.183 1.00 129.76 ? 93  MET C C   1 
ATOM   3892  O O   . MET C 3 93  ? -86.578  25.644   -34.490 1.00 130.05 ? 93  MET C O   1 
ATOM   3893  C CB  . MET C 3 93  ? -86.845  25.848   -37.546 1.00 130.68 ? 93  MET C CB  1 
ATOM   3894  C CG  . MET C 3 93  ? -86.032  24.604   -37.870 1.00 134.52 ? 93  MET C CG  1 
ATOM   3895  S SD  . MET C 3 93  ? -86.963  23.288   -38.679 1.00 138.91 ? 93  MET C SD  1 
ATOM   3896  C CE  . MET C 3 93  ? -85.814  22.831   -39.945 1.00 137.15 ? 93  MET C CE  1 
ATOM   3897  N N   . TYR C 3 94  ? -87.843  23.812   -34.841 1.00 124.28 ? 94  TYR C N   1 
ATOM   3898  C CA  . TYR C 3 94  ? -87.432  23.161   -33.599 1.00 122.45 ? 94  TYR C CA  1 
ATOM   3899  C C   . TYR C 3 94  ? -86.629  21.894   -33.836 1.00 126.32 ? 94  TYR C C   1 
ATOM   3900  O O   . TYR C 3 94  ? -87.076  21.001   -34.558 1.00 126.25 ? 94  TYR C O   1 
ATOM   3901  C CB  . TYR C 3 94  ? -88.657  22.902   -32.700 1.00 122.53 ? 94  TYR C CB  1 
ATOM   3902  C CG  . TYR C 3 94  ? -89.357  24.169   -32.252 1.00 123.32 ? 94  TYR C CG  1 
ATOM   3903  C CD1 . TYR C 3 94  ? -90.419  24.699   -32.979 1.00 125.93 ? 94  TYR C CD1 1 
ATOM   3904  C CD2 . TYR C 3 94  ? -88.947  24.847   -31.112 1.00 123.32 ? 94  TYR C CD2 1 
ATOM   3905  C CE1 . TYR C 3 94  ? -91.049  25.879   -32.583 1.00 126.68 ? 94  TYR C CE1 1 
ATOM   3906  C CE2 . TYR C 3 94  ? -89.586  26.010   -30.693 1.00 124.54 ? 94  TYR C CE2 1 
ATOM   3907  C CZ  . TYR C 3 94  ? -90.616  26.540   -31.447 1.00 130.04 ? 94  TYR C CZ  1 
ATOM   3908  O OH  . TYR C 3 94  ? -91.224  27.697   -31.032 1.00 129.44 ? 94  TYR C OH  1 
ATOM   3909  N N   . TYR C 3 95  ? -85.430  21.835   -33.246 1.00 122.53 ? 95  TYR C N   1 
ATOM   3910  C CA  . TYR C 3 95  ? -84.518  20.694   -33.327 1.00 122.13 ? 95  TYR C CA  1 
ATOM   3911  C C   . TYR C 3 95  ? -84.368  20.055   -31.950 1.00 125.95 ? 95  TYR C C   1 
ATOM   3912  O O   . TYR C 3 95  ? -84.500  20.744   -30.944 1.00 125.36 ? 95  TYR C O   1 
ATOM   3913  C CB  . TYR C 3 95  ? -83.121  21.143   -33.786 1.00 123.62 ? 95  TYR C CB  1 
ATOM   3914  C CG  . TYR C 3 95  ? -83.033  21.689   -35.193 1.00 126.97 ? 95  TYR C CG  1 
ATOM   3915  C CD1 . TYR C 3 95  ? -82.909  20.836   -36.287 1.00 129.84 ? 95  TYR C CD1 1 
ATOM   3916  C CD2 . TYR C 3 95  ? -82.956  23.058   -35.425 1.00 128.82 ? 95  TYR C CD2 1 
ATOM   3917  C CE1 . TYR C 3 95  ? -82.788  21.333   -37.587 1.00 132.19 ? 95  TYR C CE1 1 
ATOM   3918  C CE2 . TYR C 3 95  ? -82.812  23.568   -36.719 1.00 131.33 ? 95  TYR C CE2 1 
ATOM   3919  C CZ  . TYR C 3 95  ? -82.740  22.701   -37.799 1.00 137.98 ? 95  TYR C CZ  1 
ATOM   3920  O OH  . TYR C 3 95  ? -82.605  23.191   -39.077 1.00 138.34 ? 95  TYR C OH  1 
ATOM   3921  N N   . CYS C 3 96  ? -84.073  18.750   -31.907 1.00 122.67 ? 96  CYS C N   1 
ATOM   3922  C CA  . CYS C 3 96  ? -83.770  18.019   -30.675 1.00 122.13 ? 96  CYS C CA  1 
ATOM   3923  C C   . CYS C 3 96  ? -82.387  17.436   -30.905 1.00 122.75 ? 96  CYS C C   1 
ATOM   3924  O O   . CYS C 3 96  ? -82.022  17.216   -32.065 1.00 122.80 ? 96  CYS C O   1 
ATOM   3925  C CB  . CYS C 3 96  ? -84.806  16.935   -30.370 1.00 123.64 ? 96  CYS C CB  1 
ATOM   3926  S SG  . CYS C 3 96  ? -84.634  15.427   -31.366 1.00 127.74 ? 96  CYS C SG  1 
ATOM   3927  N N   . ALA C 3 97  ? -81.595  17.232   -29.847 1.00 116.57 ? 97  ALA C N   1 
ATOM   3928  C CA  . ALA C 3 97  ? -80.253  16.703   -30.061 1.00 116.18 ? 97  ALA C CA  1 
ATOM   3929  C C   . ALA C 3 97  ? -79.698  15.881   -28.921 1.00 119.77 ? 97  ALA C C   1 
ATOM   3930  O O   . ALA C 3 97  ? -79.927  16.199   -27.757 1.00 120.04 ? 97  ALA C O   1 
ATOM   3931  C CB  . ALA C 3 97  ? -79.295  17.823   -30.412 1.00 117.51 ? 97  ALA C CB  1 
ATOM   3932  N N   . ARG C 3 98  ? -78.954  14.822   -29.265 1.00 115.79 ? 98  ARG C N   1 
ATOM   3933  C CA  . ARG C 3 98  ? -78.308  13.918   -28.318 1.00 114.93 ? 98  ARG C CA  1 
ATOM   3934  C C   . ARG C 3 98  ? -77.091  14.630   -27.752 1.00 117.68 ? 98  ARG C C   1 
ATOM   3935  O O   . ARG C 3 98  ? -76.192  14.975   -28.515 1.00 119.19 ? 98  ARG C O   1 
ATOM   3936  C CB  . ARG C 3 98  ? -77.903  12.626   -29.035 1.00 116.22 ? 98  ARG C CB  1 
ATOM   3937  C CG  . ARG C 3 98  ? -77.652  11.467   -28.101 1.00 121.81 ? 98  ARG C CG  1 
ATOM   3938  C CD  . ARG C 3 98  ? -77.077  10.291   -28.845 1.00 122.19 ? 98  ARG C CD  1 
ATOM   3939  N NE  . ARG C 3 98  ? -75.647  10.445   -29.096 1.00 124.12 ? 98  ARG C NE  1 
ATOM   3940  C CZ  . ARG C 3 98  ? -74.864  9.475    -29.554 1.00 141.40 ? 98  ARG C CZ  1 
ATOM   3941  N NH1 . ARG C 3 98  ? -75.365  8.272    -29.810 1.00 128.00 ? 98  ARG C NH1 1 
ATOM   3942  N NH2 . ARG C 3 98  ? -73.573  9.696    -29.754 1.00 133.75 ? 98  ARG C NH2 1 
ATOM   3943  N N   . VAL C 3 99  ? -77.084  14.885   -26.430 1.00 111.40 ? 99  VAL C N   1 
ATOM   3944  C CA  . VAL C 3 99  ? -76.020  15.625   -25.740 1.00 110.37 ? 99  VAL C CA  1 
ATOM   3945  C C   . VAL C 3 99  ? -74.813  14.732   -25.407 1.00 113.61 ? 99  VAL C C   1 
ATOM   3946  O O   . VAL C 3 99  ? -74.976  13.595   -24.962 1.00 112.60 ? 99  VAL C O   1 
ATOM   3947  C CB  . VAL C 3 99  ? -76.549  16.408   -24.500 1.00 113.16 ? 99  VAL C CB  1 
ATOM   3948  C CG1 . VAL C 3 99  ? -75.446  17.236   -23.839 1.00 112.65 ? 99  VAL C CG1 1 
ATOM   3949  C CG2 . VAL C 3 99  ? -77.718  17.314   -24.880 1.00 113.18 ? 99  VAL C CG2 1 
ATOM   3950  N N   . VAL C 3 100 ? -73.608  15.279   -25.653 1.00 111.40 ? 100 VAL C N   1 
ATOM   3951  C CA  . VAL C 3 100 ? -72.302  14.672   -25.405 1.00 112.52 ? 100 VAL C CA  1 
ATOM   3952  C C   . VAL C 3 100 ? -71.833  15.114   -24.018 1.00 115.55 ? 100 VAL C C   1 
ATOM   3953  O O   . VAL C 3 100 ? -71.798  16.316   -23.740 1.00 114.44 ? 100 VAL C O   1 
ATOM   3954  C CB  . VAL C 3 100 ? -71.253  15.078   -26.470 1.00 119.06 ? 100 VAL C CB  1 
ATOM   3955  C CG1 . VAL C 3 100 ? -70.062  14.125   -26.452 1.00 120.28 ? 100 VAL C CG1 1 
ATOM   3956  C CG2 . VAL C 3 100 ? -71.860  15.161   -27.863 1.00 120.06 ? 100 VAL C CG2 1 
ATOM   3957  N N   . ALA C 3 101 ? -71.457  14.147   -23.160 1.00 111.86 ? 101 ALA C N   1 
ATOM   3958  C CA  . ALA C 3 101 ? -70.986  14.416   -21.799 1.00 110.79 ? 101 ALA C CA  1 
ATOM   3959  C C   . ALA C 3 101 ? -69.863  13.479   -21.359 1.00 116.26 ? 101 ALA C C   1 
ATOM   3960  O O   . ALA C 3 101 ? -69.574  12.500   -22.050 1.00 117.11 ? 101 ALA C O   1 
ATOM   3961  C CB  . ALA C 3 101 ? -72.148  14.346   -20.825 1.00 110.21 ? 101 ALA C CB  1 
ATOM   3962  N N   . ASP C 3 102 ? -69.222  13.796   -20.218 1.00 113.25 ? 102 ASP C N   1 
ATOM   3963  C CA  . ASP C 3 102 ? -68.114  13.032   -19.648 1.00 114.20 ? 102 ASP C CA  1 
ATOM   3964  C C   . ASP C 3 102 ? -68.516  11.628   -19.175 1.00 117.40 ? 102 ASP C C   1 
ATOM   3965  O O   . ASP C 3 102 ? -69.585  11.451   -18.586 1.00 116.18 ? 102 ASP C O   1 
ATOM   3966  C CB  . ASP C 3 102 ? -67.414  13.828   -18.528 1.00 116.15 ? 102 ASP C CB  1 
ATOM   3967  C CG  . ASP C 3 102 ? -68.249  14.025   -17.288 1.00 127.10 ? 102 ASP C CG  1 
ATOM   3968  O OD1 . ASP C 3 102 ? -69.077  14.963   -17.274 1.00 128.55 ? 102 ASP C OD1 1 
ATOM   3969  O OD2 . ASP C 3 102 ? -68.093  13.227   -16.343 1.00 130.81 ? 102 ASP C OD2 1 
ATOM   3970  N N   . ARG C 3 103 ? -67.630  10.642   -19.434 1.00 122.48 ? 103 ARG C N   1 
ATOM   3971  C CA  . ARG C 3 103 ? -67.788  9.230    -19.085 1.00 121.92 ? 103 ARG C CA  1 
ATOM   3972  C C   . ARG C 3 103 ? -67.398  8.900    -17.628 1.00 125.36 ? 103 ARG C C   1 
ATOM   3973  O O   . ARG C 3 103 ? -67.337  7.719    -17.263 1.00 125.40 ? 103 ARG C O   1 
ATOM   3974  C CB  . ARG C 3 103 ? -67.009  8.347    -20.082 1.00 122.15 ? 103 ARG C CB  1 
ATOM   3975  C CG  . ARG C 3 103 ? -67.810  7.927    -21.320 1.00 131.59 ? 103 ARG C CG  1 
ATOM   3976  C CD  . ARG C 3 103 ? -67.713  8.915    -22.463 1.00 141.32 ? 103 ARG C CD  1 
ATOM   3977  N NE  . ARG C 3 103 ? -68.470  8.487    -23.641 1.00 150.64 ? 103 ARG C NE  1 
ATOM   3978  C CZ  . ARG C 3 103 ? -68.829  9.300    -24.630 1.00 169.97 ? 103 ARG C CZ  1 
ATOM   3979  N NH1 . ARG C 3 103 ? -68.519  10.591   -24.585 1.00 158.13 ? 103 ARG C NH1 1 
ATOM   3980  N NH2 . ARG C 3 103 ? -69.502  8.831    -25.670 1.00 162.96 ? 103 ARG C NH2 1 
ATOM   3981  N N   . GLU C 3 104 ? -67.162  9.939    -16.797 1.00 120.87 ? 104 GLU C N   1 
ATOM   3982  C CA  . GLU C 3 104 ? -66.775  9.799    -15.387 1.00 120.33 ? 104 GLU C CA  1 
ATOM   3983  C C   . GLU C 3 104 ? -67.859  10.267   -14.412 1.00 123.99 ? 104 GLU C C   1 
ATOM   3984  O O   . GLU C 3 104 ? -67.696  10.122   -13.197 1.00 123.39 ? 104 GLU C O   1 
ATOM   3985  C CB  . GLU C 3 104 ? -65.430  10.506   -15.108 1.00 121.75 ? 104 GLU C CB  1 
ATOM   3986  C CG  . GLU C 3 104 ? -64.261  10.018   -15.954 1.00 130.10 ? 104 GLU C CG  1 
ATOM   3987  C CD  . GLU C 3 104 ? -63.961  8.537    -15.875 1.00 146.48 ? 104 GLU C CD  1 
ATOM   3988  O OE1 . GLU C 3 104 ? -64.089  7.960    -14.771 1.00 125.56 ? 104 GLU C OE1 1 
ATOM   3989  O OE2 . GLU C 3 104 ? -63.598  7.953    -16.922 1.00 145.21 ? 104 GLU C OE2 1 
ATOM   3990  N N   . GLY C 3 105 ? -68.954  10.792   -14.964 1.00 121.05 ? 105 GLY C N   1 
ATOM   3991  C CA  . GLY C 3 105 ? -70.103  11.295   -14.219 1.00 121.15 ? 105 GLY C CA  1 
ATOM   3992  C C   . GLY C 3 105 ? -69.736  12.475   -13.351 1.00 125.72 ? 105 GLY C C   1 
ATOM   3993  O O   . GLY C 3 105 ? -69.647  12.332   -12.131 1.00 125.81 ? 105 GLY C O   1 
ATOM   3994  N N   . PHE C 3 106 ? -69.475  13.632   -13.983 1.00 122.42 ? 106 PHE C N   1 
ATOM   3995  C CA  . PHE C 3 106 ? -69.053  14.864   -13.315 1.00 122.70 ? 106 PHE C CA  1 
ATOM   3996  C C   . PHE C 3 106 ? -69.954  16.061   -13.633 1.00 128.38 ? 106 PHE C C   1 
ATOM   3997  O O   . PHE C 3 106 ? -69.976  17.024   -12.863 1.00 129.20 ? 106 PHE C O   1 
ATOM   3998  C CB  . PHE C 3 106 ? -67.598  15.193   -13.683 1.00 124.06 ? 106 PHE C CB  1 
ATOM   3999  C CG  . PHE C 3 106 ? -66.487  14.545   -12.885 1.00 125.24 ? 106 PHE C CG  1 
ATOM   4000  C CD1 . PHE C 3 106 ? -65.476  15.313   -12.322 1.00 127.88 ? 106 PHE C CD1 1 
ATOM   4001  C CD2 . PHE C 3 106 ? -66.407  13.160   -12.763 1.00 127.15 ? 106 PHE C CD2 1 
ATOM   4002  C CE1 . PHE C 3 106 ? -64.430  14.714   -11.617 1.00 128.61 ? 106 PHE C CE1 1 
ATOM   4003  C CE2 . PHE C 3 106 ? -65.365  12.562   -12.048 1.00 129.77 ? 106 PHE C CE2 1 
ATOM   4004  C CZ  . PHE C 3 106 ? -64.383  13.343   -11.483 1.00 127.72 ? 106 PHE C CZ  1 
ATOM   4005  N N   . GLY C 3 107 ? -70.661  16.001   -14.762 1.00 124.97 ? 107 GLY C N   1 
ATOM   4006  C CA  . GLY C 3 107 ? -71.575  17.056   -15.186 1.00 125.64 ? 107 GLY C CA  1 
ATOM   4007  C C   . GLY C 3 107 ? -71.056  18.003   -16.250 1.00 130.19 ? 107 GLY C C   1 
ATOM   4008  O O   . GLY C 3 107 ? -71.652  19.065   -16.461 1.00 130.31 ? 107 GLY C O   1 
ATOM   4009  N N   . TYR C 3 108 ? -69.950  17.631   -16.930 1.00 126.91 ? 108 TYR C N   1 
ATOM   4010  C CA  . TYR C 3 108 ? -69.352  18.409   -18.019 1.00 127.11 ? 108 TYR C CA  1 
ATOM   4011  C C   . TYR C 3 108 ? -70.114  18.078   -19.304 1.00 130.41 ? 108 TYR C C   1 
ATOM   4012  O O   . TYR C 3 108 ? -70.215  16.899   -19.663 1.00 130.15 ? 108 TYR C O   1 
ATOM   4013  C CB  . TYR C 3 108 ? -67.871  18.028   -18.244 1.00 128.17 ? 108 TYR C CB  1 
ATOM   4014  C CG  . TYR C 3 108 ? -66.904  18.343   -17.129 1.00 130.05 ? 108 TYR C CG  1 
ATOM   4015  C CD1 . TYR C 3 108 ? -66.340  19.609   -17.008 1.00 132.48 ? 108 TYR C CD1 1 
ATOM   4016  C CD2 . TYR C 3 108 ? -66.423  17.338   -16.301 1.00 130.48 ? 108 TYR C CD2 1 
ATOM   4017  C CE1 . TYR C 3 108 ? -65.392  19.889   -16.027 1.00 133.98 ? 108 TYR C CE1 1 
ATOM   4018  C CE2 . TYR C 3 108 ? -65.479  17.603   -15.312 1.00 131.28 ? 108 TYR C CE2 1 
ATOM   4019  C CZ  . TYR C 3 108 ? -64.965  18.882   -15.177 1.00 139.82 ? 108 TYR C CZ  1 
ATOM   4020  O OH  . TYR C 3 108 ? -64.018  19.147   -14.216 1.00 140.28 ? 108 TYR C OH  1 
ATOM   4021  N N   . TYR C 3 109 ? -70.634  19.100   -20.005 1.00 126.24 ? 109 TYR C N   1 
ATOM   4022  C CA  . TYR C 3 109 ? -71.334  18.879   -21.269 1.00 125.90 ? 109 TYR C CA  1 
ATOM   4023  C C   . TYR C 3 109 ? -70.511  19.442   -22.422 1.00 130.55 ? 109 TYR C C   1 
ATOM   4024  O O   . TYR C 3 109 ? -70.154  20.622   -22.396 1.00 131.05 ? 109 TYR C O   1 
ATOM   4025  C CB  . TYR C 3 109 ? -72.761  19.434   -21.227 1.00 127.40 ? 109 TYR C CB  1 
ATOM   4026  C CG  . TYR C 3 109 ? -73.593  18.835   -20.117 1.00 128.45 ? 109 TYR C CG  1 
ATOM   4027  C CD1 . TYR C 3 109 ? -74.062  17.527   -20.198 1.00 129.63 ? 109 TYR C CD1 1 
ATOM   4028  C CD2 . TYR C 3 109 ? -73.901  19.570   -18.977 1.00 129.72 ? 109 TYR C CD2 1 
ATOM   4029  C CE1 . TYR C 3 109 ? -74.815  16.964   -19.169 1.00 129.90 ? 109 TYR C CE1 1 
ATOM   4030  C CE2 . TYR C 3 109 ? -74.657  19.020   -17.944 1.00 130.53 ? 109 TYR C CE2 1 
ATOM   4031  C CZ  . TYR C 3 109 ? -75.113  17.716   -18.044 1.00 136.52 ? 109 TYR C CZ  1 
ATOM   4032  O OH  . TYR C 3 109 ? -75.865  17.177   -17.027 1.00 136.55 ? 109 TYR C OH  1 
ATOM   4033  N N   . TYR C 3 110 ? -70.171  18.581   -23.408 1.00 104.24 ? 110 TYR C N   1 
ATOM   4034  C CA  . TYR C 3 110 ? -69.302  18.918   -24.546 1.00 104.00 ? 110 TYR C CA  1 
ATOM   4035  C C   . TYR C 3 110 ? -70.008  19.449   -25.812 1.00 106.46 ? 110 TYR C C   1 
ATOM   4036  O O   . TYR C 3 110 ? -69.331  19.838   -26.764 1.00 106.96 ? 110 TYR C O   1 
ATOM   4037  C CB  . TYR C 3 110 ? -68.422  17.709   -24.921 1.00 108.58 ? 110 TYR C CB  1 
ATOM   4038  C CG  . TYR C 3 110 ? -67.719  17.008   -23.781 1.00 111.88 ? 110 TYR C CG  1 
ATOM   4039  C CD1 . TYR C 3 110 ? -66.995  17.727   -22.835 1.00 111.59 ? 110 TYR C CD1 1 
ATOM   4040  C CD2 . TYR C 3 110 ? -67.690  15.620   -23.706 1.00 116.65 ? 110 TYR C CD2 1 
ATOM   4041  C CE1 . TYR C 3 110 ? -66.305  17.087   -21.816 1.00 113.56 ? 110 TYR C CE1 1 
ATOM   4042  C CE2 . TYR C 3 110 ? -67.003  14.966   -22.689 1.00 119.51 ? 110 TYR C CE2 1 
ATOM   4043  C CZ  . TYR C 3 110 ? -66.316  15.705   -21.744 1.00 125.02 ? 110 TYR C CZ  1 
ATOM   4044  O OH  . TYR C 3 110 ? -65.632  15.059   -20.753 1.00 128.83 ? 110 TYR C OH  1 
ATOM   4045  N N   . GLY C 3 111 ? -71.334  19.477   -25.804 1.00 100.81 ? 111 GLY C N   1 
ATOM   4046  C CA  . GLY C 3 111 ? -72.143  19.910   -26.935 1.00 99.55  ? 111 GLY C CA  1 
ATOM   4047  C C   . GLY C 3 111 ? -73.118  18.812   -27.293 1.00 105.43 ? 111 GLY C C   1 
ATOM   4048  O O   . GLY C 3 111 ? -73.329  17.902   -26.486 1.00 107.25 ? 111 GLY C O   1 
ATOM   4049  N N   . MET C 3 112 ? -73.709  18.864   -28.494 1.00 101.79 ? 112 MET C N   1 
ATOM   4050  C CA  . MET C 3 112 ? -74.667  17.838   -28.906 1.00 103.97 ? 112 MET C CA  1 
ATOM   4051  C C   . MET C 3 112 ? -74.351  17.280   -30.305 1.00 110.54 ? 112 MET C C   1 
ATOM   4052  O O   . MET C 3 112 ? -74.239  18.050   -31.256 1.00 109.64 ? 112 MET C O   1 
ATOM   4053  C CB  . MET C 3 112 ? -76.134  18.306   -28.750 1.00 105.44 ? 112 MET C CB  1 
ATOM   4054  C CG  . MET C 3 112 ? -76.427  19.747   -29.196 1.00 107.50 ? 112 MET C CG  1 
ATOM   4055  S SD  . MET C 3 112 ? -77.131  20.882   -27.947 1.00 109.61 ? 112 MET C SD  1 
ATOM   4056  C CE  . MET C 3 112 ? -78.667  20.069   -27.530 1.00 107.22 ? 112 MET C CE  1 
ATOM   4057  N N   . ASP C 3 113 ? -74.177  15.934   -30.412 1.00 111.13 ? 113 ASP C N   1 
ATOM   4058  C CA  . ASP C 3 113 ? -73.778  15.218   -31.639 1.00 114.27 ? 113 ASP C CA  1 
ATOM   4059  C C   . ASP C 3 113 ? -74.912  14.861   -32.615 1.00 119.24 ? 113 ASP C C   1 
ATOM   4060  O O   . ASP C 3 113 ? -74.919  15.383   -33.732 1.00 117.87 ? 113 ASP C O   1 
ATOM   4061  C CB  . ASP C 3 113 ? -72.933  13.952   -31.335 1.00 119.78 ? 113 ASP C CB  1 
ATOM   4062  C CG  . ASP C 3 113 ? -73.405  12.999   -30.237 1.00 136.69 ? 113 ASP C CG  1 
ATOM   4063  O OD1 . ASP C 3 113 ? -74.632  12.906   -30.007 1.00 137.85 ? 113 ASP C OD1 1 
ATOM   4064  O OD2 . ASP C 3 113 ? -72.549  12.305   -29.647 1.00 145.94 ? 113 ASP C OD2 1 
ATOM   4065  N N   . VAL C 3 114 ? -75.807  13.930   -32.238 1.00 118.47 ? 114 VAL C N   1 
ATOM   4066  C CA  . VAL C 3 114 ? -76.905  13.472   -33.092 1.00 119.85 ? 114 VAL C CA  1 
ATOM   4067  C C   . VAL C 3 114 ? -77.999  14.510   -33.071 1.00 121.70 ? 114 VAL C C   1 
ATOM   4068  O O   . VAL C 3 114 ? -78.456  14.890   -31.999 1.00 119.27 ? 114 VAL C O   1 
ATOM   4069  C CB  . VAL C 3 114 ? -77.434  12.063   -32.712 1.00 126.63 ? 114 VAL C CB  1 
ATOM   4070  C CG1 . VAL C 3 114 ? -78.410  11.542   -33.765 1.00 127.66 ? 114 VAL C CG1 1 
ATOM   4071  C CG2 . VAL C 3 114 ? -76.290  11.073   -32.509 1.00 129.57 ? 114 VAL C CG2 1 
ATOM   4072  N N   . TRP C 3 115 ? -78.398  14.984   -34.251 1.00 119.03 ? 115 TRP C N   1 
ATOM   4073  C CA  . TRP C 3 115 ? -79.435  15.998   -34.382 1.00 117.14 ? 115 TRP C CA  1 
ATOM   4074  C C   . TRP C 3 115 ? -80.626  15.478   -35.177 1.00 125.22 ? 115 TRP C C   1 
ATOM   4075  O O   . TRP C 3 115 ? -80.466  14.632   -36.064 1.00 126.59 ? 115 TRP C O   1 
ATOM   4076  C CB  . TRP C 3 115 ? -78.863  17.261   -35.044 1.00 113.83 ? 115 TRP C CB  1 
ATOM   4077  C CG  . TRP C 3 115 ? -78.035  18.133   -34.141 1.00 112.38 ? 115 TRP C CG  1 
ATOM   4078  C CD1 . TRP C 3 115 ? -76.771  17.887   -33.691 1.00 115.62 ? 115 TRP C CD1 1 
ATOM   4079  C CD2 . TRP C 3 115 ? -78.367  19.451   -33.696 1.00 109.48 ? 115 TRP C CD2 1 
ATOM   4080  N NE1 . TRP C 3 115 ? -76.319  18.949   -32.945 1.00 112.42 ? 115 TRP C NE1 1 
ATOM   4081  C CE2 . TRP C 3 115 ? -77.275  19.926   -32.936 1.00 111.81 ? 115 TRP C CE2 1 
ATOM   4082  C CE3 . TRP C 3 115 ? -79.496  20.268   -33.841 1.00 109.46 ? 115 TRP C CE3 1 
ATOM   4083  C CZ2 . TRP C 3 115 ? -77.275  21.182   -32.333 1.00 108.74 ? 115 TRP C CZ2 1 
ATOM   4084  C CZ3 . TRP C 3 115 ? -79.496  21.511   -33.237 1.00 108.90 ? 115 TRP C CZ3 1 
ATOM   4085  C CH2 . TRP C 3 115 ? -78.401  21.950   -32.481 1.00 108.40 ? 115 TRP C CH2 1 
ATOM   4086  N N   . GLY C 3 116 ? -81.806  15.999   -34.841 1.00 123.21 ? 116 GLY C N   1 
ATOM   4087  C CA  . GLY C 3 116 ? -83.059  15.671   -35.505 1.00 124.81 ? 116 GLY C CA  1 
ATOM   4088  C C   . GLY C 3 116 ? -83.185  16.372   -36.840 1.00 130.53 ? 116 GLY C C   1 
ATOM   4089  O O   . GLY C 3 116 ? -82.399  17.274   -37.157 1.00 129.46 ? 116 GLY C O   1 
ATOM   4090  N N   . GLN C 3 117 ? -84.192  15.952   -37.615 1.00 128.90 ? 117 GLN C N   1 
ATOM   4091  C CA  . GLN C 3 117 ? -84.532  16.465   -38.938 1.00 129.43 ? 117 GLN C CA  1 
ATOM   4092  C C   . GLN C 3 117 ? -84.885  17.968   -38.933 1.00 133.51 ? 117 GLN C C   1 
ATOM   4093  O O   . GLN C 3 117 ? -84.500  18.704   -39.849 1.00 132.91 ? 117 GLN C O   1 
ATOM   4094  C CB  . GLN C 3 117 ? -85.691  15.630   -39.530 1.00 131.80 ? 117 GLN C CB  1 
ATOM   4095  C CG  . GLN C 3 117 ? -87.024  15.758   -38.779 1.00 146.23 ? 117 GLN C CG  1 
ATOM   4096  C CD  . GLN C 3 117 ? -87.925  14.566   -38.924 1.00 172.67 ? 117 GLN C CD  1 
ATOM   4097  O OE1 . GLN C 3 117 ? -87.582  13.447   -38.532 1.00 172.80 ? 117 GLN C OE1 1 
ATOM   4098  N NE2 . GLN C 3 117 ? -89.134  14.798   -39.419 1.00 164.06 ? 117 GLN C NE2 1 
ATOM   4099  N N   . GLY C 3 118 ? -85.603  18.383   -37.892 1.00 130.57 ? 118 GLY C N   1 
ATOM   4100  C CA  . GLY C 3 118 ? -86.128  19.728   -37.704 1.00 129.72 ? 118 GLY C CA  1 
ATOM   4101  C C   . GLY C 3 118 ? -87.627  19.767   -37.922 1.00 134.66 ? 118 GLY C C   1 
ATOM   4102  O O   . GLY C 3 118 ? -88.114  19.449   -39.014 1.00 136.13 ? 118 GLY C O   1 
ATOM   4103  N N   . THR C 3 119 ? -88.369  20.139   -36.876 1.00 129.63 ? 119 THR C N   1 
ATOM   4104  C CA  . THR C 3 119 ? -89.819  20.236   -36.946 1.00 129.58 ? 119 THR C CA  1 
ATOM   4105  C C   . THR C 3 119 ? -90.193  21.676   -37.263 1.00 131.17 ? 119 THR C C   1 
ATOM   4106  O O   . THR C 3 119 ? -89.767  22.599   -36.564 1.00 129.46 ? 119 THR C O   1 
ATOM   4107  C CB  . THR C 3 119 ? -90.452  19.683   -35.671 1.00 142.09 ? 119 THR C CB  1 
ATOM   4108  O OG1 . THR C 3 119 ? -89.934  18.372   -35.434 1.00 144.05 ? 119 THR C OG1 1 
ATOM   4109  C CG2 . THR C 3 119 ? -91.969  19.633   -35.748 1.00 142.38 ? 119 THR C CG2 1 
ATOM   4110  N N   . THR C 3 120 ? -90.966  21.863   -38.334 1.00 127.71 ? 120 THR C N   1 
ATOM   4111  C CA  . THR C 3 120 ? -91.385  23.184   -38.791 1.00 127.39 ? 120 THR C CA  1 
ATOM   4112  C C   . THR C 3 120 ? -92.737  23.567   -38.164 1.00 130.73 ? 120 THR C C   1 
ATOM   4113  O O   . THR C 3 120 ? -93.788  23.060   -38.574 1.00 131.72 ? 120 THR C O   1 
ATOM   4114  C CB  . THR C 3 120 ? -91.334  23.251   -40.327 1.00 135.18 ? 120 THR C CB  1 
ATOM   4115  O OG1 . THR C 3 120 ? -90.129  22.626   -40.780 1.00 132.66 ? 120 THR C OG1 1 
ATOM   4116  C CG2 . THR C 3 120 ? -91.403  24.677   -40.854 1.00 134.33 ? 120 THR C CG2 1 
ATOM   4117  N N   . VAL C 3 121 ? -92.694  24.464   -37.162 1.00 124.93 ? 121 VAL C N   1 
ATOM   4118  C CA  . VAL C 3 121 ? -93.877  24.924   -36.438 1.00 124.78 ? 121 VAL C CA  1 
ATOM   4119  C C   . VAL C 3 121 ? -94.289  26.342   -36.852 1.00 129.42 ? 121 VAL C C   1 
ATOM   4120  O O   . VAL C 3 121 ? -93.536  27.297   -36.646 1.00 128.51 ? 121 VAL C O   1 
ATOM   4121  C CB  . VAL C 3 121 ? -93.709  24.770   -34.908 1.00 127.74 ? 121 VAL C CB  1 
ATOM   4122  C CG1 . VAL C 3 121 ? -94.898  25.355   -34.151 1.00 128.54 ? 121 VAL C CG1 1 
ATOM   4123  C CG2 . VAL C 3 121 ? -93.500  23.307   -34.530 1.00 127.38 ? 121 VAL C CG2 1 
ATOM   4124  N N   . THR C 3 122 ? -95.502  26.463   -37.428 1.00 127.29 ? 122 THR C N   1 
ATOM   4125  C CA  . THR C 3 122 ? -96.095  27.730   -37.866 1.00 128.28 ? 122 THR C CA  1 
ATOM   4126  C C   . THR C 3 122 ? -97.241  28.077   -36.914 1.00 133.25 ? 122 THR C C   1 
ATOM   4127  O O   . THR C 3 122 ? -98.146  27.260   -36.724 1.00 133.07 ? 122 THR C O   1 
ATOM   4128  C CB  . THR C 3 122 ? -96.574  27.644   -39.329 1.00 135.67 ? 122 THR C CB  1 
ATOM   4129  O OG1 . THR C 3 122 ? -95.665  26.854   -40.098 1.00 133.23 ? 122 THR C OG1 1 
ATOM   4130  C CG2 . THR C 3 122 ? -96.749  29.014   -39.973 1.00 135.81 ? 122 THR C CG2 1 
ATOM   4131  N N   . VAL C 3 123 ? -97.183  29.269   -36.286 1.00 130.95 ? 123 VAL C N   1 
ATOM   4132  C CA  . VAL C 3 123 ? -98.211  29.722   -35.341 1.00 132.96 ? 123 VAL C CA  1 
ATOM   4133  C C   . VAL C 3 123 ? -98.820  31.064   -35.790 1.00 140.29 ? 123 VAL C C   1 
ATOM   4134  O O   . VAL C 3 123 ? -98.444  32.125   -35.277 1.00 140.56 ? 123 VAL C O   1 
ATOM   4135  C CB  . VAL C 3 123 ? -97.760  29.740   -33.849 1.00 136.38 ? 123 VAL C CB  1 
ATOM   4136  C CG1 . VAL C 3 123 ? -98.970  29.723   -32.926 1.00 138.30 ? 123 VAL C CG1 1 
ATOM   4137  C CG2 . VAL C 3 123 ? -96.830  28.575   -33.513 1.00 134.00 ? 123 VAL C CG2 1 
ATOM   4138  N N   . SER C 3 124 ? -99.767  31.000   -36.755 1.00 139.14 ? 124 SER C N   1 
ATOM   4139  C CA  . SER C 3 124 ? -100.457 32.161   -37.332 1.00 141.72 ? 124 SER C CA  1 
ATOM   4140  C C   . SER C 3 124 ? -101.971 31.963   -37.415 1.00 147.30 ? 124 SER C C   1 
ATOM   4141  O O   . SER C 3 124 ? -102.449 30.852   -37.665 1.00 145.58 ? 124 SER C O   1 
ATOM   4142  C CB  . SER C 3 124 ? -99.887  32.499   -38.709 1.00 145.28 ? 124 SER C CB  1 
ATOM   4143  O OG  . SER C 3 124 ? -100.538 33.607   -39.310 1.00 157.05 ? 124 SER C OG  1 
ATOM   4144  N N   . SER C 3 125 ? -102.713 33.067   -37.224 1.00 147.26 ? 125 SER C N   1 
ATOM   4145  C CA  . SER C 3 125 ? -104.173 33.116   -37.252 1.00 150.45 ? 125 SER C CA  1 
ATOM   4146  C C   . SER C 3 125 ? -104.752 32.992   -38.665 1.00 157.07 ? 125 SER C C   1 
ATOM   4147  O O   . SER C 3 125 ? -105.937 32.673   -38.808 1.00 158.57 ? 125 SER C O   1 
ATOM   4148  C CB  . SER C 3 125 ? -104.669 34.392   -36.583 1.00 157.02 ? 125 SER C CB  1 
ATOM   4149  O OG  . SER C 3 125 ? -104.220 34.469   -35.241 1.00 165.88 ? 125 SER C OG  1 
ATOM   4150  N N   . ALA C 3 126 ? -103.921 33.218   -39.702 1.00 153.90 ? 126 ALA C N   1 
ATOM   4151  C CA  . ALA C 3 126 ? -104.330 33.098   -41.103 1.00 155.32 ? 126 ALA C CA  1 
ATOM   4152  C C   . ALA C 3 126 ? -104.651 31.637   -41.443 1.00 159.33 ? 126 ALA C C   1 
ATOM   4153  O O   . ALA C 3 126 ? -103.915 30.737   -41.030 1.00 156.44 ? 126 ALA C O   1 
ATOM   4154  C CB  . ALA C 3 126 ? -103.234 33.624   -42.016 1.00 155.40 ? 126 ALA C CB  1 
ATOM   4155  N N   . SER C 3 127 ? -105.776 31.408   -42.153 1.00 158.94 ? 127 SER C N   1 
ATOM   4156  C CA  . SER C 3 127 ? -106.247 30.074   -42.556 1.00 158.07 ? 127 SER C CA  1 
ATOM   4157  C C   . SER C 3 127 ? -105.590 29.570   -43.860 1.00 160.96 ? 127 SER C C   1 
ATOM   4158  O O   . SER C 3 127 ? -104.903 30.341   -44.540 1.00 160.70 ? 127 SER C O   1 
ATOM   4159  C CB  . SER C 3 127 ? -107.772 30.045   -42.657 1.00 164.49 ? 127 SER C CB  1 
ATOM   4160  O OG  . SER C 3 127 ? -108.389 30.013   -41.380 1.00 173.94 ? 127 SER C OG  1 
ATOM   4161  N N   . THR C 3 128 ? -105.792 28.268   -44.188 1.00 156.50 ? 128 THR C N   1 
ATOM   4162  C CA  . THR C 3 128 ? -105.240 27.596   -45.370 1.00 155.20 ? 128 THR C CA  1 
ATOM   4163  C C   . THR C 3 128 ? -105.782 28.222   -46.662 1.00 161.37 ? 128 THR C C   1 
ATOM   4164  O O   . THR C 3 128 ? -106.997 28.236   -46.873 1.00 162.91 ? 128 THR C O   1 
ATOM   4165  C CB  . THR C 3 128 ? -105.461 26.068   -45.292 1.00 163.57 ? 128 THR C CB  1 
ATOM   4166  O OG1 . THR C 3 128 ? -105.177 25.597   -43.972 1.00 164.07 ? 128 THR C OG1 1 
ATOM   4167  C CG2 . THR C 3 128 ? -104.618 25.299   -46.301 1.00 160.53 ? 128 THR C CG2 1 
ATOM   4168  N N   . LYS C 3 129 ? -104.872 28.758   -47.505 1.00 158.05 ? 129 LYS C N   1 
ATOM   4169  C CA  . LYS C 3 129 ? -105.198 29.410   -48.775 1.00 160.21 ? 129 LYS C CA  1 
ATOM   4170  C C   . LYS C 3 129 ? -104.180 29.074   -49.859 1.00 165.17 ? 129 LYS C C   1 
ATOM   4171  O O   . LYS C 3 129 ? -102.973 29.114   -49.618 1.00 162.87 ? 129 LYS C O   1 
ATOM   4172  C CB  . LYS C 3 129 ? -105.308 30.941   -48.604 1.00 164.52 ? 129 LYS C CB  1 
ATOM   4173  C CG  . LYS C 3 129 ? -106.028 31.640   -49.764 1.00 172.71 ? 129 LYS C CG  1 
ATOM   4174  C CD  . LYS C 3 129 ? -105.759 33.138   -49.818 1.00 178.61 ? 129 LYS C CD  1 
ATOM   4175  C CE  . LYS C 3 129 ? -106.302 33.774   -51.079 1.00 185.21 ? 129 LYS C CE  1 
ATOM   4176  N NZ  . LYS C 3 129 ? -105.399 33.580   -52.249 1.00 187.94 ? 129 LYS C NZ  1 
ATOM   4177  N N   . GLY C 3 130 ? -104.692 28.774   -51.047 1.00 172.76 ? 130 GLY C N   1 
ATOM   4178  C CA  . GLY C 3 130 ? -103.891 28.479   -52.228 1.00 172.94 ? 130 GLY C CA  1 
ATOM   4179  C C   . GLY C 3 130 ? -103.233 29.720   -52.815 1.00 176.25 ? 130 GLY C C   1 
ATOM   4180  O O   . GLY C 3 130 ? -103.636 30.845   -52.492 1.00 174.48 ? 130 GLY C O   1 
ATOM   4181  N N   . PRO C 3 131 ? -102.218 29.567   -53.699 1.00 173.48 ? 131 PRO C N   1 
ATOM   4182  C CA  . PRO C 3 131 ? -101.542 30.753   -54.244 1.00 170.69 ? 131 PRO C CA  1 
ATOM   4183  C C   . PRO C 3 131 ? -102.143 31.336   -55.515 1.00 173.35 ? 131 PRO C C   1 
ATOM   4184  O O   . PRO C 3 131 ? -102.487 30.604   -56.448 1.00 174.48 ? 131 PRO C O   1 
ATOM   4185  C CB  . PRO C 3 131 ? -100.109 30.269   -54.475 1.00 172.51 ? 131 PRO C CB  1 
ATOM   4186  C CG  . PRO C 3 131 ? -100.221 28.780   -54.644 1.00 179.81 ? 131 PRO C CG  1 
ATOM   4187  C CD  . PRO C 3 131 ? -101.588 28.324   -54.189 1.00 177.34 ? 131 PRO C CD  1 
ATOM   4188  N N   . SER C 3 132 ? -102.235 32.672   -55.552 1.00 167.03 ? 132 SER C N   1 
ATOM   4189  C CA  . SER C 3 132 ? -102.717 33.425   -56.703 1.00 165.23 ? 132 SER C CA  1 
ATOM   4190  C C   . SER C 3 132 ? -101.485 33.663   -57.603 1.00 169.57 ? 132 SER C C   1 
ATOM   4191  O O   . SER C 3 132 ? -100.804 34.683   -57.477 1.00 168.38 ? 132 SER C O   1 
ATOM   4192  C CB  . SER C 3 132 ? -103.372 34.733   -56.256 1.00 165.42 ? 132 SER C CB  1 
ATOM   4193  O OG  . SER C 3 132 ? -104.334 34.530   -55.232 1.00 170.12 ? 132 SER C OG  1 
ATOM   4194  N N   . VAL C 3 133 ? -101.141 32.651   -58.426 1.00 167.49 ? 133 VAL C N   1 
ATOM   4195  C CA  . VAL C 3 133 ? -99.982  32.645   -59.334 1.00 167.24 ? 133 VAL C CA  1 
ATOM   4196  C C   . VAL C 3 133 ? -100.186 33.634   -60.497 1.00 171.63 ? 133 VAL C C   1 
ATOM   4197  O O   . VAL C 3 133 ? -101.210 33.558   -61.186 1.00 171.99 ? 133 VAL C O   1 
ATOM   4198  C CB  . VAL C 3 133 ? -99.653  31.207   -59.850 1.00 172.17 ? 133 VAL C CB  1 
ATOM   4199  C CG1 . VAL C 3 133 ? -98.326  31.169   -60.609 1.00 171.71 ? 133 VAL C CG1 1 
ATOM   4200  C CG2 . VAL C 3 133 ? -99.644  30.189   -58.711 1.00 173.22 ? 133 VAL C CG2 1 
ATOM   4201  N N   . PHE C 3 134 ? -99.216  34.552   -60.716 1.00 167.77 ? 134 PHE C N   1 
ATOM   4202  C CA  . PHE C 3 134 ? -99.235  35.522   -61.820 1.00 167.63 ? 134 PHE C CA  1 
ATOM   4203  C C   . PHE C 3 134 ? -97.896  35.525   -62.587 1.00 173.61 ? 134 PHE C C   1 
ATOM   4204  O O   . PHE C 3 134 ? -96.841  35.514   -61.947 1.00 173.01 ? 134 PHE C O   1 
ATOM   4205  C CB  . PHE C 3 134 ? -99.590  36.956   -61.372 1.00 168.38 ? 134 PHE C CB  1 
ATOM   4206  C CG  . PHE C 3 134 ? -100.640 37.154   -60.306 1.00 168.66 ? 134 PHE C CG  1 
ATOM   4207  C CD1 . PHE C 3 134 ? -100.284 37.577   -59.038 1.00 171.20 ? 134 PHE C CD1 1 
ATOM   4208  C CD2 . PHE C 3 134 ? -101.992 37.002   -60.595 1.00 170.17 ? 134 PHE C CD2 1 
ATOM   4209  C CE1 . PHE C 3 134 ? -101.252 37.791   -58.058 1.00 171.52 ? 134 PHE C CE1 1 
ATOM   4210  C CE2 . PHE C 3 134 ? -102.963 37.209   -59.607 1.00 172.34 ? 134 PHE C CE2 1 
ATOM   4211  C CZ  . PHE C 3 134 ? -102.586 37.615   -58.349 1.00 170.15 ? 134 PHE C CZ  1 
ATOM   4212  N N   . PRO C 3 135 ? -97.896  35.559   -63.943 1.00 172.28 ? 135 PRO C N   1 
ATOM   4213  C CA  . PRO C 3 135 ? -96.613  35.585   -64.672 1.00 173.31 ? 135 PRO C CA  1 
ATOM   4214  C C   . PRO C 3 135 ? -95.976  36.977   -64.737 1.00 177.17 ? 135 PRO C C   1 
ATOM   4215  O O   . PRO C 3 135 ? -96.602  37.967   -64.348 1.00 176.54 ? 135 PRO C O   1 
ATOM   4216  C CB  . PRO C 3 135 ? -96.976  35.052   -66.070 1.00 176.16 ? 135 PRO C CB  1 
ATOM   4217  C CG  . PRO C 3 135 ? -98.486  34.954   -66.112 1.00 180.09 ? 135 PRO C CG  1 
ATOM   4218  C CD  . PRO C 3 135 ? -99.038  35.589   -64.876 1.00 174.41 ? 135 PRO C CD  1 
ATOM   4219  N N   . LEU C 3 136 ? -94.712  37.046   -65.204 1.00 174.10 ? 136 LEU C N   1 
ATOM   4220  C CA  . LEU C 3 136 ? -93.950  38.291   -65.361 1.00 174.80 ? 136 LEU C CA  1 
ATOM   4221  C C   . LEU C 3 136 ? -93.154  38.235   -66.687 1.00 181.26 ? 136 LEU C C   1 
ATOM   4222  O O   . LEU C 3 136 ? -92.191  37.471   -66.798 1.00 180.95 ? 136 LEU C O   1 
ATOM   4223  C CB  . LEU C 3 136 ? -93.022  38.543   -64.147 1.00 173.84 ? 136 LEU C CB  1 
ATOM   4224  C CG  . LEU C 3 136 ? -93.659  38.618   -62.748 1.00 175.89 ? 136 LEU C CG  1 
ATOM   4225  C CD1 . LEU C 3 136 ? -92.663  38.244   -61.682 1.00 174.90 ? 136 LEU C CD1 1 
ATOM   4226  C CD2 . LEU C 3 136 ? -94.266  39.986   -62.474 1.00 177.53 ? 136 LEU C CD2 1 
ATOM   4227  N N   . ALA C 3 137 ? -93.603  39.011   -67.701 1.00 179.92 ? 137 ALA C N   1 
ATOM   4228  C CA  . ALA C 3 137 ? -93.042  39.083   -69.063 1.00 182.28 ? 137 ALA C CA  1 
ATOM   4229  C C   . ALA C 3 137 ? -91.572  39.535   -69.123 1.00 188.63 ? 137 ALA C C   1 
ATOM   4230  O O   . ALA C 3 137 ? -91.196  40.430   -68.363 1.00 188.97 ? 137 ALA C O   1 
ATOM   4231  C CB  . ALA C 3 137 ? -93.901  39.989   -69.934 1.00 184.48 ? 137 ALA C CB  1 
ATOM   4232  N N   . PRO C 3 138 ? -90.737  38.965   -70.036 1.00 186.36 ? 138 PRO C N   1 
ATOM   4233  C CA  . PRO C 3 138 ? -89.317  39.376   -70.096 1.00 188.11 ? 138 PRO C CA  1 
ATOM   4234  C C   . PRO C 3 138 ? -89.050  40.768   -70.677 1.00 195.25 ? 138 PRO C C   1 
ATOM   4235  O O   . PRO C 3 138 ? -89.726  41.185   -71.621 1.00 196.51 ? 138 PRO C O   1 
ATOM   4236  C CB  . PRO C 3 138 ? -88.661  38.275   -70.932 1.00 190.19 ? 138 PRO C CB  1 
ATOM   4237  C CG  . PRO C 3 138 ? -89.754  37.760   -71.789 1.00 194.20 ? 138 PRO C CG  1 
ATOM   4238  C CD  . PRO C 3 138 ? -91.023  37.880   -70.998 1.00 187.50 ? 138 PRO C CD  1 
ATOM   4239  N N   . SER C 3 139 ? -88.036  41.470   -70.114 1.00 192.56 ? 139 SER C N   1 
ATOM   4240  C CA  . SER C 3 139 ? -87.609  42.819   -70.511 1.00 211.04 ? 139 SER C CA  1 
ATOM   4241  C C   . SER C 3 139 ? -86.554  42.772   -71.621 1.00 230.45 ? 139 SER C C   1 
ATOM   4242  O O   . SER C 3 139 ? -86.395  43.727   -72.382 1.00 188.35 ? 139 SER C O   1 
ATOM   4243  C CB  . SER C 3 139 ? -87.076  43.589   -69.304 1.00 213.27 ? 139 SER C CB  1 
ATOM   4244  O OG  . SER C 3 139 ? -85.960  42.943   -68.713 1.00 216.79 ? 139 SER C OG  1 
ATOM   4245  N N   . THR C 3 147 ? -79.834  38.755   -73.481 1.00 184.59 ? 147 THR C N   1 
ATOM   4246  C CA  . THR C 3 147 ? -80.039  37.708   -72.479 1.00 179.27 ? 147 THR C CA  1 
ATOM   4247  C C   . THR C 3 147 ? -81.018  38.179   -71.383 1.00 178.79 ? 147 THR C C   1 
ATOM   4248  O O   . THR C 3 147 ? -80.713  38.106   -70.188 1.00 175.87 ? 147 THR C O   1 
ATOM   4249  C CB  . THR C 3 147 ? -78.685  37.196   -71.946 1.00 189.47 ? 147 THR C CB  1 
ATOM   4250  O OG1 . THR C 3 147 ? -77.698  37.267   -72.981 1.00 193.95 ? 147 THR C OG1 1 
ATOM   4251  C CG2 . THR C 3 147 ? -78.770  35.773   -71.396 1.00 182.70 ? 147 THR C CG2 1 
ATOM   4252  N N   . ALA C 3 148 ? -82.196  38.671   -71.806 1.00 176.00 ? 148 ALA C N   1 
ATOM   4253  C CA  . ALA C 3 148 ? -83.236  39.163   -70.902 1.00 173.98 ? 148 ALA C CA  1 
ATOM   4254  C C   . ALA C 3 148 ? -84.008  38.008   -70.251 1.00 174.18 ? 148 ALA C C   1 
ATOM   4255  O O   . ALA C 3 148 ? -84.461  37.096   -70.946 1.00 173.47 ? 148 ALA C O   1 
ATOM   4256  C CB  . ALA C 3 148 ? -84.182  40.096   -71.641 1.00 177.17 ? 148 ALA C CB  1 
ATOM   4257  N N   . ALA C 3 149 ? -84.142  38.055   -68.910 1.00 168.83 ? 149 ALA C N   1 
ATOM   4258  C CA  . ALA C 3 149 ? -84.795  37.042   -68.072 1.00 165.50 ? 149 ALA C CA  1 
ATOM   4259  C C   . ALA C 3 149 ? -86.301  37.244   -67.910 1.00 167.54 ? 149 ALA C C   1 
ATOM   4260  O O   . ALA C 3 149 ? -86.793  38.362   -68.059 1.00 167.30 ? 149 ALA C O   1 
ATOM   4261  C CB  . ALA C 3 149 ? -84.129  37.007   -66.703 1.00 164.47 ? 149 ALA C CB  1 
ATOM   4262  N N   . LEU C 3 150 ? -87.024  36.152   -67.584 1.00 162.67 ? 150 LEU C N   1 
ATOM   4263  C CA  . LEU C 3 150 ? -88.469  36.155   -67.345 1.00 161.77 ? 150 LEU C CA  1 
ATOM   4264  C C   . LEU C 3 150 ? -88.830  35.635   -65.951 1.00 164.56 ? 150 LEU C C   1 
ATOM   4265  O O   . LEU C 3 150 ? -88.208  34.688   -65.463 1.00 163.45 ? 150 LEU C O   1 
ATOM   4266  C CB  . LEU C 3 150 ? -89.260  35.426   -68.447 1.00 162.36 ? 150 LEU C CB  1 
ATOM   4267  C CG  . LEU C 3 150 ? -88.785  34.041   -68.889 1.00 167.36 ? 150 LEU C CG  1 
ATOM   4268  C CD1 . LEU C 3 150 ? -89.457  32.942   -68.084 1.00 165.72 ? 150 LEU C CD1 1 
ATOM   4269  C CD2 . LEU C 3 150 ? -89.094  33.822   -70.355 1.00 172.64 ? 150 LEU C CD2 1 
ATOM   4270  N N   . GLY C 3 151 ? -89.836  36.260   -65.340 1.00 160.87 ? 151 GLY C N   1 
ATOM   4271  C CA  . GLY C 3 151 ? -90.298  35.951   -63.991 1.00 158.77 ? 151 GLY C CA  1 
ATOM   4272  C C   . GLY C 3 151 ? -91.549  35.107   -63.882 1.00 161.66 ? 151 GLY C C   1 
ATOM   4273  O O   . GLY C 3 151 ? -92.175  34.760   -64.888 1.00 161.45 ? 151 GLY C O   1 
ATOM   4274  N N   . CYS C 3 152 ? -91.911  34.775   -62.632 1.00 157.54 ? 152 CYS C N   1 
ATOM   4275  C CA  . CYS C 3 152 ? -93.060  33.952   -62.259 1.00 157.15 ? 152 CYS C CA  1 
ATOM   4276  C C   . CYS C 3 152 ? -93.375  34.235   -60.781 1.00 159.02 ? 152 CYS C C   1 
ATOM   4277  O O   . CYS C 3 152 ? -92.669  33.748   -59.894 1.00 158.47 ? 152 CYS C O   1 
ATOM   4278  C CB  . CYS C 3 152 ? -92.747  32.474   -62.499 1.00 158.39 ? 152 CYS C CB  1 
ATOM   4279  S SG  . CYS C 3 152 ? -94.201  31.413   -62.671 1.00 163.13 ? 152 CYS C SG  1 
ATOM   4280  N N   . LEU C 3 153 ? -94.395  35.073   -60.522 1.00 153.98 ? 153 LEU C N   1 
ATOM   4281  C CA  . LEU C 3 153 ? -94.804  35.445   -59.164 1.00 152.09 ? 153 LEU C CA  1 
ATOM   4282  C C   . LEU C 3 153 ? -95.790  34.439   -58.567 1.00 156.74 ? 153 LEU C C   1 
ATOM   4283  O O   . LEU C 3 153 ? -96.728  34.010   -59.246 1.00 157.55 ? 153 LEU C O   1 
ATOM   4284  C CB  . LEU C 3 153 ? -95.394  36.878   -59.126 1.00 151.21 ? 153 LEU C CB  1 
ATOM   4285  C CG  . LEU C 3 153 ? -96.016  37.367   -57.796 1.00 153.62 ? 153 LEU C CG  1 
ATOM   4286  C CD1 . LEU C 3 153 ? -94.953  37.678   -56.756 1.00 153.02 ? 153 LEU C CD1 1 
ATOM   4287  C CD2 . LEU C 3 153 ? -96.885  38.572   -58.013 1.00 154.19 ? 153 LEU C CD2 1 
ATOM   4288  N N   . VAL C 3 154 ? -95.571  34.081   -57.287 1.00 152.33 ? 154 VAL C N   1 
ATOM   4289  C CA  . VAL C 3 154 ? -96.415  33.191   -56.482 1.00 152.21 ? 154 VAL C CA  1 
ATOM   4290  C C   . VAL C 3 154 ? -96.886  34.083   -55.315 1.00 154.41 ? 154 VAL C C   1 
ATOM   4291  O O   . VAL C 3 154 ? -96.130  34.277   -54.360 1.00 153.83 ? 154 VAL C O   1 
ATOM   4292  C CB  . VAL C 3 154 ? -95.632  31.929   -56.003 1.00 156.69 ? 154 VAL C CB  1 
ATOM   4293  C CG1 . VAL C 3 154 ? -96.523  31.001   -55.186 1.00 157.91 ? 154 VAL C CG1 1 
ATOM   4294  C CG2 . VAL C 3 154 ? -95.012  31.175   -57.176 1.00 157.01 ? 154 VAL C CG2 1 
ATOM   4295  N N   . LYS C 3 155 ? -98.089  34.693   -55.434 1.00 149.26 ? 155 LYS C N   1 
ATOM   4296  C CA  . LYS C 3 155 ? -98.583  35.632   -54.424 1.00 147.84 ? 155 LYS C CA  1 
ATOM   4297  C C   . LYS C 3 155 ? -99.748  35.125   -53.586 1.00 152.61 ? 155 LYS C C   1 
ATOM   4298  O O   . LYS C 3 155 ? -100.646 34.473   -54.109 1.00 153.21 ? 155 LYS C O   1 
ATOM   4299  C CB  . LYS C 3 155 ? -98.942  36.986   -55.058 1.00 149.02 ? 155 LYS C CB  1 
ATOM   4300  C CG  . LYS C 3 155 ? -98.760  38.162   -54.102 1.00 159.15 ? 155 LYS C CG  1 
ATOM   4301  C CD  . LYS C 3 155 ? -99.485  39.413   -54.557 1.00 165.86 ? 155 LYS C CD  1 
ATOM   4302  C CE  . LYS C 3 155 ? -99.417  40.497   -53.507 1.00 171.46 ? 155 LYS C CE  1 
ATOM   4303  N NZ  . LYS C 3 155 ? -100.237 41.681   -53.869 1.00 177.45 ? 155 LYS C NZ  1 
ATOM   4304  N N   . ASP C 3 156 ? -99.725  35.475   -52.279 1.00 149.44 ? 156 ASP C N   1 
ATOM   4305  C CA  . ASP C 3 156 ? -100.714 35.211   -51.224 1.00 150.30 ? 156 ASP C CA  1 
ATOM   4306  C C   . ASP C 3 156 ? -101.116 33.734   -51.073 1.00 154.83 ? 156 ASP C C   1 
ATOM   4307  O O   . ASP C 3 156 ? -102.010 33.252   -51.772 1.00 155.77 ? 156 ASP C O   1 
ATOM   4308  C CB  . ASP C 3 156 ? -101.958 36.109   -51.386 1.00 152.17 ? 156 ASP C CB  1 
ATOM   4309  C CG  . ASP C 3 156 ? -101.665 37.590   -51.244 1.00 165.78 ? 156 ASP C CG  1 
ATOM   4310  O OD1 . ASP C 3 156 ? -101.363 38.031   -50.111 1.00 167.21 ? 156 ASP C OD1 1 
ATOM   4311  O OD2 . ASP C 3 156 ? -101.743 38.310   -52.263 1.00 171.50 ? 156 ASP C OD2 1 
ATOM   4312  N N   . TYR C 3 157 ? -100.457 33.033   -50.131 1.00 150.79 ? 157 TYR C N   1 
ATOM   4313  C CA  . TYR C 3 157 ? -100.712 31.629   -49.806 1.00 152.77 ? 157 TYR C CA  1 
ATOM   4314  C C   . TYR C 3 157 ? -100.404 31.302   -48.336 1.00 159.08 ? 157 TYR C C   1 
ATOM   4315  O O   . TYR C 3 157 ? -99.719  32.078   -47.667 1.00 157.54 ? 157 TYR C O   1 
ATOM   4316  C CB  . TYR C 3 157 ? -99.979  30.672   -50.778 1.00 153.96 ? 157 TYR C CB  1 
ATOM   4317  C CG  . TYR C 3 157 ? -98.475  30.583   -50.613 1.00 154.15 ? 157 TYR C CG  1 
ATOM   4318  C CD1 . TYR C 3 157 ? -97.904  29.669   -49.731 1.00 157.61 ? 157 TYR C CD1 1 
ATOM   4319  C CD2 . TYR C 3 157 ? -97.620  31.339   -51.410 1.00 152.56 ? 157 TYR C CD2 1 
ATOM   4320  C CE1 . TYR C 3 157 ? -96.521  29.572   -49.583 1.00 157.32 ? 157 TYR C CE1 1 
ATOM   4321  C CE2 . TYR C 3 157 ? -96.233  31.240   -51.282 1.00 152.51 ? 157 TYR C CE2 1 
ATOM   4322  C CZ  . TYR C 3 157 ? -95.688  30.354   -50.365 1.00 159.44 ? 157 TYR C CZ  1 
ATOM   4323  O OH  . TYR C 3 157 ? -94.326  30.236   -50.226 1.00 156.70 ? 157 TYR C OH  1 
ATOM   4324  N N   . PHE C 3 158 ? -100.909 30.144   -47.847 1.00 159.46 ? 158 PHE C N   1 
ATOM   4325  C CA  . PHE C 3 158 ? -100.730 29.612   -46.485 1.00 161.80 ? 158 PHE C CA  1 
ATOM   4326  C C   . PHE C 3 158 ? -101.225 28.148   -46.445 1.00 172.08 ? 158 PHE C C   1 
ATOM   4327  O O   . PHE C 3 158 ? -102.332 27.883   -46.912 1.00 173.64 ? 158 PHE C O   1 
ATOM   4328  C CB  . PHE C 3 158 ? -101.505 30.458   -45.448 1.00 163.07 ? 158 PHE C CB  1 
ATOM   4329  C CG  . PHE C 3 158 ? -101.139 30.238   -43.997 1.00 165.63 ? 158 PHE C CG  1 
ATOM   4330  C CD1 . PHE C 3 158 ? -101.766 29.251   -43.245 1.00 172.28 ? 158 PHE C CD1 1 
ATOM   4331  C CD2 . PHE C 3 158 ? -100.219 31.063   -43.363 1.00 165.08 ? 158 PHE C CD2 1 
ATOM   4332  C CE1 . PHE C 3 158 ? -101.443 29.064   -41.898 1.00 174.63 ? 158 PHE C CE1 1 
ATOM   4333  C CE2 . PHE C 3 158 ? -99.904  30.881   -42.012 1.00 169.03 ? 158 PHE C CE2 1 
ATOM   4334  C CZ  . PHE C 3 158 ? -100.523 29.887   -41.287 1.00 170.98 ? 158 PHE C CZ  1 
ATOM   4335  N N   . PRO C 3 159 ? -100.460 27.172   -45.907 1.00 171.76 ? 159 PRO C N   1 
ATOM   4336  C CA  . PRO C 3 159 ? -99.124  27.275   -45.307 1.00 170.42 ? 159 PRO C CA  1 
ATOM   4337  C C   . PRO C 3 159 ? -97.973  27.036   -46.293 1.00 172.32 ? 159 PRO C C   1 
ATOM   4338  O O   . PRO C 3 159 ? -98.184  26.517   -47.394 1.00 172.26 ? 159 PRO C O   1 
ATOM   4339  C CB  . PRO C 3 159 ? -99.180  26.215   -44.200 1.00 176.35 ? 159 PRO C CB  1 
ATOM   4340  C CG  . PRO C 3 159 ? -100.194 25.173   -44.687 1.00 184.66 ? 159 PRO C CG  1 
ATOM   4341  C CD  . PRO C 3 159 ? -100.952 25.780   -45.849 1.00 178.02 ? 159 PRO C CD  1 
ATOM   4342  N N   . GLU C 3 160 ? -96.750  27.418   -45.886 1.00 166.89 ? 160 GLU C N   1 
ATOM   4343  C CA  . GLU C 3 160 ? -95.526  27.246   -46.671 1.00 165.02 ? 160 GLU C CA  1 
ATOM   4344  C C   . GLU C 3 160 ? -95.122  25.755   -46.700 1.00 172.33 ? 160 GLU C C   1 
ATOM   4345  O O   . GLU C 3 160 ? -95.440  25.036   -45.747 1.00 174.91 ? 160 GLU C O   1 
ATOM   4346  C CB  . GLU C 3 160 ? -94.389  28.087   -46.062 1.00 163.52 ? 160 GLU C CB  1 
ATOM   4347  C CG  . GLU C 3 160 ? -93.895  29.201   -46.968 1.00 168.78 ? 160 GLU C CG  1 
ATOM   4348  C CD  . GLU C 3 160 ? -92.434  29.568   -46.789 1.00 182.12 ? 160 GLU C CD  1 
ATOM   4349  O OE1 . GLU C 3 160 ? -92.045  29.957   -45.664 1.00 158.80 ? 160 GLU C OE1 1 
ATOM   4350  O OE2 . GLU C 3 160 ? -91.679  29.474   -47.783 1.00 180.09 ? 160 GLU C OE2 1 
ATOM   4351  N N   . PRO C 3 161 ? -94.463  25.240   -47.767 1.00 142.50 ? 161 PRO C N   1 
ATOM   4352  C CA  . PRO C 3 161 ? -93.930  25.915   -48.959 1.00 142.63 ? 161 PRO C CA  1 
ATOM   4353  C C   . PRO C 3 161 ? -94.693  25.616   -50.259 1.00 147.60 ? 161 PRO C C   1 
ATOM   4354  O O   . PRO C 3 161 ? -95.782  25.038   -50.226 1.00 147.14 ? 161 PRO C O   1 
ATOM   4355  C CB  . PRO C 3 161 ? -92.506  25.342   -49.018 1.00 144.33 ? 161 PRO C CB  1 
ATOM   4356  C CG  . PRO C 3 161 ? -92.646  23.905   -48.433 1.00 148.89 ? 161 PRO C CG  1 
ATOM   4357  C CD  . PRO C 3 161 ? -94.009  23.837   -47.753 1.00 144.35 ? 161 PRO C CD  1 
ATOM   4358  N N   . VAL C 3 162 ? -94.100  26.010   -51.407 1.00 145.35 ? 162 VAL C N   1 
ATOM   4359  C CA  . VAL C 3 162 ? -94.596  25.748   -52.763 1.00 146.22 ? 162 VAL C CA  1 
ATOM   4360  C C   . VAL C 3 162 ? -93.436  25.306   -53.666 1.00 152.09 ? 162 VAL C C   1 
ATOM   4361  O O   . VAL C 3 162 ? -92.427  26.010   -53.779 1.00 151.41 ? 162 VAL C O   1 
ATOM   4362  C CB  . VAL C 3 162 ? -95.474  26.856   -53.408 1.00 150.05 ? 162 VAL C CB  1 
ATOM   4363  C CG1 . VAL C 3 162 ? -96.903  26.789   -52.906 1.00 149.94 ? 162 VAL C CG1 1 
ATOM   4364  C CG2 . VAL C 3 162 ? -94.896  28.243   -53.195 1.00 149.53 ? 162 VAL C CG2 1 
ATOM   4365  N N   . THR C 3 163 ? -93.569  24.105   -54.255 1.00 150.59 ? 163 THR C N   1 
ATOM   4366  C CA  . THR C 3 163 ? -92.587  23.483   -55.148 1.00 151.44 ? 163 THR C CA  1 
ATOM   4367  C C   . THR C 3 163 ? -92.718  24.131   -56.549 1.00 156.90 ? 163 THR C C   1 
ATOM   4368  O O   . THR C 3 163 ? -93.773  24.014   -57.180 1.00 157.48 ? 163 THR C O   1 
ATOM   4369  C CB  . THR C 3 163 ? -92.762  21.932   -55.113 1.00 158.05 ? 163 THR C CB  1 
ATOM   4370  O OG1 . THR C 3 163 ? -92.671  21.460   -53.762 1.00 154.34 ? 163 THR C OG1 1 
ATOM   4371  C CG2 . THR C 3 163 ? -91.748  21.189   -55.981 1.00 157.16 ? 163 THR C CG2 1 
ATOM   4372  N N   . VAL C 3 164 ? -91.665  24.848   -57.009 1.00 153.54 ? 164 VAL C N   1 
ATOM   4373  C CA  . VAL C 3 164 ? -91.662  25.520   -58.319 1.00 154.22 ? 164 VAL C CA  1 
ATOM   4374  C C   . VAL C 3 164 ? -90.711  24.794   -59.288 1.00 160.24 ? 164 VAL C C   1 
ATOM   4375  O O   . VAL C 3 164 ? -89.552  24.555   -58.944 1.00 159.73 ? 164 VAL C O   1 
ATOM   4376  C CB  . VAL C 3 164 ? -91.364  27.047   -58.220 1.00 157.26 ? 164 VAL C CB  1 
ATOM   4377  C CG1 . VAL C 3 164 ? -91.540  27.740   -59.571 1.00 157.86 ? 164 VAL C CG1 1 
ATOM   4378  C CG2 . VAL C 3 164 ? -92.242  27.719   -57.168 1.00 156.23 ? 164 VAL C CG2 1 
ATOM   4379  N N   . SER C 3 165 ? -91.216  24.438   -60.487 1.00 159.03 ? 165 SER C N   1 
ATOM   4380  C CA  . SER C 3 165 ? -90.464  23.751   -61.542 1.00 160.98 ? 165 SER C CA  1 
ATOM   4381  C C   . SER C 3 165 ? -90.795  24.344   -62.916 1.00 168.61 ? 165 SER C C   1 
ATOM   4382  O O   . SER C 3 165 ? -91.947  24.699   -63.159 1.00 168.69 ? 165 SER C O   1 
ATOM   4383  C CB  . SER C 3 165 ? -90.775  22.257   -61.532 1.00 164.76 ? 165 SER C CB  1 
ATOM   4384  O OG  . SER C 3 165 ? -92.119  21.999   -61.904 1.00 172.08 ? 165 SER C OG  1 
ATOM   4385  N N   . TRP C 3 166 ? -89.798  24.440   -63.814 1.00 167.40 ? 166 TRP C N   1 
ATOM   4386  C CA  . TRP C 3 166 ? -90.014  24.975   -65.164 1.00 168.77 ? 166 TRP C CA  1 
ATOM   4387  C C   . TRP C 3 166 ? -90.153  23.850   -66.181 1.00 171.80 ? 166 TRP C C   1 
ATOM   4388  O O   . TRP C 3 166 ? -89.354  22.911   -66.174 1.00 172.06 ? 166 TRP C O   1 
ATOM   4389  C CB  . TRP C 3 166 ? -88.897  25.943   -65.580 1.00 168.19 ? 166 TRP C CB  1 
ATOM   4390  C CG  . TRP C 3 166 ? -88.738  27.140   -64.692 1.00 167.93 ? 166 TRP C CG  1 
ATOM   4391  C CD1 . TRP C 3 166 ? -88.000  27.214   -63.551 1.00 169.61 ? 166 TRP C CD1 1 
ATOM   4392  C CD2 . TRP C 3 166 ? -89.296  28.447   -64.895 1.00 167.53 ? 166 TRP C CD2 1 
ATOM   4393  N NE1 . TRP C 3 166 ? -88.065  28.482   -63.024 1.00 168.20 ? 166 TRP C NE1 1 
ATOM   4394  C CE2 . TRP C 3 166 ? -88.862  29.258   -63.825 1.00 170.22 ? 166 TRP C CE2 1 
ATOM   4395  C CE3 . TRP C 3 166 ? -90.144  29.007   -65.866 1.00 169.92 ? 166 TRP C CE3 1 
ATOM   4396  C CZ2 . TRP C 3 166 ? -89.239  30.601   -63.702 1.00 169.13 ? 166 TRP C CZ2 1 
ATOM   4397  C CZ3 . TRP C 3 166 ? -90.519  30.337   -65.740 1.00 170.81 ? 166 TRP C CZ3 1 
ATOM   4398  C CH2 . TRP C 3 166 ? -90.064  31.120   -64.673 1.00 170.06 ? 166 TRP C CH2 1 
ATOM   4399  N N   . ASN C 3 167 ? -91.178  23.958   -67.051 1.00 167.50 ? 167 ASN C N   1 
ATOM   4400  C CA  . ASN C 3 167 ? -91.532  23.009   -68.113 1.00 169.41 ? 167 ASN C CA  1 
ATOM   4401  C C   . ASN C 3 167 ? -91.721  21.579   -67.569 1.00 173.91 ? 167 ASN C C   1 
ATOM   4402  O O   . ASN C 3 167 ? -91.210  20.612   -68.143 1.00 176.03 ? 167 ASN C O   1 
ATOM   4403  C CB  . ASN C 3 167 ? -90.533  23.079   -69.284 1.00 169.29 ? 167 ASN C CB  1 
ATOM   4404  C CG  . ASN C 3 167 ? -90.422  24.447   -69.906 1.00 181.74 ? 167 ASN C CG  1 
ATOM   4405  O OD1 . ASN C 3 167 ? -91.371  24.970   -70.496 1.00 175.76 ? 167 ASN C OD1 1 
ATOM   4406  N ND2 . ASN C 3 167 ? -89.256  25.055   -69.792 1.00 170.28 ? 167 ASN C ND2 1 
ATOM   4407  N N   . SER C 3 168 ? -92.458  21.472   -66.433 1.00 168.19 ? 168 SER C N   1 
ATOM   4408  C CA  . SER C 3 168 ? -92.776  20.247   -65.681 1.00 168.11 ? 168 SER C CA  1 
ATOM   4409  C C   . SER C 3 168 ? -91.521  19.503   -65.168 1.00 171.74 ? 168 SER C C   1 
ATOM   4410  O O   . SER C 3 168 ? -91.588  18.312   -64.849 1.00 172.24 ? 168 SER C O   1 
ATOM   4411  C CB  . SER C 3 168 ? -93.698  19.325   -66.481 1.00 174.02 ? 168 SER C CB  1 
ATOM   4412  O OG  . SER C 3 168 ? -94.930  19.959   -66.786 1.00 181.78 ? 168 SER C OG  1 
ATOM   4413  N N   . GLY C 3 169 ? -90.411  20.234   -65.057 1.00 167.31 ? 169 GLY C N   1 
ATOM   4414  C CA  . GLY C 3 169 ? -89.127  19.714   -64.600 1.00 167.28 ? 169 GLY C CA  1 
ATOM   4415  C C   . GLY C 3 169 ? -88.164  19.403   -65.730 1.00 173.76 ? 169 GLY C C   1 
ATOM   4416  O O   . GLY C 3 169 ? -87.554  18.329   -65.748 1.00 175.54 ? 169 GLY C O   1 
ATOM   4417  N N   . ALA C 3 170 ? -88.021  20.342   -66.684 1.00 169.99 ? 170 ALA C N   1 
ATOM   4418  C CA  . ALA C 3 170 ? -87.124  20.204   -67.833 1.00 171.62 ? 170 ALA C CA  1 
ATOM   4419  C C   . ALA C 3 170 ? -86.016  21.264   -67.790 1.00 173.06 ? 170 ALA C C   1 
ATOM   4420  O O   . ALA C 3 170 ? -84.835  20.917   -67.896 1.00 173.73 ? 170 ALA C O   1 
ATOM   4421  C CB  . ALA C 3 170 ? -87.913  20.303   -69.131 1.00 174.44 ? 170 ALA C CB  1 
ATOM   4422  N N   . LEU C 3 171 ? -86.400  22.548   -67.615 1.00 166.25 ? 171 LEU C N   1 
ATOM   4423  C CA  . LEU C 3 171 ? -85.482  23.681   -67.526 1.00 163.99 ? 171 LEU C CA  1 
ATOM   4424  C C   . LEU C 3 171 ? -84.903  23.732   -66.115 1.00 165.19 ? 171 LEU C C   1 
ATOM   4425  O O   . LEU C 3 171 ? -85.631  23.963   -65.146 1.00 162.69 ? 171 LEU C O   1 
ATOM   4426  C CB  . LEU C 3 171 ? -86.205  24.990   -67.904 1.00 162.88 ? 171 LEU C CB  1 
ATOM   4427  C CG  . LEU C 3 171 ? -85.443  26.309   -67.762 1.00 165.86 ? 171 LEU C CG  1 
ATOM   4428  C CD1 . LEU C 3 171 ? -84.344  26.438   -68.807 1.00 167.87 ? 171 LEU C CD1 1 
ATOM   4429  C CD2 . LEU C 3 171 ? -86.387  27.475   -67.890 1.00 166.49 ? 171 LEU C CD2 1 
ATOM   4430  N N   . THR C 3 172 ? -83.592  23.473   -66.012 1.00 162.18 ? 172 THR C N   1 
ATOM   4431  C CA  . THR C 3 172 ? -82.848  23.419   -64.750 1.00 160.26 ? 172 THR C CA  1 
ATOM   4432  C C   . THR C 3 172 ? -81.709  24.443   -64.681 1.00 161.24 ? 172 THR C C   1 
ATOM   4433  O O   . THR C 3 172 ? -81.373  24.917   -63.591 1.00 159.27 ? 172 THR C O   1 
ATOM   4434  C CB  . THR C 3 172 ? -82.339  21.986   -64.494 1.00 172.60 ? 172 THR C CB  1 
ATOM   4435  O OG1 . THR C 3 172 ? -81.676  21.494   -65.664 1.00 176.35 ? 172 THR C OG1 1 
ATOM   4436  C CG2 . THR C 3 172 ? -83.457  21.030   -64.090 1.00 171.15 ? 172 THR C CG2 1 
ATOM   4437  N N   . SER C 3 173 ? -81.113  24.769   -65.838 1.00 157.00 ? 173 SER C N   1 
ATOM   4438  C CA  . SER C 3 173 ? -79.998  25.709   -65.939 1.00 155.75 ? 173 SER C CA  1 
ATOM   4439  C C   . SER C 3 173 ? -80.460  27.165   -65.814 1.00 155.03 ? 173 SER C C   1 
ATOM   4440  O O   . SER C 3 173 ? -81.448  27.556   -66.441 1.00 154.63 ? 173 SER C O   1 
ATOM   4441  C CB  . SER C 3 173 ? -79.245  25.497   -67.249 1.00 162.48 ? 173 SER C CB  1 
ATOM   4442  O OG  . SER C 3 173 ? -78.911  24.133   -67.451 1.00 174.21 ? 173 SER C OG  1 
ATOM   4443  N N   . GLY C 3 174 ? -79.746  27.935   -64.989 1.00 148.18 ? 174 GLY C N   1 
ATOM   4444  C CA  . GLY C 3 174 ? -80.004  29.352   -64.740 1.00 146.10 ? 174 GLY C CA  1 
ATOM   4445  C C   . GLY C 3 174 ? -81.305  29.677   -64.031 1.00 146.91 ? 174 GLY C C   1 
ATOM   4446  O O   . GLY C 3 174 ? -81.735  30.834   -64.030 1.00 145.72 ? 174 GLY C O   1 
ATOM   4447  N N   . VAL C 3 175 ? -81.931  28.662   -63.411 1.00 142.17 ? 175 VAL C N   1 
ATOM   4448  C CA  . VAL C 3 175 ? -83.197  28.764   -62.683 1.00 140.09 ? 175 VAL C CA  1 
ATOM   4449  C C   . VAL C 3 175 ? -82.943  29.289   -61.262 1.00 142.60 ? 175 VAL C C   1 
ATOM   4450  O O   . VAL C 3 175 ? -82.158  28.690   -60.514 1.00 142.19 ? 175 VAL C O   1 
ATOM   4451  C CB  . VAL C 3 175 ? -83.952  27.401   -62.700 1.00 143.71 ? 175 VAL C CB  1 
ATOM   4452  C CG1 . VAL C 3 175 ? -85.073  27.350   -61.667 1.00 142.00 ? 175 VAL C CG1 1 
ATOM   4453  C CG2 . VAL C 3 175 ? -84.484  27.081   -64.092 1.00 145.03 ? 175 VAL C CG2 1 
ATOM   4454  N N   . HIS C 3 176 ? -83.610  30.411   -60.911 1.00 137.96 ? 176 HIS C N   1 
ATOM   4455  C CA  A HIS C 3 176 ? -83.506  31.040   -59.596 0.50 136.59 ? 176 HIS C CA  1 
ATOM   4456  C CA  B HIS C 3 176 ? -83.506  31.040   -59.596 0.50 136.63 ? 176 HIS C CA  1 
ATOM   4457  C C   . HIS C 3 176 ? -84.879  31.133   -58.924 1.00 138.93 ? 176 HIS C C   1 
ATOM   4458  O O   . HIS C 3 176 ? -85.730  31.920   -59.351 1.00 138.37 ? 176 HIS C O   1 
ATOM   4459  C CB  A HIS C 3 176 ? -82.837  32.423   -59.691 0.50 137.81 ? 176 HIS C CB  1 
ATOM   4460  C CB  B HIS C 3 176 ? -82.838  32.424   -59.691 0.50 137.90 ? 176 HIS C CB  1 
ATOM   4461  C CG  A HIS C 3 176 ? -81.349  32.374   -59.836 0.50 141.98 ? 176 HIS C CG  1 
ATOM   4462  C CG  B HIS C 3 176 ? -81.344  32.378   -59.756 0.50 142.08 ? 176 HIS C CG  1 
ATOM   4463  N ND1 A HIS C 3 176 ? -80.521  32.267   -58.734 0.50 143.47 ? 176 HIS C ND1 1 
ATOM   4464  N ND1 B HIS C 3 176 ? -80.672  32.463   -60.962 0.50 145.14 ? 176 HIS C ND1 1 
ATOM   4465  C CD2 A HIS C 3 176 ? -80.586  32.447   -60.951 0.50 145.03 ? 176 HIS C CD2 1 
ATOM   4466  C CD2 B HIS C 3 176 ? -80.439  32.276   -58.757 0.50 143.71 ? 176 HIS C CD2 1 
ATOM   4467  C CE1 A HIS C 3 176 ? -79.287  32.267   -59.211 0.50 143.95 ? 176 HIS C CE1 1 
ATOM   4468  C CE1 B HIS C 3 176 ? -79.385  32.403   -60.660 0.50 145.05 ? 176 HIS C CE1 1 
ATOM   4469  N NE2 A HIS C 3 176 ? -79.276  32.375   -60.540 0.50 145.20 ? 176 HIS C NE2 1 
ATOM   4470  N NE2 B HIS C 3 176 ? -79.196  32.292   -59.345 0.50 144.60 ? 176 HIS C NE2 1 
ATOM   4471  N N   . THR C 3 177 ? -85.103  30.310   -57.884 1.00 134.07 ? 177 THR C N   1 
ATOM   4472  C CA  . THR C 3 177 ? -86.354  30.298   -57.123 1.00 132.67 ? 177 THR C CA  1 
ATOM   4473  C C   . THR C 3 177 ? -86.068  30.925   -55.759 1.00 135.88 ? 177 THR C C   1 
ATOM   4474  O O   . THR C 3 177 ? -85.430  30.309   -54.901 1.00 135.22 ? 177 THR C O   1 
ATOM   4475  C CB  . THR C 3 177 ? -87.002  28.905   -57.102 1.00 136.56 ? 177 THR C CB  1 
ATOM   4476  O OG1 . THR C 3 177 ? -87.102  28.419   -58.442 1.00 134.16 ? 177 THR C OG1 1 
ATOM   4477  C CG2 . THR C 3 177 ? -88.390  28.919   -56.470 1.00 133.97 ? 177 THR C CG2 1 
ATOM   4478  N N   . PHE C 3 178 ? -86.495  32.184   -55.603 1.00 132.64 ? 178 PHE C N   1 
ATOM   4479  C CA  . PHE C 3 178 ? -86.284  33.005   -54.416 1.00 132.63 ? 178 PHE C CA  1 
ATOM   4480  C C   . PHE C 3 178 ? -87.111  32.575   -53.212 1.00 136.08 ? 178 PHE C C   1 
ATOM   4481  O O   . PHE C 3 178 ? -88.272  32.185   -53.384 1.00 135.73 ? 178 PHE C O   1 
ATOM   4482  C CB  . PHE C 3 178 ? -86.565  34.481   -54.734 1.00 135.20 ? 178 PHE C CB  1 
ATOM   4483  C CG  . PHE C 3 178 ? -85.559  35.095   -55.670 1.00 137.40 ? 178 PHE C CG  1 
ATOM   4484  C CD1 . PHE C 3 178 ? -84.390  35.662   -55.184 1.00 141.10 ? 178 PHE C CD1 1 
ATOM   4485  C CD2 . PHE C 3 178 ? -85.778  35.103   -57.040 1.00 139.53 ? 178 PHE C CD2 1 
ATOM   4486  C CE1 . PHE C 3 178 ? -83.461  36.229   -56.053 1.00 142.82 ? 178 PHE C CE1 1 
ATOM   4487  C CE2 . PHE C 3 178 ? -84.844  35.665   -57.906 1.00 143.11 ? 178 PHE C CE2 1 
ATOM   4488  C CZ  . PHE C 3 178 ? -83.694  36.228   -57.408 1.00 141.90 ? 178 PHE C CZ  1 
ATOM   4489  N N   . PRO C 3 179 ? -86.557  32.706   -51.980 1.00 131.88 ? 179 PRO C N   1 
ATOM   4490  C CA  . PRO C 3 179 ? -87.335  32.350   -50.784 1.00 131.10 ? 179 PRO C CA  1 
ATOM   4491  C C   . PRO C 3 179 ? -88.557  33.250   -50.575 1.00 133.85 ? 179 PRO C C   1 
ATOM   4492  O O   . PRO C 3 179 ? -88.563  34.412   -50.990 1.00 133.91 ? 179 PRO C O   1 
ATOM   4493  C CB  . PRO C 3 179 ? -86.321  32.509   -49.646 1.00 133.38 ? 179 PRO C CB  1 
ATOM   4494  C CG  . PRO C 3 179 ? -84.979  32.489   -50.307 1.00 137.92 ? 179 PRO C CG  1 
ATOM   4495  C CD  . PRO C 3 179 ? -85.198  33.151   -51.613 1.00 133.65 ? 179 PRO C CD  1 
ATOM   4496  N N   . ALA C 3 180 ? -89.599  32.693   -49.951 1.00 129.24 ? 180 ALA C N   1 
ATOM   4497  C CA  . ALA C 3 180 ? -90.845  33.401   -49.680 1.00 129.22 ? 180 ALA C CA  1 
ATOM   4498  C C   . ALA C 3 180 ? -90.739  34.326   -48.476 1.00 133.83 ? 180 ALA C C   1 
ATOM   4499  O O   . ALA C 3 180 ? -89.928  34.088   -47.577 1.00 133.11 ? 180 ALA C O   1 
ATOM   4500  C CB  . ALA C 3 180 ? -91.972  32.404   -49.471 1.00 129.41 ? 180 ALA C CB  1 
ATOM   4501  N N   . VAL C 3 181 ? -91.575  35.376   -48.460 1.00 131.75 ? 181 VAL C N   1 
ATOM   4502  C CA  . VAL C 3 181 ? -91.665  36.352   -47.370 1.00 133.29 ? 181 VAL C CA  1 
ATOM   4503  C C   . VAL C 3 181 ? -93.118  36.552   -46.943 1.00 137.23 ? 181 VAL C C   1 
ATOM   4504  O O   . VAL C 3 181 ? -93.993  36.666   -47.800 1.00 135.94 ? 181 VAL C O   1 
ATOM   4505  C CB  . VAL C 3 181 ? -90.943  37.697   -47.656 1.00 138.96 ? 181 VAL C CB  1 
ATOM   4506  C CG1 . VAL C 3 181 ? -89.437  37.576   -47.430 1.00 138.95 ? 181 VAL C CG1 1 
ATOM   4507  C CG2 . VAL C 3 181 ? -91.254  38.235   -49.054 1.00 138.74 ? 181 VAL C CG2 1 
ATOM   4508  N N   . LEU C 3 182 ? -93.378  36.563   -45.624 1.00 135.21 ? 182 LEU C N   1 
ATOM   4509  C CA  . LEU C 3 182 ? -94.725  36.758   -45.091 1.00 136.01 ? 182 LEU C CA  1 
ATOM   4510  C C   . LEU C 3 182 ? -95.127  38.222   -45.251 1.00 143.60 ? 182 LEU C C   1 
ATOM   4511  O O   . LEU C 3 182 ? -94.407  39.114   -44.797 1.00 144.54 ? 182 LEU C O   1 
ATOM   4512  C CB  . LEU C 3 182 ? -94.813  36.317   -43.620 1.00 136.34 ? 182 LEU C CB  1 
ATOM   4513  C CG  . LEU C 3 182 ? -96.211  36.343   -42.999 1.00 141.67 ? 182 LEU C CG  1 
ATOM   4514  C CD1 . LEU C 3 182 ? -96.592  34.988   -42.447 1.00 140.90 ? 182 LEU C CD1 1 
ATOM   4515  C CD2 . LEU C 3 182 ? -96.312  37.401   -41.920 1.00 146.07 ? 182 LEU C CD2 1 
ATOM   4516  N N   . GLN C 3 183 ? -96.273  38.458   -45.910 1.00 142.06 ? 183 GLN C N   1 
ATOM   4517  C CA  . GLN C 3 183 ? -96.819  39.796   -46.150 1.00 144.46 ? 183 GLN C CA  1 
ATOM   4518  C C   . GLN C 3 183 ? -97.476  40.369   -44.891 1.00 151.61 ? 183 GLN C C   1 
ATOM   4519  O O   . GLN C 3 183 ? -97.647  39.660   -43.894 1.00 151.14 ? 183 GLN C O   1 
ATOM   4520  C CB  . GLN C 3 183 ? -97.828  39.776   -47.314 1.00 145.35 ? 183 GLN C CB  1 
ATOM   4521  C CG  . GLN C 3 183 ? -97.190  39.642   -48.690 1.00 156.08 ? 183 GLN C CG  1 
ATOM   4522  C CD  . GLN C 3 183 ? -98.231  39.618   -49.770 1.00 170.76 ? 183 GLN C CD  1 
ATOM   4523  O OE1 . GLN C 3 183 ? -98.740  40.656   -50.197 1.00 168.93 ? 183 GLN C OE1 1 
ATOM   4524  N NE2 . GLN C 3 183 ? -98.578  38.428   -50.228 1.00 157.98 ? 183 GLN C NE2 1 
ATOM   4525  N N   . SER C 3 184 ? -97.862  41.656   -44.951 1.00 150.93 ? 184 SER C N   1 
ATOM   4526  C CA  . SER C 3 184 ? -98.540  42.370   -43.869 1.00 153.59 ? 184 SER C CA  1 
ATOM   4527  C C   . SER C 3 184 ? -99.886  41.698   -43.559 1.00 157.02 ? 184 SER C C   1 
ATOM   4528  O O   . SER C 3 184 ? -100.299 41.653   -42.401 1.00 157.25 ? 184 SER C O   1 
ATOM   4529  C CB  . SER C 3 184 ? -98.748  43.832   -44.253 1.00 160.72 ? 184 SER C CB  1 
ATOM   4530  O OG  . SER C 3 184 ? -97.539  44.434   -44.687 1.00 172.90 ? 184 SER C OG  1 
ATOM   4531  N N   . SER C 3 185 ? -100.529 41.128   -44.601 1.00 153.01 ? 185 SER C N   1 
ATOM   4532  C CA  . SER C 3 185 ? -101.795 40.392   -44.533 1.00 152.90 ? 185 SER C CA  1 
ATOM   4533  C C   . SER C 3 185 ? -101.657 39.090   -43.730 1.00 156.26 ? 185 SER C C   1 
ATOM   4534  O O   . SER C 3 185 ? -102.650 38.592   -43.192 1.00 155.86 ? 185 SER C O   1 
ATOM   4535  C CB  . SER C 3 185 ? -102.300 40.083   -45.941 1.00 155.25 ? 185 SER C CB  1 
ATOM   4536  O OG  . SER C 3 185 ? -101.345 39.356   -46.698 1.00 160.90 ? 185 SER C OG  1 
ATOM   4537  N N   . GLY C 3 186 ? -100.429 38.567   -43.665 1.00 152.26 ? 186 GLY C N   1 
ATOM   4538  C CA  . GLY C 3 186 ? -100.087 37.337   -42.958 1.00 150.98 ? 186 GLY C CA  1 
ATOM   4539  C C   . GLY C 3 186 ? -99.950  36.136   -43.872 1.00 152.52 ? 186 GLY C C   1 
ATOM   4540  O O   . GLY C 3 186 ? -99.853  35.001   -43.393 1.00 151.27 ? 186 GLY C O   1 
ATOM   4541  N N   . LEU C 3 187 ? -99.949  36.386   -45.199 1.00 148.13 ? 187 LEU C N   1 
ATOM   4542  C CA  . LEU C 3 187 ? -99.846  35.363   -46.236 1.00 146.29 ? 187 LEU C CA  1 
ATOM   4543  C C   . LEU C 3 187 ? -98.519  35.449   -46.984 1.00 149.46 ? 187 LEU C C   1 
ATOM   4544  O O   . LEU C 3 187 ? -98.128  36.527   -47.431 1.00 149.60 ? 187 LEU C O   1 
ATOM   4545  C CB  . LEU C 3 187 ? -101.033 35.467   -47.203 1.00 146.59 ? 187 LEU C CB  1 
ATOM   4546  C CG  . LEU C 3 187 ? -102.381 35.067   -46.621 1.00 152.00 ? 187 LEU C CG  1 
ATOM   4547  C CD1 . LEU C 3 187 ? -103.415 36.144   -46.856 1.00 156.55 ? 187 LEU C CD1 1 
ATOM   4548  C CD2 . LEU C 3 187 ? -102.845 33.748   -47.192 1.00 151.13 ? 187 LEU C CD2 1 
ATOM   4549  N N   . TYR C 3 188 ? -97.832  34.299   -47.117 1.00 145.09 ? 188 TYR C N   1 
ATOM   4550  C CA  . TYR C 3 188 ? -96.527  34.162   -47.772 1.00 144.45 ? 188 TYR C CA  1 
ATOM   4551  C C   . TYR C 3 188 ? -96.618  34.414   -49.287 1.00 149.05 ? 188 TYR C C   1 
ATOM   4552  O O   . TYR C 3 188 ? -97.683  34.220   -49.879 1.00 148.37 ? 188 TYR C O   1 
ATOM   4553  C CB  . TYR C 3 188 ? -95.925  32.768   -47.496 1.00 144.52 ? 188 TYR C CB  1 
ATOM   4554  C CG  . TYR C 3 188 ? -95.764  32.428   -46.028 1.00 146.36 ? 188 TYR C CG  1 
ATOM   4555  C CD1 . TYR C 3 188 ? -94.570  32.679   -45.360 1.00 148.55 ? 188 TYR C CD1 1 
ATOM   4556  C CD2 . TYR C 3 188 ? -96.792  31.812   -45.316 1.00 147.12 ? 188 TYR C CD2 1 
ATOM   4557  C CE1 . TYR C 3 188 ? -94.411  32.352   -44.011 1.00 149.91 ? 188 TYR C CE1 1 
ATOM   4558  C CE2 . TYR C 3 188 ? -96.647  31.483   -43.969 1.00 148.27 ? 188 TYR C CE2 1 
ATOM   4559  C CZ  . TYR C 3 188 ? -95.452  31.747   -43.321 1.00 155.63 ? 188 TYR C CZ  1 
ATOM   4560  O OH  . TYR C 3 188 ? -95.317  31.429   -41.989 1.00 155.63 ? 188 TYR C OH  1 
ATOM   4561  N N   . SER C 3 189 ? -95.500  34.865   -49.904 1.00 146.54 ? 189 SER C N   1 
ATOM   4562  C CA  . SER C 3 189 ? -95.387  35.156   -51.342 1.00 146.36 ? 189 SER C CA  1 
ATOM   4563  C C   . SER C 3 189 ? -93.935  35.071   -51.841 1.00 150.34 ? 189 SER C C   1 
ATOM   4564  O O   . SER C 3 189 ? -93.042  35.673   -51.234 1.00 150.60 ? 189 SER C O   1 
ATOM   4565  C CB  . SER C 3 189 ? -95.978  36.528   -51.667 1.00 150.55 ? 189 SER C CB  1 
ATOM   4566  O OG  . SER C 3 189 ? -95.773  36.884   -53.024 1.00 158.11 ? 189 SER C OG  1 
ATOM   4567  N N   . LEU C 3 190 ? -93.703  34.332   -52.949 1.00 146.43 ? 190 LEU C N   1 
ATOM   4568  C CA  . LEU C 3 190 ? -92.363  34.199   -53.538 1.00 146.24 ? 190 LEU C CA  1 
ATOM   4569  C C   . LEU C 3 190 ? -92.318  34.546   -55.034 1.00 150.15 ? 190 LEU C C   1 
ATOM   4570  O O   . LEU C 3 190 ? -93.348  34.837   -55.649 1.00 150.78 ? 190 LEU C O   1 
ATOM   4571  C CB  . LEU C 3 190 ? -91.702  32.823   -53.258 1.00 145.51 ? 190 LEU C CB  1 
ATOM   4572  C CG  . LEU C 3 190 ? -92.323  31.541   -53.820 1.00 149.41 ? 190 LEU C CG  1 
ATOM   4573  C CD1 . LEU C 3 190 ? -91.629  31.111   -55.108 1.00 149.16 ? 190 LEU C CD1 1 
ATOM   4574  C CD2 . LEU C 3 190 ? -92.152  30.420   -52.831 1.00 152.12 ? 190 LEU C CD2 1 
ATOM   4575  N N   . SER C 3 191 ? -91.097  34.524   -55.596 1.00 144.90 ? 191 SER C N   1 
ATOM   4576  C CA  . SER C 3 191 ? -90.776  34.823   -56.986 1.00 144.15 ? 191 SER C CA  1 
ATOM   4577  C C   . SER C 3 191 ? -89.867  33.730   -57.555 1.00 145.93 ? 191 SER C C   1 
ATOM   4578  O O   . SER C 3 191 ? -89.117  33.105   -56.803 1.00 144.62 ? 191 SER C O   1 
ATOM   4579  C CB  . SER C 3 191 ? -90.087  36.180   -57.073 1.00 148.54 ? 191 SER C CB  1 
ATOM   4580  O OG  . SER C 3 191 ? -89.326  36.461   -55.906 1.00 158.96 ? 191 SER C OG  1 
ATOM   4581  N N   . SER C 3 192 ? -89.943  33.489   -58.873 1.00 142.75 ? 192 SER C N   1 
ATOM   4582  C CA  . SER C 3 192 ? -89.121  32.487   -59.561 1.00 143.08 ? 192 SER C CA  1 
ATOM   4583  C C   . SER C 3 192 ? -88.735  32.985   -60.962 1.00 150.06 ? 192 SER C C   1 
ATOM   4584  O O   . SER C 3 192 ? -89.613  33.263   -61.782 1.00 151.21 ? 192 SER C O   1 
ATOM   4585  C CB  . SER C 3 192 ? -89.846  31.146   -59.628 1.00 145.79 ? 192 SER C CB  1 
ATOM   4586  O OG  . SER C 3 192 ? -88.930  30.066   -59.699 1.00 152.68 ? 192 SER C OG  1 
ATOM   4587  N N   . VAL C 3 193 ? -87.419  33.142   -61.216 1.00 147.29 ? 193 VAL C N   1 
ATOM   4588  C CA  . VAL C 3 193 ? -86.880  33.656   -62.489 1.00 148.27 ? 193 VAL C CA  1 
ATOM   4589  C C   . VAL C 3 193 ? -85.912  32.677   -63.175 1.00 153.23 ? 193 VAL C C   1 
ATOM   4590  O O   . VAL C 3 193 ? -85.476  31.703   -62.556 1.00 152.24 ? 193 VAL C O   1 
ATOM   4591  C CB  . VAL C 3 193 ? -86.229  35.063   -62.332 1.00 152.33 ? 193 VAL C CB  1 
ATOM   4592  C CG1 . VAL C 3 193 ? -87.235  36.111   -61.860 1.00 151.88 ? 193 VAL C CG1 1 
ATOM   4593  C CG2 . VAL C 3 193 ? -85.010  35.016   -61.416 1.00 151.75 ? 193 VAL C CG2 1 
ATOM   4594  N N   . VAL C 3 194 ? -85.557  32.969   -64.446 1.00 151.73 ? 194 VAL C N   1 
ATOM   4595  C CA  . VAL C 3 194 ? -84.599  32.200   -65.244 1.00 153.14 ? 194 VAL C CA  1 
ATOM   4596  C C   . VAL C 3 194 ? -83.933  33.111   -66.294 1.00 158.05 ? 194 VAL C C   1 
ATOM   4597  O O   . VAL C 3 194 ? -84.621  33.739   -67.100 1.00 157.37 ? 194 VAL C O   1 
ATOM   4598  C CB  . VAL C 3 194 ? -85.162  30.867   -65.830 1.00 158.41 ? 194 VAL C CB  1 
ATOM   4599  C CG1 . VAL C 3 194 ? -86.385  31.087   -66.723 1.00 159.09 ? 194 VAL C CG1 1 
ATOM   4600  C CG2 . VAL C 3 194 ? -84.078  30.068   -66.554 1.00 159.77 ? 194 VAL C CG2 1 
ATOM   4601  N N   . THR C 3 195 ? -82.589  33.196   -66.245 1.00 172.96 ? 195 THR C N   1 
ATOM   4602  C CA  . THR C 3 195 ? -81.774  33.992   -67.167 1.00 175.68 ? 195 THR C CA  1 
ATOM   4603  C C   . THR C 3 195 ? -81.756  33.287   -68.532 1.00 182.42 ? 195 THR C C   1 
ATOM   4604  O O   . THR C 3 195 ? -80.890  32.448   -68.804 1.00 183.61 ? 195 THR C O   1 
ATOM   4605  C CB  . THR C 3 195 ? -80.379  34.283   -66.567 1.00 184.82 ? 195 THR C CB  1 
ATOM   4606  O OG1 . THR C 3 195 ? -80.524  34.740   -65.222 1.00 182.58 ? 195 THR C OG1 1 
ATOM   4607  C CG2 . THR C 3 195 ? -79.590  35.308   -67.375 1.00 186.05 ? 195 THR C CG2 1 
ATOM   4608  N N   . VAL C 3 196 ? -82.760  33.608   -69.364 1.00 179.38 ? 196 VAL C N   1 
ATOM   4609  C CA  . VAL C 3 196 ? -82.955  33.044   -70.704 1.00 180.67 ? 196 VAL C CA  1 
ATOM   4610  C C   . VAL C 3 196 ? -82.322  33.917   -71.803 1.00 187.43 ? 196 VAL C C   1 
ATOM   4611  O O   . VAL C 3 196 ? -82.294  35.144   -71.657 1.00 187.23 ? 196 VAL C O   1 
ATOM   4612  C CB  . VAL C 3 196 ? -84.444  32.710   -71.015 1.00 182.91 ? 196 VAL C CB  1 
ATOM   4613  C CG1 . VAL C 3 196 ? -84.887  31.439   -70.300 1.00 180.84 ? 196 VAL C CG1 1 
ATOM   4614  C CG2 . VAL C 3 196 ? -85.372  33.879   -70.691 1.00 181.58 ? 196 VAL C CG2 1 
ATOM   4615  N N   . PRO C 3 197 ? -81.819  33.321   -72.913 1.00 186.45 ? 197 PRO C N   1 
ATOM   4616  C CA  . PRO C 3 197 ? -81.231  34.153   -73.970 1.00 189.61 ? 197 PRO C CA  1 
ATOM   4617  C C   . PRO C 3 197 ? -82.283  34.839   -74.833 1.00 193.77 ? 197 PRO C C   1 
ATOM   4618  O O   . PRO C 3 197 ? -83.385  34.315   -75.018 1.00 191.18 ? 197 PRO C O   1 
ATOM   4619  C CB  . PRO C 3 197 ? -80.391  33.161   -74.777 1.00 194.22 ? 197 PRO C CB  1 
ATOM   4620  C CG  . PRO C 3 197 ? -81.068  31.858   -74.599 1.00 196.59 ? 197 PRO C CG  1 
ATOM   4621  C CD  . PRO C 3 197 ? -81.760  31.883   -73.262 1.00 188.32 ? 197 PRO C CD  1 
ATOM   4622  N N   . SER C 3 198 ? -81.921  36.006   -75.382 1.00 193.55 ? 198 SER C N   1 
ATOM   4623  C CA  . SER C 3 198 ? -82.782  36.796   -76.260 1.00 194.83 ? 198 SER C CA  1 
ATOM   4624  C C   . SER C 3 198 ? -82.927  36.146   -77.656 1.00 203.26 ? 198 SER C C   1 
ATOM   4625  O O   . SER C 3 198 ? -83.747  36.601   -78.455 1.00 204.09 ? 198 SER C O   1 
ATOM   4626  C CB  . SER C 3 198 ? -82.245  38.220   -76.374 1.00 200.18 ? 198 SER C CB  1 
ATOM   4627  O OG  . SER C 3 198 ? -82.111  38.822   -75.097 1.00 206.38 ? 198 SER C OG  1 
ATOM   4628  N N   . SER C 3 199 ? -82.143  35.077   -77.933 1.00 202.37 ? 199 SER C N   1 
ATOM   4629  C CA  . SER C 3 199 ? -82.132  34.334   -79.200 1.00 205.70 ? 199 SER C CA  1 
ATOM   4630  C C   . SER C 3 199 ? -83.411  33.527   -79.468 1.00 209.04 ? 199 SER C C   1 
ATOM   4631  O O   . SER C 3 199 ? -83.786  33.366   -80.633 1.00 211.15 ? 199 SER C O   1 
ATOM   4632  C CB  . SER C 3 199 ? -80.914  33.417   -79.274 1.00 211.31 ? 199 SER C CB  1 
ATOM   4633  O OG  . SER C 3 199 ? -79.706  34.152   -79.370 1.00 222.87 ? 199 SER C OG  1 
ATOM   4634  N N   . SER C 3 200 ? -84.066  33.015   -78.398 1.00 202.50 ? 200 SER C N   1 
ATOM   4635  C CA  . SER C 3 200 ? -85.283  32.204   -78.502 1.00 200.82 ? 200 SER C CA  1 
ATOM   4636  C C   . SER C 3 200 ? -86.559  32.985   -78.169 1.00 203.08 ? 200 SER C C   1 
ATOM   4637  O O   . SER C 3 200 ? -87.341  33.278   -79.078 1.00 204.06 ? 200 SER C O   1 
ATOM   4638  C CB  . SER C 3 200 ? -85.170  30.944   -77.648 1.00 202.03 ? 200 SER C CB  1 
ATOM   4639  O OG  . SER C 3 200 ? -86.132  29.985   -78.051 1.00 210.05 ? 200 SER C OG  1 
ATOM   4640  N N   . LEU C 3 201 ? -86.755  33.332   -76.874 1.00 196.89 ? 201 LEU C N   1 
ATOM   4641  C CA  . LEU C 3 201 ? -87.904  34.075   -76.335 1.00 194.79 ? 201 LEU C CA  1 
ATOM   4642  C C   . LEU C 3 201 ? -89.253  33.341   -76.562 1.00 197.71 ? 201 LEU C C   1 
ATOM   4643  O O   . LEU C 3 201 ? -89.346  32.142   -76.280 1.00 195.99 ? 201 LEU C O   1 
ATOM   4644  C CB  . LEU C 3 201 ? -87.952  35.547   -76.836 1.00 196.60 ? 201 LEU C CB  1 
ATOM   4645  C CG  . LEU C 3 201 ? -86.702  36.421   -76.665 1.00 202.71 ? 201 LEU C CG  1 
ATOM   4646  C CD1 . LEU C 3 201 ? -86.766  37.627   -77.582 1.00 205.61 ? 201 LEU C CD1 1 
ATOM   4647  C CD2 . LEU C 3 201 ? -86.536  36.884   -75.228 1.00 202.60 ? 201 LEU C CD2 1 
ATOM   4648  N N   . GLY C 3 202 ? -90.256  34.071   -77.070 1.00 194.99 ? 202 GLY C N   1 
ATOM   4649  C CA  . GLY C 3 202 ? -91.619  33.611   -77.337 1.00 194.26 ? 202 GLY C CA  1 
ATOM   4650  C C   . GLY C 3 202 ? -91.799  32.410   -78.246 1.00 199.34 ? 202 GLY C C   1 
ATOM   4651  O O   . GLY C 3 202 ? -92.855  31.769   -78.205 1.00 198.10 ? 202 GLY C O   1 
ATOM   4652  N N   . THR C 3 203 ? -90.786  32.107   -79.086 1.00 198.11 ? 203 THR C N   1 
ATOM   4653  C CA  . THR C 3 203 ? -90.786  30.951   -79.994 1.00 199.57 ? 203 THR C CA  1 
ATOM   4654  C C   . THR C 3 203 ? -90.738  29.656   -79.174 1.00 200.60 ? 203 THR C C   1 
ATOM   4655  O O   . THR C 3 203 ? -91.448  28.698   -79.494 1.00 200.67 ? 203 THR C O   1 
ATOM   4656  C CB  . THR C 3 203 ? -89.627  31.038   -80.998 1.00 211.51 ? 203 THR C CB  1 
ATOM   4657  O OG1 . THR C 3 203 ? -88.385  31.079   -80.292 1.00 210.51 ? 203 THR C OG1 1 
ATOM   4658  C CG2 . THR C 3 203 ? -89.749  32.233   -81.941 1.00 213.24 ? 203 THR C CG2 1 
ATOM   4659  N N   . GLN C 3 204 ? -89.917  29.649   -78.099 1.00 194.00 ? 204 GLN C N   1 
ATOM   4660  C CA  . GLN C 3 204 ? -89.789  28.529   -77.171 1.00 190.90 ? 204 GLN C CA  1 
ATOM   4661  C C   . GLN C 3 204 ? -90.877  28.666   -76.109 1.00 190.29 ? 204 GLN C C   1 
ATOM   4662  O O   . GLN C 3 204 ? -91.037  29.743   -75.526 1.00 188.07 ? 204 GLN C O   1 
ATOM   4663  C CB  . GLN C 3 204 ? -88.398  28.513   -76.516 1.00 191.85 ? 204 GLN C CB  1 
ATOM   4664  C CG  . GLN C 3 204 ? -87.826  27.115   -76.289 1.00 202.14 ? 204 GLN C CG  1 
ATOM   4665  C CD  . GLN C 3 204 ? -88.523  26.352   -75.185 1.00 214.10 ? 204 GLN C CD  1 
ATOM   4666  O OE1 . GLN C 3 204 ? -88.313  26.601   -73.993 1.00 207.46 ? 204 GLN C OE1 1 
ATOM   4667  N NE2 . GLN C 3 204 ? -89.357  25.394   -75.561 1.00 203.61 ? 204 GLN C NE2 1 
ATOM   4668  N N   . THR C 3 205 ? -91.640  27.584   -75.881 1.00 185.73 ? 205 THR C N   1 
ATOM   4669  C CA  . THR C 3 205 ? -92.730  27.548   -74.901 1.00 183.11 ? 205 THR C CA  1 
ATOM   4670  C C   . THR C 3 205 ? -92.141  27.437   -73.484 1.00 183.43 ? 205 THR C C   1 
ATOM   4671  O O   . THR C 3 205 ? -91.601  26.386   -73.126 1.00 183.33 ? 205 THR C O   1 
ATOM   4672  C CB  . THR C 3 205 ? -93.740  26.425   -75.252 1.00 192.64 ? 205 THR C CB  1 
ATOM   4673  O OG1 . THR C 3 205 ? -94.036  26.457   -76.652 1.00 194.79 ? 205 THR C OG1 1 
ATOM   4674  C CG2 . THR C 3 205 ? -95.035  26.518   -74.445 1.00 189.09 ? 205 THR C CG2 1 
ATOM   4675  N N   . TYR C 3 206 ? -92.218  28.534   -72.696 1.00 176.61 ? 206 TYR C N   1 
ATOM   4676  C CA  . TYR C 3 206 ? -91.710  28.579   -71.321 1.00 173.54 ? 206 TYR C CA  1 
ATOM   4677  C C   . TYR C 3 206 ? -92.850  28.440   -70.308 1.00 173.77 ? 206 TYR C C   1 
ATOM   4678  O O   . TYR C 3 206 ? -93.560  29.409   -70.024 1.00 172.43 ? 206 TYR C O   1 
ATOM   4679  C CB  . TYR C 3 206 ? -90.857  29.838   -71.068 1.00 174.44 ? 206 TYR C CB  1 
ATOM   4680  C CG  . TYR C 3 206 ? -89.529  29.847   -71.797 1.00 177.35 ? 206 TYR C CG  1 
ATOM   4681  C CD1 . TYR C 3 206 ? -88.462  29.068   -71.356 1.00 179.25 ? 206 TYR C CD1 1 
ATOM   4682  C CD2 . TYR C 3 206 ? -89.323  30.669   -72.900 1.00 179.83 ? 206 TYR C CD2 1 
ATOM   4683  C CE1 . TYR C 3 206 ? -87.234  29.080   -72.018 1.00 181.75 ? 206 TYR C CE1 1 
ATOM   4684  C CE2 . TYR C 3 206 ? -88.098  30.694   -73.567 1.00 182.67 ? 206 TYR C CE2 1 
ATOM   4685  C CZ  . TYR C 3 206 ? -87.055  29.898   -73.122 1.00 189.76 ? 206 TYR C CZ  1 
ATOM   4686  O OH  . TYR C 3 206 ? -85.847  29.922   -73.776 1.00 192.65 ? 206 TYR C OH  1 
ATOM   4687  N N   . ILE C 3 207 ? -93.029  27.212   -69.786 1.00 169.05 ? 207 ILE C N   1 
ATOM   4688  C CA  . ILE C 3 207 ? -94.078  26.838   -68.828 1.00 167.67 ? 207 ILE C CA  1 
ATOM   4689  C C   . ILE C 3 207 ? -93.542  26.922   -67.393 1.00 168.71 ? 207 ILE C C   1 
ATOM   4690  O O   . ILE C 3 207 ? -92.458  26.415   -67.113 1.00 167.37 ? 207 ILE C O   1 
ATOM   4691  C CB  . ILE C 3 207 ? -94.657  25.425   -69.160 1.00 171.51 ? 207 ILE C CB  1 
ATOM   4692  C CG1 . ILE C 3 207 ? -94.919  25.243   -70.682 1.00 173.46 ? 207 ILE C CG1 1 
ATOM   4693  C CG2 . ILE C 3 207 ? -95.922  25.135   -68.352 1.00 171.96 ? 207 ILE C CG2 1 
ATOM   4694  C CD1 . ILE C 3 207 ? -94.532  23.869   -71.251 1.00 180.78 ? 207 ILE C CD1 1 
ATOM   4695  N N   . CYS C 3 208 ? -94.302  27.568   -66.495 1.00 164.67 ? 208 CYS C N   1 
ATOM   4696  C CA  . CYS C 3 208 ? -93.928  27.737   -65.089 1.00 163.93 ? 208 CYS C CA  1 
ATOM   4697  C C   . CYS C 3 208 ? -94.886  26.938   -64.188 1.00 168.34 ? 208 CYS C C   1 
ATOM   4698  O O   . CYS C 3 208 ? -95.985  27.406   -63.874 1.00 168.79 ? 208 CYS C O   1 
ATOM   4699  C CB  . CYS C 3 208 ? -93.889  29.220   -64.722 1.00 163.99 ? 208 CYS C CB  1 
ATOM   4700  S SG  . CYS C 3 208 ? -93.427  29.560   -63.003 1.00 167.48 ? 208 CYS C SG  1 
ATOM   4701  N N   . ASN C 3 209 ? -94.468  25.713   -63.805 1.00 164.49 ? 209 ASN C N   1 
ATOM   4702  C CA  . ASN C 3 209 ? -95.252  24.788   -62.977 1.00 164.65 ? 209 ASN C CA  1 
ATOM   4703  C C   . ASN C 3 209 ? -95.063  25.049   -61.486 1.00 168.10 ? 209 ASN C C   1 
ATOM   4704  O O   . ASN C 3 209 ? -93.974  24.839   -60.949 1.00 167.14 ? 209 ASN C O   1 
ATOM   4705  C CB  . ASN C 3 209 ? -94.933  23.322   -63.324 1.00 165.75 ? 209 ASN C CB  1 
ATOM   4706  C CG  . ASN C 3 209 ? -94.940  23.016   -64.800 1.00 191.42 ? 209 ASN C CG  1 
ATOM   4707  O OD1 . ASN C 3 209 ? -94.138  23.548   -65.578 1.00 184.61 ? 209 ASN C OD1 1 
ATOM   4708  N ND2 . ASN C 3 209 ? -95.824  22.122   -65.213 1.00 185.24 ? 209 ASN C ND2 1 
ATOM   4709  N N   . VAL C 3 210 ? -96.131  25.524   -60.825 1.00 165.73 ? 210 VAL C N   1 
ATOM   4710  C CA  . VAL C 3 210 ? -96.149  25.832   -59.392 1.00 166.56 ? 210 VAL C CA  1 
ATOM   4711  C C   . VAL C 3 210 ? -97.226  24.964   -58.720 1.00 172.84 ? 210 VAL C C   1 
ATOM   4712  O O   . VAL C 3 210 ? -98.336  24.853   -59.245 1.00 173.49 ? 210 VAL C O   1 
ATOM   4713  C CB  . VAL C 3 210 ? -96.370  27.350   -59.116 1.00 170.60 ? 210 VAL C CB  1 
ATOM   4714  C CG1 . VAL C 3 210 ? -96.222  27.671   -57.631 1.00 171.39 ? 210 VAL C CG1 1 
ATOM   4715  C CG2 . VAL C 3 210 ? -95.423  28.222   -59.940 1.00 169.18 ? 210 VAL C CG2 1 
ATOM   4716  N N   . ASN C 3 211 ? -96.897  24.347   -57.570 1.00 170.32 ? 211 ASN C N   1 
ATOM   4717  C CA  . ASN C 3 211 ? -97.837  23.504   -56.830 1.00 172.13 ? 211 ASN C CA  1 
ATOM   4718  C C   . ASN C 3 211 ? -97.792  23.730   -55.321 1.00 177.96 ? 211 ASN C C   1 
ATOM   4719  O O   . ASN C 3 211 ? -96.712  23.869   -54.745 1.00 177.19 ? 211 ASN C O   1 
ATOM   4720  C CB  . ASN C 3 211 ? -97.658  22.021   -57.178 1.00 173.07 ? 211 ASN C CB  1 
ATOM   4721  C CG  . ASN C 3 211 ? -96.341  21.416   -56.756 1.00 201.95 ? 211 ASN C CG  1 
ATOM   4722  O OD1 . ASN C 3 211 ? -95.337  21.498   -57.467 1.00 197.72 ? 211 ASN C OD1 1 
ATOM   4723  N ND2 . ASN C 3 211 ? -96.328  20.757   -55.605 1.00 195.56 ? 211 ASN C ND2 1 
ATOM   4724  N N   . HIS C 3 212 ? -98.973  23.770   -54.691 1.00 176.74 ? 212 HIS C N   1 
ATOM   4725  C CA  . HIS C 3 212 ? -99.141  23.923   -53.245 1.00 178.78 ? 212 HIS C CA  1 
ATOM   4726  C C   . HIS C 3 212 ? -99.499  22.537   -52.719 1.00 184.50 ? 212 HIS C C   1 
ATOM   4727  O O   . HIS C 3 212 ? -100.528 21.985   -53.110 1.00 185.24 ? 212 HIS C O   1 
ATOM   4728  C CB  . HIS C 3 212 ? -100.259 24.939   -52.945 1.00 181.29 ? 212 HIS C CB  1 
ATOM   4729  C CG  . HIS C 3 212 ? -100.248 25.490   -51.554 1.00 186.96 ? 212 HIS C CG  1 
ATOM   4730  N ND1 . HIS C 3 212 ? -100.751 24.769   -50.491 1.00 191.88 ? 212 HIS C ND1 1 
ATOM   4731  C CD2 . HIS C 3 212 ? -99.857  26.706   -51.110 1.00 188.62 ? 212 HIS C CD2 1 
ATOM   4732  C CE1 . HIS C 3 212 ? -100.620 25.552   -49.432 1.00 193.12 ? 212 HIS C CE1 1 
ATOM   4733  N NE2 . HIS C 3 212 ? -100.082 26.725   -49.756 1.00 191.58 ? 212 HIS C NE2 1 
ATOM   4734  N N   . LYS C 3 213 ? -98.615  21.937   -51.908 1.00 181.44 ? 213 LYS C N   1 
ATOM   4735  C CA  . LYS C 3 213 ? -98.829  20.590   -51.376 1.00 183.27 ? 213 LYS C CA  1 
ATOM   4736  C C   . LYS C 3 213 ? -99.992  20.525   -50.351 1.00 191.25 ? 213 LYS C C   1 
ATOM   4737  O O   . LYS C 3 213 ? -100.890 19.712   -50.585 1.00 192.31 ? 213 LYS C O   1 
ATOM   4738  C CB  . LYS C 3 213 ? -97.527  19.969   -50.828 1.00 185.40 ? 213 LYS C CB  1 
ATOM   4739  C CG  . LYS C 3 213 ? -96.476  19.651   -51.902 1.00 195.23 ? 213 LYS C CG  1 
ATOM   4740  C CD  . LYS C 3 213 ? -96.547  18.204   -52.389 1.00 205.29 ? 213 LYS C CD  1 
ATOM   4741  C CE  . LYS C 3 213 ? -95.488  17.887   -53.416 1.00 210.62 ? 213 LYS C CE  1 
ATOM   4742  N NZ  . LYS C 3 213 ? -95.515  16.452   -53.806 1.00 218.24 ? 213 LYS C NZ  1 
ATOM   4743  N N   . PRO C 3 214 ? -100.063 21.369   -49.273 1.00 190.29 ? 214 PRO C N   1 
ATOM   4744  C CA  . PRO C 3 214 ? -101.199 21.260   -48.334 1.00 194.50 ? 214 PRO C CA  1 
ATOM   4745  C C   . PRO C 3 214 ? -102.584 21.544   -48.933 1.00 199.91 ? 214 PRO C C   1 
ATOM   4746  O O   . PRO C 3 214 ? -103.413 20.635   -48.945 1.00 201.72 ? 214 PRO C O   1 
ATOM   4747  C CB  . PRO C 3 214 ? -100.837 22.242   -47.209 1.00 197.74 ? 214 PRO C CB  1 
ATOM   4748  C CG  . PRO C 3 214 ? -99.373  22.452   -47.333 1.00 198.99 ? 214 PRO C CG  1 
ATOM   4749  C CD  . PRO C 3 214 ? -99.100  22.386   -48.800 1.00 190.75 ? 214 PRO C CD  1 
ATOM   4750  N N   . SER C 3 215 ? -102.833 22.769   -49.452 1.00 194.88 ? 215 SER C N   1 
ATOM   4751  C CA  . SER C 3 215 ? -104.131 23.153   -50.030 1.00 196.19 ? 215 SER C CA  1 
ATOM   4752  C C   . SER C 3 215 ? -104.477 22.435   -51.354 1.00 198.94 ? 215 SER C C   1 
ATOM   4753  O O   . SER C 3 215 ? -105.608 22.560   -51.833 1.00 200.03 ? 215 SER C O   1 
ATOM   4754  C CB  . SER C 3 215 ? -104.227 24.670   -50.192 1.00 199.58 ? 215 SER C CB  1 
ATOM   4755  O OG  . SER C 3 215 ? -103.414 25.157   -51.246 1.00 202.98 ? 215 SER C OG  1 
ATOM   4756  N N   . ASN C 3 216 ? -103.503 21.688   -51.933 1.00 193.06 ? 216 ASN C N   1 
ATOM   4757  C CA  . ASN C 3 216 ? -103.581 20.931   -53.195 1.00 191.10 ? 216 ASN C CA  1 
ATOM   4758  C C   . ASN C 3 216 ? -103.860 21.831   -54.427 1.00 194.48 ? 216 ASN C C   1 
ATOM   4759  O O   . ASN C 3 216 ? -104.109 21.317   -55.522 1.00 193.24 ? 216 ASN C O   1 
ATOM   4760  C CB  . ASN C 3 216 ? -104.559 19.743   -53.108 1.00 192.39 ? 216 ASN C CB  1 
ATOM   4761  C CG  . ASN C 3 216 ? -103.900 18.440   -52.712 1.00 204.89 ? 216 ASN C CG  1 
ATOM   4762  O OD1 . ASN C 3 216 ? -102.901 18.006   -53.301 1.00 192.20 ? 216 ASN C OD1 1 
ATOM   4763  N ND2 . ASN C 3 216 ? -104.468 17.765   -51.726 1.00 198.61 ? 216 ASN C ND2 1 
ATOM   4764  N N   . THR C 3 217 ? -103.746 23.167   -54.253 1.00 191.48 ? 217 THR C N   1 
ATOM   4765  C CA  . THR C 3 217 ? -103.943 24.166   -55.305 1.00 189.85 ? 217 THR C CA  1 
ATOM   4766  C C   . THR C 3 217 ? -102.713 24.158   -56.227 1.00 190.87 ? 217 THR C C   1 
ATOM   4767  O O   . THR C 3 217 ? -101.723 24.840   -55.955 1.00 189.16 ? 217 THR C O   1 
ATOM   4768  C CB  . THR C 3 217 ? -104.262 25.549   -54.686 1.00 197.97 ? 217 THR C CB  1 
ATOM   4769  O OG1 . THR C 3 217 ? -105.250 25.401   -53.664 1.00 201.64 ? 217 THR C OG1 1 
ATOM   4770  C CG2 . THR C 3 217 ? -104.735 26.570   -55.723 1.00 194.95 ? 217 THR C CG2 1 
ATOM   4771  N N   . LYS C 3 218 ? -102.773 23.352   -57.299 1.00 168.59 ? 218 LYS C N   1 
ATOM   4772  C CA  . LYS C 3 218 ? -101.678 23.220   -58.262 1.00 167.42 ? 218 LYS C CA  1 
ATOM   4773  C C   . LYS C 3 218 ? -101.974 24.043   -59.528 1.00 172.71 ? 218 LYS C C   1 
ATOM   4774  O O   . LYS C 3 218 ? -102.635 23.566   -60.458 1.00 171.79 ? 218 LYS C O   1 
ATOM   4775  C CB  . LYS C 3 218 ? -101.372 21.737   -58.562 1.00 168.78 ? 218 LYS C CB  1 
ATOM   4776  C CG  . LYS C 3 218 ? -101.134 20.895   -57.309 1.00 172.79 ? 218 LYS C CG  1 
ATOM   4777  C CD  . LYS C 3 218 ? -100.537 19.536   -57.629 1.00 176.28 ? 218 LYS C CD  1 
ATOM   4778  C CE  . LYS C 3 218 ? -100.274 18.723   -56.384 1.00 180.24 ? 218 LYS C CE  1 
ATOM   4779  N NZ  . LYS C 3 218 ? -99.095  19.223   -55.627 1.00 185.45 ? 218 LYS C NZ  1 
ATOM   4780  N N   . VAL C 3 219 ? -101.509 25.309   -59.524 1.00 170.42 ? 219 VAL C N   1 
ATOM   4781  C CA  . VAL C 3 219 ? -101.716 26.276   -60.607 1.00 170.60 ? 219 VAL C CA  1 
ATOM   4782  C C   . VAL C 3 219 ? -100.467 26.401   -61.494 1.00 173.72 ? 219 VAL C C   1 
ATOM   4783  O O   . VAL C 3 219 ? -99.436  26.936   -61.070 1.00 173.03 ? 219 VAL C O   1 
ATOM   4784  C CB  . VAL C 3 219 ? -102.233 27.658   -60.089 1.00 175.63 ? 219 VAL C CB  1 
ATOM   4785  C CG1 . VAL C 3 219 ? -102.455 28.648   -61.238 1.00 175.11 ? 219 VAL C CG1 1 
ATOM   4786  C CG2 . VAL C 3 219 ? -103.512 27.502   -59.262 1.00 176.83 ? 219 VAL C CG2 1 
ATOM   4787  N N   . ASP C 3 220 ? -100.599 25.915   -62.736 1.00 170.04 ? 220 ASP C N   1 
ATOM   4788  C CA  . ASP C 3 220 ? -99.564  25.957   -63.759 1.00 169.31 ? 220 ASP C CA  1 
ATOM   4789  C C   . ASP C 3 220 ? -99.907  27.071   -64.753 1.00 173.04 ? 220 ASP C C   1 
ATOM   4790  O O   . ASP C 3 220 ? -100.989 27.055   -65.353 1.00 173.02 ? 220 ASP C O   1 
ATOM   4791  C CB  . ASP C 3 220 ? -99.449  24.586   -64.461 1.00 171.04 ? 220 ASP C CB  1 
ATOM   4792  C CG  . ASP C 3 220 ? -98.312  24.432   -65.461 1.00 180.30 ? 220 ASP C CG  1 
ATOM   4793  O OD1 . ASP C 3 220 ? -98.295  23.414   -66.184 1.00 181.09 ? 220 ASP C OD1 1 
ATOM   4794  O OD2 . ASP C 3 220 ? -97.427  25.315   -65.503 1.00 185.19 ? 220 ASP C OD2 1 
ATOM   4795  N N   . LYS C 3 221 ? -98.999  28.058   -64.890 1.00 168.96 ? 221 LYS C N   1 
ATOM   4796  C CA  . LYS C 3 221 ? -99.177  29.180   -65.814 1.00 168.53 ? 221 LYS C CA  1 
ATOM   4797  C C   . LYS C 3 221 ? -97.964  29.414   -66.705 1.00 172.92 ? 221 LYS C C   1 
ATOM   4798  O O   . LYS C 3 221 ? -96.833  29.410   -66.222 1.00 172.08 ? 221 LYS C O   1 
ATOM   4799  C CB  . LYS C 3 221 ? -99.569  30.465   -65.074 1.00 170.41 ? 221 LYS C CB  1 
ATOM   4800  C CG  . LYS C 3 221 ? -101.056 30.536   -64.731 1.00 174.23 ? 221 LYS C CG  1 
ATOM   4801  C CD  . LYS C 3 221 ? -101.462 31.895   -64.166 1.00 176.58 ? 221 LYS C CD  1 
ATOM   4802  C CE  . LYS C 3 221 ? -101.834 32.898   -65.234 1.00 175.07 ? 221 LYS C CE  1 
ATOM   4803  N NZ  . LYS C 3 221 ? -102.201 34.209   -64.646 1.00 176.75 ? 221 LYS C NZ  1 
ATOM   4804  N N   . ARG C 3 222 ? -98.211  29.619   -68.009 1.00 170.63 ? 222 ARG C N   1 
ATOM   4805  C CA  . ARG C 3 222 ? -97.183  29.877   -69.018 1.00 171.36 ? 222 ARG C CA  1 
ATOM   4806  C C   . ARG C 3 222 ? -96.803  31.359   -69.000 1.00 176.96 ? 222 ARG C C   1 
ATOM   4807  O O   . ARG C 3 222 ? -97.682  32.220   -68.887 1.00 176.43 ? 222 ARG C O   1 
ATOM   4808  C CB  . ARG C 3 222 ? -97.696  29.477   -70.416 1.00 172.23 ? 222 ARG C CB  1 
ATOM   4809  C CG  . ARG C 3 222 ? -96.599  29.323   -71.474 1.00 181.30 ? 222 ARG C CG  1 
ATOM   4810  C CD  . ARG C 3 222 ? -97.151  29.294   -72.892 1.00 183.02 ? 222 ARG C CD  1 
ATOM   4811  N NE  . ARG C 3 222 ? -97.376  30.639   -73.428 1.00 179.86 ? 222 ARG C NE  1 
ATOM   4812  C CZ  . ARG C 3 222 ? -96.520  31.291   -74.209 1.00 185.04 ? 222 ARG C CZ  1 
ATOM   4813  N NH1 . ARG C 3 222 ? -95.369  30.731   -74.562 1.00 171.22 ? 222 ARG C NH1 1 
ATOM   4814  N NH2 . ARG C 3 222 ? -96.811  32.508   -74.649 1.00 164.79 ? 222 ARG C NH2 1 
ATOM   4815  N N   . VAL C 3 223 ? -95.494  31.652   -69.116 1.00 175.10 ? 223 VAL C N   1 
ATOM   4816  C CA  . VAL C 3 223 ? -94.967  33.022   -69.140 1.00 175.92 ? 223 VAL C CA  1 
ATOM   4817  C C   . VAL C 3 223 ? -94.990  33.513   -70.596 1.00 182.19 ? 223 VAL C C   1 
ATOM   4818  O O   . VAL C 3 223 ? -94.335  32.915   -71.456 1.00 182.36 ? 223 VAL C O   1 
ATOM   4819  C CB  . VAL C 3 223 ? -93.561  33.140   -68.480 1.00 179.97 ? 223 VAL C CB  1 
ATOM   4820  C CG1 . VAL C 3 223 ? -93.067  34.585   -68.480 1.00 180.21 ? 223 VAL C CG1 1 
ATOM   4821  C CG2 . VAL C 3 223 ? -93.565  32.583   -67.057 1.00 179.20 ? 223 VAL C CG2 1 
ATOM   4822  N N   . GLU C 3 224 ? -95.773  34.581   -70.867 1.00 180.03 ? 224 GLU C N   1 
ATOM   4823  C CA  . GLU C 3 224 ? -95.938  35.158   -72.209 1.00 180.85 ? 224 GLU C CA  1 
ATOM   4824  C C   . GLU C 3 224 ? -95.209  36.518   -72.382 1.00 186.42 ? 224 GLU C C   1 
ATOM   4825  O O   . GLU C 3 224 ? -95.355  37.394   -71.524 1.00 186.41 ? 224 GLU C O   1 
ATOM   4826  C CB  . GLU C 3 224 ? -97.433  35.246   -72.619 1.00 181.63 ? 224 GLU C CB  1 
ATOM   4827  C CG  . GLU C 3 224 ? -98.342  36.078   -71.717 1.00 191.66 ? 224 GLU C CG  1 
ATOM   4828  C CD  . GLU C 3 224 ? -98.955  35.360   -70.529 1.00 210.31 ? 224 GLU C CD  1 
ATOM   4829  O OE1 . GLU C 3 224 ? -100.172 35.071   -70.577 1.00 210.86 ? 224 GLU C OE1 1 
ATOM   4830  O OE2 . GLU C 3 224 ? -98.232  35.120   -69.535 1.00 198.78 ? 224 GLU C OE2 1 
ATOM   4831  N N   . PRO C 3 225 ? -94.420  36.716   -73.473 1.00 183.38 ? 225 PRO C N   1 
ATOM   4832  C CA  . PRO C 3 225 ? -93.724  38.003   -73.649 1.00 185.60 ? 225 PRO C CA  1 
ATOM   4833  C C   . PRO C 3 225 ? -94.608  39.054   -74.311 1.00 183.87 ? 225 PRO C C   1 
ATOM   4834  O O   . PRO C 3 225 ? -95.421  39.685   -73.643 1.00 133.08 ? 225 PRO C O   1 
ATOM   4835  C CB  . PRO C 3 225 ? -92.516  37.644   -74.527 1.00 188.29 ? 225 PRO C CB  1 
ATOM   4836  C CG  . PRO C 3 225 ? -92.727  36.212   -74.969 1.00 191.84 ? 225 PRO C CG  1 
ATOM   4837  C CD  . PRO C 3 225 ? -94.109  35.798   -74.583 1.00 185.78 ? 225 PRO C CD  1 
ATOM   4838  N N   . GLU D 4 1   ? -77.632  35.466   -19.732 1.00 138.32 ? 1   GLU D N   1 
ATOM   4839  C CA  . GLU D 4 1   ? -77.068  34.789   -20.902 1.00 137.70 ? 1   GLU D CA  1 
ATOM   4840  C C   . GLU D 4 1   ? -75.598  35.164   -21.118 1.00 140.58 ? 1   GLU D C   1 
ATOM   4841  O O   . GLU D 4 1   ? -75.245  36.347   -21.094 1.00 140.49 ? 1   GLU D O   1 
ATOM   4842  C CB  . GLU D 4 1   ? -77.885  35.101   -22.177 1.00 138.24 ? 1   GLU D CB  1 
ATOM   4843  C CG  . GLU D 4 1   ? -79.308  34.559   -22.199 1.00 147.82 ? 1   GLU D CG  1 
ATOM   4844  C CD  . GLU D 4 1   ? -80.076  34.804   -23.487 1.00 161.59 ? 1   GLU D CD  1 
ATOM   4845  O OE1 . GLU D 4 1   ? -79.792  34.104   -24.485 1.00 154.71 ? 1   GLU D OE1 1 
ATOM   4846  O OE2 . GLU D 4 1   ? -80.975  35.676   -23.497 1.00 150.59 ? 1   GLU D OE2 1 
ATOM   4847  N N   . ILE D 4 2   ? -74.747  34.151   -21.338 1.00 136.14 ? 2   ILE D N   1 
ATOM   4848  C CA  . ILE D 4 2   ? -73.315  34.325   -21.605 1.00 135.91 ? 2   ILE D CA  1 
ATOM   4849  C C   . ILE D 4 2   ? -73.220  34.579   -23.111 1.00 137.70 ? 2   ILE D C   1 
ATOM   4850  O O   . ILE D 4 2   ? -73.095  33.642   -23.904 1.00 137.26 ? 2   ILE D O   1 
ATOM   4851  C CB  . ILE D 4 2   ? -72.465  33.105   -21.123 1.00 139.71 ? 2   ILE D CB  1 
ATOM   4852  C CG1 . ILE D 4 2   ? -72.738  32.763   -19.642 1.00 141.37 ? 2   ILE D CG1 1 
ATOM   4853  C CG2 . ILE D 4 2   ? -70.965  33.323   -21.361 1.00 140.48 ? 2   ILE D CG2 1 
ATOM   4854  C CD1 . ILE D 4 2   ? -73.913  31.785   -19.394 1.00 150.57 ? 2   ILE D CD1 1 
ATOM   4855  N N   . VAL D 4 3   ? -73.357  35.856   -23.495 1.00 132.34 ? 3   VAL D N   1 
ATOM   4856  C CA  . VAL D 4 3   ? -73.383  36.326   -24.878 1.00 130.68 ? 3   VAL D CA  1 
ATOM   4857  C C   . VAL D 4 3   ? -72.115  35.953   -25.646 1.00 131.85 ? 3   VAL D C   1 
ATOM   4858  O O   . VAL D 4 3   ? -71.022  36.440   -25.337 1.00 132.28 ? 3   VAL D O   1 
ATOM   4859  C CB  . VAL D 4 3   ? -73.709  37.846   -24.969 1.00 135.26 ? 3   VAL D CB  1 
ATOM   4860  C CG1 . VAL D 4 3   ? -73.595  38.366   -26.401 1.00 134.97 ? 3   VAL D CG1 1 
ATOM   4861  C CG2 . VAL D 4 3   ? -75.097  38.144   -24.407 1.00 134.81 ? 3   VAL D CG2 1 
ATOM   4862  N N   . LEU D 4 4   ? -72.283  35.069   -26.646 1.00 125.51 ? 4   LEU D N   1 
ATOM   4863  C CA  . LEU D 4 4   ? -71.216  34.643   -27.547 1.00 124.18 ? 4   LEU D CA  1 
ATOM   4864  C C   . LEU D 4 4   ? -71.304  35.526   -28.780 1.00 128.34 ? 4   LEU D C   1 
ATOM   4865  O O   . LEU D 4 4   ? -72.360  35.591   -29.420 1.00 128.01 ? 4   LEU D O   1 
ATOM   4866  C CB  . LEU D 4 4   ? -71.350  33.157   -27.935 1.00 123.11 ? 4   LEU D CB  1 
ATOM   4867  C CG  . LEU D 4 4   ? -71.055  32.117   -26.858 1.00 127.01 ? 4   LEU D CG  1 
ATOM   4868  C CD1 . LEU D 4 4   ? -71.398  30.746   -27.347 1.00 126.70 ? 4   LEU D CD1 1 
ATOM   4869  C CD2 . LEU D 4 4   ? -69.598  32.127   -26.458 1.00 128.85 ? 4   LEU D CD2 1 
ATOM   4870  N N   . THR D 4 5   ? -70.223  36.254   -29.076 1.00 125.31 ? 5   THR D N   1 
ATOM   4871  C CA  . THR D 4 5   ? -70.174  37.156   -30.220 1.00 125.62 ? 5   THR D CA  1 
ATOM   4872  C C   . THR D 4 5   ? -69.077  36.711   -31.181 1.00 131.62 ? 5   THR D C   1 
ATOM   4873  O O   . THR D 4 5   ? -67.887  36.876   -30.905 1.00 131.16 ? 5   THR D O   1 
ATOM   4874  C CB  . THR D 4 5   ? -70.102  38.621   -29.776 1.00 133.54 ? 5   THR D CB  1 
ATOM   4875  O OG1 . THR D 4 5   ? -69.354  38.715   -28.562 1.00 137.20 ? 5   THR D OG1 1 
ATOM   4876  C CG2 . THR D 4 5   ? -71.483  39.227   -29.564 1.00 130.08 ? 5   THR D CG2 1 
ATOM   4877  N N   . GLN D 4 6   ? -69.502  36.089   -32.297 1.00 130.46 ? 6   GLN D N   1 
ATOM   4878  C CA  . GLN D 4 6   ? -68.625  35.548   -33.334 1.00 131.44 ? 6   GLN D CA  1 
ATOM   4879  C C   . GLN D 4 6   ? -68.012  36.602   -34.236 1.00 139.80 ? 6   GLN D C   1 
ATOM   4880  O O   . GLN D 4 6   ? -68.681  37.564   -34.629 1.00 140.31 ? 6   GLN D O   1 
ATOM   4881  C CB  . GLN D 4 6   ? -69.339  34.473   -34.165 1.00 131.67 ? 6   GLN D CB  1 
ATOM   4882  C CG  . GLN D 4 6   ? -69.186  33.095   -33.559 1.00 138.61 ? 6   GLN D CG  1 
ATOM   4883  C CD  . GLN D 4 6   ? -69.862  32.027   -34.364 1.00 154.75 ? 6   GLN D CD  1 
ATOM   4884  O OE1 . GLN D 4 6   ? -71.007  31.653   -34.108 1.00 147.21 ? 6   GLN D OE1 1 
ATOM   4885  N NE2 . GLN D 4 6   ? -69.147  31.479   -35.324 1.00 151.72 ? 6   GLN D NE2 1 
ATOM   4886  N N   . SER D 4 7   ? -66.730  36.394   -34.576 1.00 138.62 ? 7   SER D N   1 
ATOM   4887  C CA  . SER D 4 7   ? -65.947  37.266   -35.447 1.00 139.93 ? 7   SER D CA  1 
ATOM   4888  C C   . SER D 4 7   ? -65.209  36.421   -36.510 1.00 142.54 ? 7   SER D C   1 
ATOM   4889  O O   . SER D 4 7   ? -64.588  35.412   -36.160 1.00 141.57 ? 7   SER D O   1 
ATOM   4890  C CB  . SER D 4 7   ? -64.967  38.103   -34.627 1.00 146.32 ? 7   SER D CB  1 
ATOM   4891  O OG  . SER D 4 7   ? -64.588  39.282   -35.318 1.00 160.41 ? 7   SER D OG  1 
ATOM   4892  N N   . PRO D 4 8   ? -65.291  36.776   -37.812 1.00 138.43 ? 8   PRO D N   1 
ATOM   4893  C CA  . PRO D 4 8   ? -66.001  37.927   -38.402 1.00 138.82 ? 8   PRO D CA  1 
ATOM   4894  C C   . PRO D 4 8   ? -67.483  37.631   -38.641 1.00 141.46 ? 8   PRO D C   1 
ATOM   4895  O O   . PRO D 4 8   ? -67.998  36.635   -38.143 1.00 140.62 ? 8   PRO D O   1 
ATOM   4896  C CB  . PRO D 4 8   ? -65.235  38.144   -39.712 1.00 141.08 ? 8   PRO D CB  1 
ATOM   4897  C CG  . PRO D 4 8   ? -64.854  36.755   -40.133 1.00 144.26 ? 8   PRO D CG  1 
ATOM   4898  C CD  . PRO D 4 8   ? -64.603  35.983   -38.851 1.00 139.22 ? 8   PRO D CD  1 
ATOM   4899  N N   . GLY D 4 9   ? -68.153  38.500   -39.387 1.00 137.43 ? 9   GLY D N   1 
ATOM   4900  C CA  . GLY D 4 9   ? -69.550  38.308   -39.752 1.00 135.83 ? 9   GLY D CA  1 
ATOM   4901  C C   . GLY D 4 9   ? -69.662  37.275   -40.855 1.00 136.53 ? 9   GLY D C   1 
ATOM   4902  O O   . GLY D 4 9   ? -70.534  36.403   -40.810 1.00 134.86 ? 9   GLY D O   1 
ATOM   4903  N N   . THR D 4 10  ? -68.748  37.370   -41.843 1.00 131.87 ? 10  THR D N   1 
ATOM   4904  C CA  . THR D 4 10  ? -68.630  36.485   -43.000 1.00 130.36 ? 10  THR D CA  1 
ATOM   4905  C C   . THR D 4 10  ? -67.170  36.378   -43.428 1.00 133.46 ? 10  THR D C   1 
ATOM   4906  O O   . THR D 4 10  ? -66.440  37.368   -43.382 1.00 133.66 ? 10  THR D O   1 
ATOM   4907  C CB  . THR D 4 10  ? -69.513  36.962   -44.164 1.00 137.49 ? 10  THR D CB  1 
ATOM   4908  O OG1 . THR D 4 10  ? -69.588  38.391   -44.162 1.00 141.09 ? 10  THR D OG1 1 
ATOM   4909  C CG2 . THR D 4 10  ? -70.905  36.360   -44.130 1.00 133.55 ? 10  THR D CG2 1 
ATOM   4910  N N   . LEU D 4 11  ? -66.750  35.175   -43.838 1.00 129.10 ? 11  LEU D N   1 
ATOM   4911  C CA  . LEU D 4 11  ? -65.392  34.903   -44.306 1.00 129.06 ? 11  LEU D CA  1 
ATOM   4912  C C   . LEU D 4 11  ? -65.394  34.615   -45.810 1.00 134.61 ? 11  LEU D C   1 
ATOM   4913  O O   . LEU D 4 11  ? -66.067  33.679   -46.249 1.00 134.73 ? 11  LEU D O   1 
ATOM   4914  C CB  . LEU D 4 11  ? -64.782  33.712   -43.543 1.00 127.86 ? 11  LEU D CB  1 
ATOM   4915  C CG  . LEU D 4 11  ? -63.830  34.020   -42.391 1.00 132.39 ? 11  LEU D CG  1 
ATOM   4916  C CD1 . LEU D 4 11  ? -63.514  32.769   -41.614 1.00 131.85 ? 11  LEU D CD1 1 
ATOM   4917  C CD2 . LEU D 4 11  ? -62.531  34.629   -42.882 1.00 134.63 ? 11  LEU D CD2 1 
ATOM   4918  N N   . SER D 4 12  ? -64.660  35.420   -46.599 1.00 131.19 ? 12  SER D N   1 
ATOM   4919  C CA  . SER D 4 12  ? -64.550  35.227   -48.047 1.00 130.61 ? 12  SER D CA  1 
ATOM   4920  C C   . SER D 4 12  ? -63.201  34.569   -48.325 1.00 134.12 ? 12  SER D C   1 
ATOM   4921  O O   . SER D 4 12  ? -62.161  35.217   -48.195 1.00 135.35 ? 12  SER D O   1 
ATOM   4922  C CB  . SER D 4 12  ? -64.691  36.553   -48.789 1.00 134.82 ? 12  SER D CB  1 
ATOM   4923  O OG  . SER D 4 12  ? -65.935  37.167   -48.497 1.00 141.57 ? 12  SER D OG  1 
ATOM   4924  N N   . LEU D 4 13  ? -63.215  33.262   -48.634 1.00 128.60 ? 13  LEU D N   1 
ATOM   4925  C CA  . LEU D 4 13  ? -61.998  32.478   -48.856 1.00 127.46 ? 13  LEU D CA  1 
ATOM   4926  C C   . LEU D 4 13  ? -62.046  31.663   -50.141 1.00 130.91 ? 13  LEU D C   1 
ATOM   4927  O O   . LEU D 4 13  ? -63.126  31.252   -50.566 1.00 130.66 ? 13  LEU D O   1 
ATOM   4928  C CB  . LEU D 4 13  ? -61.759  31.536   -47.661 1.00 126.42 ? 13  LEU D CB  1 
ATOM   4929  C CG  . LEU D 4 13  ? -61.355  32.191   -46.342 1.00 131.01 ? 13  LEU D CG  1 
ATOM   4930  C CD1 . LEU D 4 13  ? -62.122  31.608   -45.178 1.00 129.88 ? 13  LEU D CD1 1 
ATOM   4931  C CD2 . LEU D 4 13  ? -59.861  32.087   -46.111 1.00 133.83 ? 13  LEU D CD2 1 
ATOM   4932  N N   . SER D 4 14  ? -60.873  31.437   -50.763 1.00 127.12 ? 14  SER D N   1 
ATOM   4933  C CA  . SER D 4 14  ? -60.740  30.636   -51.982 1.00 126.46 ? 14  SER D CA  1 
ATOM   4934  C C   . SER D 4 14  ? -60.571  29.158   -51.598 1.00 127.88 ? 14  SER D C   1 
ATOM   4935  O O   . SER D 4 14  ? -59.827  28.875   -50.655 1.00 126.83 ? 14  SER D O   1 
ATOM   4936  C CB  . SER D 4 14  ? -59.542  31.100   -52.806 1.00 131.98 ? 14  SER D CB  1 
ATOM   4937  O OG  . SER D 4 14  ? -59.790  32.316   -53.493 1.00 145.81 ? 14  SER D OG  1 
ATOM   4938  N N   . PRO D 4 15  ? -61.247  28.208   -52.292 1.00 124.00 ? 15  PRO D N   1 
ATOM   4939  C CA  . PRO D 4 15  ? -61.107  26.785   -51.926 1.00 123.13 ? 15  PRO D CA  1 
ATOM   4940  C C   . PRO D 4 15  ? -59.669  26.279   -51.992 1.00 126.62 ? 15  PRO D C   1 
ATOM   4941  O O   . PRO D 4 15  ? -59.139  25.999   -53.065 1.00 126.94 ? 15  PRO D O   1 
ATOM   4942  C CB  . PRO D 4 15  ? -62.040  26.059   -52.906 1.00 125.12 ? 15  PRO D CB  1 
ATOM   4943  C CG  . PRO D 4 15  ? -62.955  27.102   -53.424 1.00 130.35 ? 15  PRO D CG  1 
ATOM   4944  C CD  . PRO D 4 15  ? -62.174  28.376   -53.428 1.00 126.30 ? 15  PRO D CD  1 
ATOM   4945  N N   . GLY D 4 16  ? -59.049  26.205   -50.825 1.00 122.61 ? 16  GLY D N   1 
ATOM   4946  C CA  . GLY D 4 16  ? -57.663  25.791   -50.661 1.00 122.35 ? 16  GLY D CA  1 
ATOM   4947  C C   . GLY D 4 16  ? -56.983  26.562   -49.551 1.00 128.31 ? 16  GLY D C   1 
ATOM   4948  O O   . GLY D 4 16  ? -56.003  26.083   -48.975 1.00 127.55 ? 16  GLY D O   1 
ATOM   4949  N N   . GLU D 4 17  ? -57.520  27.761   -49.231 1.00 126.95 ? 17  GLU D N   1 
ATOM   4950  C CA  . GLU D 4 17  ? -57.019  28.646   -48.176 1.00 127.85 ? 17  GLU D CA  1 
ATOM   4951  C C   . GLU D 4 17  ? -57.316  28.093   -46.765 1.00 133.27 ? 17  GLU D C   1 
ATOM   4952  O O   . GLU D 4 17  ? -58.007  27.079   -46.622 1.00 132.80 ? 17  GLU D O   1 
ATOM   4953  C CB  . GLU D 4 17  ? -57.581  30.074   -48.350 1.00 130.17 ? 17  GLU D CB  1 
ATOM   4954  C CG  . GLU D 4 17  ? -56.855  30.901   -49.401 1.00 139.79 ? 17  GLU D CG  1 
ATOM   4955  C CD  . GLU D 4 17  ? -57.295  32.349   -49.511 1.00 156.65 ? 17  GLU D CD  1 
ATOM   4956  O OE1 . GLU D 4 17  ? -56.479  33.242   -49.191 1.00 155.13 ? 17  GLU D OE1 1 
ATOM   4957  O OE2 . GLU D 4 17  ? -58.445  32.594   -49.940 1.00 141.78 ? 17  GLU D OE2 1 
ATOM   4958  N N   . GLY D 4 18  ? -56.767  28.758   -45.749 1.00 131.04 ? 18  GLY D N   1 
ATOM   4959  C CA  . GLY D 4 18  ? -56.932  28.381   -44.351 1.00 131.08 ? 18  GLY D CA  1 
ATOM   4960  C C   . GLY D 4 18  ? -57.866  29.287   -43.577 1.00 136.42 ? 18  GLY D C   1 
ATOM   4961  O O   . GLY D 4 18  ? -57.592  30.481   -43.429 1.00 136.71 ? 18  GLY D O   1 
ATOM   4962  N N   . ALA D 4 19  ? -58.971  28.715   -43.063 1.00 133.46 ? 19  ALA D N   1 
ATOM   4963  C CA  . ALA D 4 19  ? -59.977  29.438   -42.277 1.00 133.70 ? 19  ALA D CA  1 
ATOM   4964  C C   . ALA D 4 19  ? -59.636  29.464   -40.783 1.00 136.44 ? 19  ALA D C   1 
ATOM   4965  O O   . ALA D 4 19  ? -59.162  28.464   -40.242 1.00 135.19 ? 19  ALA D O   1 
ATOM   4966  C CB  . ALA D 4 19  ? -61.346  28.815   -42.484 1.00 134.19 ? 19  ALA D CB  1 
ATOM   4967  N N   . THR D 4 20  ? -59.884  30.614   -40.125 1.00 133.56 ? 20  THR D N   1 
ATOM   4968  C CA  . THR D 4 20  ? -59.653  30.852   -38.695 1.00 133.99 ? 20  THR D CA  1 
ATOM   4969  C C   . THR D 4 20  ? -60.868  31.628   -38.157 1.00 137.79 ? 20  THR D C   1 
ATOM   4970  O O   . THR D 4 20  ? -61.065  32.795   -38.509 1.00 138.04 ? 20  THR D O   1 
ATOM   4971  C CB  . THR D 4 20  ? -58.299  31.563   -38.475 1.00 145.83 ? 20  THR D CB  1 
ATOM   4972  O OG1 . THR D 4 20  ? -57.265  30.829   -39.136 1.00 147.79 ? 20  THR D OG1 1 
ATOM   4973  C CG2 . THR D 4 20  ? -57.945  31.724   -37.000 1.00 144.91 ? 20  THR D CG2 1 
ATOM   4974  N N   . LEU D 4 21  ? -61.695  30.963   -37.337 1.00 133.64 ? 21  LEU D N   1 
ATOM   4975  C CA  . LEU D 4 21  ? -62.928  31.550   -36.818 1.00 133.79 ? 21  LEU D CA  1 
ATOM   4976  C C   . LEU D 4 21  ? -62.903  31.802   -35.317 1.00 140.28 ? 21  LEU D C   1 
ATOM   4977  O O   . LEU D 4 21  ? -62.586  30.895   -34.543 1.00 140.26 ? 21  LEU D O   1 
ATOM   4978  C CB  . LEU D 4 21  ? -64.133  30.686   -37.207 1.00 133.01 ? 21  LEU D CB  1 
ATOM   4979  C CG  . LEU D 4 21  ? -64.366  30.519   -38.698 1.00 137.20 ? 21  LEU D CG  1 
ATOM   4980  C CD1 . LEU D 4 21  ? -63.860  29.179   -39.178 1.00 136.76 ? 21  LEU D CD1 1 
ATOM   4981  C CD2 . LEU D 4 21  ? -65.822  30.654   -39.028 1.00 140.04 ? 21  LEU D CD2 1 
ATOM   4982  N N   . SER D 4 22  ? -63.261  33.038   -34.913 1.00 138.61 ? 22  SER D N   1 
ATOM   4983  C CA  . SER D 4 22  ? -63.274  33.490   -33.518 1.00 139.55 ? 22  SER D CA  1 
ATOM   4984  C C   . SER D 4 22  ? -64.667  33.495   -32.909 1.00 142.29 ? 22  SER D C   1 
ATOM   4985  O O   . SER D 4 22  ? -65.650  33.745   -33.608 1.00 141.85 ? 22  SER D O   1 
ATOM   4986  C CB  . SER D 4 22  ? -62.665  34.885   -33.400 1.00 145.70 ? 22  SER D CB  1 
ATOM   4987  O OG  . SER D 4 22  ? -61.328  34.944   -33.870 1.00 158.12 ? 22  SER D OG  1 
ATOM   4988  N N   . CYS D 4 23  ? -64.735  33.247   -31.595 1.00 137.84 ? 23  CYS D N   1 
ATOM   4989  C CA  . CYS D 4 23  ? -65.960  33.228   -30.806 1.00 137.09 ? 23  CYS D CA  1 
ATOM   4990  C C   . CYS D 4 23  ? -65.611  33.738   -29.403 1.00 142.03 ? 23  CYS D C   1 
ATOM   4991  O O   . CYS D 4 23  ? -65.136  32.968   -28.563 1.00 142.02 ? 23  CYS D O   1 
ATOM   4992  C CB  . CYS D 4 23  ? -66.562  31.821   -30.777 1.00 136.58 ? 23  CYS D CB  1 
ATOM   4993  S SG  . CYS D 4 23  ? -68.019  31.636   -29.706 1.00 140.39 ? 23  CYS D SG  1 
ATOM   4994  N N   . ARG D 4 24  ? -65.799  35.051   -29.170 1.00 139.16 ? 24  ARG D N   1 
ATOM   4995  C CA  . ARG D 4 24  ? -65.501  35.683   -27.881 1.00 139.87 ? 24  ARG D CA  1 
ATOM   4996  C C   . ARG D 4 24  ? -66.723  35.771   -26.965 1.00 144.21 ? 24  ARG D C   1 
ATOM   4997  O O   . ARG D 4 24  ? -67.733  36.392   -27.308 1.00 143.48 ? 24  ARG D O   1 
ATOM   4998  C CB  . ARG D 4 24  ? -64.821  37.044   -28.063 1.00 140.87 ? 24  ARG D CB  1 
ATOM   4999  C CG  . ARG D 4 24  ? -63.317  36.914   -28.228 1.00 151.58 ? 24  ARG D CG  1 
ATOM   5000  C CD  . ARG D 4 24  ? -62.684  38.156   -28.822 1.00 162.98 ? 24  ARG D CD  1 
ATOM   5001  N NE  . ARG D 4 24  ? -61.600  37.812   -29.742 1.00 168.09 ? 24  ARG D NE  1 
ATOM   5002  C CZ  . ARG D 4 24  ? -61.760  37.603   -31.045 1.00 177.59 ? 24  ARG D CZ  1 
ATOM   5003  N NH1 . ARG D 4 24  ? -62.960  37.720   -31.601 1.00 163.54 ? 24  ARG D NH1 1 
ATOM   5004  N NH2 . ARG D 4 24  ? -60.720  37.288   -31.804 1.00 161.64 ? 24  ARG D NH2 1 
ATOM   5005  N N   . ALA D 4 25  ? -66.614  35.123   -25.799 1.00 141.76 ? 25  ALA D N   1 
ATOM   5006  C CA  . ALA D 4 25  ? -67.657  35.038   -24.778 1.00 141.89 ? 25  ALA D CA  1 
ATOM   5007  C C   . ALA D 4 25  ? -67.714  36.267   -23.872 1.00 147.45 ? 25  ALA D C   1 
ATOM   5008  O O   . ALA D 4 25  ? -66.680  36.888   -23.612 1.00 148.24 ? 25  ALA D O   1 
ATOM   5009  C CB  . ALA D 4 25  ? -67.449  33.787   -23.939 1.00 142.77 ? 25  ALA D CB  1 
ATOM   5010  N N   . SER D 4 26  ? -68.932  36.594   -23.377 1.00 133.48 ? 26  SER D N   1 
ATOM   5011  C CA  . SER D 4 26  ? -69.227  37.698   -22.457 1.00 134.06 ? 26  SER D CA  1 
ATOM   5012  C C   . SER D 4 26  ? -68.336  37.581   -21.208 1.00 139.60 ? 26  SER D C   1 
ATOM   5013  O O   . SER D 4 26  ? -67.619  38.523   -20.870 1.00 138.30 ? 26  SER D O   1 
ATOM   5014  C CB  . SER D 4 26  ? -70.710  37.678   -22.079 1.00 137.42 ? 26  SER D CB  1 
ATOM   5015  O OG  . SER D 4 26  ? -71.056  38.633   -21.090 1.00 145.37 ? 26  SER D OG  1 
ATOM   5016  N N   . GLN D 4 27  ? -68.347  36.395   -20.575 1.00 138.50 ? 27  GLN D N   1 
ATOM   5017  C CA  . GLN D 4 27  ? -67.551  36.034   -19.398 1.00 138.71 ? 27  GLN D CA  1 
ATOM   5018  C C   . GLN D 4 27  ? -66.760  34.745   -19.682 1.00 143.61 ? 27  GLN D C   1 
ATOM   5019  O O   . GLN D 4 27  ? -67.028  34.084   -20.688 1.00 143.83 ? 27  GLN D O   1 
ATOM   5020  C CB  . GLN D 4 27  ? -68.432  35.912   -18.130 1.00 140.45 ? 27  GLN D CB  1 
ATOM   5021  C CG  . GLN D 4 27  ? -69.695  35.057   -18.279 1.00 151.08 ? 27  GLN D CG  1 
ATOM   5022  C CD  . GLN D 4 27  ? -70.947  35.814   -17.900 1.00 168.65 ? 27  GLN D CD  1 
ATOM   5023  O OE1 . GLN D 4 27  ? -71.528  35.599   -16.832 1.00 166.15 ? 27  GLN D OE1 1 
ATOM   5024  N NE2 . GLN D 4 27  ? -71.401  36.708   -18.773 1.00 158.10 ? 27  GLN D NE2 1 
ATOM   5025  N N   . SER D 4 28  ? -65.771  34.406   -18.828 1.00 139.65 ? 28  SER D N   1 
ATOM   5026  C CA  . SER D 4 28  ? -64.944  33.211   -19.011 1.00 138.89 ? 28  SER D CA  1 
ATOM   5027  C C   . SER D 4 28  ? -65.746  31.929   -18.783 1.00 143.72 ? 28  SER D C   1 
ATOM   5028  O O   . SER D 4 28  ? -66.432  31.802   -17.764 1.00 143.44 ? 28  SER D O   1 
ATOM   5029  C CB  . SER D 4 28  ? -63.720  33.251   -18.103 1.00 141.01 ? 28  SER D CB  1 
ATOM   5030  O OG  . SER D 4 28  ? -62.818  32.204   -18.424 1.00 149.42 ? 28  SER D OG  1 
ATOM   5031  N N   . VAL D 4 29  ? -65.689  31.004   -19.766 1.00 140.81 ? 29  VAL D N   1 
ATOM   5032  C CA  . VAL D 4 29  ? -66.379  29.703   -19.746 1.00 140.67 ? 29  VAL D CA  1 
ATOM   5033  C C   . VAL D 4 29  ? -65.340  28.565   -19.871 1.00 143.73 ? 29  VAL D C   1 
ATOM   5034  O O   . VAL D 4 29  ? -64.245  28.795   -20.386 1.00 143.63 ? 29  VAL D O   1 
ATOM   5035  C CB  . VAL D 4 29  ? -67.511  29.562   -20.819 1.00 144.91 ? 29  VAL D CB  1 
ATOM   5036  C CG1 . VAL D 4 29  ? -68.642  28.680   -20.307 1.00 145.11 ? 29  VAL D CG1 1 
ATOM   5037  C CG2 . VAL D 4 29  ? -68.068  30.914   -21.266 1.00 145.11 ? 29  VAL D CG2 1 
ATOM   5038  N N   . ASP D 4 30  ? -65.684  27.348   -19.393 1.00 139.31 ? 30  ASP D N   1 
ATOM   5039  C CA  . ASP D 4 30  ? -64.822  26.160   -19.458 1.00 138.11 ? 30  ASP D CA  1 
ATOM   5040  C C   . ASP D 4 30  ? -64.598  25.752   -20.913 1.00 140.24 ? 30  ASP D C   1 
ATOM   5041  O O   . ASP D 4 30  ? -65.520  25.853   -21.726 1.00 139.82 ? 30  ASP D O   1 
ATOM   5042  C CB  . ASP D 4 30  ? -65.436  24.990   -18.651 1.00 140.30 ? 30  ASP D CB  1 
ATOM   5043  C CG  . ASP D 4 30  ? -64.490  23.859   -18.254 1.00 152.46 ? 30  ASP D CG  1 
ATOM   5044  O OD1 . ASP D 4 30  ? -63.299  23.911   -18.637 1.00 153.99 ? 30  ASP D OD1 1 
ATOM   5045  O OD2 . ASP D 4 30  ? -64.941  22.928   -17.547 1.00 156.49 ? 30  ASP D OD2 1 
ATOM   5046  N N   . SER D 4 31  ? -63.362  25.325   -21.238 1.00 135.72 ? 31  SER D N   1 
ATOM   5047  C CA  . SER D 4 31  ? -62.957  24.891   -22.582 1.00 135.47 ? 31  SER D CA  1 
ATOM   5048  C C   . SER D 4 31  ? -63.759  23.674   -23.021 1.00 136.88 ? 31  SER D C   1 
ATOM   5049  O O   . SER D 4 31  ? -64.261  23.645   -24.144 1.00 136.82 ? 31  SER D O   1 
ATOM   5050  C CB  . SER D 4 31  ? -61.465  24.571   -22.618 1.00 140.09 ? 31  SER D CB  1 
ATOM   5051  O OG  . SER D 4 31  ? -61.116  23.546   -21.702 1.00 150.71 ? 31  SER D OG  1 
ATOM   5052  N N   . SER D 4 32  ? -63.920  22.700   -22.103 1.00 130.94 ? 32  SER D N   1 
ATOM   5053  C CA  . SER D 4 32  ? -64.672  21.467   -22.321 1.00 129.66 ? 32  SER D CA  1 
ATOM   5054  C C   . SER D 4 32  ? -66.173  21.689   -22.517 1.00 130.20 ? 32  SER D C   1 
ATOM   5055  O O   . SER D 4 32  ? -66.860  20.777   -22.972 1.00 130.39 ? 32  SER D O   1 
ATOM   5056  C CB  . SER D 4 32  ? -64.410  20.466   -21.203 1.00 133.66 ? 32  SER D CB  1 
ATOM   5057  O OG  . SER D 4 32  ? -64.499  21.043   -19.910 1.00 145.19 ? 32  SER D OG  1 
ATOM   5058  N N   . SER D 4 33  ? -66.680  22.896   -22.209 1.00 123.25 ? 33  SER D N   1 
ATOM   5059  C CA  . SER D 4 33  ? -68.094  23.215   -22.388 1.00 121.74 ? 33  SER D CA  1 
ATOM   5060  C C   . SER D 4 33  ? -68.384  23.786   -23.776 1.00 121.53 ? 33  SER D C   1 
ATOM   5061  O O   . SER D 4 33  ? -69.550  23.896   -24.158 1.00 121.14 ? 33  SER D O   1 
ATOM   5062  C CB  . SER D 4 33  ? -68.585  24.159   -21.292 1.00 125.61 ? 33  SER D CB  1 
ATOM   5063  O OG  . SER D 4 33  ? -68.228  25.511   -21.532 1.00 131.88 ? 33  SER D OG  1 
ATOM   5064  N N   . LEU D 4 34  ? -67.328  24.111   -24.539 1.00 115.36 ? 34  LEU D N   1 
ATOM   5065  C CA  . LEU D 4 34  ? -67.418  24.732   -25.861 1.00 113.88 ? 34  LEU D CA  1 
ATOM   5066  C C   . LEU D 4 34  ? -67.477  23.753   -27.030 1.00 115.72 ? 34  LEU D C   1 
ATOM   5067  O O   . LEU D 4 34  ? -66.774  22.745   -27.028 1.00 114.99 ? 34  LEU D O   1 
ATOM   5068  C CB  . LEU D 4 34  ? -66.261  25.715   -26.046 1.00 114.00 ? 34  LEU D CB  1 
ATOM   5069  C CG  . LEU D 4 34  ? -66.272  26.943   -25.153 1.00 118.71 ? 34  LEU D CG  1 
ATOM   5070  C CD1 . LEU D 4 34  ? -64.862  27.343   -24.764 1.00 119.11 ? 34  LEU D CD1 1 
ATOM   5071  C CD2 . LEU D 4 34  ? -67.028  28.084   -25.799 1.00 120.44 ? 34  LEU D CD2 1 
ATOM   5072  N N   . ALA D 4 35  ? -68.314  24.069   -28.037 1.00 111.37 ? 35  ALA D N   1 
ATOM   5073  C CA  . ALA D 4 35  ? -68.491  23.252   -29.238 1.00 110.65 ? 35  ALA D CA  1 
ATOM   5074  C C   . ALA D 4 35  ? -68.687  24.094   -30.504 1.00 116.23 ? 35  ALA D C   1 
ATOM   5075  O O   . ALA D 4 35  ? -69.250  25.187   -30.434 1.00 115.75 ? 35  ALA D O   1 
ATOM   5076  C CB  . ALA D 4 35  ? -69.660  22.300   -29.060 1.00 110.67 ? 35  ALA D CB  1 
ATOM   5077  N N   . TRP D 4 36  ? -68.224  23.568   -31.658 1.00 114.26 ? 36  TRP D N   1 
ATOM   5078  C CA  . TRP D 4 36  ? -68.334  24.191   -32.980 1.00 114.54 ? 36  TRP D CA  1 
ATOM   5079  C C   . TRP D 4 36  ? -69.255  23.373   -33.898 1.00 117.52 ? 36  TRP D C   1 
ATOM   5080  O O   . TRP D 4 36  ? -69.075  22.159   -34.035 1.00 117.32 ? 36  TRP D O   1 
ATOM   5081  C CB  . TRP D 4 36  ? -66.954  24.325   -33.630 1.00 114.77 ? 36  TRP D CB  1 
ATOM   5082  C CG  . TRP D 4 36  ? -66.133  25.481   -33.144 1.00 117.26 ? 36  TRP D CG  1 
ATOM   5083  C CD1 . TRP D 4 36  ? -64.972  25.412   -32.437 1.00 121.42 ? 36  TRP D CD1 1 
ATOM   5084  C CD2 . TRP D 4 36  ? -66.344  26.874   -33.438 1.00 117.35 ? 36  TRP D CD2 1 
ATOM   5085  N NE1 . TRP D 4 36  ? -64.465  26.678   -32.234 1.00 122.08 ? 36  TRP D NE1 1 
ATOM   5086  C CE2 . TRP D 4 36  ? -65.299  27.597   -32.821 1.00 122.94 ? 36  TRP D CE2 1 
ATOM   5087  C CE3 . TRP D 4 36  ? -67.321  27.584   -34.156 1.00 117.54 ? 36  TRP D CE3 1 
ATOM   5088  C CZ2 . TRP D 4 36  ? -65.192  28.997   -32.916 1.00 122.71 ? 36  TRP D CZ2 1 
ATOM   5089  C CZ3 . TRP D 4 36  ? -67.220  28.966   -34.244 1.00 119.51 ? 36  TRP D CZ3 1 
ATOM   5090  C CH2 . TRP D 4 36  ? -66.170  29.659   -33.624 1.00 121.63 ? 36  TRP D CH2 1 
ATOM   5091  N N   . TYR D 4 37  ? -70.225  24.048   -34.538 1.00 112.88 ? 37  TYR D N   1 
ATOM   5092  C CA  . TYR D 4 37  ? -71.211  23.441   -35.434 1.00 111.27 ? 37  TYR D CA  1 
ATOM   5093  C C   . TYR D 4 37  ? -71.162  24.036   -36.843 1.00 114.81 ? 37  TYR D C   1 
ATOM   5094  O O   . TYR D 4 37  ? -70.843  25.217   -37.008 1.00 115.61 ? 37  TYR D O   1 
ATOM   5095  C CB  . TYR D 4 37  ? -72.629  23.594   -34.868 1.00 112.33 ? 37  TYR D CB  1 
ATOM   5096  C CG  . TYR D 4 37  ? -72.834  22.993   -33.495 1.00 117.50 ? 37  TYR D CG  1 
ATOM   5097  C CD1 . TYR D 4 37  ? -73.439  21.750   -33.340 1.00 119.49 ? 37  TYR D CD1 1 
ATOM   5098  C CD2 . TYR D 4 37  ? -72.492  23.699   -32.343 1.00 120.66 ? 37  TYR D CD2 1 
ATOM   5099  C CE1 . TYR D 4 37  ? -73.668  21.209   -32.073 1.00 122.43 ? 37  TYR D CE1 1 
ATOM   5100  C CE2 . TYR D 4 37  ? -72.689  23.156   -31.073 1.00 122.79 ? 37  TYR D CE2 1 
ATOM   5101  C CZ  . TYR D 4 37  ? -73.279  21.912   -30.942 1.00 131.12 ? 37  TYR D CZ  1 
ATOM   5102  O OH  . TYR D 4 37  ? -73.475  21.388   -29.685 1.00 134.85 ? 37  TYR D OH  1 
ATOM   5103  N N   . GLN D 4 38  ? -71.483  23.212   -37.860 1.00 108.95 ? 38  GLN D N   1 
ATOM   5104  C CA  . GLN D 4 38  ? -71.525  23.629   -39.262 1.00 106.77 ? 38  GLN D CA  1 
ATOM   5105  C C   . GLN D 4 38  ? -72.934  23.381   -39.809 1.00 106.49 ? 38  GLN D C   1 
ATOM   5106  O O   . GLN D 4 38  ? -73.405  22.239   -39.802 1.00 104.72 ? 38  GLN D O   1 
ATOM   5107  C CB  . GLN D 4 38  ? -70.469  22.873   -40.099 1.00 108.41 ? 38  GLN D CB  1 
ATOM   5108  C CG  . GLN D 4 38  ? -70.430  23.266   -41.585 1.00 119.39 ? 38  GLN D CG  1 
ATOM   5109  C CD  . GLN D 4 38  ? -69.899  22.192   -42.518 1.00 135.08 ? 38  GLN D CD  1 
ATOM   5110  O OE1 . GLN D 4 38  ? -70.248  21.007   -42.435 1.00 134.30 ? 38  GLN D OE1 1 
ATOM   5111  N NE2 . GLN D 4 38  ? -69.106  22.598   -43.492 1.00 119.30 ? 38  GLN D NE2 1 
ATOM   5112  N N   . GLN D 4 39  ? -73.607  24.449   -40.269 1.00 101.12 ? 39  GLN D N   1 
ATOM   5113  C CA  . GLN D 4 39  ? -74.938  24.330   -40.858 1.00 98.08  ? 39  GLN D CA  1 
ATOM   5114  C C   . GLN D 4 39  ? -74.891  24.681   -42.337 1.00 102.27 ? 39  GLN D C   1 
ATOM   5115  O O   . GLN D 4 39  ? -74.431  25.765   -42.715 1.00 103.91 ? 39  GLN D O   1 
ATOM   5116  C CB  . GLN D 4 39  ? -75.976  25.187   -40.121 1.00 98.81  ? 39  GLN D CB  1 
ATOM   5117  C CG  . GLN D 4 39  ? -77.404  24.963   -40.622 1.00 99.66  ? 39  GLN D CG  1 
ATOM   5118  C CD  . GLN D 4 39  ? -78.458  25.145   -39.559 1.00 117.82 ? 39  GLN D CD  1 
ATOM   5119  O OE1 . GLN D 4 39  ? -78.237  25.750   -38.504 1.00 116.97 ? 39  GLN D OE1 1 
ATOM   5120  N NE2 . GLN D 4 39  ? -79.643  24.627   -39.819 1.00 107.14 ? 39  GLN D NE2 1 
ATOM   5121  N N   . LYS D 4 40  ? -75.350  23.748   -43.170 1.00 131.33 ? 40  LYS D N   1 
ATOM   5122  C CA  . LYS D 4 40  ? -75.404  23.943   -44.611 1.00 132.89 ? 40  LYS D CA  1 
ATOM   5123  C C   . LYS D 4 40  ? -76.820  24.429   -44.963 1.00 139.25 ? 40  LYS D C   1 
ATOM   5124  O O   . LYS D 4 40  ? -77.741  24.139   -44.193 1.00 138.46 ? 40  LYS D O   1 
ATOM   5125  C CB  . LYS D 4 40  ? -75.048  22.635   -45.339 1.00 135.65 ? 40  LYS D CB  1 
ATOM   5126  C CG  . LYS D 4 40  ? -73.542  22.389   -45.468 1.00 141.24 ? 40  LYS D CG  1 
ATOM   5127  C CD  . LYS D 4 40  ? -73.227  20.904   -45.613 1.00 146.55 ? 40  LYS D CD  1 
ATOM   5128  C CE  . LYS D 4 40  ? -71.761  20.628   -45.838 1.00 148.32 ? 40  LYS D CE  1 
ATOM   5129  N NZ  . LYS D 4 40  ? -71.385  20.771   -47.267 1.00 156.48 ? 40  LYS D NZ  1 
ATOM   5130  N N   . PRO D 4 41  ? -77.032  25.192   -46.072 1.00 138.65 ? 41  PRO D N   1 
ATOM   5131  C CA  . PRO D 4 41  ? -78.394  25.670   -46.383 1.00 140.64 ? 41  PRO D CA  1 
ATOM   5132  C C   . PRO D 4 41  ? -79.398  24.540   -46.596 1.00 146.35 ? 41  PRO D C   1 
ATOM   5133  O O   . PRO D 4 41  ? -79.151  23.627   -47.389 1.00 146.67 ? 41  PRO D O   1 
ATOM   5134  C CB  . PRO D 4 41  ? -78.206  26.519   -47.648 1.00 144.25 ? 41  PRO D CB  1 
ATOM   5135  C CG  . PRO D 4 41  ? -76.755  26.836   -47.698 1.00 147.27 ? 41  PRO D CG  1 
ATOM   5136  C CD  . PRO D 4 41  ? -76.061  25.661   -47.083 1.00 141.09 ? 41  PRO D CD  1 
ATOM   5137  N N   . GLY D 4 42  ? -80.501  24.606   -45.849 1.00 143.66 ? 42  GLY D N   1 
ATOM   5138  C CA  . GLY D 4 42  ? -81.576  23.618   -45.883 1.00 144.88 ? 42  GLY D CA  1 
ATOM   5139  C C   . GLY D 4 42  ? -81.165  22.276   -45.318 1.00 146.72 ? 42  GLY D C   1 
ATOM   5140  O O   . GLY D 4 42  ? -81.572  21.232   -45.832 1.00 147.02 ? 42  GLY D O   1 
ATOM   5141  N N   . GLN D 4 43  ? -80.334  22.305   -44.261 1.00 141.21 ? 43  GLN D N   1 
ATOM   5142  C CA  . GLN D 4 43  ? -79.801  21.129   -43.571 1.00 139.38 ? 43  GLN D CA  1 
ATOM   5143  C C   . GLN D 4 43  ? -79.723  21.367   -42.068 1.00 141.16 ? 43  GLN D C   1 
ATOM   5144  O O   . GLN D 4 43  ? -79.496  22.498   -41.635 1.00 140.95 ? 43  GLN D O   1 
ATOM   5145  C CB  . GLN D 4 43  ? -78.396  20.793   -44.096 1.00 139.95 ? 43  GLN D CB  1 
ATOM   5146  C CG  . GLN D 4 43  ? -78.392  19.982   -45.388 1.00 167.73 ? 43  GLN D CG  1 
ATOM   5147  C CD  . GLN D 4 43  ? -76.999  19.589   -45.823 1.00 192.86 ? 43  GLN D CD  1 
ATOM   5148  O OE1 . GLN D 4 43  ? -76.180  19.100   -45.033 1.00 189.08 ? 43  GLN D OE1 1 
ATOM   5149  N NE2 . GLN D 4 43  ? -76.707  19.764   -47.107 1.00 185.86 ? 43  GLN D NE2 1 
ATOM   5150  N N   . ALA D 4 44  ? -79.881  20.293   -41.275 1.00 135.47 ? 44  ALA D N   1 
ATOM   5151  C CA  . ALA D 4 44  ? -79.771  20.328   -39.814 1.00 132.71 ? 44  ALA D CA  1 
ATOM   5152  C C   . ALA D 4 44  ? -78.282  20.526   -39.422 1.00 132.26 ? 44  ALA D C   1 
ATOM   5153  O O   . ALA D 4 44  ? -77.409  20.124   -40.200 1.00 132.21 ? 44  ALA D O   1 
ATOM   5154  C CB  . ALA D 4 44  ? -80.299  19.029   -39.228 1.00 133.07 ? 44  ALA D CB  1 
ATOM   5155  N N   . PRO D 4 45  ? -77.952  21.135   -38.254 1.00 124.87 ? 45  PRO D N   1 
ATOM   5156  C CA  . PRO D 4 45  ? -76.535  21.341   -37.909 1.00 122.47 ? 45  PRO D CA  1 
ATOM   5157  C C   . PRO D 4 45  ? -75.717  20.063   -37.715 1.00 124.72 ? 45  PRO D C   1 
ATOM   5158  O O   . PRO D 4 45  ? -76.269  18.979   -37.503 1.00 123.52 ? 45  PRO D O   1 
ATOM   5159  C CB  . PRO D 4 45  ? -76.595  22.185   -36.631 1.00 123.38 ? 45  PRO D CB  1 
ATOM   5160  C CG  . PRO D 4 45  ? -77.961  22.760   -36.604 1.00 129.16 ? 45  PRO D CG  1 
ATOM   5161  C CD  . PRO D 4 45  ? -78.827  21.714   -37.219 1.00 126.06 ? 45  PRO D CD  1 
ATOM   5162  N N   . ARG D 4 46  ? -74.387  20.205   -37.816 1.00 121.04 ? 46  ARG D N   1 
ATOM   5163  C CA  . ARG D 4 46  ? -73.415  19.119   -37.681 1.00 119.94 ? 46  ARG D CA  1 
ATOM   5164  C C   . ARG D 4 46  ? -72.419  19.496   -36.600 1.00 121.04 ? 46  ARG D C   1 
ATOM   5165  O O   . ARG D 4 46  ? -72.021  20.658   -36.521 1.00 119.92 ? 46  ARG D O   1 
ATOM   5166  C CB  . ARG D 4 46  ? -72.672  18.920   -39.018 1.00 121.56 ? 46  ARG D CB  1 
ATOM   5167  C CG  . ARG D 4 46  ? -72.077  17.527   -39.235 1.00 133.19 ? 46  ARG D CG  1 
ATOM   5168  C CD  . ARG D 4 46  ? -72.597  16.863   -40.508 1.00 147.56 ? 46  ARG D CD  1 
ATOM   5169  N NE  . ARG D 4 46  ? -72.278  17.623   -41.724 1.00 162.56 ? 46  ARG D NE  1 
ATOM   5170  C CZ  . ARG D 4 46  ? -71.200  17.426   -42.481 1.00 182.45 ? 46  ARG D CZ  1 
ATOM   5171  N NH1 . ARG D 4 46  ? -70.321  16.485   -42.165 1.00 175.52 ? 46  ARG D NH1 1 
ATOM   5172  N NH2 . ARG D 4 46  ? -70.995  18.169   -43.560 1.00 167.81 ? 46  ARG D NH2 1 
ATOM   5173  N N   . LEU D 4 47  ? -72.018  18.523   -35.770 1.00 116.06 ? 47  LEU D N   1 
ATOM   5174  C CA  . LEU D 4 47  ? -71.026  18.749   -34.723 1.00 114.67 ? 47  LEU D CA  1 
ATOM   5175  C C   . LEU D 4 47  ? -69.642  18.513   -35.334 1.00 119.63 ? 47  LEU D C   1 
ATOM   5176  O O   . LEU D 4 47  ? -69.422  17.478   -35.972 1.00 119.34 ? 47  LEU D O   1 
ATOM   5177  C CB  . LEU D 4 47  ? -71.278  17.821   -33.517 1.00 113.72 ? 47  LEU D CB  1 
ATOM   5178  C CG  . LEU D 4 47  ? -70.358  17.978   -32.303 1.00 117.25 ? 47  LEU D CG  1 
ATOM   5179  C CD1 . LEU D 4 47  ? -70.838  19.070   -31.373 1.00 116.97 ? 47  LEU D CD1 1 
ATOM   5180  C CD2 . LEU D 4 47  ? -70.274  16.692   -31.534 1.00 119.69 ? 47  LEU D CD2 1 
ATOM   5181  N N   . LEU D 4 48  ? -68.735  19.499   -35.186 1.00 117.18 ? 48  LEU D N   1 
ATOM   5182  C CA  . LEU D 4 48  ? -67.364  19.438   -35.714 1.00 117.58 ? 48  LEU D CA  1 
ATOM   5183  C C   . LEU D 4 48  ? -66.389  19.203   -34.573 1.00 120.19 ? 48  LEU D C   1 
ATOM   5184  O O   . LEU D 4 48  ? -65.612  18.245   -34.592 1.00 121.13 ? 48  LEU D O   1 
ATOM   5185  C CB  . LEU D 4 48  ? -66.963  20.748   -36.414 1.00 118.12 ? 48  LEU D CB  1 
ATOM   5186  C CG  . LEU D 4 48  ? -67.926  21.366   -37.387 1.00 123.59 ? 48  LEU D CG  1 
ATOM   5187  C CD1 . LEU D 4 48  ? -67.848  22.855   -37.300 1.00 123.57 ? 48  LEU D CD1 1 
ATOM   5188  C CD2 . LEU D 4 48  ? -67.633  20.905   -38.789 1.00 128.05 ? 48  LEU D CD2 1 
ATOM   5189  N N   . ILE D 4 49  ? -66.390  20.132   -33.612 1.00 113.58 ? 49  ILE D N   1 
ATOM   5190  C CA  . ILE D 4 49  ? -65.537  20.074   -32.443 1.00 112.41 ? 49  ILE D CA  1 
ATOM   5191  C C   . ILE D 4 49  ? -66.453  20.125   -31.229 1.00 115.39 ? 49  ILE D C   1 
ATOM   5192  O O   . ILE D 4 49  ? -67.375  20.937   -31.181 1.00 115.14 ? 49  ILE D O   1 
ATOM   5193  C CB  . ILE D 4 49  ? -64.466  21.212   -32.452 1.00 115.40 ? 49  ILE D CB  1 
ATOM   5194  C CG1 . ILE D 4 49  ? -63.606  21.216   -33.741 1.00 116.00 ? 49  ILE D CG1 1 
ATOM   5195  C CG2 . ILE D 4 49  ? -63.583  21.193   -31.201 1.00 116.49 ? 49  ILE D CG2 1 
ATOM   5196  C CD1 . ILE D 4 49  ? -62.673  19.953   -34.026 1.00 123.83 ? 49  ILE D CD1 1 
ATOM   5197  N N   . PHE D 4 50  ? -66.230  19.209   -30.290 1.00 110.85 ? 50  PHE D N   1 
ATOM   5198  C CA  . PHE D 4 50  ? -66.929  19.121   -29.017 1.00 110.07 ? 50  PHE D CA  1 
ATOM   5199  C C   . PHE D 4 50  ? -65.831  19.135   -27.954 1.00 115.87 ? 50  PHE D C   1 
ATOM   5200  O O   . PHE D 4 50  ? -64.686  18.797   -28.270 1.00 115.93 ? 50  PHE D O   1 
ATOM   5201  C CB  . PHE D 4 50  ? -67.783  17.846   -28.945 1.00 110.98 ? 50  PHE D CB  1 
ATOM   5202  C CG  . PHE D 4 50  ? -67.013  16.554   -28.840 1.00 112.50 ? 50  PHE D CG  1 
ATOM   5203  C CD1 . PHE D 4 50  ? -66.481  15.948   -29.969 1.00 115.49 ? 50  PHE D CD1 1 
ATOM   5204  C CD2 . PHE D 4 50  ? -66.845  15.926   -27.615 1.00 115.52 ? 50  PHE D CD2 1 
ATOM   5205  C CE1 . PHE D 4 50  ? -65.765  14.755   -29.870 1.00 116.80 ? 50  PHE D CE1 1 
ATOM   5206  C CE2 . PHE D 4 50  ? -66.141  14.728   -27.519 1.00 118.68 ? 50  PHE D CE2 1 
ATOM   5207  C CZ  . PHE D 4 50  ? -65.601  14.152   -28.647 1.00 116.55 ? 50  PHE D CZ  1 
ATOM   5208  N N   . ALA D 4 51  ? -66.156  19.545   -26.713 1.00 113.23 ? 51  ALA D N   1 
ATOM   5209  C CA  . ALA D 4 51  ? -65.207  19.661   -25.592 1.00 114.17 ? 51  ALA D CA  1 
ATOM   5210  C C   . ALA D 4 51  ? -64.064  20.654   -25.837 1.00 119.71 ? 51  ALA D C   1 
ATOM   5211  O O   . ALA D 4 51  ? -63.034  20.583   -25.166 1.00 120.58 ? 51  ALA D O   1 
ATOM   5212  C CB  . ALA D 4 51  ? -64.659  18.299   -25.190 1.00 115.29 ? 51  ALA D CB  1 
ATOM   5213  N N   . GLY D 4 52  ? -64.263  21.554   -26.801 1.00 116.66 ? 52  GLY D N   1 
ATOM   5214  C CA  . GLY D 4 52  ? -63.335  22.622   -27.160 1.00 117.34 ? 52  GLY D CA  1 
ATOM   5215  C C   . GLY D 4 52  ? -62.128  22.282   -28.012 1.00 123.07 ? 52  GLY D C   1 
ATOM   5216  O O   . GLY D 4 52  ? -61.596  23.165   -28.689 1.00 122.91 ? 52  GLY D O   1 
ATOM   5217  N N   . SER D 4 53  ? -61.660  21.028   -27.969 1.00 121.12 ? 53  SER D N   1 
ATOM   5218  C CA  . SER D 4 53  ? -60.482  20.612   -28.728 1.00 122.07 ? 53  SER D CA  1 
ATOM   5219  C C   . SER D 4 53  ? -60.723  19.327   -29.502 1.00 126.94 ? 53  SER D C   1 
ATOM   5220  O O   . SER D 4 53  ? -60.245  19.192   -30.630 1.00 126.37 ? 53  SER D O   1 
ATOM   5221  C CB  . SER D 4 53  ? -59.287  20.439   -27.794 1.00 127.46 ? 53  SER D CB  1 
ATOM   5222  O OG  . SER D 4 53  ? -59.048  21.600   -27.013 1.00 137.62 ? 53  SER D OG  1 
ATOM   5223  N N   . SER D 4 54  ? -61.477  18.393   -28.889 1.00 124.46 ? 54  SER D N   1 
ATOM   5224  C CA  . SER D 4 54  ? -61.788  17.056   -29.401 1.00 124.19 ? 54  SER D CA  1 
ATOM   5225  C C   . SER D 4 54  ? -62.554  17.079   -30.729 1.00 127.86 ? 54  SER D C   1 
ATOM   5226  O O   . SER D 4 54  ? -63.565  17.776   -30.846 1.00 127.45 ? 54  SER D O   1 
ATOM   5227  C CB  . SER D 4 54  ? -62.542  16.244   -28.349 1.00 126.73 ? 54  SER D CB  1 
ATOM   5228  O OG  . SER D 4 54  ? -61.940  16.364   -27.071 1.00 134.20 ? 54  SER D OG  1 
ATOM   5229  N N   . ARG D 4 55  ? -62.054  16.336   -31.730 1.00 124.18 ? 55  ARG D N   1 
ATOM   5230  C CA  . ARG D 4 55  ? -62.673  16.240   -33.055 1.00 123.66 ? 55  ARG D CA  1 
ATOM   5231  C C   . ARG D 4 55  ? -63.846  15.256   -33.013 1.00 127.34 ? 55  ARG D C   1 
ATOM   5232  O O   . ARG D 4 55  ? -63.717  14.168   -32.442 1.00 127.53 ? 55  ARG D O   1 
ATOM   5233  C CB  . ARG D 4 55  ? -61.637  15.808   -34.105 1.00 125.00 ? 55  ARG D CB  1 
ATOM   5234  C CG  . ARG D 4 55  ? -61.898  16.386   -35.490 1.00 131.85 ? 55  ARG D CG  1 
ATOM   5235  C CD  . ARG D 4 55  ? -60.980  15.789   -36.535 1.00 137.03 ? 55  ARG D CD  1 
ATOM   5236  N NE  . ARG D 4 55  ? -59.608  16.282   -36.424 1.00 146.96 ? 55  ARG D NE  1 
ATOM   5237  C CZ  . ARG D 4 55  ? -58.539  15.503   -36.283 1.00 164.00 ? 55  ARG D CZ  1 
ATOM   5238  N NH1 . ARG D 4 55  ? -58.670  14.183   -36.244 1.00 153.49 ? 55  ARG D NH1 1 
ATOM   5239  N NH2 . ARG D 4 55  ? -57.330  16.039   -36.190 1.00 151.92 ? 55  ARG D NH2 1 
ATOM   5240  N N   . ALA D 4 56  ? -64.985  15.635   -33.616 1.00 113.56 ? 56  ALA D N   1 
ATOM   5241  C CA  . ALA D 4 56  ? -66.198  14.818   -33.608 1.00 114.65 ? 56  ALA D CA  1 
ATOM   5242  C C   . ALA D 4 56  ? -66.099  13.505   -34.386 1.00 122.59 ? 56  ALA D C   1 
ATOM   5243  O O   . ALA D 4 56  ? -65.130  13.265   -35.111 1.00 122.47 ? 56  ALA D O   1 
ATOM   5244  C CB  . ALA D 4 56  ? -67.391  15.628   -34.083 1.00 113.33 ? 56  ALA D CB  1 
ATOM   5245  N N   . THR D 4 57  ? -67.120  12.649   -34.196 1.00 123.21 ? 57  THR D N   1 
ATOM   5246  C CA  . THR D 4 57  ? -67.286  11.323   -34.790 1.00 127.70 ? 57  THR D CA  1 
ATOM   5247  C C   . THR D 4 57  ? -67.455  11.423   -36.323 1.00 133.29 ? 57  THR D C   1 
ATOM   5248  O O   . THR D 4 57  ? -68.544  11.726   -36.814 1.00 132.93 ? 57  THR D O   1 
ATOM   5249  C CB  . THR D 4 57  ? -68.447  10.576   -34.074 1.00 137.80 ? 57  THR D CB  1 
ATOM   5250  O OG1 . THR D 4 57  ? -68.458  10.876   -32.668 1.00 135.06 ? 57  THR D OG1 1 
ATOM   5251  C CG2 . THR D 4 57  ? -68.400  9.072    -34.290 1.00 141.66 ? 57  THR D CG2 1 
ATOM   5252  N N   . GLY D 4 58  ? -66.365  11.191   -37.050 1.00 131.31 ? 58  GLY D N   1 
ATOM   5253  C CA  . GLY D 4 58  ? -66.347  11.234   -38.508 1.00 131.99 ? 58  GLY D CA  1 
ATOM   5254  C C   . GLY D 4 58  ? -66.196  12.625   -39.088 1.00 131.58 ? 58  GLY D C   1 
ATOM   5255  O O   . GLY D 4 58  ? -67.041  13.064   -39.871 1.00 130.39 ? 58  GLY D O   1 
ATOM   5256  N N   . ILE D 4 59  ? -65.109  13.321   -38.704 1.00 126.16 ? 59  ILE D N   1 
ATOM   5257  C CA  . ILE D 4 59  ? -64.748  14.675   -39.154 1.00 123.33 ? 59  ILE D CA  1 
ATOM   5258  C C   . ILE D 4 59  ? -63.265  14.659   -39.622 1.00 129.67 ? 59  ILE D C   1 
ATOM   5259  O O   . ILE D 4 59  ? -62.427  14.094   -38.918 1.00 130.91 ? 59  ILE D O   1 
ATOM   5260  C CB  . ILE D 4 59  ? -65.032  15.732   -38.031 1.00 122.56 ? 59  ILE D CB  1 
ATOM   5261  C CG1 . ILE D 4 59  ? -66.554  15.840   -37.679 1.00 121.24 ? 59  ILE D CG1 1 
ATOM   5262  C CG2 . ILE D 4 59  ? -64.418  17.113   -38.319 1.00 120.74 ? 59  ILE D CG2 1 
ATOM   5263  C CD1 . ILE D 4 59  ? -67.561  16.302   -38.789 1.00 124.41 ? 59  ILE D CD1 1 
ATOM   5264  N N   . PRO D 4 60  ? -62.921  15.243   -40.795 1.00 126.96 ? 60  PRO D N   1 
ATOM   5265  C CA  . PRO D 4 60  ? -61.518  15.203   -41.263 1.00 129.00 ? 60  PRO D CA  1 
ATOM   5266  C C   . PRO D 4 60  ? -60.504  15.969   -40.412 1.00 132.23 ? 60  PRO D C   1 
ATOM   5267  O O   . PRO D 4 60  ? -60.881  16.864   -39.655 1.00 129.95 ? 60  PRO D O   1 
ATOM   5268  C CB  . PRO D 4 60  ? -61.599  15.771   -42.683 1.00 131.60 ? 60  PRO D CB  1 
ATOM   5269  C CG  . PRO D 4 60  ? -62.814  16.603   -42.682 1.00 133.33 ? 60  PRO D CG  1 
ATOM   5270  C CD  . PRO D 4 60  ? -63.789  15.929   -41.772 1.00 127.89 ? 60  PRO D CD  1 
ATOM   5271  N N   . ASP D 4 61  ? -59.205  15.616   -40.574 1.00 130.55 ? 61  ASP D N   1 
ATOM   5272  C CA  . ASP D 4 61  ? -58.027  16.162   -39.879 1.00 129.56 ? 61  ASP D CA  1 
ATOM   5273  C C   . ASP D 4 61  ? -57.854  17.683   -39.953 1.00 130.15 ? 61  ASP D C   1 
ATOM   5274  O O   . ASP D 4 61  ? -57.247  18.265   -39.045 1.00 127.85 ? 61  ASP D O   1 
ATOM   5275  C CB  . ASP D 4 61  ? -56.751  15.474   -40.390 1.00 135.19 ? 61  ASP D CB  1 
ATOM   5276  C CG  . ASP D 4 61  ? -56.592  14.035   -39.942 1.00 151.02 ? 61  ASP D CG  1 
ATOM   5277  O OD1 . ASP D 4 61  ? -57.587  13.275   -40.007 1.00 152.50 ? 61  ASP D OD1 1 
ATOM   5278  O OD2 . ASP D 4 61  ? -55.465  13.657   -39.560 1.00 160.94 ? 61  ASP D OD2 1 
ATOM   5279  N N   . ARG D 4 62  ? -58.357  18.315   -41.036 1.00 126.57 ? 62  ARG D N   1 
ATOM   5280  C CA  . ARG D 4 62  ? -58.274  19.763   -41.259 1.00 124.61 ? 62  ARG D CA  1 
ATOM   5281  C C   . ARG D 4 62  ? -58.945  20.571   -40.138 1.00 124.68 ? 62  ARG D C   1 
ATOM   5282  O O   . ARG D 4 62  ? -58.350  21.524   -39.631 1.00 123.23 ? 62  ARG D O   1 
ATOM   5283  C CB  . ARG D 4 62  ? -58.797  20.158   -42.660 1.00 123.30 ? 62  ARG D CB  1 
ATOM   5284  C CG  . ARG D 4 62  ? -60.221  19.722   -42.973 1.00 126.51 ? 62  ARG D CG  1 
ATOM   5285  C CD  . ARG D 4 62  ? -60.531  19.924   -44.429 1.00 133.60 ? 62  ARG D CD  1 
ATOM   5286  N NE  . ARG D 4 62  ? -60.719  18.647   -45.113 1.00 146.14 ? 62  ARG D NE  1 
ATOM   5287  C CZ  . ARG D 4 62  ? -61.887  18.210   -45.570 1.00 159.97 ? 62  ARG D CZ  1 
ATOM   5288  N NH1 . ARG D 4 62  ? -62.979  18.953   -45.441 1.00 144.04 ? 62  ARG D NH1 1 
ATOM   5289  N NH2 . ARG D 4 62  ? -61.971  17.029   -46.169 1.00 149.44 ? 62  ARG D NH2 1 
ATOM   5290  N N   . PHE D 4 63  ? -60.146  20.141   -39.716 1.00 119.83 ? 63  PHE D N   1 
ATOM   5291  C CA  . PHE D 4 63  ? -60.921  20.794   -38.665 1.00 117.66 ? 63  PHE D CA  1 
ATOM   5292  C C   . PHE D 4 63  ? -60.286  20.583   -37.287 1.00 124.35 ? 63  PHE D C   1 
ATOM   5293  O O   . PHE D 4 63  ? -60.134  19.438   -36.850 1.00 125.53 ? 63  PHE D O   1 
ATOM   5294  C CB  . PHE D 4 63  ? -62.376  20.292   -38.671 1.00 117.89 ? 63  PHE D CB  1 
ATOM   5295  C CG  . PHE D 4 63  ? -63.187  20.656   -39.891 1.00 119.02 ? 63  PHE D CG  1 
ATOM   5296  C CD1 . PHE D 4 63  ? -63.902  21.848   -39.942 1.00 120.17 ? 63  PHE D CD1 1 
ATOM   5297  C CD2 . PHE D 4 63  ? -63.278  19.788   -40.968 1.00 122.80 ? 63  PHE D CD2 1 
ATOM   5298  C CE1 . PHE D 4 63  ? -64.666  22.176   -41.065 1.00 121.28 ? 63  PHE D CE1 1 
ATOM   5299  C CE2 . PHE D 4 63  ? -64.047  20.115   -42.088 1.00 126.02 ? 63  PHE D CE2 1 
ATOM   5300  C CZ  . PHE D 4 63  ? -64.736  21.305   -42.128 1.00 122.41 ? 63  PHE D CZ  1 
ATOM   5301  N N   . SER D 4 64  ? -59.920  21.693   -36.608 1.00 121.43 ? 64  SER D N   1 
ATOM   5302  C CA  . SER D 4 64  ? -59.301  21.671   -35.280 1.00 121.89 ? 64  SER D CA  1 
ATOM   5303  C C   . SER D 4 64  ? -59.863  22.737   -34.347 1.00 124.76 ? 64  SER D C   1 
ATOM   5304  O O   . SER D 4 64  ? -60.153  23.857   -34.771 1.00 123.37 ? 64  SER D O   1 
ATOM   5305  C CB  . SER D 4 64  ? -57.786  21.811   -35.389 1.00 128.01 ? 64  SER D CB  1 
ATOM   5306  O OG  . SER D 4 64  ? -57.402  23.028   -36.010 1.00 137.47 ? 64  SER D OG  1 
ATOM   5307  N N   . GLY D 4 65  ? -60.038  22.353   -33.091 1.00 122.50 ? 65  GLY D N   1 
ATOM   5308  C CA  . GLY D 4 65  ? -60.546  23.235   -32.052 1.00 122.73 ? 65  GLY D CA  1 
ATOM   5309  C C   . GLY D 4 65  ? -59.439  23.698   -31.132 1.00 130.81 ? 65  GLY D C   1 
ATOM   5310  O O   . GLY D 4 65  ? -58.706  22.875   -30.577 1.00 132.34 ? 65  GLY D O   1 
ATOM   5311  N N   . LYS D 4 66  ? -59.303  25.020   -30.978 1.00 128.91 ? 66  LYS D N   1 
ATOM   5312  C CA  . LYS D 4 66  ? -58.304  25.651   -30.116 1.00 131.44 ? 66  LYS D CA  1 
ATOM   5313  C C   . LYS D 4 66  ? -59.036  26.543   -29.109 1.00 137.58 ? 66  LYS D C   1 
ATOM   5314  O O   . LYS D 4 66  ? -59.812  27.408   -29.517 1.00 137.22 ? 66  LYS D O   1 
ATOM   5315  C CB  . LYS D 4 66  ? -57.314  26.467   -30.973 1.00 135.50 ? 66  LYS D CB  1 
ATOM   5316  C CG  . LYS D 4 66  ? -56.156  27.120   -30.205 1.00 149.33 ? 66  LYS D CG  1 
ATOM   5317  C CD  . LYS D 4 66  ? -55.402  28.121   -31.092 1.00 153.37 ? 66  LYS D CD  1 
ATOM   5318  C CE  . LYS D 4 66  ? -54.332  28.892   -30.359 1.00 152.54 ? 66  LYS D CE  1 
ATOM   5319  N NZ  . LYS D 4 66  ? -53.775  29.986   -31.199 1.00 153.37 ? 66  LYS D NZ  1 
ATOM   5320  N N   . THR D 4 67  ? -58.821  26.316   -27.803 1.00 136.34 ? 67  THR D N   1 
ATOM   5321  C CA  . THR D 4 67  ? -59.469  27.124   -26.768 1.00 137.77 ? 67  THR D CA  1 
ATOM   5322  C C   . THR D 4 67  ? -58.497  28.216   -26.302 1.00 145.84 ? 67  THR D C   1 
ATOM   5323  O O   . THR D 4 67  ? -57.838  28.091   -25.266 1.00 147.68 ? 67  THR D O   1 
ATOM   5324  C CB  . THR D 4 67  ? -60.085  26.254   -25.663 1.00 145.29 ? 67  THR D CB  1 
ATOM   5325  O OG1 . THR D 4 67  ? -59.152  25.254   -25.247 1.00 146.00 ? 67  THR D OG1 1 
ATOM   5326  C CG2 . THR D 4 67  ? -61.386  25.605   -26.101 1.00 139.97 ? 67  THR D CG2 1 
ATOM   5327  N N   . SER D 4 68  ? -58.416  29.289   -27.112 1.00 143.75 ? 68  SER D N   1 
ATOM   5328  C CA  . SER D 4 68  ? -57.541  30.453   -26.955 1.00 147.25 ? 68  SER D CA  1 
ATOM   5329  C C   . SER D 4 68  ? -57.785  31.289   -25.694 1.00 153.96 ? 68  SER D C   1 
ATOM   5330  O O   . SER D 4 68  ? -58.714  31.019   -24.929 1.00 152.09 ? 68  SER D O   1 
ATOM   5331  C CB  . SER D 4 68  ? -57.636  31.344   -28.192 1.00 151.41 ? 68  SER D CB  1 
ATOM   5332  O OG  . SER D 4 68  ? -57.014  30.752   -29.320 1.00 159.25 ? 68  SER D OG  1 
ATOM   5333  N N   . GLY D 4 69  ? -56.937  32.308   -25.511 1.00 155.27 ? 69  GLY D N   1 
ATOM   5334  C CA  . GLY D 4 69  ? -57.022  33.273   -24.419 1.00 159.59 ? 69  GLY D CA  1 
ATOM   5335  C C   . GLY D 4 69  ? -58.240  34.167   -24.556 1.00 164.77 ? 69  GLY D C   1 
ATOM   5336  O O   . GLY D 4 69  ? -58.708  34.739   -23.566 1.00 167.11 ? 69  GLY D O   1 
ATOM   5337  N N   . THR D 4 70  ? -58.761  34.280   -25.805 1.00 159.45 ? 70  THR D N   1 
ATOM   5338  C CA  . THR D 4 70  ? -59.969  35.023   -26.189 1.00 159.12 ? 70  THR D CA  1 
ATOM   5339  C C   . THR D 4 70  ? -61.150  34.322   -25.504 1.00 159.65 ? 70  THR D C   1 
ATOM   5340  O O   . THR D 4 70  ? -61.770  34.901   -24.606 1.00 161.20 ? 70  THR D O   1 
ATOM   5341  C CB  . THR D 4 70  ? -60.109  35.075   -27.738 1.00 164.91 ? 70  THR D CB  1 
ATOM   5342  O OG1 . THR D 4 70  ? -60.112  33.749   -28.279 1.00 157.83 ? 70  THR D OG1 1 
ATOM   5343  C CG2 . THR D 4 70  ? -59.017  35.911   -28.405 1.00 167.76 ? 70  THR D CG2 1 
ATOM   5344  N N   . ASP D 4 71  ? -61.385  33.040   -25.899 1.00 151.96 ? 71  ASP D N   1 
ATOM   5345  C CA  . ASP D 4 71  ? -62.350  32.038   -25.418 1.00 149.04 ? 71  ASP D CA  1 
ATOM   5346  C C   . ASP D 4 71  ? -62.523  30.861   -26.402 1.00 146.46 ? 71  ASP D C   1 
ATOM   5347  O O   . ASP D 4 71  ? -62.783  29.748   -25.941 1.00 145.08 ? 71  ASP D O   1 
ATOM   5348  C CB  . ASP D 4 71  ? -63.717  32.618   -24.989 1.00 151.95 ? 71  ASP D CB  1 
ATOM   5349  C CG  . ASP D 4 71  ? -63.861  32.771   -23.480 1.00 162.27 ? 71  ASP D CG  1 
ATOM   5350  O OD1 . ASP D 4 71  ? -63.719  31.753   -22.759 1.00 160.67 ? 71  ASP D OD1 1 
ATOM   5351  O OD2 . ASP D 4 71  ? -64.127  33.903   -23.021 1.00 171.98 ? 71  ASP D OD2 1 
ATOM   5352  N N   . PHE D 4 72  ? -62.363  31.082   -27.732 1.00 138.98 ? 72  PHE D N   1 
ATOM   5353  C CA  . PHE D 4 72  ? -62.533  30.004   -28.718 1.00 134.52 ? 72  PHE D CA  1 
ATOM   5354  C C   . PHE D 4 72  ? -61.961  30.306   -30.108 1.00 135.72 ? 72  PHE D C   1 
ATOM   5355  O O   . PHE D 4 72  ? -61.999  31.458   -30.542 1.00 137.78 ? 72  PHE D O   1 
ATOM   5356  C CB  . PHE D 4 72  ? -64.024  29.633   -28.844 1.00 134.46 ? 72  PHE D CB  1 
ATOM   5357  C CG  . PHE D 4 72  ? -64.355  28.165   -29.005 1.00 133.79 ? 72  PHE D CG  1 
ATOM   5358  C CD1 . PHE D 4 72  ? -65.650  27.759   -29.298 1.00 135.39 ? 72  PHE D CD1 1 
ATOM   5359  C CD2 . PHE D 4 72  ? -63.374  27.189   -28.854 1.00 135.99 ? 72  PHE D CD2 1 
ATOM   5360  C CE1 . PHE D 4 72  ? -65.958  26.405   -29.448 1.00 134.85 ? 72  PHE D CE1 1 
ATOM   5361  C CE2 . PHE D 4 72  ? -63.681  25.836   -29.017 1.00 137.40 ? 72  PHE D CE2 1 
ATOM   5362  C CZ  . PHE D 4 72  ? -64.973  25.452   -29.299 1.00 134.06 ? 72  PHE D CZ  1 
ATOM   5363  N N   . THR D 4 73  ? -61.482  29.250   -30.821 1.00 127.51 ? 73  THR D N   1 
ATOM   5364  C CA  . THR D 4 73  ? -60.913  29.305   -32.178 1.00 125.57 ? 73  THR D CA  1 
ATOM   5365  C C   . THR D 4 73  ? -61.043  27.997   -32.961 1.00 124.89 ? 73  THR D C   1 
ATOM   5366  O O   . THR D 4 73  ? -60.531  26.967   -32.529 1.00 123.31 ? 73  THR D O   1 
ATOM   5367  C CB  . THR D 4 73  ? -59.442  29.782   -32.185 1.00 130.59 ? 73  THR D CB  1 
ATOM   5368  O OG1 . THR D 4 73  ? -58.815  29.492   -30.940 1.00 127.06 ? 73  THR D OG1 1 
ATOM   5369  C CG2 . THR D 4 73  ? -59.303  31.256   -32.501 1.00 131.39 ? 73  THR D CG2 1 
ATOM   5370  N N   . LEU D 4 74  ? -61.700  28.052   -34.127 1.00 120.25 ? 74  LEU D N   1 
ATOM   5371  C CA  . LEU D 4 74  ? -61.838  26.920   -35.046 1.00 119.21 ? 74  LEU D CA  1 
ATOM   5372  C C   . LEU D 4 74  ? -60.930  27.203   -36.235 1.00 126.80 ? 74  LEU D C   1 
ATOM   5373  O O   . LEU D 4 74  ? -60.977  28.307   -36.787 1.00 127.34 ? 74  LEU D O   1 
ATOM   5374  C CB  . LEU D 4 74  ? -63.291  26.759   -35.520 1.00 117.84 ? 74  LEU D CB  1 
ATOM   5375  C CG  . LEU D 4 74  ? -63.573  25.645   -36.538 1.00 121.58 ? 74  LEU D CG  1 
ATOM   5376  C CD1 . LEU D 4 74  ? -63.922  24.351   -35.852 1.00 120.96 ? 74  LEU D CD1 1 
ATOM   5377  C CD2 . LEU D 4 74  ? -64.709  26.021   -37.444 1.00 122.61 ? 74  LEU D CD2 1 
ATOM   5378  N N   . THR D 4 75  ? -60.103  26.214   -36.629 1.00 126.17 ? 75  THR D N   1 
ATOM   5379  C CA  . THR D 4 75  ? -59.144  26.358   -37.731 1.00 128.82 ? 75  THR D CA  1 
ATOM   5380  C C   . THR D 4 75  ? -59.202  25.200   -38.738 1.00 133.64 ? 75  THR D C   1 
ATOM   5381  O O   . THR D 4 75  ? -59.196  24.031   -38.342 1.00 132.94 ? 75  THR D O   1 
ATOM   5382  C CB  . THR D 4 75  ? -57.716  26.570   -37.181 1.00 142.52 ? 75  THR D CB  1 
ATOM   5383  O OG1 . THR D 4 75  ? -57.751  27.457   -36.058 1.00 144.12 ? 75  THR D OG1 1 
ATOM   5384  C CG2 . THR D 4 75  ? -56.748  27.104   -38.233 1.00 144.92 ? 75  THR D CG2 1 
ATOM   5385  N N   . ILE D 4 76  ? -59.247  25.538   -40.041 1.00 131.39 ? 76  ILE D N   1 
ATOM   5386  C CA  . ILE D 4 76  ? -59.254  24.572   -41.145 1.00 131.96 ? 76  ILE D CA  1 
ATOM   5387  C C   . ILE D 4 76  ? -58.019  24.849   -42.016 1.00 139.90 ? 76  ILE D C   1 
ATOM   5388  O O   . ILE D 4 76  ? -57.803  25.996   -42.416 1.00 141.14 ? 76  ILE D O   1 
ATOM   5389  C CB  . ILE D 4 76  ? -60.565  24.621   -41.980 1.00 133.95 ? 76  ILE D CB  1 
ATOM   5390  C CG1 . ILE D 4 76  ? -61.816  24.657   -41.091 1.00 131.64 ? 76  ILE D CG1 1 
ATOM   5391  C CG2 . ILE D 4 76  ? -60.624  23.453   -42.971 1.00 135.64 ? 76  ILE D CG2 1 
ATOM   5392  C CD1 . ILE D 4 76  ? -62.944  25.456   -41.654 1.00 140.98 ? 76  ILE D CD1 1 
ATOM   5393  N N   . SER D 4 77  ? -57.208  23.813   -42.299 1.00 138.00 ? 77  SER D N   1 
ATOM   5394  C CA  . SER D 4 77  ? -56.004  23.955   -43.124 1.00 141.00 ? 77  SER D CA  1 
ATOM   5395  C C   . SER D 4 77  ? -56.351  24.139   -44.613 1.00 146.30 ? 77  SER D C   1 
ATOM   5396  O O   . SER D 4 77  ? -56.007  25.171   -45.198 1.00 148.02 ? 77  SER D O   1 
ATOM   5397  C CB  . SER D 4 77  ? -55.050  22.783   -42.909 1.00 146.39 ? 77  SER D CB  1 
ATOM   5398  O OG  . SER D 4 77  ? -55.700  21.531   -43.058 1.00 154.90 ? 77  SER D OG  1 
ATOM   5399  N N   . ARG D 4 78  ? -57.052  23.150   -45.209 1.00 141.60 ? 78  ARG D N   1 
ATOM   5400  C CA  . ARG D 4 78  ? -57.489  23.169   -46.608 1.00 142.61 ? 78  ARG D CA  1 
ATOM   5401  C C   . ARG D 4 78  ? -59.014  23.306   -46.664 1.00 142.70 ? 78  ARG D C   1 
ATOM   5402  O O   . ARG D 4 78  ? -59.729  22.442   -46.149 1.00 141.23 ? 78  ARG D O   1 
ATOM   5403  C CB  . ARG D 4 78  ? -57.044  21.887   -47.344 1.00 144.70 ? 78  ARG D CB  1 
ATOM   5404  C CG  . ARG D 4 78  ? -55.553  21.800   -47.636 1.00 155.09 ? 78  ARG D CG  1 
ATOM   5405  C CD  . ARG D 4 78  ? -55.202  20.473   -48.286 1.00 165.76 ? 78  ARG D CD  1 
ATOM   5406  N NE  . ARG D 4 78  ? -53.820  20.454   -48.771 1.00 175.76 ? 78  ARG D NE  1 
ATOM   5407  C CZ  . ARG D 4 78  ? -53.187  19.366   -49.203 1.00 192.80 ? 78  ARG D CZ  1 
ATOM   5408  N NH1 . ARG D 4 78  ? -53.797  18.187   -49.197 1.00 183.58 ? 78  ARG D NH1 1 
ATOM   5409  N NH2 . ARG D 4 78  ? -51.936  19.448   -49.635 1.00 180.58 ? 78  ARG D NH2 1 
ATOM   5410  N N   . LEU D 4 79  ? -59.511  24.402   -47.258 1.00 137.36 ? 79  LEU D N   1 
ATOM   5411  C CA  . LEU D 4 79  ? -60.948  24.610   -47.387 1.00 134.40 ? 79  LEU D CA  1 
ATOM   5412  C C   . LEU D 4 79  ? -61.449  23.885   -48.623 1.00 138.29 ? 79  LEU D C   1 
ATOM   5413  O O   . LEU D 4 79  ? -61.185  24.316   -49.746 1.00 141.25 ? 79  LEU D O   1 
ATOM   5414  C CB  . LEU D 4 79  ? -61.304  26.102   -47.437 1.00 134.24 ? 79  LEU D CB  1 
ATOM   5415  C CG  . LEU D 4 79  ? -61.414  26.799   -46.096 1.00 135.92 ? 79  LEU D CG  1 
ATOM   5416  C CD1 . LEU D 4 79  ? -61.033  28.236   -46.223 1.00 137.56 ? 79  LEU D CD1 1 
ATOM   5417  C CD2 . LEU D 4 79  ? -62.820  26.676   -45.516 1.00 135.79 ? 79  LEU D CD2 1 
ATOM   5418  N N   . GLU D 4 80  ? -62.121  22.747   -48.414 1.00 131.78 ? 80  GLU D N   1 
ATOM   5419  C CA  . GLU D 4 80  ? -62.676  21.940   -49.501 1.00 133.24 ? 80  GLU D CA  1 
ATOM   5420  C C   . GLU D 4 80  ? -64.021  22.553   -49.937 1.00 135.52 ? 80  GLU D C   1 
ATOM   5421  O O   . GLU D 4 80  ? -64.602  23.295   -49.145 1.00 131.39 ? 80  GLU D O   1 
ATOM   5422  C CB  . GLU D 4 80  ? -62.841  20.478   -49.053 1.00 134.23 ? 80  GLU D CB  1 
ATOM   5423  C CG  . GLU D 4 80  ? -61.538  19.775   -48.696 1.00 142.07 ? 80  GLU D CG  1 
ATOM   5424  C CD  . GLU D 4 80  ? -60.588  19.452   -49.832 1.00 150.21 ? 80  GLU D CD  1 
ATOM   5425  O OE1 . GLU D 4 80  ? -61.028  18.818   -50.818 1.00 139.28 ? 80  GLU D OE1 1 
ATOM   5426  O OE2 . GLU D 4 80  ? -59.385  19.775   -49.699 1.00 132.50 ? 80  GLU D OE2 1 
ATOM   5427  N N   . PRO D 4 81  ? -64.545  22.294   -51.165 1.00 135.97 ? 81  PRO D N   1 
ATOM   5428  C CA  . PRO D 4 81  ? -65.834  22.911   -51.562 1.00 135.83 ? 81  PRO D CA  1 
ATOM   5429  C C   . PRO D 4 81  ? -66.988  22.657   -50.598 1.00 135.88 ? 81  PRO D C   1 
ATOM   5430  O O   . PRO D 4 81  ? -67.896  23.479   -50.492 1.00 134.46 ? 81  PRO D O   1 
ATOM   5431  C CB  . PRO D 4 81  ? -66.121  22.287   -52.929 1.00 142.24 ? 81  PRO D CB  1 
ATOM   5432  C CG  . PRO D 4 81  ? -64.791  21.891   -53.451 1.00 149.60 ? 81  PRO D CG  1 
ATOM   5433  C CD  . PRO D 4 81  ? -63.995  21.463   -52.257 1.00 142.15 ? 81  PRO D CD  1 
ATOM   5434  N N   . GLU D 4 82  ? -66.925  21.523   -49.889 1.00 131.41 ? 82  GLU D N   1 
ATOM   5435  C CA  . GLU D 4 82  ? -67.894  21.059   -48.895 1.00 128.91 ? 82  GLU D CA  1 
ATOM   5436  C C   . GLU D 4 82  ? -67.890  21.936   -47.631 1.00 127.94 ? 82  GLU D C   1 
ATOM   5437  O O   . GLU D 4 82  ? -68.927  22.072   -46.982 1.00 125.39 ? 82  GLU D O   1 
ATOM   5438  C CB  . GLU D 4 82  ? -67.581  19.601   -48.494 1.00 131.20 ? 82  GLU D CB  1 
ATOM   5439  C CG  . GLU D 4 82  ? -67.299  18.647   -49.653 1.00 146.66 ? 82  GLU D CG  1 
ATOM   5440  C CD  . GLU D 4 82  ? -65.841  18.432   -50.021 1.00 156.79 ? 82  GLU D CD  1 
ATOM   5441  O OE1 . GLU D 4 82  ? -65.487  18.672   -51.197 1.00 133.32 ? 82  GLU D OE1 1 
ATOM   5442  O OE2 . GLU D 4 82  ? -65.064  17.973   -49.153 1.00 152.11 ? 82  GLU D OE2 1 
ATOM   5443  N N   . ASP D 4 83  ? -66.714  22.502   -47.280 1.00 123.13 ? 83  ASP D N   1 
ATOM   5444  C CA  . ASP D 4 83  ? -66.470  23.332   -46.091 1.00 119.46 ? 83  ASP D CA  1 
ATOM   5445  C C   . ASP D 4 83  ? -67.157  24.707   -46.115 1.00 121.54 ? 83  ASP D C   1 
ATOM   5446  O O   . ASP D 4 83  ? -67.298  25.332   -45.064 1.00 118.86 ? 83  ASP D O   1 
ATOM   5447  C CB  . ASP D 4 83  ? -64.948  23.500   -45.846 1.00 121.57 ? 83  ASP D CB  1 
ATOM   5448  C CG  . ASP D 4 83  ? -64.154  22.224   -45.596 1.00 130.32 ? 83  ASP D CG  1 
ATOM   5449  O OD1 . ASP D 4 83  ? -64.510  21.174   -46.175 1.00 133.24 ? 83  ASP D OD1 1 
ATOM   5450  O OD2 . ASP D 4 83  ? -63.136  22.292   -44.874 1.00 131.78 ? 83  ASP D OD2 1 
ATOM   5451  N N   . PHE D 4 84  ? -67.569  25.184   -47.295 1.00 120.16 ? 84  PHE D N   1 
ATOM   5452  C CA  . PHE D 4 84  ? -68.202  26.493   -47.421 1.00 120.46 ? 84  PHE D CA  1 
ATOM   5453  C C   . PHE D 4 84  ? -69.642  26.491   -46.899 1.00 124.30 ? 84  PHE D C   1 
ATOM   5454  O O   . PHE D 4 84  ? -70.578  26.150   -47.628 1.00 125.51 ? 84  PHE D O   1 
ATOM   5455  C CB  . PHE D 4 84  ? -68.080  27.021   -48.858 1.00 125.59 ? 84  PHE D CB  1 
ATOM   5456  C CG  . PHE D 4 84  ? -66.649  27.336   -49.232 1.00 128.54 ? 84  PHE D CG  1 
ATOM   5457  C CD1 . PHE D 4 84  ? -66.077  28.555   -48.893 1.00 131.71 ? 84  PHE D CD1 1 
ATOM   5458  C CD2 . PHE D 4 84  ? -65.863  26.399   -49.893 1.00 132.16 ? 84  PHE D CD2 1 
ATOM   5459  C CE1 . PHE D 4 84  ? -64.748  28.834   -49.214 1.00 134.59 ? 84  PHE D CE1 1 
ATOM   5460  C CE2 . PHE D 4 84  ? -64.532  26.681   -50.213 1.00 136.79 ? 84  PHE D CE2 1 
ATOM   5461  C CZ  . PHE D 4 84  ? -63.986  27.899   -49.879 1.00 135.16 ? 84  PHE D CZ  1 
ATOM   5462  N N   . ALA D 4 85  ? -69.801  26.826   -45.605 1.00 119.21 ? 85  ALA D N   1 
ATOM   5463  C CA  . ALA D 4 85  ? -71.100  26.857   -44.915 1.00 117.93 ? 85  ALA D CA  1 
ATOM   5464  C C   . ALA D 4 85  ? -71.104  27.858   -43.752 1.00 119.83 ? 85  ALA D C   1 
ATOM   5465  O O   . ALA D 4 85  ? -70.155  28.636   -43.617 1.00 120.35 ? 85  ALA D O   1 
ATOM   5466  C CB  . ALA D 4 85  ? -71.470  25.460   -44.421 1.00 117.31 ? 85  ALA D CB  1 
ATOM   5467  N N   . VAL D 4 86  ? -72.184  27.856   -42.939 1.00 113.79 ? 86  VAL D N   1 
ATOM   5468  C CA  . VAL D 4 86  ? -72.345  28.740   -41.779 1.00 112.20 ? 86  VAL D CA  1 
ATOM   5469  C C   . VAL D 4 86  ? -71.793  28.027   -40.550 1.00 113.32 ? 86  VAL D C   1 
ATOM   5470  O O   . VAL D 4 86  ? -72.159  26.878   -40.287 1.00 111.82 ? 86  VAL D O   1 
ATOM   5471  C CB  . VAL D 4 86  ? -73.809  29.213   -41.576 1.00 116.26 ? 86  VAL D CB  1 
ATOM   5472  C CG1 . VAL D 4 86  ? -73.883  30.349   -40.560 1.00 116.40 ? 86  VAL D CG1 1 
ATOM   5473  C CG2 . VAL D 4 86  ? -74.438  29.646   -42.898 1.00 118.33 ? 86  VAL D CG2 1 
ATOM   5474  N N   . TYR D 4 87  ? -70.903  28.706   -39.811 1.00 109.73 ? 87  TYR D N   1 
ATOM   5475  C CA  . TYR D 4 87  ? -70.244  28.147   -38.635 1.00 108.27 ? 87  TYR D CA  1 
ATOM   5476  C C   . TYR D 4 87  ? -70.700  28.784   -37.338 1.00 113.22 ? 87  TYR D C   1 
ATOM   5477  O O   . TYR D 4 87  ? -70.644  30.005   -37.193 1.00 114.80 ? 87  TYR D O   1 
ATOM   5478  C CB  . TYR D 4 87  ? -68.721  28.199   -38.800 1.00 109.48 ? 87  TYR D CB  1 
ATOM   5479  C CG  . TYR D 4 87  ? -68.230  27.139   -39.758 1.00 110.97 ? 87  TYR D CG  1 
ATOM   5480  C CD1 . TYR D 4 87  ? -68.318  27.322   -41.134 1.00 114.22 ? 87  TYR D CD1 1 
ATOM   5481  C CD2 . TYR D 4 87  ? -67.764  25.916   -39.293 1.00 110.99 ? 87  TYR D CD2 1 
ATOM   5482  C CE1 . TYR D 4 87  ? -67.918  26.327   -42.021 1.00 115.91 ? 87  TYR D CE1 1 
ATOM   5483  C CE2 . TYR D 4 87  ? -67.348  24.919   -40.170 1.00 112.63 ? 87  TYR D CE2 1 
ATOM   5484  C CZ  . TYR D 4 87  ? -67.423  25.131   -41.534 1.00 122.34 ? 87  TYR D CZ  1 
ATOM   5485  O OH  . TYR D 4 87  ? -67.020  24.143   -42.397 1.00 126.58 ? 87  TYR D OH  1 
ATOM   5486  N N   . TYR D 4 88  ? -71.167  27.945   -36.403 1.00 108.95 ? 88  TYR D N   1 
ATOM   5487  C CA  . TYR D 4 88  ? -71.678  28.365   -35.101 1.00 109.54 ? 88  TYR D CA  1 
ATOM   5488  C C   . TYR D 4 88  ? -70.853  27.827   -33.942 1.00 112.54 ? 88  TYR D C   1 
ATOM   5489  O O   . TYR D 4 88  ? -70.388  26.693   -33.990 1.00 110.00 ? 88  TYR D O   1 
ATOM   5490  C CB  . TYR D 4 88  ? -73.129  27.879   -34.921 1.00 111.22 ? 88  TYR D CB  1 
ATOM   5491  C CG  . TYR D 4 88  ? -74.154  28.627   -35.744 1.00 114.96 ? 88  TYR D CG  1 
ATOM   5492  C CD1 . TYR D 4 88  ? -74.711  29.817   -35.284 1.00 119.10 ? 88  TYR D CD1 1 
ATOM   5493  C CD2 . TYR D 4 88  ? -74.611  28.118   -36.957 1.00 115.47 ? 88  TYR D CD2 1 
ATOM   5494  C CE1 . TYR D 4 88  ? -75.667  30.503   -36.030 1.00 122.19 ? 88  TYR D CE1 1 
ATOM   5495  C CE2 . TYR D 4 88  ? -75.567  28.795   -37.712 1.00 117.66 ? 88  TYR D CE2 1 
ATOM   5496  C CZ  . TYR D 4 88  ? -76.086  29.993   -37.249 1.00 127.28 ? 88  TYR D CZ  1 
ATOM   5497  O OH  . TYR D 4 88  ? -77.023  30.671   -37.990 1.00 129.54 ? 88  TYR D OH  1 
ATOM   5498  N N   . CYS D 4 89  ? -70.710  28.626   -32.882 1.00 111.41 ? 89  CYS D N   1 
ATOM   5499  C CA  . CYS D 4 89  ? -70.060  28.186   -31.653 1.00 111.97 ? 89  CYS D CA  1 
ATOM   5500  C C   . CYS D 4 89  ? -71.143  28.063   -30.587 1.00 113.00 ? 89  CYS D C   1 
ATOM   5501  O O   . CYS D 4 89  ? -72.201  28.676   -30.721 1.00 112.71 ? 89  CYS D O   1 
ATOM   5502  C CB  . CYS D 4 89  ? -68.939  29.130   -31.222 1.00 115.33 ? 89  CYS D CB  1 
ATOM   5503  S SG  . CYS D 4 89  ? -69.470  30.831   -30.895 1.00 122.84 ? 89  CYS D SG  1 
ATOM   5504  N N   . GLN D 4 90  ? -70.913  27.245   -29.561 1.00 108.01 ? 90  GLN D N   1 
ATOM   5505  C CA  . GLN D 4 90  ? -71.892  27.056   -28.494 1.00 108.20 ? 90  GLN D CA  1 
ATOM   5506  C C   . GLN D 4 90  ? -71.204  26.763   -27.174 1.00 112.89 ? 90  GLN D C   1 
ATOM   5507  O O   . GLN D 4 90  ? -70.228  26.016   -27.141 1.00 112.38 ? 90  GLN D O   1 
ATOM   5508  C CB  . GLN D 4 90  ? -72.874  25.928   -28.853 1.00 108.27 ? 90  GLN D CB  1 
ATOM   5509  C CG  . GLN D 4 90  ? -74.012  25.734   -27.856 1.00 123.75 ? 90  GLN D CG  1 
ATOM   5510  C CD  . GLN D 4 90  ? -74.343  24.280   -27.617 1.00 144.69 ? 90  GLN D CD  1 
ATOM   5511  O OE1 . GLN D 4 90  ? -73.525  23.374   -27.820 1.00 137.77 ? 90  GLN D OE1 1 
ATOM   5512  N NE2 . GLN D 4 90  ? -75.548  24.031   -27.135 1.00 141.88 ? 90  GLN D NE2 1 
ATOM   5513  N N   . GLN D 4 91  ? -71.712  27.355   -26.092 1.00 110.98 ? 91  GLN D N   1 
ATOM   5514  C CA  . GLN D 4 91  ? -71.211  27.124   -24.745 1.00 112.81 ? 91  GLN D CA  1 
ATOM   5515  C C   . GLN D 4 91  ? -72.223  26.273   -23.972 1.00 118.50 ? 91  GLN D C   1 
ATOM   5516  O O   . GLN D 4 91  ? -73.429  26.443   -24.159 1.00 118.72 ? 91  GLN D O   1 
ATOM   5517  C CB  . GLN D 4 91  ? -70.867  28.446   -24.026 1.00 116.87 ? 91  GLN D CB  1 
ATOM   5518  C CG  . GLN D 4 91  ? -72.035  29.415   -23.793 1.00 133.24 ? 91  GLN D CG  1 
ATOM   5519  C CD  . GLN D 4 91  ? -72.799  29.160   -22.517 1.00 147.53 ? 91  GLN D CD  1 
ATOM   5520  O OE1 . GLN D 4 91  ? -72.328  28.488   -21.595 1.00 142.25 ? 91  GLN D OE1 1 
ATOM   5521  N NE2 . GLN D 4 91  ? -73.998  29.703   -22.440 1.00 140.74 ? 91  GLN D NE2 1 
ATOM   5522  N N   . CYS D 4 92  ? -71.740  25.335   -23.144 1.00 123.78 ? 92  CYS D N   1 
ATOM   5523  C CA  . CYS D 4 92  ? -72.607  24.444   -22.365 1.00 125.88 ? 92  CYS D CA  1 
ATOM   5524  C C   . CYS D 4 92  ? -72.366  24.538   -20.839 1.00 134.42 ? 92  CYS D C   1 
ATOM   5525  O O   . CYS D 4 92  ? -72.887  23.724   -20.071 1.00 135.96 ? 92  CYS D O   1 
ATOM   5526  C CB  . CYS D 4 92  ? -72.506  23.008   -22.879 1.00 124.09 ? 92  CYS D CB  1 
ATOM   5527  S SG  . CYS D 4 92  ? -72.733  22.839   -24.673 1.00 124.57 ? 92  CYS D SG  1 
ATOM   5528  N N   . GLY D 4 93  ? -71.620  25.561   -20.426 1.00 132.70 ? 93  GLY D N   1 
ATOM   5529  C CA  . GLY D 4 93  ? -71.327  25.817   -19.021 1.00 136.26 ? 93  GLY D CA  1 
ATOM   5530  C C   . GLY D 4 93  ? -72.389  26.681   -18.367 1.00 145.23 ? 93  GLY D C   1 
ATOM   5531  O O   . GLY D 4 93  ? -72.478  27.865   -18.701 1.00 144.31 ? 93  GLY D O   1 
ATOM   5532  N N   . ASN D 4 94  ? -73.182  26.132   -17.419 1.00 147.40 ? 94  ASN D N   1 
ATOM   5533  C CA  . ASN D 4 94  ? -74.277  26.810   -16.680 1.00 152.30 ? 94  ASN D CA  1 
ATOM   5534  C C   . ASN D 4 94  ? -75.433  27.302   -17.597 1.00 155.98 ? 94  ASN D C   1 
ATOM   5535  O O   . ASN D 4 94  ? -75.212  27.709   -18.748 1.00 151.28 ? 94  ASN D O   1 
ATOM   5536  C CB  . ASN D 4 94  ? -73.773  27.947   -15.751 1.00 155.11 ? 94  ASN D CB  1 
ATOM   5537  C CG  . ASN D 4 94  ? -73.671  27.586   -14.277 1.00 167.28 ? 94  ASN D CG  1 
ATOM   5538  O OD1 . ASN D 4 94  ? -74.400  28.113   -13.425 1.00 165.32 ? 94  ASN D OD1 1 
ATOM   5539  N ND2 . ASN D 4 94  ? -72.722  26.725   -13.928 1.00 152.33 ? 94  ASN D ND2 1 
ATOM   5540  N N   . SER D 4 95  ? -76.673  27.242   -17.060 1.00 156.62 ? 95  SER D N   1 
ATOM   5541  C CA  . SER D 4 95  ? -77.898  27.637   -17.763 1.00 156.28 ? 95  SER D CA  1 
ATOM   5542  C C   . SER D 4 95  ? -77.979  29.155   -18.021 1.00 161.29 ? 95  SER D C   1 
ATOM   5543  O O   . SER D 4 95  ? -77.739  29.945   -17.100 1.00 164.82 ? 95  SER D O   1 
ATOM   5544  C CB  . SER D 4 95  ? -79.138  27.145   -17.019 1.00 163.30 ? 95  SER D CB  1 
ATOM   5545  O OG  . SER D 4 95  ? -80.330  27.427   -17.737 1.00 169.21 ? 95  SER D OG  1 
ATOM   5546  N N   . PRO D 4 96  ? -78.304  29.581   -19.267 1.00 154.33 ? 96  PRO D N   1 
ATOM   5547  C CA  . PRO D 4 96  ? -78.635  28.760   -20.440 1.00 149.53 ? 96  PRO D CA  1 
ATOM   5548  C C   . PRO D 4 96  ? -77.447  28.492   -21.359 1.00 146.57 ? 96  PRO D C   1 
ATOM   5549  O O   . PRO D 4 96  ? -76.376  29.069   -21.171 1.00 145.85 ? 96  PRO D O   1 
ATOM   5550  C CB  . PRO D 4 96  ? -79.710  29.604   -21.130 1.00 151.40 ? 96  PRO D CB  1 
ATOM   5551  C CG  . PRO D 4 96  ? -79.330  31.048   -20.812 1.00 157.93 ? 96  PRO D CG  1 
ATOM   5552  C CD  . PRO D 4 96  ? -78.427  31.019   -19.587 1.00 156.53 ? 96  PRO D CD  1 
ATOM   5553  N N   . TRP D 4 97  ? -77.642  27.613   -22.350 1.00 138.55 ? 97  TRP D N   1 
ATOM   5554  C CA  . TRP D 4 97  ? -76.622  27.334   -23.351 1.00 134.00 ? 97  TRP D CA  1 
ATOM   5555  C C   . TRP D 4 97  ? -76.880  28.306   -24.490 1.00 134.90 ? 97  TRP D C   1 
ATOM   5556  O O   . TRP D 4 97  ? -78.007  28.421   -24.973 1.00 134.40 ? 97  TRP D O   1 
ATOM   5557  C CB  . TRP D 4 97  ? -76.683  25.878   -23.839 1.00 131.14 ? 97  TRP D CB  1 
ATOM   5558  C CG  . TRP D 4 97  ? -76.357  24.836   -22.804 1.00 133.91 ? 97  TRP D CG  1 
ATOM   5559  C CD1 . TRP D 4 97  ? -76.096  25.036   -21.477 1.00 139.73 ? 97  TRP D CD1 1 
ATOM   5560  C CD2 . TRP D 4 97  ? -76.279  23.421   -23.019 1.00 132.84 ? 97  TRP D CD2 1 
ATOM   5561  N NE1 . TRP D 4 97  ? -75.851  23.835   -20.857 1.00 140.07 ? 97  TRP D NE1 1 
ATOM   5562  C CE2 . TRP D 4 97  ? -75.964  22.825   -21.778 1.00 139.15 ? 97  TRP D CE2 1 
ATOM   5563  C CE3 . TRP D 4 97  ? -76.426  22.596   -24.148 1.00 131.91 ? 97  TRP D CE3 1 
ATOM   5564  C CZ2 . TRP D 4 97  ? -75.809  21.443   -21.630 1.00 138.41 ? 97  TRP D CZ2 1 
ATOM   5565  C CZ3 . TRP D 4 97  ? -76.290  21.225   -23.996 1.00 133.49 ? 97  TRP D CZ3 1 
ATOM   5566  C CH2 . TRP D 4 97  ? -75.976  20.662   -22.753 1.00 136.21 ? 97  TRP D CH2 1 
ATOM   5567  N N   . THR D 4 98  ? -75.866  29.068   -24.863 1.00 129.58 ? 98  THR D N   1 
ATOM   5568  C CA  . THR D 4 98  ? -76.034  30.062   -25.911 1.00 127.58 ? 98  THR D CA  1 
ATOM   5569  C C   . THR D 4 98  ? -75.230  29.715   -27.149 1.00 128.00 ? 98  THR D C   1 
ATOM   5570  O O   . THR D 4 98  ? -74.158  29.120   -27.054 1.00 127.23 ? 98  THR D O   1 
ATOM   5571  C CB  . THR D 4 98  ? -75.752  31.470   -25.377 1.00 134.74 ? 98  THR D CB  1 
ATOM   5572  O OG1 . THR D 4 98  ? -74.543  31.459   -24.620 1.00 132.53 ? 98  THR D OG1 1 
ATOM   5573  C CG2 . THR D 4 98  ? -76.893  32.006   -24.524 1.00 137.33 ? 98  THR D CG2 1 
ATOM   5574  N N   . PHE D 4 99  ? -75.779  30.052   -28.316 1.00 121.77 ? 99  PHE D N   1 
ATOM   5575  C CA  . PHE D 4 99  ? -75.128  29.839   -29.595 1.00 118.21 ? 99  PHE D CA  1 
ATOM   5576  C C   . PHE D 4 99  ? -74.602  31.177   -30.069 1.00 120.36 ? 99  PHE D C   1 
ATOM   5577  O O   . PHE D 4 99  ? -75.197  32.224   -29.792 1.00 119.31 ? 99  PHE D O   1 
ATOM   5578  C CB  . PHE D 4 99  ? -76.104  29.245   -30.627 1.00 118.89 ? 99  PHE D CB  1 
ATOM   5579  C CG  . PHE D 4 99  ? -76.464  27.797   -30.396 1.00 120.46 ? 99  PHE D CG  1 
ATOM   5580  C CD1 . PHE D 4 99  ? -75.738  26.780   -30.998 1.00 121.75 ? 99  PHE D CD1 1 
ATOM   5581  C CD2 . PHE D 4 99  ? -77.536  27.450   -29.583 1.00 124.34 ? 99  PHE D CD2 1 
ATOM   5582  C CE1 . PHE D 4 99  ? -76.068  25.439   -30.775 1.00 123.06 ? 99  PHE D CE1 1 
ATOM   5583  C CE2 . PHE D 4 99  ? -77.863  26.110   -29.361 1.00 127.47 ? 99  PHE D CE2 1 
ATOM   5584  C CZ  . PHE D 4 99  ? -77.125  25.113   -29.956 1.00 123.91 ? 99  PHE D CZ  1 
ATOM   5585  N N   . GLY D 4 100 ? -73.490  31.129   -30.780 1.00 117.42 ? 100 GLY D N   1 
ATOM   5586  C CA  . GLY D 4 100 ? -72.856  32.308   -31.345 1.00 118.08 ? 100 GLY D CA  1 
ATOM   5587  C C   . GLY D 4 100 ? -73.670  32.950   -32.450 1.00 124.63 ? 100 GLY D C   1 
ATOM   5588  O O   . GLY D 4 100 ? -74.740  32.452   -32.830 1.00 123.99 ? 100 GLY D O   1 
ATOM   5589  N N   . GLN D 4 101 ? -73.153  34.066   -32.975 1.00 123.20 ? 101 GLN D N   1 
ATOM   5590  C CA  . GLN D 4 101 ? -73.798  34.844   -34.036 1.00 123.08 ? 101 GLN D CA  1 
ATOM   5591  C C   . GLN D 4 101 ? -73.847  34.070   -35.360 1.00 125.34 ? 101 GLN D C   1 
ATOM   5592  O O   . GLN D 4 101 ? -74.906  34.008   -35.986 1.00 125.01 ? 101 GLN D O   1 
ATOM   5593  C CB  . GLN D 4 101 ? -73.137  36.232   -34.186 1.00 125.22 ? 101 GLN D CB  1 
ATOM   5594  C CG  . GLN D 4 101 ? -72.889  36.935   -32.841 1.00 145.45 ? 101 GLN D CG  1 
ATOM   5595  C CD  . GLN D 4 101 ? -72.942  38.438   -32.902 1.00 173.23 ? 101 GLN D CD  1 
ATOM   5596  O OE1 . GLN D 4 101 ? -72.156  39.095   -33.599 1.00 173.52 ? 101 GLN D OE1 1 
ATOM   5597  N NE2 . GLN D 4 101 ? -73.836  39.015   -32.111 1.00 164.29 ? 101 GLN D NE2 1 
ATOM   5598  N N   . GLY D 4 102 ? -72.729  33.445   -35.731 1.00 120.73 ? 102 GLY D N   1 
ATOM   5599  C CA  . GLY D 4 102 ? -72.618  32.649   -36.946 1.00 119.73 ? 102 GLY D CA  1 
ATOM   5600  C C   . GLY D 4 102 ? -71.920  33.366   -38.083 1.00 124.02 ? 102 GLY D C   1 
ATOM   5601  O O   . GLY D 4 102 ? -72.390  34.417   -38.532 1.00 124.54 ? 102 GLY D O   1 
ATOM   5602  N N   . THR D 4 103 ? -70.800  32.787   -38.576 1.00 119.22 ? 103 THR D N   1 
ATOM   5603  C CA  . THR D 4 103 ? -70.008  33.355   -39.677 1.00 118.19 ? 103 THR D CA  1 
ATOM   5604  C C   . THR D 4 103 ? -70.042  32.451   -40.910 1.00 120.03 ? 103 THR D C   1 
ATOM   5605  O O   . THR D 4 103 ? -69.462  31.362   -40.886 1.00 119.46 ? 103 THR D O   1 
ATOM   5606  C CB  . THR D 4 103 ? -68.562  33.753   -39.244 1.00 124.10 ? 103 THR D CB  1 
ATOM   5607  O OG1 . THR D 4 103 ? -67.604  33.293   -40.197 1.00 121.63 ? 103 THR D OG1 1 
ATOM   5608  C CG2 . THR D 4 103 ? -68.174  33.270   -37.845 1.00 122.58 ? 103 THR D CG2 1 
ATOM   5609  N N   . LYS D 4 104 ? -70.713  32.914   -41.988 1.00 115.53 ? 104 LYS D N   1 
ATOM   5610  C CA  . LYS D 4 104 ? -70.799  32.182   -43.253 1.00 115.42 ? 104 LYS D CA  1 
ATOM   5611  C C   . LYS D 4 104 ? -69.458  32.238   -43.987 1.00 119.32 ? 104 LYS D C   1 
ATOM   5612  O O   . LYS D 4 104 ? -68.879  33.318   -44.144 1.00 118.84 ? 104 LYS D O   1 
ATOM   5613  C CB  . LYS D 4 104 ? -71.964  32.704   -44.134 1.00 117.68 ? 104 LYS D CB  1 
ATOM   5614  C CG  . LYS D 4 104 ? -71.816  32.532   -45.672 1.00 126.01 ? 104 LYS D CG  1 
ATOM   5615  C CD  . LYS D 4 104 ? -72.029  31.092   -46.180 1.00 127.32 ? 104 LYS D CD  1 
ATOM   5616  C CE  . LYS D 4 104 ? -71.857  30.968   -47.676 1.00 120.80 ? 104 LYS D CE  1 
ATOM   5617  N NZ  . LYS D 4 104 ? -71.994  29.559   -48.130 1.00 119.18 ? 104 LYS D NZ  1 
ATOM   5618  N N   . VAL D 4 105 ? -68.979  31.061   -44.431 1.00 116.28 ? 105 VAL D N   1 
ATOM   5619  C CA  . VAL D 4 105 ? -67.741  30.908   -45.193 1.00 117.21 ? 105 VAL D CA  1 
ATOM   5620  C C   . VAL D 4 105 ? -68.146  30.818   -46.678 1.00 122.46 ? 105 VAL D C   1 
ATOM   5621  O O   . VAL D 4 105 ? -68.779  29.842   -47.086 1.00 122.89 ? 105 VAL D O   1 
ATOM   5622  C CB  . VAL D 4 105 ? -66.886  29.708   -44.689 1.00 120.69 ? 105 VAL D CB  1 
ATOM   5623  C CG1 . VAL D 4 105 ? -65.558  29.613   -45.432 1.00 122.22 ? 105 VAL D CG1 1 
ATOM   5624  C CG2 . VAL D 4 105 ? -66.634  29.818   -43.194 1.00 118.70 ? 105 VAL D CG2 1 
ATOM   5625  N N   . GLU D 4 106 ? -67.853  31.885   -47.451 1.00 118.74 ? 106 GLU D N   1 
ATOM   5626  C CA  . GLU D 4 106 ? -68.189  31.991   -48.872 1.00 120.09 ? 106 GLU D CA  1 
ATOM   5627  C C   . GLU D 4 106 ? -66.980  31.838   -49.795 1.00 126.43 ? 106 GLU D C   1 
ATOM   5628  O O   . GLU D 4 106 ? -65.859  32.180   -49.415 1.00 124.81 ? 106 GLU D O   1 
ATOM   5629  C CB  . GLU D 4 106 ? -68.974  33.289   -49.183 1.00 120.67 ? 106 GLU D CB  1 
ATOM   5630  C CG  . GLU D 4 106 ? -68.209  34.600   -49.026 1.00 131.69 ? 106 GLU D CG  1 
ATOM   5631  C CD  . GLU D 4 106 ? -68.922  35.865   -49.475 1.00 150.69 ? 106 GLU D CD  1 
ATOM   5632  O OE1 . GLU D 4 106 ? -70.134  36.011   -49.194 1.00 136.87 ? 106 GLU D OE1 1 
ATOM   5633  O OE2 . GLU D 4 106 ? -68.245  36.745   -50.052 1.00 150.12 ? 106 GLU D OE2 1 
ATOM   5634  N N   . ILE D 4 107 ? -67.225  31.326   -51.013 1.00 124.82 ? 107 ILE D N   1 
ATOM   5635  C CA  . ILE D 4 107 ? -66.204  31.119   -52.039 1.00 127.84 ? 107 ILE D CA  1 
ATOM   5636  C C   . ILE D 4 107 ? -65.792  32.488   -52.565 1.00 133.63 ? 107 ILE D C   1 
ATOM   5637  O O   . ILE D 4 107 ? -66.647  33.225   -53.060 1.00 133.67 ? 107 ILE D O   1 
ATOM   5638  C CB  . ILE D 4 107 ? -66.717  30.183   -53.172 1.00 133.83 ? 107 ILE D CB  1 
ATOM   5639  C CG1 . ILE D 4 107 ? -67.290  28.866   -52.611 1.00 134.00 ? 107 ILE D CG1 1 
ATOM   5640  C CG2 . ILE D 4 107 ? -65.617  29.899   -54.193 1.00 138.93 ? 107 ILE D CG2 1 
ATOM   5641  C CD1 . ILE D 4 107 ? -68.581  28.385   -53.296 1.00 146.20 ? 107 ILE D CD1 1 
ATOM   5642  N N   . LYS D 4 108 ? -64.500  32.840   -52.428 1.00 131.13 ? 108 LYS D N   1 
ATOM   5643  C CA  . LYS D 4 108 ? -63.944  34.120   -52.866 1.00 132.24 ? 108 LYS D CA  1 
ATOM   5644  C C   . LYS D 4 108 ? -63.787  34.134   -54.395 1.00 141.50 ? 108 LYS D C   1 
ATOM   5645  O O   . LYS D 4 108 ? -63.110  33.261   -54.948 1.00 143.90 ? 108 LYS D O   1 
ATOM   5646  C CB  . LYS D 4 108 ? -62.608  34.373   -52.155 1.00 134.31 ? 108 LYS D CB  1 
ATOM   5647  C CG  . LYS D 4 108 ? -62.138  35.819   -52.150 1.00 149.85 ? 108 LYS D CG  1 
ATOM   5648  C CD  . LYS D 4 108 ? -61.015  36.044   -51.134 1.00 163.51 ? 108 LYS D CD  1 
ATOM   5649  C CE  . LYS D 4 108 ? -59.701  35.365   -51.474 1.00 185.15 ? 108 LYS D CE  1 
ATOM   5650  N NZ  . LYS D 4 108 ? -58.761  35.358   -50.319 1.00 193.80 ? 108 LYS D NZ  1 
ATOM   5651  N N   . ARG D 4 109 ? -64.444  35.113   -55.071 1.00 138.89 ? 109 ARG D N   1 
ATOM   5652  C CA  . ARG D 4 109 ? -64.439  35.293   -56.531 1.00 142.15 ? 109 ARG D CA  1 
ATOM   5653  C C   . ARG D 4 109 ? -64.346  36.772   -56.944 1.00 147.51 ? 109 ARG D C   1 
ATOM   5654  O O   . ARG D 4 109 ? -64.387  37.658   -56.088 1.00 144.93 ? 109 ARG D O   1 
ATOM   5655  C CB  . ARG D 4 109 ? -65.648  34.588   -57.194 1.00 139.68 ? 109 ARG D CB  1 
ATOM   5656  C CG  . ARG D 4 109 ? -67.011  35.201   -56.889 1.00 142.72 ? 109 ARG D CG  1 
ATOM   5657  C CD  . ARG D 4 109 ? -67.984  34.986   -58.033 1.00 150.86 ? 109 ARG D CD  1 
ATOM   5658  N NE  . ARG D 4 109 ? -67.815  35.978   -59.099 1.00 162.28 ? 109 ARG D NE  1 
ATOM   5659  C CZ  . ARG D 4 109 ? -68.114  35.777   -60.382 1.00 171.87 ? 109 ARG D CZ  1 
ATOM   5660  N NH1 . ARG D 4 109 ? -68.584  34.602   -60.787 1.00 157.79 ? 109 ARG D NH1 1 
ATOM   5661  N NH2 . ARG D 4 109 ? -67.933  36.743   -61.271 1.00 155.17 ? 109 ARG D NH2 1 
ATOM   5662  N N   . THR D 4 110 ? -64.207  37.029   -58.255 1.00 122.21 ? 110 THR D N   1 
ATOM   5663  C CA  . THR D 4 110 ? -64.126  38.379   -58.816 1.00 124.29 ? 110 THR D CA  1 
ATOM   5664  C C   . THR D 4 110 ? -65.434  39.126   -58.603 1.00 128.49 ? 110 THR D C   1 
ATOM   5665  O O   . THR D 4 110 ? -66.500  38.504   -58.601 1.00 127.10 ? 110 THR D O   1 
ATOM   5666  C CB  . THR D 4 110 ? -63.771  38.335   -60.306 1.00 135.85 ? 110 THR D CB  1 
ATOM   5667  O OG1 . THR D 4 110 ? -64.627  37.409   -60.979 1.00 133.22 ? 110 THR D OG1 1 
ATOM   5668  C CG2 . THR D 4 110 ? -62.311  37.993   -60.547 1.00 140.53 ? 110 THR D CG2 1 
ATOM   5669  N N   . VAL D 4 111 ? -65.347  40.457   -58.411 1.00 127.09 ? 111 VAL D N   1 
ATOM   5670  C CA  . VAL D 4 111 ? -66.493  41.344   -58.196 1.00 126.36 ? 111 VAL D CA  1 
ATOM   5671  C C   . VAL D 4 111 ? -67.417  41.238   -59.404 1.00 134.79 ? 111 VAL D C   1 
ATOM   5672  O O   . VAL D 4 111 ? -66.972  41.452   -60.533 1.00 136.21 ? 111 VAL D O   1 
ATOM   5673  C CB  . VAL D 4 111 ? -66.091  42.819   -57.919 1.00 130.64 ? 111 VAL D CB  1 
ATOM   5674  C CG1 . VAL D 4 111 ? -67.137  43.508   -57.054 1.00 128.12 ? 111 VAL D CG1 1 
ATOM   5675  C CG2 . VAL D 4 111 ? -64.709  42.929   -57.275 1.00 131.81 ? 111 VAL D CG2 1 
ATOM   5676  N N   . ALA D 4 112 ? -68.672  40.833   -59.173 1.00 131.97 ? 112 ALA D N   1 
ATOM   5677  C CA  . ALA D 4 112 ? -69.658  40.670   -60.240 1.00 133.73 ? 112 ALA D CA  1 
ATOM   5678  C C   . ALA D 4 112 ? -70.803  41.661   -60.089 1.00 139.27 ? 112 ALA D C   1 
ATOM   5679  O O   . ALA D 4 112 ? -71.459  41.691   -59.047 1.00 136.84 ? 112 ALA D O   1 
ATOM   5680  C CB  . ALA D 4 112 ? -70.188  39.242   -60.261 1.00 133.74 ? 112 ALA D CB  1 
ATOM   5681  N N   . ALA D 4 113 ? -71.021  42.491   -61.121 1.00 139.42 ? 113 ALA D N   1 
ATOM   5682  C CA  . ALA D 4 113 ? -72.098  43.479   -61.151 1.00 139.33 ? 113 ALA D CA  1 
ATOM   5683  C C   . ALA D 4 113 ? -73.440  42.755   -61.388 1.00 143.80 ? 113 ALA D C   1 
ATOM   5684  O O   . ALA D 4 113 ? -73.471  41.786   -62.155 1.00 144.81 ? 113 ALA D O   1 
ATOM   5685  C CB  . ALA D 4 113 ? -71.842  44.497   -62.251 1.00 142.54 ? 113 ALA D CB  1 
ATOM   5686  N N   . PRO D 4 114 ? -74.552  43.171   -60.737 1.00 139.21 ? 114 PRO D N   1 
ATOM   5687  C CA  . PRO D 4 114 ? -75.818  42.454   -60.947 1.00 138.01 ? 114 PRO D CA  1 
ATOM   5688  C C   . PRO D 4 114 ? -76.467  42.701   -62.298 1.00 143.30 ? 114 PRO D C   1 
ATOM   5689  O O   . PRO D 4 114 ? -76.265  43.742   -62.919 1.00 144.13 ? 114 PRO D O   1 
ATOM   5690  C CB  . PRO D 4 114 ? -76.707  42.963   -59.813 1.00 138.09 ? 114 PRO D CB  1 
ATOM   5691  C CG  . PRO D 4 114 ? -76.199  44.328   -59.530 1.00 143.43 ? 114 PRO D CG  1 
ATOM   5692  C CD  . PRO D 4 114 ? -74.715  44.284   -59.777 1.00 140.24 ? 114 PRO D CD  1 
ATOM   5693  N N   . SER D 4 115 ? -77.247  41.724   -62.738 1.00 140.18 ? 115 SER D N   1 
ATOM   5694  C CA  . SER D 4 115 ? -78.030  41.805   -63.954 1.00 141.77 ? 115 SER D CA  1 
ATOM   5695  C C   . SER D 4 115 ? -79.396  42.287   -63.441 1.00 146.72 ? 115 SER D C   1 
ATOM   5696  O O   . SER D 4 115 ? -80.151  41.503   -62.863 1.00 145.73 ? 115 SER D O   1 
ATOM   5697  C CB  . SER D 4 115 ? -78.113  40.435   -64.625 1.00 144.75 ? 115 SER D CB  1 
ATOM   5698  O OG  . SER D 4 115 ? -76.827  39.854   -64.784 1.00 150.84 ? 115 SER D OG  1 
ATOM   5699  N N   . VAL D 4 116 ? -79.646  43.607   -63.534 1.00 144.51 ? 116 VAL D N   1 
ATOM   5700  C CA  . VAL D 4 116 ? -80.862  44.257   -63.023 1.00 143.80 ? 116 VAL D CA  1 
ATOM   5701  C C   . VAL D 4 116 ? -81.991  44.287   -64.068 1.00 151.25 ? 116 VAL D C   1 
ATOM   5702  O O   . VAL D 4 116 ? -81.775  44.738   -65.196 1.00 153.85 ? 116 VAL D O   1 
ATOM   5703  C CB  . VAL D 4 116 ? -80.566  45.663   -62.427 1.00 147.20 ? 116 VAL D CB  1 
ATOM   5704  C CG1 . VAL D 4 116 ? -81.826  46.298   -61.836 1.00 146.27 ? 116 VAL D CG1 1 
ATOM   5705  C CG2 . VAL D 4 116 ? -79.457  45.597   -61.378 1.00 146.00 ? 116 VAL D CG2 1 
ATOM   5706  N N   . PHE D 4 117 ? -83.195  43.805   -63.674 1.00 147.49 ? 117 PHE D N   1 
ATOM   5707  C CA  . PHE D 4 117 ? -84.406  43.763   -64.506 1.00 148.85 ? 117 PHE D CA  1 
ATOM   5708  C C   . PHE D 4 117 ? -85.647  44.178   -63.711 1.00 153.43 ? 117 PHE D C   1 
ATOM   5709  O O   . PHE D 4 117 ? -85.752  43.846   -62.530 1.00 151.31 ? 117 PHE D O   1 
ATOM   5710  C CB  . PHE D 4 117 ? -84.631  42.355   -65.090 1.00 151.01 ? 117 PHE D CB  1 
ATOM   5711  C CG  . PHE D 4 117 ? -83.438  41.711   -65.753 1.00 153.42 ? 117 PHE D CG  1 
ATOM   5712  C CD1 . PHE D 4 117 ? -82.761  40.668   -65.138 1.00 155.24 ? 117 PHE D CD1 1 
ATOM   5713  C CD2 . PHE D 4 117 ? -82.992  42.148   -66.995 1.00 158.02 ? 117 PHE D CD2 1 
ATOM   5714  C CE1 . PHE D 4 117 ? -81.661  40.067   -65.754 1.00 157.33 ? 117 PHE D CE1 1 
ATOM   5715  C CE2 . PHE D 4 117 ? -81.883  41.556   -67.605 1.00 162.08 ? 117 PHE D CE2 1 
ATOM   5716  C CZ  . PHE D 4 117 ? -81.227  40.517   -66.981 1.00 158.84 ? 117 PHE D CZ  1 
ATOM   5717  N N   . ILE D 4 118 ? -86.595  44.879   -64.363 1.00 153.25 ? 118 ILE D N   1 
ATOM   5718  C CA  . ILE D 4 118 ? -87.856  45.309   -63.743 1.00 154.00 ? 118 ILE D CA  1 
ATOM   5719  C C   . ILE D 4 118 ? -89.043  44.589   -64.426 1.00 160.29 ? 118 ILE D C   1 
ATOM   5720  O O   . ILE D 4 118 ? -89.113  44.534   -65.658 1.00 161.23 ? 118 ILE D O   1 
ATOM   5721  C CB  . ILE D 4 118 ? -88.006  46.869   -63.640 1.00 158.27 ? 118 ILE D CB  1 
ATOM   5722  C CG1 . ILE D 4 118 ? -89.257  47.277   -62.810 1.00 158.48 ? 118 ILE D CG1 1 
ATOM   5723  C CG2 . ILE D 4 118 ? -87.964  47.577   -65.013 1.00 161.91 ? 118 ILE D CG2 1 
ATOM   5724  C CD1 . ILE D 4 118 ? -89.154  48.621   -62.052 1.00 163.98 ? 118 ILE D CD1 1 
ATOM   5725  N N   . PHE D 4 119 ? -89.925  43.979   -63.613 1.00 157.61 ? 119 PHE D N   1 
ATOM   5726  C CA  . PHE D 4 119 ? -91.086  43.241   -64.104 1.00 159.13 ? 119 PHE D CA  1 
ATOM   5727  C C   . PHE D 4 119 ? -92.406  43.960   -63.834 1.00 164.25 ? 119 PHE D C   1 
ATOM   5728  O O   . PHE D 4 119 ? -92.753  44.188   -62.673 1.00 162.98 ? 119 PHE D O   1 
ATOM   5729  C CB  . PHE D 4 119 ? -91.134  41.801   -63.560 1.00 160.45 ? 119 PHE D CB  1 
ATOM   5730  C CG  . PHE D 4 119 ? -90.055  40.881   -64.077 1.00 162.02 ? 119 PHE D CG  1 
ATOM   5731  C CD1 . PHE D 4 119 ? -88.932  40.604   -63.311 1.00 163.86 ? 119 PHE D CD1 1 
ATOM   5732  C CD2 . PHE D 4 119 ? -90.170  40.274   -65.323 1.00 165.88 ? 119 PHE D CD2 1 
ATOM   5733  C CE1 . PHE D 4 119 ? -87.939  39.739   -63.782 1.00 164.82 ? 119 PHE D CE1 1 
ATOM   5734  C CE2 . PHE D 4 119 ? -89.169  39.427   -65.802 1.00 168.98 ? 119 PHE D CE2 1 
ATOM   5735  C CZ  . PHE D 4 119 ? -88.062  39.159   -65.026 1.00 165.61 ? 119 PHE D CZ  1 
ATOM   5736  N N   . PRO D 4 120 ? -93.179  44.290   -64.898 1.00 163.04 ? 120 PRO D N   1 
ATOM   5737  C CA  . PRO D 4 120 ? -94.482  44.944   -64.679 1.00 164.08 ? 120 PRO D CA  1 
ATOM   5738  C C   . PRO D 4 120 ? -95.525  43.972   -64.094 1.00 167.76 ? 120 PRO D C   1 
ATOM   5739  O O   . PRO D 4 120 ? -95.371  42.757   -64.275 1.00 167.23 ? 120 PRO D O   1 
ATOM   5740  C CB  . PRO D 4 120 ? -94.866  45.439   -66.077 1.00 167.87 ? 120 PRO D CB  1 
ATOM   5741  C CG  . PRO D 4 120 ? -94.183  44.509   -67.010 1.00 172.37 ? 120 PRO D CG  1 
ATOM   5742  C CD  . PRO D 4 120 ? -92.915  44.069   -66.337 1.00 165.92 ? 120 PRO D CD  1 
ATOM   5743  N N   . PRO D 4 121 ? -96.572  44.456   -63.372 1.00 164.30 ? 121 PRO D N   1 
ATOM   5744  C CA  . PRO D 4 121 ? -97.565  43.519   -62.809 1.00 164.40 ? 121 PRO D CA  1 
ATOM   5745  C C   . PRO D 4 121 ? -98.399  42.827   -63.879 1.00 169.23 ? 121 PRO D C   1 
ATOM   5746  O O   . PRO D 4 121 ? -98.665  43.418   -64.927 1.00 170.07 ? 121 PRO D O   1 
ATOM   5747  C CB  . PRO D 4 121 ? -98.451  44.406   -61.925 1.00 167.23 ? 121 PRO D CB  1 
ATOM   5748  C CG  . PRO D 4 121 ? -97.780  45.725   -61.844 1.00 171.21 ? 121 PRO D CG  1 
ATOM   5749  C CD  . PRO D 4 121 ? -96.915  45.856   -63.049 1.00 166.39 ? 121 PRO D CD  1 
ATOM   5750  N N   . SER D 4 122 ? -98.810  41.576   -63.612 1.00 165.64 ? 122 SER D N   1 
ATOM   5751  C CA  . SER D 4 122 ? -99.638  40.799   -64.532 1.00 167.16 ? 122 SER D CA  1 
ATOM   5752  C C   . SER D 4 122 ? -101.030 41.416   -64.639 1.00 172.37 ? 122 SER D C   1 
ATOM   5753  O O   . SER D 4 122 ? -101.532 41.967   -63.659 1.00 172.07 ? 122 SER D O   1 
ATOM   5754  C CB  . SER D 4 122 ? -99.747  39.352   -64.064 1.00 170.84 ? 122 SER D CB  1 
ATOM   5755  O OG  . SER D 4 122 ? -100.540 38.573   -64.947 1.00 182.01 ? 122 SER D OG  1 
ATOM   5756  N N   . ASP D 4 123 ? -101.647 41.322   -65.829 1.00 170.38 ? 123 ASP D N   1 
ATOM   5757  C CA  . ASP D 4 123 ? -102.988 41.855   -66.078 1.00 172.62 ? 123 ASP D CA  1 
ATOM   5758  C C   . ASP D 4 123 ? -104.081 41.035   -65.364 1.00 178.28 ? 123 ASP D C   1 
ATOM   5759  O O   . ASP D 4 123 ? -105.206 41.518   -65.209 1.00 179.40 ? 123 ASP D O   1 
ATOM   5760  C CB  . ASP D 4 123 ? -103.247 42.016   -67.581 1.00 176.08 ? 123 ASP D CB  1 
ATOM   5761  C CG  . ASP D 4 123 ? -102.320 43.026   -68.237 1.00 183.17 ? 123 ASP D CG  1 
ATOM   5762  O OD1 . ASP D 4 123 ? -102.555 44.245   -68.072 1.00 183.51 ? 123 ASP D OD1 1 
ATOM   5763  O OD2 . ASP D 4 123 ? -101.351 42.598   -68.899 1.00 187.69 ? 123 ASP D OD2 1 
ATOM   5764  N N   . GLU D 4 124 ? -103.723 39.816   -64.893 1.00 174.85 ? 124 GLU D N   1 
ATOM   5765  C CA  . GLU D 4 124 ? -104.574 38.918   -64.103 1.00 176.38 ? 124 GLU D CA  1 
ATOM   5766  C C   . GLU D 4 124 ? -104.622 39.436   -62.657 1.00 179.41 ? 124 GLU D C   1 
ATOM   5767  O O   . GLU D 4 124 ? -105.654 39.329   -61.991 1.00 181.12 ? 124 GLU D O   1 
ATOM   5768  C CB  . GLU D 4 124 ? -104.017 37.481   -64.122 1.00 177.12 ? 124 GLU D CB  1 
ATOM   5769  C CG  . GLU D 4 124 ? -104.467 36.651   -65.313 1.00 190.13 ? 124 GLU D CG  1 
ATOM   5770  C CD  . GLU D 4 124 ? -103.662 36.796   -66.592 1.00 207.66 ? 124 GLU D CD  1 
ATOM   5771  O OE1 . GLU D 4 124 ? -104.284 37.047   -67.650 1.00 210.25 ? 124 GLU D OE1 1 
ATOM   5772  O OE2 . GLU D 4 124 ? -102.423 36.612   -66.549 1.00 190.94 ? 124 GLU D OE2 1 
ATOM   5773  N N   . GLN D 4 125 ? -103.487 39.999   -62.187 1.00 173.00 ? 125 GLN D N   1 
ATOM   5774  C CA  . GLN D 4 125 ? -103.298 40.585   -60.858 1.00 171.74 ? 125 GLN D CA  1 
ATOM   5775  C C   . GLN D 4 125 ? -104.051 41.919   -60.744 1.00 175.77 ? 125 GLN D C   1 
ATOM   5776  O O   . GLN D 4 125 ? -104.477 42.289   -59.650 1.00 176.10 ? 125 GLN D O   1 
ATOM   5777  C CB  . GLN D 4 125 ? -101.795 40.762   -60.580 1.00 170.01 ? 125 GLN D CB  1 
ATOM   5778  C CG  . GLN D 4 125 ? -101.446 41.124   -59.143 1.00 179.94 ? 125 GLN D CG  1 
ATOM   5779  C CD  . GLN D 4 125 ? -99.959  41.205   -58.909 1.00 193.71 ? 125 GLN D CD  1 
ATOM   5780  O OE1 . GLN D 4 125 ? -99.190  41.713   -59.736 1.00 188.83 ? 125 GLN D OE1 1 
ATOM   5781  N NE2 . GLN D 4 125 ? -99.529  40.752   -57.746 1.00 182.44 ? 125 GLN D NE2 1 
ATOM   5782  N N   . LEU D 4 126 ? -104.221 42.629   -61.879 1.00 171.89 ? 126 LEU D N   1 
ATOM   5783  C CA  . LEU D 4 126 ? -104.951 43.897   -61.969 1.00 172.74 ? 126 LEU D CA  1 
ATOM   5784  C C   . LEU D 4 126 ? -106.429 43.698   -61.614 1.00 177.04 ? 126 LEU D C   1 
ATOM   5785  O O   . LEU D 4 126 ? -107.043 44.595   -61.033 1.00 178.12 ? 126 LEU D O   1 
ATOM   5786  C CB  . LEU D 4 126 ? -104.829 44.471   -63.390 1.00 173.22 ? 126 LEU D CB  1 
ATOM   5787  C CG  . LEU D 4 126 ? -103.883 45.656   -63.572 1.00 176.71 ? 126 LEU D CG  1 
ATOM   5788  C CD1 . LEU D 4 126 ? -102.437 45.195   -63.762 1.00 174.13 ? 126 LEU D CD1 1 
ATOM   5789  C CD2 . LEU D 4 126 ? -104.313 46.499   -64.760 1.00 181.11 ? 126 LEU D CD2 1 
ATOM   5790  N N   . LYS D 4 127 ? -106.979 42.507   -61.941 1.00 172.90 ? 127 LYS D N   1 
ATOM   5791  C CA  . LYS D 4 127 ? -108.364 42.112   -61.679 1.00 175.49 ? 127 LYS D CA  1 
ATOM   5792  C C   . LYS D 4 127 ? -108.663 41.990   -60.178 1.00 180.35 ? 127 LYS D C   1 
ATOM   5793  O O   . LYS D 4 127 ? -109.820 42.146   -59.782 1.00 183.69 ? 127 LYS D O   1 
ATOM   5794  C CB  . LYS D 4 127 ? -108.694 40.797   -62.407 1.00 178.28 ? 127 LYS D CB  1 
ATOM   5795  C CG  . LYS D 4 127 ? -110.169 40.627   -62.755 1.00 186.58 ? 127 LYS D CG  1 
ATOM   5796  C CD  . LYS D 4 127 ? -110.500 39.185   -63.107 1.00 190.90 ? 127 LYS D CD  1 
ATOM   5797  C CE  . LYS D 4 127 ? -111.985 38.965   -63.223 1.00 197.91 ? 127 LYS D CE  1 
ATOM   5798  N NZ  . LYS D 4 127 ? -112.304 37.562   -63.596 1.00 206.05 ? 127 LYS D NZ  1 
ATOM   5799  N N   . SER D 4 128 ? -107.630 41.732   -59.344 1.00 173.88 ? 128 SER D N   1 
ATOM   5800  C CA  . SER D 4 128 ? -107.797 41.596   -57.898 1.00 174.55 ? 128 SER D CA  1 
ATOM   5801  C C   . SER D 4 128 ? -107.961 42.946   -57.183 1.00 179.09 ? 128 SER D C   1 
ATOM   5802  O O   . SER D 4 128 ? -108.841 43.075   -56.329 1.00 181.45 ? 128 SER D O   1 
ATOM   5803  C CB  . SER D 4 128 ? -106.661 40.776   -57.291 1.00 175.46 ? 128 SER D CB  1 
ATOM   5804  O OG  . SER D 4 128 ? -105.430 41.479   -57.278 1.00 180.94 ? 128 SER D OG  1 
ATOM   5805  N N   . GLY D 4 129 ? -107.127 43.926   -57.546 1.00 173.50 ? 129 GLY D N   1 
ATOM   5806  C CA  . GLY D 4 129 ? -107.140 45.268   -56.965 1.00 173.95 ? 129 GLY D CA  1 
ATOM   5807  C C   . GLY D 4 129 ? -105.872 45.654   -56.221 1.00 174.87 ? 129 GLY D C   1 
ATOM   5808  O O   . GLY D 4 129 ? -105.794 46.751   -55.660 1.00 175.02 ? 129 GLY D O   1 
ATOM   5809  N N   . THR D 4 130 ? -104.878 44.743   -56.192 1.00 168.15 ? 130 THR D N   1 
ATOM   5810  C CA  . THR D 4 130 ? -103.569 44.915   -55.556 1.00 164.81 ? 130 THR D CA  1 
ATOM   5811  C C   . THR D 4 130 ? -102.527 44.284   -56.494 1.00 164.63 ? 130 THR D C   1 
ATOM   5812  O O   . THR D 4 130 ? -102.553 43.071   -56.710 1.00 163.89 ? 130 THR D O   1 
ATOM   5813  C CB  . THR D 4 130 ? -103.581 44.342   -54.116 1.00 173.03 ? 130 THR D CB  1 
ATOM   5814  O OG1 . THR D 4 130 ? -104.569 45.029   -53.345 1.00 175.20 ? 130 THR D OG1 1 
ATOM   5815  C CG2 . THR D 4 130 ? -102.232 44.459   -53.415 1.00 168.86 ? 130 THR D CG2 1 
ATOM   5816  N N   . ALA D 4 131 ? -101.652 45.121   -57.087 1.00 158.50 ? 131 ALA D N   1 
ATOM   5817  C CA  . ALA D 4 131 ? -100.620 44.692   -58.037 1.00 155.44 ? 131 ALA D CA  1 
ATOM   5818  C C   . ALA D 4 131 ? -99.203  45.017   -57.563 1.00 156.09 ? 131 ALA D C   1 
ATOM   5819  O O   . ALA D 4 131 ? -98.959  46.105   -57.039 1.00 155.86 ? 131 ALA D O   1 
ATOM   5820  C CB  . ALA D 4 131 ? -100.879 45.307   -59.401 1.00 156.73 ? 131 ALA D CB  1 
ATOM   5821  N N   . SER D 4 132 ? -98.269  44.072   -57.757 1.00 150.04 ? 132 SER D N   1 
ATOM   5822  C CA  . SER D 4 132 ? -96.878  44.212   -57.321 1.00 147.32 ? 132 SER D CA  1 
ATOM   5823  C C   . SER D 4 132 ? -95.868  44.269   -58.468 1.00 148.94 ? 132 SER D C   1 
ATOM   5824  O O   . SER D 4 132 ? -96.049  43.591   -59.479 1.00 148.49 ? 132 SER D O   1 
ATOM   5825  C CB  . SER D 4 132 ? -96.508  43.092   -56.353 1.00 150.22 ? 132 SER D CB  1 
ATOM   5826  O OG  . SER D 4 132 ? -97.436  42.990   -55.285 1.00 160.88 ? 132 SER D OG  1 
ATOM   5827  N N   . VAL D 4 133 ? -94.796  45.069   -58.294 1.00 144.53 ? 133 VAL D N   1 
ATOM   5828  C CA  . VAL D 4 133 ? -93.705  45.239   -59.268 1.00 143.70 ? 133 VAL D CA  1 
ATOM   5829  C C   . VAL D 4 133 ? -92.428  44.633   -58.661 1.00 146.74 ? 133 VAL D C   1 
ATOM   5830  O O   . VAL D 4 133 ? -92.164  44.855   -57.478 1.00 145.69 ? 133 VAL D O   1 
ATOM   5831  C CB  . VAL D 4 133 ? -93.515  46.728   -59.698 1.00 148.36 ? 133 VAL D CB  1 
ATOM   5832  C CG1 . VAL D 4 133 ? -92.425  46.874   -60.757 1.00 147.58 ? 133 VAL D CG1 1 
ATOM   5833  C CG2 . VAL D 4 133 ? -94.819  47.336   -60.207 1.00 150.18 ? 133 VAL D CG2 1 
ATOM   5834  N N   . VAL D 4 134 ? -91.658  43.850   -59.458 1.00 143.59 ? 134 VAL D N   1 
ATOM   5835  C CA  . VAL D 4 134 ? -90.425  43.178   -59.007 1.00 142.27 ? 134 VAL D CA  1 
ATOM   5836  C C   . VAL D 4 134 ? -89.160  43.728   -59.697 1.00 146.91 ? 134 VAL D C   1 
ATOM   5837  O O   . VAL D 4 134 ? -89.163  43.930   -60.909 1.00 147.45 ? 134 VAL D O   1 
ATOM   5838  C CB  . VAL D 4 134 ? -90.508  41.626   -59.117 1.00 145.69 ? 134 VAL D CB  1 
ATOM   5839  C CG1 . VAL D 4 134 ? -89.373  40.954   -58.349 1.00 143.99 ? 134 VAL D CG1 1 
ATOM   5840  C CG2 . VAL D 4 134 ? -91.854  41.102   -58.626 1.00 146.61 ? 134 VAL D CG2 1 
ATOM   5841  N N   . CYS D 4 135 ? -88.083  43.944   -58.911 1.00 143.19 ? 135 CYS D N   1 
ATOM   5842  C CA  . CYS D 4 135 ? -86.772  44.426   -59.354 1.00 143.06 ? 135 CYS D CA  1 
ATOM   5843  C C   . CYS D 4 135 ? -85.730  43.308   -59.134 1.00 144.74 ? 135 CYS D C   1 
ATOM   5844  O O   . CYS D 4 135 ? -85.101  43.242   -58.076 1.00 143.90 ? 135 CYS D O   1 
ATOM   5845  C CB  . CYS D 4 135 ? -86.398  45.708   -58.611 1.00 144.15 ? 135 CYS D CB  1 
ATOM   5846  S SG  . CYS D 4 135 ? -84.800  46.416   -59.082 1.00 148.70 ? 135 CYS D SG  1 
ATOM   5847  N N   . LEU D 4 136 ? -85.590  42.404   -60.124 1.00 140.28 ? 136 LEU D N   1 
ATOM   5848  C CA  . LEU D 4 136 ? -84.672  41.260   -60.087 1.00 138.73 ? 136 LEU D CA  1 
ATOM   5849  C C   . LEU D 4 136 ? -83.216  41.669   -60.305 1.00 141.90 ? 136 LEU D C   1 
ATOM   5850  O O   . LEU D 4 136 ? -82.912  42.389   -61.250 1.00 142.68 ? 136 LEU D O   1 
ATOM   5851  C CB  . LEU D 4 136 ? -85.114  40.184   -61.107 1.00 139.38 ? 136 LEU D CB  1 
ATOM   5852  C CG  . LEU D 4 136 ? -84.067  39.187   -61.615 1.00 143.86 ? 136 LEU D CG  1 
ATOM   5853  C CD1 . LEU D 4 136 ? -83.721  38.162   -60.562 1.00 142.98 ? 136 LEU D CD1 1 
ATOM   5854  C CD2 . LEU D 4 136 ? -84.536  38.507   -62.870 1.00 147.63 ? 136 LEU D CD2 1 
ATOM   5855  N N   . LEU D 4 137 ? -82.323  41.168   -59.444 1.00 137.16 ? 137 LEU D N   1 
ATOM   5856  C CA  . LEU D 4 137 ? -80.885  41.421   -59.478 1.00 136.90 ? 137 LEU D CA  1 
ATOM   5857  C C   . LEU D 4 137 ? -80.173  40.080   -59.659 1.00 140.45 ? 137 LEU D C   1 
ATOM   5858  O O   . LEU D 4 137 ? -79.686  39.507   -58.686 1.00 139.44 ? 137 LEU D O   1 
ATOM   5859  C CB  . LEU D 4 137 ? -80.459  42.079   -58.153 1.00 136.10 ? 137 LEU D CB  1 
ATOM   5860  C CG  . LEU D 4 137 ? -80.457  43.604   -58.081 1.00 141.25 ? 137 LEU D CG  1 
ATOM   5861  C CD1 . LEU D 4 137 ? -81.870  44.175   -58.005 1.00 141.46 ? 137 LEU D CD1 1 
ATOM   5862  C CD2 . LEU D 4 137 ? -79.688  44.064   -56.874 1.00 143.22 ? 137 LEU D CD2 1 
ATOM   5863  N N   . ASN D 4 138 ? -80.157  39.550   -60.890 1.00 137.36 ? 138 ASN D N   1 
ATOM   5864  C CA  . ASN D 4 138 ? -79.549  38.248   -61.155 1.00 137.18 ? 138 ASN D CA  1 
ATOM   5865  C C   . ASN D 4 138 ? -78.029  38.266   -61.102 1.00 140.57 ? 138 ASN D C   1 
ATOM   5866  O O   . ASN D 4 138 ? -77.406  39.229   -61.540 1.00 140.76 ? 138 ASN D O   1 
ATOM   5867  C CB  . ASN D 4 138 ? -80.048  37.644   -62.471 1.00 139.87 ? 138 ASN D CB  1 
ATOM   5868  C CG  . ASN D 4 138 ? -80.420  36.176   -62.373 1.00 165.89 ? 138 ASN D CG  1 
ATOM   5869  O OD1 . ASN D 4 138 ? -79.590  35.311   -62.074 1.00 158.74 ? 138 ASN D OD1 1 
ATOM   5870  N ND2 . ASN D 4 138 ? -81.673  35.854   -62.671 1.00 159.94 ? 138 ASN D ND2 1 
ATOM   5871  N N   . ASN D 4 139 ? -77.463  37.196   -60.510 1.00 136.44 ? 139 ASN D N   1 
ATOM   5872  C CA  . ASN D 4 139 ? -76.053  36.826   -60.323 1.00 136.54 ? 139 ASN D CA  1 
ATOM   5873  C C   . ASN D 4 139 ? -75.069  37.999   -60.075 1.00 138.95 ? 139 ASN D C   1 
ATOM   5874  O O   . ASN D 4 139 ? -74.671  38.698   -61.013 1.00 140.27 ? 139 ASN D O   1 
ATOM   5875  C CB  . ASN D 4 139 ? -75.578  35.948   -61.489 1.00 141.43 ? 139 ASN D CB  1 
ATOM   5876  C CG  . ASN D 4 139 ? -76.334  34.636   -61.628 1.00 169.96 ? 139 ASN D CG  1 
ATOM   5877  O OD1 . ASN D 4 139 ? -76.889  34.320   -62.685 1.00 166.03 ? 139 ASN D OD1 1 
ATOM   5878  N ND2 . ASN D 4 139 ? -76.367  33.829   -60.572 1.00 161.91 ? 139 ASN D ND2 1 
ATOM   5879  N N   . PHE D 4 140 ? -74.657  38.173   -58.801 1.00 132.89 ? 140 PHE D N   1 
ATOM   5880  C CA  . PHE D 4 140 ? -73.717  39.210   -58.362 1.00 132.36 ? 140 PHE D CA  1 
ATOM   5881  C C   . PHE D 4 140 ? -72.827  38.773   -57.196 1.00 133.95 ? 140 PHE D C   1 
ATOM   5882  O O   . PHE D 4 140 ? -73.144  37.810   -56.497 1.00 132.09 ? 140 PHE D O   1 
ATOM   5883  C CB  . PHE D 4 140 ? -74.441  40.539   -58.041 1.00 133.63 ? 140 PHE D CB  1 
ATOM   5884  C CG  . PHE D 4 140 ? -75.488  40.503   -56.950 1.00 133.53 ? 140 PHE D CG  1 
ATOM   5885  C CD1 . PHE D 4 140 ? -75.141  40.717   -55.622 1.00 135.51 ? 140 PHE D CD1 1 
ATOM   5886  C CD2 . PHE D 4 140 ? -76.830  40.319   -57.257 1.00 135.06 ? 140 PHE D CD2 1 
ATOM   5887  C CE1 . PHE D 4 140 ? -76.112  40.693   -54.614 1.00 135.04 ? 140 PHE D CE1 1 
ATOM   5888  C CE2 . PHE D 4 140 ? -77.800  40.302   -56.247 1.00 136.36 ? 140 PHE D CE2 1 
ATOM   5889  C CZ  . PHE D 4 140 ? -77.434  40.485   -54.934 1.00 133.47 ? 140 PHE D CZ  1 
ATOM   5890  N N   . TYR D 4 141 ? -71.710  39.487   -56.994 1.00 130.98 ? 141 TYR D N   1 
ATOM   5891  C CA  . TYR D 4 141 ? -70.777  39.229   -55.899 1.00 130.82 ? 141 TYR D CA  1 
ATOM   5892  C C   . TYR D 4 141 ? -70.109  40.533   -55.451 1.00 138.43 ? 141 TYR D C   1 
ATOM   5893  O O   . TYR D 4 141 ? -69.615  41.272   -56.302 1.00 139.44 ? 141 TYR D O   1 
ATOM   5894  C CB  . TYR D 4 141 ? -69.726  38.172   -56.290 1.00 132.48 ? 141 TYR D CB  1 
ATOM   5895  C CG  . TYR D 4 141 ? -68.851  37.707   -55.144 1.00 133.01 ? 141 TYR D CG  1 
ATOM   5896  C CD1 . TYR D 4 141 ? -69.249  36.662   -54.316 1.00 133.89 ? 141 TYR D CD1 1 
ATOM   5897  C CD2 . TYR D 4 141 ? -67.602  38.277   -54.919 1.00 134.45 ? 141 TYR D CD2 1 
ATOM   5898  C CE1 . TYR D 4 141 ? -68.441  36.218   -53.270 1.00 133.97 ? 141 TYR D CE1 1 
ATOM   5899  C CE2 . TYR D 4 141 ? -66.787  37.845   -53.873 1.00 135.04 ? 141 TYR D CE2 1 
ATOM   5900  C CZ  . TYR D 4 141 ? -67.208  36.813   -53.053 1.00 138.93 ? 141 TYR D CZ  1 
ATOM   5901  O OH  . TYR D 4 141 ? -66.403  36.388   -52.025 1.00 137.99 ? 141 TYR D OH  1 
ATOM   5902  N N   . PRO D 4 142 ? -70.060  40.844   -54.133 1.00 137.12 ? 142 PRO D N   1 
ATOM   5903  C CA  . PRO D 4 142 ? -70.589  40.071   -52.988 1.00 136.71 ? 142 PRO D CA  1 
ATOM   5904  C C   . PRO D 4 142 ? -72.093  40.266   -52.746 1.00 141.40 ? 142 PRO D C   1 
ATOM   5905  O O   . PRO D 4 142 ? -72.697  41.114   -53.408 1.00 141.23 ? 142 PRO D O   1 
ATOM   5906  C CB  . PRO D 4 142 ? -69.713  40.556   -51.829 1.00 138.93 ? 142 PRO D CB  1 
ATOM   5907  C CG  . PRO D 4 142 ? -69.413  42.000   -52.172 1.00 144.02 ? 142 PRO D CG  1 
ATOM   5908  C CD  . PRO D 4 142 ? -69.408  42.094   -53.684 1.00 139.91 ? 142 PRO D CD  1 
ATOM   5909  N N   . ARG D 4 143 ? -72.695  39.486   -51.799 1.00 138.40 ? 143 ARG D N   1 
ATOM   5910  C CA  . ARG D 4 143 ? -74.128  39.534   -51.419 1.00 137.98 ? 143 ARG D CA  1 
ATOM   5911  C C   . ARG D 4 143 ? -74.557  40.945   -50.984 1.00 142.62 ? 143 ARG D C   1 
ATOM   5912  O O   . ARG D 4 143 ? -75.728  41.320   -51.099 1.00 141.89 ? 143 ARG D O   1 
ATOM   5913  C CB  . ARG D 4 143 ? -74.412  38.532   -50.280 1.00 138.38 ? 143 ARG D CB  1 
ATOM   5914  C CG  . ARG D 4 143 ? -75.892  38.175   -50.081 1.00 148.31 ? 143 ARG D CG  1 
ATOM   5915  C CD  . ARG D 4 143 ? -76.092  37.170   -48.954 1.00 158.46 ? 143 ARG D CD  1 
ATOM   5916  N NE  . ARG D 4 143 ? -77.372  36.464   -49.062 1.00 163.22 ? 143 ARG D NE  1 
ATOM   5917  C CZ  . ARG D 4 143 ? -77.727  35.424   -48.312 1.00 173.74 ? 143 ARG D CZ  1 
ATOM   5918  N NH1 . ARG D 4 143 ? -76.903  34.952   -47.384 1.00 158.44 ? 143 ARG D NH1 1 
ATOM   5919  N NH2 . ARG D 4 143 ? -78.909  34.847   -48.484 1.00 160.52 ? 143 ARG D NH2 1 
ATOM   5920  N N   . GLU D 4 144 ? -73.579  41.711   -50.494 1.00 140.16 ? 144 GLU D N   1 
ATOM   5921  C CA  . GLU D 4 144 ? -73.665  43.071   -49.983 1.00 140.47 ? 144 GLU D CA  1 
ATOM   5922  C C   . GLU D 4 144 ? -74.078  44.068   -51.090 1.00 144.28 ? 144 GLU D C   1 
ATOM   5923  O O   . GLU D 4 144 ? -73.234  44.519   -51.873 1.00 144.03 ? 144 GLU D O   1 
ATOM   5924  C CB  . GLU D 4 144 ? -72.324  43.445   -49.303 1.00 142.69 ? 144 GLU D CB  1 
ATOM   5925  C CG  . GLU D 4 144 ? -71.892  42.499   -48.176 1.00 151.24 ? 144 GLU D CG  1 
ATOM   5926  C CD  . GLU D 4 144 ? -71.085  41.261   -48.544 1.00 161.12 ? 144 GLU D CD  1 
ATOM   5927  O OE1 . GLU D 4 144 ? -71.680  40.282   -49.049 1.00 147.98 ? 144 GLU D OE1 1 
ATOM   5928  O OE2 . GLU D 4 144 ? -69.866  41.244   -48.261 1.00 146.70 ? 144 GLU D OE2 1 
ATOM   5929  N N   . ALA D 4 145 ? -75.402  44.365   -51.163 1.00 141.14 ? 145 ALA D N   1 
ATOM   5930  C CA  . ALA D 4 145 ? -76.044  45.274   -52.132 1.00 141.74 ? 145 ALA D CA  1 
ATOM   5931  C C   . ALA D 4 145 ? -77.326  45.913   -51.556 1.00 146.86 ? 145 ALA D C   1 
ATOM   5932  O O   . ALA D 4 145 ? -77.859  45.403   -50.565 1.00 146.69 ? 145 ALA D O   1 
ATOM   5933  C CB  . ALA D 4 145 ? -76.374  44.518   -53.410 1.00 142.00 ? 145 ALA D CB  1 
ATOM   5934  N N   . LYS D 4 146 ? -77.823  47.019   -52.175 1.00 143.97 ? 146 LYS D N   1 
ATOM   5935  C CA  . LYS D 4 146 ? -79.041  47.709   -51.727 1.00 144.41 ? 146 LYS D CA  1 
ATOM   5936  C C   . LYS D 4 146 ? -79.903  48.231   -52.877 1.00 151.06 ? 146 LYS D C   1 
ATOM   5937  O O   . LYS D 4 146 ? -79.385  48.869   -53.794 1.00 151.37 ? 146 LYS D O   1 
ATOM   5938  C CB  . LYS D 4 146 ? -78.716  48.832   -50.717 1.00 147.46 ? 146 LYS D CB  1 
ATOM   5939  C CG  . LYS D 4 146 ? -79.936  49.533   -50.088 1.00 157.44 ? 146 LYS D CG  1 
ATOM   5940  C CD  . LYS D 4 146 ? -80.791  48.612   -49.207 1.00 163.60 ? 146 LYS D CD  1 
ATOM   5941  C CE  . LYS D 4 146 ? -82.139  49.209   -48.886 1.00 168.29 ? 146 LYS D CE  1 
ATOM   5942  N NZ  . LYS D 4 146 ? -82.988  48.262   -48.117 1.00 172.02 ? 146 LYS D NZ  1 
ATOM   5943  N N   . VAL D 4 147 ? -81.227  47.971   -52.800 1.00 149.78 ? 147 VAL D N   1 
ATOM   5944  C CA  . VAL D 4 147 ? -82.242  48.388   -53.781 1.00 151.23 ? 147 VAL D CA  1 
ATOM   5945  C C   . VAL D 4 147 ? -83.161  49.459   -53.154 1.00 159.58 ? 147 VAL D C   1 
ATOM   5946  O O   . VAL D 4 147 ? -83.626  49.283   -52.024 1.00 159.70 ? 147 VAL D O   1 
ATOM   5947  C CB  . VAL D 4 147 ? -83.055  47.182   -54.337 1.00 154.24 ? 147 VAL D CB  1 
ATOM   5948  C CG1 . VAL D 4 147 ? -83.929  47.593   -55.518 1.00 154.72 ? 147 VAL D CG1 1 
ATOM   5949  C CG2 . VAL D 4 147 ? -82.138  46.035   -54.740 1.00 153.06 ? 147 VAL D CG2 1 
ATOM   5950  N N   . GLN D 4 148 ? -83.412  50.563   -53.891 1.00 159.26 ? 148 GLN D N   1 
ATOM   5951  C CA  . GLN D 4 148 ? -84.268  51.676   -53.455 1.00 161.40 ? 148 GLN D CA  1 
ATOM   5952  C C   . GLN D 4 148 ? -85.371  51.922   -54.497 1.00 166.10 ? 148 GLN D C   1 
ATOM   5953  O O   . GLN D 4 148 ? -85.080  52.406   -55.593 1.00 165.81 ? 148 GLN D O   1 
ATOM   5954  C CB  . GLN D 4 148 ? -83.439  52.963   -53.235 1.00 164.37 ? 148 GLN D CB  1 
ATOM   5955  C CG  . GLN D 4 148 ? -82.436  52.899   -52.086 1.00 184.65 ? 148 GLN D CG  1 
ATOM   5956  C CD  . GLN D 4 148 ? -81.310  53.889   -52.279 1.00 206.71 ? 148 GLN D CD  1 
ATOM   5957  O OE1 . GLN D 4 148 ? -80.227  53.548   -52.766 1.00 201.72 ? 148 GLN D OE1 1 
ATOM   5958  N NE2 . GLN D 4 148 ? -81.538  55.140   -51.907 1.00 200.74 ? 148 GLN D NE2 1 
ATOM   5959  N N   . TRP D 4 149 ? -86.628  51.572   -54.162 1.00 180.81 ? 149 TRP D N   1 
ATOM   5960  C CA  . TRP D 4 149 ? -87.775  51.740   -55.061 1.00 180.78 ? 149 TRP D CA  1 
ATOM   5961  C C   . TRP D 4 149 ? -88.154  53.213   -55.232 1.00 185.69 ? 149 TRP D C   1 
ATOM   5962  O O   . TRP D 4 149 ? -88.498  53.881   -54.255 1.00 185.38 ? 149 TRP D O   1 
ATOM   5963  C CB  . TRP D 4 149 ? -88.985  50.924   -54.581 1.00 179.23 ? 149 TRP D CB  1 
ATOM   5964  C CG  . TRP D 4 149 ? -88.934  49.461   -54.920 1.00 179.85 ? 149 TRP D CG  1 
ATOM   5965  C CD1 . TRP D 4 149 ? -88.600  48.439   -54.083 1.00 182.81 ? 149 TRP D CD1 1 
ATOM   5966  C CD2 . TRP D 4 149 ? -89.295  48.856   -56.167 1.00 179.53 ? 149 TRP D CD2 1 
ATOM   5967  N NE1 . TRP D 4 149 ? -88.723  47.233   -54.732 1.00 181.95 ? 149 TRP D NE1 1 
ATOM   5968  C CE2 . TRP D 4 149 ? -89.138  47.460   -56.016 1.00 183.16 ? 149 TRP D CE2 1 
ATOM   5969  C CE3 . TRP D 4 149 ? -89.718  49.358   -57.407 1.00 180.67 ? 149 TRP D CE3 1 
ATOM   5970  C CZ2 . TRP D 4 149 ? -89.402  46.562   -57.052 1.00 182.24 ? 149 TRP D CZ2 1 
ATOM   5971  C CZ3 . TRP D 4 149 ? -89.968  48.465   -58.437 1.00 181.99 ? 149 TRP D CZ3 1 
ATOM   5972  C CH2 . TRP D 4 149 ? -89.801  47.086   -58.257 1.00 182.49 ? 149 TRP D CH2 1 
ATOM   5973  N N   . LYS D 4 150 ? -88.079  53.711   -56.478 1.00 182.76 ? 150 LYS D N   1 
ATOM   5974  C CA  . LYS D 4 150 ? -88.398  55.095   -56.838 1.00 182.55 ? 150 LYS D CA  1 
ATOM   5975  C C   . LYS D 4 150 ? -89.674  55.173   -57.680 1.00 186.01 ? 150 LYS D C   1 
ATOM   5976  O O   . LYS D 4 150 ? -89.682  54.768   -58.847 1.00 185.36 ? 150 LYS D O   1 
ATOM   5977  C CB  . LYS D 4 150 ? -87.212  55.773   -57.555 1.00 185.14 ? 150 LYS D CB  1 
ATOM   5978  C CG  . LYS D 4 150 ? -86.018  56.054   -56.652 1.00 199.80 ? 150 LYS D CG  1 
ATOM   5979  C CD  . LYS D 4 150 ? -84.858  56.659   -57.420 1.00 209.19 ? 150 LYS D CD  1 
ATOM   5980  C CE  . LYS D 4 150 ? -83.680  56.945   -56.523 1.00 219.08 ? 150 LYS D CE  1 
ATOM   5981  N NZ  . LYS D 4 150 ? -82.574  57.592   -57.274 1.00 227.65 ? 150 LYS D NZ  1 
ATOM   5982  N N   . VAL D 4 151 ? -90.758  55.676   -57.066 1.00 182.44 ? 151 VAL D N   1 
ATOM   5983  C CA  . VAL D 4 151 ? -92.061  55.862   -57.710 1.00 182.07 ? 151 VAL D CA  1 
ATOM   5984  C C   . VAL D 4 151 ? -92.191  57.365   -57.986 1.00 185.62 ? 151 VAL D C   1 
ATOM   5985  O O   . VAL D 4 151 ? -92.544  58.133   -57.083 1.00 185.56 ? 151 VAL D O   1 
ATOM   5986  C CB  . VAL D 4 151 ? -93.224  55.276   -56.855 1.00 185.90 ? 151 VAL D CB  1 
ATOM   5987  C CG1 . VAL D 4 151 ? -94.588  55.593   -57.462 1.00 185.69 ? 151 VAL D CG1 1 
ATOM   5988  C CG2 . VAL D 4 151 ? -93.062  53.772   -56.670 1.00 185.56 ? 151 VAL D CG2 1 
ATOM   5989  N N   . ASP D 4 152 ? -91.834  57.778   -59.228 1.00 181.27 ? 152 ASP D N   1 
ATOM   5990  C CA  . ASP D 4 152 ? -91.833  59.166   -59.716 1.00 180.60 ? 152 ASP D CA  1 
ATOM   5991  C C   . ASP D 4 152 ? -90.973  60.074   -58.799 1.00 183.83 ? 152 ASP D C   1 
ATOM   5992  O O   . ASP D 4 152 ? -91.510  60.953   -58.114 1.00 183.51 ? 152 ASP D O   1 
ATOM   5993  C CB  . ASP D 4 152 ? -93.278  59.706   -59.908 1.00 182.27 ? 152 ASP D CB  1 
ATOM   5994  C CG  . ASP D 4 152 ? -94.176  58.861   -60.795 1.00 188.18 ? 152 ASP D CG  1 
ATOM   5995  O OD1 . ASP D 4 152 ? -94.372  57.670   -60.479 1.00 188.35 ? 152 ASP D OD1 1 
ATOM   5996  O OD2 . ASP D 4 152 ? -94.737  59.411   -61.766 1.00 191.78 ? 152 ASP D OD2 1 
ATOM   5997  N N   . ASN D 4 153 ? -89.638  59.804   -58.751 1.00 179.71 ? 153 ASN D N   1 
ATOM   5998  C CA  . ASN D 4 153 ? -88.600  60.476   -57.934 1.00 179.24 ? 153 ASN D CA  1 
ATOM   5999  C C   . ASN D 4 153 ? -88.741  60.195   -56.427 1.00 183.13 ? 153 ASN D C   1 
ATOM   6000  O O   . ASN D 4 153 ? -87.728  60.105   -55.725 1.00 182.23 ? 153 ASN D O   1 
ATOM   6001  C CB  . ASN D 4 153 ? -88.507  61.995   -58.216 1.00 179.54 ? 153 ASN D CB  1 
ATOM   6002  C CG  . ASN D 4 153 ? -87.351  62.698   -57.535 1.00 200.36 ? 153 ASN D CG  1 
ATOM   6003  O OD1 . ASN D 4 153 ? -87.422  63.092   -56.366 1.00 193.82 ? 153 ASN D OD1 1 
ATOM   6004  N ND2 . ASN D 4 153 ? -86.261  62.875   -58.256 1.00 192.07 ? 153 ASN D ND2 1 
ATOM   6005  N N   . ALA D 4 154 ? -89.992  60.074   -55.939 1.00 180.36 ? 154 ALA D N   1 
ATOM   6006  C CA  . ALA D 4 154 ? -90.322  59.809   -54.542 1.00 180.51 ? 154 ALA D CA  1 
ATOM   6007  C C   . ALA D 4 154 ? -89.945  58.382   -54.152 1.00 183.57 ? 154 ALA D C   1 
ATOM   6008  O O   . ALA D 4 154 ? -90.571  57.415   -54.600 1.00 182.72 ? 154 ALA D O   1 
ATOM   6009  C CB  . ALA D 4 154 ? -91.802  60.069   -54.290 1.00 181.64 ? 154 ALA D CB  1 
ATOM   6010  N N   . LEU D 4 155 ? -88.884  58.266   -53.341 1.00 180.07 ? 155 LEU D N   1 
ATOM   6011  C CA  . LEU D 4 155 ? -88.357  56.998   -52.846 1.00 179.91 ? 155 LEU D CA  1 
ATOM   6012  C C   . LEU D 4 155 ? -89.355  56.379   -51.860 1.00 183.96 ? 155 LEU D C   1 
ATOM   6013  O O   . LEU D 4 155 ? -89.717  57.014   -50.862 1.00 183.86 ? 155 LEU D O   1 
ATOM   6014  C CB  . LEU D 4 155 ? -86.964  57.193   -52.204 1.00 179.82 ? 155 LEU D CB  1 
ATOM   6015  C CG  . LEU D 4 155 ? -85.801  57.471   -53.171 1.00 184.02 ? 155 LEU D CG  1 
ATOM   6016  C CD1 . LEU D 4 155 ? -85.514  58.966   -53.292 1.00 183.65 ? 155 LEU D CD1 1 
ATOM   6017  C CD2 . LEU D 4 155 ? -84.549  56.737   -52.737 1.00 186.31 ? 155 LEU D CD2 1 
ATOM   6018  N N   . GLN D 4 156 ? -89.847  55.168   -52.186 1.00 180.01 ? 156 GLN D N   1 
ATOM   6019  C CA  . GLN D 4 156 ? -90.837  54.441   -51.391 1.00 179.52 ? 156 GLN D CA  1 
ATOM   6020  C C   . GLN D 4 156 ? -90.216  53.420   -50.453 1.00 182.82 ? 156 GLN D C   1 
ATOM   6021  O O   . GLN D 4 156 ? -89.315  52.676   -50.845 1.00 182.13 ? 156 GLN D O   1 
ATOM   6022  C CB  . GLN D 4 156 ? -91.902  53.781   -52.287 1.00 180.62 ? 156 GLN D CB  1 
ATOM   6023  C CG  . GLN D 4 156 ? -92.745  54.764   -53.107 1.00 191.92 ? 156 GLN D CG  1 
ATOM   6024  C CD  . GLN D 4 156 ? -93.572  55.730   -52.289 1.00 207.39 ? 156 GLN D CD  1 
ATOM   6025  O OE1 . GLN D 4 156 ? -94.222  55.368   -51.301 1.00 201.51 ? 156 GLN D OE1 1 
ATOM   6026  N NE2 . GLN D 4 156 ? -93.594  56.983   -52.714 1.00 199.17 ? 156 GLN D NE2 1 
ATOM   6027  N N   . SER D 4 157 ? -90.719  53.388   -49.212 1.00 195.68 ? 157 SER D N   1 
ATOM   6028  C CA  . SER D 4 157 ? -90.271  52.485   -48.156 1.00 192.21 ? 157 SER D CA  1 
ATOM   6029  C C   . SER D 4 157 ? -91.477  51.895   -47.419 1.00 196.63 ? 157 SER D C   1 
ATOM   6030  O O   . SER D 4 157 ? -92.485  52.584   -47.233 1.00 199.88 ? 157 SER D O   1 
ATOM   6031  C CB  . SER D 4 157 ? -89.366  53.228   -47.178 1.00 195.14 ? 157 SER D CB  1 
ATOM   6032  O OG  . SER D 4 157 ? -88.743  52.334   -46.270 1.00 201.15 ? 157 SER D OG  1 
ATOM   6033  N N   . GLY D 4 158 ? -91.356  50.629   -47.015 1.00 189.61 ? 158 GLY D N   1 
ATOM   6034  C CA  . GLY D 4 158 ? -92.396  49.902   -46.291 1.00 189.40 ? 158 GLY D CA  1 
ATOM   6035  C C   . GLY D 4 158 ? -93.151  48.909   -47.149 1.00 191.51 ? 158 GLY D C   1 
ATOM   6036  O O   . GLY D 4 158 ? -93.280  47.736   -46.778 1.00 189.34 ? 158 GLY D O   1 
ATOM   6037  N N   . ASN D 4 159 ? -93.659  49.387   -48.304 1.00 188.70 ? 159 ASN D N   1 
ATOM   6038  C CA  . ASN D 4 159 ? -94.391  48.601   -49.302 1.00 188.46 ? 159 ASN D CA  1 
ATOM   6039  C C   . ASN D 4 159 ? -93.496  47.520   -49.920 1.00 187.24 ? 159 ASN D C   1 
ATOM   6040  O O   . ASN D 4 159 ? -93.985  46.447   -50.282 1.00 186.40 ? 159 ASN D O   1 
ATOM   6041  C CB  . ASN D 4 159 ? -94.951  49.516   -50.397 1.00 191.51 ? 159 ASN D CB  1 
ATOM   6042  C CG  . ASN D 4 159 ? -94.036  50.647   -50.817 1.00 208.57 ? 159 ASN D CG  1 
ATOM   6043  O OD1 . ASN D 4 159 ? -92.810  50.510   -50.905 1.00 196.89 ? 159 ASN D OD1 1 
ATOM   6044  N ND2 . ASN D 4 159 ? -94.619  51.806   -51.062 1.00 204.09 ? 159 ASN D ND2 1 
ATOM   6045  N N   . SER D 4 160 ? -92.184  47.809   -50.020 1.00 179.96 ? 160 SER D N   1 
ATOM   6046  C CA  . SER D 4 160 ? -91.163  46.915   -50.557 1.00 175.54 ? 160 SER D CA  1 
ATOM   6047  C C   . SER D 4 160 ? -90.774  45.817   -49.569 1.00 175.12 ? 160 SER D C   1 
ATOM   6048  O O   . SER D 4 160 ? -90.648  46.074   -48.369 1.00 174.64 ? 160 SER D O   1 
ATOM   6049  C CB  . SER D 4 160 ? -89.923  47.707   -50.957 1.00 177.51 ? 160 SER D CB  1 
ATOM   6050  O OG  . SER D 4 160 ? -89.359  48.396   -49.853 1.00 184.38 ? 160 SER D OG  1 
ATOM   6051  N N   . GLN D 4 161 ? -90.573  44.596   -50.087 1.00 168.40 ? 161 GLN D N   1 
ATOM   6052  C CA  . GLN D 4 161 ? -90.144  43.415   -49.331 1.00 165.15 ? 161 GLN D CA  1 
ATOM   6053  C C   . GLN D 4 161 ? -89.001  42.756   -50.111 1.00 166.21 ? 161 GLN D C   1 
ATOM   6054  O O   . GLN D 4 161 ? -89.124  42.567   -51.322 1.00 166.33 ? 161 GLN D O   1 
ATOM   6055  C CB  . GLN D 4 161 ? -91.315  42.439   -49.113 1.00 166.94 ? 161 GLN D CB  1 
ATOM   6056  C CG  . GLN D 4 161 ? -92.312  42.905   -48.047 1.00 178.02 ? 161 GLN D CG  1 
ATOM   6057  C CD  . GLN D 4 161 ? -93.620  42.152   -48.089 1.00 192.47 ? 161 GLN D CD  1 
ATOM   6058  O OE1 . GLN D 4 161 ? -93.664  40.919   -48.030 1.00 185.10 ? 161 GLN D OE1 1 
ATOM   6059  N NE2 . GLN D 4 161 ? -94.725  42.881   -48.146 1.00 185.42 ? 161 GLN D NE2 1 
ATOM   6060  N N   . GLU D 4 162 ? -87.874  42.459   -49.438 1.00 159.82 ? 162 GLU D N   1 
ATOM   6061  C CA  . GLU D 4 162 ? -86.693  41.876   -50.087 1.00 156.92 ? 162 GLU D CA  1 
ATOM   6062  C C   . GLU D 4 162 ? -86.461  40.399   -49.758 1.00 156.49 ? 162 GLU D C   1 
ATOM   6063  O O   . GLU D 4 162 ? -86.812  39.937   -48.670 1.00 156.08 ? 162 GLU D O   1 
ATOM   6064  C CB  . GLU D 4 162 ? -85.432  42.708   -49.784 1.00 157.90 ? 162 GLU D CB  1 
ATOM   6065  C CG  . GLU D 4 162 ? -85.274  43.944   -50.657 1.00 172.11 ? 162 GLU D CG  1 
ATOM   6066  C CD  . GLU D 4 162 ? -84.063  44.808   -50.351 1.00 197.67 ? 162 GLU D CD  1 
ATOM   6067  O OE1 . GLU D 4 162 ? -82.922  44.311   -50.492 1.00 187.14 ? 162 GLU D OE1 1 
ATOM   6068  O OE2 . GLU D 4 162 ? -84.254  45.993   -49.995 1.00 198.08 ? 162 GLU D OE2 1 
ATOM   6069  N N   . SER D 4 163 ? -85.857  39.667   -50.717 1.00 149.67 ? 163 SER D N   1 
ATOM   6070  C CA  . SER D 4 163 ? -85.499  38.250   -50.610 1.00 147.12 ? 163 SER D CA  1 
ATOM   6071  C C   . SER D 4 163 ? -84.211  37.961   -51.393 1.00 148.37 ? 163 SER D C   1 
ATOM   6072  O O   . SER D 4 163 ? -83.973  38.582   -52.430 1.00 148.00 ? 163 SER D O   1 
ATOM   6073  C CB  . SER D 4 163 ? -86.633  37.367   -51.115 1.00 150.59 ? 163 SER D CB  1 
ATOM   6074  O OG  . SER D 4 163 ? -86.355  36.008   -50.826 1.00 156.95 ? 163 SER D OG  1 
ATOM   6075  N N   . VAL D 4 164 ? -83.378  37.035   -50.887 1.00 143.22 ? 164 VAL D N   1 
ATOM   6076  C CA  . VAL D 4 164 ? -82.096  36.662   -51.504 1.00 141.65 ? 164 VAL D CA  1 
ATOM   6077  C C   . VAL D 4 164 ? -81.835  35.169   -51.486 1.00 144.45 ? 164 VAL D C   1 
ATOM   6078  O O   . VAL D 4 164 ? -82.146  34.492   -50.502 1.00 144.65 ? 164 VAL D O   1 
ATOM   6079  C CB  . VAL D 4 164 ? -80.864  37.416   -50.930 1.00 145.46 ? 164 VAL D CB  1 
ATOM   6080  C CG1 . VAL D 4 164 ? -80.654  38.750   -51.616 1.00 145.62 ? 164 VAL D CG1 1 
ATOM   6081  C CG2 . VAL D 4 164 ? -80.930  37.571   -49.408 1.00 145.98 ? 164 VAL D CG2 1 
ATOM   6082  N N   . THR D 4 165 ? -81.204  34.671   -52.557 1.00 139.50 ? 165 THR D N   1 
ATOM   6083  C CA  . THR D 4 165 ? -80.795  33.271   -52.680 1.00 138.45 ? 165 THR D CA  1 
ATOM   6084  C C   . THR D 4 165 ? -79.349  33.158   -52.229 1.00 140.60 ? 165 THR D C   1 
ATOM   6085  O O   . THR D 4 165 ? -78.588  34.118   -52.366 1.00 140.26 ? 165 THR D O   1 
ATOM   6086  C CB  . THR D 4 165 ? -80.937  32.767   -54.125 1.00 149.59 ? 165 THR D CB  1 
ATOM   6087  O OG1 . THR D 4 165 ? -80.284  33.674   -55.019 1.00 150.22 ? 165 THR D OG1 1 
ATOM   6088  C CG2 . THR D 4 165 ? -82.390  32.550   -54.536 1.00 149.56 ? 165 THR D CG2 1 
ATOM   6089  N N   . GLU D 4 166 ? -78.956  31.980   -51.723 1.00 136.21 ? 166 GLU D N   1 
ATOM   6090  C CA  . GLU D 4 166 ? -77.587  31.717   -51.278 1.00 135.89 ? 166 GLU D CA  1 
ATOM   6091  C C   . GLU D 4 166 ? -76.577  31.712   -52.444 1.00 137.92 ? 166 GLU D C   1 
ATOM   6092  O O   . GLU D 4 166 ? -76.960  31.906   -53.605 1.00 136.48 ? 166 GLU D O   1 
ATOM   6093  C CB  . GLU D 4 166 ? -77.529  30.411   -50.466 1.00 137.79 ? 166 GLU D CB  1 
ATOM   6094  C CG  . GLU D 4 166 ? -77.476  30.637   -48.964 1.00 152.61 ? 166 GLU D CG  1 
ATOM   6095  C CD  . GLU D 4 166 ? -78.790  30.877   -48.239 1.00 180.66 ? 166 GLU D CD  1 
ATOM   6096  O OE1 . GLU D 4 166 ? -79.538  31.803   -48.631 1.00 178.37 ? 166 GLU D OE1 1 
ATOM   6097  O OE2 . GLU D 4 166 ? -79.034  30.180   -47.226 1.00 176.92 ? 166 GLU D OE2 1 
ATOM   6098  N N   . GLN D 4 167 ? -75.286  31.517   -52.121 1.00 133.90 ? 167 GLN D N   1 
ATOM   6099  C CA  . GLN D 4 167 ? -74.189  31.471   -53.090 1.00 132.86 ? 167 GLN D CA  1 
ATOM   6100  C C   . GLN D 4 167 ? -74.402  30.323   -54.080 1.00 134.63 ? 167 GLN D C   1 
ATOM   6101  O O   . GLN D 4 167 ? -74.730  29.207   -53.667 1.00 134.86 ? 167 GLN D O   1 
ATOM   6102  C CB  . GLN D 4 167 ? -72.839  31.326   -52.360 1.00 135.22 ? 167 GLN D CB  1 
ATOM   6103  C CG  . GLN D 4 167 ? -71.680  32.001   -53.089 1.00 139.53 ? 167 GLN D CG  1 
ATOM   6104  C CD  . GLN D 4 167 ? -70.357  31.927   -52.363 1.00 150.78 ? 167 GLN D CD  1 
ATOM   6105  O OE1 . GLN D 4 167 ? -70.077  31.003   -51.592 1.00 147.08 ? 167 GLN D OE1 1 
ATOM   6106  N NE2 . GLN D 4 167 ? -69.490  32.884   -52.644 1.00 138.61 ? 167 GLN D NE2 1 
ATOM   6107  N N   . ASP D 4 168 ? -74.265  30.611   -55.382 1.00 129.09 ? 168 ASP D N   1 
ATOM   6108  C CA  . ASP D 4 168 ? -74.456  29.616   -56.437 1.00 127.92 ? 168 ASP D CA  1 
ATOM   6109  C C   . ASP D 4 168 ? -73.376  28.528   -56.418 1.00 131.86 ? 168 ASP D C   1 
ATOM   6110  O O   . ASP D 4 168 ? -72.209  28.821   -56.167 1.00 132.26 ? 168 ASP D O   1 
ATOM   6111  C CB  . ASP D 4 168 ? -74.525  30.290   -57.806 1.00 128.93 ? 168 ASP D CB  1 
ATOM   6112  C CG  . ASP D 4 168 ? -75.262  29.464   -58.830 1.00 139.67 ? 168 ASP D CG  1 
ATOM   6113  O OD1 . ASP D 4 168 ? -76.482  29.664   -58.982 1.00 140.75 ? 168 ASP D OD1 1 
ATOM   6114  O OD2 . ASP D 4 168 ? -74.617  28.621   -59.487 1.00 146.05 ? 168 ASP D OD2 1 
ATOM   6115  N N   . SER D 4 169 ? -73.778  27.271   -56.661 1.00 127.89 ? 169 SER D N   1 
ATOM   6116  C CA  . SER D 4 169 ? -72.881  26.113   -56.680 1.00 128.55 ? 169 SER D CA  1 
ATOM   6117  C C   . SER D 4 169 ? -71.919  26.147   -57.872 1.00 132.77 ? 169 SER D C   1 
ATOM   6118  O O   . SER D 4 169 ? -70.775  25.697   -57.767 1.00 133.11 ? 169 SER D O   1 
ATOM   6119  C CB  . SER D 4 169 ? -73.691  24.819   -56.710 1.00 131.17 ? 169 SER D CB  1 
ATOM   6120  O OG  . SER D 4 169 ? -74.489  24.716   -57.880 1.00 135.24 ? 169 SER D OG  1 
ATOM   6121  N N   . LYS D 4 170 ? -72.392  26.678   -59.008 1.00 128.85 ? 170 LYS D N   1 
ATOM   6122  C CA  . LYS D 4 170 ? -71.624  26.724   -60.245 1.00 128.65 ? 170 LYS D CA  1 
ATOM   6123  C C   . LYS D 4 170 ? -70.770  27.972   -60.399 1.00 133.34 ? 170 LYS D C   1 
ATOM   6124  O O   . LYS D 4 170 ? -69.587  27.830   -60.706 1.00 134.63 ? 170 LYS D O   1 
ATOM   6125  C CB  . LYS D 4 170 ? -72.534  26.522   -61.482 1.00 129.45 ? 170 LYS D CB  1 
ATOM   6126  C CG  . LYS D 4 170 ? -73.485  25.320   -61.393 1.00 139.06 ? 170 LYS D CG  1 
ATOM   6127  C CD  . LYS D 4 170 ? -73.212  24.228   -62.448 1.00 145.04 ? 170 LYS D CD  1 
ATOM   6128  C CE  . LYS D 4 170 ? -73.907  22.932   -62.101 1.00 151.25 ? 170 LYS D CE  1 
ATOM   6129  N NZ  . LYS D 4 170 ? -73.448  21.816   -62.962 1.00 157.73 ? 170 LYS D NZ  1 
ATOM   6130  N N   . ASP D 4 171 ? -71.345  29.183   -60.207 1.00 128.83 ? 171 ASP D N   1 
ATOM   6131  C CA  . ASP D 4 171 ? -70.593  30.432   -60.413 1.00 128.86 ? 171 ASP D CA  1 
ATOM   6132  C C   . ASP D 4 171 ? -70.407  31.336   -59.173 1.00 131.38 ? 171 ASP D C   1 
ATOM   6133  O O   . ASP D 4 171 ? -69.928  32.463   -59.326 1.00 130.90 ? 171 ASP D O   1 
ATOM   6134  C CB  . ASP D 4 171 ? -71.204  31.243   -61.566 1.00 130.32 ? 171 ASP D CB  1 
ATOM   6135  C CG  . ASP D 4 171 ? -72.620  31.731   -61.343 1.00 142.43 ? 171 ASP D CG  1 
ATOM   6136  O OD1 . ASP D 4 171 ? -73.450  30.943   -60.850 1.00 141.77 ? 171 ASP D OD1 1 
ATOM   6137  O OD2 . ASP D 4 171 ? -72.919  32.872   -61.743 1.00 152.33 ? 171 ASP D OD2 1 
ATOM   6138  N N   . SER D 4 172 ? -70.727  30.836   -57.963 1.00 127.58 ? 172 SER D N   1 
ATOM   6139  C CA  . SER D 4 172 ? -70.568  31.530   -56.675 1.00 127.83 ? 172 SER D CA  1 
ATOM   6140  C C   . SER D 4 172 ? -71.155  32.967   -56.642 1.00 131.03 ? 172 SER D C   1 
ATOM   6141  O O   . SER D 4 172 ? -70.544  33.870   -56.063 1.00 131.27 ? 172 SER D O   1 
ATOM   6142  C CB  . SER D 4 172 ? -69.102  31.518   -56.235 1.00 132.42 ? 172 SER D CB  1 
ATOM   6143  O OG  . SER D 4 172 ? -68.573  30.203   -56.207 1.00 140.12 ? 172 SER D OG  1 
ATOM   6144  N N   . THR D 4 173 ? -72.345  33.170   -57.245 1.00 126.60 ? 173 THR D N   1 
ATOM   6145  C CA  . THR D 4 173 ? -73.013  34.478   -57.297 1.00 126.15 ? 173 THR D CA  1 
ATOM   6146  C C   . THR D 4 173 ? -74.415  34.468   -56.688 1.00 130.12 ? 173 THR D C   1 
ATOM   6147  O O   . THR D 4 173 ? -75.206  33.547   -56.925 1.00 129.05 ? 173 THR D O   1 
ATOM   6148  C CB  . THR D 4 173 ? -73.082  35.008   -58.724 1.00 132.46 ? 173 THR D CB  1 
ATOM   6149  O OG1 . THR D 4 173 ? -73.782  34.060   -59.520 1.00 128.98 ? 173 THR D OG1 1 
ATOM   6150  C CG2 . THR D 4 173 ? -71.718  35.307   -59.315 1.00 132.49 ? 173 THR D CG2 1 
ATOM   6151  N N   . TYR D 4 174 ? -74.725  35.541   -55.949 1.00 127.46 ? 174 TYR D N   1 
ATOM   6152  C CA  . TYR D 4 174 ? -75.998  35.769   -55.256 1.00 127.20 ? 174 TYR D CA  1 
ATOM   6153  C C   . TYR D 4 174 ? -77.006  36.488   -56.167 1.00 132.10 ? 174 TYR D C   1 
ATOM   6154  O O   . TYR D 4 174 ? -76.608  37.107   -57.147 1.00 131.77 ? 174 TYR D O   1 
ATOM   6155  C CB  . TYR D 4 174 ? -75.758  36.596   -53.967 1.00 128.21 ? 174 TYR D CB  1 
ATOM   6156  C CG  . TYR D 4 174 ? -74.729  36.001   -53.029 1.00 128.91 ? 174 TYR D CG  1 
ATOM   6157  C CD1 . TYR D 4 174 ? -75.099  35.093   -52.043 1.00 130.41 ? 174 TYR D CD1 1 
ATOM   6158  C CD2 . TYR D 4 174 ? -73.385  36.354   -53.121 1.00 130.28 ? 174 TYR D CD2 1 
ATOM   6159  C CE1 . TYR D 4 174 ? -74.159  34.553   -51.169 1.00 131.43 ? 174 TYR D CE1 1 
ATOM   6160  C CE2 . TYR D 4 174 ? -72.433  35.809   -52.261 1.00 131.88 ? 174 TYR D CE2 1 
ATOM   6161  C CZ  . TYR D 4 174 ? -72.825  34.907   -51.289 1.00 138.84 ? 174 TYR D CZ  1 
ATOM   6162  O OH  . TYR D 4 174 ? -71.891  34.366   -50.445 1.00 141.65 ? 174 TYR D OH  1 
ATOM   6163  N N   . SER D 4 175 ? -78.304  36.409   -55.834 1.00 129.67 ? 175 SER D N   1 
ATOM   6164  C CA  . SER D 4 175 ? -79.382  37.056   -56.585 1.00 130.64 ? 175 SER D CA  1 
ATOM   6165  C C   . SER D 4 175 ? -80.415  37.675   -55.631 1.00 137.00 ? 175 SER D C   1 
ATOM   6166  O O   . SER D 4 175 ? -80.701  37.086   -54.587 1.00 137.07 ? 175 SER D O   1 
ATOM   6167  C CB  . SER D 4 175 ? -80.051  36.064   -57.530 1.00 133.77 ? 175 SER D CB  1 
ATOM   6168  O OG  . SER D 4 175 ? -79.104  35.370   -58.326 1.00 142.01 ? 175 SER D OG  1 
ATOM   6169  N N   . LEU D 4 176 ? -80.981  38.849   -55.986 1.00 134.97 ? 176 LEU D N   1 
ATOM   6170  C CA  . LEU D 4 176 ? -81.980  39.553   -55.163 1.00 136.01 ? 176 LEU D CA  1 
ATOM   6171  C C   . LEU D 4 176 ? -83.305  39.737   -55.904 1.00 141.76 ? 176 LEU D C   1 
ATOM   6172  O O   . LEU D 4 176 ? -83.313  39.941   -57.117 1.00 142.12 ? 176 LEU D O   1 
ATOM   6173  C CB  . LEU D 4 176 ? -81.439  40.925   -54.696 1.00 136.84 ? 176 LEU D CB  1 
ATOM   6174  C CG  . LEU D 4 176 ? -82.115  41.587   -53.480 1.00 142.53 ? 176 LEU D CG  1 
ATOM   6175  C CD1 . LEU D 4 176 ? -81.103  42.329   -52.637 1.00 142.66 ? 176 LEU D CD1 1 
ATOM   6176  C CD2 . LEU D 4 176 ? -83.215  42.551   -53.897 1.00 146.98 ? 176 LEU D CD2 1 
ATOM   6177  N N   . SER D 4 177 ? -84.417  39.696   -55.154 1.00 139.72 ? 177 SER D N   1 
ATOM   6178  C CA  . SER D 4 177 ? -85.773  39.902   -55.658 1.00 141.74 ? 177 SER D CA  1 
ATOM   6179  C C   . SER D 4 177 ? -86.546  40.802   -54.685 1.00 148.64 ? 177 SER D C   1 
ATOM   6180  O O   . SER D 4 177 ? -86.908  40.363   -53.590 1.00 148.69 ? 177 SER D O   1 
ATOM   6181  C CB  . SER D 4 177 ? -86.483  38.565   -55.861 1.00 144.50 ? 177 SER D CB  1 
ATOM   6182  O OG  . SER D 4 177 ? -87.873  38.724   -56.088 1.00 154.12 ? 177 SER D OG  1 
ATOM   6183  N N   . SER D 4 178 ? -86.762  42.072   -55.073 1.00 147.04 ? 178 SER D N   1 
ATOM   6184  C CA  . SER D 4 178 ? -87.500  43.042   -54.262 1.00 148.82 ? 178 SER D CA  1 
ATOM   6185  C C   . SER D 4 178 ? -88.918  43.187   -54.818 1.00 156.08 ? 178 SER D C   1 
ATOM   6186  O O   . SER D 4 178 ? -89.083  43.459   -56.007 1.00 156.87 ? 178 SER D O   1 
ATOM   6187  C CB  . SER D 4 178 ? -86.777  44.385   -54.228 1.00 152.27 ? 178 SER D CB  1 
ATOM   6188  O OG  . SER D 4 178 ? -87.264  45.200   -53.175 1.00 160.26 ? 178 SER D OG  1 
ATOM   6189  N N   . THR D 4 179 ? -89.935  42.958   -53.970 1.00 154.28 ? 179 THR D N   1 
ATOM   6190  C CA  . THR D 4 179 ? -91.347  43.012   -54.358 1.00 157.27 ? 179 THR D CA  1 
ATOM   6191  C C   . THR D 4 179 ? -92.031  44.270   -53.813 1.00 165.93 ? 179 THR D C   1 
ATOM   6192  O O   . THR D 4 179 ? -92.068  44.471   -52.597 1.00 165.41 ? 179 THR D O   1 
ATOM   6193  C CB  . THR D 4 179 ? -92.059  41.702   -53.968 1.00 161.36 ? 179 THR D CB  1 
ATOM   6194  O OG1 . THR D 4 179 ? -91.255  40.590   -54.371 1.00 156.87 ? 179 THR D OG1 1 
ATOM   6195  C CG2 . THR D 4 179 ? -93.449  41.580   -54.579 1.00 161.93 ? 179 THR D CG2 1 
ATOM   6196  N N   . LEU D 4 180 ? -92.581  45.100   -54.724 1.00 166.60 ? 180 LEU D N   1 
ATOM   6197  C CA  . LEU D 4 180 ? -93.273  46.352   -54.406 1.00 170.27 ? 180 LEU D CA  1 
ATOM   6198  C C   . LEU D 4 180 ? -94.802  46.162   -54.379 1.00 178.22 ? 180 LEU D C   1 
ATOM   6199  O O   . LEU D 4 180 ? -95.480  46.410   -55.382 1.00 180.59 ? 180 LEU D O   1 
ATOM   6200  C CB  . LEU D 4 180 ? -92.845  47.464   -55.391 1.00 171.88 ? 180 LEU D CB  1 
ATOM   6201  C CG  . LEU D 4 180 ? -93.325  48.892   -55.100 1.00 180.07 ? 180 LEU D CG  1 
ATOM   6202  C CD1 . LEU D 4 180 ? -92.473  49.561   -54.041 1.00 178.81 ? 180 LEU D CD1 1 
ATOM   6203  C CD2 . LEU D 4 180 ? -93.301  49.724   -56.350 1.00 184.63 ? 180 LEU D CD2 1 
ATOM   6204  N N   . THR D 4 181 ? -95.333  45.718   -53.218 1.00 175.00 ? 181 THR D N   1 
ATOM   6205  C CA  . THR D 4 181 ? -96.765  45.480   -52.995 1.00 177.98 ? 181 THR D CA  1 
ATOM   6206  C C   . THR D 4 181 ? -97.527  46.813   -52.892 1.00 186.75 ? 181 THR D C   1 
ATOM   6207  O O   . THR D 4 181 ? -97.267  47.595   -51.973 1.00 186.03 ? 181 THR D O   1 
ATOM   6208  C CB  . THR D 4 181 ? -97.001  44.543   -51.784 1.00 182.57 ? 181 THR D CB  1 
ATOM   6209  O OG1 . THR D 4 181 ? -96.313  45.053   -50.640 1.00 180.09 ? 181 THR D OG1 1 
ATOM   6210  C CG2 . THR D 4 181 ? -96.569  43.101   -52.050 1.00 176.51 ? 181 THR D CG2 1 
ATOM   6211  N N   . LEU D 4 182 ? -98.448  47.073   -53.854 1.00 185.48 ? 182 LEU D N   1 
ATOM   6212  C CA  . LEU D 4 182 ? -99.263  48.297   -53.932 1.00 186.22 ? 182 LEU D CA  1 
ATOM   6213  C C   . LEU D 4 182 ? -100.704 48.057   -54.410 1.00 191.95 ? 182 LEU D C   1 
ATOM   6214  O O   . LEU D 4 182 ? -100.955 47.125   -55.175 1.00 192.10 ? 182 LEU D O   1 
ATOM   6215  C CB  . LEU D 4 182 ? -98.589  49.336   -54.856 1.00 185.13 ? 182 LEU D CB  1 
ATOM   6216  C CG  . LEU D 4 182 ? -98.141  50.684   -54.254 1.00 189.27 ? 182 LEU D CG  1 
ATOM   6217  C CD1 . LEU D 4 182 ? -99.248  51.366   -53.443 1.00 190.78 ? 182 LEU D CD1 1 
ATOM   6218  C CD2 . LEU D 4 182 ? -96.855  50.549   -53.457 1.00 190.81 ? 182 LEU D CD2 1 
ATOM   6219  N N   . SER D 4 183 ? -101.640 48.924   -53.981 1.00 189.82 ? 183 SER D N   1 
ATOM   6220  C CA  . SER D 4 183 ? -103.050 48.856   -54.372 1.00 192.21 ? 183 SER D CA  1 
ATOM   6221  C C   . SER D 4 183 ? -103.237 49.414   -55.787 1.00 196.96 ? 183 SER D C   1 
ATOM   6222  O O   . SER D 4 183 ? -102.417 50.218   -56.236 1.00 194.90 ? 183 SER D O   1 
ATOM   6223  C CB  . SER D 4 183 ? -103.916 49.632   -53.384 1.00 196.90 ? 183 SER D CB  1 
ATOM   6224  O OG  . SER D 4 183 ? -103.559 51.004   -53.347 1.00 205.36 ? 183 SER D OG  1 
ATOM   6225  N N   . LYS D 4 184 ? -104.320 48.995   -56.484 1.00 196.11 ? 184 LYS D N   1 
ATOM   6226  C CA  . LYS D 4 184 ? -104.644 49.448   -57.844 1.00 196.22 ? 184 LYS D CA  1 
ATOM   6227  C C   . LYS D 4 184 ? -105.028 50.936   -57.867 1.00 199.93 ? 184 LYS D C   1 
ATOM   6228  O O   . LYS D 4 184 ? -104.743 51.620   -58.853 1.00 198.52 ? 184 LYS D O   1 
ATOM   6229  C CB  . LYS D 4 184 ? -105.759 48.586   -58.466 1.00 201.08 ? 184 LYS D CB  1 
ATOM   6230  C CG  . LYS D 4 184 ? -105.752 48.588   -59.992 1.00 212.02 ? 184 LYS D CG  1 
ATOM   6231  C CD  . LYS D 4 184 ? -107.021 47.988   -60.578 1.00 220.53 ? 184 LYS D CD  1 
ATOM   6232  C CE  . LYS D 4 184 ? -107.035 48.090   -62.083 1.00 225.63 ? 184 LYS D CE  1 
ATOM   6233  N NZ  . LYS D 4 184 ? -108.308 47.586   -62.659 1.00 229.28 ? 184 LYS D NZ  1 
ATOM   6234  N N   . ALA D 4 185 ? -105.659 51.425   -56.773 1.00 197.30 ? 185 ALA D N   1 
ATOM   6235  C CA  . ALA D 4 185 ? -106.094 52.814   -56.590 1.00 196.48 ? 185 ALA D CA  1 
ATOM   6236  C C   . ALA D 4 185 ? -104.906 53.789   -56.610 1.00 198.21 ? 185 ALA D C   1 
ATOM   6237  O O   . ALA D 4 185 ? -104.973 54.823   -57.280 1.00 196.73 ? 185 ALA D O   1 
ATOM   6238  C CB  . ALA D 4 185 ? -106.872 52.949   -55.286 1.00 198.26 ? 185 ALA D CB  1 
ATOM   6239  N N   . ASP D 4 186 ? -103.816 53.441   -55.896 1.00 194.23 ? 186 ASP D N   1 
ATOM   6240  C CA  . ASP D 4 186 ? -102.589 54.236   -55.823 1.00 192.45 ? 186 ASP D CA  1 
ATOM   6241  C C   . ASP D 4 186 ? -101.722 54.045   -57.075 1.00 196.31 ? 186 ASP D C   1 
ATOM   6242  O O   . ASP D 4 186 ? -100.878 54.896   -57.362 1.00 194.66 ? 186 ASP D O   1 
ATOM   6243  C CB  . ASP D 4 186 ? -101.792 53.881   -54.555 1.00 193.80 ? 186 ASP D CB  1 
ATOM   6244  C CG  . ASP D 4 186 ? -102.482 54.235   -53.250 1.00 203.83 ? 186 ASP D CG  1 
ATOM   6245  O OD1 . ASP D 4 186 ? -101.904 55.020   -52.468 1.00 203.75 ? 186 ASP D OD1 1 
ATOM   6246  O OD2 . ASP D 4 186 ? -103.590 53.710   -53.000 1.00 210.59 ? 186 ASP D OD2 1 
ATOM   6247  N N   . TYR D 4 187 ? -101.933 52.933   -57.815 1.00 194.31 ? 187 TYR D N   1 
ATOM   6248  C CA  . TYR D 4 187 ? -101.196 52.589   -59.036 1.00 193.85 ? 187 TYR D CA  1 
ATOM   6249  C C   . TYR D 4 187 ? -101.582 53.474   -60.227 1.00 199.40 ? 187 TYR D C   1 
ATOM   6250  O O   . TYR D 4 187 ? -100.726 53.782   -61.057 1.00 197.91 ? 187 TYR D O   1 
ATOM   6251  C CB  . TYR D 4 187 ? -101.381 51.099   -59.383 1.00 195.83 ? 187 TYR D CB  1 
ATOM   6252  C CG  . TYR D 4 187 ? -100.356 50.564   -60.362 1.00 196.36 ? 187 TYR D CG  1 
ATOM   6253  C CD1 . TYR D 4 187 ? -99.136  50.059   -59.920 1.00 197.02 ? 187 TYR D CD1 1 
ATOM   6254  C CD2 . TYR D 4 187 ? -100.616 50.534   -61.729 1.00 197.66 ? 187 TYR D CD2 1 
ATOM   6255  C CE1 . TYR D 4 187 ? -98.193  49.557   -60.816 1.00 197.03 ? 187 TYR D CE1 1 
ATOM   6256  C CE2 . TYR D 4 187 ? -99.679  50.038   -62.634 1.00 198.05 ? 187 TYR D CE2 1 
ATOM   6257  C CZ  . TYR D 4 187 ? -98.468  49.552   -62.173 1.00 203.56 ? 187 TYR D CZ  1 
ATOM   6258  O OH  . TYR D 4 187 ? -97.543  49.072   -63.066 1.00 203.15 ? 187 TYR D OH  1 
ATOM   6259  N N   . GLU D 4 188 ? -102.865 53.863   -60.320 1.00 198.56 ? 188 GLU D N   1 
ATOM   6260  C CA  . GLU D 4 188 ? -103.371 54.704   -61.406 1.00 199.08 ? 188 GLU D CA  1 
ATOM   6261  C C   . GLU D 4 188 ? -102.971 56.179   -61.265 1.00 202.62 ? 188 GLU D C   1 
ATOM   6262  O O   . GLU D 4 188 ? -102.959 56.899   -62.265 1.00 201.67 ? 188 GLU D O   1 
ATOM   6263  C CB  . GLU D 4 188 ? -104.892 54.539   -61.566 1.00 202.25 ? 188 GLU D CB  1 
ATOM   6264  C CG  . GLU D 4 188 ? -105.307 53.781   -62.822 1.00 213.86 ? 188 GLU D CG  1 
ATOM   6265  C CD  . GLU D 4 188 ? -104.913 52.317   -62.914 1.00 232.63 ? 188 GLU D CD  1 
ATOM   6266  O OE1 . GLU D 4 188 ? -105.267 51.540   -61.996 1.00 226.42 ? 188 GLU D OE1 1 
ATOM   6267  O OE2 . GLU D 4 188 ? -104.288 51.938   -63.930 1.00 224.15 ? 188 GLU D OE2 1 
ATOM   6268  N N   . LYS D 4 189 ? -102.628 56.617   -60.034 1.00 199.73 ? 189 LYS D N   1 
ATOM   6269  C CA  . LYS D 4 189 ? -102.195 57.987   -59.719 1.00 198.95 ? 189 LYS D CA  1 
ATOM   6270  C C   . LYS D 4 189 ? -100.813 58.315   -60.319 1.00 202.40 ? 189 LYS D C   1 
ATOM   6271  O O   . LYS D 4 189 ? -100.595 59.438   -60.783 1.00 201.22 ? 189 LYS D O   1 
ATOM   6272  C CB  . LYS D 4 189 ? -102.173 58.214   -58.196 1.00 201.69 ? 189 LYS D CB  1 
ATOM   6273  C CG  . LYS D 4 189 ? -103.548 58.422   -57.570 1.00 215.41 ? 189 LYS D CG  1 
ATOM   6274  C CD  . LYS D 4 189 ? -103.430 58.858   -56.117 1.00 221.48 ? 189 LYS D CD  1 
ATOM   6275  C CE  . LYS D 4 189 ? -104.775 59.150   -55.499 1.00 227.19 ? 189 LYS D CE  1 
ATOM   6276  N NZ  . LYS D 4 189 ? -104.645 59.596   -54.088 1.00 234.11 ? 189 LYS D NZ  1 
ATOM   6277  N N   . HIS D 4 190 ? -99.890  57.330   -60.296 1.00 199.10 ? 190 HIS D N   1 
ATOM   6278  C CA  . HIS D 4 190 ? -98.516  57.430   -60.805 1.00 198.00 ? 190 HIS D CA  1 
ATOM   6279  C C   . HIS D 4 190 ? -98.371  56.723   -62.166 1.00 201.68 ? 190 HIS D C   1 
ATOM   6280  O O   . HIS D 4 190 ? -99.310  56.047   -62.600 1.00 202.51 ? 190 HIS D O   1 
ATOM   6281  C CB  . HIS D 4 190 ? -97.530  56.856   -59.774 1.00 198.37 ? 190 HIS D CB  1 
ATOM   6282  C CG  . HIS D 4 190 ? -97.704  57.426   -58.402 1.00 201.72 ? 190 HIS D CG  1 
ATOM   6283  N ND1 . HIS D 4 190 ? -97.198  58.668   -58.067 1.00 203.11 ? 190 HIS D ND1 1 
ATOM   6284  C CD2 . HIS D 4 190 ? -98.349  56.912   -57.330 1.00 203.92 ? 190 HIS D CD2 1 
ATOM   6285  C CE1 . HIS D 4 190 ? -97.537  58.863   -56.804 1.00 202.81 ? 190 HIS D CE1 1 
ATOM   6286  N NE2 . HIS D 4 190 ? -98.233  57.834   -56.319 1.00 203.64 ? 190 HIS D NE2 1 
ATOM   6287  N N   . LYS D 4 191 ? -97.219  56.896   -62.854 1.00 196.90 ? 191 LYS D N   1 
ATOM   6288  C CA  . LYS D 4 191 ? -97.014  56.294   -64.176 1.00 196.90 ? 191 LYS D CA  1 
ATOM   6289  C C   . LYS D 4 191 ? -95.648  55.619   -64.382 1.00 199.57 ? 191 LYS D C   1 
ATOM   6290  O O   . LYS D 4 191 ? -95.594  54.568   -65.022 1.00 199.41 ? 191 LYS D O   1 
ATOM   6291  C CB  . LYS D 4 191 ? -97.276  57.324   -65.290 1.00 199.71 ? 191 LYS D CB  1 
ATOM   6292  C CG  . LYS D 4 191 ? -98.762  57.549   -65.606 1.00 214.40 ? 191 LYS D CG  1 
ATOM   6293  C CD  . LYS D 4 191 ? -99.343  58.776   -64.894 1.00 222.98 ? 191 LYS D CD  1 
ATOM   6294  C CE  . LYS D 4 191 ? -100.850 58.831   -64.975 1.00 231.92 ? 191 LYS D CE  1 
ATOM   6295  N NZ  . LYS D 4 191 ? -101.400 59.982   -64.210 1.00 238.99 ? 191 LYS D NZ  1 
ATOM   6296  N N   . VAL D 4 192 ? -94.553  56.216   -63.873 1.00 195.16 ? 192 VAL D N   1 
ATOM   6297  C CA  . VAL D 4 192 ? -93.202  55.659   -64.049 1.00 194.45 ? 192 VAL D CA  1 
ATOM   6298  C C   . VAL D 4 192 ? -92.645  55.094   -62.722 1.00 195.98 ? 192 VAL D C   1 
ATOM   6299  O O   . VAL D 4 192 ? -92.552  55.818   -61.728 1.00 195.05 ? 192 VAL D O   1 
ATOM   6300  C CB  . VAL D 4 192 ? -92.230  56.663   -64.746 1.00 198.64 ? 192 VAL D CB  1 
ATOM   6301  C CG1 . VAL D 4 192 ? -90.820  56.085   -64.886 1.00 198.24 ? 192 VAL D CG1 1 
ATOM   6302  C CG2 . VAL D 4 192 ? -92.764  57.090   -66.114 1.00 199.13 ? 192 VAL D CG2 1 
ATOM   6303  N N   . TYR D 4 193 ? -92.266  53.797   -62.733 1.00 191.10 ? 193 TYR D N   1 
ATOM   6304  C CA  . TYR D 4 193 ? -91.723  53.078   -61.576 1.00 189.50 ? 193 TYR D CA  1 
ATOM   6305  C C   . TYR D 4 193 ? -90.288  52.600   -61.837 1.00 191.16 ? 193 TYR D C   1 
ATOM   6306  O O   . TYR D 4 193 ? -90.028  51.970   -62.866 1.00 191.22 ? 193 TYR D O   1 
ATOM   6307  C CB  . TYR D 4 193 ? -92.622  51.887   -61.204 1.00 190.75 ? 193 TYR D CB  1 
ATOM   6308  C CG  . TYR D 4 193 ? -94.084  52.234   -61.034 1.00 192.80 ? 193 TYR D CG  1 
ATOM   6309  C CD1 . TYR D 4 193 ? -94.991  52.048   -62.072 1.00 195.81 ? 193 TYR D CD1 1 
ATOM   6310  C CD2 . TYR D 4 193 ? -94.568  52.723   -59.825 1.00 193.28 ? 193 TYR D CD2 1 
ATOM   6311  C CE1 . TYR D 4 193 ? -96.339  52.364   -61.919 1.00 197.64 ? 193 TYR D CE1 1 
ATOM   6312  C CE2 . TYR D 4 193 ? -95.915  53.031   -59.656 1.00 195.00 ? 193 TYR D CE2 1 
ATOM   6313  C CZ  . TYR D 4 193 ? -96.798  52.849   -60.705 1.00 203.56 ? 193 TYR D CZ  1 
ATOM   6314  O OH  . TYR D 4 193 ? -98.125  53.158   -60.534 1.00 205.66 ? 193 TYR D OH  1 
ATOM   6315  N N   . ALA D 4 194 ? -89.369  52.888   -60.896 1.00 185.08 ? 194 ALA D N   1 
ATOM   6316  C CA  . ALA D 4 194 ? -87.952  52.536   -61.001 1.00 183.23 ? 194 ALA D CA  1 
ATOM   6317  C C   . ALA D 4 194 ? -87.379  51.947   -59.706 1.00 184.64 ? 194 ALA D C   1 
ATOM   6318  O O   . ALA D 4 194 ? -88.025  52.021   -58.663 1.00 183.77 ? 194 ALA D O   1 
ATOM   6319  C CB  . ALA D 4 194 ? -87.156  53.767   -61.406 1.00 184.24 ? 194 ALA D CB  1 
ATOM   6320  N N   . CYS D 4 195 ? -86.169  51.351   -59.784 1.00 179.89 ? 195 CYS D N   1 
ATOM   6321  C CA  . CYS D 4 195 ? -85.439  50.793   -58.641 1.00 178.42 ? 195 CYS D CA  1 
ATOM   6322  C C   . CYS D 4 195 ? -83.935  51.114   -58.733 1.00 181.66 ? 195 CYS D C   1 
ATOM   6323  O O   . CYS D 4 195 ? -83.279  50.721   -59.700 1.00 181.52 ? 195 CYS D O   1 
ATOM   6324  C CB  . CYS D 4 195 ? -85.711  49.298   -58.440 1.00 177.75 ? 195 CYS D CB  1 
ATOM   6325  S SG  . CYS D 4 195 ? -85.288  48.238   -59.858 1.00 181.21 ? 195 CYS D SG  1 
ATOM   6326  N N   . GLU D 4 196 ? -83.412  51.892   -57.760 1.00 177.23 ? 196 GLU D N   1 
ATOM   6327  C CA  . GLU D 4 196 ? -82.003  52.291   -57.714 1.00 176.27 ? 196 GLU D CA  1 
ATOM   6328  C C   . GLU D 4 196 ? -81.176  51.174   -57.072 1.00 176.97 ? 196 GLU D C   1 
ATOM   6329  O O   . GLU D 4 196 ? -81.416  50.815   -55.918 1.00 175.53 ? 196 GLU D O   1 
ATOM   6330  C CB  . GLU D 4 196 ? -81.822  53.637   -56.975 1.00 178.75 ? 196 GLU D CB  1 
ATOM   6331  C CG  . GLU D 4 196 ? -80.482  54.309   -57.246 1.00 188.17 ? 196 GLU D CG  1 
ATOM   6332  C CD  . GLU D 4 196 ? -80.152  55.518   -56.391 1.00 201.06 ? 196 GLU D CD  1 
ATOM   6333  O OE1 . GLU D 4 196 ? -79.967  56.613   -56.968 1.00 199.66 ? 196 GLU D OE1 1 
ATOM   6334  O OE2 . GLU D 4 196 ? -80.042  55.369   -55.153 1.00 185.31 ? 196 GLU D OE2 1 
ATOM   6335  N N   . VAL D 4 197 ? -80.220  50.616   -57.837 1.00 171.88 ? 197 VAL D N   1 
ATOM   6336  C CA  . VAL D 4 197 ? -79.340  49.530   -57.398 1.00 169.33 ? 197 VAL D CA  1 
ATOM   6337  C C   . VAL D 4 197 ? -77.945  50.084   -57.070 1.00 171.66 ? 197 VAL D C   1 
ATOM   6338  O O   . VAL D 4 197 ? -77.330  50.747   -57.908 1.00 172.53 ? 197 VAL D O   1 
ATOM   6339  C CB  . VAL D 4 197 ? -79.323  48.366   -58.426 1.00 172.14 ? 197 VAL D CB  1 
ATOM   6340  C CG1 . VAL D 4 197 ? -78.258  47.325   -58.092 1.00 170.01 ? 197 VAL D CG1 1 
ATOM   6341  C CG2 . VAL D 4 197 ? -80.698  47.714   -58.521 1.00 172.02 ? 197 VAL D CG2 1 
ATOM   6342  N N   . THR D 4 198 ? -77.472  49.825   -55.840 1.00 165.55 ? 198 THR D N   1 
ATOM   6343  C CA  . THR D 4 198 ? -76.178  50.277   -55.330 1.00 164.74 ? 198 THR D CA  1 
ATOM   6344  C C   . THR D 4 198 ? -75.329  49.054   -54.959 1.00 166.68 ? 198 THR D C   1 
ATOM   6345  O O   . THR D 4 198 ? -75.673  48.332   -54.019 1.00 164.67 ? 198 THR D O   1 
ATOM   6346  C CB  . THR D 4 198 ? -76.388  51.245   -54.152 1.00 168.93 ? 198 THR D CB  1 
ATOM   6347  O OG1 . THR D 4 198 ? -77.231  50.618   -53.184 1.00 167.60 ? 198 THR D OG1 1 
ATOM   6348  C CG2 . THR D 4 198 ? -77.003  52.572   -54.580 1.00 166.74 ? 198 THR D CG2 1 
ATOM   6349  N N   . HIS D 4 199 ? -74.242  48.804   -55.722 1.00 163.63 ? 199 HIS D N   1 
ATOM   6350  C CA  . HIS D 4 199 ? -73.352  47.648   -55.531 1.00 161.68 ? 199 HIS D CA  1 
ATOM   6351  C C   . HIS D 4 199 ? -71.867  47.968   -55.818 1.00 166.72 ? 199 HIS D C   1 
ATOM   6352  O O   . HIS D 4 199 ? -71.570  48.969   -56.479 1.00 168.21 ? 199 HIS D O   1 
ATOM   6353  C CB  . HIS D 4 199 ? -73.846  46.474   -56.402 1.00 161.16 ? 199 HIS D CB  1 
ATOM   6354  C CG  . HIS D 4 199 ? -73.157  45.168   -56.150 1.00 162.04 ? 199 HIS D CG  1 
ATOM   6355  N ND1 . HIS D 4 199 ? -72.254  44.648   -57.055 1.00 162.99 ? 199 HIS D ND1 1 
ATOM   6356  C CD2 . HIS D 4 199 ? -73.259  44.322   -55.099 1.00 162.02 ? 199 HIS D CD2 1 
ATOM   6357  C CE1 . HIS D 4 199 ? -71.841  43.506   -56.531 1.00 160.04 ? 199 HIS D CE1 1 
ATOM   6358  N NE2 . HIS D 4 199 ? -72.419  43.268   -55.356 1.00 159.67 ? 199 HIS D NE2 1 
ATOM   6359  N N   . GLN D 4 200 ? -70.941  47.115   -55.304 1.00 162.11 ? 200 GLN D N   1 
ATOM   6360  C CA  . GLN D 4 200 ? -69.486  47.234   -55.480 1.00 162.26 ? 200 GLN D CA  1 
ATOM   6361  C C   . GLN D 4 200 ? -69.070  46.966   -56.932 1.00 167.42 ? 200 GLN D C   1 
ATOM   6362  O O   . GLN D 4 200 ? -68.131  47.597   -57.421 1.00 168.42 ? 200 GLN D O   1 
ATOM   6363  C CB  . GLN D 4 200 ? -68.734  46.295   -54.514 1.00 161.06 ? 200 GLN D CB  1 
ATOM   6364  C CG  . GLN D 4 200 ? -67.262  46.679   -54.289 1.00 175.72 ? 200 GLN D CG  1 
ATOM   6365  C CD  . GLN D 4 200 ? -66.452  45.670   -53.494 1.00 191.82 ? 200 GLN D CD  1 
ATOM   6366  O OE1 . GLN D 4 200 ? -66.962  44.664   -52.983 1.00 187.84 ? 200 GLN D OE1 1 
ATOM   6367  N NE2 . GLN D 4 200 ? -65.154  45.922   -53.370 1.00 179.02 ? 200 GLN D NE2 1 
ATOM   6368  N N   . GLY D 4 201 ? -69.777  46.049   -57.597 1.00 163.97 ? 201 GLY D N   1 
ATOM   6369  C CA  . GLY D 4 201 ? -69.540  45.679   -58.990 1.00 164.90 ? 201 GLY D CA  1 
ATOM   6370  C C   . GLY D 4 201 ? -69.889  46.760   -59.993 1.00 174.11 ? 201 GLY D C   1 
ATOM   6371  O O   . GLY D 4 201 ? -69.372  46.754   -61.116 1.00 174.95 ? 201 GLY D O   1 
ATOM   6372  N N   . LEU D 4 202 ? -70.769  47.700   -59.588 1.00 173.32 ? 202 LEU D N   1 
ATOM   6373  C CA  . LEU D 4 202 ? -71.229  48.826   -60.400 1.00 175.95 ? 202 LEU D CA  1 
ATOM   6374  C C   . LEU D 4 202 ? -70.320  50.047   -60.272 1.00 183.03 ? 202 LEU D C   1 
ATOM   6375  O O   . LEU D 4 202 ? -69.924  50.420   -59.162 1.00 182.68 ? 202 LEU D O   1 
ATOM   6376  C CB  . LEU D 4 202 ? -72.668  49.210   -60.019 1.00 176.38 ? 202 LEU D CB  1 
ATOM   6377  C CG  . LEU D 4 202 ? -73.774  48.396   -60.669 1.00 180.19 ? 202 LEU D CG  1 
ATOM   6378  C CD1 . LEU D 4 202 ? -74.901  48.148   -59.696 1.00 179.63 ? 202 LEU D CD1 1 
ATOM   6379  C CD2 . LEU D 4 202 ? -74.300  49.089   -61.906 1.00 184.37 ? 202 LEU D CD2 1 
ATOM   6380  N N   . SER D 4 203 ? -70.008  50.676   -61.422 1.00 182.20 ? 203 SER D N   1 
ATOM   6381  C CA  . SER D 4 203 ? -69.193  51.889   -61.518 1.00 184.74 ? 203 SER D CA  1 
ATOM   6382  C C   . SER D 4 203 ? -70.016  53.092   -61.037 1.00 190.75 ? 203 SER D C   1 
ATOM   6383  O O   . SER D 4 203 ? -69.504  53.955   -60.321 1.00 191.73 ? 203 SER D O   1 
ATOM   6384  C CB  . SER D 4 203 ? -68.732  52.104   -62.958 1.00 189.87 ? 203 SER D CB  1 
ATOM   6385  O OG  . SER D 4 203 ? -69.831  52.228   -63.848 1.00 199.43 ? 203 SER D OG  1 
ATOM   6386  N N   . SER D 4 204 ? -71.299  53.125   -61.424 1.00 187.60 ? 204 SER D N   1 
ATOM   6387  C CA  . SER D 4 204 ? -72.259  54.162   -61.070 1.00 189.02 ? 204 SER D CA  1 
ATOM   6388  C C   . SER D 4 204 ? -73.560  53.504   -60.589 1.00 192.28 ? 204 SER D C   1 
ATOM   6389  O O   . SER D 4 204 ? -73.962  52.491   -61.171 1.00 190.31 ? 204 SER D O   1 
ATOM   6390  C CB  . SER D 4 204 ? -72.535  55.054   -62.276 1.00 194.54 ? 204 SER D CB  1 
ATOM   6391  O OG  . SER D 4 204 ? -72.914  54.289   -63.409 1.00 201.72 ? 204 SER D OG  1 
ATOM   6392  N N   . PRO D 4 205 ? -74.233  54.044   -59.539 1.00 190.23 ? 205 PRO D N   1 
ATOM   6393  C CA  . PRO D 4 205 ? -75.495  53.431   -59.077 1.00 189.17 ? 205 PRO D CA  1 
ATOM   6394  C C   . PRO D 4 205 ? -76.629  53.627   -60.092 1.00 194.61 ? 205 PRO D C   1 
ATOM   6395  O O   . PRO D 4 205 ? -77.368  54.616   -60.033 1.00 195.59 ? 205 PRO D O   1 
ATOM   6396  C CB  . PRO D 4 205 ? -75.770  54.134   -57.734 1.00 191.47 ? 205 PRO D CB  1 
ATOM   6397  C CG  . PRO D 4 205 ? -74.517  54.906   -57.410 1.00 197.09 ? 205 PRO D CG  1 
ATOM   6398  C CD  . PRO D 4 205 ? -73.895  55.228   -58.727 1.00 193.62 ? 205 PRO D CD  1 
ATOM   6399  N N   . VAL D 4 206 ? -76.737  52.683   -61.049 1.00 190.71 ? 206 VAL D N   1 
ATOM   6400  C CA  . VAL D 4 206 ? -77.721  52.726   -62.130 1.00 191.27 ? 206 VAL D CA  1 
ATOM   6401  C C   . VAL D 4 206 ? -79.137  52.418   -61.619 1.00 194.78 ? 206 VAL D C   1 
ATOM   6402  O O   . VAL D 4 206 ? -79.308  51.688   -60.640 1.00 192.66 ? 206 VAL D O   1 
ATOM   6403  C CB  . VAL D 4 206 ? -77.296  51.851   -63.344 1.00 194.93 ? 206 VAL D CB  1 
ATOM   6404  C CG1 . VAL D 4 206 ? -77.693  50.384   -63.172 1.00 192.93 ? 206 VAL D CG1 1 
ATOM   6405  C CG2 . VAL D 4 206 ? -77.834  52.419   -64.656 1.00 196.34 ? 206 VAL D CG2 1 
ATOM   6406  N N   . THR D 4 207 ? -80.137  53.011   -62.281 1.00 177.03 ? 207 THR D N   1 
ATOM   6407  C CA  . THR D 4 207 ? -81.559  52.874   -61.974 1.00 176.91 ? 207 THR D CA  1 
ATOM   6408  C C   . THR D 4 207 ? -82.275  52.369   -63.240 1.00 180.96 ? 207 THR D C   1 
ATOM   6409  O O   . THR D 4 207 ? -81.925  52.798   -64.344 1.00 180.96 ? 207 THR D O   1 
ATOM   6410  C CB  . THR D 4 207 ? -82.113  54.232   -61.477 1.00 186.44 ? 207 THR D CB  1 
ATOM   6411  O OG1 . THR D 4 207 ? -81.179  54.848   -60.581 1.00 185.88 ? 207 THR D OG1 1 
ATOM   6412  C CG2 . THR D 4 207 ? -83.466  54.104   -60.792 1.00 185.25 ? 207 THR D CG2 1 
ATOM   6413  N N   . LYS D 4 208 ? -83.252  51.449   -63.086 1.00 176.99 ? 208 LYS D N   1 
ATOM   6414  C CA  . LYS D 4 208 ? -84.005  50.901   -64.222 1.00 176.55 ? 208 LYS D CA  1 
ATOM   6415  C C   . LYS D 4 208 ? -85.513  51.127   -64.068 1.00 181.49 ? 208 LYS D C   1 
ATOM   6416  O O   . LYS D 4 208 ? -86.137  50.583   -63.154 1.00 180.74 ? 208 LYS D O   1 
ATOM   6417  C CB  . LYS D 4 208 ? -83.647  49.423   -64.498 1.00 178.43 ? 208 LYS D CB  1 
ATOM   6418  C CG  . LYS D 4 208 ? -82.157  49.156   -64.800 1.00 188.78 ? 208 LYS D CG  1 
ATOM   6419  C CD  . LYS D 4 208 ? -81.619  49.880   -66.049 1.00 196.59 ? 208 LYS D CD  1 
ATOM   6420  C CE  . LYS D 4 208 ? -80.115  49.783   -66.179 1.00 203.38 ? 208 LYS D CE  1 
ATOM   6421  N NZ  . LYS D 4 208 ? -79.578  50.733   -67.190 1.00 208.75 ? 208 LYS D NZ  1 
ATOM   6422  N N   . SER D 4 209 ? -86.080  51.960   -64.966 1.00 179.30 ? 209 SER D N   1 
ATOM   6423  C CA  . SER D 4 209 ? -87.482  52.392   -64.981 1.00 179.53 ? 209 SER D CA  1 
ATOM   6424  C C   . SER D 4 209 ? -88.364  51.745   -66.060 1.00 184.68 ? 209 SER D C   1 
ATOM   6425  O O   . SER D 4 209 ? -87.852  51.221   -67.050 1.00 184.43 ? 209 SER D O   1 
ATOM   6426  C CB  . SER D 4 209 ? -87.551  53.912   -65.110 1.00 183.10 ? 209 SER D CB  1 
ATOM   6427  O OG  . SER D 4 209 ? -86.910  54.358   -66.294 1.00 191.38 ? 209 SER D OG  1 
ATOM   6428  N N   . PHE D 4 210 ? -89.702  51.819   -65.864 1.00 182.11 ? 210 PHE D N   1 
ATOM   6429  C CA  . PHE D 4 210 ? -90.715  51.314   -66.795 1.00 182.30 ? 210 PHE D CA  1 
ATOM   6430  C C   . PHE D 4 210 ? -91.942  52.240   -66.862 1.00 188.10 ? 210 PHE D C   1 
ATOM   6431  O O   . PHE D 4 210 ? -92.446  52.682   -65.825 1.00 187.48 ? 210 PHE D O   1 
ATOM   6432  C CB  . PHE D 4 210 ? -91.092  49.840   -66.504 1.00 183.90 ? 210 PHE D CB  1 
ATOM   6433  C CG  . PHE D 4 210 ? -92.258  49.560   -65.577 1.00 185.13 ? 210 PHE D CG  1 
ATOM   6434  C CD1 . PHE D 4 210 ? -92.069  49.468   -64.205 1.00 187.91 ? 210 PHE D CD1 1 
ATOM   6435  C CD2 . PHE D 4 210 ? -93.531  49.324   -66.084 1.00 187.18 ? 210 PHE D CD2 1 
ATOM   6436  C CE1 . PHE D 4 210 ? -93.140  49.183   -63.354 1.00 188.73 ? 210 PHE D CE1 1 
ATOM   6437  C CE2 . PHE D 4 210 ? -94.604  49.050   -65.230 1.00 189.91 ? 210 PHE D CE2 1 
ATOM   6438  C CZ  . PHE D 4 210 ? -94.399  48.976   -63.871 1.00 187.89 ? 210 PHE D CZ  1 
ATOM   6439  N N   . ASN D 4 211 ? -92.403  52.537   -68.093 1.00 186.45 ? 211 ASN D N   1 
ATOM   6440  C CA  . ASN D 4 211 ? -93.567  53.388   -68.355 1.00 186.95 ? 211 ASN D CA  1 
ATOM   6441  C C   . ASN D 4 211 ? -94.854  52.554   -68.390 1.00 191.92 ? 211 ASN D C   1 
ATOM   6442  O O   . ASN D 4 211 ? -94.894  51.510   -69.050 1.00 191.78 ? 211 ASN D O   1 
ATOM   6443  C CB  . ASN D 4 211 ? -93.381  54.211   -69.646 1.00 188.63 ? 211 ASN D CB  1 
ATOM   6444  C CG  . ASN D 4 211 ? -93.146  53.408   -70.910 1.00 215.72 ? 211 ASN D CG  1 
ATOM   6445  O OD1 . ASN D 4 211 ? -92.324  52.485   -70.961 1.00 210.42 ? 211 ASN D OD1 1 
ATOM   6446  N ND2 . ASN D 4 211 ? -93.840  53.774   -71.976 1.00 208.42 ? 211 ASN D ND2 1 
ATOM   6447  N N   . ARG D 4 212 ? -95.889  53.008   -67.654 1.00 188.94 ? 212 ARG D N   1 
ATOM   6448  C CA  . ARG D 4 212 ? -97.191  52.343   -67.532 1.00 189.17 ? 212 ARG D CA  1 
ATOM   6449  C C   . ARG D 4 212 ? -97.895  52.150   -68.877 1.00 193.19 ? 212 ARG D C   1 
ATOM   6450  O O   . ARG D 4 212 ? -97.987  53.091   -69.668 1.00 192.42 ? 212 ARG D O   1 
ATOM   6451  C CB  . ARG D 4 212 ? -98.106  53.124   -66.576 1.00 189.95 ? 212 ARG D CB  1 
ATOM   6452  C CG  . ARG D 4 212 ? -98.511  52.360   -65.323 1.00 200.03 ? 212 ARG D CG  1 
ATOM   6453  C CD  . ARG D 4 212 ? -99.485  53.169   -64.483 1.00 210.33 ? 212 ARG D CD  1 
ATOM   6454  N NE  . ARG D 4 212 ? -100.848 53.116   -65.015 1.00 219.67 ? 212 ARG D NE  1 
ATOM   6455  C CZ  . ARG D 4 212 ? -101.750 54.082   -64.873 1.00 234.41 ? 212 ARG D CZ  1 
ATOM   6456  N NH1 . ARG D 4 212 ? -101.441 55.200   -64.227 1.00 221.17 ? 212 ARG D NH1 1 
ATOM   6457  N NH2 . ARG D 4 212 ? -102.963 53.945   -65.391 1.00 221.97 ? 212 ARG D NH2 1 
ATOM   6458  N N   . GLY D 4 213 ? -98.371  50.927   -69.109 1.00 190.26 ? 213 GLY D N   1 
ATOM   6459  C CA  . GLY D 4 213 ? -99.111  50.535   -70.305 1.00 190.35 ? 213 GLY D CA  1 
ATOM   6460  C C   . GLY D 4 213 ? -98.321  50.508   -71.597 1.00 193.91 ? 213 GLY D C   1 
ATOM   6461  O O   . GLY D 4 213 ? -98.058  49.430   -72.137 1.00 193.98 ? 213 GLY D O   1 
ATOM   6462  N N   . GLU D 4 214 ? -97.976  51.701   -72.118 1.00 189.67 ? 214 GLU D N   1 
ATOM   6463  C CA  . GLU D 4 214 ? -97.238  51.907   -73.372 1.00 189.12 ? 214 GLU D CA  1 
ATOM   6464  C C   . GLU D 4 214 ? -95.838  51.273   -73.348 1.00 193.15 ? 214 GLU D C   1 
ATOM   6465  O O   . GLU D 4 214 ? -95.160  51.315   -72.320 1.00 192.60 ? 214 GLU D O   1 
ATOM   6466  C CB  . GLU D 4 214 ? -97.170  53.409   -73.724 1.00 189.77 ? 214 GLU D CB  1 
ATOM   6467  C CG  . GLU D 4 214 ? -98.524  54.024   -74.054 1.00 197.36 ? 214 GLU D CG  1 
ATOM   6468  C CD  . GLU D 4 214 ? -98.582  55.537   -74.150 1.00 207.47 ? 214 GLU D CD  1 
ATOM   6469  O OE1 . GLU D 4 214 ? -98.102  56.220   -73.216 1.00 194.35 ? 214 GLU D OE1 1 
ATOM   6470  O OE2 . GLU D 4 214 ? -99.175  56.040   -75.131 1.00 197.44 ? 214 GLU D OE2 1 
ATOM   6471  N N   . CYS D 4 215 ? -95.429  50.657   -74.475 1.00 190.05 ? 215 CYS D N   1 
ATOM   6472  C CA  . CYS D 4 215 ? -94.133  49.985   -74.619 1.00 217.64 ? 215 CYS D CA  1 
ATOM   6473  C C   . CYS D 4 215 ? -92.998  50.992   -74.799 1.00 227.64 ? 215 CYS D C   1 
ATOM   6474  O O   . CYS D 4 215 ? -91.909  50.795   -74.268 1.00 182.73 ? 215 CYS D O   1 
ATOM   6475  C CB  . CYS D 4 215 ? -94.168  48.966   -75.756 1.00 218.73 ? 215 CYS D CB  1 
ATOM   6476  S SG  . CYS D 4 215 ? -95.370  47.629   -75.521 1.00 223.23 ? 215 CYS D SG  1 
ATOM   6477  N N   . ILE E 1 10  ? -31.290  -62.177  23.389  1.00 173.53 ? 10  ILE E N   1 
ATOM   6478  C CA  . ILE E 1 10  ? -32.418  -62.857  24.028  1.00 173.24 ? 10  ILE E CA  1 
ATOM   6479  C C   . ILE E 1 10  ? -33.645  -62.950  23.103  1.00 178.27 ? 10  ILE E C   1 
ATOM   6480  O O   . ILE E 1 10  ? -34.180  -61.922  22.682  1.00 177.24 ? 10  ILE E O   1 
ATOM   6481  C CB  . ILE E 1 10  ? -32.786  -62.265  25.428  1.00 174.81 ? 10  ILE E CB  1 
ATOM   6482  C CG1 . ILE E 1 10  ? -32.923  -60.724  25.418  1.00 174.36 ? 10  ILE E CG1 1 
ATOM   6483  C CG2 . ILE E 1 10  ? -31.814  -62.725  26.508  1.00 175.28 ? 10  ILE E CG2 1 
ATOM   6484  C CD1 . ILE E 1 10  ? -34.311  -60.241  25.638  1.00 181.03 ? 10  ILE E CD1 1 
ATOM   6485  N N   . GLU E 1 11  ? -34.082  -64.189  22.787  1.00 176.53 ? 11  GLU E N   1 
ATOM   6486  C CA  . GLU E 1 11  ? -35.272  -64.438  21.963  1.00 177.49 ? 11  GLU E CA  1 
ATOM   6487  C C   . GLU E 1 11  ? -36.518  -64.070  22.782  1.00 181.49 ? 11  GLU E C   1 
ATOM   6488  O O   . GLU E 1 11  ? -37.421  -63.408  22.265  1.00 180.75 ? 11  GLU E O   1 
ATOM   6489  C CB  . GLU E 1 11  ? -35.307  -65.903  21.459  1.00 180.81 ? 11  GLU E CB  1 
ATOM   6490  C CG  . GLU E 1 11  ? -36.657  -66.426  20.965  1.00 191.06 ? 11  GLU E CG  1 
ATOM   6491  C CD  . GLU E 1 11  ? -37.382  -65.621  19.901  1.00 212.70 ? 11  GLU E CD  1 
ATOM   6492  O OE1 . GLU E 1 11  ? -36.777  -65.343  18.841  1.00 217.95 ? 11  GLU E OE1 1 
ATOM   6493  O OE2 . GLU E 1 11  ? -38.565  -65.278  20.126  1.00 203.51 ? 11  GLU E OE2 1 
ATOM   6494  N N   . GLY E 1 12  ? -36.523  -64.485  24.051  1.00 178.49 ? 12  GLY E N   1 
ATOM   6495  C CA  . GLY E 1 12  ? -37.588  -64.197  25.002  1.00 177.92 ? 12  GLY E CA  1 
ATOM   6496  C C   . GLY E 1 12  ? -37.422  -62.810  25.584  1.00 181.42 ? 12  GLY E C   1 
ATOM   6497  O O   . GLY E 1 12  ? -36.624  -62.614  26.507  1.00 180.44 ? 12  GLY E O   1 
ATOM   6498  N N   . GLY E 1 13  ? -38.160  -61.855  25.013  1.00 177.85 ? 13  GLY E N   1 
ATOM   6499  C CA  . GLY E 1 13  ? -38.142  -60.447  25.392  1.00 176.25 ? 13  GLY E CA  1 
ATOM   6500  C C   . GLY E 1 13  ? -38.712  -60.145  26.761  1.00 179.03 ? 13  GLY E C   1 
ATOM   6501  O O   . GLY E 1 13  ? -39.915  -60.323  26.984  1.00 178.75 ? 13  GLY E O   1 
ATOM   6502  N N   . TRP E 1 14  ? -37.840  -59.645  27.677  1.00 174.84 ? 14  TRP E N   1 
ATOM   6503  C CA  . TRP E 1 14  ? -38.142  -59.284  29.075  1.00 174.23 ? 14  TRP E CA  1 
ATOM   6504  C C   . TRP E 1 14  ? -39.342  -58.337  29.223  1.00 176.65 ? 14  TRP E C   1 
ATOM   6505  O O   . TRP E 1 14  ? -39.691  -57.636  28.270  1.00 175.94 ? 14  TRP E O   1 
ATOM   6506  C CB  . TRP E 1 14  ? -36.897  -58.714  29.793  1.00 172.79 ? 14  TRP E CB  1 
ATOM   6507  C CG  . TRP E 1 14  ? -35.797  -59.710  30.056  1.00 174.08 ? 14  TRP E CG  1 
ATOM   6508  C CD1 . TRP E 1 14  ? -35.883  -60.856  30.795  1.00 176.90 ? 14  TRP E CD1 1 
ATOM   6509  C CD2 . TRP E 1 14  ? -34.416  -59.590  29.662  1.00 174.14 ? 14  TRP E CD2 1 
ATOM   6510  N NE1 . TRP E 1 14  ? -34.658  -61.486  30.841  1.00 176.30 ? 14  TRP E NE1 1 
ATOM   6511  C CE2 . TRP E 1 14  ? -33.738  -60.728  30.159  1.00 178.07 ? 14  TRP E CE2 1 
ATOM   6512  C CE3 . TRP E 1 14  ? -33.687  -58.635  28.924  1.00 175.49 ? 14  TRP E CE3 1 
ATOM   6513  C CZ2 . TRP E 1 14  ? -32.367  -60.941  29.936  1.00 177.68 ? 14  TRP E CZ2 1 
ATOM   6514  C CZ3 . TRP E 1 14  ? -32.332  -58.847  28.704  1.00 177.23 ? 14  TRP E CZ3 1 
ATOM   6515  C CH2 . TRP E 1 14  ? -31.685  -59.986  29.208  1.00 178.11 ? 14  TRP E CH2 1 
ATOM   6516  N N   . THR E 1 15  ? -39.997  -58.355  30.409  1.00 172.37 ? 15  THR E N   1 
ATOM   6517  C CA  . THR E 1 15  ? -41.196  -57.557  30.713  1.00 171.93 ? 15  THR E CA  1 
ATOM   6518  C C   . THR E 1 15  ? -41.173  -56.939  32.116  1.00 172.57 ? 15  THR E C   1 
ATOM   6519  O O   . THR E 1 15  ? -41.549  -55.777  32.283  1.00 172.03 ? 15  THR E O   1 
ATOM   6520  C CB  . THR E 1 15  ? -42.480  -58.401  30.514  1.00 183.85 ? 15  THR E CB  1 
ATOM   6521  O OG1 . THR E 1 15  ? -42.382  -59.616  31.264  1.00 183.46 ? 15  THR E OG1 1 
ATOM   6522  C CG2 . THR E 1 15  ? -42.777  -58.707  29.042  1.00 184.36 ? 15  THR E CG2 1 
ATOM   6523  N N   . GLY E 1 16  ? -40.752  -57.735  33.097  1.00 166.98 ? 16  GLY E N   1 
ATOM   6524  C CA  . GLY E 1 16  ? -40.695  -57.361  34.505  1.00 166.24 ? 16  GLY E CA  1 
ATOM   6525  C C   . GLY E 1 16  ? -39.713  -56.271  34.873  1.00 167.38 ? 16  GLY E C   1 
ATOM   6526  O O   . GLY E 1 16  ? -39.904  -55.615  35.900  1.00 167.99 ? 16  GLY E O   1 
ATOM   6527  N N   . MET E 1 17  ? -38.649  -56.073  34.065  1.00 160.76 ? 17  MET E N   1 
ATOM   6528  C CA  . MET E 1 17  ? -37.620  -55.064  34.337  1.00 159.40 ? 17  MET E CA  1 
ATOM   6529  C C   . MET E 1 17  ? -38.133  -53.629  34.178  1.00 162.06 ? 17  MET E C   1 
ATOM   6530  O O   . MET E 1 17  ? -38.831  -53.332  33.212  1.00 161.44 ? 17  MET E O   1 
ATOM   6531  C CB  . MET E 1 17  ? -36.361  -55.311  33.497  1.00 160.74 ? 17  MET E CB  1 
ATOM   6532  C CG  . MET E 1 17  ? -35.168  -54.509  33.974  1.00 164.49 ? 17  MET E CG  1 
ATOM   6533  S SD  . MET E 1 17  ? -33.553  -55.080  33.412  1.00 168.31 ? 17  MET E SD  1 
ATOM   6534  C CE  . MET E 1 17  ? -33.544  -54.443  31.758  1.00 164.85 ? 17  MET E CE  1 
ATOM   6535  N N   . VAL E 1 18  ? -37.799  -52.759  35.152  1.00 158.03 ? 18  VAL E N   1 
ATOM   6536  C CA  . VAL E 1 18  ? -38.166  -51.333  35.204  1.00 157.80 ? 18  VAL E CA  1 
ATOM   6537  C C   . VAL E 1 18  ? -36.945  -50.455  35.543  1.00 159.16 ? 18  VAL E C   1 
ATOM   6538  O O   . VAL E 1 18  ? -37.067  -49.237  35.692  1.00 159.25 ? 18  VAL E O   1 
ATOM   6539  C CB  . VAL E 1 18  ? -39.373  -51.042  36.148  1.00 163.39 ? 18  VAL E CB  1 
ATOM   6540  C CG1 . VAL E 1 18  ? -40.697  -51.444  35.504  1.00 163.17 ? 18  VAL E CG1 1 
ATOM   6541  C CG2 . VAL E 1 18  ? -39.203  -51.693  37.523  1.00 164.06 ? 18  VAL E CG2 1 
ATOM   6542  N N   . ASP E 1 19  ? -35.775  -51.092  35.672  1.00 153.29 ? 19  ASP E N   1 
ATOM   6543  C CA  . ASP E 1 19  ? -34.511  -50.453  36.024  1.00 152.43 ? 19  ASP E CA  1 
ATOM   6544  C C   . ASP E 1 19  ? -33.876  -49.761  34.813  1.00 151.86 ? 19  ASP E C   1 
ATOM   6545  O O   . ASP E 1 19  ? -33.356  -48.650  34.946  1.00 151.79 ? 19  ASP E O   1 
ATOM   6546  C CB  . ASP E 1 19  ? -33.545  -51.484  36.648  1.00 154.31 ? 19  ASP E CB  1 
ATOM   6547  C CG  . ASP E 1 19  ? -34.207  -52.499  37.572  1.00 165.86 ? 19  ASP E CG  1 
ATOM   6548  O OD1 . ASP E 1 19  ? -34.564  -52.125  38.710  1.00 168.35 ? 19  ASP E OD1 1 
ATOM   6549  O OD2 . ASP E 1 19  ? -34.373  -53.664  37.153  1.00 169.86 ? 19  ASP E OD2 1 
ATOM   6550  N N   . GLY E 1 20  ? -33.933  -50.424  33.656  1.00 144.70 ? 20  GLY E N   1 
ATOM   6551  C CA  . GLY E 1 20  ? -33.374  -49.922  32.406  1.00 142.61 ? 20  GLY E CA  1 
ATOM   6552  C C   . GLY E 1 20  ? -33.803  -50.682  31.167  1.00 142.36 ? 20  GLY E C   1 
ATOM   6553  O O   . GLY E 1 20  ? -34.955  -51.113  31.060  1.00 142.09 ? 20  GLY E O   1 
ATOM   6554  N N   . TRP E 1 21  ? -32.868  -50.839  30.218  1.00 135.60 ? 21  TRP E N   1 
ATOM   6555  C CA  . TRP E 1 21  ? -33.095  -51.508  28.944  1.00 133.69 ? 21  TRP E CA  1 
ATOM   6556  C C   . TRP E 1 21  ? -32.400  -52.854  28.824  1.00 136.19 ? 21  TRP E C   1 
ATOM   6557  O O   . TRP E 1 21  ? -32.987  -53.793  28.288  1.00 135.26 ? 21  TRP E O   1 
ATOM   6558  C CB  . TRP E 1 21  ? -32.630  -50.610  27.786  1.00 131.82 ? 21  TRP E CB  1 
ATOM   6559  C CG  . TRP E 1 21  ? -33.434  -49.360  27.549  1.00 132.33 ? 21  TRP E CG  1 
ATOM   6560  C CD1 . TRP E 1 21  ? -34.705  -49.099  27.977  1.00 135.24 ? 21  TRP E CD1 1 
ATOM   6561  C CD2 . TRP E 1 21  ? -33.050  -48.247  26.731  1.00 131.40 ? 21  TRP E CD2 1 
ATOM   6562  N NE1 . TRP E 1 21  ? -35.116  -47.870  27.516  1.00 134.14 ? 21  TRP E NE1 1 
ATOM   6563  C CE2 . TRP E 1 21  ? -34.123  -47.328  26.740  1.00 134.88 ? 21  TRP E CE2 1 
ATOM   6564  C CE3 . TRP E 1 21  ? -31.889  -47.922  26.009  1.00 132.32 ? 21  TRP E CE3 1 
ATOM   6565  C CZ2 . TRP E 1 21  ? -34.066  -46.103  26.065  1.00 133.25 ? 21  TRP E CZ2 1 
ATOM   6566  C CZ3 . TRP E 1 21  ? -31.833  -46.707  25.345  1.00 132.92 ? 21  TRP E CZ3 1 
ATOM   6567  C CH2 . TRP E 1 21  ? -32.905  -45.808  25.388  1.00 132.95 ? 21  TRP E CH2 1 
ATOM   6568  N N   . TYR E 1 22  ? -31.150  -52.946  29.301  1.00 133.01 ? 22  TYR E N   1 
ATOM   6569  C CA  . TYR E 1 22  ? -30.313  -54.142  29.162  1.00 132.96 ? 22  TYR E CA  1 
ATOM   6570  C C   . TYR E 1 22  ? -29.982  -54.874  30.479  1.00 137.41 ? 22  TYR E C   1 
ATOM   6571  O O   . TYR E 1 22  ? -29.547  -54.242  31.445  1.00 137.30 ? 22  TYR E O   1 
ATOM   6572  C CB  . TYR E 1 22  ? -29.005  -53.790  28.410  1.00 133.77 ? 22  TYR E CB  1 
ATOM   6573  C CG  . TYR E 1 22  ? -29.189  -52.922  27.180  1.00 133.57 ? 22  TYR E CG  1 
ATOM   6574  C CD1 . TYR E 1 22  ? -29.127  -51.535  27.266  1.00 134.86 ? 22  TYR E CD1 1 
ATOM   6575  C CD2 . TYR E 1 22  ? -29.385  -53.489  25.925  1.00 133.90 ? 22  TYR E CD2 1 
ATOM   6576  C CE1 . TYR E 1 22  ? -29.302  -50.730  26.142  1.00 134.25 ? 22  TYR E CE1 1 
ATOM   6577  C CE2 . TYR E 1 22  ? -29.542  -52.695  24.788  1.00 134.12 ? 22  TYR E CE2 1 
ATOM   6578  C CZ  . TYR E 1 22  ? -29.496  -51.314  24.900  1.00 138.01 ? 22  TYR E CZ  1 
ATOM   6579  O OH  . TYR E 1 22  ? -29.640  -50.524  23.784  1.00 133.17 ? 22  TYR E OH  1 
ATOM   6580  N N   . GLY E 1 23  ? -30.155  -56.202  30.463  1.00 133.52 ? 23  GLY E N   1 
ATOM   6581  C CA  . GLY E 1 23  ? -29.847  -57.117  31.559  1.00 156.58 ? 23  GLY E CA  1 
ATOM   6582  C C   . GLY E 1 23  ? -30.556  -56.839  32.865  1.00 181.53 ? 23  GLY E C   1 
ATOM   6583  O O   . GLY E 1 23  ? -30.010  -57.098  33.939  1.00 141.34 ? 23  GLY E O   1 
ATOM   6584  N N   . ALA E 1 36  ? -30.305  -54.538  35.760  1.00 151.69 ? 36  ALA E N   1 
ATOM   6585  C CA  . ALA E 1 36  ? -29.887  -53.774  34.591  1.00 152.01 ? 36  ALA E CA  1 
ATOM   6586  C C   . ALA E 1 36  ? -28.542  -53.081  34.770  1.00 157.53 ? 36  ALA E C   1 
ATOM   6587  O O   . ALA E 1 36  ? -28.333  -52.415  35.787  1.00 157.75 ? 36  ALA E O   1 
ATOM   6588  C CB  . ALA E 1 36  ? -30.951  -52.754  34.225  1.00 152.58 ? 36  ALA E CB  1 
ATOM   6589  N N   . ASP E 1 37  ? -27.633  -53.222  33.777  1.00 154.49 ? 37  ASP E N   1 
ATOM   6590  C CA  . ASP E 1 37  ? -26.312  -52.582  33.812  1.00 154.45 ? 37  ASP E CA  1 
ATOM   6591  C C   . ASP E 1 37  ? -26.476  -51.106  33.461  1.00 157.20 ? 37  ASP E C   1 
ATOM   6592  O O   . ASP E 1 37  ? -27.012  -50.788  32.396  1.00 156.21 ? 37  ASP E O   1 
ATOM   6593  C CB  . ASP E 1 37  ? -25.312  -53.279  32.863  1.00 156.79 ? 37  ASP E CB  1 
ATOM   6594  C CG  . ASP E 1 37  ? -23.892  -52.717  32.899  1.00 169.52 ? 37  ASP E CG  1 
ATOM   6595  O OD1 . ASP E 1 37  ? -23.268  -52.735  33.990  1.00 169.97 ? 37  ASP E OD1 1 
ATOM   6596  O OD2 . ASP E 1 37  ? -23.390  -52.303  31.830  1.00 176.49 ? 37  ASP E OD2 1 
ATOM   6597  N N   . LEU E 1 38  ? -26.038  -50.213  34.378  1.00 153.67 ? 38  LEU E N   1 
ATOM   6598  C CA  . LEU E 1 38  ? -26.145  -48.758  34.243  1.00 153.48 ? 38  LEU E CA  1 
ATOM   6599  C C   . LEU E 1 38  ? -25.289  -48.176  33.118  1.00 155.67 ? 38  LEU E C   1 
ATOM   6600  O O   . LEU E 1 38  ? -25.800  -47.346  32.376  1.00 155.06 ? 38  LEU E O   1 
ATOM   6601  C CB  . LEU E 1 38  ? -25.866  -48.033  35.576  1.00 154.14 ? 38  LEU E CB  1 
ATOM   6602  C CG  . LEU E 1 38  ? -26.666  -46.737  35.805  1.00 159.33 ? 38  LEU E CG  1 
ATOM   6603  C CD1 . LEU E 1 38  ? -27.150  -46.636  37.237  1.00 159.79 ? 38  LEU E CD1 1 
ATOM   6604  C CD2 . LEU E 1 38  ? -25.864  -45.495  35.414  1.00 162.40 ? 38  LEU E CD2 1 
ATOM   6605  N N   . LYS E 1 39  ? -24.010  -48.602  32.986  1.00 151.02 ? 39  LYS E N   1 
ATOM   6606  C CA  . LYS E 1 39  ? -23.089  -48.109  31.949  1.00 150.35 ? 39  LYS E CA  1 
ATOM   6607  C C   . LYS E 1 39  ? -23.585  -48.389  30.526  1.00 152.57 ? 39  LYS E C   1 
ATOM   6608  O O   . LYS E 1 39  ? -23.397  -47.548  29.646  1.00 152.31 ? 39  LYS E O   1 
ATOM   6609  C CB  . LYS E 1 39  ? -21.666  -48.663  32.147  1.00 152.91 ? 39  LYS E CB  1 
ATOM   6610  C CG  . LYS E 1 39  ? -20.592  -47.804  31.481  1.00 168.86 ? 39  LYS E CG  1 
ATOM   6611  C CD  . LYS E 1 39  ? -19.269  -48.538  31.335  1.00 179.29 ? 39  LYS E CD  1 
ATOM   6612  C CE  . LYS E 1 39  ? -18.267  -47.776  30.493  1.00 189.99 ? 39  LYS E CE  1 
ATOM   6613  N NZ  . LYS E 1 39  ? -18.579  -47.845  29.037  1.00 198.11 ? 39  LYS E NZ  1 
ATOM   6614  N N   . SER E 1 40  ? -24.226  -49.558  30.311  1.00 147.75 ? 40  SER E N   1 
ATOM   6615  C CA  . SER E 1 40  ? -24.764  -49.959  29.010  1.00 147.16 ? 40  SER E CA  1 
ATOM   6616  C C   . SER E 1 40  ? -25.978  -49.109  28.615  1.00 150.27 ? 40  SER E C   1 
ATOM   6617  O O   . SER E 1 40  ? -25.981  -48.532  27.527  1.00 149.69 ? 40  SER E O   1 
ATOM   6618  C CB  . SER E 1 40  ? -25.111  -51.445  28.997  1.00 150.03 ? 40  SER E CB  1 
ATOM   6619  O OG  . SER E 1 40  ? -26.075  -51.784  29.981  1.00 156.44 ? 40  SER E OG  1 
ATOM   6620  N N   . THR E 1 41  ? -26.994  -49.011  29.510  1.00 146.58 ? 41  THR E N   1 
ATOM   6621  C CA  . THR E 1 41  ? -28.210  -48.220  29.277  1.00 146.28 ? 41  THR E CA  1 
ATOM   6622  C C   . THR E 1 41  ? -27.897  -46.717  29.247  1.00 150.89 ? 41  THR E C   1 
ATOM   6623  O O   . THR E 1 41  ? -28.509  -46.003  28.462  1.00 150.32 ? 41  THR E O   1 
ATOM   6624  C CB  . THR E 1 41  ? -29.360  -48.545  30.275  1.00 152.54 ? 41  THR E CB  1 
ATOM   6625  O OG1 . THR E 1 41  ? -29.131  -47.924  31.543  1.00 150.99 ? 41  THR E OG1 1 
ATOM   6626  C CG2 . THR E 1 41  ? -29.646  -50.034  30.452  1.00 151.55 ? 41  THR E CG2 1 
ATOM   6627  N N   . GLN E 1 42  ? -26.956  -46.244  30.100  1.00 148.37 ? 42  GLN E N   1 
ATOM   6628  C CA  . GLN E 1 42  ? -26.535  -44.836  30.178  1.00 148.70 ? 42  GLN E CA  1 
ATOM   6629  C C   . GLN E 1 42  ? -25.929  -44.386  28.841  1.00 152.37 ? 42  GLN E C   1 
ATOM   6630  O O   . GLN E 1 42  ? -26.310  -43.330  28.341  1.00 152.12 ? 42  GLN E O   1 
ATOM   6631  C CB  . GLN E 1 42  ? -25.562  -44.607  31.357  1.00 150.74 ? 42  GLN E CB  1 
ATOM   6632  C CG  . GLN E 1 42  ? -25.094  -43.166  31.554  1.00 174.17 ? 42  GLN E CG  1 
ATOM   6633  C CD  . GLN E 1 42  ? -23.665  -42.980  31.097  1.00 195.05 ? 42  GLN E CD  1 
ATOM   6634  O OE1 . GLN E 1 42  ? -22.710  -43.385  31.773  1.00 189.35 ? 42  GLN E OE1 1 
ATOM   6635  N NE2 . GLN E 1 42  ? -23.485  -42.364  29.936  1.00 187.98 ? 42  GLN E NE2 1 
ATOM   6636  N N   . ASN E 1 43  ? -25.033  -45.209  28.247  1.00 147.98 ? 43  ASN E N   1 
ATOM   6637  C CA  . ASN E 1 43  ? -24.403  -44.930  26.951  1.00 147.06 ? 43  ASN E CA  1 
ATOM   6638  C C   . ASN E 1 43  ? -25.391  -45.079  25.789  1.00 148.41 ? 43  ASN E C   1 
ATOM   6639  O O   . ASN E 1 43  ? -25.188  -44.473  24.733  1.00 147.76 ? 43  ASN E O   1 
ATOM   6640  C CB  . ASN E 1 43  ? -23.158  -45.796  26.739  1.00 148.41 ? 43  ASN E CB  1 
ATOM   6641  C CG  . ASN E 1 43  ? -21.965  -45.361  27.558  1.00 174.74 ? 43  ASN E CG  1 
ATOM   6642  O OD1 . ASN E 1 43  ? -21.597  -44.178  27.599  1.00 170.91 ? 43  ASN E OD1 1 
ATOM   6643  N ND2 . ASN E 1 43  ? -21.309  -46.316  28.205  1.00 167.45 ? 43  ASN E ND2 1 
ATOM   6644  N N   . ALA E 1 44  ? -26.464  -45.872  25.992  1.00 143.16 ? 44  ALA E N   1 
ATOM   6645  C CA  . ALA E 1 44  ? -27.528  -46.073  25.010  1.00 142.24 ? 44  ALA E CA  1 
ATOM   6646  C C   . ALA E 1 44  ? -28.471  -44.854  25.006  1.00 142.78 ? 44  ALA E C   1 
ATOM   6647  O O   . ALA E 1 44  ? -28.686  -44.282  23.940  1.00 142.20 ? 44  ALA E O   1 
ATOM   6648  C CB  . ALA E 1 44  ? -28.293  -47.350  25.312  1.00 143.31 ? 44  ALA E CB  1 
ATOM   6649  N N   . ILE E 1 45  ? -28.979  -44.427  26.200  1.00 136.46 ? 45  ILE E N   1 
ATOM   6650  C CA  . ILE E 1 45  ? -29.844  -43.249  26.404  1.00 134.32 ? 45  ILE E CA  1 
ATOM   6651  C C   . ILE E 1 45  ? -29.177  -42.013  25.780  1.00 136.21 ? 45  ILE E C   1 
ATOM   6652  O O   . ILE E 1 45  ? -29.826  -41.287  25.026  1.00 134.97 ? 45  ILE E O   1 
ATOM   6653  C CB  . ILE E 1 45  ? -30.169  -43.053  27.922  1.00 136.89 ? 45  ILE E CB  1 
ATOM   6654  C CG1 . ILE E 1 45  ? -31.216  -44.072  28.400  1.00 137.01 ? 45  ILE E CG1 1 
ATOM   6655  C CG2 . ILE E 1 45  ? -30.619  -41.616  28.249  1.00 137.21 ? 45  ILE E CG2 1 
ATOM   6656  C CD1 . ILE E 1 45  ? -31.181  -44.366  29.896  1.00 144.55 ? 45  ILE E CD1 1 
ATOM   6657  N N   . ASP E 1 46  ? -27.872  -41.817  26.073  1.00 135.62 ? 46  ASP E N   1 
ATOM   6658  C CA  . ASP E 1 46  ? -27.036  -40.728  25.569  1.00 135.86 ? 46  ASP E CA  1 
ATOM   6659  C C   . ASP E 1 46  ? -26.939  -40.756  24.037  1.00 135.66 ? 46  ASP E C   1 
ATOM   6660  O O   . ASP E 1 46  ? -27.205  -39.732  23.406  1.00 135.56 ? 46  ASP E O   1 
ATOM   6661  C CB  . ASP E 1 46  ? -25.631  -40.774  26.210  1.00 140.59 ? 46  ASP E CB  1 
ATOM   6662  C CG  . ASP E 1 46  ? -25.556  -40.463  27.700  1.00 154.35 ? 46  ASP E CG  1 
ATOM   6663  O OD1 . ASP E 1 46  ? -26.627  -40.391  28.356  1.00 155.11 ? 46  ASP E OD1 1 
ATOM   6664  O OD2 . ASP E 1 46  ? -24.425  -40.346  28.222  1.00 162.66 ? 46  ASP E OD2 1 
ATOM   6665  N N   . GLU E 1 47  ? -26.602  -41.922  23.436  1.00 128.40 ? 47  GLU E N   1 
ATOM   6666  C CA  . GLU E 1 47  ? -26.500  -42.040  21.978  1.00 125.09 ? 47  GLU E CA  1 
ATOM   6667  C C   . GLU E 1 47  ? -27.855  -41.882  21.277  1.00 124.73 ? 47  GLU E C   1 
ATOM   6668  O O   . GLU E 1 47  ? -27.898  -41.369  20.160  1.00 123.18 ? 47  GLU E O   1 
ATOM   6669  C CB  . GLU E 1 47  ? -25.802  -43.336  21.560  1.00 125.59 ? 47  GLU E CB  1 
ATOM   6670  C CG  . GLU E 1 47  ? -25.044  -43.187  20.253  1.00 136.73 ? 47  GLU E CG  1 
ATOM   6671  C CD  . GLU E 1 47  ? -24.545  -44.474  19.630  1.00 165.06 ? 47  GLU E CD  1 
ATOM   6672  O OE1 . GLU E 1 47  ? -23.862  -45.256  20.332  1.00 165.77 ? 47  GLU E OE1 1 
ATOM   6673  O OE2 . GLU E 1 47  ? -24.793  -44.675  18.419  1.00 160.70 ? 47  GLU E OE2 1 
ATOM   6674  N N   . ILE E 1 48  ? -28.957  -42.295  21.941  1.00 119.36 ? 48  ILE E N   1 
ATOM   6675  C CA  . ILE E 1 48  ? -30.311  -42.151  21.402  1.00 116.67 ? 48  ILE E CA  1 
ATOM   6676  C C   . ILE E 1 48  ? -30.677  -40.664  21.364  1.00 119.74 ? 48  ILE E C   1 
ATOM   6677  O O   . ILE E 1 48  ? -30.951  -40.151  20.281  1.00 118.56 ? 48  ILE E O   1 
ATOM   6678  C CB  . ILE E 1 48  ? -31.369  -43.014  22.167  1.00 119.33 ? 48  ILE E CB  1 
ATOM   6679  C CG1 . ILE E 1 48  ? -31.124  -44.544  22.035  1.00 118.76 ? 48  ILE E CG1 1 
ATOM   6680  C CG2 . ILE E 1 48  ? -32.802  -42.650  21.774  1.00 118.99 ? 48  ILE E CG2 1 
ATOM   6681  C CD1 . ILE E 1 48  ? -31.068  -45.163  20.627  1.00 123.05 ? 48  ILE E CD1 1 
ATOM   6682  N N   . THR E 1 49  ? -30.635  -39.976  22.535  1.00 116.81 ? 49  THR E N   1 
ATOM   6683  C CA  . THR E 1 49  ? -30.963  -38.549  22.698  1.00 116.95 ? 49  THR E CA  1 
ATOM   6684  C C   . THR E 1 49  ? -30.151  -37.638  21.769  1.00 120.15 ? 49  THR E C   1 
ATOM   6685  O O   . THR E 1 49  ? -30.671  -36.623  21.301  1.00 118.76 ? 49  THR E O   1 
ATOM   6686  C CB  . THR E 1 49  ? -30.866  -38.111  24.164  1.00 124.93 ? 49  THR E CB  1 
ATOM   6687  O OG1 . THR E 1 49  ? -29.592  -38.482  24.688  1.00 125.84 ? 49  THR E OG1 1 
ATOM   6688  C CG2 . THR E 1 49  ? -31.986  -38.693  25.026  1.00 123.16 ? 49  THR E CG2 1 
ATOM   6689  N N   . ASN E 1 50  ? -28.901  -38.022  21.477  1.00 117.58 ? 50  ASN E N   1 
ATOM   6690  C CA  . ASN E 1 50  ? -28.033  -37.282  20.566  1.00 118.04 ? 50  ASN E CA  1 
ATOM   6691  C C   . ASN E 1 50  ? -28.416  -37.542  19.112  1.00 119.87 ? 50  ASN E C   1 
ATOM   6692  O O   . ASN E 1 50  ? -28.336  -36.615  18.305  1.00 120.27 ? 50  ASN E O   1 
ATOM   6693  C CB  . ASN E 1 50  ? -26.557  -37.602  20.821  1.00 121.64 ? 50  ASN E CB  1 
ATOM   6694  C CG  . ASN E 1 50  ? -25.967  -36.824  21.973  1.00 156.56 ? 50  ASN E CG  1 
ATOM   6695  O OD1 . ASN E 1 50  ? -25.072  -35.995  21.788  1.00 156.56 ? 50  ASN E OD1 1 
ATOM   6696  N ND2 . ASN E 1 50  ? -26.463  -37.046  23.190  1.00 149.96 ? 50  ASN E ND2 1 
ATOM   6697  N N   . LYS E 1 51  ? -28.863  -38.780  18.779  1.00 113.33 ? 51  LYS E N   1 
ATOM   6698  C CA  . LYS E 1 51  ? -29.306  -39.129  17.424  1.00 110.32 ? 51  LYS E CA  1 
ATOM   6699  C C   . LYS E 1 51  ? -30.654  -38.482  17.124  1.00 111.25 ? 51  LYS E C   1 
ATOM   6700  O O   . LYS E 1 51  ? -30.908  -38.097  15.981  1.00 110.02 ? 51  LYS E O   1 
ATOM   6701  C CB  . LYS E 1 51  ? -29.353  -40.652  17.217  1.00 111.24 ? 51  LYS E CB  1 
ATOM   6702  C CG  . LYS E 1 51  ? -28.369  -41.161  16.159  1.00 124.49 ? 51  LYS E CG  1 
ATOM   6703  C CD  . LYS E 1 51  ? -26.908  -41.122  16.636  1.00 133.97 ? 51  LYS E CD  1 
ATOM   6704  C CE  . LYS E 1 51  ? -25.935  -41.658  15.618  1.00 136.87 ? 51  LYS E CE  1 
ATOM   6705  N NZ  . LYS E 1 51  ? -24.625  -41.985  16.240  1.00 138.03 ? 51  LYS E NZ  1 
ATOM   6706  N N   . VAL E 1 52  ? -31.487  -38.318  18.168  1.00 106.85 ? 52  VAL E N   1 
ATOM   6707  C CA  . VAL E 1 52  ? -32.805  -37.686  18.096  1.00 105.76 ? 52  VAL E CA  1 
ATOM   6708  C C   . VAL E 1 52  ? -32.654  -36.205  17.734  1.00 111.87 ? 52  VAL E C   1 
ATOM   6709  O O   . VAL E 1 52  ? -33.277  -35.754  16.772  1.00 110.51 ? 52  VAL E O   1 
ATOM   6710  C CB  . VAL E 1 52  ? -33.613  -37.914  19.402  1.00 109.19 ? 52  VAL E CB  1 
ATOM   6711  C CG1 . VAL E 1 52  ? -34.794  -36.958  19.516  1.00 108.61 ? 52  VAL E CG1 1 
ATOM   6712  C CG2 . VAL E 1 52  ? -34.090  -39.355  19.503  1.00 108.21 ? 52  VAL E CG2 1 
ATOM   6713  N N   . ASN E 1 53  ? -31.807  -35.464  18.486  1.00 111.54 ? 53  ASN E N   1 
ATOM   6714  C CA  . ASN E 1 53  ? -31.537  -34.040  18.254  1.00 113.04 ? 53  ASN E CA  1 
ATOM   6715  C C   . ASN E 1 53  ? -30.859  -33.794  16.904  1.00 117.07 ? 53  ASN E C   1 
ATOM   6716  O O   . ASN E 1 53  ? -31.054  -32.735  16.301  1.00 117.34 ? 53  ASN E O   1 
ATOM   6717  C CB  . ASN E 1 53  ? -30.700  -33.453  19.391  1.00 118.57 ? 53  ASN E CB  1 
ATOM   6718  C CG  . ASN E 1 53  ? -31.520  -33.087  20.606  1.00 149.38 ? 53  ASN E CG  1 
ATOM   6719  O OD1 . ASN E 1 53  ? -31.930  -33.947  21.395  1.00 141.36 ? 53  ASN E OD1 1 
ATOM   6720  N ND2 . ASN E 1 53  ? -31.803  -31.797  20.773  1.00 144.17 ? 53  ASN E ND2 1 
ATOM   6721  N N   . SER E 1 54  ? -30.077  -34.784  16.433  1.00 112.54 ? 54  SER E N   1 
ATOM   6722  C CA  . SER E 1 54  ? -29.367  -34.729  15.160  1.00 111.77 ? 54  SER E CA  1 
ATOM   6723  C C   . SER E 1 54  ? -30.273  -35.023  13.975  1.00 112.24 ? 54  SER E C   1 
ATOM   6724  O O   . SER E 1 54  ? -30.063  -34.433  12.919  1.00 112.06 ? 54  SER E O   1 
ATOM   6725  C CB  . SER E 1 54  ? -28.173  -35.672  15.164  1.00 116.39 ? 54  SER E CB  1 
ATOM   6726  O OG  . SER E 1 54  ? -27.258  -35.297  16.180  1.00 128.82 ? 54  SER E OG  1 
ATOM   6727  N N   . VAL E 1 55  ? -31.270  -35.922  14.134  1.00 106.13 ? 55  VAL E N   1 
ATOM   6728  C CA  . VAL E 1 55  ? -32.205  -36.246  13.051  1.00 104.67 ? 55  VAL E CA  1 
ATOM   6729  C C   . VAL E 1 55  ? -33.223  -35.108  12.852  1.00 108.45 ? 55  VAL E C   1 
ATOM   6730  O O   . VAL E 1 55  ? -33.668  -34.879  11.727  1.00 108.02 ? 55  VAL E O   1 
ATOM   6731  C CB  . VAL E 1 55  ? -32.855  -37.643  13.183  1.00 107.57 ? 55  VAL E CB  1 
ATOM   6732  C CG1 . VAL E 1 55  ? -33.837  -37.704  14.342  1.00 106.89 ? 55  VAL E CG1 1 
ATOM   6733  C CG2 . VAL E 1 55  ? -33.521  -38.078  11.877  1.00 107.37 ? 55  VAL E CG2 1 
ATOM   6734  N N   . ILE E 1 56  ? -33.560  -34.381  13.934  1.00 105.52 ? 56  ILE E N   1 
ATOM   6735  C CA  . ILE E 1 56  ? -34.450  -33.219  13.874  1.00 105.57 ? 56  ILE E CA  1 
ATOM   6736  C C   . ILE E 1 56  ? -33.688  -32.131  13.105  1.00 113.61 ? 56  ILE E C   1 
ATOM   6737  O O   . ILE E 1 56  ? -34.255  -31.506  12.203  1.00 113.59 ? 56  ILE E O   1 
ATOM   6738  C CB  . ILE E 1 56  ? -34.903  -32.776  15.294  1.00 108.17 ? 56  ILE E CB  1 
ATOM   6739  C CG1 . ILE E 1 56  ? -35.930  -33.770  15.861  1.00 107.29 ? 56  ILE E CG1 1 
ATOM   6740  C CG2 . ILE E 1 56  ? -35.474  -31.350  15.294  1.00 108.67 ? 56  ILE E CG2 1 
ATOM   6741  C CD1 . ILE E 1 56  ? -36.029  -33.812  17.356  1.00 114.66 ? 56  ILE E CD1 1 
ATOM   6742  N N   . GLU E 1 57  ? -32.381  -31.971  13.424  1.00 112.90 ? 57  GLU E N   1 
ATOM   6743  C CA  . GLU E 1 57  ? -31.457  -31.042  12.772  1.00 114.61 ? 57  GLU E CA  1 
ATOM   6744  C C   . GLU E 1 57  ? -31.320  -31.419  11.287  1.00 118.24 ? 57  GLU E C   1 
ATOM   6745  O O   . GLU E 1 57  ? -31.388  -30.535  10.433  1.00 118.18 ? 57  GLU E O   1 
ATOM   6746  C CB  . GLU E 1 57  ? -30.085  -31.068  13.479  1.00 117.77 ? 57  GLU E CB  1 
ATOM   6747  C CG  . GLU E 1 57  ? -29.077  -30.040  12.976  1.00 135.14 ? 57  GLU E CG  1 
ATOM   6748  C CD  . GLU E 1 57  ? -28.297  -30.405  11.723  1.00 162.26 ? 57  GLU E CD  1 
ATOM   6749  O OE1 . GLU E 1 57  ? -27.639  -31.471  11.711  1.00 157.27 ? 57  GLU E OE1 1 
ATOM   6750  O OE2 . GLU E 1 57  ? -28.340  -29.616  10.751  1.00 157.98 ? 57  GLU E OE2 1 
ATOM   6751  N N   . LYS E 1 58  ? -31.150  -32.730  10.994  1.00 114.17 ? 58  LYS E N   1 
ATOM   6752  C CA  . LYS E 1 58  ? -31.002  -33.270  9.642   1.00 114.18 ? 58  LYS E CA  1 
ATOM   6753  C C   . LYS E 1 58  ? -32.248  -33.060  8.793   1.00 116.52 ? 58  LYS E C   1 
ATOM   6754  O O   . LYS E 1 58  ? -32.121  -32.935  7.582   1.00 117.32 ? 58  LYS E O   1 
ATOM   6755  C CB  . LYS E 1 58  ? -30.582  -34.749  9.663   1.00 117.24 ? 58  LYS E CB  1 
ATOM   6756  C CG  . LYS E 1 58  ? -29.646  -35.127  8.521   1.00 140.19 ? 58  LYS E CG  1 
ATOM   6757  C CD  . LYS E 1 58  ? -28.924  -36.444  8.774   1.00 153.38 ? 58  LYS E CD  1 
ATOM   6758  C CE  . LYS E 1 58  ? -27.806  -36.641  7.775   1.00 169.44 ? 58  LYS E CE  1 
ATOM   6759  N NZ  . LYS E 1 58  ? -27.036  -37.879  8.044   1.00 179.81 ? 58  LYS E NZ  1 
ATOM   6760  N N   . MET E 1 59  ? -33.437  -32.999  9.418   1.00 111.10 ? 59  MET E N   1 
ATOM   6761  C CA  . MET E 1 59  ? -34.695  -32.745  8.713   1.00 110.48 ? 59  MET E CA  1 
ATOM   6762  C C   . MET E 1 59  ? -34.861  -31.247  8.479   1.00 114.41 ? 59  MET E C   1 
ATOM   6763  O O   . MET E 1 59  ? -35.226  -30.842  7.376   1.00 114.97 ? 59  MET E O   1 
ATOM   6764  C CB  . MET E 1 59  ? -35.883  -33.289  9.502   1.00 111.70 ? 59  MET E CB  1 
ATOM   6765  C CG  . MET E 1 59  ? -36.011  -34.779  9.441   1.00 115.15 ? 59  MET E CG  1 
ATOM   6766  S SD  . MET E 1 59  ? -37.028  -35.374  10.800  1.00 118.03 ? 59  MET E SD  1 
ATOM   6767  C CE  . MET E 1 59  ? -38.645  -35.307  10.037  1.00 114.77 ? 59  MET E CE  1 
ATOM   6768  N N   . ASN E 1 60  ? -34.575  -30.427  9.518   1.00 110.10 ? 60  ASN E N   1 
ATOM   6769  C CA  . ASN E 1 60  ? -34.640  -28.961  9.480   1.00 109.94 ? 60  ASN E CA  1 
ATOM   6770  C C   . ASN E 1 60  ? -33.665  -28.397  8.439   1.00 113.89 ? 60  ASN E C   1 
ATOM   6771  O O   . ASN E 1 60  ? -34.018  -27.463  7.718   1.00 113.53 ? 60  ASN E O   1 
ATOM   6772  C CB  . ASN E 1 60  ? -34.357  -28.369  10.867  1.00 110.97 ? 60  ASN E CB  1 
ATOM   6773  C CG  . ASN E 1 60  ? -35.526  -28.395  11.830  1.00 133.45 ? 60  ASN E CG  1 
ATOM   6774  O OD1 . ASN E 1 60  ? -36.340  -29.322  11.858  1.00 122.81 ? 60  ASN E OD1 1 
ATOM   6775  N ND2 . ASN E 1 60  ? -35.609  -27.390  12.683  1.00 129.32 ? 60  ASN E ND2 1 
ATOM   6776  N N   . THR E 1 61  ? -32.454  -28.988  8.340   1.00 110.46 ? 61  THR E N   1 
ATOM   6777  C CA  . THR E 1 61  ? -31.463  -28.570  7.353   1.00 111.42 ? 61  THR E CA  1 
ATOM   6778  C C   . THR E 1 61  ? -31.875  -29.058  5.966   1.00 115.47 ? 61  THR E C   1 
ATOM   6779  O O   . THR E 1 61  ? -31.543  -28.403  4.979   1.00 117.30 ? 61  THR E O   1 
ATOM   6780  C CB  . THR E 1 61  ? -30.024  -28.939  7.767   1.00 118.89 ? 61  THR E CB  1 
ATOM   6781  O OG1 . THR E 1 61  ? -29.116  -28.144  7.009   1.00 122.01 ? 61  THR E OG1 1 
ATOM   6782  C CG2 . THR E 1 61  ? -29.690  -30.418  7.581   1.00 115.66 ? 61  THR E CG2 1 
ATOM   6783  N N   . GLN E 1 62  ? -32.624  -30.183  5.897   1.00 110.47 ? 62  GLN E N   1 
ATOM   6784  C CA  . GLN E 1 62  ? -33.116  -30.750  4.641   1.00 111.19 ? 62  GLN E CA  1 
ATOM   6785  C C   . GLN E 1 62  ? -34.279  -29.946  4.096   1.00 114.27 ? 62  GLN E C   1 
ATOM   6786  O O   . GLN E 1 62  ? -34.408  -29.838  2.884   1.00 115.26 ? 62  GLN E O   1 
ATOM   6787  C CB  . GLN E 1 62  ? -33.492  -32.232  4.784   1.00 112.19 ? 62  GLN E CB  1 
ATOM   6788  C CG  . GLN E 1 62  ? -33.646  -32.983  3.457   1.00 133.11 ? 62  GLN E CG  1 
ATOM   6789  C CD  . GLN E 1 62  ? -32.440  -32.883  2.543   1.00 160.62 ? 62  GLN E CD  1 
ATOM   6790  O OE1 . GLN E 1 62  ? -31.293  -33.132  2.937   1.00 157.01 ? 62  GLN E OE1 1 
ATOM   6791  N NE2 . GLN E 1 62  ? -32.675  -32.524  1.292   1.00 157.39 ? 62  GLN E NE2 1 
ATOM   6792  N N   . PHE E 1 63  ? -35.119  -29.375  4.973   1.00 109.04 ? 63  PHE E N   1 
ATOM   6793  C CA  . PHE E 1 63  ? -36.231  -28.531  4.542   1.00 109.12 ? 63  PHE E CA  1 
ATOM   6794  C C   . PHE E 1 63  ? -35.672  -27.266  3.900   1.00 114.31 ? 63  PHE E C   1 
ATOM   6795  O O   . PHE E 1 63  ? -36.192  -26.811  2.880   1.00 115.18 ? 63  PHE E O   1 
ATOM   6796  C CB  . PHE E 1 63  ? -37.169  -28.210  5.720   1.00 109.44 ? 63  PHE E CB  1 
ATOM   6797  C CG  . PHE E 1 63  ? -38.214  -27.149  5.465   1.00 110.91 ? 63  PHE E CG  1 
ATOM   6798  C CD1 . PHE E 1 63  ? -38.068  -25.870  5.985   1.00 113.39 ? 63  PHE E CD1 1 
ATOM   6799  C CD2 . PHE E 1 63  ? -39.349  -27.430  4.710   1.00 113.70 ? 63  PHE E CD2 1 
ATOM   6800  C CE1 . PHE E 1 63  ? -39.032  -24.889  5.751   1.00 114.19 ? 63  PHE E CE1 1 
ATOM   6801  C CE2 . PHE E 1 63  ? -40.309  -26.446  4.470   1.00 116.38 ? 63  PHE E CE2 1 
ATOM   6802  C CZ  . PHE E 1 63  ? -40.144  -25.183  4.993   1.00 113.78 ? 63  PHE E CZ  1 
ATOM   6803  N N   . THR E 1 64  ? -34.585  -26.724  4.497   1.00 111.06 ? 64  THR E N   1 
ATOM   6804  C CA  . THR E 1 64  ? -33.850  -25.542  4.036   1.00 112.31 ? 64  THR E CA  1 
ATOM   6805  C C   . THR E 1 64  ? -33.165  -25.884  2.706   1.00 118.41 ? 64  THR E C   1 
ATOM   6806  O O   . THR E 1 64  ? -33.154  -25.054  1.794   1.00 119.43 ? 64  THR E O   1 
ATOM   6807  C CB  . THR E 1 64  ? -32.853  -25.069  5.120   1.00 120.27 ? 64  THR E CB  1 
ATOM   6808  O OG1 . THR E 1 64  ? -33.497  -25.053  6.398   1.00 117.73 ? 64  THR E OG1 1 
ATOM   6809  C CG2 . THR E 1 64  ? -32.277  -23.689  4.828   1.00 120.35 ? 64  THR E CG2 1 
ATOM   6810  N N   . ALA E 1 65  ? -32.631  -27.122  2.596   1.00 115.54 ? 65  ALA E N   1 
ATOM   6811  C CA  . ALA E 1 65  ? -31.981  -27.648  1.396   1.00 117.64 ? 65  ALA E CA  1 
ATOM   6812  C C   . ALA E 1 65  ? -32.986  -27.827  0.252   1.00 123.17 ? 65  ALA E C   1 
ATOM   6813  O O   . ALA E 1 65  ? -32.688  -27.392  -0.861  1.00 125.44 ? 65  ALA E O   1 
ATOM   6814  C CB  . ALA E 1 65  ? -31.295  -28.970  1.699   1.00 118.08 ? 65  ALA E CB  1 
ATOM   6815  N N   . VAL E 1 66  ? -34.160  -28.472  0.508   1.00 118.44 ? 66  VAL E N   1 
ATOM   6816  C CA  . VAL E 1 66  ? -35.237  -28.683  -0.484  1.00 119.56 ? 66  VAL E CA  1 
ATOM   6817  C C   . VAL E 1 66  ? -35.870  -27.308  -0.838  1.00 125.71 ? 66  VAL E C   1 
ATOM   6818  O O   . VAL E 1 66  ? -36.479  -27.170  -1.904  1.00 127.57 ? 66  VAL E O   1 
ATOM   6819  C CB  . VAL E 1 66  ? -36.288  -29.766  -0.057  1.00 121.51 ? 66  VAL E CB  1 
ATOM   6820  C CG1 . VAL E 1 66  ? -37.331  -30.010  -1.144  1.00 123.20 ? 66  VAL E CG1 1 
ATOM   6821  C CG2 . VAL E 1 66  ? -35.617  -31.086  0.289   1.00 120.84 ? 66  VAL E CG2 1 
ATOM   6822  N N   . GLY E 1 67  ? -35.622  -26.301  0.024   1.00 121.31 ? 67  GLY E N   1 
ATOM   6823  C CA  . GLY E 1 67  ? -36.056  -24.909  -0.110  1.00 121.30 ? 67  GLY E CA  1 
ATOM   6824  C C   . GLY E 1 67  ? -35.604  -24.224  -1.387  1.00 128.01 ? 67  GLY E C   1 
ATOM   6825  O O   . GLY E 1 67  ? -35.995  -23.081  -1.652  1.00 127.82 ? 67  GLY E O   1 
ATOM   6826  N N   . LYS E 1 68  ? -34.790  -24.943  -2.198  1.00 126.50 ? 68  LYS E N   1 
ATOM   6827  C CA  . LYS E 1 68  ? -34.300  -24.553  -3.518  1.00 129.44 ? 68  LYS E CA  1 
ATOM   6828  C C   . LYS E 1 68  ? -35.308  -25.013  -4.627  1.00 136.33 ? 68  LYS E C   1 
ATOM   6829  O O   . LYS E 1 68  ? -34.924  -25.292  -5.769  1.00 139.13 ? 68  LYS E O   1 
ATOM   6830  C CB  . LYS E 1 68  ? -32.856  -25.063  -3.741  1.00 132.63 ? 68  LYS E CB  1 
ATOM   6831  C CG  . LYS E 1 68  ? -32.689  -26.571  -3.937  1.00 138.08 ? 68  LYS E CG  1 
ATOM   6832  C CD  . LYS E 1 68  ? -31.224  -26.928  -4.119  1.00 143.36 ? 68  LYS E CD  1 
ATOM   6833  C CE  . LYS E 1 68  ? -31.036  -28.080  -5.067  1.00 150.30 ? 68  LYS E CE  1 
ATOM   6834  N NZ  . LYS E 1 68  ? -29.659  -28.105  -5.624  1.00 157.64 ? 68  LYS E NZ  1 
ATOM   6835  N N   . GLU E 1 69  ? -36.570  -25.062  -4.228  1.00 131.67 ? 69  GLU E N   1 
ATOM   6836  C CA  . GLU E 1 69  ? -37.662  -25.448  -5.099  1.00 145.82 ? 69  GLU E CA  1 
ATOM   6837  C C   . GLU E 1 69  ? -37.494  -26.869  -5.595  1.00 142.12 ? 69  GLU E C   1 
ATOM   6838  O O   . GLU E 1 69  ? -38.219  -27.761  -5.166  1.00 92.71  ? 69  GLU E O   1 
ATOM   6839  C CB  . GLU E 1 69  ? -37.779  -24.468  -6.260  1.00 147.36 ? 69  GLU E CB  1 
ATOM   6840  C CG  . GLU E 1 69  ? -38.164  -23.061  -5.832  1.00 157.68 ? 69  GLU E CG  1 
ATOM   6841  C CD  . GLU E 1 69  ? -37.210  -22.474  -4.810  1.00 174.57 ? 69  GLU E CD  1 
ATOM   6842  O OE1 . GLU E 1 69  ? -37.009  -23.104  -3.752  1.00 164.22 ? 69  GLU E OE1 1 
ATOM   6843  O OE2 . GLU E 1 69  ? -36.664  -21.380  -5.062  1.00 165.69 ? 69  GLU E OE2 1 
ATOM   6844  N N   . LYS E 1 83  ? -47.859  -20.293  -5.687  1.00 170.67 ? 83  LYS E N   1 
ATOM   6845  C CA  . LYS E 1 83  ? -46.445  -20.358  -5.349  1.00 170.65 ? 83  LYS E CA  1 
ATOM   6846  C C   . LYS E 1 83  ? -46.023  -21.805  -5.163  1.00 174.26 ? 83  LYS E C   1 
ATOM   6847  O O   . LYS E 1 83  ? -45.562  -22.188  -4.091  1.00 173.71 ? 83  LYS E O   1 
ATOM   6848  C CB  . LYS E 1 83  ? -46.155  -19.556  -4.078  1.00 173.45 ? 83  LYS E CB  1 
ATOM   6849  C CG  . LYS E 1 83  ? -44.681  -19.287  -3.792  1.00 190.75 ? 83  LYS E CG  1 
ATOM   6850  C CD  . LYS E 1 83  ? -43.728  -20.244  -4.496  1.00 201.19 ? 83  LYS E CD  1 
ATOM   6851  C CE  . LYS E 1 83  ? -43.055  -19.589  -5.693  1.00 211.56 ? 83  LYS E CE  1 
ATOM   6852  N NZ  . LYS E 1 83  ? -41.910  -20.393  -6.201  1.00 219.68 ? 83  LYS E NZ  1 
ATOM   6853  N N   . VAL E 1 84  ? -46.193  -22.587  -6.227  1.00 170.36 ? 84  VAL E N   1 
ATOM   6854  C CA  . VAL E 1 84  ? -45.861  -24.017  -6.276  1.00 169.47 ? 84  VAL E CA  1 
ATOM   6855  C C   . VAL E 1 84  ? -45.861  -24.723  -4.929  1.00 171.56 ? 84  VAL E C   1 
ATOM   6856  O O   . VAL E 1 84  ? -45.150  -25.701  -4.741  1.00 170.83 ? 84  VAL E O   1 
ATOM   6857  C CB  . VAL E 1 84  ? -44.516  -24.294  -6.986  1.00 173.28 ? 84  VAL E CB  1 
ATOM   6858  C CG1 . VAL E 1 84  ? -44.585  -25.615  -7.730  1.00 173.29 ? 84  VAL E CG1 1 
ATOM   6859  C CG2 . VAL E 1 84  ? -44.160  -23.173  -7.948  1.00 173.02 ? 84  VAL E CG2 1 
ATOM   6860  N N   . ASP E 1 85  ? -46.658  -24.204  -3.999  1.00 166.98 ? 85  ASP E N   1 
ATOM   6861  C CA  . ASP E 1 85  ? -46.781  -24.774  -2.665  1.00 166.01 ? 85  ASP E CA  1 
ATOM   6862  C C   . ASP E 1 85  ? -46.927  -26.285  -2.793  1.00 168.63 ? 85  ASP E C   1 
ATOM   6863  O O   . ASP E 1 85  ? -45.950  -27.027  -2.720  1.00 168.08 ? 85  ASP E O   1 
ATOM   6864  C CB  . ASP E 1 85  ? -48.020  -24.208  -1.962  1.00 167.56 ? 85  ASP E CB  1 
ATOM   6865  C CG  . ASP E 1 85  ? -47.749  -22.911  -1.233  1.00 173.22 ? 85  ASP E CG  1 
ATOM   6866  O OD1 . ASP E 1 85  ? -46.601  -22.687  -0.809  1.00 172.80 ? 85  ASP E OD1 1 
ATOM   6867  O OD2 . ASP E 1 85  ? -48.697  -22.115  -1.073  1.00 177.56 ? 85  ASP E OD2 1 
ATOM   6868  N N   . ASP E 1 86  ? -48.162  -26.728  -2.991  1.00 164.12 ? 86  ASP E N   1 
ATOM   6869  C CA  . ASP E 1 86  ? -48.468  -28.157  -3.161  1.00 163.39 ? 86  ASP E CA  1 
ATOM   6870  C C   . ASP E 1 86  ? -47.410  -28.949  -3.926  1.00 165.94 ? 86  ASP E C   1 
ATOM   6871  O O   . ASP E 1 86  ? -47.206  -30.125  -3.622  1.00 165.38 ? 86  ASP E O   1 
ATOM   6872  C CB  . ASP E 1 86  ? -49.852  -28.358  -3.799  1.00 165.36 ? 86  ASP E CB  1 
ATOM   6873  C CG  . ASP E 1 86  ? -50.475  -29.712  -3.507  1.00 174.80 ? 86  ASP E CG  1 
ATOM   6874  O OD1 . ASP E 1 86  ? -50.701  -30.481  -4.468  1.00 175.15 ? 86  ASP E OD1 1 
ATOM   6875  O OD2 . ASP E 1 86  ? -50.767  -29.989  -2.322  1.00 180.35 ? 86  ASP E OD2 1 
ATOM   6876  N N   . GLY E 1 87  ? -46.796  -28.344  -4.926  1.00 161.85 ? 87  GLY E N   1 
ATOM   6877  C CA  . GLY E 1 87  ? -45.805  -29.070  -5.680  1.00 161.23 ? 87  GLY E CA  1 
ATOM   6878  C C   . GLY E 1 87  ? -44.739  -29.401  -4.677  1.00 163.24 ? 87  GLY E C   1 
ATOM   6879  O O   . GLY E 1 87  ? -44.546  -30.544  -4.280  1.00 162.75 ? 87  GLY E O   1 
ATOM   6880  N N   . PHE E 1 88  ? -44.056  -28.354  -4.255  1.00 158.53 ? 88  PHE E N   1 
ATOM   6881  C CA  . PHE E 1 88  ? -42.985  -28.452  -3.295  1.00 153.28 ? 88  PHE E CA  1 
ATOM   6882  C C   . PHE E 1 88  ? -43.267  -29.425  -2.178  1.00 151.29 ? 88  PHE E C   1 
ATOM   6883  O O   . PHE E 1 88  ? -42.613  -30.445  -2.052  1.00 148.66 ? 88  PHE E O   1 
ATOM   6884  C CB  . PHE E 1 88  ? -42.746  -27.073  -2.690  1.00 154.67 ? 88  PHE E CB  1 
ATOM   6885  C CG  . PHE E 1 88  ? -41.802  -27.067  -1.527  1.00 151.92 ? 88  PHE E CG  1 
ATOM   6886  C CD1 . PHE E 1 88  ? -42.177  -27.578  -0.309  1.00 153.44 ? 88  PHE E CD1 1 
ATOM   6887  C CD2 . PHE E 1 88  ? -40.552  -26.521  -1.653  1.00 151.42 ? 88  PHE E CD2 1 
ATOM   6888  C CE1 . PHE E 1 88  ? -41.312  -27.561  0.756   1.00 150.94 ? 88  PHE E CE1 1 
ATOM   6889  C CE2 . PHE E 1 88  ? -39.680  -26.497  -0.590  1.00 150.80 ? 88  PHE E CE2 1 
ATOM   6890  C CZ  . PHE E 1 88  ? -40.062  -27.016  0.618   1.00 147.64 ? 88  PHE E CZ  1 
ATOM   6891  N N   . LEU E 1 89  ? -44.234  -29.063  -1.358  1.00 145.60 ? 89  LEU E N   1 
ATOM   6892  C CA  . LEU E 1 89  ? -44.591  -29.823  -0.165  1.00 141.52 ? 89  LEU E CA  1 
ATOM   6893  C C   . LEU E 1 89  ? -44.525  -31.318  -0.379  1.00 143.17 ? 89  LEU E C   1 
ATOM   6894  O O   . LEU E 1 89  ? -43.825  -31.975  0.383   1.00 140.00 ? 89  LEU E O   1 
ATOM   6895  C CB  . LEU E 1 89  ? -45.947  -29.394  0.408   1.00 141.98 ? 89  LEU E CB  1 
ATOM   6896  C CG  . LEU E 1 89  ? -45.929  -28.087  1.197   1.00 145.52 ? 89  LEU E CG  1 
ATOM   6897  C CD1 . LEU E 1 89  ? -47.293  -27.450  1.232   1.00 147.38 ? 89  LEU E CD1 1 
ATOM   6898  C CD2 . LEU E 1 89  ? -45.382  -28.290  2.598   1.00 144.33 ? 89  LEU E CD2 1 
ATOM   6899  N N   . ASP E 1 90  ? -45.145  -31.840  -1.464  1.00 141.39 ? 90  ASP E N   1 
ATOM   6900  C CA  . ASP E 1 90  ? -45.140  -33.267  -1.825  1.00 140.62 ? 90  ASP E CA  1 
ATOM   6901  C C   . ASP E 1 90  ? -43.749  -33.917  -1.702  1.00 139.80 ? 90  ASP E C   1 
ATOM   6902  O O   . ASP E 1 90  ? -43.620  -35.017  -1.154  1.00 136.99 ? 90  ASP E O   1 
ATOM   6903  C CB  . ASP E 1 90  ? -45.705  -33.469  -3.244  1.00 146.53 ? 90  ASP E CB  1 
ATOM   6904  C CG  . ASP E 1 90  ? -47.214  -33.356  -3.370  1.00 161.64 ? 90  ASP E CG  1 
ATOM   6905  O OD1 . ASP E 1 90  ? -47.926  -33.768  -2.422  1.00 160.96 ? 90  ASP E OD1 1 
ATOM   6906  O OD2 . ASP E 1 90  ? -47.688  -32.938  -4.448  1.00 171.83 ? 90  ASP E OD2 1 
ATOM   6907  N N   . ILE E 1 91  ? -42.713  -33.200  -2.173  1.00 135.46 ? 91  ILE E N   1 
ATOM   6908  C CA  . ILE E 1 91  ? -41.312  -33.614  -2.131  1.00 132.77 ? 91  ILE E CA  1 
ATOM   6909  C C   . ILE E 1 91  ? -40.862  -33.704  -0.659  1.00 130.92 ? 91  ILE E C   1 
ATOM   6910  O O   . ILE E 1 91  ? -40.755  -34.812  -0.130  1.00 128.07 ? 91  ILE E O   1 
ATOM   6911  C CB  . ILE E 1 91  ? -40.399  -32.657  -2.978  1.00 137.35 ? 91  ILE E CB  1 
ATOM   6912  C CG1 . ILE E 1 91  ? -41.014  -32.287  -4.356  1.00 141.25 ? 91  ILE E CG1 1 
ATOM   6913  C CG2 . ILE E 1 91  ? -38.990  -33.228  -3.137  1.00 136.99 ? 91  ILE E CG2 1 
ATOM   6914  C CD1 . ILE E 1 91  ? -40.553  -30.895  -4.945  1.00 145.86 ? 91  ILE E CD1 1 
ATOM   6915  N N   . TRP E 1 92  ? -40.665  -32.536  0.000   1.00 126.62 ? 92  TRP E N   1 
ATOM   6916  C CA  . TRP E 1 92  ? -40.202  -32.390  1.385   1.00 124.10 ? 92  TRP E CA  1 
ATOM   6917  C C   . TRP E 1 92  ? -40.909  -33.321  2.377   1.00 128.90 ? 92  TRP E C   1 
ATOM   6918  O O   . TRP E 1 92  ? -40.237  -33.954  3.190   1.00 126.85 ? 92  TRP E O   1 
ATOM   6919  C CB  . TRP E 1 92  ? -40.275  -30.916  1.851   1.00 122.34 ? 92  TRP E CB  1 
ATOM   6920  C CG  . TRP E 1 92  ? -40.513  -30.725  3.329   1.00 120.88 ? 92  TRP E CG  1 
ATOM   6921  C CD1 . TRP E 1 92  ? -41.648  -30.255  3.920   1.00 123.56 ? 92  TRP E CD1 1 
ATOM   6922  C CD2 . TRP E 1 92  ? -39.605  -31.043  4.398   1.00 118.03 ? 92  TRP E CD2 1 
ATOM   6923  N NE1 . TRP E 1 92  ? -41.498  -30.238  5.287   1.00 120.81 ? 92  TRP E NE1 1 
ATOM   6924  C CE2 . TRP E 1 92  ? -40.262  -30.737  5.610   1.00 120.79 ? 92  TRP E CE2 1 
ATOM   6925  C CE3 . TRP E 1 92  ? -38.307  -31.580  4.451   1.00 118.22 ? 92  TRP E CE3 1 
ATOM   6926  C CZ2 . TRP E 1 92  ? -39.653  -30.922  6.858   1.00 118.14 ? 92  TRP E CZ2 1 
ATOM   6927  C CZ3 . TRP E 1 92  ? -37.714  -31.781  5.688   1.00 117.76 ? 92  TRP E CZ3 1 
ATOM   6928  C CH2 . TRP E 1 92  ? -38.378  -31.442  6.872   1.00 117.48 ? 92  TRP E CH2 1 
ATOM   6929  N N   . THR E 1 93  ? -42.249  -33.396  2.310   1.00 127.52 ? 93  THR E N   1 
ATOM   6930  C CA  . THR E 1 93  ? -43.080  -34.227  3.187   1.00 126.66 ? 93  THR E CA  1 
ATOM   6931  C C   . THR E 1 93  ? -42.724  -35.708  3.098   1.00 129.45 ? 93  THR E C   1 
ATOM   6932  O O   . THR E 1 93  ? -42.837  -36.410  4.102   1.00 127.26 ? 93  THR E O   1 
ATOM   6933  C CB  . THR E 1 93  ? -44.560  -33.965  2.938   1.00 141.85 ? 93  THR E CB  1 
ATOM   6934  O OG1 . THR E 1 93  ? -44.838  -34.222  1.562   1.00 149.41 ? 93  THR E OG1 1 
ATOM   6935  C CG2 . THR E 1 93  ? -44.963  -32.538  3.279   1.00 140.43 ? 93  THR E CG2 1 
ATOM   6936  N N   . TYR E 1 94  ? -42.275  -36.177  1.915   1.00 127.59 ? 94  TYR E N   1 
ATOM   6937  C CA  . TYR E 1 94  ? -41.837  -37.561  1.748   1.00 127.52 ? 94  TYR E CA  1 
ATOM   6938  C C   . TYR E 1 94  ? -40.403  -37.718  2.237   1.00 127.29 ? 94  TYR E C   1 
ATOM   6939  O O   . TYR E 1 94  ? -40.081  -38.748  2.827   1.00 126.28 ? 94  TYR E O   1 
ATOM   6940  C CB  . TYR E 1 94  ? -41.977  -38.048  0.294   1.00 132.24 ? 94  TYR E CB  1 
ATOM   6941  C CG  . TYR E 1 94  ? -41.657  -39.522  0.113   1.00 136.13 ? 94  TYR E CG  1 
ATOM   6942  C CD1 . TYR E 1 94  ? -42.508  -40.510  0.609   1.00 138.92 ? 94  TYR E CD1 1 
ATOM   6943  C CD2 . TYR E 1 94  ? -40.508  -39.930  -0.562  1.00 137.26 ? 94  TYR E CD2 1 
ATOM   6944  C CE1 . TYR E 1 94  ? -42.215  -41.868  0.455   1.00 140.56 ? 94  TYR E CE1 1 
ATOM   6945  C CE2 . TYR E 1 94  ? -40.214  -41.287  -0.738  1.00 138.60 ? 94  TYR E CE2 1 
ATOM   6946  C CZ  . TYR E 1 94  ? -41.070  -42.253  -0.224  1.00 146.32 ? 94  TYR E CZ  1 
ATOM   6947  O OH  . TYR E 1 94  ? -40.802  -43.594  -0.385  1.00 145.79 ? 94  TYR E OH  1 
ATOM   6948  N N   . ASN E 1 95  ? -39.550  -36.696  2.005   1.00 121.37 ? 95  ASN E N   1 
ATOM   6949  C CA  . ASN E 1 95  ? -38.147  -36.677  2.428   1.00 118.90 ? 95  ASN E CA  1 
ATOM   6950  C C   . ASN E 1 95  ? -38.029  -36.640  3.957   1.00 119.56 ? 95  ASN E C   1 
ATOM   6951  O O   . ASN E 1 95  ? -37.120  -37.257  4.518   1.00 118.58 ? 95  ASN E O   1 
ATOM   6952  C CB  . ASN E 1 95  ? -37.411  -35.490  1.803   1.00 119.72 ? 95  ASN E CB  1 
ATOM   6953  C CG  . ASN E 1 95  ? -35.948  -35.724  1.483   1.00 148.87 ? 95  ASN E CG  1 
ATOM   6954  O OD1 . ASN E 1 95  ? -35.402  -36.833  1.604   1.00 148.85 ? 95  ASN E OD1 1 
ATOM   6955  N ND2 . ASN E 1 95  ? -35.281  -34.675  1.027   1.00 138.62 ? 95  ASN E ND2 1 
ATOM   6956  N N   . ALA E 1 96  ? -38.964  -35.936  4.626   1.00 114.16 ? 96  ALA E N   1 
ATOM   6957  C CA  . ALA E 1 96  ? -39.031  -35.829  6.085   1.00 111.61 ? 96  ALA E CA  1 
ATOM   6958  C C   . ALA E 1 96  ? -39.491  -37.159  6.666   1.00 112.27 ? 96  ALA E C   1 
ATOM   6959  O O   . ALA E 1 96  ? -38.940  -37.605  7.668   1.00 110.28 ? 96  ALA E O   1 
ATOM   6960  C CB  . ALA E 1 96  ? -39.988  -34.719  6.487   1.00 112.44 ? 96  ALA E CB  1 
ATOM   6961  N N   . GLU E 1 97  ? -40.478  -37.806  6.011   1.00 109.17 ? 97  GLU E N   1 
ATOM   6962  C CA  . GLU E 1 97  ? -41.000  -39.110  6.412   1.00 109.17 ? 97  GLU E CA  1 
ATOM   6963  C C   . GLU E 1 97  ? -39.916  -40.166  6.230   1.00 113.10 ? 97  GLU E C   1 
ATOM   6964  O O   . GLU E 1 97  ? -39.736  -41.003  7.107   1.00 112.09 ? 97  GLU E O   1 
ATOM   6965  C CB  . GLU E 1 97  ? -42.271  -39.474  5.617   1.00 112.17 ? 97  GLU E CB  1 
ATOM   6966  C CG  . GLU E 1 97  ? -43.549  -38.961  6.257   1.00 124.87 ? 97  GLU E CG  1 
ATOM   6967  C CD  . GLU E 1 97  ? -44.833  -39.136  5.462   1.00 153.50 ? 97  GLU E CD  1 
ATOM   6968  O OE1 . GLU E 1 97  ? -45.729  -39.873  5.933   1.00 154.27 ? 97  GLU E OE1 1 
ATOM   6969  O OE2 . GLU E 1 97  ? -44.975  -38.475  4.409   1.00 153.03 ? 97  GLU E OE2 1 
ATOM   6970  N N   . LEU E 1 98  ? -39.156  -40.071  5.122   1.00 111.26 ? 98  LEU E N   1 
ATOM   6971  C CA  . LEU E 1 98  ? -38.060  -40.969  4.750   1.00 111.99 ? 98  LEU E CA  1 
ATOM   6972  C C   . LEU E 1 98  ? -36.990  -41.049  5.842   1.00 115.00 ? 98  LEU E C   1 
ATOM   6973  O O   . LEU E 1 98  ? -36.586  -42.153  6.199   1.00 114.96 ? 98  LEU E O   1 
ATOM   6974  C CB  . LEU E 1 98  ? -37.432  -40.501  3.420   1.00 112.75 ? 98  LEU E CB  1 
ATOM   6975  C CG  . LEU E 1 98  ? -36.669  -41.535  2.602   1.00 117.88 ? 98  LEU E CG  1 
ATOM   6976  C CD1 . LEU E 1 98  ? -37.032  -41.421  1.143   1.00 119.61 ? 98  LEU E CD1 1 
ATOM   6977  C CD2 . LEU E 1 98  ? -35.167  -41.375  2.778   1.00 118.40 ? 98  LEU E CD2 1 
ATOM   6978  N N   . LEU E 1 99  ? -36.550  -39.886  6.374   1.00 110.70 ? 99  LEU E N   1 
ATOM   6979  C CA  . LEU E 1 99  ? -35.527  -39.799  7.419   1.00 109.97 ? 99  LEU E CA  1 
ATOM   6980  C C   . LEU E 1 99  ? -35.959  -40.463  8.717   1.00 112.98 ? 99  LEU E C   1 
ATOM   6981  O O   . LEU E 1 99  ? -35.125  -41.066  9.388   1.00 112.01 ? 99  LEU E O   1 
ATOM   6982  C CB  . LEU E 1 99  ? -35.115  -38.341  7.671   1.00 109.58 ? 99  LEU E CB  1 
ATOM   6983  C CG  . LEU E 1 99  ? -33.758  -37.924  7.107   1.00 114.44 ? 99  LEU E CG  1 
ATOM   6984  C CD1 . LEU E 1 99  ? -33.684  -36.425  6.927   1.00 114.11 ? 99  LEU E CD1 1 
ATOM   6985  C CD2 . LEU E 1 99  ? -32.603  -38.417  7.991   1.00 117.40 ? 99  LEU E CD2 1 
ATOM   6986  N N   . VAL E 1 100 ? -37.261  -40.368  9.053   1.00 110.22 ? 100 VAL E N   1 
ATOM   6987  C CA  . VAL E 1 100 ? -37.860  -40.976  10.248  1.00 110.66 ? 100 VAL E CA  1 
ATOM   6988  C C   . VAL E 1 100 ? -37.863  -42.509  10.099  1.00 116.30 ? 100 VAL E C   1 
ATOM   6989  O O   . VAL E 1 100 ? -37.362  -43.194  10.990  1.00 116.87 ? 100 VAL E O   1 
ATOM   6990  C CB  . VAL E 1 100 ? -39.266  -40.382  10.569  1.00 114.31 ? 100 VAL E CB  1 
ATOM   6991  C CG1 . VAL E 1 100 ? -40.038  -41.230  11.585  1.00 114.30 ? 100 VAL E CG1 1 
ATOM   6992  C CG2 . VAL E 1 100 ? -39.154  -38.940  11.049  1.00 113.08 ? 100 VAL E CG2 1 
ATOM   6993  N N   . LEU E 1 101 ? -38.382  -43.032  8.956   1.00 112.83 ? 101 LEU E N   1 
ATOM   6994  C CA  . LEU E 1 101 ? -38.442  -44.471  8.641   1.00 113.35 ? 101 LEU E CA  1 
ATOM   6995  C C   . LEU E 1 101 ? -37.029  -45.073  8.582   1.00 115.03 ? 101 LEU E C   1 
ATOM   6996  O O   . LEU E 1 101 ? -36.834  -46.240  8.944   1.00 115.64 ? 101 LEU E O   1 
ATOM   6997  C CB  . LEU E 1 101 ? -39.163  -44.723  7.297   1.00 114.49 ? 101 LEU E CB  1 
ATOM   6998  C CG  . LEU E 1 101 ? -40.580  -44.158  7.105   1.00 119.72 ? 101 LEU E CG  1 
ATOM   6999  C CD1 . LEU E 1 101 ? -40.841  -43.835  5.647   1.00 121.05 ? 101 LEU E CD1 1 
ATOM   7000  C CD2 . LEU E 1 101 ? -41.641  -45.104  7.617   1.00 123.04 ? 101 LEU E CD2 1 
ATOM   7001  N N   . LEU E 1 102 ? -36.051  -44.260  8.130   1.00 108.43 ? 102 LEU E N   1 
ATOM   7002  C CA  . LEU E 1 102 ? -34.651  -44.636  7.999   1.00 107.19 ? 102 LEU E CA  1 
ATOM   7003  C C   . LEU E 1 102 ? -33.920  -44.623  9.330   1.00 107.52 ? 102 LEU E C   1 
ATOM   7004  O O   . LEU E 1 102 ? -33.166  -45.552  9.604   1.00 107.81 ? 102 LEU E O   1 
ATOM   7005  C CB  . LEU E 1 102 ? -33.947  -43.722  7.005   1.00 106.69 ? 102 LEU E CB  1 
ATOM   7006  C CG  . LEU E 1 102 ? -32.985  -44.438  6.082   1.00 112.46 ? 102 LEU E CG  1 
ATOM   7007  C CD1 . LEU E 1 102 ? -33.354  -44.209  4.635   1.00 112.74 ? 102 LEU E CD1 1 
ATOM   7008  C CD2 . LEU E 1 102 ? -31.553  -44.033  6.362   1.00 115.66 ? 102 LEU E CD2 1 
ATOM   7009  N N   . GLU E 1 103 ? -34.125  -43.582  10.155  1.00 101.58 ? 103 GLU E N   1 
ATOM   7010  C CA  . GLU E 1 103 ? -33.458  -43.501  11.454  1.00 101.44 ? 103 GLU E CA  1 
ATOM   7011  C C   . GLU E 1 103 ? -34.035  -44.489  12.461  1.00 106.03 ? 103 GLU E C   1 
ATOM   7012  O O   . GLU E 1 103 ? -33.301  -44.945  13.337  1.00 106.88 ? 103 GLU E O   1 
ATOM   7013  C CB  . GLU E 1 103 ? -33.429  -42.068  12.003  1.00 101.73 ? 103 GLU E CB  1 
ATOM   7014  C CG  . GLU E 1 103 ? -32.238  -41.780  12.910  1.00 112.92 ? 103 GLU E CG  1 
ATOM   7015  C CD  . GLU E 1 103 ? -30.854  -41.946  12.308  1.00 137.85 ? 103 GLU E CD  1 
ATOM   7016  O OE1 . GLU E 1 103 ? -30.647  -41.520  11.148  1.00 133.30 ? 103 GLU E OE1 1 
ATOM   7017  O OE2 . GLU E 1 103 ? -29.967  -42.483  13.012  1.00 135.86 ? 103 GLU E OE2 1 
ATOM   7018  N N   . ASN E 1 104 ? -35.333  -44.845  12.319  1.00 102.34 ? 104 ASN E N   1 
ATOM   7019  C CA  . ASN E 1 104 ? -36.010  -45.833  13.167  1.00 103.13 ? 104 ASN E CA  1 
ATOM   7020  C C   . ASN E 1 104 ? -35.460  -47.233  12.869  1.00 109.25 ? 104 ASN E C   1 
ATOM   7021  O O   . ASN E 1 104 ? -35.289  -48.033  13.789  1.00 110.72 ? 104 ASN E O   1 
ATOM   7022  C CB  . ASN E 1 104 ? -37.530  -45.800  12.969  1.00 101.09 ? 104 ASN E CB  1 
ATOM   7023  C CG  . ASN E 1 104 ? -38.248  -44.696  13.705  1.00 115.71 ? 104 ASN E CG  1 
ATOM   7024  O OD1 . ASN E 1 104 ? -37.789  -44.178  14.728  1.00 104.38 ? 104 ASN E OD1 1 
ATOM   7025  N ND2 . ASN E 1 104 ? -39.424  -44.340  13.210  1.00 108.69 ? 104 ASN E ND2 1 
ATOM   7026  N N   . GLU E 1 105 ? -35.160  -47.512  11.584  1.00 105.71 ? 105 GLU E N   1 
ATOM   7027  C CA  . GLU E 1 105 ? -34.565  -48.768  11.132  1.00 107.42 ? 105 GLU E CA  1 
ATOM   7028  C C   . GLU E 1 105 ? -33.164  -48.889  11.756  1.00 112.03 ? 105 GLU E C   1 
ATOM   7029  O O   . GLU E 1 105 ? -32.801  -49.964  12.223  1.00 112.29 ? 105 GLU E O   1 
ATOM   7030  C CB  . GLU E 1 105 ? -34.479  -48.784  9.595   1.00 108.49 ? 105 GLU E CB  1 
ATOM   7031  C CG  . GLU E 1 105 ? -34.374  -50.171  8.984   1.00 123.07 ? 105 GLU E CG  1 
ATOM   7032  C CD  . GLU E 1 105 ? -35.706  -50.841  8.719   1.00 146.14 ? 105 GLU E CD  1 
ATOM   7033  O OE1 . GLU E 1 105 ? -36.346  -50.504  7.698   1.00 132.55 ? 105 GLU E OE1 1 
ATOM   7034  O OE2 . GLU E 1 105 ? -36.116  -51.696  9.538   1.00 144.29 ? 105 GLU E OE2 1 
ATOM   7035  N N   . ARG E 1 106 ? -32.417  -47.761  11.813  1.00 109.00 ? 106 ARG E N   1 
ATOM   7036  C CA  . ARG E 1 106 ? -31.075  -47.659  12.395  1.00 110.09 ? 106 ARG E CA  1 
ATOM   7037  C C   . ARG E 1 106 ? -31.062  -47.715  13.926  1.00 116.65 ? 106 ARG E C   1 
ATOM   7038  O O   . ARG E 1 106 ? -30.081  -48.192  14.489  1.00 118.38 ? 106 ARG E O   1 
ATOM   7039  C CB  . ARG E 1 106 ? -30.337  -46.411  11.890  1.00 107.99 ? 106 ARG E CB  1 
ATOM   7040  C CG  . ARG E 1 106 ? -29.642  -46.631  10.553  1.00 118.44 ? 106 ARG E CG  1 
ATOM   7041  C CD  . ARG E 1 106 ? -28.578  -45.588  10.272  1.00 131.34 ? 106 ARG E CD  1 
ATOM   7042  N NE  . ARG E 1 106 ? -29.134  -44.388  9.645   1.00 145.20 ? 106 ARG E NE  1 
ATOM   7043  C CZ  . ARG E 1 106 ? -28.408  -43.375  9.180   1.00 163.46 ? 106 ARG E CZ  1 
ATOM   7044  N NH1 . ARG E 1 106 ? -27.083  -43.404  9.259   1.00 153.35 ? 106 ARG E NH1 1 
ATOM   7045  N NH2 . ARG E 1 106 ? -29.003  -42.325  8.630   1.00 150.32 ? 106 ARG E NH2 1 
ATOM   7046  N N   . THR E 1 107 ? -32.132  -47.229  14.593  1.00 113.26 ? 107 THR E N   1 
ATOM   7047  C CA  . THR E 1 107 ? -32.266  -47.236  16.059  1.00 114.81 ? 107 THR E CA  1 
ATOM   7048  C C   . THR E 1 107 ? -32.497  -48.665  16.578  1.00 123.06 ? 107 THR E C   1 
ATOM   7049  O O   . THR E 1 107 ? -31.796  -49.102  17.491  1.00 124.09 ? 107 THR E O   1 
ATOM   7050  C CB  . THR E 1 107 ? -33.374  -46.258  16.512  1.00 120.59 ? 107 THR E CB  1 
ATOM   7051  O OG1 . THR E 1 107 ? -33.064  -44.942  16.059  1.00 119.82 ? 107 THR E OG1 1 
ATOM   7052  C CG2 . THR E 1 107 ? -33.576  -46.243  18.025  1.00 118.24 ? 107 THR E CG2 1 
ATOM   7053  N N   . LEU E 1 108 ? -33.479  -49.381  15.992  1.00 122.17 ? 108 LEU E N   1 
ATOM   7054  C CA  . LEU E 1 108 ? -33.840  -50.755  16.355  1.00 125.84 ? 108 LEU E CA  1 
ATOM   7055  C C   . LEU E 1 108 ? -32.723  -51.751  16.050  1.00 135.92 ? 108 LEU E C   1 
ATOM   7056  O O   . LEU E 1 108 ? -32.574  -52.740  16.770  1.00 138.90 ? 108 LEU E O   1 
ATOM   7057  C CB  . LEU E 1 108 ? -35.157  -51.177  15.694  1.00 125.16 ? 108 LEU E CB  1 
ATOM   7058  C CG  . LEU E 1 108 ? -36.413  -50.480  16.231  1.00 128.28 ? 108 LEU E CG  1 
ATOM   7059  C CD1 . LEU E 1 108 ? -37.456  -50.328  15.154  1.00 127.15 ? 108 LEU E CD1 1 
ATOM   7060  C CD2 . LEU E 1 108 ? -36.992  -51.212  17.430  1.00 132.84 ? 108 LEU E CD2 1 
ATOM   7061  N N   . ASP E 1 109 ? -31.928  -51.476  15.000  1.00 133.55 ? 109 ASP E N   1 
ATOM   7062  C CA  . ASP E 1 109 ? -30.777  -52.294  14.627  1.00 136.22 ? 109 ASP E CA  1 
ATOM   7063  C C   . ASP E 1 109 ? -29.597  -51.987  15.559  1.00 140.72 ? 109 ASP E C   1 
ATOM   7064  O O   . ASP E 1 109 ? -28.751  -52.858  15.760  1.00 143.40 ? 109 ASP E O   1 
ATOM   7065  C CB  . ASP E 1 109 ? -30.398  -52.081  13.147  1.00 137.29 ? 109 ASP E CB  1 
ATOM   7066  C CG  . ASP E 1 109 ? -31.299  -52.788  12.137  1.00 153.89 ? 109 ASP E CG  1 
ATOM   7067  O OD1 . ASP E 1 109 ? -32.525  -52.883  12.390  1.00 155.64 ? 109 ASP E OD1 1 
ATOM   7068  O OD2 . ASP E 1 109 ? -30.784  -53.207  11.071  1.00 160.62 ? 109 ASP E OD2 1 
ATOM   7069  N N   . TYR E 1 110 ? -29.557  -50.761  16.144  1.00 134.78 ? 110 TYR E N   1 
ATOM   7070  C CA  . TYR E 1 110 ? -28.525  -50.331  17.095  1.00 135.82 ? 110 TYR E CA  1 
ATOM   7071  C C   . TYR E 1 110 ? -28.731  -51.005  18.453  1.00 146.26 ? 110 TYR E C   1 
ATOM   7072  O O   . TYR E 1 110 ? -27.752  -51.441  19.060  1.00 149.14 ? 110 TYR E O   1 
ATOM   7073  C CB  . TYR E 1 110 ? -28.479  -48.794  17.228  1.00 133.12 ? 110 TYR E CB  1 
ATOM   7074  C CG  . TYR E 1 110 ? -27.840  -48.282  18.503  1.00 134.34 ? 110 TYR E CG  1 
ATOM   7075  C CD1 . TYR E 1 110 ? -26.459  -48.284  18.665  1.00 137.78 ? 110 TYR E CD1 1 
ATOM   7076  C CD2 . TYR E 1 110 ? -28.616  -47.776  19.539  1.00 134.32 ? 110 TYR E CD2 1 
ATOM   7077  C CE1 . TYR E 1 110 ? -25.866  -47.815  19.836  1.00 139.94 ? 110 TYR E CE1 1 
ATOM   7078  C CE2 . TYR E 1 110 ? -28.036  -47.306  20.716  1.00 136.54 ? 110 TYR E CE2 1 
ATOM   7079  C CZ  . TYR E 1 110 ? -26.658  -47.316  20.855  1.00 144.67 ? 110 TYR E CZ  1 
ATOM   7080  O OH  . TYR E 1 110 ? -26.080  -46.857  22.016  1.00 146.49 ? 110 TYR E OH  1 
ATOM   7081  N N   . HIS E 1 111 ? -29.998  -51.068  18.932  1.00 144.62 ? 111 HIS E N   1 
ATOM   7082  C CA  . HIS E 1 111 ? -30.384  -51.705  20.199  1.00 148.33 ? 111 HIS E CA  1 
ATOM   7083  C C   . HIS E 1 111 ? -30.079  -53.205  20.150  1.00 156.74 ? 111 HIS E C   1 
ATOM   7084  O O   . HIS E 1 111 ? -29.499  -53.746  21.093  1.00 159.27 ? 111 HIS E O   1 
ATOM   7085  C CB  . HIS E 1 111 ? -31.876  -51.488  20.481  1.00 147.93 ? 111 HIS E CB  1 
ATOM   7086  C CG  . HIS E 1 111 ? -32.204  -50.156  21.075  1.00 149.69 ? 111 HIS E CG  1 
ATOM   7087  N ND1 . HIS E 1 111 ? -31.991  -49.894  22.416  1.00 153.43 ? 111 HIS E ND1 1 
ATOM   7088  C CD2 . HIS E 1 111 ? -32.764  -49.066  20.501  1.00 148.45 ? 111 HIS E CD2 1 
ATOM   7089  C CE1 . HIS E 1 111 ? -32.404  -48.653  22.609  1.00 150.40 ? 111 HIS E CE1 1 
ATOM   7090  N NE2 . HIS E 1 111 ? -32.874  -48.113  21.484  1.00 147.69 ? 111 HIS E NE2 1 
ATOM   7091  N N   . ASP E 1 112 ? -30.446  -53.854  19.023  1.00 153.88 ? 112 ASP E N   1 
ATOM   7092  C CA  . ASP E 1 112 ? -30.228  -55.267  18.709  1.00 157.13 ? 112 ASP E CA  1 
ATOM   7093  C C   . ASP E 1 112 ? -28.736  -55.615  18.804  1.00 164.00 ? 112 ASP E C   1 
ATOM   7094  O O   . ASP E 1 112 ? -28.389  -56.646  19.378  1.00 167.47 ? 112 ASP E O   1 
ATOM   7095  C CB  . ASP E 1 112 ? -30.781  -55.564  17.300  1.00 157.13 ? 112 ASP E CB  1 
ATOM   7096  C CG  . ASP E 1 112 ? -30.415  -56.917  16.718  1.00 171.70 ? 112 ASP E CG  1 
ATOM   7097  O OD1 . ASP E 1 112 ? -29.751  -56.945  15.657  1.00 170.93 ? 112 ASP E OD1 1 
ATOM   7098  O OD2 . ASP E 1 112 ? -30.807  -57.949  17.315  1.00 182.22 ? 112 ASP E OD2 1 
ATOM   7099  N N   . SER E 1 113 ? -27.867  -54.732  18.269  1.00 159.14 ? 113 SER E N   1 
ATOM   7100  C CA  . SER E 1 113 ? -26.411  -54.873  18.284  1.00 161.29 ? 113 SER E CA  1 
ATOM   7101  C C   . SER E 1 113 ? -25.828  -54.739  19.691  1.00 169.84 ? 113 SER E C   1 
ATOM   7102  O O   . SER E 1 113 ? -24.790  -55.338  19.964  1.00 173.46 ? 113 SER E O   1 
ATOM   7103  C CB  . SER E 1 113 ? -25.760  -53.865  17.343  1.00 161.08 ? 113 SER E CB  1 
ATOM   7104  O OG  . SER E 1 113 ? -25.943  -54.234  15.986  1.00 166.25 ? 113 SER E OG  1 
ATOM   7105  N N   . ASN E 1 114 ? -26.488  -53.970  20.581  1.00 145.32 ? 114 ASN E N   1 
ATOM   7106  C CA  . ASN E 1 114 ? -26.035  -53.787  21.964  1.00 144.52 ? 114 ASN E CA  1 
ATOM   7107  C C   . ASN E 1 114 ? -26.378  -54.989  22.840  1.00 149.21 ? 114 ASN E C   1 
ATOM   7108  O O   . ASN E 1 114 ? -25.614  -55.318  23.750  1.00 147.71 ? 114 ASN E O   1 
ATOM   7109  C CB  . ASN E 1 114 ? -26.606  -52.510  22.566  1.00 145.81 ? 114 ASN E CB  1 
ATOM   7110  C CG  . ASN E 1 114 ? -26.184  -51.237  21.874  1.00 169.67 ? 114 ASN E CG  1 
ATOM   7111  O OD1 . ASN E 1 114 ? -26.974  -50.301  21.741  1.00 166.27 ? 114 ASN E OD1 1 
ATOM   7112  N ND2 . ASN E 1 114 ? -24.934  -51.159  21.428  1.00 160.57 ? 114 ASN E ND2 1 
ATOM   7113  N N   . VAL E 1 115 ? -27.531  -55.634  22.567  1.00 147.91 ? 115 VAL E N   1 
ATOM   7114  C CA  . VAL E 1 115 ? -28.026  -56.820  23.278  1.00 148.36 ? 115 VAL E CA  1 
ATOM   7115  C C   . VAL E 1 115 ? -27.035  -57.987  23.087  1.00 151.68 ? 115 VAL E C   1 
ATOM   7116  O O   . VAL E 1 115 ? -26.590  -58.583  24.073  1.00 150.79 ? 115 VAL E O   1 
ATOM   7117  C CB  . VAL E 1 115 ? -29.481  -57.181  22.842  1.00 153.90 ? 115 VAL E CB  1 
ATOM   7118  C CG1 . VAL E 1 115 ? -29.920  -58.542  23.385  1.00 153.97 ? 115 VAL E CG1 1 
ATOM   7119  C CG2 . VAL E 1 115 ? -30.469  -56.094  23.259  1.00 154.25 ? 115 VAL E CG2 1 
ATOM   7120  N N   . LYS E 1 116 ? -26.672  -58.271  21.818  1.00 148.51 ? 116 LYS E N   1 
ATOM   7121  C CA  . LYS E 1 116 ? -25.732  -59.320  21.422  1.00 148.27 ? 116 LYS E CA  1 
ATOM   7122  C C   . LYS E 1 116 ? -24.337  -59.074  22.001  1.00 151.38 ? 116 LYS E C   1 
ATOM   7123  O O   . LYS E 1 116 ? -23.699  -60.021  22.461  1.00 151.02 ? 116 LYS E O   1 
ATOM   7124  C CB  . LYS E 1 116 ? -25.673  -59.455  19.892  1.00 151.90 ? 116 LYS E CB  1 
ATOM   7125  C CG  . LYS E 1 116 ? -26.951  -60.026  19.280  1.00 173.05 ? 116 LYS E CG  1 
ATOM   7126  C CD  . LYS E 1 116 ? -26.798  -60.335  17.793  1.00 188.52 ? 116 LYS E CD  1 
ATOM   7127  C CE  . LYS E 1 116 ? -27.379  -59.267  16.895  1.00 206.40 ? 116 LYS E CE  1 
ATOM   7128  N NZ  . LYS E 1 116 ? -26.497  -58.072  16.806  1.00 218.13 ? 116 LYS E NZ  1 
ATOM   7129  N N   . ASN E 1 117 ? -23.887  -57.802  22.011  1.00 147.31 ? 117 ASN E N   1 
ATOM   7130  C CA  . ASN E 1 117 ? -22.588  -57.403  22.551  1.00 146.55 ? 117 ASN E CA  1 
ATOM   7131  C C   . ASN E 1 117 ? -22.528  -57.474  24.077  1.00 151.80 ? 117 ASN E C   1 
ATOM   7132  O O   . ASN E 1 117 ? -21.437  -57.650  24.623  1.00 151.57 ? 117 ASN E O   1 
ATOM   7133  C CB  . ASN E 1 117 ? -22.169  -56.035  22.030  1.00 145.13 ? 117 ASN E CB  1 
ATOM   7134  C CG  . ASN E 1 117 ? -21.706  -56.052  20.593  1.00 165.52 ? 117 ASN E CG  1 
ATOM   7135  O OD1 . ASN E 1 117 ? -22.219  -56.794  19.741  1.00 156.05 ? 117 ASN E OD1 1 
ATOM   7136  N ND2 . ASN E 1 117 ? -20.733  -55.212  20.286  1.00 160.24 ? 117 ASN E ND2 1 
ATOM   7137  N N   . LEU E 1 118 ? -23.687  -57.363  24.765  1.00 149.38 ? 118 LEU E N   1 
ATOM   7138  C CA  . LEU E 1 118 ? -23.744  -57.487  26.225  1.00 149.89 ? 118 LEU E CA  1 
ATOM   7139  C C   . LEU E 1 118 ? -23.641  -58.971  26.608  1.00 155.66 ? 118 LEU E C   1 
ATOM   7140  O O   . LEU E 1 118 ? -22.987  -59.298  27.602  1.00 155.54 ? 118 LEU E O   1 
ATOM   7141  C CB  . LEU E 1 118 ? -25.012  -56.850  26.812  1.00 150.18 ? 118 LEU E CB  1 
ATOM   7142  C CG  . LEU E 1 118 ? -24.948  -56.524  28.310  1.00 155.01 ? 118 LEU E CG  1 
ATOM   7143  C CD1 . LEU E 1 118 ? -25.451  -55.131  28.582  1.00 155.31 ? 118 LEU E CD1 1 
ATOM   7144  C CD2 . LEU E 1 118 ? -25.729  -57.531  29.136  1.00 157.62 ? 118 LEU E CD2 1 
ATOM   7145  N N   . TYR E 1 119 ? -24.270  -59.861  25.807  1.00 153.57 ? 119 TYR E N   1 
ATOM   7146  C CA  . TYR E 1 119 ? -24.210  -61.313  25.993  1.00 154.25 ? 119 TYR E CA  1 
ATOM   7147  C C   . TYR E 1 119 ? -22.798  -61.810  25.679  1.00 158.68 ? 119 TYR E C   1 
ATOM   7148  O O   . TYR E 1 119 ? -22.300  -62.706  26.352  1.00 158.45 ? 119 TYR E O   1 
ATOM   7149  C CB  . TYR E 1 119 ? -25.286  -62.038  25.150  1.00 156.15 ? 119 TYR E CB  1 
ATOM   7150  C CG  . TYR E 1 119 ? -25.043  -63.518  24.923  1.00 158.37 ? 119 TYR E CG  1 
ATOM   7151  C CD1 . TYR E 1 119 ? -25.181  -64.438  25.962  1.00 160.57 ? 119 TYR E CD1 1 
ATOM   7152  C CD2 . TYR E 1 119 ? -24.698  -64.002  23.667  1.00 159.35 ? 119 TYR E CD2 1 
ATOM   7153  C CE1 . TYR E 1 119 ? -24.942  -65.799  25.762  1.00 161.82 ? 119 TYR E CE1 1 
ATOM   7154  C CE2 . TYR E 1 119 ? -24.472  -65.360  23.452  1.00 160.58 ? 119 TYR E CE2 1 
ATOM   7155  C CZ  . TYR E 1 119 ? -24.593  -66.257  24.503  1.00 168.52 ? 119 TYR E CZ  1 
ATOM   7156  O OH  . TYR E 1 119 ? -24.367  -67.599  24.305  1.00 169.64 ? 119 TYR E OH  1 
ATOM   7157  N N   . GLU E 1 120 ? -22.149  -61.198  24.669  1.00 155.84 ? 120 GLU E N   1 
ATOM   7158  C CA  . GLU E 1 120 ? -20.784  -61.521  24.255  1.00 156.26 ? 120 GLU E CA  1 
ATOM   7159  C C   . GLU E 1 120 ? -19.726  -61.067  25.269  1.00 161.47 ? 120 GLU E C   1 
ATOM   7160  O O   . GLU E 1 120 ? -18.602  -61.564  25.220  1.00 161.33 ? 120 GLU E O   1 
ATOM   7161  C CB  . GLU E 1 120 ? -20.487  -60.987  22.844  1.00 157.52 ? 120 GLU E CB  1 
ATOM   7162  C CG  . GLU E 1 120 ? -20.356  -62.072  21.786  1.00 169.25 ? 120 GLU E CG  1 
ATOM   7163  C CD  . GLU E 1 120 ? -21.589  -62.927  21.556  1.00 192.69 ? 120 GLU E CD  1 
ATOM   7164  O OE1 . GLU E 1 120 ? -22.502  -62.481  20.824  1.00 183.77 ? 120 GLU E OE1 1 
ATOM   7165  O OE2 . GLU E 1 120 ? -21.638  -64.051  22.105  1.00 190.94 ? 120 GLU E OE2 1 
ATOM   7166  N N   . LYS E 1 121 ? -20.083  -60.142  26.190  1.00 159.03 ? 121 LYS E N   1 
ATOM   7167  C CA  . LYS E 1 121 ? -19.190  -59.671  27.255  1.00 159.88 ? 121 LYS E CA  1 
ATOM   7168  C C   . LYS E 1 121 ? -19.146  -60.741  28.357  1.00 166.73 ? 121 LYS E C   1 
ATOM   7169  O O   . LYS E 1 121 ? -18.061  -61.080  28.833  1.00 167.80 ? 121 LYS E O   1 
ATOM   7170  C CB  . LYS E 1 121 ? -19.658  -58.313  27.823  1.00 161.91 ? 121 LYS E CB  1 
ATOM   7171  C CG  . LYS E 1 121 ? -18.610  -57.612  28.689  1.00 171.09 ? 121 LYS E CG  1 
ATOM   7172  C CD  . LYS E 1 121 ? -19.215  -56.531  29.575  1.00 175.83 ? 121 LYS E CD  1 
ATOM   7173  C CE  . LYS E 1 121 ? -18.213  -56.009  30.575  1.00 182.31 ? 121 LYS E CE  1 
ATOM   7174  N NZ  . LYS E 1 121 ? -18.842  -55.104  31.571  1.00 188.71 ? 121 LYS E NZ  1 
ATOM   7175  N N   . VAL E 1 122 ? -20.331  -61.283  28.730  1.00 163.83 ? 122 VAL E N   1 
ATOM   7176  C CA  . VAL E 1 122 ? -20.531  -62.331  29.747  1.00 164.50 ? 122 VAL E CA  1 
ATOM   7177  C C   . VAL E 1 122 ? -19.955  -63.680  29.261  1.00 168.54 ? 122 VAL E C   1 
ATOM   7178  O O   . VAL E 1 122 ? -19.264  -64.363  30.022  1.00 168.97 ? 122 VAL E O   1 
ATOM   7179  C CB  . VAL E 1 122 ? -22.033  -62.438  30.143  1.00 168.16 ? 122 VAL E CB  1 
ATOM   7180  C CG1 . VAL E 1 122 ? -22.281  -63.567  31.142  1.00 168.61 ? 122 VAL E CG1 1 
ATOM   7181  C CG2 . VAL E 1 122 ? -22.553  -61.112  30.691  1.00 167.94 ? 122 VAL E CG2 1 
ATOM   7182  N N   . ARG E 1 123 ? -20.240  -64.044  27.991  1.00 164.43 ? 123 ARG E N   1 
ATOM   7183  C CA  . ARG E 1 123 ? -19.787  -65.273  27.336  1.00 164.58 ? 123 ARG E CA  1 
ATOM   7184  C C   . ARG E 1 123 ? -18.253  -65.320  27.173  1.00 170.25 ? 123 ARG E C   1 
ATOM   7185  O O   . ARG E 1 123 ? -17.677  -66.406  27.237  1.00 170.80 ? 123 ARG E O   1 
ATOM   7186  C CB  . ARG E 1 123 ? -20.499  -65.443  25.983  1.00 163.54 ? 123 ARG E CB  1 
ATOM   7187  C CG  . ARG E 1 123 ? -20.647  -66.887  25.521  1.00 171.35 ? 123 ARG E CG  1 
ATOM   7188  C CD  . ARG E 1 123 ? -20.209  -67.059  24.075  1.00 179.27 ? 123 ARG E CD  1 
ATOM   7189  N NE  . ARG E 1 123 ? -18.783  -66.760  23.899  1.00 188.29 ? 123 ARG E NE  1 
ATOM   7190  C CZ  . ARG E 1 123 ? -18.294  -65.896  23.015  1.00 199.06 ? 123 ARG E CZ  1 
ATOM   7191  N NH1 . ARG E 1 123 ? -19.105  -65.253  22.185  1.00 184.32 ? 123 ARG E NH1 1 
ATOM   7192  N NH2 . ARG E 1 123 ? -16.987  -65.683  22.940  1.00 182.44 ? 123 ARG E NH2 1 
ATOM   7193  N N   . SER E 1 124 ? -17.598  -64.151  26.976  1.00 167.36 ? 124 SER E N   1 
ATOM   7194  C CA  . SER E 1 124 ? -16.139  -64.045  26.833  1.00 168.26 ? 124 SER E CA  1 
ATOM   7195  C C   . SER E 1 124 ? -15.410  -64.157  28.179  1.00 175.38 ? 124 SER E C   1 
ATOM   7196  O O   . SER E 1 124 ? -14.223  -64.489  28.199  1.00 176.22 ? 124 SER E O   1 
ATOM   7197  C CB  . SER E 1 124 ? -15.750  -62.750  26.129  1.00 170.81 ? 124 SER E CB  1 
ATOM   7198  O OG  . SER E 1 124 ? -16.185  -62.752  24.779  1.00 178.01 ? 124 SER E OG  1 
ATOM   7199  N N   . GLN E 1 125 ? -16.117  -63.876  29.294  1.00 173.20 ? 125 GLN E N   1 
ATOM   7200  C CA  . GLN E 1 125 ? -15.584  -63.958  30.662  1.00 175.00 ? 125 GLN E CA  1 
ATOM   7201  C C   . GLN E 1 125 ? -15.686  -65.393  31.234  1.00 180.50 ? 125 GLN E C   1 
ATOM   7202  O O   . GLN E 1 125 ? -15.009  -65.717  32.218  1.00 182.14 ? 125 GLN E O   1 
ATOM   7203  C CB  . GLN E 1 125 ? -16.313  -62.964  31.587  1.00 176.40 ? 125 GLN E CB  1 
ATOM   7204  C CG  . GLN E 1 125 ? -15.914  -61.503  31.388  1.00 194.07 ? 125 GLN E CG  1 
ATOM   7205  C CD  . GLN E 1 125 ? -16.882  -60.553  32.053  1.00 218.67 ? 125 GLN E CD  1 
ATOM   7206  O OE1 . GLN E 1 125 ? -18.092  -60.570  31.798  1.00 215.42 ? 125 GLN E OE1 1 
ATOM   7207  N NE2 . GLN E 1 125 ? -16.366  -59.679  32.900  1.00 212.67 ? 125 GLN E NE2 1 
ATOM   7208  N N   . LEU E 1 126 ? -16.536  -66.241  30.616  1.00 175.84 ? 126 LEU E N   1 
ATOM   7209  C CA  . LEU E 1 126 ? -16.776  -67.621  31.038  1.00 196.42 ? 126 LEU E CA  1 
ATOM   7210  C C   . LEU E 1 126 ? -16.365  -68.595  29.943  1.00 203.55 ? 126 LEU E C   1 
ATOM   7211  O O   . LEU E 1 126 ? -16.023  -69.737  30.237  1.00 163.42 ? 126 LEU E O   1 
ATOM   7212  C CB  . LEU E 1 126 ? -18.261  -67.821  31.396  1.00 195.86 ? 126 LEU E CB  1 
ATOM   7213  C CG  . LEU E 1 126 ? -18.870  -66.844  32.419  1.00 200.97 ? 126 LEU E CG  1 
ATOM   7214  C CD1 . LEU E 1 126 ? -20.364  -66.710  32.223  1.00 200.02 ? 126 LEU E CD1 1 
ATOM   7215  C CD2 . LEU E 1 126 ? -18.553  -67.256  33.851  1.00 205.35 ? 126 LEU E CD2 1 
ATOM   7216  N N   . CYS E 1 148 ? -19.837  -62.323  44.165  1.00 190.63 ? 148 CYS E N   1 
ATOM   7217  C CA  . CYS E 1 148 ? -20.090  -63.563  43.433  1.00 190.55 ? 148 CYS E CA  1 
ATOM   7218  C C   . CYS E 1 148 ? -20.481  -63.274  41.979  1.00 195.69 ? 148 CYS E C   1 
ATOM   7219  O O   . CYS E 1 148 ? -19.807  -63.746  41.064  1.00 195.05 ? 148 CYS E O   1 
ATOM   7220  C CB  . CYS E 1 148 ? -21.146  -64.406  44.148  1.00 190.65 ? 148 CYS E CB  1 
ATOM   7221  S SG  . CYS E 1 148 ? -21.728  -65.843  43.204  1.00 194.30 ? 148 CYS E SG  1 
ATOM   7222  N N   . MET E 1 149 ? -21.575  -62.513  41.781  1.00 193.40 ? 149 MET E N   1 
ATOM   7223  C CA  . MET E 1 149 ? -22.137  -62.142  40.478  1.00 193.55 ? 149 MET E CA  1 
ATOM   7224  C C   . MET E 1 149 ? -21.504  -60.863  39.926  1.00 197.79 ? 149 MET E C   1 
ATOM   7225  O O   . MET E 1 149 ? -21.433  -60.695  38.706  1.00 197.22 ? 149 MET E O   1 
ATOM   7226  C CB  . MET E 1 149 ? -23.655  -61.947  40.608  1.00 195.95 ? 149 MET E CB  1 
ATOM   7227  C CG  . MET E 1 149 ? -24.427  -62.297  39.359  1.00 199.71 ? 149 MET E CG  1 
ATOM   7228  S SD  . MET E 1 149 ? -25.406  -63.799  39.580  1.00 204.03 ? 149 MET E SD  1 
ATOM   7229  C CE  . MET E 1 149 ? -26.426  -63.730  38.133  1.00 200.66 ? 149 MET E CE  1 
ATOM   7230  N N   . GLU E 1 150 ? -21.059  -59.963  40.830  1.00 194.63 ? 150 GLU E N   1 
ATOM   7231  C CA  . GLU E 1 150 ? -20.454  -58.655  40.537  1.00 194.37 ? 150 GLU E CA  1 
ATOM   7232  C C   . GLU E 1 150 ? -19.140  -58.722  39.735  1.00 197.64 ? 150 GLU E C   1 
ATOM   7233  O O   . GLU E 1 150 ? -18.773  -57.728  39.104  1.00 197.09 ? 150 GLU E O   1 
ATOM   7234  C CB  . GLU E 1 150 ? -20.259  -57.840  41.833  1.00 195.86 ? 150 GLU E CB  1 
ATOM   7235  C CG  . GLU E 1 150 ? -21.538  -57.238  42.401  1.00 205.77 ? 150 GLU E CG  1 
ATOM   7236  C CD  . GLU E 1 150 ? -22.499  -58.205  43.070  1.00 224.12 ? 150 GLU E CD  1 
ATOM   7237  O OE1 . GLU E 1 150 ? -22.133  -58.788  44.118  1.00 215.96 ? 150 GLU E OE1 1 
ATOM   7238  O OE2 . GLU E 1 150 ? -23.625  -58.374  42.547  1.00 216.83 ? 150 GLU E OE2 1 
ATOM   7239  N N   . SER E 1 151 ? -18.442  -59.883  39.760  1.00 193.69 ? 151 SER E N   1 
ATOM   7240  C CA  . SER E 1 151 ? -17.184  -60.116  39.036  1.00 193.12 ? 151 SER E CA  1 
ATOM   7241  C C   . SER E 1 151 ? -17.397  -60.143  37.519  1.00 195.74 ? 151 SER E C   1 
ATOM   7242  O O   . SER E 1 151 ? -16.553  -59.634  36.778  1.00 195.09 ? 151 SER E O   1 
ATOM   7243  C CB  . SER E 1 151 ? -16.517  -61.406  39.510  1.00 196.57 ? 151 SER E CB  1 
ATOM   7244  O OG  . SER E 1 151 ? -17.383  -62.525  39.400  1.00 204.64 ? 151 SER E OG  1 
ATOM   7245  N N   . VAL E 1 152 ? -18.534  -60.729  37.072  1.00 191.68 ? 152 VAL E N   1 
ATOM   7246  C CA  . VAL E 1 152 ? -18.941  -60.835  35.664  1.00 191.25 ? 152 VAL E CA  1 
ATOM   7247  C C   . VAL E 1 152 ? -19.384  -59.451  35.176  1.00 195.46 ? 152 VAL E C   1 
ATOM   7248  O O   . VAL E 1 152 ? -19.017  -59.042  34.073  1.00 194.86 ? 152 VAL E O   1 
ATOM   7249  C CB  . VAL E 1 152 ? -20.047  -61.906  35.438  1.00 194.63 ? 152 VAL E CB  1 
ATOM   7250  C CG1 . VAL E 1 152 ? -20.241  -62.185  33.953  1.00 194.33 ? 152 VAL E CG1 1 
ATOM   7251  C CG2 . VAL E 1 152 ? -19.732  -63.205  36.173  1.00 194.37 ? 152 VAL E CG2 1 
ATOM   7252  N N   . LYS E 1 153 ? -20.162  -58.735  36.018  1.00 192.62 ? 153 LYS E N   1 
ATOM   7253  C CA  . LYS E 1 153 ? -20.676  -57.383  35.768  1.00 192.75 ? 153 LYS E CA  1 
ATOM   7254  C C   . LYS E 1 153 ? -19.520  -56.385  35.582  1.00 197.66 ? 153 LYS E C   1 
ATOM   7255  O O   . LYS E 1 153 ? -19.558  -55.567  34.655  1.00 197.43 ? 153 LYS E O   1 
ATOM   7256  C CB  . LYS E 1 153 ? -21.598  -56.925  36.921  1.00 195.01 ? 153 LYS E CB  1 
ATOM   7257  C CG  . LYS E 1 153 ? -22.878  -57.742  37.070  1.00 205.99 ? 153 LYS E CG  1 
ATOM   7258  C CD  . LYS E 1 153 ? -23.552  -57.492  38.416  1.00 212.93 ? 153 LYS E CD  1 
ATOM   7259  C CE  . LYS E 1 153 ? -24.709  -58.432  38.647  1.00 219.85 ? 153 LYS E CE  1 
ATOM   7260  N NZ  . LYS E 1 153 ? -25.216  -58.355  40.042  1.00 227.56 ? 153 LYS E NZ  1 
ATOM   7261  N N   . ASN E 1 154 ? -18.485  -56.482  36.451  1.00 194.42 ? 154 ASN E N   1 
ATOM   7262  C CA  . ASN E 1 154 ? -17.295  -55.628  36.426  1.00 219.72 ? 154 ASN E CA  1 
ATOM   7263  C C   . ASN E 1 154 ? -16.204  -56.257  35.561  1.00 230.95 ? 154 ASN E C   1 
ATOM   7264  O O   . ASN E 1 154 ? -16.470  -56.689  34.440  1.00 185.34 ? 154 ASN E O   1 
ATOM   7265  C CB  . ASN E 1 154 ? -16.776  -55.397  37.851  1.00 220.48 ? 154 ASN E CB  1 
ATOM   7266  C CG  . ASN E 1 154 ? -16.039  -54.094  38.048  1.00 243.44 ? 154 ASN E CG  1 
ATOM   7267  O OD1 . ASN E 1 154 ? -14.977  -53.848  37.462  1.00 238.48 ? 154 ASN E OD1 1 
ATOM   7268  N ND2 . ASN E 1 154 ? -16.564  -53.248  38.921  1.00 234.82 ? 154 ASN E ND2 1 
ATOM   7269  N N   . TYR E 1 159 ? -13.389  -66.345  35.722  1.00 206.17 ? 159 TYR E N   1 
ATOM   7270  C CA  . TYR E 1 159 ? -13.297  -67.772  35.417  1.00 205.66 ? 159 TYR E CA  1 
ATOM   7271  C C   . TYR E 1 159 ? -12.225  -68.543  36.243  1.00 210.51 ? 159 TYR E C   1 
ATOM   7272  O O   . TYR E 1 159 ? -12.548  -69.659  36.652  1.00 209.73 ? 159 TYR E O   1 
ATOM   7273  C CB  . TYR E 1 159 ? -13.108  -68.018  33.905  1.00 206.42 ? 159 TYR E CB  1 
ATOM   7274  C CG  . TYR E 1 159 ? -13.307  -69.459  33.480  1.00 207.00 ? 159 TYR E CG  1 
ATOM   7275  C CD1 . TYR E 1 159 ? -14.584  -69.985  33.299  1.00 207.95 ? 159 TYR E CD1 1 
ATOM   7276  C CD2 . TYR E 1 159 ? -12.218  -70.289  33.224  1.00 207.93 ? 159 TYR E CD2 1 
ATOM   7277  C CE1 . TYR E 1 159 ? -14.773  -71.311  32.907  1.00 207.84 ? 159 TYR E CE1 1 
ATOM   7278  C CE2 . TYR E 1 159 ? -12.395  -71.612  32.821  1.00 208.29 ? 159 TYR E CE2 1 
ATOM   7279  C CZ  . TYR E 1 159 ? -13.675  -72.122  32.669  1.00 213.79 ? 159 TYR E CZ  1 
ATOM   7280  O OH  . TYR E 1 159 ? -13.848  -73.428  32.275  1.00 213.54 ? 159 TYR E OH  1 
ATOM   7281  N N   . PRO E 1 160 ? -10.984  -68.031  36.515  1.00 207.98 ? 160 PRO E N   1 
ATOM   7282  C CA  . PRO E 1 160 ? -10.004  -68.840  37.277  1.00 207.87 ? 160 PRO E CA  1 
ATOM   7283  C C   . PRO E 1 160 ? -10.393  -69.217  38.710  1.00 210.62 ? 160 PRO E C   1 
ATOM   7284  O O   . PRO E 1 160 ? -9.845   -70.188  39.237  1.00 209.71 ? 160 PRO E O   1 
ATOM   7285  C CB  . PRO E 1 160 ? -8.733   -67.982  37.255  1.00 210.77 ? 160 PRO E CB  1 
ATOM   7286  C CG  . PRO E 1 160 ? -8.915   -67.052  36.113  1.00 215.76 ? 160 PRO E CG  1 
ATOM   7287  C CD  . PRO E 1 160 ? -10.378  -66.748  36.103  1.00 210.46 ? 160 PRO E CD  1 
ATOM   7288  N N   . LYS E 1 161 ? -11.324  -68.466  39.338  1.00 206.93 ? 161 LYS E N   1 
ATOM   7289  C CA  . LYS E 1 161 ? -11.800  -68.735  40.699  1.00 206.46 ? 161 LYS E CA  1 
ATOM   7290  C C   . LYS E 1 161 ? -12.683  -69.992  40.743  1.00 210.22 ? 161 LYS E C   1 
ATOM   7291  O O   . LYS E 1 161 ? -12.663  -70.715  41.741  1.00 209.34 ? 161 LYS E O   1 
ATOM   7292  C CB  . LYS E 1 161 ? -12.561  -67.521  41.264  1.00 208.96 ? 161 LYS E CB  1 
ATOM   7293  C CG  . LYS E 1 161 ? -12.754  -67.563  42.780  1.00 217.07 ? 161 LYS E CG  1 
ATOM   7294  C CD  . LYS E 1 161 ? -13.762  -66.530  43.264  1.00 222.65 ? 161 LYS E CD  1 
ATOM   7295  C CE  . LYS E 1 161 ? -14.114  -66.708  44.723  1.00 225.37 ? 161 LYS E CE  1 
ATOM   7296  N NZ  . LYS E 1 161 ? -15.023  -67.864  44.946  1.00 227.92 ? 161 LYS E NZ  1 
ATOM   7297  N N   . TYR E 1 162 ? -13.451  -70.245  39.661  1.00 207.30 ? 162 TYR E N   1 
ATOM   7298  C CA  . TYR E 1 162 ? -14.375  -71.381  39.536  1.00 206.90 ? 162 TYR E CA  1 
ATOM   7299  C C   . TYR E 1 162 ? -13.990  -72.393  38.417  1.00 210.75 ? 162 TYR E C   1 
ATOM   7300  O O   . TYR E 1 162 ? -14.765  -73.318  38.147  1.00 210.26 ? 162 TYR E O   1 
ATOM   7301  C CB  . TYR E 1 162 ? -15.827  -70.871  39.354  1.00 208.10 ? 162 TYR E CB  1 
ATOM   7302  C CG  . TYR E 1 162 ? -16.424  -70.203  40.579  1.00 210.43 ? 162 TYR E CG  1 
ATOM   7303  C CD1 . TYR E 1 162 ? -16.197  -68.855  40.845  1.00 213.13 ? 162 TYR E CD1 1 
ATOM   7304  C CD2 . TYR E 1 162 ? -17.261  -70.905  41.442  1.00 211.05 ? 162 TYR E CD2 1 
ATOM   7305  C CE1 . TYR E 1 162 ? -16.753  -68.232  41.964  1.00 214.44 ? 162 TYR E CE1 1 
ATOM   7306  C CE2 . TYR E 1 162 ? -17.827  -70.291  42.562  1.00 212.43 ? 162 TYR E CE2 1 
ATOM   7307  C CZ  . TYR E 1 162 ? -17.566  -68.954  42.822  1.00 219.20 ? 162 TYR E CZ  1 
ATOM   7308  O OH  . TYR E 1 162 ? -18.117  -68.336  43.919  1.00 218.51 ? 162 TYR E OH  1 
ATOM   7309  N N   . SER E 1 163 ? -12.792  -72.227  37.789  1.00 207.09 ? 163 SER E N   1 
ATOM   7310  C CA  . SER E 1 163 ? -12.281  -73.088  36.707  1.00 206.53 ? 163 SER E CA  1 
ATOM   7311  C C   . SER E 1 163 ? -12.072  -74.545  37.134  1.00 209.26 ? 163 SER E C   1 
ATOM   7312  O O   . SER E 1 163 ? -12.380  -75.455  36.359  1.00 208.68 ? 163 SER E O   1 
ATOM   7313  C CB  . SER E 1 163 ? -10.987  -72.524  36.125  1.00 210.65 ? 163 SER E CB  1 
ATOM   7314  O OG  . SER E 1 163 ? -10.558  -73.262  34.992  1.00 219.28 ? 163 SER E OG  1 
ATOM   7315  N N   . GLU E 1 164 ? -11.542  -74.760  38.357  1.00 204.92 ? 164 GLU E N   1 
ATOM   7316  C CA  . GLU E 1 164 ? -11.287  -76.088  38.925  1.00 203.61 ? 164 GLU E CA  1 
ATOM   7317  C C   . GLU E 1 164 ? -12.591  -76.822  39.299  1.00 205.05 ? 164 GLU E C   1 
ATOM   7318  O O   . GLU E 1 164 ? -12.661  -78.050  39.195  1.00 204.04 ? 164 GLU E O   1 
ATOM   7319  C CB  . GLU E 1 164 ? -10.283  -76.018  40.104  1.00 204.88 ? 164 GLU E CB  1 
ATOM   7320  C CG  . GLU E 1 164 ? -10.800  -75.452  41.424  1.00 214.02 ? 164 GLU E CG  1 
ATOM   7321  C CD  . GLU E 1 164 ? -11.142  -73.974  41.461  1.00 228.75 ? 164 GLU E CD  1 
ATOM   7322  O OE1 . GLU E 1 164 ? -10.216  -73.140  41.331  1.00 222.64 ? 164 GLU E OE1 1 
ATOM   7323  O OE2 . GLU E 1 164 ? -12.335  -73.651  41.660  1.00 216.27 ? 164 GLU E OE2 1 
ATOM   7324  N N   . GLU E 1 165 ? -13.620  -76.052  39.710  1.00 200.27 ? 165 GLU E N   1 
ATOM   7325  C CA  . GLU E 1 165 ? -14.948  -76.533  40.094  1.00 199.06 ? 165 GLU E CA  1 
ATOM   7326  C C   . GLU E 1 165 ? -15.696  -77.066  38.863  1.00 200.72 ? 165 GLU E C   1 
ATOM   7327  O O   . GLU E 1 165 ? -16.387  -78.082  38.958  1.00 199.99 ? 165 GLU E O   1 
ATOM   7328  C CB  . GLU E 1 165 ? -15.736  -75.388  40.755  1.00 200.80 ? 165 GLU E CB  1 
ATOM   7329  C CG  . GLU E 1 165 ? -17.030  -75.807  41.430  1.00 212.20 ? 165 GLU E CG  1 
ATOM   7330  C CD  . GLU E 1 165 ? -17.895  -74.632  41.838  1.00 235.87 ? 165 GLU E CD  1 
ATOM   7331  O OE1 . GLU E 1 165 ? -17.626  -74.044  42.910  1.00 232.60 ? 165 GLU E OE1 1 
ATOM   7332  O OE2 . GLU E 1 165 ? -18.824  -74.283  41.074  1.00 231.69 ? 165 GLU E OE2 1 
ATOM   7333  N N   . ALA E 1 166 ? -15.540  -76.376  37.715  1.00 195.82 ? 166 ALA E N   1 
ATOM   7334  C CA  . ALA E 1 166 ? -16.168  -76.711  36.436  1.00 194.71 ? 166 ALA E CA  1 
ATOM   7335  C C   . ALA E 1 166 ? -15.694  -78.045  35.859  1.00 196.01 ? 166 ALA E C   1 
ATOM   7336  O O   . ALA E 1 166 ? -16.517  -78.788  35.326  1.00 194.95 ? 166 ALA E O   1 
ATOM   7337  C CB  . ALA E 1 166 ? -15.943  -75.591  35.432  1.00 195.73 ? 166 ALA E CB  1 
ATOM   7338  N N   . LYS E 1 167 ? -14.382  -78.352  35.971  1.00 191.45 ? 167 LYS E N   1 
ATOM   7339  C CA  . LYS E 1 167 ? -13.793  -79.598  35.465  1.00 190.77 ? 167 LYS E CA  1 
ATOM   7340  C C   . LYS E 1 167 ? -14.336  -80.839  36.177  1.00 192.20 ? 167 LYS E C   1 
ATOM   7341  O O   . LYS E 1 167 ? -14.516  -81.872  35.531  1.00 191.96 ? 167 LYS E O   1 
ATOM   7342  C CB  . LYS E 1 167 ? -12.258  -79.552  35.502  1.00 193.95 ? 167 LYS E CB  1 
ATOM   7343  C CG  . LYS E 1 167 ? -11.605  -80.440  34.446  1.00 210.12 ? 167 LYS E CG  1 
ATOM   7344  C CD  . LYS E 1 167 ? -10.091  -80.499  34.603  1.00 221.00 ? 167 LYS E CD  1 
ATOM   7345  C CE  . LYS E 1 167 ? -9.432   -81.405  33.590  1.00 230.89 ? 167 LYS E CE  1 
ATOM   7346  N NZ  . LYS E 1 167 ? -9.373   -80.784  32.239  1.00 239.65 ? 167 LYS E NZ  1 
ATOM   7347  N N   . LEU E 1 168 ? -14.622  -80.725  37.493  1.00 186.53 ? 168 LEU E N   1 
ATOM   7348  C CA  . LEU E 1 168 ? -15.192  -81.800  38.314  1.00 184.90 ? 168 LEU E CA  1 
ATOM   7349  C C   . LEU E 1 168 ? -16.635  -82.094  37.860  1.00 186.88 ? 168 LEU E C   1 
ATOM   7350  O O   . LEU E 1 168 ? -17.054  -83.255  37.859  1.00 185.99 ? 168 LEU E O   1 
ATOM   7351  C CB  . LEU E 1 168 ? -15.160  -81.403  39.804  1.00 184.51 ? 168 LEU E CB  1 
ATOM   7352  C CG  . LEU E 1 168 ? -15.286  -82.540  40.824  1.00 188.45 ? 168 LEU E CG  1 
ATOM   7353  C CD1 . LEU E 1 168 ? -13.925  -82.961  41.344  1.00 188.25 ? 168 LEU E CD1 1 
ATOM   7354  C CD2 . LEU E 1 168 ? -16.156  -82.127  41.994  1.00 190.23 ? 168 LEU E CD2 1 
ATOM   7355  N N   . ASN E 1 169 ? -17.373  -81.036  37.452  1.00 182.43 ? 169 ASN E N   1 
ATOM   7356  C CA  . ASN E 1 169 ? -18.755  -81.114  36.973  1.00 181.66 ? 169 ASN E CA  1 
ATOM   7357  C C   . ASN E 1 169 ? -18.856  -81.467  35.483  1.00 184.56 ? 169 ASN E C   1 
ATOM   7358  O O   . ASN E 1 169 ? -19.880  -82.002  35.059  1.00 183.61 ? 169 ASN E O   1 
ATOM   7359  C CB  . ASN E 1 169 ? -19.514  -79.830  37.297  1.00 181.01 ? 169 ASN E CB  1 
ATOM   7360  C CG  . ASN E 1 169 ? -19.839  -79.688  38.764  1.00 197.15 ? 169 ASN E CG  1 
ATOM   7361  O OD1 . ASN E 1 169 ? -20.853  -80.197  39.253  1.00 189.63 ? 169 ASN E OD1 1 
ATOM   7362  N ND2 . ASN E 1 169 ? -18.984  -78.994  39.502  1.00 187.20 ? 169 ASN E ND2 1 
ATOM   7363  N N   . ARG E 1 170 ? -17.797  -81.179  34.697  1.00 181.05 ? 170 ARG E N   1 
ATOM   7364  C CA  . ARG E 1 170 ? -17.732  -81.499  33.268  1.00 180.99 ? 170 ARG E CA  1 
ATOM   7365  C C   . ARG E 1 170 ? -17.401  -82.980  33.060  1.00 186.12 ? 170 ARG E C   1 
ATOM   7366  O O   . ARG E 1 170 ? -17.998  -83.617  32.192  1.00 185.84 ? 170 ARG E O   1 
ATOM   7367  C CB  . ARG E 1 170 ? -16.722  -80.601  32.537  1.00 179.59 ? 170 ARG E CB  1 
ATOM   7368  C CG  . ARG E 1 170 ? -17.314  -79.267  32.113  1.00 184.42 ? 170 ARG E CG  1 
ATOM   7369  C CD  . ARG E 1 170 ? -16.349  -78.453  31.282  1.00 186.62 ? 170 ARG E CD  1 
ATOM   7370  N NE  . ARG E 1 170 ? -15.533  -77.555  32.101  1.00 186.91 ? 170 ARG E NE  1 
ATOM   7371  C CZ  . ARG E 1 170 ? -14.273  -77.794  32.449  1.00 194.94 ? 170 ARG E CZ  1 
ATOM   7372  N NH1 . ARG E 1 170 ? -13.673  -78.916  32.070  1.00 182.10 ? 170 ARG E NH1 1 
ATOM   7373  N NH2 . ARG E 1 170 ? -13.604  -76.916  33.185  1.00 176.37 ? 170 ARG E NH2 1 
ATOM   7374  N N   . GLU E 1 171 ? -16.468  -83.525  33.874  1.00 183.40 ? 171 GLU E N   1 
ATOM   7375  C CA  . GLU E 1 171 ? -16.035  -84.928  33.837  1.00 183.79 ? 171 GLU E CA  1 
ATOM   7376  C C   . GLU E 1 171 ? -17.142  -85.903  34.278  1.00 188.25 ? 171 GLU E C   1 
ATOM   7377  O O   . GLU E 1 171 ? -17.313  -86.943  33.638  1.00 188.48 ? 171 GLU E O   1 
ATOM   7378  C CB  . GLU E 1 171 ? -14.748  -85.139  34.664  1.00 184.97 ? 171 GLU E CB  1 
ATOM   7379  C CG  . GLU E 1 171 ? -13.476  -84.694  33.954  1.00 194.27 ? 171 GLU E CG  1 
ATOM   7380  C CD  . GLU E 1 171 ? -12.167  -84.954  34.678  1.00 201.87 ? 171 GLU E CD  1 
ATOM   7381  O OE1 . GLU E 1 171 ? -11.885  -86.131  34.999  1.00 181.49 ? 171 GLU E OE1 1 
ATOM   7382  O OE2 . GLU E 1 171 ? -11.388  -83.989  34.860  1.00 191.66 ? 171 GLU E OE2 1 
ATOM   7383  N N   . GLU E 1 172 ? -17.892  -85.565  35.355  1.00 184.52 ? 172 GLU E N   1 
ATOM   7384  C CA  . GLU E 1 172 ? -18.993  -86.389  35.882  1.00 184.35 ? 172 GLU E CA  1 
ATOM   7385  C C   . GLU E 1 172 ? -20.233  -86.403  34.966  1.00 188.52 ? 172 GLU E C   1 
ATOM   7386  O O   . GLU E 1 172 ? -21.040  -87.334  35.048  1.00 188.08 ? 172 GLU E O   1 
ATOM   7387  C CB  . GLU E 1 172 ? -19.366  -85.976  37.319  1.00 185.43 ? 172 GLU E CB  1 
ATOM   7388  C CG  . GLU E 1 172 ? -18.536  -86.669  38.391  1.00 195.54 ? 172 GLU E CG  1 
ATOM   7389  C CD  . GLU E 1 172 ? -19.178  -87.862  39.078  1.00 212.95 ? 172 GLU E CD  1 
ATOM   7390  O OE1 . GLU E 1 172 ? -19.415  -88.893  38.408  1.00 203.48 ? 172 GLU E OE1 1 
ATOM   7391  O OE2 . GLU E 1 172 ? -19.391  -87.785  40.309  1.00 207.31 ? 172 GLU E OE2 1 
ATOM   7392  N N   . ILE E 1 173 ? -20.374  -85.379  34.095  1.00 185.11 ? 173 ILE E N   1 
ATOM   7393  C CA  . ILE E 1 173 ? -21.486  -85.245  33.150  1.00 184.79 ? 173 ILE E CA  1 
ATOM   7394  C C   . ILE E 1 173 ? -21.136  -85.899  31.791  1.00 188.79 ? 173 ILE E C   1 
ATOM   7395  O O   . ILE E 1 173 ? -21.968  -86.627  31.243  1.00 188.84 ? 173 ILE E O   1 
ATOM   7396  C CB  . ILE E 1 173 ? -21.961  -83.754  33.063  1.00 187.26 ? 173 ILE E CB  1 
ATOM   7397  C CG1 . ILE E 1 173 ? -23.161  -83.493  34.007  1.00 187.38 ? 173 ILE E CG1 1 
ATOM   7398  C CG2 . ILE E 1 173 ? -22.294  -83.288  31.637  1.00 187.77 ? 173 ILE E CG2 1 
ATOM   7399  C CD1 . ILE E 1 173 ? -22.850  -83.370  35.517  1.00 192.77 ? 173 ILE E CD1 1 
ATOM   7400  N N   . ASP E 1 174 ? -19.909  -85.668  31.273  1.00 184.84 ? 174 ASP E N   1 
ATOM   7401  C CA  . ASP E 1 174 ? -19.462  -86.233  29.996  1.00 201.52 ? 174 ASP E CA  1 
ATOM   7402  C C   . ASP E 1 174 ? -19.040  -87.697  30.135  1.00 194.19 ? 174 ASP E C   1 
ATOM   7403  O O   . ASP E 1 174 ? -18.271  -88.043  31.030  1.00 139.94 ? 174 ASP E O   1 
ATOM   7404  C CB  . ASP E 1 174 ? -18.331  -85.389  29.373  1.00 203.43 ? 174 ASP E CB  1 
ATOM   7405  C CG  . ASP E 1 174 ? -18.675  -83.929  29.124  1.00 210.14 ? 174 ASP E CG  1 
ATOM   7406  O OD1 . ASP E 1 174 ? -19.836  -83.644  28.753  1.00 209.67 ? 174 ASP E OD1 1 
ATOM   7407  O OD2 . ASP E 1 174 ? -17.776  -83.075  29.279  1.00 215.00 ? 174 ASP E OD2 1 
ATOM   7408  N N   . ASN F 2 11  ? -42.129  -52.567  29.483  1.00 136.26 ? 20  ASN F N   1 
ATOM   7409  C CA  . ASN F 2 11  ? -42.447  -52.907  28.099  1.00 134.67 ? 20  ASN F CA  1 
ATOM   7410  C C   . ASN F 2 11  ? -43.918  -52.677  27.734  1.00 137.95 ? 20  ASN F C   1 
ATOM   7411  O O   . ASN F 2 11  ? -44.244  -52.621  26.546  1.00 136.57 ? 20  ASN F O   1 
ATOM   7412  C CB  . ASN F 2 11  ? -42.028  -54.342  27.778  1.00 135.52 ? 20  ASN F CB  1 
ATOM   7413  C CG  . ASN F 2 11  ? -40.546  -54.601  27.932  1.00 160.19 ? 20  ASN F CG  1 
ATOM   7414  O OD1 . ASN F 2 11  ? -40.086  -54.908  29.038  1.00 154.43 ? 20  ASN F OD1 1 
ATOM   7415  N ND2 . ASN F 2 11  ? -39.822  -54.456  26.777  1.00 153.70 ? 20  ASN F ND2 1 
ATOM   7416  N N   . ASN F 2 12  ? -44.785  -52.519  28.757  1.00 135.25 ? 21  ASN F N   1 
ATOM   7417  C CA  . ASN F 2 12  ? -46.241  -52.313  28.697  1.00 133.94 ? 21  ASN F CA  1 
ATOM   7418  C C   . ASN F 2 12  ? -46.748  -51.287  27.633  1.00 136.44 ? 21  ASN F C   1 
ATOM   7419  O O   . ASN F 2 12  ? -47.885  -51.411  27.168  1.00 134.85 ? 21  ASN F O   1 
ATOM   7420  C CB  . ASN F 2 12  ? -46.735  -51.923  30.100  1.00 136.05 ? 21  ASN F CB  1 
ATOM   7421  C CG  . ASN F 2 12  ? -48.196  -51.616  30.214  1.00 165.51 ? 21  ASN F CG  1 
ATOM   7422  O OD1 . ASN F 2 12  ? -48.590  -50.455  30.357  1.00 160.54 ? 21  ASN F OD1 1 
ATOM   7423  N ND2 . ASN F 2 12  ? -49.036  -52.644  30.196  1.00 158.00 ? 21  ASN F ND2 1 
ATOM   7424  N N   . SER F 2 13  ? -45.887  -50.320  27.228  1.00 132.82 ? 22  SER F N   1 
ATOM   7425  C CA  . SER F 2 13  ? -46.171  -49.250  26.261  1.00 131.26 ? 22  SER F CA  1 
ATOM   7426  C C   . SER F 2 13  ? -46.730  -49.728  24.920  1.00 132.15 ? 22  SER F C   1 
ATOM   7427  O O   . SER F 2 13  ? -46.313  -50.763  24.402  1.00 131.44 ? 22  SER F O   1 
ATOM   7428  C CB  . SER F 2 13  ? -44.935  -48.384  26.041  1.00 135.15 ? 22  SER F CB  1 
ATOM   7429  O OG  . SER F 2 13  ? -45.257  -47.149  25.422  1.00 141.54 ? 22  SER F OG  1 
ATOM   7430  N N   . THR F 2 14  ? -47.673  -48.948  24.367  1.00 126.92 ? 23  THR F N   1 
ATOM   7431  C CA  . THR F 2 14  ? -48.354  -49.222  23.101  1.00 125.76 ? 23  THR F CA  1 
ATOM   7432  C C   . THR F 2 14  ? -47.727  -48.540  21.885  1.00 130.73 ? 23  THR F C   1 
ATOM   7433  O O   . THR F 2 14  ? -47.846  -49.083  20.783  1.00 130.32 ? 23  THR F O   1 
ATOM   7434  C CB  . THR F 2 14  ? -49.847  -48.887  23.199  1.00 128.92 ? 23  THR F CB  1 
ATOM   7435  O OG1 . THR F 2 14  ? -50.453  -49.171  21.937  1.00 126.67 ? 23  THR F OG1 1 
ATOM   7436  C CG2 . THR F 2 14  ? -50.115  -47.423  23.600  1.00 126.52 ? 23  THR F CG2 1 
ATOM   7437  N N   . ASP F 2 15  ? -47.121  -47.335  22.081  1.00 128.27 ? 24  ASP F N   1 
ATOM   7438  C CA  . ASP F 2 15  ? -46.478  -46.464  21.076  1.00 128.01 ? 24  ASP F CA  1 
ATOM   7439  C C   . ASP F 2 15  ? -45.883  -47.228  19.890  1.00 129.98 ? 24  ASP F C   1 
ATOM   7440  O O   . ASP F 2 15  ? -45.084  -48.143  20.095  1.00 130.28 ? 24  ASP F O   1 
ATOM   7441  C CB  . ASP F 2 15  ? -45.409  -45.567  21.735  1.00 130.83 ? 24  ASP F CB  1 
ATOM   7442  C CG  . ASP F 2 15  ? -45.884  -44.624  22.834  1.00 145.52 ? 24  ASP F CG  1 
ATOM   7443  O OD1 . ASP F 2 15  ? -47.098  -44.294  22.861  1.00 146.02 ? 24  ASP F OD1 1 
ATOM   7444  O OD2 . ASP F 2 15  ? -45.031  -44.171  23.638  1.00 152.87 ? 24  ASP F OD2 1 
ATOM   7445  N N   . THR F 2 16  ? -46.306  -46.885  18.662  1.00 124.51 ? 25  THR F N   1 
ATOM   7446  C CA  . THR F 2 16  ? -45.873  -47.571  17.445  1.00 123.54 ? 25  THR F CA  1 
ATOM   7447  C C   . THR F 2 16  ? -45.035  -46.669  16.510  1.00 124.42 ? 25  THR F C   1 
ATOM   7448  O O   . THR F 2 16  ? -45.363  -45.497  16.304  1.00 123.41 ? 25  THR F O   1 
ATOM   7449  C CB  . THR F 2 16  ? -47.082  -48.229  16.742  1.00 134.70 ? 25  THR F CB  1 
ATOM   7450  O OG1 . THR F 2 16  ? -46.632  -48.976  15.613  1.00 135.10 ? 25  THR F OG1 1 
ATOM   7451  C CG2 . THR F 2 16  ? -48.171  -47.227  16.325  1.00 134.69 ? 25  THR F CG2 1 
ATOM   7452  N N   . VAL F 2 17  ? -43.943  -47.241  15.960  1.00 119.52 ? 26  VAL F N   1 
ATOM   7453  C CA  . VAL F 2 17  ? -43.013  -46.582  15.031  1.00 118.59 ? 26  VAL F CA  1 
ATOM   7454  C C   . VAL F 2 17  ? -43.033  -47.294  13.670  1.00 122.11 ? 26  VAL F C   1 
ATOM   7455  O O   . VAL F 2 17  ? -43.400  -48.464  13.605  1.00 122.19 ? 26  VAL F O   1 
ATOM   7456  C CB  . VAL F 2 17  ? -41.564  -46.443  15.590  1.00 122.34 ? 26  VAL F CB  1 
ATOM   7457  C CG1 . VAL F 2 17  ? -41.534  -45.665  16.899  1.00 122.75 ? 26  VAL F CG1 1 
ATOM   7458  C CG2 . VAL F 2 17  ? -40.874  -47.796  15.747  1.00 122.28 ? 26  VAL F CG2 1 
ATOM   7459  N N   . ASP F 2 18  ? -42.640  -46.603  12.591  1.00 117.83 ? 27  ASP F N   1 
ATOM   7460  C CA  . ASP F 2 18  ? -42.617  -47.205  11.255  1.00 117.79 ? 27  ASP F CA  1 
ATOM   7461  C C   . ASP F 2 18  ? -41.216  -47.162  10.674  1.00 119.95 ? 27  ASP F C   1 
ATOM   7462  O O   . ASP F 2 18  ? -40.548  -46.132  10.778  1.00 119.47 ? 27  ASP F O   1 
ATOM   7463  C CB  . ASP F 2 18  ? -43.590  -46.484  10.311  1.00 120.76 ? 27  ASP F CB  1 
ATOM   7464  C CG  . ASP F 2 18  ? -45.042  -46.872  10.468  1.00 137.63 ? 27  ASP F CG  1 
ATOM   7465  O OD1 . ASP F 2 18  ? -45.717  -46.297  11.344  1.00 140.23 ? 27  ASP F OD1 1 
ATOM   7466  O OD2 . ASP F 2 18  ? -45.525  -47.685  9.662   1.00 144.05 ? 27  ASP F OD2 1 
ATOM   7467  N N   . THR F 2 19  ? -40.768  -48.272  10.061  1.00 114.96 ? 28  THR F N   1 
ATOM   7468  C CA  . THR F 2 19  ? -39.443  -48.357  9.434   1.00 112.60 ? 28  THR F CA  1 
ATOM   7469  C C   . THR F 2 19  ? -39.586  -48.472  7.907   1.00 114.87 ? 28  THR F C   1 
ATOM   7470  O O   . THR F 2 19  ? -40.687  -48.285  7.396   1.00 115.26 ? 28  THR F O   1 
ATOM   7471  C CB  . THR F 2 19  ? -38.580  -49.465  10.070  1.00 118.20 ? 28  THR F CB  1 
ATOM   7472  O OG1 . THR F 2 19  ? -39.103  -50.747  9.736   1.00 117.43 ? 28  THR F OG1 1 
ATOM   7473  C CG2 . THR F 2 19  ? -38.423  -49.321  11.577  1.00 116.48 ? 28  THR F CG2 1 
ATOM   7474  N N   . VAL F 2 20  ? -38.486  -48.756  7.180   1.00 109.54 ? 29  VAL F N   1 
ATOM   7475  C CA  . VAL F 2 20  ? -38.510  -48.905  5.715   1.00 108.93 ? 29  VAL F CA  1 
ATOM   7476  C C   . VAL F 2 20  ? -39.042  -50.304  5.356   1.00 114.32 ? 29  VAL F C   1 
ATOM   7477  O O   . VAL F 2 20  ? -39.751  -50.461  4.357   1.00 114.87 ? 29  VAL F O   1 
ATOM   7478  C CB  . VAL F 2 20  ? -37.129  -48.637  5.058   1.00 110.17 ? 29  VAL F CB  1 
ATOM   7479  C CG1 . VAL F 2 20  ? -37.284  -48.317  3.574   1.00 109.61 ? 29  VAL F CG1 1 
ATOM   7480  C CG2 . VAL F 2 20  ? -36.371  -47.520  5.776   1.00 108.55 ? 29  VAL F CG2 1 
ATOM   7481  N N   . LEU F 2 21  ? -38.694  -51.310  6.187   1.00 122.78 ? 30  LEU F N   1 
ATOM   7482  C CA  . LEU F 2 21  ? -39.107  -52.706  6.033   1.00 124.07 ? 30  LEU F CA  1 
ATOM   7483  C C   . LEU F 2 21  ? -40.506  -52.910  6.655   1.00 129.25 ? 30  LEU F C   1 
ATOM   7484  O O   . LEU F 2 21  ? -41.528  -52.753  5.975   1.00 129.28 ? 30  LEU F O   1 
ATOM   7485  C CB  . LEU F 2 21  ? -38.086  -53.661  6.717   1.00 125.12 ? 30  LEU F CB  1 
ATOM   7486  C CG  . LEU F 2 21  ? -36.607  -53.620  6.307   1.00 129.50 ? 30  LEU F CG  1 
ATOM   7487  C CD1 . LEU F 2 21  ? -35.729  -54.208  7.399   1.00 130.84 ? 30  LEU F CD1 1 
ATOM   7488  C CD2 . LEU F 2 21  ? -36.368  -54.373  5.007   1.00 133.26 ? 30  LEU F CD2 1 
ATOM   7489  N N   . GLU F 2 22  ? -40.523  -53.249  7.961   1.00 126.68 ? 31  GLU F N   1 
ATOM   7490  C CA  . GLU F 2 22  ? -41.683  -53.528  8.800   1.00 127.55 ? 31  GLU F CA  1 
ATOM   7491  C C   . GLU F 2 22  ? -42.369  -52.219  9.176   1.00 131.30 ? 31  GLU F C   1 
ATOM   7492  O O   . GLU F 2 22  ? -41.747  -51.352  9.792   1.00 129.96 ? 31  GLU F O   1 
ATOM   7493  C CB  . GLU F 2 22  ? -41.212  -54.268  10.064  1.00 129.82 ? 31  GLU F CB  1 
ATOM   7494  C CG  . GLU F 2 22  ? -42.253  -55.162  10.712  1.00 141.96 ? 31  GLU F CG  1 
ATOM   7495  C CD  . GLU F 2 22  ? -41.833  -55.767  12.040  1.00 165.84 ? 31  GLU F CD  1 
ATOM   7496  O OE1 . GLU F 2 22  ? -40.760  -56.412  12.100  1.00 159.23 ? 31  GLU F OE1 1 
ATOM   7497  O OE2 . GLU F 2 22  ? -42.610  -55.641  13.014  1.00 161.85 ? 31  GLU F OE2 1 
ATOM   7498  N N   . LYS F 2 23  ? -43.643  -52.068  8.792   1.00 129.22 ? 32  LYS F N   1 
ATOM   7499  C CA  . LYS F 2 23  ? -44.414  -50.862  9.096   1.00 128.92 ? 32  LYS F CA  1 
ATOM   7500  C C   . LYS F 2 23  ? -45.320  -51.070  10.319  1.00 134.95 ? 32  LYS F C   1 
ATOM   7501  O O   . LYS F 2 23  ? -45.878  -52.155  10.497  1.00 136.47 ? 32  LYS F O   1 
ATOM   7502  C CB  . LYS F 2 23  ? -45.208  -50.384  7.867   1.00 132.24 ? 32  LYS F CB  1 
ATOM   7503  C CG  . LYS F 2 23  ? -44.343  -49.907  6.691   1.00 142.02 ? 32  LYS F CG  1 
ATOM   7504  C CD  . LYS F 2 23  ? -43.881  -48.447  6.814   1.00 145.60 ? 32  LYS F CD  1 
ATOM   7505  C CE  . LYS F 2 23  ? -43.421  -47.852  5.496   1.00 150.03 ? 32  LYS F CE  1 
ATOM   7506  N NZ  . LYS F 2 23  ? -42.120  -48.405  5.024   1.00 152.99 ? 32  LYS F NZ  1 
ATOM   7507  N N   . ASN F 2 24  ? -45.443  -50.023  11.161  1.00 131.14 ? 33  ASN F N   1 
ATOM   7508  C CA  . ASN F 2 24  ? -46.212  -49.957  12.413  1.00 131.77 ? 33  ASN F CA  1 
ATOM   7509  C C   . ASN F 2 24  ? -45.788  -51.064  13.399  1.00 136.17 ? 33  ASN F C   1 
ATOM   7510  O O   . ASN F 2 24  ? -46.537  -52.008  13.665  1.00 137.72 ? 33  ASN F O   1 
ATOM   7511  C CB  . ASN F 2 24  ? -47.754  -49.885  12.194  1.00 136.66 ? 33  ASN F CB  1 
ATOM   7512  C CG  . ASN F 2 24  ? -48.369  -48.588  12.731  1.00 171.55 ? 33  ASN F CG  1 
ATOM   7513  O OD1 . ASN F 2 24  ? -47.647  -47.615  12.973  1.00 166.52 ? 33  ASN F OD1 1 
ATOM   7514  N ND2 . ASN F 2 24  ? -49.695  -48.454  12.972  1.00 170.11 ? 33  ASN F ND2 1 
ATOM   7515  N N   . VAL F 2 25  ? -44.560  -50.918  13.932  1.00 131.68 ? 34  VAL F N   1 
ATOM   7516  C CA  . VAL F 2 25  ? -43.904  -51.814  14.900  1.00 132.60 ? 34  VAL F CA  1 
ATOM   7517  C C   . VAL F 2 25  ? -44.033  -51.207  16.306  1.00 136.70 ? 34  VAL F C   1 
ATOM   7518  O O   . VAL F 2 25  ? -43.759  -50.015  16.480  1.00 135.32 ? 34  VAL F O   1 
ATOM   7519  C CB  . VAL F 2 25  ? -42.405  -52.060  14.548  1.00 136.33 ? 34  VAL F CB  1 
ATOM   7520  C CG1 . VAL F 2 25  ? -41.826  -53.228  15.345  1.00 138.12 ? 34  VAL F CG1 1 
ATOM   7521  C CG2 . VAL F 2 25  ? -42.204  -52.276  13.053  1.00 135.76 ? 34  VAL F CG2 1 
ATOM   7522  N N   . THR F 2 26  ? -44.425  -52.033  17.303  1.00 134.19 ? 35  THR F N   1 
ATOM   7523  C CA  . THR F 2 26  ? -44.581  -51.620  18.706  1.00 133.58 ? 35  THR F CA  1 
ATOM   7524  C C   . THR F 2 26  ? -43.205  -51.303  19.299  1.00 134.76 ? 35  THR F C   1 
ATOM   7525  O O   . THR F 2 26  ? -42.251  -52.036  19.041  1.00 135.53 ? 35  THR F O   1 
ATOM   7526  C CB  . THR F 2 26  ? -45.335  -52.704  19.511  1.00 146.17 ? 35  THR F CB  1 
ATOM   7527  O OG1 . THR F 2 26  ? -46.413  -53.222  18.724  1.00 148.55 ? 35  THR F OG1 1 
ATOM   7528  C CG2 . THR F 2 26  ? -45.866  -52.185  20.850  1.00 143.94 ? 35  THR F CG2 1 
ATOM   7529  N N   . VAL F 2 27  ? -43.098  -50.190  20.049  1.00 128.26 ? 36  VAL F N   1 
ATOM   7530  C CA  . VAL F 2 27  ? -41.855  -49.733  20.678  1.00 127.82 ? 36  VAL F CA  1 
ATOM   7531  C C   . VAL F 2 27  ? -42.140  -49.181  22.106  1.00 131.92 ? 36  VAL F C   1 
ATOM   7532  O O   . VAL F 2 27  ? -43.138  -48.484  22.307  1.00 130.25 ? 36  VAL F O   1 
ATOM   7533  C CB  . VAL F 2 27  ? -41.086  -48.770  19.730  1.00 129.65 ? 36  VAL F CB  1 
ATOM   7534  C CG1 . VAL F 2 27  ? -40.386  -47.647  20.470  1.00 129.56 ? 36  VAL F CG1 1 
ATOM   7535  C CG2 . VAL F 2 27  ? -40.095  -49.539  18.872  1.00 130.13 ? 36  VAL F CG2 1 
ATOM   7536  N N   . THR F 2 28  ? -41.296  -49.562  23.101  1.00 130.49 ? 37  THR F N   1 
ATOM   7537  C CA  . THR F 2 28  ? -41.434  -49.202  24.529  1.00 130.95 ? 37  THR F CA  1 
ATOM   7538  C C   . THR F 2 28  ? -41.232  -47.701  24.801  1.00 131.84 ? 37  THR F C   1 
ATOM   7539  O O   . THR F 2 28  ? -42.110  -47.055  25.374  1.00 130.43 ? 37  THR F O   1 
ATOM   7540  C CB  . THR F 2 28  ? -40.530  -50.078  25.422  1.00 141.93 ? 37  THR F CB  1 
ATOM   7541  O OG1 . THR F 2 28  ? -39.154  -49.871  25.091  1.00 141.45 ? 37  THR F OG1 1 
ATOM   7542  C CG2 . THR F 2 28  ? -40.867  -51.542  25.319  1.00 141.58 ? 37  THR F CG2 1 
ATOM   7543  N N   . HIS F 2 29  ? -40.079  -47.158  24.412  1.00 127.63 ? 38  HIS F N   1 
ATOM   7544  C CA  . HIS F 2 29  ? -39.790  -45.743  24.590  1.00 126.51 ? 38  HIS F CA  1 
ATOM   7545  C C   . HIS F 2 29  ? -39.710  -45.154  23.193  1.00 125.61 ? 38  HIS F C   1 
ATOM   7546  O O   . HIS F 2 29  ? -39.028  -45.718  22.340  1.00 124.99 ? 38  HIS F O   1 
ATOM   7547  C CB  . HIS F 2 29  ? -38.468  -45.549  25.350  1.00 131.00 ? 38  HIS F CB  1 
ATOM   7548  C CG  . HIS F 2 29  ? -38.371  -46.303  26.645  1.00 137.92 ? 38  HIS F CG  1 
ATOM   7549  N ND1 . HIS F 2 29  ? -38.360  -47.690  26.677  1.00 141.47 ? 38  HIS F ND1 1 
ATOM   7550  C CD2 . HIS F 2 29  ? -38.217  -45.838  27.908  1.00 142.17 ? 38  HIS F CD2 1 
ATOM   7551  C CE1 . HIS F 2 29  ? -38.248  -48.020  27.954  1.00 143.99 ? 38  HIS F CE1 1 
ATOM   7552  N NE2 . HIS F 2 29  ? -38.139  -46.940  28.731  1.00 144.83 ? 38  HIS F NE2 1 
ATOM   7553  N N   . SER F 2 30  ? -40.444  -44.056  22.941  1.00 118.60 ? 39  SER F N   1 
ATOM   7554  C CA  . SER F 2 30  ? -40.486  -43.359  21.646  1.00 115.72 ? 39  SER F CA  1 
ATOM   7555  C C   . SER F 2 30  ? -41.041  -41.950  21.773  1.00 117.14 ? 39  SER F C   1 
ATOM   7556  O O   . SER F 2 30  ? -41.951  -41.721  22.577  1.00 116.69 ? 39  SER F O   1 
ATOM   7557  C CB  . SER F 2 30  ? -41.311  -44.138  20.629  1.00 117.16 ? 39  SER F CB  1 
ATOM   7558  O OG  . SER F 2 30  ? -42.590  -44.423  21.162  1.00 124.62 ? 39  SER F OG  1 
ATOM   7559  N N   . VAL F 2 31  ? -40.514  -41.015  20.955  1.00 111.64 ? 40  VAL F N   1 
ATOM   7560  C CA  . VAL F 2 31  ? -40.920  -39.615  20.981  1.00 110.44 ? 40  VAL F CA  1 
ATOM   7561  C C   . VAL F 2 31  ? -41.557  -39.168  19.658  1.00 110.25 ? 40  VAL F C   1 
ATOM   7562  O O   . VAL F 2 31  ? -41.089  -39.548  18.582  1.00 108.52 ? 40  VAL F O   1 
ATOM   7563  C CB  . VAL F 2 31  ? -39.753  -38.701  21.434  1.00 116.32 ? 40  VAL F CB  1 
ATOM   7564  C CG1 . VAL F 2 31  ? -38.748  -38.436  20.310  1.00 116.26 ? 40  VAL F CG1 1 
ATOM   7565  C CG2 . VAL F 2 31  ? -40.270  -37.400  22.042  1.00 116.91 ? 40  VAL F CG2 1 
ATOM   7566  N N   . ASN F 2 32  ? -42.641  -38.369  19.766  1.00 105.54 ? 41  ASN F N   1 
ATOM   7567  C CA  . ASN F 2 32  ? -43.386  -37.816  18.635  1.00 104.70 ? 41  ASN F CA  1 
ATOM   7568  C C   . ASN F 2 32  ? -42.634  -36.598  18.080  1.00 108.72 ? 41  ASN F C   1 
ATOM   7569  O O   . ASN F 2 32  ? -41.705  -36.112  18.727  1.00 109.87 ? 41  ASN F O   1 
ATOM   7570  C CB  . ASN F 2 32  ? -44.812  -37.433  19.079  1.00 104.41 ? 41  ASN F CB  1 
ATOM   7571  C CG  . ASN F 2 32  ? -45.817  -37.165  17.966  1.00 126.48 ? 41  ASN F CG  1 
ATOM   7572  O OD1 . ASN F 2 32  ? -45.659  -37.556  16.800  1.00 121.25 ? 41  ASN F OD1 1 
ATOM   7573  N ND2 . ASN F 2 32  ? -46.904  -36.504  18.316  1.00 118.67 ? 41  ASN F ND2 1 
ATOM   7574  N N   . LEU F 2 33  ? -43.009  -36.128  16.872  1.00 103.78 ? 42  LEU F N   1 
ATOM   7575  C CA  . LEU F 2 33  ? -42.415  -34.952  16.218  1.00 103.51 ? 42  LEU F CA  1 
ATOM   7576  C C   . LEU F 2 33  ? -43.504  -34.049  15.652  1.00 108.47 ? 42  LEU F C   1 
ATOM   7577  O O   . LEU F 2 33  ? -43.295  -32.850  15.482  1.00 108.65 ? 42  LEU F O   1 
ATOM   7578  C CB  . LEU F 2 33  ? -41.478  -35.365  15.075  1.00 102.39 ? 42  LEU F CB  1 
ATOM   7579  C CG  . LEU F 2 33  ? -40.287  -36.240  15.421  1.00 105.74 ? 42  LEU F CG  1 
ATOM   7580  C CD1 . LEU F 2 33  ? -39.742  -36.896  14.185  1.00 105.22 ? 42  LEU F CD1 1 
ATOM   7581  C CD2 . LEU F 2 33  ? -39.207  -35.450  16.119  1.00 108.86 ? 42  LEU F CD2 1 
ATOM   7582  N N   . LEU F 2 34  ? -44.658  -34.646  15.347  1.00 105.87 ? 43  LEU F N   1 
ATOM   7583  C CA  . LEU F 2 34  ? -45.799  -34.006  14.718  1.00 108.13 ? 43  LEU F CA  1 
ATOM   7584  C C   . LEU F 2 34  ? -46.872  -33.555  15.710  1.00 111.85 ? 43  LEU F C   1 
ATOM   7585  O O   . LEU F 2 34  ? -47.219  -34.302  16.628  1.00 110.51 ? 43  LEU F O   1 
ATOM   7586  C CB  . LEU F 2 34  ? -46.385  -35.003  13.703  1.00 108.68 ? 43  LEU F CB  1 
ATOM   7587  C CG  . LEU F 2 34  ? -47.332  -34.464  12.640  1.00 117.25 ? 43  LEU F CG  1 
ATOM   7588  C CD1 . LEU F 2 34  ? -46.932  -34.962  11.276  1.00 117.38 ? 43  LEU F CD1 1 
ATOM   7589  C CD2 . LEU F 2 34  ? -48.755  -34.895  12.933  1.00 123.24 ? 43  LEU F CD2 1 
ATOM   7590  N N   . GLU F 2 35  ? -47.416  -32.335  15.488  1.00 109.30 ? 44  GLU F N   1 
ATOM   7591  C CA  . GLU F 2 35  ? -48.525  -31.766  16.252  1.00 109.88 ? 44  GLU F CA  1 
ATOM   7592  C C   . GLU F 2 35  ? -49.722  -31.596  15.320  1.00 115.42 ? 44  GLU F C   1 
ATOM   7593  O O   . GLU F 2 35  ? -49.658  -30.846  14.349  1.00 117.01 ? 44  GLU F O   1 
ATOM   7594  C CB  . GLU F 2 35  ? -48.155  -30.449  16.959  1.00 112.31 ? 44  GLU F CB  1 
ATOM   7595  C CG  . GLU F 2 35  ? -49.253  -29.930  17.885  1.00 125.01 ? 44  GLU F CG  1 
ATOM   7596  C CD  . GLU F 2 35  ? -49.433  -30.607  19.237  1.00 147.04 ? 44  GLU F CD  1 
ATOM   7597  O OE1 . GLU F 2 35  ? -49.575  -29.873  20.241  1.00 148.69 ? 44  GLU F OE1 1 
ATOM   7598  O OE2 . GLU F 2 35  ? -49.494  -31.858  19.293  1.00 135.46 ? 44  GLU F OE2 1 
ATOM   7599  N N   . ASP F 2 36  ? -50.792  -32.336  15.607  1.00 96.06  ? 45  ASP F N   1 
ATOM   7600  C CA  . ASP F 2 36  ? -52.033  -32.359  14.839  1.00 95.70  ? 45  ASP F CA  1 
ATOM   7601  C C   . ASP F 2 36  ? -53.138  -31.568  15.529  1.00 97.64  ? 45  ASP F C   1 
ATOM   7602  O O   . ASP F 2 36  ? -54.151  -31.233  14.907  1.00 97.28  ? 45  ASP F O   1 
ATOM   7603  C CB  . ASP F 2 36  ? -52.478  -33.818  14.613  1.00 99.12  ? 45  ASP F CB  1 
ATOM   7604  C CG  . ASP F 2 36  ? -52.211  -34.742  15.788  1.00 114.44 ? 45  ASP F CG  1 
ATOM   7605  O OD1 . ASP F 2 36  ? -51.094  -35.296  15.861  1.00 117.40 ? 45  ASP F OD1 1 
ATOM   7606  O OD2 . ASP F 2 36  ? -53.107  -34.879  16.655  1.00 119.74 ? 45  ASP F OD2 1 
ATOM   7607  N N   . LYS F 2 37  ? -52.904  -31.224  16.800  1.00 93.25  ? 46  LYS F N   1 
ATOM   7608  C CA  . LYS F 2 37  ? -53.856  -30.551  17.672  1.00 91.73  ? 46  LYS F CA  1 
ATOM   7609  C C   . LYS F 2 37  ? -53.722  -29.016  17.706  1.00 95.17  ? 46  LYS F C   1 
ATOM   7610  O O   . LYS F 2 37  ? -52.627  -28.476  17.892  1.00 95.21  ? 46  LYS F O   1 
ATOM   7611  C CB  . LYS F 2 37  ? -53.769  -31.158  19.083  1.00 94.02  ? 46  LYS F CB  1 
ATOM   7612  C CG  . LYS F 2 37  ? -54.100  -32.649  19.105  1.00 112.98 ? 46  LYS F CG  1 
ATOM   7613  C CD  . LYS F 2 37  ? -53.716  -33.312  20.407  1.00 127.58 ? 46  LYS F CD  1 
ATOM   7614  C CE  . LYS F 2 37  ? -54.215  -34.737  20.444  1.00 143.61 ? 46  LYS F CE  1 
ATOM   7615  N NZ  . LYS F 2 37  ? -54.007  -35.373  21.775  1.00 152.23 ? 46  LYS F NZ  1 
ATOM   7616  N N   . HIS F 2 38  ? -54.872  -28.328  17.545  1.00 91.05  ? 47  HIS F N   1 
ATOM   7617  C CA  . HIS F 2 38  ? -55.016  -26.868  17.552  1.00 90.30  ? 47  HIS F CA  1 
ATOM   7618  C C   . HIS F 2 38  ? -56.474  -26.445  17.911  1.00 93.42  ? 47  HIS F C   1 
ATOM   7619  O O   . HIS F 2 38  ? -57.412  -27.241  17.800  1.00 92.82  ? 47  HIS F O   1 
ATOM   7620  C CB  . HIS F 2 38  ? -54.634  -26.303  16.170  1.00 91.72  ? 47  HIS F CB  1 
ATOM   7621  C CG  . HIS F 2 38  ? -55.768  -26.333  15.200  1.00 95.70  ? 47  HIS F CG  1 
ATOM   7622  N ND1 . HIS F 2 38  ? -56.268  -27.526  14.709  1.00 98.78  ? 47  HIS F ND1 1 
ATOM   7623  C CD2 . HIS F 2 38  ? -56.515  -25.317  14.718  1.00 97.31  ? 47  HIS F CD2 1 
ATOM   7624  C CE1 . HIS F 2 38  ? -57.282  -27.195  13.926  1.00 98.80  ? 47  HIS F CE1 1 
ATOM   7625  N NE2 . HIS F 2 38  ? -57.472  -25.875  13.905  1.00 98.25  ? 47  HIS F NE2 1 
ATOM   7626  N N   . ASN F 2 39  ? -56.645  -25.178  18.308  1.00 89.67  ? 48  ASN F N   1 
ATOM   7627  C CA  . ASN F 2 39  ? -57.937  -24.555  18.606  1.00 88.95  ? 48  ASN F CA  1 
ATOM   7628  C C   . ASN F 2 39  ? -58.388  -23.834  17.340  1.00 94.76  ? 48  ASN F C   1 
ATOM   7629  O O   . ASN F 2 39  ? -57.548  -23.392  16.555  1.00 95.49  ? 48  ASN F O   1 
ATOM   7630  C CB  . ASN F 2 39  ? -57.800  -23.543  19.761  1.00 84.76  ? 48  ASN F CB  1 
ATOM   7631  C CG  . ASN F 2 39  ? -56.783  -22.423  19.562  1.00 91.17  ? 48  ASN F CG  1 
ATOM   7632  O OD1 . ASN F 2 39  ? -55.841  -22.513  18.776  1.00 71.43  ? 48  ASN F OD1 1 
ATOM   7633  N ND2 . ASN F 2 39  ? -56.911  -21.361  20.329  1.00 86.84  ? 48  ASN F ND2 1 
ATOM   7634  N N   . GLY F 2 40  ? -59.693  -23.679  17.163  1.00 91.41  ? 49  GLY F N   1 
ATOM   7635  C CA  . GLY F 2 40  ? -60.236  -22.978  16.003  1.00 91.77  ? 49  GLY F CA  1 
ATOM   7636  C C   . GLY F 2 40  ? -60.074  -21.468  16.064  1.00 94.86  ? 49  GLY F C   1 
ATOM   7637  O O   . GLY F 2 40  ? -60.434  -20.767  15.113  1.00 96.42  ? 49  GLY F O   1 
ATOM   7638  N N   . LYS F 2 41  ? -59.523  -20.958  17.181  1.00 88.43  ? 50  LYS F N   1 
ATOM   7639  C CA  . LYS F 2 41  ? -59.336  -19.537  17.453  1.00 87.34  ? 50  LYS F CA  1 
ATOM   7640  C C   . LYS F 2 41  ? -58.093  -18.970  16.796  1.00 90.17  ? 50  LYS F C   1 
ATOM   7641  O O   . LYS F 2 41  ? -57.093  -19.676  16.672  1.00 89.48  ? 50  LYS F O   1 
ATOM   7642  C CB  . LYS F 2 41  ? -59.266  -19.295  18.974  1.00 90.14  ? 50  LYS F CB  1 
ATOM   7643  C CG  . LYS F 2 41  ? -60.503  -19.745  19.770  1.00 102.74 ? 50  LYS F CG  1 
ATOM   7644  C CD  . LYS F 2 41  ? -60.292  -19.677  21.286  1.00 107.92 ? 50  LYS F CD  1 
ATOM   7645  C CE  . LYS F 2 41  ? -59.991  -21.033  21.884  1.00 115.74 ? 50  LYS F CE  1 
ATOM   7646  N NZ  . LYS F 2 41  ? -59.357  -20.920  23.224  1.00 125.76 ? 50  LYS F NZ  1 
ATOM   7647  N N   . LEU F 2 42  ? -58.161  -17.680  16.394  1.00 86.95  ? 51  LEU F N   1 
ATOM   7648  C CA  . LEU F 2 42  ? -57.044  -16.908  15.840  1.00 86.91  ? 51  LEU F CA  1 
ATOM   7649  C C   . LEU F 2 42  ? -56.560  -15.970  16.965  1.00 94.81  ? 51  LEU F C   1 
ATOM   7650  O O   . LEU F 2 42  ? -56.969  -14.809  17.056  1.00 94.78  ? 51  LEU F O   1 
ATOM   7651  C CB  . LEU F 2 42  ? -57.443  -16.101  14.586  1.00 86.11  ? 51  LEU F CB  1 
ATOM   7652  C CG  . LEU F 2 42  ? -57.817  -16.862  13.325  1.00 89.84  ? 51  LEU F CG  1 
ATOM   7653  C CD1 . LEU F 2 42  ? -58.408  -15.931  12.307  1.00 89.74  ? 51  LEU F CD1 1 
ATOM   7654  C CD2 . LEU F 2 42  ? -56.622  -17.531  12.711  1.00 91.67  ? 51  LEU F CD2 1 
ATOM   7655  N N   . CYS F 2 43  ? -55.731  -16.514  17.855  1.00 93.49  ? 52  CYS F N   1 
ATOM   7656  C CA  . CYS F 2 43  ? -55.208  -15.818  19.021  1.00 94.68  ? 52  CYS F CA  1 
ATOM   7657  C C   . CYS F 2 43  ? -54.225  -14.695  18.662  1.00 94.66  ? 52  CYS F C   1 
ATOM   7658  O O   . CYS F 2 43  ? -53.644  -14.712  17.579  1.00 92.36  ? 52  CYS F O   1 
ATOM   7659  C CB  . CYS F 2 43  ? -54.589  -16.826  19.985  1.00 97.00  ? 52  CYS F CB  1 
ATOM   7660  S SG  . CYS F 2 43  ? -55.693  -18.192  20.443  1.00 101.23 ? 52  CYS F SG  1 
ATOM   7661  N N   . LYS F 2 44  ? -54.047  -13.717  19.570  1.00 90.94  ? 53  LYS F N   1 
ATOM   7662  C CA  . LYS F 2 44  ? -53.099  -12.623  19.367  1.00 90.75  ? 53  LYS F CA  1 
ATOM   7663  C C   . LYS F 2 44  ? -51.677  -13.098  19.584  1.00 94.06  ? 53  LYS F C   1 
ATOM   7664  O O   . LYS F 2 44  ? -51.319  -13.529  20.682  1.00 94.59  ? 53  LYS F O   1 
ATOM   7665  C CB  . LYS F 2 44  ? -53.439  -11.350  20.174  1.00 94.63  ? 53  LYS F CB  1 
ATOM   7666  C CG  . LYS F 2 44  ? -53.682  -11.473  21.675  1.00 109.46 ? 53  LYS F CG  1 
ATOM   7667  C CD  . LYS F 2 44  ? -54.481  -10.258  22.172  1.00 119.24 ? 53  LYS F CD  1 
ATOM   7668  C CE  . LYS F 2 44  ? -54.450  -10.095  23.672  1.00 128.01 ? 53  LYS F CE  1 
ATOM   7669  N NZ  . LYS F 2 44  ? -55.472  -9.124   24.144  1.00 133.01 ? 53  LYS F NZ  1 
ATOM   7670  N N   . LEU F 2 45  ? -50.886  -13.069  18.508  1.00 90.14  ? 54  LEU F N   1 
ATOM   7671  C CA  . LEU F 2 45  ? -49.498  -13.523  18.498  1.00 91.43  ? 54  LEU F CA  1 
ATOM   7672  C C   . LEU F 2 45  ? -48.596  -12.773  19.482  1.00 98.57  ? 54  LEU F C   1 
ATOM   7673  O O   . LEU F 2 45  ? -48.357  -11.573  19.323  1.00 98.69  ? 54  LEU F O   1 
ATOM   7674  C CB  . LEU F 2 45  ? -48.923  -13.486  17.076  1.00 90.85  ? 54  LEU F CB  1 
ATOM   7675  C CG  . LEU F 2 45  ? -47.485  -13.942  16.943  1.00 97.26  ? 54  LEU F CG  1 
ATOM   7676  C CD1 . LEU F 2 45  ? -47.410  -15.393  16.524  1.00 97.12  ? 54  LEU F CD1 1 
ATOM   7677  C CD2 . LEU F 2 45  ? -46.721  -13.046  16.008  1.00 101.00 ? 54  LEU F CD2 1 
ATOM   7678  N N   . ARG F 2 46  ? -48.075  -13.522  20.479  1.00 97.23  ? 55  ARG F N   1 
ATOM   7679  C CA  . ARG F 2 46  ? -47.185  -13.088  21.562  1.00 100.59 ? 55  ARG F CA  1 
ATOM   7680  C C   . ARG F 2 46  ? -47.597  -11.712  22.119  1.00 105.54 ? 55  ARG F C   1 
ATOM   7681  O O   . ARG F 2 46  ? -46.790  -10.789  22.224  1.00 108.05 ? 55  ARG F O   1 
ATOM   7682  C CB  . ARG F 2 46  ? -45.678  -13.182  21.179  1.00 106.23 ? 55  ARG F CB  1 
ATOM   7683  C CG  . ARG F 2 46  ? -45.226  -12.432  19.911  1.00 127.19 ? 55  ARG F CG  1 
ATOM   7684  C CD  . ARG F 2 46  ? -44.153  -13.182  19.122  1.00 146.91 ? 55  ARG F CD  1 
ATOM   7685  N NE  . ARG F 2 46  ? -43.859  -12.528  17.840  1.00 158.86 ? 55  ARG F NE  1 
ATOM   7686  C CZ  . ARG F 2 46  ? -43.201  -13.095  16.830  1.00 172.26 ? 55  ARG F CZ  1 
ATOM   7687  N NH1 . ARG F 2 46  ? -42.763  -14.346  16.930  1.00 156.85 ? 55  ARG F NH1 1 
ATOM   7688  N NH2 . ARG F 2 46  ? -42.990  -12.420  15.706  1.00 158.85 ? 55  ARG F NH2 1 
ATOM   7689  N N   . GLY F 2 47  A -48.879  -11.604  22.453  1.00 100.38 ? 55  GLY F N   1 
ATOM   7690  C CA  . GLY F 2 47  A -49.470  -10.402  23.027  1.00 101.10 ? 55  GLY F CA  1 
ATOM   7691  C C   . GLY F 2 47  A -50.140  -9.477   22.035  1.00 102.42 ? 55  GLY F C   1 
ATOM   7692  O O   . GLY F 2 47  A -51.324  -9.166   22.201  1.00 101.69 ? 55  GLY F O   1 
ATOM   7693  N N   . VAL F 2 48  ? -49.383  -9.001   21.015  1.00 97.13  ? 56  VAL F N   1 
ATOM   7694  C CA  . VAL F 2 48  ? -49.896  -8.084   19.986  1.00 94.64  ? 56  VAL F CA  1 
ATOM   7695  C C   . VAL F 2 48  ? -50.951  -8.754   19.104  1.00 95.87  ? 56  VAL F C   1 
ATOM   7696  O O   . VAL F 2 48  ? -50.734  -9.848   18.591  1.00 94.38  ? 56  VAL F O   1 
ATOM   7697  C CB  . VAL F 2 48  ? -48.807  -7.375   19.156  1.00 98.72  ? 56  VAL F CB  1 
ATOM   7698  C CG1 . VAL F 2 48  ? -48.299  -6.144   19.887  1.00 101.26 ? 56  VAL F CG1 1 
ATOM   7699  C CG2 . VAL F 2 48  ? -47.659  -8.312   18.794  1.00 99.24  ? 56  VAL F CG2 1 
ATOM   7700  N N   . ALA F 2 49  ? -52.115  -8.103   18.989  1.00 91.85  ? 57  ALA F N   1 
ATOM   7701  C CA  . ALA F 2 49  ? -53.282  -8.586   18.251  1.00 89.56  ? 57  ALA F CA  1 
ATOM   7702  C C   . ALA F 2 49  ? -53.198  -8.417   16.729  1.00 91.19  ? 57  ALA F C   1 
ATOM   7703  O O   . ALA F 2 49  ? -52.555  -7.470   16.273  1.00 91.11  ? 57  ALA F O   1 
ATOM   7704  C CB  . ALA F 2 49  ? -54.545  -7.930   18.795  1.00 90.58  ? 57  ALA F CB  1 
ATOM   7705  N N   . PRO F 2 50  ? -53.867  -9.292   15.925  1.00 85.52  ? 58  PRO F N   1 
ATOM   7706  C CA  . PRO F 2 50  ? -53.816  -9.133   14.459  1.00 84.43  ? 58  PRO F CA  1 
ATOM   7707  C C   . PRO F 2 50  ? -54.647  -7.962   13.927  1.00 89.57  ? 58  PRO F C   1 
ATOM   7708  O O   . PRO F 2 50  ? -55.243  -7.237   14.719  1.00 90.71  ? 58  PRO F O   1 
ATOM   7709  C CB  . PRO F 2 50  ? -54.362  -10.459  13.955  1.00 85.15  ? 58  PRO F CB  1 
ATOM   7710  C CG  . PRO F 2 50  ? -55.272  -10.911  15.012  1.00 89.52  ? 58  PRO F CG  1 
ATOM   7711  C CD  . PRO F 2 50  ? -54.663  -10.478  16.300  1.00 86.21  ? 58  PRO F CD  1 
ATOM   7712  N N   . LEU F 2 51  ? -54.694  -7.775   12.591  1.00 85.96  ? 59  LEU F N   1 
ATOM   7713  C CA  . LEU F 2 51  ? -55.460  -6.693   11.972  1.00 86.03  ? 59  LEU F CA  1 
ATOM   7714  C C   . LEU F 2 51  ? -56.537  -7.277   11.088  1.00 90.92  ? 59  LEU F C   1 
ATOM   7715  O O   . LEU F 2 51  ? -56.260  -7.710   9.974   1.00 91.76  ? 59  LEU F O   1 
ATOM   7716  C CB  . LEU F 2 51  ? -54.543  -5.751   11.180  1.00 86.27  ? 59  LEU F CB  1 
ATOM   7717  C CG  . LEU F 2 51  ? -55.139  -4.413   10.759  1.00 90.84  ? 59  LEU F CG  1 
ATOM   7718  C CD1 . LEU F 2 51  ? -54.788  -3.316   11.762  1.00 91.11  ? 59  LEU F CD1 1 
ATOM   7719  C CD2 . LEU F 2 51  ? -54.631  -4.022   9.385   1.00 95.17  ? 59  LEU F CD2 1 
ATOM   7720  N N   . HIS F 2 52  ? -57.762  -7.311   11.589  1.00 87.39  ? 60  HIS F N   1 
ATOM   7721  C CA  . HIS F 2 52  ? -58.875  -7.876   10.847  1.00 87.99  ? 60  HIS F CA  1 
ATOM   7722  C C   . HIS F 2 52  ? -59.539  -6.844   9.925   1.00 94.31  ? 60  HIS F C   1 
ATOM   7723  O O   . HIS F 2 52  ? -59.815  -5.722   10.359  1.00 94.85  ? 60  HIS F O   1 
ATOM   7724  C CB  . HIS F 2 52  ? -59.881  -8.496   11.817  1.00 89.13  ? 60  HIS F CB  1 
ATOM   7725  C CG  . HIS F 2 52  ? -60.934  -9.331   11.164  1.00 92.96  ? 60  HIS F CG  1 
ATOM   7726  N ND1 . HIS F 2 52  ? -62.202  -8.838   10.940  1.00 95.54  ? 60  HIS F ND1 1 
ATOM   7727  C CD2 . HIS F 2 52  ? -60.874  -10.607  10.721  1.00 94.63  ? 60  HIS F CD2 1 
ATOM   7728  C CE1 . HIS F 2 52  ? -62.870  -9.823   10.368  1.00 95.85  ? 60  HIS F CE1 1 
ATOM   7729  N NE2 . HIS F 2 52  ? -62.112  -10.908  10.217  1.00 95.64  ? 60  HIS F NE2 1 
ATOM   7730  N N   . LEU F 2 53  ? -59.774  -7.224   8.646   1.00 91.59  ? 61  LEU F N   1 
ATOM   7731  C CA  . LEU F 2 53  ? -60.432  -6.384   7.633   1.00 92.06  ? 61  LEU F CA  1 
ATOM   7732  C C   . LEU F 2 53  ? -61.696  -7.130   7.196   1.00 98.54  ? 61  LEU F C   1 
ATOM   7733  O O   . LEU F 2 53  ? -61.646  -7.928   6.260   1.00 98.90  ? 61  LEU F O   1 
ATOM   7734  C CB  . LEU F 2 53  ? -59.516  -6.104   6.406   1.00 91.78  ? 61  LEU F CB  1 
ATOM   7735  C CG  . LEU F 2 53  ? -58.004  -5.938   6.606   1.00 95.10  ? 61  LEU F CG  1 
ATOM   7736  C CD1 . LEU F 2 53  ? -57.278  -6.034   5.291   1.00 94.89  ? 61  LEU F CD1 1 
ATOM   7737  C CD2 . LEU F 2 53  ? -57.675  -4.617   7.245   1.00 98.38  ? 61  LEU F CD2 1 
ATOM   7738  N N   . GLY F 2 54  ? -62.782  -6.916   7.936   1.00 97.50  ? 62  GLY F N   1 
ATOM   7739  C CA  . GLY F 2 54  ? -64.081  -7.561   7.745   1.00 100.47 ? 62  GLY F CA  1 
ATOM   7740  C C   . GLY F 2 54  ? -64.531  -7.725   6.307   1.00 108.92 ? 62  GLY F C   1 
ATOM   7741  O O   . GLY F 2 54  ? -64.268  -8.765   5.693   1.00 109.31 ? 62  GLY F O   1 
ATOM   7742  N N   . LYS F 2 55  ? -65.223  -6.699   5.763   1.00 108.49 ? 63  LYS F N   1 
ATOM   7743  C CA  . LYS F 2 55  ? -65.701  -6.662   4.371   1.00 110.64 ? 63  LYS F CA  1 
ATOM   7744  C C   . LYS F 2 55  ? -64.714  -5.832   3.541   1.00 113.31 ? 63  LYS F C   1 
ATOM   7745  O O   . LYS F 2 55  ? -65.117  -4.986   2.746   1.00 113.81 ? 63  LYS F O   1 
ATOM   7746  C CB  . LYS F 2 55  ? -67.168  -6.146   4.270   1.00 115.84 ? 63  LYS F CB  1 
ATOM   7747  C CG  . LYS F 2 55  ? -67.468  -4.778   4.920   1.00 129.48 ? 63  LYS F CG  1 
ATOM   7748  C CD  . LYS F 2 55  ? -68.250  -3.838   3.982   1.00 139.73 ? 63  LYS F CD  1 
ATOM   7749  C CE  . LYS F 2 55  ? -69.755  -3.996   4.071   1.00 152.66 ? 63  LYS F CE  1 
ATOM   7750  N NZ  . LYS F 2 55  ? -70.467  -3.127   3.095   1.00 161.17 ? 63  LYS F NZ  1 
ATOM   7751  N N   . CYS F 2 56  ? -63.405  -6.079   3.759   1.00 107.76 ? 64  CYS F N   1 
ATOM   7752  C CA  . CYS F 2 56  ? -62.301  -5.348   3.145   1.00 106.24 ? 64  CYS F CA  1 
ATOM   7753  C C   . CYS F 2 56  ? -61.117  -6.246   2.813   1.00 107.89 ? 64  CYS F C   1 
ATOM   7754  O O   . CYS F 2 56  ? -60.900  -7.243   3.498   1.00 107.84 ? 64  CYS F O   1 
ATOM   7755  C CB  . CYS F 2 56  ? -61.872  -4.230   4.090   1.00 105.07 ? 64  CYS F CB  1 
ATOM   7756  S SG  . CYS F 2 56  ? -61.407  -2.692   3.262   1.00 108.60 ? 64  CYS F SG  1 
ATOM   7757  N N   . ASN F 2 57  ? -60.314  -5.862   1.807   1.00 102.55 ? 65  ASN F N   1 
ATOM   7758  C CA  . ASN F 2 57  ? -59.059  -6.543   1.487   1.00 101.92 ? 65  ASN F CA  1 
ATOM   7759  C C   . ASN F 2 57  ? -57.921  -5.573   1.813   1.00 106.31 ? 65  ASN F C   1 
ATOM   7760  O O   . ASN F 2 57  ? -58.203  -4.432   2.184   1.00 104.91 ? 65  ASN F O   1 
ATOM   7761  C CB  . ASN F 2 57  ? -59.007  -7.057   0.047   1.00 99.97  ? 65  ASN F CB  1 
ATOM   7762  C CG  . ASN F 2 57  ? -59.267  -6.031   -1.014  1.00 114.96 ? 65  ASN F CG  1 
ATOM   7763  O OD1 . ASN F 2 57  ? -58.590  -5.005   -1.114  1.00 104.07 ? 65  ASN F OD1 1 
ATOM   7764  N ND2 . ASN F 2 57  ? -60.218  -6.327   -1.880  1.00 109.60 ? 65  ASN F ND2 1 
ATOM   7765  N N   . ILE F 2 58  ? -56.654  -6.012   1.718   1.00 105.00 ? 66  ILE F N   1 
ATOM   7766  C CA  . ILE F 2 58  ? -55.495  -5.161   2.044   1.00 104.61 ? 66  ILE F CA  1 
ATOM   7767  C C   . ILE F 2 58  ? -55.423  -3.914   1.124   1.00 109.65 ? 66  ILE F C   1 
ATOM   7768  O O   . ILE F 2 58  ? -55.090  -2.837   1.620   1.00 108.53 ? 66  ILE F O   1 
ATOM   7769  C CB  . ILE F 2 58  ? -54.162  -5.966   2.108   1.00 108.53 ? 66  ILE F CB  1 
ATOM   7770  C CG1 . ILE F 2 58  ? -54.270  -7.088   3.173   1.00 108.86 ? 66  ILE F CG1 1 
ATOM   7771  C CG2 . ILE F 2 58  ? -52.961  -5.058   2.420   1.00 108.43 ? 66  ILE F CG2 1 
ATOM   7772  C CD1 . ILE F 2 58  ? -53.372  -8.258   2.978   1.00 119.53 ? 66  ILE F CD1 1 
ATOM   7773  N N   . ALA F 2 59  ? -55.799  -4.041   -0.173  1.00 107.52 ? 67  ALA F N   1 
ATOM   7774  C CA  . ALA F 2 59  ? -55.808  -2.908   -1.110  1.00 107.13 ? 67  ALA F CA  1 
ATOM   7775  C C   . ALA F 2 59  ? -56.851  -1.874   -0.688  1.00 107.52 ? 67  ALA F C   1 
ATOM   7776  O O   . ALA F 2 59  ? -56.496  -0.723   -0.446  1.00 106.53 ? 67  ALA F O   1 
ATOM   7777  C CB  . ALA F 2 59  ? -56.066  -3.380   -2.535  1.00 110.41 ? 67  ALA F CB  1 
ATOM   7778  N N   . GLY F 2 60  ? -58.097  -2.311   -0.518  1.00 101.89 ? 68  GLY F N   1 
ATOM   7779  C CA  . GLY F 2 60  ? -59.180  -1.454   -0.062  1.00 100.26 ? 68  GLY F CA  1 
ATOM   7780  C C   . GLY F 2 60  ? -58.900  -0.821   1.284   1.00 100.39 ? 68  GLY F C   1 
ATOM   7781  O O   . GLY F 2 60  ? -59.306  0.318    1.514   1.00 99.61  ? 68  GLY F O   1 
ATOM   7782  N N   . TRP F 2 61  ? -58.167  -1.537   2.169   1.00 94.78  ? 69  TRP F N   1 
ATOM   7783  C CA  . TRP F 2 61  ? -57.811  -1.024   3.492   1.00 93.16  ? 69  TRP F CA  1 
ATOM   7784  C C   . TRP F 2 61  ? -56.776  0.097    3.419   1.00 95.69  ? 69  TRP F C   1 
ATOM   7785  O O   . TRP F 2 61  ? -56.978  1.167    4.006   1.00 95.22  ? 69  TRP F O   1 
ATOM   7786  C CB  . TRP F 2 61  ? -57.293  -2.136   4.431   1.00 91.76  ? 69  TRP F CB  1 
ATOM   7787  C CG  . TRP F 2 61  ? -56.676  -1.579   5.687   1.00 92.22  ? 69  TRP F CG  1 
ATOM   7788  C CD1 . TRP F 2 61  ? -57.312  -0.866   6.656   1.00 94.90  ? 69  TRP F CD1 1 
ATOM   7789  C CD2 . TRP F 2 61  ? -55.286  -1.587   6.045   1.00 92.15  ? 69  TRP F CD2 1 
ATOM   7790  N NE1 . TRP F 2 61  ? -56.413  -0.447   7.606   1.00 94.35  ? 69  TRP F NE1 1 
ATOM   7791  C CE2 . TRP F 2 61  ? -55.162  -0.879   7.261   1.00 95.85  ? 69  TRP F CE2 1 
ATOM   7792  C CE3 . TRP F 2 61  ? -54.131  -2.131   5.464   1.00 94.39  ? 69  TRP F CE3 1 
ATOM   7793  C CZ2 . TRP F 2 61  ? -53.935  -0.713   7.914   1.00 95.73  ? 69  TRP F CZ2 1 
ATOM   7794  C CZ3 . TRP F 2 61  ? -52.915  -1.972   6.116   1.00 96.36  ? 69  TRP F CZ3 1 
ATOM   7795  C CH2 . TRP F 2 61  ? -52.826  -1.270   7.326   1.00 96.82  ? 69  TRP F CH2 1 
ATOM   7796  N N   . ILE F 2 62  ? -55.639  -0.185   2.758   1.00 90.44  ? 70  ILE F N   1 
ATOM   7797  C CA  . ILE F 2 62  ? -54.513  0.729    2.661   1.00 88.60  ? 70  ILE F CA  1 
ATOM   7798  C C   . ILE F 2 62  ? -54.845  1.964    1.831   1.00 92.38  ? 70  ILE F C   1 
ATOM   7799  O O   . ILE F 2 62  ? -54.351  3.041    2.167   1.00 92.42  ? 70  ILE F O   1 
ATOM   7800  C CB  . ILE F 2 62  ? -53.223  0.004    2.196   1.00 91.78  ? 70  ILE F CB  1 
ATOM   7801  C CG1 . ILE F 2 62  ? -51.964  0.773    2.627   1.00 92.36  ? 70  ILE F CG1 1 
ATOM   7802  C CG2 . ILE F 2 62  ? -53.207  -0.341   0.699   1.00 92.25  ? 70  ILE F CG2 1 
ATOM   7803  C CD1 . ILE F 2 62  ? -51.587  0.588    4.079   1.00 98.25  ? 70  ILE F CD1 1 
ATOM   7804  N N   . LEU F 2 63  ? -55.686  1.815    0.769   1.00 88.16  ? 71  LEU F N   1 
ATOM   7805  C CA  . LEU F 2 63  ? -56.078  2.924    -0.119  1.00 86.58  ? 71  LEU F CA  1 
ATOM   7806  C C   . LEU F 2 63  ? -57.042  3.883    0.563   1.00 89.04  ? 71  LEU F C   1 
ATOM   7807  O O   . LEU F 2 63  ? -57.023  5.080    0.275   1.00 88.80  ? 71  LEU F O   1 
ATOM   7808  C CB  . LEU F 2 63  ? -56.701  2.427    -1.435  1.00 87.19  ? 71  LEU F CB  1 
ATOM   7809  C CG  . LEU F 2 63  ? -55.779  1.810    -2.465  1.00 92.31  ? 71  LEU F CG  1 
ATOM   7810  C CD1 . LEU F 2 63  ? -56.579  1.050    -3.491  1.00 94.48  ? 71  LEU F CD1 1 
ATOM   7811  C CD2 . LEU F 2 63  ? -54.913  2.858    -3.146  1.00 93.76  ? 71  LEU F CD2 1 
ATOM   7812  N N   . GLY F 2 64  ? -57.884  3.344    1.440   1.00 83.73  ? 72  GLY F N   1 
ATOM   7813  C CA  . GLY F 2 64  ? -58.887  4.113    2.162   1.00 82.18  ? 72  GLY F CA  1 
ATOM   7814  C C   . GLY F 2 64  ? -60.247  4.041    1.512   1.00 83.71  ? 72  GLY F C   1 
ATOM   7815  O O   . GLY F 2 64  ? -60.960  5.044    1.478   1.00 81.61  ? 72  GLY F O   1 
ATOM   7816  N N   . ASN F 2 65  ? -60.610  2.834    1.005   1.00 82.44  ? 73  ASN F N   1 
ATOM   7817  C CA  . ASN F 2 65  ? -61.889  2.517    0.357   1.00 85.40  ? 73  ASN F CA  1 
ATOM   7818  C C   . ASN F 2 65  ? -63.040  2.986    1.272   1.00 92.10  ? 73  ASN F C   1 
ATOM   7819  O O   . ASN F 2 65  ? -63.014  2.668    2.464   1.00 91.83  ? 73  ASN F O   1 
ATOM   7820  C CB  . ASN F 2 65  ? -61.983  1.007    0.025   1.00 87.47  ? 73  ASN F CB  1 
ATOM   7821  C CG  . ASN F 2 65  ? -63.301  0.515    -0.546  1.00 114.35 ? 73  ASN F CG  1 
ATOM   7822  O OD1 . ASN F 2 65  ? -63.873  1.086    -1.483  1.00 109.06 ? 73  ASN F OD1 1 
ATOM   7823  N ND2 . ASN F 2 65  ? -63.781  -0.607   -0.029  1.00 109.82 ? 73  ASN F ND2 1 
ATOM   7824  N N   . PRO F 2 66  ? -64.002  3.801    0.766   1.00 90.14  ? 74  PRO F N   1 
ATOM   7825  C CA  . PRO F 2 66  ? -65.054  4.344    1.637   1.00 91.29  ? 74  PRO F CA  1 
ATOM   7826  C C   . PRO F 2 66  ? -65.852  3.328    2.455   1.00 99.16  ? 74  PRO F C   1 
ATOM   7827  O O   . PRO F 2 66  ? -66.425  3.702    3.484   1.00 99.94  ? 74  PRO F O   1 
ATOM   7828  C CB  . PRO F 2 66  ? -65.941  5.126    0.669   1.00 94.72  ? 74  PRO F CB  1 
ATOM   7829  C CG  . PRO F 2 66  ? -65.591  4.630    -0.679  1.00 99.64  ? 74  PRO F CG  1 
ATOM   7830  C CD  . PRO F 2 66  ? -64.145  4.327    -0.601  1.00 92.88  ? 74  PRO F CD  1 
ATOM   7831  N N   . GLU F 2 67  ? -65.859  2.048    2.041   1.00 97.59  ? 75  GLU F N   1 
ATOM   7832  C CA  . GLU F 2 67  ? -66.557  0.992    2.779   1.00 99.06  ? 75  GLU F CA  1 
ATOM   7833  C C   . GLU F 2 67  ? -65.749  0.517    3.998   1.00 101.51 ? 75  GLU F C   1 
ATOM   7834  O O   . GLU F 2 67  ? -66.265  -0.277   4.791   1.00 102.99 ? 75  GLU F O   1 
ATOM   7835  C CB  . GLU F 2 67  ? -66.937  -0.179   1.857   1.00 102.48 ? 75  GLU F CB  1 
ATOM   7836  C CG  . GLU F 2 67  ? -67.919  0.194    0.754   1.00 120.22 ? 75  GLU F CG  1 
ATOM   7837  C CD  . GLU F 2 67  ? -69.221  0.834    1.203   1.00 153.77 ? 75  GLU F CD  1 
ATOM   7838  O OE1 . GLU F 2 67  ? -70.077  0.118    1.772   1.00 168.97 ? 75  GLU F OE1 1 
ATOM   7839  O OE2 . GLU F 2 67  ? -69.384  2.055    0.983   1.00 147.36 ? 75  GLU F OE2 1 
ATOM   7840  N N   . CYS F 2 68  ? -64.492  1.022    4.154   1.00 94.48  ? 76  CYS F N   1 
ATOM   7841  C CA  . CYS F 2 68  ? -63.565  0.701    5.244   1.00 104.40 ? 76  CYS F CA  1 
ATOM   7842  C C   . CYS F 2 68  ? -62.991  1.974    5.841   1.00 111.11 ? 76  CYS F C   1 
ATOM   7843  O O   . CYS F 2 68  ? -62.331  1.919    6.874   1.00 79.13  ? 76  CYS F O   1 
ATOM   7844  C CB  . CYS F 2 68  ? -62.459  -0.233   4.759   1.00 103.83 ? 76  CYS F CB  1 
ATOM   7845  S SG  . CYS F 2 68  ? -63.029  -1.530   3.634   1.00 109.62 ? 76  CYS F SG  1 
ATOM   7846  N N   . ALA F 2 74  ? -55.413  0.826    13.501  1.00 108.74 ? 82  ALA F N   1 
ATOM   7847  C CA  . ALA F 2 74  ? -54.584  0.391    14.632  1.00 109.91 ? 82  ALA F CA  1 
ATOM   7848  C C   . ALA F 2 74  ? -53.077  0.713    14.441  1.00 113.23 ? 82  ALA F C   1 
ATOM   7849  O O   . ALA F 2 74  ? -52.574  0.618    13.319  1.00 111.75 ? 82  ALA F O   1 
ATOM   7850  C CB  . ALA F 2 74  ? -54.780  -1.097   14.885  1.00 110.03 ? 82  ALA F CB  1 
ATOM   7851  N N   . SER F 2 75  ? -52.370  1.090    15.544  1.00 109.63 ? 83  SER F N   1 
ATOM   7852  C CA  . SER F 2 75  ? -50.941  1.442    15.556  1.00 109.52 ? 83  SER F CA  1 
ATOM   7853  C C   . SER F 2 75  ? -50.015  0.264    15.268  1.00 110.98 ? 83  SER F C   1 
ATOM   7854  O O   . SER F 2 75  ? -48.946  0.468    14.700  1.00 111.56 ? 83  SER F O   1 
ATOM   7855  C CB  . SER F 2 75  ? -50.550  2.091    16.880  1.00 115.57 ? 83  SER F CB  1 
ATOM   7856  O OG  . SER F 2 75  ? -49.141  2.199    17.027  1.00 124.57 ? 83  SER F OG  1 
ATOM   7857  N N   . SER F 2 76  A -50.381  -0.945   15.713  1.00 104.90 ? 83  SER F N   1 
ATOM   7858  C CA  . SER F 2 76  A -49.572  -2.148   15.501  1.00 103.85 ? 83  SER F CA  1 
ATOM   7859  C C   . SER F 2 76  A -50.421  -3.412   15.398  1.00 105.71 ? 83  SER F C   1 
ATOM   7860  O O   . SER F 2 76  A -51.552  -3.450   15.895  1.00 105.42 ? 83  SER F O   1 
ATOM   7861  C CB  . SER F 2 76  A -48.505  -2.297   16.585  1.00 108.56 ? 83  SER F CB  1 
ATOM   7862  O OG  . SER F 2 76  A -48.955  -1.861   17.857  1.00 115.43 ? 83  SER F OG  1 
ATOM   7863  N N   . TRP F 2 77  ? -49.884  -4.435   14.718  1.00 100.43 ? 84  TRP F N   1 
ATOM   7864  C CA  . TRP F 2 77  ? -50.527  -5.738   14.571  1.00 98.35  ? 84  TRP F CA  1 
ATOM   7865  C C   . TRP F 2 77  ? -49.497  -6.827   14.352  1.00 104.14 ? 84  TRP F C   1 
ATOM   7866  O O   . TRP F 2 77  ? -48.389  -6.545   13.889  1.00 106.22 ? 84  TRP F O   1 
ATOM   7867  C CB  . TRP F 2 77  ? -51.587  -5.748   13.471  1.00 94.59  ? 84  TRP F CB  1 
ATOM   7868  C CG  . TRP F 2 77  ? -51.043  -5.464   12.112  1.00 95.08  ? 84  TRP F CG  1 
ATOM   7869  C CD1 . TRP F 2 77  ? -50.624  -6.375   11.187  1.00 97.98  ? 84  TRP F CD1 1 
ATOM   7870  C CD2 . TRP F 2 77  ? -50.871  -4.178   11.518  1.00 94.71  ? 84  TRP F CD2 1 
ATOM   7871  N NE1 . TRP F 2 77  ? -50.205  -5.733   10.050  1.00 97.61  ? 84  TRP F NE1 1 
ATOM   7872  C CE2 . TRP F 2 77  ? -50.343  -4.381   10.226  1.00 98.84  ? 84  TRP F CE2 1 
ATOM   7873  C CE3 . TRP F 2 77  ? -51.111  -2.866   11.952  1.00 96.11  ? 84  TRP F CE3 1 
ATOM   7874  C CZ2 . TRP F 2 77  ? -50.053  -3.318   9.363   1.00 98.23  ? 84  TRP F CZ2 1 
ATOM   7875  C CZ3 . TRP F 2 77  ? -50.821  -1.817   11.097  1.00 97.40  ? 84  TRP F CZ3 1 
ATOM   7876  C CH2 . TRP F 2 77  ? -50.296  -2.046   9.822   1.00 97.81  ? 84  TRP F CH2 1 
ATOM   7877  N N   . SER F 2 78  ? -49.858  -8.066   14.692  1.00 99.49  ? 85  SER F N   1 
ATOM   7878  C CA  . SER F 2 78  ? -48.978  -9.224   14.562  1.00 100.00 ? 85  SER F CA  1 
ATOM   7879  C C   . SER F 2 78  ? -49.055  -9.917   13.189  1.00 103.32 ? 85  SER F C   1 
ATOM   7880  O O   . SER F 2 78  ? -48.089  -10.567  12.781  1.00 104.29 ? 85  SER F O   1 
ATOM   7881  C CB  . SER F 2 78  ? -49.246  -10.209  15.690  1.00 103.54 ? 85  SER F CB  1 
ATOM   7882  O OG  . SER F 2 78  ? -50.634  -10.339  15.953  1.00 111.10 ? 85  SER F OG  1 
ATOM   7883  N N   . TYR F 2 79  ? -50.208  -9.781   12.489  1.00 98.28  ? 86  TYR F N   1 
ATOM   7884  C CA  . TYR F 2 79  ? -50.525  -10.345  11.163  1.00 97.29  ? 86  TYR F CA  1 
ATOM   7885  C C   . TYR F 2 79  ? -51.849  -9.765   10.663  1.00 99.01  ? 86  TYR F C   1 
ATOM   7886  O O   . TYR F 2 79  ? -52.610  -9.230   11.462  1.00 97.23  ? 86  TYR F O   1 
ATOM   7887  C CB  . TYR F 2 79  ? -50.573  -11.889  11.185  1.00 98.66  ? 86  TYR F CB  1 
ATOM   7888  C CG  . TYR F 2 79  ? -51.541  -12.487  12.186  1.00 99.43  ? 86  TYR F CG  1 
ATOM   7889  C CD1 . TYR F 2 79  ? -51.232  -12.536  13.543  1.00 101.60 ? 86  TYR F CD1 1 
ATOM   7890  C CD2 . TYR F 2 79  ? -52.726  -13.081  11.768  1.00 99.33  ? 86  TYR F CD2 1 
ATOM   7891  C CE1 . TYR F 2 79  ? -52.110  -13.101  14.466  1.00 100.78 ? 86  TYR F CE1 1 
ATOM   7892  C CE2 . TYR F 2 79  ? -53.595  -13.681  12.679  1.00 99.35  ? 86  TYR F CE2 1 
ATOM   7893  C CZ  . TYR F 2 79  ? -53.285  -13.685  14.028  1.00 104.23 ? 86  TYR F CZ  1 
ATOM   7894  O OH  . TYR F 2 79  ? -54.151  -14.248  14.935  1.00 103.42 ? 86  TYR F OH  1 
ATOM   7895  N N   . ILE F 2 80  ? -52.126  -9.843   9.358   1.00 96.07  ? 87  ILE F N   1 
ATOM   7896  C CA  . ILE F 2 80  ? -53.388  -9.302   8.836   1.00 95.25  ? 87  ILE F CA  1 
ATOM   7897  C C   . ILE F 2 80  ? -54.387  -10.430  8.584   1.00 98.80  ? 87  ILE F C   1 
ATOM   7898  O O   . ILE F 2 80  ? -54.038  -11.430  7.953   1.00 100.08 ? 87  ILE F O   1 
ATOM   7899  C CB  . ILE F 2 80  ? -53.221  -8.406   7.575   1.00 98.86  ? 87  ILE F CB  1 
ATOM   7900  C CG1 . ILE F 2 80  ? -51.863  -7.684   7.519   1.00 99.90  ? 87  ILE F CG1 1 
ATOM   7901  C CG2 . ILE F 2 80  ? -54.380  -7.418   7.430   1.00 98.98  ? 87  ILE F CG2 1 
ATOM   7902  C CD1 . ILE F 2 80  ? -51.280  -7.729   6.150   1.00 107.19 ? 87  ILE F CD1 1 
ATOM   7903  N N   . VAL F 2 81  ? -55.623  -10.267  9.079   1.00 93.29  ? 88  VAL F N   1 
ATOM   7904  C CA  . VAL F 2 81  ? -56.697  -11.238  8.883   1.00 92.53  ? 88  VAL F CA  1 
ATOM   7905  C C   . VAL F 2 81  ? -57.670  -10.653  7.869   1.00 95.18  ? 88  VAL F C   1 
ATOM   7906  O O   . VAL F 2 81  ? -58.307  -9.630   8.124   1.00 94.21  ? 88  VAL F O   1 
ATOM   7907  C CB  . VAL F 2 81  ? -57.393  -11.698  10.187  1.00 95.72  ? 88  VAL F CB  1 
ATOM   7908  C CG1 . VAL F 2 81  ? -58.252  -12.933  9.935   1.00 96.34  ? 88  VAL F CG1 1 
ATOM   7909  C CG2 . VAL F 2 81  ? -56.377  -11.987  11.274  1.00 95.11  ? 88  VAL F CG2 1 
ATOM   7910  N N   . GLU F 2 82  ? -57.738  -11.285  6.700   1.00 91.75  ? 89  GLU F N   1 
ATOM   7911  C CA  . GLU F 2 82  ? -58.584  -10.873  5.590   1.00 92.38  ? 89  GLU F CA  1 
ATOM   7912  C C   . GLU F 2 82  ? -59.581  -11.999  5.321   1.00 98.44  ? 89  GLU F C   1 
ATOM   7913  O O   . GLU F 2 82  ? -59.175  -13.155  5.191   1.00 98.75  ? 89  GLU F O   1 
ATOM   7914  C CB  . GLU F 2 82  ? -57.693  -10.612  4.367   1.00 94.40  ? 89  GLU F CB  1 
ATOM   7915  C CG  . GLU F 2 82  ? -58.369  -9.955   3.181   1.00 104.77 ? 89  GLU F CG  1 
ATOM   7916  C CD  . GLU F 2 82  ? -57.530  -10.012  1.919   1.00 124.51 ? 89  GLU F CD  1 
ATOM   7917  O OE1 . GLU F 2 82  ? -57.969  -10.671  0.948   1.00 132.40 ? 89  GLU F OE1 1 
ATOM   7918  O OE2 . GLU F 2 82  ? -56.417  -9.435   1.914   1.00 105.97 ? 89  GLU F OE2 1 
ATOM   7919  N N   . THR F 2 83  ? -60.884  -11.675  5.292   1.00 96.03  ? 90  THR F N   1 
ATOM   7920  C CA  . THR F 2 83  ? -61.947  -12.645  5.033   1.00 97.97  ? 90  THR F CA  1 
ATOM   7921  C C   . THR F 2 83  ? -61.814  -13.050  3.558   1.00 106.21 ? 90  THR F C   1 
ATOM   7922  O O   . THR F 2 83  ? -61.594  -12.163  2.726   1.00 107.10 ? 90  THR F O   1 
ATOM   7923  C CB  . THR F 2 83  ? -63.315  -12.000  5.322   1.00 106.34 ? 90  THR F CB  1 
ATOM   7924  O OG1 . THR F 2 83  ? -63.284  -11.392  6.610   1.00 106.94 ? 90  THR F OG1 1 
ATOM   7925  C CG2 . THR F 2 83  ? -64.477  -12.988  5.251   1.00 107.27 ? 90  THR F CG2 1 
ATOM   7926  N N   . PRO F 2 84  A -61.898  -14.356  3.197   1.00 105.23 ? 90  PRO F N   1 
ATOM   7927  C CA  . PRO F 2 84  A -61.799  -14.723  1.768   1.00 108.41 ? 90  PRO F CA  1 
ATOM   7928  C C   . PRO F 2 84  A -62.955  -14.138  0.943   1.00 116.49 ? 90  PRO F C   1 
ATOM   7929  O O   . PRO F 2 84  A -62.766  -13.717  -0.203  1.00 116.67 ? 90  PRO F O   1 
ATOM   7930  C CB  . PRO F 2 84  A -61.817  -16.253  1.792   1.00 111.65 ? 90  PRO F CB  1 
ATOM   7931  C CG  . PRO F 2 84  A -62.478  -16.616  3.072   1.00 114.23 ? 90  PRO F CG  1 
ATOM   7932  C CD  . PRO F 2 84  A -62.124  -15.543  4.047   1.00 106.51 ? 90  PRO F CD  1 
ATOM   7933  N N   . SER F 2 85  ? -64.134  -14.050  1.583   1.00 116.21 ? 91  SER F N   1 
ATOM   7934  C CA  . SER F 2 85  ? -65.392  -13.520  1.066   1.00 119.86 ? 91  SER F CA  1 
ATOM   7935  C C   . SER F 2 85  ? -65.341  -11.999  0.802   1.00 124.78 ? 91  SER F C   1 
ATOM   7936  O O   . SER F 2 85  ? -66.153  -11.495  0.024   1.00 126.85 ? 91  SER F O   1 
ATOM   7937  C CB  . SER F 2 85  ? -66.524  -13.850  2.037   1.00 125.00 ? 91  SER F CB  1 
ATOM   7938  O OG  . SER F 2 85  ? -66.496  -15.212  2.440   1.00 136.67 ? 91  SER F OG  1 
ATOM   7939  N N   . SER F 2 86  ? -64.396  -11.277  1.449   1.00 119.67 ? 92  SER F N   1 
ATOM   7940  C CA  . SER F 2 86  ? -64.214  -9.828   1.309   1.00 118.74 ? 92  SER F CA  1 
ATOM   7941  C C   . SER F 2 86  ? -63.661  -9.456   -0.062  1.00 124.89 ? 92  SER F C   1 
ATOM   7942  O O   . SER F 2 86  ? -62.553  -9.868   -0.426  1.00 123.77 ? 92  SER F O   1 
ATOM   7943  C CB  . SER F 2 86  ? -63.324  -9.276   2.420   1.00 119.22 ? 92  SER F CB  1 
ATOM   7944  O OG  . SER F 2 86  ? -61.944  -9.514   2.187   1.00 126.38 ? 92  SER F OG  1 
ATOM   7945  N N   . ASP F 2 87  ? -64.458  -8.689   -0.823  1.00 124.72 ? 93  ASP F N   1 
ATOM   7946  C CA  . ASP F 2 87  ? -64.136  -8.226   -2.172  1.00 126.96 ? 93  ASP F CA  1 
ATOM   7947  C C   . ASP F 2 87  ? -64.073  -6.693   -2.228  1.00 128.88 ? 93  ASP F C   1 
ATOM   7948  O O   . ASP F 2 87  ? -63.826  -6.132   -3.304  1.00 130.14 ? 93  ASP F O   1 
ATOM   7949  C CB  . ASP F 2 87  ? -65.169  -8.766   -3.186  1.00 134.13 ? 93  ASP F CB  1 
ATOM   7950  C CG  . ASP F 2 87  ? -65.180  -10.277  -3.355  1.00 152.05 ? 93  ASP F CG  1 
ATOM   7951  O OD1 . ASP F 2 87  ? -64.220  -10.816  -3.960  1.00 154.11 ? 93  ASP F OD1 1 
ATOM   7952  O OD2 . ASP F 2 87  ? -66.177  -10.916  -2.935  1.00 160.52 ? 93  ASP F OD2 1 
ATOM   7953  N N   . ASN F 2 88  ? -64.265  -6.020   -1.066  1.00 121.84 ? 94  ASN F N   1 
ATOM   7954  C CA  . ASN F 2 88  ? -64.252  -4.558   -0.989  1.00 119.53 ? 94  ASN F CA  1 
ATOM   7955  C C   . ASN F 2 88  ? -62.845  -3.958   -0.953  1.00 118.24 ? 94  ASN F C   1 
ATOM   7956  O O   . ASN F 2 88  ? -62.220  -3.835   0.101   1.00 114.80 ? 94  ASN F O   1 
ATOM   7957  C CB  . ASN F 2 88  ? -65.129  -4.038   0.142   1.00 120.56 ? 94  ASN F CB  1 
ATOM   7958  C CG  . ASN F 2 88  ? -66.488  -3.619   -0.341  1.00 150.30 ? 94  ASN F CG  1 
ATOM   7959  O OD1 . ASN F 2 88  ? -67.294  -3.064   0.417   1.00 144.38 ? 94  ASN F OD1 1 
ATOM   7960  N ND2 . ASN F 2 88  ? -66.708  -3.910   -1.641  1.00 147.11 ? 94  ASN F ND2 1 
ATOM   7961  N N   . GLY F 2 89  ? -62.399  -3.579   -2.148  1.00 114.64 ? 95  GLY F N   1 
ATOM   7962  C CA  . GLY F 2 89  ? -61.103  -2.990   -2.466  1.00 112.19 ? 95  GLY F CA  1 
ATOM   7963  C C   . GLY F 2 89  ? -61.067  -2.610   -3.931  1.00 116.55 ? 95  GLY F C   1 
ATOM   7964  O O   . GLY F 2 89  ? -61.561  -3.366   -4.779  1.00 119.96 ? 95  GLY F O   1 
ATOM   7965  N N   . THR F 2 90  ? -60.505  -1.420   -4.232  1.00 109.29 ? 96  THR F N   1 
ATOM   7966  C CA  . THR F 2 90  ? -60.417  -0.799   -5.569  1.00 109.48 ? 96  THR F CA  1 
ATOM   7967  C C   . THR F 2 90  ? -61.838  -0.562   -6.168  1.00 113.42 ? 96  THR F C   1 
ATOM   7968  O O   . THR F 2 90  ? -62.184  -1.129   -7.210  1.00 115.08 ? 96  THR F O   1 
ATOM   7969  C CB  . THR F 2 90  ? -59.437  -1.510   -6.545  1.00 115.25 ? 96  THR F CB  1 
ATOM   7970  O OG1 . THR F 2 90  ? -59.990  -2.747   -6.989  1.00 118.96 ? 96  THR F OG1 1 
ATOM   7971  C CG2 . THR F 2 90  ? -58.049  -1.710   -5.960  1.00 109.61 ? 96  THR F CG2 1 
ATOM   7972  N N   . CYS F 2 91  ? -62.645  0.293    -5.476  1.00 108.17 ? 97  CYS F N   1 
ATOM   7973  C CA  . CYS F 2 91  ? -64.003  0.738    -5.838  1.00 109.55 ? 97  CYS F CA  1 
ATOM   7974  C C   . CYS F 2 91  ? -63.969  1.315    -7.244  1.00 111.86 ? 97  CYS F C   1 
ATOM   7975  O O   . CYS F 2 91  ? -64.867  1.055    -8.039  1.00 114.52 ? 97  CYS F O   1 
ATOM   7976  C CB  . CYS F 2 91  ? -64.516  1.766    -4.833  1.00 108.45 ? 97  CYS F CB  1 
ATOM   7977  S SG  . CYS F 2 91  ? -63.403  3.177    -4.585  1.00 109.20 ? 97  CYS F SG  1 
ATOM   7978  N N   . TYR F 2 92  ? -62.918  2.090    -7.553  1.00 104.59 ? 98  TYR F N   1 
ATOM   7979  C CA  . TYR F 2 92  ? -62.704  2.616    -8.891  1.00 105.40 ? 98  TYR F CA  1 
ATOM   7980  C C   . TYR F 2 92  ? -61.919  1.515    -9.617  1.00 112.30 ? 98  TYR F C   1 
ATOM   7981  O O   . TYR F 2 92  ? -60.945  1.005    -9.047  1.00 110.34 ? 98  TYR F O   1 
ATOM   7982  C CB  . TYR F 2 92  ? -61.927  3.947    -8.870  1.00 102.65 ? 98  TYR F CB  1 
ATOM   7983  C CG  . TYR F 2 92  ? -61.952  4.654    -10.206 1.00 104.33 ? 98  TYR F CG  1 
ATOM   7984  C CD1 . TYR F 2 92  ? -61.103  4.268    -11.235 1.00 107.74 ? 98  TYR F CD1 1 
ATOM   7985  C CD2 . TYR F 2 92  ? -62.850  5.685    -10.454 1.00 104.99 ? 98  TYR F CD2 1 
ATOM   7986  C CE1 . TYR F 2 92  ? -61.154  4.879    -12.481 1.00 110.43 ? 98  TYR F CE1 1 
ATOM   7987  C CE2 . TYR F 2 92  ? -62.901  6.315    -11.696 1.00 107.55 ? 98  TYR F CE2 1 
ATOM   7988  C CZ  . TYR F 2 92  ? -62.051  5.904    -12.707 1.00 115.88 ? 98  TYR F CZ  1 
ATOM   7989  O OH  . TYR F 2 92  ? -62.078  6.503    -13.935 1.00 119.22 ? 98  TYR F OH  1 
ATOM   7990  N N   . PRO F 2 93  ? -62.354  1.075    -10.828 1.00 113.31 ? 99  PRO F N   1 
ATOM   7991  C CA  . PRO F 2 93  ? -61.636  -0.020   -11.511 1.00 115.63 ? 99  PRO F CA  1 
ATOM   7992  C C   . PRO F 2 93  ? -60.196  0.333    -11.885 1.00 118.68 ? 99  PRO F C   1 
ATOM   7993  O O   . PRO F 2 93  ? -59.904  1.486    -12.205 1.00 118.06 ? 99  PRO F O   1 
ATOM   7994  C CB  . PRO F 2 93  ? -62.495  -0.274   -12.754 1.00 122.25 ? 99  PRO F CB  1 
ATOM   7995  C CG  . PRO F 2 93  ? -63.174  1.031    -13.007 1.00 126.13 ? 99  PRO F CG  1 
ATOM   7996  C CD  . PRO F 2 93  ? -63.499  1.545    -11.638 1.00 117.64 ? 99  PRO F CD  1 
ATOM   7997  N N   . GLY F 2 94  ? -59.313  -0.655   -11.831 1.00 104.84 ? 100 GLY F N   1 
ATOM   7998  C CA  . GLY F 2 94  ? -57.916  -0.453   -12.193 1.00 103.37 ? 100 GLY F CA  1 
ATOM   7999  C C   . GLY F 2 94  ? -56.981  -1.592   -11.858 1.00 105.38 ? 100 GLY F C   1 
ATOM   8000  O O   . GLY F 2 94  ? -57.416  -2.731   -11.677 1.00 107.93 ? 100 GLY F O   1 
ATOM   8001  N N   . ASP F 2 95  ? -55.682  -1.288   -11.796 1.00 98.05  ? 101 ASP F N   1 
ATOM   8002  C CA  . ASP F 2 95  ? -54.673  -2.286   -11.477 1.00 98.51  ? 101 ASP F CA  1 
ATOM   8003  C C   . ASP F 2 95  ? -53.759  -1.814   -10.351 1.00 96.12  ? 101 ASP F C   1 
ATOM   8004  O O   . ASP F 2 95  ? -53.147  -0.748   -10.452 1.00 92.85  ? 101 ASP F O   1 
ATOM   8005  C CB  . ASP F 2 95  ? -53.866  -2.674   -12.730 1.00 104.73 ? 101 ASP F CB  1 
ATOM   8006  C CG  . ASP F 2 95  ? -54.683  -3.274   -13.863 1.00 118.98 ? 101 ASP F CG  1 
ATOM   8007  O OD1 . ASP F 2 95  ? -55.447  -4.234   -13.605 1.00 121.50 ? 101 ASP F OD1 1 
ATOM   8008  O OD2 . ASP F 2 95  ? -54.521  -2.816   -15.018 1.00 126.41 ? 101 ASP F OD2 1 
ATOM   8009  N N   . PHE F 2 96  ? -53.698  -2.597   -9.263  1.00 91.33  ? 102 PHE F N   1 
ATOM   8010  C CA  . PHE F 2 96  ? -52.837  -2.290   -8.131  1.00 88.65  ? 102 PHE F CA  1 
ATOM   8011  C C   . PHE F 2 96  ? -51.496  -2.899   -8.461  1.00 97.42  ? 102 PHE F C   1 
ATOM   8012  O O   . PHE F 2 96  ? -51.354  -4.129   -8.525  1.00 100.80 ? 102 PHE F O   1 
ATOM   8013  C CB  . PHE F 2 96  ? -53.388  -2.852   -6.806  1.00 88.65  ? 102 PHE F CB  1 
ATOM   8014  C CG  . PHE F 2 96  ? -52.939  -2.084   -5.584  1.00 86.48  ? 102 PHE F CG  1 
ATOM   8015  C CD1 . PHE F 2 96  ? -51.594  -2.024   -5.232  1.00 89.40  ? 102 PHE F CD1 1 
ATOM   8016  C CD2 . PHE F 2 96  ? -53.858  -1.417   -4.786  1.00 85.84  ? 102 PHE F CD2 1 
ATOM   8017  C CE1 . PHE F 2 96  ? -51.178  -1.299   -4.115  1.00 87.79  ? 102 PHE F CE1 1 
ATOM   8018  C CE2 . PHE F 2 96  ? -53.440  -0.702   -3.662  1.00 86.35  ? 102 PHE F CE2 1 
ATOM   8019  C CZ  . PHE F 2 96  ? -52.104  -0.647   -3.335  1.00 84.41  ? 102 PHE F CZ  1 
ATOM   8020  N N   . ILE F 2 97  ? -50.524  -2.028   -8.724  1.00 94.17  ? 103 ILE F N   1 
ATOM   8021  C CA  . ILE F 2 97  ? -49.166  -2.403   -9.112  1.00 96.96  ? 103 ILE F CA  1 
ATOM   8022  C C   . ILE F 2 97  ? -48.395  -2.875   -7.870  1.00 99.57  ? 103 ILE F C   1 
ATOM   8023  O O   . ILE F 2 97  ? -48.406  -2.179   -6.848  1.00 95.73  ? 103 ILE F O   1 
ATOM   8024  C CB  . ILE F 2 97  ? -48.489  -1.217   -9.858  1.00 100.19 ? 103 ILE F CB  1 
ATOM   8025  C CG1 . ILE F 2 97  ? -49.470  -0.517   -10.865 1.00 100.67 ? 103 ILE F CG1 1 
ATOM   8026  C CG2 . ILE F 2 97  ? -47.168  -1.624   -10.509 1.00 104.34 ? 103 ILE F CG2 1 
ATOM   8027  C CD1 . ILE F 2 97  ? -50.051  -1.338   -12.070 1.00 114.71 ? 103 ILE F CD1 1 
ATOM   8028  N N   . ASP F 2 98  ? -47.792  -4.095   -7.948  1.00 98.49  ? 104 ASP F N   1 
ATOM   8029  C CA  . ASP F 2 98  ? -47.029  -4.768   -6.879  1.00 98.03  ? 104 ASP F CA  1 
ATOM   8030  C C   . ASP F 2 98  ? -47.875  -5.043   -5.629  1.00 97.05  ? 104 ASP F C   1 
ATOM   8031  O O   . ASP F 2 98  ? -47.328  -5.064   -4.524  1.00 94.41  ? 104 ASP F O   1 
ATOM   8032  C CB  . ASP F 2 98  ? -45.760  -3.971   -6.475  1.00 99.59  ? 104 ASP F CB  1 
ATOM   8033  C CG  . ASP F 2 98  ? -44.712  -3.696   -7.536  1.00 116.52 ? 104 ASP F CG  1 
ATOM   8034  O OD1 . ASP F 2 98  ? -44.560  -4.535   -8.462  1.00 121.77 ? 104 ASP F OD1 1 
ATOM   8035  O OD2 . ASP F 2 98  ? -43.978  -2.689   -7.392  1.00 121.90 ? 104 ASP F OD2 1 
ATOM   8036  N N   . TYR F 2 99  ? -49.196  -5.247   -5.789  1.00 93.36  ? 105 TYR F N   1 
ATOM   8037  C CA  . TYR F 2 99  ? -50.099  -5.489   -4.652  1.00 91.56  ? 105 TYR F CA  1 
ATOM   8038  C C   . TYR F 2 99  ? -49.620  -6.667   -3.793  1.00 99.36  ? 105 TYR F C   1 
ATOM   8039  O O   . TYR F 2 99  ? -49.573  -6.562   -2.563  1.00 97.30  ? 105 TYR F O   1 
ATOM   8040  C CB  . TYR F 2 99  ? -51.574  -5.653   -5.111  1.00 92.12  ? 105 TYR F CB  1 
ATOM   8041  C CG  . TYR F 2 99  ? -52.548  -6.074   -4.025  1.00 90.91  ? 105 TYR F CG  1 
ATOM   8042  C CD1 . TYR F 2 99  ? -52.683  -5.335   -2.856  1.00 89.04  ? 105 TYR F CD1 1 
ATOM   8043  C CD2 . TYR F 2 99  ? -53.354  -7.197   -4.181  1.00 93.95  ? 105 TYR F CD2 1 
ATOM   8044  C CE1 . TYR F 2 99  ? -53.544  -5.741   -1.840  1.00 88.45  ? 105 TYR F CE1 1 
ATOM   8045  C CE2 . TYR F 2 99  ? -54.246  -7.590   -3.186  1.00 93.78  ? 105 TYR F CE2 1 
ATOM   8046  C CZ  . TYR F 2 99  ? -54.345  -6.852   -2.020  1.00 96.39  ? 105 TYR F CZ  1 
ATOM   8047  O OH  . TYR F 2 99  ? -55.208  -7.241   -1.027  1.00 99.11  ? 105 TYR F OH  1 
ATOM   8048  N N   . GLU F 2 100 ? -49.218  -7.757   -4.471  1.00 100.96 ? 106 GLU F N   1 
ATOM   8049  C CA  . GLU F 2 100 ? -48.697  -9.014   -3.927  1.00 103.97 ? 106 GLU F CA  1 
ATOM   8050  C C   . GLU F 2 100 ? -47.420  -8.739   -3.128  1.00 106.05 ? 106 GLU F C   1 
ATOM   8051  O O   . GLU F 2 100 ? -47.210  -9.329   -2.069  1.00 105.42 ? 106 GLU F O   1 
ATOM   8052  C CB  . GLU F 2 100 ? -48.409  -10.024  -5.067  1.00 111.19 ? 106 GLU F CB  1 
ATOM   8053  C CG  . GLU F 2 100 ? -49.126  -9.775   -6.397  1.00 128.85 ? 106 GLU F CG  1 
ATOM   8054  C CD  . GLU F 2 100 ? -48.485  -8.771   -7.347  1.00 160.62 ? 106 GLU F CD  1 
ATOM   8055  O OE1 . GLU F 2 100 ? -47.379  -9.055   -7.865  1.00 160.66 ? 106 GLU F OE1 1 
ATOM   8056  O OE2 . GLU F 2 100 ? -49.109  -7.712   -7.600  1.00 155.27 ? 106 GLU F OE2 1 
ATOM   8057  N N   . GLU F 2 101 ? -46.583  -7.818   -3.639  1.00 102.15 ? 107 GLU F N   1 
ATOM   8058  C CA  . GLU F 2 101 ? -45.338  -7.404   -3.008  1.00 101.76 ? 107 GLU F CA  1 
ATOM   8059  C C   . GLU F 2 101 ? -45.642  -6.498   -1.841  1.00 99.98  ? 107 GLU F C   1 
ATOM   8060  O O   . GLU F 2 101 ? -44.881  -6.518   -0.888  1.00 100.26 ? 107 GLU F O   1 
ATOM   8061  C CB  . GLU F 2 101 ? -44.402  -6.707   -4.011  1.00 105.13 ? 107 GLU F CB  1 
ATOM   8062  C CG  . GLU F 2 101 ? -43.551  -7.659   -4.850  1.00 125.38 ? 107 GLU F CG  1 
ATOM   8063  C CD  . GLU F 2 101 ? -44.027  -8.006   -6.255  1.00 152.75 ? 107 GLU F CD  1 
ATOM   8064  O OE1 . GLU F 2 101 ? -43.986  -9.207   -6.609  1.00 160.20 ? 107 GLU F OE1 1 
ATOM   8065  O OE2 . GLU F 2 101 ? -44.406  -7.084   -7.014  1.00 140.16 ? 107 GLU F OE2 1 
ATOM   8066  N N   . LEU F 2 102 ? -46.760  -5.734   -1.892  1.00 92.44  ? 108 LEU F N   1 
ATOM   8067  C CA  . LEU F 2 102 ? -47.191  -4.841   -0.804  1.00 89.12  ? 108 LEU F CA  1 
ATOM   8068  C C   . LEU F 2 102 ? -47.777  -5.620   0.388   1.00 93.37  ? 108 LEU F C   1 
ATOM   8069  O O   . LEU F 2 102 ? -47.477  -5.291   1.546   1.00 91.46  ? 108 LEU F O   1 
ATOM   8070  C CB  . LEU F 2 102 ? -48.169  -3.743   -1.301  1.00 86.53  ? 108 LEU F CB  1 
ATOM   8071  C CG  . LEU F 2 102 ? -48.657  -2.675   -0.275  1.00 87.65  ? 108 LEU F CG  1 
ATOM   8072  C CD1 . LEU F 2 102 ? -47.504  -1.953   0.402   1.00 88.08  ? 108 LEU F CD1 1 
ATOM   8073  C CD2 . LEU F 2 102 ? -49.531  -1.644   -0.931  1.00 86.78  ? 108 LEU F CD2 1 
ATOM   8074  N N   . ARG F 2 103 ? -48.601  -6.657   0.098   1.00 91.40  ? 109 ARG F N   1 
ATOM   8075  C CA  . ARG F 2 103 ? -49.214  -7.541   1.096   1.00 91.19  ? 109 ARG F CA  1 
ATOM   8076  C C   . ARG F 2 103 ? -48.134  -8.110   2.010   1.00 98.59  ? 109 ARG F C   1 
ATOM   8077  O O   . ARG F 2 103 ? -48.304  -8.101   3.225   1.00 97.15  ? 109 ARG F O   1 
ATOM   8078  C CB  . ARG F 2 103 ? -50.008  -8.661   0.422   1.00 92.19  ? 109 ARG F CB  1 
ATOM   8079  C CG  . ARG F 2 103 ? -51.329  -8.181   -0.150  1.00 101.66 ? 109 ARG F CG  1 
ATOM   8080  C CD  . ARG F 2 103 ? -52.113  -9.293   -0.817  1.00 120.90 ? 109 ARG F CD  1 
ATOM   8081  N NE  . ARG F 2 103 ? -52.759  -10.182  0.150   1.00 134.06 ? 109 ARG F NE  1 
ATOM   8082  C CZ  . ARG F 2 103 ? -52.360  -11.423  0.412   1.00 154.37 ? 109 ARG F CZ  1 
ATOM   8083  N NH1 . ARG F 2 103 ? -51.325  -11.948  -0.235  1.00 150.08 ? 109 ARG F NH1 1 
ATOM   8084  N NH2 . ARG F 2 103 ? -52.999  -12.153  1.315   1.00 138.13 ? 109 ARG F NH2 1 
ATOM   8085  N N   . GLU F 2 104 ? -46.990  -8.523   1.423   1.00 99.77  ? 110 GLU F N   1 
ATOM   8086  C CA  . GLU F 2 104 ? -45.792  -9.017   2.112   1.00 102.25 ? 110 GLU F CA  1 
ATOM   8087  C C   . GLU F 2 104 ? -45.273  -7.930   3.106   1.00 102.76 ? 110 GLU F C   1 
ATOM   8088  O O   . GLU F 2 104 ? -45.125  -8.222   4.299   1.00 102.83 ? 110 GLU F O   1 
ATOM   8089  C CB  . GLU F 2 104 ? -44.711  -9.402   1.055   1.00 107.62 ? 110 GLU F CB  1 
ATOM   8090  C CG  . GLU F 2 104 ? -43.339  -9.826   1.589   1.00 123.75 ? 110 GLU F CG  1 
ATOM   8091  C CD  . GLU F 2 104 ? -42.107  -9.427   0.780   1.00 151.79 ? 110 GLU F CD  1 
ATOM   8092  O OE1 . GLU F 2 104 ? -42.234  -9.178   -0.442  1.00 159.26 ? 110 GLU F OE1 1 
ATOM   8093  O OE2 . GLU F 2 104 ? -41.001  -9.388   1.369   1.00 141.10 ? 110 GLU F OE2 1 
ATOM   8094  N N   . GLN F 2 105 ? -45.057  -6.678   2.616   1.00 95.57  ? 111 GLN F N   1 
ATOM   8095  C CA  . GLN F 2 105 ? -44.532  -5.554   3.406   1.00 92.98  ? 111 GLN F CA  1 
ATOM   8096  C C   . GLN F 2 105 ? -45.374  -5.250   4.624   1.00 95.31  ? 111 GLN F C   1 
ATOM   8097  O O   . GLN F 2 105 ? -44.831  -4.935   5.681   1.00 94.83  ? 111 GLN F O   1 
ATOM   8098  C CB  . GLN F 2 105 ? -44.388  -4.272   2.568   1.00 92.39  ? 111 GLN F CB  1 
ATOM   8099  C CG  . GLN F 2 105 ? -43.726  -4.438   1.205   1.00 104.83 ? 111 GLN F CG  1 
ATOM   8100  C CD  . GLN F 2 105 ? -42.254  -4.775   1.229   1.00 125.02 ? 111 GLN F CD  1 
ATOM   8101  O OE1 . GLN F 2 105 ? -41.414  -3.995   1.691   1.00 122.46 ? 111 GLN F OE1 1 
ATOM   8102  N NE2 . GLN F 2 105 ? -41.902  -5.912   0.645   1.00 117.24 ? 111 GLN F NE2 1 
ATOM   8103  N N   . LEU F 2 106 ? -46.696  -5.361   4.479   1.00 91.14  ? 112 LEU F N   1 
ATOM   8104  C CA  . LEU F 2 106 ? -47.627  -5.046   5.548   1.00 89.70  ? 112 LEU F CA  1 
ATOM   8105  C C   . LEU F 2 106 ? -48.008  -6.218   6.482   1.00 98.95  ? 112 LEU F C   1 
ATOM   8106  O O   . LEU F 2 106 ? -48.837  -6.002   7.373   1.00 97.67  ? 112 LEU F O   1 
ATOM   8107  C CB  . LEU F 2 106 ? -48.876  -4.414   4.941   1.00 87.16  ? 112 LEU F CB  1 
ATOM   8108  C CG  . LEU F 2 106 ? -48.755  -2.942   4.643   1.00 89.89  ? 112 LEU F CG  1 
ATOM   8109  C CD1 . LEU F 2 106 ? -49.538  -2.583   3.429   1.00 89.33  ? 112 LEU F CD1 1 
ATOM   8110  C CD2 . LEU F 2 106 ? -49.231  -2.123   5.804   1.00 91.25  ? 112 LEU F CD2 1 
ATOM   8111  N N   . SER F 2 107 ? -47.389  -7.425   6.326   1.00 100.35 ? 113 SER F N   1 
ATOM   8112  C CA  . SER F 2 107 ? -47.692  -8.622   7.143   1.00 102.48 ? 113 SER F CA  1 
ATOM   8113  C C   . SER F 2 107 ? -47.783  -8.338   8.654   1.00 105.44 ? 113 SER F C   1 
ATOM   8114  O O   . SER F 2 107 ? -48.873  -8.428   9.222   1.00 104.31 ? 113 SER F O   1 
ATOM   8115  C CB  . SER F 2 107 ? -46.713  -9.758   6.857   1.00 110.33 ? 113 SER F CB  1 
ATOM   8116  O OG  . SER F 2 107 ? -46.938  -10.858  7.726   1.00 121.64 ? 113 SER F OG  1 
ATOM   8117  N N   . SER F 2 108 ? -46.655  -7.958   9.279   1.00 101.72 ? 114 SER F N   1 
ATOM   8118  C CA  . SER F 2 108 ? -46.586  -7.618   10.698  1.00 100.86 ? 114 SER F CA  1 
ATOM   8119  C C   . SER F 2 108 ? -46.016  -6.208   10.832  1.00 102.84 ? 114 SER F C   1 
ATOM   8120  O O   . SER F 2 108 ? -45.191  -5.813   10.004  1.00 102.54 ? 114 SER F O   1 
ATOM   8121  C CB  . SER F 2 108 ? -45.715  -8.623   11.439  1.00 107.49 ? 114 SER F CB  1 
ATOM   8122  O OG  . SER F 2 108 ? -45.906  -8.539   12.842  1.00 117.27 ? 114 SER F OG  1 
ATOM   8123  N N   . VAL F 2 109 ? -46.468  -5.441   11.853  1.00 98.48  ? 115 VAL F N   1 
ATOM   8124  C CA  . VAL F 2 109 ? -46.029  -4.058   12.084  1.00 97.58  ? 115 VAL F CA  1 
ATOM   8125  C C   . VAL F 2 109 ? -45.847  -3.728   13.600  1.00 102.68 ? 115 VAL F C   1 
ATOM   8126  O O   . VAL F 2 109 ? -46.644  -4.154   14.448  1.00 101.88 ? 115 VAL F O   1 
ATOM   8127  C CB  . VAL F 2 109 ? -46.960  -3.055   11.333  1.00 98.71  ? 115 VAL F CB  1 
ATOM   8128  C CG1 . VAL F 2 109 ? -47.318  -1.828   12.165  1.00 97.96  ? 115 VAL F CG1 1 
ATOM   8129  C CG2 . VAL F 2 109 ? -46.354  -2.642   10.000  1.00 98.06  ? 115 VAL F CG2 1 
ATOM   8130  N N   . SER F 2 110 ? -44.767  -2.959   13.901  1.00 100.79 ? 116 SER F N   1 
ATOM   8131  C CA  . SER F 2 110 ? -44.372  -2.480   15.230  1.00 102.55 ? 116 SER F CA  1 
ATOM   8132  C C   . SER F 2 110 ? -44.988  -1.100   15.538  1.00 107.53 ? 116 SER F C   1 
ATOM   8133  O O   . SER F 2 110 ? -45.456  -0.877   16.660  1.00 108.63 ? 116 SER F O   1 
ATOM   8134  C CB  . SER F 2 110 ? -42.852  -2.428   15.347  1.00 107.49 ? 116 SER F CB  1 
ATOM   8135  O OG  . SER F 2 110 ? -42.290  -3.716   15.155  1.00 114.52 ? 116 SER F OG  1 
ATOM   8136  N N   . SER F 2 111 A -44.988  -0.183   14.537  1.00 103.33 ? 116 SER F N   1 
ATOM   8137  C CA  . SER F 2 111 A -45.579  1.169    14.588  1.00 102.29 ? 116 SER F CA  1 
ATOM   8138  C C   . SER F 2 111 A -46.188  1.516    13.214  1.00 103.63 ? 116 SER F C   1 
ATOM   8139  O O   . SER F 2 111 A -45.597  1.172    12.184  1.00 102.60 ? 116 SER F O   1 
ATOM   8140  C CB  . SER F 2 111 A -44.542  2.211    14.998  1.00 107.80 ? 116 SER F CB  1 
ATOM   8141  O OG  . SER F 2 111 A -45.138  3.487    15.173  1.00 114.43 ? 116 SER F OG  1 
ATOM   8142  N N   . PHE F 2 112 B -47.376  2.167    13.201  1.00 98.98  ? 116 PHE F N   1 
ATOM   8143  C CA  . PHE F 2 112 B -48.101  2.516    11.971  1.00 96.72  ? 116 PHE F CA  1 
ATOM   8144  C C   . PHE F 2 112 B -48.889  3.827    12.078  1.00 101.62 ? 116 PHE F C   1 
ATOM   8145  O O   . PHE F 2 112 B -50.106  3.831    12.295  1.00 100.71 ? 116 PHE F O   1 
ATOM   8146  C CB  . PHE F 2 112 B -49.003  1.352    11.529  1.00 96.71  ? 116 PHE F CB  1 
ATOM   8147  C CG  . PHE F 2 112 B -49.483  1.399    10.102  1.00 96.07  ? 116 PHE F CG  1 
ATOM   8148  C CD1 . PHE F 2 112 B -48.664  0.981    9.061   1.00 98.96  ? 116 PHE F CD1 1 
ATOM   8149  C CD2 . PHE F 2 112 B -50.773  1.809    9.801   1.00 96.61  ? 116 PHE F CD2 1 
ATOM   8150  C CE1 . PHE F 2 112 B -49.122  0.993    7.745   1.00 98.43  ? 116 PHE F CE1 1 
ATOM   8151  C CE2 . PHE F 2 112 B -51.232  1.810    8.484   1.00 98.07  ? 116 PHE F CE2 1 
ATOM   8152  C CZ  . PHE F 2 112 B -50.406  1.392    7.467   1.00 96.18  ? 116 PHE F CZ  1 
ATOM   8153  N N   . GLU F 2 113 C -48.182  4.941    11.891  1.00 99.87  ? 116 GLU F N   1 
ATOM   8154  C CA  . GLU F 2 113 C -48.755  6.276    11.964  1.00 100.47 ? 116 GLU F CA  1 
ATOM   8155  C C   . GLU F 2 113 C -49.303  6.700    10.606  1.00 102.07 ? 116 GLU F C   1 
ATOM   8156  O O   . GLU F 2 113 C -48.559  6.757    9.627   1.00 100.76 ? 116 GLU F O   1 
ATOM   8157  C CB  . GLU F 2 113 C -47.702  7.286    12.474  1.00 105.06 ? 116 GLU F CB  1 
ATOM   8158  C CG  . GLU F 2 113 C -48.233  8.703    12.697  1.00 122.34 ? 116 GLU F CG  1 
ATOM   8159  C CD  . GLU F 2 113 C -47.238  9.857    12.672  1.00 152.95 ? 116 GLU F CD  1 
ATOM   8160  O OE1 . GLU F 2 113 C -46.009  9.605    12.651  1.00 149.79 ? 116 GLU F OE1 1 
ATOM   8161  O OE2 . GLU F 2 113 C -47.698  11.023   12.675  1.00 148.38 ? 116 GLU F OE2 1 
ATOM   8162  N N   . ARG F 2 114 ? -50.606  6.986    10.554  1.00 98.36  ? 117 ARG F N   1 
ATOM   8163  C CA  . ARG F 2 114 ? -51.266  7.508    9.363   1.00 96.78  ? 117 ARG F CA  1 
ATOM   8164  C C   . ARG F 2 114 ? -51.240  9.028    9.554   1.00 100.98 ? 117 ARG F C   1 
ATOM   8165  O O   . ARG F 2 114 ? -51.661  9.526    10.610  1.00 101.80 ? 117 ARG F O   1 
ATOM   8166  C CB  . ARG F 2 114 ? -52.702  6.961    9.241   1.00 96.63  ? 117 ARG F CB  1 
ATOM   8167  C CG  . ARG F 2 114 ? -53.544  7.585    8.130   1.00 111.08 ? 117 ARG F CG  1 
ATOM   8168  C CD  . ARG F 2 114 ? -54.923  6.962    8.132   1.00 136.72 ? 117 ARG F CD  1 
ATOM   8169  N NE  . ARG F 2 114 ? -55.957  7.847    7.591   1.00 159.64 ? 117 ARG F NE  1 
ATOM   8170  C CZ  . ARG F 2 114 ? -56.676  8.702    8.315   1.00 180.06 ? 117 ARG F CZ  1 
ATOM   8171  N NH1 . ARG F 2 114 ? -56.459  8.826    9.621   1.00 165.82 ? 117 ARG F NH1 1 
ATOM   8172  N NH2 . ARG F 2 114 ? -57.609  9.449    7.738   1.00 171.63 ? 117 ARG F NH2 1 
ATOM   8173  N N   . PHE F 2 115 ? -50.685  9.753    8.573   1.00 96.80  ? 118 PHE F N   1 
ATOM   8174  C CA  . PHE F 2 115 ? -50.569  11.209   8.661   1.00 98.33  ? 118 PHE F CA  1 
ATOM   8175  C C   . PHE F 2 115 ? -50.918  11.904   7.360   1.00 101.01 ? 118 PHE F C   1 
ATOM   8176  O O   . PHE F 2 115 ? -50.685  11.342   6.294   1.00 99.06  ? 118 PHE F O   1 
ATOM   8177  C CB  . PHE F 2 115 ? -49.159  11.624   9.145   1.00 102.46 ? 118 PHE F CB  1 
ATOM   8178  C CG  . PHE F 2 115 ? -48.010  11.356   8.197   1.00 103.25 ? 118 PHE F CG  1 
ATOM   8179  C CD1 . PHE F 2 115 ? -47.407  10.105   8.142   1.00 105.38 ? 118 PHE F CD1 1 
ATOM   8180  C CD2 . PHE F 2 115 ? -47.495  12.369   7.401   1.00 106.12 ? 118 PHE F CD2 1 
ATOM   8181  C CE1 . PHE F 2 115 ? -46.336  9.860    7.278   1.00 106.54 ? 118 PHE F CE1 1 
ATOM   8182  C CE2 . PHE F 2 115 ? -46.427  12.123   6.535   1.00 109.42 ? 118 PHE F CE2 1 
ATOM   8183  C CZ  . PHE F 2 115 ? -45.854  10.871   6.482   1.00 106.83 ? 118 PHE F CZ  1 
ATOM   8184  N N   . GLU F 2 116 ? -51.448  13.136   7.445   1.00 98.62  ? 119 GLU F N   1 
ATOM   8185  C CA  . GLU F 2 116 ? -51.770  13.939   6.269   1.00 97.66  ? 119 GLU F CA  1 
ATOM   8186  C C   . GLU F 2 116 ? -50.437  14.421   5.672   1.00 104.57 ? 119 GLU F C   1 
ATOM   8187  O O   . GLU F 2 116 ? -49.859  15.414   6.138   1.00 107.79 ? 119 GLU F O   1 
ATOM   8188  C CB  . GLU F 2 116 ? -52.711  15.112   6.623   1.00 100.18 ? 119 GLU F CB  1 
ATOM   8189  C CG  . GLU F 2 116 ? -54.008  15.123   5.827   1.00 101.29 ? 119 GLU F CG  1 
ATOM   8190  C CD  . GLU F 2 116 ? -55.041  16.179   6.186   1.00 104.08 ? 119 GLU F CD  1 
ATOM   8191  O OE1 . GLU F 2 116 ? -55.179  16.513   7.385   1.00 86.03  ? 119 GLU F OE1 1 
ATOM   8192  O OE2 . GLU F 2 116 ? -55.762  16.630   5.268   1.00 90.72  ? 119 GLU F OE2 1 
ATOM   8193  N N   . ILE F 2 117 ? -49.904  13.638   4.710   1.00 99.08  ? 120 ILE F N   1 
ATOM   8194  C CA  . ILE F 2 117 ? -48.636  13.917   4.031   1.00 99.90  ? 120 ILE F CA  1 
ATOM   8195  C C   . ILE F 2 117 ? -48.740  15.228   3.238   1.00 104.93 ? 120 ILE F C   1 
ATOM   8196  O O   . ILE F 2 117 ? -47.872  16.101   3.366   1.00 108.58 ? 120 ILE F O   1 
ATOM   8197  C CB  . ILE F 2 117 ? -48.137  12.698   3.194   1.00 101.34 ? 120 ILE F CB  1 
ATOM   8198  C CG1 . ILE F 2 117 ? -46.759  12.984   2.540   1.00 103.81 ? 120 ILE F CG1 1 
ATOM   8199  C CG2 . ILE F 2 117 ? -49.187  12.200   2.172   1.00 99.40  ? 120 ILE F CG2 1 
ATOM   8200  C CD1 . ILE F 2 117 ? -46.006  11.779   2.053   1.00 109.34 ? 120 ILE F CD1 1 
ATOM   8201  N N   . PHE F 2 118 ? -49.835  15.365   2.463   1.00 97.27  ? 121 PHE F N   1 
ATOM   8202  C CA  . PHE F 2 118 ? -50.165  16.538   1.673   1.00 96.85  ? 121 PHE F CA  1 
ATOM   8203  C C   . PHE F 2 118 ? -51.627  16.875   1.995   1.00 99.15  ? 121 PHE F C   1 
ATOM   8204  O O   . PHE F 2 118 ? -52.532  16.379   1.310   1.00 96.93  ? 121 PHE F O   1 
ATOM   8205  C CB  . PHE F 2 118 ? -49.978  16.270   0.174   1.00 97.20  ? 121 PHE F CB  1 
ATOM   8206  C CG  . PHE F 2 118 ? -48.630  15.764   -0.289  1.00 98.94  ? 121 PHE F CG  1 
ATOM   8207  C CD1 . PHE F 2 118 ? -47.524  16.609   -0.321  1.00 104.86 ? 121 PHE F CD1 1 
ATOM   8208  C CD2 . PHE F 2 118 ? -48.489  14.473   -0.786  1.00 98.92  ? 121 PHE F CD2 1 
ATOM   8209  C CE1 . PHE F 2 118 ? -46.287  16.154   -0.794  1.00 106.95 ? 121 PHE F CE1 1 
ATOM   8210  C CE2 . PHE F 2 118 ? -47.254  14.021   -1.261  1.00 102.95 ? 121 PHE F CE2 1 
ATOM   8211  C CZ  . PHE F 2 118 ? -46.162  14.866   -1.264  1.00 104.12 ? 121 PHE F CZ  1 
ATOM   8212  N N   . PRO F 2 119 ? -51.874  17.665   3.076   1.00 97.17  ? 122 PRO F N   1 
ATOM   8213  C CA  . PRO F 2 119 ? -53.259  17.973   3.474   1.00 97.20  ? 122 PRO F CA  1 
ATOM   8214  C C   . PRO F 2 119 ? -54.126  18.635   2.410   1.00 99.82  ? 122 PRO F C   1 
ATOM   8215  O O   . PRO F 2 119 ? -53.700  19.591   1.756   1.00 101.30 ? 122 PRO F O   1 
ATOM   8216  C CB  . PRO F 2 119 ? -53.089  18.869   4.711   1.00 102.43 ? 122 PRO F CB  1 
ATOM   8217  C CG  . PRO F 2 119 ? -51.712  19.401   4.615   1.00 108.39 ? 122 PRO F CG  1 
ATOM   8218  C CD  . PRO F 2 119 ? -50.916  18.283   4.014   1.00 101.40 ? 122 PRO F CD  1 
ATOM   8219  N N   . LYS F 2 120 ? -55.360  18.113   2.268   1.00 93.23  ? 123 LYS F N   1 
ATOM   8220  C CA  . LYS F 2 120 ? -56.386  18.544   1.320   1.00 92.77  ? 123 LYS F CA  1 
ATOM   8221  C C   . LYS F 2 120 ? -56.584  20.061   1.305   1.00 99.82  ? 123 LYS F C   1 
ATOM   8222  O O   . LYS F 2 120 ? -56.676  20.645   0.229   1.00 100.72 ? 123 LYS F O   1 
ATOM   8223  C CB  . LYS F 2 120 ? -57.705  17.817   1.622   1.00 94.27  ? 123 LYS F CB  1 
ATOM   8224  C CG  . LYS F 2 120 ? -58.629  17.615   0.425   1.00 94.90  ? 123 LYS F CG  1 
ATOM   8225  C CD  . LYS F 2 120 ? -59.919  16.975   0.889   1.00 94.52  ? 123 LYS F CD  1 
ATOM   8226  C CE  . LYS F 2 120 ? -61.095  17.350   0.040   1.00 98.70  ? 123 LYS F CE  1 
ATOM   8227  N NZ  . LYS F 2 120 ? -62.360  17.110   0.776   1.00 104.69 ? 123 LYS F NZ  1 
ATOM   8228  N N   . THR F 2 121 ? -56.584  20.693   2.482   1.00 98.65  ? 124 THR F N   1 
ATOM   8229  C CA  . THR F 2 121 ? -56.760  22.132   2.660   1.00 102.86 ? 124 THR F CA  1 
ATOM   8230  C C   . THR F 2 121 ? -55.733  22.968   1.882   1.00 107.56 ? 124 THR F C   1 
ATOM   8231  O O   . THR F 2 121 ? -56.077  23.538   0.850   1.00 106.50 ? 124 THR F O   1 
ATOM   8232  C CB  . THR F 2 121 ? -56.770  22.495   4.158   1.00 124.44 ? 124 THR F CB  1 
ATOM   8233  O OG1 . THR F 2 121 ? -55.557  22.037   4.766   1.00 131.25 ? 124 THR F OG1 1 
ATOM   8234  C CG2 . THR F 2 121 ? -57.965  21.935   4.900   1.00 123.33 ? 124 THR F CG2 1 
ATOM   8235  N N   . SER F 2 122 ? -54.475  23.008   2.363   1.00 106.48 ? 125 SER F N   1 
ATOM   8236  C CA  . SER F 2 122 ? -53.379  23.799   1.804   1.00 109.37 ? 125 SER F CA  1 
ATOM   8237  C C   . SER F 2 122 ? -52.736  23.236   0.527   1.00 112.40 ? 125 SER F C   1 
ATOM   8238  O O   . SER F 2 122 ? -52.943  23.808   -0.540  1.00 112.60 ? 125 SER F O   1 
ATOM   8239  C CB  . SER F 2 122 ? -52.311  24.038   2.864   1.00 116.72 ? 125 SER F CB  1 
ATOM   8240  O OG  . SER F 2 122 ? -51.817  22.806   3.363   1.00 125.86 ? 125 SER F OG  1 
ATOM   8241  N N   . SER F 2 123 ? -51.946  22.146   0.647   1.00 108.03 ? 126 SER F N   1 
ATOM   8242  C CA  . SER F 2 123 ? -51.142  21.445   -0.369  1.00 106.48 ? 126 SER F CA  1 
ATOM   8243  C C   . SER F 2 123 ? -51.491  21.660   -1.848  1.00 108.35 ? 126 SER F C   1 
ATOM   8244  O O   . SER F 2 123 ? -50.570  21.837   -2.645  1.00 109.89 ? 126 SER F O   1 
ATOM   8245  C CB  . SER F 2 123 ? -51.115  19.948   -0.099  1.00 108.41 ? 126 SER F CB  1 
ATOM   8246  O OG  . SER F 2 123 ? -50.385  19.704   1.090   1.00 122.67 ? 126 SER F OG  1 
ATOM   8247  N N   . TRP F 2 124 ? -52.776  21.603   -2.223  1.00 101.22 ? 127 TRP F N   1 
ATOM   8248  C CA  . TRP F 2 124 ? -53.186  21.749   -3.616  1.00 100.06 ? 127 TRP F CA  1 
ATOM   8249  C C   . TRP F 2 124 ? -54.033  23.015   -3.814  1.00 105.43 ? 127 TRP F C   1 
ATOM   8250  O O   . TRP F 2 124 ? -55.263  22.945   -3.726  1.00 104.90 ? 127 TRP F O   1 
ATOM   8251  C CB  . TRP F 2 124 ? -53.891  20.465   -4.087  1.00 95.87  ? 127 TRP F CB  1 
ATOM   8252  C CG  . TRP F 2 124 ? -53.267  19.219   -3.521  1.00 95.36  ? 127 TRP F CG  1 
ATOM   8253  C CD1 . TRP F 2 124 ? -53.741  18.456   -2.493  1.00 96.88  ? 127 TRP F CD1 1 
ATOM   8254  C CD2 . TRP F 2 124 ? -51.981  18.688   -3.851  1.00 95.38  ? 127 TRP F CD2 1 
ATOM   8255  N NE1 . TRP F 2 124 ? -52.854  17.446   -2.203  1.00 95.32  ? 127 TRP F NE1 1 
ATOM   8256  C CE2 . TRP F 2 124 ? -51.760  17.570   -3.017  1.00 97.89  ? 127 TRP F CE2 1 
ATOM   8257  C CE3 . TRP F 2 124 ? -51.001  19.031   -4.798  1.00 98.58  ? 127 TRP F CE3 1 
ATOM   8258  C CZ2 . TRP F 2 124 ? -50.607  16.788   -3.109  1.00 97.52  ? 127 TRP F CZ2 1 
ATOM   8259  C CZ3 . TRP F 2 124 ? -49.863  18.251   -4.892  1.00 100.37 ? 127 TRP F CZ3 1 
ATOM   8260  C CH2 . TRP F 2 124 ? -49.670  17.150   -4.048  1.00 99.59  ? 127 TRP F CH2 1 
ATOM   8261  N N   . PRO F 2 125 ? -53.391  24.191   -4.046  1.00 104.13 ? 128 PRO F N   1 
ATOM   8262  C CA  . PRO F 2 125 ? -54.158  25.446   -4.154  1.00 106.52 ? 128 PRO F CA  1 
ATOM   8263  C C   . PRO F 2 125 ? -54.570  25.880   -5.559  1.00 110.24 ? 128 PRO F C   1 
ATOM   8264  O O   . PRO F 2 125 ? -55.575  26.579   -5.698  1.00 111.41 ? 128 PRO F O   1 
ATOM   8265  C CB  . PRO F 2 125 ? -53.234  26.475   -3.506  1.00 112.06 ? 128 PRO F CB  1 
ATOM   8266  C CG  . PRO F 2 125 ? -51.847  25.903   -3.675  1.00 116.15 ? 128 PRO F CG  1 
ATOM   8267  C CD  . PRO F 2 125 ? -51.943  24.463   -4.116  1.00 107.50 ? 128 PRO F CD  1 
ATOM   8268  N N   . ASN F 2 126 ? -53.794  25.503   -6.589  1.00 118.81 ? 129 ASN F N   1 
ATOM   8269  C CA  . ASN F 2 126 ? -54.108  25.853   -7.973  1.00 119.51 ? 129 ASN F CA  1 
ATOM   8270  C C   . ASN F 2 126 ? -54.837  24.715   -8.691  1.00 121.17 ? 129 ASN F C   1 
ATOM   8271  O O   . ASN F 2 126 ? -54.816  24.630   -9.923  1.00 120.89 ? 129 ASN F O   1 
ATOM   8272  C CB  . ASN F 2 126 ? -52.855  26.307   -8.716  1.00 122.46 ? 129 ASN F CB  1 
ATOM   8273  C CG  . ASN F 2 126 ? -52.293  27.608   -8.197  1.00 148.17 ? 129 ASN F CG  1 
ATOM   8274  O OD1 . ASN F 2 126 ? -53.016  28.574   -7.922  1.00 142.79 ? 129 ASN F OD1 1 
ATOM   8275  N ND2 . ASN F 2 126 ? -50.980  27.670   -8.067  1.00 142.63 ? 129 ASN F ND2 1 
ATOM   8276  N N   . HIS F 2 127 ? -55.511  23.850   -7.899  1.00 116.67 ? 130 HIS F N   1 
ATOM   8277  C CA  . HIS F 2 127 ? -56.262  22.681   -8.368  1.00 113.99 ? 130 HIS F CA  1 
ATOM   8278  C C   . HIS F 2 127 ? -57.553  22.432   -7.567  1.00 115.24 ? 130 HIS F C   1 
ATOM   8279  O O   . HIS F 2 127 ? -57.678  22.856   -6.413  1.00 114.51 ? 130 HIS F O   1 
ATOM   8280  C CB  . HIS F 2 127 ? -55.362  21.430   -8.365  1.00 113.14 ? 130 HIS F CB  1 
ATOM   8281  C CG  . HIS F 2 127 ? -54.098  21.614   -9.145  1.00 118.26 ? 130 HIS F CG  1 
ATOM   8282  N ND1 . HIS F 2 127 ? -52.919  21.998   -8.529  1.00 121.15 ? 130 HIS F ND1 1 
ATOM   8283  C CD2 . HIS F 2 127 ? -53.895  21.551   -10.480 1.00 121.19 ? 130 HIS F CD2 1 
ATOM   8284  C CE1 . HIS F 2 127 ? -52.027  22.106   -9.500  1.00 122.36 ? 130 HIS F CE1 1 
ATOM   8285  N NE2 . HIS F 2 127 ? -52.565  21.845   -10.690 1.00 122.87 ? 130 HIS F NE2 1 
ATOM   8286  N N   . ASP F 2 128 ? -58.514  21.750   -8.206  1.00 110.46 ? 131 ASP F N   1 
ATOM   8287  C CA  . ASP F 2 128 ? -59.796  21.391   -7.616  1.00 109.52 ? 131 ASP F CA  1 
ATOM   8288  C C   . ASP F 2 128 ? -59.654  20.011   -6.984  1.00 110.66 ? 131 ASP F C   1 
ATOM   8289  O O   . ASP F 2 128 ? -59.437  19.013   -7.676  1.00 108.93 ? 131 ASP F O   1 
ATOM   8290  C CB  . ASP F 2 128 ? -60.908  21.408   -8.688  1.00 112.36 ? 131 ASP F CB  1 
ATOM   8291  C CG  . ASP F 2 128 ? -62.336  21.222   -8.190  1.00 124.50 ? 131 ASP F CG  1 
ATOM   8292  O OD1 . ASP F 2 128 ? -62.552  20.369   -7.300  1.00 123.90 ? 131 ASP F OD1 1 
ATOM   8293  O OD2 . ASP F 2 128 ? -63.249  21.869   -8.751  1.00 131.45 ? 131 ASP F OD2 1 
ATOM   8294  N N   . SER F 2 129 ? -59.754  19.971   -5.659  1.00 106.67 ? 132 SER F N   1 
ATOM   8295  C CA  . SER F 2 129 ? -59.644  18.751   -4.863  1.00 104.33 ? 132 SER F CA  1 
ATOM   8296  C C   . SER F 2 129 ? -61.020  18.204   -4.470  1.00 107.59 ? 132 SER F C   1 
ATOM   8297  O O   . SER F 2 129 ? -61.172  16.996   -4.265  1.00 106.71 ? 132 SER F O   1 
ATOM   8298  C CB  . SER F 2 129 ? -58.800  19.011   -3.617  1.00 107.66 ? 132 SER F CB  1 
ATOM   8299  O OG  . SER F 2 129 ? -58.954  20.327   -3.109  1.00 115.38 ? 132 SER F OG  1 
ATOM   8300  N N   . ASP F 2 130 ? -62.018  19.099   -4.382  1.00 104.25 ? 133 ASP F N   1 
ATOM   8301  C CA  . ASP F 2 130 ? -63.381  18.795   -3.959  1.00 103.70 ? 133 ASP F CA  1 
ATOM   8302  C C   . ASP F 2 130 ? -64.238  18.055   -5.000  1.00 105.35 ? 133 ASP F C   1 
ATOM   8303  O O   . ASP F 2 130 ? -65.151  17.328   -4.596  1.00 104.84 ? 133 ASP F O   1 
ATOM   8304  C CB  . ASP F 2 130 ? -64.089  20.074   -3.481  1.00 108.08 ? 133 ASP F CB  1 
ATOM   8305  C CG  . ASP F 2 130 ? -63.281  20.922   -2.506  1.00 121.95 ? 133 ASP F CG  1 
ATOM   8306  O OD1 . ASP F 2 130 ? -62.940  20.414   -1.410  1.00 122.31 ? 133 ASP F OD1 1 
ATOM   8307  O OD2 . ASP F 2 130 ? -63.005  22.098   -2.831  1.00 132.76 ? 133 ASP F OD2 1 
ATOM   8308  N N   . LYS F 2 131 A -63.964  18.224   -6.314  1.00 100.94 ? 133 LYS F N   1 
ATOM   8309  C CA  . LYS F 2 131 A -64.750  17.548   -7.360  1.00 99.94  ? 133 LYS F CA  1 
ATOM   8310  C C   . LYS F 2 131 A -64.221  16.140   -7.721  1.00 101.57 ? 133 LYS F C   1 
ATOM   8311  O O   . LYS F 2 131 A -64.854  15.429   -8.504  1.00 100.71 ? 133 LYS F O   1 
ATOM   8312  C CB  . LYS F 2 131 A -64.931  18.426   -8.622  1.00 102.81 ? 133 LYS F CB  1 
ATOM   8313  C CG  . LYS F 2 131 A -66.403  18.752   -8.951  1.00 100.97 ? 133 LYS F CG  1 
ATOM   8314  C CD  . LYS F 2 131 A -67.201  17.569   -9.549  1.00 97.21  ? 133 LYS F CD  1 
ATOM   8315  C CE  . LYS F 2 131 A -68.688  17.657   -9.270  1.00 84.74  ? 133 LYS F CE  1 
ATOM   8316  N NZ  . LYS F 2 131 A -69.338  16.317   -9.264  1.00 75.60  ? 133 LYS F NZ  1 
ATOM   8317  N N   . GLY F 2 132 ? -63.123  15.726   -7.094  1.00 97.26  ? 134 GLY F N   1 
ATOM   8318  C CA  . GLY F 2 132 ? -62.526  14.414   -7.319  1.00 96.27  ? 134 GLY F CA  1 
ATOM   8319  C C   . GLY F 2 132 ? -63.252  13.240   -6.681  1.00 100.24 ? 134 GLY F C   1 
ATOM   8320  O O   . GLY F 2 132 ? -62.618  12.411   -6.015  1.00 99.83  ? 134 GLY F O   1 
ATOM   8321  N N   . VAL F 2 133 ? -64.583  13.146   -6.899  1.00 97.04  ? 135 VAL F N   1 
ATOM   8322  C CA  . VAL F 2 133 ? -65.445  12.072   -6.382  1.00 97.15  ? 135 VAL F CA  1 
ATOM   8323  C C   . VAL F 2 133 ? -66.266  11.426   -7.492  1.00 101.97 ? 135 VAL F C   1 
ATOM   8324  O O   . VAL F 2 133 ? -66.692  12.106   -8.428  1.00 102.60 ? 135 VAL F O   1 
ATOM   8325  C CB  . VAL F 2 133 ? -66.330  12.469   -5.172  1.00 102.19 ? 135 VAL F CB  1 
ATOM   8326  C CG1 . VAL F 2 133 ? -65.517  12.489   -3.886  1.00 101.80 ? 135 VAL F CG1 1 
ATOM   8327  C CG2 . VAL F 2 133 ? -67.049  13.797   -5.394  1.00 103.32 ? 135 VAL F CG2 1 
ATOM   8328  N N   . THR F 2 134 ? -66.502  10.114   -7.373  1.00 98.48  ? 136 THR F N   1 
ATOM   8329  C CA  . THR F 2 134 ? -67.232  9.346    -8.373  1.00 99.66  ? 136 THR F CA  1 
ATOM   8330  C C   . THR F 2 134 ? -68.255  8.378    -7.755  1.00 103.85 ? 136 THR F C   1 
ATOM   8331  O O   . THR F 2 134 ? -68.164  8.050    -6.574  1.00 102.43 ? 136 THR F O   1 
ATOM   8332  C CB  . THR F 2 134 ? -66.219  8.658    -9.293  1.00 110.91 ? 136 THR F CB  1 
ATOM   8333  O OG1 . THR F 2 134 ? -66.850  8.314    -10.525 1.00 116.48 ? 136 THR F OG1 1 
ATOM   8334  C CG2 . THR F 2 134 ? -65.533  7.449    -8.643  1.00 108.03 ? 136 THR F CG2 1 
ATOM   8335  N N   . ALA F 2 135 ? -69.223  7.926    -8.566  1.00 102.59 ? 137 ALA F N   1 
ATOM   8336  C CA  . ALA F 2 135 ? -70.266  6.984    -8.163  1.00 103.96 ? 137 ALA F CA  1 
ATOM   8337  C C   . ALA F 2 135 ? -69.735  5.558    -8.036  1.00 108.22 ? 137 ALA F C   1 
ATOM   8338  O O   . ALA F 2 135 ? -70.342  4.747    -7.340  1.00 109.21 ? 137 ALA F O   1 
ATOM   8339  C CB  . ALA F 2 135 ? -71.417  7.027    -9.149  1.00 107.44 ? 137 ALA F CB  1 
ATOM   8340  N N   . ALA F 2 136 ? -68.599  5.250    -8.691  1.00 103.85 ? 138 ALA F N   1 
ATOM   8341  C CA  . ALA F 2 136 ? -67.952  3.937    -8.629  1.00 103.85 ? 138 ALA F CA  1 
ATOM   8342  C C   . ALA F 2 136 ? -67.428  3.660    -7.215  1.00 108.20 ? 138 ALA F C   1 
ATOM   8343  O O   . ALA F 2 136 ? -67.214  2.501    -6.852  1.00 108.41 ? 138 ALA F O   1 
ATOM   8344  C CB  . ALA F 2 136 ? -66.812  3.877    -9.622  1.00 104.20 ? 138 ALA F CB  1 
ATOM   8345  N N   . CYS F 2 137 ? -67.229  4.731    -6.420  1.00 105.31 ? 139 CYS F N   1 
ATOM   8346  C CA  . CYS F 2 137 ? -66.786  4.672    -5.026  1.00 105.28 ? 139 CYS F CA  1 
ATOM   8347  C C   . CYS F 2 137 ? -67.877  5.248    -4.117  1.00 111.65 ? 139 CYS F C   1 
ATOM   8348  O O   . CYS F 2 137 ? -67.768  6.391    -3.682  1.00 111.51 ? 139 CYS F O   1 
ATOM   8349  C CB  . CYS F 2 137 ? -65.455  5.394    -4.839  1.00 103.98 ? 139 CYS F CB  1 
ATOM   8350  S SG  . CYS F 2 137 ? -64.094  4.673    -5.780  1.00 107.24 ? 139 CYS F SG  1 
ATOM   8351  N N   . PRO F 2 138 ? -68.964  4.512    -3.831  1.00 110.13 ? 140 PRO F N   1 
ATOM   8352  C CA  . PRO F 2 138 ? -70.004  5.097    -2.982  1.00 111.27 ? 140 PRO F CA  1 
ATOM   8353  C C   . PRO F 2 138 ? -69.765  4.908    -1.491  1.00 114.54 ? 140 PRO F C   1 
ATOM   8354  O O   . PRO F 2 138 ? -68.951  4.081    -1.074  1.00 111.62 ? 140 PRO F O   1 
ATOM   8355  C CB  . PRO F 2 138 ? -71.287  4.406    -3.459  1.00 115.70 ? 140 PRO F CB  1 
ATOM   8356  C CG  . PRO F 2 138 ? -70.831  3.161    -4.191  1.00 120.56 ? 140 PRO F CG  1 
ATOM   8357  C CD  . PRO F 2 138 ? -69.328  3.148    -4.255  1.00 113.47 ? 140 PRO F CD  1 
ATOM   8358  N N   . HIS F 2 139 ? -70.489  5.708    -0.690  1.00 114.38 ? 141 HIS F N   1 
ATOM   8359  C CA  . HIS F 2 139 ? -70.495  5.715    0.771   1.00 116.70 ? 141 HIS F CA  1 
ATOM   8360  C C   . HIS F 2 139 ? -71.758  6.430    1.220   1.00 123.08 ? 141 HIS F C   1 
ATOM   8361  O O   . HIS F 2 139 ? -71.876  7.644    1.035   1.00 121.93 ? 141 HIS F O   1 
ATOM   8362  C CB  . HIS F 2 139 ? -69.217  6.360    1.332   1.00 116.34 ? 141 HIS F CB  1 
ATOM   8363  C CG  . HIS F 2 139 ? -69.294  6.810    2.758   1.00 122.63 ? 141 HIS F CG  1 
ATOM   8364  N ND1 . HIS F 2 139 ? -69.801  5.997    3.770   1.00 127.61 ? 141 HIS F ND1 1 
ATOM   8365  C CD2 . HIS F 2 139 ? -68.876  7.972    3.302   1.00 125.23 ? 141 HIS F CD2 1 
ATOM   8366  C CE1 . HIS F 2 139 ? -69.709  6.711    4.879   1.00 129.76 ? 141 HIS F CE1 1 
ATOM   8367  N NE2 . HIS F 2 139 ? -69.147  7.898    4.650   1.00 128.75 ? 141 HIS F NE2 1 
ATOM   8368  N N   . ALA F 2 140 ? -72.721  5.652    1.751   1.00 123.25 ? 142 ALA F N   1 
ATOM   8369  C CA  . ALA F 2 140 ? -74.039  6.097    2.215   1.00 127.05 ? 142 ALA F CA  1 
ATOM   8370  C C   . ALA F 2 140 ? -74.866  6.750    1.089   1.00 131.15 ? 142 ALA F C   1 
ATOM   8371  O O   . ALA F 2 140 ? -75.620  7.703    1.327   1.00 132.90 ? 142 ALA F O   1 
ATOM   8372  C CB  . ALA F 2 140 ? -73.898  7.026    3.420   1.00 129.81 ? 142 ALA F CB  1 
ATOM   8373  N N   . GLY F 2 141 ? -74.714  6.213    -0.123  1.00 125.35 ? 143 GLY F N   1 
ATOM   8374  C CA  . GLY F 2 141 ? -75.395  6.691    -1.324  1.00 124.33 ? 143 GLY F CA  1 
ATOM   8375  C C   . GLY F 2 141 ? -74.635  7.768    -2.077  1.00 123.08 ? 143 GLY F C   1 
ATOM   8376  O O   . GLY F 2 141 ? -74.733  7.860    -3.305  1.00 121.52 ? 143 GLY F O   1 
ATOM   8377  N N   . ALA F 2 142 ? -73.865  8.586    -1.336  1.00 116.98 ? 144 ALA F N   1 
ATOM   8378  C CA  . ALA F 2 142 ? -73.058  9.704    -1.832  1.00 113.37 ? 144 ALA F CA  1 
ATOM   8379  C C   . ALA F 2 142 ? -71.903  9.266    -2.692  1.00 110.58 ? 144 ALA F C   1 
ATOM   8380  O O   . ALA F 2 142 ? -71.309  8.219    -2.441  1.00 108.46 ? 144 ALA F O   1 
ATOM   8381  C CB  . ALA F 2 142 ? -72.526  10.524   -0.660  1.00 114.58 ? 144 ALA F CB  1 
ATOM   8382  N N   . LYS F 2 143 ? -71.565  10.092   -3.693  1.00 105.23 ? 145 LYS F N   1 
ATOM   8383  C CA  . LYS F 2 143 ? -70.413  9.854    -4.556  1.00 103.17 ? 145 LYS F CA  1 
ATOM   8384  C C   . LYS F 2 143 ? -69.195  10.143   -3.665  1.00 105.84 ? 145 LYS F C   1 
ATOM   8385  O O   . LYS F 2 143 ? -69.010  11.283   -3.230  1.00 106.83 ? 145 LYS F O   1 
ATOM   8386  C CB  . LYS F 2 143 ? -70.424  10.795   -5.781  1.00 105.23 ? 145 LYS F CB  1 
ATOM   8387  C CG  . LYS F 2 143 ? -71.216  10.302   -6.984  1.00 111.98 ? 145 LYS F CG  1 
ATOM   8388  C CD  . LYS F 2 143 ? -71.240  11.356   -8.091  1.00 120.41 ? 145 LYS F CD  1 
ATOM   8389  C CE  . LYS F 2 143 ? -71.812  10.826   -9.375  1.00 131.23 ? 145 LYS F CE  1 
ATOM   8390  N NZ  . LYS F 2 143 ? -70.770  10.288   -10.287 1.00 138.52 ? 145 LYS F NZ  1 
ATOM   8391  N N   . SER F 2 144 ? -68.436  9.099    -3.313  1.00 99.71  ? 146 SER F N   1 
ATOM   8392  C CA  . SER F 2 144 ? -67.272  9.249    -2.448  1.00 97.88  ? 146 SER F CA  1 
ATOM   8393  C C   . SER F 2 144 ? -65.983  8.930    -3.220  1.00 99.81  ? 146 SER F C   1 
ATOM   8394  O O   . SER F 2 144 ? -65.978  8.968    -4.454  1.00 99.33  ? 146 SER F O   1 
ATOM   8395  C CB  . SER F 2 144 ? -67.426  8.370    -1.209  1.00 101.66 ? 146 SER F CB  1 
ATOM   8396  O OG  . SER F 2 144 ? -66.485  8.701    -0.204  1.00 110.46 ? 146 SER F OG  1 
ATOM   8397  N N   . PHE F 2 145 ? -64.893  8.644    -2.493  1.00 94.88  ? 147 PHE F N   1 
ATOM   8398  C CA  . PHE F 2 145 ? -63.573  8.332    -3.024  1.00 92.42  ? 147 PHE F CA  1 
ATOM   8399  C C   . PHE F 2 145 ? -62.709  7.749    -1.887  1.00 96.25  ? 147 PHE F C   1 
ATOM   8400  O O   . PHE F 2 145 ? -63.191  7.625    -0.756  1.00 97.20  ? 147 PHE F O   1 
ATOM   8401  C CB  . PHE F 2 145 ? -62.938  9.610    -3.625  1.00 93.43  ? 147 PHE F CB  1 
ATOM   8402  C CG  . PHE F 2 145 ? -61.804  9.348    -4.585  1.00 93.64  ? 147 PHE F CG  1 
ATOM   8403  C CD1 . PHE F 2 145 ? -62.018  8.643    -5.762  1.00 96.13  ? 147 PHE F CD1 1 
ATOM   8404  C CD2 . PHE F 2 145 ? -60.520  9.803    -4.311  1.00 94.82  ? 147 PHE F CD2 1 
ATOM   8405  C CE1 . PHE F 2 145 ? -60.965  8.373    -6.630  1.00 96.39  ? 147 PHE F CE1 1 
ATOM   8406  C CE2 . PHE F 2 145 ? -59.469  9.534    -5.182  1.00 96.71  ? 147 PHE F CE2 1 
ATOM   8407  C CZ  . PHE F 2 145 ? -59.697  8.818    -6.333  1.00 94.88  ? 147 PHE F CZ  1 
ATOM   8408  N N   . TYR F 2 146 ? -61.455  7.360    -2.190  1.00 91.46  ? 148 TYR F N   1 
ATOM   8409  C CA  . TYR F 2 146 ? -60.511  6.820    -1.208  1.00 90.70  ? 148 TYR F CA  1 
ATOM   8410  C C   . TYR F 2 146 ? -60.047  7.943    -0.277  1.00 92.83  ? 148 TYR F C   1 
ATOM   8411  O O   . TYR F 2 146 ? -59.616  8.997    -0.748  1.00 91.02  ? 148 TYR F O   1 
ATOM   8412  C CB  . TYR F 2 146 ? -59.298  6.187    -1.893  1.00 90.79  ? 148 TYR F CB  1 
ATOM   8413  C CG  . TYR F 2 146 ? -59.608  5.162    -2.962  1.00 92.13  ? 148 TYR F CG  1 
ATOM   8414  C CD1 . TYR F 2 146 ? -59.807  3.825    -2.635  1.00 94.74  ? 148 TYR F CD1 1 
ATOM   8415  C CD2 . TYR F 2 146 ? -59.597  5.509    -4.311  1.00 92.45  ? 148 TYR F CD2 1 
ATOM   8416  C CE1 . TYR F 2 146 ? -60.010  2.863    -3.621  1.00 96.11  ? 148 TYR F CE1 1 
ATOM   8417  C CE2 . TYR F 2 146 ? -59.813  4.558    -5.305  1.00 93.71  ? 148 TYR F CE2 1 
ATOM   8418  C CZ  . TYR F 2 146 ? -60.009  3.235    -4.955  1.00 103.58 ? 148 TYR F CZ  1 
ATOM   8419  O OH  . TYR F 2 146 ? -60.240  2.309    -5.934  1.00 108.88 ? 148 TYR F OH  1 
ATOM   8420  N N   . LYS F 2 147 ? -60.152  7.723    1.038   1.00 90.46  ? 149 LYS F N   1 
ATOM   8421  C CA  . LYS F 2 147 ? -59.803  8.723    2.045   1.00 92.02  ? 149 LYS F CA  1 
ATOM   8422  C C   . LYS F 2 147 ? -58.344  9.133    2.048   1.00 92.15  ? 149 LYS F C   1 
ATOM   8423  O O   . LYS F 2 147 ? -58.051  10.302   2.280   1.00 92.79  ? 149 LYS F O   1 
ATOM   8424  C CB  . LYS F 2 147 ? -60.223  8.256    3.449   1.00 98.94  ? 149 LYS F CB  1 
ATOM   8425  C CG  . LYS F 2 147 ? -60.924  9.335    4.274   1.00 128.49 ? 149 LYS F CG  1 
ATOM   8426  C CD  . LYS F 2 147 ? -59.979  10.097   5.208   1.00 145.75 ? 149 LYS F CD  1 
ATOM   8427  C CE  . LYS F 2 147 ? -60.699  11.233   5.900   1.00 165.06 ? 149 LYS F CE  1 
ATOM   8428  N NZ  . LYS F 2 147 ? -59.840  11.922   6.898   1.00 177.82 ? 149 LYS F NZ  1 
ATOM   8429  N N   . ASN F 2 148 ? -57.442  8.189    1.774   1.00 85.41  ? 150 ASN F N   1 
ATOM   8430  C CA  . ASN F 2 148 ? -56.003  8.433    1.823   1.00 84.78  ? 150 ASN F CA  1 
ATOM   8431  C C   . ASN F 2 148 ? -55.396  9.133    0.577   1.00 88.00  ? 150 ASN F C   1 
ATOM   8432  O O   . ASN F 2 148 ? -54.235  9.547    0.655   1.00 88.48  ? 150 ASN F O   1 
ATOM   8433  C CB  . ASN F 2 148 ? -55.257  7.138    2.139   1.00 80.16  ? 150 ASN F CB  1 
ATOM   8434  C CG  . ASN F 2 148 ? -55.767  6.438    3.373   1.00 93.22  ? 150 ASN F CG  1 
ATOM   8435  O OD1 . ASN F 2 148 ? -56.268  7.056    4.324   1.00 93.64  ? 150 ASN F OD1 1 
ATOM   8436  N ND2 . ASN F 2 148 ? -55.670  5.125    3.374   1.00 78.08  ? 150 ASN F ND2 1 
ATOM   8437  N N   . LEU F 2 149 ? -56.152  9.292    -0.542  1.00 82.37  ? 151 LEU F N   1 
ATOM   8438  C CA  . LEU F 2 149 ? -55.629  9.992    -1.728  1.00 80.97  ? 151 LEU F CA  1 
ATOM   8439  C C   . LEU F 2 149 ? -56.685  10.869   -2.431  1.00 87.49  ? 151 LEU F C   1 
ATOM   8440  O O   . LEU F 2 149 ? -57.840  10.471   -2.550  1.00 87.78  ? 151 LEU F O   1 
ATOM   8441  C CB  . LEU F 2 149 ? -54.904  9.070    -2.730  1.00 78.97  ? 151 LEU F CB  1 
ATOM   8442  C CG  . LEU F 2 149 ? -55.392  7.644    -2.932  1.00 81.78  ? 151 LEU F CG  1 
ATOM   8443  C CD1 . LEU F 2 149 ? -56.540  7.594    -3.904  1.00 80.93  ? 151 LEU F CD1 1 
ATOM   8444  C CD2 . LEU F 2 149 ? -54.274  6.773    -3.471  1.00 84.84  ? 151 LEU F CD2 1 
ATOM   8445  N N   . ILE F 2 150 ? -56.276  12.076   -2.867  1.00 85.64  ? 152 ILE F N   1 
ATOM   8446  C CA  . ILE F 2 150 ? -57.121  13.082   -3.527  1.00 86.63  ? 152 ILE F CA  1 
ATOM   8447  C C   . ILE F 2 150 ? -57.044  12.973   -5.061  1.00 91.99  ? 152 ILE F C   1 
ATOM   8448  O O   . ILE F 2 150 ? -55.946  12.957   -5.628  1.00 91.50  ? 152 ILE F O   1 
ATOM   8449  C CB  . ILE F 2 150 ? -56.721  14.521   -3.068  1.00 91.96  ? 152 ILE F CB  1 
ATOM   8450  C CG1 . ILE F 2 150 ? -56.653  14.672   -1.536  1.00 94.33  ? 152 ILE F CG1 1 
ATOM   8451  C CG2 . ILE F 2 150 ? -57.619  15.590   -3.685  1.00 93.47  ? 152 ILE F CG2 1 
ATOM   8452  C CD1 . ILE F 2 150 ? -55.468  15.555   -1.055  1.00 104.50 ? 152 ILE F CD1 1 
ATOM   8453  N N   . TRP F 2 151 ? -58.216  12.963   -5.729  1.00 90.32  ? 153 TRP F N   1 
ATOM   8454  C CA  . TRP F 2 151 ? -58.303  12.954   -7.191  1.00 91.60  ? 153 TRP F CA  1 
ATOM   8455  C C   . TRP F 2 151 ? -58.228  14.419   -7.639  1.00 98.37  ? 153 TRP F C   1 
ATOM   8456  O O   . TRP F 2 151 ? -59.215  15.157   -7.524  1.00 98.91  ? 153 TRP F O   1 
ATOM   8457  C CB  . TRP F 2 151 ? -59.622  12.295   -7.647  1.00 90.51  ? 153 TRP F CB  1 
ATOM   8458  C CG  . TRP F 2 151 ? -59.798  12.086   -9.131  1.00 92.48  ? 153 TRP F CG  1 
ATOM   8459  C CD1 . TRP F 2 151 ? -58.966  12.490   -10.136 1.00 96.60  ? 153 TRP F CD1 1 
ATOM   8460  C CD2 . TRP F 2 151 ? -60.886  11.406   -9.763  1.00 93.23  ? 153 TRP F CD2 1 
ATOM   8461  N NE1 . TRP F 2 151 ? -59.469  12.101   -11.352 1.00 97.28  ? 153 TRP F NE1 1 
ATOM   8462  C CE2 . TRP F 2 151 ? -60.642  11.423   -11.154 1.00 98.48  ? 153 TRP F CE2 1 
ATOM   8463  C CE3 . TRP F 2 151 ? -62.042  10.765   -9.287  1.00 94.45  ? 153 TRP F CE3 1 
ATOM   8464  C CZ2 . TRP F 2 151 ? -61.513  10.831   -12.074 1.00 99.69  ? 153 TRP F CZ2 1 
ATOM   8465  C CZ3 . TRP F 2 151 ? -62.912  10.189   -10.200 1.00 97.53  ? 153 TRP F CZ3 1 
ATOM   8466  C CH2 . TRP F 2 151 ? -62.644  10.220   -11.575 1.00 100.01 ? 153 TRP F CH2 1 
ATOM   8467  N N   . LEU F 2 152 ? -57.038  14.850   -8.099  1.00 96.24  ? 154 LEU F N   1 
ATOM   8468  C CA  . LEU F 2 152 ? -56.827  16.236   -8.521  1.00 97.65  ? 154 LEU F CA  1 
ATOM   8469  C C   . LEU F 2 152 ? -57.247  16.527   -9.956  1.00 102.89 ? 154 LEU F C   1 
ATOM   8470  O O   . LEU F 2 152 ? -56.716  15.935   -10.904 1.00 103.42 ? 154 LEU F O   1 
ATOM   8471  C CB  . LEU F 2 152 ? -55.386  16.704   -8.280  1.00 98.26  ? 154 LEU F CB  1 
ATOM   8472  C CG  . LEU F 2 152 ? -55.062  17.262   -6.902  1.00 102.51 ? 154 LEU F CG  1 
ATOM   8473  C CD1 . LEU F 2 152 ? -53.784  18.010   -6.950  1.00 104.78 ? 154 LEU F CD1 1 
ATOM   8474  C CD2 . LEU F 2 152 ? -56.124  18.218   -6.404  1.00 105.18 ? 154 LEU F CD2 1 
ATOM   8475  N N   . VAL F 2 153 ? -58.184  17.482   -10.095 1.00 99.01  ? 155 VAL F N   1 
ATOM   8476  C CA  . VAL F 2 153 ? -58.732  17.962   -11.364 1.00 100.02 ? 155 VAL F CA  1 
ATOM   8477  C C   . VAL F 2 153 ? -58.483  19.486   -11.543 1.00 105.78 ? 155 VAL F C   1 
ATOM   8478  O O   . VAL F 2 153 ? -58.148  20.165   -10.568 1.00 104.64 ? 155 VAL F O   1 
ATOM   8479  C CB  . VAL F 2 153 ? -60.212  17.543   -11.555 1.00 102.86 ? 155 VAL F CB  1 
ATOM   8480  C CG1 . VAL F 2 153 ? -60.314  16.062   -11.887 1.00 101.42 ? 155 VAL F CG1 1 
ATOM   8481  C CG2 . VAL F 2 153 ? -61.055  17.869   -10.326 1.00 101.53 ? 155 VAL F CG2 1 
ATOM   8482  N N   . LYS F 2 154 ? -58.604  20.003   -12.788 1.00 105.69 ? 156 LYS F N   1 
ATOM   8483  C CA  . LYS F 2 154 ? -58.337  21.406   -13.143 1.00 109.06 ? 156 LYS F CA  1 
ATOM   8484  C C   . LYS F 2 154 ? -59.216  22.431   -12.408 1.00 115.03 ? 156 LYS F C   1 
ATOM   8485  O O   . LYS F 2 154 ? -60.427  22.246   -12.290 1.00 113.79 ? 156 LYS F O   1 
ATOM   8486  C CB  . LYS F 2 154 ? -58.393  21.633   -14.670 1.00 114.83 ? 156 LYS F CB  1 
ATOM   8487  C CG  . LYS F 2 154 ? -59.756  21.412   -15.324 1.00 125.94 ? 156 LYS F CG  1 
ATOM   8488  C CD  . LYS F 2 154 ? -59.720  21.700   -16.807 1.00 137.64 ? 156 LYS F CD  1 
ATOM   8489  C CE  . LYS F 2 154 ? -61.107  21.824   -17.370 1.00 146.75 ? 156 LYS F CE  1 
ATOM   8490  N NZ  . LYS F 2 154 ? -61.090  21.949   -18.849 1.00 160.31 ? 156 LYS F NZ  1 
ATOM   8491  N N   . LYS F 2 155 ? -58.586  23.518   -11.927 1.00 115.30 ? 157 LYS F N   1 
ATOM   8492  C CA  . LYS F 2 155 ? -59.254  24.607   -11.211 1.00 117.17 ? 157 LYS F CA  1 
ATOM   8493  C C   . LYS F 2 155 ? -59.787  25.624   -12.229 1.00 126.21 ? 157 LYS F C   1 
ATOM   8494  O O   . LYS F 2 155 ? -59.116  26.617   -12.525 1.00 129.34 ? 157 LYS F O   1 
ATOM   8495  C CB  . LYS F 2 155 ? -58.278  25.259   -10.206 1.00 121.16 ? 157 LYS F CB  1 
ATOM   8496  C CG  . LYS F 2 155 ? -58.939  26.122   -9.131  1.00 134.69 ? 157 LYS F CG  1 
ATOM   8497  C CD  . LYS F 2 155 ? -57.888  26.810   -8.256  1.00 145.55 ? 157 LYS F CD  1 
ATOM   8498  C CE  . LYS F 2 155 ? -58.480  27.795   -7.279  1.00 154.52 ? 157 LYS F CE  1 
ATOM   8499  N NZ  . LYS F 2 155 ? -57.431  28.529   -6.525  1.00 163.91 ? 157 LYS F NZ  1 
ATOM   8500  N N   . GLY F 2 156 ? -60.968  25.332   -12.778 1.00 123.31 ? 158 GLY F N   1 
ATOM   8501  C CA  . GLY F 2 156 ? -61.649  26.156   -13.775 1.00 126.50 ? 158 GLY F CA  1 
ATOM   8502  C C   . GLY F 2 156 ? -60.827  26.447   -15.016 1.00 135.11 ? 158 GLY F C   1 
ATOM   8503  O O   . GLY F 2 156 ? -60.297  27.553   -15.153 1.00 138.61 ? 158 GLY F O   1 
ATOM   8504  N N   . ASN F 2 157 ? -60.714  25.447   -15.922 1.00 131.23 ? 159 ASN F N   1 
ATOM   8505  C CA  . ASN F 2 157 ? -59.973  25.448   -17.201 1.00 134.12 ? 159 ASN F CA  1 
ATOM   8506  C C   . ASN F 2 157 ? -58.515  25.997   -17.081 1.00 139.44 ? 159 ASN F C   1 
ATOM   8507  O O   . ASN F 2 157 ? -58.079  26.814   -17.902 1.00 143.05 ? 159 ASN F O   1 
ATOM   8508  C CB  . ASN F 2 157 ? -60.763  26.126   -18.354 1.00 136.12 ? 159 ASN F CB  1 
ATOM   8509  C CG  . ASN F 2 157 ? -61.206  27.556   -18.142 1.00 154.34 ? 159 ASN F CG  1 
ATOM   8510  O OD1 . ASN F 2 157 ? -62.385  27.836   -17.899 1.00 150.19 ? 159 ASN F OD1 1 
ATOM   8511  N ND2 . ASN F 2 157 ? -60.286  28.501   -18.281 1.00 144.06 ? 159 ASN F ND2 1 
ATOM   8512  N N   . SER F 2 158 ? -57.761  25.500   -16.066 1.00 132.59 ? 160 SER F N   1 
ATOM   8513  C CA  . SER F 2 158 ? -56.361  25.857   -15.791 1.00 133.25 ? 160 SER F CA  1 
ATOM   8514  C C   . SER F 2 158 ? -55.706  24.875   -14.808 1.00 132.49 ? 160 SER F C   1 
ATOM   8515  O O   . SER F 2 158 ? -55.867  25.004   -13.590 1.00 129.53 ? 160 SER F O   1 
ATOM   8516  C CB  . SER F 2 158 ? -56.240  27.296   -15.286 1.00 139.12 ? 160 SER F CB  1 
ATOM   8517  O OG  . SER F 2 158 ? -54.888  27.714   -15.200 1.00 149.90 ? 160 SER F OG  1 
ATOM   8518  N N   . TYR F 2 159 ? -54.977  23.886   -15.354 1.00 109.21 ? 161 TYR F N   1 
ATOM   8519  C CA  . TYR F 2 159 ? -54.232  22.867   -14.604 1.00 107.36 ? 161 TYR F CA  1 
ATOM   8520  C C   . TYR F 2 159 ? -52.716  23.136   -14.781 1.00 111.61 ? 161 TYR F C   1 
ATOM   8521  O O   . TYR F 2 159 ? -52.103  22.594   -15.710 1.00 111.64 ? 161 TYR F O   1 
ATOM   8522  C CB  . TYR F 2 159 ? -54.577  21.449   -15.107 1.00 108.10 ? 161 TYR F CB  1 
ATOM   8523  C CG  . TYR F 2 159 ? -54.155  20.301   -14.208 1.00 108.53 ? 161 TYR F CG  1 
ATOM   8524  C CD1 . TYR F 2 159 ? -55.096  19.436   -13.667 1.00 109.33 ? 161 TYR F CD1 1 
ATOM   8525  C CD2 . TYR F 2 159 ? -52.809  20.024   -13.973 1.00 109.41 ? 161 TYR F CD2 1 
ATOM   8526  C CE1 . TYR F 2 159 ? -54.719  18.368   -12.856 1.00 108.74 ? 161 TYR F CE1 1 
ATOM   8527  C CE2 . TYR F 2 159 ? -52.419  18.961   -13.155 1.00 108.71 ? 161 TYR F CE2 1 
ATOM   8528  C CZ  . TYR F 2 159 ? -53.379  18.125   -12.612 1.00 113.50 ? 161 TYR F CZ  1 
ATOM   8529  O OH  . TYR F 2 159 ? -53.017  17.046   -11.843 1.00 112.08 ? 161 TYR F OH  1 
ATOM   8530  N N   . PRO F 2 160 ? -52.083  23.951   -13.909 1.00 108.14 ? 162 PRO F N   1 
ATOM   8531  C CA  . PRO F 2 160 ? -50.637  24.191   -14.061 1.00 109.03 ? 162 PRO F CA  1 
ATOM   8532  C C   . PRO F 2 160 ? -49.807  23.033   -13.510 1.00 111.36 ? 162 PRO F C   1 
ATOM   8533  O O   . PRO F 2 160 ? -50.324  22.229   -12.729 1.00 108.84 ? 162 PRO F O   1 
ATOM   8534  C CB  . PRO F 2 160 ? -50.401  25.490   -13.274 1.00 111.61 ? 162 PRO F CB  1 
ATOM   8535  C CG  . PRO F 2 160 ? -51.765  25.902   -12.711 1.00 115.24 ? 162 PRO F CG  1 
ATOM   8536  C CD  . PRO F 2 160 ? -52.626  24.689   -12.752 1.00 109.00 ? 162 PRO F CD  1 
ATOM   8537  N N   . LYS F 2 161 ? -48.524  22.944   -13.919 1.00 109.49 ? 163 LYS F N   1 
ATOM   8538  C CA  . LYS F 2 161 ? -47.611  21.892   -13.471 1.00 109.09 ? 163 LYS F CA  1 
ATOM   8539  C C   . LYS F 2 161 ? -47.418  21.949   -11.951 1.00 114.94 ? 163 LYS F C   1 
ATOM   8540  O O   . LYS F 2 161 ? -46.806  22.900   -11.450 1.00 116.09 ? 163 LYS F O   1 
ATOM   8541  C CB  . LYS F 2 161 ? -46.257  21.990   -14.198 1.00 112.65 ? 163 LYS F CB  1 
ATOM   8542  C CG  . LYS F 2 161 ? -45.291  20.835   -13.899 1.00 122.77 ? 163 LYS F CG  1 
ATOM   8543  C CD  . LYS F 2 161 ? -43.836  21.193   -14.217 1.00 129.77 ? 163 LYS F CD  1 
ATOM   8544  C CE  . LYS F 2 161 ? -43.073  21.668   -13.002 1.00 133.48 ? 163 LYS F CE  1 
ATOM   8545  N NZ  . LYS F 2 161 ? -41.761  22.266   -13.370 1.00 135.50 ? 163 LYS F NZ  1 
ATOM   8546  N N   . LEU F 2 162 ? -47.977  20.948   -11.224 1.00 110.77 ? 164 LEU F N   1 
ATOM   8547  C CA  . LEU F 2 162 ? -47.847  20.828   -9.763  1.00 109.87 ? 164 LEU F CA  1 
ATOM   8548  C C   . LEU F 2 162 ? -46.555  20.102   -9.420  1.00 113.66 ? 164 LEU F C   1 
ATOM   8549  O O   . LEU F 2 162 ? -46.136  19.217   -10.176 1.00 113.24 ? 164 LEU F O   1 
ATOM   8550  C CB  . LEU F 2 162 ? -49.061  20.126   -9.109  1.00 108.05 ? 164 LEU F CB  1 
ATOM   8551  C CG  . LEU F 2 162 ? -49.400  18.687   -9.527  1.00 111.42 ? 164 LEU F CG  1 
ATOM   8552  C CD1 . LEU F 2 162 ? -49.073  17.698   -8.424  1.00 109.92 ? 164 LEU F CD1 1 
ATOM   8553  C CD2 . LEU F 2 162 ? -50.852  18.564   -9.856  1.00 113.15 ? 164 LEU F CD2 1 
ATOM   8554  N N   . SER F 2 163 ? -45.918  20.475   -8.296  1.00 110.59 ? 165 SER F N   1 
ATOM   8555  C CA  . SER F 2 163 ? -44.667  19.837   -7.886  1.00 111.64 ? 165 SER F CA  1 
ATOM   8556  C C   . SER F 2 163 ? -44.470  19.835   -6.366  1.00 113.84 ? 165 SER F C   1 
ATOM   8557  O O   . SER F 2 163 ? -43.564  20.497   -5.845  1.00 115.18 ? 165 SER F O   1 
ATOM   8558  C CB  . SER F 2 163 ? -43.471  20.444   -8.623  1.00 119.54 ? 165 SER F CB  1 
ATOM   8559  O OG  . SER F 2 163 ? -42.376  19.543   -8.689  1.00 133.43 ? 165 SER F OG  1 
ATOM   8560  N N   . LYS F 2 164 ? -45.309  19.063   -5.657  1.00 107.74 ? 166 LYS F N   1 
ATOM   8561  C CA  . LYS F 2 164 ? -45.197  18.938   -4.208  1.00 107.58 ? 166 LYS F CA  1 
ATOM   8562  C C   . LYS F 2 164 ? -44.149  17.912   -3.859  1.00 112.87 ? 166 LYS F C   1 
ATOM   8563  O O   . LYS F 2 164 ? -44.032  16.896   -4.547  1.00 112.27 ? 166 LYS F O   1 
ATOM   8564  C CB  . LYS F 2 164 ? -46.534  18.573   -3.562  1.00 107.89 ? 166 LYS F CB  1 
ATOM   8565  C CG  . LYS F 2 164 ? -47.255  19.767   -2.941  1.00 124.98 ? 166 LYS F CG  1 
ATOM   8566  C CD  . LYS F 2 164 ? -46.896  19.984   -1.471  1.00 137.90 ? 166 LYS F CD  1 
ATOM   8567  C CE  . LYS F 2 164 ? -47.528  21.233   -0.910  1.00 150.08 ? 166 LYS F CE  1 
ATOM   8568  N NZ  . LYS F 2 164 ? -47.719  21.145   0.564   1.00 159.56 ? 166 LYS F NZ  1 
ATOM   8569  N N   . SER F 2 165 ? -43.384  18.177   -2.793  1.00 110.87 ? 167 SER F N   1 
ATOM   8570  C CA  . SER F 2 165 ? -42.321  17.282   -2.356  1.00 111.75 ? 167 SER F CA  1 
ATOM   8571  C C   . SER F 2 165 ? -42.334  17.069   -0.848  1.00 117.01 ? 167 SER F C   1 
ATOM   8572  O O   . SER F 2 165 ? -42.360  18.042   -0.088  1.00 118.98 ? 167 SER F O   1 
ATOM   8573  C CB  . SER F 2 165 ? -40.963  17.815   -2.799  1.00 116.96 ? 167 SER F CB  1 
ATOM   8574  O OG  . SER F 2 165 ? -40.926  18.080   -4.191  1.00 124.40 ? 167 SER F OG  1 
ATOM   8575  N N   . TYR F 2 166 ? -42.312  15.798   -0.412  1.00 111.66 ? 168 TYR F N   1 
ATOM   8576  C CA  . TYR F 2 166 ? -42.282  15.460   1.011   1.00 111.34 ? 168 TYR F CA  1 
ATOM   8577  C C   . TYR F 2 166 ? -40.903  14.967   1.418   1.00 114.91 ? 168 TYR F C   1 
ATOM   8578  O O   . TYR F 2 166 ? -40.336  14.105   0.753   1.00 114.17 ? 168 TYR F O   1 
ATOM   8579  C CB  . TYR F 2 166 ? -43.365  14.426   1.387   1.00 110.50 ? 168 TYR F CB  1 
ATOM   8580  C CG  . TYR F 2 166 ? -43.274  13.954   2.825   1.00 112.96 ? 168 TYR F CG  1 
ATOM   8581  C CD1 . TYR F 2 166 ? -43.731  14.750   3.872   1.00 115.35 ? 168 TYR F CD1 1 
ATOM   8582  C CD2 . TYR F 2 166 ? -42.707  12.723   3.142   1.00 114.04 ? 168 TYR F CD2 1 
ATOM   8583  C CE1 . TYR F 2 166 ? -43.628  14.331   5.197   1.00 116.81 ? 168 TYR F CE1 1 
ATOM   8584  C CE2 . TYR F 2 166 ? -42.610  12.289   4.463   1.00 115.71 ? 168 TYR F CE2 1 
ATOM   8585  C CZ  . TYR F 2 166 ? -43.064  13.100   5.488   1.00 123.13 ? 168 TYR F CZ  1 
ATOM   8586  O OH  . TYR F 2 166 ? -42.962  12.681   6.793   1.00 125.24 ? 168 TYR F OH  1 
ATOM   8587  N N   . ILE F 2 167 ? -40.405  15.473   2.543   1.00 112.02 ? 169 ILE F N   1 
ATOM   8588  C CA  . ILE F 2 167 ? -39.110  15.102   3.097   1.00 114.04 ? 169 ILE F CA  1 
ATOM   8589  C C   . ILE F 2 167 ? -39.397  14.292   4.345   1.00 115.70 ? 169 ILE F C   1 
ATOM   8590  O O   . ILE F 2 167 ? -40.111  14.769   5.225   1.00 114.21 ? 169 ILE F O   1 
ATOM   8591  C CB  . ILE F 2 167 ? -38.242  16.366   3.369   1.00 120.48 ? 169 ILE F CB  1 
ATOM   8592  C CG1 . ILE F 2 167 ? -38.120  17.272   2.105   1.00 120.96 ? 169 ILE F CG1 1 
ATOM   8593  C CG2 . ILE F 2 167 ? -36.853  15.983   3.899   1.00 124.73 ? 169 ILE F CG2 1 
ATOM   8594  C CD1 . ILE F 2 167 ? -39.202  18.417   1.940   1.00 127.66 ? 169 ILE F CD1 1 
ATOM   8595  N N   . ASN F 2 168 ? -38.881  13.056   4.402   1.00 112.83 ? 170 ASN F N   1 
ATOM   8596  C CA  . ASN F 2 168 ? -39.122  12.145   5.521   1.00 113.22 ? 170 ASN F CA  1 
ATOM   8597  C C   . ASN F 2 168 ? -38.446  12.575   6.827   1.00 121.67 ? 170 ASN F C   1 
ATOM   8598  O O   . ASN F 2 168 ? -37.231  12.441   6.984   1.00 124.78 ? 170 ASN F O   1 
ATOM   8599  C CB  . ASN F 2 168 ? -38.761  10.704   5.162   1.00 113.08 ? 170 ASN F CB  1 
ATOM   8600  C CG  . ASN F 2 168 ? -39.356  9.669    6.091   1.00 129.55 ? 170 ASN F CG  1 
ATOM   8601  O OD1 . ASN F 2 168 ? -39.948  9.969    7.138   1.00 117.35 ? 170 ASN F OD1 1 
ATOM   8602  N ND2 . ASN F 2 168 ? -39.215  8.413    5.723   1.00 123.81 ? 170 ASN F ND2 1 
ATOM   8603  N N   . ASP F 2 169 ? -39.261  13.059   7.772   1.00 117.86 ? 171 ASP F N   1 
ATOM   8604  C CA  . ASP F 2 169 ? -38.817  13.508   9.092   1.00 120.85 ? 171 ASP F CA  1 
ATOM   8605  C C   . ASP F 2 169 ? -39.236  12.525   10.199  1.00 124.75 ? 171 ASP F C   1 
ATOM   8606  O O   . ASP F 2 169 ? -38.729  12.616   11.321  1.00 127.55 ? 171 ASP F O   1 
ATOM   8607  C CB  . ASP F 2 169 ? -39.356  14.926   9.383   1.00 123.04 ? 171 ASP F CB  1 
ATOM   8608  C CG  . ASP F 2 169 ? -40.871  15.026   9.429   1.00 134.49 ? 171 ASP F CG  1 
ATOM   8609  O OD1 . ASP F 2 169 ? -41.421  15.218   10.539  1.00 135.30 ? 171 ASP F OD1 1 
ATOM   8610  O OD2 . ASP F 2 169 ? -41.508  14.898   8.360   1.00 141.33 ? 171 ASP F OD2 1 
ATOM   8611  N N   . LYS F 2 170 ? -40.151  11.582   9.868   1.00 117.77 ? 172 LYS F N   1 
ATOM   8612  C CA  . LYS F 2 170 ? -40.734  10.583   10.777  1.00 116.42 ? 172 LYS F CA  1 
ATOM   8613  C C   . LYS F 2 170 ? -39.728  9.571    11.367  1.00 122.77 ? 172 LYS F C   1 
ATOM   8614  O O   . LYS F 2 170 ? -40.008  8.979    12.414  1.00 123.53 ? 172 LYS F O   1 
ATOM   8615  C CB  . LYS F 2 170 ? -41.910  9.840    10.108  1.00 114.45 ? 172 LYS F CB  1 
ATOM   8616  C CG  . LYS F 2 170 ? -43.020  10.747   9.561   1.00 126.65 ? 172 LYS F CG  1 
ATOM   8617  C CD  . LYS F 2 170 ? -43.838  11.468   10.640  1.00 136.18 ? 172 LYS F CD  1 
ATOM   8618  C CE  . LYS F 2 170 ? -44.568  12.662   10.072  1.00 144.50 ? 172 LYS F CE  1 
ATOM   8619  N NZ  . LYS F 2 170 ? -45.322  13.402   11.117  1.00 154.72 ? 172 LYS F NZ  1 
ATOM   8620  N N   . GLY F 2 171 ? -38.590  9.371    10.704  1.00 119.81 ? 173 GLY F N   1 
ATOM   8621  C CA  . GLY F 2 171 ? -37.569  8.431    11.161  1.00 121.66 ? 173 GLY F CA  1 
ATOM   8622  C C   . GLY F 2 171 ? -37.837  6.990    10.769  1.00 121.84 ? 173 GLY F C   1 
ATOM   8623  O O   . GLY F 2 171 ? -36.914  6.171    10.751  1.00 122.99 ? 173 GLY F O   1 
ATOM   8624  N N   . LYS F 2 172 ? -39.112  6.672    10.465  1.00 113.93 ? 174 LYS F N   1 
ATOM   8625  C CA  . LYS F 2 172 ? -39.610  5.359    10.039  1.00 110.90 ? 174 LYS F CA  1 
ATOM   8626  C C   . LYS F 2 172 ? -39.721  5.331    8.512   1.00 110.92 ? 174 LYS F C   1 
ATOM   8627  O O   . LYS F 2 172 ? -39.639  6.385    7.876   1.00 110.61 ? 174 LYS F O   1 
ATOM   8628  C CB  . LYS F 2 172 ? -41.006  5.102    10.649  1.00 110.51 ? 174 LYS F CB  1 
ATOM   8629  C CG  . LYS F 2 172 ? -41.019  4.858    12.162  1.00 124.84 ? 174 LYS F CG  1 
ATOM   8630  C CD  . LYS F 2 172 ? -42.429  4.575    12.695  1.00 130.98 ? 174 LYS F CD  1 
ATOM   8631  C CE  . LYS F 2 172 ? -43.224  5.827    12.997  1.00 138.05 ? 174 LYS F CE  1 
ATOM   8632  N NZ  . LYS F 2 172 ? -44.650  5.522    13.285  1.00 140.98 ? 174 LYS F NZ  1 
ATOM   8633  N N   . GLU F 2 173 ? -39.906  4.132    7.923   1.00 104.34 ? 175 GLU F N   1 
ATOM   8634  C CA  . GLU F 2 173 ? -40.110  3.972    6.482   1.00 101.42 ? 175 GLU F CA  1 
ATOM   8635  C C   . GLU F 2 173 ? -41.520  4.501    6.202   1.00 100.68 ? 175 GLU F C   1 
ATOM   8636  O O   . GLU F 2 173 ? -42.472  4.053    6.842   1.00 99.36  ? 175 GLU F O   1 
ATOM   8637  C CB  . GLU F 2 173 ? -40.005  2.492    6.070   1.00 102.29 ? 175 GLU F CB  1 
ATOM   8638  C CG  . GLU F 2 173 ? -38.789  2.165    5.217   1.00 116.46 ? 175 GLU F CG  1 
ATOM   8639  C CD  . GLU F 2 173 ? -38.622  0.712    4.799   1.00 137.93 ? 175 GLU F CD  1 
ATOM   8640  O OE1 . GLU F 2 173 ? -39.257  -0.173   5.419   1.00 121.52 ? 175 GLU F OE1 1 
ATOM   8641  O OE2 . GLU F 2 173 ? -37.815  0.455    3.875   1.00 139.03 ? 175 GLU F OE2 1 
ATOM   8642  N N   . VAL F 2 174 ? -41.645  5.500    5.317   1.00 94.69  ? 176 VAL F N   1 
ATOM   8643  C CA  . VAL F 2 174 ? -42.931  6.118    4.996   1.00 91.06  ? 176 VAL F CA  1 
ATOM   8644  C C   . VAL F 2 174 ? -43.514  5.530    3.698   1.00 91.01  ? 176 VAL F C   1 
ATOM   8645  O O   . VAL F 2 174 ? -42.924  5.691    2.627   1.00 91.32  ? 176 VAL F O   1 
ATOM   8646  C CB  . VAL F 2 174 ? -42.838  7.675    5.003   1.00 95.72  ? 176 VAL F CB  1 
ATOM   8647  C CG1 . VAL F 2 174 ? -44.074  8.329    4.382   1.00 93.15  ? 176 VAL F CG1 1 
ATOM   8648  C CG2 . VAL F 2 174 ? -42.629  8.194    6.419   1.00 97.27  ? 176 VAL F CG2 1 
ATOM   8649  N N   . LEU F 2 175 ? -44.665  4.825    3.817   1.00 83.07  ? 177 LEU F N   1 
ATOM   8650  C CA  . LEU F 2 175 ? -45.380  4.237    2.687   1.00 79.81  ? 177 LEU F CA  1 
ATOM   8651  C C   . LEU F 2 175 ? -46.259  5.318    2.064   1.00 83.76  ? 177 LEU F C   1 
ATOM   8652  O O   . LEU F 2 175 ? -47.075  5.918    2.760   1.00 83.58  ? 177 LEU F O   1 
ATOM   8653  C CB  . LEU F 2 175 ? -46.217  3.020    3.132   1.00 77.57  ? 177 LEU F CB  1 
ATOM   8654  C CG  . LEU F 2 175 ? -47.310  2.533    2.171   1.00 79.20  ? 177 LEU F CG  1 
ATOM   8655  C CD1 . LEU F 2 175 ? -46.734  2.002    0.889   1.00 80.28  ? 177 LEU F CD1 1 
ATOM   8656  C CD2 . LEU F 2 175 ? -48.168  1.475    2.801   1.00 78.57  ? 177 LEU F CD2 1 
ATOM   8657  N N   . VAL F 2 176 ? -46.076  5.576    0.763   1.00 80.75  ? 178 VAL F N   1 
ATOM   8658  C CA  . VAL F 2 176 ? -46.821  6.593    0.020   1.00 80.03  ? 178 VAL F CA  1 
ATOM   8659  C C   . VAL F 2 176 ? -47.558  5.931    -1.138  1.00 87.00  ? 178 VAL F C   1 
ATOM   8660  O O   . VAL F 2 176 ? -46.926  5.268    -1.963  1.00 87.77  ? 178 VAL F O   1 
ATOM   8661  C CB  . VAL F 2 176 ? -45.892  7.738    -0.466  1.00 84.64  ? 178 VAL F CB  1 
ATOM   8662  C CG1 . VAL F 2 176 ? -46.656  8.751    -1.308  1.00 83.26  ? 178 VAL F CG1 1 
ATOM   8663  C CG2 . VAL F 2 176 ? -45.199  8.429    0.702   1.00 85.92  ? 178 VAL F CG2 1 
ATOM   8664  N N   . LEU F 2 177 ? -48.881  6.115    -1.207  1.00 84.88  ? 179 LEU F N   1 
ATOM   8665  C CA  . LEU F 2 177 ? -49.704  5.561    -2.286  1.00 84.94  ? 179 LEU F CA  1 
ATOM   8666  C C   . LEU F 2 177 ? -50.291  6.690    -3.126  1.00 91.88  ? 179 LEU F C   1 
ATOM   8667  O O   . LEU F 2 177 ? -50.642  7.744    -2.590  1.00 92.36  ? 179 LEU F O   1 
ATOM   8668  C CB  . LEU F 2 177 ? -50.840  4.695    -1.737  1.00 83.27  ? 179 LEU F CB  1 
ATOM   8669  C CG  . LEU F 2 177 ? -50.453  3.407    -1.051  1.00 87.83  ? 179 LEU F CG  1 
ATOM   8670  C CD1 . LEU F 2 177 ? -50.484  3.577    0.449   1.00 88.17  ? 179 LEU F CD1 1 
ATOM   8671  C CD2 . LEU F 2 177 ? -51.412  2.313    -1.417  1.00 88.34  ? 179 LEU F CD2 1 
ATOM   8672  N N   . TRP F 2 178 ? -50.398  6.467    -4.440  1.00 89.87  ? 180 TRP F N   1 
ATOM   8673  C CA  . TRP F 2 178 ? -50.946  7.431    -5.391  1.00 91.16  ? 180 TRP F CA  1 
ATOM   8674  C C   . TRP F 2 178 ? -51.535  6.697    -6.578  1.00 99.38  ? 180 TRP F C   1 
ATOM   8675  O O   . TRP F 2 178 ? -51.133  5.567    -6.875  1.00 99.53  ? 180 TRP F O   1 
ATOM   8676  C CB  . TRP F 2 178 ? -49.868  8.422    -5.869  1.00 91.52  ? 180 TRP F CB  1 
ATOM   8677  C CG  . TRP F 2 178 ? -48.783  7.803    -6.710  1.00 93.44  ? 180 TRP F CG  1 
ATOM   8678  C CD1 . TRP F 2 178 ? -48.752  7.714    -8.070  1.00 96.95  ? 180 TRP F CD1 1 
ATOM   8679  C CD2 . TRP F 2 178 ? -47.565  7.201    -6.240  1.00 94.21  ? 180 TRP F CD2 1 
ATOM   8680  N NE1 . TRP F 2 178 ? -47.599  7.081    -8.477  1.00 97.30  ? 180 TRP F NE1 1 
ATOM   8681  C CE2 . TRP F 2 178 ? -46.851  6.758    -7.374  1.00 98.80  ? 180 TRP F CE2 1 
ATOM   8682  C CE3 . TRP F 2 178 ? -47.011  6.982    -4.966  1.00 95.57  ? 180 TRP F CE3 1 
ATOM   8683  C CZ2 . TRP F 2 178 ? -45.613  6.112    -7.273  1.00 99.17  ? 180 TRP F CZ2 1 
ATOM   8684  C CZ3 . TRP F 2 178 ? -45.785  6.342    -4.870  1.00 98.06  ? 180 TRP F CZ3 1 
ATOM   8685  C CH2 . TRP F 2 178 ? -45.105  5.906    -6.012  1.00 99.51  ? 180 TRP F CH2 1 
ATOM   8686  N N   . GLY F 2 179 ? -52.443  7.366    -7.274  1.00 98.50  ? 181 GLY F N   1 
ATOM   8687  C CA  . GLY F 2 179 ? -53.088  6.805    -8.451  1.00 99.58  ? 181 GLY F CA  1 
ATOM   8688  C C   . GLY F 2 179 ? -52.774  7.560    -9.723  1.00 106.86 ? 181 GLY F C   1 
ATOM   8689  O O   . GLY F 2 179 ? -52.311  8.705    -9.675  1.00 107.72 ? 181 GLY F O   1 
ATOM   8690  N N   . ILE F 2 180 ? -53.005  6.899    -10.870 1.00 104.38 ? 182 ILE F N   1 
ATOM   8691  C CA  . ILE F 2 180 ? -52.845  7.460    -12.209 1.00 106.09 ? 182 ILE F CA  1 
ATOM   8692  C C   . ILE F 2 180 ? -54.153  7.166    -12.924 1.00 111.60 ? 182 ILE F C   1 
ATOM   8693  O O   . ILE F 2 180 ? -54.470  6.000    -13.161 1.00 112.16 ? 182 ILE F O   1 
ATOM   8694  C CB  . ILE F 2 180 ? -51.611  6.896    -12.975 1.00 110.52 ? 182 ILE F CB  1 
ATOM   8695  C CG1 . ILE F 2 180 ? -50.270  7.093    -12.203 1.00 111.38 ? 182 ILE F CG1 1 
ATOM   8696  C CG2 . ILE F 2 180 ? -51.527  7.451    -14.403 1.00 112.94 ? 182 ILE F CG2 1 
ATOM   8697  C CD1 . ILE F 2 180 ? -49.823  8.522    -11.862 1.00 119.91 ? 182 ILE F CD1 1 
ATOM   8698  N N   . HIS F 2 181 ? -54.935  8.215    -13.210 1.00 108.72 ? 183 HIS F N   1 
ATOM   8699  C CA  . HIS F 2 181 ? -56.226  8.100    -13.883 1.00 109.18 ? 183 HIS F CA  1 
ATOM   8700  C C   . HIS F 2 181 ? -56.047  8.042    -15.405 1.00 115.85 ? 183 HIS F C   1 
ATOM   8701  O O   . HIS F 2 181 ? -55.381  8.904    -15.977 1.00 116.97 ? 183 HIS F O   1 
ATOM   8702  C CB  . HIS F 2 181 ? -57.143  9.264    -13.472 1.00 109.59 ? 183 HIS F CB  1 
ATOM   8703  C CG  . HIS F 2 181 ? -58.490  9.249    -14.128 1.00 113.66 ? 183 HIS F CG  1 
ATOM   8704  N ND1 . HIS F 2 181 ? -58.826  10.167   -15.104 1.00 117.18 ? 183 HIS F ND1 1 
ATOM   8705  C CD2 . HIS F 2 181 ? -59.539  8.420    -13.932 1.00 114.80 ? 183 HIS F CD2 1 
ATOM   8706  C CE1 . HIS F 2 181 ? -60.065  9.875    -15.460 1.00 117.03 ? 183 HIS F CE1 1 
ATOM   8707  N NE2 . HIS F 2 181 ? -60.536  8.833    -14.782 1.00 115.94 ? 183 HIS F NE2 1 
ATOM   8708  N N   . HIS F 2 182 ? -56.633  7.024    -16.053 1.00 112.74 ? 184 HIS F N   1 
ATOM   8709  C CA  . HIS F 2 182 ? -56.572  6.853    -17.507 1.00 114.47 ? 184 HIS F CA  1 
ATOM   8710  C C   . HIS F 2 182 ? -57.988  7.108    -18.090 1.00 118.98 ? 184 HIS F C   1 
ATOM   8711  O O   . HIS F 2 182 ? -58.852  6.226    -18.021 1.00 118.99 ? 184 HIS F O   1 
ATOM   8712  C CB  . HIS F 2 182 ? -55.998  5.470    -17.889 1.00 115.24 ? 184 HIS F CB  1 
ATOM   8713  C CG  . HIS F 2 182 ? -54.653  5.180    -17.286 1.00 117.51 ? 184 HIS F CG  1 
ATOM   8714  N ND1 . HIS F 2 182 ? -53.488  5.369    -17.999 1.00 120.36 ? 184 HIS F ND1 1 
ATOM   8715  C CD2 . HIS F 2 182 ? -54.336  4.722    -16.052 1.00 117.18 ? 184 HIS F CD2 1 
ATOM   8716  C CE1 . HIS F 2 182 ? -52.502  5.027    -17.184 1.00 118.60 ? 184 HIS F CE1 1 
ATOM   8717  N NE2 . HIS F 2 182 ? -52.962  4.633    -16.000 1.00 117.11 ? 184 HIS F NE2 1 
ATOM   8718  N N   . PRO F 2 183 ? -58.263  8.346    -18.578 1.00 115.29 ? 185 PRO F N   1 
ATOM   8719  C CA  . PRO F 2 183 ? -59.609  8.663    -19.092 1.00 116.17 ? 185 PRO F CA  1 
ATOM   8720  C C   . PRO F 2 183 ? -59.962  7.890    -20.347 1.00 122.97 ? 185 PRO F C   1 
ATOM   8721  O O   . PRO F 2 183 ? -59.110  7.715    -21.210 1.00 123.82 ? 185 PRO F O   1 
ATOM   8722  C CB  . PRO F 2 183 ? -59.539  10.167   -19.382 1.00 118.90 ? 185 PRO F CB  1 
ATOM   8723  C CG  . PRO F 2 183 ? -58.307  10.654   -18.707 1.00 121.95 ? 185 PRO F CG  1 
ATOM   8724  C CD  . PRO F 2 183 ? -57.367  9.508    -18.701 1.00 116.95 ? 185 PRO F CD  1 
ATOM   8725  N N   . SER F 2 184 ? -61.217  7.438    -20.448 1.00 121.32 ? 186 SER F N   1 
ATOM   8726  C CA  . SER F 2 184 ? -61.723  6.666    -21.589 1.00 124.04 ? 186 SER F CA  1 
ATOM   8727  C C   . SER F 2 184 ? -61.653  7.407    -22.938 1.00 131.87 ? 186 SER F C   1 
ATOM   8728  O O   . SER F 2 184 ? -61.089  6.868    -23.890 1.00 133.31 ? 186 SER F O   1 
ATOM   8729  C CB  . SER F 2 184 ? -63.136  6.168    -21.314 1.00 127.47 ? 186 SER F CB  1 
ATOM   8730  O OG  . SER F 2 184 ? -63.960  7.215    -20.828 1.00 135.68 ? 186 SER F OG  1 
ATOM   8731  N N   . THR F 2 185 ? -62.204  8.637    -23.010 1.00 129.52 ? 187 THR F N   1 
ATOM   8732  C CA  . THR F 2 185 ? -62.195  9.463    -24.224 1.00 132.19 ? 187 THR F CA  1 
ATOM   8733  C C   . THR F 2 185 ? -61.139  10.556   -24.124 1.00 133.76 ? 187 THR F C   1 
ATOM   8734  O O   . THR F 2 185 ? -60.750  10.950   -23.021 1.00 129.65 ? 187 THR F O   1 
ATOM   8735  C CB  . THR F 2 185 ? -63.586  10.069   -24.514 1.00 146.32 ? 187 THR F CB  1 
ATOM   8736  O OG1 . THR F 2 185 ? -63.930  11.025   -23.510 1.00 145.94 ? 187 THR F OG1 1 
ATOM   8737  C CG2 . THR F 2 185 ? -64.675  9.022    -24.639 1.00 147.31 ? 187 THR F CG2 1 
ATOM   8738  N N   . SER F 2 186 ? -60.676  11.048   -25.282 1.00 133.37 ? 188 SER F N   1 
ATOM   8739  C CA  . SER F 2 186 ? -59.694  12.126   -25.345 1.00 133.70 ? 188 SER F CA  1 
ATOM   8740  C C   . SER F 2 186 ? -60.286  13.401   -24.728 1.00 137.43 ? 188 SER F C   1 
ATOM   8741  O O   . SER F 2 186 ? -59.573  14.156   -24.066 1.00 135.79 ? 188 SER F O   1 
ATOM   8742  C CB  . SER F 2 186 ? -59.268  12.370   -26.788 1.00 141.04 ? 188 SER F CB  1 
ATOM   8743  O OG  . SER F 2 186 ? -58.615  13.621   -26.883 1.00 152.65 ? 188 SER F OG  1 
ATOM   8744  N N   . ALA F 2 187 ? -61.603  13.598   -24.928 1.00 141.13 ? 189 ALA F N   1 
ATOM   8745  C CA  . ALA F 2 187 ? -62.401  14.709   -24.418 1.00 142.32 ? 189 ALA F CA  1 
ATOM   8746  C C   . ALA F 2 187 ? -62.418  14.743   -22.900 1.00 142.73 ? 189 ALA F C   1 
ATOM   8747  O O   . ALA F 2 187 ? -62.417  15.831   -22.319 1.00 142.31 ? 189 ALA F O   1 
ATOM   8748  C CB  . ALA F 2 187 ? -63.819  14.598   -24.940 1.00 147.22 ? 189 ALA F CB  1 
ATOM   8749  N N   . ASP F 2 188 ? -62.447  13.551   -22.261 1.00 136.57 ? 190 ASP F N   1 
ATOM   8750  C CA  . ASP F 2 188 ? -62.451  13.410   -20.803 1.00 133.07 ? 190 ASP F CA  1 
ATOM   8751  C C   . ASP F 2 188 ? -61.151  13.958   -20.207 1.00 132.19 ? 190 ASP F C   1 
ATOM   8752  O O   . ASP F 2 188 ? -61.194  14.644   -19.187 1.00 130.81 ? 190 ASP F O   1 
ATOM   8753  C CB  . ASP F 2 188 ? -62.715  11.951   -20.375 1.00 133.63 ? 190 ASP F CB  1 
ATOM   8754  C CG  . ASP F 2 188 ? -64.182  11.559   -20.228 1.00 141.75 ? 190 ASP F CG  1 
ATOM   8755  O OD1 . ASP F 2 188 ? -65.032  12.123   -20.964 1.00 144.89 ? 190 ASP F OD1 1 
ATOM   8756  O OD2 . ASP F 2 188 ? -64.472  10.646   -19.422 1.00 144.40 ? 190 ASP F OD2 1 
ATOM   8757  N N   . GLN F 2 189 ? -60.014  13.712   -20.883 1.00 126.03 ? 191 GLN F N   1 
ATOM   8758  C CA  . GLN F 2 189 ? -58.700  14.213   -20.482 1.00 122.79 ? 191 GLN F CA  1 
ATOM   8759  C C   . GLN F 2 189 ? -58.699  15.751   -20.521 1.00 126.76 ? 191 GLN F C   1 
ATOM   8760  O O   . GLN F 2 189 ? -58.220  16.390   -19.587 1.00 123.53 ? 191 GLN F O   1 
ATOM   8761  C CB  . GLN F 2 189 ? -57.627  13.639   -21.421 1.00 123.94 ? 191 GLN F CB  1 
ATOM   8762  C CG  . GLN F 2 189 ? -56.214  14.172   -21.199 1.00 130.38 ? 191 GLN F CG  1 
ATOM   8763  C CD  . GLN F 2 189 ? -55.581  13.630   -19.951 1.00 134.43 ? 191 GLN F CD  1 
ATOM   8764  O OE1 . GLN F 2 189 ? -55.602  12.426   -19.693 1.00 124.77 ? 191 GLN F OE1 1 
ATOM   8765  N NE2 . GLN F 2 189 ? -54.967  14.506   -19.178 1.00 124.65 ? 191 GLN F NE2 1 
ATOM   8766  N N   . GLN F 2 190 ? -59.260  16.334   -21.590 1.00 127.57 ? 192 GLN F N   1 
ATOM   8767  C CA  . GLN F 2 190 ? -59.345  17.781   -21.764 1.00 129.84 ? 192 GLN F CA  1 
ATOM   8768  C C   . GLN F 2 190 ? -60.285  18.417   -20.726 1.00 134.91 ? 192 GLN F C   1 
ATOM   8769  O O   . GLN F 2 190 ? -60.043  19.542   -20.288 1.00 135.21 ? 192 GLN F O   1 
ATOM   8770  C CB  . GLN F 2 190 ? -59.806  18.119   -23.194 1.00 135.19 ? 192 GLN F CB  1 
ATOM   8771  C CG  . GLN F 2 190 ? -59.055  19.288   -23.851 1.00 154.68 ? 192 GLN F CG  1 
ATOM   8772  C CD  . GLN F 2 190 ? -59.521  20.673   -23.431 1.00 178.81 ? 192 GLN F CD  1 
ATOM   8773  O OE1 . GLN F 2 190 ? -58.711  21.557   -23.128 1.00 173.86 ? 192 GLN F OE1 1 
ATOM   8774  N NE2 . GLN F 2 190 ? -60.828  20.917   -23.453 1.00 174.53 ? 192 GLN F NE2 1 
ATOM   8775  N N   . SER F 2 191 ? -61.341  17.694   -20.317 1.00 131.19 ? 193 SER F N   1 
ATOM   8776  C CA  . SER F 2 191 ? -62.317  18.225   -19.366 1.00 131.29 ? 193 SER F CA  1 
ATOM   8777  C C   . SER F 2 191 ? -61.902  18.105   -17.902 1.00 131.52 ? 193 SER F C   1 
ATOM   8778  O O   . SER F 2 191 ? -62.385  18.879   -17.068 1.00 131.97 ? 193 SER F O   1 
ATOM   8779  C CB  . SER F 2 191 ? -63.683  17.594   -19.590 1.00 137.23 ? 193 SER F CB  1 
ATOM   8780  O OG  . SER F 2 191 ? -63.624  16.190   -19.435 1.00 145.36 ? 193 SER F OG  1 
ATOM   8781  N N   . LEU F 2 192 ? -61.024  17.135   -17.587 1.00 123.84 ? 194 LEU F N   1 
ATOM   8782  C CA  . LEU F 2 192 ? -60.551  16.894   -16.224 1.00 119.71 ? 194 LEU F CA  1 
ATOM   8783  C C   . LEU F 2 192 ? -59.210  17.552   -15.944 1.00 122.54 ? 194 LEU F C   1 
ATOM   8784  O O   . LEU F 2 192 ? -59.000  18.048   -14.838 1.00 120.64 ? 194 LEU F O   1 
ATOM   8785  C CB  . LEU F 2 192 ? -60.428  15.387   -15.943 1.00 117.28 ? 194 LEU F CB  1 
ATOM   8786  C CG  . LEU F 2 192 ? -61.694  14.552   -15.943 1.00 122.36 ? 194 LEU F CG  1 
ATOM   8787  C CD1 . LEU F 2 192 ? -61.359  13.098   -16.122 1.00 121.09 ? 194 LEU F CD1 1 
ATOM   8788  C CD2 . LEU F 2 192 ? -62.519  14.772   -14.682 1.00 124.15 ? 194 LEU F CD2 1 
ATOM   8789  N N   . TYR F 2 193 ? -58.277  17.501   -16.915 1.00 120.34 ? 195 TYR F N   1 
ATOM   8790  C CA  . TYR F 2 193 ? -56.915  18.007   -16.733 1.00 119.43 ? 195 TYR F CA  1 
ATOM   8791  C C   . TYR F 2 193 ? -56.441  19.014   -17.800 1.00 127.50 ? 195 TYR F C   1 
ATOM   8792  O O   . TYR F 2 193 ? -55.337  19.540   -17.653 1.00 126.74 ? 195 TYR F O   1 
ATOM   8793  C CB  . TYR F 2 193 ? -55.926  16.826   -16.620 1.00 117.95 ? 195 TYR F CB  1 
ATOM   8794  C CG  . TYR F 2 193 ? -56.473  15.643   -15.847 1.00 117.33 ? 195 TYR F CG  1 
ATOM   8795  C CD1 . TYR F 2 193 ? -56.649  15.707   -14.468 1.00 117.85 ? 195 TYR F CD1 1 
ATOM   8796  C CD2 . TYR F 2 193 ? -56.861  14.479   -16.500 1.00 118.02 ? 195 TYR F CD2 1 
ATOM   8797  C CE1 . TYR F 2 193 ? -57.179  14.634   -13.757 1.00 116.91 ? 195 TYR F CE1 1 
ATOM   8798  C CE2 . TYR F 2 193 ? -57.395  13.400   -15.800 1.00 117.51 ? 195 TYR F CE2 1 
ATOM   8799  C CZ  . TYR F 2 193 ? -57.552  13.483   -14.429 1.00 120.54 ? 195 TYR F CZ  1 
ATOM   8800  O OH  . TYR F 2 193 ? -58.065  12.425   -13.733 1.00 116.98 ? 195 TYR F OH  1 
ATOM   8801  N N   . GLN F 2 194 ? -57.268  19.275   -18.854 1.00 127.50 ? 196 GLN F N   1 
ATOM   8802  C CA  . GLN F 2 194 ? -57.092  20.207   -19.994 1.00 130.33 ? 196 GLN F CA  1 
ATOM   8803  C C   . GLN F 2 194 ? -55.806  19.997   -20.841 1.00 134.84 ? 196 GLN F C   1 
ATOM   8804  O O   . GLN F 2 194 ? -55.796  20.380   -22.016 1.00 137.23 ? 196 GLN F O   1 
ATOM   8805  C CB  . GLN F 2 194 ? -57.240  21.696   -19.585 1.00 133.15 ? 196 GLN F CB  1 
ATOM   8806  C CG  . GLN F 2 194 ? -55.976  22.397   -19.057 1.00 151.97 ? 196 GLN F CG  1 
ATOM   8807  C CD  . GLN F 2 194 ? -56.003  23.908   -19.153 1.00 172.88 ? 196 GLN F CD  1 
ATOM   8808  O OE1 . GLN F 2 194 ? -56.994  24.527   -19.565 1.00 170.85 ? 196 GLN F OE1 1 
ATOM   8809  N NE2 . GLN F 2 194 ? -54.896  24.538   -18.779 1.00 162.65 ? 196 GLN F NE2 1 
ATOM   8810  N N   . ASN F 2 195 ? -54.749  19.412   -20.263 1.00 128.87 ? 197 ASN F N   1 
ATOM   8811  C CA  . ASN F 2 195 ? -53.487  19.163   -20.941 1.00 128.46 ? 197 ASN F CA  1 
ATOM   8812  C C   . ASN F 2 195 ? -53.580  17.819   -21.644 1.00 131.98 ? 197 ASN F C   1 
ATOM   8813  O O   . ASN F 2 195 ? -53.537  16.772   -20.991 1.00 129.66 ? 197 ASN F O   1 
ATOM   8814  C CB  . ASN F 2 195 ? -52.322  19.223   -19.949 1.00 126.58 ? 197 ASN F CB  1 
ATOM   8815  C CG  . ASN F 2 195 ? -52.162  20.584   -19.320 1.00 146.66 ? 197 ASN F CG  1 
ATOM   8816  O OD1 . ASN F 2 195 ? -51.435  21.443   -19.826 1.00 144.34 ? 197 ASN F OD1 1 
ATOM   8817  N ND2 . ASN F 2 195 ? -52.862  20.823   -18.217 1.00 134.50 ? 197 ASN F ND2 1 
ATOM   8818  N N   . ALA F 2 196 ? -53.791  17.856   -22.975 1.00 130.53 ? 198 ALA F N   1 
ATOM   8819  C CA  . ALA F 2 196 ? -53.923  16.662   -23.808 1.00 130.93 ? 198 ALA F CA  1 
ATOM   8820  C C   . ALA F 2 196 ? -52.700  15.763   -23.677 1.00 133.05 ? 198 ALA F C   1 
ATOM   8821  O O   . ALA F 2 196 ? -52.860  14.553   -23.540 1.00 131.48 ? 198 ALA F O   1 
ATOM   8822  C CB  . ALA F 2 196 ? -54.147  17.052   -25.256 1.00 135.17 ? 198 ALA F CB  1 
ATOM   8823  N N   . ASP F 2 197 ? -51.487  16.354   -23.681 1.00 130.01 ? 199 ASP F N   1 
ATOM   8824  C CA  . ASP F 2 197 ? -50.242  15.615   -23.490 1.00 128.78 ? 199 ASP F CA  1 
ATOM   8825  C C   . ASP F 2 197 ? -49.746  15.870   -22.070 1.00 128.92 ? 199 ASP F C   1 
ATOM   8826  O O   . ASP F 2 197 ? -48.828  16.667   -21.833 1.00 128.19 ? 199 ASP F O   1 
ATOM   8827  C CB  . ASP F 2 197 ? -49.189  15.958   -24.552 1.00 133.32 ? 199 ASP F CB  1 
ATOM   8828  C CG  . ASP F 2 197 ? -48.094  14.913   -24.632 1.00 152.98 ? 199 ASP F CG  1 
ATOM   8829  O OD1 . ASP F 2 197 ? -48.279  13.911   -25.369 1.00 155.80 ? 199 ASP F OD1 1 
ATOM   8830  O OD2 . ASP F 2 197 ? -47.062  15.079   -23.936 1.00 161.28 ? 199 ASP F OD2 1 
ATOM   8831  N N   . ALA F 2 198 ? -50.431  15.224   -21.117 1.00 122.90 ? 200 ALA F N   1 
ATOM   8832  C CA  . ALA F 2 198 ? -50.148  15.310   -19.692 1.00 120.11 ? 200 ALA F CA  1 
ATOM   8833  C C   . ALA F 2 198 ? -49.247  14.171   -19.276 1.00 120.61 ? 200 ALA F C   1 
ATOM   8834  O O   . ALA F 2 198 ? -49.316  13.075   -19.836 1.00 119.68 ? 200 ALA F O   1 
ATOM   8835  C CB  . ALA F 2 198 ? -51.439  15.272   -18.893 1.00 120.13 ? 200 ALA F CB  1 
ATOM   8836  N N   . TYR F 2 199 ? -48.389  14.443   -18.299 1.00 115.87 ? 201 TYR F N   1 
ATOM   8837  C CA  . TYR F 2 199 ? -47.454  13.471   -17.759 1.00 115.02 ? 201 TYR F CA  1 
ATOM   8838  C C   . TYR F 2 199 ? -47.511  13.475   -16.241 1.00 116.79 ? 201 TYR F C   1 
ATOM   8839  O O   . TYR F 2 199 ? -48.043  14.412   -15.636 1.00 116.44 ? 201 TYR F O   1 
ATOM   8840  C CB  . TYR F 2 199 ? -46.020  13.778   -18.244 1.00 117.92 ? 201 TYR F CB  1 
ATOM   8841  C CG  . TYR F 2 199 ? -45.347  14.942   -17.543 1.00 120.31 ? 201 TYR F CG  1 
ATOM   8842  C CD1 . TYR F 2 199 ? -45.489  16.243   -18.016 1.00 123.48 ? 201 TYR F CD1 1 
ATOM   8843  C CD2 . TYR F 2 199 ? -44.539  14.738   -16.428 1.00 121.01 ? 201 TYR F CD2 1 
ATOM   8844  C CE1 . TYR F 2 199 ? -44.863  17.315   -17.383 1.00 125.85 ? 201 TYR F CE1 1 
ATOM   8845  C CE2 . TYR F 2 199 ? -43.922  15.804   -15.776 1.00 123.04 ? 201 TYR F CE2 1 
ATOM   8846  C CZ  . TYR F 2 199 ? -44.080  17.092   -16.262 1.00 133.39 ? 201 TYR F CZ  1 
ATOM   8847  O OH  . TYR F 2 199 ? -43.456  18.147   -15.638 1.00 136.21 ? 201 TYR F OH  1 
ATOM   8848  N N   . VAL F 2 200 ? -46.943  12.431   -15.627 1.00 112.20 ? 202 VAL F N   1 
ATOM   8849  C CA  . VAL F 2 200 ? -46.810  12.294   -14.175 1.00 110.85 ? 202 VAL F CA  1 
ATOM   8850  C C   . VAL F 2 200 ? -45.385  11.806   -13.896 1.00 115.43 ? 202 VAL F C   1 
ATOM   8851  O O   . VAL F 2 200 ? -44.798  11.133   -14.738 1.00 115.98 ? 202 VAL F O   1 
ATOM   8852  C CB  . VAL F 2 200 ? -47.868  11.385   -13.486 1.00 113.11 ? 202 VAL F CB  1 
ATOM   8853  C CG1 . VAL F 2 200 ? -47.931  11.685   -12.000 1.00 112.02 ? 202 VAL F CG1 1 
ATOM   8854  C CG2 . VAL F 2 200 ? -49.255  11.534   -14.105 1.00 112.75 ? 202 VAL F CG2 1 
ATOM   8855  N N   . PHE F 2 201 ? -44.814  12.189   -12.750 1.00 111.62 ? 203 PHE F N   1 
ATOM   8856  C CA  . PHE F 2 201 ? -43.484  11.769   -12.333 1.00 112.58 ? 203 PHE F CA  1 
ATOM   8857  C C   . PHE F 2 201 ? -43.394  11.673   -10.819 1.00 113.62 ? 203 PHE F C   1 
ATOM   8858  O O   . PHE F 2 201 ? -43.721  12.638   -10.124 1.00 113.00 ? 203 PHE F O   1 
ATOM   8859  C CB  . PHE F 2 201 ? -42.375  12.684   -12.893 1.00 116.54 ? 203 PHE F CB  1 
ATOM   8860  C CG  . PHE F 2 201 ? -41.015  12.313   -12.349 1.00 120.93 ? 203 PHE F CG  1 
ATOM   8861  C CD1 . PHE F 2 201 ? -40.410  13.081   -11.360 1.00 125.53 ? 203 PHE F CD1 1 
ATOM   8862  C CD2 . PHE F 2 201 ? -40.381  11.142   -12.756 1.00 125.34 ? 203 PHE F CD2 1 
ATOM   8863  C CE1 . PHE F 2 201 ? -39.178  12.707   -10.819 1.00 129.13 ? 203 PHE F CE1 1 
ATOM   8864  C CE2 . PHE F 2 201 ? -39.148  10.768   -12.214 1.00 130.80 ? 203 PHE F CE2 1 
ATOM   8865  C CZ  . PHE F 2 201 ? -38.554  11.554   -11.252 1.00 130.04 ? 203 PHE F CZ  1 
ATOM   8866  N N   . VAL F 2 202 ? -42.929  10.515   -10.311 1.00 108.38 ? 204 VAL F N   1 
ATOM   8867  C CA  . VAL F 2 202 ? -42.742  10.280   -8.880  1.00 107.61 ? 204 VAL F CA  1 
ATOM   8868  C C   . VAL F 2 202 ? -41.268  9.959    -8.614  1.00 113.29 ? 204 VAL F C   1 
ATOM   8869  O O   . VAL F 2 202 ? -40.785  8.895    -9.008  1.00 113.90 ? 204 VAL F O   1 
ATOM   8870  C CB  . VAL F 2 202 ? -43.712  9.226    -8.301  1.00 109.77 ? 204 VAL F CB  1 
ATOM   8871  C CG1 . VAL F 2 202 ? -43.532  9.105    -6.795  1.00 110.34 ? 204 VAL F CG1 1 
ATOM   8872  C CG2 . VAL F 2 202 ? -45.156  9.578    -8.628  1.00 107.45 ? 204 VAL F CG2 1 
ATOM   8873  N N   . GLY F 2 203 ? -40.575  10.900   -7.973  1.00 110.69 ? 205 GLY F N   1 
ATOM   8874  C CA  . GLY F 2 203 ? -39.153  10.793   -7.673  1.00 113.49 ? 205 GLY F CA  1 
ATOM   8875  C C   . GLY F 2 203 ? -38.781  10.690   -6.208  1.00 119.64 ? 205 GLY F C   1 
ATOM   8876  O O   . GLY F 2 203 ? -39.010  11.619   -5.433  1.00 120.12 ? 205 GLY F O   1 
ATOM   8877  N N   . SER F 2 204 ? -38.166  9.554    -5.842  1.00 116.38 ? 206 SER F N   1 
ATOM   8878  C CA  . SER F 2 204 ? -37.634  9.185    -4.527  1.00 117.30 ? 206 SER F CA  1 
ATOM   8879  C C   . SER F 2 204 ? -36.192  8.733    -4.793  1.00 124.28 ? 206 SER F C   1 
ATOM   8880  O O   . SER F 2 204 ? -35.796  8.662    -5.958  1.00 123.82 ? 206 SER F O   1 
ATOM   8881  C CB  . SER F 2 204 ? -38.457  8.035    -3.946  1.00 117.66 ? 206 SER F CB  1 
ATOM   8882  O OG  . SER F 2 204 ? -37.844  7.405    -2.835  1.00 123.43 ? 206 SER F OG  1 
ATOM   8883  N N   . SER F 2 205 ? -35.399  8.446    -3.752  1.00 124.42 ? 207 SER F N   1 
ATOM   8884  C CA  . SER F 2 205 ? -34.038  7.958    -3.989  1.00 128.64 ? 207 SER F CA  1 
ATOM   8885  C C   . SER F 2 205 ? -34.084  6.516    -4.519  1.00 134.50 ? 207 SER F C   1 
ATOM   8886  O O   . SER F 2 205 ? -33.323  6.175    -5.427  1.00 135.50 ? 207 SER F O   1 
ATOM   8887  C CB  . SER F 2 205 ? -33.184  8.053    -2.731  1.00 136.28 ? 207 SER F CB  1 
ATOM   8888  O OG  . SER F 2 205 ? -32.872  9.404    -2.436  1.00 147.02 ? 207 SER F OG  1 
ATOM   8889  N N   . ARG F 2 206 ? -35.022  5.696    -3.994  1.00 130.76 ? 208 ARG F N   1 
ATOM   8890  C CA  . ARG F 2 206 ? -35.205  4.307    -4.425  1.00 130.76 ? 208 ARG F CA  1 
ATOM   8891  C C   . ARG F 2 206 ? -36.204  4.170    -5.595  1.00 129.70 ? 208 ARG F C   1 
ATOM   8892  O O   . ARG F 2 206 ? -35.994  3.323    -6.462  1.00 129.89 ? 208 ARG F O   1 
ATOM   8893  C CB  . ARG F 2 206 ? -35.553  3.361    -3.245  1.00 132.58 ? 208 ARG F CB  1 
ATOM   8894  C CG  . ARG F 2 206 ? -36.799  3.705    -2.417  1.00 140.57 ? 208 ARG F CG  1 
ATOM   8895  C CD  . ARG F 2 206 ? -37.316  2.486    -1.652  1.00 148.24 ? 208 ARG F CD  1 
ATOM   8896  N NE  . ARG F 2 206 ? -36.545  2.187    -0.439  1.00 154.78 ? 208 ARG F NE  1 
ATOM   8897  C CZ  . ARG F 2 206 ? -36.766  1.140    0.355   1.00 164.71 ? 208 ARG F CZ  1 
ATOM   8898  N NH1 . ARG F 2 206 ? -37.740  0.281    0.079   1.00 150.00 ? 208 ARG F NH1 1 
ATOM   8899  N NH2 . ARG F 2 206 ? -36.014  0.946    1.431   1.00 149.95 ? 208 ARG F NH2 1 
ATOM   8900  N N   . TYR F 2 207 ? -37.259  5.012    -5.634  1.00 121.74 ? 209 TYR F N   1 
ATOM   8901  C CA  . TYR F 2 207 ? -38.282  4.985    -6.687  1.00 117.76 ? 209 TYR F CA  1 
ATOM   8902  C C   . TYR F 2 207 ? -38.112  6.116    -7.704  1.00 119.25 ? 209 TYR F C   1 
ATOM   8903  O O   . TYR F 2 207 ? -37.864  7.251    -7.316  1.00 118.07 ? 209 TYR F O   1 
ATOM   8904  C CB  . TYR F 2 207 ? -39.698  5.059    -6.068  1.00 116.01 ? 209 TYR F CB  1 
ATOM   8905  C CG  . TYR F 2 207 ? -40.819  4.805    -7.057  1.00 114.52 ? 209 TYR F CG  1 
ATOM   8906  C CD1 . TYR F 2 207 ? -41.363  5.844    -7.809  1.00 114.27 ? 209 TYR F CD1 1 
ATOM   8907  C CD2 . TYR F 2 207 ? -41.347  3.530    -7.229  1.00 115.00 ? 209 TYR F CD2 1 
ATOM   8908  C CE1 . TYR F 2 207 ? -42.364  5.609    -8.747  1.00 112.88 ? 209 TYR F CE1 1 
ATOM   8909  C CE2 . TYR F 2 207 ? -42.365  3.287    -8.148  1.00 113.66 ? 209 TYR F CE2 1 
ATOM   8910  C CZ  . TYR F 2 207 ? -42.870  4.329    -8.904  1.00 118.57 ? 209 TYR F CZ  1 
ATOM   8911  O OH  . TYR F 2 207 ? -43.868  4.084    -9.813  1.00 118.12 ? 209 TYR F OH  1 
ATOM   8912  N N   . SER F 2 208 ? -38.316  5.815    -8.997  1.00 114.88 ? 210 SER F N   1 
ATOM   8913  C CA  . SER F 2 208 ? -38.282  6.796    -10.084 1.00 113.67 ? 210 SER F CA  1 
ATOM   8914  C C   . SER F 2 208 ? -39.003  6.284    -11.315 1.00 116.61 ? 210 SER F C   1 
ATOM   8915  O O   . SER F 2 208 ? -38.515  5.379    -12.000 1.00 118.12 ? 210 SER F O   1 
ATOM   8916  C CB  . SER F 2 208 ? -36.858  7.240    -10.417 1.00 119.32 ? 210 SER F CB  1 
ATOM   8917  O OG  . SER F 2 208 ? -36.497  8.372    -9.643  1.00 126.34 ? 210 SER F OG  1 
ATOM   8918  N N   . LYS F 2 209 ? -40.187  6.842    -11.573 1.00 109.03 ? 211 LYS F N   1 
ATOM   8919  C CA  . LYS F 2 209 ? -40.984  6.468    -12.729 1.00 109.83 ? 211 LYS F CA  1 
ATOM   8920  C C   . LYS F 2 209 ? -41.790  7.634    -13.283 1.00 114.58 ? 211 LYS F C   1 
ATOM   8921  O O   . LYS F 2 209 ? -42.250  8.492    -12.526 1.00 112.11 ? 211 LYS F O   1 
ATOM   8922  C CB  . LYS F 2 209 ? -41.883  5.255    -12.435 1.00 111.35 ? 211 LYS F CB  1 
ATOM   8923  C CG  . LYS F 2 209 ? -41.917  4.281    -13.609 1.00 129.58 ? 211 LYS F CG  1 
ATOM   8924  C CD  . LYS F 2 209 ? -43.108  3.336    -13.587 1.00 137.52 ? 211 LYS F CD  1 
ATOM   8925  C CE  . LYS F 2 209 ? -43.190  2.557    -14.881 1.00 146.85 ? 211 LYS F CE  1 
ATOM   8926  N NZ  . LYS F 2 209 ? -44.394  1.691    -14.936 1.00 153.92 ? 211 LYS F NZ  1 
ATOM   8927  N N   . THR F 2 210 ? -41.950  7.652    -14.618 1.00 114.46 ? 212 THR F N   1 
ATOM   8928  C CA  . THR F 2 210 ? -42.711  8.646    -15.375 1.00 114.88 ? 212 THR F CA  1 
ATOM   8929  C C   . THR F 2 210 ? -43.990  7.964    -15.882 1.00 118.82 ? 212 THR F C   1 
ATOM   8930  O O   . THR F 2 210 ? -43.948  6.793    -16.264 1.00 120.19 ? 212 THR F O   1 
ATOM   8931  C CB  . THR F 2 210 ? -41.861  9.208    -16.531 1.00 127.83 ? 212 THR F CB  1 
ATOM   8932  O OG1 . THR F 2 210 ? -40.515  9.415    -16.096 1.00 128.45 ? 212 THR F OG1 1 
ATOM   8933  C CG2 . THR F 2 210 ? -42.415  10.505   -17.087 1.00 127.93 ? 212 THR F CG2 1 
ATOM   8934  N N   . PHE F 2 211 ? -45.117  8.686    -15.880 1.00 113.80 ? 213 PHE F N   1 
ATOM   8935  C CA  . PHE F 2 211 ? -46.407  8.154    -16.315 1.00 113.49 ? 213 PHE F CA  1 
ATOM   8936  C C   . PHE F 2 211 ? -47.084  9.023    -17.364 1.00 116.48 ? 213 PHE F C   1 
ATOM   8937  O O   . PHE F 2 211 ? -46.919  10.243   -17.371 1.00 115.55 ? 213 PHE F O   1 
ATOM   8938  C CB  . PHE F 2 211 ? -47.357  7.978    -15.120 1.00 113.25 ? 213 PHE F CB  1 
ATOM   8939  C CG  . PHE F 2 211 ? -46.771  7.277    -13.920 1.00 114.32 ? 213 PHE F CG  1 
ATOM   8940  C CD1 . PHE F 2 211 ? -46.718  5.890    -13.862 1.00 118.68 ? 213 PHE F CD1 1 
ATOM   8941  C CD2 . PHE F 2 211 ? -46.299  8.004    -12.834 1.00 115.79 ? 213 PHE F CD2 1 
ATOM   8942  C CE1 . PHE F 2 211 ? -46.181  5.244    -12.749 1.00 118.78 ? 213 PHE F CE1 1 
ATOM   8943  C CE2 . PHE F 2 211 ? -45.772  7.356    -11.716 1.00 117.89 ? 213 PHE F CE2 1 
ATOM   8944  C CZ  . PHE F 2 211 ? -45.715  5.981    -11.683 1.00 116.46 ? 213 PHE F CZ  1 
ATOM   8945  N N   . LYS F 2 212 ? -47.865  8.381    -18.237 1.00 113.40 ? 214 LYS F N   1 
ATOM   8946  C CA  . LYS F 2 212 ? -48.653  9.021    -19.285 1.00 114.99 ? 214 LYS F CA  1 
ATOM   8947  C C   . LYS F 2 212 ? -49.995  8.289    -19.375 1.00 119.08 ? 214 LYS F C   1 
ATOM   8948  O O   . LYS F 2 212 ? -50.026  7.075    -19.147 1.00 118.21 ? 214 LYS F O   1 
ATOM   8949  C CB  . LYS F 2 212 ? -47.911  9.024    -20.627 1.00 120.99 ? 214 LYS F CB  1 
ATOM   8950  C CG  . LYS F 2 212 ? -47.670  10.431   -21.161 1.00 136.58 ? 214 LYS F CG  1 
ATOM   8951  C CD  . LYS F 2 212 ? -46.891  10.429   -22.469 1.00 150.28 ? 214 LYS F CD  1 
ATOM   8952  C CE  . LYS F 2 212 ? -46.637  11.829   -22.976 1.00 161.08 ? 214 LYS F CE  1 
ATOM   8953  N NZ  . LYS F 2 212 ? -45.769  11.826   -24.187 1.00 171.23 ? 214 LYS F NZ  1 
ATOM   8954  N N   . PRO F 2 213 ? -51.123  8.993    -19.640 1.00 116.63 ? 215 PRO F N   1 
ATOM   8955  C CA  . PRO F 2 213 ? -52.423  8.304    -19.650 1.00 116.31 ? 215 PRO F CA  1 
ATOM   8956  C C   . PRO F 2 213 ? -52.702  7.447    -20.878 1.00 123.20 ? 215 PRO F C   1 
ATOM   8957  O O   . PRO F 2 213 ? -52.464  7.865    -22.010 1.00 125.34 ? 215 PRO F O   1 
ATOM   8958  C CB  . PRO F 2 213 ? -53.428  9.445    -19.507 1.00 117.92 ? 215 PRO F CB  1 
ATOM   8959  C CG  . PRO F 2 213 ? -52.752  10.613   -20.127 1.00 124.28 ? 215 PRO F CG  1 
ATOM   8960  C CD  . PRO F 2 213 ? -51.278  10.442   -19.899 1.00 119.21 ? 215 PRO F CD  1 
ATOM   8961  N N   . GLU F 2 214 ? -53.228  6.247    -20.635 1.00 120.08 ? 216 GLU F N   1 
ATOM   8962  C CA  . GLU F 2 214 ? -53.614  5.287    -21.656 1.00 123.59 ? 216 GLU F CA  1 
ATOM   8963  C C   . GLU F 2 214 ? -55.091  5.554    -21.964 1.00 126.97 ? 216 GLU F C   1 
ATOM   8964  O O   . GLU F 2 214 ? -55.976  4.902    -21.397 1.00 125.11 ? 216 GLU F O   1 
ATOM   8965  C CB  . GLU F 2 214 ? -53.397  3.842    -21.156 1.00 125.05 ? 216 GLU F CB  1 
ATOM   8966  C CG  . GLU F 2 214 ? -51.941  3.418    -21.003 1.00 141.75 ? 216 GLU F CG  1 
ATOM   8967  C CD  . GLU F 2 214 ? -51.713  1.939    -20.737 1.00 174.93 ? 216 GLU F CD  1 
ATOM   8968  O OE1 . GLU F 2 214 ? -52.338  1.388    -19.799 1.00 180.02 ? 216 GLU F OE1 1 
ATOM   8969  O OE2 . GLU F 2 214 ? -50.878  1.338    -21.450 1.00 169.58 ? 216 GLU F OE2 1 
ATOM   8970  N N   . ILE F 2 215 ? -55.352  6.563    -22.823 1.00 124.66 ? 217 ILE F N   1 
ATOM   8971  C CA  . ILE F 2 215 ? -56.711  6.968    -23.192 1.00 125.62 ? 217 ILE F CA  1 
ATOM   8972  C C   . ILE F 2 215 ? -57.339  5.952    -24.152 1.00 133.81 ? 217 ILE F C   1 
ATOM   8973  O O   . ILE F 2 215 ? -56.938  5.861    -25.322 1.00 137.57 ? 217 ILE F O   1 
ATOM   8974  C CB  . ILE F 2 215 ? -56.788  8.442    -23.693 1.00 129.74 ? 217 ILE F CB  1 
ATOM   8975  C CG1 . ILE F 2 215 ? -56.462  9.423    -22.551 1.00 126.40 ? 217 ILE F CG1 1 
ATOM   8976  C CG2 . ILE F 2 215 ? -58.163  8.767    -24.294 1.00 132.93 ? 217 ILE F CG2 1 
ATOM   8977  C CD1 . ILE F 2 215 ? -55.794  10.700   -22.976 1.00 135.06 ? 217 ILE F CD1 1 
ATOM   8978  N N   . ALA F 2 216 ? -58.321  5.177    -23.623 1.00 129.06 ? 218 ALA F N   1 
ATOM   8979  C CA  . ALA F 2 216 ? -59.070  4.132    -24.331 1.00 131.86 ? 218 ALA F CA  1 
ATOM   8980  C C   . ALA F 2 216 ? -60.364  3.770    -23.603 1.00 133.77 ? 218 ALA F C   1 
ATOM   8981  O O   . ALA F 2 216 ? -60.371  3.675    -22.374 1.00 129.57 ? 218 ALA F O   1 
ATOM   8982  C CB  . ALA F 2 216 ? -58.212  2.882    -24.488 1.00 133.42 ? 218 ALA F CB  1 
ATOM   8983  N N   . ILE F 2 217 ? -61.450  3.538    -24.366 1.00 133.22 ? 219 ILE F N   1 
ATOM   8984  C CA  . ILE F 2 217 ? -62.738  3.115    -23.817 1.00 132.17 ? 219 ILE F CA  1 
ATOM   8985  C C   . ILE F 2 217 ? -62.631  1.623    -23.492 1.00 134.44 ? 219 ILE F C   1 
ATOM   8986  O O   . ILE F 2 217 ? -62.393  0.800    -24.383 1.00 137.21 ? 219 ILE F O   1 
ATOM   8987  C CB  . ILE F 2 217 ? -63.940  3.464    -24.756 1.00 139.49 ? 219 ILE F CB  1 
ATOM   8988  C CG1 . ILE F 2 217 ? -64.302  4.966    -24.667 1.00 139.20 ? 219 ILE F CG1 1 
ATOM   8989  C CG2 . ILE F 2 217 ? -65.176  2.589    -24.456 1.00 141.64 ? 219 ILE F CG2 1 
ATOM   8990  C CD1 . ILE F 2 217 ? -65.238  5.492    -25.780 1.00 151.82 ? 219 ILE F CD1 1 
ATOM   8991  N N   . ARG F 2 218 ? -62.769  1.297    -22.210 1.00 126.83 ? 220 ARG F N   1 
ATOM   8992  C CA  . ARG F 2 218 ? -62.689  -0.070   -21.706 1.00 126.39 ? 220 ARG F CA  1 
ATOM   8993  C C   . ARG F 2 218 ? -64.091  -0.564   -21.236 1.00 131.07 ? 220 ARG F C   1 
ATOM   8994  O O   . ARG F 2 218 ? -65.003  0.271    -21.162 1.00 130.23 ? 220 ARG F O   1 
ATOM   8995  C CB  . ARG F 2 218 ? -61.607  -0.153   -20.605 1.00 121.48 ? 220 ARG F CB  1 
ATOM   8996  C CG  . ARG F 2 218 ? -60.192  -0.232   -21.181 1.00 128.90 ? 220 ARG F CG  1 
ATOM   8997  C CD  . ARG F 2 218 ? -59.134  0.280    -20.227 1.00 130.99 ? 220 ARG F CD  1 
ATOM   8998  N NE  . ARG F 2 218 ? -59.168  1.739    -20.093 1.00 137.16 ? 220 ARG F NE  1 
ATOM   8999  C CZ  . ARG F 2 218 ? -58.181  2.556    -20.455 1.00 150.57 ? 220 ARG F CZ  1 
ATOM   9000  N NH1 . ARG F 2 218 ? -57.064  2.069    -20.983 1.00 138.08 ? 220 ARG F NH1 1 
ATOM   9001  N NH2 . ARG F 2 218 ? -58.306  3.866    -20.293 1.00 134.75 ? 220 ARG F NH2 1 
ATOM   9002  N N   . PRO F 2 219 ? -64.323  -1.890   -20.974 1.00 129.02 ? 221 PRO F N   1 
ATOM   9003  C CA  . PRO F 2 219 ? -65.665  -2.324   -20.531 1.00 129.68 ? 221 PRO F CA  1 
ATOM   9004  C C   . PRO F 2 219 ? -66.079  -1.685   -19.206 1.00 128.26 ? 221 PRO F C   1 
ATOM   9005  O O   . PRO F 2 219 ? -65.214  -1.419   -18.364 1.00 124.89 ? 221 PRO F O   1 
ATOM   9006  C CB  . PRO F 2 219 ? -65.521  -3.843   -20.392 1.00 133.38 ? 221 PRO F CB  1 
ATOM   9007  C CG  . PRO F 2 219 ? -64.063  -4.073   -20.183 1.00 135.98 ? 221 PRO F CG  1 
ATOM   9008  C CD  . PRO F 2 219 ? -63.394  -3.040   -21.035 1.00 131.56 ? 221 PRO F CD  1 
ATOM   9009  N N   . LYS F 2 220 ? -67.388  -1.418   -19.031 1.00 123.55 ? 222 LYS F N   1 
ATOM   9010  C CA  . LYS F 2 220 ? -67.912  -0.776   -17.829 1.00 119.43 ? 222 LYS F CA  1 
ATOM   9011  C C   . LYS F 2 220 ? -67.818  -1.672   -16.590 1.00 119.24 ? 222 LYS F C   1 
ATOM   9012  O O   . LYS F 2 220 ? -68.768  -2.378   -16.237 1.00 121.15 ? 222 LYS F O   1 
ATOM   9013  C CB  . LYS F 2 220 ? -69.334  -0.229   -18.046 1.00 124.71 ? 222 LYS F CB  1 
ATOM   9014  C CG  . LYS F 2 220 ? -69.364  1.256    -18.381 1.00 143.33 ? 222 LYS F CG  1 
ATOM   9015  C CD  . LYS F 2 220 ? -70.761  1.850    -18.217 1.00 156.63 ? 222 LYS F CD  1 
ATOM   9016  C CE  . LYS F 2 220 ? -70.846  3.309    -18.619 1.00 169.85 ? 222 LYS F CE  1 
ATOM   9017  N NZ  . LYS F 2 220 ? -70.156  4.214    -17.655 1.00 173.50 ? 222 LYS F NZ  1 
ATOM   9018  N N   . VAL F 2 221 ? -66.638  -1.646   -15.948 1.00 110.73 ? 223 VAL F N   1 
ATOM   9019  C CA  . VAL F 2 221 ? -66.343  -2.369   -14.708 1.00 107.37 ? 223 VAL F CA  1 
ATOM   9020  C C   . VAL F 2 221 ? -66.665  -1.356   -13.617 1.00 107.14 ? 223 VAL F C   1 
ATOM   9021  O O   . VAL F 2 221 ? -66.055  -0.286   -13.577 1.00 104.49 ? 223 VAL F O   1 
ATOM   9022  C CB  . VAL F 2 221 ? -64.881  -2.888   -14.656 1.00 109.49 ? 223 VAL F CB  1 
ATOM   9023  C CG1 . VAL F 2 221 ? -64.544  -3.451   -13.281 1.00 106.90 ? 223 VAL F CG1 1 
ATOM   9024  C CG2 . VAL F 2 221 ? -64.634  -3.938   -15.739 1.00 112.87 ? 223 VAL F CG2 1 
ATOM   9025  N N   . ARG F 2 222 ? -67.690  -1.655   -12.796 1.00 104.03 ? 224 ARG F N   1 
ATOM   9026  C CA  . ARG F 2 222 ? -68.239  -0.759   -11.767 1.00 101.94 ? 224 ARG F CA  1 
ATOM   9027  C C   . ARG F 2 222 ? -68.740  0.530    -12.455 1.00 105.64 ? 224 ARG F C   1 
ATOM   9028  O O   . ARG F 2 222 ? -68.506  1.650    -12.001 1.00 102.73 ? 224 ARG F O   1 
ATOM   9029  C CB  . ARG F 2 222 ? -67.270  -0.545   -10.577 1.00 99.06  ? 224 ARG F CB  1 
ATOM   9030  C CG  . ARG F 2 222 ? -67.196  -1.778   -9.658  1.00 108.73 ? 224 ARG F CG  1 
ATOM   9031  C CD  . ARG F 2 222 ? -66.467  -1.567   -8.337  1.00 110.77 ? 224 ARG F CD  1 
ATOM   9032  N NE  . ARG F 2 222 ? -67.110  -0.556   -7.496  1.00 117.84 ? 224 ARG F NE  1 
ATOM   9033  C CZ  . ARG F 2 222 ? -68.118  -0.793   -6.660  1.00 136.66 ? 224 ARG F CZ  1 
ATOM   9034  N NH1 . ARG F 2 222 ? -68.615  -2.018   -6.537  1.00 125.92 ? 224 ARG F NH1 1 
ATOM   9035  N NH2 . ARG F 2 222 ? -68.645  0.194    -5.952  1.00 126.06 ? 224 ARG F NH2 1 
ATOM   9036  N N   . ASP F 2 223 ? -69.411  0.308    -13.607 1.00 106.50 ? 225 ASP F N   1 
ATOM   9037  C CA  . ASP F 2 223 ? -69.991  1.253    -14.564 1.00 109.51 ? 225 ASP F CA  1 
ATOM   9038  C C   . ASP F 2 223 ? -69.077  2.457    -14.856 1.00 111.33 ? 225 ASP F C   1 
ATOM   9039  O O   . ASP F 2 223 ? -69.547  3.592    -14.980 1.00 111.71 ? 225 ASP F O   1 
ATOM   9040  C CB  . ASP F 2 223 ? -71.416  1.675    -14.173 1.00 114.26 ? 225 ASP F CB  1 
ATOM   9041  C CG  . ASP F 2 223 ? -72.488  0.876    -14.904 1.00 138.85 ? 225 ASP F CG  1 
ATOM   9042  O OD1 . ASP F 2 223 ? -72.656  -0.329   -14.587 1.00 142.33 ? 225 ASP F OD1 1 
ATOM   9043  O OD2 . ASP F 2 223 ? -73.154  1.452    -15.798 1.00 149.85 ? 225 ASP F OD2 1 
ATOM   9044  N N   . ARG F 2 224 ? -67.767  2.174    -15.011 1.00 105.28 ? 226 ARG F N   1 
ATOM   9045  C CA  . ARG F 2 224 ? -66.732  3.145    -15.347 1.00 102.85 ? 226 ARG F CA  1 
ATOM   9046  C C   . ARG F 2 224 ? -65.963  2.667    -16.568 1.00 108.87 ? 226 ARG F C   1 
ATOM   9047  O O   . ARG F 2 224 ? -65.446  1.544    -16.580 1.00 108.23 ? 226 ARG F O   1 
ATOM   9048  C CB  . ARG F 2 224 ? -65.782  3.395    -14.163 1.00 96.26  ? 226 ARG F CB  1 
ATOM   9049  C CG  . ARG F 2 224 ? -66.323  4.371    -13.141 1.00 97.03  ? 226 ARG F CG  1 
ATOM   9050  C CD  . ARG F 2 224 ? -66.301  5.813    -13.610 1.00 106.25 ? 226 ARG F CD  1 
ATOM   9051  N NE  . ARG F 2 224 ? -67.423  6.565    -13.052 1.00 116.79 ? 226 ARG F NE  1 
ATOM   9052  C CZ  . ARG F 2 224 ? -68.577  6.762    -13.680 1.00 138.10 ? 226 ARG F CZ  1 
ATOM   9053  N NH1 . ARG F 2 224 ? -68.767  6.280    -14.903 1.00 132.39 ? 226 ARG F NH1 1 
ATOM   9054  N NH2 . ARG F 2 224 ? -69.548  7.451    -13.093 1.00 126.34 ? 226 ARG F NH2 1 
ATOM   9055  N N   . GLU F 2 225 ? -65.915  3.512    -17.606 1.00 107.83 ? 227 GLU F N   1 
ATOM   9056  C CA  . GLU F 2 225 ? -65.215  3.202    -18.849 1.00 110.18 ? 227 GLU F CA  1 
ATOM   9057  C C   . GLU F 2 225 ? -63.693  3.357    -18.695 1.00 111.95 ? 227 GLU F C   1 
ATOM   9058  O O   . GLU F 2 225 ? -62.936  2.592    -19.293 1.00 113.16 ? 227 GLU F O   1 
ATOM   9059  C CB  . GLU F 2 225 ? -65.765  4.039    -20.014 1.00 115.10 ? 227 GLU F CB  1 
ATOM   9060  C CG  . GLU F 2 225 ? -67.191  3.685    -20.406 1.00 130.38 ? 227 GLU F CG  1 
ATOM   9061  C CD  . GLU F 2 225 ? -67.456  3.577    -21.897 1.00 160.23 ? 227 GLU F CD  1 
ATOM   9062  O OE1 . GLU F 2 225 ? -67.276  4.589    -22.616 1.00 160.28 ? 227 GLU F OE1 1 
ATOM   9063  O OE2 . GLU F 2 225 ? -67.865  2.481    -22.344 1.00 155.26 ? 227 GLU F OE2 1 
ATOM   9064  N N   . GLY F 2 226 ? -63.270  4.325    -17.882 1.00 105.17 ? 228 GLY F N   1 
ATOM   9065  C CA  . GLY F 2 226 ? -61.861  4.585    -17.600 1.00 102.43 ? 228 GLY F CA  1 
ATOM   9066  C C   . GLY F 2 226 ? -61.306  3.717    -16.484 1.00 101.73 ? 228 GLY F C   1 
ATOM   9067  O O   . GLY F 2 226 ? -62.045  2.950    -15.860 1.00 101.20 ? 228 GLY F O   1 
ATOM   9068  N N   . ARG F 2 227 ? -59.991  3.819    -16.233 1.00 94.79  ? 229 ARG F N   1 
ATOM   9069  C CA  . ARG F 2 227 ? -59.324  3.041    -15.189 1.00 92.11  ? 229 ARG F CA  1 
ATOM   9070  C C   . ARG F 2 227 ? -58.352  3.894    -14.372 1.00 94.24  ? 229 ARG F C   1 
ATOM   9071  O O   . ARG F 2 227 ? -57.986  4.994    -14.787 1.00 92.53  ? 229 ARG F O   1 
ATOM   9072  C CB  . ARG F 2 227 ? -58.583  1.823    -15.782 1.00 93.13  ? 229 ARG F CB  1 
ATOM   9073  C CG  . ARG F 2 227 ? -59.447  0.833    -16.564 1.00 102.05 ? 229 ARG F CG  1 
ATOM   9074  C CD  . ARG F 2 227 ? -60.134  -0.209   -15.704 1.00 102.24 ? 229 ARG F CD  1 
ATOM   9075  N NE  . ARG F 2 227 ? -60.773  -1.230   -16.539 1.00 107.04 ? 229 ARG F NE  1 
ATOM   9076  C CZ  . ARG F 2 227 ? -62.019  -1.157   -17.002 1.00 115.03 ? 229 ARG F CZ  1 
ATOM   9077  N NH1 . ARG F 2 227 ? -62.788  -0.118   -16.700 1.00 101.80 ? 229 ARG F NH1 1 
ATOM   9078  N NH2 . ARG F 2 227 ? -62.507  -2.126   -17.763 1.00 93.20  ? 229 ARG F NH2 1 
ATOM   9079  N N   . MET F 2 228 ? -57.948  3.380    -13.202 1.00 90.89  ? 230 MET F N   1 
ATOM   9080  C CA  . MET F 2 228 ? -57.007  4.042    -12.310 1.00 89.44  ? 230 MET F CA  1 
ATOM   9081  C C   . MET F 2 228 ? -55.967  3.038    -11.864 1.00 97.43  ? 230 MET F C   1 
ATOM   9082  O O   . MET F 2 228 ? -56.314  2.058    -11.209 1.00 98.08  ? 230 MET F O   1 
ATOM   9083  C CB  . MET F 2 228 ? -57.728  4.595    -11.070 1.00 89.80  ? 230 MET F CB  1 
ATOM   9084  C CG  . MET F 2 228 ? -57.852  6.094    -11.043 1.00 92.95  ? 230 MET F CG  1 
ATOM   9085  S SD  . MET F 2 228 ? -58.462  6.701    -9.443  1.00 95.38  ? 230 MET F SD  1 
ATOM   9086  C CE  . MET F 2 228 ? -59.383  8.109    -9.984  1.00 93.86  ? 230 MET F CE  1 
ATOM   9087  N N   . ASN F 2 229 ? -54.697  3.266    -12.196 1.00 96.35  ? 231 ASN F N   1 
ATOM   9088  C CA  . ASN F 2 229 ? -53.645  2.374    -11.717 1.00 97.09  ? 231 ASN F CA  1 
ATOM   9089  C C   . ASN F 2 229 ? -53.159  2.878    -10.351 1.00 100.55 ? 231 ASN F C   1 
ATOM   9090  O O   . ASN F 2 229 ? -52.991  4.088    -10.174 1.00 99.22  ? 231 ASN F O   1 
ATOM   9091  C CB  . ASN F 2 229 ? -52.506  2.258    -12.727 1.00 99.92  ? 231 ASN F CB  1 
ATOM   9092  C CG  . ASN F 2 229 ? -52.818  1.380    -13.912 1.00 136.57 ? 231 ASN F CG  1 
ATOM   9093  O OD1 . ASN F 2 229 ? -53.707  0.517    -13.877 1.00 135.70 ? 231 ASN F OD1 1 
ATOM   9094  N ND2 . ASN F 2 229 ? -52.071  1.566    -14.990 1.00 130.67 ? 231 ASN F ND2 1 
ATOM   9095  N N   . TYR F 2 230 ? -52.992  1.965    -9.377  1.00 97.07  ? 232 TYR F N   1 
ATOM   9096  C CA  . TYR F 2 230 ? -52.564  2.323    -8.025  1.00 95.00  ? 232 TYR F CA  1 
ATOM   9097  C C   . TYR F 2 230 ? -51.117  1.918    -7.796  1.00 96.94  ? 232 TYR F C   1 
ATOM   9098  O O   . TYR F 2 230 ? -50.798  0.725    -7.828  1.00 96.86  ? 232 TYR F O   1 
ATOM   9099  C CB  . TYR F 2 230 ? -53.508  1.714    -6.968  1.00 96.22  ? 232 TYR F CB  1 
ATOM   9100  C CG  . TYR F 2 230 ? -54.966  1.973    -7.270  1.00 98.77  ? 232 TYR F CG  1 
ATOM   9101  C CD1 . TYR F 2 230 ? -55.528  3.228    -7.065  1.00 100.35 ? 232 TYR F CD1 1 
ATOM   9102  C CD2 . TYR F 2 230 ? -55.775  0.976    -7.809  1.00 100.92 ? 232 TYR F CD2 1 
ATOM   9103  C CE1 . TYR F 2 230 ? -56.865  3.484    -7.377  1.00 101.94 ? 232 TYR F CE1 1 
ATOM   9104  C CE2 . TYR F 2 230 ? -57.115  1.219    -8.120  1.00 102.14 ? 232 TYR F CE2 1 
ATOM   9105  C CZ  . TYR F 2 230 ? -57.656  2.476    -7.902  1.00 106.66 ? 232 TYR F CZ  1 
ATOM   9106  O OH  . TYR F 2 230 ? -58.962  2.741    -8.229  1.00 103.35 ? 232 TYR F OH  1 
ATOM   9107  N N   . TYR F 2 231 ? -50.239  2.923    -7.599  1.00 92.38  ? 233 TYR F N   1 
ATOM   9108  C CA  . TYR F 2 231 ? -48.799  2.731    -7.375  1.00 93.08  ? 233 TYR F CA  1 
ATOM   9109  C C   . TYR F 2 231 ? -48.387  3.066    -5.941  1.00 95.47  ? 233 TYR F C   1 
ATOM   9110  O O   . TYR F 2 231 ? -49.012  3.916    -5.294  1.00 94.30  ? 233 TYR F O   1 
ATOM   9111  C CB  . TYR F 2 231 ? -47.965  3.558    -8.365  1.00 95.50  ? 233 TYR F CB  1 
ATOM   9112  C CG  . TYR F 2 231 ? -48.224  3.249    -9.822  1.00 99.88  ? 233 TYR F CG  1 
ATOM   9113  C CD1 . TYR F 2 231 ? -49.268  3.862    -10.510 1.00 101.74 ? 233 TYR F CD1 1 
ATOM   9114  C CD2 . TYR F 2 231 ? -47.378  2.408    -10.537 1.00 103.09 ? 233 TYR F CD2 1 
ATOM   9115  C CE1 . TYR F 2 231 ? -49.496  3.602    -11.858 1.00 104.27 ? 233 TYR F CE1 1 
ATOM   9116  C CE2 . TYR F 2 231 ? -47.593  2.146    -11.890 1.00 106.02 ? 233 TYR F CE2 1 
ATOM   9117  C CZ  . TYR F 2 231 ? -48.664  2.735    -12.542 1.00 113.19 ? 233 TYR F CZ  1 
ATOM   9118  O OH  . TYR F 2 231 ? -48.894  2.483    -13.873 1.00 117.73 ? 233 TYR F OH  1 
ATOM   9119  N N   . TRP F 2 232 ? -47.326  2.401    -5.448  1.00 91.96  ? 234 TRP F N   1 
ATOM   9120  C CA  . TRP F 2 232 ? -46.831  2.605    -4.088  1.00 91.02  ? 234 TRP F CA  1 
ATOM   9121  C C   . TRP F 2 232 ? -45.306  2.496    -3.964  1.00 98.07  ? 234 TRP F C   1 
ATOM   9122  O O   . TRP F 2 232 ? -44.669  1.734    -4.703  1.00 100.14 ? 234 TRP F O   1 
ATOM   9123  C CB  . TRP F 2 232 ? -47.515  1.618    -3.124  1.00 89.06  ? 234 TRP F CB  1 
ATOM   9124  C CG  . TRP F 2 232 ? -47.030  0.205    -3.256  1.00 91.16  ? 234 TRP F CG  1 
ATOM   9125  C CD1 . TRP F 2 232 ? -47.500  -0.749   -4.109  1.00 95.08  ? 234 TRP F CD1 1 
ATOM   9126  C CD2 . TRP F 2 232 ? -45.950  -0.395   -2.535  1.00 92.42  ? 234 TRP F CD2 1 
ATOM   9127  N NE1 . TRP F 2 232 ? -46.788  -1.912   -3.954  1.00 96.62  ? 234 TRP F NE1 1 
ATOM   9128  C CE2 . TRP F 2 232 ? -45.820  -1.719   -3.004  1.00 98.42  ? 234 TRP F CE2 1 
ATOM   9129  C CE3 . TRP F 2 232 ? -45.060  0.065    -1.549  1.00 93.57  ? 234 TRP F CE3 1 
ATOM   9130  C CZ2 . TRP F 2 232 ? -44.862  -2.599   -2.493  1.00 100.05 ? 234 TRP F CZ2 1 
ATOM   9131  C CZ3 . TRP F 2 232 ? -44.121  -0.809   -1.037  1.00 97.16  ? 234 TRP F CZ3 1 
ATOM   9132  C CH2 . TRP F 2 232 ? -44.022  -2.122   -1.512  1.00 99.92  ? 234 TRP F CH2 1 
ATOM   9133  N N   . THR F 2 233 ? -44.740  3.212    -2.973  1.00 94.49  ? 235 THR F N   1 
ATOM   9134  C CA  . THR F 2 233 ? -43.320  3.173    -2.627  1.00 96.19  ? 235 THR F CA  1 
ATOM   9135  C C   . THR F 2 233 ? -43.085  3.493    -1.154  1.00 100.55 ? 235 THR F C   1 
ATOM   9136  O O   . THR F 2 233 ? -43.942  4.074    -0.486  1.00 98.98  ? 235 THR F O   1 
ATOM   9137  C CB  . THR F 2 233 ? -42.445  4.037    -3.558  1.00 105.45 ? 235 THR F CB  1 
ATOM   9138  O OG1 . THR F 2 233 ? -41.077  3.678    -3.347  1.00 105.25 ? 235 THR F OG1 1 
ATOM   9139  C CG2 . THR F 2 233 ? -42.609  5.527    -3.309  1.00 104.71 ? 235 THR F CG2 1 
ATOM   9140  N N   . LEU F 2 234 ? -41.899  3.123    -0.668  1.00 99.33  ? 236 LEU F N   1 
ATOM   9141  C CA  . LEU F 2 234 ? -41.448  3.385    0.691   1.00 99.86  ? 236 LEU F CA  1 
ATOM   9142  C C   . LEU F 2 234 ? -40.351  4.437    0.614   1.00 104.89 ? 236 LEU F C   1 
ATOM   9143  O O   . LEU F 2 234 ? -39.510  4.396    -0.287  1.00 106.65 ? 236 LEU F O   1 
ATOM   9144  C CB  . LEU F 2 234 ? -40.914  2.107    1.360   1.00 101.85 ? 236 LEU F CB  1 
ATOM   9145  C CG  . LEU F 2 234 ? -41.773  0.851    1.227   1.00 106.12 ? 236 LEU F CG  1 
ATOM   9146  C CD1 . LEU F 2 234 ? -40.973  -0.389   1.567   1.00 109.19 ? 236 LEU F CD1 1 
ATOM   9147  C CD2 . LEU F 2 234 ? -43.049  0.950    2.054   1.00 106.44 ? 236 LEU F CD2 1 
ATOM   9148  N N   . VAL F 2 235 ? -40.391  5.409    1.516   1.00 99.41  ? 237 VAL F N   1 
ATOM   9149  C CA  . VAL F 2 235 ? -39.398  6.469    1.554   1.00 99.47  ? 237 VAL F CA  1 
ATOM   9150  C C   . VAL F 2 235 ? -38.617  6.311    2.842   1.00 107.41 ? 237 VAL F C   1 
ATOM   9151  O O   . VAL F 2 235 ? -39.193  6.291    3.928   1.00 107.71 ? 237 VAL F O   1 
ATOM   9152  C CB  . VAL F 2 235 ? -40.013  7.876    1.373   1.00 100.78 ? 237 VAL F CB  1 
ATOM   9153  C CG1 . VAL F 2 235 ? -38.973  8.971    1.575   1.00 101.99 ? 237 VAL F CG1 1 
ATOM   9154  C CG2 . VAL F 2 235 ? -40.664  8.005    0.004   1.00 98.86  ? 237 VAL F CG2 1 
ATOM   9155  N N   . GLU F 2 236 ? -37.310  6.135    2.707   1.00 107.20 ? 238 GLU F N   1 
ATOM   9156  C CA  . GLU F 2 236 ? -36.390  5.969    3.824   1.00 110.38 ? 238 GLU F CA  1 
ATOM   9157  C C   . GLU F 2 236 ? -36.311  7.305    4.596   1.00 115.71 ? 238 GLU F C   1 
ATOM   9158  O O   . GLU F 2 236 ? -36.501  8.353    3.974   1.00 114.05 ? 238 GLU F O   1 
ATOM   9159  C CB  . GLU F 2 236 ? -34.991  5.575    3.292   1.00 114.45 ? 238 GLU F CB  1 
ATOM   9160  C CG  . GLU F 2 236 ? -34.963  4.351    2.383   1.00 123.59 ? 238 GLU F CG  1 
ATOM   9161  C CD  . GLU F 2 236 ? -34.569  4.619    0.941   1.00 138.98 ? 238 GLU F CD  1 
ATOM   9162  O OE1 . GLU F 2 236 ? -33.583  4.005    0.474   1.00 140.50 ? 238 GLU F OE1 1 
ATOM   9163  O OE2 . GLU F 2 236 ? -35.250  5.427    0.271   1.00 125.57 ? 238 GLU F OE2 1 
ATOM   9164  N N   . PRO F 2 237 ? -36.057  7.311    5.928   1.00 115.52 ? 239 PRO F N   1 
ATOM   9165  C CA  . PRO F 2 237 ? -35.954  8.592    6.653   1.00 116.54 ? 239 PRO F CA  1 
ATOM   9166  C C   . PRO F 2 237 ? -34.878  9.517    6.089   1.00 121.16 ? 239 PRO F C   1 
ATOM   9167  O O   . PRO F 2 237 ? -33.768  9.065    5.807   1.00 122.41 ? 239 PRO F O   1 
ATOM   9168  C CB  . PRO F 2 237 ? -35.629  8.167    8.089   1.00 121.36 ? 239 PRO F CB  1 
ATOM   9169  C CG  . PRO F 2 237 ? -35.061  6.794    7.969   1.00 127.38 ? 239 PRO F CG  1 
ATOM   9170  C CD  . PRO F 2 237 ? -35.820  6.171    6.837   1.00 119.85 ? 239 PRO F CD  1 
ATOM   9171  N N   . GLY F 2 238 ? -35.241  10.786   5.898   1.00 116.97 ? 240 GLY F N   1 
ATOM   9172  C CA  . GLY F 2 238 ? -34.358  11.819   5.359   1.00 118.06 ? 240 GLY F CA  1 
ATOM   9173  C C   . GLY F 2 238 ? -34.537  12.086   3.877   1.00 118.57 ? 240 GLY F C   1 
ATOM   9174  O O   . GLY F 2 238 ? -34.292  13.203   3.413   1.00 119.22 ? 240 GLY F O   1 
ATOM   9175  N N   . ASP F 2 239 ? -34.962  11.050   3.126   1.00 111.30 ? 241 ASP F N   1 
ATOM   9176  C CA  . ASP F 2 239 ? -35.194  11.082   1.682   1.00 108.45 ? 241 ASP F CA  1 
ATOM   9177  C C   . ASP F 2 239 ? -36.459  11.882   1.319   1.00 108.48 ? 241 ASP F C   1 
ATOM   9178  O O   . ASP F 2 239 ? -37.415  11.930   2.100   1.00 107.31 ? 241 ASP F O   1 
ATOM   9179  C CB  . ASP F 2 239 ? -35.245  9.639    1.140   1.00 109.23 ? 241 ASP F CB  1 
ATOM   9180  C CG  . ASP F 2 239 ? -35.361  9.472    -0.362  1.00 117.62 ? 241 ASP F CG  1 
ATOM   9181  O OD1 . ASP F 2 239 ? -34.990  10.410   -1.099  1.00 118.04 ? 241 ASP F OD1 1 
ATOM   9182  O OD2 . ASP F 2 239 ? -35.780  8.387    -0.803  1.00 125.55 ? 241 ASP F OD2 1 
ATOM   9183  N N   . LYS F 2 240 ? -36.443  12.518   0.131   1.00 103.67 ? 242 LYS F N   1 
ATOM   9184  C CA  . LYS F 2 240 ? -37.530  13.350   -0.393  1.00 101.85 ? 242 LYS F CA  1 
ATOM   9185  C C   . LYS F 2 240 ? -38.250  12.715   -1.586  1.00 103.38 ? 242 LYS F C   1 
ATOM   9186  O O   . LYS F 2 240 ? -37.610  12.315   -2.560  1.00 104.22 ? 242 LYS F O   1 
ATOM   9187  C CB  . LYS F 2 240 ? -37.008  14.757   -0.760  1.00 106.48 ? 242 LYS F CB  1 
ATOM   9188  C CG  . LYS F 2 240 ? -38.051  15.708   -1.357  1.00 116.83 ? 242 LYS F CG  1 
ATOM   9189  C CD  . LYS F 2 240 ? -37.437  16.620   -2.408  1.00 125.79 ? 242 LYS F CD  1 
ATOM   9190  C CE  . LYS F 2 240 ? -37.282  18.035   -1.910  1.00 141.09 ? 242 LYS F CE  1 
ATOM   9191  N NZ  . LYS F 2 240 ? -36.587  18.896   -2.901  1.00 154.04 ? 242 LYS F NZ  1 
ATOM   9192  N N   . ILE F 2 241 ? -39.584  12.667   -1.519  1.00 96.89  ? 243 ILE F N   1 
ATOM   9193  C CA  . ILE F 2 241 ? -40.418  12.153   -2.596  1.00 94.86  ? 243 ILE F CA  1 
ATOM   9194  C C   . ILE F 2 241 ? -41.122  13.332   -3.293  1.00 99.64  ? 243 ILE F C   1 
ATOM   9195  O O   . ILE F 2 241 ? -41.881  14.065   -2.653  1.00 99.25  ? 243 ILE F O   1 
ATOM   9196  C CB  . ILE F 2 241 ? -41.356  10.994   -2.145  1.00 95.88  ? 243 ILE F CB  1 
ATOM   9197  C CG1 . ILE F 2 241 ? -42.196  10.454   -3.333  1.00 94.77  ? 243 ILE F CG1 1 
ATOM   9198  C CG2 . ILE F 2 241 ? -42.221  11.364   -0.916  1.00 95.52  ? 243 ILE F CG2 1 
ATOM   9199  C CD1 . ILE F 2 241 ? -42.935  9.159    -3.084  1.00 99.24  ? 243 ILE F CD1 1 
ATOM   9200  N N   . THR F 2 242 ? -40.807  13.542   -4.586  1.00 96.77  ? 244 THR F N   1 
ATOM   9201  C CA  . THR F 2 242 ? -41.345  14.623   -5.418  1.00 96.81  ? 244 THR F CA  1 
ATOM   9202  C C   . THR F 2 242 ? -42.484  14.093   -6.280  1.00 101.33 ? 244 THR F C   1 
ATOM   9203  O O   . THR F 2 242 ? -42.466  12.926   -6.671  1.00 100.24 ? 244 THR F O   1 
ATOM   9204  C CB  . THR F 2 242 ? -40.206  15.284   -6.220  1.00 98.72  ? 244 THR F CB  1 
ATOM   9205  O OG1 . THR F 2 242 ? -39.214  15.740   -5.305  1.00 98.72  ? 244 THR F OG1 1 
ATOM   9206  C CG2 . THR F 2 242 ? -40.669  16.464   -7.076  1.00 95.73  ? 244 THR F CG2 1 
ATOM   9207  N N   . PHE F 2 243 ? -43.481  14.949   -6.554  1.00 99.66  ? 245 PHE F N   1 
ATOM   9208  C CA  . PHE F 2 243 ? -44.645  14.616   -7.365  1.00 99.36  ? 245 PHE F CA  1 
ATOM   9209  C C   . PHE F 2 243 ? -44.892  15.654   -8.461  1.00 105.15 ? 245 PHE F C   1 
ATOM   9210  O O   . PHE F 2 243 ? -45.601  16.637   -8.233  1.00 105.39 ? 245 PHE F O   1 
ATOM   9211  C CB  . PHE F 2 243 ? -45.883  14.449   -6.477  1.00 100.05 ? 245 PHE F CB  1 
ATOM   9212  C CG  . PHE F 2 243 ? -46.065  13.068   -5.900  1.00 100.62 ? 245 PHE F CG  1 
ATOM   9213  C CD1 . PHE F 2 243 ? -45.329  12.654   -4.796  1.00 103.83 ? 245 PHE F CD1 1 
ATOM   9214  C CD2 . PHE F 2 243 ? -47.018  12.200   -6.423  1.00 102.40 ? 245 PHE F CD2 1 
ATOM   9215  C CE1 . PHE F 2 243 ? -45.521  11.387   -4.246  1.00 103.89 ? 245 PHE F CE1 1 
ATOM   9216  C CE2 . PHE F 2 243 ? -47.212  10.933   -5.869  1.00 104.44 ? 245 PHE F CE2 1 
ATOM   9217  C CZ  . PHE F 2 243 ? -46.455  10.531   -4.790  1.00 102.42 ? 245 PHE F CZ  1 
ATOM   9218  N N   . GLU F 2 244 ? -44.307  15.426   -9.650  1.00 102.91 ? 246 GLU F N   1 
ATOM   9219  C CA  . GLU F 2 244 ? -44.464  16.293   -10.819 1.00 104.94 ? 246 GLU F CA  1 
ATOM   9220  C C   . GLU F 2 244 ? -45.656  15.834   -11.666 1.00 107.56 ? 246 GLU F C   1 
ATOM   9221  O O   . GLU F 2 244 ? -45.712  14.660   -12.025 1.00 105.85 ? 246 GLU F O   1 
ATOM   9222  C CB  . GLU F 2 244 ? -43.171  16.317   -11.653 1.00 108.57 ? 246 GLU F CB  1 
ATOM   9223  C CG  . GLU F 2 244 ? -42.209  17.408   -11.212 1.00 122.25 ? 246 GLU F CG  1 
ATOM   9224  C CD  . GLU F 2 244 ? -40.871  17.484   -11.923 1.00 145.75 ? 246 GLU F CD  1 
ATOM   9225  O OE1 . GLU F 2 244 ? -40.825  17.230   -13.149 1.00 148.65 ? 246 GLU F OE1 1 
ATOM   9226  O OE2 . GLU F 2 244 ? -39.873  17.850   -11.260 1.00 136.29 ? 246 GLU F OE2 1 
ATOM   9227  N N   . ALA F 2 245 ? -46.622  16.742   -11.959 1.00 104.89 ? 247 ALA F N   1 
ATOM   9228  C CA  . ALA F 2 245 ? -47.808  16.402   -12.761 1.00 104.70 ? 247 ALA F CA  1 
ATOM   9229  C C   . ALA F 2 245 ? -48.439  17.577   -13.494 1.00 110.79 ? 247 ALA F C   1 
ATOM   9230  O O   . ALA F 2 245 ? -48.463  18.696   -12.981 1.00 110.60 ? 247 ALA F O   1 
ATOM   9231  C CB  . ALA F 2 245 ? -48.859  15.711   -11.902 1.00 103.02 ? 247 ALA F CB  1 
ATOM   9232  N N   . THR F 2 246 ? -48.980  17.294   -14.692 1.00 109.19 ? 248 THR F N   1 
ATOM   9233  C CA  . THR F 2 246 ? -49.706  18.234   -15.554 1.00 111.71 ? 248 THR F CA  1 
ATOM   9234  C C   . THR F 2 246 ? -51.101  17.672   -15.856 1.00 114.93 ? 248 THR F C   1 
ATOM   9235  O O   . THR F 2 246 ? -51.831  18.223   -16.684 1.00 117.61 ? 248 THR F O   1 
ATOM   9236  C CB  . THR F 2 246 ? -48.913  18.567   -16.824 1.00 123.74 ? 248 THR F CB  1 
ATOM   9237  O OG1 . THR F 2 246 ? -48.524  17.359   -17.480 1.00 124.94 ? 248 THR F OG1 1 
ATOM   9238  C CG2 . THR F 2 246 ? -47.711  19.456   -16.550 1.00 123.03 ? 248 THR F CG2 1 
ATOM   9239  N N   . GLY F 2 247 ? -51.463  16.613   -15.129 1.00 107.43 ? 249 GLY F N   1 
ATOM   9240  C CA  . GLY F 2 247 ? -52.747  15.931   -15.229 1.00 105.87 ? 249 GLY F CA  1 
ATOM   9241  C C   . GLY F 2 247 ? -52.672  14.464   -14.876 1.00 105.85 ? 249 GLY F C   1 
ATOM   9242  O O   . GLY F 2 247 ? -51.579  13.908   -14.726 1.00 105.09 ? 249 GLY F O   1 
ATOM   9243  N N   . ASN F 2 248 ? -53.854  13.842   -14.703 1.00 99.54  ? 250 ASN F N   1 
ATOM   9244  C CA  . ASN F 2 248 ? -54.091  12.418   -14.428 1.00 96.43  ? 250 ASN F CA  1 
ATOM   9245  C C   . ASN F 2 248 ? -53.637  11.911   -13.059 1.00 94.62  ? 250 ASN F C   1 
ATOM   9246  O O   . ASN F 2 248 ? -54.014  10.795   -12.694 1.00 93.39  ? 250 ASN F O   1 
ATOM   9247  C CB  . ASN F 2 248 ? -53.493  11.547   -15.532 1.00 98.38  ? 250 ASN F CB  1 
ATOM   9248  C CG  . ASN F 2 248 ? -54.041  11.911   -16.880 1.00 131.75 ? 250 ASN F CG  1 
ATOM   9249  O OD1 . ASN F 2 248 ? -53.480  12.738   -17.602 1.00 127.14 ? 250 ASN F OD1 1 
ATOM   9250  N ND2 . ASN F 2 248 ? -55.208  11.384   -17.195 1.00 127.99 ? 250 ASN F ND2 1 
ATOM   9251  N N   . LEU F 2 249 ? -52.866  12.701   -12.294 1.00 87.84  ? 251 LEU F N   1 
ATOM   9252  C CA  . LEU F 2 249 ? -52.391  12.246   -10.992 1.00 84.68  ? 251 LEU F CA  1 
ATOM   9253  C C   . LEU F 2 249 ? -53.463  12.332   -9.944  1.00 87.45  ? 251 LEU F C   1 
ATOM   9254  O O   . LEU F 2 249 ? -54.213  13.312   -9.916  1.00 88.12  ? 251 LEU F O   1 
ATOM   9255  C CB  . LEU F 2 249 ? -51.108  12.987   -10.546 1.00 84.68  ? 251 LEU F CB  1 
ATOM   9256  C CG  . LEU F 2 249 ? -50.472  12.654   -9.164  1.00 87.34  ? 251 LEU F CG  1 
ATOM   9257  C CD1 . LEU F 2 249 ? -50.056  11.194   -9.045  1.00 86.07  ? 251 LEU F CD1 1 
ATOM   9258  C CD2 . LEU F 2 249 ? -49.275  13.526   -8.901  1.00 91.12  ? 251 LEU F CD2 1 
ATOM   9259  N N   . VAL F 2 250 ? -53.550  11.267   -9.112  1.00 82.94  ? 252 VAL F N   1 
ATOM   9260  C CA  . VAL F 2 250 ? -54.424  11.114   -7.944  1.00 81.71  ? 252 VAL F CA  1 
ATOM   9261  C C   . VAL F 2 250 ? -53.444  11.169   -6.751  1.00 84.98  ? 252 VAL F C   1 
ATOM   9262  O O   . VAL F 2 250 ? -52.910  10.144   -6.301  1.00 83.44  ? 252 VAL F O   1 
ATOM   9263  C CB  . VAL F 2 250 ? -55.290  9.825    -7.973  1.00 84.64  ? 252 VAL F CB  1 
ATOM   9264  C CG1 . VAL F 2 250 ? -56.270  9.811    -6.821  1.00 83.88  ? 252 VAL F CG1 1 
ATOM   9265  C CG2 . VAL F 2 250 ? -56.038  9.677    -9.290  1.00 85.70  ? 252 VAL F CG2 1 
ATOM   9266  N N   . VAL F 2 251 ? -53.143  12.410   -6.331  1.00 82.21  ? 253 VAL F N   1 
ATOM   9267  C CA  . VAL F 2 251 ? -52.176  12.790   -5.292  1.00 81.61  ? 253 VAL F CA  1 
ATOM   9268  C C   . VAL F 2 251 ? -52.419  12.129   -3.922  1.00 83.80  ? 253 VAL F C   1 
ATOM   9269  O O   . VAL F 2 251 ? -53.576  11.927   -3.566  1.00 82.75  ? 253 VAL F O   1 
ATOM   9270  C CB  . VAL F 2 251 ? -52.079  14.335   -5.144  1.00 86.94  ? 253 VAL F CB  1 
ATOM   9271  C CG1 . VAL F 2 251 ? -51.555  14.992   -6.412  1.00 88.10  ? 253 VAL F CG1 1 
ATOM   9272  C CG2 . VAL F 2 251 ? -53.404  14.956   -4.715  1.00 87.56  ? 253 VAL F CG2 1 
ATOM   9273  N N   . PRO F 2 252 ? -51.370  11.855   -3.105  1.00 80.38  ? 254 PRO F N   1 
ATOM   9274  C CA  . PRO F 2 252 ? -51.624  11.304   -1.770  1.00 80.14  ? 254 PRO F CA  1 
ATOM   9275  C C   . PRO F 2 252 ? -52.113  12.376   -0.783  1.00 87.20  ? 254 PRO F C   1 
ATOM   9276  O O   . PRO F 2 252 ? -51.721  13.543   -0.872  1.00 88.25  ? 254 PRO F O   1 
ATOM   9277  C CB  . PRO F 2 252 ? -50.253  10.749   -1.344  1.00 81.65  ? 254 PRO F CB  1 
ATOM   9278  C CG  . PRO F 2 252 ? -49.348  10.905   -2.530  1.00 86.24  ? 254 PRO F CG  1 
ATOM   9279  C CD  . PRO F 2 252 ? -49.920  12.013   -3.333  1.00 82.56  ? 254 PRO F CD  1 
ATOM   9280  N N   . ARG F 2 253 ? -52.993  11.975   0.143   1.00 85.00  ? 255 ARG F N   1 
ATOM   9281  C CA  . ARG F 2 253 ? -53.490  12.818   1.226   1.00 87.08  ? 255 ARG F CA  1 
ATOM   9282  C C   . ARG F 2 253 ? -52.848  12.274   2.491   1.00 95.03  ? 255 ARG F C   1 
ATOM   9283  O O   . ARG F 2 253 ? -52.170  13.021   3.193   1.00 96.57  ? 255 ARG F O   1 
ATOM   9284  C CB  . ARG F 2 253 ? -55.025  12.777   1.343   1.00 86.38  ? 255 ARG F CB  1 
ATOM   9285  C CG  . ARG F 2 253 ? -55.575  13.764   2.379   1.00 91.39  ? 255 ARG F CG  1 
ATOM   9286  C CD  . ARG F 2 253 ? -57.082  13.879   2.332   1.00 89.80  ? 255 ARG F CD  1 
ATOM   9287  N NE  . ARG F 2 253 ? -57.599  14.641   3.469   1.00 95.15  ? 255 ARG F NE  1 
ATOM   9288  C CZ  . ARG F 2 253 ? -58.866  14.622   3.872   1.00 111.07 ? 255 ARG F CZ  1 
ATOM   9289  N NH1 . ARG F 2 253 ? -59.763  13.880   3.233   1.00 101.04 ? 255 ARG F NH1 1 
ATOM   9290  N NH2 . ARG F 2 253 ? -59.246  15.339   4.921   1.00 97.78  ? 255 ARG F NH2 1 
ATOM   9291  N N   . TYR F 2 254 ? -53.038  10.965   2.760   1.00 92.43  ? 256 TYR F N   1 
ATOM   9292  C CA  . TYR F 2 254 ? -52.464  10.292   3.918   1.00 93.81  ? 256 TYR F CA  1 
ATOM   9293  C C   . TYR F 2 254 ? -51.395  9.281    3.521   1.00 98.47  ? 256 TYR F C   1 
ATOM   9294  O O   . TYR F 2 254 ? -51.579  8.535    2.557   1.00 98.07  ? 256 TYR F O   1 
ATOM   9295  C CB  . TYR F 2 254 ? -53.546  9.605    4.757   1.00 95.74  ? 256 TYR F CB  1 
ATOM   9296  C CG  . TYR F 2 254 ? -54.534  10.556   5.391   1.00 99.84  ? 256 TYR F CG  1 
ATOM   9297  C CD1 . TYR F 2 254 ? -55.747  10.846   4.773   1.00 102.25 ? 256 TYR F CD1 1 
ATOM   9298  C CD2 . TYR F 2 254 ? -54.281  11.127   6.634   1.00 102.46 ? 256 TYR F CD2 1 
ATOM   9299  C CE1 . TYR F 2 254 ? -56.675  11.702   5.365   1.00 105.33 ? 256 TYR F CE1 1 
ATOM   9300  C CE2 . TYR F 2 254 ? -55.205  11.980   7.240   1.00 105.34 ? 256 TYR F CE2 1 
ATOM   9301  C CZ  . TYR F 2 254 ? -56.400  12.269   6.598   1.00 113.21 ? 256 TYR F CZ  1 
ATOM   9302  O OH  . TYR F 2 254 ? -57.317  13.110   7.185   1.00 115.61 ? 256 TYR F OH  1 
ATOM   9303  N N   . ALA F 2 255 ? -50.273  9.267    4.271   1.00 94.99  ? 257 ALA F N   1 
ATOM   9304  C CA  . ALA F 2 255 ? -49.155  8.331    4.109   1.00 93.58  ? 257 ALA F CA  1 
ATOM   9305  C C   . ALA F 2 255 ? -48.971  7.558    5.414   1.00 96.47  ? 257 ALA F C   1 
ATOM   9306  O O   . ALA F 2 255 ? -49.605  7.899    6.419   1.00 96.92  ? 257 ALA F O   1 
ATOM   9307  C CB  . ALA F 2 255 ? -47.882  9.073    3.748   1.00 94.83  ? 257 ALA F CB  1 
ATOM   9308  N N   . PHE F 2 256 ? -48.126  6.511    5.409   1.00 91.92  ? 258 PHE F N   1 
ATOM   9309  C CA  . PHE F 2 256 ? -47.956  5.700    6.608   1.00 92.76  ? 258 PHE F CA  1 
ATOM   9310  C C   . PHE F 2 256 ? -46.514  5.521    7.042   1.00 97.87  ? 258 PHE F C   1 
ATOM   9311  O O   . PHE F 2 256 ? -45.756  4.779    6.414   1.00 97.57  ? 258 PHE F O   1 
ATOM   9312  C CB  . PHE F 2 256 ? -48.660  4.347    6.455   1.00 94.13  ? 258 PHE F CB  1 
ATOM   9313  C CG  . PHE F 2 256 ? -50.034  4.431    5.825   1.00 94.13  ? 258 PHE F CG  1 
ATOM   9314  C CD1 . PHE F 2 256 ? -51.128  4.875    6.559   1.00 97.77  ? 258 PHE F CD1 1 
ATOM   9315  C CD2 . PHE F 2 256 ? -50.229  4.091    4.489   1.00 94.42  ? 258 PHE F CD2 1 
ATOM   9316  C CE1 . PHE F 2 256 ? -52.392  4.964    5.971   1.00 97.61  ? 258 PHE F CE1 1 
ATOM   9317  C CE2 . PHE F 2 256 ? -51.493  4.187    3.902   1.00 96.12  ? 258 PHE F CE2 1 
ATOM   9318  C CZ  . PHE F 2 256 ? -52.565  4.617    4.647   1.00 94.97  ? 258 PHE F CZ  1 
ATOM   9319  N N   . ALA F 2 257 ? -46.148  6.212    8.136   1.00 96.48  ? 259 ALA F N   1 
ATOM   9320  C CA  . ALA F 2 257 ? -44.835  6.135    8.774   1.00 99.16  ? 259 ALA F CA  1 
ATOM   9321  C C   . ALA F 2 257 ? -44.847  4.845    9.584   1.00 105.69 ? 259 ALA F C   1 
ATOM   9322  O O   . ALA F 2 257 ? -45.436  4.783    10.665  1.00 106.82 ? 259 ALA F O   1 
ATOM   9323  C CB  . ALA F 2 257 ? -44.617  7.336    9.683   1.00 101.68 ? 259 ALA F CB  1 
ATOM   9324  N N   . MET F 2 258 ? -44.259  3.796    9.018   1.00 102.94 ? 260 MET F N   1 
ATOM   9325  C CA  . MET F 2 258 ? -44.278  2.468    9.606   1.00 104.64 ? 260 MET F CA  1 
ATOM   9326  C C   . MET F 2 258 ? -42.919  1.893    9.976   1.00 113.98 ? 260 MET F C   1 
ATOM   9327  O O   . MET F 2 258 ? -41.907  2.155    9.317   1.00 114.28 ? 260 MET F O   1 
ATOM   9328  C CB  . MET F 2 258 ? -45.021  1.499    8.686   1.00 105.13 ? 260 MET F CB  1 
ATOM   9329  C CG  . MET F 2 258 ? -44.513  1.525    7.267   1.00 107.26 ? 260 MET F CG  1 
ATOM   9330  S SD  . MET F 2 258 ? -44.824  -0.005   6.405   1.00 111.92 ? 260 MET F SD  1 
ATOM   9331  C CE  . MET F 2 258 ? -46.415  0.311    5.789   1.00 105.97 ? 260 MET F CE  1 
ATOM   9332  N N   . GLU F 2 259 ? -42.931  1.062    11.025  1.00 114.07 ? 261 GLU F N   1 
ATOM   9333  C CA  . GLU F 2 259 ? -41.790  0.334    11.573  1.00 117.34 ? 261 GLU F CA  1 
ATOM   9334  C C   . GLU F 2 259 ? -42.160  -1.146   11.411  1.00 122.43 ? 261 GLU F C   1 
ATOM   9335  O O   . GLU F 2 259 ? -43.106  -1.624   12.046  1.00 122.53 ? 261 GLU F O   1 
ATOM   9336  C CB  . GLU F 2 259 ? -41.607  0.713    13.054  1.00 121.40 ? 261 GLU F CB  1 
ATOM   9337  C CG  . GLU F 2 259 ? -40.265  0.341    13.651  1.00 133.02 ? 261 GLU F CG  1 
ATOM   9338  C CD  . GLU F 2 259 ? -40.193  0.547    15.151  1.00 152.85 ? 261 GLU F CD  1 
ATOM   9339  O OE1 . GLU F 2 259 ? -40.495  1.670    15.620  1.00 141.33 ? 261 GLU F OE1 1 
ATOM   9340  O OE2 . GLU F 2 259 ? -39.833  -0.419   15.861  1.00 147.96 ? 261 GLU F OE2 1 
ATOM   9341  N N   . ARG F 2 260 ? -41.478  -1.841   10.496  1.00 130.99 ? 262 ARG F N   1 
ATOM   9342  C CA  . ARG F 2 260 ? -41.780  -3.238   10.207  1.00 128.21 ? 262 ARG F CA  1 
ATOM   9343  C C   . ARG F 2 260 ? -41.310  -4.219   11.270  1.00 134.55 ? 262 ARG F C   1 
ATOM   9344  O O   . ARG F 2 260 ? -40.243  -4.046   11.856  1.00 137.67 ? 262 ARG F O   1 
ATOM   9345  C CB  . ARG F 2 260 ? -41.218  -3.644   8.841   1.00 128.40 ? 262 ARG F CB  1 
ATOM   9346  C CG  . ARG F 2 260 ? -42.190  -3.457   7.688   1.00 132.88 ? 262 ARG F CG  1 
ATOM   9347  C CD  . ARG F 2 260 ? -41.830  -4.342   6.505   1.00 134.74 ? 262 ARG F CD  1 
ATOM   9348  N NE  . ARG F 2 260 ? -40.700  -3.826   5.730   1.00 140.99 ? 262 ARG F NE  1 
ATOM   9349  C CZ  . ARG F 2 260 ? -40.810  -2.959   4.729   1.00 153.26 ? 262 ARG F CZ  1 
ATOM   9350  N NH1 . ARG F 2 260 ? -42.001  -2.490   4.375   1.00 134.61 ? 262 ARG F NH1 1 
ATOM   9351  N NH2 . ARG F 2 260 ? -39.731  -2.552   4.076   1.00 144.65 ? 262 ARG F NH2 1 
ATOM   9352  N N   . ASN F 2 261 ? -42.118  -5.262   11.498  1.00 129.56 ? 263 ASN F N   1 
ATOM   9353  C CA  . ASN F 2 261 ? -41.824  -6.384   12.388  1.00 129.54 ? 263 ASN F CA  1 
ATOM   9354  C C   . ASN F 2 261 ? -41.467  -7.560   11.454  1.00 134.16 ? 263 ASN F C   1 
ATOM   9355  O O   . ASN F 2 261 ? -41.653  -7.434   10.239  1.00 133.03 ? 263 ASN F O   1 
ATOM   9356  C CB  . ASN F 2 261 ? -43.049  -6.707   13.270  1.00 128.45 ? 263 ASN F CB  1 
ATOM   9357  C CG  . ASN F 2 261 ? -42.830  -7.764   14.336  1.00 159.84 ? 263 ASN F CG  1 
ATOM   9358  O OD1 . ASN F 2 261 ? -43.372  -8.877   14.266  1.00 151.92 ? 263 ASN F OD1 1 
ATOM   9359  N ND2 . ASN F 2 261 ? -42.051  -7.435   15.364  1.00 157.49 ? 263 ASN F ND2 1 
ATOM   9360  N N   . ALA F 2 262 ? -40.905  -8.664   12.004  1.00 132.24 ? 264 ALA F N   1 
ATOM   9361  C CA  . ALA F 2 262 ? -40.509  -9.876   11.274  1.00 131.74 ? 264 ALA F CA  1 
ATOM   9362  C C   . ALA F 2 262 ? -41.595  -10.292  10.285  1.00 132.92 ? 264 ALA F C   1 
ATOM   9363  O O   . ALA F 2 262 ? -42.599  -10.888  10.686  1.00 130.01 ? 264 ALA F O   1 
ATOM   9364  C CB  . ALA F 2 262 ? -40.224  -11.004  12.258  1.00 132.05 ? 264 ALA F CB  1 
ATOM   9365  N N   . GLY F 2 263 ? -41.404  -9.903   9.022   1.00 130.97 ? 265 GLY F N   1 
ATOM   9366  C CA  . GLY F 2 263 ? -42.344  -10.140  7.928   1.00 129.26 ? 265 GLY F CA  1 
ATOM   9367  C C   . GLY F 2 263 ? -42.721  -11.592  7.710   1.00 131.23 ? 265 GLY F C   1 
ATOM   9368  O O   . GLY F 2 263 ? -42.074  -12.286  6.918   1.00 131.92 ? 265 GLY F O   1 
ATOM   9369  N N   . SER F 2 264 ? -43.773  -12.063  8.417   1.00 124.85 ? 266 SER F N   1 
ATOM   9370  C CA  . SER F 2 264 ? -44.235  -13.448  8.316   1.00 122.20 ? 266 SER F CA  1 
ATOM   9371  C C   . SER F 2 264 ? -45.352  -13.620  7.243   1.00 124.00 ? 266 SER F C   1 
ATOM   9372  O O   . SER F 2 264 ? -45.017  -13.704  6.060   1.00 125.48 ? 266 SER F O   1 
ATOM   9373  C CB  . SER F 2 264 ? -44.610  -14.018  9.685   1.00 123.53 ? 266 SER F CB  1 
ATOM   9374  O OG  . SER F 2 264 ? -43.499  -14.653  10.306  1.00 129.04 ? 266 SER F OG  1 
ATOM   9375  N N   . GLY F 2 265 A -46.630  -13.652  7.625   1.00 116.93 ? 266 GLY F N   1 
ATOM   9376  C CA  . GLY F 2 265 A -47.680  -13.860  6.634   1.00 115.17 ? 266 GLY F CA  1 
ATOM   9377  C C   . GLY F 2 265 A -49.016  -13.184  6.849   1.00 116.61 ? 266 GLY F C   1 
ATOM   9378  O O   . GLY F 2 265 A -49.231  -12.484  7.847   1.00 116.34 ? 266 GLY F O   1 
ATOM   9379  N N   . ILE F 2 266 ? -49.924  -13.415  5.874   1.00 110.77 ? 267 ILE F N   1 
ATOM   9380  C CA  . ILE F 2 266 ? -51.297  -12.907  5.818   1.00 108.96 ? 267 ILE F CA  1 
ATOM   9381  C C   . ILE F 2 266 ? -52.236  -14.101  5.863   1.00 108.06 ? 267 ILE F C   1 
ATOM   9382  O O   . ILE F 2 266 ? -52.182  -14.977  4.991   1.00 107.51 ? 267 ILE F O   1 
ATOM   9383  C CB  . ILE F 2 266 ? -51.580  -12.022  4.569   1.00 113.78 ? 267 ILE F CB  1 
ATOM   9384  C CG1 . ILE F 2 266 ? -50.508  -10.942  4.357   1.00 116.54 ? 267 ILE F CG1 1 
ATOM   9385  C CG2 . ILE F 2 266 ? -52.961  -11.400  4.654   1.00 114.08 ? 267 ILE F CG2 1 
ATOM   9386  C CD1 . ILE F 2 266 ? -49.412  -11.310  3.316   1.00 132.17 ? 267 ILE F CD1 1 
ATOM   9387  N N   . ILE F 2 267 ? -53.085  -14.127  6.899   1.00 101.07 ? 268 ILE F N   1 
ATOM   9388  C CA  . ILE F 2 267 ? -54.075  -15.166  7.151   1.00 98.44  ? 268 ILE F CA  1 
ATOM   9389  C C   . ILE F 2 267 ? -55.384  -14.780  6.474   1.00 103.87 ? 268 ILE F C   1 
ATOM   9390  O O   . ILE F 2 267 ? -56.019  -13.792  6.852   1.00 104.16 ? 268 ILE F O   1 
ATOM   9391  C CB  . ILE F 2 267 ? -54.183  -15.459  8.677   1.00 99.40  ? 268 ILE F CB  1 
ATOM   9392  C CG1 . ILE F 2 267 ? -53.071  -16.437  9.094   1.00 97.76  ? 268 ILE F CG1 1 
ATOM   9393  C CG2 . ILE F 2 267 ? -55.562  -15.984  9.078   1.00 100.49 ? 268 ILE F CG2 1 
ATOM   9394  C CD1 . ILE F 2 267 ? -52.893  -16.680  10.542  1.00 101.36 ? 268 ILE F CD1 1 
ATOM   9395  N N   . ILE F 2 268 ? -55.747  -15.533  5.428   1.00 101.38 ? 269 ILE F N   1 
ATOM   9396  C CA  . ILE F 2 268 ? -56.983  -15.323  4.674   1.00 103.22 ? 269 ILE F CA  1 
ATOM   9397  C C   . ILE F 2 268 ? -57.944  -16.415  5.143   1.00 108.16 ? 269 ILE F C   1 
ATOM   9398  O O   . ILE F 2 268 ? -58.129  -17.426  4.462   1.00 109.04 ? 269 ILE F O   1 
ATOM   9399  C CB  . ILE F 2 268 ? -56.753  -15.280  3.129   1.00 107.72 ? 269 ILE F CB  1 
ATOM   9400  C CG1 . ILE F 2 268 ? -55.606  -14.329  2.753   1.00 109.11 ? 269 ILE F CG1 1 
ATOM   9401  C CG2 . ILE F 2 268 ? -58.017  -14.883  2.378   1.00 110.36 ? 269 ILE F CG2 1 
ATOM   9402  C CD1 . ILE F 2 268 ? -54.294  -15.044  2.403   1.00 123.66 ? 269 ILE F CD1 1 
ATOM   9403  N N   . SER F 2 269 ? -58.490  -16.242  6.360   1.00 104.24 ? 270 SER F N   1 
ATOM   9404  C CA  . SER F 2 269 ? -59.375  -17.232  6.965   1.00 104.77 ? 270 SER F CA  1 
ATOM   9405  C C   . SER F 2 269 ? -60.616  -16.640  7.606   1.00 111.25 ? 270 SER F C   1 
ATOM   9406  O O   . SER F 2 269 ? -60.562  -15.543  8.166   1.00 110.62 ? 270 SER F O   1 
ATOM   9407  C CB  . SER F 2 269 ? -58.616  -18.072  7.980   1.00 106.50 ? 270 SER F CB  1 
ATOM   9408  O OG  . SER F 2 269 ? -59.403  -19.157  8.445   1.00 118.30 ? 270 SER F OG  1 
ATOM   9409  N N   . ASP F 2 270 ? -61.731  -17.398  7.544   1.00 110.35 ? 271 ASP F N   1 
ATOM   9410  C CA  . ASP F 2 270 ? -63.027  -17.028  8.116   1.00 112.70 ? 271 ASP F CA  1 
ATOM   9411  C C   . ASP F 2 270 ? -63.172  -17.472  9.595   1.00 114.30 ? 271 ASP F C   1 
ATOM   9412  O O   . ASP F 2 270 ? -64.191  -17.168  10.215  1.00 115.94 ? 271 ASP F O   1 
ATOM   9413  C CB  . ASP F 2 270 ? -64.181  -17.570  7.236   1.00 118.28 ? 271 ASP F CB  1 
ATOM   9414  C CG  . ASP F 2 270 ? -64.967  -16.514  6.467   1.00 137.10 ? 271 ASP F CG  1 
ATOM   9415  O OD1 . ASP F 2 270 ? -65.580  -15.635  7.117   1.00 140.39 ? 271 ASP F OD1 1 
ATOM   9416  O OD2 . ASP F 2 270 ? -65.042  -16.617  5.222   1.00 145.04 ? 271 ASP F OD2 1 
ATOM   9417  N N   . THR F 2 271 ? -62.139  -18.155  10.162  1.00 107.58 ? 272 THR F N   1 
ATOM   9418  C CA  . THR F 2 271 ? -62.100  -18.638  11.560  1.00 106.84 ? 272 THR F CA  1 
ATOM   9419  C C   . THR F 2 271 ? -62.183  -17.466  12.574  1.00 110.40 ? 272 THR F C   1 
ATOM   9420  O O   . THR F 2 271 ? -61.745  -16.366  12.244  1.00 109.40 ? 272 THR F O   1 
ATOM   9421  C CB  . THR F 2 271 ? -60.894  -19.578  11.803  1.00 109.15 ? 272 THR F CB  1 
ATOM   9422  O OG1 . THR F 2 271 ? -59.677  -18.938  11.416  1.00 106.05 ? 272 THR F OG1 1 
ATOM   9423  C CG2 . THR F 2 271 ? -61.040  -20.918  11.084  1.00 107.56 ? 272 THR F CG2 1 
ATOM   9424  N N   . PRO F 2 272 ? -62.777  -17.640  13.778  1.00 108.66 ? 273 PRO F N   1 
ATOM   9425  C CA  . PRO F 2 272 ? -62.897  -16.498  14.705  1.00 109.79 ? 273 PRO F CA  1 
ATOM   9426  C C   . PRO F 2 272 ? -61.590  -16.066  15.367  1.00 113.53 ? 273 PRO F C   1 
ATOM   9427  O O   . PRO F 2 272 ? -60.588  -16.776  15.286  1.00 111.68 ? 273 PRO F O   1 
ATOM   9428  C CB  . PRO F 2 272 ? -63.898  -17.000  15.742  1.00 115.04 ? 273 PRO F CB  1 
ATOM   9429  C CG  . PRO F 2 272 ? -63.692  -18.477  15.769  1.00 119.20 ? 273 PRO F CG  1 
ATOM   9430  C CD  . PRO F 2 272 ? -63.388  -18.860  14.348  1.00 112.48 ? 273 PRO F CD  1 
ATOM   9431  N N   . VAL F 2 273 ? -61.612  -14.905  16.034  1.00 111.66 ? 274 VAL F N   1 
ATOM   9432  C CA  . VAL F 2 273 ? -60.460  -14.341  16.742  1.00 110.60 ? 274 VAL F CA  1 
ATOM   9433  C C   . VAL F 2 273 ? -60.860  -14.041  18.192  1.00 117.37 ? 274 VAL F C   1 
ATOM   9434  O O   . VAL F 2 273 ? -61.836  -13.328  18.423  1.00 119.04 ? 274 VAL F O   1 
ATOM   9435  C CB  . VAL F 2 273 ? -59.823  -13.135  15.982  1.00 113.27 ? 274 VAL F CB  1 
ATOM   9436  C CG1 . VAL F 2 273 ? -60.879  -12.236  15.354  1.00 114.56 ? 274 VAL F CG1 1 
ATOM   9437  C CG2 . VAL F 2 273 ? -58.879  -12.325  16.866  1.00 113.04 ? 274 VAL F CG2 1 
ATOM   9438  N N   . HIS F 2 274 ? -60.126  -14.626  19.159  1.00 114.73 ? 275 HIS F N   1 
ATOM   9439  C CA  . HIS F 2 274 ? -60.378  -14.477  20.599  1.00 117.66 ? 275 HIS F CA  1 
ATOM   9440  C C   . HIS F 2 274 ? -59.226  -13.798  21.358  1.00 120.79 ? 275 HIS F C   1 
ATOM   9441  O O   . HIS F 2 274 ? -58.159  -13.565  20.787  1.00 117.32 ? 275 HIS F O   1 
ATOM   9442  C CB  . HIS F 2 274 ? -60.750  -15.831  21.222  1.00 120.50 ? 275 HIS F CB  1 
ATOM   9443  C CG  . HIS F 2 274 ? -62.089  -16.322  20.779  1.00 126.20 ? 275 HIS F CG  1 
ATOM   9444  N ND1 . HIS F 2 274 ? -62.274  -16.880  19.528  1.00 126.36 ? 275 HIS F ND1 1 
ATOM   9445  C CD2 . HIS F 2 274 ? -63.280  -16.281  21.423  1.00 132.64 ? 275 HIS F CD2 1 
ATOM   9446  C CE1 . HIS F 2 274 ? -63.561  -17.186  19.459  1.00 129.22 ? 275 HIS F CE1 1 
ATOM   9447  N NE2 . HIS F 2 274 ? -64.210  -16.838  20.573  1.00 133.22 ? 275 HIS F NE2 1 
ATOM   9448  N N   . ASP F 2 275 ? -59.450  -13.481  22.647  1.00 121.03 ? 276 ASP F N   1 
ATOM   9449  C CA  . ASP F 2 275 ? -58.482  -12.784  23.494  1.00 122.45 ? 276 ASP F CA  1 
ATOM   9450  C C   . ASP F 2 275 ? -57.259  -13.630  23.909  1.00 127.25 ? 276 ASP F C   1 
ATOM   9451  O O   . ASP F 2 275 ? -56.345  -13.085  24.536  1.00 129.28 ? 276 ASP F O   1 
ATOM   9452  C CB  . ASP F 2 275 ? -59.174  -12.173  24.728  1.00 128.77 ? 276 ASP F CB  1 
ATOM   9453  C CG  . ASP F 2 275 ? -58.521  -10.894  25.237  1.00 144.28 ? 276 ASP F CG  1 
ATOM   9454  O OD1 . ASP F 2 275 ? -57.965  -10.916  26.358  1.00 147.96 ? 276 ASP F OD1 1 
ATOM   9455  O OD2 . ASP F 2 275 ? -58.566  -9.872   24.512  1.00 149.98 ? 276 ASP F OD2 1 
ATOM   9456  N N   . CYS F 2 276 ? -57.215  -14.931  23.535  1.00 121.67 ? 277 CYS F N   1 
ATOM   9457  C CA  . CYS F 2 276 ? -56.097  -15.852  23.827  1.00 120.52 ? 277 CYS F CA  1 
ATOM   9458  C C   . CYS F 2 276 ? -54.750  -15.367  23.250  1.00 122.14 ? 277 CYS F C   1 
ATOM   9459  O O   . CYS F 2 276 ? -54.731  -14.528  22.346  1.00 120.02 ? 277 CYS F O   1 
ATOM   9460  C CB  . CYS F 2 276 ? -56.424  -17.270  23.352  1.00 119.66 ? 277 CYS F CB  1 
ATOM   9461  S SG  . CYS F 2 276 ? -57.101  -17.357  21.666  1.00 120.57 ? 277 CYS F SG  1 
ATOM   9462  N N   . ASN F 2 277 ? -53.634  -15.893  23.780  1.00 118.98 ? 278 ASN F N   1 
ATOM   9463  C CA  . ASN F 2 277 ? -52.281  -15.602  23.297  1.00 117.36 ? 278 ASN F CA  1 
ATOM   9464  C C   . ASN F 2 277 ? -51.732  -16.864  22.626  1.00 118.84 ? 278 ASN F C   1 
ATOM   9465  O O   . ASN F 2 277 ? -52.153  -17.967  22.982  1.00 118.64 ? 278 ASN F O   1 
ATOM   9466  C CB  . ASN F 2 277 ? -51.355  -15.202  24.447  1.00 122.34 ? 278 ASN F CB  1 
ATOM   9467  C CG  . ASN F 2 277 ? -51.699  -13.927  25.175  1.00 160.20 ? 278 ASN F CG  1 
ATOM   9468  O OD1 . ASN F 2 277 ? -52.175  -12.944  24.580  1.00 150.32 ? 278 ASN F OD1 1 
ATOM   9469  N ND2 . ASN F 2 277 ? -51.397  -13.963  26.495  1.00 168.11 ? 278 ASN F ND2 1 
ATOM   9470  N N   . THR F 2 278 ? -50.800  -16.715  21.661  1.00 113.67 ? 279 THR F N   1 
ATOM   9471  C CA  . THR F 2 278 ? -50.187  -17.865  20.983  1.00 112.03 ? 279 THR F CA  1 
ATOM   9472  C C   . THR F 2 278 ? -48.756  -17.570  20.495  1.00 116.21 ? 279 THR F C   1 
ATOM   9473  O O   . THR F 2 278 ? -48.444  -16.427  20.149  1.00 116.48 ? 279 THR F O   1 
ATOM   9474  C CB  . THR F 2 278 ? -51.094  -18.426  19.870  1.00 116.71 ? 279 THR F CB  1 
ATOM   9475  O OG1 . THR F 2 278 ? -50.646  -19.736  19.517  1.00 114.30 ? 279 THR F OG1 1 
ATOM   9476  C CG2 . THR F 2 278 ? -51.183  -17.517  18.634  1.00 113.54 ? 279 THR F CG2 1 
ATOM   9477  N N   . THR F 2 279 ? -47.895  -18.613  20.485  1.00 111.84 ? 280 THR F N   1 
ATOM   9478  C CA  . THR F 2 279 ? -46.504  -18.546  20.017  1.00 111.15 ? 280 THR F CA  1 
ATOM   9479  C C   . THR F 2 279 ? -46.499  -18.788  18.519  1.00 110.46 ? 280 THR F C   1 
ATOM   9480  O O   . THR F 2 279 ? -45.708  -18.182  17.799  1.00 109.63 ? 280 THR F O   1 
ATOM   9481  C CB  . THR F 2 279 ? -45.633  -19.607  20.717  1.00 124.14 ? 280 THR F CB  1 
ATOM   9482  O OG1 . THR F 2 279 ? -46.187  -20.909  20.505  1.00 123.14 ? 280 THR F OG1 1 
ATOM   9483  C CG2 . THR F 2 279 ? -45.478  -19.354  22.204  1.00 128.98 ? 280 THR F CG2 1 
ATOM   9484  N N   . CYS F 2 280 ? -47.393  -19.686  18.065  1.00 104.49 ? 281 CYS F N   1 
ATOM   9485  C CA  . CYS F 2 280 ? -47.563  -20.095  16.678  1.00 102.02 ? 281 CYS F CA  1 
ATOM   9486  C C   . CYS F 2 280 ? -49.020  -19.926  16.237  1.00 102.44 ? 281 CYS F C   1 
ATOM   9487  O O   . CYS F 2 280 ? -49.934  -20.350  16.949  1.00 103.39 ? 281 CYS F O   1 
ATOM   9488  C CB  . CYS F 2 280 ? -47.082  -21.531  16.488  1.00 102.52 ? 281 CYS F CB  1 
ATOM   9489  S SG  . CYS F 2 280 ? -47.095  -22.098  14.769  1.00 104.90 ? 281 CYS F SG  1 
ATOM   9490  N N   . GLN F 2 281 ? -49.230  -19.316  15.060  1.00 95.05  ? 282 GLN F N   1 
ATOM   9491  C CA  . GLN F 2 281 ? -50.561  -19.055  14.522  1.00 92.70  ? 282 GLN F CA  1 
ATOM   9492  C C   . GLN F 2 281 ? -50.684  -19.477  13.061  1.00 95.05  ? 282 GLN F C   1 
ATOM   9493  O O   . GLN F 2 281 ? -49.827  -19.130  12.244  1.00 94.41  ? 282 GLN F O   1 
ATOM   9494  C CB  . GLN F 2 281 ? -50.919  -17.568  14.709  1.00 94.02  ? 282 GLN F CB  1 
ATOM   9495  C CG  . GLN F 2 281 ? -52.323  -17.173  14.268  1.00 97.31  ? 282 GLN F CG  1 
ATOM   9496  C CD  . GLN F 2 281 ? -53.395  -17.829  15.091  1.00 110.26 ? 282 GLN F CD  1 
ATOM   9497  O OE1 . GLN F 2 281 ? -53.654  -17.447  16.233  1.00 109.31 ? 282 GLN F OE1 1 
ATOM   9498  N NE2 . GLN F 2 281 ? -54.032  -18.838  14.530  1.00 95.16  ? 282 GLN F NE2 1 
ATOM   9499  N N   . THR F 2 282 ? -51.760  -20.231  12.739  1.00 91.17  ? 283 THR F N   1 
ATOM   9500  C CA  . THR F 2 282 ? -52.080  -20.708  11.380  1.00 89.84  ? 283 THR F CA  1 
ATOM   9501  C C   . THR F 2 282 ? -53.520  -20.338  11.013  1.00 91.57  ? 283 THR F C   1 
ATOM   9502  O O   . THR F 2 282 ? -54.340  -20.283  11.925  1.00 90.70  ? 283 THR F O   1 
ATOM   9503  C CB  . THR F 2 282 ? -51.883  -22.233  11.223  1.00 99.00  ? 283 THR F CB  1 
ATOM   9504  O OG1 . THR F 2 282 ? -53.014  -22.944  11.733  1.00 95.01  ? 283 THR F OG1 1 
ATOM   9505  C CG2 . THR F 2 282 ? -50.580  -22.744  11.817  1.00 100.30 ? 283 THR F CG2 1 
ATOM   9506  N N   . PRO F 2 283 ? -53.870  -20.153  9.709   1.00 88.77  ? 284 PRO F N   1 
ATOM   9507  C CA  . PRO F 2 283 ? -55.266  -19.835  9.351   1.00 91.16  ? 284 PRO F CA  1 
ATOM   9508  C C   . PRO F 2 283 ? -56.324  -20.813  9.897   1.00 100.70 ? 284 PRO F C   1 
ATOM   9509  O O   . PRO F 2 283 ? -57.455  -20.398  10.189  1.00 102.12 ? 284 PRO F O   1 
ATOM   9510  C CB  . PRO F 2 283 ? -55.241  -19.838  7.819   1.00 92.71  ? 284 PRO F CB  1 
ATOM   9511  C CG  . PRO F 2 283 ? -53.847  -19.554  7.459   1.00 95.29  ? 284 PRO F CG  1 
ATOM   9512  C CD  . PRO F 2 283 ? -53.020  -20.208  8.503   1.00 89.67  ? 284 PRO F CD  1 
ATOM   9513  N N   . LYS F 2 284 ? -55.942  -22.105  10.050  1.00 98.77  ? 285 LYS F N   1 
ATOM   9514  C CA  . LYS F 2 284 ? -56.783  -23.176  10.585  1.00 100.00 ? 285 LYS F CA  1 
ATOM   9515  C C   . LYS F 2 284 ? -57.024  -22.968  12.101  1.00 107.60 ? 285 LYS F C   1 
ATOM   9516  O O   . LYS F 2 284 ? -58.100  -23.297  12.609  1.00 108.83 ? 285 LYS F O   1 
ATOM   9517  C CB  . LYS F 2 284 ? -56.113  -24.526  10.312  1.00 100.55 ? 285 LYS F CB  1 
ATOM   9518  C CG  . LYS F 2 284 ? -57.086  -25.643  10.010  1.00 109.92 ? 285 LYS F CG  1 
ATOM   9519  C CD  . LYS F 2 284 ? -56.356  -26.890  9.558   1.00 117.81 ? 285 LYS F CD  1 
ATOM   9520  C CE  . LYS F 2 284 ? -57.295  -28.059  9.398   1.00 137.91 ? 285 LYS F CE  1 
ATOM   9521  N NZ  . LYS F 2 284 ? -56.597  -29.249  8.845   1.00 149.70 ? 285 LYS F NZ  1 
ATOM   9522  N N   . GLY F 2 285 ? -56.021  -22.409  12.785  1.00 105.57 ? 286 GLY F N   1 
ATOM   9523  C CA  . GLY F 2 285 ? -56.053  -22.108  14.212  1.00 107.55 ? 286 GLY F CA  1 
ATOM   9524  C C   . GLY F 2 285 ? -54.685  -22.027  14.863  1.00 113.30 ? 286 GLY F C   1 
ATOM   9525  O O   . GLY F 2 285 ? -53.680  -22.400  14.252  1.00 111.70 ? 286 GLY F O   1 
ATOM   9526  N N   . ALA F 2 286 ? -54.633  -21.535  16.115  1.00 112.72 ? 287 ALA F N   1 
ATOM   9527  C CA  . ALA F 2 286 ? -53.386  -21.352  16.869  1.00 112.94 ? 287 ALA F CA  1 
ATOM   9528  C C   . ALA F 2 286 ? -52.775  -22.660  17.379  1.00 116.34 ? 287 ALA F C   1 
ATOM   9529  O O   . ALA F 2 286 ? -53.494  -23.637  17.579  1.00 116.07 ? 287 ALA F O   1 
ATOM   9530  C CB  . ALA F 2 286 ? -53.617  -20.388  18.024  1.00 115.59 ? 287 ALA F CB  1 
ATOM   9531  N N   . ILE F 2 287 ? -51.439  -22.680  17.563  1.00 104.20 ? 288 ILE F N   1 
ATOM   9532  C CA  . ILE F 2 287 ? -50.709  -23.846  18.078  1.00 105.96 ? 288 ILE F CA  1 
ATOM   9533  C C   . ILE F 2 287 ? -49.792  -23.469  19.237  1.00 115.43 ? 288 ILE F C   1 
ATOM   9534  O O   . ILE F 2 287 ? -49.043  -22.488  19.148  1.00 116.13 ? 288 ILE F O   1 
ATOM   9535  C CB  . ILE F 2 287 ? -49.917  -24.674  17.027  1.00 108.56 ? 288 ILE F CB  1 
ATOM   9536  C CG1 . ILE F 2 287 ? -50.399  -24.451  15.577  1.00 107.03 ? 288 ILE F CG1 1 
ATOM   9537  C CG2 . ILE F 2 287 ? -49.934  -26.160  17.415  1.00 110.56 ? 288 ILE F CG2 1 
ATOM   9538  C CD1 . ILE F 2 287 ? -49.396  -24.839  14.537  1.00 108.12 ? 288 ILE F CD1 1 
ATOM   9539  N N   . ASN F 2 288 ? -49.828  -24.281  20.306  1.00 115.83 ? 289 ASN F N   1 
ATOM   9540  C CA  . ASN F 2 288 ? -48.981  -24.125  21.485  1.00 119.68 ? 289 ASN F CA  1 
ATOM   9541  C C   . ASN F 2 288 ? -48.297  -25.468  21.712  1.00 124.56 ? 289 ASN F C   1 
ATOM   9542  O O   . ASN F 2 288 ? -48.806  -26.312  22.456  1.00 125.11 ? 289 ASN F O   1 
ATOM   9543  C CB  . ASN F 2 288 ? -49.805  -23.673  22.701  1.00 126.92 ? 289 ASN F CB  1 
ATOM   9544  C CG  . ASN F 2 288 ? -49.003  -23.376  23.949  1.00 176.99 ? 289 ASN F CG  1 
ATOM   9545  O OD1 . ASN F 2 288 ? -47.884  -22.815  23.905  1.00 171.32 ? 289 ASN F OD1 1 
ATOM   9546  N ND2 . ASN F 2 288 ? -49.610  -23.745  25.084  1.00 185.31 ? 289 ASN F ND2 1 
ATOM   9547  N N   . THR F 2 289 ? -47.171  -25.685  21.000  1.00 121.19 ? 290 THR F N   1 
ATOM   9548  C CA  . THR F 2 289 ? -46.411  -26.938  21.042  1.00 122.12 ? 290 THR F CA  1 
ATOM   9549  C C   . THR F 2 289 ? -44.880  -26.761  21.039  1.00 126.17 ? 290 THR F C   1 
ATOM   9550  O O   . THR F 2 289 ? -44.349  -25.770  20.522  1.00 125.99 ? 290 THR F O   1 
ATOM   9551  C CB  . THR F 2 289 ? -46.859  -27.889  19.910  1.00 131.39 ? 290 THR F CB  1 
ATOM   9552  O OG1 . THR F 2 289 ? -46.260  -29.164  20.118  1.00 134.64 ? 290 THR F OG1 1 
ATOM   9553  C CG2 . THR F 2 289 ? -46.513  -27.375  18.508  1.00 128.04 ? 290 THR F CG2 1 
ATOM   9554  N N   . SER F 2 290 ? -44.188  -27.767  21.605  1.00 122.59 ? 291 SER F N   1 
ATOM   9555  C CA  . SER F 2 290 ? -42.731  -27.860  21.682  1.00 123.10 ? 291 SER F CA  1 
ATOM   9556  C C   . SER F 2 290 ? -42.208  -28.763  20.550  1.00 121.89 ? 291 SER F C   1 
ATOM   9557  O O   . SER F 2 290 ? -40.996  -28.806  20.310  1.00 121.87 ? 291 SER F O   1 
ATOM   9558  C CB  . SER F 2 290 ? -42.301  -28.383  23.051  1.00 130.36 ? 291 SER F CB  1 
ATOM   9559  O OG  . SER F 2 290 ? -43.066  -29.507  23.456  1.00 138.80 ? 291 SER F OG  1 
ATOM   9560  N N   . LEU F 2 291 ? -43.142  -29.451  19.836  1.00 114.18 ? 292 LEU F N   1 
ATOM   9561  C CA  . LEU F 2 291 ? -42.874  -30.362  18.717  1.00 111.71 ? 292 LEU F CA  1 
ATOM   9562  C C   . LEU F 2 291 ? -42.212  -29.676  17.521  1.00 112.59 ? 292 LEU F C   1 
ATOM   9563  O O   . LEU F 2 291 ? -42.595  -28.556  17.187  1.00 111.67 ? 292 LEU F O   1 
ATOM   9564  C CB  . LEU F 2 291 ? -44.159  -31.081  18.261  1.00 110.46 ? 292 LEU F CB  1 
ATOM   9565  C CG  . LEU F 2 291 ? -44.537  -32.401  18.949  1.00 116.90 ? 292 LEU F CG  1 
ATOM   9566  C CD1 . LEU F 2 291 ? -43.330  -33.237  19.279  1.00 118.53 ? 292 LEU F CD1 1 
ATOM   9567  C CD2 . LEU F 2 291 ? -45.330  -32.168  20.211  1.00 122.38 ? 292 LEU F CD2 1 
ATOM   9568  N N   . PRO F 2 292 ? -41.232  -30.323  16.850  1.00 107.55 ? 293 PRO F N   1 
ATOM   9569  C CA  . PRO F 2 292 ? -40.565  -29.655  15.720  1.00 106.24 ? 293 PRO F CA  1 
ATOM   9570  C C   . PRO F 2 292 ? -41.335  -29.642  14.402  1.00 106.70 ? 293 PRO F C   1 
ATOM   9571  O O   . PRO F 2 292 ? -40.951  -28.909  13.489  1.00 105.97 ? 293 PRO F O   1 
ATOM   9572  C CB  . PRO F 2 292 ? -39.247  -30.416  15.596  1.00 109.34 ? 293 PRO F CB  1 
ATOM   9573  C CG  . PRO F 2 292 ? -39.566  -31.779  16.076  1.00 114.25 ? 293 PRO F CG  1 
ATOM   9574  C CD  . PRO F 2 292 ? -40.637  -31.651  17.117  1.00 110.13 ? 293 PRO F CD  1 
ATOM   9575  N N   . PHE F 2 293 ? -42.399  -30.454  14.283  1.00 101.76 ? 294 PHE F N   1 
ATOM   9576  C CA  . PHE F 2 293 ? -43.191  -30.521  13.052  1.00 100.29 ? 294 PHE F CA  1 
ATOM   9577  C C   . PHE F 2 293 ? -44.674  -30.443  13.306  1.00 100.67 ? 294 PHE F C   1 
ATOM   9578  O O   . PHE F 2 293 ? -45.130  -30.767  14.400  1.00 101.56 ? 294 PHE F O   1 
ATOM   9579  C CB  . PHE F 2 293 ? -42.820  -31.751  12.218  1.00 103.31 ? 294 PHE F CB  1 
ATOM   9580  C CG  . PHE F 2 293 ? -41.372  -31.708  11.808  1.00 105.92 ? 294 PHE F CG  1 
ATOM   9581  C CD1 . PHE F 2 293 ? -40.947  -30.857  10.796  1.00 109.56 ? 294 PHE F CD1 1 
ATOM   9582  C CD2 . PHE F 2 293 ? -40.418  -32.456  12.490  1.00 109.23 ? 294 PHE F CD2 1 
ATOM   9583  C CE1 . PHE F 2 293 ? -39.599  -30.781  10.452  1.00 111.84 ? 294 PHE F CE1 1 
ATOM   9584  C CE2 . PHE F 2 293 ? -39.068  -32.374  12.150  1.00 112.85 ? 294 PHE F CE2 1 
ATOM   9585  C CZ  . PHE F 2 293 ? -38.668  -31.544  11.129  1.00 111.53 ? 294 PHE F CZ  1 
ATOM   9586  N N   . GLN F 2 294 ? -45.426  -29.968  12.309  1.00 93.15  ? 295 GLN F N   1 
ATOM   9587  C CA  . GLN F 2 294 ? -46.867  -29.798  12.424  1.00 90.83  ? 295 GLN F CA  1 
ATOM   9588  C C   . GLN F 2 294 ? -47.568  -30.114  11.111  1.00 92.68  ? 295 GLN F C   1 
ATOM   9589  O O   . GLN F 2 294 ? -47.093  -29.703  10.055  1.00 92.35  ? 295 GLN F O   1 
ATOM   9590  C CB  . GLN F 2 294 ? -47.176  -28.380  12.961  1.00 90.52  ? 295 GLN F CB  1 
ATOM   9591  C CG  . GLN F 2 294 ? -48.348  -27.627  12.328  1.00 92.06  ? 295 GLN F CG  1 
ATOM   9592  C CD  . GLN F 2 294 ? -47.899  -26.655  11.268  1.00 92.22  ? 295 GLN F CD  1 
ATOM   9593  O OE1 . GLN F 2 294 ? -48.205  -26.807  10.092  1.00 70.91  ? 295 GLN F OE1 1 
ATOM   9594  N NE2 . GLN F 2 294 ? -47.178  -25.623  11.667  1.00 94.18  ? 295 GLN F NE2 1 
ATOM   9595  N N   . ASN F 2 295 ? -48.690  -30.842  11.181  1.00 88.20  ? 296 ASN F N   1 
ATOM   9596  C CA  . ASN F 2 295 ? -49.468  -31.194  10.002  1.00 89.38  ? 296 ASN F CA  1 
ATOM   9597  C C   . ASN F 2 295 ? -50.770  -30.372  9.865   1.00 95.03  ? 296 ASN F C   1 
ATOM   9598  O O   . ASN F 2 295 ? -51.626  -30.720  9.043   1.00 98.43  ? 296 ASN F O   1 
ATOM   9599  C CB  . ASN F 2 295 ? -49.729  -32.707  9.966   1.00 88.58  ? 296 ASN F CB  1 
ATOM   9600  C CG  . ASN F 2 295 ? -50.934  -33.196  10.745  1.00 102.32 ? 296 ASN F CG  1 
ATOM   9601  O OD1 . ASN F 2 295 ? -51.362  -32.607  11.741  1.00 90.06  ? 296 ASN F OD1 1 
ATOM   9602  N ND2 . ASN F 2 295 ? -51.506  -34.303  10.304  1.00 97.49  ? 296 ASN F ND2 1 
ATOM   9603  N N   . ILE F 2 296 ? -50.897  -29.267  10.636  1.00 88.51  ? 297 ILE F N   1 
ATOM   9604  C CA  . ILE F 2 296 ? -52.093  -28.414  10.686  1.00 87.01  ? 297 ILE F CA  1 
ATOM   9605  C C   . ILE F 2 296 ? -52.295  -27.560  9.401   1.00 91.65  ? 297 ILE F C   1 
ATOM   9606  O O   . ILE F 2 296 ? -53.286  -27.772  8.701   1.00 93.32  ? 297 ILE F O   1 
ATOM   9607  C CB  . ILE F 2 296 ? -52.126  -27.564  11.991  1.00 87.92  ? 297 ILE F CB  1 
ATOM   9608  C CG1 . ILE F 2 296 ? -52.138  -28.480  13.226  1.00 89.19  ? 297 ILE F CG1 1 
ATOM   9609  C CG2 . ILE F 2 296 ? -53.328  -26.612  12.024  1.00 87.30  ? 297 ILE F CG2 1 
ATOM   9610  C CD1 . ILE F 2 296 ? -51.510  -27.913  14.441  1.00 97.22  ? 297 ILE F CD1 1 
ATOM   9611  N N   . HIS F 2 297 ? -51.406  -26.587  9.118   1.00 87.59  ? 298 HIS F N   1 
ATOM   9612  C CA  . HIS F 2 297 ? -51.549  -25.696  7.961   1.00 88.40  ? 298 HIS F CA  1 
ATOM   9613  C C   . HIS F 2 297 ? -50.196  -25.150  7.472   1.00 92.89  ? 298 HIS F C   1 
ATOM   9614  O O   . HIS F 2 297 ? -49.370  -24.747  8.302   1.00 91.41  ? 298 HIS F O   1 
ATOM   9615  C CB  . HIS F 2 297 ? -52.486  -24.533  8.307   1.00 87.80  ? 298 HIS F CB  1 
ATOM   9616  C CG  . HIS F 2 297 ? -52.978  -23.790  7.114   1.00 93.03  ? 298 HIS F CG  1 
ATOM   9617  N ND1 . HIS F 2 297 ? -52.219  -22.806  6.513   1.00 95.76  ? 298 HIS F ND1 1 
ATOM   9618  C CD2 . HIS F 2 297 ? -54.139  -23.923  6.436   1.00 96.68  ? 298 HIS F CD2 1 
ATOM   9619  C CE1 . HIS F 2 297 ? -52.942  -22.367  5.497   1.00 97.20  ? 298 HIS F CE1 1 
ATOM   9620  N NE2 . HIS F 2 297 ? -54.108  -23.004  5.415   1.00 97.97  ? 298 HIS F NE2 1 
ATOM   9621  N N   . PRO F 2 298 ? -49.963  -25.095  6.137   1.00 91.61  ? 299 PRO F N   1 
ATOM   9622  C CA  . PRO F 2 298 ? -48.672  -24.594  5.632   1.00 93.06  ? 299 PRO F CA  1 
ATOM   9623  C C   . PRO F 2 298 ? -48.339  -23.144  5.991   1.00 98.95  ? 299 PRO F C   1 
ATOM   9624  O O   . PRO F 2 298 ? -47.162  -22.854  6.218   1.00 100.72 ? 299 PRO F O   1 
ATOM   9625  C CB  . PRO F 2 298 ? -48.770  -24.811  4.124   1.00 98.12  ? 299 PRO F CB  1 
ATOM   9626  C CG  . PRO F 2 298 ? -50.229  -24.882  3.844   1.00 103.00 ? 299 PRO F CG  1 
ATOM   9627  C CD  . PRO F 2 298 ? -50.821  -25.557  5.028   1.00 95.88  ? 299 PRO F CD  1 
ATOM   9628  N N   . ILE F 2 299 ? -49.350  -22.246  6.059   1.00 94.89  ? 300 ILE F N   1 
ATOM   9629  C CA  . ILE F 2 299 ? -49.148  -20.839  6.435   1.00 94.71  ? 300 ILE F CA  1 
ATOM   9630  C C   . ILE F 2 299 ? -48.986  -20.775  7.960   1.00 96.62  ? 300 ILE F C   1 
ATOM   9631  O O   . ILE F 2 299 ? -49.847  -21.272  8.683   1.00 94.43  ? 300 ILE F O   1 
ATOM   9632  C CB  . ILE F 2 299 ? -50.286  -19.911  5.924   1.00 98.60  ? 300 ILE F CB  1 
ATOM   9633  C CG1 . ILE F 2 299 ? -50.436  -19.976  4.386   1.00 103.17 ? 300 ILE F CG1 1 
ATOM   9634  C CG2 . ILE F 2 299 ? -50.082  -18.466  6.400   1.00 99.25  ? 300 ILE F CG2 1 
ATOM   9635  C CD1 . ILE F 2 299 ? -51.804  -19.396  3.800   1.00 116.11 ? 300 ILE F CD1 1 
ATOM   9636  N N   . THR F 2 300 ? -47.866  -20.202  8.441   1.00 94.31  ? 301 THR F N   1 
ATOM   9637  C CA  . THR F 2 300 ? -47.534  -20.092  9.870   1.00 92.84  ? 301 THR F CA  1 
ATOM   9638  C C   . THR F 2 300 ? -46.947  -18.724  10.215  1.00 97.82  ? 301 THR F C   1 
ATOM   9639  O O   . THR F 2 300 ? -46.225  -18.142  9.403   1.00 101.08 ? 301 THR F O   1 
ATOM   9640  C CB  . THR F 2 300 ? -46.540  -21.194  10.286  1.00 101.26 ? 301 THR F CB  1 
ATOM   9641  O OG1 . THR F 2 300 ? -45.356  -21.116  9.492   1.00 107.21 ? 301 THR F OG1 1 
ATOM   9642  C CG2 . THR F 2 300 ? -47.131  -22.599  10.233  1.00 97.31  ? 301 THR F CG2 1 
ATOM   9643  N N   . ILE F 2 301 ? -47.226  -18.234  11.433  1.00 92.65  ? 302 ILE F N   1 
ATOM   9644  C CA  . ILE F 2 301 ? -46.747  -16.941  11.936  1.00 94.72  ? 302 ILE F CA  1 
ATOM   9645  C C   . ILE F 2 301 ? -46.133  -17.116  13.338  1.00 99.95  ? 302 ILE F C   1 
ATOM   9646  O O   . ILE F 2 301 ? -46.807  -17.613  14.235  1.00 98.29  ? 302 ILE F O   1 
ATOM   9647  C CB  . ILE F 2 301 ? -47.903  -15.887  11.869  1.00 97.33  ? 302 ILE F CB  1 
ATOM   9648  C CG1 . ILE F 2 301 ? -48.120  -15.408  10.422  1.00 99.48  ? 302 ILE F CG1 1 
ATOM   9649  C CG2 . ILE F 2 301 ? -47.671  -14.681  12.786  1.00 99.22  ? 302 ILE F CG2 1 
ATOM   9650  C CD1 . ILE F 2 301 ? -49.537  -15.264  10.015  1.00 107.10 ? 302 ILE F CD1 1 
ATOM   9651  N N   . GLY F 2 302 ? -44.870  -16.716  13.502  1.00 100.10 ? 303 GLY F N   1 
ATOM   9652  C CA  . GLY F 2 302 ? -44.136  -16.827  14.765  1.00 102.19 ? 303 GLY F CA  1 
ATOM   9653  C C   . GLY F 2 302 ? -43.287  -18.080  14.836  1.00 107.04 ? 303 GLY F C   1 
ATOM   9654  O O   . GLY F 2 302 ? -43.125  -18.758  13.811  1.00 105.69 ? 303 GLY F O   1 
ATOM   9655  N N   . LYS F 2 303 ? -42.726  -18.404  16.044  1.00 105.71 ? 304 LYS F N   1 
ATOM   9656  C CA  . LYS F 2 303 ? -41.916  -19.620  16.237  1.00 105.87 ? 304 LYS F CA  1 
ATOM   9657  C C   . LYS F 2 303 ? -42.821  -20.811  15.985  1.00 106.83 ? 304 LYS F C   1 
ATOM   9658  O O   . LYS F 2 303 ? -43.669  -21.145  16.821  1.00 105.06 ? 304 LYS F O   1 
ATOM   9659  C CB  . LYS F 2 303 ? -41.223  -19.672  17.618  1.00 111.29 ? 304 LYS F CB  1 
ATOM   9660  C CG  . LYS F 2 303 ? -39.831  -19.043  17.595  1.00 126.92 ? 304 LYS F CG  1 
ATOM   9661  C CD  . LYS F 2 303 ? -38.887  -19.549  18.695  1.00 137.09 ? 304 LYS F CD  1 
ATOM   9662  C CE  . LYS F 2 303 ? -37.481  -19.001  18.507  1.00 152.74 ? 304 LYS F CE  1 
ATOM   9663  N NZ  . LYS F 2 303 ? -36.553  -19.375  19.612  1.00 164.55 ? 304 LYS F NZ  1 
ATOM   9664  N N   . CYS F 2 304 ? -42.711  -21.367  14.763  1.00 102.81 ? 305 CYS F N   1 
ATOM   9665  C CA  . CYS F 2 304 ? -43.587  -22.421  14.289  1.00 100.47 ? 305 CYS F CA  1 
ATOM   9666  C C   . CYS F 2 304 ? -42.895  -23.694  13.833  1.00 102.68 ? 305 CYS F C   1 
ATOM   9667  O O   . CYS F 2 304 ? -41.863  -23.627  13.154  1.00 103.86 ? 305 CYS F O   1 
ATOM   9668  C CB  . CYS F 2 304 ? -44.488  -21.879  13.190  1.00 100.21 ? 305 CYS F CB  1 
ATOM   9669  S SG  . CYS F 2 304 ? -45.827  -20.830  13.797  1.00 103.50 ? 305 CYS F SG  1 
ATOM   9670  N N   . PRO F 2 305 ? -43.532  -24.861  14.107  1.00 96.09  ? 306 PRO F N   1 
ATOM   9671  C CA  . PRO F 2 305 ? -42.981  -26.132  13.626  1.00 95.42  ? 306 PRO F CA  1 
ATOM   9672  C C   . PRO F 2 305 ? -43.257  -26.250  12.131  1.00 99.93  ? 306 PRO F C   1 
ATOM   9673  O O   . PRO F 2 305 ? -44.413  -26.128  11.714  1.00 99.32  ? 306 PRO F O   1 
ATOM   9674  C CB  . PRO F 2 305 ? -43.767  -27.180  14.425  1.00 96.30  ? 306 PRO F CB  1 
ATOM   9675  C CG  . PRO F 2 305 ? -44.547  -26.430  15.443  1.00 100.98 ? 306 PRO F CG  1 
ATOM   9676  C CD  . PRO F 2 305 ? -44.776  -25.090  14.863  1.00 96.36  ? 306 PRO F CD  1 
ATOM   9677  N N   . LYS F 2 306 ? -42.190  -26.427  11.325  1.00 97.81  ? 307 LYS F N   1 
ATOM   9678  C CA  . LYS F 2 306 ? -42.247  -26.533  9.861   1.00 98.17  ? 307 LYS F CA  1 
ATOM   9679  C C   . LYS F 2 306 ? -43.328  -27.520  9.405   1.00 101.96 ? 307 LYS F C   1 
ATOM   9680  O O   . LYS F 2 306 ? -43.402  -28.629  9.938   1.00 102.07 ? 307 LYS F O   1 
ATOM   9681  C CB  . LYS F 2 306 ? -40.867  -26.900  9.297   1.00 101.86 ? 307 LYS F CB  1 
ATOM   9682  C CG  . LYS F 2 306 ? -39.858  -25.762  9.383   1.00 111.43 ? 307 LYS F CG  1 
ATOM   9683  C CD  . LYS F 2 306 ? -38.443  -26.286  9.521   1.00 119.70 ? 307 LYS F CD  1 
ATOM   9684  C CE  . LYS F 2 306 ? -37.444  -25.175  9.649   1.00 131.98 ? 307 LYS F CE  1 
ATOM   9685  N NZ  . LYS F 2 306 ? -36.052  -25.666  9.470   1.00 140.11 ? 307 LYS F NZ  1 
ATOM   9686  N N   . TYR F 2 307 ? -44.203  -27.085  8.476   1.00 98.40  ? 308 TYR F N   1 
ATOM   9687  C CA  . TYR F 2 307 ? -45.321  -27.891  7.977   1.00 98.60  ? 308 TYR F CA  1 
ATOM   9688  C C   . TYR F 2 307 ? -44.900  -29.148  7.226   1.00 104.19 ? 308 TYR F C   1 
ATOM   9689  O O   . TYR F 2 307 ? -43.930  -29.143  6.469   1.00 105.45 ? 308 TYR F O   1 
ATOM   9690  C CB  . TYR F 2 307 ? -46.296  -27.050  7.122   1.00 100.93 ? 308 TYR F CB  1 
ATOM   9691  C CG  . TYR F 2 307 ? -47.525  -27.802  6.637   1.00 103.98 ? 308 TYR F CG  1 
ATOM   9692  C CD1 . TYR F 2 307 ? -48.551  -28.142  7.513   1.00 104.83 ? 308 TYR F CD1 1 
ATOM   9693  C CD2 . TYR F 2 307 ? -47.662  -28.169  5.303   1.00 107.51 ? 308 TYR F CD2 1 
ATOM   9694  C CE1 . TYR F 2 307 ? -49.684  -28.827  7.073   1.00 107.08 ? 308 TYR F CE1 1 
ATOM   9695  C CE2 . TYR F 2 307 ? -48.784  -28.867  4.854   1.00 110.06 ? 308 TYR F CE2 1 
ATOM   9696  C CZ  . TYR F 2 307 ? -49.793  -29.198  5.744   1.00 116.01 ? 308 TYR F CZ  1 
ATOM   9697  O OH  . TYR F 2 307 ? -50.906  -29.885  5.313   1.00 119.09 ? 308 TYR F OH  1 
ATOM   9698  N N   . VAL F 2 308 ? -45.661  -30.224  7.459   1.00 101.18 ? 309 VAL F N   1 
ATOM   9699  C CA  . VAL F 2 308 ? -45.561  -31.552  6.842   1.00 103.14 ? 309 VAL F CA  1 
ATOM   9700  C C   . VAL F 2 308 ? -46.988  -32.070  6.549   1.00 109.04 ? 309 VAL F C   1 
ATOM   9701  O O   . VAL F 2 308 ? -47.934  -31.656  7.217   1.00 107.77 ? 309 VAL F O   1 
ATOM   9702  C CB  . VAL F 2 308 ? -44.712  -32.569  7.653   1.00 106.13 ? 309 VAL F CB  1 
ATOM   9703  C CG1 . VAL F 2 308 ? -43.223  -32.372  7.398   1.00 105.71 ? 309 VAL F CG1 1 
ATOM   9704  C CG2 . VAL F 2 308 ? -45.026  -32.509  9.146   1.00 104.13 ? 309 VAL F CG2 1 
ATOM   9705  N N   . LYS F 2 309 ? -47.151  -32.933  5.538   1.00 108.42 ? 310 LYS F N   1 
ATOM   9706  C CA  . LYS F 2 309 ? -48.460  -33.468  5.165   1.00 110.58 ? 310 LYS F CA  1 
ATOM   9707  C C   . LYS F 2 309 ? -48.751  -34.820  5.826   1.00 117.14 ? 310 LYS F C   1 
ATOM   9708  O O   . LYS F 2 309 ? -49.890  -35.296  5.773   1.00 118.71 ? 310 LYS F O   1 
ATOM   9709  C CB  . LYS F 2 309 ? -48.604  -33.541  3.635   1.00 116.38 ? 310 LYS F CB  1 
ATOM   9710  C CG  . LYS F 2 309 ? -48.887  -32.187  2.985   1.00 125.37 ? 310 LYS F CG  1 
ATOM   9711  C CD  . LYS F 2 309 ? -49.134  -32.291  1.488   1.00 139.75 ? 310 LYS F CD  1 
ATOM   9712  C CE  . LYS F 2 309 ? -50.600  -32.210  1.125   1.00 155.37 ? 310 LYS F CE  1 
ATOM   9713  N NZ  . LYS F 2 309 ? -50.814  -32.252  -0.347  1.00 171.65 ? 310 LYS F NZ  1 
ATOM   9714  N N   . SER F 2 310 ? -47.720  -35.412  6.472   1.00 113.71 ? 311 SER F N   1 
ATOM   9715  C CA  . SER F 2 310 ? -47.740  -36.711  7.159   1.00 115.06 ? 311 SER F CA  1 
ATOM   9716  C C   . SER F 2 310 ? -48.812  -36.860  8.246   1.00 119.34 ? 311 SER F C   1 
ATOM   9717  O O   . SER F 2 310 ? -49.185  -35.875  8.887   1.00 116.56 ? 311 SER F O   1 
ATOM   9718  C CB  . SER F 2 310 ? -46.363  -37.030  7.734   1.00 116.51 ? 311 SER F CB  1 
ATOM   9719  O OG  . SER F 2 310 ? -45.696  -35.875  8.212   1.00 119.96 ? 311 SER F OG  1 
ATOM   9720  N N   . THR F 2 311 ? -49.297  -38.108  8.441   1.00 119.11 ? 312 THR F N   1 
ATOM   9721  C CA  . THR F 2 311 ? -50.311  -38.493  9.437   1.00 119.73 ? 312 THR F CA  1 
ATOM   9722  C C   . THR F 2 311 ? -49.717  -38.352  10.843  1.00 119.23 ? 312 THR F C   1 
ATOM   9723  O O   . THR F 2 311 ? -50.367  -37.795  11.734  1.00 116.63 ? 312 THR F O   1 
ATOM   9724  C CB  . THR F 2 311 ? -50.796  -39.938  9.185   1.00 140.09 ? 312 THR F CB  1 
ATOM   9725  O OG1 . THR F 2 311 ? -50.855  -40.203  7.780   1.00 146.73 ? 312 THR F OG1 1 
ATOM   9726  C CG2 . THR F 2 311 ? -52.146  -40.227  9.829   1.00 142.60 ? 312 THR F CG2 1 
ATOM   9727  N N   . LYS F 2 312 ? -48.477  -38.865  11.021  1.00 115.14 ? 313 LYS F N   1 
ATOM   9728  C CA  . LYS F 2 312 ? -47.689  -38.819  12.253  1.00 113.02 ? 313 LYS F CA  1 
ATOM   9729  C C   . LYS F 2 312 ? -46.219  -39.135  11.977  1.00 113.95 ? 313 LYS F C   1 
ATOM   9730  O O   . LYS F 2 312 ? -45.905  -39.861  11.028  1.00 114.54 ? 313 LYS F O   1 
ATOM   9731  C CB  . LYS F 2 312 ? -48.249  -39.779  13.320  1.00 118.51 ? 313 LYS F CB  1 
ATOM   9732  C CG  . LYS F 2 312 ? -48.294  -39.169  14.721  1.00 138.16 ? 313 LYS F CG  1 
ATOM   9733  C CD  . LYS F 2 312 ? -49.650  -38.536  15.045  1.00 151.57 ? 313 LYS F CD  1 
ATOM   9734  C CE  . LYS F 2 312 ? -49.806  -38.301  16.527  1.00 165.56 ? 313 LYS F CE  1 
ATOM   9735  N NZ  . LYS F 2 312 ? -51.189  -37.886  16.875  1.00 178.10 ? 313 LYS F NZ  1 
ATOM   9736  N N   . LEU F 2 313 ? -45.327  -38.574  12.814  1.00 107.22 ? 314 LEU F N   1 
ATOM   9737  C CA  . LEU F 2 313 ? -43.877  -38.783  12.768  1.00 105.67 ? 314 LEU F CA  1 
ATOM   9738  C C   . LEU F 2 313 ? -43.412  -39.200  14.166  1.00 109.06 ? 314 LEU F C   1 
ATOM   9739  O O   . LEU F 2 313 ? -43.608  -38.441  15.121  1.00 107.43 ? 314 LEU F O   1 
ATOM   9740  C CB  . LEU F 2 313 ? -43.137  -37.509  12.321  1.00 102.96 ? 314 LEU F CB  1 
ATOM   9741  C CG  . LEU F 2 313 ? -43.353  -37.047  10.897  1.00 107.19 ? 314 LEU F CG  1 
ATOM   9742  C CD1 . LEU F 2 313 ? -42.838  -35.647  10.718  1.00 105.31 ? 314 LEU F CD1 1 
ATOM   9743  C CD2 . LEU F 2 313 ? -42.670  -37.967  9.914   1.00 111.96 ? 314 LEU F CD2 1 
ATOM   9744  N N   . ARG F 2 314 ? -42.816  -40.410  14.290  1.00 106.37 ? 315 ARG F N   1 
ATOM   9745  C CA  . ARG F 2 314 ? -42.366  -40.941  15.580  1.00 106.65 ? 315 ARG F CA  1 
ATOM   9746  C C   . ARG F 2 314 ? -40.942  -41.484  15.541  1.00 109.57 ? 315 ARG F C   1 
ATOM   9747  O O   . ARG F 2 314 ? -40.607  -42.251  14.643  1.00 110.82 ? 315 ARG F O   1 
ATOM   9748  C CB  . ARG F 2 314 ? -43.353  -42.010  16.093  1.00 108.20 ? 315 ARG F CB  1 
ATOM   9749  C CG  . ARG F 2 314 ? -43.157  -42.370  17.555  1.00 113.59 ? 315 ARG F CG  1 
ATOM   9750  C CD  . ARG F 2 314 ? -44.436  -42.821  18.203  1.00 114.68 ? 315 ARG F CD  1 
ATOM   9751  N NE  . ARG F 2 314 ? -44.619  -42.129  19.474  1.00 116.71 ? 315 ARG F NE  1 
ATOM   9752  C CZ  . ARG F 2 314 ? -45.384  -41.057  19.633  1.00 129.24 ? 315 ARG F CZ  1 
ATOM   9753  N NH1 . ARG F 2 314 ? -46.069  -40.565  18.608  1.00 109.84 ? 315 ARG F NH1 1 
ATOM   9754  N NH2 . ARG F 2 314 ? -45.484  -40.477  20.822  1.00 123.21 ? 315 ARG F NH2 1 
ATOM   9755  N N   . LEU F 2 315 ? -40.120  -41.100  16.527  1.00 103.93 ? 316 LEU F N   1 
ATOM   9756  C CA  . LEU F 2 315 ? -38.742  -41.556  16.648  1.00 103.54 ? 316 LEU F CA  1 
ATOM   9757  C C   . LEU F 2 315 ? -38.621  -42.581  17.745  1.00 111.77 ? 316 LEU F C   1 
ATOM   9758  O O   . LEU F 2 315 ? -39.054  -42.321  18.868  1.00 114.01 ? 316 LEU F O   1 
ATOM   9759  C CB  . LEU F 2 315 ? -37.799  -40.392  16.938  1.00 101.62 ? 316 LEU F CB  1 
ATOM   9760  C CG  . LEU F 2 315 ? -37.475  -39.480  15.780  1.00 103.18 ? 316 LEU F CG  1 
ATOM   9761  C CD1 . LEU F 2 315 ? -36.771  -38.254  16.276  1.00 102.51 ? 316 LEU F CD1 1 
ATOM   9762  C CD2 . LEU F 2 315 ? -36.645  -40.192  14.726  1.00 104.59 ? 316 LEU F CD2 1 
ATOM   9763  N N   . ALA F 2 316 ? -38.013  -43.736  17.428  1.00 109.10 ? 317 ALA F N   1 
ATOM   9764  C CA  . ALA F 2 316 ? -37.808  -44.843  18.358  1.00 111.91 ? 317 ALA F CA  1 
ATOM   9765  C C   . ALA F 2 316 ? -36.726  -44.511  19.368  1.00 116.26 ? 317 ALA F C   1 
ATOM   9766  O O   . ALA F 2 316 ? -35.728  -43.880  19.018  1.00 113.11 ? 317 ALA F O   1 
ATOM   9767  C CB  . ALA F 2 316 ? -37.440  -46.103  17.596  1.00 113.78 ? 317 ALA F CB  1 
ATOM   9768  N N   . THR F 2 317 ? -36.936  -44.928  20.622  1.00 117.63 ? 318 THR F N   1 
ATOM   9769  C CA  . THR F 2 317 ? -36.014  -44.712  21.738  1.00 120.38 ? 318 THR F CA  1 
ATOM   9770  C C   . THR F 2 317 ? -35.614  -46.085  22.363  1.00 131.02 ? 318 THR F C   1 
ATOM   9771  O O   . THR F 2 317 ? -34.463  -46.242  22.758  1.00 131.97 ? 318 THR F O   1 
ATOM   9772  C CB  . THR F 2 317 ? -36.611  -43.659  22.707  1.00 128.09 ? 318 THR F CB  1 
ATOM   9773  O OG1 . THR F 2 317 ? -36.911  -42.472  21.974  1.00 120.82 ? 318 THR F OG1 1 
ATOM   9774  C CG2 . THR F 2 317 ? -35.711  -43.324  23.894  1.00 130.91 ? 318 THR F CG2 1 
ATOM   9775  N N   . GLY F 2 318 ? -36.540  -47.054  22.393  1.00 131.31 ? 319 GLY F N   1 
ATOM   9776  C CA  . GLY F 2 318 ? -36.315  -48.411  22.909  1.00 135.96 ? 319 GLY F CA  1 
ATOM   9777  C C   . GLY F 2 318 ? -36.852  -49.506  21.999  1.00 142.01 ? 319 GLY F C   1 
ATOM   9778  O O   . GLY F 2 318 ? -37.492  -49.202  20.993  1.00 138.93 ? 319 GLY F O   1 
ATOM   9779  N N   . LEU F 2 319 ? -36.622  -50.790  22.332  1.00 143.41 ? 320 LEU F N   1 
ATOM   9780  C CA  . LEU F 2 319 ? -37.105  -51.905  21.496  1.00 145.80 ? 320 LEU F CA  1 
ATOM   9781  C C   . LEU F 2 319 ? -38.628  -52.189  21.635  1.00 152.22 ? 320 LEU F C   1 
ATOM   9782  O O   . LEU F 2 319 ? -39.360  -51.350  22.153  1.00 150.76 ? 320 LEU F O   1 
ATOM   9783  C CB  . LEU F 2 319 ? -36.278  -53.188  21.745  1.00 149.94 ? 320 LEU F CB  1 
ATOM   9784  C CG  . LEU F 2 319 ? -34.949  -53.355  20.989  1.00 152.67 ? 320 LEU F CG  1 
ATOM   9785  C CD1 . LEU F 2 319 ? -34.087  -54.410  21.645  1.00 156.68 ? 320 LEU F CD1 1 
ATOM   9786  C CD2 . LEU F 2 319 ? -35.159  -53.744  19.528  1.00 153.02 ? 320 LEU F CD2 1 
ATOM   9787  N N   . ARG F 2 320 ? -39.086  -53.376  21.160  1.00 153.55 ? 321 ARG F N   1 
ATOM   9788  C CA  . ARG F 2 320 ? -40.472  -53.887  21.172  1.00 157.90 ? 321 ARG F CA  1 
ATOM   9789  C C   . ARG F 2 320 ? -40.816  -54.640  22.496  1.00 169.26 ? 321 ARG F C   1 
ATOM   9790  O O   . ARG F 2 320 ? -40.409  -54.156  23.551  1.00 168.49 ? 321 ARG F O   1 
ATOM   9791  C CB  . ARG F 2 320 ? -40.764  -54.731  19.898  1.00 157.64 ? 321 ARG F CB  1 
ATOM   9792  C CG  . ARG F 2 320 ? -39.728  -55.806  19.533  1.00 171.24 ? 321 ARG F CG  1 
ATOM   9793  C CD  . ARG F 2 320 ? -38.525  -55.289  18.730  1.00 170.35 ? 321 ARG F CD  1 
ATOM   9794  N NE  . ARG F 2 320 ? -38.809  -55.081  17.305  1.00 165.95 ? 321 ARG F NE  1 
ATOM   9795  C CZ  . ARG F 2 320 ? -37.888  -55.088  16.343  1.00 163.36 ? 321 ARG F CZ  1 
ATOM   9796  N NH1 . ARG F 2 320 ? -36.608  -55.299  16.638  1.00 142.75 ? 321 ARG F NH1 1 
ATOM   9797  N NH2 . ARG F 2 320 ? -38.240  -54.898  15.079  1.00 142.03 ? 321 ARG F NH2 1 
ATOM   9798  N N   . ASN F 2 321 ? -41.567  -55.794  22.468  1.00 105.73 ? 322 ASN F N   1 
ATOM   9799  C CA  . ASN F 2 321 ? -41.895  -56.559  23.696  1.00 140.56 ? 322 ASN F CA  1 
ATOM   9800  C C   . ASN F 2 321 ? -40.652  -57.176  24.367  1.00 179.75 ? 322 ASN F C   1 
ATOM   9801  O O   . ASN F 2 321 ? -40.061  -58.138  23.877  1.00 142.32 ? 322 ASN F O   1 
ATOM   9802  C CB  . ASN F 2 321 ? -42.985  -57.632  23.463  1.00 141.96 ? 322 ASN F CB  1 
ATOM   9803  C CG  . ASN F 2 321 ? -43.196  -58.588  24.640  1.00 160.63 ? 322 ASN F CG  1 
ATOM   9804  O OD1 . ASN F 2 321 ? -42.888  -59.786  24.563  1.00 154.73 ? 322 ASN F OD1 1 
ATOM   9805  N ND2 . ASN F 2 321 ? -43.709  -58.081  25.761  1.00 149.89 ? 322 ASN F ND2 1 
ATOM   9806  N N   . GLU G 3 1   ? -25.151  -98.354  23.756  1.00 165.83 ? 1   GLU H N   1 
ATOM   9807  C CA  . GLU G 3 1   ? -23.932  -98.918  24.339  1.00 160.72 ? 1   GLU H CA  1 
ATOM   9808  C C   . GLU G 3 1   ? -22.840  -99.171  23.291  1.00 155.98 ? 1   GLU H C   1 
ATOM   9809  O O   . GLU G 3 1   ? -23.133  -99.201  22.095  1.00 153.39 ? 1   GLU H O   1 
ATOM   9810  C CB  . GLU G 3 1   ? -24.244  -100.212 25.118  1.00 160.34 ? 1   GLU H CB  1 
ATOM   9811  C CG  . GLU G 3 1   ? -24.700  -99.980  26.553  1.00 179.32 ? 1   GLU H CG  1 
ATOM   9812  C CD  . GLU G 3 1   ? -23.631  -99.652  27.583  1.00 205.86 ? 1   GLU H CD  1 
ATOM   9813  O OE1 . GLU G 3 1   ? -23.939  -98.880  28.520  1.00 197.35 ? 1   GLU H OE1 1 
ATOM   9814  O OE2 . GLU G 3 1   ? -22.503  -100.190 27.481  1.00 193.76 ? 1   GLU H OE2 1 
ATOM   9815  N N   . VAL G 3 2   ? -21.582  -99.352  23.753  1.00 148.21 ? 2   VAL H N   1 
ATOM   9816  C CA  . VAL G 3 2   ? -20.398  -99.630  22.923  1.00 140.52 ? 2   VAL H CA  1 
ATOM   9817  C C   . VAL G 3 2   ? -19.694  -100.933 23.421  1.00 136.07 ? 2   VAL H C   1 
ATOM   9818  O O   . VAL G 3 2   ? -18.794  -100.864 24.266  1.00 136.96 ? 2   VAL H O   1 
ATOM   9819  C CB  . VAL G 3 2   ? -19.443  -98.394  22.780  1.00 146.25 ? 2   VAL H CB  1 
ATOM   9820  C CG1 . VAL G 3 2   ? -19.992  -97.387  21.773  1.00 148.21 ? 2   VAL H CG1 1 
ATOM   9821  C CG2 . VAL G 3 2   ? -19.157  -97.715  24.125  1.00 151.98 ? 2   VAL H CG2 1 
ATOM   9822  N N   . GLN G 3 3   ? -20.140  -102.124 22.928  1.00 124.14 ? 3   GLN H N   1 
ATOM   9823  C CA  . GLN G 3 3   ? -19.599  -103.410 23.401  1.00 118.12 ? 3   GLN H CA  1 
ATOM   9824  C C   . GLN G 3 3   ? -19.266  -104.439 22.321  1.00 111.38 ? 3   GLN H C   1 
ATOM   9825  O O   . GLN G 3 3   ? -19.895  -104.481 21.272  1.00 108.24 ? 3   GLN H O   1 
ATOM   9826  C CB  . GLN G 3 3   ? -20.509  -104.073 24.466  1.00 122.21 ? 3   GLN H CB  1 
ATOM   9827  C CG  . GLN G 3 3   ? -21.955  -103.556 24.580  1.00 141.62 ? 3   GLN H CG  1 
ATOM   9828  C CD  . GLN G 3 3   ? -22.925  -104.139 23.575  1.00 152.53 ? 3   GLN H CD  1 
ATOM   9829  O OE1 . GLN G 3 3   ? -22.906  -105.337 23.250  1.00 140.70 ? 3   GLN H OE1 1 
ATOM   9830  N NE2 . GLN G 3 3   ? -23.855  -103.311 23.124  1.00 146.71 ? 3   GLN H NE2 1 
ATOM   9831  N N   . LEU G 3 4   ? -18.273  -105.295 22.624  1.00 103.94 ? 4   LEU H N   1 
ATOM   9832  C CA  . LEU G 3 4   ? -17.808  -106.395 21.782  1.00 98.77  ? 4   LEU H CA  1 
ATOM   9833  C C   . LEU G 3 4   ? -18.261  -107.725 22.371  1.00 102.25 ? 4   LEU H C   1 
ATOM   9834  O O   . LEU G 3 4   ? -18.000  -108.019 23.541  1.00 102.63 ? 4   LEU H O   1 
ATOM   9835  C CB  . LEU G 3 4   ? -16.278  -106.374 21.606  1.00 96.33  ? 4   LEU H CB  1 
ATOM   9836  C CG  . LEU G 3 4   ? -15.714  -105.335 20.637  1.00 99.90  ? 4   LEU H CG  1 
ATOM   9837  C CD1 . LEU G 3 4   ? -14.253  -105.104 20.899  1.00 99.44  ? 4   LEU H CD1 1 
ATOM   9838  C CD2 . LEU G 3 4   ? -15.902  -105.756 19.191  1.00 98.61  ? 4   LEU H CD2 1 
ATOM   9839  N N   . VAL G 3 5   ? -18.969  -108.508 21.561  1.00 98.09  ? 5   VAL H N   1 
ATOM   9840  C CA  . VAL G 3 5   ? -19.510  -109.800 21.962  1.00 98.42  ? 5   VAL H CA  1 
ATOM   9841  C C   . VAL G 3 5   ? -18.771  -110.894 21.195  1.00 100.40 ? 5   VAL H C   1 
ATOM   9842  O O   . VAL G 3 5   ? -19.039  -111.105 20.012  1.00 100.33 ? 5   VAL H O   1 
ATOM   9843  C CB  . VAL G 3 5   ? -21.051  -109.865 21.741  1.00 105.26 ? 5   VAL H CB  1 
ATOM   9844  C CG1 . VAL G 3 5   ? -21.635  -111.180 22.256  1.00 105.36 ? 5   VAL H CG1 1 
ATOM   9845  C CG2 . VAL G 3 5   ? -21.767  -108.668 22.373  1.00 109.49 ? 5   VAL H CG2 1 
ATOM   9846  N N   . GLN G 3 6   ? -17.837  -111.582 21.864  1.00 95.21  ? 6   GLN H N   1 
ATOM   9847  C CA  . GLN G 3 6   ? -17.048  -112.658 21.260  1.00 92.75  ? 6   GLN H CA  1 
ATOM   9848  C C   . GLN G 3 6   ? -17.810  -113.982 21.185  1.00 97.90  ? 6   GLN H C   1 
ATOM   9849  O O   . GLN G 3 6   ? -18.901  -114.104 21.746  1.00 98.53  ? 6   GLN H O   1 
ATOM   9850  C CB  . GLN G 3 6   ? -15.735  -112.847 22.026  1.00 93.27  ? 6   GLN H CB  1 
ATOM   9851  C CG  . GLN G 3 6   ? -14.637  -111.911 21.593  1.00 87.98  ? 6   GLN H CG  1 
ATOM   9852  C CD  . GLN G 3 6   ? -13.375  -112.249 22.324  1.00 98.80  ? 6   GLN H CD  1 
ATOM   9853  O OE1 . GLN G 3 6   ? -13.134  -111.776 23.435  1.00 94.28  ? 6   GLN H OE1 1 
ATOM   9854  N NE2 . GLN G 3 6   ? -12.567  -113.119 21.744  1.00 89.38  ? 6   GLN H NE2 1 
ATOM   9855  N N   . SER G 3 7   ? -17.223  -114.975 20.488  1.00 95.70  ? 7   SER H N   1 
ATOM   9856  C CA  . SER G 3 7   ? -17.766  -116.326 20.344  1.00 97.61  ? 7   SER H CA  1 
ATOM   9857  C C   . SER G 3 7   ? -17.693  -117.071 21.687  1.00 105.75 ? 7   SER H C   1 
ATOM   9858  O O   . SER G 3 7   ? -16.866  -116.732 22.543  1.00 105.85 ? 7   SER H O   1 
ATOM   9859  C CB  . SER G 3 7   ? -16.977  -117.100 19.290  1.00 101.85 ? 7   SER H CB  1 
ATOM   9860  O OG  . SER G 3 7   ? -17.362  -118.463 19.209  1.00 112.45 ? 7   SER H OG  1 
ATOM   9861  N N   . GLY G 3 8   ? -18.547  -118.086 21.842  1.00 104.71 ? 8   GLY H N   1 
ATOM   9862  C CA  . GLY G 3 8   ? -18.597  -118.924 23.038  1.00 105.88 ? 8   GLY H CA  1 
ATOM   9863  C C   . GLY G 3 8   ? -17.407  -119.861 23.171  1.00 109.58 ? 8   GLY H C   1 
ATOM   9864  O O   . GLY G 3 8   ? -16.635  -120.030 22.217  1.00 109.73 ? 8   GLY H O   1 
ATOM   9865  N N   . ALA G 3 9   ? -17.260  -120.482 24.366  1.00 105.15 ? 9   ALA H N   1 
ATOM   9866  C CA  . ALA G 3 9   ? -16.187  -121.425 24.700  1.00 104.99 ? 9   ALA H CA  1 
ATOM   9867  C C   . ALA G 3 9   ? -16.109  -122.578 23.703  1.00 107.06 ? 9   ALA H C   1 
ATOM   9868  O O   . ALA G 3 9   ? -17.140  -123.139 23.324  1.00 107.06 ? 9   ALA H O   1 
ATOM   9869  C CB  . ALA G 3 9   ? -16.388  -121.963 26.104  1.00 107.11 ? 9   ALA H CB  1 
ATOM   9870  N N   . GLU G 3 10  ? -14.890  -122.897 23.248  1.00 103.20 ? 10  GLU H N   1 
ATOM   9871  C CA  . GLU G 3 10  ? -14.666  -123.946 22.255  1.00 105.33 ? 10  GLU H CA  1 
ATOM   9872  C C   . GLU G 3 10  ? -13.627  -124.980 22.709  1.00 110.01 ? 10  GLU H C   1 
ATOM   9873  O O   . GLU G 3 10  ? -12.525  -124.614 23.122  1.00 110.36 ? 10  GLU H O   1 
ATOM   9874  C CB  . GLU G 3 10  ? -14.274  -123.332 20.892  1.00 106.77 ? 10  GLU H CB  1 
ATOM   9875  C CG  . GLU G 3 10  ? -15.359  -122.503 20.209  1.00 117.41 ? 10  GLU H CG  1 
ATOM   9876  C CD  . GLU G 3 10  ? -16.594  -123.248 19.730  1.00 150.54 ? 10  GLU H CD  1 
ATOM   9877  O OE1 . GLU G 3 10  ? -16.437  -124.305 19.078  1.00 150.24 ? 10  GLU H OE1 1 
ATOM   9878  O OE2 . GLU G 3 10  ? -17.720  -122.759 19.985  1.00 146.60 ? 10  GLU H OE2 1 
ATOM   9879  N N   . VAL G 3 11  ? -13.994  -126.274 22.645  1.00 107.34 ? 11  VAL H N   1 
ATOM   9880  C CA  . VAL G 3 11  ? -13.115  -127.393 23.006  1.00 110.18 ? 11  VAL H CA  1 
ATOM   9881  C C   . VAL G 3 11  ? -13.036  -128.335 21.804  1.00 119.38 ? 11  VAL H C   1 
ATOM   9882  O O   . VAL G 3 11  ? -14.061  -128.883 21.381  1.00 119.95 ? 11  VAL H O   1 
ATOM   9883  C CB  . VAL G 3 11  ? -13.558  -128.143 24.294  1.00 113.41 ? 11  VAL H CB  1 
ATOM   9884  C CG1 . VAL G 3 11  ? -12.573  -129.253 24.652  1.00 117.32 ? 11  VAL H CG1 1 
ATOM   9885  C CG2 . VAL G 3 11  ? -13.742  -127.188 25.469  1.00 109.37 ? 11  VAL H CG2 1 
ATOM   9886  N N   . LYS G 3 12  ? -11.826  -128.499 21.243  1.00 117.73 ? 12  LYS H N   1 
ATOM   9887  C CA  . LYS G 3 12  ? -11.569  -129.366 20.092  1.00 122.08 ? 12  LYS H CA  1 
ATOM   9888  C C   . LYS G 3 12  ? -10.224  -130.052 20.229  1.00 129.76 ? 12  LYS H C   1 
ATOM   9889  O O   . LYS G 3 12  ? -9.287   -129.459 20.755  1.00 127.08 ? 12  LYS H O   1 
ATOM   9890  C CB  . LYS G 3 12  ? -11.640  -128.584 18.764  1.00 123.15 ? 12  LYS H CB  1 
ATOM   9891  C CG  . LYS G 3 12  ? -13.045  -128.479 18.169  1.00 130.19 ? 12  LYS H CG  1 
ATOM   9892  C CD  . LYS G 3 12  ? -13.028  -127.988 16.724  1.00 137.19 ? 12  LYS H CD  1 
ATOM   9893  C CE  . LYS G 3 12  ? -14.420  -127.825 16.162  1.00 138.90 ? 12  LYS H CE  1 
ATOM   9894  N NZ  . LYS G 3 12  ? -14.399  -127.592 14.693  1.00 153.20 ? 12  LYS H NZ  1 
ATOM   9895  N N   . LYS G 3 13  ? -10.129  -131.297 19.749  1.00 132.68 ? 13  LYS H N   1 
ATOM   9896  C CA  . LYS G 3 13  ? -8.906   -132.099 19.776  1.00 139.38 ? 13  LYS H CA  1 
ATOM   9897  C C   . LYS G 3 13  ? -7.899   -131.556 18.744  1.00 146.19 ? 13  LYS H C   1 
ATOM   9898  O O   . LYS G 3 13  ? -8.331   -131.011 17.727  1.00 143.48 ? 13  LYS H O   1 
ATOM   9899  C CB  . LYS G 3 13  ? -9.234   -133.581 19.533  1.00 148.61 ? 13  LYS H CB  1 
ATOM   9900  C CG  . LYS G 3 13  ? -10.070  -134.192 20.655  1.00 168.73 ? 13  LYS H CG  1 
ATOM   9901  C CD  . LYS G 3 13  ? -10.577  -135.574 20.308  1.00 189.64 ? 13  LYS H CD  1 
ATOM   9902  C CE  . LYS G 3 13  ? -11.651  -136.016 21.267  1.00 203.08 ? 13  LYS H CE  1 
ATOM   9903  N NZ  . LYS G 3 13  ? -11.958  -137.464 21.125  1.00 213.24 ? 13  LYS H NZ  1 
ATOM   9904  N N   . PRO G 3 14  ? -6.569   -131.647 18.992  1.00 146.26 ? 14  PRO H N   1 
ATOM   9905  C CA  . PRO G 3 14  ? -5.596   -131.060 18.051  1.00 148.84 ? 14  PRO H CA  1 
ATOM   9906  C C   . PRO G 3 14  ? -5.652   -131.584 16.623  1.00 158.79 ? 14  PRO H C   1 
ATOM   9907  O O   . PRO G 3 14  ? -6.017   -132.735 16.387  1.00 163.21 ? 14  PRO H O   1 
ATOM   9908  C CB  . PRO G 3 14  ? -4.246   -131.344 18.709  1.00 155.44 ? 14  PRO H CB  1 
ATOM   9909  C CG  . PRO G 3 14  ? -4.557   -131.517 20.150  1.00 156.25 ? 14  PRO H CG  1 
ATOM   9910  C CD  . PRO G 3 14  ? -5.881   -132.218 20.165  1.00 150.31 ? 14  PRO H CD  1 
ATOM   9911  N N   . GLY G 3 15  ? -5.300   -130.702 15.693  1.00 155.71 ? 15  GLY H N   1 
ATOM   9912  C CA  . GLY G 3 15  ? -5.307   -130.957 14.258  1.00 161.91 ? 15  GLY H CA  1 
ATOM   9913  C C   . GLY G 3 15  ? -6.515   -130.346 13.574  1.00 160.64 ? 15  GLY H C   1 
ATOM   9914  O O   . GLY G 3 15  ? -6.427   -129.928 12.415  1.00 162.62 ? 15  GLY H O   1 
ATOM   9915  N N   . GLU G 3 16  ? -7.648   -130.278 14.309  1.00 149.75 ? 16  GLU H N   1 
ATOM   9916  C CA  . GLU G 3 16  ? -8.943   -129.756 13.866  1.00 144.01 ? 16  GLU H CA  1 
ATOM   9917  C C   . GLU G 3 16  ? -8.919   -128.287 13.435  1.00 143.16 ? 16  GLU H C   1 
ATOM   9918  O O   . GLU G 3 16  ? -7.974   -127.559 13.745  1.00 141.09 ? 16  GLU H O   1 
ATOM   9919  C CB  . GLU G 3 16  ? -10.007  -129.970 14.957  1.00 139.90 ? 16  GLU H CB  1 
ATOM   9920  C CG  . GLU G 3 16  ? -10.568  -131.378 15.014  1.00 155.03 ? 16  GLU H CG  1 
ATOM   9921  C CD  . GLU G 3 16  ? -11.723  -131.534 15.982  1.00 160.65 ? 16  GLU H CD  1 
ATOM   9922  O OE1 . GLU G 3 16  ? -11.478  -131.947 17.137  1.00 135.10 ? 16  GLU H OE1 1 
ATOM   9923  O OE2 . GLU G 3 16  ? -12.873  -131.227 15.593  1.00 157.19 ? 16  GLU H OE2 1 
ATOM   9924  N N   . SER G 3 17  ? -9.976   -127.862 12.715  1.00 137.58 ? 17  SER H N   1 
ATOM   9925  C CA  . SER G 3 17  ? -10.159  -126.494 12.235  1.00 132.60 ? 17  SER H CA  1 
ATOM   9926  C C   . SER G 3 17  ? -11.255  -125.801 13.051  1.00 127.14 ? 17  SER H C   1 
ATOM   9927  O O   . SER G 3 17  ? -12.381  -126.306 13.140  1.00 126.44 ? 17  SER H O   1 
ATOM   9928  C CB  . SER G 3 17  ? -10.504  -126.486 10.748  1.00 141.41 ? 17  SER H CB  1 
ATOM   9929  O OG  . SER G 3 17  ? -10.600  -125.164 10.242  1.00 151.06 ? 17  SER H OG  1 
ATOM   9930  N N   . LEU G 3 18  ? -10.903  -124.655 13.660  1.00 116.49 ? 18  LEU H N   1 
ATOM   9931  C CA  . LEU G 3 18  ? -11.790  -123.849 14.499  1.00 108.38 ? 18  LEU H CA  1 
ATOM   9932  C C   . LEU G 3 18  ? -11.718  -122.382 14.085  1.00 109.50 ? 18  LEU H C   1 
ATOM   9933  O O   . LEU G 3 18  ? -10.640  -121.894 13.762  1.00 110.93 ? 18  LEU H O   1 
ATOM   9934  C CB  . LEU G 3 18  ? -11.377  -124.001 15.980  1.00 105.96 ? 18  LEU H CB  1 
ATOM   9935  C CG  . LEU G 3 18  ? -12.279  -123.355 17.031  1.00 103.92 ? 18  LEU H CG  1 
ATOM   9936  C CD1 . LEU G 3 18  ? -13.384  -124.296 17.454  1.00 104.67 ? 18  LEU H CD1 1 
ATOM   9937  C CD2 . LEU G 3 18  ? -11.488  -122.932 18.240  1.00 102.46 ? 18  LEU H CD2 1 
ATOM   9938  N N   . THR G 3 19  ? -12.861  -121.682 14.105  1.00 102.07 ? 19  THR H N   1 
ATOM   9939  C CA  . THR G 3 19  ? -12.951  -120.250 13.793  1.00 98.66  ? 19  THR H CA  1 
ATOM   9940  C C   . THR G 3 19  ? -13.821  -119.568 14.857  1.00 98.62  ? 19  THR H C   1 
ATOM   9941  O O   . THR G 3 19  ? -14.964  -119.987 15.073  1.00 97.97  ? 19  THR H O   1 
ATOM   9942  C CB  . THR G 3 19  ? -13.353  -119.980 12.318  1.00 106.42 ? 19  THR H CB  1 
ATOM   9943  O OG1 . THR G 3 19  ? -13.554  -118.577 12.123  1.00 99.49  ? 19  THR H OG1 1 
ATOM   9944  C CG2 . THR G 3 19  ? -14.586  -120.768 11.862  1.00 106.61 ? 19  THR H CG2 1 
ATOM   9945  N N   . ILE G 3 20  ? -13.257  -118.563 15.562  1.00 92.80  ? 20  ILE H N   1 
ATOM   9946  C CA  . ILE G 3 20  ? -13.963  -117.850 16.635  1.00 89.72  ? 20  ILE H CA  1 
ATOM   9947  C C   . ILE G 3 20  ? -14.285  -116.409 16.240  1.00 93.85  ? 20  ILE H C   1 
ATOM   9948  O O   . ILE G 3 20  ? -13.425  -115.694 15.727  1.00 94.41  ? 20  ILE H O   1 
ATOM   9949  C CB  . ILE G 3 20  ? -13.266  -117.948 18.019  1.00 92.24  ? 20  ILE H CB  1 
ATOM   9950  C CG1 . ILE G 3 20  ? -11.770  -117.538 17.953  1.00 93.92  ? 20  ILE H CG1 1 
ATOM   9951  C CG2 . ILE G 3 20  ? -13.452  -119.356 18.602  1.00 94.37  ? 20  ILE H CG2 1 
ATOM   9952  C CD1 . ILE G 3 20  ? -11.156  -117.105 19.270  1.00 99.34  ? 20  ILE H CD1 1 
ATOM   9953  N N   . SER G 3 21  ? -15.549  -116.013 16.458  1.00 89.74  ? 21  SER H N   1 
ATOM   9954  C CA  . SER G 3 21  ? -16.097  -114.698 16.139  1.00 88.41  ? 21  SER H CA  1 
ATOM   9955  C C   . SER G 3 21  ? -15.888  -113.667 17.254  1.00 92.11  ? 21  SER H C   1 
ATOM   9956  O O   . SER G 3 21  ? -15.446  -114.012 18.356  1.00 92.88  ? 21  SER H O   1 
ATOM   9957  C CB  . SER G 3 21  ? -17.571  -114.809 15.754  1.00 92.01  ? 21  SER H CB  1 
ATOM   9958  O OG  . SER G 3 21  ? -18.330  -115.515 16.722  1.00 102.35 ? 21  SER H OG  1 
ATOM   9959  N N   . CYS G 3 22  ? -16.190  -112.393 16.942  1.00 87.18  ? 22  CYS H N   1 
ATOM   9960  C CA  . CYS G 3 22  ? -16.065  -111.217 17.802  1.00 86.79  ? 22  CYS H CA  1 
ATOM   9961  C C   . CYS G 3 22  ? -16.959  -110.183 17.121  1.00 88.62  ? 22  CYS H C   1 
ATOM   9962  O O   . CYS G 3 22  ? -16.609  -109.697 16.048  1.00 89.42  ? 22  CYS H O   1 
ATOM   9963  C CB  . CYS G 3 22  ? -14.597  -110.782 17.870  1.00 88.09  ? 22  CYS H CB  1 
ATOM   9964  S SG  . CYS G 3 22  ? -14.323  -109.031 18.250  1.00 93.42  ? 22  CYS H SG  1 
ATOM   9965  N N   . LYS G 3 23  ? -18.160  -109.939 17.686  1.00 83.25  ? 23  LYS H N   1 
ATOM   9966  C CA  . LYS G 3 23  ? -19.199  -109.060 17.117  1.00 83.15  ? 23  LYS H CA  1 
ATOM   9967  C C   . LYS G 3 23  ? -19.259  -107.648 17.721  1.00 90.13  ? 23  LYS H C   1 
ATOM   9968  O O   . LYS G 3 23  ? -19.640  -107.479 18.883  1.00 93.20  ? 23  LYS H O   1 
ATOM   9969  C CB  . LYS G 3 23  ? -20.576  -109.742 17.209  1.00 84.65  ? 23  LYS H CB  1 
ATOM   9970  C CG  . LYS G 3 23  ? -21.473  -109.498 16.015  1.00 85.50  ? 23  LYS H CG  1 
ATOM   9971  C CD  . LYS G 3 23  ? -22.467  -108.387 16.261  1.00 94.21  ? 23  LYS H CD  1 
ATOM   9972  C CE  . LYS G 3 23  ? -23.380  -108.200 15.078  1.00 102.09 ? 23  LYS H CE  1 
ATOM   9973  N NZ  . LYS G 3 23  ? -24.172  -106.949 15.191  1.00 113.27 ? 23  LYS H NZ  1 
ATOM   9974  N N   . GLY G 3 24  ? -18.915  -106.655 16.902  1.00 86.18  ? 24  GLY H N   1 
ATOM   9975  C CA  . GLY G 3 24  ? -18.931  -105.246 17.272  1.00 89.21  ? 24  GLY H CA  1 
ATOM   9976  C C   . GLY G 3 24  ? -20.346  -104.726 17.342  1.00 99.52  ? 24  GLY H C   1 
ATOM   9977  O O   . GLY G 3 24  ? -21.109  -104.905 16.390  1.00 100.00 ? 24  GLY H O   1 
ATOM   9978  N N   . SER G 3 25  ? -20.716  -104.095 18.475  1.00 101.00 ? 25  SER H N   1 
ATOM   9979  C CA  . SER G 3 25  ? -22.082  -103.602 18.699  1.00 105.29 ? 25  SER H CA  1 
ATOM   9980  C C   . SER G 3 25  ? -22.186  -102.135 19.135  1.00 112.11 ? 25  SER H C   1 
ATOM   9981  O O   . SER G 3 25  ? -21.413  -101.669 19.971  1.00 112.45 ? 25  SER H O   1 
ATOM   9982  C CB  . SER G 3 25  ? -22.811  -104.498 19.703  1.00 112.09 ? 25  SER H CB  1 
ATOM   9983  O OG  . SER G 3 25  ? -22.475  -105.874 19.585  1.00 119.70 ? 25  SER H OG  1 
ATOM   9984  N N   . GLY G 3 26  ? -23.177  -101.448 18.579  1.00 111.69 ? 26  GLY H N   1 
ATOM   9985  C CA  . GLY G 3 26  ? -23.505  -100.059 18.887  1.00 117.57 ? 26  GLY H CA  1 
ATOM   9986  C C   . GLY G 3 26  ? -22.528  -98.995  18.427  1.00 120.85 ? 26  GLY H C   1 
ATOM   9987  O O   . GLY G 3 26  ? -22.542  -97.879  18.959  1.00 125.46 ? 26  GLY H O   1 
ATOM   9988  N N   . TYR G 3 27  ? -21.688  -99.316  17.424  1.00 112.16 ? 27  TYR H N   1 
ATOM   9989  C CA  . TYR G 3 27  ? -20.697  -98.385  16.868  1.00 111.95 ? 27  TYR H CA  1 
ATOM   9990  C C   . TYR G 3 27  ? -20.344  -98.709  15.398  1.00 111.93 ? 27  TYR H C   1 
ATOM   9991  O O   . TYR G 3 27  ? -20.639  -99.813  14.918  1.00 107.99 ? 27  TYR H O   1 
ATOM   9992  C CB  . TYR G 3 27  ? -19.432  -98.329  17.767  1.00 112.11 ? 27  TYR H CB  1 
ATOM   9993  C CG  . TYR G 3 27  ? -18.411  -99.411  17.486  1.00 107.17 ? 27  TYR H CG  1 
ATOM   9994  C CD1 . TYR G 3 27  ? -18.590  -100.707 17.957  1.00 105.61 ? 27  TYR H CD1 1 
ATOM   9995  C CD2 . TYR G 3 27  ? -17.266  -99.138  16.751  1.00 106.17 ? 27  TYR H CD2 1 
ATOM   9996  C CE1 . TYR G 3 27  ? -17.656  -101.708 17.693  1.00 100.48 ? 27  TYR H CE1 1 
ATOM   9997  C CE2 . TYR G 3 27  ? -16.328  -100.130 16.477  1.00 102.95 ? 27  TYR H CE2 1 
ATOM   9998  C CZ  . TYR G 3 27  ? -16.523  -101.412 16.954  1.00 105.47 ? 27  TYR H CZ  1 
ATOM   9999  O OH  . TYR G 3 27  ? -15.591  -102.377 16.674  1.00 102.53 ? 27  TYR H OH  1 
ATOM   10000 N N   . SER G 3 28  ? -19.689  -97.749  14.701  1.00 110.69 ? 28  SER H N   1 
ATOM   10001 C CA  . SER G 3 28  ? -19.247  -97.908  13.315  1.00 109.70 ? 28  SER H CA  1 
ATOM   10002 C C   . SER G 3 28  ? -18.026  -98.825  13.299  1.00 108.16 ? 28  SER H C   1 
ATOM   10003 O O   . SER G 3 28  ? -16.889  -98.357  13.340  1.00 106.96 ? 28  SER H O   1 
ATOM   10004 C CB  . SER G 3 28  ? -18.935  -96.554  12.684  1.00 117.19 ? 28  SER H CB  1 
ATOM   10005 O OG  . SER G 3 28  ? -18.463  -96.708  11.357  1.00 125.87 ? 28  SER H OG  1 
ATOM   10006 N N   . PHE G 3 29  ? -18.288  -100.145 13.281  1.00 101.66 ? 29  PHE H N   1 
ATOM   10007 C CA  . PHE G 3 29  ? -17.320  -101.246 13.309  1.00 97.32  ? 29  PHE H CA  1 
ATOM   10008 C C   . PHE G 3 29  ? -16.154  -101.076 12.346  1.00 99.32  ? 29  PHE H C   1 
ATOM   10009 O O   . PHE G 3 29  ? -15.014  -101.369 12.716  1.00 96.17  ? 29  PHE H O   1 
ATOM   10010 C CB  . PHE G 3 29  ? -18.046  -102.580 13.070  1.00 97.36  ? 29  PHE H CB  1 
ATOM   10011 C CG  . PHE G 3 29  ? -17.202  -103.831 13.132  1.00 95.27  ? 29  PHE H CG  1 
ATOM   10012 C CD1 . PHE G 3 29  ? -16.882  -104.414 14.350  1.00 96.50  ? 29  PHE H CD1 1 
ATOM   10013 C CD2 . PHE G 3 29  ? -16.773  -104.456 11.971  1.00 96.10  ? 29  PHE H CD2 1 
ATOM   10014 C CE1 . PHE G 3 29  ? -16.127  -105.588 14.407  1.00 94.27  ? 29  PHE H CE1 1 
ATOM   10015 C CE2 . PHE G 3 29  ? -16.035  -105.640 12.028  1.00 96.01  ? 29  PHE H CE2 1 
ATOM   10016 C CZ  . PHE G 3 29  ? -15.713  -106.195 13.246  1.00 92.06  ? 29  PHE H CZ  1 
ATOM   10017 N N   . SER G 3 30  ? -16.447  -100.608 11.123  1.00 98.13  ? 30  SER H N   1 
ATOM   10018 C CA  . SER G 3 30  ? -15.482  -100.394 10.045  1.00 98.61  ? 30  SER H CA  1 
ATOM   10019 C C   . SER G 3 30  ? -14.505  -99.225  10.279  1.00 103.53 ? 30  SER H C   1 
ATOM   10020 O O   . SER G 3 30  ? -13.395  -99.265  9.743   1.00 102.07 ? 30  SER H O   1 
ATOM   10021 C CB  . SER G 3 30  ? -16.195  -100.245 8.704   1.00 105.63 ? 30  SER H CB  1 
ATOM   10022 O OG  . SER G 3 30  ? -17.542  -99.818  8.844   1.00 118.33 ? 30  SER H OG  1 
ATOM   10023 N N   . SER G 3 31  ? -14.904  -98.201  11.078  1.00 102.08 ? 31  SER H N   1 
ATOM   10024 C CA  . SER G 3 31  ? -14.064  -97.034  11.393  1.00 103.17 ? 31  SER H CA  1 
ATOM   10025 C C   . SER G 3 31  ? -12.834  -97.392  12.243  1.00 103.81 ? 31  SER H C   1 
ATOM   10026 O O   . SER G 3 31  ? -11.713  -97.007  11.893  1.00 103.93 ? 31  SER H O   1 
ATOM   10027 C CB  . SER G 3 31  ? -14.879  -95.940  12.082  1.00 109.50 ? 31  SER H CB  1 
ATOM   10028 O OG  . SER G 3 31  ? -15.746  -95.267  11.184  1.00 120.70 ? 31  SER H OG  1 
ATOM   10029 N N   . TYR G 3 32  ? -13.048  -98.134  13.342  1.00 96.97  ? 32  TYR H N   1 
ATOM   10030 C CA  . TYR G 3 32  ? -12.001  -98.527  14.279  1.00 94.02  ? 32  TYR H CA  1 
ATOM   10031 C C   . TYR G 3 32  ? -11.388  -99.883  13.936  1.00 93.73  ? 32  TYR H C   1 
ATOM   10032 O O   . TYR G 3 32  ? -12.112  -100.794 13.527  1.00 92.38  ? 32  TYR H O   1 
ATOM   10033 C CB  . TYR G 3 32  ? -12.564  -98.574  15.702  1.00 95.31  ? 32  TYR H CB  1 
ATOM   10034 C CG  . TYR G 3 32  ? -13.213  -97.297  16.190  1.00 101.48 ? 32  TYR H CG  1 
ATOM   10035 C CD1 . TYR G 3 32  ? -12.504  -96.382  16.959  1.00 105.79 ? 32  TYR H CD1 1 
ATOM   10036 C CD2 . TYR G 3 32  ? -14.560  -97.048  15.962  1.00 104.70 ? 32  TYR H CD2 1 
ATOM   10037 C CE1 . TYR G 3 32  ? -13.113  -95.230  17.459  1.00 112.02 ? 32  TYR H CE1 1 
ATOM   10038 C CE2 . TYR G 3 32  ? -15.179  -95.899  16.451  1.00 110.04 ? 32  TYR H CE2 1 
ATOM   10039 C CZ  . TYR G 3 32  ? -14.453  -94.990  17.200  1.00 121.60 ? 32  TYR H CZ  1 
ATOM   10040 O OH  . TYR G 3 32  ? -15.078  -93.860  17.682  1.00 128.57 ? 32  TYR H OH  1 
ATOM   10041 N N   . TRP G 3 33  ? -10.053  -100.019 14.142  1.00 87.93  ? 33  TRP H N   1 
ATOM   10042 C CA  . TRP G 3 33  ? -9.268   -101.243 13.921  1.00 84.90  ? 33  TRP H CA  1 
ATOM   10043 C C   . TRP G 3 33  ? -9.610   -102.270 15.013  1.00 88.23  ? 33  TRP H C   1 
ATOM   10044 O O   . TRP G 3 33  ? -9.796   -101.871 16.155  1.00 89.48  ? 33  TRP H O   1 
ATOM   10045 C CB  . TRP G 3 33  ? -7.760   -100.925 14.009  1.00 83.26  ? 33  TRP H CB  1 
ATOM   10046 C CG  . TRP G 3 33  ? -7.110   -100.427 12.746  1.00 85.89  ? 33  TRP H CG  1 
ATOM   10047 C CD1 . TRP G 3 33  ? -7.096   -99.143  12.280  1.00 91.18  ? 33  TRP H CD1 1 
ATOM   10048 C CD2 . TRP G 3 33  ? -6.256   -101.177 11.872  1.00 84.61  ? 33  TRP H CD2 1 
ATOM   10049 N NE1 . TRP G 3 33  ? -6.341   -99.063  11.131  1.00 91.06  ? 33  TRP H NE1 1 
ATOM   10050 C CE2 . TRP G 3 33  ? -5.810   -100.296 10.861  1.00 90.29  ? 33  TRP H CE2 1 
ATOM   10051 C CE3 . TRP G 3 33  ? -5.844   -102.516 11.828  1.00 84.15  ? 33  TRP H CE3 1 
ATOM   10052 C CZ2 . TRP G 3 33  ? -5.004   -100.722 9.802   1.00 89.76  ? 33  TRP H CZ2 1 
ATOM   10053 C CZ3 . TRP G 3 33  ? -5.064   -102.943 10.766  1.00 85.90  ? 33  TRP H CZ3 1 
ATOM   10054 C CH2 . TRP G 3 33  ? -4.644   -102.050 9.773   1.00 88.45  ? 33  TRP H CH2 1 
ATOM   10055 N N   . ILE G 3 34  ? -9.676   -103.579 14.681  1.00 82.84  ? 34  ILE H N   1 
ATOM   10056 C CA  . ILE G 3 34  ? -9.954   -104.661 15.646  1.00 80.81  ? 34  ILE H CA  1 
ATOM   10057 C C   . ILE G 3 34  ? -8.737   -105.567 15.752  1.00 83.24  ? 34  ILE H C   1 
ATOM   10058 O O   . ILE G 3 34  ? -8.277   -106.095 14.745  1.00 83.78  ? 34  ILE H O   1 
ATOM   10059 C CB  . ILE G 3 34  ? -11.255  -105.461 15.312  1.00 83.47  ? 34  ILE H CB  1 
ATOM   10060 C CG1 . ILE G 3 34  ? -12.528  -104.579 15.396  1.00 86.19  ? 34  ILE H CG1 1 
ATOM   10061 C CG2 . ILE G 3 34  ? -11.392  -106.743 16.158  1.00 81.74  ? 34  ILE H CG2 1 
ATOM   10062 C CD1 . ILE G 3 34  ? -12.913  -104.048 16.791  1.00 96.48  ? 34  ILE H CD1 1 
ATOM   10063 N N   . GLY G 3 35  ? -8.236   -105.736 16.964  1.00 79.29  ? 35  GLY H N   1 
ATOM   10064 C CA  . GLY G 3 35  ? -7.088   -106.587 17.242  1.00 79.12  ? 35  GLY H CA  1 
ATOM   10065 C C   . GLY G 3 35  ? -7.448   -107.905 17.891  1.00 84.23  ? 35  GLY H C   1 
ATOM   10066 O O   . GLY G 3 35  ? -8.629   -108.204 18.076  1.00 85.47  ? 35  GLY H O   1 
ATOM   10067 N N   . TRP G 3 36  ? -6.431   -108.701 18.242  1.00 79.61  ? 36  TRP H N   1 
ATOM   10068 C CA  . TRP G 3 36  ? -6.612   -109.992 18.899  1.00 78.41  ? 36  TRP H CA  1 
ATOM   10069 C C   . TRP G 3 36  ? -5.481   -110.254 19.896  1.00 82.22  ? 36  TRP H C   1 
ATOM   10070 O O   . TRP G 3 36  ? -4.310   -110.179 19.528  1.00 83.04  ? 36  TRP H O   1 
ATOM   10071 C CB  . TRP G 3 36  ? -6.715   -111.120 17.864  1.00 76.47  ? 36  TRP H CB  1 
ATOM   10072 C CG  . TRP G 3 36  ? -8.057   -111.247 17.216  1.00 76.72  ? 36  TRP H CG  1 
ATOM   10073 C CD1 . TRP G 3 36  ? -8.456   -110.673 16.047  1.00 79.56  ? 36  TRP H CD1 1 
ATOM   10074 C CD2 . TRP G 3 36  ? -9.167   -112.029 17.681  1.00 75.80  ? 36  TRP H CD2 1 
ATOM   10075 N NE1 . TRP G 3 36  ? -9.750   -111.040 15.754  1.00 78.91  ? 36  TRP H NE1 1 
ATOM   10076 C CE2 . TRP G 3 36  ? -10.213  -111.873 16.741  1.00 79.85  ? 36  TRP H CE2 1 
ATOM   10077 C CE3 . TRP G 3 36  ? -9.387   -112.841 18.806  1.00 76.92  ? 36  TRP H CE3 1 
ATOM   10078 C CZ2 . TRP G 3 36  ? -11.458  -112.497 16.893  1.00 78.52  ? 36  TRP H CZ2 1 
ATOM   10079 C CZ3 . TRP G 3 36  ? -10.624  -113.450 18.957  1.00 77.90  ? 36  TRP H CZ3 1 
ATOM   10080 C CH2 . TRP G 3 36  ? -11.641  -113.279 18.008  1.00 78.09  ? 36  TRP H CH2 1 
ATOM   10081 N N   . VAL G 3 37  ? -5.831   -110.546 21.157  1.00 77.84  ? 37  VAL H N   1 
ATOM   10082 C CA  . VAL G 3 37  ? -4.879   -110.805 22.238  1.00 79.11  ? 37  VAL H CA  1 
ATOM   10083 C C   . VAL G 3 37  ? -5.122   -112.191 22.887  1.00 87.37  ? 37  VAL H C   1 
ATOM   10084 O O   . VAL G 3 37  ? -6.211   -112.456 23.395  1.00 86.84  ? 37  VAL H O   1 
ATOM   10085 C CB  . VAL G 3 37  ? -4.854   -109.641 23.274  1.00 82.77  ? 37  VAL H CB  1 
ATOM   10086 C CG1 . VAL G 3 37  ? -3.958   -109.967 24.464  1.00 84.14  ? 37  VAL H CG1 1 
ATOM   10087 C CG2 . VAL G 3 37  ? -4.415   -108.329 22.624  1.00 82.35  ? 37  VAL H CG2 1 
ATOM   10088 N N   . ARG G 3 38  ? -4.096   -113.069 22.846  1.00 86.72  ? 38  ARG H N   1 
ATOM   10089 C CA  . ARG G 3 38  ? -4.094   -114.418 23.426  1.00 87.87  ? 38  ARG H CA  1 
ATOM   10090 C C   . ARG G 3 38  ? -3.544   -114.351 24.853  1.00 96.77  ? 38  ARG H C   1 
ATOM   10091 O O   . ARG G 3 38  ? -2.730   -113.485 25.165  1.00 97.58  ? 38  ARG H O   1 
ATOM   10092 C CB  . ARG G 3 38  ? -3.245   -115.380 22.556  1.00 86.25  ? 38  ARG H CB  1 
ATOM   10093 C CG  . ARG G 3 38  ? -2.847   -116.704 23.221  1.00 94.92  ? 38  ARG H CG  1 
ATOM   10094 C CD  . ARG G 3 38  ? -2.362   -117.747 22.244  1.00 107.47 ? 38  ARG H CD  1 
ATOM   10095 N NE  . ARG G 3 38  ? -0.942   -118.043 22.409  1.00 129.24 ? 38  ARG H NE  1 
ATOM   10096 C CZ  . ARG G 3 38  ? -0.297   -119.016 21.770  1.00 157.10 ? 38  ARG H CZ  1 
ATOM   10097 N NH1 . ARG G 3 38  ? -0.945   -119.804 20.917  1.00 148.42 ? 38  ARG H NH1 1 
ATOM   10098 N NH2 . ARG G 3 38  ? 0.999    -119.209 21.978  1.00 152.87 ? 38  ARG H NH2 1 
ATOM   10099 N N   . ARG G 3 39  ? -3.985   -115.274 25.705  1.00 96.36  ? 39  ARG H N   1 
ATOM   10100 C CA  . ARG G 3 39  ? -3.547   -115.417 27.084  1.00 99.63  ? 39  ARG H CA  1 
ATOM   10101 C C   . ARG G 3 39  ? -3.461   -116.917 27.345  1.00 107.20 ? 39  ARG H C   1 
ATOM   10102 O O   . ARG G 3 39  ? -4.483   -117.610 27.348  1.00 105.51 ? 39  ARG H O   1 
ATOM   10103 C CB  . ARG G 3 39  ? -4.523   -114.690 28.045  1.00 99.71  ? 39  ARG H CB  1 
ATOM   10104 C CG  . ARG G 3 39  ? -4.563   -115.191 29.498  1.00 110.69 ? 39  ARG H CG  1 
ATOM   10105 C CD  . ARG G 3 39  ? -3.485   -114.595 30.370  1.00 122.07 ? 39  ARG H CD  1 
ATOM   10106 N NE  . ARG G 3 39  ? -3.848   -113.259 30.836  1.00 130.61 ? 39  ARG H NE  1 
ATOM   10107 C CZ  . ARG G 3 39  ? -3.041   -112.464 31.529  1.00 150.00 ? 39  ARG H CZ  1 
ATOM   10108 N NH1 . ARG G 3 39  ? -1.810   -112.857 31.832  1.00 141.81 ? 39  ARG H NH1 1 
ATOM   10109 N NH2 . ARG G 3 39  ? -3.454   -111.267 31.915  1.00 139.24 ? 39  ARG H NH2 1 
ATOM   10110 N N   . MET G 3 40  ? -2.242   -117.428 27.499  1.00 108.19 ? 40  MET H N   1 
ATOM   10111 C CA  . MET G 3 40  ? -2.063   -118.847 27.769  1.00 111.30 ? 40  MET H CA  1 
ATOM   10112 C C   . MET G 3 40  ? -2.197   -119.149 29.275  1.00 119.60 ? 40  MET H C   1 
ATOM   10113 O O   . MET G 3 40  ? -1.853   -118.281 30.082  1.00 121.20 ? 40  MET H O   1 
ATOM   10114 C CB  . MET G 3 40  ? -0.748   -119.354 27.179  1.00 115.65 ? 40  MET H CB  1 
ATOM   10115 C CG  . MET G 3 40  ? -0.924   -119.925 25.795  1.00 117.92 ? 40  MET H CG  1 
ATOM   10116 S SD  . MET G 3 40  ? 0.195    -121.292 25.426  1.00 126.58 ? 40  MET H SD  1 
ATOM   10117 C CE  . MET G 3 40  ? -0.515   -122.605 26.422  1.00 125.84 ? 40  MET H CE  1 
ATOM   10118 N N   . PRO G 3 41  ? -2.721   -120.336 29.686  1.00 117.22 ? 41  PRO H N   1 
ATOM   10119 C CA  . PRO G 3 41  ? -2.876   -120.616 31.127  1.00 119.72 ? 41  PRO H CA  1 
ATOM   10120 C C   . PRO G 3 41  ? -1.584   -120.494 31.931  1.00 126.10 ? 41  PRO H C   1 
ATOM   10121 O O   . PRO G 3 41  ? -0.626   -121.231 31.702  1.00 127.41 ? 41  PRO H O   1 
ATOM   10122 C CB  . PRO G 3 41  ? -3.455   -122.036 31.161  1.00 122.85 ? 41  PRO H CB  1 
ATOM   10123 C CG  . PRO G 3 41  ? -3.134   -122.619 29.827  1.00 126.37 ? 41  PRO H CG  1 
ATOM   10124 C CD  . PRO G 3 41  ? -3.208   -121.471 28.876  1.00 118.13 ? 41  PRO H CD  1 
ATOM   10125 N N   . GLY G 3 42  ? -1.576   -119.525 32.839  1.00 124.00 ? 42  GLY H N   1 
ATOM   10126 C CA  . GLY G 3 42  ? -0.442   -119.233 33.706  1.00 128.20 ? 42  GLY H CA  1 
ATOM   10127 C C   . GLY G 3 42  ? 0.697    -118.551 32.981  1.00 132.26 ? 42  GLY H C   1 
ATOM   10128 O O   . GLY G 3 42  ? 1.864    -118.796 33.296  1.00 136.32 ? 42  GLY H O   1 
ATOM   10129 N N   . LYS G 3 43  ? 0.360    -117.701 31.996  1.00 124.02 ? 43  LYS H N   1 
ATOM   10130 C CA  . LYS G 3 43  ? 1.316    -116.935 31.192  1.00 122.51 ? 43  LYS H CA  1 
ATOM   10131 C C   . LYS G 3 43  ? 0.815    -115.497 30.968  1.00 123.16 ? 43  LYS H C   1 
ATOM   10132 O O   . LYS G 3 43  ? -0.284   -115.157 31.407  1.00 121.23 ? 43  LYS H O   1 
ATOM   10133 C CB  . LYS G 3 43  ? 1.607    -117.655 29.861  1.00 123.33 ? 43  LYS H CB  1 
ATOM   10134 C CG  . LYS G 3 43  ? 2.671    -118.747 29.972  1.00 135.01 ? 43  LYS H CG  1 
ATOM   10135 C CD  . LYS G 3 43  ? 2.062    -120.144 30.037  1.00 141.57 ? 43  LYS H CD  1 
ATOM   10136 C CE  . LYS G 3 43  ? 2.960    -121.161 30.697  1.00 153.97 ? 43  LYS H CE  1 
ATOM   10137 N NZ  . LYS G 3 43  ? 4.057    -121.604 29.797  1.00 163.16 ? 43  LYS H NZ  1 
ATOM   10138 N N   . GLY G 3 44  ? 1.634    -114.666 30.326  1.00 119.47 ? 44  GLY H N   1 
ATOM   10139 C CA  . GLY G 3 44  ? 1.299    -113.274 30.041  1.00 117.48 ? 44  GLY H CA  1 
ATOM   10140 C C   . GLY G 3 44  ? 0.447    -113.084 28.799  1.00 118.43 ? 44  GLY H C   1 
ATOM   10141 O O   . GLY G 3 44  ? 0.167    -114.048 28.075  1.00 117.60 ? 44  GLY H O   1 
ATOM   10142 N N   . LEU G 3 45  ? 0.026    -111.826 28.548  1.00 112.50 ? 45  LEU H N   1 
ATOM   10143 C CA  . LEU G 3 45  ? -0.789   -111.474 27.384  1.00 108.51 ? 45  LEU H CA  1 
ATOM   10144 C C   . LEU G 3 45  ? 0.066    -111.358 26.126  1.00 111.43 ? 45  LEU H C   1 
ATOM   10145 O O   . LEU G 3 45  ? 1.047    -110.615 26.098  1.00 112.21 ? 45  LEU H O   1 
ATOM   10146 C CB  . LEU G 3 45  ? -1.589   -110.185 27.619  1.00 107.54 ? 45  LEU H CB  1 
ATOM   10147 C CG  . LEU G 3 45  ? -2.685   -110.264 28.665  1.00 112.62 ? 45  LEU H CG  1 
ATOM   10148 C CD1 . LEU G 3 45  ? -3.022   -108.894 29.187  1.00 113.72 ? 45  LEU H CD1 1 
ATOM   10149 C CD2 . LEU G 3 45  ? -3.927   -110.947 28.121  1.00 112.45 ? 45  LEU H CD2 1 
ATOM   10150 N N   . GLU G 3 46  ? -0.306   -112.115 25.098  1.00 106.17 ? 46  GLU H N   1 
ATOM   10151 C CA  . GLU G 3 46  ? 0.379    -112.163 23.814  1.00 105.33 ? 46  GLU H CA  1 
ATOM   10152 C C   . GLU G 3 46  ? -0.481   -111.457 22.778  1.00 107.36 ? 46  GLU H C   1 
ATOM   10153 O O   . GLU G 3 46  ? -1.666   -111.760 22.664  1.00 105.59 ? 46  GLU H O   1 
ATOM   10154 C CB  . GLU G 3 46  ? 0.616    -113.631 23.390  1.00 107.56 ? 46  GLU H CB  1 
ATOM   10155 C CG  . GLU G 3 46  ? 1.465    -114.443 24.361  1.00 122.34 ? 46  GLU H CG  1 
ATOM   10156 C CD  . GLU G 3 46  ? 1.306    -115.951 24.283  1.00 141.14 ? 46  GLU H CD  1 
ATOM   10157 O OE1 . GLU G 3 46  ? 0.822    -116.548 25.273  1.00 137.06 ? 46  GLU H OE1 1 
ATOM   10158 O OE2 . GLU G 3 46  ? 1.693    -116.540 23.246  1.00 130.98 ? 46  GLU H OE2 1 
ATOM   10159 N N   . TRP G 3 47  ? 0.100    -110.519 22.028  1.00 111.82 ? 47  TRP H N   1 
ATOM   10160 C CA  . TRP G 3 47  ? -0.633   -109.829 20.968  1.00 109.79 ? 47  TRP H CA  1 
ATOM   10161 C C   . TRP G 3 47  ? -0.515   -110.639 19.662  1.00 110.39 ? 47  TRP H C   1 
ATOM   10162 O O   . TRP G 3 47  ? 0.580    -111.084 19.305  1.00 111.29 ? 47  TRP H O   1 
ATOM   10163 C CB  . TRP G 3 47  ? -0.117   -108.400 20.807  1.00 110.34 ? 47  TRP H CB  1 
ATOM   10164 C CG  . TRP G 3 47  ? -0.775   -107.597 19.723  1.00 109.90 ? 47  TRP H CG  1 
ATOM   10165 C CD1 . TRP G 3 47  ? -1.890   -106.820 19.843  1.00 111.58 ? 47  TRP H CD1 1 
ATOM   10166 C CD2 . TRP G 3 47  ? -0.302   -107.419 18.376  1.00 109.36 ? 47  TRP H CD2 1 
ATOM   10167 N NE1 . TRP G 3 47  ? -2.165   -106.201 18.645  1.00 109.77 ? 47  TRP H NE1 1 
ATOM   10168 C CE2 . TRP G 3 47  ? -1.198   -106.539 17.731  1.00 111.64 ? 47  TRP H CE2 1 
ATOM   10169 C CE3 . TRP G 3 47  ? 0.791    -107.926 17.646  1.00 112.06 ? 47  TRP H CE3 1 
ATOM   10170 C CZ2 . TRP G 3 47  ? -1.028   -106.142 16.396  1.00 110.25 ? 47  TRP H CZ2 1 
ATOM   10171 C CZ3 . TRP G 3 47  ? 0.949    -107.546 16.319  1.00 112.89 ? 47  TRP H CZ3 1 
ATOM   10172 C CH2 . TRP G 3 47  ? 0.045    -106.668 15.707  1.00 111.70 ? 47  TRP H CH2 1 
ATOM   10173 N N   . MET G 3 48  ? -1.648   -110.852 18.975  1.00 103.04 ? 48  MET H N   1 
ATOM   10174 C CA  . MET G 3 48  ? -1.703   -111.647 17.752  1.00 101.17 ? 48  MET H CA  1 
ATOM   10175 C C   . MET G 3 48  ? -1.683   -110.838 16.464  1.00 104.85 ? 48  MET H C   1 
ATOM   10176 O O   . MET G 3 48  ? -0.903   -111.161 15.571  1.00 106.20 ? 48  MET H O   1 
ATOM   10177 C CB  . MET G 3 48  ? -2.906   -112.585 17.766  1.00 101.54 ? 48  MET H CB  1 
ATOM   10178 C CG  . MET G 3 48  ? -2.811   -113.651 18.811  1.00 106.09 ? 48  MET H CG  1 
ATOM   10179 S SD  . MET G 3 48  ? -4.209   -114.781 18.739  1.00 108.75 ? 48  MET H SD  1 
ATOM   10180 C CE  . MET G 3 48  ? -5.356   -113.883 19.678  1.00 105.09 ? 48  MET H CE  1 
ATOM   10181 N N   . GLY G 3 49  ? -2.562   -109.842 16.348  1.00 98.85  ? 49  GLY H N   1 
ATOM   10182 C CA  . GLY G 3 49  ? -2.664   -109.008 15.153  1.00 96.99  ? 49  GLY H CA  1 
ATOM   10183 C C   . GLY G 3 49  ? -3.787   -107.992 15.187  1.00 96.50  ? 49  GLY H C   1 
ATOM   10184 O O   . GLY G 3 49  ? -4.482   -107.883 16.201  1.00 95.80  ? 49  GLY H O   1 
ATOM   10185 N N   . ILE G 3 50  ? -3.986   -107.252 14.058  1.00 89.78  ? 50  ILE H N   1 
ATOM   10186 C CA  . ILE G 3 50  ? -5.033   -106.217 13.884  1.00 87.33  ? 50  ILE H CA  1 
ATOM   10187 C C   . ILE G 3 50  ? -5.612   -106.153 12.461  1.00 91.63  ? 50  ILE H C   1 
ATOM   10188 O O   . ILE G 3 50  ? -4.873   -106.360 11.498  1.00 93.29  ? 50  ILE H O   1 
ATOM   10189 C CB  . ILE G 3 50  ? -4.597   -104.792 14.338  1.00 90.04  ? 50  ILE H CB  1 
ATOM   10190 C CG1 . ILE G 3 50  ? -3.217   -104.397 13.765  1.00 91.20  ? 50  ILE H CG1 1 
ATOM   10191 C CG2 . ILE G 3 50  ? -4.666   -104.623 15.852  1.00 91.15  ? 50  ILE H CG2 1 
ATOM   10192 C CD1 . ILE G 3 50  ? -2.925   -102.895 13.734  1.00 93.88  ? 50  ILE H CD1 1 
ATOM   10193 N N   . ILE G 3 51  ? -6.917   -105.822 12.329  1.00 87.16  ? 51  ILE H N   1 
ATOM   10194 C CA  . ILE G 3 51  ? -7.602   -105.653 11.039  1.00 87.56  ? 51  ILE H CA  1 
ATOM   10195 C C   . ILE G 3 51  ? -8.382   -104.351 11.010  1.00 93.52  ? 51  ILE H C   1 
ATOM   10196 O O   . ILE G 3 51  ? -9.102   -104.062 11.966  1.00 92.95  ? 51  ILE H O   1 
ATOM   10197 C CB  . ILE G 3 51  ? -8.569   -106.818 10.634  1.00 90.33  ? 51  ILE H CB  1 
ATOM   10198 C CG1 . ILE G 3 51  ? -7.893   -108.199 10.628  1.00 91.55  ? 51  ILE H CG1 1 
ATOM   10199 C CG2 . ILE G 3 51  ? -9.241   -106.528 9.262   1.00 91.12  ? 51  ILE H CG2 1 
ATOM   10200 C CD1 . ILE G 3 51  ? -8.732   -109.300 9.977   1.00 91.24  ? 51  ILE H CD1 1 
ATOM   10201 N N   . ASN G 3 52  ? -8.286   -103.594 9.898   1.00 92.06  ? 52  ASN H N   1 
ATOM   10202 C CA  . ASN G 3 52  ? -9.116   -102.412 9.693   1.00 92.17  ? 52  ASN H CA  1 
ATOM   10203 C C   . ASN G 3 52  ? -10.298  -102.974 8.904   1.00 96.95  ? 52  ASN H C   1 
ATOM   10204 O O   . ASN G 3 52  ? -10.088  -103.349 7.756   1.00 98.49  ? 52  ASN H O   1 
ATOM   10205 C CB  . ASN G 3 52  ? -8.388   -101.324 8.886   1.00 94.99  ? 52  ASN H CB  1 
ATOM   10206 C CG  . ASN G 3 52  ? -9.168   -100.028 8.711   1.00 118.65 ? 52  ASN H CG  1 
ATOM   10207 O OD1 . ASN G 3 52  ? -9.257   -99.493  7.611   1.00 116.28 ? 52  ASN H OD1 1 
ATOM   10208 N ND2 . ASN G 3 52  ? -9.722   -99.461  9.783   1.00 105.49 ? 52  ASN H ND2 1 
ATOM   10209 N N   . PRO G 3 53  ? -11.505  -103.133 9.499   1.00 92.66  ? 53  PRO H N   1 
ATOM   10210 C CA  . PRO G 3 53  ? -12.629  -103.758 8.768   1.00 92.97  ? 53  PRO H CA  1 
ATOM   10211 C C   . PRO G 3 53  ? -13.027  -103.138 7.421   1.00 98.96  ? 53  PRO H C   1 
ATOM   10212 O O   . PRO G 3 53  ? -13.522  -103.881 6.569   1.00 99.69  ? 53  PRO H O   1 
ATOM   10213 C CB  . PRO G 3 53  ? -13.779  -103.698 9.766   1.00 93.92  ? 53  PRO H CB  1 
ATOM   10214 C CG  . PRO G 3 53  ? -13.108  -103.637 11.100  1.00 98.16  ? 53  PRO H CG  1 
ATOM   10215 C CD  . PRO G 3 53  ? -11.898  -102.798 10.879  1.00 93.88  ? 53  PRO H CD  1 
ATOM   10216 N N   . ARG G 3 54  ? -12.828  -101.819 7.210   1.00 95.79  ? 54  ARG H N   1 
ATOM   10217 C CA  . ARG G 3 54  ? -13.155  -101.197 5.916   1.00 96.45  ? 54  ARG H CA  1 
ATOM   10218 C C   . ARG G 3 54  ? -12.113  -101.545 4.832   1.00 100.10 ? 54  ARG H C   1 
ATOM   10219 O O   . ARG G 3 54  ? -12.496  -101.820 3.695   1.00 100.87 ? 54  ARG H O   1 
ATOM   10220 C CB  . ARG G 3 54  ? -13.408  -99.671  6.026   1.00 98.78  ? 54  ARG H CB  1 
ATOM   10221 C CG  . ARG G 3 54  ? -12.344  -98.880  6.786   1.00 117.21 ? 54  ARG H CG  1 
ATOM   10222 C CD  . ARG G 3 54  ? -12.260  -97.426  6.359   1.00 139.20 ? 54  ARG H CD  1 
ATOM   10223 N NE  . ARG G 3 54  ? -10.893  -96.910  6.499   1.00 161.38 ? 54  ARG H NE  1 
ATOM   10224 C CZ  . ARG G 3 54  ? -10.440  -95.798  5.926   1.00 181.48 ? 54  ARG H CZ  1 
ATOM   10225 N NH1 . ARG G 3 54  ? -11.241  -95.058  5.167   1.00 172.29 ? 54  ARG H NH1 1 
ATOM   10226 N NH2 . ARG G 3 54  ? -9.180   -95.418  6.104   1.00 168.01 ? 54  ARG H NH2 1 
ATOM   10227 N N   . ASP G 3 55  ? -10.807  -101.563 5.206   1.00 95.77  ? 55  ASP H N   1 
ATOM   10228 C CA  . ASP G 3 55  ? -9.656   -101.877 4.341   1.00 96.38  ? 55  ASP H CA  1 
ATOM   10229 C C   . ASP G 3 55  ? -9.405   -103.390 4.233   1.00 99.76  ? 55  ASP H C   1 
ATOM   10230 O O   . ASP G 3 55  ? -8.687   -103.825 3.336   1.00 100.42 ? 55  ASP H O   1 
ATOM   10231 C CB  . ASP G 3 55  ? -8.371   -101.158 4.840   1.00 97.87  ? 55  ASP H CB  1 
ATOM   10232 C CG  . ASP G 3 55  ? -8.190   -99.701  4.404   1.00 105.83 ? 55  ASP H CG  1 
ATOM   10233 O OD1 . ASP G 3 55  ? -8.390   -99.404  3.203   1.00 108.02 ? 55  ASP H OD1 1 
ATOM   10234 O OD2 . ASP G 3 55  ? -7.754   -98.882  5.240   1.00 107.55 ? 55  ASP H OD2 1 
ATOM   10235 N N   . SER G 3 56  ? -9.996   -104.182 5.151   1.00 95.68  ? 56  SER H N   1 
ATOM   10236 C CA  . SER G 3 56  ? -9.894   -105.644 5.283   1.00 96.46  ? 56  SER H CA  1 
ATOM   10237 C C   . SER G 3 56  ? -8.448   -106.165 5.269   1.00 102.63 ? 56  SER H C   1 
ATOM   10238 O O   . SER G 3 56  ? -8.208   -107.321 4.919   1.00 102.74 ? 56  SER H O   1 
ATOM   10239 C CB  . SER G 3 56  ? -10.760  -106.352 4.247   1.00 102.30 ? 56  SER H CB  1 
ATOM   10240 O OG  . SER G 3 56  ? -10.380  -105.985 2.932   1.00 118.12 ? 56  SER H OG  1 
ATOM   10241 N N   . ASP G 3 57  ? -7.494   -105.312 5.682   1.00 101.72 ? 57  ASP H N   1 
ATOM   10242 C CA  . ASP G 3 57  ? -6.068   -105.639 5.734   1.00 104.37 ? 57  ASP H CA  1 
ATOM   10243 C C   . ASP G 3 57  ? -5.647   -106.176 7.106   1.00 108.32 ? 57  ASP H C   1 
ATOM   10244 O O   . ASP G 3 57  ? -6.131   -105.691 8.134   1.00 106.54 ? 57  ASP H O   1 
ATOM   10245 C CB  . ASP G 3 57  ? -5.197   -104.438 5.298   1.00 107.94 ? 57  ASP H CB  1 
ATOM   10246 C CG  . ASP G 3 57  ? -5.106   -103.266 6.273   1.00 120.76 ? 57  ASP H CG  1 
ATOM   10247 O OD1 . ASP G 3 57  ? -6.172   -102.830 6.789   1.00 121.70 ? 57  ASP H OD1 1 
ATOM   10248 O OD2 . ASP G 3 57  ? -3.974   -102.749 6.479   1.00 123.01 ? 57  ASP H OD2 1 
ATOM   10249 N N   . THR G 3 58  ? -4.737   -107.170 7.113   1.00 106.03 ? 58  THR H N   1 
ATOM   10250 C CA  . THR G 3 58  ? -4.254   -107.822 8.332   1.00 105.30 ? 58  THR H CA  1 
ATOM   10251 C C   . THR G 3 58  ? -2.759   -107.632 8.536   1.00 109.94 ? 58  THR H C   1 
ATOM   10252 O O   . THR G 3 58  ? -1.976   -107.742 7.586   1.00 111.17 ? 58  THR H O   1 
ATOM   10253 C CB  . THR G 3 58  ? -4.605   -109.320 8.321   1.00 114.87 ? 58  THR H CB  1 
ATOM   10254 O OG1 . THR G 3 58  ? -5.864   -109.528 7.677   1.00 118.00 ? 58  THR H OG1 1 
ATOM   10255 C CG2 . THR G 3 58  ? -4.633   -109.923 9.711   1.00 111.15 ? 58  THR H CG2 1 
ATOM   10256 N N   . ARG G 3 59  ? -2.374   -107.371 9.795   1.00 105.87 ? 59  ARG H N   1 
ATOM   10257 C CA  . ARG G 3 59  ? -0.991   -107.201 10.234  1.00 107.36 ? 59  ARG H CA  1 
ATOM   10258 C C   . ARG G 3 59  ? -0.772   -108.197 11.382  1.00 113.55 ? 59  ARG H C   1 
ATOM   10259 O O   . ARG G 3 59  ? -1.160   -107.916 12.516  1.00 112.77 ? 59  ARG H O   1 
ATOM   10260 C CB  . ARG G 3 59  ? -0.713   -105.740 10.668  1.00 105.54 ? 59  ARG H CB  1 
ATOM   10261 C CG  . ARG G 3 59  ? -1.203   -104.698 9.665   1.00 111.04 ? 59  ARG H CG  1 
ATOM   10262 C CD  . ARG G 3 59  ? -0.504   -103.363 9.768   1.00 122.42 ? 59  ARG H CD  1 
ATOM   10263 N NE  . ARG G 3 59  ? -0.828   -102.523 8.612   1.00 137.07 ? 59  ARG H NE  1 
ATOM   10264 C CZ  . ARG G 3 59  ? -0.070   -102.403 7.523   1.00 158.15 ? 59  ARG H CZ  1 
ATOM   10265 N NH1 . ARG G 3 59  ? 1.090    -103.047 7.435   1.00 148.48 ? 59  ARG H NH1 1 
ATOM   10266 N NH2 . ARG G 3 59  ? -0.457   -101.626 6.521   1.00 148.03 ? 59  ARG H NH2 1 
ATOM   10267 N N   . TYR G 3 60  ? -0.223   -109.392 11.065  1.00 112.65 ? 60  TYR H N   1 
ATOM   10268 C CA  . TYR G 3 60  ? 0.023    -110.474 12.031  1.00 113.83 ? 60  TYR H CA  1 
ATOM   10269 C C   . TYR G 3 60  ? 1.319    -110.279 12.824  1.00 120.42 ? 60  TYR H C   1 
ATOM   10270 O O   . TYR G 3 60  ? 2.265    -109.658 12.333  1.00 122.54 ? 60  TYR H O   1 
ATOM   10271 C CB  . TYR G 3 60  ? 0.109    -111.845 11.332  1.00 116.42 ? 60  TYR H CB  1 
ATOM   10272 C CG  . TYR G 3 60  ? -1.100   -112.272 10.531  1.00 118.50 ? 60  TYR H CG  1 
ATOM   10273 C CD1 . TYR G 3 60  ? -1.215   -111.948 9.181   1.00 121.93 ? 60  TYR H CD1 1 
ATOM   10274 C CD2 . TYR G 3 60  ? -2.058   -113.118 11.080  1.00 118.03 ? 60  TYR H CD2 1 
ATOM   10275 C CE1 . TYR G 3 60  ? -2.293   -112.393 8.418   1.00 123.18 ? 60  TYR H CE1 1 
ATOM   10276 C CE2 . TYR G 3 60  ? -3.146   -113.562 10.329  1.00 118.26 ? 60  TYR H CE2 1 
ATOM   10277 C CZ  . TYR G 3 60  ? -3.260   -113.194 8.998   1.00 129.17 ? 60  TYR H CZ  1 
ATOM   10278 O OH  . TYR G 3 60  ? -4.328   -113.609 8.240   1.00 132.34 ? 60  TYR H OH  1 
ATOM   10279 N N   . SER G 3 61  ? 1.374    -110.869 14.028  1.00 116.37 ? 61  SER H N   1 
ATOM   10280 C CA  . SER G 3 61  ? 2.548    -110.881 14.896  1.00 117.89 ? 61  SER H CA  1 
ATOM   10281 C C   . SER G 3 61  ? 3.471    -112.006 14.381  1.00 121.71 ? 61  SER H C   1 
ATOM   10282 O O   . SER G 3 61  ? 2.953    -113.019 13.911  1.00 120.01 ? 61  SER H O   1 
ATOM   10283 C CB  . SER G 3 61  ? 2.126    -111.168 16.338  1.00 121.11 ? 61  SER H CB  1 
ATOM   10284 O OG  . SER G 3 61  ? 3.210    -111.397 17.224  1.00 132.37 ? 61  SER H OG  1 
ATOM   10285 N N   . PRO G 3 62  ? 4.817    -111.876 14.467  1.00 120.01 ? 62  PRO H N   1 
ATOM   10286 C CA  . PRO G 3 62  ? 5.701    -112.963 14.003  1.00 121.78 ? 62  PRO H CA  1 
ATOM   10287 C C   . PRO G 3 62  ? 5.406    -114.335 14.615  1.00 126.25 ? 62  PRO H C   1 
ATOM   10288 O O   . PRO G 3 62  ? 5.502    -115.345 13.917  1.00 126.31 ? 62  PRO H O   1 
ATOM   10289 C CB  . PRO G 3 62  ? 7.088    -112.478 14.416  1.00 126.50 ? 62  PRO H CB  1 
ATOM   10290 C CG  . PRO G 3 62  ? 6.972    -111.011 14.451  1.00 130.59 ? 62  PRO H CG  1 
ATOM   10291 C CD  . PRO G 3 62  ? 5.604    -110.740 14.980  1.00 123.13 ? 62  PRO H CD  1 
ATOM   10292 N N   . SER G 3 63  ? 5.030    -114.366 15.909  1.00 123.17 ? 63  SER H N   1 
ATOM   10293 C CA  . SER G 3 63  ? 4.691    -115.579 16.661  1.00 122.98 ? 63  SER H CA  1 
ATOM   10294 C C   . SER G 3 63  ? 3.379    -116.242 16.195  1.00 125.77 ? 63  SER H C   1 
ATOM   10295 O O   . SER G 3 63  ? 3.167    -117.417 16.509  1.00 126.45 ? 63  SER H O   1 
ATOM   10296 C CB  . SER G 3 63  ? 4.601    -115.270 18.153  1.00 126.32 ? 63  SER H CB  1 
ATOM   10297 O OG  . SER G 3 63  ? 5.828    -114.774 18.660  1.00 137.51 ? 63  SER H OG  1 
ATOM   10298 N N   . PHE G 3 64  ? 2.500    -115.500 15.467  1.00 119.66 ? 64  PHE H N   1 
ATOM   10299 C CA  . PHE G 3 64  ? 1.190    -115.990 15.006  1.00 116.34 ? 64  PHE H CA  1 
ATOM   10300 C C   . PHE G 3 64  ? 0.983    -115.944 13.483  1.00 117.95 ? 64  PHE H C   1 
ATOM   10301 O O   . PHE G 3 64  ? -0.023   -116.464 12.998  1.00 115.39 ? 64  PHE H O   1 
ATOM   10302 C CB  . PHE G 3 64  ? 0.055    -115.238 15.729  1.00 116.21 ? 64  PHE H CB  1 
ATOM   10303 C CG  . PHE G 3 64  ? 0.007    -115.433 17.227  1.00 118.13 ? 64  PHE H CG  1 
ATOM   10304 C CD1 . PHE G 3 64  ? 0.662    -114.552 18.082  1.00 122.85 ? 64  PHE H CD1 1 
ATOM   10305 C CD2 . PHE G 3 64  ? -0.703   -116.489 17.785  1.00 119.24 ? 64  PHE H CD2 1 
ATOM   10306 C CE1 . PHE G 3 64  ? 0.622    -114.734 19.469  1.00 124.84 ? 64  PHE H CE1 1 
ATOM   10307 C CE2 . PHE G 3 64  ? -0.749   -116.667 19.170  1.00 123.08 ? 64  PHE H CE2 1 
ATOM   10308 C CZ  . PHE G 3 64  ? -0.087   -115.788 20.004  1.00 123.11 ? 64  PHE H CZ  1 
ATOM   10309 N N   . GLN G 3 65  ? 1.924    -115.332 12.737  1.00 115.95 ? 65  GLN H N   1 
ATOM   10310 C CA  . GLN G 3 65  ? 1.883    -115.214 11.276  1.00 116.33 ? 65  GLN H CA  1 
ATOM   10311 C C   . GLN G 3 65  ? 1.987    -116.596 10.626  1.00 123.90 ? 65  GLN H C   1 
ATOM   10312 O O   . GLN G 3 65  ? 2.883    -117.373 10.962  1.00 125.50 ? 65  GLN H O   1 
ATOM   10313 C CB  . GLN G 3 65  ? 2.998    -114.267 10.775  1.00 118.98 ? 65  GLN H CB  1 
ATOM   10314 C CG  . GLN G 3 65  ? 3.196    -114.207 9.253   1.00 119.24 ? 65  GLN H CG  1 
ATOM   10315 C CD  . GLN G 3 65  ? 2.181    -113.351 8.542   1.00 124.54 ? 65  GLN H CD  1 
ATOM   10316 O OE1 . GLN G 3 65  ? 2.183    -112.122 8.643   1.00 113.95 ? 65  GLN H OE1 1 
ATOM   10317 N NE2 . GLN G 3 65  ? 1.325    -113.981 7.752   1.00 118.34 ? 65  GLN H NE2 1 
ATOM   10318 N N   . GLY G 3 66  ? 1.047    -116.888 9.729   1.00 121.17 ? 66  GLY H N   1 
ATOM   10319 C CA  . GLY G 3 66  ? 0.980    -118.154 9.007   1.00 122.60 ? 66  GLY H CA  1 
ATOM   10320 C C   . GLY G 3 66  ? 0.159    -119.212 9.716   1.00 125.84 ? 66  GLY H C   1 
ATOM   10321 O O   . GLY G 3 66  ? -0.695   -119.854 9.094   1.00 126.04 ? 66  GLY H O   1 
ATOM   10322 N N   . GLN G 3 67  ? 0.416    -119.392 11.030  1.00 120.91 ? 67  GLN H N   1 
ATOM   10323 C CA  . GLN G 3 67  ? -0.249   -120.361 11.911  1.00 118.95 ? 67  GLN H CA  1 
ATOM   10324 C C   . GLN G 3 67  ? -1.773   -120.126 11.967  1.00 120.91 ? 67  GLN H C   1 
ATOM   10325 O O   . GLN G 3 67  ? -2.549   -120.969 11.497  1.00 120.03 ? 67  GLN H O   1 
ATOM   10326 C CB  . GLN G 3 67  ? 0.376    -120.323 13.328  1.00 119.85 ? 67  GLN H CB  1 
ATOM   10327 C CG  . GLN G 3 67  ? 1.903    -120.371 13.367  1.00 115.48 ? 67  GLN H CG  1 
ATOM   10328 C CD  . GLN G 3 67  ? 2.439    -121.683 12.863  1.00 127.19 ? 67  GLN H CD  1 
ATOM   10329 O OE1 . GLN G 3 67  ? 2.394    -122.704 13.549  1.00 123.52 ? 67  GLN H OE1 1 
ATOM   10330 N NE2 . GLN G 3 67  ? 2.926    -121.693 11.636  1.00 117.01 ? 67  GLN H NE2 1 
ATOM   10331 N N   . VAL G 3 68  ? -2.180   -118.960 12.512  1.00 116.10 ? 68  VAL H N   1 
ATOM   10332 C CA  . VAL G 3 68  ? -3.571   -118.524 12.643  1.00 113.40 ? 68  VAL H CA  1 
ATOM   10333 C C   . VAL G 3 68  ? -3.885   -117.470 11.565  1.00 117.26 ? 68  VAL H C   1 
ATOM   10334 O O   . VAL G 3 68  ? -2.983   -116.746 11.117  1.00 117.88 ? 68  VAL H O   1 
ATOM   10335 C CB  . VAL G 3 68  ? -3.889   -118.047 14.090  1.00 115.84 ? 68  VAL H CB  1 
ATOM   10336 C CG1 . VAL G 3 68  ? -3.251   -116.695 14.406  1.00 116.05 ? 68  VAL H CG1 1 
ATOM   10337 C CG2 . VAL G 3 68  ? -5.385   -118.012 14.351  1.00 113.79 ? 68  VAL H CG2 1 
ATOM   10338 N N   . THR G 3 69  ? -5.156   -117.415 11.137  1.00 112.24 ? 69  THR H N   1 
ATOM   10339 C CA  . THR G 3 69  ? -5.630   -116.485 10.114  1.00 111.47 ? 69  THR H CA  1 
ATOM   10340 C C   . THR G 3 69  ? -6.707   -115.566 10.715  1.00 112.02 ? 69  THR H C   1 
ATOM   10341 O O   . THR G 3 69  ? -7.684   -116.058 11.279  1.00 109.82 ? 69  THR H O   1 
ATOM   10342 C CB  . THR G 3 69  ? -6.059   -117.260 8.837   1.00 118.33 ? 69  THR H CB  1 
ATOM   10343 O OG1 . THR G 3 69  ? -5.087   -118.272 8.527   1.00 117.53 ? 69  THR H OG1 1 
ATOM   10344 C CG2 . THR G 3 69  ? -6.249   -116.348 7.624   1.00 116.01 ? 69  THR H CG2 1 
ATOM   10345 N N   . ILE G 3 70  ? -6.495   -114.235 10.634  1.00 108.01 ? 70  ILE H N   1 
ATOM   10346 C CA  . ILE G 3 70  ? -7.435   -113.236 11.153  1.00 106.09 ? 70  ILE H CA  1 
ATOM   10347 C C   . ILE G 3 70  ? -8.318   -112.775 10.009  1.00 111.07 ? 70  ILE H C   1 
ATOM   10348 O O   . ILE G 3 70  ? -7.830   -112.187 9.046   1.00 111.88 ? 70  ILE H O   1 
ATOM   10349 C CB  . ILE G 3 70  ? -6.760   -112.042 11.889  1.00 108.89 ? 70  ILE H CB  1 
ATOM   10350 C CG1 . ILE G 3 70  ? -5.654   -112.506 12.854  1.00 110.47 ? 70  ILE H CG1 1 
ATOM   10351 C CG2 . ILE G 3 70  ? -7.800   -111.220 12.634  1.00 107.80 ? 70  ILE H CG2 1 
ATOM   10352 C CD1 . ILE G 3 70  ? -4.619   -111.445 13.205  1.00 116.28 ? 70  ILE H CD1 1 
ATOM   10353 N N   . SER G 3 71  ? -9.615   -113.064 10.114  1.00 107.88 ? 71  SER H N   1 
ATOM   10354 C CA  . SER G 3 71  ? -10.623  -112.717 9.114   1.00 108.20 ? 71  SER H CA  1 
ATOM   10355 C C   . SER G 3 71  ? -11.494  -111.563 9.629   1.00 112.02 ? 71  SER H C   1 
ATOM   10356 O O   . SER G 3 71  ? -11.581  -111.356 10.838  1.00 110.96 ? 71  SER H O   1 
ATOM   10357 C CB  . SER G 3 71  ? -11.501  -113.933 8.810   1.00 112.00 ? 71  SER H CB  1 
ATOM   10358 O OG  . SER G 3 71  ? -10.777  -115.153 8.746   1.00 120.43 ? 71  SER H OG  1 
ATOM   10359 N N   . ALA G 3 72  ? -12.129  -110.806 8.719   1.00 109.54 ? 72  ALA H N   1 
ATOM   10360 C CA  . ALA G 3 72  ? -13.019  -109.706 9.093   1.00 108.97 ? 72  ALA H CA  1 
ATOM   10361 C C   . ALA G 3 72  ? -14.174  -109.537 8.109   1.00 115.18 ? 72  ALA H C   1 
ATOM   10362 O O   . ALA G 3 72  ? -13.966  -109.542 6.889   1.00 116.98 ? 72  ALA H O   1 
ATOM   10363 C CB  . ALA G 3 72  ? -12.243  -108.408 9.218   1.00 109.60 ? 72  ALA H CB  1 
ATOM   10364 N N   . ASP G 3 73  ? -15.395  -109.394 8.647   1.00 110.84 ? 73  ASP H N   1 
ATOM   10365 C CA  . ASP G 3 73  ? -16.600  -109.180 7.857   1.00 110.84 ? 73  ASP H CA  1 
ATOM   10366 C C   . ASP G 3 73  ? -17.320  -107.923 8.338   1.00 112.27 ? 73  ASP H C   1 
ATOM   10367 O O   . ASP G 3 73  ? -18.127  -107.980 9.274   1.00 111.31 ? 73  ASP H O   1 
ATOM   10368 C CB  . ASP G 3 73  ? -17.521  -110.407 7.878   1.00 113.30 ? 73  ASP H CB  1 
ATOM   10369 C CG  . ASP G 3 73  ? -18.438  -110.481 6.672   1.00 130.10 ? 73  ASP H CG  1 
ATOM   10370 O OD1 . ASP G 3 73  ? -19.137  -109.482 6.393   1.00 130.59 ? 73  ASP H OD1 1 
ATOM   10371 O OD2 . ASP G 3 73  ? -18.502  -111.557 6.041   1.00 141.87 ? 73  ASP H OD2 1 
ATOM   10372 N N   . LYS G 3 74  ? -16.997  -106.782 7.693   1.00 107.26 ? 74  LYS H N   1 
ATOM   10373 C CA  . LYS G 3 74  ? -17.546  -105.451 7.968   1.00 105.46 ? 74  LYS H CA  1 
ATOM   10374 C C   . LYS G 3 74  ? -19.061  -105.382 7.800   1.00 107.54 ? 74  LYS H C   1 
ATOM   10375 O O   . LYS G 3 74  ? -19.699  -104.597 8.498   1.00 106.50 ? 74  LYS H O   1 
ATOM   10376 C CB  . LYS G 3 74  ? -16.847  -104.373 7.117   1.00 108.51 ? 74  LYS H CB  1 
ATOM   10377 C CG  . LYS G 3 74  ? -16.650  -104.747 5.639   1.00 124.95 ? 74  LYS H CG  1 
ATOM   10378 C CD  . LYS G 3 74  ? -16.210  -103.554 4.799   1.00 132.33 ? 74  LYS H CD  1 
ATOM   10379 C CE  . LYS G 3 74  ? -15.504  -103.966 3.536   1.00 139.53 ? 74  LYS H CE  1 
ATOM   10380 N NZ  . LYS G 3 74  ? -15.099  -102.781 2.736   1.00 147.43 ? 74  LYS H NZ  1 
ATOM   10381 N N   . SER G 3 75  ? -19.630  -106.210 6.886   1.00 104.24 ? 75  SER H N   1 
ATOM   10382 C CA  . SER G 3 75  ? -21.070  -106.289 6.579   1.00 104.15 ? 75  SER H CA  1 
ATOM   10383 C C   . SER G 3 75  ? -21.881  -106.810 7.762   1.00 104.20 ? 75  SER H C   1 
ATOM   10384 O O   . SER G 3 75  ? -22.919  -106.231 8.085   1.00 103.78 ? 75  SER H O   1 
ATOM   10385 C CB  . SER G 3 75  ? -21.316  -107.150 5.344   1.00 110.60 ? 75  SER H CB  1 
ATOM   10386 O OG  . SER G 3 75  ? -20.544  -106.708 4.237   1.00 123.75 ? 75  SER H OG  1 
ATOM   10387 N N   . ILE G 3 76  ? -21.395  -107.888 8.415   1.00 98.07  ? 76  ILE H N   1 
ATOM   10388 C CA  . ILE G 3 76  ? -22.010  -108.504 9.600   1.00 96.13  ? 76  ILE H CA  1 
ATOM   10389 C C   . ILE G 3 76  ? -21.468  -107.815 10.875  1.00 98.61  ? 76  ILE H C   1 
ATOM   10390 O O   . ILE G 3 76  ? -21.980  -108.061 11.970  1.00 98.86  ? 76  ILE H O   1 
ATOM   10391 C CB  . ILE G 3 76  ? -21.780  -110.053 9.664   1.00 98.55  ? 76  ILE H CB  1 
ATOM   10392 C CG1 . ILE G 3 76  ? -21.664  -110.708 8.271   1.00 100.05 ? 76  ILE H CG1 1 
ATOM   10393 C CG2 . ILE G 3 76  ? -22.858  -110.733 10.514  1.00 98.69  ? 76  ILE H CG2 1 
ATOM   10394 C CD1 . ILE G 3 76  ? -21.026  -112.124 8.259   1.00 107.87 ? 76  ILE H CD1 1 
ATOM   10395 N N   . SER G 3 77  ? -20.444  -106.938 10.717  1.00 93.25  ? 77  SER H N   1 
ATOM   10396 C CA  . SER G 3 77  ? -19.725  -106.225 11.781  1.00 91.63  ? 77  SER H CA  1 
ATOM   10397 C C   . SER G 3 77  ? -19.111  -107.236 12.767  1.00 94.37  ? 77  SER H C   1 
ATOM   10398 O O   . SER G 3 77  ? -19.288  -107.126 13.983  1.00 94.92  ? 77  SER H O   1 
ATOM   10399 C CB  . SER G 3 77  ? -20.594  -105.159 12.453  1.00 93.79  ? 77  SER H CB  1 
ATOM   10400 O OG  . SER G 3 77  ? -21.584  -105.714 13.302  1.00 100.23 ? 77  SER H OG  1 
ATOM   10401 N N   . THR G 3 78  ? -18.415  -108.251 12.207  1.00 88.61  ? 78  THR H N   1 
ATOM   10402 C CA  . THR G 3 78  ? -17.799  -109.345 12.955  1.00 87.29  ? 78  THR H CA  1 
ATOM   10403 C C   . THR G 3 78  ? -16.380  -109.632 12.515  1.00 91.10  ? 78  THR H C   1 
ATOM   10404 O O   . THR G 3 78  ? -16.106  -109.714 11.318  1.00 91.92  ? 78  THR H O   1 
ATOM   10405 C CB  . THR G 3 78  ? -18.605  -110.638 12.796  1.00 90.32  ? 78  THR H CB  1 
ATOM   10406 O OG1 . THR G 3 78  ? -19.944  -110.353 12.404  1.00 89.71  ? 78  THR H OG1 1 
ATOM   10407 C CG2 . THR G 3 78  ? -18.580  -111.493 14.044  1.00 87.01  ? 78  THR H CG2 1 
ATOM   10408 N N   . ALA G 3 79  ? -15.493  -109.846 13.490  1.00 86.59  ? 79  ALA H N   1 
ATOM   10409 C CA  . ALA G 3 79  ? -14.097  -110.209 13.270  1.00 86.52  ? 79  ALA H CA  1 
ATOM   10410 C C   . ALA G 3 79  ? -13.954  -111.690 13.588  1.00 89.86  ? 79  ALA H C   1 
ATOM   10411 O O   . ALA G 3 79  ? -14.725  -112.210 14.398  1.00 90.33  ? 79  ALA H O   1 
ATOM   10412 C CB  . ALA G 3 79  ? -13.204  -109.399 14.190  1.00 87.61  ? 79  ALA H CB  1 
ATOM   10413 N N   . TYR G 3 80  ? -12.984  -112.371 12.960  1.00 84.64  ? 80  TYR H N   1 
ATOM   10414 C CA  . TYR G 3 80  ? -12.753  -113.797 13.184  1.00 84.05  ? 80  TYR H CA  1 
ATOM   10415 C C   . TYR G 3 80  ? -11.289  -114.120 13.441  1.00 88.96  ? 80  TYR H C   1 
ATOM   10416 O O   . TYR G 3 80  ? -10.411  -113.347 13.065  1.00 89.16  ? 80  TYR H O   1 
ATOM   10417 C CB  . TYR G 3 80  ? -13.289  -114.645 12.009  1.00 85.13  ? 80  TYR H CB  1 
ATOM   10418 C CG  . TYR G 3 80  ? -14.711  -114.331 11.614  1.00 85.88  ? 80  TYR H CG  1 
ATOM   10419 C CD1 . TYR G 3 80  ? -15.770  -114.638 12.456  1.00 87.51  ? 80  TYR H CD1 1 
ATOM   10420 C CD2 . TYR G 3 80  ? -14.998  -113.719 10.399  1.00 86.99  ? 80  TYR H CD2 1 
ATOM   10421 C CE1 . TYR G 3 80  ? -17.081  -114.319 12.115  1.00 89.13  ? 80  TYR H CE1 1 
ATOM   10422 C CE2 . TYR G 3 80  ? -16.307  -113.403 10.042  1.00 87.74  ? 80  TYR H CE2 1 
ATOM   10423 C CZ  . TYR G 3 80  ? -17.347  -113.707 10.905  1.00 95.23  ? 80  TYR H CZ  1 
ATOM   10424 O OH  . TYR G 3 80  ? -18.652  -113.415 10.589  1.00 97.60  ? 80  TYR H OH  1 
ATOM   10425 N N   . LEU G 3 81  ? -11.030  -115.273 14.071  1.00 86.53  ? 81  LEU H N   1 
ATOM   10426 C CA  . LEU G 3 81  ? -9.685   -115.779 14.328  1.00 88.00  ? 81  LEU H CA  1 
ATOM   10427 C C   . LEU G 3 81  ? -9.679   -117.253 13.895  1.00 94.57  ? 81  LEU H C   1 
ATOM   10428 O O   . LEU G 3 81  ? -9.741   -118.162 14.725  1.00 94.05  ? 81  LEU H O   1 
ATOM   10429 C CB  . LEU G 3 81  ? -9.297   -115.587 15.808  1.00 88.16  ? 81  LEU H CB  1 
ATOM   10430 C CG  . LEU G 3 81  ? -7.816   -115.743 16.153  1.00 93.48  ? 81  LEU H CG  1 
ATOM   10431 C CD1 . LEU G 3 81  ? -7.025   -114.498 15.802  1.00 94.22  ? 81  LEU H CD1 1 
ATOM   10432 C CD2 . LEU G 3 81  ? -7.641   -116.033 17.605  1.00 94.52  ? 81  LEU H CD2 1 
ATOM   10433 N N   . GLN G 3 82  ? -9.680   -117.464 12.569  1.00 105.00 ? 82  GLN H N   1 
ATOM   10434 C CA  . GLN G 3 82  ? -9.720   -118.764 11.896  1.00 108.32 ? 82  GLN H CA  1 
ATOM   10435 C C   . GLN G 3 82  ? -8.411   -119.542 12.058  1.00 117.38 ? 82  GLN H C   1 
ATOM   10436 O O   . GLN G 3 82  ? -7.335   -118.982 11.845  1.00 117.99 ? 82  GLN H O   1 
ATOM   10437 C CB  . GLN G 3 82  ? -10.069  -118.567 10.404  1.00 110.53 ? 82  GLN H CB  1 
ATOM   10438 C CG  . GLN G 3 82  ? -10.590  -119.823 9.696   1.00 135.66 ? 82  GLN H CG  1 
ATOM   10439 C CD  . GLN G 3 82  ? -11.687  -119.553 8.684   1.00 161.50 ? 82  GLN H CD  1 
ATOM   10440 O OE1 . GLN G 3 82  ? -11.725  -118.515 8.009   1.00 158.65 ? 82  GLN H OE1 1 
ATOM   10441 N NE2 . GLN G 3 82  ? -12.595  -120.510 8.533   1.00 154.25 ? 82  GLN H NE2 1 
ATOM   10442 N N   . TRP G 3 83  ? -8.514   -120.838 12.427  1.00 117.10 ? 83  TRP H N   1 
ATOM   10443 C CA  . TRP G 3 83  ? -7.380   -121.749 12.605  1.00 120.68 ? 83  TRP H CA  1 
ATOM   10444 C C   . TRP G 3 83  ? -7.303   -122.772 11.490  1.00 127.01 ? 83  TRP H C   1 
ATOM   10445 O O   . TRP G 3 83  ? -8.269   -123.501 11.242  1.00 126.71 ? 83  TRP H O   1 
ATOM   10446 C CB  . TRP G 3 83  ? -7.421   -122.464 13.962  1.00 119.83 ? 83  TRP H CB  1 
ATOM   10447 C CG  . TRP G 3 83  ? -6.778   -121.690 15.065  1.00 119.62 ? 83  TRP H CG  1 
ATOM   10448 C CD1 . TRP G 3 83  ? -5.441   -121.511 15.276  1.00 124.06 ? 83  TRP H CD1 1 
ATOM   10449 C CD2 . TRP G 3 83  ? -7.449   -121.003 16.126  1.00 116.71 ? 83  TRP H CD2 1 
ATOM   10450 N NE1 . TRP G 3 83  ? -5.237   -120.743 16.398  1.00 121.68 ? 83  TRP H NE1 1 
ATOM   10451 C CE2 . TRP G 3 83  ? -6.455   -120.410 16.937  1.00 120.73 ? 83  TRP H CE2 1 
ATOM   10452 C CE3 . TRP G 3 83  ? -8.800   -120.827 16.472  1.00 115.98 ? 83  TRP H CE3 1 
ATOM   10453 C CZ2 . TRP G 3 83  ? -6.771   -119.651 18.074  1.00 117.92 ? 83  TRP H CZ2 1 
ATOM   10454 C CZ3 . TRP G 3 83  ? -9.112   -120.075 17.595  1.00 115.48 ? 83  TRP H CZ3 1 
ATOM   10455 C CH2 . TRP G 3 83  ? -8.106   -119.508 18.390  1.00 115.99 ? 83  TRP H CH2 1 
ATOM   10456 N N   . SER G 3 84  ? -6.134   -122.823 10.827  1.00 125.69 ? 84  SER H N   1 
ATOM   10457 C CA  . SER G 3 84  ? -5.823   -123.735 9.726   1.00 129.15 ? 84  SER H CA  1 
ATOM   10458 C C   . SER G 3 84  ? -5.846   -125.178 10.272  1.00 134.13 ? 84  SER H C   1 
ATOM   10459 O O   . SER G 3 84  ? -6.664   -125.993 9.841   1.00 134.72 ? 84  SER H O   1 
ATOM   10460 C CB  . SER G 3 84  ? -4.458   -123.384 9.125   1.00 135.13 ? 84  SER H CB  1 
ATOM   10461 O OG  . SER G 3 84  ? -4.237   -121.983 9.034   1.00 138.59 ? 84  SER H OG  1 
ATOM   10462 N N   . SER G 3 85  ? -4.988   -125.451 11.272  1.00 130.34 ? 85  SER H N   1 
ATOM   10463 C CA  . SER G 3 85  ? -4.874   -126.720 11.990  1.00 131.62 ? 85  SER H CA  1 
ATOM   10464 C C   . SER G 3 85  ? -4.470   -126.384 13.417  1.00 130.32 ? 85  SER H C   1 
ATOM   10465 O O   . SER G 3 85  ? -3.550   -125.585 13.630  1.00 128.58 ? 85  SER H O   1 
ATOM   10466 C CB  . SER G 3 85  ? -3.846   -127.638 11.334  1.00 141.13 ? 85  SER H CB  1 
ATOM   10467 O OG  . SER G 3 85  ? -3.835   -128.918 11.946  1.00 152.54 ? 85  SER H OG  1 
ATOM   10468 N N   . LEU G 3 86  ? -5.195   -126.950 14.390  1.00 124.82 ? 86  LEU H N   1 
ATOM   10469 C CA  . LEU G 3 86  ? -4.965   -126.686 15.806  1.00 122.19 ? 86  LEU H CA  1 
ATOM   10470 C C   . LEU G 3 86  ? -3.788   -127.439 16.398  1.00 129.46 ? 86  LEU H C   1 
ATOM   10471 O O   . LEU G 3 86  ? -3.552   -128.598 16.060  1.00 132.95 ? 86  LEU H O   1 
ATOM   10472 C CB  . LEU G 3 86  ? -6.234   -126.940 16.630  1.00 119.86 ? 86  LEU H CB  1 
ATOM   10473 C CG  . LEU G 3 86  ? -7.300   -125.850 16.598  1.00 120.60 ? 86  LEU H CG  1 
ATOM   10474 C CD1 . LEU G 3 86  ? -8.625   -126.392 17.051  1.00 120.33 ? 86  LEU H CD1 1 
ATOM   10475 C CD2 . LEU G 3 86  ? -6.913   -124.663 17.457  1.00 119.71 ? 86  LEU H CD2 1 
ATOM   10476 N N   . LYS G 3 87  ? -3.047   -126.758 17.284  1.00 124.44 ? 87  LYS H N   1 
ATOM   10477 C CA  . LYS G 3 87  ? -1.896   -127.302 18.008  1.00 126.16 ? 87  LYS H CA  1 
ATOM   10478 C C   . LYS G 3 87  ? -2.292   -127.379 19.476  1.00 128.71 ? 87  LYS H C   1 
ATOM   10479 O O   . LYS G 3 87  ? -3.170   -126.627 19.905  1.00 125.68 ? 87  LYS H O   1 
ATOM   10480 C CB  . LYS G 3 87  ? -0.659   -126.383 17.874  1.00 128.22 ? 87  LYS H CB  1 
ATOM   10481 C CG  . LYS G 3 87  ? -0.146   -126.147 16.453  1.00 142.38 ? 87  LYS H CG  1 
ATOM   10482 C CD  . LYS G 3 87  ? -0.542   -124.770 15.901  1.00 150.99 ? 87  LYS H CD  1 
ATOM   10483 C CE  . LYS G 3 87  ? 0.456    -123.671 16.208  1.00 161.30 ? 87  LYS H CE  1 
ATOM   10484 N NZ  . LYS G 3 87  ? 0.236    -123.061 17.549  1.00 167.73 ? 87  LYS H NZ  1 
ATOM   10485 N N   . ALA G 3 88  ? -1.619   -128.241 20.262  1.00 126.74 ? 88  ALA H N   1 
ATOM   10486 C CA  . ALA G 3 88  ? -1.869   -128.357 21.702  1.00 124.54 ? 88  ALA H CA  1 
ATOM   10487 C C   . ALA G 3 88  ? -1.470   -127.050 22.409  1.00 124.43 ? 88  ALA H C   1 
ATOM   10488 O O   . ALA G 3 88  ? -1.971   -126.762 23.495  1.00 121.22 ? 88  ALA H O   1 
ATOM   10489 C CB  . ALA G 3 88  ? -1.089   -129.527 22.277  1.00 128.25 ? 88  ALA H CB  1 
ATOM   10490 N N   . SER G 3 89  ? -0.595   -126.250 21.756  1.00 121.46 ? 89  SER H N   1 
ATOM   10491 C CA  . SER G 3 89  ? -0.120   -124.946 22.219  1.00 119.09 ? 89  SER H CA  1 
ATOM   10492 C C   . SER G 3 89  ? -1.204   -123.869 22.072  1.00 119.82 ? 89  SER H C   1 
ATOM   10493 O O   . SER G 3 89  ? -1.125   -122.839 22.744  1.00 117.87 ? 89  SER H O   1 
ATOM   10494 C CB  . SER G 3 89  ? 1.134    -124.533 21.456  1.00 125.00 ? 89  SER H CB  1 
ATOM   10495 O OG  . SER G 3 89  ? 0.860    -124.332 20.079  1.00 136.57 ? 89  SER H OG  1 
ATOM   10496 N N   . ASP G 3 90  ? -2.214   -124.108 21.201  1.00 115.53 ? 90  ASP H N   1 
ATOM   10497 C CA  . ASP G 3 90  ? -3.327   -123.183 20.961  1.00 112.32 ? 90  ASP H CA  1 
ATOM   10498 C C   . ASP G 3 90  ? -4.359   -123.159 22.115  1.00 115.08 ? 90  ASP H C   1 
ATOM   10499 O O   . ASP G 3 90  ? -5.292   -122.351 22.082  1.00 113.42 ? 90  ASP H O   1 
ATOM   10500 C CB  . ASP G 3 90  ? -3.992   -123.454 19.595  1.00 114.46 ? 90  ASP H CB  1 
ATOM   10501 C CG  . ASP G 3 90  ? -3.206   -122.980 18.377  1.00 124.03 ? 90  ASP H CG  1 
ATOM   10502 O OD1 . ASP G 3 90  ? -2.249   -122.183 18.552  1.00 124.75 ? 90  ASP H OD1 1 
ATOM   10503 O OD2 . ASP G 3 90  ? -3.568   -123.376 17.247  1.00 129.54 ? 90  ASP H OD2 1 
ATOM   10504 N N   . THR G 3 91  ? -4.170   -124.018 23.148  1.00 111.66 ? 91  THR H N   1 
ATOM   10505 C CA  . THR G 3 91  ? -5.021   -124.085 24.340  1.00 109.58 ? 91  THR H CA  1 
ATOM   10506 C C   . THR G 3 91  ? -4.805   -122.779 25.095  1.00 109.44 ? 91  THR H C   1 
ATOM   10507 O O   . THR G 3 91  ? -3.808   -122.643 25.805  1.00 109.43 ? 91  THR H O   1 
ATOM   10508 C CB  . THR G 3 91  ? -4.659   -125.316 25.198  1.00 123.96 ? 91  THR H CB  1 
ATOM   10509 O OG1 . THR G 3 91  ? -4.524   -126.472 24.369  1.00 130.30 ? 91  THR H OG1 1 
ATOM   10510 C CG2 . THR G 3 91  ? -5.668   -125.576 26.309  1.00 122.30 ? 91  THR H CG2 1 
ATOM   10511 N N   . ALA G 3 92  ? -5.692   -121.791 24.875  1.00 102.61 ? 92  ALA H N   1 
ATOM   10512 C CA  . ALA G 3 92  ? -5.567   -120.465 25.484  1.00 100.12 ? 92  ALA H CA  1 
ATOM   10513 C C   . ALA G 3 92  ? -6.880   -119.688 25.537  1.00 100.84 ? 92  ALA H C   1 
ATOM   10514 O O   . ALA G 3 92  ? -7.892   -120.133 24.993  1.00 100.31 ? 92  ALA H O   1 
ATOM   10515 C CB  . ALA G 3 92  ? -4.527   -119.653 24.722  1.00 101.17 ? 92  ALA H CB  1 
ATOM   10516 N N   . MET G 3 93  ? -6.838   -118.509 26.192  1.00 95.28  ? 93  MET H N   1 
ATOM   10517 C CA  . MET G 3 93  ? -7.926   -117.537 26.320  1.00 92.99  ? 93  MET H CA  1 
ATOM   10518 C C   . MET G 3 93  ? -7.702   -116.462 25.234  1.00 94.65  ? 93  MET H C   1 
ATOM   10519 O O   . MET G 3 93  ? -6.626   -115.868 25.165  1.00 94.39  ? 93  MET H O   1 
ATOM   10520 C CB  . MET G 3 93  ? -7.925   -116.933 27.741  1.00 94.72  ? 93  MET H CB  1 
ATOM   10521 C CG  . MET G 3 93  ? -8.882   -115.767 27.944  1.00 96.73  ? 93  MET H CG  1 
ATOM   10522 S SD  . MET G 3 93  ? -10.626  -116.198 27.846  1.00 99.74  ? 93  MET H SD  1 
ATOM   10523 C CE  . MET G 3 93  ? -11.235  -115.311 29.234  1.00 96.33  ? 93  MET H CE  1 
ATOM   10524 N N   . TYR G 3 94  ? -8.695   -116.249 24.366  1.00 88.75  ? 94  TYR H N   1 
ATOM   10525 C CA  . TYR G 3 94  ? -8.552   -115.309 23.264  1.00 87.43  ? 94  TYR H CA  1 
ATOM   10526 C C   . TYR G 3 94  ? -9.492   -114.122 23.382  1.00 90.29  ? 94  TYR H C   1 
ATOM   10527 O O   . TYR G 3 94  ? -10.705  -114.298 23.534  1.00 89.91  ? 94  TYR H O   1 
ATOM   10528 C CB  . TYR G 3 94  ? -8.722   -116.040 21.922  1.00 88.95  ? 94  TYR H CB  1 
ATOM   10529 C CG  . TYR G 3 94  ? -7.660   -117.089 21.664  1.00 92.65  ? 94  TYR H CG  1 
ATOM   10530 C CD1 . TYR G 3 94  ? -7.859   -118.420 22.025  1.00 95.26  ? 94  TYR H CD1 1 
ATOM   10531 C CD2 . TYR G 3 94  ? -6.450   -116.752 21.070  1.00 94.64  ? 94  TYR H CD2 1 
ATOM   10532 C CE1 . TYR G 3 94  ? -6.872   -119.384 21.810  1.00 96.57  ? 94  TYR H CE1 1 
ATOM   10533 C CE2 . TYR G 3 94  ? -5.471   -117.711 20.822  1.00 97.22  ? 94  TYR H CE2 1 
ATOM   10534 C CZ  . TYR G 3 94  ? -5.672   -119.019 21.223  1.00 102.30 ? 94  TYR H CZ  1 
ATOM   10535 O OH  . TYR G 3 94  ? -4.689   -119.947 20.994  1.00 103.83 ? 94  TYR H OH  1 
ATOM   10536 N N   . TYR G 3 95  ? -8.923   -112.910 23.336  1.00 85.72  ? 95  TYR H N   1 
ATOM   10537 C CA  . TYR G 3 95  ? -9.656   -111.643 23.406  1.00 84.15  ? 95  TYR H CA  1 
ATOM   10538 C C   . TYR G 3 95  ? -9.525   -110.901 22.085  1.00 88.21  ? 95  TYR H C   1 
ATOM   10539 O O   . TYR G 3 95  ? -8.527   -111.073 21.393  1.00 88.65  ? 95  TYR H O   1 
ATOM   10540 C CB  . TYR G 3 95  ? -9.078   -110.736 24.508  1.00 85.28  ? 95  TYR H CB  1 
ATOM   10541 C CG  . TYR G 3 95  ? -9.227   -111.239 25.926  1.00 86.95  ? 95  TYR H CG  1 
ATOM   10542 C CD1 . TYR G 3 95  ? -10.403  -111.032 26.639  1.00 89.39  ? 95  TYR H CD1 1 
ATOM   10543 C CD2 . TYR G 3 95  ? -8.154   -111.822 26.594  1.00 87.88  ? 95  TYR H CD2 1 
ATOM   10544 C CE1 . TYR G 3 95  ? -10.534  -111.466 27.958  1.00 92.83  ? 95  TYR H CE1 1 
ATOM   10545 C CE2 . TYR G 3 95  ? -8.261   -112.230 27.923  1.00 89.21  ? 95  TYR H CE2 1 
ATOM   10546 C CZ  . TYR G 3 95  ? -9.455   -112.055 28.602  1.00 100.52 ? 95  TYR H CZ  1 
ATOM   10547 O OH  . TYR G 3 95  ? -9.565   -112.465 29.912  1.00 102.71 ? 95  TYR H OH  1 
ATOM   10548 N N   . CYS G 3 96  ? -10.517  -110.067 21.742  1.00 84.38  ? 96  CYS H N   1 
ATOM   10549 C CA  . CYS G 3 96  ? -10.485  -109.182 20.575  1.00 84.16  ? 96  CYS H CA  1 
ATOM   10550 C C   . CYS G 3 96  ? -10.680  -107.787 21.140  1.00 86.03  ? 96  CYS H C   1 
ATOM   10551 O O   . CYS G 3 96  ? -11.286  -107.659 22.204  1.00 85.81  ? 96  CYS H O   1 
ATOM   10552 C CB  . CYS G 3 96  ? -11.555  -109.539 19.542  1.00 83.97  ? 96  CYS H CB  1 
ATOM   10553 S SG  . CYS G 3 96  ? -13.223  -108.975 19.965  1.00 87.02  ? 96  CYS H SG  1 
ATOM   10554 N N   . ALA G 3 97  ? -10.129  -106.754 20.502  1.00 81.60  ? 97  ALA H N   1 
ATOM   10555 C CA  . ALA G 3 97  ? -10.286  -105.412 21.055  1.00 81.91  ? 97  ALA H CA  1 
ATOM   10556 C C   . ALA G 3 97  ? -10.303  -104.294 20.037  1.00 88.20  ? 97  ALA H C   1 
ATOM   10557 O O   . ALA G 3 97  ? -9.570   -104.341 19.050  1.00 90.15  ? 97  ALA H O   1 
ATOM   10558 C CB  . ALA G 3 97  ? -9.230   -105.143 22.102  1.00 83.83  ? 97  ALA H CB  1 
ATOM   10559 N N   . ARG G 3 98  ? -11.148  -103.277 20.288  1.00 83.53  ? 98  ARG H N   1 
ATOM   10560 C CA  . ARG G 3 98  ? -11.302  -102.098 19.444  1.00 82.79  ? 98  ARG H CA  1 
ATOM   10561 C C   . ARG G 3 98  ? -10.097  -101.207 19.690  1.00 89.47  ? 98  ARG H C   1 
ATOM   10562 O O   . ARG G 3 98  ? -9.897   -100.758 20.818  1.00 91.02  ? 98  ARG H O   1 
ATOM   10563 C CB  . ARG G 3 98  ? -12.604  -101.374 19.796  1.00 79.13  ? 98  ARG H CB  1 
ATOM   10564 C CG  . ARG G 3 98  ? -13.083  -100.435 18.720  1.00 79.76  ? 98  ARG H CG  1 
ATOM   10565 C CD  . ARG G 3 98  ? -14.248  -99.613  19.200  1.00 80.74  ? 98  ARG H CD  1 
ATOM   10566 N NE  . ARG G 3 98  ? -13.824  -98.498  20.041  1.00 90.24  ? 98  ARG H NE  1 
ATOM   10567 C CZ  . ARG G 3 98  ? -14.624  -97.513  20.428  1.00 104.10 ? 98  ARG H CZ  1 
ATOM   10568 N NH1 . ARG G 3 98  ? -15.896  -97.492  20.047  1.00 85.51  ? 98  ARG H NH1 1 
ATOM   10569 N NH2 . ARG G 3 98  ? -14.158  -96.535  21.192  1.00 96.55  ? 98  ARG H NH2 1 
ATOM   10570 N N   . VAL G 3 99  ? -9.276   -100.990 18.650  1.00 86.66  ? 99  VAL H N   1 
ATOM   10571 C CA  . VAL G 3 99  ? -8.037   -100.213 18.722  1.00 89.20  ? 99  VAL H CA  1 
ATOM   10572 C C   . VAL G 3 99  ? -8.304   -98.704  18.633  1.00 95.25  ? 99  VAL H C   1 
ATOM   10573 O O   . VAL G 3 99  ? -9.108   -98.262  17.815  1.00 94.18  ? 99  VAL H O   1 
ATOM   10574 C CB  . VAL G 3 99  ? -6.968   -100.701 17.701  1.00 93.92  ? 99  VAL H CB  1 
ATOM   10575 C CG1 . VAL G 3 99  ? -5.661   -99.929  17.850  1.00 96.92  ? 99  VAL H CG1 1 
ATOM   10576 C CG2 . VAL G 3 99  ? -6.702   -102.196 17.853  1.00 92.51  ? 99  VAL H CG2 1 
ATOM   10577 N N   . VAL G 3 100 ? -7.623   -97.933  19.501  1.00 94.39  ? 100 VAL H N   1 
ATOM   10578 C CA  . VAL G 3 100 ? -7.667   -96.476  19.607  1.00 96.80  ? 100 VAL H CA  1 
ATOM   10579 C C   . VAL G 3 100 ? -6.558   -95.914  18.735  1.00 104.67 ? 100 VAL H C   1 
ATOM   10580 O O   . VAL G 3 100 ? -5.397   -96.313  18.884  1.00 105.88 ? 100 VAL H O   1 
ATOM   10581 C CB  . VAL G 3 100 ? -7.494   -95.988  21.067  1.00 102.59 ? 100 VAL H CB  1 
ATOM   10582 C CG1 . VAL G 3 100 ? -7.954   -94.540  21.220  1.00 104.74 ? 100 VAL H CG1 1 
ATOM   10583 C CG2 . VAL G 3 100 ? -8.215   -96.894  22.056  1.00 100.47 ? 100 VAL H CG2 1 
ATOM   10584 N N   . ALA G 3 101 ? -6.911   -94.981  17.833  1.00 103.09 ? 101 ALA H N   1 
ATOM   10585 C CA  . ALA G 3 101 ? -5.954   -94.367  16.917  1.00 106.00 ? 101 ALA H CA  1 
ATOM   10586 C C   . ALA G 3 101 ? -6.263   -92.896  16.663  1.00 112.24 ? 101 ALA H C   1 
ATOM   10587 O O   . ALA G 3 101 ? -7.319   -92.402  17.074  1.00 110.26 ? 101 ALA H O   1 
ATOM   10588 C CB  . ALA G 3 101 ? -5.919   -95.140  15.602  1.00 105.71 ? 101 ALA H CB  1 
ATOM   10589 N N   . ASP G 3 102 ? -5.321   -92.195  15.995  1.00 113.32 ? 102 ASP H N   1 
ATOM   10590 C CA  . ASP G 3 102 ? -5.432   -90.780  15.642  1.00 116.53 ? 102 ASP H CA  1 
ATOM   10591 C C   . ASP G 3 102 ? -6.572   -90.512  14.638  1.00 120.82 ? 102 ASP H C   1 
ATOM   10592 O O   . ASP G 3 102 ? -6.785   -91.293  13.698  1.00 118.20 ? 102 ASP H O   1 
ATOM   10593 C CB  . ASP G 3 102 ? -4.086   -90.231  15.133  1.00 122.01 ? 102 ASP H CB  1 
ATOM   10594 C CG  . ASP G 3 102 ? -3.634   -90.810  13.811  1.00 132.83 ? 102 ASP H CG  1 
ATOM   10595 O OD1 . ASP G 3 102 ? -3.043   -91.910  13.815  1.00 131.89 ? 102 ASP H OD1 1 
ATOM   10596 O OD2 . ASP G 3 102 ? -3.906   -90.183  12.768  1.00 142.64 ? 102 ASP H OD2 1 
ATOM   10597 N N   . ARG G 3 103 ? -7.297   -89.400  14.847  1.00 115.88 ? 103 ARG H N   1 
ATOM   10598 C CA  . ARG G 3 103 ? -8.433   -88.969  14.020  1.00 116.52 ? 103 ARG H CA  1 
ATOM   10599 C C   . ARG G 3 103 ? -8.027   -88.215  12.736  1.00 120.19 ? 103 ARG H C   1 
ATOM   10600 O O   . ARG G 3 103 ? -8.896   -87.661  12.050  1.00 119.63 ? 103 ARG H O   1 
ATOM   10601 C CB  . ARG G 3 103 ? -9.403   -88.121  14.865  1.00 119.93 ? 103 ARG H CB  1 
ATOM   10602 C CG  . ARG G 3 103 ? -10.468  -88.914  15.613  1.00 135.08 ? 103 ARG H CG  1 
ATOM   10603 C CD  . ARG G 3 103 ? -10.033  -89.372  16.997  1.00 144.87 ? 103 ARG H CD  1 
ATOM   10604 N NE  . ARG G 3 103 ? -11.108  -90.103  17.669  1.00 149.98 ? 103 ARG H NE  1 
ATOM   10605 C CZ  . ARG G 3 103 ? -10.924  -90.979  18.652  1.00 164.39 ? 103 ARG H CZ  1 
ATOM   10606 N NH1 . ARG G 3 103 ? -9.703   -91.240  19.100  1.00 157.61 ? 103 ARG H NH1 1 
ATOM   10607 N NH2 . ARG G 3 103 ? -11.962  -91.613  19.186  1.00 146.25 ? 103 ARG H NH2 1 
ATOM   10608 N N   . GLU G 3 104 ? -6.713   -88.207  12.412  1.00 116.68 ? 104 GLU H N   1 
ATOM   10609 C CA  . GLU G 3 104 ? -6.146   -87.529  11.239  1.00 116.31 ? 104 GLU H CA  1 
ATOM   10610 C C   . GLU G 3 104 ? -5.628   -88.495  10.168  1.00 120.25 ? 104 GLU H C   1 
ATOM   10611 O O   . GLU G 3 104 ? -5.211   -88.053  9.089   1.00 119.30 ? 104 GLU H O   1 
ATOM   10612 C CB  . GLU G 3 104 ? -5.062   -86.517  11.657  1.00 117.60 ? 104 GLU H CB  1 
ATOM   10613 C CG  . GLU G 3 104 ? -5.548   -85.436  12.616  1.00 127.12 ? 104 GLU H CG  1 
ATOM   10614 C CD  . GLU G 3 104 ? -6.739   -84.607  12.165  1.00 141.28 ? 104 GLU H CD  1 
ATOM   10615 O OE1 . GLU G 3 104 ? -6.820   -84.293  10.955  1.00 138.98 ? 104 GLU H OE1 1 
ATOM   10616 O OE2 . GLU G 3 104 ? -7.590   -84.273  13.023  1.00 127.18 ? 104 GLU H OE2 1 
ATOM   10617 N N   . GLY G 3 105 ? -5.698   -89.796  10.474  1.00 117.51 ? 105 GLY H N   1 
ATOM   10618 C CA  . GLY G 3 105 ? -5.267   -90.883  9.604   1.00 117.70 ? 105 GLY H CA  1 
ATOM   10619 C C   . GLY G 3 105 ? -3.785   -90.820  9.322   1.00 122.30 ? 105 GLY H C   1 
ATOM   10620 O O   . GLY G 3 105 ? -3.381   -90.442  8.221   1.00 122.59 ? 105 GLY H O   1 
ATOM   10621 N N   . PHE G 3 106 ? -2.970   -91.146  10.334  1.00 119.01 ? 106 PHE H N   1 
ATOM   10622 C CA  . PHE G 3 106 ? -1.511   -91.096  10.260  1.00 119.68 ? 106 PHE H CA  1 
ATOM   10623 C C   . PHE G 3 106 ? -0.843   -92.425  10.620  1.00 124.08 ? 106 PHE H C   1 
ATOM   10624 O O   . PHE G 3 106 ? 0.295    -92.662  10.213  1.00 124.68 ? 106 PHE H O   1 
ATOM   10625 C CB  . PHE G 3 106 ? -0.974   -89.977  11.167  1.00 121.64 ? 106 PHE H CB  1 
ATOM   10626 C CG  . PHE G 3 106 ? -0.909   -88.567  10.619  1.00 123.49 ? 106 PHE H CG  1 
ATOM   10627 C CD1 . PHE G 3 106 ? 0.258    -87.826  10.713  1.00 126.60 ? 106 PHE H CD1 1 
ATOM   10628 C CD2 . PHE G 3 106 ? -2.042   -87.949  10.099  1.00 125.87 ? 106 PHE H CD2 1 
ATOM   10629 C CE1 . PHE G 3 106 ? 0.306    -86.510  10.254  1.00 127.80 ? 106 PHE H CE1 1 
ATOM   10630 C CE2 . PHE G 3 106 ? -1.989   -86.636  9.626   1.00 128.86 ? 106 PHE H CE2 1 
ATOM   10631 C CZ  . PHE G 3 106 ? -0.818   -85.923  9.714   1.00 127.10 ? 106 PHE H CZ  1 
ATOM   10632 N N   . GLY G 3 107 ? -1.529   -93.262  11.390  1.00 120.27 ? 107 GLY H N   1 
ATOM   10633 C CA  . GLY G 3 107 ? -1.002   -94.563  11.785  1.00 120.54 ? 107 GLY H CA  1 
ATOM   10634 C C   . GLY G 3 107 ? -0.496   -94.654  13.208  1.00 124.90 ? 107 GLY H C   1 
ATOM   10635 O O   . GLY G 3 107 ? 0.190    -95.621  13.551  1.00 124.70 ? 107 GLY H O   1 
ATOM   10636 N N   . TYR G 3 108 ? -0.824   -93.654  14.048  1.00 121.68 ? 108 TYR H N   1 
ATOM   10637 C CA  . TYR G 3 108 ? -0.446   -93.663  15.461  1.00 121.71 ? 108 TYR H CA  1 
ATOM   10638 C C   . TYR G 3 108 ? -1.490   -94.499  16.209  1.00 127.42 ? 108 TYR H C   1 
ATOM   10639 O O   . TYR G 3 108 ? -2.684   -94.201  16.114  1.00 127.25 ? 108 TYR H O   1 
ATOM   10640 C CB  . TYR G 3 108 ? -0.456   -92.238  16.046  1.00 122.52 ? 108 TYR H CB  1 
ATOM   10641 C CG  . TYR G 3 108 ? 0.546    -91.259  15.464  1.00 124.42 ? 108 TYR H CG  1 
ATOM   10642 C CD1 . TYR G 3 108 ? 1.860    -91.218  15.924  1.00 126.92 ? 108 TYR H CD1 1 
ATOM   10643 C CD2 . TYR G 3 108 ? 0.144    -90.274  14.563  1.00 124.90 ? 108 TYR H CD2 1 
ATOM   10644 C CE1 . TYR G 3 108 ? 2.769    -90.271  15.443  1.00 128.39 ? 108 TYR H CE1 1 
ATOM   10645 C CE2 . TYR G 3 108 ? 1.045    -89.326  14.071  1.00 125.73 ? 108 TYR H CE2 1 
ATOM   10646 C CZ  . TYR G 3 108 ? 2.356    -89.331  14.510  1.00 133.74 ? 108 TYR H CZ  1 
ATOM   10647 O OH  . TYR G 3 108 ? 3.232    -88.390  14.029  1.00 135.58 ? 108 TYR H OH  1 
ATOM   10648 N N   . TYR G 3 109 ? -1.058   -95.537  16.943  1.00 100.42 ? 109 TYR H N   1 
ATOM   10649 C CA  . TYR G 3 109 ? -1.990   -96.365  17.718  1.00 99.29  ? 109 TYR H CA  1 
ATOM   10650 C C   . TYR G 3 109 ? -1.784   -96.140  19.219  1.00 104.38 ? 109 TYR H C   1 
ATOM   10651 O O   . TYR G 3 109 ? -0.665   -96.291  19.707  1.00 105.16 ? 109 TYR H O   1 
ATOM   10652 C CB  . TYR G 3 109 ? -1.902   -97.844  17.318  1.00 99.79  ? 109 TYR H CB  1 
ATOM   10653 C CG  . TYR G 3 109 ? -2.175   -98.071  15.848  1.00 101.79 ? 109 TYR H CG  1 
ATOM   10654 C CD1 . TYR G 3 109 ? -3.463   -97.963  15.332  1.00 102.70 ? 109 TYR H CD1 1 
ATOM   10655 C CD2 . TYR G 3 109 ? -1.142   -98.368  14.966  1.00 104.65 ? 109 TYR H CD2 1 
ATOM   10656 C CE1 . TYR G 3 109 ? -3.718   -98.151  13.972  1.00 104.21 ? 109 TYR H CE1 1 
ATOM   10657 C CE2 . TYR G 3 109 ? -1.385   -98.565  13.603  1.00 106.54 ? 109 TYR H CE2 1 
ATOM   10658 C CZ  . TYR G 3 109 ? -2.677   -98.456  13.109  1.00 111.65 ? 109 TYR H CZ  1 
ATOM   10659 O OH  . TYR G 3 109 ? -2.921   -98.632  11.766  1.00 109.43 ? 109 TYR H OH  1 
ATOM   10660 N N   . TYR G 3 110 ? -2.855   -95.731  19.932  1.00 100.11 ? 110 TYR H N   1 
ATOM   10661 C CA  . TYR G 3 110 ? -2.825   -95.377  21.356  1.00 99.90  ? 110 TYR H CA  1 
ATOM   10662 C C   . TYR G 3 110 ? -3.139   -96.527  22.357  1.00 102.91 ? 110 TYR H C   1 
ATOM   10663 O O   . TYR G 3 110 ? -3.049   -96.319  23.570  1.00 103.49 ? 110 TYR H O   1 
ATOM   10664 C CB  . TYR G 3 110 ? -3.766   -94.181  21.630  1.00 101.48 ? 110 TYR H CB  1 
ATOM   10665 C CG  . TYR G 3 110 ? -3.667   -93.003  20.671  1.00 104.12 ? 110 TYR H CG  1 
ATOM   10666 C CD1 . TYR G 3 110 ? -2.434   -92.433  20.352  1.00 106.77 ? 110 TYR H CD1 1 
ATOM   10667 C CD2 . TYR G 3 110 ? -4.811   -92.394  20.165  1.00 105.13 ? 110 TYR H CD2 1 
ATOM   10668 C CE1 . TYR G 3 110 ? -2.342   -91.327  19.501  1.00 107.94 ? 110 TYR H CE1 1 
ATOM   10669 C CE2 . TYR G 3 110 ? -4.731   -91.284  19.319  1.00 107.06 ? 110 TYR H CE2 1 
ATOM   10670 C CZ  . TYR G 3 110 ? -3.495   -90.759  18.983  1.00 114.00 ? 110 TYR H CZ  1 
ATOM   10671 O OH  . TYR G 3 110 ? -3.422   -89.665  18.152  1.00 115.59 ? 110 TYR H OH  1 
ATOM   10672 N N   . GLY G 3 111 ? -3.489   -97.707  21.852  1.00 97.20  ? 111 GLY H N   1 
ATOM   10673 C CA  . GLY G 3 111 ? -3.859   -98.867  22.665  1.00 95.20  ? 111 GLY H CA  1 
ATOM   10674 C C   . GLY G 3 111 ? -5.221   -99.371  22.237  1.00 95.95  ? 111 GLY H C   1 
ATOM   10675 O O   . GLY G 3 111 ? -5.687   -98.983  21.165  1.00 95.93  ? 111 GLY H O   1 
ATOM   10676 N N   . MET G 3 112 ? -5.880   -100.225 23.047  1.00 89.88  ? 112 MET H N   1 
ATOM   10677 C CA  . MET G 3 112 ? -7.211   -100.744 22.689  1.00 88.63  ? 112 MET H CA  1 
ATOM   10678 C C   . MET G 3 112 ? -8.234   -100.582 23.838  1.00 91.95  ? 112 MET H C   1 
ATOM   10679 O O   . MET G 3 112 ? -7.985   -101.054 24.946  1.00 90.76  ? 112 MET H O   1 
ATOM   10680 C CB  . MET G 3 112 ? -7.159   -102.184 22.124  1.00 90.31  ? 112 MET H CB  1 
ATOM   10681 C CG  . MET G 3 112 ? -6.232   -103.155 22.860  1.00 93.67  ? 112 MET H CG  1 
ATOM   10682 S SD  . MET G 3 112 ? -4.898   -103.942 21.877  1.00 98.09  ? 112 MET H SD  1 
ATOM   10683 C CE  . MET G 3 112 ? -5.830   -104.856 20.627  1.00 94.42  ? 112 MET H CE  1 
ATOM   10684 N N   . ASP G 3 113 ? -9.372   -99.881  23.561  1.00 89.49  ? 113 ASP H N   1 
ATOM   10685 C CA  . ASP G 3 113 ? -10.420  -99.529  24.535  1.00 90.55  ? 113 ASP H CA  1 
ATOM   10686 C C   . ASP G 3 113 ? -11.493  -100.603 24.795  1.00 95.10  ? 113 ASP H C   1 
ATOM   10687 O O   . ASP G 3 113 ? -11.564  -101.114 25.916  1.00 96.56  ? 113 ASP H O   1 
ATOM   10688 C CB  . ASP G 3 113 ? -11.106  -98.180  24.199  1.00 93.86  ? 113 ASP H CB  1 
ATOM   10689 C CG  . ASP G 3 113 ? -11.555  -97.915  22.760  1.00 105.59 ? 113 ASP H CG  1 
ATOM   10690 O OD1 . ASP G 3 113 ? -11.877  -98.885  22.042  1.00 105.91 ? 113 ASP H OD1 1 
ATOM   10691 O OD2 . ASP G 3 113 ? -11.634  -96.729  22.374  1.00 112.11 ? 113 ASP H OD2 1 
ATOM   10692 N N   . VAL G 3 114 ? -12.366  -100.885 23.814  1.00 90.24  ? 114 VAL H N   1 
ATOM   10693 C CA  . VAL G 3 114 ? -13.451  -101.854 23.958  1.00 89.82  ? 114 VAL H CA  1 
ATOM   10694 C C   . VAL G 3 114 ? -12.872  -103.250 23.830  1.00 92.24  ? 114 VAL H C   1 
ATOM   10695 O O   . VAL G 3 114 ? -12.191  -103.546 22.850  1.00 91.12  ? 114 VAL H O   1 
ATOM   10696 C CB  . VAL G 3 114 ? -14.616  -101.617 22.961  1.00 94.40  ? 114 VAL H CB  1 
ATOM   10697 C CG1 . VAL G 3 114 ? -15.816  -102.499 23.299  1.00 94.80  ? 114 VAL H CG1 1 
ATOM   10698 C CG2 . VAL G 3 114 ? -15.031  -100.151 22.925  1.00 95.49  ? 114 VAL H CG2 1 
ATOM   10699 N N   . TRP G 3 115 ? -13.117  -104.091 24.830  1.00 88.42  ? 115 TRP H N   1 
ATOM   10700 C CA  . TRP G 3 115 ? -12.621  -105.458 24.840  1.00 87.51  ? 115 TRP H CA  1 
ATOM   10701 C C   . TRP G 3 115 ? -13.774  -106.467 24.865  1.00 95.23  ? 115 TRP H C   1 
ATOM   10702 O O   . TRP G 3 115 ? -14.849  -106.183 25.410  1.00 95.93  ? 115 TRP H O   1 
ATOM   10703 C CB  . TRP G 3 115 ? -11.698  -105.670 26.042  1.00 85.51  ? 115 TRP H CB  1 
ATOM   10704 C CG  . TRP G 3 115 ? -10.317  -105.103 25.895  1.00 85.63  ? 115 TRP H CG  1 
ATOM   10705 C CD1 . TRP G 3 115 ? -9.956   -103.787 25.950  1.00 88.82  ? 115 TRP H CD1 1 
ATOM   10706 C CD2 . TRP G 3 115 ? -9.099   -105.849 25.816  1.00 84.97  ? 115 TRP H CD2 1 
ATOM   10707 N NE1 . TRP G 3 115 ? -8.589   -103.665 25.841  1.00 87.78  ? 115 TRP H NE1 1 
ATOM   10708 C CE2 . TRP G 3 115 ? -8.037   -104.916 25.768  1.00 89.04  ? 115 TRP H CE2 1 
ATOM   10709 C CE3 . TRP G 3 115 ? -8.801   -107.220 25.739  1.00 85.96  ? 115 TRP H CE3 1 
ATOM   10710 C CZ2 . TRP G 3 115 ? -6.702   -105.311 25.654  1.00 88.74  ? 115 TRP H CZ2 1 
ATOM   10711 C CZ3 . TRP G 3 115 ? -7.479   -107.609 25.621  1.00 87.84  ? 115 TRP H CZ3 1 
ATOM   10712 C CH2 . TRP G 3 115 ? -6.446   -106.663 25.573  1.00 88.87  ? 115 TRP H CH2 1 
ATOM   10713 N N   . GLY G 3 116 ? -13.527  -107.634 24.269  1.00 93.36  ? 116 GLY H N   1 
ATOM   10714 C CA  . GLY G 3 116 ? -14.471  -108.749 24.229  1.00 94.22  ? 116 GLY H CA  1 
ATOM   10715 C C   . GLY G 3 116 ? -14.506  -109.483 25.559  1.00 100.17 ? 116 GLY H C   1 
ATOM   10716 O O   . GLY G 3 116 ? -13.636  -109.258 26.408  1.00 98.70  ? 116 GLY H O   1 
ATOM   10717 N N   . GLN G 3 117 ? -15.505  -110.368 25.772  1.00 99.61  ? 117 GLN H N   1 
ATOM   10718 C CA  . GLN G 3 117 ? -15.621  -111.092 27.051  1.00 100.64 ? 117 GLN H CA  1 
ATOM   10719 C C   . GLN G 3 117 ? -14.504  -112.158 27.262  1.00 106.77 ? 117 GLN H C   1 
ATOM   10720 O O   . GLN G 3 117 ? -14.139  -112.450 28.411  1.00 106.57 ? 117 GLN H O   1 
ATOM   10721 C CB  . GLN G 3 117 ? -17.038  -111.678 27.257  1.00 102.67 ? 117 GLN H CB  1 
ATOM   10722 C CG  . GLN G 3 117 ? -17.321  -113.050 26.645  1.00 106.32 ? 117 GLN H CG  1 
ATOM   10723 C CD  . GLN G 3 117 ? -17.635  -113.003 25.177  1.00 118.68 ? 117 GLN H CD  1 
ATOM   10724 O OE1 . GLN G 3 117 ? -17.874  -111.938 24.593  1.00 110.70 ? 117 GLN H OE1 1 
ATOM   10725 N NE2 . GLN G 3 117 ? -17.657  -114.175 24.557  1.00 111.29 ? 117 GLN H NE2 1 
ATOM   10726 N N   . GLY G 3 118 ? -13.971  -112.689 26.157  1.00 104.14 ? 118 GLY H N   1 
ATOM   10727 C CA  . GLY G 3 118 ? -12.922  -113.698 26.186  1.00 103.72 ? 118 GLY H CA  1 
ATOM   10728 C C   . GLY G 3 118 ? -13.436  -115.064 25.781  1.00 107.22 ? 118 GLY H C   1 
ATOM   10729 O O   . GLY G 3 118 ? -14.350  -115.612 26.412  1.00 107.71 ? 118 GLY H O   1 
ATOM   10730 N N   . THR G 3 119 ? -12.863  -115.611 24.709  1.00 102.23 ? 119 THR H N   1 
ATOM   10731 C CA  . THR G 3 119 ? -13.237  -116.927 24.213  1.00 102.44 ? 119 THR H CA  1 
ATOM   10732 C C   . THR G 3 119 ? -12.283  -117.957 24.801  1.00 106.09 ? 119 THR H C   1 
ATOM   10733 O O   . THR G 3 119 ? -11.065  -117.819 24.670  1.00 105.67 ? 119 THR H O   1 
ATOM   10734 C CB  . THR G 3 119 ? -13.299  -116.925 22.689  1.00 110.50 ? 119 THR H CB  1 
ATOM   10735 O OG1 . THR G 3 119 ? -14.142  -115.850 22.271  1.00 109.10 ? 119 THR H OG1 1 
ATOM   10736 C CG2 . THR G 3 119 ? -13.820  -118.237 22.130  1.00 110.65 ? 119 THR H CG2 1 
ATOM   10737 N N   . THR G 3 120 ? -12.841  -118.972 25.471  1.00 102.48 ? 120 THR H N   1 
ATOM   10738 C CA  . THR G 3 120 ? -12.062  -120.021 26.123  1.00 102.45 ? 120 THR H CA  1 
ATOM   10739 C C   . THR G 3 120 ? -11.851  -121.207 25.169  1.00 107.52 ? 120 THR H C   1 
ATOM   10740 O O   . THR G 3 120 ? -12.770  -121.995 24.935  1.00 107.40 ? 120 THR H O   1 
ATOM   10741 C CB  . THR G 3 120 ? -12.689  -120.377 27.474  1.00 106.14 ? 120 THR H CB  1 
ATOM   10742 O OG1 . THR G 3 120 ? -13.066  -119.172 28.148  1.00 103.29 ? 120 THR H OG1 1 
ATOM   10743 C CG2 . THR G 3 120 ? -11.756  -121.187 28.354  1.00 104.67 ? 120 THR H CG2 1 
ATOM   10744 N N   . VAL G 3 121 ? -10.630  -121.316 24.615  1.00 105.00 ? 121 VAL H N   1 
ATOM   10745 C CA  . VAL G 3 121 ? -10.259  -122.363 23.664  1.00 106.18 ? 121 VAL H CA  1 
ATOM   10746 C C   . VAL G 3 121 ? -9.376   -123.439 24.310  1.00 112.67 ? 121 VAL H C   1 
ATOM   10747 O O   . VAL G 3 121 ? -8.257   -123.148 24.743  1.00 112.34 ? 121 VAL H O   1 
ATOM   10748 C CB  . VAL G 3 121 ? -9.639   -121.775 22.369  1.00 109.79 ? 121 VAL H CB  1 
ATOM   10749 C CG1 . VAL G 3 121 ? -9.154   -122.871 21.429  1.00 111.15 ? 121 VAL H CG1 1 
ATOM   10750 C CG2 . VAL G 3 121 ? -10.631  -120.865 21.656  1.00 108.68 ? 121 VAL H CG2 1 
ATOM   10751 N N   . THR G 3 122 ? -9.889   -124.682 24.355  1.00 111.45 ? 122 THR H N   1 
ATOM   10752 C CA  . THR G 3 122 ? -9.190   -125.851 24.896  1.00 113.59 ? 122 THR H CA  1 
ATOM   10753 C C   . THR G 3 122 ? -8.804   -126.764 23.729  1.00 121.03 ? 122 THR H C   1 
ATOM   10754 O O   . THR G 3 122 ? -9.671   -127.142 22.937  1.00 120.71 ? 122 THR H O   1 
ATOM   10755 C CB  . THR G 3 122 ? -10.059  -126.586 25.934  1.00 123.60 ? 122 THR H CB  1 
ATOM   10756 O OG1 . THR G 3 122 ? -10.801  -125.644 26.712  1.00 124.12 ? 122 THR H OG1 1 
ATOM   10757 C CG2 . THR G 3 122 ? -9.247   -127.499 26.847  1.00 123.10 ? 122 THR H CG2 1 
ATOM   10758 N N   . VAL G 3 123 ? -7.503   -127.079 23.595  1.00 121.10 ? 123 VAL H N   1 
ATOM   10759 C CA  . VAL G 3 123 ? -6.997   -127.935 22.513  1.00 124.14 ? 123 VAL H CA  1 
ATOM   10760 C C   . VAL G 3 123 ? -6.249   -129.162 23.080  1.00 132.38 ? 123 VAL H C   1 
ATOM   10761 O O   . VAL G 3 123 ? -5.014   -129.175 23.132  1.00 132.65 ? 123 VAL H O   1 
ATOM   10762 C CB  . VAL G 3 123 ? -6.175   -127.184 21.424  1.00 128.59 ? 123 VAL H CB  1 
ATOM   10763 C CG1 . VAL G 3 123 ? -6.124   -127.998 20.141  1.00 130.76 ? 123 VAL H CG1 1 
ATOM   10764 C CG2 . VAL G 3 123 ? -6.729   -125.791 21.136  1.00 126.05 ? 123 VAL H CG2 1 
ATOM   10765 N N   . SER G 3 124 ? -7.016   -130.191 23.499  1.00 132.05 ? 124 SER H N   1 
ATOM   10766 C CA  . SER G 3 124 ? -6.501   -131.441 24.070  1.00 135.15 ? 124 SER H CA  1 
ATOM   10767 C C   . SER G 3 124 ? -7.174   -132.688 23.476  1.00 143.01 ? 124 SER H C   1 
ATOM   10768 O O   . SER G 3 124 ? -8.368   -132.663 23.152  1.00 142.28 ? 124 SER H O   1 
ATOM   10769 C CB  . SER G 3 124 ? -6.641   -131.435 25.588  1.00 137.78 ? 124 SER H CB  1 
ATOM   10770 O OG  . SER G 3 124 ? -6.169   -132.647 26.153  1.00 148.35 ? 124 SER H OG  1 
ATOM   10771 N N   . SER G 3 125 ? -6.393   -133.779 23.351  1.00 142.67 ? 125 SER H N   1 
ATOM   10772 C CA  . SER G 3 125 ? -6.830   -135.064 22.794  1.00 144.74 ? 125 SER H CA  1 
ATOM   10773 C C   . SER G 3 125 ? -7.726   -135.860 23.756  1.00 149.70 ? 125 SER H C   1 
ATOM   10774 O O   . SER G 3 125 ? -8.457   -136.752 23.325  1.00 149.64 ? 125 SER H O   1 
ATOM   10775 C CB  . SER G 3 125 ? -5.615   -135.901 22.402  1.00 150.46 ? 125 SER H CB  1 
ATOM   10776 O OG  . SER G 3 125 ? -4.793   -135.218 21.469  1.00 155.18 ? 125 SER H OG  1 
ATOM   10777 N N   . ALA G 3 126 ? -7.645   -135.518 25.055  1.00 147.45 ? 126 ALA H N   1 
ATOM   10778 C CA  . ALA G 3 126 ? -8.282   -136.102 26.240  1.00 148.79 ? 126 ALA H CA  1 
ATOM   10779 C C   . ALA G 3 126 ? -9.707   -136.658 26.087  1.00 155.40 ? 126 ALA H C   1 
ATOM   10780 O O   . ALA G 3 126 ? -9.943   -137.778 26.550  1.00 157.43 ? 126 ALA H O   1 
ATOM   10781 C CB  . ALA G 3 126 ? -8.263   -135.096 27.375  1.00 147.44 ? 126 ALA H CB  1 
ATOM   10782 N N   . SER G 3 127 ? -10.655  -135.880 25.493  1.00 151.39 ? 127 SER H N   1 
ATOM   10783 C CA  . SER G 3 127 ? -12.091  -136.213 25.298  1.00 151.79 ? 127 SER H CA  1 
ATOM   10784 C C   . SER G 3 127 ? -12.933  -136.077 26.589  1.00 156.43 ? 127 SER H C   1 
ATOM   10785 O O   . SER G 3 127 ? -12.394  -136.206 27.689  1.00 156.41 ? 127 SER H O   1 
ATOM   10786 C CB  . SER G 3 127 ? -12.296  -137.591 24.664  1.00 157.78 ? 127 SER H CB  1 
ATOM   10787 O OG  . SER G 3 127 ? -11.235  -137.956 23.798  1.00 167.07 ? 127 SER H OG  1 
ATOM   10788 N N   . THR G 3 128 ? -14.258  -135.835 26.437  1.00 153.38 ? 128 THR H N   1 
ATOM   10789 C CA  . THR G 3 128 ? -15.239  -135.638 27.519  1.00 153.48 ? 128 THR H CA  1 
ATOM   10790 C C   . THR G 3 128 ? -15.308  -136.806 28.520  1.00 160.74 ? 128 THR H C   1 
ATOM   10791 O O   . THR G 3 128 ? -15.627  -137.934 28.143  1.00 162.06 ? 128 THR H O   1 
ATOM   10792 C CB  . THR G 3 128 ? -16.642  -135.310 26.941  1.00 162.92 ? 128 THR H CB  1 
ATOM   10793 O OG1 . THR G 3 128 ? -16.534  -134.455 25.801  1.00 162.87 ? 128 THR H OG1 1 
ATOM   10794 C CG2 . THR G 3 128 ? -17.567  -134.672 27.967  1.00 160.63 ? 128 THR H CG2 1 
ATOM   10795 N N   . LYS G 3 129 ? -15.014  -136.515 29.797  1.00 158.82 ? 129 LYS H N   1 
ATOM   10796 C CA  . LYS G 3 129 ? -15.080  -137.457 30.918  1.00 161.66 ? 129 LYS H CA  1 
ATOM   10797 C C   . LYS G 3 129 ? -15.559  -136.746 32.181  1.00 167.32 ? 129 LYS H C   1 
ATOM   10798 O O   . LYS G 3 129 ? -15.085  -135.655 32.499  1.00 164.57 ? 129 LYS H O   1 
ATOM   10799 C CB  . LYS G 3 129 ? -13.723  -138.148 31.179  1.00 165.48 ? 129 LYS H CB  1 
ATOM   10800 C CG  . LYS G 3 129 ? -13.836  -139.388 32.079  1.00 181.09 ? 129 LYS H CG  1 
ATOM   10801 C CD  . LYS G 3 129 ? -12.505  -139.811 32.693  1.00 189.46 ? 129 LYS H CD  1 
ATOM   10802 C CE  . LYS G 3 129 ? -12.658  -140.897 33.736  1.00 194.87 ? 129 LYS H CE  1 
ATOM   10803 N NZ  . LYS G 3 129 ? -13.079  -140.357 35.057  1.00 197.30 ? 129 LYS H NZ  1 
ATOM   10804 N N   . GLY G 3 130 ? -16.478  -137.391 32.891  1.00 166.36 ? 130 GLY H N   1 
ATOM   10805 C CA  . GLY G 3 130 ? -17.020  -136.904 34.153  1.00 167.06 ? 130 GLY H CA  1 
ATOM   10806 C C   . GLY G 3 130 ? -16.027  -137.018 35.302  1.00 172.88 ? 130 GLY H C   1 
ATOM   10807 O O   . GLY G 3 130 ? -15.034  -137.749 35.191  1.00 172.27 ? 130 GLY H O   1 
ATOM   10808 N N   . PRO G 3 131 ? -16.264  -136.324 36.440  1.00 170.90 ? 131 PRO H N   1 
ATOM   10809 C CA  . PRO G 3 131 ? -15.295  -136.387 37.543  1.00 170.03 ? 131 PRO H CA  1 
ATOM   10810 C C   . PRO G 3 131 ? -15.516  -137.499 38.554  1.00 175.86 ? 131 PRO H C   1 
ATOM   10811 O O   . PRO G 3 131 ? -16.644  -137.741 38.993  1.00 175.82 ? 131 PRO H O   1 
ATOM   10812 C CB  . PRO G 3 131 ? -15.414  -135.010 38.195  1.00 170.83 ? 131 PRO H CB  1 
ATOM   10813 C CG  . PRO G 3 131 ? -16.797  -134.528 37.848  1.00 176.30 ? 131 PRO H CG  1 
ATOM   10814 C CD  . PRO G 3 131 ? -17.369  -135.395 36.754  1.00 173.24 ? 131 PRO H CD  1 
ATOM   10815 N N   . SER G 3 132 ? -14.412  -138.147 38.944  1.00 173.80 ? 132 SER H N   1 
ATOM   10816 C CA  . SER G 3 132 ? -14.401  -139.199 39.954  1.00 174.83 ? 132 SER H CA  1 
ATOM   10817 C C   . SER G 3 132 ? -14.249  -138.488 41.313  1.00 179.64 ? 132 SER H C   1 
ATOM   10818 O O   . SER G 3 132 ? -13.131  -138.296 41.798  1.00 178.29 ? 132 SER H O   1 
ATOM   10819 C CB  . SER G 3 132 ? -13.267  -140.190 39.686  1.00 178.62 ? 132 SER H CB  1 
ATOM   10820 O OG  . SER G 3 132 ? -13.259  -140.656 38.344  1.00 188.06 ? 132 SER H OG  1 
ATOM   10821 N N   . VAL G 3 133 ? -15.380  -137.996 41.858  1.00 177.97 ? 133 VAL H N   1 
ATOM   10822 C CA  . VAL G 3 133 ? -15.461  -137.244 43.120  1.00 177.94 ? 133 VAL H CA  1 
ATOM   10823 C C   . VAL G 3 133 ? -15.181  -138.160 44.326  1.00 184.15 ? 133 VAL H C   1 
ATOM   10824 O O   . VAL G 3 133 ? -15.832  -139.202 44.461  1.00 184.55 ? 133 VAL H O   1 
ATOM   10825 C CB  . VAL G 3 133 ? -16.826  -136.495 43.269  1.00 181.72 ? 133 VAL H CB  1 
ATOM   10826 C CG1 . VAL G 3 133 ? -16.817  -135.541 44.462  1.00 180.77 ? 133 VAL H CG1 1 
ATOM   10827 C CG2 . VAL G 3 133 ? -17.199  -135.742 41.994  1.00 181.75 ? 133 VAL H CG2 1 
ATOM   10828 N N   . PHE G 3 134 ? -14.217  -137.770 45.197  1.00 181.41 ? 134 PHE H N   1 
ATOM   10829 C CA  . PHE G 3 134 ? -13.873  -138.502 46.425  1.00 181.85 ? 134 PHE H CA  1 
ATOM   10830 C C   . PHE G 3 134 ? -13.833  -137.561 47.644  1.00 185.55 ? 134 PHE H C   1 
ATOM   10831 O O   . PHE G 3 134 ? -13.271  -136.466 47.531  1.00 184.68 ? 134 PHE H O   1 
ATOM   10832 C CB  . PHE G 3 134 ? -12.547  -139.284 46.323  1.00 184.07 ? 134 PHE H CB  1 
ATOM   10833 C CG  . PHE G 3 134 ? -12.207  -139.979 45.026  1.00 185.99 ? 134 PHE H CG  1 
ATOM   10834 C CD1 . PHE G 3 134 ? -12.839  -141.166 44.661  1.00 189.73 ? 134 PHE H CD1 1 
ATOM   10835 C CD2 . PHE G 3 134 ? -11.188  -139.504 44.217  1.00 187.88 ? 134 PHE H CD2 1 
ATOM   10836 C CE1 . PHE G 3 134 ? -12.499  -141.821 43.469  1.00 191.04 ? 134 PHE H CE1 1 
ATOM   10837 C CE2 . PHE G 3 134 ? -10.848  -140.159 43.034  1.00 190.84 ? 134 PHE H CE2 1 
ATOM   10838 C CZ  . PHE G 3 134 ? -11.499  -141.315 42.670  1.00 189.70 ? 134 PHE H CZ  1 
ATOM   10839 N N   . PRO G 3 135 ? -14.401  -137.955 48.818  1.00 182.13 ? 135 PRO H N   1 
ATOM   10840 C CA  . PRO G 3 135 ? -14.344  -137.061 49.990  1.00 181.45 ? 135 PRO H CA  1 
ATOM   10841 C C   . PRO G 3 135 ? -13.001  -137.114 50.726  1.00 183.84 ? 135 PRO H C   1 
ATOM   10842 O O   . PRO G 3 135 ? -12.158  -137.965 50.427  1.00 183.78 ? 135 PRO H O   1 
ATOM   10843 C CB  . PRO G 3 135 ? -15.510  -137.541 50.876  1.00 183.23 ? 135 PRO H CB  1 
ATOM   10844 C CG  . PRO G 3 135 ? -16.028  -138.813 50.251  1.00 187.91 ? 135 PRO H CG  1 
ATOM   10845 C CD  . PRO G 3 135 ? -15.099  -139.215 49.147  1.00 183.94 ? 135 PRO H CD  1 
ATOM   10846 N N   . LEU G 3 136 ? -12.793  -136.177 51.673  1.00 178.81 ? 136 LEU H N   1 
ATOM   10847 C CA  . LEU G 3 136 ? -11.583  -136.085 52.496  1.00 178.49 ? 136 LEU H CA  1 
ATOM   10848 C C   . LEU G 3 136 ? -11.989  -135.740 53.945  1.00 182.72 ? 136 LEU H C   1 
ATOM   10849 O O   . LEU G 3 136 ? -12.428  -134.617 54.215  1.00 182.06 ? 136 LEU H O   1 
ATOM   10850 C CB  . LEU G 3 136 ? -10.581  -135.054 51.919  1.00 177.67 ? 136 LEU H CB  1 
ATOM   10851 C CG  . LEU G 3 136 ? -10.085  -135.250 50.481  1.00 180.65 ? 136 LEU H CG  1 
ATOM   10852 C CD1 . LEU G 3 136 ? -9.664   -133.939 49.876  1.00 179.52 ? 136 LEU H CD1 1 
ATOM   10853 C CD2 . LEU G 3 136 ? -8.961   -136.267 50.406  1.00 182.91 ? 136 LEU H CD2 1 
ATOM   10854 N N   . ALA G 3 137 ? -11.887  -136.737 54.856  1.00 179.82 ? 137 ALA H N   1 
ATOM   10855 C CA  . ALA G 3 137 ? -12.261  -136.658 56.277  1.00 180.20 ? 137 ALA H CA  1 
ATOM   10856 C C   . ALA G 3 137 ? -11.485  -135.594 57.078  1.00 184.58 ? 137 ALA H C   1 
ATOM   10857 O O   . ALA G 3 137 ? -10.284  -135.430 56.849  1.00 184.80 ? 137 ALA H O   1 
ATOM   10858 C CB  . ALA G 3 137 ? -12.106  -138.024 56.933  1.00 181.77 ? 137 ALA H CB  1 
ATOM   10859 N N   . PRO G 3 138 ? -12.136  -134.882 58.037  1.00 180.99 ? 138 PRO H N   1 
ATOM   10860 C CA  . PRO G 3 138 ? -11.412  -133.847 58.803  1.00 185.26 ? 138 PRO H CA  1 
ATOM   10861 C C   . PRO G 3 138 ? -10.404  -134.377 59.826  1.00 202.19 ? 138 PRO H C   1 
ATOM   10862 O O   . PRO G 3 138 ? -10.639  -135.395 60.475  1.00 158.36 ? 138 PRO H O   1 
ATOM   10863 C CB  . PRO G 3 138 ? -12.534  -133.050 59.469  1.00 186.12 ? 138 PRO H CB  1 
ATOM   10864 C CG  . PRO G 3 138 ? -13.656  -134.013 59.594  1.00 188.52 ? 138 PRO H CG  1 
ATOM   10865 C CD  . PRO G 3 138 ? -13.564  -134.938 58.420  1.00 182.49 ? 138 PRO H CD  1 
ATOM   10866 N N   . ALA G 3 148 ? -10.787  -127.890 63.074  1.00 181.33 ? 148 ALA H N   1 
ATOM   10867 C CA  . ALA G 3 148 ? -10.273  -128.739 62.002  1.00 180.47 ? 148 ALA H CA  1 
ATOM   10868 C C   . ALA G 3 148 ? -11.195  -128.735 60.770  1.00 182.42 ? 148 ALA H C   1 
ATOM   10869 O O   . ALA G 3 148 ? -12.404  -128.933 60.899  1.00 180.60 ? 148 ALA H O   1 
ATOM   10870 C CB  . ALA G 3 148 ? -10.054  -130.157 62.508  1.00 182.26 ? 148 ALA H CB  1 
ATOM   10871 N N   . ALA G 3 149 ? -10.607  -128.492 59.580  1.00 178.97 ? 149 ALA H N   1 
ATOM   10872 C CA  . ALA G 3 149 ? -11.286  -128.393 58.280  1.00 177.11 ? 149 ALA H CA  1 
ATOM   10873 C C   . ALA G 3 149 ? -11.460  -129.734 57.568  1.00 181.63 ? 149 ALA H C   1 
ATOM   10874 O O   . ALA G 3 149 ? -10.702  -130.671 57.820  1.00 182.32 ? 149 ALA H O   1 
ATOM   10875 C CB  . ALA G 3 149 ? -10.531  -127.425 57.379  1.00 176.95 ? 149 ALA H CB  1 
ATOM   10876 N N   . LEU G 3 150 ? -12.454  -129.808 56.659  1.00 177.62 ? 150 LEU H N   1 
ATOM   10877 C CA  . LEU G 3 150 ? -12.750  -130.996 55.850  1.00 177.30 ? 150 LEU H CA  1 
ATOM   10878 C C   . LEU G 3 150 ? -12.690  -130.704 54.350  1.00 180.24 ? 150 LEU H C   1 
ATOM   10879 O O   . LEU G 3 150 ? -13.114  -129.633 53.908  1.00 179.30 ? 150 LEU H O   1 
ATOM   10880 C CB  . LEU G 3 150 ? -14.075  -131.678 56.245  1.00 177.23 ? 150 LEU H CB  1 
ATOM   10881 C CG  . LEU G 3 150 ? -15.324  -130.805 56.410  1.00 181.60 ? 150 LEU H CG  1 
ATOM   10882 C CD1 . LEU G 3 150 ? -16.103  -130.702 55.111  1.00 180.62 ? 150 LEU H CD1 1 
ATOM   10883 C CD2 . LEU G 3 150 ? -16.235  -131.383 57.471  1.00 184.84 ? 150 LEU H CD2 1 
ATOM   10884 N N   . GLY G 3 151 ? -12.169  -131.668 53.594  1.00 176.24 ? 151 GLY H N   1 
ATOM   10885 C CA  . GLY G 3 151 ? -11.975  -131.563 52.152  1.00 174.55 ? 151 GLY H CA  1 
ATOM   10886 C C   . GLY G 3 151 ? -12.999  -132.260 51.282  1.00 176.13 ? 151 GLY H C   1 
ATOM   10887 O O   . GLY G 3 151 ? -13.908  -132.933 51.780  1.00 175.99 ? 151 GLY H O   1 
ATOM   10888 N N   . CYS G 3 152 ? -12.839  -132.085 49.959  1.00 170.19 ? 152 CYS H N   1 
ATOM   10889 C CA  . CYS G 3 152 ? -13.699  -132.629 48.911  1.00 168.76 ? 152 CYS H CA  1 
ATOM   10890 C C   . CYS G 3 152 ? -12.899  -132.609 47.602  1.00 167.88 ? 152 CYS H C   1 
ATOM   10891 O O   . CYS G 3 152 ? -12.731  -131.548 46.994  1.00 166.51 ? 152 CYS H O   1 
ATOM   10892 C CB  . CYS G 3 152 ? -14.984  -131.806 48.803  1.00 169.25 ? 152 CYS H CB  1 
ATOM   10893 S SG  . CYS G 3 152 ? -16.372  -132.674 48.029  1.00 173.66 ? 152 CYS H SG  1 
ATOM   10894 N N   . LEU G 3 153 ? -12.357  -133.772 47.203  1.00 161.82 ? 153 LEU H N   1 
ATOM   10895 C CA  . LEU G 3 153 ? -11.558  -133.900 45.981  1.00 159.75 ? 153 LEU H CA  1 
ATOM   10896 C C   . LEU G 3 153 ? -12.430  -134.163 44.756  1.00 161.90 ? 153 LEU H C   1 
ATOM   10897 O O   . LEU G 3 153 ? -13.354  -134.979 44.817  1.00 162.43 ? 153 LEU H O   1 
ATOM   10898 C CB  . LEU G 3 153 ? -10.477  -134.999 46.132  1.00 159.84 ? 153 LEU H CB  1 
ATOM   10899 C CG  . LEU G 3 153 ? -9.647   -135.370 44.882  1.00 163.34 ? 153 LEU H CG  1 
ATOM   10900 C CD1 . LEU G 3 153 ? -8.632   -134.291 44.530  1.00 162.05 ? 153 LEU H CD1 1 
ATOM   10901 C CD2 . LEU G 3 153 ? -8.950   -136.689 45.067  1.00 166.29 ? 153 LEU H CD2 1 
ATOM   10902 N N   . VAL G 3 154 ? -12.117  -133.467 43.643  1.00 155.85 ? 154 VAL H N   1 
ATOM   10903 C CA  . VAL G 3 154 ? -12.760  -133.599 42.332  1.00 154.78 ? 154 VAL H CA  1 
ATOM   10904 C C   . VAL G 3 154 ? -11.617  -134.055 41.405  1.00 156.85 ? 154 VAL H C   1 
ATOM   10905 O O   . VAL G 3 154 ? -10.826  -133.220 40.963  1.00 155.35 ? 154 VAL H O   1 
ATOM   10906 C CB  . VAL G 3 154 ? -13.414  -132.261 41.873  1.00 157.71 ? 154 VAL H CB  1 
ATOM   10907 C CG1 . VAL G 3 154 ? -14.101  -132.415 40.523  1.00 157.95 ? 154 VAL H CG1 1 
ATOM   10908 C CG2 . VAL G 3 154 ? -14.400  -131.734 42.912  1.00 157.75 ? 154 VAL H CG2 1 
ATOM   10909 N N   . LYS G 3 155 ? -11.478  -135.381 41.187  1.00 152.96 ? 155 LYS H N   1 
ATOM   10910 C CA  . LYS G 3 155 ? -10.370  -135.924 40.396  1.00 151.69 ? 155 LYS H CA  1 
ATOM   10911 C C   . LYS G 3 155 ? -10.762  -136.491 39.037  1.00 155.79 ? 155 LYS H C   1 
ATOM   10912 O O   . LYS G 3 155 ? -11.796  -137.143 38.911  1.00 156.97 ? 155 LYS H O   1 
ATOM   10913 C CB  . LYS G 3 155 ? -9.584   -136.975 41.198  1.00 153.77 ? 155 LYS H CB  1 
ATOM   10914 C CG  . LYS G 3 155 ? -8.109   -137.043 40.812  1.00 161.16 ? 155 LYS H CG  1 
ATOM   10915 C CD  . LYS G 3 155 ? -7.440   -138.322 41.280  1.00 172.62 ? 155 LYS H CD  1 
ATOM   10916 C CE  . LYS G 3 155 ? -6.032   -138.423 40.747  1.00 183.87 ? 155 LYS H CE  1 
ATOM   10917 N NZ  . LYS G 3 155 ? -5.397   -139.723 41.085  1.00 194.58 ? 155 LYS H NZ  1 
ATOM   10918 N N   . ASP G 3 156 ? -9.882   -136.259 38.034  1.00 150.39 ? 156 ASP H N   1 
ATOM   10919 C CA  . ASP G 3 156 ? -9.924   -136.714 36.636  1.00 149.72 ? 156 ASP H CA  1 
ATOM   10920 C C   . ASP G 3 156 ? -11.239  -136.403 35.896  1.00 152.40 ? 156 ASP H C   1 
ATOM   10921 O O   . ASP G 3 156 ? -12.205  -137.168 35.977  1.00 153.58 ? 156 ASP H O   1 
ATOM   10922 C CB  . ASP G 3 156 ? -9.563   -138.210 36.525  1.00 152.32 ? 156 ASP H CB  1 
ATOM   10923 C CG  . ASP G 3 156 ? -8.149   -138.531 36.979  1.00 160.04 ? 156 ASP H CG  1 
ATOM   10924 O OD1 . ASP G 3 156 ? -7.192   -138.143 36.270  1.00 159.04 ? 156 ASP H OD1 1 
ATOM   10925 O OD2 . ASP G 3 156 ? -7.999   -139.179 38.034  1.00 165.93 ? 156 ASP H OD2 1 
ATOM   10926 N N   . TYR G 3 157 ? -11.247  -135.278 35.154  1.00 146.12 ? 157 TYR H N   1 
ATOM   10927 C CA  . TYR G 3 157 ? -12.383  -134.816 34.351  1.00 145.96 ? 157 TYR H CA  1 
ATOM   10928 C C   . TYR G 3 157 ? -11.935  -134.008 33.130  1.00 148.52 ? 157 TYR H C   1 
ATOM   10929 O O   . TYR G 3 157 ? -10.789  -133.556 33.072  1.00 146.45 ? 157 TYR H O   1 
ATOM   10930 C CB  . TYR G 3 157 ? -13.424  -134.047 35.203  1.00 146.53 ? 157 TYR H CB  1 
ATOM   10931 C CG  . TYR G 3 157 ? -13.013  -132.662 35.666  1.00 144.93 ? 157 TYR H CG  1 
ATOM   10932 C CD1 . TYR G 3 157 ? -13.252  -131.543 34.875  1.00 146.14 ? 157 TYR H CD1 1 
ATOM   10933 C CD2 . TYR G 3 157 ? -12.473  -132.460 36.933  1.00 144.04 ? 157 TYR H CD2 1 
ATOM   10934 C CE1 . TYR G 3 157 ? -12.883  -130.268 35.296  1.00 144.45 ? 157 TYR H CE1 1 
ATOM   10935 C CE2 . TYR G 3 157 ? -12.118  -131.186 37.373  1.00 143.06 ? 157 TYR H CE2 1 
ATOM   10936 C CZ  . TYR G 3 157 ? -12.329  -130.091 36.551  1.00 147.34 ? 157 TYR H CZ  1 
ATOM   10937 O OH  . TYR G 3 157 ? -11.993  -128.828 36.965  1.00 144.67 ? 157 TYR H OH  1 
ATOM   10938 N N   . PHE G 3 158 ? -12.845  -133.830 32.163  1.00 145.92 ? 158 PHE H N   1 
ATOM   10939 C CA  . PHE G 3 158 ? -12.621  -133.058 30.941  1.00 145.16 ? 158 PHE H CA  1 
ATOM   10940 C C   . PHE G 3 158 ? -13.976  -132.622 30.363  1.00 152.64 ? 158 PHE H C   1 
ATOM   10941 O O   . PHE G 3 158 ? -14.895  -133.442 30.366  1.00 155.11 ? 158 PHE H O   1 
ATOM   10942 C CB  . PHE G 3 158 ? -11.812  -133.867 29.918  1.00 146.47 ? 158 PHE H CB  1 
ATOM   10943 C CG  . PHE G 3 158 ? -11.180  -133.036 28.831  1.00 146.02 ? 158 PHE H CG  1 
ATOM   10944 C CD1 . PHE G 3 158 ? -11.789  -132.909 27.590  1.00 150.11 ? 158 PHE H CD1 1 
ATOM   10945 C CD2 . PHE G 3 158 ? -9.973   -132.382 29.047  1.00 144.92 ? 158 PHE H CD2 1 
ATOM   10946 C CE1 . PHE G 3 158 ? -11.200  -132.149 26.579  1.00 149.43 ? 158 PHE H CE1 1 
ATOM   10947 C CE2 . PHE G 3 158 ? -9.386   -131.617 28.038  1.00 146.00 ? 158 PHE H CE2 1 
ATOM   10948 C CZ  . PHE G 3 158 ? -10.006  -131.504 26.811  1.00 145.45 ? 158 PHE H CZ  1 
ATOM   10949 N N   . PRO G 3 159 ? -14.187  -131.358 29.919  1.00 149.05 ? 159 PRO H N   1 
ATOM   10950 C CA  . PRO G 3 159 ? -13.235  -130.241 29.806  1.00 146.36 ? 159 PRO H CA  1 
ATOM   10951 C C   . PRO G 3 159 ? -12.955  -129.495 31.123  1.00 147.61 ? 159 PRO H C   1 
ATOM   10952 O O   . PRO G 3 159 ? -12.310  -130.081 31.984  1.00 146.80 ? 159 PRO H O   1 
ATOM   10953 C CB  . PRO G 3 159 ? -13.857  -129.374 28.708  1.00 149.18 ? 159 PRO H CB  1 
ATOM   10954 C CG  . PRO G 3 159 ? -15.330  -129.587 28.856  1.00 156.48 ? 159 PRO H CG  1 
ATOM   10955 C CD  . PRO G 3 159 ? -15.510  -130.993 29.371  1.00 153.08 ? 159 PRO H CD  1 
ATOM   10956 N N   . GLU G 3 160 ? -13.385  -128.228 31.290  1.00 142.81 ? 160 GLU H N   1 
ATOM   10957 C CA  . GLU G 3 160 ? -13.043  -127.484 32.501  1.00 141.16 ? 160 GLU H CA  1 
ATOM   10958 C C   . GLU G 3 160 ? -14.238  -127.042 33.409  1.00 147.30 ? 160 GLU H C   1 
ATOM   10959 O O   . GLU G 3 160 ? -14.069  -127.184 34.624  1.00 146.80 ? 160 GLU H O   1 
ATOM   10960 C CB  . GLU G 3 160 ? -12.151  -126.277 32.143  1.00 140.01 ? 160 GLU H CB  1 
ATOM   10961 C CG  . GLU G 3 160 ? -11.606  -125.468 33.316  1.00 149.24 ? 160 GLU H CG  1 
ATOM   10962 C CD  . GLU G 3 160 ? -10.614  -126.144 34.246  1.00 170.84 ? 160 GLU H CD  1 
ATOM   10963 O OE1 . GLU G 3 160 ? -11.058  -126.852 35.180  1.00 162.29 ? 160 GLU H OE1 1 
ATOM   10964 O OE2 . GLU G 3 160 ? -9.397   -125.892 34.094  1.00 165.69 ? 160 GLU H OE2 1 
ATOM   10965 N N   . PRO G 3 161 ? -15.396  -126.492 32.933  1.00 146.02 ? 161 PRO H N   1 
ATOM   10966 C CA  . PRO G 3 161 ? -16.430  -126.017 33.886  1.00 147.06 ? 161 PRO H CA  1 
ATOM   10967 C C   . PRO G 3 161 ? -17.001  -127.051 34.881  1.00 153.59 ? 161 PRO H C   1 
ATOM   10968 O O   . PRO G 3 161 ? -17.706  -127.992 34.496  1.00 155.30 ? 161 PRO H O   1 
ATOM   10969 C CB  . PRO G 3 161 ? -17.525  -125.438 32.979  1.00 150.32 ? 161 PRO H CB  1 
ATOM   10970 C CG  . PRO G 3 161 ? -17.277  -126.036 31.638  1.00 155.50 ? 161 PRO H CG  1 
ATOM   10971 C CD  . PRO G 3 161 ? -15.791  -126.185 31.543  1.00 148.65 ? 161 PRO H CD  1 
ATOM   10972 N N   . VAL G 3 162 ? -16.684  -126.842 36.188  1.00 149.33 ? 162 VAL H N   1 
ATOM   10973 C CA  . VAL G 3 162 ? -17.114  -127.637 37.351  1.00 149.42 ? 162 VAL H CA  1 
ATOM   10974 C C   . VAL G 3 162 ? -17.504  -126.678 38.490  1.00 152.47 ? 162 VAL H C   1 
ATOM   10975 O O   . VAL G 3 162 ? -16.652  -125.947 39.003  1.00 150.03 ? 162 VAL H O   1 
ATOM   10976 C CB  . VAL G 3 162 ? -16.044  -128.683 37.779  1.00 152.52 ? 162 VAL H CB  1 
ATOM   10977 C CG1 . VAL G 3 162 ? -16.247  -129.148 39.217  1.00 152.44 ? 162 VAL H CG1 1 
ATOM   10978 C CG2 . VAL G 3 162 ? -16.046  -129.878 36.837  1.00 153.46 ? 162 VAL H CG2 1 
ATOM   10979 N N   . THR G 3 163 ? -18.795  -126.666 38.858  1.00 150.88 ? 163 THR H N   1 
ATOM   10980 C CA  . THR G 3 163 ? -19.315  -125.801 39.920  1.00 150.73 ? 163 THR H CA  1 
ATOM   10981 C C   . THR G 3 163 ? -19.438  -126.603 41.212  1.00 156.23 ? 163 THR H C   1 
ATOM   10982 O O   . THR G 3 163 ? -20.082  -127.653 41.223  1.00 156.88 ? 163 THR H O   1 
ATOM   10983 C CB  . THR G 3 163 ? -20.637  -125.130 39.495  1.00 158.10 ? 163 THR H CB  1 
ATOM   10984 O OG1 . THR G 3 163 ? -20.576  -124.757 38.115  1.00 157.21 ? 163 THR H OG1 1 
ATOM   10985 C CG2 . THR G 3 163 ? -20.977  -123.909 40.349  1.00 155.51 ? 163 THR H CG2 1 
ATOM   10986 N N   . VAL G 3 164 ? -18.800  -126.121 42.292  1.00 153.16 ? 164 VAL H N   1 
ATOM   10987 C CA  . VAL G 3 164 ? -18.807  -126.777 43.606  1.00 153.81 ? 164 VAL H CA  1 
ATOM   10988 C C   . VAL G 3 164 ? -19.581  -125.918 44.618  1.00 160.58 ? 164 VAL H C   1 
ATOM   10989 O O   . VAL G 3 164 ? -19.309  -124.721 44.742  1.00 159.55 ? 164 VAL H O   1 
ATOM   10990 C CB  . VAL G 3 164 ? -17.373  -127.140 44.104  1.00 156.82 ? 164 VAL H CB  1 
ATOM   10991 C CG1 . VAL G 3 164 ? -17.418  -127.958 45.394  1.00 156.86 ? 164 VAL H CG1 1 
ATOM   10992 C CG2 . VAL G 3 164 ? -16.583  -127.892 43.035  1.00 156.51 ? 164 VAL H CG2 1 
ATOM   10993 N N   . SER G 3 165 ? -20.550  -126.536 45.327  1.00 160.25 ? 165 SER H N   1 
ATOM   10994 C CA  . SER G 3 165 ? -21.388  -125.889 46.342  1.00 161.35 ? 165 SER H CA  1 
ATOM   10995 C C   . SER G 3 165 ? -21.581  -126.803 47.555  1.00 167.20 ? 165 SER H C   1 
ATOM   10996 O O   . SER G 3 165 ? -21.707  -128.013 47.386  1.00 166.58 ? 165 SER H O   1 
ATOM   10997 C CB  . SER G 3 165 ? -22.747  -125.521 45.753  1.00 166.71 ? 165 SER H CB  1 
ATOM   10998 O OG  . SER G 3 165 ? -23.504  -126.676 45.427  1.00 178.67 ? 165 SER H OG  1 
ATOM   10999 N N   . TRP G 3 166 ? -21.614  -126.231 48.771  1.00 165.66 ? 166 TRP H N   1 
ATOM   11000 C CA  . TRP G 3 166 ? -21.807  -127.015 49.994  1.00 166.50 ? 166 TRP H CA  1 
ATOM   11001 C C   . TRP G 3 166 ? -23.252  -126.936 50.465  1.00 170.22 ? 166 TRP H C   1 
ATOM   11002 O O   . TRP G 3 166 ? -23.828  -125.845 50.510  1.00 169.30 ? 166 TRP H O   1 
ATOM   11003 C CB  . TRP G 3 166 ? -20.848  -126.577 51.113  1.00 165.92 ? 166 TRP H CB  1 
ATOM   11004 C CG  . TRP G 3 166 ? -19.389  -126.698 50.776  1.00 167.65 ? 166 TRP H CG  1 
ATOM   11005 C CD1 . TRP G 3 166 ? -18.623  -125.776 50.129  1.00 170.46 ? 166 TRP H CD1 1 
ATOM   11006 C CD2 . TRP G 3 166 ? -18.515  -127.787 51.103  1.00 167.98 ? 166 TRP H CD2 1 
ATOM   11007 N NE1 . TRP G 3 166 ? -17.325  -126.223 50.026  1.00 170.18 ? 166 TRP H NE1 1 
ATOM   11008 C CE2 . TRP G 3 166 ? -17.232  -127.459 50.610  1.00 172.08 ? 166 TRP H CE2 1 
ATOM   11009 C CE3 . TRP G 3 166 ? -18.695  -129.023 51.746  1.00 169.71 ? 166 TRP H CE3 1 
ATOM   11010 C CZ2 . TRP G 3 166 ? -16.132  -128.316 50.746  1.00 171.79 ? 166 TRP H CZ2 1 
ATOM   11011 C CZ3 . TRP G 3 166 ? -17.605  -129.873 51.877  1.00 171.72 ? 166 TRP H CZ3 1 
ATOM   11012 C CH2 . TRP G 3 166 ? -16.341  -129.515 51.387  1.00 172.42 ? 166 TRP H CH2 1 
ATOM   11013 N N   . ASN G 3 167 ? -23.830  -128.107 50.813  1.00 190.95 ? 167 ASN H N   1 
ATOM   11014 C CA  . ASN G 3 167 ? -25.209  -128.306 51.288  1.00 196.55 ? 167 ASN H CA  1 
ATOM   11015 C C   . ASN G 3 167 ? -26.244  -127.714 50.313  1.00 201.35 ? 167 ASN H C   1 
ATOM   11016 O O   . ASN G 3 167 ? -27.179  -127.020 50.728  1.00 206.27 ? 167 ASN H O   1 
ATOM   11017 C CB  . ASN G 3 167 ? -25.385  -127.797 52.733  1.00 204.00 ? 167 ASN H CB  1 
ATOM   11018 C CG  . ASN G 3 167 ? -24.453  -128.450 53.726  1.00 229.49 ? 167 ASN H CG  1 
ATOM   11019 O OD1 . ASN G 3 167 ? -24.529  -129.654 53.992  1.00 223.72 ? 167 ASN H OD1 1 
ATOM   11020 N ND2 . ASN G 3 167 ? -23.553  -127.666 54.300  1.00 222.22 ? 167 ASN H ND2 1 
ATOM   11021 N N   . SER G 3 168 ? -26.041  -127.993 48.998  1.00 192.82 ? 168 SER H N   1 
ATOM   11022 C CA  . SER G 3 168 ? -26.845  -127.544 47.848  1.00 192.71 ? 168 SER H CA  1 
ATOM   11023 C C   . SER G 3 168 ? -26.903  -126.002 47.708  1.00 197.22 ? 168 SER H C   1 
ATOM   11024 O O   . SER G 3 168 ? -27.790  -125.469 47.035  1.00 199.21 ? 168 SER H O   1 
ATOM   11025 C CB  . SER G 3 168 ? -28.241  -128.169 47.867  1.00 200.47 ? 168 SER H CB  1 
ATOM   11026 O OG  . SER G 3 168 ? -28.179  -129.585 47.807  1.00 206.10 ? 168 SER H OG  1 
ATOM   11027 N N   . GLY G 3 169 ? -25.924  -125.321 48.305  1.00 191.53 ? 169 GLY H N   1 
ATOM   11028 C CA  . GLY G 3 169 ? -25.810  -123.867 48.293  1.00 192.12 ? 169 GLY H CA  1 
ATOM   11029 C C   . GLY G 3 169 ? -26.301  -123.212 49.569  1.00 200.31 ? 169 GLY H C   1 
ATOM   11030 O O   . GLY G 3 169 ? -27.054  -122.235 49.513  1.00 204.05 ? 169 GLY H O   1 
ATOM   11031 N N   . ALA G 3 170 ? -25.876  -123.748 50.730  1.00 196.37 ? 170 ALA H N   1 
ATOM   11032 C CA  . ALA G 3 170 ? -26.245  -123.233 52.049  1.00 201.57 ? 170 ALA H CA  1 
ATOM   11033 C C   . ALA G 3 170 ? -25.014  -122.713 52.796  1.00 201.88 ? 170 ALA H C   1 
ATOM   11034 O O   . ALA G 3 170 ? -25.028  -121.575 53.273  1.00 204.54 ? 170 ALA H O   1 
ATOM   11035 C CB  . ALA G 3 170 ? -26.949  -124.312 52.859  1.00 206.30 ? 170 ALA H CB  1 
ATOM   11036 N N   . LEU G 3 171 ? -23.948  -123.542 52.878  1.00 192.20 ? 171 LEU H N   1 
ATOM   11037 C CA  . LEU G 3 171 ? -22.682  -123.204 53.529  1.00 189.08 ? 171 LEU H CA  1 
ATOM   11038 C C   . LEU G 3 171 ? -21.857  -122.337 52.582  1.00 187.07 ? 171 LEU H C   1 
ATOM   11039 O O   . LEU G 3 171 ? -21.436  -122.798 51.517  1.00 181.94 ? 171 LEU H O   1 
ATOM   11040 C CB  . LEU G 3 171 ? -21.932  -124.486 53.945  1.00 186.30 ? 171 LEU H CB  1 
ATOM   11041 C CG  . LEU G 3 171 ? -20.527  -124.344 54.536  1.00 188.36 ? 171 LEU H CG  1 
ATOM   11042 C CD1 . LEU G 3 171 ? -20.564  -123.736 55.931  1.00 193.60 ? 171 LEU H CD1 1 
ATOM   11043 C CD2 . LEU G 3 171 ? -19.848  -125.687 54.597  1.00 187.60 ? 171 LEU H CD2 1 
ATOM   11044 N N   . THR G 3 172 ? -21.667  -121.066 52.966  1.00 184.35 ? 172 THR H N   1 
ATOM   11045 C CA  . THR G 3 172 ? -20.956  -120.054 52.179  1.00 180.13 ? 172 THR H CA  1 
ATOM   11046 C C   . THR G 3 172 ? -19.731  -119.488 52.901  1.00 181.05 ? 172 THR H C   1 
ATOM   11047 O O   . THR G 3 172 ? -18.759  -119.102 52.249  1.00 176.30 ? 172 THR H O   1 
ATOM   11048 C CB  . THR G 3 172 ? -21.927  -118.936 51.752  1.00 191.55 ? 172 THR H CB  1 
ATOM   11049 O OG1 . THR G 3 172 ? -22.668  -118.481 52.891  1.00 197.44 ? 172 THR H OG1 1 
ATOM   11050 C CG2 . THR G 3 172 ? -22.887  -119.379 50.651  1.00 190.11 ? 172 THR H CG2 1 
ATOM   11051 N N   . SER G 3 173 ? -19.786  -119.426 54.240  1.00 180.63 ? 173 SER H N   1 
ATOM   11052 C CA  . SER G 3 173 ? -18.713  -118.889 55.072  1.00 179.72 ? 173 SER H CA  1 
ATOM   11053 C C   . SER G 3 173 ? -17.543  -119.866 55.196  1.00 178.42 ? 173 SER H C   1 
ATOM   11054 O O   . SER G 3 173 ? -17.757  -121.057 55.433  1.00 178.48 ? 173 SER H O   1 
ATOM   11055 C CB  . SER G 3 173 ? -19.248  -118.517 56.452  1.00 189.78 ? 173 SER H CB  1 
ATOM   11056 O OG  . SER G 3 173 ? -20.393  -117.684 56.356  1.00 204.37 ? 173 SER H OG  1 
ATOM   11057 N N   . GLY G 3 174 ? -16.325  -119.348 55.015  1.00 170.30 ? 174 GLY H N   1 
ATOM   11058 C CA  . GLY G 3 174 ? -15.075  -120.101 55.117  1.00 165.76 ? 174 GLY H CA  1 
ATOM   11059 C C   . GLY G 3 174 ? -14.854  -121.170 54.064  1.00 163.03 ? 174 GLY H C   1 
ATOM   11060 O O   . GLY G 3 174 ? -13.982  -122.026 54.229  1.00 159.61 ? 174 GLY H O   1 
ATOM   11061 N N   . VAL G 3 175 ? -15.633  -121.114 52.970  1.00 158.24 ? 175 VAL H N   1 
ATOM   11062 C CA  . VAL G 3 175 ? -15.581  -122.049 51.846  1.00 154.67 ? 175 VAL H CA  1 
ATOM   11063 C C   . VAL G 3 175 ? -14.442  -121.660 50.893  1.00 154.72 ? 175 VAL H C   1 
ATOM   11064 O O   . VAL G 3 175 ? -14.417  -120.530 50.393  1.00 154.69 ? 175 VAL H O   1 
ATOM   11065 C CB  . VAL G 3 175 ? -16.965  -122.125 51.137  1.00 159.83 ? 175 VAL H CB  1 
ATOM   11066 C CG1 . VAL G 3 175 ? -16.871  -122.788 49.763  1.00 156.03 ? 175 VAL H CG1 1 
ATOM   11067 C CG2 . VAL G 3 175 ? -17.996  -122.832 52.016  1.00 163.45 ? 175 VAL H CG2 1 
ATOM   11068 N N   . HIS G 3 176 ? -13.503  -122.602 50.654  1.00 147.65 ? 176 HIS H N   1 
ATOM   11069 C CA  . HIS G 3 176 ? -12.350  -122.421 49.765  1.00 143.91 ? 176 HIS H CA  1 
ATOM   11070 C C   . HIS G 3 176 ? -12.370  -123.456 48.637  1.00 143.20 ? 176 HIS H C   1 
ATOM   11071 O O   . HIS G 3 176 ? -12.116  -124.636 48.880  1.00 141.78 ? 176 HIS H O   1 
ATOM   11072 C CB  . HIS G 3 176 ? -11.019  -122.505 50.545  1.00 144.62 ? 176 HIS H CB  1 
ATOM   11073 C CG  . HIS G 3 176 ? -10.595  -121.230 51.205  1.00 149.28 ? 176 HIS H CG  1 
ATOM   11074 N ND1 . HIS G 3 176 ? -10.838  -120.997 52.549  1.00 153.86 ? 176 HIS H ND1 1 
ATOM   11075 C CD2 . HIS G 3 176 ? -9.914   -120.177 50.696  1.00 150.13 ? 176 HIS H CD2 1 
ATOM   11076 C CE1 . HIS G 3 176 ? -10.322  -119.806 52.805  1.00 153.76 ? 176 HIS H CE1 1 
ATOM   11077 N NE2 . HIS G 3 176 ? -9.754   -119.274 51.721  1.00 151.82 ? 176 HIS H NE2 1 
ATOM   11078 N N   . THR G 3 177 ? -12.684  -123.013 47.409  1.00 137.93 ? 177 THR H N   1 
ATOM   11079 C CA  . THR G 3 177 ? -12.705  -123.879 46.232  1.00 136.20 ? 177 THR H CA  1 
ATOM   11080 C C   . THR G 3 177 ? -11.499  -123.516 45.369  1.00 138.25 ? 177 THR H C   1 
ATOM   11081 O O   . THR G 3 177 ? -11.481  -122.473 44.714  1.00 137.39 ? 177 THR H O   1 
ATOM   11082 C CB  . THR G 3 177 ? -14.071  -123.851 45.524  1.00 147.90 ? 177 THR H CB  1 
ATOM   11083 O OG1 . THR G 3 177 ? -15.099  -124.104 46.484  1.00 150.94 ? 177 THR H OG1 1 
ATOM   11084 C CG2 . THR G 3 177 ? -14.170  -124.883 44.404  1.00 145.98 ? 177 THR H CG2 1 
ATOM   11085 N N   . PHE G 3 178 ? -10.471  -124.367 45.429  1.00 134.73 ? 178 PHE H N   1 
ATOM   11086 C CA  . PHE G 3 178 ? -9.193   -124.203 44.740  1.00 134.37 ? 178 PHE H CA  1 
ATOM   11087 C C   . PHE G 3 178 ? -9.270   -124.400 43.236  1.00 138.39 ? 178 PHE H C   1 
ATOM   11088 O O   . PHE G 3 178 ? -10.006  -125.282 42.783  1.00 138.54 ? 178 PHE H O   1 
ATOM   11089 C CB  . PHE G 3 178 ? -8.145   -125.154 45.333  1.00 136.67 ? 178 PHE H CB  1 
ATOM   11090 C CG  . PHE G 3 178 ? -7.745   -124.801 46.741  1.00 138.98 ? 178 PHE H CG  1 
ATOM   11091 C CD1 . PHE G 3 178 ? -6.715   -123.904 46.981  1.00 142.26 ? 178 PHE H CD1 1 
ATOM   11092 C CD2 . PHE G 3 178 ? -8.399   -125.367 47.830  1.00 141.89 ? 178 PHE H CD2 1 
ATOM   11093 C CE1 . PHE G 3 178 ? -6.350   -123.573 48.283  1.00 144.03 ? 178 PHE H CE1 1 
ATOM   11094 C CE2 . PHE G 3 178 ? -8.036   -125.029 49.133  1.00 145.84 ? 178 PHE H CE2 1 
ATOM   11095 C CZ  . PHE G 3 178 ? -7.016   -124.132 49.349  1.00 144.04 ? 178 PHE H CZ  1 
ATOM   11096 N N   . PRO G 3 179 ? -8.470   -123.639 42.443  1.00 134.44 ? 179 PRO H N   1 
ATOM   11097 C CA  . PRO G 3 179 ? -8.492   -123.825 40.983  1.00 134.12 ? 179 PRO H CA  1 
ATOM   11098 C C   . PRO G 3 179 ? -7.956   -125.189 40.561  1.00 138.74 ? 179 PRO H C   1 
ATOM   11099 O O   . PRO G 3 179 ? -7.142   -125.792 41.262  1.00 138.21 ? 179 PRO H O   1 
ATOM   11100 C CB  . PRO G 3 179 ? -7.616   -122.684 40.457  1.00 136.49 ? 179 PRO H CB  1 
ATOM   11101 C CG  . PRO G 3 179 ? -7.509   -121.713 41.588  1.00 140.78 ? 179 PRO H CG  1 
ATOM   11102 C CD  . PRO G 3 179 ? -7.539   -122.557 42.819  1.00 136.32 ? 179 PRO H CD  1 
ATOM   11103 N N   . ALA G 3 180 ? -8.453   -125.688 39.429  1.00 136.89 ? 180 ALA H N   1 
ATOM   11104 C CA  . ALA G 3 180 ? -8.070   -126.988 38.891  1.00 138.18 ? 180 ALA H CA  1 
ATOM   11105 C C   . ALA G 3 180 ? -6.718   -126.950 38.182  1.00 144.35 ? 180 ALA H C   1 
ATOM   11106 O O   . ALA G 3 180 ? -6.299   -125.897 37.687  1.00 145.21 ? 180 ALA H O   1 
ATOM   11107 C CB  . ALA G 3 180 ? -9.148   -127.490 37.944  1.00 138.72 ? 180 ALA H CB  1 
ATOM   11108 N N   . VAL G 3 181 ? -6.041   -128.111 38.136  1.00 141.05 ? 181 VAL H N   1 
ATOM   11109 C CA  . VAL G 3 181 ? -4.754   -128.295 37.461  1.00 143.07 ? 181 VAL H CA  1 
ATOM   11110 C C   . VAL G 3 181 ? -4.807   -129.519 36.549  1.00 146.09 ? 181 VAL H C   1 
ATOM   11111 O O   . VAL G 3 181 ? -5.327   -130.560 36.954  1.00 144.06 ? 181 VAL H O   1 
ATOM   11112 C CB  . VAL G 3 181 ? -3.524   -128.313 38.413  1.00 148.31 ? 181 VAL H CB  1 
ATOM   11113 C CG1 . VAL G 3 181 ? -3.119   -126.901 38.818  1.00 147.50 ? 181 VAL H CG1 1 
ATOM   11114 C CG2 . VAL G 3 181 ? -3.760   -129.191 39.643  1.00 146.96 ? 181 VAL H CG2 1 
ATOM   11115 N N   . LEU G 3 182 ? -4.297   -129.387 35.312  1.00 144.59 ? 182 LEU H N   1 
ATOM   11116 C CA  . LEU G 3 182 ? -4.276   -130.491 34.357  1.00 146.76 ? 182 LEU H CA  1 
ATOM   11117 C C   . LEU G 3 182 ? -3.201   -131.496 34.768  1.00 153.45 ? 182 LEU H C   1 
ATOM   11118 O O   . LEU G 3 182 ? -2.041   -131.116 34.942  1.00 156.14 ? 182 LEU H O   1 
ATOM   11119 C CB  . LEU G 3 182 ? -4.036   -129.984 32.925  1.00 149.87 ? 182 LEU H CB  1 
ATOM   11120 C CG  . LEU G 3 182 ? -4.137   -131.041 31.820  1.00 157.88 ? 182 LEU H CG  1 
ATOM   11121 C CD1 . LEU G 3 182 ? -5.164   -130.654 30.785  1.00 157.34 ? 182 LEU H CD1 1 
ATOM   11122 C CD2 . LEU G 3 182 ? -2.791   -131.283 31.167  1.00 166.74 ? 182 LEU H CD2 1 
ATOM   11123 N N   . GLN G 3 183 ? -3.599   -132.770 34.938  1.00 149.00 ? 183 GLN H N   1 
ATOM   11124 C CA  . GLN G 3 183 ? -2.700   -133.860 35.324  1.00 151.38 ? 183 GLN H CA  1 
ATOM   11125 C C   . GLN G 3 183 ? -1.842   -134.319 34.144  1.00 160.62 ? 183 GLN H C   1 
ATOM   11126 O O   . GLN G 3 183 ? -2.070   -133.904 33.004  1.00 161.02 ? 183 GLN H O   1 
ATOM   11127 C CB  . GLN G 3 183 ? -3.490   -135.050 35.900  1.00 150.56 ? 183 GLN H CB  1 
ATOM   11128 C CG  . GLN G 3 183 ? -4.040   -134.816 37.298  1.00 161.05 ? 183 GLN H CG  1 
ATOM   11129 C CD  . GLN G 3 183 ? -4.821   -136.008 37.778  1.00 175.62 ? 183 GLN H CD  1 
ATOM   11130 O OE1 . GLN G 3 183 ? -4.256   -137.005 38.243  1.00 172.34 ? 183 GLN H OE1 1 
ATOM   11131 N NE2 . GLN G 3 183 ? -6.139   -135.936 37.661  1.00 162.87 ? 183 GLN H NE2 1 
ATOM   11132 N N   . SER G 3 184 ? -0.859   -135.196 34.425  1.00 161.39 ? 184 SER H N   1 
ATOM   11133 C CA  . SER G 3 184 ? 0.043    -135.778 33.430  1.00 167.53 ? 184 SER H CA  1 
ATOM   11134 C C   . SER G 3 184 ? -0.762   -136.591 32.402  1.00 172.38 ? 184 SER H C   1 
ATOM   11135 O O   . SER G 3 184 ? -0.416   -136.603 31.220  1.00 176.48 ? 184 SER H O   1 
ATOM   11136 C CB  . SER G 3 184 ? 1.088    -136.652 34.115  1.00 174.16 ? 184 SER H CB  1 
ATOM   11137 O OG  . SER G 3 184 ? 1.740    -135.952 35.165  1.00 180.02 ? 184 SER H OG  1 
ATOM   11138 N N   . SER G 3 185 ? -1.874   -137.211 32.858  1.00 164.77 ? 185 SER H N   1 
ATOM   11139 C CA  . SER G 3 185 ? -2.816   -137.992 32.053  1.00 164.26 ? 185 SER H CA  1 
ATOM   11140 C C   . SER G 3 185 ? -3.561   -137.111 31.035  1.00 167.43 ? 185 SER H C   1 
ATOM   11141 O O   . SER G 3 185 ? -4.020   -137.616 30.008  1.00 168.85 ? 185 SER H O   1 
ATOM   11142 C CB  . SER G 3 185 ? -3.820   -138.702 32.959  1.00 162.99 ? 185 SER H CB  1 
ATOM   11143 O OG  . SER G 3 185 ? -4.517   -137.788 33.792  1.00 165.83 ? 185 SER H OG  1 
ATOM   11144 N N   . GLY G 3 186 ? -3.663   -135.815 31.338  1.00 161.48 ? 186 GLY H N   1 
ATOM   11145 C CA  . GLY G 3 186 ? -4.336   -134.820 30.511  1.00 160.15 ? 186 GLY H CA  1 
ATOM   11146 C C   . GLY G 3 186 ? -5.724   -134.456 31.002  1.00 158.33 ? 186 GLY H C   1 
ATOM   11147 O O   . GLY G 3 186 ? -6.466   -133.762 30.301  1.00 156.28 ? 186 GLY H O   1 
ATOM   11148 N N   . LEU G 3 187 ? -6.079   -134.917 32.219  1.00 152.52 ? 187 LEU H N   1 
ATOM   11149 C CA  . LEU G 3 187 ? -7.373   -134.676 32.857  1.00 148.22 ? 187 LEU H CA  1 
ATOM   11150 C C   . LEU G 3 187 ? -7.238   -133.694 34.009  1.00 151.43 ? 187 LEU H C   1 
ATOM   11151 O O   . LEU G 3 187 ? -6.343   -133.839 34.842  1.00 151.79 ? 187 LEU H O   1 
ATOM   11152 C CB  . LEU G 3 187 ? -7.970   -135.994 33.374  1.00 147.00 ? 187 LEU H CB  1 
ATOM   11153 C CG  . LEU G 3 187 ? -8.488   -136.953 32.317  1.00 153.18 ? 187 LEU H CG  1 
ATOM   11154 C CD1 . LEU G 3 187 ? -7.903   -138.341 32.505  1.00 155.45 ? 187 LEU H CD1 1 
ATOM   11155 C CD2 . LEU G 3 187 ? -10.002  -136.987 32.310  1.00 152.45 ? 187 LEU H CD2 1 
ATOM   11156 N N   . TYR G 3 188 ? -8.135   -132.705 34.064  1.00 146.97 ? 188 TYR H N   1 
ATOM   11157 C CA  . TYR G 3 188 ? -8.165   -131.693 35.119  1.00 145.60 ? 188 TYR H CA  1 
ATOM   11158 C C   . TYR G 3 188 ? -8.631   -132.298 36.454  1.00 150.94 ? 188 TYR H C   1 
ATOM   11159 O O   . TYR G 3 188 ? -9.349   -133.302 36.458  1.00 150.19 ? 188 TYR H O   1 
ATOM   11160 C CB  . TYR G 3 188 ? -9.074   -130.518 34.715  1.00 144.99 ? 188 TYR H CB  1 
ATOM   11161 C CG  . TYR G 3 188 ? -8.680   -129.830 33.425  1.00 148.85 ? 188 TYR H CG  1 
ATOM   11162 C CD1 . TYR G 3 188 ? -7.842   -128.719 33.432  1.00 151.75 ? 188 TYR H CD1 1 
ATOM   11163 C CD2 . TYR G 3 188 ? -9.176   -130.265 32.200  1.00 151.09 ? 188 TYR H CD2 1 
ATOM   11164 C CE1 . TYR G 3 188 ? -7.492   -128.068 32.249  1.00 154.91 ? 188 TYR H CE1 1 
ATOM   11165 C CE2 . TYR G 3 188 ? -8.829   -129.626 31.011  1.00 154.49 ? 188 TYR H CE2 1 
ATOM   11166 C CZ  . TYR G 3 188 ? -7.994   -128.522 31.041  1.00 162.53 ? 188 TYR H CZ  1 
ATOM   11167 O OH  . TYR G 3 188 ? -7.649   -127.893 29.871  1.00 165.57 ? 188 TYR H OH  1 
ATOM   11168 N N   . SER G 3 189 ? -8.202   -131.690 37.584  1.00 148.84 ? 189 SER H N   1 
ATOM   11169 C CA  . SER G 3 189 ? -8.547   -132.110 38.949  1.00 147.95 ? 189 SER H CA  1 
ATOM   11170 C C   . SER G 3 189 ? -8.435   -130.952 39.955  1.00 150.87 ? 189 SER H C   1 
ATOM   11171 O O   . SER G 3 189 ? -7.407   -130.265 39.989  1.00 150.92 ? 189 SER H O   1 
ATOM   11172 C CB  . SER G 3 189 ? -7.678   -133.287 39.396  1.00 153.95 ? 189 SER H CB  1 
ATOM   11173 O OG  . SER G 3 189 ? -7.911   -133.639 40.751  1.00 162.90 ? 189 SER H OG  1 
ATOM   11174 N N   . LEU G 3 190 ? -9.488   -130.749 40.781  1.00 146.28 ? 190 LEU H N   1 
ATOM   11175 C CA  . LEU G 3 190 ? -9.488   -129.700 41.806  1.00 145.52 ? 190 LEU H CA  1 
ATOM   11176 C C   . LEU G 3 190 ? -9.830   -130.225 43.211  1.00 150.02 ? 190 LEU H C   1 
ATOM   11177 O O   . LEU G 3 190 ? -10.137  -131.407 43.394  1.00 149.65 ? 190 LEU H O   1 
ATOM   11178 C CB  . LEU G 3 190 ? -10.360  -128.476 41.428  1.00 144.63 ? 190 LEU H CB  1 
ATOM   11179 C CG  . LEU G 3 190 ? -11.873  -128.630 41.269  1.00 148.30 ? 190 LEU H CG  1 
ATOM   11180 C CD1 . LEU G 3 190 ? -12.604  -128.202 42.530  1.00 148.37 ? 190 LEU H CD1 1 
ATOM   11181 C CD2 . LEU G 3 190 ? -12.364  -127.749 40.153  1.00 150.29 ? 190 LEU H CD2 1 
ATOM   11182 N N   . SER G 3 191 ? -9.750   -129.319 44.195  1.00 147.27 ? 191 SER H N   1 
ATOM   11183 C CA  . SER G 3 191 ? -10.008  -129.553 45.612  1.00 147.92 ? 191 SER H CA  1 
ATOM   11184 C C   . SER G 3 191 ? -10.936  -128.470 46.156  1.00 153.51 ? 191 SER H C   1 
ATOM   11185 O O   . SER G 3 191 ? -10.931  -127.350 45.642  1.00 152.86 ? 191 SER H O   1 
ATOM   11186 C CB  . SER G 3 191 ? -8.692   -129.546 46.383  1.00 151.38 ? 191 SER H CB  1 
ATOM   11187 O OG  . SER G 3 191 ? -7.729   -128.692 45.784  1.00 156.67 ? 191 SER H OG  1 
ATOM   11188 N N   . SER G 3 192 ? -11.742  -128.804 47.179  1.00 152.25 ? 192 SER H N   1 
ATOM   11189 C CA  . SER G 3 192 ? -12.675  -127.866 47.814  1.00 153.81 ? 192 SER H CA  1 
ATOM   11190 C C   . SER G 3 192 ? -12.750  -128.130 49.324  1.00 161.48 ? 192 SER H C   1 
ATOM   11191 O O   . SER G 3 192 ? -13.119  -129.232 49.741  1.00 162.13 ? 192 SER H O   1 
ATOM   11192 C CB  . SER G 3 192 ? -14.056  -127.948 47.166  1.00 156.65 ? 192 SER H CB  1 
ATOM   11193 O OG  . SER G 3 192 ? -14.759  -126.723 47.288  1.00 164.32 ? 192 SER H OG  1 
ATOM   11194 N N   . VAL G 3 193 ? -12.354  -127.131 50.140  1.00 159.52 ? 193 VAL H N   1 
ATOM   11195 C CA  . VAL G 3 193 ? -12.321  -127.232 51.608  1.00 161.58 ? 193 VAL H CA  1 
ATOM   11196 C C   . VAL G 3 193 ? -13.191  -126.170 52.307  1.00 169.69 ? 193 VAL H C   1 
ATOM   11197 O O   . VAL G 3 193 ? -13.636  -125.213 51.668  1.00 169.02 ? 193 VAL H O   1 
ATOM   11198 C CB  . VAL G 3 193 ? -10.867  -127.220 52.166  1.00 164.55 ? 193 VAL H CB  1 
ATOM   11199 C CG1 . VAL G 3 193 ? -10.049  -128.399 51.648  1.00 162.77 ? 193 VAL H CG1 1 
ATOM   11200 C CG2 . VAL G 3 193 ? -10.165  -125.897 51.877  1.00 163.50 ? 193 VAL H CG2 1 
ATOM   11201 N N   . VAL G 3 194 ? -13.400  -126.338 53.631  1.00 177.90 ? 194 VAL H N   1 
ATOM   11202 C CA  . VAL G 3 194 ? -14.141  -125.406 54.485  1.00 178.31 ? 194 VAL H CA  1 
ATOM   11203 C C   . VAL G 3 194 ? -13.634  -125.502 55.939  1.00 182.93 ? 194 VAL H C   1 
ATOM   11204 O O   . VAL G 3 194 ? -13.641  -126.585 56.531  1.00 182.13 ? 194 VAL H O   1 
ATOM   11205 C CB  . VAL G 3 194 ? -15.696  -125.493 54.352  1.00 181.96 ? 194 VAL H CB  1 
ATOM   11206 C CG1 . VAL G 3 194 ? -16.235  -126.887 54.673  1.00 181.62 ? 194 VAL H CG1 1 
ATOM   11207 C CG2 . VAL G 3 194 ? -16.394  -124.420 55.185  1.00 181.90 ? 194 VAL H CG2 1 
ATOM   11208 N N   . THR G 3 195 ? -13.167  -124.360 56.486  1.00 180.44 ? 195 THR H N   1 
ATOM   11209 C CA  . THR G 3 195 ? -12.661  -124.247 57.856  1.00 180.44 ? 195 THR H CA  1 
ATOM   11210 C C   . THR G 3 195 ? -13.853  -124.312 58.822  1.00 184.85 ? 195 THR H C   1 
ATOM   11211 O O   . THR G 3 195 ? -14.450  -123.284 59.164  1.00 184.36 ? 195 THR H O   1 
ATOM   11212 C CB  . THR G 3 195 ? -11.763  -122.998 58.012  1.00 188.81 ? 195 THR H CB  1 
ATOM   11213 O OG1 . THR G 3 195 ? -10.828  -122.943 56.932  1.00 189.03 ? 195 THR H OG1 1 
ATOM   11214 C CG2 . THR G 3 195 ? -11.017  -122.970 59.346  1.00 186.75 ? 195 THR H CG2 1 
ATOM   11215 N N   . VAL G 3 196 ? -14.217  -125.545 59.210  1.00 181.98 ? 196 VAL H N   1 
ATOM   11216 C CA  . VAL G 3 196 ? -15.338  -125.844 60.109  1.00 182.11 ? 196 VAL H CA  1 
ATOM   11217 C C   . VAL G 3 196 ? -14.890  -125.971 61.575  1.00 185.28 ? 196 VAL H C   1 
ATOM   11218 O O   . VAL G 3 196 ? -13.770  -126.428 61.828  1.00 184.75 ? 196 VAL H O   1 
ATOM   11219 C CB  . VAL G 3 196 ? -16.175  -127.072 59.651  1.00 186.65 ? 196 VAL H CB  1 
ATOM   11220 C CG1 . VAL G 3 196 ? -17.079  -126.721 58.473  1.00 186.59 ? 196 VAL H CG1 1 
ATOM   11221 C CG2 . VAL G 3 196 ? -15.292  -128.278 59.332  1.00 186.41 ? 196 VAL H CG2 1 
ATOM   11222 N N   . PRO G 3 197 ? -15.738  -125.589 62.558  1.00 181.41 ? 197 PRO H N   1 
ATOM   11223 C CA  . PRO G 3 197 ? -15.318  -125.727 63.961  1.00 180.98 ? 197 PRO H CA  1 
ATOM   11224 C C   . PRO G 3 197 ? -15.412  -127.163 64.469  1.00 184.53 ? 197 PRO H C   1 
ATOM   11225 O O   . PRO G 3 197 ? -16.253  -127.940 64.010  1.00 184.67 ? 197 PRO H O   1 
ATOM   11226 C CB  . PRO G 3 197 ? -16.268  -124.794 64.710  1.00 182.87 ? 197 PRO H CB  1 
ATOM   11227 C CG  . PRO G 3 197 ? -17.502  -124.770 63.881  1.00 187.79 ? 197 PRO H CG  1 
ATOM   11228 C CD  . PRO G 3 197 ? -17.102  -125.025 62.454  1.00 183.17 ? 197 PRO H CD  1 
ATOM   11229 N N   . SER G 3 198 ? -14.554  -127.503 65.438  1.00 180.41 ? 198 SER H N   1 
ATOM   11230 C CA  . SER G 3 198 ? -14.518  -128.823 66.059  1.00 180.70 ? 198 SER H CA  1 
ATOM   11231 C C   . SER G 3 198 ? -15.715  -129.044 67.010  1.00 186.70 ? 198 SER H C   1 
ATOM   11232 O O   . SER G 3 198 ? -15.900  -130.156 67.507  1.00 187.19 ? 198 SER H O   1 
ATOM   11233 C CB  . SER G 3 198 ? -13.196  -129.027 66.792  1.00 182.93 ? 198 SER H CB  1 
ATOM   11234 O OG  . SER G 3 198 ? -12.083  -128.796 65.944  1.00 189.27 ? 198 SER H OG  1 
ATOM   11235 N N   . SER G 3 199 ? -16.530  -127.986 67.248  1.00 184.16 ? 199 SER H N   1 
ATOM   11236 C CA  . SER G 3 199 ? -17.709  -127.993 68.123  1.00 185.22 ? 199 SER H CA  1 
ATOM   11237 C C   . SER G 3 199 ? -18.884  -128.848 67.614  1.00 192.09 ? 199 SER H C   1 
ATOM   11238 O O   . SER G 3 199 ? -19.616  -129.398 68.438  1.00 193.04 ? 199 SER H O   1 
ATOM   11239 C CB  . SER G 3 199 ? -18.176  -126.570 68.419  1.00 187.34 ? 199 SER H CB  1 
ATOM   11240 O OG  . SER G 3 199 ? -17.243  -125.871 69.225  1.00 193.14 ? 199 SER H OG  1 
ATOM   11241 N N   . SER G 3 200 ? -19.088  -128.948 66.281  1.00 189.59 ? 200 SER H N   1 
ATOM   11242 C CA  . SER G 3 200 ? -20.181  -129.744 65.711  1.00 191.13 ? 200 SER H CA  1 
ATOM   11243 C C   . SER G 3 200 ? -19.737  -130.566 64.491  1.00 196.39 ? 200 SER H C   1 
ATOM   11244 O O   . SER G 3 200 ? -20.260  -130.391 63.385  1.00 195.62 ? 200 SER H O   1 
ATOM   11245 C CB  . SER G 3 200 ? -21.400  -128.873 65.410  1.00 194.42 ? 200 SER H CB  1 
ATOM   11246 O OG  . SER G 3 200 ? -22.530  -129.662 65.072  1.00 203.32 ? 200 SER H OG  1 
ATOM   11247 N N   . LEU G 3 201 ? -18.762  -131.470 64.713  1.00 194.47 ? 201 LEU H N   1 
ATOM   11248 C CA  . LEU G 3 201 ? -18.221  -132.374 63.691  1.00 194.84 ? 201 LEU H CA  1 
ATOM   11249 C C   . LEU G 3 201 ? -18.965  -133.710 63.686  1.00 202.17 ? 201 LEU H C   1 
ATOM   11250 O O   . LEU G 3 201 ? -19.154  -134.314 64.746  1.00 203.39 ? 201 LEU H O   1 
ATOM   11251 C CB  . LEU G 3 201 ? -16.690  -132.597 63.816  1.00 193.84 ? 201 LEU H CB  1 
ATOM   11252 C CG  . LEU G 3 201 ? -15.973  -132.356 65.161  1.00 198.18 ? 201 LEU H CG  1 
ATOM   11253 C CD1 . LEU G 3 201 ? -16.278  -133.451 66.186  1.00 199.67 ? 201 LEU H CD1 1 
ATOM   11254 C CD2 . LEU G 3 201 ? -14.478  -132.291 64.959  1.00 199.41 ? 201 LEU H CD2 1 
ATOM   11255 N N   . GLY G 3 202 ? -19.405  -134.136 62.501  1.00 199.64 ? 202 GLY H N   1 
ATOM   11256 C CA  . GLY G 3 202 ? -20.152  -135.378 62.315  1.00 201.64 ? 202 GLY H CA  1 
ATOM   11257 C C   . GLY G 3 202 ? -21.639  -135.233 62.570  1.00 208.00 ? 202 GLY H C   1 
ATOM   11258 O O   . GLY G 3 202 ? -22.452  -135.707 61.768  1.00 208.51 ? 202 GLY H O   1 
ATOM   11259 N N   . THR G 3 203 ? -21.998  -134.574 63.706  1.00 205.38 ? 203 THR H N   1 
ATOM   11260 C CA  . THR G 3 203 ? -23.368  -134.285 64.162  1.00 206.66 ? 203 THR H CA  1 
ATOM   11261 C C   . THR G 3 203 ? -24.107  -133.453 63.107  1.00 209.98 ? 203 THR H C   1 
ATOM   11262 O O   . THR G 3 203 ? -25.269  -133.734 62.806  1.00 210.87 ? 203 THR H O   1 
ATOM   11263 C CB  . THR G 3 203 ? -23.354  -133.594 65.540  1.00 212.48 ? 203 THR H CB  1 
ATOM   11264 O OG1 . THR G 3 203 ? -22.626  -132.367 65.455  1.00 208.43 ? 203 THR H OG1 1 
ATOM   11265 C CG2 . THR G 3 203 ? -22.772  -134.480 66.640  1.00 211.70 ? 203 THR H CG2 1 
ATOM   11266 N N   . GLN G 3 204 ? -23.408  -132.456 62.525  1.00 204.59 ? 204 GLN H N   1 
ATOM   11267 C CA  . GLN G 3 204 ? -23.926  -131.615 61.452  1.00 203.41 ? 204 GLN H CA  1 
ATOM   11268 C C   . GLN G 3 204 ? -23.654  -132.325 60.121  1.00 206.88 ? 204 GLN H C   1 
ATOM   11269 O O   . GLN G 3 204 ? -22.523  -132.760 59.875  1.00 205.79 ? 204 GLN H O   1 
ATOM   11270 C CB  . GLN G 3 204 ? -23.259  -130.228 61.471  1.00 202.92 ? 204 GLN H CB  1 
ATOM   11271 C CG  . GLN G 3 204 ? -24.198  -129.082 61.093  1.00 222.04 ? 204 GLN H CG  1 
ATOM   11272 C CD  . GLN G 3 204 ? -24.571  -129.061 59.627  1.00 243.80 ? 204 GLN H CD  1 
ATOM   11273 O OE1 . GLN G 3 204 ? -23.784  -128.658 58.762  1.00 238.82 ? 204 GLN H OE1 1 
ATOM   11274 N NE2 . GLN G 3 204 ? -25.791  -129.482 59.317  1.00 237.07 ? 204 GLN H NE2 1 
ATOM   11275 N N   . THR G 3 205 ? -24.696  -132.467 59.283  1.00 203.58 ? 205 THR H N   1 
ATOM   11276 C CA  . THR G 3 205 ? -24.604  -133.122 57.976  1.00 202.76 ? 205 THR H CA  1 
ATOM   11277 C C   . THR G 3 205 ? -23.920  -132.176 56.972  1.00 203.77 ? 205 THR H C   1 
ATOM   11278 O O   . THR G 3 205 ? -24.515  -131.169 56.578  1.00 202.79 ? 205 THR H O   1 
ATOM   11279 C CB  . THR G 3 205 ? -25.998  -133.616 57.519  1.00 212.26 ? 205 THR H CB  1 
ATOM   11280 O OG1 . THR G 3 205 ? -26.656  -134.272 58.607  1.00 214.31 ? 205 THR H OG1 1 
ATOM   11281 C CG2 . THR G 3 205 ? -25.930  -134.550 56.310  1.00 210.55 ? 205 THR H CG2 1 
ATOM   11282 N N   . TYR G 3 206 ? -22.661  -132.488 56.592  1.00 198.67 ? 206 TYR H N   1 
ATOM   11283 C CA  . TYR G 3 206 ? -21.882  -131.691 55.638  1.00 196.42 ? 206 TYR H CA  1 
ATOM   11284 C C   . TYR G 3 206 ? -21.879  -132.338 54.249  1.00 197.76 ? 206 TYR H C   1 
ATOM   11285 O O   . TYR G 3 206 ? -21.122  -133.281 53.998  1.00 197.18 ? 206 TYR H O   1 
ATOM   11286 C CB  . TYR G 3 206 ? -20.453  -131.418 56.152  1.00 197.29 ? 206 TYR H CB  1 
ATOM   11287 C CG  . TYR G 3 206 ? -20.390  -130.474 57.335  1.00 199.79 ? 206 TYR H CG  1 
ATOM   11288 C CD1 . TYR G 3 206 ? -20.566  -129.102 57.170  1.00 201.11 ? 206 TYR H CD1 1 
ATOM   11289 C CD2 . TYR G 3 206 ? -20.107  -130.945 58.613  1.00 201.63 ? 206 TYR H CD2 1 
ATOM   11290 C CE1 . TYR G 3 206 ? -20.499  -128.227 58.254  1.00 201.95 ? 206 TYR H CE1 1 
ATOM   11291 C CE2 . TYR G 3 206 ? -20.034  -130.080 59.705  1.00 202.70 ? 206 TYR H CE2 1 
ATOM   11292 C CZ  . TYR G 3 206 ? -20.230  -128.720 59.521  1.00 209.72 ? 206 TYR H CZ  1 
ATOM   11293 O OH  . TYR G 3 206 ? -20.155  -127.864 60.596  1.00 211.10 ? 206 TYR H OH  1 
ATOM   11294 N N   . ILE G 3 207 ? -22.756  -131.832 53.360  1.00 192.41 ? 207 ILE H N   1 
ATOM   11295 C CA  . ILE G 3 207 ? -22.951  -132.316 51.987  1.00 190.90 ? 207 ILE H CA  1 
ATOM   11296 C C   . ILE G 3 207 ? -22.098  -131.494 51.007  1.00 191.10 ? 207 ILE H C   1 
ATOM   11297 O O   . ILE G 3 207 ? -22.105  -130.265 51.071  1.00 190.13 ? 207 ILE H O   1 
ATOM   11298 C CB  . ILE G 3 207 ? -24.466  -132.312 51.604  1.00 194.59 ? 207 ILE H CB  1 
ATOM   11299 C CG1 . ILE G 3 207 ? -25.356  -132.881 52.743  1.00 196.76 ? 207 ILE H CG1 1 
ATOM   11300 C CG2 . ILE G 3 207 ? -24.710  -133.061 50.289  1.00 195.09 ? 207 ILE H CG2 1 
ATOM   11301 C CD1 . ILE G 3 207 ? -26.667  -132.129 52.976  1.00 203.79 ? 207 ILE H CD1 1 
ATOM   11302 N N   . CYS G 3 208 ? -21.363  -132.176 50.112  1.00 185.38 ? 208 CYS H N   1 
ATOM   11303 C CA  . CYS G 3 208 ? -20.500  -131.539 49.117  1.00 183.38 ? 208 CYS H CA  1 
ATOM   11304 C C   . CYS G 3 208 ? -21.059  -131.779 47.705  1.00 186.14 ? 208 CYS H C   1 
ATOM   11305 O O   . CYS G 3 208 ? -20.829  -132.839 47.115  1.00 185.83 ? 208 CYS H O   1 
ATOM   11306 C CB  . CYS G 3 208 ? -19.061  -132.034 49.264  1.00 183.09 ? 208 CYS H CB  1 
ATOM   11307 S SG  . CYS G 3 208 ? -17.889  -131.319 48.081  1.00 185.83 ? 208 CYS H SG  1 
ATOM   11308 N N   . ASN G 3 209 ? -21.825  -130.795 47.184  1.00 181.30 ? 209 ASN H N   1 
ATOM   11309 C CA  . ASN G 3 209 ? -22.473  -130.853 45.866  1.00 179.77 ? 209 ASN H CA  1 
ATOM   11310 C C   . ASN G 3 209 ? -21.545  -130.386 44.747  1.00 180.47 ? 209 ASN H C   1 
ATOM   11311 O O   . ASN G 3 209 ? -21.185  -129.209 44.683  1.00 179.76 ? 209 ASN H O   1 
ATOM   11312 C CB  . ASN G 3 209 ? -23.787  -130.055 45.856  1.00 181.33 ? 209 ASN H CB  1 
ATOM   11313 C CG  . ASN G 3 209 ? -24.698  -130.339 47.024  1.00 209.15 ? 209 ASN H CG  1 
ATOM   11314 O OD1 . ASN G 3 209 ? -24.360  -130.084 48.186  1.00 205.63 ? 209 ASN H OD1 1 
ATOM   11315 N ND2 . ASN G 3 209 ? -25.889  -130.840 46.738  1.00 202.00 ? 209 ASN H ND2 1 
ATOM   11316 N N   . VAL G 3 210 ? -21.148  -131.323 43.875  1.00 175.06 ? 210 VAL H N   1 
ATOM   11317 C CA  . VAL G 3 210 ? -20.263  -131.070 42.734  1.00 173.59 ? 210 VAL H CA  1 
ATOM   11318 C C   . VAL G 3 210 ? -21.015  -131.448 41.448  1.00 174.61 ? 210 VAL H C   1 
ATOM   11319 O O   . VAL G 3 210 ? -21.651  -132.504 41.403  1.00 174.04 ? 210 VAL H O   1 
ATOM   11320 C CB  . VAL G 3 210 ? -18.905  -131.829 42.859  1.00 177.78 ? 210 VAL H CB  1 
ATOM   11321 C CG1 . VAL G 3 210 ? -17.942  -131.433 41.743  1.00 177.23 ? 210 VAL H CG1 1 
ATOM   11322 C CG2 . VAL G 3 210 ? -18.253  -131.608 44.225  1.00 178.35 ? 210 VAL H CG2 1 
ATOM   11323 N N   . ASN G 3 211 ? -20.952  -130.587 40.415  1.00 169.22 ? 211 ASN H N   1 
ATOM   11324 C CA  . ASN G 3 211 ? -21.614  -130.841 39.136  1.00 167.35 ? 211 ASN H CA  1 
ATOM   11325 C C   . ASN G 3 211 ? -20.754  -130.481 37.928  1.00 168.82 ? 211 ASN H C   1 
ATOM   11326 O O   . ASN G 3 211 ? -20.089  -129.442 37.922  1.00 168.88 ? 211 ASN H O   1 
ATOM   11327 C CB  . ASN G 3 211 ? -22.986  -130.158 39.068  1.00 168.10 ? 211 ASN H CB  1 
ATOM   11328 C CG  . ASN G 3 211 ? -22.953  -128.649 39.069  1.00 190.64 ? 211 ASN H CG  1 
ATOM   11329 O OD1 . ASN G 3 211 ? -22.893  -128.004 40.120  1.00 186.14 ? 211 ASN H OD1 1 
ATOM   11330 N ND2 . ASN G 3 211 ? -23.019  -128.051 37.887  1.00 180.97 ? 211 ASN H ND2 1 
ATOM   11331 N N   . HIS G 3 212 ? -20.773  -131.352 36.909  1.00 163.20 ? 212 HIS H N   1 
ATOM   11332 C CA  . HIS G 3 212 ? -20.059  -131.167 35.647  1.00 161.86 ? 212 HIS H CA  1 
ATOM   11333 C C   . HIS G 3 212 ? -21.120  -130.757 34.629  1.00 164.67 ? 212 HIS H C   1 
ATOM   11334 O O   . HIS G 3 212 ? -22.046  -131.527 34.371  1.00 163.45 ? 212 HIS H O   1 
ATOM   11335 C CB  . HIS G 3 212 ? -19.367  -132.478 35.231  1.00 161.68 ? 212 HIS H CB  1 
ATOM   11336 C CG  . HIS G 3 212 ? -18.286  -132.317 34.209  1.00 164.44 ? 212 HIS H CG  1 
ATOM   11337 N ND1 . HIS G 3 212 ? -18.581  -132.160 32.871  1.00 165.23 ? 212 HIS H ND1 1 
ATOM   11338 C CD2 . HIS G 3 212 ? -16.941  -132.362 34.358  1.00 166.34 ? 212 HIS H CD2 1 
ATOM   11339 C CE1 . HIS G 3 212 ? -17.413  -132.080 32.254  1.00 164.63 ? 212 HIS H CE1 1 
ATOM   11340 N NE2 . HIS G 3 212 ? -16.399  -132.191 33.110  1.00 165.70 ? 212 HIS H NE2 1 
ATOM   11341 N N   . LYS G 3 213 ? -21.040  -129.519 34.117  1.00 161.49 ? 213 LYS H N   1 
ATOM   11342 C CA  . LYS G 3 213 ? -22.028  -129.004 33.165  1.00 160.80 ? 213 LYS H CA  1 
ATOM   11343 C C   . LYS G 3 213 ? -21.956  -129.703 31.785  1.00 163.96 ? 213 LYS H C   1 
ATOM   11344 O O   . LYS G 3 213 ? -23.001  -130.208 31.366  1.00 162.06 ? 213 LYS H O   1 
ATOM   11345 C CB  . LYS G 3 213 ? -21.978  -127.467 33.044  1.00 164.32 ? 213 LYS H CB  1 
ATOM   11346 C CG  . LYS G 3 213 ? -22.439  -126.720 34.304  1.00 177.91 ? 213 LYS H CG  1 
ATOM   11347 C CD  . LYS G 3 213 ? -23.919  -126.324 34.263  1.00 181.47 ? 213 LYS H CD  1 
ATOM   11348 C CE  . LYS G 3 213 ? -24.326  -125.546 35.489  1.00 184.20 ? 213 LYS H CE  1 
ATOM   11349 N NZ  . LYS G 3 213 ? -25.725  -125.063 35.390  1.00 188.52 ? 213 LYS H NZ  1 
ATOM   11350 N N   . PRO G 3 214 ? -20.784  -129.821 31.088  1.00 161.72 ? 214 PRO H N   1 
ATOM   11351 C CA  . PRO G 3 214 ? -20.779  -130.503 29.776  1.00 160.63 ? 214 PRO H CA  1 
ATOM   11352 C C   . PRO G 3 214 ? -21.179  -131.986 29.799  1.00 164.16 ? 214 PRO H C   1 
ATOM   11353 O O   . PRO G 3 214 ? -22.195  -132.328 29.192  1.00 162.89 ? 214 PRO H O   1 
ATOM   11354 C CB  . PRO G 3 214 ? -19.347  -130.292 29.259  1.00 162.90 ? 214 PRO H CB  1 
ATOM   11355 C CG  . PRO G 3 214 ? -18.824  -129.141 30.035  1.00 168.95 ? 214 PRO H CG  1 
ATOM   11356 C CD  . PRO G 3 214 ? -19.443  -129.276 31.389  1.00 164.66 ? 214 PRO H CD  1 
ATOM   11357 N N   . SER G 3 215 ? -20.423  -132.853 30.512  1.00 161.34 ? 215 SER H N   1 
ATOM   11358 C CA  . SER G 3 215 ? -20.703  -134.295 30.584  1.00 160.68 ? 215 SER H CA  1 
ATOM   11359 C C   . SER G 3 215 ? -21.986  -134.658 31.358  1.00 166.71 ? 215 SER H C   1 
ATOM   11360 O O   . SER G 3 215 ? -22.398  -135.821 31.337  1.00 165.47 ? 215 SER H O   1 
ATOM   11361 C CB  . SER G 3 215 ? -19.501  -135.054 31.141  1.00 163.61 ? 215 SER H CB  1 
ATOM   11362 O OG  . SER G 3 215 ? -19.317  -134.838 32.529  1.00 171.26 ? 215 SER H OG  1 
ATOM   11363 N N   . ASN G 3 216 ? -22.610  -133.661 32.034  1.00 166.37 ? 216 ASN H N   1 
ATOM   11364 C CA  . ASN G 3 216 ? -23.829  -133.758 32.857  1.00 167.88 ? 216 ASN H CA  1 
ATOM   11365 C C   . ASN G 3 216 ? -23.670  -134.709 34.070  1.00 175.13 ? 216 ASN H C   1 
ATOM   11366 O O   . ASN G 3 216 ? -24.655  -135.008 34.753  1.00 175.37 ? 216 ASN H O   1 
ATOM   11367 C CB  . ASN G 3 216 ? -25.079  -134.088 32.017  1.00 167.78 ? 216 ASN H CB  1 
ATOM   11368 C CG  . ASN G 3 216 ? -25.845  -132.866 31.559  1.00 186.15 ? 216 ASN H CG  1 
ATOM   11369 O OD1 . ASN G 3 216 ? -26.199  -131.983 32.352  1.00 180.02 ? 216 ASN H OD1 1 
ATOM   11370 N ND2 . ASN G 3 216 ? -26.147  -132.805 30.270  1.00 176.22 ? 216 ASN H ND2 1 
ATOM   11371 N N   . THR G 3 217 ? -22.419  -135.120 34.369  1.00 173.72 ? 217 THR H N   1 
ATOM   11372 C CA  . THR G 3 217 ? -22.075  -135.996 35.490  1.00 175.37 ? 217 THR H CA  1 
ATOM   11373 C C   . THR G 3 217 ? -22.144  -135.178 36.789  1.00 182.08 ? 217 THR H C   1 
ATOM   11374 O O   . THR G 3 217 ? -21.167  -134.530 37.172  1.00 182.43 ? 217 THR H O   1 
ATOM   11375 C CB  . THR G 3 217 ? -20.707  -136.680 35.241  1.00 184.22 ? 217 THR H CB  1 
ATOM   11376 O OG1 . THR G 3 217 ? -20.663  -137.193 33.908  1.00 183.40 ? 217 THR H OG1 1 
ATOM   11377 C CG2 . THR G 3 217 ? -20.412  -137.801 36.239  1.00 183.20 ? 217 THR H CG2 1 
ATOM   11378 N N   . LYS G 3 218 ? -23.318  -135.187 37.442  1.00 175.28 ? 218 LYS H N   1 
ATOM   11379 C CA  . LYS G 3 218 ? -23.546  -134.447 38.685  1.00 174.97 ? 218 LYS H CA  1 
ATOM   11380 C C   . LYS G 3 218 ? -23.474  -135.391 39.893  1.00 178.98 ? 218 LYS H C   1 
ATOM   11381 O O   . LYS G 3 218 ? -24.471  -136.012 40.272  1.00 178.22 ? 218 LYS H O   1 
ATOM   11382 C CB  . LYS G 3 218 ? -24.863  -133.643 38.625  1.00 177.64 ? 218 LYS H CB  1 
ATOM   11383 C CG  . LYS G 3 218 ? -24.976  -132.743 37.394  1.00 190.25 ? 218 LYS H CG  1 
ATOM   11384 C CD  . LYS G 3 218 ? -26.114  -131.743 37.512  1.00 199.65 ? 218 LYS H CD  1 
ATOM   11385 C CE  . LYS G 3 218 ? -26.197  -130.838 36.308  1.00 210.98 ? 218 LYS H CE  1 
ATOM   11386 N NZ  . LYS G 3 218 ? -25.115  -129.819 36.301  1.00 220.40 ? 218 LYS H NZ  1 
ATOM   11387 N N   . VAL G 3 219 ? -22.262  -135.524 40.463  1.00 176.36 ? 219 VAL H N   1 
ATOM   11388 C CA  . VAL G 3 219 ? -21.966  -136.406 41.600  1.00 176.64 ? 219 VAL H CA  1 
ATOM   11389 C C   . VAL G 3 219 ? -21.890  -135.603 42.922  1.00 180.46 ? 219 VAL H C   1 
ATOM   11390 O O   . VAL G 3 219 ? -20.943  -134.839 43.125  1.00 180.20 ? 219 VAL H O   1 
ATOM   11391 C CB  . VAL G 3 219 ? -20.699  -137.292 41.346  1.00 181.25 ? 219 VAL H CB  1 
ATOM   11392 C CG1 . VAL G 3 219 ? -20.406  -138.215 42.528  1.00 181.16 ? 219 VAL H CG1 1 
ATOM   11393 C CG2 . VAL G 3 219 ? -20.830  -138.107 40.057  1.00 181.46 ? 219 VAL H CG2 1 
ATOM   11394 N N   . ASP G 3 220 ? -22.892  -135.777 43.813  1.00 176.52 ? 220 ASP H N   1 
ATOM   11395 C CA  . ASP G 3 220 ? -22.963  -135.108 45.121  1.00 176.10 ? 220 ASP H CA  1 
ATOM   11396 C C   . ASP G 3 220 ? -22.685  -136.113 46.252  1.00 179.56 ? 220 ASP H C   1 
ATOM   11397 O O   . ASP G 3 220 ? -23.503  -137.001 46.507  1.00 178.94 ? 220 ASP H O   1 
ATOM   11398 C CB  . ASP G 3 220 ? -24.326  -134.405 45.309  1.00 178.10 ? 220 ASP H CB  1 
ATOM   11399 C CG  . ASP G 3 220 ? -24.644  -133.301 44.308  1.00 187.37 ? 220 ASP H CG  1 
ATOM   11400 O OD1 . ASP G 3 220 ? -25.725  -132.690 44.427  1.00 188.78 ? 220 ASP H OD1 1 
ATOM   11401 O OD2 . ASP G 3 220 ? -23.801  -133.034 43.421  1.00 191.41 ? 220 ASP H OD2 1 
ATOM   11402 N N   . LYS G 3 221 ? -21.512  -135.985 46.902  1.00 176.08 ? 221 LYS H N   1 
ATOM   11403 C CA  . LYS G 3 221 ? -21.049  -136.877 47.965  1.00 176.11 ? 221 LYS H CA  1 
ATOM   11404 C C   . LYS G 3 221 ? -20.904  -136.173 49.307  1.00 181.67 ? 221 LYS H C   1 
ATOM   11405 O O   . LYS G 3 221 ? -20.379  -135.061 49.367  1.00 180.87 ? 221 LYS H O   1 
ATOM   11406 C CB  . LYS G 3 221 ? -19.725  -137.552 47.564  1.00 178.18 ? 221 LYS H CB  1 
ATOM   11407 C CG  . LYS G 3 221 ? -19.917  -138.766 46.659  1.00 187.00 ? 221 LYS H CG  1 
ATOM   11408 C CD  . LYS G 3 221 ? -18.621  -139.530 46.413  1.00 193.34 ? 221 LYS H CD  1 
ATOM   11409 C CE  . LYS G 3 221 ? -18.339  -140.579 47.462  1.00 198.59 ? 221 LYS H CE  1 
ATOM   11410 N NZ  . LYS G 3 221 ? -17.064  -141.289 47.191  1.00 205.10 ? 221 LYS H NZ  1 
ATOM   11411 N N   . ARG G 3 222 ? -21.368  -136.833 50.383  1.00 179.99 ? 222 ARG H N   1 
ATOM   11412 C CA  . ARG G 3 222 ? -21.298  -136.333 51.758  1.00 180.82 ? 222 ARG H CA  1 
ATOM   11413 C C   . ARG G 3 222 ? -19.911  -136.623 52.345  1.00 185.32 ? 222 ARG H C   1 
ATOM   11414 O O   . ARG G 3 222 ? -19.369  -137.712 52.137  1.00 184.55 ? 222 ARG H O   1 
ATOM   11415 C CB  . ARG G 3 222 ? -22.393  -136.991 52.623  1.00 182.10 ? 222 ARG H CB  1 
ATOM   11416 C CG  . ARG G 3 222 ? -22.677  -136.268 53.940  1.00 196.44 ? 222 ARG H CG  1 
ATOM   11417 C CD  . ARG G 3 222 ? -23.472  -137.121 54.915  1.00 209.83 ? 222 ARG H CD  1 
ATOM   11418 N NE  . ARG G 3 222 ? -22.615  -138.028 55.686  1.00 222.67 ? 222 ARG H NE  1 
ATOM   11419 C CZ  . ARG G 3 222 ? -22.155  -137.778 56.910  1.00 239.84 ? 222 ARG H CZ  1 
ATOM   11420 N NH1 . ARG G 3 222 ? -22.465  -136.643 57.525  1.00 229.14 ? 222 ARG H NH1 1 
ATOM   11421 N NH2 . ARG G 3 222 ? -21.386  -138.663 57.530  1.00 226.48 ? 222 ARG H NH2 1 
ATOM   11422 N N   . VAL G 3 223 ? -19.344  -135.647 53.077  1.00 182.96 ? 223 VAL H N   1 
ATOM   11423 C CA  . VAL G 3 223 ? -18.034  -135.777 53.726  1.00 183.32 ? 223 VAL H CA  1 
ATOM   11424 C C   . VAL G 3 223 ? -18.255  -136.404 55.115  1.00 189.82 ? 223 VAL H C   1 
ATOM   11425 O O   . VAL G 3 223 ? -18.958  -135.822 55.949  1.00 190.22 ? 223 VAL H O   1 
ATOM   11426 C CB  . VAL G 3 223 ? -17.250  -134.433 53.785  1.00 186.48 ? 223 VAL H CB  1 
ATOM   11427 C CG1 . VAL G 3 223 ? -15.874  -134.617 54.424  1.00 186.35 ? 223 VAL H CG1 1 
ATOM   11428 C CG2 . VAL G 3 223 ? -17.109  -133.813 52.398  1.00 185.45 ? 223 VAL H CG2 1 
ATOM   11429 N N   . GLU G 3 224 ? -17.679  -137.606 55.340  1.00 187.30 ? 224 GLU H N   1 
ATOM   11430 C CA  . GLU G 3 224 ? -17.810  -138.360 56.594  1.00 187.72 ? 224 GLU H CA  1 
ATOM   11431 C C   . GLU G 3 224 ? -16.512  -138.356 57.446  1.00 191.09 ? 224 GLU H C   1 
ATOM   11432 O O   . GLU G 3 224 ? -15.431  -138.618 56.909  1.00 190.46 ? 224 GLU H O   1 
ATOM   11433 C CB  . GLU G 3 224 ? -18.339  -139.801 56.348  1.00 189.04 ? 224 GLU H CB  1 
ATOM   11434 C CG  . GLU G 3 224 ? -17.500  -140.696 55.439  1.00 199.87 ? 224 GLU H CG  1 
ATOM   11435 C CD  . GLU G 3 224 ? -17.782  -140.598 53.952  1.00 217.16 ? 224 GLU H CD  1 
ATOM   11436 O OE1 . GLU G 3 224 ? -18.408  -141.536 53.407  1.00 201.74 ? 224 GLU H OE1 1 
ATOM   11437 O OE2 . GLU G 3 224 ? -17.349  -139.605 53.324  1.00 214.30 ? 224 GLU H OE2 1 
ATOM   11438 N N   . PRO G 3 225 ? -16.592  -138.055 58.769  1.00 187.55 ? 225 PRO H N   1 
ATOM   11439 C CA  . PRO G 3 225 ? -15.372  -138.048 59.593  1.00 189.82 ? 225 PRO H CA  1 
ATOM   11440 C C   . PRO G 3 225 ? -15.005  -139.437 60.101  1.00 201.48 ? 225 PRO H C   1 
ATOM   11441 O O   . PRO G 3 225 ? -14.400  -140.218 59.374  1.00 159.80 ? 225 PRO H O   1 
ATOM   11442 C CB  . PRO G 3 225 ? -15.719  -137.097 60.747  1.00 191.77 ? 225 PRO H CB  1 
ATOM   11443 C CG  . PRO G 3 225 ? -17.194  -136.797 60.617  1.00 195.57 ? 225 PRO H CG  1 
ATOM   11444 C CD  . PRO G 3 225 ? -17.772  -137.702 59.579  1.00 190.04 ? 225 PRO H CD  1 
ATOM   11445 N N   . GLU H 4 1   ? 11.224   -108.229 19.207  1.00 150.86 ? 1   GLU L N   1 
ATOM   11446 C CA  . GLU H 4 1   ? 10.239   -107.790 20.195  1.00 144.82 ? 1   GLU L CA  1 
ATOM   11447 C C   . GLU H 4 1   ? 10.827   -106.751 21.136  1.00 145.39 ? 1   GLU L C   1 
ATOM   11448 O O   . GLU H 4 1   ? 11.924   -106.946 21.657  1.00 146.51 ? 1   GLU L O   1 
ATOM   11449 C CB  . GLU H 4 1   ? 9.668    -108.983 20.995  1.00 144.69 ? 1   GLU L CB  1 
ATOM   11450 C CG  . GLU H 4 1   ? 8.785    -109.902 20.161  1.00 161.42 ? 1   GLU L CG  1 
ATOM   11451 C CD  . GLU H 4 1   ? 8.149    -111.076 20.878  1.00 192.66 ? 1   GLU L CD  1 
ATOM   11452 O OE1 . GLU H 4 1   ? 7.268    -110.850 21.741  1.00 190.82 ? 1   GLU L OE1 1 
ATOM   11453 O OE2 . GLU H 4 1   ? 8.485    -112.229 20.522  1.00 191.15 ? 1   GLU L OE2 1 
ATOM   11454 N N   . ILE H 4 2   ? 10.092   -105.651 21.359  1.00 138.17 ? 2   ILE L N   1 
ATOM   11455 C CA  . ILE H 4 2   ? 10.489   -104.563 22.257  1.00 136.12 ? 2   ILE L CA  1 
ATOM   11456 C C   . ILE H 4 2   ? 10.044   -105.001 23.651  1.00 137.31 ? 2   ILE L C   1 
ATOM   11457 O O   . ILE H 4 2   ? 8.921    -104.717 24.077  1.00 133.28 ? 2   ILE L O   1 
ATOM   11458 C CB  . ILE H 4 2   ? 9.899    -103.187 21.814  1.00 137.80 ? 2   ILE L CB  1 
ATOM   11459 C CG1 . ILE H 4 2   ? 10.207   -102.870 20.329  1.00 142.30 ? 2   ILE L CG1 1 
ATOM   11460 C CG2 . ILE H 4 2   ? 10.378   -102.057 22.720  1.00 137.22 ? 2   ILE L CG2 1 
ATOM   11461 C CD1 . ILE H 4 2   ? 9.179    -103.392 19.325  1.00 145.69 ? 2   ILE L CD1 1 
ATOM   11462 N N   . VAL H 4 3   ? 10.918   -105.766 24.322  1.00 136.18 ? 3   VAL L N   1 
ATOM   11463 C CA  . VAL H 4 3   ? 10.681   -106.370 25.634  1.00 133.93 ? 3   VAL L CA  1 
ATOM   11464 C C   . VAL H 4 3   ? 10.352   -105.331 26.708  1.00 134.20 ? 3   VAL L C   1 
ATOM   11465 O O   . VAL H 4 3   ? 11.201   -104.505 27.067  1.00 134.93 ? 3   VAL L O   1 
ATOM   11466 C CB  . VAL H 4 3   ? 11.840   -107.317 26.058  1.00 141.89 ? 3   VAL L CB  1 
ATOM   11467 C CG1 . VAL H 4 3   ? 11.657   -107.833 27.486  1.00 139.80 ? 3   VAL L CG1 1 
ATOM   11468 C CG2 . VAL H 4 3   ? 11.978   -108.485 25.084  1.00 145.59 ? 3   VAL L CG2 1 
ATOM   11469 N N   . LEU H 4 4   ? 9.100    -105.386 27.204  1.00 126.65 ? 4   LEU L N   1 
ATOM   11470 C CA  . LEU H 4 4   ? 8.616    -104.535 28.283  1.00 123.26 ? 4   LEU L CA  1 
ATOM   11471 C C   . LEU H 4 4   ? 8.786    -105.322 29.575  1.00 126.50 ? 4   LEU L C   1 
ATOM   11472 O O   . LEU H 4 4   ? 8.269    -106.440 29.693  1.00 126.45 ? 4   LEU L O   1 
ATOM   11473 C CB  . LEU H 4 4   ? 7.142    -104.132 28.088  1.00 120.19 ? 4   LEU L CB  1 
ATOM   11474 C CG  . LEU H 4 4   ? 6.827    -103.144 26.970  1.00 125.57 ? 4   LEU L CG  1 
ATOM   11475 C CD1 . LEU H 4 4   ? 5.351    -102.992 26.807  1.00 123.19 ? 4   LEU L CD1 1 
ATOM   11476 C CD2 . LEU H 4 4   ? 7.407    -101.778 27.249  1.00 129.47 ? 4   LEU L CD2 1 
ATOM   11477 N N   . THR H 4 5   ? 9.559    -104.765 30.517  1.00 121.75 ? 5   THR L N   1 
ATOM   11478 C CA  . THR H 4 5   ? 9.821    -105.406 31.798  1.00 120.17 ? 5   THR L CA  1 
ATOM   11479 C C   . THR H 4 5   ? 9.297    -104.524 32.931  1.00 119.30 ? 5   THR L C   1 
ATOM   11480 O O   . THR H 4 5   ? 9.884    -103.485 33.248  1.00 118.63 ? 5   THR L O   1 
ATOM   11481 C CB  . THR H 4 5   ? 11.290   -105.835 31.916  1.00 131.15 ? 5   THR L CB  1 
ATOM   11482 O OG1 . THR H 4 5   ? 12.120   -104.892 31.231  1.00 133.07 ? 5   THR L OG1 1 
ATOM   11483 C CG2 . THR H 4 5   ? 11.528   -107.230 31.348  1.00 131.72 ? 5   THR L CG2 1 
ATOM   11484 N N   . GLN H 4 6   ? 8.152    -104.934 33.505  1.00 113.46 ? 6   GLN L N   1 
ATOM   11485 C CA  . GLN H 4 6   ? 7.464    -104.227 34.585  1.00 111.64 ? 6   GLN L CA  1 
ATOM   11486 C C   . GLN H 4 6   ? 8.125    -104.374 35.951  1.00 117.10 ? 6   GLN L C   1 
ATOM   11487 O O   . GLN H 4 6   ? 8.595    -105.458 36.313  1.00 117.80 ? 6   GLN L O   1 
ATOM   11488 C CB  . GLN H 4 6   ? 5.986    -104.624 34.654  1.00 110.73 ? 6   GLN L CB  1 
ATOM   11489 C CG  . GLN H 4 6   ? 5.127    -103.751 33.770  1.00 121.44 ? 6   GLN L CG  1 
ATOM   11490 C CD  . GLN H 4 6   ? 3.670    -104.106 33.829  1.00 137.81 ? 6   GLN L CD  1 
ATOM   11491 O OE1 . GLN H 4 6   ? 3.157    -104.871 33.007  1.00 130.94 ? 6   GLN L OE1 1 
ATOM   11492 N NE2 . GLN H 4 6   ? 2.961    -103.520 34.780  1.00 130.72 ? 6   GLN L NE2 1 
ATOM   11493 N N   . SER H 4 7   ? 8.137    -103.264 36.710  1.00 113.63 ? 7   SER L N   1 
ATOM   11494 C CA  . SER H 4 7   ? 8.695    -103.181 38.057  1.00 114.08 ? 7   SER L CA  1 
ATOM   11495 C C   . SER H 4 7   ? 7.692    -102.479 39.000  1.00 116.45 ? 7   SER L C   1 
ATOM   11496 O O   . SER H 4 7   ? 7.165    -101.423 38.642  1.00 115.79 ? 7   SER L O   1 
ATOM   11497 C CB  . SER H 4 7   ? 10.035   -102.451 38.041  1.00 119.51 ? 7   SER L CB  1 
ATOM   11498 O OG  . SER H 4 7   ? 10.814   -102.775 39.181  1.00 129.38 ? 7   SER L OG  1 
ATOM   11499 N N   . PRO H 4 8   ? 7.370    -103.056 40.181  1.00 112.71 ? 8   PRO L N   1 
ATOM   11500 C CA  . PRO H 4 8   ? 7.892    -104.308 40.752  1.00 114.06 ? 8   PRO L CA  1 
ATOM   11501 C C   . PRO H 4 8   ? 7.143    -105.534 40.236  1.00 118.52 ? 8   PRO L C   1 
ATOM   11502 O O   . PRO H 4 8   ? 6.375    -105.427 39.278  1.00 116.82 ? 8   PRO L O   1 
ATOM   11503 C CB  . PRO H 4 8   ? 7.678    -104.094 42.253  1.00 116.19 ? 8   PRO L CB  1 
ATOM   11504 C CG  . PRO H 4 8   ? 6.400    -103.311 42.317  1.00 118.95 ? 8   PRO L CG  1 
ATOM   11505 C CD  . PRO H 4 8   ? 6.400    -102.418 41.095  1.00 113.51 ? 8   PRO L CD  1 
ATOM   11506 N N   . GLY H 4 9   ? 7.383    -106.680 40.866  1.00 117.45 ? 9   GLY L N   1 
ATOM   11507 C CA  . GLY H 4 9   ? 6.698    -107.920 40.529  1.00 118.06 ? 9   GLY L CA  1 
ATOM   11508 C C   . GLY H 4 9   ? 5.287    -107.898 41.083  1.00 120.27 ? 9   GLY L C   1 
ATOM   11509 O O   . GLY H 4 9   ? 4.330    -108.278 40.400  1.00 119.34 ? 9   GLY L O   1 
ATOM   11510 N N   . THR H 4 10  ? 5.162    -107.422 42.331  1.00 116.10 ? 10  THR L N   1 
ATOM   11511 C CA  . THR H 4 10  ? 3.912    -107.286 43.076  1.00 115.17 ? 10  THR L CA  1 
ATOM   11512 C C   . THR H 4 10  ? 3.995    -106.086 44.015  1.00 117.61 ? 10  THR L C   1 
ATOM   11513 O O   . THR H 4 10  ? 5.050    -105.835 44.607  1.00 118.15 ? 10  THR L O   1 
ATOM   11514 C CB  . THR H 4 10  ? 3.589    -108.575 43.857  1.00 126.63 ? 10  THR L CB  1 
ATOM   11515 O OG1 . THR H 4 10  ? 4.801    -109.197 44.286  1.00 128.95 ? 10  THR L OG1 1 
ATOM   11516 C CG2 . THR H 4 10  ? 2.758    -109.561 43.050  1.00 125.43 ? 10  THR L CG2 1 
ATOM   11517 N N   . LEU H 4 11  ? 2.884    -105.346 44.145  1.00 112.63 ? 11  LEU L N   1 
ATOM   11518 C CA  . LEU H 4 11  ? 2.793    -104.186 45.027  1.00 112.97 ? 11  LEU L CA  1 
ATOM   11519 C C   . LEU H 4 11  ? 1.869    -104.488 46.212  1.00 119.17 ? 11  LEU L C   1 
ATOM   11520 O O   . LEU H 4 11  ? 0.699    -104.809 46.007  1.00 119.03 ? 11  LEU L O   1 
ATOM   11521 C CB  . LEU H 4 11  ? 2.281    -102.951 44.261  1.00 111.56 ? 11  LEU L CB  1 
ATOM   11522 C CG  . LEU H 4 11  ? 3.314    -101.935 43.791  1.00 115.64 ? 11  LEU L CG  1 
ATOM   11523 C CD1 . LEU H 4 11  ? 2.686    -100.933 42.882  1.00 115.29 ? 11  LEU L CD1 1 
ATOM   11524 C CD2 . LEU H 4 11  ? 3.948    -101.195 44.946  1.00 119.45 ? 11  LEU L CD2 1 
ATOM   11525 N N   . SER H 4 12  ? 2.396    -104.401 47.442  1.00 116.97 ? 12  SER L N   1 
ATOM   11526 C CA  . SER H 4 12  ? 1.618    -104.636 48.655  1.00 118.58 ? 12  SER L CA  1 
ATOM   11527 C C   . SER H 4 12  ? 1.289    -103.272 49.258  1.00 122.03 ? 12  SER L C   1 
ATOM   11528 O O   . SER H 4 12  ? 2.175    -102.605 49.798  1.00 122.83 ? 12  SER L O   1 
ATOM   11529 C CB  . SER H 4 12  ? 2.401    -105.511 49.629  1.00 124.97 ? 12  SER L CB  1 
ATOM   11530 O OG  . SER H 4 12  ? 2.732    -106.761 49.049  1.00 135.05 ? 12  SER L OG  1 
ATOM   11531 N N   . LEU H 4 13  ? 0.029    -102.831 49.111  1.00 117.55 ? 13  LEU L N   1 
ATOM   11532 C CA  . LEU H 4 13  ? -0.423   -101.520 49.582  1.00 118.89 ? 13  LEU L CA  1 
ATOM   11533 C C   . LEU H 4 13  ? -1.712   -101.584 50.395  1.00 125.77 ? 13  LEU L C   1 
ATOM   11534 O O   . LEU H 4 13  ? -2.537   -102.462 50.157  1.00 125.28 ? 13  LEU L O   1 
ATOM   11535 C CB  . LEU H 4 13  ? -0.625   -100.590 48.384  1.00 117.36 ? 13  LEU L CB  1 
ATOM   11536 C CG  . LEU H 4 13  ? 0.638    -100.149 47.648  1.00 121.32 ? 13  LEU L CG  1 
ATOM   11537 C CD1 . LEU H 4 13  ? 0.462    -100.241 46.143  1.00 119.23 ? 13  LEU L CD1 1 
ATOM   11538 C CD2 . LEU H 4 13  ? 1.058    -98.753  48.065  1.00 127.69 ? 13  LEU L CD2 1 
ATOM   11539 N N   . SER H 4 14  ? -1.881   -100.653 51.358  1.00 125.07 ? 14  SER L N   1 
ATOM   11540 C CA  . SER H 4 14  ? -3.080   -100.548 52.201  1.00 127.98 ? 14  SER L CA  1 
ATOM   11541 C C   . SER H 4 14  ? -4.123   -99.684  51.479  1.00 130.35 ? 14  SER L C   1 
ATOM   11542 O O   . SER H 4 14  ? -3.742   -98.659  50.908  1.00 129.26 ? 14  SER L O   1 
ATOM   11543 C CB  . SER H 4 14  ? -2.745   -99.931  53.556  1.00 135.99 ? 14  SER L CB  1 
ATOM   11544 O OG  . SER H 4 14  ? -2.085   -100.837 54.424  1.00 147.19 ? 14  SER L OG  1 
ATOM   11545 N N   . PRO H 4 15  ? -5.427   -100.067 51.478  1.00 127.06 ? 15  PRO L N   1 
ATOM   11546 C CA  . PRO H 4 15  ? -6.439   -99.254  50.775  1.00 127.02 ? 15  PRO L CA  1 
ATOM   11547 C C   . PRO H 4 15  ? -6.520   -97.818  51.282  1.00 133.63 ? 15  PRO L C   1 
ATOM   11548 O O   . PRO H 4 15  ? -7.107   -97.543  52.322  1.00 137.65 ? 15  PRO L O   1 
ATOM   11549 C CB  . PRO H 4 15  ? -7.746   -100.035 50.977  1.00 130.51 ? 15  PRO L CB  1 
ATOM   11550 C CG  . PRO H 4 15  ? -7.330   -101.406 51.355  1.00 134.13 ? 15  PRO L CG  1 
ATOM   11551 C CD  . PRO H 4 15  ? -6.040   -101.256 52.100  1.00 130.15 ? 15  PRO L CD  1 
ATOM   11552 N N   . GLY H 4 16  ? -5.887   -96.925  50.540  1.00 128.88 ? 16  GLY L N   1 
ATOM   11553 C CA  . GLY H 4 16  ? -5.799   -95.511  50.866  1.00 132.79 ? 16  GLY L CA  1 
ATOM   11554 C C   . GLY H 4 16  ? -4.461   -94.937  50.460  1.00 136.20 ? 16  GLY L C   1 
ATOM   11555 O O   . GLY H 4 16  ? -4.351   -93.730  50.238  1.00 138.98 ? 16  GLY L O   1 
ATOM   11556 N N   . GLU H 4 17  ? -3.440   -95.809  50.337  1.00 129.24 ? 17  GLU L N   1 
ATOM   11557 C CA  . GLU H 4 17  ? -2.078   -95.449  49.935  1.00 127.38 ? 17  GLU L CA  1 
ATOM   11558 C C   . GLU H 4 17  ? -1.985   -95.085  48.439  1.00 128.26 ? 17  GLU L C   1 
ATOM   11559 O O   . GLU H 4 17  ? -2.963   -95.217  47.700  1.00 125.59 ? 17  GLU L O   1 
ATOM   11560 C CB  . GLU H 4 17  ? -1.085   -96.570  50.302  1.00 126.25 ? 17  GLU L CB  1 
ATOM   11561 C CG  . GLU H 4 17  ? -0.663   -96.578  51.763  1.00 140.60 ? 17  GLU L CG  1 
ATOM   11562 C CD  . GLU H 4 17  ? 0.411    -97.592  52.120  1.00 161.88 ? 17  GLU L CD  1 
ATOM   11563 O OE1 . GLU H 4 17  ? 1.538    -97.165  52.463  1.00 145.67 ? 17  GLU L OE1 1 
ATOM   11564 O OE2 . GLU H 4 17  ? 0.124    -98.810  52.071  1.00 160.36 ? 17  GLU L OE2 1 
ATOM   11565 N N   . GLY H 4 18  ? -0.815   -94.601  48.028  1.00 125.72 ? 18  GLY L N   1 
ATOM   11566 C CA  . GLY H 4 18  ? -0.541   -94.195  46.656  1.00 124.77 ? 18  GLY L CA  1 
ATOM   11567 C C   . GLY H 4 18  ? 0.341    -95.161  45.890  1.00 125.99 ? 18  GLY L C   1 
ATOM   11568 O O   . GLY H 4 18  ? 1.500    -95.383  46.261  1.00 125.31 ? 18  GLY L O   1 
ATOM   11569 N N   . ALA H 4 19  ? -0.198   -95.726  44.801  1.00 120.50 ? 19  ALA L N   1 
ATOM   11570 C CA  . ALA H 4 19  ? 0.511    -96.676  43.942  1.00 117.33 ? 19  ALA L CA  1 
ATOM   11571 C C   . ALA H 4 19  ? 1.311    -95.974  42.841  1.00 122.44 ? 19  ALA L C   1 
ATOM   11572 O O   . ALA H 4 19  ? 0.834    -94.990  42.275  1.00 123.95 ? 19  ALA L O   1 
ATOM   11573 C CB  . ALA H 4 19  ? -0.476   -97.652  43.324  1.00 116.04 ? 19  ALA L CB  1 
ATOM   11574 N N   . THR H 4 20  ? 2.524    -96.495  42.539  1.00 117.86 ? 20  THR L N   1 
ATOM   11575 C CA  . THR H 4 20  ? 3.443    -95.991  41.507  1.00 117.50 ? 20  THR L CA  1 
ATOM   11576 C C   . THR H 4 20  ? 4.019    -97.201  40.754  1.00 116.94 ? 20  THR L C   1 
ATOM   11577 O O   . THR H 4 20  ? 4.804    -97.959  41.323  1.00 115.91 ? 20  THR L O   1 
ATOM   11578 C CB  . THR H 4 20  ? 4.511    -95.071  42.143  1.00 132.10 ? 20  THR L CB  1 
ATOM   11579 O OG1 . THR H 4 20  ? 3.873    -94.062  42.934  1.00 136.30 ? 20  THR L OG1 1 
ATOM   11580 C CG2 . THR H 4 20  ? 5.415    -94.414  41.108  1.00 132.91 ? 20  THR L CG2 1 
ATOM   11581 N N   . LEU H 4 21  ? 3.607    -97.395  39.497  1.00 111.47 ? 21  LEU L N   1 
ATOM   11582 C CA  . LEU H 4 21  ? 4.015    -98.551  38.701  1.00 109.56 ? 21  LEU L CA  1 
ATOM   11583 C C   . LEU H 4 21  ? 4.919    -98.211  37.515  1.00 116.00 ? 21  LEU L C   1 
ATOM   11584 O O   . LEU H 4 21  ? 4.587    -97.338  36.714  1.00 116.04 ? 21  LEU L O   1 
ATOM   11585 C CB  . LEU H 4 21  ? 2.782    -99.341  38.242  1.00 107.73 ? 21  LEU L CB  1 
ATOM   11586 C CG  . LEU H 4 21  ? 1.894    -99.889  39.352  1.00 111.73 ? 21  LEU L CG  1 
ATOM   11587 C CD1 . LEU H 4 21  ? 0.674    -99.030  39.549  1.00 112.58 ? 21  LEU L CD1 1 
ATOM   11588 C CD2 . LEU H 4 21  ? 1.459    -101.288 39.049  1.00 113.77 ? 21  LEU L CD2 1 
ATOM   11589 N N   . SER H 4 22  ? 6.056    -98.930  37.399  1.00 114.55 ? 22  SER L N   1 
ATOM   11590 C CA  . SER H 4 22  ? 7.064    -98.753  36.347  1.00 116.34 ? 22  SER L CA  1 
ATOM   11591 C C   . SER H 4 22  ? 6.971    -99.805  35.246  1.00 120.62 ? 22  SER L C   1 
ATOM   11592 O O   . SER H 4 22  ? 6.608    -100.955 35.508  1.00 118.57 ? 22  SER L O   1 
ATOM   11593 C CB  . SER H 4 22  ? 8.467    -98.779  36.944  1.00 121.89 ? 22  SER L CB  1 
ATOM   11594 O OG  . SER H 4 22  ? 8.659    -97.778  37.931  1.00 133.80 ? 22  SER L OG  1 
ATOM   11595 N N   . CYS H 4 23  ? 7.338    -99.406  34.019  1.00 120.05 ? 23  CYS L N   1 
ATOM   11596 C CA  . CYS H 4 23  ? 7.352    -100.252 32.827  1.00 120.70 ? 23  CYS L CA  1 
ATOM   11597 C C   . CYS H 4 23  ? 8.507    -99.791  31.941  1.00 128.46 ? 23  CYS L C   1 
ATOM   11598 O O   . CYS H 4 23  ? 8.357    -98.833  31.176  1.00 128.98 ? 23  CYS L O   1 
ATOM   11599 C CB  . CYS H 4 23  ? 6.006    -100.185 32.101  1.00 120.08 ? 23  CYS L CB  1 
ATOM   11600 S SG  . CYS H 4 23  ? 5.942    -101.080 30.519  1.00 124.30 ? 23  CYS L SG  1 
ATOM   11601 N N   . ARG H 4 24  ? 9.677    -100.449 32.081  1.00 127.80 ? 24  ARG L N   1 
ATOM   11602 C CA  . ARG H 4 24  ? 10.881   -100.110 31.313  1.00 130.96 ? 24  ARG L CA  1 
ATOM   11603 C C   . ARG H 4 24  ? 11.041   -100.954 30.046  1.00 134.57 ? 24  ARG L C   1 
ATOM   11604 O O   . ARG H 4 24  ? 11.144   -102.181 30.111  1.00 133.00 ? 24  ARG L O   1 
ATOM   11605 C CB  . ARG H 4 24  ? 12.143   -100.141 32.190  1.00 133.30 ? 24  ARG L CB  1 
ATOM   11606 C CG  . ARG H 4 24  ? 12.366   -98.813  32.900  1.00 146.17 ? 24  ARG L CG  1 
ATOM   11607 C CD  . ARG H 4 24  ? 13.313   -98.922  34.071  1.00 160.22 ? 24  ARG L CD  1 
ATOM   11608 N NE  . ARG H 4 24  ? 12.877   -98.076  35.184  1.00 171.29 ? 24  ARG L NE  1 
ATOM   11609 C CZ  . ARG H 4 24  ? 12.073   -98.477  36.164  1.00 182.44 ? 24  ARG L CZ  1 
ATOM   11610 N NH1 . ARG H 4 24  ? 11.607   -99.722  36.182  1.00 168.32 ? 24  ARG L NH1 1 
ATOM   11611 N NH2 . ARG H 4 24  ? 11.728   -97.640  37.132  1.00 166.59 ? 24  ARG L NH2 1 
ATOM   11612 N N   . ALA H 4 25  ? 11.046   -100.268 28.894  1.00 133.03 ? 25  ALA L N   1 
ATOM   11613 C CA  . ALA H 4 25  ? 11.162   -100.855 27.564  1.00 135.04 ? 25  ALA L CA  1 
ATOM   11614 C C   . ALA H 4 25  ? 12.606   -101.171 27.166  1.00 142.71 ? 25  ALA L C   1 
ATOM   11615 O O   . ALA H 4 25  ? 13.527   -100.464 27.582  1.00 143.90 ? 25  ALA L O   1 
ATOM   11616 C CB  . ALA H 4 25  ? 10.541   -99.918  26.542  1.00 136.80 ? 25  ALA L CB  1 
ATOM   11617 N N   . SER H 4 26  ? 12.785   -102.227 26.336  1.00 132.88 ? 26  SER L N   1 
ATOM   11618 C CA  . SER H 4 26  ? 14.061   -102.693 25.781  1.00 136.61 ? 26  SER L CA  1 
ATOM   11619 C C   . SER H 4 26  ? 14.766   -101.536 25.057  1.00 145.23 ? 26  SER L C   1 
ATOM   11620 O O   . SER H 4 26  ? 15.916   -101.218 25.372  1.00 148.98 ? 26  SER L O   1 
ATOM   11621 C CB  . SER H 4 26  ? 13.821   -103.864 24.827  1.00 139.46 ? 26  SER L CB  1 
ATOM   11622 O OG  . SER H 4 26  ? 14.990   -104.292 24.146  1.00 149.73 ? 26  SER L OG  1 
ATOM   11623 N N   . GLN H 4 27  ? 14.043   -100.881 24.132  1.00 141.10 ? 27  GLN L N   1 
ATOM   11624 C CA  . GLN H 4 27  ? 14.495   -99.717  23.364  1.00 144.80 ? 27  GLN L CA  1 
ATOM   11625 C C   . GLN H 4 27  ? 13.484   -98.569  23.528  1.00 146.39 ? 27  GLN L C   1 
ATOM   11626 O O   . GLN H 4 27  ? 12.397   -98.797  24.058  1.00 141.31 ? 27  GLN L O   1 
ATOM   11627 C CB  . GLN H 4 27  ? 14.743   -100.076 21.881  1.00 149.09 ? 27  GLN L CB  1 
ATOM   11628 C CG  . GLN H 4 27  ? 13.614   -100.854 21.193  1.00 163.73 ? 27  GLN L CG  1 
ATOM   11629 C CD  . GLN H 4 27  ? 14.093   -102.156 20.585  1.00 187.05 ? 27  GLN L CD  1 
ATOM   11630 O OE1 . GLN H 4 27  ? 14.236   -102.289 19.363  1.00 184.37 ? 27  GLN L OE1 1 
ATOM   11631 N NE2 . GLN H 4 27  ? 14.330   -103.157 21.423  1.00 179.23 ? 27  GLN L NE2 1 
ATOM   11632 N N   . SER H 4 28  ? 13.846   -97.339  23.119  1.00 146.75 ? 28  SER L N   1 
ATOM   11633 C CA  . SER H 4 28  ? 12.961   -96.178  23.252  1.00 145.32 ? 28  SER L CA  1 
ATOM   11634 C C   . SER H 4 28  ? 11.776   -96.269  22.298  1.00 145.14 ? 28  SER L C   1 
ATOM   11635 O O   . SER H 4 28  ? 11.964   -96.516  21.106  1.00 146.31 ? 28  SER L O   1 
ATOM   11636 C CB  . SER H 4 28  ? 13.731   -94.877  23.040  1.00 155.54 ? 28  SER L CB  1 
ATOM   11637 O OG  . SER H 4 28  ? 12.923   -93.744  23.318  1.00 165.43 ? 28  SER L OG  1 
ATOM   11638 N N   . VAL H 4 29  ? 10.554   -96.117  22.842  1.00 137.31 ? 29  VAL L N   1 
ATOM   11639 C CA  . VAL H 4 29  ? 9.281    -96.164  22.097  1.00 134.45 ? 29  VAL L CA  1 
ATOM   11640 C C   . VAL H 4 29  ? 8.534    -94.828  22.276  1.00 138.45 ? 29  VAL L C   1 
ATOM   11641 O O   . VAL H 4 29  ? 8.782    -94.124  23.262  1.00 139.21 ? 29  VAL L O   1 
ATOM   11642 C CB  . VAL H 4 29  ? 8.365    -97.374  22.467  1.00 133.35 ? 29  VAL L CB  1 
ATOM   11643 C CG1 . VAL H 4 29  ? 7.554    -97.843  21.257  1.00 131.77 ? 29  VAL L CG1 1 
ATOM   11644 C CG2 . VAL H 4 29  ? 9.150    -98.537  23.072  1.00 132.95 ? 29  VAL L CG2 1 
ATOM   11645 N N   . ASP H 4 30  ? 7.634    -94.476  21.321  1.00 133.60 ? 30  ASP L N   1 
ATOM   11646 C CA  . ASP H 4 30  ? 6.842    -93.241  21.365  1.00 133.28 ? 30  ASP L CA  1 
ATOM   11647 C C   . ASP H 4 30  ? 5.901    -93.267  22.569  1.00 132.08 ? 30  ASP L C   1 
ATOM   11648 O O   . ASP H 4 30  ? 5.362    -94.325  22.906  1.00 127.57 ? 30  ASP L O   1 
ATOM   11649 C CB  . ASP H 4 30  ? 6.043    -93.042  20.055  1.00 135.17 ? 30  ASP L CB  1 
ATOM   11650 C CG  . ASP H 4 30  ? 5.533    -91.624  19.770  1.00 146.65 ? 30  ASP L CG  1 
ATOM   11651 O OD1 . ASP H 4 30  ? 5.752    -90.722  20.621  1.00 148.79 ? 30  ASP L OD1 1 
ATOM   11652 O OD2 . ASP H 4 30  ? 4.928    -91.413  18.687  1.00 150.11 ? 30  ASP L OD2 1 
ATOM   11653 N N   . SER H 4 31  ? 5.743    -92.108  23.236  1.00 129.84 ? 31  SER L N   1 
ATOM   11654 C CA  . SER H 4 31  ? 4.888    -91.938  24.416  1.00 126.43 ? 31  SER L CA  1 
ATOM   11655 C C   . SER H 4 31  ? 3.439    -92.227  24.067  1.00 123.49 ? 31  SER L C   1 
ATOM   11656 O O   . SER H 4 31  ? 2.773    -92.958  24.796  1.00 119.47 ? 31  SER L O   1 
ATOM   11657 C CB  . SER H 4 31  ? 5.028    -90.528  24.988  1.00 134.72 ? 31  SER L CB  1 
ATOM   11658 O OG  . SER H 4 31  ? 4.689    -89.533  24.034  1.00 150.66 ? 31  SER L OG  1 
ATOM   11659 N N   . SER H 4 32  ? 2.980    -91.697  22.914  1.00 119.27 ? 32  SER L N   1 
ATOM   11660 C CA  . SER H 4 32  ? 1.626    -91.866  22.393  1.00 115.50 ? 32  SER L CA  1 
ATOM   11661 C C   . SER H 4 32  ? 1.303    -93.308  21.984  1.00 114.50 ? 32  SER L C   1 
ATOM   11662 O O   . SER H 4 32  ? 0.133    -93.628  21.795  1.00 110.90 ? 32  SER L O   1 
ATOM   11663 C CB  . SER H 4 32  ? 1.354    -90.886  21.255  1.00 121.17 ? 32  SER L CB  1 
ATOM   11664 O OG  . SER H 4 32  ? 2.406    -90.861  20.304  1.00 132.14 ? 32  SER L OG  1 
ATOM   11665 N N   . SER H 4 33  ? 2.319    -94.182  21.883  1.00 110.99 ? 33  SER L N   1 
ATOM   11666 C CA  . SER H 4 33  ? 2.115    -95.593  21.552  1.00 108.28 ? 33  SER L CA  1 
ATOM   11667 C C   . SER H 4 33  ? 1.907    -96.468  22.816  1.00 110.27 ? 33  SER L C   1 
ATOM   11668 O O   . SER H 4 33  ? 1.502    -97.627  22.693  1.00 108.31 ? 33  SER L O   1 
ATOM   11669 C CB  . SER H 4 33  ? 3.266    -96.124  20.702  1.00 113.43 ? 33  SER L CB  1 
ATOM   11670 O OG  . SER H 4 33  ? 4.405    -96.464  21.477  1.00 122.69 ? 33  SER L OG  1 
ATOM   11671 N N   . LEU H 4 34  ? 2.173    -95.909  24.022  1.00 106.72 ? 34  LEU L N   1 
ATOM   11672 C CA  . LEU H 4 34  ? 2.056    -96.633  25.294  1.00 104.40 ? 34  LEU L CA  1 
ATOM   11673 C C   . LEU H 4 34  ? 0.670    -96.563  25.961  1.00 104.79 ? 34  LEU L C   1 
ATOM   11674 O O   . LEU H 4 34  ? 0.000    -95.530  25.909  1.00 104.01 ? 34  LEU L O   1 
ATOM   11675 C CB  . LEU H 4 34  ? 3.144    -96.187  26.274  1.00 106.34 ? 34  LEU L CB  1 
ATOM   11676 C CG  . LEU H 4 34  ? 4.551    -96.737  26.033  1.00 113.26 ? 34  LEU L CG  1 
ATOM   11677 C CD1 . LEU H 4 34  ? 5.584    -95.893  26.750  1.00 116.13 ? 34  LEU L CD1 1 
ATOM   11678 C CD2 . LEU H 4 34  ? 4.669    -98.201  26.462  1.00 113.83 ? 34  LEU L CD2 1 
ATOM   11679 N N   . ALA H 4 35  ? 0.253    -97.682  26.592  1.00 99.21  ? 35  ALA L N   1 
ATOM   11680 C CA  . ALA H 4 35  ? -1.039   -97.811  27.272  1.00 97.01  ? 35  ALA L CA  1 
ATOM   11681 C C   . ALA H 4 35  ? -0.962   -98.681  28.525  1.00 99.25  ? 35  ALA L C   1 
ATOM   11682 O O   . ALA H 4 35  ? -0.160   -99.615  28.570  1.00 98.40  ? 35  ALA L O   1 
ATOM   11683 C CB  . ALA H 4 35  ? -2.089   -98.367  26.317  1.00 96.33  ? 35  ALA L CB  1 
ATOM   11684 N N   . TRP H 4 36  ? -1.811   -98.372  29.534  1.00 95.53  ? 36  TRP L N   1 
ATOM   11685 C CA  . TRP H 4 36  ? -1.925   -99.090  30.812  1.00 95.78  ? 36  TRP L CA  1 
ATOM   11686 C C   . TRP H 4 36  ? -3.285   -99.785  30.938  1.00 96.07  ? 36  TRP L C   1 
ATOM   11687 O O   . TRP H 4 36  ? -4.326   -99.153  30.742  1.00 94.47  ? 36  TRP L O   1 
ATOM   11688 C CB  . TRP H 4 36  ? -1.729   -98.135  31.992  1.00 96.40  ? 36  TRP L CB  1 
ATOM   11689 C CG  . TRP H 4 36  ? -0.302   -97.783  32.293  1.00 99.94  ? 36  TRP L CG  1 
ATOM   11690 C CD1 . TRP H 4 36  ? 0.287    -96.560  32.150  1.00 103.59 ? 36  TRP L CD1 1 
ATOM   11691 C CD2 . TRP H 4 36  ? 0.686    -98.637  32.888  1.00 100.23 ? 36  TRP L CD2 1 
ATOM   11692 N NE1 . TRP H 4 36  ? 1.586    -96.604  32.600  1.00 104.52 ? 36  TRP L NE1 1 
ATOM   11693 C CE2 . TRP H 4 36  ? 1.864    -97.873  33.037  1.00 105.62 ? 36  TRP L CE2 1 
ATOM   11694 C CE3 . TRP H 4 36  ? 0.688    -99.978  33.317  1.00 101.90 ? 36  TRP L CE3 1 
ATOM   11695 C CZ2 . TRP H 4 36  ? 3.026    -98.399  33.607  1.00 105.98 ? 36  TRP L CZ2 1 
ATOM   11696 C CZ3 . TRP H 4 36  ? 1.844    -100.500 33.875  1.00 104.33 ? 36  TRP L CZ3 1 
ATOM   11697 C CH2 . TRP H 4 36  ? 2.996    -99.716  34.011  1.00 105.98 ? 36  TRP L CH2 1 
ATOM   11698 N N   . TYR H 4 37  ? -3.269   -101.080 31.286  1.00 91.90  ? 37  TYR L N   1 
ATOM   11699 C CA  . TYR H 4 37  ? -4.458   -101.917 31.430  1.00 91.63  ? 37  TYR L CA  1 
ATOM   11700 C C   . TYR H 4 37  ? -4.586   -102.517 32.834  1.00 96.95  ? 37  TYR L C   1 
ATOM   11701 O O   . TYR H 4 37  ? -3.574   -102.790 33.485  1.00 97.75  ? 37  TYR L O   1 
ATOM   11702 C CB  . TYR H 4 37  ? -4.458   -103.053 30.391  1.00 92.37  ? 37  TYR L CB  1 
ATOM   11703 C CG  . TYR H 4 37  ? -4.397   -102.596 28.949  1.00 93.02  ? 37  TYR L CG  1 
ATOM   11704 C CD1 . TYR H 4 37  ? -5.544   -102.546 28.164  1.00 94.17  ? 37  TYR L CD1 1 
ATOM   11705 C CD2 . TYR H 4 37  ? -3.182   -102.290 28.346  1.00 93.75  ? 37  TYR L CD2 1 
ATOM   11706 C CE1 . TYR H 4 37  ? -5.486   -102.168 26.826  1.00 94.30  ? 37  TYR L CE1 1 
ATOM   11707 C CE2 . TYR H 4 37  ? -3.115   -101.888 27.017  1.00 93.64  ? 37  TYR L CE2 1 
ATOM   11708 C CZ  . TYR H 4 37  ? -4.268   -101.830 26.261  1.00 101.66 ? 37  TYR L CZ  1 
ATOM   11709 O OH  . TYR H 4 37  ? -4.186   -101.425 24.955  1.00 107.50 ? 37  TYR L OH  1 
ATOM   11710 N N   . GLN H 4 38  ? -5.833   -102.727 33.292  1.00 93.13  ? 38  GLN L N   1 
ATOM   11711 C CA  . GLN H 4 38  ? -6.129   -103.328 34.591  1.00 94.64  ? 38  GLN L CA  1 
ATOM   11712 C C   . GLN H 4 38  ? -6.964   -104.589 34.370  1.00 101.15 ? 38  GLN L C   1 
ATOM   11713 O O   . GLN H 4 38  ? -8.055   -104.507 33.798  1.00 101.64 ? 38  GLN L O   1 
ATOM   11714 C CB  . GLN H 4 38  ? -6.873   -102.330 35.508  1.00 96.44  ? 38  GLN L CB  1 
ATOM   11715 C CG  . GLN H 4 38  ? -7.213   -102.876 36.906  1.00 111.97 ? 38  GLN L CG  1 
ATOM   11716 C CD  . GLN H 4 38  ? -8.409   -102.222 37.577  1.00 130.14 ? 38  GLN L CD  1 
ATOM   11717 O OE1 . GLN H 4 38  ? -9.465   -102.000 36.973  1.00 125.15 ? 38  GLN L OE1 1 
ATOM   11718 N NE2 . GLN H 4 38  ? -8.298   -101.981 38.876  1.00 122.41 ? 38  GLN L NE2 1 
ATOM   11719 N N   . GLN H 4 39  ? -6.452   -105.750 34.813  1.00 99.11  ? 39  GLN L N   1 
ATOM   11720 C CA  . GLN H 4 39  ? -7.184   -107.010 34.704  1.00 100.90 ? 39  GLN L CA  1 
ATOM   11721 C C   . GLN H 4 39  ? -7.547   -107.526 36.083  1.00 109.54 ? 39  GLN L C   1 
ATOM   11722 O O   . GLN H 4 39  ? -6.674   -107.690 36.939  1.00 109.93 ? 39  GLN L O   1 
ATOM   11723 C CB  . GLN H 4 39  ? -6.408   -108.064 33.903  1.00 101.58 ? 39  GLN L CB  1 
ATOM   11724 C CG  . GLN H 4 39  ? -7.220   -109.339 33.645  1.00 105.79 ? 39  GLN L CG  1 
ATOM   11725 C CD  . GLN H 4 39  ? -6.875   -110.027 32.348  1.00 115.87 ? 39  GLN L CD  1 
ATOM   11726 O OE1 . GLN H 4 39  ? -5.822   -109.803 31.743  1.00 109.65 ? 39  GLN L OE1 1 
ATOM   11727 N NE2 . GLN H 4 39  ? -7.759   -110.896 31.893  1.00 105.74 ? 39  GLN L NE2 1 
ATOM   11728 N N   . LYS H 4 40  ? -8.841   -107.757 36.300  1.00 109.59 ? 40  LYS L N   1 
ATOM   11729 C CA  . LYS H 4 40  ? -9.343   -108.283 37.564  1.00 113.99 ? 40  LYS L CA  1 
ATOM   11730 C C   . LYS H 4 40  ? -9.467   -109.809 37.418  1.00 122.97 ? 40  LYS L C   1 
ATOM   11731 O O   . LYS H 4 40  ? -9.615   -110.273 36.283  1.00 122.08 ? 40  LYS L O   1 
ATOM   11732 C CB  . LYS H 4 40  ? -10.691  -107.628 37.918  1.00 117.32 ? 40  LYS L CB  1 
ATOM   11733 C CG  . LYS H 4 40  ? -10.560  -106.257 38.580  1.00 117.58 ? 40  LYS L CG  1 
ATOM   11734 C CD  . LYS H 4 40  ? -11.802  -105.396 38.343  1.00 120.52 ? 40  LYS L CD  1 
ATOM   11735 C CE  . LYS H 4 40  ? -11.754  -104.083 39.079  1.00 123.25 ? 40  LYS L CE  1 
ATOM   11736 N NZ  . LYS H 4 40  ? -12.175  -104.234 40.496  1.00 136.83 ? 40  LYS L NZ  1 
ATOM   11737 N N   . PRO H 4 41  ? -9.370   -110.615 38.511  1.00 124.48 ? 41  PRO L N   1 
ATOM   11738 C CA  . PRO H 4 41  ? -9.479   -112.079 38.355  1.00 127.91 ? 41  PRO L CA  1 
ATOM   11739 C C   . PRO H 4 41  ? -10.811  -112.528 37.754  1.00 134.36 ? 41  PRO L C   1 
ATOM   11740 O O   . PRO H 4 41  ? -11.881  -112.153 38.247  1.00 136.40 ? 41  PRO L O   1 
ATOM   11741 C CB  . PRO H 4 41  ? -9.286   -112.613 39.783  1.00 134.08 ? 41  PRO L CB  1 
ATOM   11742 C CG  . PRO H 4 41  ? -8.631   -111.510 40.531  1.00 136.46 ? 41  PRO L CG  1 
ATOM   11743 C CD  . PRO H 4 41  ? -9.165   -110.250 39.927  1.00 128.45 ? 41  PRO L CD  1 
ATOM   11744 N N   . GLY H 4 42  ? -10.715  -113.303 36.672  1.00 129.86 ? 42  GLY L N   1 
ATOM   11745 C CA  . GLY H 4 42  ? -11.859  -113.828 35.935  1.00 130.85 ? 42  GLY L CA  1 
ATOM   11746 C C   . GLY H 4 42  ? -12.631  -112.748 35.204  1.00 129.73 ? 42  GLY L C   1 
ATOM   11747 O O   . GLY H 4 42  ? -13.862  -112.799 35.139  1.00 132.04 ? 42  GLY L O   1 
ATOM   11748 N N   . GLN H 4 43  ? -11.903  -111.756 34.664  1.00 119.38 ? 43  GLN L N   1 
ATOM   11749 C CA  . GLN H 4 43  ? -12.454  -110.619 33.936  1.00 115.38 ? 43  GLN L CA  1 
ATOM   11750 C C   . GLN H 4 43  ? -11.555  -110.227 32.765  1.00 115.67 ? 43  GLN L C   1 
ATOM   11751 O O   . GLN H 4 43  ? -10.337  -110.389 32.844  1.00 115.18 ? 43  GLN L O   1 
ATOM   11752 C CB  . GLN H 4 43  ? -12.605  -109.413 34.876  1.00 116.11 ? 43  GLN L CB  1 
ATOM   11753 C CG  . GLN H 4 43  ? -13.877  -109.423 35.713  1.00 133.06 ? 43  GLN L CG  1 
ATOM   11754 C CD  . GLN H 4 43  ? -14.036  -108.170 36.543  1.00 157.06 ? 43  GLN L CD  1 
ATOM   11755 O OE1 . GLN H 4 43  ? -13.880  -107.038 36.061  1.00 152.54 ? 43  GLN L OE1 1 
ATOM   11756 N NE2 . GLN H 4 43  ? -14.386  -108.344 37.809  1.00 152.09 ? 43  GLN L NE2 1 
ATOM   11757 N N   . ALA H 4 44  ? -12.159  -109.673 31.696  1.00 109.14 ? 44  ALA L N   1 
ATOM   11758 C CA  . ALA H 4 44  ? -11.459  -109.164 30.516  1.00 104.48 ? 44  ALA L CA  1 
ATOM   11759 C C   . ALA H 4 44  ? -10.692  -107.871 30.882  1.00 104.43 ? 44  ALA L C   1 
ATOM   11760 O O   . ALA H 4 44  ? -11.137  -107.162 31.788  1.00 105.53 ? 44  ALA L O   1 
ATOM   11761 C CB  . ALA H 4 44  ? -12.465  -108.873 29.416  1.00 103.70 ? 44  ALA L CB  1 
ATOM   11762 N N   . PRO H 4 45  ? -9.561   -107.527 30.213  1.00 96.69  ? 45  PRO L N   1 
ATOM   11763 C CA  . PRO H 4 45  ? -8.832   -106.298 30.586  1.00 94.41  ? 45  PRO L CA  1 
ATOM   11764 C C   . PRO H 4 45  ? -9.598   -104.993 30.366  1.00 94.90  ? 45  PRO L C   1 
ATOM   11765 O O   . PRO H 4 45  ? -10.570  -104.944 29.608  1.00 93.22  ? 45  PRO L O   1 
ATOM   11766 C CB  . PRO H 4 45  ? -7.558   -106.360 29.732  1.00 94.77  ? 45  PRO L CB  1 
ATOM   11767 C CG  . PRO H 4 45  ? -7.448   -107.778 29.299  1.00 100.55 ? 45  PRO L CG  1 
ATOM   11768 C CD  . PRO H 4 45  ? -8.855   -108.246 29.137  1.00 97.14  ? 45  PRO L CD  1 
ATOM   11769 N N   . ARG H 4 46  ? -9.152   -103.936 31.057  1.00 90.82  ? 46  ARG L N   1 
ATOM   11770 C CA  . ARG H 4 46  ? -9.742   -102.599 31.009  1.00 90.08  ? 46  ARG L CA  1 
ATOM   11771 C C   . ARG H 4 46  ? -8.663   -101.606 30.637  1.00 92.07  ? 46  ARG L C   1 
ATOM   11772 O O   . ARG H 4 46  ? -7.536   -101.736 31.111  1.00 91.77  ? 46  ARG L O   1 
ATOM   11773 C CB  . ARG H 4 46  ? -10.314  -102.235 32.394  1.00 94.54  ? 46  ARG L CB  1 
ATOM   11774 C CG  . ARG H 4 46  ? -11.433  -101.182 32.393  1.00 108.83 ? 46  ARG L CG  1 
ATOM   11775 C CD  . ARG H 4 46  ? -12.734  -101.696 33.015  1.00 124.54 ? 46  ARG L CD  1 
ATOM   11776 N NE  . ARG H 4 46  ? -12.571  -102.099 34.416  1.00 150.84 ? 46  ARG L NE  1 
ATOM   11777 C CZ  . ARG H 4 46  ? -12.774  -101.298 35.458  1.00 181.59 ? 46  ARG L CZ  1 
ATOM   11778 N NH1 . ARG H 4 46  ? -13.163  -100.040 35.271  1.00 174.86 ? 46  ARG L NH1 1 
ATOM   11779 N NH2 . ARG H 4 46  ? -12.592  -101.746 36.694  1.00 174.93 ? 46  ARG L NH2 1 
ATOM   11780 N N   . LEU H 4 47  ? -8.997   -100.619 29.793  1.00 100.08 ? 47  LEU L N   1 
ATOM   11781 C CA  . LEU H 4 47  ? -8.057   -99.570  29.400  1.00 100.38 ? 47  LEU L CA  1 
ATOM   11782 C C   . LEU H 4 47  ? -8.155   -98.442  30.432  1.00 103.24 ? 47  LEU L C   1 
ATOM   11783 O O   . LEU H 4 47  ? -9.261   -97.984  30.732  1.00 103.12 ? 47  LEU L O   1 
ATOM   11784 C CB  . LEU H 4 47  ? -8.368   -99.064  27.974  1.00 102.44 ? 47  LEU L CB  1 
ATOM   11785 C CG  . LEU H 4 47  ? -7.430   -98.002  27.385  1.00 107.95 ? 47  LEU L CG  1 
ATOM   11786 C CD1 . LEU H 4 47  ? -6.204   -98.629  26.744  1.00 109.49 ? 47  LEU L CD1 1 
ATOM   11787 C CD2 . LEU H 4 47  ? -8.145   -97.167  26.355  1.00 111.39 ? 47  LEU L CD2 1 
ATOM   11788 N N   . LEU H 4 48  ? -7.007   -98.042  31.014  1.00 99.20  ? 48  LEU L N   1 
ATOM   11789 C CA  . LEU H 4 48  ? -6.929   -96.977  32.028  1.00 98.63  ? 48  LEU L CA  1 
ATOM   11790 C C   . LEU H 4 48  ? -6.335   -95.724  31.399  1.00 104.47 ? 48  LEU L C   1 
ATOM   11791 O O   . LEU H 4 48  ? -6.939   -94.649  31.439  1.00 105.21 ? 48  LEU L O   1 
ATOM   11792 C CB  . LEU H 4 48  ? -6.037   -97.378  33.215  1.00 97.75  ? 48  LEU L CB  1 
ATOM   11793 C CG  . LEU H 4 48  ? -6.224   -98.740  33.820  1.00 101.46 ? 48  LEU L CG  1 
ATOM   11794 C CD1 . LEU H 4 48  ? -4.905   -99.281  34.259  1.00 102.06 ? 48  LEU L CD1 1 
ATOM   11795 C CD2 . LEU H 4 48  ? -7.173   -98.680  34.983  1.00 103.83 ? 48  LEU L CD2 1 
ATOM   11796 N N   . ILE H 4 49  ? -5.111   -95.858  30.878  1.00 100.67 ? 49  ILE L N   1 
ATOM   11797 C CA  . ILE H 4 49  ? -4.389   -94.781  30.232  1.00 100.90 ? 49  ILE L CA  1 
ATOM   11798 C C   . ILE H 4 49  ? -4.040   -95.265  28.830  1.00 108.46 ? 49  ILE L C   1 
ATOM   11799 O O   . ILE H 4 49  ? -3.588   -96.396  28.658  1.00 108.90 ? 49  ILE L O   1 
ATOM   11800 C CB  . ILE H 4 49  ? -3.142   -94.348  31.067  1.00 103.37 ? 49  ILE L CB  1 
ATOM   11801 C CG1 . ILE H 4 49  ? -3.494   -93.956  32.526  1.00 102.83 ? 49  ILE L CG1 1 
ATOM   11802 C CG2 . ILE H 4 49  ? -2.339   -93.244  30.381  1.00 104.83 ? 49  ILE L CG2 1 
ATOM   11803 C CD1 . ILE H 4 49  ? -4.431   -92.700  32.762  1.00 109.13 ? 49  ILE L CD1 1 
ATOM   11804 N N   . PHE H 4 50  ? -4.319   -94.429  27.833  1.00 106.88 ? 50  PHE L N   1 
ATOM   11805 C CA  . PHE H 4 50  ? -3.997   -94.654  26.427  1.00 108.29 ? 50  PHE L CA  1 
ATOM   11806 C C   . PHE H 4 50  ? -3.189   -93.431  25.999  1.00 112.72 ? 50  PHE L C   1 
ATOM   11807 O O   . PHE H 4 50  ? -3.298   -92.385  26.647  1.00 111.69 ? 50  PHE L O   1 
ATOM   11808 C CB  . PHE H 4 50  ? -5.276   -94.821  25.586  1.00 111.00 ? 50  PHE L CB  1 
ATOM   11809 C CG  . PHE H 4 50  ? -6.102   -93.569  25.409  1.00 112.92 ? 50  PHE L CG  1 
ATOM   11810 C CD1 . PHE H 4 50  ? -6.981   -93.148  26.401  1.00 115.23 ? 50  PHE L CD1 1 
ATOM   11811 C CD2 . PHE H 4 50  ? -6.020   -92.822  24.237  1.00 116.55 ? 50  PHE L CD2 1 
ATOM   11812 C CE1 . PHE H 4 50  ? -7.740   -91.986  26.237  1.00 117.32 ? 50  PHE L CE1 1 
ATOM   11813 C CE2 . PHE H 4 50  ? -6.778   -91.659  24.073  1.00 120.17 ? 50  PHE L CE2 1 
ATOM   11814 C CZ  . PHE H 4 50  ? -7.634   -91.249  25.073  1.00 117.80 ? 50  PHE L CZ  1 
ATOM   11815 N N   . ALA H 4 51  ? -2.368   -93.557  24.940  1.00 110.62 ? 51  ALA L N   1 
ATOM   11816 C CA  . ALA H 4 51  ? -1.499   -92.490  24.422  1.00 111.38 ? 51  ALA L CA  1 
ATOM   11817 C C   . ALA H 4 51  ? -0.442   -91.987  25.431  1.00 115.17 ? 51  ALA L C   1 
ATOM   11818 O O   . ALA H 4 51  ? 0.079    -90.879  25.275  1.00 115.08 ? 51  ALA L O   1 
ATOM   11819 C CB  . ALA H 4 51  ? -2.319   -91.328  23.869  1.00 112.36 ? 51  ALA L CB  1 
ATOM   11820 N N   . GLY H 4 52  ? -0.129   -92.816  26.432  1.00 111.57 ? 52  GLY L N   1 
ATOM   11821 C CA  . GLY H 4 52  ? 0.878    -92.547  27.451  1.00 111.67 ? 52  GLY L CA  1 
ATOM   11822 C C   . GLY H 4 52  ? 0.427    -91.769  28.668  1.00 115.60 ? 52  GLY L C   1 
ATOM   11823 O O   . GLY H 4 52  ? 0.790    -92.138  29.790  1.00 114.29 ? 52  GLY L O   1 
ATOM   11824 N N   . SER H 4 53  ? -0.344   -90.674  28.464  1.00 114.25 ? 53  SER L N   1 
ATOM   11825 C CA  . SER H 4 53  ? -0.809   -89.795  29.554  1.00 114.78 ? 53  SER L CA  1 
ATOM   11826 C C   . SER H 4 53  ? -2.334   -89.515  29.581  1.00 117.72 ? 53  SER L C   1 
ATOM   11827 O O   . SER H 4 53  ? -2.861   -89.159  30.644  1.00 116.85 ? 53  SER L O   1 
ATOM   11828 C CB  . SER H 4 53  ? -0.034   -88.478  29.549  1.00 122.02 ? 53  SER L CB  1 
ATOM   11829 O OG  . SER H 4 53  ? -0.188   -87.781  28.322  1.00 138.06 ? 53  SER L OG  1 
ATOM   11830 N N   . SER H 4 54  ? -3.028   -89.651  28.418  1.00 113.79 ? 54  SER L N   1 
ATOM   11831 C CA  . SER H 4 54  ? -4.480   -89.436  28.276  1.00 112.68 ? 54  SER L CA  1 
ATOM   11832 C C   . SER H 4 54  ? -5.299   -90.466  29.077  1.00 113.27 ? 54  SER L C   1 
ATOM   11833 O O   . SER H 4 54  ? -5.051   -91.669  28.967  1.00 112.58 ? 54  SER L O   1 
ATOM   11834 C CB  . SER H 4 54  ? -4.885   -89.452  26.803  1.00 116.19 ? 54  SER L CB  1 
ATOM   11835 O OG  . SER H 4 54  ? -4.030   -88.638  26.015  1.00 121.06 ? 54  SER L OG  1 
ATOM   11836 N N   . ARG H 4 55  ? -6.252   -89.985  29.902  1.00 107.56 ? 55  ARG L N   1 
ATOM   11837 C CA  . ARG H 4 55  ? -7.112   -90.840  30.727  1.00 105.59 ? 55  ARG L CA  1 
ATOM   11838 C C   . ARG H 4 55  ? -8.242   -91.419  29.876  1.00 107.02 ? 55  ARG L C   1 
ATOM   11839 O O   . ARG H 4 55  ? -8.860   -90.688  29.103  1.00 108.19 ? 55  ARG L O   1 
ATOM   11840 C CB  . ARG H 4 55  ? -7.667   -90.058  31.926  1.00 106.27 ? 55  ARG L CB  1 
ATOM   11841 C CG  . ARG H 4 55  ? -7.892   -90.912  33.171  1.00 112.96 ? 55  ARG L CG  1 
ATOM   11842 C CD  . ARG H 4 55  ? -8.624   -90.154  34.261  1.00 119.13 ? 55  ARG L CD  1 
ATOM   11843 N NE  . ARG H 4 55  ? -7.780   -89.155  34.917  1.00 125.61 ? 55  ARG L NE  1 
ATOM   11844 C CZ  . ARG H 4 55  ? -8.071   -87.861  35.000  1.00 141.74 ? 55  ARG L CZ  1 
ATOM   11845 N NH1 . ARG H 4 55  ? -9.198   -87.391  34.477  1.00 129.52 ? 55  ARG L NH1 1 
ATOM   11846 N NH2 . ARG H 4 55  ? -7.243   -87.028  35.615  1.00 131.13 ? 55  ARG L NH2 1 
ATOM   11847 N N   . ALA H 4 56  ? -8.512   -92.726  30.017  1.00 100.58 ? 56  ALA L N   1 
ATOM   11848 C CA  . ALA H 4 56  ? -9.530   -93.422  29.233  1.00 100.96 ? 56  ALA L CA  1 
ATOM   11849 C C   . ALA H 4 56  ? -10.971  -92.992  29.508  1.00 107.49 ? 56  ALA L C   1 
ATOM   11850 O O   . ALA H 4 56  ? -11.246  -92.252  30.456  1.00 107.32 ? 56  ALA L O   1 
ATOM   11851 C CB  . ALA H 4 56  ? -9.388   -94.922  29.398  1.00 100.43 ? 56  ALA L CB  1 
ATOM   11852 N N   . THR H 4 57  ? -11.883  -93.471  28.640  1.00 106.75 ? 57  THR L N   1 
ATOM   11853 C CA  . THR H 4 57  ? -13.328  -93.231  28.639  1.00 109.13 ? 57  THR L CA  1 
ATOM   11854 C C   . THR H 4 57  ? -13.990  -93.829  29.899  1.00 112.38 ? 57  THR L C   1 
ATOM   11855 O O   . THR H 4 57  ? -14.245  -95.035  29.958  1.00 111.09 ? 57  THR L O   1 
ATOM   11856 C CB  . THR H 4 57  ? -13.940  -93.757  27.309  1.00 119.41 ? 57  THR L CB  1 
ATOM   11857 O OG1 . THR H 4 57  ? -13.049  -93.522  26.208  1.00 117.51 ? 57  THR L OG1 1 
ATOM   11858 C CG2 . THR H 4 57  ? -15.298  -93.155  27.011  1.00 122.75 ? 57  THR L CG2 1 
ATOM   11859 N N   . GLY H 4 58  ? -14.228  -92.976  30.893  1.00 110.13 ? 58  GLY L N   1 
ATOM   11860 C CA  . GLY H 4 58  ? -14.856  -93.359  32.154  1.00 110.24 ? 58  GLY L CA  1 
ATOM   11861 C C   . GLY H 4 58  ? -13.911  -93.978  33.164  1.00 112.54 ? 58  GLY L C   1 
ATOM   11862 O O   . GLY H 4 58  ? -14.134  -95.105  33.617  1.00 110.84 ? 58  GLY L O   1 
ATOM   11863 N N   . ILE H 4 59  ? -12.846  -93.234  33.523  1.00 109.20 ? 59  ILE L N   1 
ATOM   11864 C CA  . ILE H 4 59  ? -11.814  -93.625  34.495  1.00 107.14 ? 59  ILE L CA  1 
ATOM   11865 C C   . ILE H 4 59  ? -11.640  -92.472  35.514  1.00 115.34 ? 59  ILE L C   1 
ATOM   11866 O O   . ILE H 4 59  ? -11.555  -91.317  35.087  1.00 116.74 ? 59  ILE L O   1 
ATOM   11867 C CB  . ILE H 4 59  ? -10.481  -94.012  33.770  1.00 108.13 ? 59  ILE L CB  1 
ATOM   11868 C CG1 . ILE H 4 59  ? -10.641  -95.271  32.862  1.00 107.83 ? 59  ILE L CG1 1 
ATOM   11869 C CG2 . ILE H 4 59  ? -9.284   -94.155  34.725  1.00 107.06 ? 59  ILE L CG2 1 
ATOM   11870 C CD1 . ILE H 4 59  ? -11.049  -96.650  33.528  1.00 112.90 ? 59  ILE L CD1 1 
ATOM   11871 N N   . PRO H 4 60  ? -11.600  -92.748  36.846  1.00 113.68 ? 60  PRO L N   1 
ATOM   11872 C CA  . PRO H 4 60  ? -11.471  -91.649  37.826  1.00 115.88 ? 60  PRO L CA  1 
ATOM   11873 C C   . PRO H 4 60  ? -10.149  -90.874  37.794  1.00 122.19 ? 60  PRO L C   1 
ATOM   11874 O O   . PRO H 4 60  ? -9.142   -91.378  37.293  1.00 120.51 ? 60  PRO L O   1 
ATOM   11875 C CB  . PRO H 4 60  ? -11.687  -92.347  39.171  1.00 117.22 ? 60  PRO L CB  1 
ATOM   11876 C CG  . PRO H 4 60  ? -11.312  -93.749  38.927  1.00 119.05 ? 60  PRO L CG  1 
ATOM   11877 C CD  . PRO H 4 60  ? -11.718  -94.054  37.525  1.00 114.07 ? 60  PRO L CD  1 
ATOM   11878 N N   . ASP H 4 61  ? -10.171  -89.645  38.361  1.00 122.07 ? 61  ASP L N   1 
ATOM   11879 C CA  . ASP H 4 61  ? -9.067   -88.679  38.463  1.00 122.90 ? 61  ASP L CA  1 
ATOM   11880 C C   . ASP H 4 61  ? -7.783   -89.207  39.112  1.00 125.85 ? 61  ASP L C   1 
ATOM   11881 O O   . ASP H 4 61  ? -6.703   -88.693  38.809  1.00 125.77 ? 61  ASP L O   1 
ATOM   11882 C CB  . ASP H 4 61  ? -9.541   -87.416  39.203  1.00 128.02 ? 61  ASP L CB  1 
ATOM   11883 C CG  . ASP H 4 61  ? -10.498  -86.542  38.409  1.00 145.49 ? 61  ASP L CG  1 
ATOM   11884 O OD1 . ASP H 4 61  ? -11.441  -87.096  37.790  1.00 146.72 ? 61  ASP L OD1 1 
ATOM   11885 O OD2 . ASP H 4 61  ? -10.323  -85.303  38.428  1.00 155.53 ? 61  ASP L OD2 1 
ATOM   11886 N N   . ARG H 4 62  ? -7.904   -90.209  40.012  1.00 121.58 ? 62  ARG L N   1 
ATOM   11887 C CA  . ARG H 4 62  ? -6.789   -90.831  40.734  1.00 120.84 ? 62  ARG L CA  1 
ATOM   11888 C C   . ARG H 4 62  ? -5.767   -91.494  39.803  1.00 124.60 ? 62  ARG L C   1 
ATOM   11889 O O   . ARG H 4 62  ? -4.573   -91.362  40.050  1.00 125.00 ? 62  ARG L O   1 
ATOM   11890 C CB  . ARG H 4 62  ? -7.280   -91.801  41.831  1.00 118.57 ? 62  ARG L CB  1 
ATOM   11891 C CG  . ARG H 4 62  ? -8.257   -92.886  41.379  1.00 119.46 ? 62  ARG L CG  1 
ATOM   11892 C CD  . ARG H 4 62  ? -9.020   -93.442  42.560  1.00 120.99 ? 62  ARG L CD  1 
ATOM   11893 N NE  . ARG H 4 62  ? -9.733   -94.681  42.240  1.00 122.48 ? 62  ARG L NE  1 
ATOM   11894 C CZ  . ARG H 4 62  ? -11.058  -94.807  42.215  1.00 135.81 ? 62  ARG L CZ  1 
ATOM   11895 N NH1 . ARG H 4 62  ? -11.837  -93.762  42.466  1.00 126.56 ? 62  ARG L NH1 1 
ATOM   11896 N NH2 . ARG H 4 62  ? -11.613  -95.976  41.926  1.00 119.17 ? 62  ARG L NH2 1 
ATOM   11897 N N   . PHE H 4 63  ? -6.230   -92.162  38.727  1.00 120.63 ? 63  PHE L N   1 
ATOM   11898 C CA  . PHE H 4 63  ? -5.392   -92.830  37.731  1.00 120.29 ? 63  PHE L CA  1 
ATOM   11899 C C   . PHE H 4 63  ? -4.758   -91.819  36.767  1.00 127.05 ? 63  PHE L C   1 
ATOM   11900 O O   . PHE H 4 63  ? -5.482   -91.079  36.095  1.00 127.53 ? 63  PHE L O   1 
ATOM   11901 C CB  . PHE H 4 63  ? -6.218   -93.867  36.950  1.00 120.86 ? 63  PHE L CB  1 
ATOM   11902 C CG  . PHE H 4 63  ? -6.697   -95.056  37.753  1.00 121.51 ? 63  PHE L CG  1 
ATOM   11903 C CD1 . PHE H 4 63  ? -5.912   -96.197  37.874  1.00 123.86 ? 63  PHE L CD1 1 
ATOM   11904 C CD2 . PHE H 4 63  ? -7.954   -95.056  38.344  1.00 123.75 ? 63  PHE L CD2 1 
ATOM   11905 C CE1 . PHE H 4 63  ? -6.361   -97.305  38.599  1.00 124.01 ? 63  PHE L CE1 1 
ATOM   11906 C CE2 . PHE H 4 63  ? -8.403   -96.166  39.071  1.00 125.95 ? 63  PHE L CE2 1 
ATOM   11907 C CZ  . PHE H 4 63  ? -7.604   -97.284  39.190  1.00 123.14 ? 63  PHE L CZ  1 
ATOM   11908 N N   . SER H 4 64  ? -3.409   -91.792  36.696  1.00 125.13 ? 64  SER L N   1 
ATOM   11909 C CA  . SER H 4 64  ? -2.646   -90.879  35.825  1.00 126.14 ? 64  SER L CA  1 
ATOM   11910 C C   . SER H 4 64  ? -1.442   -91.552  35.154  1.00 130.88 ? 64  SER L C   1 
ATOM   11911 O O   . SER H 4 64  ? -0.807   -92.417  35.756  1.00 131.65 ? 64  SER L O   1 
ATOM   11912 C CB  . SER H 4 64  ? -2.183   -89.652  36.607  1.00 131.91 ? 64  SER L CB  1 
ATOM   11913 O OG  . SER H 4 64  ? -1.337   -89.998  37.693  1.00 143.35 ? 64  SER L OG  1 
ATOM   11914 N N   . GLY H 4 65  ? -1.104   -91.106  33.949  1.00 127.51 ? 65  GLY L N   1 
ATOM   11915 C CA  . GLY H 4 65  ? 0.020    -91.645  33.188  1.00 128.20 ? 65  GLY L CA  1 
ATOM   11916 C C   . GLY H 4 65  ? 1.152    -90.660  32.984  1.00 133.52 ? 65  GLY L C   1 
ATOM   11917 O O   . GLY H 4 65  ? 0.912    -89.497  32.647  1.00 133.29 ? 65  GLY L O   1 
ATOM   11918 N N   . LYS H 4 66  ? 2.399    -91.122  33.182  1.00 131.53 ? 66  LYS L N   1 
ATOM   11919 C CA  . LYS H 4 66  ? 3.614    -90.308  33.031  1.00 133.23 ? 66  LYS L CA  1 
ATOM   11920 C C   . LYS H 4 66  ? 4.667    -91.062  32.208  1.00 138.61 ? 66  LYS L C   1 
ATOM   11921 O O   . LYS H 4 66  ? 4.670    -92.290  32.218  1.00 138.35 ? 66  LYS L O   1 
ATOM   11922 C CB  . LYS H 4 66  ? 4.209    -89.968  34.415  1.00 137.58 ? 66  LYS L CB  1 
ATOM   11923 C CG  . LYS H 4 66  ? 3.318    -89.142  35.343  1.00 149.21 ? 66  LYS L CG  1 
ATOM   11924 C CD  . LYS H 4 66  ? 4.050    -88.783  36.636  1.00 160.74 ? 66  LYS L CD  1 
ATOM   11925 C CE  . LYS H 4 66  ? 3.293    -87.776  37.469  1.00 169.44 ? 66  LYS L CE  1 
ATOM   11926 N NZ  . LYS H 4 66  ? 4.147    -87.163  38.524  1.00 178.69 ? 66  LYS L NZ  1 
ATOM   11927 N N   . THR H 4 67  ? 5.547    -90.339  31.482  1.00 137.10 ? 67  THR L N   1 
ATOM   11928 C CA  . THR H 4 67  ? 6.645    -90.930  30.691  1.00 139.96 ? 67  THR L CA  1 
ATOM   11929 C C   . THR H 4 67  ? 7.764    -89.915  30.447  1.00 147.44 ? 67  THR L C   1 
ATOM   11930 O O   . THR H 4 67  ? 7.487    -88.764  30.090  1.00 146.46 ? 67  THR L O   1 
ATOM   11931 C CB  . THR H 4 67  ? 6.188    -91.545  29.341  1.00 146.29 ? 67  THR L CB  1 
ATOM   11932 O OG1 . THR H 4 67  ? 4.830    -91.967  29.395  1.00 144.74 ? 67  THR L OG1 1 
ATOM   11933 C CG2 . THR H 4 67  ? 7.066    -92.711  28.904  1.00 146.06 ? 67  THR L CG2 1 
ATOM   11934 N N   . SER H 4 68  ? 9.028    -90.358  30.616  1.00 147.30 ? 68  SER L N   1 
ATOM   11935 C CA  . SER H 4 68  ? 10.245   -89.567  30.401  1.00 149.88 ? 68  SER L CA  1 
ATOM   11936 C C   . SER H 4 68  ? 11.442   -90.504  30.250  1.00 158.92 ? 68  SER L C   1 
ATOM   11937 O O   . SER H 4 68  ? 11.839   -91.164  31.211  1.00 160.50 ? 68  SER L O   1 
ATOM   11938 C CB  . SER H 4 68  ? 10.471   -88.579  31.542  1.00 153.22 ? 68  SER L CB  1 
ATOM   11939 O OG  . SER H 4 68  ? 10.457   -89.249  32.791  1.00 162.75 ? 68  SER L OG  1 
ATOM   11940 N N   . GLY H 4 69  ? 11.973   -90.575  29.032  1.00 158.24 ? 69  GLY L N   1 
ATOM   11941 C CA  . GLY H 4 69  ? 13.102   -91.433  28.686  1.00 163.21 ? 69  GLY L CA  1 
ATOM   11942 C C   . GLY H 4 69  ? 12.677   -92.832  28.286  1.00 168.03 ? 69  GLY L C   1 
ATOM   11943 O O   . GLY H 4 69  ? 12.402   -93.090  27.109  1.00 167.18 ? 69  GLY L O   1 
ATOM   11944 N N   . THR H 4 70  ? 12.635   -93.752  29.271  1.00 165.81 ? 70  THR L N   1 
ATOM   11945 C CA  . THR H 4 70  ? 12.240   -95.157  29.087  1.00 165.85 ? 70  THR L CA  1 
ATOM   11946 C C   . THR H 4 70  ? 11.515   -95.707  30.338  1.00 166.76 ? 70  THR L C   1 
ATOM   11947 O O   . THR H 4 70  ? 11.212   -96.899  30.395  1.00 167.35 ? 70  THR L O   1 
ATOM   11948 C CB  . THR H 4 70  ? 13.465   -96.043  28.727  1.00 179.68 ? 70  THR L CB  1 
ATOM   11949 O OG1 . THR H 4 70  ? 14.617   -95.251  28.422  1.00 181.84 ? 70  THR L OG1 1 
ATOM   11950 C CG2 . THR H 4 70  ? 13.171   -97.016  27.594  1.00 178.58 ? 70  THR L CG2 1 
ATOM   11951 N N   . ASP H 4 71  ? 11.212   -94.835  31.315  1.00 160.06 ? 71  ASP L N   1 
ATOM   11952 C CA  . ASP H 4 71  ? 10.620   -95.203  32.600  1.00 158.05 ? 71  ASP L CA  1 
ATOM   11953 C C   . ASP H 4 71  ? 9.134    -95.625  32.548  1.00 155.78 ? 71  ASP L C   1 
ATOM   11954 O O   . ASP H 4 71  ? 8.846    -96.741  32.980  1.00 155.73 ? 71  ASP L O   1 
ATOM   11955 C CB  . ASP H 4 71  ? 10.853   -94.089  33.621  1.00 160.43 ? 71  ASP L CB  1 
ATOM   11956 C CG  . ASP H 4 71  ? 12.334   -93.862  33.866  1.00 176.39 ? 71  ASP L CG  1 
ATOM   11957 O OD1 . ASP H 4 71  ? 12.882   -94.485  34.797  1.00 181.35 ? 71  ASP L OD1 1 
ATOM   11958 O OD2 . ASP H 4 71  ? 12.963   -93.131  33.067  1.00 181.70 ? 71  ASP L OD2 1 
ATOM   11959 N N   . PHE H 4 72  ? 8.208    -94.754  32.060  1.00 147.22 ? 72  PHE L N   1 
ATOM   11960 C CA  . PHE H 4 72  ? 6.751    -94.994  31.930  1.00 142.37 ? 72  PHE L CA  1 
ATOM   11961 C C   . PHE H 4 72  ? 6.043    -95.390  33.259  1.00 140.45 ? 72  PHE L C   1 
ATOM   11962 O O   . PHE H 4 72  ? 6.212    -96.510  33.752  1.00 140.67 ? 72  PHE L O   1 
ATOM   11963 C CB  . PHE H 4 72  ? 6.463    -96.008  30.812  1.00 145.08 ? 72  PHE L CB  1 
ATOM   11964 C CG  . PHE H 4 72  ? 5.015    -96.182  30.418  1.00 144.54 ? 72  PHE L CG  1 
ATOM   11965 C CD1 . PHE H 4 72  ? 4.192    -95.078  30.216  1.00 146.21 ? 72  PHE L CD1 1 
ATOM   11966 C CD2 . PHE H 4 72  ? 4.494    -97.447  30.170  1.00 147.39 ? 72  PHE L CD2 1 
ATOM   11967 C CE1 . PHE H 4 72  ? 2.859    -95.241  29.825  1.00 145.11 ? 72  PHE L CE1 1 
ATOM   11968 C CE2 . PHE H 4 72  ? 3.164    -97.611  29.772  1.00 147.89 ? 72  PHE L CE2 1 
ATOM   11969 C CZ  . PHE H 4 72  ? 2.359    -96.506  29.592  1.00 144.05 ? 72  PHE L CZ  1 
ATOM   11970 N N   . THR H 4 73  ? 5.213    -94.464  33.800  1.00 132.03 ? 73  THR L N   1 
ATOM   11971 C CA  . THR H 4 73  ? 4.533    -94.574  35.098  1.00 129.32 ? 73  THR L CA  1 
ATOM   11972 C C   . THR H 4 73  ? 3.002    -94.488  35.094  1.00 126.73 ? 73  THR L C   1 
ATOM   11973 O O   . THR H 4 73  ? 2.414    -93.691  34.366  1.00 123.64 ? 73  THR L O   1 
ATOM   11974 C CB  . THR H 4 73  ? 5.083    -93.490  36.048  1.00 140.10 ? 73  THR L CB  1 
ATOM   11975 O OG1 . THR H 4 73  ? 6.487    -93.330  35.848  1.00 144.29 ? 73  THR L OG1 1 
ATOM   11976 C CG2 . THR H 4 73  ? 4.815    -93.790  37.509  1.00 139.88 ? 73  THR L CG2 1 
ATOM   11977 N N   . LEU H 4 74  ? 2.381    -95.278  35.990  1.00 122.34 ? 74  LEU L N   1 
ATOM   11978 C CA  . LEU H 4 74  ? 0.949    -95.326  36.295  1.00 119.71 ? 74  LEU L CA  1 
ATOM   11979 C C   . LEU H 4 74  ? 0.839    -95.019  37.791  1.00 123.59 ? 74  LEU L C   1 
ATOM   11980 O O   . LEU H 4 74  ? 1.214    -95.851  38.623  1.00 123.87 ? 74  LEU L O   1 
ATOM   11981 C CB  . LEU H 4 74  ? 0.350    -96.726  35.982  1.00 118.67 ? 74  LEU L CB  1 
ATOM   11982 C CG  . LEU H 4 74  ? -1.196   -96.946  35.970  1.00 120.53 ? 74  LEU L CG  1 
ATOM   11983 C CD1 . LEU H 4 74  ? -1.796   -97.008  37.368  1.00 120.13 ? 74  LEU L CD1 1 
ATOM   11984 C CD2 . LEU H 4 74  ? -1.923   -95.972  35.067  1.00 121.29 ? 74  LEU L CD2 1 
ATOM   11985 N N   . THR H 4 75  ? 0.348    -93.820  38.126  1.00 120.04 ? 75  THR L N   1 
ATOM   11986 C CA  . THR H 4 75  ? 0.216    -93.365  39.510  1.00 121.10 ? 75  THR L CA  1 
ATOM   11987 C C   . THR H 4 75  ? -1.243   -93.223  39.950  1.00 124.41 ? 75  THR L C   1 
ATOM   11988 O O   . THR H 4 75  ? -2.049   -92.633  39.230  1.00 123.77 ? 75  THR L O   1 
ATOM   11989 C CB  . THR H 4 75  ? 1.024    -92.070  39.733  1.00 130.74 ? 75  THR L CB  1 
ATOM   11990 O OG1 . THR H 4 75  ? 2.282    -92.155  39.055  1.00 132.34 ? 75  THR L OG1 1 
ATOM   11991 C CG2 . THR H 4 75  ? 1.255    -91.768  41.210  1.00 131.20 ? 75  THR L CG2 1 
ATOM   11992 N N   . ILE H 4 76  ? -1.571   -93.762  41.140  1.00 112.58 ? 76  ILE L N   1 
ATOM   11993 C CA  . ILE H 4 76  ? -2.903   -93.679  41.751  1.00 112.59 ? 76  ILE L CA  1 
ATOM   11994 C C   . ILE H 4 76  ? -2.749   -92.979  43.102  1.00 121.05 ? 76  ILE L C   1 
ATOM   11995 O O   . ILE H 4 76  ? -1.904   -93.391  43.901  1.00 121.80 ? 76  ILE L O   1 
ATOM   11996 C CB  . ILE H 4 76  ? -3.595   -95.066  41.903  1.00 113.44 ? 76  ILE L CB  1 
ATOM   11997 C CG1 . ILE H 4 76  ? -3.489   -95.913  40.621  1.00 111.01 ? 76  ILE L CG1 1 
ATOM   11998 C CG2 . ILE H 4 76  ? -5.057   -94.901  42.345  1.00 114.35 ? 76  ILE L CG2 1 
ATOM   11999 C CD1 . ILE H 4 76  ? -3.377   -97.377  40.870  1.00 111.11 ? 76  ILE L CD1 1 
ATOM   12000 N N   . SER H 4 77  ? -3.549   -91.927  43.357  1.00 120.16 ? 77  SER L N   1 
ATOM   12001 C CA  . SER H 4 77  ? -3.488   -91.183  44.623  1.00 123.50 ? 77  SER L CA  1 
ATOM   12002 C C   . SER H 4 77  ? -4.105   -91.981  45.789  1.00 126.42 ? 77  SER L C   1 
ATOM   12003 O O   . SER H 4 77  ? -3.403   -92.289  46.756  1.00 127.41 ? 77  SER L O   1 
ATOM   12004 C CB  . SER H 4 77  ? -4.130   -89.804  44.482  1.00 130.38 ? 77  SER L CB  1 
ATOM   12005 O OG  . SER H 4 77  ? -5.437   -89.877  43.934  1.00 141.50 ? 77  SER L OG  1 
ATOM   12006 N N   . ARG H 4 78  ? -5.401   -92.343  45.672  1.00 120.45 ? 78  ARG L N   1 
ATOM   12007 C CA  . ARG H 4 78  ? -6.135   -93.120  46.674  1.00 119.18 ? 78  ARG L CA  1 
ATOM   12008 C C   . ARG H 4 78  ? -6.449   -94.506  46.108  1.00 117.51 ? 78  ARG L C   1 
ATOM   12009 O O   . ARG H 4 78  ? -7.141   -94.612  45.092  1.00 114.90 ? 78  ARG L O   1 
ATOM   12010 C CB  . ARG H 4 78  ? -7.441   -92.404  47.085  1.00 120.69 ? 78  ARG L CB  1 
ATOM   12011 C CG  . ARG H 4 78  ? -7.259   -91.160  47.947  1.00 134.41 ? 78  ARG L CG  1 
ATOM   12012 C CD  . ARG H 4 78  ? -8.600   -90.537  48.274  1.00 147.53 ? 78  ARG L CD  1 
ATOM   12013 N NE  . ARG H 4 78  ? -8.465   -89.283  49.016  1.00 164.90 ? 78  ARG L NE  1 
ATOM   12014 C CZ  . ARG H 4 78  ? -9.487   -88.548  49.446  1.00 180.95 ? 78  ARG L CZ  1 
ATOM   12015 N NH1 . ARG H 4 78  ? -10.736  -88.940  49.224  1.00 166.29 ? 78  ARG L NH1 1 
ATOM   12016 N NH2 . ARG H 4 78  ? -9.268   -87.416  50.101  1.00 168.87 ? 78  ARG L NH2 1 
ATOM   12017 N N   . LEU H 4 79  ? -5.920   -95.564  46.745  1.00 112.52 ? 79  LEU L N   1 
ATOM   12018 C CA  . LEU H 4 79  ? -6.182   -96.931  46.307  1.00 109.43 ? 79  LEU L CA  1 
ATOM   12019 C C   . LEU H 4 79  ? -7.491   -97.405  46.909  1.00 113.34 ? 79  LEU L C   1 
ATOM   12020 O O   . LEU H 4 79  ? -7.562   -97.680  48.107  1.00 114.44 ? 79  LEU L O   1 
ATOM   12021 C CB  . LEU H 4 79  ? -5.034   -97.879  46.670  1.00 109.17 ? 79  LEU L CB  1 
ATOM   12022 C CG  . LEU H 4 79  ? -3.865   -97.889  45.710  1.00 113.39 ? 79  LEU L CG  1 
ATOM   12023 C CD1 . LEU H 4 79  ? -2.598   -98.192  46.434  1.00 115.25 ? 79  LEU L CD1 1 
ATOM   12024 C CD2 . LEU H 4 79  ? -4.077   -98.883  44.588  1.00 113.04 ? 79  LEU L CD2 1 
ATOM   12025 N N   . GLU H 4 80  ? -8.541   -97.442  46.089  1.00 108.98 ? 80  GLU L N   1 
ATOM   12026 C CA  . GLU H 4 80  ? -9.865   -97.886  46.520  1.00 109.15 ? 80  GLU L CA  1 
ATOM   12027 C C   . GLU H 4 80  ? -9.905   -99.430  46.505  1.00 110.84 ? 80  GLU L C   1 
ATOM   12028 O O   . GLU H 4 80  ? -9.070   -100.019 45.818  1.00 110.28 ? 80  GLU L O   1 
ATOM   12029 C CB  . GLU H 4 80  ? -10.953  -97.280  45.612  1.00 111.26 ? 80  GLU L CB  1 
ATOM   12030 C CG  . GLU H 4 80  ? -11.048  -95.759  45.671  1.00 124.98 ? 80  GLU L CG  1 
ATOM   12031 C CD  . GLU H 4 80  ? -11.575  -95.142  46.957  1.00 145.27 ? 80  GLU L CD  1 
ATOM   12032 O OE1 . GLU H 4 80  ? -12.671  -95.545  47.410  1.00 135.15 ? 80  GLU L OE1 1 
ATOM   12033 O OE2 . GLU H 4 80  ? -10.911  -94.222  47.489  1.00 137.43 ? 80  GLU L OE2 1 
ATOM   12034 N N   . PRO H 4 81  ? -10.828  -100.121 47.230  1.00 106.14 ? 81  PRO L N   1 
ATOM   12035 C CA  . PRO H 4 81  ? -10.827  -101.599 47.206  1.00 104.83 ? 81  PRO L CA  1 
ATOM   12036 C C   . PRO H 4 81  ? -10.909  -102.213 45.810  1.00 109.53 ? 81  PRO L C   1 
ATOM   12037 O O   . PRO H 4 81  ? -10.406  -103.314 45.586  1.00 109.14 ? 81  PRO L O   1 
ATOM   12038 C CB  . PRO H 4 81  ? -12.059  -101.966 48.029  1.00 106.88 ? 81  PRO L CB  1 
ATOM   12039 C CG  . PRO H 4 81  ? -12.272  -100.816 48.915  1.00 112.79 ? 81  PRO L CG  1 
ATOM   12040 C CD  . PRO H 4 81  ? -11.887  -99.612  48.122  1.00 108.87 ? 81  PRO L CD  1 
ATOM   12041 N N   . GLU H 4 82  ? -11.530  -101.478 44.877  1.00 106.80 ? 82  GLU L N   1 
ATOM   12042 C CA  . GLU H 4 82  ? -11.731  -101.837 43.474  1.00 106.46 ? 82  GLU L CA  1 
ATOM   12043 C C   . GLU H 4 82  ? -10.407  -101.845 42.697  1.00 108.86 ? 82  GLU L C   1 
ATOM   12044 O O   . GLU H 4 82  ? -10.274  -102.607 41.741  1.00 109.03 ? 82  GLU L O   1 
ATOM   12045 C CB  . GLU H 4 82  ? -12.697  -100.834 42.806  1.00 109.60 ? 82  GLU L CB  1 
ATOM   12046 C CG  . GLU H 4 82  ? -13.960  -100.507 43.596  1.00 128.96 ? 82  GLU L CG  1 
ATOM   12047 C CD  . GLU H 4 82  ? -13.917  -99.264  44.473  1.00 159.99 ? 82  GLU L CD  1 
ATOM   12048 O OE1 . GLU H 4 82  ? -14.156  -99.396  45.695  1.00 159.65 ? 82  GLU L OE1 1 
ATOM   12049 O OE2 . GLU H 4 82  ? -13.696  -98.155  43.932  1.00 157.48 ? 82  GLU L OE2 1 
ATOM   12050 N N   . ASP H 4 83  ? -9.447   -100.973 43.094  1.00 103.90 ? 83  ASP L N   1 
ATOM   12051 C CA  . ASP H 4 83  ? -8.139   -100.776 42.457  1.00 102.59 ? 83  ASP L CA  1 
ATOM   12052 C C   . ASP H 4 83  ? -7.166   -101.949 42.620  1.00 105.76 ? 83  ASP L C   1 
ATOM   12053 O O   . ASP H 4 83  ? -6.196   -102.037 41.865  1.00 104.84 ? 83  ASP L O   1 
ATOM   12054 C CB  . ASP H 4 83  ? -7.487   -99.466  42.951  1.00 104.97 ? 83  ASP L CB  1 
ATOM   12055 C CG  . ASP H 4 83  ? -8.248   -98.177  42.666  1.00 117.81 ? 83  ASP L CG  1 
ATOM   12056 O OD1 . ASP H 4 83  ? -9.494   -98.204  42.677  1.00 118.82 ? 83  ASP L OD1 1 
ATOM   12057 O OD2 . ASP H 4 83  ? -7.596   -97.126  42.510  1.00 127.66 ? 83  ASP L OD2 1 
ATOM   12058 N N   . PHE H 4 84  ? -7.411   -102.843 43.592  1.00 103.00 ? 84  PHE L N   1 
ATOM   12059 C CA  . PHE H 4 84  ? -6.527   -103.981 43.843  1.00 103.54 ? 84  PHE L CA  1 
ATOM   12060 C C   . PHE H 4 84  ? -6.673   -105.063 42.774  1.00 109.44 ? 84  PHE L C   1 
ATOM   12061 O O   . PHE H 4 84  ? -7.543   -105.929 42.873  1.00 109.62 ? 84  PHE L O   1 
ATOM   12062 C CB  . PHE H 4 84  ? -6.700   -104.519 45.281  1.00 105.57 ? 84  PHE L CB  1 
ATOM   12063 C CG  . PHE H 4 84  ? -6.222   -103.527 46.316  1.00 108.08 ? 84  PHE L CG  1 
ATOM   12064 C CD1 . PHE H 4 84  ? -4.876   -103.445 46.656  1.00 112.03 ? 84  PHE L CD1 1 
ATOM   12065 C CD2 . PHE H 4 84  ? -7.109   -102.640 46.913  1.00 110.49 ? 84  PHE L CD2 1 
ATOM   12066 C CE1 . PHE H 4 84  ? -4.427   -102.497 47.578  1.00 114.41 ? 84  PHE L CE1 1 
ATOM   12067 C CE2 . PHE H 4 84  ? -6.658   -101.696 47.839  1.00 114.73 ? 84  PHE L CE2 1 
ATOM   12068 C CZ  . PHE H 4 84  ? -5.322   -101.636 48.170  1.00 113.97 ? 84  PHE L CZ  1 
ATOM   12069 N N   . ALA H 4 85  ? -5.845   -104.971 41.717  1.00 107.22 ? 85  ALA L N   1 
ATOM   12070 C CA  . ALA H 4 85  ? -5.858   -105.906 40.583  1.00 107.84 ? 85  ALA L CA  1 
ATOM   12071 C C   . ALA H 4 85  ? -4.479   -106.007 39.918  1.00 112.50 ? 85  ALA L C   1 
ATOM   12072 O O   . ALA H 4 85  ? -3.502   -105.481 40.460  1.00 112.26 ? 85  ALA L O   1 
ATOM   12073 C CB  . ALA H 4 85  ? -6.917   -105.489 39.562  1.00 108.50 ? 85  ALA L CB  1 
ATOM   12074 N N   . VAL H 4 86  ? -4.402   -106.710 38.764  1.00 109.39 ? 86  VAL L N   1 
ATOM   12075 C CA  . VAL H 4 86  ? -3.168   -106.902 38.002  1.00 110.10 ? 86  VAL L CA  1 
ATOM   12076 C C   . VAL H 4 86  ? -3.065   -105.780 36.973  1.00 114.02 ? 86  VAL L C   1 
ATOM   12077 O O   . VAL H 4 86  ? -4.018   -105.534 36.228  1.00 113.65 ? 86  VAL L O   1 
ATOM   12078 C CB  . VAL H 4 86  ? -3.066   -108.309 37.354  1.00 115.53 ? 86  VAL L CB  1 
ATOM   12079 C CG1 . VAL H 4 86  ? -1.651   -108.573 36.842  1.00 116.76 ? 86  VAL L CG1 1 
ATOM   12080 C CG2 . VAL H 4 86  ? -3.487   -109.404 38.327  1.00 115.79 ? 86  VAL L CG2 1 
ATOM   12081 N N   . TYR H 4 87  ? -1.912   -105.096 36.944  1.00 111.12 ? 87  TYR L N   1 
ATOM   12082 C CA  . TYR H 4 87  ? -1.674   -103.967 36.054  1.00 111.00 ? 87  TYR L CA  1 
ATOM   12083 C C   . TYR H 4 87  ? -0.664   -104.276 34.964  1.00 116.67 ? 87  TYR L C   1 
ATOM   12084 O O   . TYR H 4 87  ? 0.456    -104.702 35.255  1.00 118.35 ? 87  TYR L O   1 
ATOM   12085 C CB  . TYR H 4 87  ? -1.295   -102.716 36.861  1.00 111.99 ? 87  TYR L CB  1 
ATOM   12086 C CG  . TYR H 4 87  ? -2.501   -102.112 37.545  1.00 114.08 ? 87  TYR L CG  1 
ATOM   12087 C CD1 . TYR H 4 87  ? -2.997   -102.647 38.731  1.00 116.52 ? 87  TYR L CD1 1 
ATOM   12088 C CD2 . TYR H 4 87  ? -3.204   -101.063 36.961  1.00 114.62 ? 87  TYR L CD2 1 
ATOM   12089 C CE1 . TYR H 4 87  ? -4.144   -102.132 39.336  1.00 116.82 ? 87  TYR L CE1 1 
ATOM   12090 C CE2 . TYR H 4 87  ? -4.345   -100.531 37.564  1.00 115.33 ? 87  TYR L CE2 1 
ATOM   12091 C CZ  . TYR H 4 87  ? -4.808   -101.065 38.754  1.00 121.04 ? 87  TYR L CZ  1 
ATOM   12092 O OH  . TYR H 4 87  ? -5.931   -100.541 39.344  1.00 119.90 ? 87  TYR L OH  1 
ATOM   12093 N N   . TYR H 4 88  ? -1.076   -104.066 33.704  1.00 111.89 ? 88  TYR L N   1 
ATOM   12094 C CA  . TYR H 4 88  ? -0.265   -104.330 32.520  1.00 111.98 ? 88  TYR L CA  1 
ATOM   12095 C C   . TYR H 4 88  ? 0.032    -103.073 31.719  1.00 113.89 ? 88  TYR L C   1 
ATOM   12096 O O   . TYR H 4 88  ? -0.825   -102.202 31.598  1.00 111.80 ? 88  TYR L O   1 
ATOM   12097 C CB  . TYR H 4 88  ? -0.992   -105.328 31.596  1.00 114.07 ? 88  TYR L CB  1 
ATOM   12098 C CG  . TYR H 4 88  ? -1.007   -106.753 32.096  1.00 116.63 ? 88  TYR L CG  1 
ATOM   12099 C CD1 . TYR H 4 88  ? 0.064    -107.608 31.856  1.00 120.58 ? 88  TYR L CD1 1 
ATOM   12100 C CD2 . TYR H 4 88  ? -2.115   -107.265 32.760  1.00 116.96 ? 88  TYR L CD2 1 
ATOM   12101 C CE1 . TYR H 4 88  ? 0.049    -108.928 32.298  1.00 123.16 ? 88  TYR L CE1 1 
ATOM   12102 C CE2 . TYR H 4 88  ? -2.143   -108.583 33.205  1.00 119.27 ? 88  TYR L CE2 1 
ATOM   12103 C CZ  . TYR H 4 88  ? -1.054   -109.410 32.978  1.00 129.15 ? 88  TYR L CZ  1 
ATOM   12104 O OH  . TYR H 4 88  ? -1.063   -110.710 33.416  1.00 132.59 ? 88  TYR L OH  1 
ATOM   12105 N N   . CYS H 4 89  ? 1.230    -103.003 31.132  1.00 110.95 ? 89  CYS L N   1 
ATOM   12106 C CA  . CYS H 4 89  ? 1.590    -101.921 30.225  1.00 110.21 ? 89  CYS L CA  1 
ATOM   12107 C C   . CYS H 4 89  ? 1.673    -102.516 28.820  1.00 115.09 ? 89  CYS L C   1 
ATOM   12108 O O   . CYS H 4 89  ? 1.843    -103.727 28.682  1.00 115.70 ? 89  CYS L O   1 
ATOM   12109 C CB  . CYS H 4 89  ? 2.891    -101.234 30.636  1.00 110.63 ? 89  CYS L CB  1 
ATOM   12110 S SG  . CYS H 4 89  ? 4.337    -102.322 30.672  1.00 117.01 ? 89  CYS L SG  1 
ATOM   12111 N N   . GLN H 4 90  ? 1.515    -101.689 27.785  1.00 112.17 ? 90  GLN L N   1 
ATOM   12112 C CA  . GLN H 4 90  ? 1.580    -102.165 26.408  1.00 114.35 ? 90  GLN L CA  1 
ATOM   12113 C C   . GLN H 4 90  ? 2.123    -101.087 25.482  1.00 120.28 ? 90  GLN L C   1 
ATOM   12114 O O   . GLN H 4 90  ? 1.775    -99.917  25.634  1.00 118.81 ? 90  GLN L O   1 
ATOM   12115 C CB  . GLN H 4 90  ? 0.194    -102.635 25.939  1.00 116.48 ? 90  GLN L CB  1 
ATOM   12116 C CG  . GLN H 4 90  ? 0.167    -103.267 24.549  1.00 124.80 ? 90  GLN L CG  1 
ATOM   12117 C CD  . GLN H 4 90  ? -1.051   -102.874 23.754  1.00 130.39 ? 90  GLN L CD  1 
ATOM   12118 O OE1 . GLN H 4 90  ? -1.683   -101.836 23.985  1.00 119.67 ? 90  GLN L OE1 1 
ATOM   12119 N NE2 . GLN H 4 90  ? -1.379   -103.681 22.762  1.00 124.28 ? 90  GLN L NE2 1 
ATOM   12120 N N   . GLN H 4 91  ? 2.970    -101.488 24.525  1.00 119.62 ? 91  GLN L N   1 
ATOM   12121 C CA  . GLN H 4 91  ? 3.516    -100.591 23.512  1.00 119.92 ? 91  GLN L CA  1 
ATOM   12122 C C   . GLN H 4 91  ? 2.855    -100.901 22.167  1.00 128.35 ? 91  GLN L C   1 
ATOM   12123 O O   . GLN H 4 91  ? 2.584    -102.069 21.879  1.00 130.19 ? 91  GLN L O   1 
ATOM   12124 C CB  . GLN H 4 91  ? 5.054    -100.661 23.455  1.00 121.69 ? 91  GLN L CB  1 
ATOM   12125 C CG  . GLN H 4 91  ? 5.657    -102.018 23.076  1.00 129.79 ? 91  GLN L CG  1 
ATOM   12126 C CD  . GLN H 4 91  ? 5.805    -102.225 21.584  1.00 141.88 ? 91  GLN L CD  1 
ATOM   12127 O OE1 . GLN H 4 91  ? 5.774    -101.288 20.778  1.00 132.01 ? 91  GLN L OE1 1 
ATOM   12128 N NE2 . GLN H 4 91  ? 5.978    -103.469 21.181  1.00 140.51 ? 91  GLN L NE2 1 
ATOM   12129 N N   . CYS H 4 92  ? 2.562    -99.863  21.363  1.00 126.43 ? 92  CYS L N   1 
ATOM   12130 C CA  . CYS H 4 92  ? 1.901    -100.030 20.062  1.00 128.90 ? 92  CYS L CA  1 
ATOM   12131 C C   . CYS H 4 92  ? 2.728    -99.459  18.887  1.00 134.68 ? 92  CYS L C   1 
ATOM   12132 O O   . CYS H 4 92  ? 2.222    -99.355  17.761  1.00 135.61 ? 92  CYS L O   1 
ATOM   12133 C CB  . CYS H 4 92  ? 0.482    -99.470  20.091  1.00 129.02 ? 92  CYS L CB  1 
ATOM   12134 S SG  . CYS H 4 92  ? -0.522   -100.082 21.469  1.00 132.76 ? 92  CYS L SG  1 
ATOM   12135 N N   . GLY H 4 93  ? 4.000    -99.147  19.170  1.00 131.24 ? 93  GLY L N   1 
ATOM   12136 C CA  . GLY H 4 93  ? 4.985    -98.623  18.232  1.00 131.50 ? 93  GLY L CA  1 
ATOM   12137 C C   . GLY H 4 93  ? 5.498    -99.688  17.291  1.00 138.62 ? 93  GLY L C   1 
ATOM   12138 O O   . GLY H 4 93  ? 4.827    -99.955  16.287  1.00 140.30 ? 93  GLY L O   1 
ATOM   12139 N N   . ASN H 4 94  ? 6.654    -100.311 17.567  1.00 135.59 ? 94  ASN L N   1 
ATOM   12140 C CA  . ASN H 4 94  ? 7.132    -101.320 16.622  1.00 137.95 ? 94  ASN L CA  1 
ATOM   12141 C C   . ASN H 4 94  ? 6.395    -102.645 16.784  1.00 140.97 ? 94  ASN L C   1 
ATOM   12142 O O   . ASN H 4 94  ? 6.304    -103.176 17.891  1.00 138.97 ? 94  ASN L O   1 
ATOM   12143 C CB  . ASN H 4 94  ? 8.656    -101.482 16.663  1.00 141.78 ? 94  ASN L CB  1 
ATOM   12144 C CG  . ASN H 4 94  ? 9.241    -102.263 15.504  1.00 171.74 ? 94  ASN L CG  1 
ATOM   12145 O OD1 . ASN H 4 94  ? 9.621    -101.702 14.470  1.00 164.51 ? 94  ASN L OD1 1 
ATOM   12146 N ND2 . ASN H 4 94  ? 9.372    -103.570 15.667  1.00 168.75 ? 94  ASN L ND2 1 
ATOM   12147 N N   . SER H 4 95  ? 5.804    -103.127 15.675  1.00 135.12 ? 95  SER L N   1 
ATOM   12148 C CA  . SER H 4 95  ? 5.088    -104.398 15.627  1.00 134.96 ? 95  SER L CA  1 
ATOM   12149 C C   . SER H 4 95  ? 6.135    -105.518 15.803  1.00 141.64 ? 95  SER L C   1 
ATOM   12150 O O   . SER H 4 95  ? 7.227    -105.398 15.241  1.00 145.01 ? 95  SER L O   1 
ATOM   12151 C CB  . SER H 4 95  ? 4.333    -104.549 14.308  1.00 138.57 ? 95  SER L CB  1 
ATOM   12152 O OG  . SER H 4 95  ? 3.381    -105.601 14.359  1.00 144.48 ? 95  SER L OG  1 
ATOM   12153 N N   . PRO H 4 96  ? 5.891    -106.555 16.637  1.00 136.35 ? 96  PRO L N   1 
ATOM   12154 C CA  . PRO H 4 96  ? 4.652    -106.847 17.376  1.00 132.40 ? 96  PRO L CA  1 
ATOM   12155 C C   . PRO H 4 96  ? 4.466    -105.981 18.605  1.00 130.49 ? 96  PRO L C   1 
ATOM   12156 O O   . PRO H 4 96  ? 5.443    -105.543 19.217  1.00 130.07 ? 96  PRO L O   1 
ATOM   12157 C CB  . PRO H 4 96  ? 4.814    -108.325 17.752  1.00 135.71 ? 96  PRO L CB  1 
ATOM   12158 C CG  . PRO H 4 96  ? 6.294    -108.504 17.896  1.00 143.15 ? 96  PRO L CG  1 
ATOM   12159 C CD  . PRO H 4 96  ? 6.902    -107.614 16.842  1.00 140.72 ? 96  PRO L CD  1 
ATOM   12160 N N   . TRP H 4 97  ? 3.202    -105.736 18.949  1.00 122.70 ? 97  TRP L N   1 
ATOM   12161 C CA  . TRP H 4 97  ? 2.824    -104.991 20.135  1.00 119.52 ? 97  TRP L CA  1 
ATOM   12162 C C   . TRP H 4 97  ? 3.077    -105.932 21.303  1.00 122.52 ? 97  TRP L C   1 
ATOM   12163 O O   . TRP H 4 97  ? 2.662    -107.091 21.273  1.00 122.39 ? 97  TRP L O   1 
ATOM   12164 C CB  . TRP H 4 97  ? 1.344    -104.570 20.073  1.00 116.12 ? 97  TRP L CB  1 
ATOM   12165 C CG  . TRP H 4 97  ? 1.003    -103.571 18.999  1.00 116.90 ? 97  TRP L CG  1 
ATOM   12166 C CD1 . TRP H 4 97  ? 1.837    -103.070 18.040  1.00 121.47 ? 97  TRP L CD1 1 
ATOM   12167 C CD2 . TRP H 4 97  ? -0.278   -102.962 18.775  1.00 114.74 ? 97  TRP L CD2 1 
ATOM   12168 N NE1 . TRP H 4 97  ? 1.154    -102.192 17.232  1.00 120.16 ? 97  TRP L NE1 1 
ATOM   12169 C CE2 . TRP H 4 97  ? -0.147   -102.108 17.659  1.00 119.26 ? 97  TRP L CE2 1 
ATOM   12170 C CE3 . TRP H 4 97  ? -1.523   -103.045 19.416  1.00 113.84 ? 97  TRP L CE3 1 
ATOM   12171 C CZ2 . TRP H 4 97  ? -1.217   -101.355 17.164  1.00 116.82 ? 97  TRP L CZ2 1 
ATOM   12172 C CZ3 . TRP H 4 97  ? -2.581   -102.301 18.920  1.00 113.80 ? 97  TRP L CZ3 1 
ATOM   12173 C CH2 . TRP H 4 97  ? -2.420   -101.463 17.814  1.00 114.66 ? 97  TRP L CH2 1 
ATOM   12174 N N   . THR H 4 98  ? 3.834    -105.475 22.284  1.00 118.25 ? 98  THR L N   1 
ATOM   12175 C CA  . THR H 4 98  ? 4.168    -106.324 23.414  1.00 117.87 ? 98  THR L CA  1 
ATOM   12176 C C   . THR H 4 98  ? 3.531    -105.815 24.693  1.00 119.90 ? 98  THR L C   1 
ATOM   12177 O O   . THR H 4 98  ? 3.362    -104.610 24.873  1.00 117.86 ? 98  THR L O   1 
ATOM   12178 C CB  . THR H 4 98  ? 5.691    -106.525 23.516  1.00 126.79 ? 98  THR L CB  1 
ATOM   12179 O OG1 . THR H 4 98  ? 6.348    -105.266 23.377  1.00 125.22 ? 98  THR L OG1 1 
ATOM   12180 C CG2 . THR H 4 98  ? 6.232    -107.494 22.467  1.00 127.08 ? 98  THR L CG2 1 
ATOM   12181 N N   . PHE H 4 99  ? 3.138    -106.748 25.557  1.00 117.13 ? 99  PHE L N   1 
ATOM   12182 C CA  . PHE H 4 99  ? 2.553    -106.443 26.853  1.00 115.78 ? 99  PHE L CA  1 
ATOM   12183 C C   . PHE H 4 99  ? 3.613    -106.679 27.902  1.00 122.32 ? 99  PHE L C   1 
ATOM   12184 O O   . PHE H 4 99  ? 4.462    -107.561 27.747  1.00 122.85 ? 99  PHE L O   1 
ATOM   12185 C CB  . PHE H 4 99  ? 1.317    -107.318 27.133  1.00 116.62 ? 99  PHE L CB  1 
ATOM   12186 C CG  . PHE H 4 99  ? 0.090    -106.955 26.330  1.00 117.42 ? 99  PHE L CG  1 
ATOM   12187 C CD1 . PHE H 4 99  ? -0.847   -106.058 26.827  1.00 118.96 ? 99  PHE L CD1 1 
ATOM   12188 C CD2 . PHE H 4 99  ? -0.131   -107.515 25.075  1.00 120.70 ? 99  PHE L CD2 1 
ATOM   12189 C CE1 . PHE H 4 99  ? -1.977   -105.712 26.079  1.00 119.34 ? 99  PHE L CE1 1 
ATOM   12190 C CE2 . PHE H 4 99  ? -1.258   -107.167 24.326  1.00 122.80 ? 99  PHE L CE2 1 
ATOM   12191 C CZ  . PHE H 4 99  ? -2.173   -106.265 24.832  1.00 119.42 ? 99  PHE L CZ  1 
ATOM   12192 N N   . GLY H 4 100 ? 3.552    -105.891 28.964  1.00 120.70 ? 100 GLY L N   1 
ATOM   12193 C CA  . GLY H 4 100 ? 4.469    -105.992 30.089  1.00 122.00 ? 100 GLY L CA  1 
ATOM   12194 C C   . GLY H 4 100 ? 4.294    -107.269 30.887  1.00 128.67 ? 100 GLY L C   1 
ATOM   12195 O O   . GLY H 4 100 ? 3.412    -108.089 30.596  1.00 128.28 ? 100 GLY L O   1 
ATOM   12196 N N   . GLN H 4 101 ? 5.147    -107.436 31.906  1.00 126.55 ? 101 GLN L N   1 
ATOM   12197 C CA  . GLN H 4 101 ? 5.154    -108.608 32.779  1.00 126.58 ? 101 GLN L CA  1 
ATOM   12198 C C   . GLN H 4 101 ? 3.875    -108.687 33.635  1.00 127.94 ? 101 GLN L C   1 
ATOM   12199 O O   . GLN H 4 101 ? 3.251    -109.749 33.704  1.00 127.29 ? 101 GLN L O   1 
ATOM   12200 C CB  . GLN H 4 101 ? 6.440    -108.654 33.634  1.00 128.70 ? 101 GLN L CB  1 
ATOM   12201 C CG  . GLN H 4 101 ? 7.721    -108.373 32.831  1.00 152.66 ? 101 GLN L CG  1 
ATOM   12202 C CD  . GLN H 4 101 ? 8.966    -109.060 33.351  1.00 176.63 ? 101 GLN L CD  1 
ATOM   12203 O OE1 . GLN H 4 101 ? 9.647    -109.786 32.616  1.00 173.38 ? 101 GLN L OE1 1 
ATOM   12204 N NE2 . GLN H 4 101 ? 9.330    -108.809 34.608  1.00 168.70 ? 101 GLN L NE2 1 
ATOM   12205 N N   . GLY H 4 102 ? 3.478    -107.557 34.223  1.00 122.54 ? 102 GLY L N   1 
ATOM   12206 C CA  . GLY H 4 102 ? 2.281    -107.461 35.046  1.00 121.02 ? 102 GLY L CA  1 
ATOM   12207 C C   . GLY H 4 102 ? 2.571    -107.456 36.531  1.00 123.53 ? 102 GLY L C   1 
ATOM   12208 O O   . GLY H 4 102 ? 3.149    -108.417 37.057  1.00 123.01 ? 102 GLY L O   1 
ATOM   12209 N N   . THR H 4 103 ? 2.161    -106.357 37.208  1.00 119.07 ? 103 THR L N   1 
ATOM   12210 C CA  . THR H 4 103 ? 2.310    -106.141 38.652  1.00 118.49 ? 103 THR L CA  1 
ATOM   12211 C C   . THR H 4 103 ? 0.944    -106.275 39.328  1.00 121.58 ? 103 THR L C   1 
ATOM   12212 O O   . THR H 4 103 ? 0.014    -105.558 38.953  1.00 121.65 ? 103 THR L O   1 
ATOM   12213 C CB  . THR H 4 103 ? 2.925    -104.759 38.929  1.00 126.15 ? 103 THR L CB  1 
ATOM   12214 O OG1 . THR H 4 103 ? 4.071    -104.567 38.098  1.00 128.68 ? 103 THR L OG1 1 
ATOM   12215 C CG2 . THR H 4 103 ? 3.293    -104.558 40.398  1.00 123.69 ? 103 THR L CG2 1 
ATOM   12216 N N   . LYS H 4 104 ? 0.821    -107.191 40.313  1.00 117.00 ? 104 LYS L N   1 
ATOM   12217 C CA  . LYS H 4 104 ? -0.429   -107.383 41.054  1.00 116.55 ? 104 LYS L CA  1 
ATOM   12218 C C   . LYS H 4 104 ? -0.429   -106.468 42.257  1.00 119.43 ? 104 LYS L C   1 
ATOM   12219 O O   . LYS H 4 104 ? 0.538    -106.443 43.020  1.00 119.04 ? 104 LYS L O   1 
ATOM   12220 C CB  . LYS H 4 104 ? -0.627   -108.846 41.497  1.00 118.69 ? 104 LYS L CB  1 
ATOM   12221 C CG  . LYS H 4 104 ? -2.087   -109.220 41.778  1.00 131.69 ? 104 LYS L CG  1 
ATOM   12222 C CD  . LYS H 4 104 ? -2.478   -109.183 43.256  1.00 140.89 ? 104 LYS L CD  1 
ATOM   12223 C CE  . LYS H 4 104 ? -3.938   -109.538 43.435  1.00 151.08 ? 104 LYS L CE  1 
ATOM   12224 N NZ  . LYS H 4 104 ? -4.366   -109.497 44.860  1.00 159.83 ? 104 LYS L NZ  1 
ATOM   12225 N N   . VAL H 4 105 ? -1.506   -105.714 42.423  1.00 115.78 ? 105 VAL L N   1 
ATOM   12226 C CA  . VAL H 4 105 ? -1.643   -104.804 43.548  1.00 116.75 ? 105 VAL L CA  1 
ATOM   12227 C C   . VAL H 4 105 ? -2.491   -105.535 44.602  1.00 122.49 ? 105 VAL L C   1 
ATOM   12228 O O   . VAL H 4 105 ? -3.676   -105.794 44.372  1.00 122.98 ? 105 VAL L O   1 
ATOM   12229 C CB  . VAL H 4 105 ? -2.208   -103.425 43.106  1.00 121.17 ? 105 VAL L CB  1 
ATOM   12230 C CG1 . VAL H 4 105 ? -2.272   -102.452 44.276  1.00 123.00 ? 105 VAL L CG1 1 
ATOM   12231 C CG2 . VAL H 4 105 ? -1.371   -102.828 41.979  1.00 119.55 ? 105 VAL L CG2 1 
ATOM   12232 N N   . GLU H 4 106 ? -1.846   -105.948 45.714  1.00 119.31 ? 106 GLU L N   1 
ATOM   12233 C CA  . GLU H 4 106 ? -2.476   -106.688 46.818  1.00 120.06 ? 106 GLU L CA  1 
ATOM   12234 C C   . GLU H 4 106 ? -2.696   -105.836 48.068  1.00 125.96 ? 106 GLU L C   1 
ATOM   12235 O O   . GLU H 4 106 ? -1.938   -104.898 48.326  1.00 125.99 ? 106 GLU L O   1 
ATOM   12236 C CB  . GLU H 4 106 ? -1.709   -107.994 47.156  1.00 120.03 ? 106 GLU L CB  1 
ATOM   12237 C CG  . GLU H 4 106 ? -0.308   -107.830 47.741  1.00 129.17 ? 106 GLU L CG  1 
ATOM   12238 C CD  . GLU H 4 106 ? 0.397    -109.098 48.202  1.00 146.49 ? 106 GLU L CD  1 
ATOM   12239 O OE1 . GLU H 4 106 ? 0.314    -110.132 47.501  1.00 142.19 ? 106 GLU L OE1 1 
ATOM   12240 O OE2 . GLU H 4 106 ? 1.099    -109.035 49.236  1.00 140.71 ? 106 GLU L OE2 1 
ATOM   12241 N N   . ILE H 4 107 ? -3.735   -106.177 48.843  1.00 124.19 ? 107 ILE L N   1 
ATOM   12242 C CA  . ILE H 4 107 ? -4.088   -105.494 50.085  1.00 127.02 ? 107 ILE L CA  1 
ATOM   12243 C C   . ILE H 4 107 ? -3.033   -105.849 51.131  1.00 131.18 ? 107 ILE L C   1 
ATOM   12244 O O   . ILE H 4 107 ? -2.824   -107.029 51.424  1.00 129.78 ? 107 ILE L O   1 
ATOM   12245 C CB  . ILE H 4 107 ? -5.524   -105.862 50.550  1.00 132.52 ? 107 ILE L CB  1 
ATOM   12246 C CG1 . ILE H 4 107 ? -6.561   -105.668 49.421  1.00 133.32 ? 107 ILE L CG1 1 
ATOM   12247 C CG2 . ILE H 4 107 ? -5.918   -105.078 51.805  1.00 137.05 ? 107 ILE L CG2 1 
ATOM   12248 C CD1 . ILE H 4 107 ? -7.613   -106.781 49.333  1.00 142.57 ? 107 ILE L CD1 1 
ATOM   12249 N N   . LYS H 4 108 ? -2.337   -104.833 51.650  1.00 129.45 ? 108 LYS L N   1 
ATOM   12250 C CA  . LYS H 4 108 ? -1.307   -105.044 52.664  1.00 129.58 ? 108 LYS L CA  1 
ATOM   12251 C C   . LYS H 4 108 ? -1.966   -105.423 53.972  1.00 137.23 ? 108 LYS L C   1 
ATOM   12252 O O   . LYS H 4 108 ? -2.981   -104.836 54.355  1.00 139.86 ? 108 LYS L O   1 
ATOM   12253 C CB  . LYS H 4 108 ? -0.431   -103.789 52.861  1.00 132.62 ? 108 LYS L CB  1 
ATOM   12254 C CG  . LYS H 4 108 ? 1.070    -104.004 52.650  1.00 139.09 ? 108 LYS L CG  1 
ATOM   12255 C CD  . LYS H 4 108 ? 1.846    -104.407 53.902  1.00 144.14 ? 108 LYS L CD  1 
ATOM   12256 C CE  . LYS H 4 108 ? 3.331    -104.515 53.631  1.00 143.54 ? 108 LYS L CE  1 
ATOM   12257 N NZ  . LYS H 4 108 ? 3.693    -105.765 52.906  1.00 143.95 ? 108 LYS L NZ  1 
ATOM   12258 N N   . ARG H 4 109 ? -1.408   -106.433 54.630  1.00 118.90 ? 109 ARG L N   1 
ATOM   12259 C CA  . ARG H 4 109 ? -1.870   -106.911 55.932  1.00 119.03 ? 109 ARG L CA  1 
ATOM   12260 C C   . ARG H 4 109 ? -0.730   -107.543 56.765  1.00 122.87 ? 109 ARG L C   1 
ATOM   12261 O O   . ARG H 4 109 ? 0.387    -107.706 56.269  1.00 121.70 ? 109 ARG L O   1 
ATOM   12262 C CB  . ARG H 4 109 ? -3.092   -107.852 55.798  1.00 118.39 ? 109 ARG L CB  1 
ATOM   12263 C CG  . ARG H 4 109 ? -2.809   -109.208 55.158  1.00 121.42 ? 109 ARG L CG  1 
ATOM   12264 C CD  . ARG H 4 109 ? -3.742   -110.283 55.683  1.00 125.79 ? 109 ARG L CD  1 
ATOM   12265 N NE  . ARG H 4 109 ? -3.284   -110.829 56.962  1.00 131.31 ? 109 ARG L NE  1 
ATOM   12266 C CZ  . ARG H 4 109 ? -4.085   -111.346 57.889  1.00 146.61 ? 109 ARG L CZ  1 
ATOM   12267 N NH1 . ARG H 4 109 ? -5.399   -111.375 57.700  1.00 135.77 ? 109 ARG L NH1 1 
ATOM   12268 N NH2 . ARG H 4 109 ? -3.580   -111.821 59.021  1.00 133.11 ? 109 ARG L NH2 1 
ATOM   12269 N N   . THR H 4 110 ? -1.020   -107.884 58.029  1.00 120.03 ? 110 THR L N   1 
ATOM   12270 C CA  . THR H 4 110 ? -0.068   -108.515 58.942  1.00 118.65 ? 110 THR L CA  1 
ATOM   12271 C C   . THR H 4 110 ? 0.304    -109.903 58.442  1.00 121.83 ? 110 THR L C   1 
ATOM   12272 O O   . THR H 4 110 ? -0.528   -110.576 57.825  1.00 121.21 ? 110 THR L O   1 
ATOM   12273 C CB  . THR H 4 110 ? -0.645   -108.592 60.361  1.00 128.80 ? 110 THR L CB  1 
ATOM   12274 O OG1 . THR H 4 110 ? -1.965   -109.140 60.316  1.00 130.57 ? 110 THR L OG1 1 
ATOM   12275 C CG2 . THR H 4 110 ? -0.657   -107.245 61.067  1.00 129.25 ? 110 THR L CG2 1 
ATOM   12276 N N   . VAL H 4 111 ? 1.559    -110.321 58.702  1.00 118.17 ? 111 VAL L N   1 
ATOM   12277 C CA  . VAL H 4 111 ? 2.102    -111.631 58.314  1.00 116.83 ? 111 VAL L CA  1 
ATOM   12278 C C   . VAL H 4 111 ? 1.242    -112.716 58.955  1.00 121.37 ? 111 VAL L C   1 
ATOM   12279 O O   . VAL H 4 111 ? 1.074    -112.723 60.176  1.00 121.09 ? 111 VAL L O   1 
ATOM   12280 C CB  . VAL H 4 111 ? 3.608    -111.820 58.670  1.00 119.18 ? 111 VAL L CB  1 
ATOM   12281 C CG1 . VAL H 4 111 ? 4.278    -112.787 57.702  1.00 118.05 ? 111 VAL L CG1 1 
ATOM   12282 C CG2 . VAL H 4 111 ? 4.359    -110.491 58.703  1.00 119.59 ? 111 VAL L CG2 1 
ATOM   12283 N N   . ALA H 4 112 ? 0.640    -113.578 58.128  1.00 118.43 ? 112 ALA L N   1 
ATOM   12284 C CA  . ALA H 4 112 ? -0.223   -114.652 58.610  1.00 118.58 ? 112 ALA L CA  1 
ATOM   12285 C C   . ALA H 4 112 ? 0.379    -116.016 58.313  1.00 121.89 ? 112 ALA L C   1 
ATOM   12286 O O   . ALA H 4 112 ? 0.663    -116.321 57.158  1.00 121.49 ? 112 ALA L O   1 
ATOM   12287 C CB  . ALA H 4 112 ? -1.610   -114.533 57.991  1.00 120.57 ? 112 ALA L CB  1 
ATOM   12288 N N   . ALA H 4 113 ? 0.603    -116.822 59.360  1.00 118.43 ? 113 ALA L N   1 
ATOM   12289 C CA  . ALA H 4 113 ? 1.140    -118.176 59.236  1.00 118.12 ? 113 ALA L CA  1 
ATOM   12290 C C   . ALA H 4 113 ? 0.035    -119.099 58.698  1.00 123.78 ? 113 ALA L C   1 
ATOM   12291 O O   . ALA H 4 113 ? -1.131   -118.921 59.064  1.00 124.37 ? 113 ALA L O   1 
ATOM   12292 C CB  . ALA H 4 113 ? 1.628    -118.671 60.589  1.00 118.58 ? 113 ALA L CB  1 
ATOM   12293 N N   . PRO H 4 114 ? 0.345    -120.064 57.808  1.00 121.64 ? 114 PRO L N   1 
ATOM   12294 C CA  . PRO H 4 114 ? -0.726   -120.914 57.266  1.00 123.15 ? 114 PRO L CA  1 
ATOM   12295 C C   . PRO H 4 114 ? -1.285   -121.935 58.245  1.00 130.06 ? 114 PRO L C   1 
ATOM   12296 O O   . PRO H 4 114 ? -0.602   -122.356 59.177  1.00 128.60 ? 114 PRO L O   1 
ATOM   12297 C CB  . PRO H 4 114 ? -0.064   -121.591 56.065  1.00 124.74 ? 114 PRO L CB  1 
ATOM   12298 C CG  . PRO H 4 114 ? 1.371    -121.657 56.427  1.00 128.31 ? 114 PRO L CG  1 
ATOM   12299 C CD  . PRO H 4 114 ? 1.658    -120.416 57.229  1.00 122.95 ? 114 PRO L CD  1 
ATOM   12300 N N   . SER H 4 115 ? -2.545   -122.322 58.014  1.00 130.76 ? 115 SER L N   1 
ATOM   12301 C CA  . SER H 4 115 ? -3.257   -123.350 58.765  1.00 133.00 ? 115 SER L CA  1 
ATOM   12302 C C   . SER H 4 115 ? -3.036   -124.633 57.929  1.00 140.12 ? 115 SER L C   1 
ATOM   12303 O O   . SER H 4 115 ? -3.767   -124.888 56.959  1.00 140.40 ? 115 SER L O   1 
ATOM   12304 C CB  . SER H 4 115 ? -4.741   -122.998 58.894  1.00 137.79 ? 115 SER L CB  1 
ATOM   12305 O OG  . SER H 4 115 ? -4.973   -121.602 59.036  1.00 144.81 ? 115 SER L OG  1 
ATOM   12306 N N   . VAL H 4 116 ? -1.945   -125.374 58.251  1.00 137.85 ? 116 VAL L N   1 
ATOM   12307 C CA  . VAL H 4 116 ? -1.513   -126.572 57.516  1.00 138.56 ? 116 VAL L CA  1 
ATOM   12308 C C   . VAL H 4 116 ? -2.262   -127.831 57.976  1.00 146.95 ? 116 VAL L C   1 
ATOM   12309 O O   . VAL H 4 116 ? -2.295   -128.128 59.172  1.00 147.10 ? 116 VAL L O   1 
ATOM   12310 C CB  . VAL H 4 116 ? 0.034    -126.757 57.533  1.00 140.75 ? 116 VAL L CB  1 
ATOM   12311 C CG1 . VAL H 4 116 ? 0.463    -127.959 56.696  1.00 141.20 ? 116 VAL L CG1 1 
ATOM   12312 C CG2 . VAL H 4 116 ? 0.749    -125.497 57.052  1.00 139.05 ? 116 VAL L CG2 1 
ATOM   12313 N N   . PHE H 4 117 ? -2.858   -128.563 57.007  1.00 146.88 ? 117 PHE L N   1 
ATOM   12314 C CA  . PHE H 4 117 ? -3.603   -129.811 57.227  1.00 149.62 ? 117 PHE L CA  1 
ATOM   12315 C C   . PHE H 4 117 ? -3.262   -130.858 56.159  1.00 156.67 ? 117 PHE L C   1 
ATOM   12316 O O   . PHE H 4 117 ? -3.070   -130.502 54.993  1.00 155.93 ? 117 PHE L O   1 
ATOM   12317 C CB  . PHE H 4 117 ? -5.124   -129.560 57.221  1.00 152.35 ? 117 PHE L CB  1 
ATOM   12318 C CG  . PHE H 4 117 ? -5.611   -128.420 58.081  1.00 153.55 ? 117 PHE L CG  1 
ATOM   12319 C CD1 . PHE H 4 117 ? -6.044   -127.231 57.506  1.00 155.75 ? 117 PHE L CD1 1 
ATOM   12320 C CD2 . PHE H 4 117 ? -5.641   -128.535 59.466  1.00 156.64 ? 117 PHE L CD2 1 
ATOM   12321 C CE1 . PHE H 4 117 ? -6.503   -126.178 58.298  1.00 156.73 ? 117 PHE L CE1 1 
ATOM   12322 C CE2 . PHE H 4 117 ? -6.087   -127.475 60.260  1.00 159.44 ? 117 PHE L CE2 1 
ATOM   12323 C CZ  . PHE H 4 117 ? -6.517   -126.304 59.670  1.00 156.74 ? 117 PHE L CZ  1 
ATOM   12324 N N   . ILE H 4 118 ? -3.211   -132.147 56.553  1.00 155.98 ? 118 ILE L N   1 
ATOM   12325 C CA  . ILE H 4 118 ? -2.939   -133.262 55.637  1.00 157.40 ? 118 ILE L CA  1 
ATOM   12326 C C   . ILE H 4 118 ? -4.189   -134.161 55.537  1.00 164.68 ? 118 ILE L C   1 
ATOM   12327 O O   . ILE H 4 118 ? -4.778   -134.516 56.561  1.00 165.09 ? 118 ILE L O   1 
ATOM   12328 C CB  . ILE H 4 118 ? -1.602   -134.025 55.950  1.00 160.81 ? 118 ILE L CB  1 
ATOM   12329 C CG1 . ILE H 4 118 ? -1.259   -135.067 54.848  1.00 162.63 ? 118 ILE L CG1 1 
ATOM   12330 C CG2 . ILE H 4 118 ? -1.570   -134.642 57.365  1.00 162.26 ? 118 ILE L CG2 1 
ATOM   12331 C CD1 . ILE H 4 118 ? 0.244    -135.349 54.626  1.00 168.54 ? 118 ILE L CD1 1 
ATOM   12332 N N   . PHE H 4 119 ? -4.622   -134.459 54.297  1.00 163.49 ? 119 PHE L N   1 
ATOM   12333 C CA  . PHE H 4 119 ? -5.800   -135.283 54.040  1.00 166.12 ? 119 PHE L CA  1 
ATOM   12334 C C   . PHE H 4 119 ? -5.449   -136.664 53.493  1.00 172.92 ? 119 PHE L C   1 
ATOM   12335 O O   . PHE H 4 119 ? -4.858   -136.764 52.416  1.00 172.38 ? 119 PHE L O   1 
ATOM   12336 C CB  . PHE H 4 119 ? -6.814   -134.579 53.121  1.00 167.58 ? 119 PHE L CB  1 
ATOM   12337 C CG  . PHE H 4 119 ? -7.512   -133.392 53.735  1.00 168.37 ? 119 PHE L CG  1 
ATOM   12338 C CD1 . PHE H 4 119 ? -8.686   -133.552 54.462  1.00 173.01 ? 119 PHE L CD1 1 
ATOM   12339 C CD2 . PHE H 4 119 ? -7.002   -132.112 53.580  1.00 168.86 ? 119 PHE L CD2 1 
ATOM   12340 C CE1 . PHE H 4 119 ? -9.330   -132.450 55.029  1.00 173.51 ? 119 PHE L CE1 1 
ATOM   12341 C CE2 . PHE H 4 119 ? -7.653   -131.009 54.138  1.00 171.22 ? 119 PHE L CE2 1 
ATOM   12342 C CZ  . PHE H 4 119 ? -8.815   -131.185 54.856  1.00 170.76 ? 119 PHE L CZ  1 
ATOM   12343 N N   . PRO H 4 120 ? -5.842   -137.748 54.204  1.00 172.35 ? 120 PRO L N   1 
ATOM   12344 C CA  . PRO H 4 120 ? -5.562   -139.099 53.689  1.00 174.68 ? 120 PRO L CA  1 
ATOM   12345 C C   . PRO H 4 120 ? -6.447   -139.446 52.481  1.00 179.31 ? 120 PRO L C   1 
ATOM   12346 O O   . PRO H 4 120 ? -7.521   -138.849 52.346  1.00 178.05 ? 120 PRO L O   1 
ATOM   12347 C CB  . PRO H 4 120 ? -5.846   -139.999 54.896  1.00 178.79 ? 120 PRO L CB  1 
ATOM   12348 C CG  . PRO H 4 120 ? -6.841   -139.255 55.704  1.00 182.49 ? 120 PRO L CG  1 
ATOM   12349 C CD  . PRO H 4 120 ? -6.570   -137.795 55.492  1.00 174.88 ? 120 PRO L CD  1 
ATOM   12350 N N   . PRO H 4 121 ? -6.029   -140.374 51.577  1.00 177.94 ? 121 PRO L N   1 
ATOM   12351 C CA  . PRO H 4 121 ? -6.883   -140.702 50.421  1.00 178.92 ? 121 PRO L CA  1 
ATOM   12352 C C   . PRO H 4 121 ? -8.167   -141.415 50.821  1.00 185.36 ? 121 PRO L C   1 
ATOM   12353 O O   . PRO H 4 121 ? -8.171   -142.172 51.797  1.00 186.84 ? 121 PRO L O   1 
ATOM   12354 C CB  . PRO H 4 121 ? -6.005   -141.618 49.559  1.00 182.24 ? 121 PRO L CB  1 
ATOM   12355 C CG  . PRO H 4 121 ? -4.647   -141.562 50.137  1.00 186.07 ? 121 PRO L CG  1 
ATOM   12356 C CD  . PRO H 4 121 ? -4.792   -141.178 51.568  1.00 180.80 ? 121 PRO L CD  1 
ATOM   12357 N N   . SER H 4 122 ? -9.256   -141.168 50.068  1.00 181.78 ? 122 SER L N   1 
ATOM   12358 C CA  . SER H 4 122 ? -10.554  -141.796 50.315  1.00 183.47 ? 122 SER L CA  1 
ATOM   12359 C C   . SER H 4 122 ? -10.470  -143.292 50.029  1.00 190.31 ? 122 SER L C   1 
ATOM   12360 O O   . SER H 4 122 ? -9.731   -143.705 49.132  1.00 190.33 ? 122 SER L O   1 
ATOM   12361 C CB  . SER H 4 122 ? -11.633  -141.159 49.447  1.00 185.59 ? 122 SER L CB  1 
ATOM   12362 O OG  . SER H 4 122 ? -12.901  -141.748 49.685  1.00 194.88 ? 122 SER L OG  1 
ATOM   12363 N N   . ASP H 4 123 ? -11.226  -144.100 50.792  1.00 189.16 ? 123 ASP L N   1 
ATOM   12364 C CA  . ASP H 4 123 ? -11.261  -145.554 50.624  1.00 192.35 ? 123 ASP L CA  1 
ATOM   12365 C C   . ASP H 4 123 ? -11.983  -145.970 49.327  1.00 197.34 ? 123 ASP L C   1 
ATOM   12366 O O   . ASP H 4 123 ? -11.829  -147.108 48.880  1.00 199.12 ? 123 ASP L O   1 
ATOM   12367 C CB  . ASP H 4 123 ? -11.830  -146.242 51.875  1.00 196.62 ? 123 ASP L CB  1 
ATOM   12368 C CG  . ASP H 4 123 ? -10.968  -146.035 53.109  1.00 202.95 ? 123 ASP L CG  1 
ATOM   12369 O OD1 . ASP H 4 123 ? -9.923   -146.712 53.225  1.00 203.95 ? 123 ASP L OD1 1 
ATOM   12370 O OD2 . ASP H 4 123 ? -11.331  -145.187 53.950  1.00 206.22 ? 123 ASP L OD2 1 
ATOM   12371 N N   . GLU H 4 124 ? -12.732  -145.025 48.709  1.00 192.56 ? 124 GLU L N   1 
ATOM   12372 C CA  . GLU H 4 124 ? -13.421  -145.183 47.424  1.00 192.93 ? 124 GLU L CA  1 
ATOM   12373 C C   . GLU H 4 124 ? -12.383  -145.062 46.297  1.00 195.18 ? 124 GLU L C   1 
ATOM   12374 O O   . GLU H 4 124 ? -12.495  -145.745 45.276  1.00 196.18 ? 124 GLU L O   1 
ATOM   12375 C CB  . GLU H 4 124 ? -14.504  -144.102 47.252  1.00 192.39 ? 124 GLU L CB  1 
ATOM   12376 C CG  . GLU H 4 124 ? -15.846  -144.453 47.873  1.00 204.21 ? 124 GLU L CG  1 
ATOM   12377 C CD  . GLU H 4 124 ? -16.022  -144.143 49.348  1.00 220.15 ? 124 GLU L CD  1 
ATOM   12378 O OE1 . GLU H 4 124 ? -16.430  -145.062 50.095  1.00 217.92 ? 124 GLU L OE1 1 
ATOM   12379 O OE2 . GLU H 4 124 ? -15.804  -142.977 49.751  1.00 206.13 ? 124 GLU L OE2 1 
ATOM   12380 N N   . GLN H 4 125 ? -11.372  -144.188 46.504  1.00 188.77 ? 125 GLN L N   1 
ATOM   12381 C CA  . GLN H 4 125 ? -10.256  -143.923 45.593  1.00 187.27 ? 125 GLN L CA  1 
ATOM   12382 C C   . GLN H 4 125 ? -9.278   -145.107 45.580  1.00 193.92 ? 125 GLN L C   1 
ATOM   12383 O O   . GLN H 4 125 ? -8.624   -145.350 44.565  1.00 193.94 ? 125 GLN L O   1 
ATOM   12384 C CB  . GLN H 4 125 ? -9.548   -142.622 46.005  1.00 185.32 ? 125 GLN L CB  1 
ATOM   12385 C CG  . GLN H 4 125 ? -8.534   -142.095 44.996  1.00 195.56 ? 125 GLN L CG  1 
ATOM   12386 C CD  . GLN H 4 125 ? -7.928   -140.778 45.407  1.00 211.86 ? 125 GLN L CD  1 
ATOM   12387 O OE1 . GLN H 4 125 ? -7.618   -140.535 46.581  1.00 207.77 ? 125 GLN L OE1 1 
ATOM   12388 N NE2 . GLN H 4 125 ? -7.697   -139.914 44.432  1.00 201.74 ? 125 GLN L NE2 1 
ATOM   12389 N N   . LEU H 4 126 ? -9.192   -145.845 46.703  1.00 192.95 ? 126 LEU L N   1 
ATOM   12390 C CA  . LEU H 4 126 ? -8.348   -147.033 46.853  1.00 196.13 ? 126 LEU L CA  1 
ATOM   12391 C C   . LEU H 4 126 ? -8.799   -148.144 45.896  1.00 202.87 ? 126 LEU L C   1 
ATOM   12392 O O   . LEU H 4 126 ? -7.965   -148.907 45.405  1.00 204.47 ? 126 LEU L O   1 
ATOM   12393 C CB  . LEU H 4 126 ? -8.411   -147.537 48.304  1.00 197.89 ? 126 LEU L CB  1 
ATOM   12394 C CG  . LEU H 4 126 ? -7.196   -147.262 49.183  1.00 201.79 ? 126 LEU L CG  1 
ATOM   12395 C CD1 . LEU H 4 126 ? -7.261   -145.875 49.799  1.00 198.17 ? 126 LEU L CD1 1 
ATOM   12396 C CD2 . LEU H 4 126 ? -7.093   -148.295 50.287  1.00 207.82 ? 126 LEU L CD2 1 
ATOM   12397 N N   . LYS H 4 127 ? -10.120  -148.208 45.618  1.00 199.49 ? 127 LYS L N   1 
ATOM   12398 C CA  . LYS H 4 127 ? -10.748  -149.179 44.723  1.00 201.74 ? 127 LYS L CA  1 
ATOM   12399 C C   . LYS H 4 127 ? -10.318  -149.004 43.262  1.00 205.32 ? 127 LYS L C   1 
ATOM   12400 O O   . LYS H 4 127 ? -10.362  -149.973 42.501  1.00 207.44 ? 127 LYS L O   1 
ATOM   12401 C CB  . LYS H 4 127 ? -12.281  -149.122 44.852  1.00 203.62 ? 127 LYS L CB  1 
ATOM   12402 C CG  . LYS H 4 127 ? -12.971  -150.463 44.612  1.00 213.72 ? 127 LYS L CG  1 
ATOM   12403 C CD  . LYS H 4 127 ? -12.958  -151.349 45.863  1.00 218.32 ? 127 LYS L CD  1 
ATOM   12404 C CE  . LYS H 4 127 ? -13.448  -152.752 45.594  1.00 221.21 ? 127 LYS L CE  1 
ATOM   12405 N NZ  . LYS H 4 127 ? -13.343  -153.608 46.804  1.00 224.40 ? 127 LYS L NZ  1 
ATOM   12406 N N   . SER H 4 128 ? -9.903   -147.782 42.877  1.00 198.28 ? 128 SER L N   1 
ATOM   12407 C CA  . SER H 4 128 ? -9.457   -147.483 41.512  1.00 197.49 ? 128 SER L CA  1 
ATOM   12408 C C   . SER H 4 128 ? -8.040   -148.005 41.210  1.00 202.85 ? 128 SER L C   1 
ATOM   12409 O O   . SER H 4 128 ? -7.825   -148.588 40.144  1.00 204.98 ? 128 SER L O   1 
ATOM   12410 C CB  . SER H 4 128 ? -9.577   -145.992 41.207  1.00 197.52 ? 128 SER L CB  1 
ATOM   12411 O OG  . SER H 4 128 ? -8.600   -145.220 41.885  1.00 202.57 ? 128 SER L OG  1 
ATOM   12412 N N   . GLY H 4 129 ? -7.107   -147.793 42.143  1.00 197.65 ? 129 GLY L N   1 
ATOM   12413 C CA  . GLY H 4 129 ? -5.715   -148.223 42.017  1.00 198.58 ? 129 GLY L CA  1 
ATOM   12414 C C   . GLY H 4 129 ? -4.699   -147.095 41.994  1.00 198.44 ? 129 GLY L C   1 
ATOM   12415 O O   . GLY H 4 129 ? -3.499   -147.348 41.861  1.00 198.99 ? 129 GLY L O   1 
ATOM   12416 N N   . THR H 4 130 ? -5.180   -145.841 42.103  1.00 190.21 ? 130 THR L N   1 
ATOM   12417 C CA  . THR H 4 130 ? -4.381   -144.612 42.125  1.00 186.36 ? 130 THR L CA  1 
ATOM   12418 C C   . THR H 4 130 ? -5.015   -143.685 43.174  1.00 185.94 ? 130 THR L C   1 
ATOM   12419 O O   . THR H 4 130 ? -6.155   -143.246 42.996  1.00 184.32 ? 130 THR L O   1 
ATOM   12420 C CB  . THR H 4 130 ? -4.267   -144.006 40.702  1.00 191.84 ? 130 THR L CB  1 
ATOM   12421 O OG1 . THR H 4 130 ? -3.641   -144.954 39.836  1.00 193.51 ? 130 THR L OG1 1 
ATOM   12422 C CG2 . THR H 4 130 ? -3.475   -142.704 40.670  1.00 186.91 ? 130 THR L CG2 1 
ATOM   12423 N N   . ALA H 4 131 ? -4.292   -143.434 44.283  1.00 180.48 ? 131 ALA L N   1 
ATOM   12424 C CA  . ALA H 4 131 ? -4.759   -142.602 45.394  1.00 177.14 ? 131 ALA L CA  1 
ATOM   12425 C C   . ALA H 4 131 ? -3.865   -141.384 45.642  1.00 176.47 ? 131 ALA L C   1 
ATOM   12426 O O   . ALA H 4 131 ? -2.639   -141.496 45.606  1.00 176.32 ? 131 ALA L O   1 
ATOM   12427 C CB  . ALA H 4 131 ? -4.878   -143.440 46.654  1.00 179.50 ? 131 ALA L CB  1 
ATOM   12428 N N   . SER H 4 132 ? -4.486   -140.223 45.906  1.00 169.33 ? 132 SER L N   1 
ATOM   12429 C CA  . SER H 4 132 ? -3.773   -138.965 46.127  1.00 166.12 ? 132 SER L CA  1 
ATOM   12430 C C   . SER H 4 132 ? -3.913   -138.413 47.547  1.00 167.72 ? 132 SER L C   1 
ATOM   12431 O O   . SER H 4 132 ? -4.974   -138.547 48.157  1.00 167.32 ? 132 SER L O   1 
ATOM   12432 C CB  . SER H 4 132 ? -4.213   -137.919 45.108  1.00 167.58 ? 132 SER L CB  1 
ATOM   12433 O OG  . SER H 4 132 ? -4.117   -138.409 43.780  1.00 175.75 ? 132 SER L OG  1 
ATOM   12434 N N   . VAL H 4 133 ? -2.837   -137.779 48.059  1.00 162.51 ? 133 VAL L N   1 
ATOM   12435 C CA  . VAL H 4 133 ? -2.785   -137.155 49.392  1.00 160.57 ? 133 VAL L CA  1 
ATOM   12436 C C   . VAL H 4 133 ? -2.678   -135.626 49.197  1.00 160.91 ? 133 VAL L C   1 
ATOM   12437 O O   . VAL H 4 133 ? -1.910   -135.182 48.339  1.00 160.24 ? 133 VAL L O   1 
ATOM   12438 C CB  . VAL H 4 133 ? -1.635   -137.727 50.277  1.00 165.05 ? 133 VAL L CB  1 
ATOM   12439 C CG1 . VAL H 4 133 ? -1.643   -137.114 51.674  1.00 163.41 ? 133 VAL L CG1 1 
ATOM   12440 C CG2 . VAL H 4 133 ? -1.711   -139.247 50.373  1.00 167.75 ? 133 VAL L CG2 1 
ATOM   12441 N N   . VAL H 4 134 ? -3.465   -134.831 49.967  1.00 154.52 ? 134 VAL L N   1 
ATOM   12442 C CA  . VAL H 4 134 ? -3.491   -133.363 49.870  1.00 151.30 ? 134 VAL L CA  1 
ATOM   12443 C C   . VAL H 4 134 ? -2.947   -132.677 51.138  1.00 152.95 ? 134 VAL L C   1 
ATOM   12444 O O   . VAL H 4 134 ? -3.290   -133.081 52.247  1.00 152.92 ? 134 VAL L O   1 
ATOM   12445 C CB  . VAL H 4 134 ? -4.889   -132.808 49.472  1.00 154.51 ? 134 VAL L CB  1 
ATOM   12446 C CG1 . VAL H 4 134 ? -4.806   -131.339 49.060  1.00 152.52 ? 134 VAL L CG1 1 
ATOM   12447 C CG2 . VAL H 4 134 ? -5.520   -133.630 48.351  1.00 155.67 ? 134 VAL L CG2 1 
ATOM   12448 N N   . CYS H 4 135 ? -2.114   -131.628 50.952  1.00 147.55 ? 135 CYS L N   1 
ATOM   12449 C CA  . CYS H 4 135 ? -1.508   -130.806 52.008  1.00 145.73 ? 135 CYS L CA  1 
ATOM   12450 C C   . CYS H 4 135 ? -2.073   -129.371 51.904  1.00 146.40 ? 135 CYS L C   1 
ATOM   12451 O O   . CYS H 4 135 ? -1.495   -128.522 51.219  1.00 146.35 ? 135 CYS L O   1 
ATOM   12452 C CB  . CYS H 4 135 ? 0.016    -130.828 51.891  1.00 146.04 ? 135 CYS L CB  1 
ATOM   12453 S SG  . CYS H 4 135 ? 0.886    -129.859 53.150  1.00 148.52 ? 135 CYS L SG  1 
ATOM   12454 N N   . LEU H 4 136 ? -3.232   -129.126 52.552  1.00 139.61 ? 136 LEU L N   1 
ATOM   12455 C CA  . LEU H 4 136 ? -3.931   -127.836 52.547  1.00 136.67 ? 136 LEU L CA  1 
ATOM   12456 C C   . LEU H 4 136 ? -3.255   -126.800 53.444  1.00 135.20 ? 136 LEU L C   1 
ATOM   12457 O O   . LEU H 4 136 ? -2.954   -127.086 54.599  1.00 134.95 ? 136 LEU L O   1 
ATOM   12458 C CB  . LEU H 4 136 ? -5.415   -128.035 52.929  1.00 137.66 ? 136 LEU L CB  1 
ATOM   12459 C CG  . LEU H 4 136 ? -6.188   -126.839 53.491  1.00 142.08 ? 136 LEU L CG  1 
ATOM   12460 C CD1 . LEU H 4 136 ? -6.517   -125.835 52.415  1.00 141.37 ? 136 LEU L CD1 1 
ATOM   12461 C CD2 . LEU H 4 136 ? -7.446   -127.290 54.188  1.00 146.99 ? 136 LEU L CD2 1 
ATOM   12462 N N   . LEU H 4 137 ? -3.060   -125.591 52.909  1.00 127.77 ? 137 LEU L N   1 
ATOM   12463 C CA  . LEU H 4 137 ? -2.443   -124.464 53.601  1.00 125.51 ? 137 LEU L CA  1 
ATOM   12464 C C   . LEU H 4 137 ? -3.465   -123.335 53.662  1.00 127.56 ? 137 LEU L C   1 
ATOM   12465 O O   . LEU H 4 137 ? -3.411   -122.414 52.848  1.00 126.90 ? 137 LEU L O   1 
ATOM   12466 C CB  . LEU H 4 137 ? -1.192   -124.022 52.819  1.00 124.78 ? 137 LEU L CB  1 
ATOM   12467 C CG  . LEU H 4 137 ? 0.148    -124.644 53.207  1.00 129.08 ? 137 LEU L CG  1 
ATOM   12468 C CD1 . LEU H 4 137 ? 0.264    -126.090 52.738  1.00 130.22 ? 137 LEU L CD1 1 
ATOM   12469 C CD2 . LEU H 4 137 ? 1.278    -123.852 52.610  1.00 130.45 ? 137 LEU L CD2 1 
ATOM   12470 N N   . ASN H 4 138 ? -4.411   -123.417 54.615  1.00 123.39 ? 138 ASN L N   1 
ATOM   12471 C CA  . ASN H 4 138 ? -5.493   -122.437 54.717  1.00 123.46 ? 138 ASN L CA  1 
ATOM   12472 C C   . ASN H 4 138 ? -5.103   -121.103 55.351  1.00 126.41 ? 138 ASN L C   1 
ATOM   12473 O O   . ASN H 4 138 ? -4.438   -121.066 56.381  1.00 125.62 ? 138 ASN L O   1 
ATOM   12474 C CB  . ASN H 4 138 ? -6.719   -123.024 55.428  1.00 125.48 ? 138 ASN L CB  1 
ATOM   12475 C CG  . ASN H 4 138 ? -8.048   -122.598 54.819  1.00 147.53 ? 138 ASN L CG  1 
ATOM   12476 O OD1 . ASN H 4 138 ? -8.834   -121.852 55.418  1.00 139.39 ? 138 ASN L OD1 1 
ATOM   12477 N ND2 . ASN H 4 138 ? -8.347   -123.084 53.619  1.00 140.10 ? 138 ASN L ND2 1 
ATOM   12478 N N   . ASN H 4 139 ? -5.551   -120.010 54.702  1.00 122.92 ? 139 ASN L N   1 
ATOM   12479 C CA  . ASN H 4 139 ? -5.450   -118.589 55.051  1.00 122.60 ? 139 ASN L CA  1 
ATOM   12480 C C   . ASN H 4 139 ? -4.084   -118.138 55.631  1.00 125.14 ? 139 ASN L C   1 
ATOM   12481 O O   . ASN H 4 139 ? -3.821   -118.273 56.831  1.00 123.54 ? 139 ASN L O   1 
ATOM   12482 C CB  . ASN H 4 139 ? -6.613   -118.185 55.973  1.00 125.19 ? 139 ASN L CB  1 
ATOM   12483 C CG  . ASN H 4 139 ? -7.996   -118.322 55.344  1.00 149.25 ? 139 ASN L CG  1 
ATOM   12484 O OD1 . ASN H 4 139 ? -8.895   -118.970 55.892  1.00 143.06 ? 139 ASN L OD1 1 
ATOM   12485 N ND2 . ASN H 4 139 ? -8.213   -117.701 54.190  1.00 141.41 ? 139 ASN L ND2 1 
ATOM   12486 N N   . PHE H 4 140 ? -3.238   -117.566 54.747  1.00 122.87 ? 140 PHE L N   1 
ATOM   12487 C CA  . PHE H 4 140 ? -1.901   -117.047 55.062  1.00 122.85 ? 140 PHE L CA  1 
ATOM   12488 C C   . PHE H 4 140 ? -1.520   -115.818 54.220  1.00 128.39 ? 140 PHE L C   1 
ATOM   12489 O O   . PHE H 4 140 ? -2.145   -115.567 53.189  1.00 129.01 ? 140 PHE L O   1 
ATOM   12490 C CB  . PHE H 4 140 ? -0.840   -118.149 54.917  1.00 124.09 ? 140 PHE L CB  1 
ATOM   12491 C CG  . PHE H 4 140 ? -0.640   -118.689 53.524  1.00 126.06 ? 140 PHE L CG  1 
ATOM   12492 C CD1 . PHE H 4 140 ? 0.299    -118.123 52.671  1.00 129.53 ? 140 PHE L CD1 1 
ATOM   12493 C CD2 . PHE H 4 140 ? -1.342   -119.802 53.086  1.00 128.85 ? 140 PHE L CD2 1 
ATOM   12494 C CE1 . PHE H 4 140 ? 0.492    -118.627 51.386  1.00 131.07 ? 140 PHE L CE1 1 
ATOM   12495 C CE2 . PHE H 4 140 ? -1.146   -120.308 51.803  1.00 132.21 ? 140 PHE L CE2 1 
ATOM   12496 C CZ  . PHE H 4 140 ? -0.230   -119.717 50.961  1.00 130.49 ? 140 PHE L CZ  1 
ATOM   12497 N N   . TYR H 4 141 ? -0.462   -115.084 54.639  1.00 125.22 ? 141 TYR L N   1 
ATOM   12498 C CA  . TYR H 4 141 ? 0.045    -113.880 53.972  1.00 125.87 ? 141 TYR L CA  1 
ATOM   12499 C C   . TYR H 4 141 ? 1.549    -113.714 54.243  1.00 130.25 ? 141 TYR L C   1 
ATOM   12500 O O   . TYR H 4 141 ? 1.965    -113.820 55.395  1.00 128.39 ? 141 TYR L O   1 
ATOM   12501 C CB  . TYR H 4 141 ? -0.740   -112.630 54.420  1.00 127.87 ? 141 TYR L CB  1 
ATOM   12502 C CG  . TYR H 4 141 ? -0.412   -111.368 53.649  1.00 129.72 ? 141 TYR L CG  1 
ATOM   12503 C CD1 . TYR H 4 141 ? -1.072   -111.060 52.463  1.00 132.44 ? 141 TYR L CD1 1 
ATOM   12504 C CD2 . TYR H 4 141 ? 0.519    -110.456 54.132  1.00 130.36 ? 141 TYR L CD2 1 
ATOM   12505 C CE1 . TYR H 4 141 ? -0.791   -109.889 51.763  1.00 133.85 ? 141 TYR L CE1 1 
ATOM   12506 C CE2 . TYR H 4 141 ? 0.813    -109.287 53.437  1.00 132.22 ? 141 TYR L CE2 1 
ATOM   12507 C CZ  . TYR H 4 141 ? 0.149    -109.003 52.258  1.00 138.79 ? 141 TYR L CZ  1 
ATOM   12508 O OH  . TYR H 4 141 ? 0.427    -107.845 51.580  1.00 139.98 ? 141 TYR L OH  1 
ATOM   12509 N N   . PRO H 4 142 ? 2.387    -113.449 53.220  1.00 129.71 ? 142 PRO L N   1 
ATOM   12510 C CA  . PRO H 4 142 ? 2.062    -113.278 51.790  1.00 132.27 ? 142 PRO L CA  1 
ATOM   12511 C C   . PRO H 4 142 ? 1.915    -114.602 51.022  1.00 139.24 ? 142 PRO L C   1 
ATOM   12512 O O   . PRO H 4 142 ? 2.194    -115.661 51.595  1.00 139.33 ? 142 PRO L O   1 
ATOM   12513 C CB  . PRO H 4 142 ? 3.215    -112.401 51.293  1.00 134.50 ? 142 PRO L CB  1 
ATOM   12514 C CG  . PRO H 4 142 ? 4.397    -112.840 52.139  1.00 136.83 ? 142 PRO L CG  1 
ATOM   12515 C CD  . PRO H 4 142 ? 3.834    -113.287 53.469  1.00 130.68 ? 142 PRO L CD  1 
ATOM   12516 N N   . ARG H 4 143 ? 1.480    -114.540 49.728  1.00 137.10 ? 143 ARG L N   1 
ATOM   12517 C CA  . ARG H 4 143 ? 1.283    -115.697 48.827  1.00 137.60 ? 143 ARG L CA  1 
ATOM   12518 C C   . ARG H 4 143 ? 2.561    -116.546 48.700  1.00 142.94 ? 143 ARG L C   1 
ATOM   12519 O O   . ARG H 4 143 ? 2.498    -117.752 48.447  1.00 142.64 ? 143 ARG L O   1 
ATOM   12520 C CB  . ARG H 4 143 ? 0.838    -115.207 47.428  1.00 139.30 ? 143 ARG L CB  1 
ATOM   12521 C CG  . ARG H 4 143 ? 0.210    -116.286 46.533  1.00 147.21 ? 143 ARG L CG  1 
ATOM   12522 C CD  . ARG H 4 143 ? -0.233   -115.745 45.183  1.00 150.92 ? 143 ARG L CD  1 
ATOM   12523 N NE  . ARG H 4 143 ? -1.249   -116.596 44.550  1.00 151.30 ? 143 ARG L NE  1 
ATOM   12524 C CZ  . ARG H 4 143 ? -1.932   -116.272 43.453  1.00 161.32 ? 143 ARG L CZ  1 
ATOM   12525 N NH1 . ARG H 4 143 ? -1.716   -115.111 42.846  1.00 150.87 ? 143 ARG L NH1 1 
ATOM   12526 N NH2 . ARG H 4 143 ? -2.837   -117.106 42.957  1.00 144.10 ? 143 ARG L NH2 1 
ATOM   12527 N N   . GLU H 4 144 ? 3.706    -115.885 48.897  1.00 140.50 ? 144 GLU L N   1 
ATOM   12528 C CA  . GLU H 4 144 ? 5.072    -116.389 48.821  1.00 140.39 ? 144 GLU L CA  1 
ATOM   12529 C C   . GLU H 4 144 ? 5.345    -117.466 49.898  1.00 142.70 ? 144 GLU L C   1 
ATOM   12530 O O   . GLU H 4 144 ? 5.632    -117.136 51.052  1.00 141.23 ? 144 GLU L O   1 
ATOM   12531 C CB  . GLU H 4 144 ? 6.058    -115.197 48.900  1.00 142.17 ? 144 GLU L CB  1 
ATOM   12532 C CG  . GLU H 4 144 ? 5.849    -114.120 47.831  1.00 153.64 ? 144 GLU L CG  1 
ATOM   12533 C CD  . GLU H 4 144 ? 4.861    -113.000 48.129  1.00 170.34 ? 144 GLU L CD  1 
ATOM   12534 O OE1 . GLU H 4 144 ? 3.634    -113.236 48.030  1.00 155.58 ? 144 GLU L OE1 1 
ATOM   12535 O OE2 . GLU H 4 144 ? 5.317    -111.866 48.401  1.00 164.88 ? 144 GLU L OE2 1 
ATOM   12536 N N   . ALA H 4 145 ? 5.208    -118.757 49.503  1.00 139.23 ? 145 ALA L N   1 
ATOM   12537 C CA  . ALA H 4 145 ? 5.395    -119.954 50.343  1.00 138.43 ? 145 ALA L CA  1 
ATOM   12538 C C   . ALA H 4 145 ? 5.824    -121.182 49.510  1.00 143.47 ? 145 ALA L C   1 
ATOM   12539 O O   . ALA H 4 145 ? 5.659    -121.169 48.288  1.00 144.55 ? 145 ALA L O   1 
ATOM   12540 C CB  . ALA H 4 145 ? 4.104    -120.267 51.089  1.00 138.61 ? 145 ALA L CB  1 
ATOM   12541 N N   . LYS H 4 146 ? 6.356    -122.246 50.169  1.00 139.76 ? 146 LYS L N   1 
ATOM   12542 C CA  . LYS H 4 146 ? 6.790    -123.480 49.494  1.00 140.86 ? 146 LYS L CA  1 
ATOM   12543 C C   . LYS H 4 146 ? 6.499    -124.755 50.295  1.00 144.50 ? 146 LYS L C   1 
ATOM   12544 O O   . LYS H 4 146 ? 6.804    -124.816 51.486  1.00 143.39 ? 146 LYS L O   1 
ATOM   12545 C CB  . LYS H 4 146 ? 8.281    -123.408 49.085  1.00 144.38 ? 146 LYS L CB  1 
ATOM   12546 C CG  . LYS H 4 146 ? 8.799    -124.597 48.255  1.00 160.92 ? 146 LYS L CG  1 
ATOM   12547 C CD  . LYS H 4 146 ? 8.137    -124.714 46.872  1.00 170.65 ? 146 LYS L CD  1 
ATOM   12548 C CE  . LYS H 4 146 ? 8.398    -126.050 46.225  1.00 182.67 ? 146 LYS L CE  1 
ATOM   12549 N NZ  . LYS H 4 146 ? 7.676    -126.179 44.934  1.00 192.07 ? 146 LYS L NZ  1 
ATOM   12550 N N   . VAL H 4 147 ? 5.931    -125.776 49.615  1.00 141.92 ? 147 VAL L N   1 
ATOM   12551 C CA  . VAL H 4 147 ? 5.579    -127.090 50.176  1.00 142.27 ? 147 VAL L CA  1 
ATOM   12552 C C   . VAL H 4 147 ? 6.501    -128.175 49.578  1.00 149.26 ? 147 VAL L C   1 
ATOM   12553 O O   . VAL H 4 147 ? 6.700    -128.206 48.361  1.00 150.15 ? 147 VAL L O   1 
ATOM   12554 C CB  . VAL H 4 147 ? 4.072    -127.433 49.976  1.00 145.81 ? 147 VAL L CB  1 
ATOM   12555 C CG1 . VAL H 4 147 ? 3.667    -128.678 50.764  1.00 146.04 ? 147 VAL L CG1 1 
ATOM   12556 C CG2 . VAL H 4 147 ? 3.180    -126.258 50.355  1.00 144.30 ? 147 VAL L CG2 1 
ATOM   12557 N N   . GLN H 4 148 ? 7.054    -129.058 50.438  1.00 146.93 ? 148 GLN L N   1 
ATOM   12558 C CA  . GLN H 4 148 ? 7.944    -130.160 50.043  1.00 148.89 ? 148 GLN L CA  1 
ATOM   12559 C C   . GLN H 4 148 ? 7.387    -131.492 50.568  1.00 154.73 ? 148 GLN L C   1 
ATOM   12560 O O   . GLN H 4 148 ? 7.415    -131.730 51.777  1.00 154.10 ? 148 GLN L O   1 
ATOM   12561 C CB  . GLN H 4 148 ? 9.378    -129.927 50.567  1.00 150.02 ? 148 GLN L CB  1 
ATOM   12562 C CG  . GLN H 4 148 ? 10.103   -128.724 49.964  1.00 163.03 ? 148 GLN L CG  1 
ATOM   12563 C CD  . GLN H 4 148 ? 11.195   -128.218 50.878  1.00 181.50 ? 148 GLN L CD  1 
ATOM   12564 O OE1 . GLN H 4 148 ? 11.008   -127.261 51.639  1.00 174.31 ? 148 GLN L OE1 1 
ATOM   12565 N NE2 . GLN H 4 148 ? 12.360   -128.852 50.831  1.00 176.02 ? 148 GLN L NE2 1 
ATOM   12566 N N   . TRP H 4 149 ? 6.868    -132.348 49.667  1.00 171.12 ? 149 TRP L N   1 
ATOM   12567 C CA  . TRP H 4 149 ? 6.295    -133.648 50.034  1.00 171.33 ? 149 TRP L CA  1 
ATOM   12568 C C   . TRP H 4 149 ? 7.370    -134.647 50.466  1.00 174.36 ? 149 TRP L C   1 
ATOM   12569 O O   . TRP H 4 149 ? 8.259    -134.976 49.679  1.00 173.89 ? 149 TRP L O   1 
ATOM   12570 C CB  . TRP H 4 149 ? 5.452    -134.231 48.890  1.00 170.84 ? 149 TRP L CB  1 
ATOM   12571 C CG  . TRP H 4 149 ? 4.068    -133.659 48.772  1.00 172.77 ? 149 TRP L CG  1 
ATOM   12572 C CD1 . TRP H 4 149 ? 3.645    -132.720 47.880  1.00 176.44 ? 149 TRP L CD1 1 
ATOM   12573 C CD2 . TRP H 4 149 ? 2.912    -134.042 49.532  1.00 173.10 ? 149 TRP L CD2 1 
ATOM   12574 N NE1 . TRP H 4 149 ? 2.299    -132.487 48.038  1.00 176.66 ? 149 TRP L NE1 1 
ATOM   12575 C CE2 . TRP H 4 149 ? 1.826    -133.277 49.054  1.00 177.90 ? 149 TRP L CE2 1 
ATOM   12576 C CE3 . TRP H 4 149 ? 2.692    -134.945 50.587  1.00 174.07 ? 149 TRP L CE3 1 
ATOM   12577 C CZ2 . TRP H 4 149 ? 0.537    -133.397 49.583  1.00 177.84 ? 149 TRP L CZ2 1 
ATOM   12578 C CZ3 . TRP H 4 149 ? 1.416    -135.053 51.118  1.00 176.04 ? 149 TRP L CZ3 1 
ATOM   12579 C CH2 . TRP H 4 149 ? 0.359    -134.280 50.623  1.00 177.53 ? 149 TRP L CH2 1 
ATOM   12580 N N   . LYS H 4 150 ? 7.285    -135.120 51.722  1.00 170.35 ? 150 LYS L N   1 
ATOM   12581 C CA  . LYS H 4 150 ? 8.220    -136.076 52.313  1.00 169.58 ? 150 LYS L CA  1 
ATOM   12582 C C   . LYS H 4 150 ? 7.556    -137.437 52.551  1.00 172.90 ? 150 LYS L C   1 
ATOM   12583 O O   . LYS H 4 150 ? 6.710    -137.574 53.438  1.00 171.98 ? 150 LYS L O   1 
ATOM   12584 C CB  . LYS H 4 150 ? 8.839    -135.519 53.612  1.00 171.72 ? 150 LYS L CB  1 
ATOM   12585 C CG  . LYS H 4 150 ? 9.812    -134.364 53.394  1.00 178.73 ? 150 LYS L CG  1 
ATOM   12586 C CD  . LYS H 4 150 ? 10.340   -133.812 54.707  1.00 183.06 ? 150 LYS L CD  1 
ATOM   12587 C CE  . LYS H 4 150 ? 11.315   -132.683 54.493  1.00 185.81 ? 150 LYS L CE  1 
ATOM   12588 N NZ  . LYS H 4 150 ? 11.872   -132.196 55.780  1.00 190.87 ? 150 LYS L NZ  1 
ATOM   12589 N N   . VAL H 4 151 ? 7.935    -138.433 51.735  1.00 169.61 ? 151 VAL L N   1 
ATOM   12590 C CA  . VAL H 4 151 ? 7.445    -139.810 51.827  1.00 169.45 ? 151 VAL L CA  1 
ATOM   12591 C C   . VAL H 4 151 ? 8.576    -140.633 52.457  1.00 173.66 ? 151 VAL L C   1 
ATOM   12592 O O   . VAL H 4 151 ? 9.518    -141.030 51.762  1.00 173.08 ? 151 VAL L O   1 
ATOM   12593 C CB  . VAL H 4 151 ? 6.972    -140.353 50.448  1.00 173.19 ? 151 VAL L CB  1 
ATOM   12594 C CG1 . VAL H 4 151 ? 6.590    -141.831 50.518  1.00 172.82 ? 151 VAL L CG1 1 
ATOM   12595 C CG2 . VAL H 4 151 ? 5.810    -139.524 49.908  1.00 173.18 ? 151 VAL L CG2 1 
ATOM   12596 N N   . ASP H 4 152 ? 8.501    -140.822 53.796  1.00 171.02 ? 152 ASP L N   1 
ATOM   12597 C CA  . ASP H 4 152 ? 9.483    -141.532 54.632  1.00 171.67 ? 152 ASP L CA  1 
ATOM   12598 C C   . ASP H 4 152 ? 10.896   -140.926 54.462  1.00 177.40 ? 152 ASP L C   1 
ATOM   12599 O O   . ASP H 4 152 ? 11.794   -141.579 53.921  1.00 177.23 ? 152 ASP L O   1 
ATOM   12600 C CB  . ASP H 4 152 ? 9.451    -143.062 54.375  1.00 173.44 ? 152 ASP L CB  1 
ATOM   12601 C CG  . ASP H 4 152 ? 8.088    -143.716 54.535  1.00 181.94 ? 152 ASP L CG  1 
ATOM   12602 O OD1 . ASP H 4 152 ? 7.145    -143.301 53.832  1.00 181.80 ? 152 ASP L OD1 1 
ATOM   12603 O OD2 . ASP H 4 152 ? 7.983    -144.684 55.316  1.00 187.97 ? 152 ASP L OD2 1 
ATOM   12604 N N   . ASN H 4 153 ? 11.054   -139.640 54.877  1.00 175.25 ? 153 ASN L N   1 
ATOM   12605 C CA  . ASN H 4 153 ? 12.267   -138.793 54.792  1.00 175.83 ? 153 ASN L CA  1 
ATOM   12606 C C   . ASN H 4 153 ? 12.652   -138.419 53.339  1.00 179.50 ? 153 ASN L C   1 
ATOM   12607 O O   . ASN H 4 153 ? 13.165   -137.318 53.106  1.00 179.05 ? 153 ASN L O   1 
ATOM   12608 C CB  . ASN H 4 153 ? 13.464   -139.384 55.555  1.00 179.08 ? 153 ASN L CB  1 
ATOM   12609 C CG  . ASN H 4 153 ? 14.646   -138.445 55.666  1.00 206.23 ? 153 ASN L CG  1 
ATOM   12610 O OD1 . ASN H 4 153 ? 15.492   -138.368 54.767  1.00 201.00 ? 153 ASN L OD1 1 
ATOM   12611 N ND2 . ASN H 4 153 ? 14.725   -137.701 56.766  1.00 198.50 ? 153 ASN L ND2 1 
ATOM   12612 N N   . ALA H 4 154 ? 12.405   -139.331 52.380  1.00 175.51 ? 154 ALA L N   1 
ATOM   12613 C CA  . ALA H 4 154 ? 12.687   -139.147 50.960  1.00 174.63 ? 154 ALA L CA  1 
ATOM   12614 C C   . ALA H 4 154 ? 11.735   -138.118 50.344  1.00 176.30 ? 154 ALA L C   1 
ATOM   12615 O O   . ALA H 4 154 ? 10.534   -138.371 50.191  1.00 174.96 ? 154 ALA L O   1 
ATOM   12616 C CB  . ALA H 4 154 ? 12.591   -140.477 50.226  1.00 175.44 ? 154 ALA L CB  1 
ATOM   12617 N N   . LEU H 4 155 ? 12.289   -136.936 50.031  1.00 172.44 ? 155 LEU L N   1 
ATOM   12618 C CA  . LEU H 4 155 ? 11.567   -135.815 49.435  1.00 171.87 ? 155 LEU L CA  1 
ATOM   12619 C C   . LEU H 4 155 ? 11.167   -136.167 47.998  1.00 174.44 ? 155 LEU L C   1 
ATOM   12620 O O   . LEU H 4 155 ? 12.031   -136.491 47.178  1.00 174.09 ? 155 LEU L O   1 
ATOM   12621 C CB  . LEU H 4 155 ? 12.413   -134.523 49.495  1.00 172.06 ? 155 LEU L CB  1 
ATOM   12622 C CG  . LEU H 4 155 ? 12.573   -133.877 50.883  1.00 176.96 ? 155 LEU L CG  1 
ATOM   12623 C CD1 . LEU H 4 155 ? 13.880   -134.288 51.542  1.00 177.29 ? 155 LEU L CD1 1 
ATOM   12624 C CD2 . LEU H 4 155 ? 12.495   -132.365 50.795  1.00 179.77 ? 155 LEU L CD2 1 
ATOM   12625 N N   . GLN H 4 156 ? 9.848    -136.168 47.724  1.00 169.86 ? 156 GLN L N   1 
ATOM   12626 C CA  . GLN H 4 156 ? 9.275    -136.515 46.422  1.00 169.05 ? 156 GLN L CA  1 
ATOM   12627 C C   . GLN H 4 156 ? 8.980    -135.299 45.555  1.00 171.78 ? 156 GLN L C   1 
ATOM   12628 O O   . GLN H 4 156 ? 8.435    -134.305 46.038  1.00 171.46 ? 156 GLN L O   1 
ATOM   12629 C CB  . GLN H 4 156 ? 8.019    -137.389 46.577  1.00 170.30 ? 156 GLN L CB  1 
ATOM   12630 C CG  . GLN H 4 156 ? 8.270    -138.748 47.238  1.00 184.96 ? 156 GLN L CG  1 
ATOM   12631 C CD  . GLN H 4 156 ? 9.209    -139.664 46.481  1.00 204.00 ? 156 GLN L CD  1 
ATOM   12632 O OE1 . GLN H 4 156 ? 9.134    -139.819 45.252  1.00 198.85 ? 156 GLN L OE1 1 
ATOM   12633 N NE2 . GLN H 4 156 ? 10.097   -140.323 47.213  1.00 195.74 ? 156 GLN L NE2 1 
ATOM   12634 N N   . SER H 4 157 ? 9.337    -135.398 44.266  1.00 167.39 ? 157 SER L N   1 
ATOM   12635 C CA  . SER H 4 157 ? 9.145    -134.354 43.265  1.00 167.10 ? 157 SER L CA  1 
ATOM   12636 C C   . SER H 4 157 ? 8.599    -134.955 41.968  1.00 170.78 ? 157 SER L C   1 
ATOM   12637 O O   . SER H 4 157 ? 8.976    -136.071 41.604  1.00 169.64 ? 157 SER L O   1 
ATOM   12638 C CB  . SER H 4 157 ? 10.462   -133.633 43.001  1.00 170.17 ? 157 SER L CB  1 
ATOM   12639 O OG  . SER H 4 157 ? 10.264   -132.481 42.199  1.00 180.00 ? 157 SER L OG  1 
ATOM   12640 N N   . GLY H 4 158 ? 7.723    -134.210 41.294  1.00 168.40 ? 158 GLY L N   1 
ATOM   12641 C CA  . GLY H 4 158 ? 7.106    -134.620 40.035  1.00 169.02 ? 158 GLY L CA  1 
ATOM   12642 C C   . GLY H 4 158 ? 5.670    -135.082 40.180  1.00 173.65 ? 158 GLY L C   1 
ATOM   12643 O O   . GLY H 4 158 ? 4.783    -134.608 39.461  1.00 174.30 ? 158 GLY L O   1 
ATOM   12644 N N   . ASN H 4 159 ? 5.440    -136.021 41.120  1.00 172.61 ? 159 ASN L N   1 
ATOM   12645 C CA  . ASN H 4 159 ? 4.127    -136.586 41.458  1.00 173.52 ? 159 ASN L CA  1 
ATOM   12646 C C   . ASN H 4 159 ? 3.198    -135.512 42.034  1.00 174.24 ? 159 ASN L C   1 
ATOM   12647 O O   . ASN H 4 159 ? 1.982    -135.575 41.835  1.00 174.10 ? 159 ASN L O   1 
ATOM   12648 C CB  . ASN H 4 159 ? 4.282    -137.744 42.453  1.00 177.41 ? 159 ASN L CB  1 
ATOM   12649 C CG  . ASN H 4 159 ? 5.341    -137.539 43.516  1.00 204.74 ? 159 ASN L CG  1 
ATOM   12650 O OD1 . ASN H 4 159 ? 5.543    -136.437 44.045  1.00 197.57 ? 159 ASN L OD1 1 
ATOM   12651 N ND2 . ASN H 4 159 ? 6.062    -138.600 43.834  1.00 200.94 ? 159 ASN L ND2 1 
ATOM   12652 N N   . SER H 4 160 ? 3.786    -134.521 42.732  1.00 167.77 ? 160 SER L N   1 
ATOM   12653 C CA  . SER H 4 160 ? 3.090    -133.395 43.348  1.00 164.33 ? 160 SER L CA  1 
ATOM   12654 C C   . SER H 4 160 ? 2.686    -132.336 42.324  1.00 164.55 ? 160 SER L C   1 
ATOM   12655 O O   . SER H 4 160 ? 3.453    -132.028 41.407  1.00 163.40 ? 160 SER L O   1 
ATOM   12656 C CB  . SER H 4 160 ? 3.960    -132.760 44.427  1.00 166.94 ? 160 SER L CB  1 
ATOM   12657 O OG  . SER H 4 160 ? 5.184    -132.276 43.897  1.00 175.38 ? 160 SER L OG  1 
ATOM   12658 N N   . GLN H 4 161 ? 1.481    -131.775 42.498  1.00 159.09 ? 161 GLN L N   1 
ATOM   12659 C CA  . GLN H 4 161 ? 0.919    -130.705 41.668  1.00 156.41 ? 161 GLN L CA  1 
ATOM   12660 C C   . GLN H 4 161 ? 0.363    -129.635 42.611  1.00 157.60 ? 161 GLN L C   1 
ATOM   12661 O O   . GLN H 4 161 ? -0.356   -129.972 43.555  1.00 157.76 ? 161 GLN L O   1 
ATOM   12662 C CB  . GLN H 4 161 ? -0.172   -131.244 40.721  1.00 158.75 ? 161 GLN L CB  1 
ATOM   12663 C CG  . GLN H 4 161 ? 0.377    -132.041 39.536  1.00 170.29 ? 161 GLN L CG  1 
ATOM   12664 C CD  . GLN H 4 161 ? -0.677   -132.868 38.839  1.00 183.83 ? 161 GLN L CD  1 
ATOM   12665 O OE1 . GLN H 4 161 ? -1.737   -132.373 38.437  1.00 176.67 ? 161 GLN L OE1 1 
ATOM   12666 N NE2 . GLN H 4 161 ? -0.386   -134.149 38.644  1.00 176.99 ? 161 GLN L NE2 1 
ATOM   12667 N N   . GLU H 4 162 ? 0.735    -128.360 42.394  1.00 151.33 ? 162 GLU L N   1 
ATOM   12668 C CA  . GLU H 4 162 ? 0.304    -127.257 43.258  1.00 149.15 ? 162 GLU L CA  1 
ATOM   12669 C C   . GLU H 4 162 ? -0.746   -126.337 42.625  1.00 150.96 ? 162 GLU L C   1 
ATOM   12670 O O   . GLU H 4 162 ? -0.761   -126.151 41.403  1.00 151.02 ? 162 GLU L O   1 
ATOM   12671 C CB  . GLU H 4 162 ? 1.512    -126.442 43.750  1.00 149.83 ? 162 GLU L CB  1 
ATOM   12672 C CG  . GLU H 4 162 ? 2.237    -127.053 44.940  1.00 160.84 ? 162 GLU L CG  1 
ATOM   12673 C CD  . GLU H 4 162 ? 3.455    -126.280 45.414  1.00 179.72 ? 162 GLU L CD  1 
ATOM   12674 O OE1 . GLU H 4 162 ? 3.298    -125.114 45.846  1.00 171.67 ? 162 GLU L OE1 1 
ATOM   12675 O OE2 . GLU H 4 162 ? 4.567    -126.855 45.381  1.00 173.03 ? 162 GLU L OE2 1 
ATOM   12676 N N   . SER H 4 163 ? -1.615   -125.753 43.480  1.00 144.93 ? 163 SER L N   1 
ATOM   12677 C CA  . SER H 4 163 ? -2.673   -124.810 43.109  1.00 142.76 ? 163 SER L CA  1 
ATOM   12678 C C   . SER H 4 163 ? -2.884   -123.778 44.224  1.00 143.66 ? 163 SER L C   1 
ATOM   12679 O O   . SER H 4 163 ? -2.725   -124.106 45.404  1.00 143.65 ? 163 SER L O   1 
ATOM   12680 C CB  . SER H 4 163 ? -3.973   -125.547 42.817  1.00 146.90 ? 163 SER L CB  1 
ATOM   12681 O OG  . SER H 4 163 ? -4.919   -124.648 42.265  1.00 154.05 ? 163 SER L OG  1 
ATOM   12682 N N   . VAL H 4 164 ? -3.225   -122.531 43.851  1.00 137.55 ? 164 VAL L N   1 
ATOM   12683 C CA  . VAL H 4 164 ? -3.443   -121.431 44.801  1.00 135.89 ? 164 VAL L CA  1 
ATOM   12684 C C   . VAL H 4 164 ? -4.650   -120.582 44.468  1.00 139.54 ? 164 VAL L C   1 
ATOM   12685 O O   . VAL H 4 164 ? -4.908   -120.301 43.292  1.00 139.84 ? 164 VAL L O   1 
ATOM   12686 C CB  . VAL H 4 164 ? -2.204   -120.521 45.029  1.00 138.84 ? 164 VAL L CB  1 
ATOM   12687 C CG1 . VAL H 4 164 ? -1.291   -121.080 46.100  1.00 138.81 ? 164 VAL L CG1 1 
ATOM   12688 C CG2 . VAL H 4 164 ? -1.442   -120.238 43.738  1.00 138.79 ? 164 VAL L CG2 1 
ATOM   12689 N N   . THR H 4 165 ? -5.353   -120.121 45.517  1.00 134.79 ? 165 THR L N   1 
ATOM   12690 C CA  . THR H 4 165 ? -6.495   -119.220 45.384  1.00 134.06 ? 165 THR L CA  1 
ATOM   12691 C C   . THR H 4 165 ? -5.999   -117.796 45.526  1.00 136.77 ? 165 THR L C   1 
ATOM   12692 O O   . THR H 4 165 ? -5.016   -117.561 46.235  1.00 136.52 ? 165 THR L O   1 
ATOM   12693 C CB  . THR H 4 165 ? -7.574   -119.504 46.430  1.00 138.91 ? 165 THR L CB  1 
ATOM   12694 O OG1 . THR H 4 165 ? -6.983   -119.560 47.724  1.00 134.44 ? 165 THR L OG1 1 
ATOM   12695 C CG2 . THR H 4 165 ? -8.355   -120.767 46.137  1.00 139.57 ? 165 THR L CG2 1 
ATOM   12696 N N   . GLU H 4 166 ? -6.690   -116.845 44.867  1.00 132.17 ? 166 GLU L N   1 
ATOM   12697 C CA  . GLU H 4 166 ? -6.388   -115.413 44.916  1.00 131.21 ? 166 GLU L CA  1 
ATOM   12698 C C   . GLU H 4 166 ? -6.645   -114.834 46.327  1.00 132.96 ? 166 GLU L C   1 
ATOM   12699 O O   . GLU H 4 166 ? -7.207   -115.525 47.193  1.00 131.10 ? 166 GLU L O   1 
ATOM   12700 C CB  . GLU H 4 166 ? -7.205   -114.653 43.850  1.00 133.16 ? 166 GLU L CB  1 
ATOM   12701 C CG  . GLU H 4 166 ? -6.645   -114.745 42.439  1.00 142.07 ? 166 GLU L CG  1 
ATOM   12702 C CD  . GLU H 4 166 ? -5.352   -113.996 42.174  1.00 169.32 ? 166 GLU L CD  1 
ATOM   12703 O OE1 . GLU H 4 166 ? -5.058   -113.017 42.899  1.00 168.11 ? 166 GLU L OE1 1 
ATOM   12704 O OE2 . GLU H 4 166 ? -4.634   -114.387 41.226  1.00 167.02 ? 166 GLU L OE2 1 
ATOM   12705 N N   . GLN H 4 167 ? -6.215   -113.569 46.550  1.00 129.60 ? 167 GLN L N   1 
ATOM   12706 C CA  . GLN H 4 167 ? -6.371   -112.852 47.818  1.00 129.43 ? 167 GLN L CA  1 
ATOM   12707 C C   . GLN H 4 167 ? -7.838   -112.848 48.249  1.00 133.84 ? 167 GLN L C   1 
ATOM   12708 O O   . GLN H 4 167 ? -8.719   -112.568 47.431  1.00 134.25 ? 167 GLN L O   1 
ATOM   12709 C CB  . GLN H 4 167 ? -5.817   -111.422 47.702  1.00 131.80 ? 167 GLN L CB  1 
ATOM   12710 C CG  . GLN H 4 167 ? -5.233   -110.894 49.008  1.00 138.26 ? 167 GLN L CG  1 
ATOM   12711 C CD  . GLN H 4 167 ? -4.628   -109.516 48.900  1.00 149.04 ? 167 GLN L CD  1 
ATOM   12712 O OE1 . GLN H 4 167 ? -5.017   -108.681 48.065  1.00 143.27 ? 167 GLN L OE1 1 
ATOM   12713 N NE2 . GLN H 4 167 ? -3.688   -109.231 49.788  1.00 138.11 ? 167 GLN L NE2 1 
ATOM   12714 N N   . ASP H 4 168 ? -8.096   -113.222 49.513  1.00 129.83 ? 168 ASP L N   1 
ATOM   12715 C CA  . ASP H 4 168 ? -9.443   -113.297 50.069  1.00 129.36 ? 168 ASP L CA  1 
ATOM   12716 C C   . ASP H 4 168 ? -10.103  -111.921 50.181  1.00 134.36 ? 168 ASP L C   1 
ATOM   12717 O O   . ASP H 4 168 ? -9.441   -110.939 50.528  1.00 134.78 ? 168 ASP L O   1 
ATOM   12718 C CB  . ASP H 4 168 ? -9.431   -114.008 51.423  1.00 130.06 ? 168 ASP L CB  1 
ATOM   12719 C CG  . ASP H 4 168 ? -10.762  -114.627 51.766  1.00 137.79 ? 168 ASP L CG  1 
ATOM   12720 O OD1 . ASP H 4 168 ? -10.959  -115.817 51.452  1.00 137.83 ? 168 ASP L OD1 1 
ATOM   12721 O OD2 . ASP H 4 168 ? -11.609  -113.922 52.352  1.00 142.85 ? 168 ASP L OD2 1 
ATOM   12722 N N   . SER H 4 169 ? -11.404  -111.852 49.855  1.00 130.93 ? 169 SER L N   1 
ATOM   12723 C CA  . SER H 4 169 ? -12.200  -110.624 49.903  1.00 131.50 ? 169 SER L CA  1 
ATOM   12724 C C   . SER H 4 169 ? -12.429  -110.142 51.342  1.00 133.89 ? 169 SER L C   1 
ATOM   12725 O O   . SER H 4 169 ? -12.480  -108.934 51.588  1.00 134.92 ? 169 SER L O   1 
ATOM   12726 C CB  . SER H 4 169 ? -13.541  -110.838 49.208  1.00 135.41 ? 169 SER L CB  1 
ATOM   12727 O OG  . SER H 4 169 ? -14.318  -111.833 49.853  1.00 142.57 ? 169 SER L OG  1 
ATOM   12728 N N   . LYS H 4 170 ? -12.556  -111.087 52.279  1.00 127.70 ? 170 LYS L N   1 
ATOM   12729 C CA  . LYS H 4 170 ? -12.835  -110.780 53.670  1.00 126.73 ? 170 LYS L CA  1 
ATOM   12730 C C   . LYS H 4 170 ? -11.585  -110.549 54.520  1.00 130.61 ? 170 LYS L C   1 
ATOM   12731 O O   . LYS H 4 170 ? -11.531  -109.537 55.218  1.00 131.05 ? 170 LYS L O   1 
ATOM   12732 C CB  . LYS H 4 170 ? -13.738  -111.842 54.307  1.00 127.99 ? 170 LYS L CB  1 
ATOM   12733 C CG  . LYS H 4 170 ? -14.981  -112.218 53.493  1.00 140.33 ? 170 LYS L CG  1 
ATOM   12734 C CD  . LYS H 4 170 ? -15.660  -113.425 54.118  1.00 148.13 ? 170 LYS L CD  1 
ATOM   12735 C CE  . LYS H 4 170 ? -16.401  -114.300 53.131  1.00 150.58 ? 170 LYS L CE  1 
ATOM   12736 N NZ  . LYS H 4 170 ? -17.068  -115.459 53.795  1.00 150.76 ? 170 LYS L NZ  1 
ATOM   12737 N N   . ASP H 4 171 ? -10.586  -111.466 54.475  1.00 127.04 ? 171 ASP L N   1 
ATOM   12738 C CA  . ASP H 4 171 ? -9.396   -111.351 55.329  1.00 127.34 ? 171 ASP L CA  1 
ATOM   12739 C C   . ASP H 4 171 ? -8.041   -111.195 54.603  1.00 133.21 ? 171 ASP L C   1 
ATOM   12740 O O   . ASP H 4 171 ? -7.002   -111.255 55.267  1.00 133.03 ? 171 ASP L O   1 
ATOM   12741 C CB  . ASP H 4 171 ? -9.332   -112.531 56.317  1.00 127.56 ? 171 ASP L CB  1 
ATOM   12742 C CG  . ASP H 4 171 ? -9.176   -113.903 55.695  1.00 131.01 ? 171 ASP L CG  1 
ATOM   12743 O OD1 . ASP H 4 171 ? -9.861   -114.184 54.693  1.00 129.45 ? 171 ASP L OD1 1 
ATOM   12744 O OD2 . ASP H 4 171 ? -8.442   -114.726 56.268  1.00 136.22 ? 171 ASP L OD2 1 
ATOM   12745 N N   . SER H 4 172 ? -8.053   -110.943 53.273  1.00 131.00 ? 172 SER L N   1 
ATOM   12746 C CA  . SER H 4 172 ? -6.867   -110.720 52.425  1.00 131.93 ? 172 SER L CA  1 
ATOM   12747 C C   . SER H 4 172 ? -5.773   -111.798 52.580  1.00 135.55 ? 172 SER L C   1 
ATOM   12748 O O   . SER H 4 172 ? -4.580   -111.482 52.603  1.00 136.58 ? 172 SER L O   1 
ATOM   12749 C CB  . SER H 4 172 ? -6.304   -109.316 52.642  1.00 137.77 ? 172 SER L CB  1 
ATOM   12750 O OG  . SER H 4 172 ? -7.297   -108.326 52.435  1.00 148.95 ? 172 SER L OG  1 
ATOM   12751 N N   . THR H 4 173 ? -6.190   -113.077 52.666  1.00 130.36 ? 173 THR L N   1 
ATOM   12752 C CA  . THR H 4 173 ? -5.270   -114.204 52.836  1.00 129.47 ? 173 THR L CA  1 
ATOM   12753 C C   . THR H 4 173 ? -5.385   -115.249 51.735  1.00 132.64 ? 173 THR L C   1 
ATOM   12754 O O   . THR H 4 173 ? -6.485   -115.618 51.321  1.00 131.14 ? 173 THR L O   1 
ATOM   12755 C CB  . THR H 4 173 ? -5.441   -114.854 54.204  1.00 135.95 ? 173 THR L CB  1 
ATOM   12756 O OG1 . THR H 4 173 ? -6.777   -115.321 54.309  1.00 134.06 ? 173 THR L OG1 1 
ATOM   12757 C CG2 . THR H 4 173 ? -5.092   -113.923 55.358  1.00 135.14 ? 173 THR L CG2 1 
ATOM   12758 N N   . TYR H 4 174 ? -4.230   -115.753 51.304  1.00 130.81 ? 174 TYR L N   1 
ATOM   12759 C CA  . TYR H 4 174 ? -4.091   -116.767 50.265  1.00 131.23 ? 174 TYR L CA  1 
ATOM   12760 C C   . TYR H 4 174 ? -4.146   -118.173 50.873  1.00 136.04 ? 174 TYR L C   1 
ATOM   12761 O O   . TYR H 4 174 ? -3.926   -118.337 52.074  1.00 135.89 ? 174 TYR L O   1 
ATOM   12762 C CB  . TYR H 4 174 ? -2.773   -116.560 49.491  1.00 133.28 ? 174 TYR L CB  1 
ATOM   12763 C CG  . TYR H 4 174 ? -2.597   -115.167 48.921  1.00 135.95 ? 174 TYR L CG  1 
ATOM   12764 C CD1 . TYR H 4 174 ? -3.056   -114.851 47.648  1.00 138.31 ? 174 TYR L CD1 1 
ATOM   12765 C CD2 . TYR H 4 174 ? -1.956   -114.171 49.649  1.00 137.67 ? 174 TYR L CD2 1 
ATOM   12766 C CE1 . TYR H 4 174 ? -2.884   -113.574 47.112  1.00 140.51 ? 174 TYR L CE1 1 
ATOM   12767 C CE2 . TYR H 4 174 ? -1.794   -112.887 49.132  1.00 139.76 ? 174 TYR L CE2 1 
ATOM   12768 C CZ  . TYR H 4 174 ? -2.263   -112.592 47.863  1.00 147.47 ? 174 TYR L CZ  1 
ATOM   12769 O OH  . TYR H 4 174 ? -2.113   -111.330 47.349  1.00 149.51 ? 174 TYR L OH  1 
ATOM   12770 N N   . SER H 4 175 ? -4.448   -119.184 50.039  1.00 132.75 ? 175 SER L N   1 
ATOM   12771 C CA  . SER H 4 175 ? -4.535   -120.588 50.440  1.00 132.48 ? 175 SER L CA  1 
ATOM   12772 C C   . SER H 4 175 ? -3.925   -121.504 49.361  1.00 137.65 ? 175 SER L C   1 
ATOM   12773 O O   . SER H 4 175 ? -4.122   -121.252 48.167  1.00 137.59 ? 175 SER L O   1 
ATOM   12774 C CB  . SER H 4 175 ? -5.982   -120.970 50.742  1.00 134.63 ? 175 SER L CB  1 
ATOM   12775 O OG  . SER H 4 175 ? -6.572   -120.097 51.693  1.00 138.98 ? 175 SER L OG  1 
ATOM   12776 N N   . LEU H 4 176 ? -3.171   -122.548 49.779  1.00 135.06 ? 176 LEU L N   1 
ATOM   12777 C CA  . LEU H 4 176 ? -2.510   -123.495 48.867  1.00 135.81 ? 176 LEU L CA  1 
ATOM   12778 C C   . LEU H 4 176 ? -3.051   -124.915 49.028  1.00 141.19 ? 176 LEU L C   1 
ATOM   12779 O O   . LEU H 4 176 ? -3.391   -125.331 50.139  1.00 141.17 ? 176 LEU L O   1 
ATOM   12780 C CB  . LEU H 4 176 ? -0.978   -123.485 49.086  1.00 136.30 ? 176 LEU L CB  1 
ATOM   12781 C CG  . LEU H 4 176 ? -0.082   -124.036 47.955  1.00 141.34 ? 176 LEU L CG  1 
ATOM   12782 C CD1 . LEU H 4 176 ? 1.206    -123.251 47.851  1.00 141.50 ? 176 LEU L CD1 1 
ATOM   12783 C CD2 . LEU H 4 176 ? 0.247    -125.505 48.159  1.00 145.26 ? 176 LEU L CD2 1 
ATOM   12784 N N   . SER H 4 177 ? -3.087   -125.666 47.914  1.00 138.78 ? 177 SER L N   1 
ATOM   12785 C CA  . SER H 4 177 ? -3.518   -127.059 47.862  1.00 140.56 ? 177 SER L CA  1 
ATOM   12786 C C   . SER H 4 177 ? -2.553   -127.859 46.977  1.00 146.76 ? 177 SER L C   1 
ATOM   12787 O O   . SER H 4 177 ? -2.558   -127.701 45.751  1.00 146.55 ? 177 SER L O   1 
ATOM   12788 C CB  . SER H 4 177 ? -4.954   -127.158 47.351  1.00 144.34 ? 177 SER L CB  1 
ATOM   12789 O OG  . SER H 4 177 ? -5.327   -128.494 47.054  1.00 155.81 ? 177 SER L OG  1 
ATOM   12790 N N   . SER H 4 178 ? -1.700   -128.689 47.607  1.00 144.94 ? 178 SER L N   1 
ATOM   12791 C CA  . SER H 4 178 ? -0.734   -129.530 46.895  1.00 146.33 ? 178 SER L CA  1 
ATOM   12792 C C   . SER H 4 178 ? -1.264   -130.966 46.848  1.00 152.38 ? 178 SER L C   1 
ATOM   12793 O O   . SER H 4 178 ? -1.588   -131.532 47.892  1.00 152.72 ? 178 SER L O   1 
ATOM   12794 C CB  . SER H 4 178 ? 0.643    -129.463 47.555  1.00 149.57 ? 178 SER L CB  1 
ATOM   12795 O OG  . SER H 4 178 ? 1.653    -129.958 46.689  1.00 157.30 ? 178 SER L OG  1 
ATOM   12796 N N   . THR H 4 179 ? -1.393   -131.532 45.634  1.00 149.94 ? 179 THR L N   1 
ATOM   12797 C CA  . THR H 4 179 ? -1.922   -132.881 45.421  1.00 152.69 ? 179 THR L CA  1 
ATOM   12798 C C   . THR H 4 179 ? -0.813   -133.869 45.045  1.00 159.55 ? 179 THR L C   1 
ATOM   12799 O O   . THR H 4 179 ? -0.131   -133.671 44.038  1.00 158.44 ? 179 THR L O   1 
ATOM   12800 C CB  . THR H 4 179 ? -3.084   -132.844 44.412  1.00 158.90 ? 179 THR L CB  1 
ATOM   12801 O OG1 . THR H 4 179 ? -3.973   -131.780 44.758  1.00 154.14 ? 179 THR L OG1 1 
ATOM   12802 C CG2 . THR H 4 179 ? -3.855   -134.160 44.351  1.00 161.05 ? 179 THR L CG2 1 
ATOM   12803 N N   . LEU H 4 180 ? -0.652   -134.935 45.857  1.00 164.65 ? 180 LEU L N   1 
ATOM   12804 C CA  . LEU H 4 180 ? 0.354    -135.983 45.671  1.00 166.07 ? 180 LEU L CA  1 
ATOM   12805 C C   . LEU H 4 180 ? -0.244   -137.224 44.981  1.00 175.38 ? 180 LEU L C   1 
ATOM   12806 O O   . LEU H 4 180 ? -0.656   -138.176 45.650  1.00 175.29 ? 180 LEU L O   1 
ATOM   12807 C CB  . LEU H 4 180 ? 1.015    -136.335 47.025  1.00 164.23 ? 180 LEU L CB  1 
ATOM   12808 C CG  . LEU H 4 180 ? 2.223    -137.282 47.000  1.00 169.41 ? 180 LEU L CG  1 
ATOM   12809 C CD1 . LEU H 4 180 ? 3.494    -136.552 46.621  1.00 168.44 ? 180 LEU L CD1 1 
ATOM   12810 C CD2 . LEU H 4 180 ? 2.412    -137.937 48.341  1.00 170.43 ? 180 LEU L CD2 1 
ATOM   12811 N N   . THR H 4 181 ? -0.285   -137.199 43.631  1.00 176.50 ? 181 THR L N   1 
ATOM   12812 C CA  . THR H 4 181 ? -0.814   -138.286 42.795  1.00 181.45 ? 181 THR L CA  1 
ATOM   12813 C C   . THR H 4 181 ? 0.149    -139.483 42.793  1.00 188.08 ? 181 THR L C   1 
ATOM   12814 O O   . THR H 4 181 ? 1.287    -139.349 42.333  1.00 187.14 ? 181 THR L O   1 
ATOM   12815 C CB  . THR H 4 181 ? -1.169   -137.786 41.372  1.00 192.70 ? 181 THR L CB  1 
ATOM   12816 O OG1 . THR H 4 181 ? -0.046   -137.108 40.803  1.00 191.61 ? 181 THR L OG1 1 
ATOM   12817 C CG2 . THR H 4 181 ? -2.393   -136.876 41.350  1.00 191.79 ? 181 THR L CG2 1 
ATOM   12818 N N   . LEU H 4 182 ? -0.307   -140.641 43.335  1.00 187.28 ? 182 LEU L N   1 
ATOM   12819 C CA  . LEU H 4 182 ? 0.472    -141.887 43.437  1.00 188.33 ? 182 LEU L CA  1 
ATOM   12820 C C   . LEU H 4 182 ? -0.359   -143.159 43.202  1.00 196.84 ? 182 LEU L C   1 
ATOM   12821 O O   . LEU H 4 182 ? -1.556   -143.182 43.492  1.00 197.68 ? 182 LEU L O   1 
ATOM   12822 C CB  . LEU H 4 182 ? 1.169    -141.980 44.812  1.00 184.78 ? 182 LEU L CB  1 
ATOM   12823 C CG  . LEU H 4 182 ? 2.712    -142.006 44.860  1.00 187.86 ? 182 LEU L CG  1 
ATOM   12824 C CD1 . LEU H 4 182 ? 3.314    -143.039 43.907  1.00 190.59 ? 182 LEU L CD1 1 
ATOM   12825 C CD2 . LEU H 4 182 ? 3.309    -140.626 44.649  1.00 188.34 ? 182 LEU L CD2 1 
ATOM   12826 N N   . SER H 4 183 ? 0.292    -144.226 42.705  1.00 195.80 ? 183 SER L N   1 
ATOM   12827 C CA  . SER H 4 183 ? -0.343   -145.523 42.459  1.00 199.49 ? 183 SER L CA  1 
ATOM   12828 C C   . SER H 4 183 ? -0.518   -146.290 43.773  1.00 202.27 ? 183 SER L C   1 
ATOM   12829 O O   . SER H 4 183 ? 0.223    -146.034 44.727  1.00 198.23 ? 183 SER L O   1 
ATOM   12830 C CB  . SER H 4 183 ? 0.491    -146.344 41.481  1.00 205.62 ? 183 SER L CB  1 
ATOM   12831 O OG  . SER H 4 183 ? 1.789    -146.601 41.991  1.00 210.30 ? 183 SER L OG  1 
ATOM   12832 N N   . LYS H 4 184 ? -1.486   -147.234 43.819  1.00 202.50 ? 184 LYS L N   1 
ATOM   12833 C CA  . LYS H 4 184 ? -1.765   -148.061 45.002  1.00 201.45 ? 184 LYS L CA  1 
ATOM   12834 C C   . LYS H 4 184 ? -0.609   -149.026 45.303  1.00 206.11 ? 184 LYS L C   1 
ATOM   12835 O O   . LYS H 4 184 ? -0.359   -149.324 46.473  1.00 202.79 ? 184 LYS L O   1 
ATOM   12836 C CB  . LYS H 4 184 ? -3.089   -148.831 44.841  1.00 207.35 ? 184 LYS L CB  1 
ATOM   12837 C CG  . LYS H 4 184 ? -3.729   -149.225 46.169  1.00 215.72 ? 184 LYS L CG  1 
ATOM   12838 C CD  . LYS H 4 184 ? -4.866   -150.217 45.995  1.00 227.38 ? 184 LYS L CD  1 
ATOM   12839 C CE  . LYS H 4 184 ? -5.418   -150.658 47.330  1.00 234.37 ? 184 LYS L CE  1 
ATOM   12840 N NZ  . LYS H 4 184 ? -6.469   -151.698 47.186  1.00 245.73 ? 184 LYS L NZ  1 
ATOM   12841 N N   . ALA H 4 185 ? 0.092    -149.495 44.243  1.00 206.84 ? 185 ALA L N   1 
ATOM   12842 C CA  . ALA H 4 185 ? 1.238    -150.410 44.317  1.00 207.05 ? 185 ALA L CA  1 
ATOM   12843 C C   . ALA H 4 185 ? 2.410    -149.795 45.095  1.00 208.84 ? 185 ALA L C   1 
ATOM   12844 O O   . ALA H 4 185 ? 2.995    -150.465 45.950  1.00 206.68 ? 185 ALA L O   1 
ATOM   12845 C CB  . ALA H 4 185 ? 1.683    -150.805 42.915  1.00 211.41 ? 185 ALA L CB  1 
ATOM   12846 N N   . ASP H 4 186 ? 2.728    -148.514 44.814  1.00 205.69 ? 186 ASP L N   1 
ATOM   12847 C CA  . ASP H 4 186 ? 3.797    -147.763 45.475  1.00 202.94 ? 186 ASP L CA  1 
ATOM   12848 C C   . ASP H 4 186 ? 3.356    -147.260 46.855  1.00 205.90 ? 186 ASP L C   1 
ATOM   12849 O O   . ASP H 4 186 ? 4.210    -146.965 47.694  1.00 203.44 ? 186 ASP L O   1 
ATOM   12850 C CB  . ASP H 4 186 ? 4.256    -146.588 44.593  1.00 204.63 ? 186 ASP L CB  1 
ATOM   12851 C CG  . ASP H 4 186 ? 4.915    -146.992 43.285  1.00 218.46 ? 186 ASP L CG  1 
ATOM   12852 O OD1 . ASP H 4 186 ? 6.086    -146.610 43.068  1.00 217.94 ? 186 ASP L OD1 1 
ATOM   12853 O OD2 . ASP H 4 186 ? 4.250    -147.669 42.466  1.00 228.42 ? 186 ASP L OD2 1 
ATOM   12854 N N   . TYR H 4 187 ? 2.027    -147.168 47.085  1.00 204.26 ? 187 TYR L N   1 
ATOM   12855 C CA  . TYR H 4 187 ? 1.428    -146.704 48.342  1.00 202.48 ? 187 TYR L CA  1 
ATOM   12856 C C   . TYR H 4 187 ? 1.570    -147.725 49.479  1.00 207.42 ? 187 TYR L C   1 
ATOM   12857 O O   . TYR H 4 187 ? 1.730    -147.328 50.635  1.00 205.35 ? 187 TYR L O   1 
ATOM   12858 C CB  . TYR H 4 187 ? -0.050   -146.327 48.134  1.00 204.59 ? 187 TYR L CB  1 
ATOM   12859 C CG  . TYR H 4 187 ? -0.623   -145.465 49.238  1.00 203.61 ? 187 TYR L CG  1 
ATOM   12860 C CD1 . TYR H 4 187 ? -0.510   -144.079 49.198  1.00 203.77 ? 187 TYR L CD1 1 
ATOM   12861 C CD2 . TYR H 4 187 ? -1.305   -146.033 50.310  1.00 204.04 ? 187 TYR L CD2 1 
ATOM   12862 C CE1 . TYR H 4 187 ? -1.047   -143.279 50.205  1.00 202.77 ? 187 TYR L CE1 1 
ATOM   12863 C CE2 . TYR H 4 187 ? -1.842   -145.245 51.325  1.00 203.19 ? 187 TYR L CE2 1 
ATOM   12864 C CZ  . TYR H 4 187 ? -1.708   -143.868 51.271  1.00 209.52 ? 187 TYR L CZ  1 
ATOM   12865 O OH  . TYR H 4 187 ? -2.230   -143.094 52.277  1.00 209.81 ? 187 TYR L OH  1 
ATOM   12866 N N   . GLU H 4 188 ? 1.489    -149.029 49.156  1.00 206.50 ? 188 GLU L N   1 
ATOM   12867 C CA  . GLU H 4 188 ? 1.604    -150.107 50.140  1.00 206.05 ? 188 GLU L CA  1 
ATOM   12868 C C   . GLU H 4 188 ? 3.044    -150.345 50.614  1.00 208.36 ? 188 GLU L C   1 
ATOM   12869 O O   . GLU H 4 188 ? 3.240    -150.898 51.699  1.00 207.08 ? 188 GLU L O   1 
ATOM   12870 C CB  . GLU H 4 188 ? 0.957    -151.398 49.616  1.00 210.20 ? 188 GLU L CB  1 
ATOM   12871 C CG  . GLU H 4 188 ? -0.345   -151.766 50.315  1.00 223.12 ? 188 GLU L CG  1 
ATOM   12872 C CD  . GLU H 4 188 ? -1.525   -150.829 50.126  1.00 247.72 ? 188 GLU L CD  1 
ATOM   12873 O OE1 . GLU H 4 188 ? -1.905   -150.567 48.962  1.00 247.94 ? 188 GLU L OE1 1 
ATOM   12874 O OE2 . GLU H 4 188 ? -2.099   -150.392 51.150  1.00 239.06 ? 188 GLU L OE2 1 
ATOM   12875 N N   . LYS H 4 189 ? 4.041    -149.912 49.811  1.00 204.89 ? 189 LYS L N   1 
ATOM   12876 C CA  . LYS H 4 189 ? 5.474    -150.032 50.112  1.00 203.81 ? 189 LYS L CA  1 
ATOM   12877 C C   . LYS H 4 189 ? 5.898    -149.131 51.289  1.00 205.59 ? 189 LYS L C   1 
ATOM   12878 O O   . LYS H 4 189 ? 6.723    -149.542 52.110  1.00 205.13 ? 189 LYS L O   1 
ATOM   12879 C CB  . LYS H 4 189 ? 6.322    -149.709 48.867  1.00 206.90 ? 189 LYS L CB  1 
ATOM   12880 C CG  . LYS H 4 189 ? 6.372    -150.823 47.828  1.00 220.09 ? 189 LYS L CG  1 
ATOM   12881 C CD  . LYS H 4 189 ? 7.399    -150.514 46.746  1.00 227.52 ? 189 LYS L CD  1 
ATOM   12882 C CE  . LYS H 4 189 ? 7.536    -151.626 45.738  1.00 236.92 ? 189 LYS L CE  1 
ATOM   12883 N NZ  . LYS H 4 189 ? 8.572    -151.314 44.720  1.00 244.14 ? 189 LYS L NZ  1 
ATOM   12884 N N   . HIS H 4 190 ? 5.332    -147.906 51.354  1.00 200.36 ? 190 HIS L N   1 
ATOM   12885 C CA  . HIS H 4 190 ? 5.602    -146.888 52.380  1.00 198.14 ? 190 HIS L CA  1 
ATOM   12886 C C   . HIS H 4 190 ? 4.460    -146.817 53.410  1.00 198.70 ? 190 HIS L C   1 
ATOM   12887 O O   . HIS H 4 190 ? 3.424    -147.459 53.209  1.00 198.73 ? 190 HIS L O   1 
ATOM   12888 C CB  . HIS H 4 190 ? 5.838    -145.521 51.714  1.00 198.40 ? 190 HIS L CB  1 
ATOM   12889 C CG  . HIS H 4 190 ? 6.862    -145.561 50.621  1.00 202.56 ? 190 HIS L CG  1 
ATOM   12890 N ND1 . HIS H 4 190 ? 8.217    -145.561 50.901  1.00 204.30 ? 190 HIS L ND1 1 
ATOM   12891 C CD2 . HIS H 4 190 ? 6.693    -145.626 49.280  1.00 205.36 ? 190 HIS L CD2 1 
ATOM   12892 C CE1 . HIS H 4 190 ? 8.826    -145.616 49.727  1.00 204.34 ? 190 HIS L CE1 1 
ATOM   12893 N NE2 . HIS H 4 190 ? 7.950    -145.657 48.722  1.00 205.40 ? 190 HIS L NE2 1 
ATOM   12894 N N   . LYS H 4 191 ? 4.649    -146.065 54.521  1.00 192.64 ? 191 LYS L N   1 
ATOM   12895 C CA  . LYS H 4 191 ? 3.627    -145.974 55.571  1.00 191.62 ? 191 LYS L CA  1 
ATOM   12896 C C   . LYS H 4 191 ? 3.355    -144.554 56.100  1.00 192.28 ? 191 LYS L C   1 
ATOM   12897 O O   . LYS H 4 191 ? 2.196    -144.229 56.364  1.00 191.28 ? 191 LYS L O   1 
ATOM   12898 C CB  . LYS H 4 191 ? 3.958    -146.925 56.737  1.00 195.36 ? 191 LYS L CB  1 
ATOM   12899 C CG  . LYS H 4 191 ? 3.591    -148.393 56.480  1.00 212.93 ? 191 LYS L CG  1 
ATOM   12900 C CD  . LYS H 4 191 ? 4.781    -149.229 55.989  1.00 223.95 ? 191 LYS L CD  1 
ATOM   12901 C CE  . LYS H 4 191 ? 4.359    -150.583 55.469  1.00 235.44 ? 191 LYS L CE  1 
ATOM   12902 N NZ  . LYS H 4 191 ? 5.510    -151.349 54.920  1.00 243.71 ? 191 LYS L NZ  1 
ATOM   12903 N N   . VAL H 4 192 ? 4.401    -143.723 56.278  1.00 187.14 ? 192 VAL L N   1 
ATOM   12904 C CA  . VAL H 4 192 ? 4.242    -142.360 56.811  1.00 185.46 ? 192 VAL L CA  1 
ATOM   12905 C C   . VAL H 4 192 ? 4.487    -141.293 55.719  1.00 186.64 ? 192 VAL L C   1 
ATOM   12906 O O   . VAL H 4 192 ? 5.558    -141.262 55.106  1.00 186.35 ? 192 VAL L O   1 
ATOM   12907 C CB  . VAL H 4 192 ? 5.085    -142.122 58.100  1.00 190.25 ? 192 VAL L CB  1 
ATOM   12908 C CG1 . VAL H 4 192 ? 4.939    -140.692 58.618  1.00 189.49 ? 192 VAL L CG1 1 
ATOM   12909 C CG2 . VAL H 4 192 ? 4.710    -143.119 59.196  1.00 191.37 ? 192 VAL L CG2 1 
ATOM   12910 N N   . TYR H 4 193 ? 3.483    -140.418 55.497  1.00 180.72 ? 193 TYR L N   1 
ATOM   12911 C CA  . TYR H 4 193 ? 3.519    -139.342 54.499  1.00 178.47 ? 193 TYR L CA  1 
ATOM   12912 C C   . TYR H 4 193 ? 3.415    -137.965 55.159  1.00 180.23 ? 193 TYR L C   1 
ATOM   12913 O O   . TYR H 4 193 ? 2.515    -137.740 55.972  1.00 180.12 ? 193 TYR L O   1 
ATOM   12914 C CB  . TYR H 4 193 ? 2.398    -139.523 53.463  1.00 179.18 ? 193 TYR L CB  1 
ATOM   12915 C CG  . TYR H 4 193 ? 2.344    -140.897 52.830  1.00 181.60 ? 193 TYR L CG  1 
ATOM   12916 C CD1 . TYR H 4 193 ? 1.479    -141.875 53.312  1.00 184.49 ? 193 TYR L CD1 1 
ATOM   12917 C CD2 . TYR H 4 193 ? 3.138    -141.211 51.732  1.00 182.56 ? 193 TYR L CD2 1 
ATOM   12918 C CE1 . TYR H 4 193 ? 1.423    -143.140 52.729  1.00 186.75 ? 193 TYR L CE1 1 
ATOM   12919 C CE2 . TYR H 4 193 ? 3.083    -142.468 51.134  1.00 184.86 ? 193 TYR L CE2 1 
ATOM   12920 C CZ  . TYR H 4 193 ? 2.222    -143.429 51.634  1.00 192.88 ? 193 TYR L CZ  1 
ATOM   12921 O OH  . TYR H 4 193 ? 2.174    -144.666 51.041  1.00 195.00 ? 193 TYR L OH  1 
ATOM   12922 N N   . ALA H 4 194 ? 4.326    -137.044 54.795  1.00 174.65 ? 194 ALA L N   1 
ATOM   12923 C CA  . ALA H 4 194 ? 4.391    -135.690 55.351  1.00 172.89 ? 194 ALA L CA  1 
ATOM   12924 C C   . ALA H 4 194 ? 4.607    -134.604 54.285  1.00 173.40 ? 194 ALA L C   1 
ATOM   12925 O O   . ALA H 4 194 ? 4.928    -134.926 53.143  1.00 172.94 ? 194 ALA L O   1 
ATOM   12926 C CB  . ALA H 4 194 ? 5.504    -135.625 56.385  1.00 174.95 ? 194 ALA L CB  1 
ATOM   12927 N N   . CYS H 4 195 ? 4.418    -133.320 54.664  1.00 167.43 ? 195 CYS L N   1 
ATOM   12928 C CA  . CYS H 4 195 ? 4.640    -132.152 53.804  1.00 164.95 ? 195 CYS L CA  1 
ATOM   12929 C C   . CYS H 4 195 ? 5.309    -131.009 54.585  1.00 166.69 ? 195 CYS L C   1 
ATOM   12930 O O   . CYS H 4 195 ? 4.752    -130.529 55.572  1.00 166.01 ? 195 CYS L O   1 
ATOM   12931 C CB  . CYS H 4 195 ? 3.366    -131.702 53.077  1.00 164.02 ? 195 CYS L CB  1 
ATOM   12932 S SG  . CYS H 4 195 ? 1.979    -131.250 54.163  1.00 167.45 ? 195 CYS L SG  1 
ATOM   12933 N N   . GLU H 4 196 ? 6.538    -130.630 54.184  1.00 162.57 ? 196 GLU L N   1 
ATOM   12934 C CA  . GLU H 4 196 ? 7.308    -129.564 54.832  1.00 162.33 ? 196 GLU L CA  1 
ATOM   12935 C C   . GLU H 4 196 ? 6.869    -128.205 54.282  1.00 162.82 ? 196 GLU L C   1 
ATOM   12936 O O   . GLU H 4 196 ? 6.987    -127.959 53.081  1.00 161.47 ? 196 GLU L O   1 
ATOM   12937 C CB  . GLU H 4 196 ? 8.828    -129.783 54.661  1.00 165.22 ? 196 GLU L CB  1 
ATOM   12938 C CG  . GLU H 4 196 ? 9.678    -128.978 55.635  1.00 179.03 ? 196 GLU L CG  1 
ATOM   12939 C CD  . GLU H 4 196 ? 11.176   -128.983 55.387  1.00 202.70 ? 196 GLU L CD  1 
ATOM   12940 O OE1 . GLU H 4 196 ? 11.921   -129.440 56.283  1.00 192.70 ? 196 GLU L OE1 1 
ATOM   12941 O OE2 . GLU H 4 196 ? 11.608   -128.497 54.316  1.00 198.96 ? 196 GLU L OE2 1 
ATOM   12942 N N   . VAL H 4 197 ? 6.340    -127.341 55.162  1.00 157.85 ? 197 VAL L N   1 
ATOM   12943 C CA  . VAL H 4 197 ? 5.849    -126.003 54.814  1.00 154.86 ? 197 VAL L CA  1 
ATOM   12944 C C   . VAL H 4 197 ? 6.861    -124.942 55.257  1.00 158.94 ? 197 VAL L C   1 
ATOM   12945 O O   . VAL H 4 197 ? 7.251    -124.910 56.426  1.00 161.58 ? 197 VAL L O   1 
ATOM   12946 C CB  . VAL H 4 197 ? 4.417    -125.767 55.370  1.00 157.72 ? 197 VAL L CB  1 
ATOM   12947 C CG1 . VAL H 4 197 ? 3.973    -124.317 55.209  1.00 155.31 ? 197 VAL L CG1 1 
ATOM   12948 C CG2 . VAL H 4 197 ? 3.420    -126.707 54.704  1.00 157.17 ? 197 VAL L CG2 1 
ATOM   12949 N N   . THR H 4 198 ? 7.297    -124.096 54.310  1.00 152.52 ? 198 THR L N   1 
ATOM   12950 C CA  . THR H 4 198 ? 8.276    -123.027 54.528  1.00 152.11 ? 198 THR L CA  1 
ATOM   12951 C C   . THR H 4 198 ? 7.632    -121.677 54.191  1.00 152.67 ? 198 THR L C   1 
ATOM   12952 O O   . THR H 4 198 ? 7.322    -121.422 53.026  1.00 150.27 ? 198 THR L O   1 
ATOM   12953 C CB  . THR H 4 198 ? 9.551    -123.307 53.708  1.00 161.61 ? 198 THR L CB  1 
ATOM   12954 O OG1 . THR H 4 198 ? 9.187    -123.519 52.342  1.00 160.09 ? 198 THR L OG1 1 
ATOM   12955 C CG2 . THR H 4 198 ? 10.330   -124.519 54.217  1.00 163.12 ? 198 THR L CG2 1 
ATOM   12956 N N   . HIS H 4 199 ? 7.401    -120.829 55.215  1.00 149.27 ? 199 HIS L N   1 
ATOM   12957 C CA  . HIS H 4 199 ? 6.739    -119.521 55.067  1.00 146.59 ? 199 HIS L CA  1 
ATOM   12958 C C   . HIS H 4 199 ? 7.317    -118.435 56.007  1.00 151.60 ? 199 HIS L C   1 
ATOM   12959 O O   . HIS H 4 199 ? 7.989    -118.767 56.990  1.00 155.14 ? 199 HIS L O   1 
ATOM   12960 C CB  . HIS H 4 199 ? 5.218    -119.692 55.283  1.00 146.33 ? 199 HIS L CB  1 
ATOM   12961 C CG  . HIS H 4 199 ? 4.396    -118.482 54.965  1.00 147.04 ? 199 HIS L CG  1 
ATOM   12962 N ND1 . HIS H 4 199 ? 3.823    -117.721 55.963  1.00 149.01 ? 199 HIS L ND1 1 
ATOM   12963 C CD2 . HIS H 4 199 ? 4.080    -117.939 53.766  1.00 146.20 ? 199 HIS L CD2 1 
ATOM   12964 C CE1 . HIS H 4 199 ? 3.175    -116.747 55.345  1.00 145.70 ? 199 HIS L CE1 1 
ATOM   12965 N NE2 . HIS H 4 199 ? 3.301    -116.837 54.023  1.00 144.28 ? 199 HIS L NE2 1 
ATOM   12966 N N   . GLN H 4 200 ? 7.058    -117.138 55.686  1.00 144.56 ? 200 GLN L N   1 
ATOM   12967 C CA  . GLN H 4 200 ? 7.498    -115.969 56.462  1.00 144.46 ? 200 GLN L CA  1 
ATOM   12968 C C   . GLN H 4 200 ? 6.774    -115.884 57.820  1.00 148.34 ? 200 GLN L C   1 
ATOM   12969 O O   . GLN H 4 200 ? 7.379    -115.464 58.808  1.00 150.54 ? 200 GLN L O   1 
ATOM   12970 C CB  . GLN H 4 200 ? 7.307    -114.668 55.655  1.00 142.05 ? 200 GLN L CB  1 
ATOM   12971 C CG  . GLN H 4 200 ? 8.139    -113.486 56.174  1.00 152.83 ? 200 GLN L CG  1 
ATOM   12972 C CD  . GLN H 4 200 ? 7.835    -112.152 55.525  1.00 163.78 ? 200 GLN L CD  1 
ATOM   12973 O OE1 . GLN H 4 200 ? 7.040    -112.039 54.585  1.00 156.26 ? 200 GLN L OE1 1 
ATOM   12974 N NE2 . GLN H 4 200 ? 8.473    -111.100 56.017  1.00 154.08 ? 200 GLN L NE2 1 
ATOM   12975 N N   . GLY H 4 201 ? 5.504    -116.294 57.845  1.00 142.66 ? 201 GLY L N   1 
ATOM   12976 C CA  . GLY H 4 201 ? 4.667    -116.301 59.042  1.00 143.91 ? 201 GLY L CA  1 
ATOM   12977 C C   . GLY H 4 201 ? 5.083    -117.325 60.080  1.00 151.58 ? 201 GLY L C   1 
ATOM   12978 O O   . GLY H 4 201 ? 4.755    -117.174 61.260  1.00 153.38 ? 201 GLY L O   1 
ATOM   12979 N N   . LEU H 4 202 ? 5.813    -118.375 59.643  1.00 149.46 ? 202 LEU L N   1 
ATOM   12980 C CA  . LEU H 4 202 ? 6.313    -119.464 60.482  1.00 153.56 ? 202 LEU L CA  1 
ATOM   12981 C C   . LEU H 4 202 ? 7.677    -119.159 61.088  1.00 163.40 ? 202 LEU L C   1 
ATOM   12982 O O   . LEU H 4 202 ? 8.578    -118.685 60.389  1.00 161.52 ? 202 LEU L O   1 
ATOM   12983 C CB  . LEU H 4 202 ? 6.388    -120.773 59.681  1.00 152.53 ? 202 LEU L CB  1 
ATOM   12984 C CG  . LEU H 4 202 ? 5.093    -121.558 59.562  1.00 155.66 ? 202 LEU L CG  1 
ATOM   12985 C CD1 . LEU H 4 202 ? 4.963    -122.177 58.197  1.00 153.37 ? 202 LEU L CD1 1 
ATOM   12986 C CD2 . LEU H 4 202 ? 5.011    -122.634 60.617  1.00 161.54 ? 202 LEU L CD2 1 
ATOM   12987 N N   . SER H 4 203 ? 7.823    -119.455 62.396  1.00 166.83 ? 203 SER L N   1 
ATOM   12988 C CA  . SER H 4 203 ? 9.061    -119.286 63.164  1.00 172.43 ? 203 SER L CA  1 
ATOM   12989 C C   . SER H 4 203 ? 10.059   -120.384 62.768  1.00 179.29 ? 203 SER L C   1 
ATOM   12990 O O   . SER H 4 203 ? 11.253   -120.121 62.605  1.00 180.75 ? 203 SER L O   1 
ATOM   12991 C CB  . SER H 4 203 ? 8.773    -119.349 64.663  1.00 180.98 ? 203 SER L CB  1 
ATOM   12992 O OG  . SER H 4 203 ? 8.190    -120.588 65.036  1.00 190.69 ? 203 SER L OG  1 
ATOM   12993 N N   . SER H 4 204 ? 9.545    -121.611 62.604  1.00 176.01 ? 204 SER L N   1 
ATOM   12994 C CA  . SER H 4 204 ? 10.306   -122.791 62.215  1.00 177.33 ? 204 SER L CA  1 
ATOM   12995 C C   . SER H 4 204 ? 9.568    -123.515 61.080  1.00 179.43 ? 204 SER L C   1 
ATOM   12996 O O   . SER H 4 204 ? 8.334    -123.586 61.128  1.00 177.36 ? 204 SER L O   1 
ATOM   12997 C CB  . SER H 4 204 ? 10.476   -123.723 63.411  1.00 184.66 ? 204 SER L CB  1 
ATOM   12998 O OG  . SER H 4 204 ? 9.226    -124.019 64.014  1.00 190.69 ? 204 SER L OG  1 
ATOM   12999 N N   . PRO H 4 205 ? 10.281   -124.051 60.053  1.00 176.08 ? 205 PRO L N   1 
ATOM   13000 C CA  . PRO H 4 205 ? 9.586    -124.766 58.964  1.00 172.63 ? 205 PRO L CA  1 
ATOM   13001 C C   . PRO H 4 205 ? 8.995    -126.096 59.446  1.00 178.59 ? 205 PRO L C   1 
ATOM   13002 O O   . PRO H 4 205 ? 9.656    -127.140 59.391  1.00 179.71 ? 205 PRO L O   1 
ATOM   13003 C CB  . PRO H 4 205 ? 10.680   -124.948 57.896  1.00 173.62 ? 205 PRO L CB  1 
ATOM   13004 C CG  . PRO H 4 205 ? 11.841   -124.103 58.343  1.00 180.48 ? 205 PRO L CG  1 
ATOM   13005 C CD  . PRO H 4 205 ? 11.740   -124.044 59.830  1.00 179.86 ? 205 PRO L CD  1 
ATOM   13006 N N   . VAL H 4 206 ? 7.748    -126.039 59.954  1.00 175.28 ? 206 VAL L N   1 
ATOM   13007 C CA  . VAL H 4 206 ? 7.040    -127.191 60.508  1.00 176.82 ? 206 VAL L CA  1 
ATOM   13008 C C   . VAL H 4 206 ? 6.584    -128.154 59.407  1.00 179.49 ? 206 VAL L C   1 
ATOM   13009 O O   . VAL H 4 206 ? 6.325    -127.738 58.276  1.00 175.86 ? 206 VAL L O   1 
ATOM   13010 C CB  . VAL H 4 206 ? 5.897    -126.769 61.476  1.00 181.39 ? 206 VAL L CB  1 
ATOM   13011 C CG1 . VAL H 4 206 ? 4.598    -126.451 60.738  1.00 177.57 ? 206 VAL L CG1 1 
ATOM   13012 C CG2 . VAL H 4 206 ? 5.673    -127.816 62.565  1.00 184.36 ? 206 VAL L CG2 1 
ATOM   13013 N N   . THR H 4 207 ? 6.523    -129.447 59.753  1.00 171.15 ? 207 THR L N   1 
ATOM   13014 C CA  . THR H 4 207 ? 6.124    -130.545 58.874  1.00 171.94 ? 207 THR L CA  1 
ATOM   13015 C C   . THR H 4 207 ? 4.946    -131.280 59.531  1.00 176.16 ? 207 THR L C   1 
ATOM   13016 O O   . THR H 4 207 ? 4.945    -131.448 60.754  1.00 175.04 ? 207 THR L O   1 
ATOM   13017 C CB  . THR H 4 207 ? 7.337    -131.471 58.620  1.00 181.85 ? 207 THR L CB  1 
ATOM   13018 O OG1 . THR H 4 207 ? 8.519    -130.688 58.406  1.00 182.64 ? 207 THR L OG1 1 
ATOM   13019 C CG2 . THR H 4 207 ? 7.127    -132.408 57.443  1.00 181.47 ? 207 THR L CG2 1 
ATOM   13020 N N   . LYS H 4 208 ? 3.939    -131.694 58.732  1.00 173.88 ? 208 LYS L N   1 
ATOM   13021 C CA  . LYS H 4 208 ? 2.766    -132.409 59.249  1.00 174.15 ? 208 LYS L CA  1 
ATOM   13022 C C   . LYS H 4 208 ? 2.586    -133.774 58.574  1.00 179.66 ? 208 LYS L C   1 
ATOM   13023 O O   . LYS H 4 208 ? 2.329    -133.849 57.372  1.00 179.16 ? 208 LYS L O   1 
ATOM   13024 C CB  . LYS H 4 208 ? 1.487    -131.545 59.196  1.00 177.15 ? 208 LYS L CB  1 
ATOM   13025 C CG  . LYS H 4 208 ? 1.561    -130.220 59.985  1.00 193.82 ? 208 LYS L CG  1 
ATOM   13026 C CD  . LYS H 4 208 ? 1.809    -130.391 61.504  1.00 202.43 ? 208 LYS L CD  1 
ATOM   13027 C CE  . LYS H 4 208 ? 2.107    -129.083 62.201  1.00 206.58 ? 208 LYS L CE  1 
ATOM   13028 N NZ  . LYS H 4 208 ? 2.654    -129.293 63.570  1.00 207.39 ? 208 LYS L NZ  1 
ATOM   13029 N N   . SER H 4 209 ? 2.749    -134.852 59.371  1.00 177.76 ? 209 SER L N   1 
ATOM   13030 C CA  . SER H 4 209 ? 2.706    -136.255 58.950  1.00 178.45 ? 209 SER L CA  1 
ATOM   13031 C C   . SER H 4 209 ? 1.439    -137.025 59.342  1.00 184.70 ? 209 SER L C   1 
ATOM   13032 O O   . SER H 4 209 ? 0.713    -136.612 60.249  1.00 184.20 ? 209 SER L O   1 
ATOM   13033 C CB  . SER H 4 209 ? 3.931    -136.992 59.484  1.00 181.65 ? 209 SER L CB  1 
ATOM   13034 O OG  . SER H 4 209 ? 3.995    -136.928 60.901  1.00 189.92 ? 209 SER L OG  1 
ATOM   13035 N N   . PHE H 4 210 ? 1.200    -138.170 58.662  1.00 183.47 ? 210 PHE L N   1 
ATOM   13036 C CA  . PHE H 4 210 ? 0.076    -139.077 58.913  1.00 184.39 ? 210 PHE L CA  1 
ATOM   13037 C C   . PHE H 4 210 ? 0.482    -140.553 58.752  1.00 190.99 ? 210 PHE L C   1 
ATOM   13038 O O   . PHE H 4 210 ? 1.158    -140.909 57.782  1.00 190.84 ? 210 PHE L O   1 
ATOM   13039 C CB  . PHE H 4 210 ? -1.173   -138.705 58.072  1.00 186.38 ? 210 PHE L CB  1 
ATOM   13040 C CG  . PHE H 4 210 ? -1.355   -139.359 56.717  1.00 187.71 ? 210 PHE L CG  1 
ATOM   13041 C CD1 . PHE H 4 210 ? -0.792   -138.802 55.576  1.00 190.66 ? 210 PHE L CD1 1 
ATOM   13042 C CD2 . PHE H 4 210 ? -2.144   -140.494 56.574  1.00 189.47 ? 210 PHE L CD2 1 
ATOM   13043 C CE1 . PHE H 4 210 ? -0.983   -139.392 54.324  1.00 191.25 ? 210 PHE L CE1 1 
ATOM   13044 C CE2 . PHE H 4 210 ? -2.322   -141.089 55.323  1.00 191.92 ? 210 PHE L CE2 1 
ATOM   13045 C CZ  . PHE H 4 210 ? -1.745   -140.531 54.206  1.00 189.90 ? 210 PHE L CZ  1 
ATOM   13046 N N   . ASN H 4 211 ? 0.073    -141.399 59.720  1.00 189.37 ? 211 ASN L N   1 
ATOM   13047 C CA  . ASN H 4 211 ? 0.346    -142.841 59.728  1.00 189.97 ? 211 ASN L CA  1 
ATOM   13048 C C   . ASN H 4 211 ? -0.758   -143.610 58.986  1.00 195.17 ? 211 ASN L C   1 
ATOM   13049 O O   . ASN H 4 211 ? -1.946   -143.372 59.229  1.00 195.06 ? 211 ASN L O   1 
ATOM   13050 C CB  . ASN H 4 211 ? 0.535    -143.363 61.165  1.00 191.17 ? 211 ASN L CB  1 
ATOM   13051 C CG  . ASN H 4 211 ? -0.636   -143.146 62.106  1.00 216.34 ? 211 ASN L CG  1 
ATOM   13052 O OD1 . ASN H 4 211 ? -1.216   -142.054 62.202  1.00 211.29 ? 211 ASN L OD1 1 
ATOM   13053 N ND2 . ASN H 4 211 ? -0.983   -144.183 62.854  1.00 208.27 ? 211 ASN L ND2 1 
ATOM   13054 N N   . ARG H 4 212 ? -0.354   -144.510 58.064  1.00 192.24 ? 212 ARG L N   1 
ATOM   13055 C CA  . ARG H 4 212 ? -1.248   -145.323 57.231  1.00 192.18 ? 212 ARG L CA  1 
ATOM   13056 C C   . ARG H 4 212 ? -2.205   -146.194 58.047  1.00 197.90 ? 212 ARG L C   1 
ATOM   13057 O O   . ARG H 4 212 ? -1.774   -146.884 58.976  1.00 197.78 ? 212 ARG L O   1 
ATOM   13058 C CB  . ARG H 4 212 ? -0.432   -146.206 56.275  1.00 190.84 ? 212 ARG L CB  1 
ATOM   13059 C CG  . ARG H 4 212 ? -0.664   -145.913 54.801  1.00 194.83 ? 212 ARG L CG  1 
ATOM   13060 C CD  . ARG H 4 212 ? 0.107    -146.883 53.923  1.00 199.38 ? 212 ARG L CD  1 
ATOM   13061 N NE  . ARG H 4 212 ? -0.560   -148.182 53.819  1.00 202.65 ? 212 ARG L NE  1 
ATOM   13062 C CZ  . ARG H 4 212 ? 0.068    -149.336 53.617  1.00 214.60 ? 212 ARG L CZ  1 
ATOM   13063 N NH1 . ARG H 4 212 ? 1.390    -149.371 53.509  1.00 200.81 ? 212 ARG L NH1 1 
ATOM   13064 N NH2 . ARG H 4 212 ? -0.620   -150.467 53.540  1.00 200.72 ? 212 ARG L NH2 1 
ATOM   13065 N N   . GLY H 4 213 ? -3.488   -146.136 57.687  1.00 195.60 ? 213 GLY L N   1 
ATOM   13066 C CA  . GLY H 4 213 ? -4.563   -146.911 58.300  1.00 196.33 ? 213 GLY L CA  1 
ATOM   13067 C C   . GLY H 4 213 ? -4.907   -146.559 59.734  1.00 201.67 ? 213 GLY L C   1 
ATOM   13068 O O   . GLY H 4 213 ? -5.981   -146.005 59.994  1.00 201.91 ? 213 GLY L O   1 
ATOM   13069 N N   . GLU H 4 214 ? -4.008   -146.922 60.677  1.00 198.45 ? 214 GLU L N   1 
ATOM   13070 C CA  . GLU H 4 214 ? -4.150   -146.705 62.122  1.00 198.55 ? 214 GLU L CA  1 
ATOM   13071 C C   . GLU H 4 214 ? -4.279   -145.221 62.491  1.00 202.90 ? 214 GLU L C   1 
ATOM   13072 O O   . GLU H 4 214 ? -3.617   -144.371 61.887  1.00 202.09 ? 214 GLU L O   1 
ATOM   13073 C CB  . GLU H 4 214 ? -3.004   -147.381 62.895  1.00 199.54 ? 214 GLU L CB  1 
ATOM   13074 C CG  . GLU H 4 214 ? -3.021   -148.903 62.812  1.00 207.79 ? 214 GLU L CG  1 
ATOM   13075 C CD  . GLU H 4 214 ? -1.794   -149.610 63.357  1.00 221.82 ? 214 GLU L CD  1 
ATOM   13076 O OE1 . GLU H 4 214 ? -0.667   -149.265 62.932  1.00 210.79 ? 214 GLU L OE1 1 
ATOM   13077 O OE2 . GLU H 4 214 ? -1.963   -150.538 64.180  1.00 213.88 ? 214 GLU L OE2 1 
ATOM   13078 N N   . CYS H 4 215 ? -5.157   -144.922 63.470  1.00 200.26 ? 215 CYS L N   1 
ATOM   13079 C CA  . CYS H 4 215 ? -5.453   -143.567 63.938  1.00 233.98 ? 215 CYS L CA  1 
ATOM   13080 C C   . CYS H 4 215 ? -4.333   -142.990 64.791  1.00 253.53 ? 215 CYS L C   1 
ATOM   13081 O O   . CYS H 4 215 ? -4.018   -141.808 64.662  1.00 213.01 ? 215 CYS L O   1 
ATOM   13082 C CB  . CYS H 4 215 ? -6.793   -143.529 64.669  1.00 235.54 ? 215 CYS L CB  1 
ATOM   13083 S SG  . CYS H 4 215 ? -8.208   -144.062 63.665  1.00 240.19 ? 215 CYS L SG  1 
HETATM 13084 C C1  . NAG I 5 .   ? -11.283  -56.369  -28.466 1.00 168.05 ? 401 NAG B C1  1 
HETATM 13085 C C2  . NAG I 5 .   ? -10.023  -55.782  -27.820 1.00 169.14 ? 401 NAG B C2  1 
HETATM 13086 C C3  . NAG I 5 .   ? -8.827   -56.223  -28.667 1.00 166.74 ? 401 NAG B C3  1 
HETATM 13087 C C4  . NAG I 5 .   ? -8.797   -57.742  -28.834 1.00 166.76 ? 401 NAG B C4  1 
HETATM 13088 C C5  . NAG I 5 .   ? -10.122  -58.265  -29.398 1.00 165.76 ? 401 NAG B C5  1 
HETATM 13089 C C6  . NAG I 5 .   ? -10.221  -59.778  -29.421 1.00 163.14 ? 401 NAG B C6  1 
HETATM 13090 C C7  . NAG I 5 .   ? -10.560  -53.637  -26.681 1.00 174.78 ? 401 NAG B C7  1 
HETATM 13091 C C8  . NAG I 5 .   ? -10.605  -52.145  -26.839 1.00 175.15 ? 401 NAG B C8  1 
HETATM 13092 N N2  . NAG I 5 .   ? -10.088  -54.328  -27.743 1.00 172.26 ? 401 NAG B N2  1 
HETATM 13093 O O3  . NAG I 5 .   ? -7.616   -55.778  -28.063 1.00 164.63 ? 401 NAG B O3  1 
HETATM 13094 O O4  . NAG I 5 .   ? -7.718   -58.089  -29.699 1.00 167.48 ? 401 NAG B O4  1 
HETATM 13095 O O5  . NAG I 5 .   ? -11.220  -57.795  -28.593 1.00 166.96 ? 401 NAG B O5  1 
HETATM 13096 O O6  . NAG I 5 .   ? -11.494  -60.228  -29.877 1.00 160.75 ? 401 NAG B O6  1 
HETATM 13097 O O7  . NAG I 5 .   ? -10.942  -54.190  -25.653 1.00 175.96 ? 401 NAG B O7  1 
HETATM 13098 C C1  . NAG J 5 .   ? -44.585  -29.051  -33.283 1.00 178.54 ? 402 NAG B C1  1 
HETATM 13099 C C2  . NAG J 5 .   ? -43.316  -28.497  -33.937 1.00 177.06 ? 402 NAG B C2  1 
HETATM 13100 C C3  . NAG J 5 .   ? -43.171  -27.129  -33.270 1.00 175.52 ? 402 NAG B C3  1 
HETATM 13101 C C4  . NAG J 5 .   ? -44.351  -26.225  -33.635 1.00 176.83 ? 402 NAG B C4  1 
HETATM 13102 C C5  . NAG J 5 .   ? -45.702  -26.912  -33.408 1.00 178.43 ? 402 NAG B C5  1 
HETATM 13103 C C6  . NAG J 5 .   ? -46.829  -26.243  -34.169 1.00 179.35 ? 402 NAG B C6  1 
HETATM 13104 C C7  . NAG J 5 .   ? -41.410  -29.831  -34.778 1.00 176.28 ? 402 NAG B C7  1 
HETATM 13105 C C8  . NAG J 5 .   ? -40.405  -30.880  -34.404 1.00 176.09 ? 402 NAG B C8  1 
HETATM 13106 N N2  . NAG J 5 .   ? -42.118  -29.305  -33.758 1.00 177.10 ? 402 NAG B N2  1 
HETATM 13107 O O3  . NAG J 5 .   ? -41.941  -26.522  -33.655 1.00 173.42 ? 402 NAG B O3  1 
HETATM 13108 O O4  . NAG J 5 .   ? -44.314  -25.039  -32.848 1.00 176.65 ? 402 NAG B O4  1 
HETATM 13109 O O5  . NAG J 5 .   ? -45.668  -28.292  -33.834 1.00 178.80 ? 402 NAG B O5  1 
HETATM 13110 O O6  . NAG J 5 .   ? -48.049  -26.971  -34.084 1.00 179.86 ? 402 NAG B O6  1 
HETATM 13111 O O7  . NAG J 5 .   ? -41.590  -29.493  -35.945 1.00 175.80 ? 402 NAG B O7  1 
HETATM 13112 C C1  . NAG K 5 .   ? -49.041  -23.548  26.384  1.00 178.62 ? 401 NAG F C1  1 
HETATM 13113 C C2  . NAG K 5 .   ? -50.013  -24.001  27.475  1.00 179.17 ? 401 NAG F C2  1 
HETATM 13114 C C3  . NAG K 5 .   ? -49.351  -23.928  28.853  1.00 182.54 ? 401 NAG F C3  1 
HETATM 13115 C C4  . NAG K 5 .   ? -48.014  -24.671  28.858  1.00 184.83 ? 401 NAG F C4  1 
HETATM 13116 C C5  . NAG K 5 .   ? -47.125  -24.189  27.708  1.00 183.15 ? 401 NAG F C5  1 
HETATM 13117 C C6  . NAG K 5 .   ? -45.817  -24.945  27.566  1.00 181.92 ? 401 NAG F C6  1 
HETATM 13118 C C7  . NAG K 5 .   ? -52.300  -23.489  26.728  1.00 174.09 ? 401 NAG F C7  1 
HETATM 13119 C C8  . NAG K 5 .   ? -53.416  -22.490  26.770  1.00 173.89 ? 401 NAG F C8  1 
HETATM 13120 N N2  . NAG K 5 .   ? -51.209  -23.176  27.437  1.00 175.88 ? 401 NAG F N2  1 
HETATM 13121 O O3  . NAG K 5 .   ? -50.221  -24.485  29.835  1.00 182.37 ? 401 NAG F O3  1 
HETATM 13122 O O4  . NAG K 5 .   ? -47.363  -24.467  30.112  1.00 186.59 ? 401 NAG F O4  1 
HETATM 13123 O O5  . NAG K 5 .   ? -47.827  -24.309  26.455  1.00 181.44 ? 401 NAG F O5  1 
HETATM 13124 O O6  . NAG K 5 .   ? -45.985  -26.229  26.973  1.00 180.73 ? 401 NAG F O6  1 
HETATM 13125 O O7  . NAG K 5 .   ? -52.377  -24.524  26.072  1.00 173.61 ? 401 NAG F O7  1 
HETATM 13126 C C1  . NAG L 5 .   ? -51.594  -12.871  27.411  1.00 147.27 ? 402 NAG F C1  1 
HETATM 13127 C C2  . NAG L 5 .   ? -50.469  -11.834  27.335  1.00 149.53 ? 402 NAG F C2  1 
HETATM 13128 C C3  . NAG L 5 .   ? -50.763  -10.818  28.440  1.00 149.23 ? 402 NAG F C3  1 
HETATM 13129 C C4  . NAG L 5 .   ? -52.138  -10.184  28.248  1.00 149.19 ? 402 NAG F C4  1 
HETATM 13130 C C5  . NAG L 5 .   ? -53.232  -11.251  28.167  1.00 148.71 ? 402 NAG F C5  1 
HETATM 13131 C C6  . NAG L 5 .   ? -54.566  -10.688  27.725  1.00 148.45 ? 402 NAG F C6  1 
HETATM 13132 C C7  . NAG L 5 .   ? -48.330  -12.805  26.527  1.00 154.47 ? 402 NAG F C7  1 
HETATM 13133 C C8  . NAG L 5 .   ? -46.971  -13.288  26.943  1.00 154.38 ? 402 NAG F C8  1 
HETATM 13134 N N2  . NAG L 5 .   ? -49.149  -12.421  27.527  1.00 152.46 ? 402 NAG F N2  1 
HETATM 13135 O O3  . NAG L 5 .   ? -49.753  -9.812   28.460  1.00 148.94 ? 402 NAG F O3  1 
HETATM 13136 O O4  . NAG L 5 .   ? -52.414  -9.286   29.322  1.00 148.80 ? 402 NAG F O4  1 
HETATM 13137 O O5  . NAG L 5 .   ? -52.880  -12.272  27.210  1.00 147.79 ? 402 NAG F O5  1 
HETATM 13138 O O6  . NAG L 5 .   ? -55.530  -11.712  27.529  1.00 148.08 ? 402 NAG F O6  1 
HETATM 13139 O O7  . NAG L 5 .   ? -48.673  -12.776  25.348  1.00 155.44 ? 402 NAG F O7  1 
HETATM 13140 C C1  . NAG M 5 .   ? -67.882  -3.540   -2.369  1.00 136.74 ? 403 NAG F C1  1 
HETATM 13141 C C2  . NAG M 5 .   ? -69.154  -4.256   -1.913  1.00 136.89 ? 403 NAG F C2  1 
HETATM 13142 C C3  . NAG M 5 .   ? -70.046  -3.917   -3.110  1.00 135.90 ? 403 NAG F C3  1 
HETATM 13143 C C4  . NAG M 5 .   ? -70.299  -2.408   -3.198  1.00 136.05 ? 403 NAG F C4  1 
HETATM 13144 C C5  . NAG M 5 .   ? -68.999  -1.594   -3.173  1.00 133.81 ? 403 NAG F C5  1 
HETATM 13145 C C6  . NAG M 5 .   ? -69.187  -0.151   -2.770  1.00 129.32 ? 403 NAG F C6  1 
HETATM 13146 C C7  . NAG M 5 .   ? -68.748  -6.334   -0.634  1.00 140.32 ? 403 NAG F C7  1 
HETATM 13147 C C8  . NAG M 5 .   ? -68.317  -7.768   -0.739  1.00 140.59 ? 403 NAG F C8  1 
HETATM 13148 N N2  . NAG M 5 .   ? -68.947  -5.692   -1.803  1.00 138.44 ? 403 NAG F N2  1 
HETATM 13149 O O3  . NAG M 5 .   ? -71.276  -4.632   -3.043  1.00 135.14 ? 403 NAG F O3  1 
HETATM 13150 O O4  . NAG M 5 .   ? -70.991  -2.122   -4.412  1.00 136.77 ? 403 NAG F O4  1 
HETATM 13151 O O5  . NAG M 5 .   ? -68.060  -2.138   -2.233  1.00 135.21 ? 403 NAG F O5  1 
HETATM 13152 O O6  . NAG M 5 .   ? -67.930  0.501    -2.618  1.00 126.03 ? 403 NAG F O6  1 
HETATM 13153 O O7  . NAG M 5 .   ? -68.909  -5.783   0.454   1.00 140.84 ? 403 NAG F O7  1 
HETATM 13154 C C1  . NAG N 5 .   ? -38.397  -54.655  26.639  1.00 148.71 ? 404 NAG F C1  1 
HETATM 13155 C C2  . NAG N 5 .   ? -37.594  -54.527  27.940  1.00 146.73 ? 404 NAG F C2  1 
HETATM 13156 C C3  . NAG N 5 .   ? -36.135  -54.957  27.736  1.00 145.84 ? 404 NAG F C3  1 
HETATM 13157 C C4  . NAG N 5 .   ? -36.032  -56.272  26.965  1.00 146.40 ? 404 NAG F C4  1 
HETATM 13158 C C5  . NAG N 5 .   ? -36.784  -56.145  25.640  1.00 147.93 ? 404 NAG F C5  1 
HETATM 13159 C C6  . NAG N 5 .   ? -36.736  -57.384  24.770  1.00 146.42 ? 404 NAG F C6  1 
HETATM 13160 C C7  . NAG N 5 .   ? -37.910  -52.663  29.541  1.00 145.36 ? 404 NAG F C7  1 
HETATM 13161 C C8  . NAG N 5 .   ? -38.254  -51.207  29.649  1.00 144.42 ? 404 NAG F C8  1 
HETATM 13162 N N2  . NAG N 5 .   ? -37.661  -53.118  28.302  1.00 145.89 ? 404 NAG F N2  1 
HETATM 13163 O O3  . NAG N 5 .   ? -35.475  -55.084  28.988  1.00 145.05 ? 404 NAG F O3  1 
HETATM 13164 O O4  . NAG N 5 .   ? -34.661  -56.603  26.744  1.00 145.03 ? 404 NAG F O4  1 
HETATM 13165 O O5  . NAG N 5 .   ? -38.173  -55.878  25.917  1.00 149.33 ? 404 NAG F O5  1 
HETATM 13166 O O6  . NAG N 5 .   ? -35.477  -57.561  24.135  1.00 145.13 ? 404 NAG F O6  1 
HETATM 13167 O O7  . NAG N 5 .   ? -37.868  -53.394  30.524  1.00 146.35 ? 404 NAG F O7  1 
HETATM 13168 C C1  . NAG O 5 .   ? -50.677  -49.476  12.744  1.00 160.37 ? 405 NAG F C1  1 
HETATM 13169 C C2  . NAG O 5 .   ? -51.215  -50.019  14.072  1.00 161.16 ? 405 NAG F C2  1 
HETATM 13170 C C3  . NAG O 5 .   ? -52.736  -50.185  14.151  1.00 160.95 ? 405 NAG F C3  1 
HETATM 13171 C C4  . NAG O 5 .   ? -53.446  -49.088  13.367  1.00 161.02 ? 405 NAG F C4  1 
HETATM 13172 C C5  . NAG O 5 .   ? -53.012  -49.158  11.904  1.00 160.58 ? 405 NAG F C5  1 
HETATM 13173 C C6  . NAG O 5 .   ? -53.705  -48.144  11.016  1.00 159.94 ? 405 NAG F C6  1 
HETATM 13174 C C7  . NAG O 5 .   ? -50.244  -51.691  15.642  1.00 161.24 ? 405 NAG F C7  1 
HETATM 13175 C C8  . NAG O 5 .   ? -49.535  -53.011  15.737  1.00 160.46 ? 405 NAG F C8  1 
HETATM 13176 N N2  . NAG O 5 .   ? -50.550  -51.279  14.393  1.00 161.52 ? 405 NAG F N2  1 
HETATM 13177 O O3  . NAG O 5 .   ? -53.168  -50.183  15.508  1.00 160.18 ? 405 NAG F O3  1 
HETATM 13178 O O4  . NAG O 5 .   ? -54.859  -49.245  13.495  1.00 160.76 ? 405 NAG F O4  1 
HETATM 13179 O O5  . NAG O 5 .   ? -51.595  -48.904  11.785  1.00 160.38 ? 405 NAG F O5  1 
HETATM 13180 O O6  . NAG O 5 .   ? -53.284  -48.248  9.660   1.00 159.51 ? 405 NAG F O6  1 
HETATM 13181 O O7  . NAG O 5 .   ? -50.525  -51.034  16.641  1.00 161.66 ? 405 NAG F O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . THR A 15  ? 2.1592 2.3299 2.2395 0.1198  -0.0867 -0.0582 15  THR A N   
2     C CA  . THR A 15  ? 2.1561 2.3296 2.2393 0.1221  -0.0883 -0.0605 15  THR A CA  
3     C C   . THR A 15  ? 2.2137 2.3906 2.2959 0.1204  -0.0873 -0.0637 15  THR A C   
4     O O   . THR A 15  ? 2.1972 2.3779 2.2821 0.1213  -0.0867 -0.0661 15  THR A O   
5     C CB  . THR A 15  ? 2.2408 2.4107 2.3253 0.1246  -0.0906 -0.0576 15  THR A CB  
6     O OG1 . THR A 15  ? 2.2404 2.4070 2.3212 0.1220  -0.0908 -0.0550 15  THR A OG1 
7     C CG2 . THR A 15  ? 2.2066 2.3729 2.2934 0.1281  -0.0915 -0.0541 15  THR A CG2 
8     N N   . GLY A 16  ? 2.1937 2.3693 2.2724 0.1181  -0.0866 -0.0631 16  GLY A N   
9     C CA  . GLY A 16  ? 2.2058 2.3830 2.2826 0.1171  -0.0855 -0.0655 16  GLY A CA  
10    C C   . GLY A 16  ? 2.2805 2.4606 2.3586 0.1168  -0.0835 -0.0672 16  GLY A C   
11    O O   . GLY A 16  ? 2.2844 2.4651 2.3617 0.1170  -0.0823 -0.0687 16  GLY A O   
12    N N   . MET A 17  ? 2.2427 2.4240 2.3226 0.1163  -0.0828 -0.0667 17  MET A N   
13    C CA  . MET A 17  ? 2.2431 2.4270 2.3251 0.1160  -0.0814 -0.0678 17  MET A CA  
14    C C   . MET A 17  ? 2.2941 2.4800 2.3786 0.1168  -0.0816 -0.0688 17  MET A C   
15    O O   . MET A 17  ? 2.2857 2.4726 2.3719 0.1176  -0.0827 -0.0688 17  MET A O   
16    C CB  . MET A 17  ? 2.2731 2.4575 2.3564 0.1148  -0.0807 -0.0671 17  MET A CB  
17    C CG  . MET A 17  ? 2.3225 2.5094 2.4087 0.1146  -0.0793 -0.0679 17  MET A CG  
18    S SD  . MET A 17  ? 2.3795 2.5671 2.4676 0.1129  -0.0775 -0.0674 17  MET A SD  
19    C CE  . MET A 17  ? 2.3363 2.5262 2.4260 0.1128  -0.0744 -0.0659 17  MET A CE  
20    N N   . VAL A 18  ? 2.2565 2.4431 2.3419 0.1169  -0.0801 -0.0688 18  VAL A N   
21    C CA  . VAL A 18  ? 2.2546 2.4432 2.3430 0.1171  -0.0792 -0.0681 18  VAL A CA  
22    C C   . VAL A 18  ? 2.3023 2.4916 2.3932 0.1166  -0.0785 -0.0668 18  VAL A C   
23    O O   . VAL A 18  ? 2.2983 2.4886 2.3918 0.1164  -0.0773 -0.0649 18  VAL A O   
24    C CB  . VAL A 18  ? 2.3066 2.4938 2.3939 0.1177  -0.0773 -0.0680 18  VAL A CB  
25    C CG1 . VAL A 18  ? 2.3032 2.4914 2.3911 0.1184  -0.0781 -0.0690 18  VAL A CG1 
26    C CG2 . VAL A 18  ? 2.3081 2.4911 2.3909 0.1182  -0.0762 -0.0682 18  VAL A CG2 
27    N N   . ASP A 19  ? 2.2555 2.4445 2.3466 0.1165  -0.0789 -0.0672 19  ASP A N   
28    C CA  . ASP A 19  ? 2.6060 2.7959 2.7008 0.1165  -0.0786 -0.0660 19  ASP A CA  
29    C C   . ASP A 19  ? 2.7998 2.9913 2.8959 0.1148  -0.0800 -0.0671 19  ASP A C   
30    O O   . ASP A 19  ? 2.2541 2.4467 2.3497 0.1135  -0.0815 -0.0676 19  ASP A O   
31    C CB  . ASP A 19  ? 2.6302 2.8191 2.7258 0.1187  -0.0768 -0.0654 19  ASP A CB  
32    C CG  . ASP A 19  ? 2.7652 2.9549 2.8592 0.1186  -0.0762 -0.0668 19  ASP A CG  
33    O OD1 . ASP A 19  ? 2.7707 2.9589 2.8607 0.1189  -0.0759 -0.0671 19  ASP A OD1 
34    O OD2 . ASP A 19  ? 2.8479 3.0399 2.9446 0.1178  -0.0758 -0.0672 19  ASP A OD2 
35    N N   . ALA A 36  ? 2.5526 2.6469 2.5185 0.3014  -0.1582 0.3297  36  ALA A N   
36    C CA  . ALA A 36  ? 2.5415 2.5794 2.5080 0.3194  -0.1499 0.3043  36  ALA A CA  
37    C C   . ALA A 36  ? 2.5619 2.5746 2.5536 0.3606  -0.1182 0.2778  36  ALA A C   
38    O O   . ALA A 36  ? 2.5614 2.5514 2.5335 0.3733  -0.1159 0.2499  36  ALA A O   
39    C CB  . ALA A 36  ? 2.5949 2.5670 2.4963 0.2992  -0.1763 0.2656  36  ALA A CB  
40    N N   . ASP A 37  ? 2.4908 2.5037 2.5245 0.3799  -0.0921 0.2859  37  ASP A N   
41    C CA  . ASP A 37  ? 2.4578 2.4513 2.5165 0.4159  -0.0579 0.2613  37  ASP A CA  
42    C C   . ASP A 37  ? 2.5425 2.4579 2.5528 0.4216  -0.0721 0.2112  37  ASP A C   
43    O O   . ASP A 37  ? 2.5570 2.4407 2.5470 0.4076  -0.0878 0.2045  37  ASP A O   
44    C CB  . ASP A 37  ? 2.4383 2.4607 2.5575 0.4264  -0.0195 0.2900  37  ASP A CB  
45    C CG  . ASP A 37  ? 2.4909 2.5037 2.6389 0.4598  0.0232  0.2667  37  ASP A CG  
46    O OD1 . ASP A 37  ? 2.4635 2.5030 2.6322 0.4830  0.0445  0.2614  37  ASP A OD1 
47    O OD2 . ASP A 37  ? 2.5504 2.5316 2.7019 0.4623  0.0375  0.2545  37  ASP A OD2 
48    N N   . LEU A 38  ? 2.5044 2.3886 2.4992 0.4429  -0.0657 0.1784  38  LEU A N   
49    C CA  . LEU A 38  ? 2.5238 2.3335 2.4774 0.4491  -0.0760 0.1357  38  LEU A CA  
50    C C   . LEU A 38  ? 2.5630 2.3519 2.5335 0.4650  -0.0573 0.1224  38  LEU A C   
51    O O   . LEU A 38  ? 2.5768 2.3218 2.5179 0.4543  -0.0739 0.1051  38  LEU A O   
52    C CB  . LEU A 38  ? 2.5255 2.3013 2.4612 0.4677  -0.0727 0.1088  38  LEU A CB  
53    C CG  . LEU A 38  ? 2.6185 2.3155 2.4992 0.4555  -0.0938 0.0772  38  LEU A CG  
54    C CD1 . LEU A 38  ? 2.6422 2.3170 2.4942 0.4483  -0.1027 0.0690  38  LEU A CD1 
55    C CD2 . LEU A 38  ? 2.6330 2.2788 2.5152 0.4814  -0.0798 0.0489  38  LEU A CD2 
56    N N   . LYS A 39  ? 2.4838 2.3068 2.5024 0.4879  -0.0197 0.1311  39  LYS A N   
57    C CA  . LYS A 39  ? 2.4614 2.2689 2.4953 0.4980  0.0034  0.1190  39  LYS A CA  
58    C C   . LYS A 39  ? 2.5171 2.3200 2.5478 0.4731  -0.0087 0.1343  39  LYS A C   
59    O O   . LYS A 39  ? 2.5157 2.2838 2.5321 0.4717  -0.0105 0.1151  39  LYS A O   
60    C CB  . LYS A 39  ? 2.4471 2.2978 2.5353 0.5218  0.0542  0.1280  39  LYS A CB  
61    C CG  . LYS A 39  ? 2.6085 2.4346 2.7013 0.5347  0.0810  0.1025  39  LYS A CG  
62    C CD  . LYS A 39  ? 2.6869 2.5613 2.8373 0.5469  0.1397  0.1179  39  LYS A CD  
63    C CE  . LYS A 39  ? 2.7763 2.6293 2.9268 0.5491  0.1677  0.0949  39  LYS A CE  
64    N NZ  . LYS A 39  ? 2.8845 2.7195 3.0228 0.5177  0.1562  0.1063  39  LYS A NZ  
65    N N   . SER A 40  ? 2.4730 2.3106 2.5183 0.4539  -0.0171 0.1700  40  SER A N   
66    C CA  . SER A 40  ? 2.4785 2.3074 2.5230 0.4326  -0.0294 0.1867  40  SER A CA  
67    C C   . SER A 40  ? 2.5486 2.3329 2.5426 0.4185  -0.0692 0.1638  40  SER A C   
68    O O   . SER A 40  ? 2.5433 2.2971 2.5289 0.4155  -0.0725 0.1509  40  SER A O   
69    C CB  . SER A 40  ? 2.5210 2.3973 2.5982 0.4178  -0.0261 0.2344  40  SER A CB  
70    O OG  . SER A 40  ? 2.6654 2.5633 2.7223 0.4070  -0.0534 0.2436  40  SER A OG  
71    N N   . THR A 41  ? 2.5221 2.3040 2.4844 0.4084  -0.0947 0.1588  41  THR A N   
72    C CA  . THR A 41  ? 2.5506 2.2934 2.4684 0.3929  -0.1233 0.1378  41  THR A CA  
73    C C   . THR A 41  ? 2.6200 2.3146 2.5178 0.4056  -0.1201 0.1027  41  THR A C   
74    O O   . THR A 41  ? 2.6309 2.2965 2.5107 0.3976  -0.1314 0.0896  41  THR A O   
75    C CB  . THR A 41  ? 2.6338 2.3876 2.5227 0.3717  -0.1445 0.1439  41  THR A CB  
76    O OG1 . THR A 41  ? 2.6369 2.3548 2.4879 0.3543  -0.1631 0.1248  41  THR A OG1 
77    C CG2 . THR A 41  ? 2.6154 2.3686 2.4950 0.3801  -0.1385 0.1339  41  THR A CG2 
78    N N   . GLN A 42  ? 2.5720 2.2601 2.4768 0.4266  -0.1028 0.0896  42  GLN A N   
79    C CA  . GLN A 42  ? 2.5741 2.2165 2.4646 0.4404  -0.0978 0.0609  42  GLN A CA  
80    C C   . GLN A 42  ? 2.6091 2.2465 2.5134 0.4437  -0.0889 0.0568  42  GLN A C   
81    O O   . GLN A 42  ? 2.6165 2.2212 2.5030 0.4390  -0.0984 0.0425  42  GLN A O   
82    C CB  . GLN A 42  ? 2.5746 2.2133 2.4751 0.4658  -0.0789 0.0497  42  GLN A CB  
83    C CG  . GLN A 42  ? 2.7831 2.3704 2.6701 0.4815  -0.0737 0.0229  42  GLN A CG  
84    C CD  . GLN A 42  ? 3.0039 2.6051 2.9194 0.5031  -0.0469 0.0164  42  GLN A CD  
85    O OE1 . GLN A 42  ? 2.9248 2.5473 2.8642 0.5256  -0.0227 0.0144  42  GLN A OE1 
86    N NE2 . GLN A 42  ? 2.9012 2.4937 2.8157 0.4955  -0.0475 0.0127  42  GLN A NE2 
87    N N   . ASN A 43  ? 2.5349 2.2059 2.4726 0.4483  -0.0680 0.0722  43  ASN A N   
88    C CA  . ASN A 43  ? 2.5160 2.1829 2.4658 0.4457  -0.0563 0.0701  43  ASN A CA  
89    C C   . ASN A 43  ? 2.5597 2.2176 2.5001 0.4265  -0.0776 0.0782  43  ASN A C   
90    O O   . ASN A 43  ? 2.5526 2.1959 2.4919 0.4224  -0.0769 0.0703  43  ASN A O   
91    C CB  . ASN A 43  ? 2.5166 2.2162 2.5050 0.4519  -0.0193 0.0847  43  ASN A CB  
92    C CG  . ASN A 43  ? 2.8653 2.5705 2.8658 0.4746  0.0096  0.0684  43  ASN A CG  
93    O OD1 . ASN A 43  ? 2.8167 2.4946 2.8001 0.4833  0.0083  0.0439  43  ASN A OD1 
94    N ND2 . ASN A 43  ? 2.7460 2.4893 2.7804 0.4856  0.0394  0.0838  43  ASN A ND2 
95    N N   . ALA A 44  ? 2.5151 2.1833 2.4488 0.4149  -0.0961 0.0934  44  ALA A N   
96    C CA  . ALA A 44  ? 2.5178 2.1766 2.4425 0.4001  -0.1162 0.0989  44  ALA A CA  
97    C C   . ALA A 44  ? 2.5617 2.1910 2.4562 0.3963  -0.1332 0.0759  44  ALA A C   
98    O O   . ALA A 44  ? 2.5591 2.1742 2.4536 0.3946  -0.1369 0.0684  44  ALA A O   
99    C CB  . ALA A 44  ? 2.5352 2.2183 2.4639 0.3884  -0.1273 0.1240  44  ALA A CB  
100   N N   . ILE A 45  ? 2.5082 2.1273 2.3800 0.3943  -0.1389 0.0662  45  ILE A N   
101   C CA  . ILE A 45  ? 2.5131 2.1000 2.3597 0.3877  -0.1454 0.0481  45  ILE A CA  
102   C C   . ILE A 45  ? 2.5268 2.0944 2.3814 0.3984  -0.1364 0.0361  45  ILE A C   
103   O O   . ILE A 45  ? 2.5214 2.0777 2.3738 0.3925  -0.1398 0.0309  45  ILE A O   
104   C CB  . ILE A 45  ? 2.5717 2.1427 2.3952 0.3830  -0.1455 0.0418  45  ILE A CB  
105   C CG1 . ILE A 45  ? 2.5963 2.1873 2.4036 0.3622  -0.1579 0.0531  45  ILE A CG1 
106   C CG2 . ILE A 45  ? 2.5957 2.1212 2.4008 0.3792  -0.1403 0.0250  45  ILE A CG2 
107   C CD1 . ILE A 45  ? 2.6822 2.2738 2.4740 0.3577  -0.1575 0.0544  45  ILE A CD1 
108   N N   . ASP A 46  ? 2.4513 2.0207 2.3182 0.4136  -0.1228 0.0332  46  ASP A N   
109   C CA  . ASP A 46  ? 2.4272 1.9849 2.3016 0.4220  -0.1134 0.0242  46  ASP A CA  
110   C C   . ASP A 46  ? 2.4367 2.0085 2.3243 0.4151  -0.1147 0.0291  46  ASP A C   
111   O O   . ASP A 46  ? 2.4295 1.9916 2.3163 0.4114  -0.1179 0.0248  46  ASP A O   
112   C CB  . ASP A 46  ? 2.4348 1.9980 2.3202 0.4392  -0.0948 0.0195  46  ASP A CB  
113   C CG  . ASP A 46  ? 2.5724 2.1123 2.4464 0.4516  -0.0916 0.0105  46  ASP A CG  
114   O OD1 . ASP A 46  ? 2.5944 2.1140 2.4489 0.4420  -0.1037 0.0102  46  ASP A OD1 
115   O OD2 . ASP A 46  ? 2.6422 2.1830 2.5267 0.4702  -0.0745 0.0029  46  ASP A OD2 
116   N N   . GLU A 47  ? 2.3637 1.9566 2.2660 0.4121  -0.1104 0.0408  47  GLU A N   
117   C CA  . GLU A 47  ? 2.3442 1.9418 2.2583 0.4040  -0.1101 0.0462  47  GLU A CA  
118   C C   . GLU A 47  ? 2.3736 1.9631 2.2815 0.3975  -0.1286 0.0454  47  GLU A C   
119   O O   . GLU A 47  ? 2.3668 1.9541 2.2814 0.3941  -0.1301 0.0431  47  GLU A O   
120   C CB  . GLU A 47  ? 2.3526 1.9645 2.2863 0.4004  -0.0961 0.0632  47  GLU A CB  
121   C CG  . GLU A 47  ? 2.4926 2.1130 2.4407 0.4013  -0.0668 0.0622  47  GLU A CG  
122   C CD  . GLU A 47  ? 2.7234 2.3552 2.6971 0.3942  -0.0422 0.0829  47  GLU A CD  
123   O OE1 . GLU A 47  ? 2.5864 2.2369 2.5742 0.4001  -0.0322 0.0973  47  GLU A OE1 
124   O OE2 . GLU A 47  ? 2.6252 2.2470 2.6070 0.3809  -0.0291 0.0866  47  GLU A OE2 
125   N N   . ILE A 48  ? 2.3142 1.9016 2.2098 0.3948  -0.1401 0.0464  48  ILE A N   
126   C CA  . ILE A 48  ? 2.3050 1.8873 2.1950 0.3893  -0.1516 0.0428  48  ILE A CA  
127   C C   . ILE A 48  ? 2.3370 1.9086 2.2239 0.3896  -0.1472 0.0315  48  ILE A C   
128   O O   . ILE A 48  ? 2.3191 1.8939 2.2183 0.3906  -0.1472 0.0296  48  ILE A O   
129   C CB  . ILE A 48  ? 2.3574 1.9439 2.2325 0.3810  -0.1609 0.0474  48  ILE A CB  
130   C CG1 . ILE A 48  ? 2.3541 1.9560 2.2403 0.3791  -0.1653 0.0672  48  ILE A CG1 
131   C CG2 . ILE A 48  ? 2.3740 1.9551 2.2411 0.3746  -0.1652 0.0383  48  ILE A CG2 
132   C CD1 . ILE A 48  ? 2.4052 2.0023 2.3113 0.3814  -0.1672 0.0765  48  ILE A CD1 
133   N N   . THR A 49  ? 2.2921 1.8497 2.1661 0.3889  -0.1412 0.0268  49  THR A N   
134   C CA  . THR A 49  ? 2.2849 1.8262 2.1594 0.3871  -0.1319 0.0226  49  THR A CA  
135   C C   . THR A 49  ? 2.2957 1.8460 2.1890 0.3922  -0.1279 0.0255  49  THR A C   
136   O O   . THR A 49  ? 2.2841 1.8356 2.1897 0.3892  -0.1214 0.0287  49  THR A O   
137   C CB  . THR A 49  ? 2.3954 1.9089 2.2529 0.3857  -0.1251 0.0193  49  THR A CB  
138   O OG1 . THR A 49  ? 2.3959 1.9113 2.2533 0.3974  -0.1252 0.0185  49  THR A OG1 
139   C CG2 . THR A 49  ? 2.3838 1.8869 2.2193 0.3720  -0.1263 0.0164  49  THR A CG2 
140   N N   . ASN A 50  ? 2.2275 1.7883 2.1252 0.3972  -0.1283 0.0263  50  ASN A N   
141   C CA  . ASN A 50  ? 2.2064 1.7796 2.1170 0.3962  -0.1244 0.0287  50  ASN A CA  
142   C C   . ASN A 50  ? 2.2368 1.8263 2.1604 0.3912  -0.1302 0.0317  50  ASN A C   
143   O O   . ASN A 50  ? 2.2217 1.8240 2.1579 0.3873  -0.1289 0.0355  50  ASN A O   
144   C CB  . ASN A 50  ? 2.2002 1.7771 2.1087 0.3998  -0.1156 0.0260  50  ASN A CB  
145   C CG  . ASN A 50  ? 2.4476 2.0075 2.3493 0.4082  -0.1080 0.0218  50  ASN A CG  
146   O OD1 . ASN A 50  ? 2.3490 1.9122 2.2547 0.4080  -0.1014 0.0218  50  ASN A OD1 
147   N ND2 . ASN A 50  ? 2.3405 1.8793 2.2310 0.4147  -0.1089 0.0184  50  ASN A ND2 
148   N N   . LYS A 51  ? 2.1882 1.7763 2.1106 0.3917  -0.1365 0.0319  51  LYS A N   
149   C CA  . LYS A 51  ? 2.1738 1.7658 2.1080 0.3904  -0.1425 0.0334  51  LYS A CA  
150   C C   . LYS A 51  ? 2.2187 1.8159 2.1617 0.3942  -0.1445 0.0301  51  LYS A C   
151   O O   . LYS A 51  ? 2.2026 1.8083 2.1617 0.3962  -0.1459 0.0299  51  LYS A O   
152   C CB  . LYS A 51  ? 2.2080 1.7907 2.1397 0.3909  -0.1471 0.0383  51  LYS A CB  
153   C CG  . LYS A 51  ? 2.4171 1.9907 2.3614 0.3894  -0.1500 0.0422  51  LYS A CG  
154   C CD  . LYS A 51  ? 2.5546 2.1154 2.5002 0.3886  -0.1517 0.0541  51  LYS A CD  
155   C CE  . LYS A 51  ? 2.6617 2.2000 2.6208 0.3854  -0.1501 0.0617  51  LYS A CE  
156   N NZ  . LYS A 51  ? 2.7493 2.2739 2.7154 0.3824  -0.1471 0.0811  51  LYS A NZ  
157   N N   . VAL A 52  ? 2.1797 1.7712 2.1136 0.3940  -0.1404 0.0275  52  VAL A N   
158   C CA  . VAL A 52  ? 2.1686 1.7644 2.1118 0.3942  -0.1313 0.0246  52  VAL A CA  
159   C C   . VAL A 52  ? 2.1908 1.8001 2.1554 0.3933  -0.1188 0.0325  52  VAL A C   
160   O O   . VAL A 52  ? 2.1677 1.7963 2.1566 0.3974  -0.1120 0.0344  52  VAL A O   
161   C CB  . VAL A 52  ? 2.2391 1.8193 2.1616 0.3869  -0.1257 0.0204  52  VAL A CB  
162   C CG1 . VAL A 52  ? 2.2340 1.8148 2.1672 0.3814  -0.1040 0.0193  52  VAL A CG1 
163   C CG2 . VAL A 52  ? 2.2465 1.8252 2.1543 0.3857  -0.1382 0.0168  52  VAL A CG2 
164   N N   . ASN A 53  ? 2.1394 1.7403 2.0982 0.3891  -0.1149 0.0389  53  ASN A N   
165   C CA  . ASN A 53  ? 2.1157 1.7292 2.0958 0.3859  -0.1038 0.0527  53  ASN A CA  
166   C C   . ASN A 53  ? 2.1175 1.7614 2.1147 0.3852  -0.1110 0.0584  53  ASN A C   
167   O O   . ASN A 53  ? 2.0924 1.7616 2.1167 0.3824  -0.1021 0.0726  53  ASN A O   
168   C CB  . ASN A 53  ? 2.1364 1.7269 2.1035 0.3836  -0.1006 0.0572  53  ASN A CB  
169   C CG  . ASN A 53  ? 2.4289 1.9868 2.3886 0.3798  -0.0858 0.0586  53  ASN A CG  
170   O OD1 . ASN A 53  ? 2.3609 1.8982 2.2975 0.3787  -0.0885 0.0469  53  ASN A OD1 
171   N ND2 . ASN A 53  ? 2.3237 1.8752 2.3037 0.3745  -0.0679 0.0760  53  ASN A ND2 
172   N N   . SER A 54  ? 2.0573 1.6991 2.0406 0.3850  -0.1240 0.0497  54  SER A N   
173   C CA  . SER A 54  ? 2.0337 1.6955 2.0260 0.3788  -0.1294 0.0526  54  SER A CA  
174   C C   . SER A 54  ? 2.0344 1.7075 2.0457 0.3851  -0.1320 0.0501  54  SER A C   
175   O O   . SER A 54  ? 2.0179 1.7158 2.0471 0.3802  -0.1322 0.0571  54  SER A O   
176   C CB  . SER A 54  ? 2.0953 1.7432 2.0672 0.3725  -0.1333 0.0457  54  SER A CB  
177   O OG  . SER A 54  ? 2.2343 1.8764 2.1930 0.3701  -0.1273 0.0459  54  SER A OG  
178   N N   . VAL A 55  ? 1.9667 1.6230 1.9746 0.3958  -0.1339 0.0403  55  VAL A N   
179   C CA  . VAL A 55  ? 1.9364 1.5985 1.9633 0.4069  -0.1347 0.0347  55  VAL A CA  
180   C C   . VAL A 55  ? 1.9555 1.6478 2.0140 0.4134  -0.1174 0.0406  55  VAL A C   
181   O O   . VAL A 55  ? 1.9212 1.6339 2.0065 0.4223  -0.1140 0.0405  55  VAL A O   
182   C CB  . VAL A 55  ? 1.9887 1.6235 2.0024 0.4156  -0.1423 0.0236  55  VAL A CB  
183   C CG1 . VAL A 55  ? 1.9970 1.6279 2.0010 0.4170  -0.1344 0.0192  55  VAL A CG1 
184   C CG2 . VAL A 55  ? 1.9648 1.5968 1.9974 0.4291  -0.1455 0.0166  55  VAL A CG2 
185   N N   . ILE A 56  ? 1.9202 1.6139 1.9788 0.4085  -0.1027 0.0476  56  ILE A N   
186   C CA  . ILE A 56  ? 1.8991 1.6200 1.9929 0.4102  -0.0768 0.0597  56  ILE A CA  
187   C C   . ILE A 56  ? 1.9174 1.6740 2.0373 0.4042  -0.0765 0.0800  56  ILE A C   
188   O O   . ILE A 56  ? 1.8785 1.6725 2.0379 0.4108  -0.0627 0.0894  56  ILE A O   
189   C CB  . ILE A 56  ? 1.9618 1.6616 2.0455 0.4011  -0.0581 0.0645  56  ILE A CB  
190   C CG1 . ILE A 56  ? 1.9815 1.6581 2.0444 0.4032  -0.0539 0.0454  56  ILE A CG1 
191   C CG2 . ILE A 56  ? 1.9564 1.6810 2.0816 0.3964  -0.0253 0.0877  56  ILE A CG2 
192   C CD1 . ILE A 56  ? 2.1086 1.7509 2.1421 0.3897  -0.0474 0.0442  56  ILE A CD1 
193   N N   . GLU A 57  ? 1.8852 1.6340 1.9836 0.3916  -0.0909 0.0861  57  GLU A N   
194   C CA  . GLU A 57  ? 1.8690 1.6513 1.9824 0.3797  -0.0945 0.1050  57  GLU A CA  
195   C C   . GLU A 57  ? 1.8832 1.6872 2.0068 0.3811  -0.1054 0.0996  57  GLU A C   
196   O O   . GLU A 57  ? 1.8551 1.7036 2.0121 0.3776  -0.0994 0.1172  57  GLU A O   
197   C CB  . GLU A 57  ? 1.9108 1.6733 1.9912 0.3669  -0.1061 0.1046  57  GLU A CB  
198   C CG  . GLU A 57  ? 2.0474 1.8447 2.1382 0.3500  -0.1084 0.1249  57  GLU A CG  
199   C CD  . GLU A 57  ? 2.3764 2.1937 2.4599 0.3373  -0.1213 0.1198  57  GLU A CD  
200   O OE1 . GLU A 57  ? 2.2994 2.0873 2.3514 0.3337  -0.1294 0.1001  57  GLU A OE1 
201   O OE2 . GLU A 57  ? 2.3124 2.1748 2.4235 0.3286  -0.1201 0.1377  57  GLU A OE2 
202   N N   . LYS A 58  ? 1.8337 1.6047 1.9312 0.3855  -0.1197 0.0780  58  LYS A N   
203   C CA  . LYS A 58  ? 1.8090 1.5811 1.9106 0.3863  -0.1294 0.0704  58  LYS A CA  
204   C C   . LYS A 58  ? 1.7909 1.5859 1.9310 0.4064  -0.1199 0.0690  58  LYS A C   
205   O O   . LYS A 58  ? 1.7762 1.5885 1.9327 0.4062  -0.1240 0.0704  58  LYS A O   
206   C CB  . LYS A 58  ? 1.8608 1.5831 1.9297 0.3859  -0.1413 0.0529  58  LYS A CB  
207   C CG  . LYS A 58  ? 1.9953 1.7077 2.0549 0.3698  -0.1486 0.0512  58  LYS A CG  
208   C CD  . LYS A 58  ? 2.1027 1.7667 2.1321 0.3616  -0.1513 0.0424  58  LYS A CD  
209   C CE  . LYS A 58  ? 2.2107 1.8633 2.2267 0.3352  -0.1491 0.0437  58  LYS A CE  
210   N NZ  . LYS A 58  ? 2.3420 1.9539 2.3340 0.3234  -0.1411 0.0406  58  LYS A NZ  
211   N N   . MET A 59  ? 1.7010 1.4965 1.8559 0.4225  -0.1038 0.0654  59  MET A N   
212   C CA  . MET A 59  ? 1.6496 1.4715 1.8460 0.4438  -0.0856 0.0626  59  MET A CA  
213   C C   . MET A 59  ? 1.6708 1.5525 1.9139 0.4396  -0.0633 0.0900  59  MET A C   
214   O O   . MET A 59  ? 1.6207 1.5411 1.9033 0.4506  -0.0550 0.0955  59  MET A O   
215   C CB  . MET A 59  ? 1.6762 1.4766 1.8681 0.4573  -0.0710 0.0475  59  MET A CB  
216   C CG  . MET A 59  ? 1.7297 1.4829 1.8902 0.4661  -0.0902 0.0247  59  MET A CG  
217   S SD  . MET A 59  ? 1.7979 1.5273 1.9361 0.4667  -0.0785 0.0126  59  MET A SD  
218   C CE  . MET A 59  ? 1.7161 1.4676 1.8942 0.4928  -0.0509 -0.0020 59  MET A CE  
219   N N   . ASN A 60  ? 1.6534 1.5414 1.8949 0.4241  -0.0526 0.1098  60  ASN A N   
220   C CA  . ASN A 60  ? 1.6323 1.5724 1.9194 0.4157  -0.0293 0.1445  60  ASN A CA  
221   C C   . ASN A 60  ? 1.6687 1.6508 1.9678 0.4025  -0.0456 0.1626  60  ASN A C   
222   O O   . ASN A 60  ? 1.6308 1.6721 1.9823 0.4045  -0.0278 0.1875  60  ASN A O   
223   C CB  . ASN A 60  ? 1.6728 1.5917 1.9465 0.4003  -0.0195 0.1608  60  ASN A CB  
224   C CG  . ASN A 60  ? 1.9398 1.8345 2.2201 0.4063  0.0114  0.1561  60  ASN A CG  
225   O OD1 . ASN A 60  ? 1.8699 1.7429 2.1373 0.4194  0.0145  0.1290  60  ASN A OD1 
226   N ND2 . ASN A 60  ? 1.8242 1.7174 2.1221 0.3936  0.0359  0.1833  60  ASN A ND2 
227   N N   . THR A 61  ? 1.6513 1.6063 1.9040 0.3870  -0.0758 0.1509  61  THR A N   
228   C CA  . THR A 61  ? 1.6468 1.6365 1.9007 0.3672  -0.0910 0.1641  61  THR A CA  
229   C C   . THR A 61  ? 1.6704 1.6710 1.9411 0.3799  -0.0959 0.1506  61  THR A C   
230   O O   . THR A 61  ? 1.6456 1.6950 1.9399 0.3683  -0.0983 0.1683  61  THR A O   
231   C CB  . THR A 61  ? 1.7944 1.7530 1.9954 0.3425  -0.1117 0.1569  61  THR A CB  
232   O OG1 . THR A 61  ? 1.7962 1.8017 2.0037 0.3162  -0.1187 0.1785  61  THR A OG1 
233   C CG2 . THR A 61  ? 1.7951 1.6962 1.9535 0.3451  -0.1269 0.1240  61  THR A CG2 
234   N N   . GLN A 62  ? 1.6282 1.5835 1.8881 0.4037  -0.0970 0.1209  62  GLN A N   
235   C CA  . GLN A 62  ? 1.6061 1.5572 1.8820 0.4219  -0.1007 0.1046  62  GLN A CA  
236   C C   . GLN A 62  ? 1.6331 1.6422 1.9736 0.4458  -0.0738 0.1166  62  GLN A C   
237   O O   . GLN A 62  ? 1.6108 1.6454 1.9784 0.4544  -0.0749 0.1164  62  GLN A O   
238   C CB  . GLN A 62  ? 1.6344 1.5148 1.8785 0.4392  -0.1106 0.0724  62  GLN A CB  
239   C CG  . GLN A 62  ? 1.7300 1.5840 1.9788 0.4535  -0.1204 0.0547  62  GLN A CG  
240   C CD  . GLN A 62  ? 1.9993 1.8527 2.2316 0.4250  -0.1360 0.0615  62  GLN A CD  
241   O OE1 . GLN A 62  ? 1.9999 1.8290 2.1911 0.3948  -0.1468 0.0641  62  GLN A OE1 
242   N NE2 . GLN A 62  ? 1.8723 1.7532 2.1368 0.4331  -0.1342 0.0637  62  GLN A NE2 
243   N N   . PHE A 63  ? 1.5854 1.6150 1.9531 0.4553  -0.0454 0.1277  63  PHE A N   
244   C CA  . PHE A 63  ? 1.5367 1.6275 1.9739 0.4759  -0.0082 0.1434  63  PHE A CA  
245   C C   . PHE A 63  ? 1.5693 1.7349 2.0479 0.4582  -0.0037 0.1835  63  PHE A C   
246   O O   . PHE A 63  ? 1.5123 1.7332 2.0453 0.4741  0.0127  0.1935  63  PHE A O   
247   C CB  . PHE A 63  ? 1.5581 1.6463 2.0111 0.4813  0.0274  0.1486  63  PHE A CB  
248   C CG  . PHE A 63  ? 1.5248 1.6810 2.0557 0.4954  0.0779  0.1733  63  PHE A CG  
249   C CD1 . PHE A 63  ? 1.5175 1.6918 2.0882 0.5288  0.1039  0.1535  63  PHE A CD1 
250   C CD2 . PHE A 63  ? 1.5456 1.7470 2.1143 0.4760  0.1038  0.2181  63  PHE A CD2 
251   C CE1 . PHE A 63  ? 1.4778 1.7208 2.1275 0.5425  0.1590  0.1774  63  PHE A CE1 
252   C CE2 . PHE A 63  ? 1.5317 1.7989 2.1805 0.4872  0.1581  0.2467  63  PHE A CE2 
253   C CZ  . PHE A 63  ? 1.4606 1.7514 2.1508 0.5204  0.1874  0.2258  63  PHE A CZ  
254   N N   . THR A 64  ? 1.5697 1.7381 2.0224 0.4254  -0.0187 0.2066  64  THR A N   
255   C CA  . THR A 64  ? 1.5623 1.7986 2.0432 0.4002  -0.0203 0.2484  64  THR A CA  
256   C C   . THR A 64  ? 1.6064 1.8545 2.0728 0.3904  -0.0482 0.2386  64  THR A C   
257   O O   . THR A 64  ? 1.5713 1.8922 2.0840 0.3843  -0.0415 0.2670  64  THR A O   
258   C CB  . THR A 64  ? 1.7278 1.9475 2.1744 0.3701  -0.0310 0.2676  64  THR A CB  
259   O OG1 . THR A 64  ? 1.7098 1.8930 2.1560 0.3802  -0.0086 0.2660  64  THR A OG1 
260   C CG2 . THR A 64  ? 1.7158 2.0110 2.2005 0.3443  -0.0262 0.3189  64  THR A CG2 
261   N N   . ALA A 65  ? 1.5915 1.7670 1.9962 0.3873  -0.0759 0.2006  65  ALA A N   
262   C CA  . ALA A 65  ? 1.5965 1.7595 1.9784 0.3751  -0.0991 0.1860  65  ALA A CA  
263   C C   . ALA A 65  ? 1.5933 1.7769 2.0232 0.4087  -0.0871 0.1760  65  ALA A C   
264   O O   . ALA A 65  ? 1.5837 1.8061 2.0312 0.3981  -0.0940 0.1864  65  ALA A O   
265   C CB  . ALA A 65  ? 1.6506 1.7238 1.9642 0.3667  -0.1207 0.1514  65  ALA A CB  
266   N N   . VAL A 66  ? 1.4993 1.6650 1.9547 0.4486  -0.0655 0.1581  66  VAL A N   
267   C CA  . VAL A 66  ? 1.4277 1.6166 1.9366 0.4880  -0.0461 0.1466  66  VAL A CA  
268   C C   . VAL A 66  ? 1.3850 1.6795 1.9745 0.4935  -0.0104 0.1882  66  VAL A C   
269   O O   . VAL A 66  ? 1.3322 1.6554 1.9738 0.5236  0.0285  0.1903  66  VAL A O   
270   C CB  . VAL A 66  ? 1.4653 1.5907 1.9657 0.5265  -0.0369 0.1075  66  VAL A CB  
271   C CG1 . VAL A 66  ? 1.4078 1.5508 1.9595 0.5685  -0.0196 0.0910  66  VAL A CG1 
272   C CG2 . VAL A 66  ? 1.5105 1.5396 1.9374 0.5154  -0.0702 0.0784  66  VAL A CG2 
273   N N   . GLY A 67  ? 1.3215 1.6731 1.9189 0.4595  -0.0215 0.2239  67  GLY A N   
274   C CA  . GLY A 67  ? 1.2661 1.7241 1.9391 0.4553  0.0066  0.2732  67  GLY A CA  
275   C C   . GLY A 67  ? 1.2717 1.7754 1.9747 0.4598  -0.0016 0.2757  67  GLY A C   
276   O O   . GLY A 67  ? 1.2525 1.8358 1.9849 0.4326  -0.0041 0.3171  67  GLY A O   
277   N N   . LYS A 68  ? 1.2099 1.6572 1.9016 0.4929  -0.0081 0.2308  68  LYS A N   
278   C CA  . LYS A 68  ? 1.1739 1.6383 1.8880 0.5059  -0.0162 0.2209  68  LYS A CA  
279   C C   . LYS A 68  ? 1.1529 1.7016 1.9661 0.5506  0.0295  0.2352  68  LYS A C   
280   O O   . LYS A 68  ? 1.1098 1.6254 1.9444 0.5990  0.0479  0.1997  68  LYS A O   
281   C CB  . LYS A 68  ? 1.2184 1.5684 1.8723 0.5202  -0.0433 0.1674  68  LYS A CB  
282   C CG  . LYS A 68  ? 1.3820 1.6607 1.9483 0.4714  -0.0827 0.1582  68  LYS A CG  
283   C CD  . LYS A 68  ? 1.4890 1.7783 2.0401 0.4387  -0.1046 0.1645  68  LYS A CD  
284   C CE  . LYS A 68  ? 1.6487 1.8609 2.1139 0.3895  -0.1340 0.1516  68  LYS A CE  
285   N NZ  . LYS A 68  ? 1.7697 1.9679 2.2145 0.3597  -0.1506 0.1477  68  LYS A NZ  
286   N N   . GLU A 69  ? 1.6176 1.8602 1.8188 0.2447  0.1290  0.0804  69  GLU A N   
287   C CA  . GLU A 69  ? 1.8618 2.1024 2.0568 0.2434  0.1247  0.0824  69  GLU A CA  
288   C C   . GLU A 69  ? 2.2333 2.4721 2.4234 0.2383  0.1211  0.0825  69  GLU A C   
289   O O   . GLU A 69  ? 1.7355 1.9739 1.9287 0.2371  0.1195  0.0829  69  GLU A O   
290   C CB  . GLU A 69  ? 1.8723 2.1133 2.0718 0.2477  0.1232  0.0870  69  GLU A CB  
291   C CG  . GLU A 69  ? 1.9856 2.2282 2.1868 0.2518  0.1257  0.0870  69  GLU A CG  
292   C CD  . GLU A 69  ? 2.2002 2.4403 2.4045 0.2565  0.1254  0.0914  69  GLU A CD  
293   O OE1 . GLU A 69  ? 1.9771 2.2160 2.1774 0.2571  0.1262  0.0920  69  GLU A OE1 
294   O OE2 . GLU A 69  ? 2.1680 2.4059 2.3786 0.2598  0.1247  0.0946  69  GLU A OE2 
295   N N   . LYS A 83  ? 1.9124 2.1592 2.0998 0.2509  0.1318  0.0768  83  LYS A N   
296   C CA  . LYS A 83  ? 1.9114 2.1565 2.1014 0.2529  0.1290  0.0775  83  LYS A CA  
297   C C   . LYS A 83  ? 1.9841 2.2281 2.1725 0.2523  0.1285  0.0789  83  LYS A C   
298   O O   . LYS A 83  ? 1.9739 2.2150 2.1619 0.2520  0.1272  0.0803  83  LYS A O   
299   C CB  . LYS A 83  ? 1.9258 2.1721 2.1226 0.2570  0.1306  0.0765  83  LYS A CB  
300   C CG  . LYS A 83  ? 1.9038 2.1442 2.1030 0.2596  0.1281  0.0785  83  LYS A CG  
301   C CD  . LYS A 83  ? 1.8761 2.1161 2.0835 0.2659  0.1300  0.0781  83  LYS A CD  
302   C CE  . LYS A 83  ? 1.7925 2.0232 2.0029 0.2694  0.1279  0.0821  83  LYS A CE  
303   N NZ  . LYS A 83  ? 1.7981 2.0285 2.0112 0.2685  0.1254  0.0832  83  LYS A NZ  
304   N N   . VAL A 84  ? 1.9629 2.2093 2.1513 0.2515  0.1303  0.0794  84  VAL A N   
305   C CA  . VAL A 84  ? 1.9720 2.2178 2.1592 0.2503  0.1294  0.0806  84  VAL A CA  
306   C C   . VAL A 84  ? 2.0494 2.2932 2.2348 0.2495  0.1280  0.0816  84  VAL A C   
307   O O   . VAL A 84  ? 2.0422 2.2847 2.2279 0.2493  0.1274  0.0815  84  VAL A O   
308   C CB  . VAL A 84  ? 2.0169 2.2665 2.2060 0.2491  0.1316  0.0829  84  VAL A CB  
309   C CG1 . VAL A 84  ? 2.0170 2.2657 2.2048 0.2472  0.1294  0.0845  84  VAL A CG1 
310   C CG2 . VAL A 84  ? 2.0077 2.2630 2.2018 0.2508  0.1348  0.0823  84  VAL A CG2 
311   N N   . ASP A 85  ? 2.0274 2.2706 2.2116 0.2496  0.1287  0.0832  85  ASP A N   
312   C CA  . ASP A 85  ? 2.0347 2.2769 2.2190 0.2508  0.1280  0.0844  85  ASP A CA  
313   C C   . ASP A 85  ? 2.1073 2.3515 2.2913 0.2510  0.1273  0.0834  85  ASP A C   
314   O O   . ASP A 85  ? 2.1002 2.3470 2.2872 0.2524  0.1275  0.0845  85  ASP A O   
315   C CB  . ASP A 85  ? 2.0583 2.2964 2.2407 0.2518  0.1297  0.0874  85  ASP A CB  
316   C CG  . ASP A 85  ? 2.1546 2.3900 2.3397 0.2523  0.1302  0.0916  85  ASP A CG  
317   O OD1 . ASP A 85  ? 2.1627 2.3961 2.3474 0.2505  0.1329  0.0951  85  ASP A OD1 
318   O OD2 . ASP A 85  ? 2.1903 2.4261 2.3793 0.2543  0.1285  0.0922  85  ASP A OD2 
319   N N   . ASP A 86  ? 2.0820 2.3263 2.2642 0.2498  0.1267  0.0821  86  ASP A N   
320   C CA  . ASP A 86  ? 2.0869 2.3331 2.2692 0.2489  0.1253  0.0827  86  ASP A CA  
321   C C   . ASP A 86  ? 2.1364 2.3838 2.3234 0.2486  0.1260  0.0851  86  ASP A C   
322   O O   . ASP A 86  ? 2.1305 2.3815 2.3200 0.2476  0.1263  0.0882  86  ASP A O   
323   C CB  . ASP A 86  ? 2.1152 2.3602 2.2959 0.2479  0.1244  0.0811  86  ASP A CB  
324   C CG  . ASP A 86  ? 2.2698 2.5165 2.4498 0.2459  0.1219  0.0827  86  ASP A CG  
325   O OD1 . ASP A 86  ? 2.2777 2.5242 2.4621 0.2458  0.1210  0.0857  86  ASP A OD1 
326   O OD2 . ASP A 86  ? 2.3588 2.6060 2.5336 0.2443  0.1211  0.0818  86  ASP A OD2 
327   N N   . GLY A 87  ? 2.0907 2.3349 2.2787 0.2490  0.1271  0.0846  87  GLY A N   
328   C CA  . GLY A 87  ? 2.0853 2.3273 2.2762 0.2482  0.1296  0.0872  87  GLY A CA  
329   C C   . GLY A 87  ? 2.1252 2.3724 2.3203 0.2477  0.1326  0.0890  87  GLY A C   
330   O O   . GLY A 87  ? 2.1160 2.3660 2.3158 0.2464  0.1357  0.0933  87  GLY A O   
331   N N   . PHE A 88  ? 1.8785 1.7480 2.1600 0.1358  -0.0536 -0.2070 88  PHE A N   
332   C CA  . PHE A 88  ? 1.8857 1.7347 2.1480 0.1500  -0.0382 -0.2035 88  PHE A CA  
333   C C   . PHE A 88  ? 1.9086 1.7632 2.1640 0.1749  -0.0324 -0.2106 88  PHE A C   
334   O O   . PHE A 88  ? 1.9138 1.7607 2.1479 0.1888  -0.0223 -0.2126 88  PHE A O   
335   C CB  . PHE A 88  ? 1.9114 1.7404 2.1856 0.1382  -0.0375 -0.1914 88  PHE A CB  
336   C CG  . PHE A 88  ? 1.9384 1.7573 2.2106 0.1559  -0.0282 -0.1901 88  PHE A CG  
337   C CD1 . PHE A 88  ? 1.9678 1.7910 2.2657 0.1580  -0.0307 -0.1910 88  PHE A CD1 
338   C CD2 . PHE A 88  ? 1.9800 1.7846 2.2241 0.1695  -0.0173 -0.1885 88  PHE A CD2 
339   C CE1 . PHE A 88  ? 1.9864 1.7982 2.2810 0.1728  -0.0205 -0.1910 88  PHE A CE1 
340   C CE2 . PHE A 88  ? 2.0177 1.8142 2.2587 0.1840  -0.0105 -0.1887 88  PHE A CE2 
341   C CZ  . PHE A 88  ? 1.9867 1.7858 2.2526 0.1851  -0.0112 -0.1900 88  PHE A CZ  
342   N N   . LEU A 89  ? 1.8337 1.6989 2.1067 0.1779  -0.0395 -0.2136 89  LEU A N   
343   C CA  . LEU A 89  ? 1.8286 1.6932 2.0939 0.1960  -0.0351 -0.2187 89  LEU A CA  
344   C C   . LEU A 89  ? 1.8644 1.7336 2.1090 0.2086  -0.0325 -0.2225 89  LEU A C   
345   O O   . LEU A 89  ? 1.8672 1.7248 2.0963 0.2202  -0.0235 -0.2243 89  LEU A O   
346   C CB  . LEU A 89  ? 1.8192 1.6942 2.1037 0.1938  -0.0448 -0.2204 89  LEU A CB  
347   C CG  . LEU A 89  ? 1.8855 1.7460 2.1772 0.1993  -0.0365 -0.2210 89  LEU A CG  
348   C CD1 . LEU A 89  ? 1.8823 1.7342 2.1984 0.1868  -0.0344 -0.2144 89  LEU A CD1 
349   C CD2 . LEU A 89  ? 1.9139 1.7819 2.2130 0.2017  -0.0438 -0.2239 89  LEU A CD2 
350   N N   . ASP A 90  ? 1.8085 1.6941 2.0546 0.2047  -0.0409 -0.2228 90  ASP A N   
351   C CA  . ASP A 90  ? 1.8114 1.7022 2.0441 0.2151  -0.0390 -0.2236 90  ASP A CA  
352   C C   . ASP A 90  ? 1.8661 1.7449 2.0844 0.2200  -0.0255 -0.2244 90  ASP A C   
353   O O   . ASP A 90  ? 1.8583 1.7340 2.0677 0.2316  -0.0209 -0.2249 90  ASP A O   
354   C CB  . ASP A 90  ? 1.8262 1.7373 2.0660 0.2078  -0.0505 -0.2229 90  ASP A CB  
355   C CG  . ASP A 90  ? 1.9687 1.8953 2.2191 0.2055  -0.0675 -0.2215 90  ASP A CG  
356   O OD1 . ASP A 90  ? 1.9859 1.9089 2.2287 0.2169  -0.0698 -0.2188 90  ASP A OD1 
357   O OD2 . ASP A 90  ? 2.0345 1.9758 2.2988 0.1907  -0.0801 -0.2225 90  ASP A OD2 
358   N N   . ILE A 91  ? 1.8309 1.7011 2.0470 0.2094  -0.0205 -0.2228 91  ILE A N   
359   C CA  . ILE A 91  ? 1.8401 1.6968 2.0390 0.2120  -0.0086 -0.2222 91  ILE A CA  
360   C C   . ILE A 91  ? 1.9025 1.7473 2.0904 0.2250  -0.0027 -0.2232 91  ILE A C   
361   O O   . ILE A 91  ? 1.9047 1.7487 2.0836 0.2352  0.0021  -0.2260 91  ILE A O   
362   C CB  . ILE A 91  ? 1.8790 1.7237 2.0737 0.1941  -0.0068 -0.2167 91  ILE A CB  
363   C CG1 . ILE A 91  ? 1.8716 1.7272 2.0759 0.1769  -0.0139 -0.2174 91  ILE A CG1 
364   C CG2 . ILE A 91  ? 1.9064 1.7337 2.0773 0.1975  0.0052  -0.2143 91  ILE A CG2 
365   C CD1 . ILE A 91  ? 1.9295 1.7716 2.1365 0.1512  -0.0184 -0.2102 91  ILE A CD1 
366   N N   . TRP A 92  ? 1.8594 1.6950 2.0504 0.2230  -0.0039 -0.2207 92  TRP A N   
367   C CA  . TRP A 92  ? 1.8627 1.6867 2.0435 0.2327  0.0003  -0.2221 92  TRP A CA  
368   C C   . TRP A 92  ? 1.9157 1.7425 2.0941 0.2431  -0.0007 -0.2287 92  TRP A C   
369   O O   . TRP A 92  ? 1.9118 1.7323 2.0773 0.2501  0.0020  -0.2317 92  TRP A O   
370   C CB  . TRP A 92  ? 1.8427 1.6576 2.0336 0.2272  -0.0004 -0.2173 92  TRP A CB  
371   C CG  . TRP A 92  ? 1.8580 1.6654 2.0462 0.2362  0.0025  -0.2219 92  TRP A CG  
372   C CD1 . TRP A 92  ? 1.8926 1.7000 2.0938 0.2362  0.0019  -0.2252 92  TRP A CD1 
373   C CD2 . TRP A 92  ? 1.8610 1.6585 2.0305 0.2446  0.0061  -0.2244 92  TRP A CD2 
374   N NE1 . TRP A 92  ? 1.8936 1.6889 2.0845 0.2429  0.0070  -0.2299 92  TRP A NE1 
375   C CE2 . TRP A 92  ? 1.9147 1.7054 2.0866 0.2479  0.0083  -0.2299 92  TRP A CE2 
376   C CE3 . TRP A 92  ? 1.8793 1.6728 2.0287 0.2489  0.0070  -0.2229 92  TRP A CE3 
377   C CZ2 . TRP A 92  ? 1.9114 1.6922 2.0672 0.2535  0.0102  -0.2347 92  TRP A CZ2 
378   C CZ3 . TRP A 92  ? 1.9004 1.6871 2.0349 0.2561  0.0068  -0.2272 92  TRP A CZ3 
379   C CH2 . TRP A 92  ? 1.9106 1.6914 2.0488 0.2576  0.0079  -0.2334 92  TRP A CH2 
380   N N   . THR A 93  ? 1.8767 1.7113 2.0662 0.2421  -0.0064 -0.2296 93  THR A N   
381   C CA  . THR A 93  ? 1.8824 1.7139 2.0671 0.2480  -0.0089 -0.2319 93  THR A CA  
382   C C   . THR A 93  ? 1.9349 1.7689 2.1136 0.2529  -0.0087 -0.2315 93  THR A C   
383   O O   . THR A 93  ? 1.9364 1.7606 2.1079 0.2555  -0.0096 -0.2327 93  THR A O   
384   C CB  . THR A 93  ? 1.9984 1.8364 2.1924 0.2450  -0.0165 -0.2296 93  THR A CB  
385   O OG1 . THR A 93  ? 2.0251 1.8808 2.2284 0.2413  -0.0229 -0.2264 93  THR A OG1 
386   C CG2 . THR A 93  ? 1.9647 1.7976 2.1682 0.2404  -0.0156 -0.2307 93  THR A CG2 
387   N N   . TYR A 94  ? 1.8854 1.7302 2.0684 0.2522  -0.0071 -0.2297 94  TYR A N   
388   C CA  . TYR A 94  ? 1.8857 1.7329 2.0685 0.2571  -0.0045 -0.2289 94  TYR A CA  
389   C C   . TYR A 94  ? 1.9182 1.7572 2.0903 0.2600  0.0020  -0.2327 94  TYR A C   
390   O O   . TYR A 94  ? 1.9108 1.7469 2.0829 0.2638  0.0017  -0.2337 94  TYR A O   
391   C CB  . TYR A 94  ? 1.9058 1.7665 2.0977 0.2550  -0.0034 -0.2259 94  TYR A CB  
392   C CG  . TYR A 94  ? 1.9460 1.8087 2.1436 0.2606  0.0010  -0.2238 94  TYR A CG  
393   C CD1 . TYR A 94  ? 1.9752 1.8373 2.1807 0.2640  -0.0054 -0.2174 94  TYR A CD1 
394   C CD2 . TYR A 94  ? 1.9645 1.8269 2.1603 0.2609  0.0118  -0.2264 94  TYR A CD2 
395   C CE1 . TYR A 94  ? 1.9977 1.8609 2.2149 0.2677  -0.0017 -0.2131 94  TYR A CE1 
396   C CE2 . TYR A 94  ? 1.9834 1.8479 2.1897 0.2660  0.0174  -0.2244 94  TYR A CE2 
397   C CZ  . TYR A 94  ? 2.0971 1.9630 2.3172 0.2694  0.0104  -0.2175 94  TYR A CZ  
398   O OH  . TYR A 94  ? 2.1254 1.9926 2.3622 0.2732  0.0158  -0.2134 94  TYR A OH  
399   N N   . ASN A 95  ? 1.8654 1.6996 2.0286 0.2570  0.0059  -0.2331 95  ASN A N   
400   C CA  . ASN A 95  ? 1.8615 1.6870 2.0091 0.2600  0.0098  -0.2343 95  ASN A CA  
401   C C   . ASN A 95  ? 1.8884 1.7066 2.0290 0.2639  0.0051  -0.2386 95  ASN A C   
402   O O   . ASN A 95  ? 1.8841 1.7001 2.0156 0.2676  0.0039  -0.2416 95  ASN A O   
403   C CB  . ASN A 95  ? 1.8756 1.6933 2.0134 0.2536  0.0129  -0.2288 95  ASN A CB  
404   C CG  . ASN A 95  ? 2.1566 1.9654 2.2745 0.2547  0.0180  -0.2261 95  ASN A CG  
405   O OD1 . ASN A 95  ? 2.0748 1.8862 2.1889 0.2610  0.0205  -0.2299 95  ASN A OD1 
406   N ND2 . ASN A 95  ? 2.0633 1.8593 2.1684 0.2470  0.0193  -0.2175 95  ASN A ND2 
407   N N   . ALA A 96  ? 1.8251 1.6393 1.9699 0.2616  0.0021  -0.2396 96  ALA A N   
408   C CA  . ALA A 96  ? 1.8184 1.6225 1.9555 0.2620  -0.0011 -0.2447 96  ALA A CA  
409   C C   . ALA A 96  ? 1.8524 1.6548 1.9920 0.2607  -0.0061 -0.2472 96  ALA A C   
410   O O   . ALA A 96  ? 1.8522 1.6483 1.9837 0.2594  -0.0105 -0.2522 96  ALA A O   
411   C CB  . ALA A 96  ? 1.8296 1.6272 1.9717 0.2587  0.0003  -0.2445 96  ALA A CB  
412   N N   . GLU A 97  ? 1.7926 1.6004 1.9441 0.2596  -0.0074 -0.2423 97  GLU A N   
413   C CA  . GLU A 97  ? 1.7894 1.5928 1.9462 0.2565  -0.0132 -0.2394 97  GLU A CA  
414   C C   . GLU A 97  ? 1.8322 1.6418 1.9948 0.2591  -0.0132 -0.2404 97  GLU A C   
415   O O   . GLU A 97  ? 1.8224 1.6245 1.9865 0.2540  -0.0197 -0.2415 97  GLU A O   
416   C CB  . GLU A 97  ? 1.8052 1.6133 1.9721 0.2560  -0.0157 -0.2304 97  GLU A CB  
417   C CG  . GLU A 97  ? 1.9305 1.7256 2.0896 0.2508  -0.0197 -0.2279 97  GLU A CG  
418   C CD  . GLU A 97  ? 2.1043 1.9048 2.2686 0.2509  -0.0251 -0.2179 97  GLU A CD  
419   O OE1 . GLU A 97  ? 1.8427 1.6285 2.0008 0.2458  -0.0321 -0.2091 97  GLU A OE1 
420   O OE2 . GLU A 97  ? 2.0652 1.8826 2.2373 0.2542  -0.0241 -0.2181 97  GLU A OE2 
421   N N   . LEU A 98  ? 1.7902 1.6113 1.9552 0.2647  -0.0060 -0.2402 98  LEU A N   
422   C CA  . LEU A 98  ? 1.7871 1.6136 1.9564 0.2682  -0.0026 -0.2414 98  LEU A CA  
423   C C   . LEU A 98  ? 1.8301 1.6517 1.9879 0.2678  -0.0085 -0.2480 98  LEU A C   
424   O O   . LEU A 98  ? 1.8240 1.6470 1.9922 0.2663  -0.0130 -0.2491 98  LEU A O   
425   C CB  . LEU A 98  ? 1.7894 1.6218 1.9538 0.2714  0.0078  -0.2402 98  LEU A CB  
426   C CG  . LEU A 98  ? 1.8518 1.6890 2.0242 0.2746  0.0159  -0.2397 98  LEU A CG  
427   C CD1 . LEU A 98  ? 1.8563 1.6986 2.0338 0.2730  0.0253  -0.2361 98  LEU A CD1 
428   C CD2 . LEU A 98  ? 1.8870 1.7194 2.0409 0.2774  0.0185  -0.2433 98  LEU A CD2 
429   N N   . LEU A 99  ? 1.7784 1.5949 1.9171 0.2684  -0.0097 -0.2515 99  LEU A N   
430   C CA  . LEU A 99  ? 1.7702 1.5835 1.8940 0.2684  -0.0176 -0.2575 99  LEU A CA  
431   C C   . LEU A 99  ? 1.8409 1.6477 1.9696 0.2594  -0.0289 -0.2627 99  LEU A C   
432   O O   . LEU A 99  ? 1.8405 1.6494 1.9667 0.2566  -0.0385 -0.2680 99  LEU A O   
433   C CB  . LEU A 99  ? 1.7657 1.5735 1.8701 0.2708  -0.0163 -0.2569 99  LEU A CB  
434   C CG  . LEU A 99  ? 1.8169 1.6255 1.9033 0.2766  -0.0143 -0.2526 99  LEU A CG  
435   C CD1 . LEU A 99  ? 1.8184 1.6188 1.8932 0.2769  -0.0106 -0.2453 99  LEU A CD1 
436   C CD2 . LEU A 99  ? 1.8362 1.6473 1.9086 0.2787  -0.0257 -0.2577 99  LEU A CD2 
437   N N   . VAL A 100 ? 1.8054 1.6027 1.9396 0.2527  -0.0289 -0.2606 100 VAL A N   
438   C CA  . VAL A 100 ? 1.8077 1.5908 1.9429 0.2393  -0.0389 -0.2628 100 VAL A CA  
439   C C   . VAL A 100 ? 1.8448 1.6302 2.0013 0.2335  -0.0455 -0.2578 100 VAL A C   
440   O O   . VAL A 100 ? 1.8332 1.6145 1.9923 0.2232  -0.0574 -0.2622 100 VAL A O   
441   C CB  . VAL A 100 ? 1.8712 1.6387 2.0011 0.2335  -0.0356 -0.2597 100 VAL A CB  
442   C CG1 . VAL A 100 ? 1.8809 1.6274 2.0103 0.2161  -0.0452 -0.2574 100 VAL A CG1 
443   C CG2 . VAL A 100 ? 1.8716 1.6340 1.9851 0.2362  -0.0301 -0.2661 100 VAL A CG2 
444   N N   . LEU A 101 ? 1.7989 1.5916 1.9727 0.2393  -0.0386 -0.2482 101 LEU A N   
445   C CA  . LEU A 101 ? 1.7933 1.5884 1.9931 0.2356  -0.0421 -0.2401 101 LEU A CA  
446   C C   . LEU A 101 ? 1.8306 1.6377 2.0390 0.2389  -0.0438 -0.2466 101 LEU A C   
447   O O   . LEU A 101 ? 1.8166 1.6222 2.0467 0.2302  -0.0524 -0.2437 101 LEU A O   
448   C CB  . LEU A 101 ? 1.7951 1.5985 2.0094 0.2439  -0.0322 -0.2294 101 LEU A CB  
449   C CG  . LEU A 101 ? 1.8596 1.6556 2.0661 0.2428  -0.0319 -0.2215 101 LEU A CG  
450   C CD1 . LEU A 101 ? 1.8571 1.6688 2.0686 0.2537  -0.0218 -0.2181 101 LEU A CD1 
451   C CD2 . LEU A 101 ? 1.8952 1.6743 2.1113 0.2309  -0.0420 -0.2073 101 LEU A CD2 
452   N N   . LEU A 102 ? 1.7914 1.6084 1.9824 0.2502  -0.0366 -0.2537 102 LEU A N   
453   C CA  . LEU A 102 ? 1.7881 1.6151 1.9785 0.2553  -0.0376 -0.2592 102 LEU A CA  
454   C C   . LEU A 102 ? 1.8469 1.6723 2.0261 0.2473  -0.0547 -0.2683 102 LEU A C   
455   O O   . LEU A 102 ? 1.8440 1.6758 2.0374 0.2433  -0.0638 -0.2712 102 LEU A O   
456   C CB  . LEU A 102 ? 1.7922 1.6242 1.9617 0.2677  -0.0248 -0.2597 102 LEU A CB  
457   C CG  . LEU A 102 ? 1.8551 1.6942 2.0302 0.2746  -0.0162 -0.2592 102 LEU A CG  
458   C CD1 . LEU A 102 ? 1.8668 1.7057 2.0423 0.2799  0.0017  -0.2534 102 LEU A CD1 
459   C CD2 . LEU A 102 ? 1.8900 1.7301 2.0378 0.2791  -0.0217 -0.2640 102 LEU A CD2 
460   N N   . GLU A 103 ? 1.8056 1.6232 1.9609 0.2443  -0.0595 -0.2732 103 GLU A N   
461   C CA  . GLU A 103 ? 1.7980 1.6142 1.9402 0.2355  -0.0767 -0.2829 103 GLU A CA  
462   C C   . GLU A 103 ? 1.8551 1.6602 2.0143 0.2144  -0.0915 -0.2843 103 GLU A C   
463   O O   . GLU A 103 ? 1.8362 1.6443 1.9949 0.2036  -0.1091 -0.2924 103 GLU A O   
464   C CB  . GLU A 103 ? 1.8175 1.6284 1.9300 0.2393  -0.0756 -0.2871 103 GLU A CB  
465   C CG  . GLU A 103 ? 1.9475 1.7678 2.0396 0.2546  -0.0713 -0.2852 103 GLU A CG  
466   C CD  . GLU A 103 ? 2.2226 2.0516 2.2990 0.2546  -0.0885 -0.2917 103 GLU A CD  
467   O OE1 . GLU A 103 ? 2.1036 1.9302 2.1561 0.2559  -0.0953 -0.2943 103 GLU A OE1 
468   O OE2 . GLU A 103 ? 2.1820 2.0211 2.2712 0.2536  -0.0958 -0.2935 103 GLU A OE2 
469   N N   . ASN A 104 ? 2.1908 2.0583 2.1524 0.3947  -0.3082 0.1643  104 ASN A N   
470   C CA  . ASN A 104 ? 2.1894 2.0615 2.1533 0.3990  -0.3086 0.1669  104 ASN A CA  
471   C C   . ASN A 104 ? 2.2557 2.1270 2.2209 0.3981  -0.3010 0.1721  104 ASN A C   
472   O O   . ASN A 104 ? 2.2505 2.1230 2.2170 0.4004  -0.2984 0.1734  104 ASN A O   
473   C CB  . ASN A 104 ? 2.1714 2.0430 2.1370 0.4002  -0.3202 0.1677  104 ASN A CB  
474   C CG  . ASN A 104 ? 2.3519 2.2256 2.3172 0.4041  -0.3295 0.1614  104 ASN A CG  
475   O OD1 . ASN A 104 ? 2.2510 2.1289 2.2155 0.4073  -0.3255 0.1568  104 ASN A OD1 
476   N ND2 . ASN A 104 ? 2.2403 2.1121 2.2064 0.4040  -0.3431 0.1611  104 ASN A ND2 
477   N N   . GLU A 105 ? 2.2240 2.0929 2.1888 0.3943  -0.2980 0.1743  105 GLU A N   
478   C CA  . GLU A 105 ? 2.2264 2.0958 2.1936 0.3941  -0.2905 0.1776  105 GLU A CA  
479   C C   . GLU A 105 ? 2.2906 2.1593 2.2555 0.3955  -0.2848 0.1759  105 GLU A C   
480   O O   . GLU A 105 ? 2.2771 2.1471 2.2459 0.3970  -0.2822 0.1770  105 GLU A O   
481   C CB  . GLU A 105 ? 2.2471 2.1148 2.2118 0.3897  -0.2878 0.1790  105 GLU A CB  
482   C CG  . GLU A 105 ? 2.3611 2.2329 2.3314 0.3899  -0.2813 0.1824  105 GLU A CG  
483   C CD  . GLU A 105 ? 2.5497 2.4262 2.5278 0.3890  -0.2860 0.1876  105 GLU A CD  
484   O OE1 . GLU A 105 ? 2.3826 2.2603 2.3583 0.3841  -0.2892 0.1900  105 GLU A OE1 
485   O OE2 . GLU A 105 ? 2.4672 2.3445 2.4531 0.3925  -0.2878 0.1900  105 GLU A OE2 
486   N N   . ARG A 106 ? 2.2700 2.1355 2.2292 0.3947  -0.2849 0.1735  106 ARG A N   
487   C CA  . ARG A 106 ? 2.2779 2.1424 2.2341 0.3956  -0.2823 0.1734  106 ARG A CA  
488   C C   . ARG A 106 ? 2.3482 2.2188 2.3063 0.3970  -0.2839 0.1729  106 ARG A C   
489   O O   . ARG A 106 ? 2.3403 2.2117 2.2974 0.3968  -0.2831 0.1743  106 ARG A O   
490   C CB  . ARG A 106 ? 2.2848 2.1419 2.2354 0.3940  -0.2831 0.1727  106 ARG A CB  
491   C CG  . ARG A 106 ? 2.4455 2.2930 2.3900 0.3926  -0.2802 0.1742  106 ARG A CG  
492   C CD  . ARG A 106 ? 2.6142 2.4501 2.5520 0.3917  -0.2820 0.1751  106 ARG A CD  
493   N NE  . ARG A 106 ? 2.7840 2.6111 2.7200 0.3875  -0.2861 0.1731  106 ARG A NE  
494   C CZ  . ARG A 106 ? 3.0346 2.8468 2.9653 0.3853  -0.2891 0.1739  106 ARG A CZ  
495   N NH1 . ARG A 106 ? 2.8954 2.7000 2.8212 0.3879  -0.2885 0.1780  106 ARG A NH1 
496   N NH2 . ARG A 106 ? 2.9127 2.7156 2.8432 0.3803  -0.2946 0.1711  106 ARG A NH2 
497   N N   . THR A 107 ? 2.3270 2.2014 2.2866 0.3981  -0.2873 0.1709  107 THR A N   
498   C CA  . THR A 107 ? 2.3352 2.2150 2.2943 0.3992  -0.2882 0.1699  107 THR A CA  
499   C C   . THR A 107 ? 2.4029 2.2804 2.3636 0.3989  -0.2886 0.1723  107 THR A C   
500   O O   . THR A 107 ? 2.3988 2.2774 2.3576 0.3968  -0.2883 0.1730  107 THR A O   
501   C CB  . THR A 107 ? 2.4608 2.3441 2.4199 0.4018  -0.2922 0.1659  107 THR A CB  
502   O OG1 . THR A 107 ? 2.4710 2.3549 2.4308 0.4012  -0.2929 0.1630  107 THR A OG1 
503   C CG2 . THR A 107 ? 2.4453 2.3343 2.4017 0.4033  -0.2920 0.1643  107 THR A CG2 
504   N N   . LEU A 108 ? 2.3731 2.2466 2.3378 0.4000  -0.2906 0.1740  108 LEU A N   
505   C CA  . LEU A 108 ? 2.3768 2.2451 2.3458 0.3997  -0.2922 0.1767  108 LEU A CA  
506   C C   . LEU A 108 ? 2.4280 2.2949 2.4007 0.3974  -0.2893 0.1774  108 LEU A C   
507   O O   . LEU A 108 ? 2.4191 2.2813 2.3944 0.3955  -0.2918 0.1780  108 LEU A O   
508   C CB  . LEU A 108 ? 2.3783 2.2432 2.3524 0.4017  -0.2960 0.1799  108 LEU A CB  
509   C CG  . LEU A 108 ? 2.4401 2.3035 2.4104 0.4050  -0.3031 0.1796  108 LEU A CG  
510   C CD1 . LEU A 108 ? 2.4398 2.3032 2.4138 0.4059  -0.3085 0.1826  108 LEU A CD1 
511   C CD2 . LEU A 108 ? 2.4799 2.3345 2.4485 0.4063  -0.3074 0.1817  108 LEU A CD2 
512   N N   . ASP A 109 ? 2.3898 2.2591 2.3621 0.3975  -0.2854 0.1767  109 ASP A N   
513   C CA  . ASP A 109 ? 2.3906 2.2590 2.3653 0.3969  -0.2838 0.1762  109 ASP A CA  
514   C C   . ASP A 109 ? 2.4298 2.2988 2.3988 0.3949  -0.2868 0.1757  109 ASP A C   
515   O O   . ASP A 109 ? 2.4275 2.2946 2.3987 0.3936  -0.2900 0.1752  109 ASP A O   
516   C CB  . ASP A 109 ? 2.4217 2.2905 2.3952 0.3982  -0.2789 0.1759  109 ASP A CB  
517   C CG  . ASP A 109 ? 2.5766 2.4470 2.5573 0.3987  -0.2758 0.1773  109 ASP A CG  
518   O OD1 . ASP A 109 ? 2.5900 2.4606 2.5747 0.3985  -0.2786 0.1796  109 ASP A OD1 
519   O OD2 . ASP A 109 ? 2.6468 2.5183 2.6283 0.3996  -0.2710 0.1764  109 ASP A OD2 
520   N N   . TYR A 110 ? 2.3752 2.2475 2.3378 0.3944  -0.2870 0.1758  110 TYR A N   
521   C CA  . TYR A 110 ? 2.3683 2.2437 2.3259 0.3918  -0.2900 0.1770  110 TYR A CA  
522   C C   . TYR A 110 ? 2.4303 2.3060 2.3873 0.3877  -0.2941 0.1770  110 TYR A C   
523   O O   . TYR A 110 ? 2.4319 2.3076 2.3870 0.3836  -0.2994 0.1783  110 TYR A O   
524   C CB  . TYR A 110 ? 2.3735 2.2534 2.3272 0.3925  -0.2882 0.1771  110 TYR A CB  
525   C CG  . TYR A 110 ? 2.3870 2.2738 2.3372 0.3893  -0.2904 0.1788  110 TYR A CG  
526   C CD1 . TYR A 110 ? 2.4133 2.3003 2.3608 0.3870  -0.2948 0.1829  110 TYR A CD1 
527   C CD2 . TYR A 110 ? 2.3942 2.2880 2.3431 0.3887  -0.2889 0.1769  110 TYR A CD2 
528   C CE1 . TYR A 110 ? 2.4258 2.3211 2.3704 0.3828  -0.2976 0.1859  110 TYR A CE1 
529   C CE2 . TYR A 110 ? 2.4062 2.3088 2.3516 0.3850  -0.2897 0.1787  110 TYR A CE2 
530   C CZ  . TYR A 110 ? 2.4954 2.3996 2.4392 0.3814  -0.2940 0.1837  110 TYR A CZ  
531   O OH  . TYR A 110 ? 2.4928 2.4075 2.4335 0.3765  -0.2955 0.1869  110 TYR A OH  
532   N N   . HIS A 111 ? 2.3882 2.2626 2.3457 0.3884  -0.2933 0.1760  111 HIS A N   
533   C CA  . HIS A 111 ? 2.3892 2.2595 2.3438 0.3843  -0.2973 0.1761  111 HIS A CA  
534   C C   . HIS A 111 ? 2.4289 2.2896 2.3893 0.3808  -0.3026 0.1765  111 HIS A C   
535   O O   . HIS A 111 ? 2.4217 2.2790 2.3790 0.3743  -0.3087 0.1768  111 HIS A O   
536   C CB  . HIS A 111 ? 2.4024 2.2694 2.3556 0.3878  -0.2966 0.1753  111 HIS A CB  
537   C CG  . HIS A 111 ? 2.4469 2.3229 2.3938 0.3901  -0.2938 0.1731  111 HIS A CG  
538   N ND1 . HIS A 111 ? 2.4745 2.3546 2.4134 0.3863  -0.2939 0.1724  111 HIS A ND1 
539   C CD2 . HIS A 111 ? 2.4666 2.3482 2.4148 0.3953  -0.2917 0.1708  111 HIS A CD2 
540   C CE1 . HIS A 111 ? 2.4676 2.3574 2.4045 0.3905  -0.2905 0.1693  111 HIS A CE1 
541   N NE2 . HIS A 111 ? 2.4670 2.3570 2.4097 0.3959  -0.2901 0.1679  111 HIS A NE2 
542   N N   . ASP A 112 ? 2.3808 2.2378 2.3503 0.3846  -0.3009 0.1763  112 ASP A N   
543   C CA  . ASP A 112 ? 2.3771 2.2264 2.3563 0.3830  -0.3048 0.1757  112 ASP A CA  
544   C C   . ASP A 112 ? 2.4158 2.2668 2.3946 0.3796  -0.3101 0.1739  112 ASP A C   
545   O O   . ASP A 112 ? 2.4116 2.2549 2.3944 0.3744  -0.3185 0.1725  112 ASP A O   
546   C CB  . ASP A 112 ? 2.3998 2.2508 2.3883 0.3884  -0.2992 0.1760  112 ASP A CB  
547   C CG  . ASP A 112 ? 2.5419 2.3893 2.5431 0.3883  -0.3010 0.1742  112 ASP A CG  
548   O OD1 . ASP A 112 ? 2.5422 2.3960 2.5461 0.3916  -0.2968 0.1722  112 ASP A OD1 
549   O OD2 . ASP A 112 ? 2.6392 2.4764 2.6478 0.3852  -0.3069 0.1744  112 ASP A OD2 
550   N N   . SER A 113 ? 2.3655 2.2245 2.3391 0.3823  -0.3074 0.1743  113 SER A N   
551   C CA  . SER A 113 ? 2.3629 2.2231 2.3341 0.3807  -0.3143 0.1740  113 SER A CA  
552   C C   . SER A 113 ? 2.4206 2.2814 2.3847 0.3728  -0.3233 0.1761  113 SER A C   
553   O O   . SER A 113 ? 2.4211 2.2796 2.3854 0.3689  -0.3342 0.1757  113 SER A O   
554   C CB  . SER A 113 ? 2.4020 2.2666 2.3680 0.3860  -0.3097 0.1755  113 SER A CB  
555   O OG  . SER A 113 ? 2.5033 2.3666 2.4745 0.3917  -0.3037 0.1732  113 SER A OG  
556   N N   . ASN A 114 ? 2.2495 2.2185 2.1506 0.3809  -0.1743 -0.1436 114 ASN A N   
557   C CA  . ASN A 114 ? 2.2541 2.2268 2.1509 0.3856  -0.1708 -0.1414 114 ASN A CA  
558   C C   . ASN A 114 ? 2.3158 2.2941 2.2068 0.3906  -0.1707 -0.1426 114 ASN A C   
559   O O   . ASN A 114 ? 2.3140 2.2950 2.2009 0.3933  -0.1678 -0.1394 114 ASN A O   
560   C CB  . ASN A 114 ? 2.2680 2.2429 2.1661 0.3879  -0.1707 -0.1434 114 ASN A CB  
561   C CG  . ASN A 114 ? 2.6016 2.5719 2.5060 0.3829  -0.1701 -0.1411 114 ASN A CG  
562   O OD1 . ASN A 114 ? 2.5732 2.5430 2.4797 0.3833  -0.1721 -0.1450 114 ASN A OD1 
563   N ND2 . ASN A 114 ? 2.4788 2.4436 2.3846 0.3781  -0.1683 -0.1343 114 ASN A ND2 
564   N N   . VAL A 115 ? 2.2756 2.2552 2.1661 0.3907  -0.1752 -0.1464 115 VAL A N   
565   C CA  . VAL A 115 ? 2.2756 2.2589 2.1611 0.3940  -0.1764 -0.1469 115 VAL A CA  
566   C C   . VAL A 115 ? 2.3100 2.2959 2.1941 0.3943  -0.1730 -0.1428 115 VAL A C   
567   O O   . VAL A 115 ? 2.2991 2.2870 2.1784 0.3976  -0.1705 -0.1419 115 VAL A O   
568   C CB  . VAL A 115 ? 2.3309 2.3133 2.2158 0.3920  -0.1844 -0.1492 115 VAL A CB  
569   C CG1 . VAL A 115 ? 2.3332 2.3185 2.2136 0.3936  -0.1863 -0.1473 115 VAL A CG1 
570   C CG2 . VAL A 115 ? 2.3361 2.3120 2.2164 0.3940  -0.1893 -0.1540 115 VAL A CG2 
571   N N   . LYS A 116 ? 2.2639 2.2490 2.1508 0.3917  -0.1733 -0.1403 116 LYS A N   
572   C CA  . LYS A 116 ? 2.2630 2.2485 2.1454 0.3942  -0.1707 -0.1362 116 LYS A CA  
573   C C   . LYS A 116 ? 2.3185 2.2968 2.1938 0.3959  -0.1677 -0.1340 116 LYS A C   
574   O O   . LYS A 116 ? 2.3199 2.2982 2.1876 0.3995  -0.1666 -0.1323 116 LYS A O   
575   C CB  . LYS A 116 ? 2.2907 2.2764 2.1763 0.3927  -0.1717 -0.1336 116 LYS A CB  
576   C CG  . LYS A 116 ? 2.4517 2.4481 2.3437 0.3904  -0.1762 -0.1326 116 LYS A CG  
577   C CD  . LYS A 116 ? 2.5782 2.5790 2.4733 0.3903  -0.1765 -0.1282 116 LYS A CD  
578   C CE  . LYS A 116 ? 2.7164 2.7152 2.6198 0.3835  -0.1807 -0.1304 116 LYS A CE  
579   N NZ  . LYS A 116 ? 2.8334 2.8179 2.7355 0.3819  -0.1779 -0.1333 116 LYS A NZ  
580   N N   . ASN A 117 ? 2.2721 2.2442 2.1493 0.3929  -0.1676 -0.1332 117 ASN A N   
581   C CA  . ASN A 117 ? 2.2736 2.2386 2.1442 0.3925  -0.1672 -0.1284 117 ASN A CA  
582   C C   . ASN A 117 ? 2.3200 2.2924 2.1888 0.3944  -0.1663 -0.1281 117 ASN A C   
583   O O   . ASN A 117 ? 2.3117 2.2804 2.1729 0.3943  -0.1676 -0.1234 117 ASN A O   
584   C CB  . ASN A 117 ? 2.2938 2.2511 2.1681 0.3875  -0.1680 -0.1252 117 ASN A CB  
585   C CG  . ASN A 117 ? 2.6388 2.5839 2.5104 0.3857  -0.1692 -0.1235 117 ASN A CG  
586   O OD1 . ASN A 117 ? 2.5619 2.5095 2.4345 0.3878  -0.1690 -0.1263 117 ASN A OD1 
587   N ND2 . ASN A 117 ? 2.5612 2.4931 2.4291 0.3817  -0.1711 -0.1177 117 ASN A ND2 
588   N N   . LEU A 118 ? 2.2853 2.2668 2.1592 0.3963  -0.1653 -0.1327 118 LEU A N   
589   C CA  . LEU A 118 ? 2.2921 2.2811 2.1639 0.3995  -0.1641 -0.1328 118 LEU A CA  
590   C C   . LEU A 118 ? 2.3607 2.3507 2.2269 0.4016  -0.1643 -0.1343 118 LEU A C   
591   O O   . LEU A 118 ? 2.3602 2.3530 2.2221 0.4024  -0.1641 -0.1323 118 LEU A O   
592   C CB  . LEU A 118 ? 2.2932 2.2875 2.1682 0.4028  -0.1636 -0.1371 118 LEU A CB  
593   C CG  . LEU A 118 ? 2.3547 2.3574 2.2274 0.4074  -0.1615 -0.1356 118 LEU A CG  
594   C CD1 . LEU A 118 ? 2.3562 2.3635 2.2315 0.4108  -0.1601 -0.1347 118 LEU A CD1 
595   C CD2 . LEU A 118 ? 2.3928 2.3965 2.2608 0.4115  -0.1619 -0.1404 118 LEU A CD2 
596   N N   . TYR A 119 ? 2.3251 2.3142 2.1919 0.4019  -0.1650 -0.1367 119 TYR A N   
597   C CA  . TYR A 119 ? 2.3290 2.3201 2.1912 0.4040  -0.1649 -0.1369 119 TYR A CA  
598   C C   . TYR A 119 ? 2.3853 2.3704 2.2388 0.4051  -0.1651 -0.1333 119 TYR A C   
599   O O   . TYR A 119 ? 2.3801 2.3655 2.2270 0.4069  -0.1653 -0.1332 119 TYR A O   
600   C CB  . TYR A 119 ? 2.3462 2.3408 2.2123 0.4038  -0.1664 -0.1373 119 TYR A CB  
601   C CG  . TYR A 119 ? 2.3766 2.3748 2.2387 0.4063  -0.1657 -0.1348 119 TYR A CG  
602   C CD1 . TYR A 119 ? 2.4084 2.4065 2.2677 0.4087  -0.1649 -0.1311 119 TYR A CD1 
603   C CD2 . TYR A 119 ? 2.3863 2.3880 2.2467 0.4071  -0.1656 -0.1356 119 TYR A CD2 
604   C CE1 . TYR A 119 ? 2.4301 2.4333 2.2845 0.4131  -0.1637 -0.1279 119 TYR A CE1 
605   C CE2 . TYR A 119 ? 2.3997 2.4056 2.2566 0.4096  -0.1646 -0.1326 119 TYR A CE2 
606   C CZ  . TYR A 119 ? 2.5056 2.5132 2.3593 0.4132  -0.1635 -0.1286 119 TYR A CZ  
607   O OH  . TYR A 119 ? 2.5178 2.5313 2.3670 0.4177  -0.1620 -0.1249 119 TYR A OH  
608   N N   . GLU A 120 ? 2.3509 2.3279 2.2023 0.4040  -0.1660 -0.1304 120 GLU A N   
609   C CA  . GLU A 120 ? 2.3588 2.3240 2.1971 0.4059  -0.1682 -0.1263 120 GLU A CA  
610   C C   . GLU A 120 ? 2.4174 2.3773 2.2486 0.4033  -0.1717 -0.1227 120 GLU A C   
611   O O   . GLU A 120 ? 2.4251 2.3736 2.2416 0.4050  -0.1759 -0.1195 120 GLU A O   
612   C CB  . GLU A 120 ? 2.3774 2.3329 2.2143 0.4057  -0.1689 -0.1239 120 GLU A CB  
613   C CG  . GLU A 120 ? 2.4929 2.4464 2.3221 0.4123  -0.1680 -0.1230 120 GLU A CG  
614   C CD  . GLU A 120 ? 2.6524 2.6226 2.4914 0.4141  -0.1652 -0.1249 120 GLU A CD  
615   O OE1 . GLU A 120 ? 2.4909 2.4676 2.3412 0.4111  -0.1649 -0.1254 120 GLU A OE1 
616   O OE2 . GLU A 120 ? 2.5507 2.5271 2.3858 0.4179  -0.1643 -0.1250 120 GLU A OE2 
617   N N   . LYS A 121 ? 2.3663 2.3347 2.2064 0.3999  -0.1709 -0.1223 121 LYS A N   
618   C CA  . LYS A 121 ? 2.3645 2.3338 2.2007 0.3968  -0.1745 -0.1167 121 LYS A CA  
619   C C   . LYS A 121 ? 2.4156 2.3913 2.2477 0.3987  -0.1749 -0.1194 121 LYS A C   
620   O O   . LYS A 121 ? 2.4181 2.3882 2.2393 0.3971  -0.1806 -0.1153 121 LYS A O   
621   C CB  . LYS A 121 ? 2.3838 2.3638 2.2314 0.3944  -0.1723 -0.1141 121 LYS A CB  
622   C CG  . LYS A 121 ? 2.4792 2.4620 2.3238 0.3901  -0.1770 -0.1040 121 LYS A CG  
623   C CD  . LYS A 121 ? 2.5457 2.5459 2.4016 0.3909  -0.1732 -0.1013 121 LYS A CD  
624   C CE  . LYS A 121 ? 2.6016 2.6107 2.4560 0.3868  -0.1781 -0.0893 121 LYS A CE  
625   N NZ  . LYS A 121 ? 2.6417 2.6720 2.5063 0.3906  -0.1731 -0.0863 121 LYS A NZ  
626   N N   . VAL A 122 ? 2.3642 2.3496 2.2038 0.4016  -0.1702 -0.1260 122 VAL A N   
627   C CA  . VAL A 122 ? 2.3584 2.3495 2.1961 0.4031  -0.1697 -0.1296 122 VAL A CA  
628   C C   . VAL A 122 ? 2.4051 2.3882 2.2319 0.4054  -0.1716 -0.1306 122 VAL A C   
629   O O   . VAL A 122 ? 2.4012 2.3831 2.2202 0.4050  -0.1748 -0.1305 122 VAL A O   
630   C CB  . VAL A 122 ? 2.4002 2.3991 2.2467 0.4053  -0.1655 -0.1351 122 VAL A CB  
631   C CG1 . VAL A 122 ? 2.3960 2.3983 2.2403 0.4062  -0.1651 -0.1384 122 VAL A CG1 
632   C CG2 . VAL A 122 ? 2.3960 2.4015 2.2490 0.4059  -0.1638 -0.1343 122 VAL A CG2 
633   N N   . ARG A 123 ? 2.3556 2.3345 2.1817 0.4084  -0.1699 -0.1311 123 ARG A N   
634   C CA  . ARG A 123 ? 2.3535 2.3268 2.1687 0.4134  -0.1706 -0.1310 123 ARG A CA  
635   C C   . ARG A 123 ? 2.4192 2.3769 2.2159 0.4149  -0.1769 -0.1273 123 ARG A C   
636   O O   . ARG A 123 ? 2.4226 2.3750 2.2062 0.4195  -0.1792 -0.1279 123 ARG A O   
637   C CB  . ARG A 123 ? 2.3260 2.3019 2.1461 0.4167  -0.1673 -0.1303 123 ARG A CB  
638   C CG  . ARG A 123 ? 2.3652 2.3456 2.1803 0.4229  -0.1654 -0.1296 123 ARG A CG  
639   C CD  . ARG A 123 ? 2.3869 2.3622 2.1940 0.4294  -0.1650 -0.1259 123 ARG A CD  
640   N NE  . ARG A 123 ? 2.4256 2.3820 2.2141 0.4325  -0.1697 -0.1243 123 ARG A NE  
641   C CZ  . ARG A 123 ? 2.5666 2.5111 2.3503 0.4327  -0.1716 -0.1217 123 ARG A CZ  
642   N NH1 . ARG A 123 ? 2.3961 2.3475 2.1935 0.4302  -0.1684 -0.1213 123 ARG A NH1 
643   N NH2 . ARG A 123 ? 2.3888 2.3125 2.1526 0.4348  -0.1779 -0.1191 123 ARG A NH2 
644   N N   . SER A 124 ? 2.3791 2.3280 2.1732 0.4111  -0.1809 -0.1227 124 SER A N   
645   C CA  . SER A 124 ? 2.3910 2.3207 2.1651 0.4110  -0.1899 -0.1173 124 SER A CA  
646   C C   . SER A 124 ? 2.4416 2.3718 2.2094 0.4062  -0.1969 -0.1151 124 SER A C   
647   O O   . SER A 124 ? 2.4528 2.3660 2.1997 0.4067  -0.2066 -0.1113 124 SER A O   
648   C CB  . SER A 124 ? 2.4379 2.3572 2.2120 0.4071  -0.1926 -0.1113 124 SER A CB  
649   O OG  . SER A 124 ? 2.5481 2.4634 2.3238 0.4118  -0.1881 -0.1129 124 SER A OG  
650   N N   . GLN A 125 ? 2.3825 2.3311 2.1664 0.4019  -0.1930 -0.1170 125 GLN A N   
651   C CA  . GLN A 125 ? 2.3777 2.3321 2.1595 0.3970  -0.1987 -0.1148 125 GLN A CA  
652   C C   . GLN A 125 ? 2.4136 2.3701 2.1903 0.4000  -0.1982 -0.1215 125 GLN A C   
653   O O   . GLN A 125 ? 2.4096 2.3662 2.1792 0.3962  -0.2052 -0.1202 125 GLN A O   
654   C CB  . GLN A 125 ? 2.3819 2.3558 2.1822 0.3931  -0.1940 -0.1132 125 GLN A CB  
655   C CG  . GLN A 125 ? 2.5587 2.5330 2.3628 0.3885  -0.1968 -0.1037 125 GLN A CG  
656   C CD  . GLN A 125 ? 2.7858 2.7800 2.6076 0.3886  -0.1896 -0.1035 125 GLN A CD  
657   O OE1 . GLN A 125 ? 2.7230 2.7225 2.5544 0.3932  -0.1814 -0.1109 125 GLN A OE1 
658   N NE2 . GLN A 125 ? 2.6846 2.6901 2.5098 0.3842  -0.1935 -0.0937 125 GLN A NE2 
659   N N   . LEU A 126 ? 2.3542 2.3132 2.1348 0.4060  -0.1907 -0.1277 126 LEU A N   
660   C CA  . LEU A 126 ? 2.5154 2.4774 2.2931 0.4090  -0.1889 -0.1331 126 LEU A CA  
661   C C   . LEU A 126 ? 2.7274 2.6781 2.4898 0.4174  -0.1895 -0.1335 126 LEU A C   
662   O O   . LEU A 126 ? 2.2281 2.1758 1.9800 0.4207  -0.1915 -0.1361 126 LEU A O   
663   C CB  . LEU A 126 ? 2.5009 2.4781 2.2971 0.4086  -0.1801 -0.1376 126 LEU A CB  
664   C CG  . LEU A 126 ? 2.5479 2.5361 2.3576 0.4038  -0.1781 -0.1378 126 LEU A CG  
665   C CD1 . LEU A 126 ? 2.5387 2.5341 2.3615 0.4054  -0.1712 -0.1407 126 LEU A CD1 
666   C CD2 . LEU A 126 ? 2.5814 2.5746 2.3900 0.4001  -0.1811 -0.1394 126 LEU A CD2 
667   N N   . CYS A 148 ? 2.6701 2.5319 2.8086 0.0283  -0.0802 0.2720  148 CYS A N   
668   C CA  . CYS A 148 ? 2.6703 2.5321 2.8175 0.0264  -0.0827 0.2765  148 CYS A CA  
669   C C   . CYS A 148 ? 2.7327 2.5977 2.8820 0.0326  -0.0796 0.2768  148 CYS A C   
670   O O   . CYS A 148 ? 2.7201 2.5903 2.8783 0.0353  -0.0779 0.2769  148 CYS A O   
671   C CB  . CYS A 148 ? 2.6820 2.5324 2.8248 0.0178  -0.0873 0.2826  148 CYS A CB  
672   S SG  . CYS A 148 ? 2.7293 2.5774 2.8852 0.0156  -0.0907 0.2928  148 CYS A SG  
673   N N   . MET A 149 ? 2.7095 2.5712 2.8509 0.0343  -0.0787 0.2769  149 MET A N   
674   C CA  . MET A 149 ? 2.7130 2.5793 2.8566 0.0388  -0.0777 0.2773  149 MET A CA  
675   C C   . MET A 149 ? 2.7689 2.6416 2.9129 0.0420  -0.0741 0.2725  149 MET A C   
676   O O   . MET A 149 ? 2.7610 2.6388 2.9087 0.0438  -0.0733 0.2722  149 MET A O   
677   C CB  . MET A 149 ? 2.7506 2.6109 2.8866 0.0380  -0.0807 0.2806  149 MET A CB  
678   C CG  . MET A 149 ? 2.7968 2.6617 2.9379 0.0410  -0.0837 0.2849  149 MET A CG  
679   S SD  . MET A 149 ? 2.8585 2.7134 2.9997 0.0374  -0.0907 0.2969  149 MET A SD  
680   C CE  . MET A 149 ? 2.8097 2.6739 2.9580 0.0434  -0.0939 0.3016  149 MET A CE  
681   N N   . GLU A 150 ? 2.7352 2.6063 2.8755 0.0415  -0.0723 0.2702  150 GLU A N   
682   C CA  . GLU A 150 ? 2.7333 2.6079 2.8755 0.0428  -0.0699 0.2692  150 GLU A CA  
683   C C   . GLU A 150 ? 2.7814 2.6588 2.9255 0.0432  -0.0701 0.2690  150 GLU A C   
684   O O   . GLU A 150 ? 2.7775 2.6557 2.9224 0.0422  -0.0696 0.2702  150 GLU A O   
685   C CB  . GLU A 150 ? 2.7550 2.6256 2.8943 0.0427  -0.0676 0.2693  150 GLU A CB  
686   C CG  . GLU A 150 ? 2.8982 2.7634 3.0342 0.0423  -0.0644 0.2690  150 GLU A CG  
687   C CD  . GLU A 150 ? 3.1919 3.0485 3.3183 0.0396  -0.0660 0.2687  150 GLU A CD  
688   O OE1 . GLU A 150 ? 3.2323 3.0835 3.3529 0.0366  -0.0665 0.2683  150 GLU A OE1 
689   O OE2 . GLU A 150 ? 3.0947 2.9496 3.2190 0.0395  -0.0679 0.2698  150 GLU A OE2 
690   N N   . SER A 151 ? 2.7339 2.6113 2.8791 0.0434  -0.0710 0.2683  151 SER A N   
691   C CA  . SER A 151 ? 2.7289 2.6061 2.8736 0.0438  -0.0702 0.2676  151 SER A CA  
692   C C   . SER A 151 ? 2.7621 2.6385 2.9058 0.0433  -0.0674 0.2670  151 SER A C   
693   O O   . SER A 151 ? 2.7583 2.6310 2.8962 0.0415  -0.0664 0.2668  151 SER A O   
694   C CB  . SER A 151 ? 2.7767 2.6546 2.9264 0.0438  -0.0713 0.2670  151 SER A CB  
695   O OG  . SER A 151 ? 2.8951 2.7730 3.0516 0.0430  -0.0708 0.2687  151 SER A OG  
696   N N   . VAL A 152 ? 2.7034 2.5823 2.8514 0.0442  -0.0670 0.2677  152 VAL A N   
697   C CA  . VAL A 152 ? 2.6938 2.5740 2.8423 0.0440  -0.0650 0.2676  152 VAL A CA  
698   C C   . VAL A 152 ? 2.7098 2.5929 2.8563 0.0406  -0.0673 0.2674  152 VAL A C   
699   O O   . VAL A 152 ? 2.7016 2.5834 2.8447 0.0369  -0.0662 0.2667  152 VAL A O   
700   C CB  . VAL A 152 ? 2.7435 2.6261 2.8990 0.0464  -0.0658 0.2710  152 VAL A CB  
701   C CG1 . VAL A 152 ? 2.7428 2.6276 2.8999 0.0471  -0.0631 0.2713  152 VAL A CG1 
702   C CG2 . VAL A 152 ? 2.7425 2.6218 2.9045 0.0472  -0.0650 0.2738  152 VAL A CG2 
703   N N   . LYS A 153 ? 2.6455 2.5312 2.7944 0.0407  -0.0701 0.2686  153 LYS A N   
704   C CA  . LYS A 153 ? 2.6308 2.5201 2.7834 0.0372  -0.0721 0.2697  153 LYS A CA  
705   C C   . LYS A 153 ? 2.6780 2.5628 2.8285 0.0324  -0.0718 0.2717  153 LYS A C   
706   O O   . LYS A 153 ? 2.6705 2.5566 2.8237 0.0260  -0.0737 0.2736  153 LYS A O   
707   C CB  . LYS A 153 ? 2.6513 2.5409 2.8065 0.0390  -0.0726 0.2704  153 LYS A CB  
708   C CG  . LYS A 153 ? 2.7180 2.6087 2.8722 0.0418  -0.0751 0.2707  153 LYS A CG  
709   C CD  . LYS A 153 ? 2.7895 2.6739 2.9396 0.0427  -0.0740 0.2709  153 LYS A CD  
710   C CE  . LYS A 153 ? 2.8490 2.7293 2.9935 0.0438  -0.0778 0.2732  153 LYS A CE  
711   N NZ  . LYS A 153 ? 2.9282 2.7970 3.0630 0.0427  -0.0759 0.2731  153 LYS A NZ  
712   N N   . ASN A 154 ? 2.6358 2.5149 2.7815 0.0343  -0.0706 0.2726  154 ASN A N   
713   C CA  . ASN A 154 ? 3.0022 2.8747 3.1440 0.0304  -0.0720 0.2771  154 ASN A CA  
714   C C   . ASN A 154 ? 3.4070 3.2722 3.5377 0.0283  -0.0714 0.2757  154 ASN A C   
715   O O   . ASN A 154 ? 2.9258 2.7907 3.0538 0.0260  -0.0695 0.2728  154 ASN A O   
716   C CB  . ASN A 154 ? 3.0019 2.8731 3.1444 0.0343  -0.0724 0.2797  154 ASN A CB  
717   C CG  . ASN A 154 ? 3.2403 3.1061 3.3843 0.0306  -0.0749 0.2885  154 ASN A CG  
718   O OD1 . ASN A 154 ? 3.1594 3.0176 3.2956 0.0266  -0.0781 0.2929  154 ASN A OD1 
719   N ND2 . ASN A 154 ? 3.1236 2.9913 3.2773 0.0318  -0.0732 0.2925  154 ASN A ND2 
720   N N   . TYR A 159 ? 2.7112 2.3766 2.5673 0.1486  -0.1277 0.0358  159 TYR A N   
721   C CA  . TYR A 159 ? 2.7115 2.3822 2.5533 0.1541  -0.1302 0.0239  159 TYR A CA  
722   C C   . TYR A 159 ? 2.7670 2.4381 2.6125 0.1602  -0.1354 0.0305  159 TYR A C   
723   O O   . TYR A 159 ? 2.7648 2.4468 2.6024 0.1646  -0.1311 0.0243  159 TYR A O   
724   C CB  . TYR A 159 ? 2.7279 2.3900 2.5599 0.1516  -0.1366 0.0131  159 TYR A CB  
725   C CG  . TYR A 159 ? 2.7504 2.4197 2.5679 0.1580  -0.1358 0.0036  159 TYR A CG  
726   C CD1 . TYR A 159 ? 2.7665 2.4503 2.5792 0.1592  -0.1297 -0.0026 159 TYR A CD1 
727   C CD2 . TYR A 159 ? 2.7706 2.4304 2.5797 0.1630  -0.1427 0.0030  159 TYR A CD2 
728   C CE1 . TYR A 159 ? 2.7755 2.4635 2.5781 0.1646  -0.1294 -0.0063 159 TYR A CE1 
729   C CE2 . TYR A 159 ? 2.7842 2.4494 2.5808 0.1685  -0.1402 -0.0026 159 TYR A CE2 
730   C CZ  . TYR A 159 ? 2.8661 2.5452 2.6608 0.1689  -0.1330 -0.0059 159 TYR A CZ  
731   O OH  . TYR A 159 ? 2.8784 2.5608 2.6642 0.1740  -0.1309 -0.0067 159 TYR A OH  
732   N N   . PRO A 160 ? 2.7222 2.3823 2.5817 0.1604  -0.1463 0.0438  160 PRO A N   
733   C CA  . PRO A 160 ? 2.7168 2.3830 2.5836 0.1662  -0.1537 0.0493  160 PRO A CA  
734   C C   . PRO A 160 ? 2.7474 2.4347 2.6237 0.1720  -0.1438 0.0556  160 PRO A C   
735   O O   . PRO A 160 ? 2.7349 2.4329 2.6151 0.1752  -0.1472 0.0545  160 PRO A O   
736   C CB  . PRO A 160 ? 2.7454 2.3939 2.6288 0.1654  -0.1710 0.0659  160 PRO A CB  
737   C CG  . PRO A 160 ? 2.8098 2.4362 2.6856 0.1582  -0.1737 0.0632  160 PRO A CG  
738   C CD  . PRO A 160 ? 2.7453 2.3852 2.6163 0.1546  -0.1554 0.0556  160 PRO A CD  
739   N N   . LYS A 161 ? 2.6988 2.3912 2.5777 0.1739  -0.1317 0.0623  161 LYS A N   
740   C CA  . LYS A 161 ? 2.6923 2.4004 2.5746 0.1828  -0.1211 0.0688  161 LYS A CA  
741   C C   . LYS A 161 ? 2.7436 2.4575 2.6047 0.1839  -0.1141 0.0512  161 LYS A C   
742   O O   . LYS A 161 ? 2.7354 2.4599 2.5984 0.1898  -0.1103 0.0530  161 LYS A O   
743   C CB  . LYS A 161 ? 2.7247 2.4313 2.6099 0.1870  -0.1101 0.0817  161 LYS A CB  
744   C CG  . LYS A 161 ? 2.8486 2.5680 2.7395 0.2009  -0.1002 0.0955  161 LYS A CG  
745   C CD  . LYS A 161 ? 2.9348 2.6498 2.8179 0.2076  -0.0866 0.1050  161 LYS A CD  
746   C CE  . LYS A 161 ? 3.0236 2.7480 2.9030 0.2255  -0.0752 0.1163  161 LYS A CE  
747   N NZ  . LYS A 161 ? 3.1138 2.8369 2.9646 0.2293  -0.0714 0.0961  161 LYS A NZ  
748   N N   . TYR A 162 ? 2.7039 2.4103 2.5472 0.1782  -0.1136 0.0366  162 TYR A N   
749   C CA  . TYR A 162 ? 2.7030 2.4104 2.5281 0.1785  -0.1100 0.0240  162 TYR A CA  
750   C C   . TYR A 162 ? 2.7469 2.4514 2.5659 0.1733  -0.1163 0.0143  162 TYR A C   
751   O O   . TYR A 162 ? 2.7407 2.4442 2.5475 0.1728  -0.1145 0.0077  162 TYR A O   
752   C CB  . TYR A 162 ? 2.7230 2.4263 2.5345 0.1795  -0.1052 0.0199  162 TYR A CB  
753   C CG  . TYR A 162 ? 2.7532 2.4564 2.5611 0.1884  -0.0970 0.0285  162 TYR A CG  
754   C CD1 . TYR A 162 ? 2.7765 2.4797 2.5962 0.1898  -0.0931 0.0408  162 TYR A CD1 
755   C CD2 . TYR A 162 ? 2.7738 2.4731 2.5646 0.1965  -0.0933 0.0261  162 TYR A CD2 
756   C CE1 . TYR A 162 ? 2.7923 2.4947 2.6066 0.2010  -0.0836 0.0515  162 TYR A CE1 
757   C CE2 . TYR A 162 ? 2.7972 2.4929 2.5790 0.2085  -0.0853 0.0345  162 TYR A CE2 
758   C CZ  . TYR A 162 ? 2.8813 2.5798 2.6746 0.2117  -0.0794 0.0475  162 TYR A CZ  
759   O OH  . TYR A 162 ? 2.9006 2.5949 2.6831 0.2263  -0.0696 0.0584  162 TYR A OH  
760   N N   . SER A 163 ? 2.7026 2.4028 2.5289 0.1710  -0.1246 0.0159  163 SER A N   
761   C CA  . SER A 163 ? 2.7019 2.3963 2.5189 0.1696  -0.1301 0.0088  163 SER A CA  
762   C C   . SER A 163 ? 2.7471 2.4479 2.5613 0.1695  -0.1283 0.0061  163 SER A C   
763   O O   . SER A 163 ? 2.7448 2.4423 2.5475 0.1691  -0.1266 0.0015  163 SER A O   
764   C CB  . SER A 163 ? 2.7506 2.4331 2.5718 0.1697  -0.1418 0.0122  163 SER A CB  
765   O OG  . SER A 163 ? 2.8645 2.5376 2.6706 0.1718  -0.1462 0.0055  163 SER A OG  
766   N N   . GLU A 164 ? 2.6951 2.4062 2.5227 0.1699  -0.1286 0.0111  164 GLU A N   
767   C CA  . GLU A 164 ? 2.6843 2.4038 2.5142 0.1672  -0.1268 0.0088  164 GLU A CA  
768   C C   . GLU A 164 ? 2.7258 2.4436 2.5448 0.1657  -0.1174 0.0058  164 GLU A C   
769   O O   . GLU A 164 ? 2.7178 2.4342 2.5325 0.1611  -0.1156 0.0033  164 GLU A O   
770   C CB  . GLU A 164 ? 2.6912 2.4261 2.5439 0.1682  -0.1318 0.0159  164 GLU A CB  
771   C CG  . GLU A 164 ? 2.8260 2.5710 2.6894 0.1733  -0.1249 0.0237  164 GLU A CG  
772   C CD  . GLU A 164 ? 3.0653 2.8047 2.9305 0.1791  -0.1235 0.0324  164 GLU A CD  
773   O OE1 . GLU A 164 ? 2.9616 2.7007 2.8425 0.1804  -0.1331 0.0423  164 GLU A OE1 
774   O OE2 . GLU A 164 ? 2.9956 2.7292 2.8471 0.1823  -0.1140 0.0309  164 GLU A OE2 
775   N N   . GLU A 165 ? 2.6801 2.3946 2.4938 0.1699  -0.1129 0.0075  165 GLU A N   
776   C CA  . GLU A 165 ? 2.6796 2.3861 2.4795 0.1710  -0.1084 0.0059  165 GLU A CA  
777   C C   . GLU A 165 ? 2.7141 2.4109 2.5026 0.1683  -0.1113 0.0033  165 GLU A C   
778   O O   . GLU A 165 ? 2.7097 2.3979 2.4908 0.1661  -0.1115 0.0045  165 GLU A O   
779   C CB  . GLU A 165 ? 2.7062 2.4101 2.5010 0.1787  -0.1050 0.0091  165 GLU A CB  
780   C CG  . GLU A 165 ? 2.8491 2.5400 2.6256 0.1833  -0.1031 0.0083  165 GLU A CG  
781   C CD  . GLU A 165 ? 3.0834 2.7687 2.8493 0.1926  -0.1006 0.0109  165 GLU A CD  
782   O OE1 . GLU A 165 ? 2.9993 2.6892 2.7685 0.2010  -0.0941 0.0175  165 GLU A OE1 
783   O OE2 . GLU A 165 ? 2.9818 2.6599 2.7379 0.1922  -0.1053 0.0078  165 GLU A OE2 
784   N N   . ALA A 166 ? 2.6555 2.3531 2.4447 0.1690  -0.1143 0.0019  166 ALA A N   
785   C CA  . ALA A 166 ? 2.6453 2.3391 2.4286 0.1691  -0.1173 0.0019  166 ALA A CA  
786   C C   . ALA A 166 ? 2.6588 2.3500 2.4405 0.1673  -0.1169 0.0050  166 ALA A C   
787   O O   . ALA A 166 ? 2.6508 2.3373 2.4292 0.1679  -0.1183 0.0107  166 ALA A O   
788   C CB  . ALA A 166 ? 2.6555 2.3520 2.4417 0.1706  -0.1197 -0.0005 166 ALA A CB  
789   N N   . LYS A 167 ? 2.5887 2.2826 2.3739 0.1657  -0.1162 0.0034  167 LYS A N   
790   C CA  . LYS A 167 ? 2.5725 2.2637 2.3548 0.1644  -0.1148 0.0066  167 LYS A CA  
791   C C   . LYS A 167 ? 2.6026 2.2906 2.3866 0.1578  -0.1111 0.0115  167 LYS A C   
792   O O   . LYS A 167 ? 2.5940 2.2759 2.3750 0.1569  -0.1091 0.0193  167 LYS A O   
793   C CB  . LYS A 167 ? 2.5933 2.2872 2.3780 0.1647  -0.1182 0.0031  167 LYS A CB  
794   C CG  . LYS A 167 ? 2.6464 2.3335 2.4204 0.1686  -0.1178 0.0058  167 LYS A CG  
795   C CD  . LYS A 167 ? 2.6799 2.3669 2.4541 0.1694  -0.1249 0.0021  167 LYS A CD  
796   C CE  . LYS A 167 ? 2.6948 2.3717 2.4529 0.1758  -0.1241 0.0050  167 LYS A CE  
797   N NZ  . LYS A 167 ? 2.7513 2.4142 2.4914 0.1887  -0.1268 0.0053  167 LYS A NZ  
798   N N   . LEU A 168 ? 2.5494 2.2393 2.3381 0.1540  -0.1102 0.0090  168 LEU A N   
799   C CA  . LEU A 168 ? 2.5426 2.2247 2.3316 0.1470  -0.1080 0.0130  168 LEU A CA  
800   C C   . LEU A 168 ? 2.5956 2.2613 2.3754 0.1489  -0.1119 0.0210  168 LEU A C   
801   O O   . LEU A 168 ? 2.5894 2.2424 2.3691 0.1430  -0.1124 0.0301  168 LEU A O   
802   C CB  . LEU A 168 ? 2.5407 2.2281 2.3344 0.1467  -0.1064 0.0084  168 LEU A CB  
803   C CG  . LEU A 168 ? 2.5936 2.2757 2.3908 0.1380  -0.1036 0.0101  168 LEU A CG  
804   C CD1 . LEU A 168 ? 2.5749 2.2771 2.3908 0.1310  -0.1014 0.0066  168 LEU A CD1 
805   C CD2 . LEU A 168 ? 2.6339 2.3069 2.4226 0.1435  -0.1034 0.0091  168 LEU A CD2 
806   N N   . ASN A 169 ? 2.5546 2.2203 2.3291 0.1566  -0.1164 0.0193  169 ASN A N   
807   C CA  . ASN A 169 ? 2.5566 2.2104 2.3256 0.1601  -0.1247 0.0272  169 ASN A CA  
808   C C   . ASN A 169 ? 2.5948 2.2526 2.3696 0.1632  -0.1273 0.0369  169 ASN A C   
809   O O   . ASN A 169 ? 2.5856 2.2337 2.3621 0.1649  -0.1356 0.0497  169 ASN A O   
810   C CB  . ASN A 169 ? 2.5752 2.2297 2.3376 0.1665  -0.1291 0.0209  169 ASN A CB  
811   C CG  . ASN A 169 ? 2.8953 2.5390 2.6472 0.1678  -0.1279 0.0172  169 ASN A CG  
812   O OD1 . ASN A 169 ? 2.8413 2.4641 2.5816 0.1692  -0.1354 0.0221  169 ASN A OD1 
813   N ND2 . ASN A 169 ? 2.7865 2.4420 2.5420 0.1692  -0.1197 0.0105  169 ASN A ND2 
814   N N   . ARG A 170 ? 2.5498 2.2200 2.3275 0.1658  -0.1216 0.0329  170 ARG A N   
815   C CA  . ARG A 170 ? 2.5459 2.2200 2.3264 0.1724  -0.1216 0.0425  170 ARG A CA  
816   C C   . ARG A 170 ? 2.6124 2.2785 2.3941 0.1699  -0.1168 0.0561  170 ARG A C   
817   O O   . ARG A 170 ? 2.6039 2.2672 2.3908 0.1751  -0.1191 0.0735  170 ARG A O   
818   C CB  . ARG A 170 ? 2.5212 2.2048 2.2986 0.1780  -0.1184 0.0329  170 ARG A CB  
819   C CG  . ARG A 170 ? 2.5435 2.2353 2.3242 0.1814  -0.1235 0.0267  170 ARG A CG  
820   C CD  . ARG A 170 ? 2.4976 2.1927 2.2748 0.1861  -0.1219 0.0195  170 ARG A CD  
821   N NE  . ARG A 170 ? 2.4307 2.1236 2.2065 0.1812  -0.1216 0.0086  170 ARG A NE  
822   C CZ  . ARG A 170 ? 2.5233 2.2106 2.2945 0.1803  -0.1207 0.0057  170 ARG A CZ  
823   N NH1 . ARG A 170 ? 2.3507 2.0333 2.1149 0.1835  -0.1181 0.0104  170 ARG A NH1 
824   N NH2 . ARG A 170 ? 2.3146 2.0013 2.0898 0.1769  -0.1233 0.0001  170 ARG A NH2 
825   N N   . GLU A 171 ? 2.5828 2.2467 2.3627 0.1618  -0.1106 0.0504  171 GLU A N   
826   C CA  . GLU A 171 ? 2.5846 2.2413 2.3666 0.1561  -0.1046 0.0618  171 GLU A CA  
827   C C   . GLU A 171 ? 2.6390 2.2791 2.4271 0.1484  -0.1085 0.0776  171 GLU A C   
828   O O   . GLU A 171 ? 2.6352 2.2669 2.4282 0.1484  -0.1063 0.0975  171 GLU A O   
829   C CB  . GLU A 171 ? 2.5976 2.2605 2.3801 0.1479  -0.0995 0.0495  171 GLU A CB  
830   C CG  . GLU A 171 ? 2.7523 2.4230 2.5273 0.1562  -0.0982 0.0419  171 GLU A CG  
831   C CD  . GLU A 171 ? 3.0409 2.7189 2.8193 0.1493  -0.0978 0.0321  171 GLU A CD  
832   O OE1 . GLU A 171 ? 3.0261 2.7032 2.8103 0.1395  -0.0930 0.0373  171 GLU A OE1 
833   O OE2 . GLU A 171 ? 2.9479 2.6327 2.7253 0.1534  -0.1037 0.0209  171 GLU A OE2 
834   N N   . GLU A 172 ? 2.5974 2.2295 2.3841 0.1433  -0.1151 0.0712  172 GLU A N   
835   C CA  . GLU A 172 ? 2.5991 2.2075 2.3870 0.1367  -0.1230 0.0852  172 GLU A CA  
836   C C   . GLU A 172 ? 2.6500 2.2496 2.4420 0.1453  -0.1358 0.1041  172 GLU A C   
837   O O   . GLU A 172 ? 2.6444 2.2213 2.4410 0.1409  -0.1445 0.1240  172 GLU A O   
838   C CB  . GLU A 172 ? 2.6218 2.2209 2.4012 0.1325  -0.1267 0.0718  172 GLU A CB  
839   C CG  . GLU A 172 ? 2.7355 2.3345 2.5185 0.1198  -0.1180 0.0649  172 GLU A CG  
840   C CD  . GLU A 172 ? 2.9559 2.5258 2.7388 0.1082  -0.1225 0.0771  172 GLU A CD  
841   O OE1 . GLU A 172 ? 2.8742 2.4309 2.6651 0.1021  -0.1235 0.0968  172 GLU A OE1 
842   O OE2 . GLU A 172 ? 2.8424 2.4012 2.6175 0.1055  -0.1246 0.0685  172 GLU A OE2 
843   N N   . ILE A 173 ? 2.6072 2.2246 2.4000 0.1571  -0.1385 0.0994  173 ILE A N   
844   C CA  . ILE A 173 ? 2.6052 2.2234 2.4074 0.1666  -0.1520 0.1162  173 ILE A CA  
845   C C   . ILE A 173 ? 2.6524 2.2805 2.4668 0.1745  -0.1463 0.1366  173 ILE A C   
846   O O   . ILE A 173 ? 2.6475 2.2671 2.4757 0.1783  -0.1563 0.1637  173 ILE A O   
847   C CB  . ILE A 173 ? 2.6414 2.2744 2.4403 0.1736  -0.1591 0.0999  173 ILE A CB  
848   C CG1 . ILE A 173 ? 2.6570 2.2709 2.4475 0.1722  -0.1749 0.0983  173 ILE A CG1 
849   C CG2 . ILE A 173 ? 2.6382 2.2920 2.4512 0.1849  -0.1640 0.1088  173 ILE A CG2 
850   C CD1 . ILE A 173 ? 2.7607 2.3600 2.5335 0.1654  -0.1689 0.0820  173 ILE A CD1 
851   N N   . ASP A 174 ? 2.6063 2.2494 2.4148 0.1787  -0.1316 0.1262  174 ASP A N   
852   C CA  . ASP A 174 ? 2.9294 2.5798 2.7428 0.1901  -0.1238 0.1443  174 ASP A CA  
853   C C   . ASP A 174 ? 3.2526 2.8875 3.0676 0.1836  -0.1149 0.1630  174 ASP A C   
854   O O   . ASP A 174 ? 2.7200 2.3483 2.5271 0.1712  -0.1074 0.1500  174 ASP A O   
855   C CB  . ASP A 174 ? 2.9526 2.6180 2.7534 0.1991  -0.1141 0.1258  174 ASP A CB  
856   C CG  . ASP A 174 ? 3.0358 2.7158 2.8373 0.2037  -0.1212 0.1092  174 ASP A CG  
857   O OD1 . ASP A 174 ? 3.0314 2.7184 2.8470 0.2077  -0.1328 0.1190  174 ASP A OD1 
858   O OD2 . ASP A 174 ? 3.0911 2.7750 2.8808 0.2030  -0.1167 0.0881  174 ASP A OD2 
859   N N   . ASN B 11  ? 2.1284 2.5199 2.1979 0.2821  -0.2211 0.2978  20  ASN B N   
860   C CA  . ASN B 11  ? 2.1274 2.4406 2.1898 0.2833  -0.2182 0.2706  20  ASN B CA  
861   C C   . ASN B 11  ? 2.2120 2.4759 2.2205 0.3140  -0.2041 0.2492  20  ASN B C   
862   O O   . ASN B 11  ? 2.2037 2.4163 2.2079 0.3197  -0.2011 0.2347  20  ASN B O   
863   C CB  . ASN B 11  ? 2.1120 2.3848 2.2112 0.2490  -0.2349 0.2678  20  ASN B CB  
864   C CG  . ASN B 11  ? 2.3487 2.6633 2.5078 0.2163  -0.2635 0.2857  20  ASN B CG  
865   O OD1 . ASN B 11  ? 2.2726 2.6287 2.4563 0.1931  -0.2782 0.3060  20  ASN B OD1 
866   N ND2 . ASN B 11  ? 2.2106 2.5133 2.3932 0.2167  -0.2770 0.2787  20  ASN B ND2 
867   N N   . ASN B 12  ? 2.2075 2.4921 2.1766 0.3370  -0.2007 0.2502  21  ASN B N   
868   C CA  . ASN B 12  ? 2.2522 2.4926 2.1674 0.3721  -0.2029 0.2309  21  ASN B CA  
869   C C   . ASN B 12  ? 2.3213 2.5335 2.2194 0.3952  -0.2011 0.2127  21  ASN B C   
870   O O   . ASN B 12  ? 2.3417 2.4955 2.2170 0.4123  -0.2167 0.2003  21  ASN B O   
871   C CB  . ASN B 12  ? 2.2994 2.5911 2.1706 0.4040  -0.2004 0.2344  21  ASN B CB  
872   C CG  . ASN B 12  ? 2.5900 2.9465 2.4388 0.4372  -0.1864 0.2335  21  ASN B CG  
873   O OD1 . ASN B 12  ? 2.5303 2.8705 2.3309 0.4782  -0.1914 0.2111  21  ASN B OD1 
874   N ND2 . ASN B 12  ? 2.4608 2.8893 2.3490 0.4205  -0.1748 0.2595  21  ASN B ND2 
875   N N   . SER B 13  ? 2.2687 2.5193 2.1798 0.3956  -0.1887 0.2139  22  SER B N   
876   C CA  . SER B 13  ? 2.2753 2.5056 2.1719 0.4137  -0.1880 0.1970  22  SER B CA  
877   C C   . SER B 13  ? 2.3128 2.4858 2.2285 0.4014  -0.1933 0.1927  22  SER B C   
878   O O   . SER B 13  ? 2.2811 2.4466 2.2293 0.3777  -0.1879 0.2016  22  SER B O   
879   C CB  . SER B 13  ? 2.3067 2.5850 2.2137 0.4148  -0.1749 0.2024  22  SER B CB  
880   O OG  . SER B 13  ? 2.4270 2.7233 2.3001 0.4457  -0.1743 0.1885  22  SER B OG  
881   N N   . THR B 14  ? 2.2929 2.4314 2.1906 0.4207  -0.2084 0.1813  23  THR B N   
882   C CA  . THR B 14  ? 2.2875 2.3842 2.2072 0.4140  -0.2168 0.1865  23  THR B CA  
883   C C   . THR B 14  ? 2.3246 2.4383 2.2537 0.4119  -0.2044 0.1818  23  THR B C   
884   O O   . THR B 14  ? 2.3177 2.4115 2.2647 0.4095  -0.2096 0.1898  23  THR B O   
885   C CB  . THR B 14  ? 2.4244 2.4752 2.3316 0.4336  -0.2523 0.1860  23  THR B CB  
886   O OG1 . THR B 14  ? 2.4195 2.4391 2.3622 0.4232  -0.2619 0.2057  23  THR B OG1 
887   C CG2 . THR B 14  ? 2.4169 2.4792 2.2926 0.4630  -0.2729 0.1647  23  THR B CG2 
888   N N   . ASP B 15  ? 2.2688 2.4194 2.1889 0.4129  -0.1898 0.1740  24  ASP B N   
889   C CA  . ASP B 15  ? 2.2504 2.4088 2.1744 0.4110  -0.1800 0.1684  24  ASP B CA  
890   C C   . ASP B 15  ? 2.2851 2.4243 2.2296 0.4010  -0.1726 0.1764  24  ASP B C   
891   O O   . ASP B 15  ? 2.2785 2.4131 2.2389 0.3914  -0.1680 0.1861  24  ASP B O   
892   C CB  . ASP B 15  ? 2.2633 2.4555 2.1891 0.4074  -0.1689 0.1725  24  ASP B CB  
893   C CG  . ASP B 15  ? 2.3819 2.6105 2.2887 0.4228  -0.1692 0.1696  24  ASP B CG  
894   O OD1 . ASP B 15  ? 2.4093 2.6433 2.2963 0.4373  -0.1773 0.1649  24  ASP B OD1 
895   O OD2 . ASP B 15  ? 2.4333 2.6848 2.3449 0.4235  -0.1627 0.1746  24  ASP B OD2 
896   N N   . THR B 16  ? 2.2338 2.3657 2.1778 0.4048  -0.1726 0.1725  25  THR B N   
897   C CA  . THR B 16  ? 2.2253 2.3496 2.1827 0.4035  -0.1625 0.1827  25  THR B CA  
898   C C   . THR B 16  ? 2.2719 2.3948 2.2175 0.4076  -0.1534 0.1736  25  THR B C   
899   O O   . THR B 16  ? 2.2716 2.3933 2.2073 0.4074  -0.1586 0.1631  25  THR B O   
900   C CB  . THR B 16  ? 2.3295 2.4480 2.3059 0.4054  -0.1736 0.2004  25  THR B CB  
901   O OG1 . THR B 16  ? 2.3237 2.4488 2.3137 0.4089  -0.1582 0.2163  25  THR B OG1 
902   C CG2 . THR B 16  ? 2.3140 2.4347 2.2901 0.4082  -0.1950 0.1959  25  THR B CG2 
903   N N   . VAL B 17  ? 2.2290 2.3466 2.1744 0.4132  -0.1443 0.1758  26  VAL B N   
904   C CA  . VAL B 17  ? 2.2400 2.3434 2.1677 0.4242  -0.1412 0.1672  26  VAL B CA  
905   C C   . VAL B 17  ? 2.2962 2.4043 2.2202 0.4406  -0.1294 0.1750  26  VAL B C   
906   O O   . VAL B 17  ? 2.2833 2.4067 2.2250 0.4424  -0.1232 0.1899  26  VAL B O   
907   C CB  . VAL B 17  ? 2.2996 2.3889 2.2246 0.4267  -0.1528 0.1623  26  VAL B CB  
908   C CG1 . VAL B 17  ? 2.2843 2.3853 2.2188 0.4128  -0.1616 0.1654  26  VAL B CG1 
909   C CG2 . VAL B 17  ? 2.3019 2.3943 2.2396 0.4312  -0.1579 0.1660  26  VAL B CG2 
910   N N   . ASP B 18  ? 2.2734 2.3690 2.1743 0.4546  -0.1262 0.1677  27  ASP B N   
911   C CA  . ASP B 18  ? 2.2929 2.4035 2.1834 0.4776  -0.1121 0.1770  27  ASP B CA  
912   C C   . ASP B 18  ? 2.3757 2.4572 2.2293 0.5073  -0.1161 0.1605  27  ASP B C   
913   O O   . ASP B 18  ? 2.3804 2.4221 2.2178 0.5056  -0.1329 0.1452  27  ASP B O   
914   C CB  . ASP B 18  ? 2.3096 2.4417 2.2072 0.4708  -0.1080 0.1900  27  ASP B CB  
915   C CG  . ASP B 18  ? 2.4021 2.5580 2.3386 0.4489  -0.1179 0.2089  27  ASP B CG  
916   O OD1 . ASP B 18  ? 2.3938 2.5342 2.3349 0.4313  -0.1332 0.1958  27  ASP B OD1 
917   O OD2 . ASP B 18  ? 2.4653 2.6558 2.4283 0.4530  -0.1141 0.2397  27  ASP B OD2 
918   N N   . THR B 19  ? 2.3519 2.4517 2.1934 0.5385  -0.1048 0.1656  28  THR B N   
919   C CA  . THR B 19  ? 2.3951 2.4671 2.1937 0.5797  -0.1144 0.1472  28  THR B CA  
920   C C   . THR B 19  ? 2.4741 2.5754 2.2431 0.6144  -0.0916 0.1566  28  THR B C   
921   O O   . THR B 19  ? 2.4487 2.5998 2.2425 0.6016  -0.0700 0.1842  28  THR B O   
922   C CB  . THR B 19  ? 2.4821 2.5489 2.2873 0.5945  -0.1307 0.1377  28  THR B CB  
923   O OG1 . THR B 19  ? 2.4377 2.5513 2.2756 0.5874  -0.1093 0.1578  28  THR B OG1 
924   C CG2 . THR B 19  ? 2.4435 2.4769 2.2697 0.5683  -0.1636 0.1286  28  THR B CG2 
925   N N   . VAL B 20  ? 2.4791 2.5508 2.1961 0.6613  -0.1020 0.1367  29  VAL B N   
926   C CA  . VAL B 20  ? 2.5172 2.6172 2.1925 0.7060  -0.0811 0.1430  29  VAL B CA  
927   C C   . VAL B 20  ? 2.5481 2.7291 2.2441 0.7265  -0.0494 0.1720  29  VAL B C   
928   O O   . VAL B 20  ? 2.5430 2.7839 2.2425 0.7361  -0.0218 0.2026  29  VAL B O   
929   C CB  . VAL B 20  ? 2.6423 2.6805 2.2483 0.7612  -0.1080 0.1101  29  VAL B CB  
930   C CG1 . VAL B 20  ? 2.6888 2.7445 2.2431 0.8006  -0.0877 0.1151  29  VAL B CG1 
931   C CG2 . VAL B 20  ? 2.6384 2.5883 2.2409 0.7394  -0.1510 0.0884  29  VAL B CG2 
932   N N   . LEU B 21  ? 2.4886 2.6737 2.2051 0.7308  -0.0560 0.1670  30  LEU B N   
933   C CA  . LEU B 21  ? 2.4808 2.7337 2.2225 0.7499  -0.0291 0.1948  30  LEU B CA  
934   C C   . LEU B 21  ? 2.4585 2.7537 2.2715 0.6997  -0.0125 0.2382  30  LEU B C   
935   O O   . LEU B 21  ? 2.4442 2.8035 2.2787 0.7051  0.0124  0.2812  30  LEU B O   
936   C CB  . LEU B 21  ? 2.5037 2.7356 2.2388 0.7751  -0.0497 0.1678  30  LEU B CB  
937   C CG  . LEU B 21  ? 2.6374 2.8341 2.3015 0.8411  -0.0747 0.1283  30  LEU B CG  
938   C CD1 . LEU B 21  ? 2.6422 2.7703 2.3093 0.8325  -0.1292 0.0914  30  LEU B CD1 
939   C CD2 . LEU B 21  ? 2.7162 2.9748 2.3558 0.9052  -0.0498 0.1361  30  LEU B CD2 
940   N N   . GLU B 22  ? 2.3684 2.6284 2.2189 0.6538  -0.0313 0.2307  31  GLU B N   
941   C CA  . GLU B 22  ? 2.3126 2.5927 2.2242 0.6103  -0.0272 0.2659  31  GLU B CA  
942   C C   . GLU B 22  ? 2.3131 2.5626 2.2360 0.5674  -0.0451 0.2595  31  GLU B C   
943   O O   . GLU B 22  ? 2.3098 2.5134 2.2060 0.5596  -0.0624 0.2251  31  GLU B O   
944   C CB  . GLU B 22  ? 2.3147 2.5841 2.2601 0.5967  -0.0330 0.2668  31  GLU B CB  
945   C CG  . GLU B 22  ? 2.4466 2.6607 2.3826 0.5775  -0.0618 0.2265  31  GLU B CG  
946   C CD  . GLU B 22  ? 2.6561 2.8582 2.6321 0.5522  -0.0715 0.2292  31  GLU B CD  
947   O OE1 . GLU B 22  ? 2.5281 2.7410 2.5455 0.5286  -0.0628 0.2621  31  GLU B OE1 
948   O OE2 . GLU B 22  ? 2.5714 2.7480 2.5406 0.5537  -0.0949 0.1997  31  GLU B OE2 
949   N N   . LYS B 23  ? 2.2304 2.5064 2.1969 0.5425  -0.0460 0.2955  32  LYS B N   
950   C CA  . LYS B 23  ? 2.1962 2.4497 2.1752 0.5078  -0.0675 0.2899  32  LYS B CA  
951   C C   . LYS B 23  ? 2.2213 2.4526 2.2346 0.4793  -0.0851 0.2958  32  LYS B C   
952   O O   . LYS B 23  ? 2.2096 2.4507 2.2537 0.4798  -0.0811 0.3215  32  LYS B O   
953   C CB  . LYS B 23  ? 2.2114 2.5062 2.2123 0.5033  -0.0709 0.3222  32  LYS B CB  
954   C CG  . LYS B 23  ? 2.3244 2.6361 2.2859 0.5273  -0.0561 0.3137  32  LYS B CG  
955   C CD  . LYS B 23  ? 2.4016 2.6607 2.3266 0.5138  -0.0701 0.2710  32  LYS B CD  
956   C CE  . LYS B 23  ? 2.5253 2.7871 2.4093 0.5364  -0.0599 0.2627  32  LYS B CE  
957   N NZ  . LYS B 23  ? 2.6701 2.9171 2.5031 0.5822  -0.0444 0.2441  32  LYS B NZ  
958   N N   . ASN B 24  ? 2.1700 2.3702 2.1758 0.4573  -0.1050 0.2727  33  ASN B N   
959   C CA  . ASN B 24  ? 2.1536 2.3291 2.1768 0.4362  -0.1252 0.2708  33  ASN B CA  
960   C C   . ASN B 24  ? 2.1819 2.3389 2.2073 0.4327  -0.1202 0.2634  33  ASN B C   
961   O O   . ASN B 24  ? 2.1661 2.3214 2.2220 0.4285  -0.1218 0.2883  33  ASN B O   
962   C CB  . ASN B 24  ? 2.1910 2.3760 2.2561 0.4275  -0.1487 0.3073  33  ASN B CB  
963   C CG  . ASN B 24  ? 2.5872 2.7769 2.6541 0.4199  -0.1740 0.3027  33  ASN B CG  
964   O OD1 . ASN B 24  ? 2.5475 2.7703 2.6327 0.4221  -0.1774 0.3253  33  ASN B OD1 
965   N ND2 . ASN B 24  ? 2.4906 2.6526 2.5407 0.4117  -0.1943 0.2743  33  ASN B ND2 
966   N N   . VAL B 25  ? 2.1318 2.2736 2.1311 0.4319  -0.1194 0.2326  34  VAL B N   
967   C CA  . VAL B 25  ? 2.1202 2.2492 2.1259 0.4239  -0.1230 0.2234  34  VAL B CA  
968   C C   . VAL B 25  ? 2.1410 2.2588 2.1421 0.4052  -0.1377 0.2107  34  VAL B C   
969   O O   . VAL B 25  ? 2.1377 2.2571 2.1194 0.4067  -0.1413 0.1964  34  VAL B O   
970   C CB  . VAL B 25  ? 2.1874 2.3160 2.1764 0.4421  -0.1212 0.2059  34  VAL B CB  
971   C CG1 . VAL B 25  ? 2.1796 2.3003 2.1890 0.4310  -0.1332 0.2008  34  VAL B CG1 
972   C CG2 . VAL B 25  ? 2.2074 2.3553 2.1855 0.4725  -0.1036 0.2151  34  VAL B CG2 
973   N N   . THR B 26  ? 2.0752 2.1825 2.0939 0.3895  -0.1458 0.2187  35  THR B N   
974   C CA  . THR B 26  ? 2.0608 2.1667 2.0721 0.3771  -0.1576 0.2108  35  THR B CA  
975   C C   . THR B 26  ? 2.0962 2.2178 2.1072 0.3705  -0.1622 0.2003  35  THR B C   
976   O O   . THR B 26  ? 2.0990 2.2188 2.1261 0.3670  -0.1667 0.1993  35  THR B O   
977   C CB  . THR B 26  ? 2.1311 2.2150 2.1573 0.3650  -0.1677 0.2231  35  THR B CB  
978   O OG1 . THR B 26  ? 2.1129 2.1782 2.1545 0.3712  -0.1711 0.2434  35  THR B OG1 
979   C CG2 . THR B 26  ? 2.1144 2.1992 2.1200 0.3648  -0.1797 0.2159  35  THR B CG2 
980   N N   . VAL B 27  ? 2.0314 2.1705 2.0289 0.3708  -0.1663 0.1956  36  VAL B N   
981   C CA  . VAL B 27  ? 2.0122 2.1721 2.0199 0.3644  -0.1778 0.1978  36  VAL B CA  
982   C C   . VAL B 27  ? 2.0421 2.2353 2.0488 0.3581  -0.1811 0.2069  36  VAL B C   
983   O O   . VAL B 27  ? 2.0455 2.2437 2.0285 0.3695  -0.1732 0.2020  36  VAL B O   
984   C CB  . VAL B 27  ? 2.0652 2.2157 2.0619 0.3787  -0.1800 0.1914  36  VAL B CB  
985   C CG1 . VAL B 27  ? 2.0578 2.2288 2.0614 0.3762  -0.1927 0.2016  36  VAL B CG1 
986   C CG2 . VAL B 27  ? 2.0713 2.2027 2.0752 0.3868  -0.1900 0.1858  36  VAL B CG2 
987   N N   . THR B 28  ? 1.9735 2.1947 2.0080 0.3423  -0.1968 0.2218  37  THR B N   
988   C CA  . THR B 28  ? 1.9566 2.2270 1.9979 0.3365  -0.2003 0.2401  37  THR B CA  
989   C C   . THR B 28  ? 1.9893 2.2906 2.0235 0.3508  -0.1964 0.2502  37  THR B C   
990   O O   . THR B 28  ? 1.9885 2.3015 1.9921 0.3680  -0.1809 0.2430  37  THR B O   
991   C CB  . THR B 28  ? 2.0200 2.3166 2.1063 0.3103  -0.2249 0.2595  37  THR B CB  
992   O OG1 . THR B 28  ? 1.9938 2.2864 2.1097 0.3071  -0.2507 0.2661  37  THR B OG1 
993   C CG2 . THR B 28  ? 1.9939 2.2575 2.0881 0.2937  -0.2272 0.2490  37  THR B CG2 
994   N N   . HIS B 29  ? 1.9361 2.2446 2.0000 0.3459  -0.2161 0.2669  38  HIS B N   
995   C CA  . HIS B 29  ? 1.9354 2.2659 2.0042 0.3559  -0.2177 0.2848  38  HIS B CA  
996   C C   . HIS B 29  ? 1.9937 2.2681 2.0390 0.3690  -0.2130 0.2631  38  HIS B C   
997   O O   . HIS B 29  ? 1.9919 2.2267 2.0466 0.3692  -0.2331 0.2596  38  HIS B O   
998   C CB  . HIS B 29  ? 1.9306 2.3000 2.0555 0.3421  -0.2528 0.3272  38  HIS B CB  
999   C CG  . HIS B 29  ? 1.9536 2.3867 2.1115 0.3240  -0.2633 0.3550  38  HIS B CG  
1000  N ND1 . HIS B 29  ? 1.9569 2.3993 2.1676 0.3010  -0.3055 0.3747  38  HIS B ND1 
1001  C CD2 . HIS B 29  ? 1.9732 2.4636 2.1179 0.3276  -0.2413 0.3657  38  HIS B CD2 
1002  C CE1 . HIS B 29  ? 1.9338 2.4408 2.1662 0.2853  -0.3057 0.3992  38  HIS B CE1 
1003  N NE2 . HIS B 29  ? 1.9511 2.4886 2.1411 0.3032  -0.2655 0.3949  38  HIS B NE2 
1004  N N   . SER B 30  ? 1.9558 2.2270 1.9692 0.3821  -0.1907 0.2475  39  SER B N   
1005  C CA  . SER B 30  ? 1.9611 2.1838 1.9532 0.3902  -0.1858 0.2271  39  SER B CA  
1006  C C   . SER B 30  ? 1.9884 2.2258 1.9673 0.3990  -0.1744 0.2245  39  SER B C   
1007  O O   . SER B 30  ? 1.9878 2.2645 1.9536 0.4079  -0.1635 0.2215  39  SER B O   
1008  C CB  . SER B 30  ? 2.0248 2.2130 1.9929 0.3932  -0.1752 0.1995  39  SER B CB  
1009  O OG  . SER B 30  ? 2.1605 2.3673 2.1142 0.3965  -0.1654 0.1907  39  SER B OG  
1010  N N   . VAL B 31  ? 1.9256 2.1262 1.9048 0.3993  -0.1799 0.2230  40  VAL B N   
1011  C CA  . VAL B 31  ? 1.9139 2.1198 1.8860 0.4043  -0.1722 0.2192  40  VAL B CA  
1012  C C   . VAL B 31  ? 1.9415 2.0944 1.8895 0.4024  -0.1697 0.1862  40  VAL B C   
1013  O O   . VAL B 31  ? 1.9417 2.0476 1.8840 0.3989  -0.1759 0.1791  40  VAL B O   
1014  C CB  . VAL B 31  ? 1.9613 2.1782 1.9684 0.4018  -0.1849 0.2587  40  VAL B CB  
1015  C CG1 . VAL B 31  ? 1.9691 2.1118 1.9842 0.3961  -0.2072 0.2625  40  VAL B CG1 
1016  C CG2 . VAL B 31  ? 1.9589 2.2125 1.9657 0.4104  -0.1715 0.2638  40  VAL B CG2 
1017  N N   . ASN B 32  ? 1.8789 2.0440 1.8131 0.4069  -0.1642 0.1666  41  ASN B N   
1018  C CA  . ASN B 32  ? 1.8714 1.9972 1.7923 0.4003  -0.1688 0.1382  41  ASN B CA  
1019  C C   . ASN B 32  ? 1.9261 2.0090 1.8567 0.3901  -0.1739 0.1439  41  ASN B C   
1020  O O   . ASN B 32  ? 1.9257 2.0154 1.8762 0.3913  -0.1756 0.1726  41  ASN B O   
1021  C CB  . ASN B 32  ? 1.8718 2.0265 1.7799 0.4101  -0.1742 0.1145  41  ASN B CB  
1022  C CG  . ASN B 32  ? 2.1887 2.3147 2.0926 0.4008  -0.1906 0.0870  41  ASN B CG  
1023  O OD1 . ASN B 32  ? 2.1064 2.2007 2.0130 0.3882  -0.1923 0.0867  41  ASN B OD1 
1024  N ND2 . ASN B 32  ? 2.1015 2.2445 1.9999 0.4095  -0.2074 0.0647  41  ASN B ND2 
1025  N N   . LEU B 33  ? 1.8831 1.9208 1.8046 0.3786  -0.1801 0.1220  42  LEU B N   
1026  C CA  . LEU B 33  ? 1.8848 1.8663 1.8119 0.3662  -0.1878 0.1232  42  LEU B CA  
1027  C C   . LEU B 33  ? 1.9180 1.8882 1.8434 0.3519  -0.1954 0.0937  42  LEU B C   
1028  O O   . LEU B 33  ? 1.9115 1.8455 1.8468 0.3393  -0.2018 0.0921  42  LEU B O   
1029  C CB  . LEU B 33  ? 1.9035 1.8255 1.8177 0.3662  -0.1940 0.1268  42  LEU B CB  
1030  C CG  . LEU B 33  ? 1.9788 1.8983 1.8964 0.3807  -0.1995 0.1512  42  LEU B CG  
1031  C CD1 . LEU B 33  ? 2.0066 1.8807 1.8986 0.3912  -0.2050 0.1419  42  LEU B CD1 
1032  C CD2 . LEU B 33  ? 2.0186 1.9177 1.9629 0.3807  -0.2166 0.1839  42  LEU B CD2 
1033  N N   . LEU B 34  ? 1.8614 1.8590 1.7800 0.3522  -0.2010 0.0735  43  LEU B N   
1034  C CA  . LEU B 34  ? 1.8437 1.8369 1.7686 0.3370  -0.2211 0.0466  43  LEU B CA  
1035  C C   . LEU B 34  ? 1.8792 1.9154 1.8079 0.3482  -0.2356 0.0282  43  LEU B C   
1036  O O   . LEU B 34  ? 1.8833 1.9621 1.8025 0.3711  -0.2325 0.0323  43  LEU B O   
1037  C CB  . LEU B 34  ? 1.8411 1.8411 1.7654 0.3328  -0.2289 0.0455  43  LEU B CB  
1038  C CG  . LEU B 34  ? 1.8850 1.8772 1.8257 0.3100  -0.2559 0.0290  43  LEU B CG  
1039  C CD1 . LEU B 34  ? 1.8885 1.8630 1.8250 0.3022  -0.2482 0.0427  43  LEU B CD1 
1040  C CD2 . LEU B 34  ? 1.9140 1.9496 1.8713 0.3152  -0.2872 0.0205  43  LEU B CD2 
1041  N N   . GLU B 35  ? 1.8168 1.8383 1.7573 0.3339  -0.2553 0.0052  44  GLU B N   
1042  C CA  . GLU B 35  ? 1.8113 1.8685 1.7529 0.3486  -0.2791 -0.0211 44  GLU B CA  
1043  C C   . GLU B 35  ? 1.8338 1.8819 1.7927 0.3297  -0.3240 -0.0484 44  GLU B C   
1044  O O   . GLU B 35  ? 1.8129 1.8236 1.7904 0.2973  -0.3358 -0.0570 44  GLU B O   
1045  C CB  . GLU B 35  ? 1.8319 1.8901 1.7795 0.3521  -0.2697 -0.0235 44  GLU B CB  
1046  C CG  . GLU B 35  ? 1.9936 2.0989 1.9331 0.3807  -0.2920 -0.0527 44  GLU B CG  
1047  C CD  . GLU B 35  ? 2.3397 2.5076 2.2516 0.4265  -0.2785 -0.0436 44  GLU B CD  
1048  O OE1 . GLU B 35  ? 2.2700 2.4802 2.1728 0.4556  -0.2719 -0.0480 44  GLU B OE1 
1049  O OE2 . GLU B 35  ? 2.3047 2.4811 2.2035 0.4350  -0.2754 -0.0321 44  GLU B OE2 
1050  N N   . ASP B 36  ? 1.7893 1.8693 1.7457 0.3491  -0.3544 -0.0577 45  ASP B N   
1051  C CA  . ASP B 36  ? 1.7724 1.8534 1.7552 0.3355  -0.4114 -0.0743 45  ASP B CA  
1052  C C   . ASP B 36  ? 1.8076 1.9053 1.7916 0.3552  -0.4618 -0.1125 45  ASP B C   
1053  O O   . ASP B 36  ? 1.7797 1.8731 1.7954 0.3380  -0.5212 -0.1310 45  ASP B O   
1054  C CB  . ASP B 36  ? 1.8084 1.9053 1.7958 0.3452  -0.4225 -0.0500 45  ASP B CB  
1055  C CG  . ASP B 36  ? 2.0266 2.1426 1.9813 0.3818  -0.3958 -0.0382 45  ASP B CG  
1056  O OD1 . ASP B 36  ? 2.0385 2.1513 1.9800 0.3806  -0.3462 -0.0141 45  ASP B OD1 
1057  O OD2 . ASP B 36  ? 2.1482 2.2802 2.0898 0.4130  -0.4293 -0.0546 45  ASP B OD2 
1058  N N   . LYS B 37  ? 2.0233 2.3049 1.3452 0.3893  0.0870  0.1402  46  LYS B N   
1059  C CA  . LYS B 37  ? 2.0000 2.2931 1.3310 0.3552  0.0903  0.1292  46  LYS B CA  
1060  C C   . LYS B 37  ? 2.0313 2.2529 1.3874 0.3282  0.0932  0.1145  46  LYS B C   
1061  O O   . LYS B 37  ? 2.0397 2.1957 1.4010 0.3384  0.0992  0.1214  46  LYS B O   
1062  C CB  . LYS B 37  ? 2.0472 2.3696 1.3583 0.3686  0.1013  0.1470  46  LYS B CB  
1063  C CG  . LYS B 37  ? 2.1319 2.4261 1.4238 0.4099  0.1108  0.1771  46  LYS B CG  
1064  C CD  . LYS B 37  ? 2.1766 2.5478 1.4414 0.4430  0.1096  0.1946  46  LYS B CD  
1065  C CE  . LYS B 37  ? 2.2449 2.5822 1.4894 0.4884  0.1182  0.2258  46  LYS B CE  
1066  N NZ  . LYS B 37  ? 2.2931 2.5807 1.5365 0.5132  0.1117  0.2242  46  LYS B NZ  
1067  N N   . HIS B 38  ? 1.9579 2.1936 1.3290 0.2938  0.0883  0.0936  47  HIS B N   
1068  C CA  . HIS B 38  ? 1.9375 2.1187 1.3315 0.2684  0.0902  0.0778  47  HIS B CA  
1069  C C   . HIS B 38  ? 1.9719 2.1796 1.3720 0.2383  0.0859  0.0571  47  HIS B C   
1070  O O   . HIS B 38  ? 1.9619 2.2271 1.3540 0.2301  0.0775  0.0512  47  HIS B O   
1071  C CB  . HIS B 38  ? 1.9263 2.0763 1.3400 0.2635  0.0829  0.0699  47  HIS B CB  
1072  C CG  . HIS B 38  ? 1.9449 2.1409 1.3666 0.2466  0.0691  0.0589  47  HIS B CG  
1073  N ND1 . HIS B 38  ? 1.9477 2.1306 1.3901 0.2157  0.0637  0.0419  47  HIS B ND1 
1074  C CD2 . HIS B 38  ? 1.9645 2.2220 1.3753 0.2557  0.0600  0.0650  47  HIS B CD2 
1075  C CE1 . HIS B 38  ? 1.9291 2.1608 1.3741 0.2042  0.0511  0.0398  47  HIS B CE1 
1076  N NE2 . HIS B 38  ? 1.9406 2.2229 1.3670 0.2266  0.0483  0.0531  47  HIS B NE2 
1077  N N   . ASN B 39  ? 1.9223 2.0881 1.3362 0.2219  0.0909  0.0449  48  ASN B N   
1078  C CA  . ASN B 39  ? 1.9135 2.0894 1.3336 0.1966  0.0866  0.0216  48  ASN B CA  
1079  C C   . ASN B 39  ? 1.9678 2.1170 1.4098 0.1761  0.0767  0.0074  48  ASN B C   
1080  O O   . ASN B 39  ? 1.9577 2.0724 1.4132 0.1814  0.0778  0.0140  48  ASN B O   
1081  C CB  . ASN B 39  ? 1.8796 2.0305 1.3008 0.1956  0.0977  0.0172  48  ASN B CB  
1082  C CG  . ASN B 39  ? 1.9135 2.0054 1.3504 0.1970  0.1052  0.0225  48  ASN B CG  
1083  O OD1 . ASN B 39  ? 1.7536 1.8186 1.1973 0.2051  0.1050  0.0338  48  ASN B OD1 
1084  N ND2 . ASN B 39  ? 1.7775 1.8540 1.2191 0.1904  0.1120  0.0139  48  ASN B ND2 
1085  N N   . GLY B 40  ? 1.9312 2.0951 1.3772 0.1526  0.0671  -0.0118 49  GLY B N   
1086  C CA  . GLY B 40  ? 1.9181 2.0560 1.3855 0.1317  0.0574  -0.0221 49  GLY B CA  
1087  C C   . GLY B 40  ? 1.9688 2.0497 1.4524 0.1278  0.0636  -0.0317 49  GLY B C   
1088  O O   . GLY B 40  ? 1.9553 2.0113 1.4578 0.1140  0.0573  -0.0373 49  GLY B O   
1089  N N   . LYS B 41  ? 1.9377 2.0037 1.4142 0.1405  0.0761  -0.0314 50  LYS B N   
1090  C CA  . LYS B 41  ? 1.9387 1.9628 1.4269 0.1394  0.0836  -0.0398 50  LYS B CA  
1091  C C   . LYS B 41  ? 1.9858 1.9788 1.4889 0.1471  0.0897  -0.0261 50  LYS B C   
1092  O O   . LYS B 41  ? 1.9816 1.9801 1.4796 0.1603  0.0926  -0.0090 50  LYS B O   
1093  C CB  . LYS B 41  ? 1.9867 2.0221 1.4604 0.1488  0.0940  -0.0428 50  LYS B CB  
1094  C CG  . LYS B 41  ? 2.1469 2.2179 1.6052 0.1427  0.0886  -0.0616 50  LYS B CG  
1095  C CD  . LYS B 41  ? 2.2043 2.3025 1.6475 0.1562  0.0996  -0.0598 50  LYS B CD  
1096  C CE  . LYS B 41  ? 2.2154 2.3637 1.6403 0.1679  0.1024  -0.0419 50  LYS B CE  
1097  N NZ  . LYS B 41  ? 2.2473 2.4175 1.6620 0.1836  0.1156  -0.0273 50  LYS B NZ  
1098  N N   . LEU B 42  ? 1.9406 1.9015 1.4613 0.1403  0.0914  -0.0350 51  LEU B N   
1099  C CA  . LEU B 42  ? 1.9200 1.8552 1.4566 0.1447  0.0978  -0.0266 51  LEU B CA  
1100  C C   . LEU B 42  ? 1.9755 1.8985 1.5087 0.1492  0.1106  -0.0273 51  LEU B C   
1101  O O   . LEU B 42  ? 1.9676 1.8784 1.5094 0.1451  0.1131  -0.0391 51  LEU B O   
1102  C CB  . LEU B 42  ? 1.9025 1.8224 1.4617 0.1347  0.0915  -0.0330 51  LEU B CB  
1103  C CG  . LEU B 42  ? 1.9464 1.8842 1.5137 0.1279  0.0788  -0.0281 51  LEU B CG  
1104  C CD1 . LEU B 42  ? 1.9413 1.8649 1.5308 0.1167  0.0735  -0.0325 51  LEU B CD1 
1105  C CD2 . LEU B 42  ? 1.9564 1.9064 1.5250 0.1400  0.0790  -0.0143 51  LEU B CD2 
1106  N N   . CYS B 43  ? 1.9411 1.8717 1.4606 0.1585  0.1182  -0.0130 52  CYS B N   
1107  C CA  . CYS B 43  ? 1.9510 1.8806 1.4658 0.1611  0.1301  -0.0075 52  CYS B CA  
1108  C C   . CYS B 43  ? 1.9481 1.8522 1.4794 0.1565  0.1369  -0.0034 52  CYS B C   
1109  O O   . CYS B 43  ? 1.9364 1.8226 1.4802 0.1549  0.1336  -0.0011 52  CYS B O   
1110  C CB  . CYS B 43  ? 1.9880 1.9332 1.4845 0.1712  0.1355  0.0122  52  CYS B CB  
1111  S SG  . CYS B 43  ? 2.0561 2.0455 1.5321 0.1775  0.1283  0.0083  52  CYS B SG  
1112  N N   . LYS B 44  ? 1.8751 1.7855 1.4064 0.1544  0.1462  -0.0035 53  LYS B N   
1113  C CA  . LYS B 44  ? 1.8524 1.7495 1.3979 0.1475  0.1538  0.0008  53  LYS B CA  
1114  C C   . LYS B 44  ? 1.8979 1.7757 1.4416 0.1455  0.1579  0.0217  53  LYS B C   
1115  O O   . LYS B 44  ? 1.9142 1.7981 1.4425 0.1506  0.1609  0.0374  53  LYS B O   
1116  C CB  . LYS B 44  ? 1.8876 1.8091 1.4294 0.1471  0.1625  -0.0019 53  LYS B CB  
1117  C CG  . LYS B 44  ? 2.0343 1.9702 1.5739 0.1534  0.1583  -0.0252 53  LYS B CG  
1118  C CD  . LYS B 44  ? 2.1606 2.1297 1.6925 0.1585  0.1666  -0.0281 53  LYS B CD  
1119  C CE  . LYS B 44  ? 2.2571 2.2362 1.7826 0.1692  0.1613  -0.0549 53  LYS B CE  
1120  N NZ  . LYS B 44  ? 2.3286 2.3468 1.8460 0.1786  0.1690  -0.0600 53  LYS B NZ  
1121  N N   . LEU B 45  ? 1.8413 1.6955 1.4002 0.1390  0.1576  0.0216  54  LEU B N   
1122  C CA  . LEU B 45  ? 1.8631 1.6888 1.4201 0.1367  0.1601  0.0375  54  LEU B CA  
1123  C C   . LEU B 45  ? 1.9425 1.7688 1.4994 0.1236  0.1708  0.0517  54  LEU B C   
1124  O O   . LEU B 45  ? 1.9221 1.7637 1.4910 0.1130  0.1755  0.0443  54  LEU B O   
1125  C CB  . LEU B 45  ? 1.8521 1.6557 1.4248 0.1348  0.1545  0.0283  54  LEU B CB  
1126  C CG  . LEU B 45  ? 1.9405 1.7058 1.5116 0.1330  0.1551  0.0385  54  LEU B CG  
1127  C CD1 . LEU B 45  ? 1.9553 1.7059 1.5126 0.1524  0.1474  0.0434  54  LEU B CD1 
1128  C CD2 . LEU B 45  ? 1.9620 1.7171 1.5534 0.1222  0.1541  0.0253  54  LEU B CD2 
1129  N N   . ARG B 46  ? 1.9434 1.7566 1.4865 0.1248  0.1747  0.0744  55  ARG B N   
1130  C CA  . ARG B 46  ? 1.9749 1.7881 1.5162 0.1102  0.1842  0.0960  55  ARG B CA  
1131  C C   . ARG B 46  ? 2.0049 1.8651 1.5515 0.1010  0.1911  0.0913  55  ARG B C   
1132  O O   . ARG B 46  ? 2.0141 1.8786 1.5699 0.0825  0.1974  0.0990  55  ARG B O   
1133  C CB  . ARG B 46  ? 2.0262 1.7909 1.5765 0.0948  0.1846  0.1036  55  ARG B CB  
1134  C CG  . ARG B 46  ? 2.1738 1.9289 1.7440 0.0855  0.1809  0.0803  55  ARG B CG  
1135  C CD  . ARG B 46  ? 2.3741 2.0776 1.9495 0.0731  0.1791  0.0841  55  ARG B CD  
1136  N NE  . ARG B 46  ? 2.4932 2.1913 2.0855 0.0711  0.1733  0.0590  55  ARG B NE  
1137  C CZ  . ARG B 46  ? 2.7180 2.3761 2.3172 0.0617  0.1698  0.0524  55  ARG B CZ  
1138  N NH1 . ARG B 46  ? 2.6249 2.2342 2.2150 0.0521  0.1709  0.0697  55  ARG B NH1 
1139  N NH2 . ARG B 46  ? 2.5196 2.1864 2.1349 0.0621  0.1646  0.0284  55  ARG B NH2 
1140  N N   . GLY B 47  A 1.9329 1.8296 1.4726 0.1145  0.1894  0.0780  55  GLY B N   
1141  C CA  . GLY B 47  A 1.9173 1.8601 1.4585 0.1134  0.1947  0.0694  55  GLY B CA  
1142  C C   . GLY B 47  A 1.9332 1.8802 1.4875 0.1159  0.1915  0.0428  55  GLY B C   
1143  O O   . GLY B 47  A 1.9267 1.9001 1.4759 0.1279  0.1899  0.0260  55  GLY B O   
1144  N N   . VAL B 48  ? 1.8614 1.7827 1.4322 0.1056  0.1904  0.0387  56  VAL B N   
1145  C CA  . VAL B 48  ? 1.8206 1.7476 1.4064 0.1080  0.1883  0.0182  56  VAL B CA  
1146  C C   . VAL B 48  ? 1.8186 1.7326 1.4038 0.1221  0.1781  0.0014  56  VAL B C   
1147  O O   . VAL B 48  ? 1.8225 1.7130 1.4046 0.1246  0.1712  0.0042  56  VAL B O   
1148  C CB  . VAL B 48  ? 1.8634 1.7779 1.4680 0.0928  0.1901  0.0184  56  VAL B CB  
1149  C CG1 . VAL B 48  ? 1.8676 1.8177 1.4777 0.0797  0.2000  0.0243  56  VAL B CG1 
1150  C CG2 . VAL B 48  ? 1.8778 1.7513 1.4822 0.0839  0.1869  0.0296  56  VAL B CG2 
1151  N N   . ALA B 49  ? 1.7233 1.6537 1.3106 0.1316  0.1769  -0.0153 57  ALA B N   
1152  C CA  . ALA B 49  ? 1.6940 1.6112 1.2814 0.1413  0.1669  -0.0308 57  ALA B CA  
1153  C C   . ALA B 49  ? 1.6740 1.5731 1.2805 0.1383  0.1610  -0.0343 57  ALA B C   
1154  O O   . ALA B 49  ? 1.6582 1.5645 1.2796 0.1337  0.1661  -0.0329 57  ALA B O   
1155  C CB  . ALA B 49  ? 1.7126 1.6463 1.2937 0.1535  0.1675  -0.0473 57  ALA B CB  
1156  N N   . PRO B 50  ? 1.5882 1.4722 1.1953 0.1403  0.1502  -0.0381 58  PRO B N   
1157  C CA  . PRO B 50  ? 1.5501 1.4274 1.1766 0.1380  0.1444  -0.0386 58  PRO B CA  
1158  C C   . PRO B 50  ? 1.5521 1.4311 1.1906 0.1429  0.1429  -0.0478 58  PRO B C   
1159  O O   . PRO B 50  ? 1.5670 1.4445 1.1958 0.1501  0.1438  -0.0575 58  PRO B O   
1160  C CB  . PRO B 50  ? 1.5728 1.4426 1.1933 0.1378  0.1334  -0.0360 58  PRO B CB  
1161  C CG  . PRO B 50  ? 1.6546 1.5258 1.2553 0.1408  0.1316  -0.0413 58  PRO B CG  
1162  C CD  . PRO B 50  ? 1.6169 1.4980 1.2077 0.1435  0.1427  -0.0409 58  PRO B CD  
1163  N N   . LEU B 51  ? 1.4514 1.3346 1.1105 0.1413  0.1403  -0.0448 59  LEU B N   
1164  C CA  . LEU B 51  ? 1.4301 1.3146 1.1032 0.1473  0.1389  -0.0483 59  LEU B CA  
1165  C C   . LEU B 51  ? 1.4847 1.3553 1.1626 0.1445  0.1257  -0.0464 59  LEU B C   
1166  O O   . LEU B 51  ? 1.4722 1.3544 1.1639 0.1395  0.1201  -0.0378 59  LEU B O   
1167  C CB  . LEU B 51  ? 1.4015 1.3104 1.0958 0.1469  0.1454  -0.0432 59  LEU B CB  
1168  C CG  . LEU B 51  ? 1.4517 1.3695 1.1612 0.1566  0.1467  -0.0430 59  LEU B CG  
1169  C CD1 . LEU B 51  ? 1.4474 1.3865 1.1552 0.1646  0.1593  -0.0469 59  LEU B CD1 
1170  C CD2 . LEU B 51  ? 1.4852 1.4248 1.2190 0.1539  0.1433  -0.0340 59  LEU B CD2 
1171  N N   . HIS B 52  ? 1.4620 1.3109 1.1281 0.1466  0.1200  -0.0552 60  HIS B N   
1172  C CA  . HIS B 52  ? 1.4690 1.3024 1.1388 0.1387  0.1064  -0.0532 60  HIS B CA  
1173  C C   . HIS B 52  ? 1.5427 1.3618 1.2286 0.1431  0.1039  -0.0506 60  HIS B C   
1174  O O   . HIS B 52  ? 1.5590 1.3611 1.2393 0.1554  0.1086  -0.0607 60  HIS B O   
1175  C CB  . HIS B 52  ? 1.5050 1.3215 1.1526 0.1344  0.0997  -0.0655 60  HIS B CB  
1176  C CG  . HIS B 52  ? 1.5605 1.3655 1.2112 0.1204  0.0848  -0.0631 60  HIS B CG  
1177  N ND1 . HIS B 52  ? 1.5684 1.3949 1.2172 0.1095  0.0775  -0.0538 60  HIS B ND1 
1178  C CD2 . HIS B 52  ? 1.6140 1.3886 1.2686 0.1152  0.0758  -0.0680 60  HIS B CD2 
1179  C CE1 . HIS B 52  ? 1.5795 1.3953 1.2320 0.0952  0.0644  -0.0525 60  HIS B CE1 
1180  N NE2 . HIS B 52  ? 1.6140 1.3940 1.2705 0.0964  0.0625  -0.0607 60  HIS B NE2 
1181  N N   . LEU B 53  ? 1.4988 1.3276 1.2041 0.1350  0.0961  -0.0356 61  LEU B N   
1182  C CA  . LEU B 53  ? 1.5137 1.3321 1.2375 0.1377  0.0927  -0.0258 61  LEU B CA  
1183  C C   . LEU B 53  ? 1.6218 1.4162 1.3467 0.1215  0.0770  -0.0202 61  LEU B C   
1184  O O   . LEU B 53  ? 1.6008 1.4195 1.3409 0.1092  0.0688  -0.0029 61  LEU B O   
1185  C CB  . LEU B 53  ? 1.4732 1.3340 1.2225 0.1407  0.0972  -0.0091 61  LEU B CB  
1186  C CG  . LEU B 53  ? 1.4979 1.3891 1.2487 0.1499  0.1110  -0.0142 61  LEU B CG  
1187  C CD1 . LEU B 53  ? 1.4579 1.3946 1.2308 0.1475  0.1111  -0.0024 61  LEU B CD1 
1188  C CD2 . LEU B 53  ? 1.5431 1.4302 1.2938 0.1658  0.1218  -0.0194 61  LEU B CD2 
1189  N N   . GLY B 54  ? 1.6462 1.3973 1.3541 0.1204  0.0721  -0.0360 62  GLY B N   
1190  C CA  . GLY B 54  ? 1.6912 1.4121 1.3986 0.1012  0.0563  -0.0340 62  GLY B CA  
1191  C C   . GLY B 54  ? 1.7885 1.4831 1.5158 0.1024  0.0521  -0.0183 62  GLY B C   
1192  O O   . GLY B 54  ? 1.7993 1.4798 1.5296 0.1241  0.0615  -0.0208 62  GLY B O   
1193  N N   . LYS B 55  ? 1.7662 1.4593 1.5075 0.0797  0.0384  0.0009  63  LYS B N   
1194  C CA  . LYS B 55  ? 1.8017 1.4709 1.5645 0.0771  0.0328  0.0232  63  LYS B CA  
1195  C C   . LYS B 55  ? 1.8371 1.5417 1.6200 0.1002  0.0462  0.0394  63  LYS B C   
1196  O O   . LYS B 55  ? 1.8614 1.5370 1.6529 0.1151  0.0493  0.0473  63  LYS B O   
1197  C CB  . LYS B 55  ? 1.9119 1.4999 1.6623 0.0785  0.0260  0.0078  63  LYS B CB  
1198  C CG  . LYS B 55  ? 2.1371 1.6903 1.8807 0.0450  0.0073  0.0045  63  LYS B CG  
1199  C CD  . LYS B 55  ? 2.2688 1.7359 1.9953 0.0479  0.0002  -0.0204 63  LYS B CD  
1200  C CE  . LYS B 55  ? 2.2918 1.7319 2.0065 0.0123  -0.0176 -0.0328 63  LYS B CE  
1201  N NZ  . LYS B 55  ? 2.3805 1.7357 2.0759 0.0162  -0.0253 -0.0642 63  LYS B NZ  
1202  N N   . CYS B 56  ? 1.7494 1.5170 1.5380 0.1043  0.0540  0.0424  64  CYS B N   
1203  C CA  . CYS B 56  ? 1.7089 1.5245 1.5155 0.1224  0.0665  0.0531  64  CYS B CA  
1204  C C   . CYS B 56  ? 1.6715 1.5490 1.4828 0.1169  0.0680  0.0548  64  CYS B C   
1205  O O   . CYS B 56  ? 1.6691 1.5449 1.4618 0.1091  0.0654  0.0406  64  CYS B O   
1206  C CB  . CYS B 56  ? 1.7270 1.5271 1.5209 0.1468  0.0812  0.0340  64  CYS B CB  
1207  S SG  . CYS B 56  ? 1.7517 1.5994 1.5696 0.1697  0.0953  0.0496  64  CYS B SG  
1208  N N   . ASN B 57  ? 1.5433 1.4762 1.3784 0.1233  0.0720  0.0711  65  ASN B N   
1209  C CA  . ASN B 57  ? 1.4717 1.4613 1.3111 0.1226  0.0734  0.0689  65  ASN B CA  
1210  C C   . ASN B 57  ? 1.4502 1.4636 1.2929 0.1395  0.0887  0.0574  65  ASN B C   
1211  O O   . ASN B 57  ? 1.4675 1.4638 1.3116 0.1516  0.0975  0.0561  65  ASN B O   
1212  C CB  . ASN B 57  ? 1.4397 1.4850 1.3039 0.1147  0.0636  0.0939  65  ASN B CB  
1213  C CG  . ASN B 57  ? 1.7015 1.7641 1.5921 0.1206  0.0651  0.1182  65  ASN B CG  
1214  O OD1 . ASN B 57  ? 1.6155 1.6967 1.5157 0.1376  0.0771  0.1164  65  ASN B OD1 
1215  N ND2 . ASN B 57  ? 1.6023 1.6625 1.5054 0.1059  0.0528  0.1434  65  ASN B ND2 
1216  N N   . ILE B 58  ? 1.3261 1.3782 1.1692 0.1407  0.0916  0.0486  66  ILE B N   
1217  C CA  . ILE B 58  ? 1.2842 1.3610 1.1313 0.1510  0.1048  0.0368  66  ILE B CA  
1218  C C   . ILE B 58  ? 1.3072 1.4218 1.1794 0.1615  0.1109  0.0507  66  ILE B C   
1219  O O   . ILE B 58  ? 1.3094 1.4200 1.1793 0.1712  0.1225  0.0441  66  ILE B O   
1220  C CB  . ILE B 58  ? 1.2932 1.4016 1.1389 0.1490  0.1040  0.0254  66  ILE B CB  
1221  C CG1 . ILE B 58  ? 1.3191 1.3865 1.1371 0.1430  0.1009  0.0130  66  ILE B CG1 
1222  C CG2 . ILE B 58  ? 1.2750 1.4124 1.1286 0.1547  0.1160  0.0137  66  ILE B CG2 
1223  C CD1 . ILE B 58  ? 1.4075 1.4964 1.2213 0.1436  0.0956  0.0060  66  ILE B CD1 
1224  N N   . ALA B 59  ? 1.2423 1.3979 1.1377 0.1603  0.1031  0.0721  67  ALA B N   
1225  C CA  . ALA B 59  ? 1.2263 1.4277 1.1483 0.1713  0.1080  0.0911  67  ALA B CA  
1226  C C   . ALA B 59  ? 1.2904 1.4515 1.2096 0.1825  0.1148  0.0985  67  ALA B C   
1227  O O   . ALA B 59  ? 1.2895 1.4836 1.2193 0.1974  0.1262  0.1006  67  ALA B O   
1228  C CB  . ALA B 59  ? 1.2243 1.4710 1.1695 0.1658  0.0963  0.1176  67  ALA B CB  
1229  N N   . GLY B 60  ? 1.3913 1.5605 1.1510 -0.0180 0.0708  -0.0140 68  GLY B N   
1230  C CA  . GLY B 60  ? 1.3821 1.5234 1.1506 -0.0326 0.0659  -0.0226 68  GLY B CA  
1231  C C   . GLY B 60  ? 1.4083 1.5140 1.1580 -0.0341 0.0766  -0.0498 68  GLY B C   
1232  O O   . GLY B 60  ? 1.3937 1.4868 1.1462 -0.0357 0.0783  -0.0647 68  GLY B O   
1233  N N   . TRP B 61  ? 1.3674 1.4628 1.0985 -0.0330 0.0833  -0.0534 69  TRP B N   
1234  C CA  . TRP B 61  ? 1.3797 1.4562 1.0984 -0.0338 0.0932  -0.0680 69  TRP B CA  
1235  C C   . TRP B 61  ? 1.3797 1.4546 1.1071 -0.0271 0.1019  -0.0770 69  TRP B C   
1236  O O   . TRP B 61  ? 1.3776 1.4428 1.1036 -0.0294 0.1080  -0.0869 69  TRP B O   
1237  C CB  . TRP B 61  ? 1.3886 1.4625 1.0928 -0.0346 0.0963  -0.0623 69  TRP B CB  
1238  C CG  . TRP B 61  ? 1.4179 1.4869 1.1200 -0.0344 0.1059  -0.0656 69  TRP B CG  
1239  C CD1 . TRP B 61  ? 1.4673 1.5387 1.1650 -0.0348 0.1116  -0.0689 69  TRP B CD1 
1240  C CD2 . TRP B 61  ? 1.4180 1.4861 1.1273 -0.0320 0.1055  -0.0614 69  TRP B CD2 
1241  N NE1 . TRP B 61  ? 1.4662 1.5429 1.1727 -0.0365 0.1182  -0.0602 69  TRP B NE1 
1242  C CE2 . TRP B 61  ? 1.4768 1.5455 1.1929 -0.0364 0.1119  -0.0565 69  TRP B CE2 
1243  C CE3 . TRP B 61  ? 1.4323 1.5044 1.1456 -0.0229 0.0950  -0.0608 69  TRP B CE3 
1244  C CZ2 . TRP B 61  ? 1.4708 1.5365 1.2051 -0.0378 0.1059  -0.0476 69  TRP B CZ2 
1245  C CZ3 . TRP B 61  ? 1.4589 1.5240 1.1842 -0.0195 0.0859  -0.0600 69  TRP B CZ3 
1246  C CH2 . TRP B 61  ? 1.4746 1.5328 1.2140 -0.0297 0.0902  -0.0520 69  TRP B CH2 
1247  N N   . ILE B 62  ? 1.3055 1.3937 1.0427 -0.0149 0.0990  -0.0740 70  ILE B N   
1248  C CA  . ILE B 62  ? 1.2958 1.3797 1.0476 -0.0023 0.0999  -0.0849 70  ILE B CA  
1249  C C   . ILE B 62  ? 1.3209 1.4089 1.0846 0.0043  0.1048  -0.0953 70  ILE B C   
1250  O O   . ILE B 62  ? 1.3229 1.3958 1.0956 0.0085  0.1095  -0.1083 70  ILE B O   
1251  C CB  . ILE B 62  ? 1.3394 1.4363 1.0968 0.0170  0.0860  -0.0835 70  ILE B CB  
1252  C CG1 . ILE B 62  ? 1.3543 1.4328 1.1322 0.0272  0.0769  -0.0943 70  ILE B CG1 
1253  C CG2 . ILE B 62  ? 1.3365 1.4733 1.0981 0.0389  0.0786  -0.0793 70  ILE B CG2 
1254  C CD1 . ILE B 62  ? 1.4638 1.5206 1.2446 0.0085  0.0768  -0.0855 70  ILE B CD1 
1255  N N   . LEU B 63  ? 1.2487 1.3577 1.0162 0.0040  0.1026  -0.0873 71  LEU B N   
1256  C CA  . LEU B 63  ? 1.2222 1.3383 1.0029 0.0087  0.1069  -0.0950 71  LEU B CA  
1257  C C   . LEU B 63  ? 1.2792 1.3668 1.0483 -0.0098 0.1095  -0.1074 71  LEU B C   
1258  O O   . LEU B 63  ? 1.2817 1.3606 1.0533 -0.0070 0.1162  -0.1235 71  LEU B O   
1259  C CB  . LEU B 63  ? 1.2043 1.3629 1.0020 0.0141  0.0994  -0.0734 71  LEU B CB  
1260  C CG  . LEU B 63  ? 1.2458 1.4540 1.0559 0.0441  0.0957  -0.0626 71  LEU B CG  
1261  C CD1 . LEU B 63  ? 1.2378 1.4991 1.0643 0.0436  0.0869  -0.0283 71  LEU B CD1 
1262  C CD2 . LEU B 63  ? 1.2738 1.4935 1.0988 0.0719  0.1021  -0.0816 71  LEU B CD2 
1263  N N   . GLY B 64  ? 1.2259 1.3023 0.9805 -0.0239 0.1018  -0.1025 72  GLY B N   
1264  C CA  . GLY B 64  ? 1.2272 1.2854 0.9672 -0.0331 0.0956  -0.1166 72  GLY B CA  
1265  C C   . GLY B 64  ? 1.2741 1.3337 1.0250 -0.0409 0.0737  -0.1113 72  GLY B C   
1266  O O   . GLY B 64  ? 1.2722 1.3194 1.0183 -0.0438 0.0639  -0.1279 72  GLY B O   
1267  N N   . ASN B 65  ? 1.2382 1.3135 1.0059 -0.0445 0.0619  -0.0868 73  ASN B N   
1268  C CA  . ASN B 65  ? 1.2508 1.3293 1.0423 -0.0544 0.0334  -0.0717 73  ASN B CA  
1269  C C   . ASN B 65  ? 1.3354 1.3845 1.1125 -0.0559 0.0091  -0.0929 73  ASN B C   
1270  O O   . ASN B 65  ? 1.3439 1.3852 1.0988 -0.0491 0.0120  -0.1017 73  ASN B O   
1271  C CB  . ASN B 65  ? 1.2931 1.3952 1.1018 -0.0571 0.0260  -0.0389 73  ASN B CB  
1272  C CG  . ASN B 65  ? 1.7377 1.8460 1.5828 -0.0696 -0.0085 -0.0133 73  ASN B CG  
1273  O OD1 . ASN B 65  ? 1.6857 1.7959 1.5578 -0.0769 -0.0271 -0.0087 73  ASN B OD1 
1274  N ND2 . ASN B 65  ? 1.7010 1.8131 1.5522 -0.0730 -0.0204 0.0067  73  ASN B ND2 
1275  N N   . PRO B 66  ? 1.3119 1.3488 1.0998 -0.0602 -0.0166 -0.1041 74  PRO B N   
1276  C CA  . PRO B 66  ? 1.3487 1.3628 1.1186 -0.0522 -0.0471 -0.1314 74  PRO B CA  
1277  C C   . PRO B 66  ? 1.4650 1.4714 1.2427 -0.0459 -0.0773 -0.1260 74  PRO B C   
1278  O O   . PRO B 66  ? 1.4829 1.4813 1.2368 -0.0275 -0.0953 -0.1523 74  PRO B O   
1279  C CB  . PRO B 66  ? 1.3704 1.3734 1.1592 -0.0596 -0.0766 -0.1397 74  PRO B CB  
1280  C CG  . PRO B 66  ? 1.3945 1.4199 1.2263 -0.0745 -0.0698 -0.1030 74  PRO B CG  
1281  C CD  . PRO B 66  ? 1.3145 1.3618 1.1310 -0.0685 -0.0221 -0.0945 74  PRO B CD  
1282  N N   . GLU B 67  ? 1.4402 1.4551 1.2498 -0.0568 -0.0827 -0.0923 75  GLU B N   
1283  C CA  . GLU B 67  ? 1.4616 1.4671 1.2833 -0.0519 -0.1094 -0.0839 75  GLU B CA  
1284  C C   . GLU B 67  ? 1.5057 1.5146 1.2883 -0.0363 -0.0804 -0.0972 75  GLU B C   
1285  O O   . GLU B 67  ? 1.5176 1.5173 1.3006 -0.0242 -0.0999 -0.1015 75  GLU B O   
1286  C CB  . GLU B 67  ? 1.4733 1.4957 1.3378 -0.0694 -0.1168 -0.0386 75  GLU B CB  
1287  C CG  . GLU B 67  ? 1.6435 1.6797 1.5559 -0.0864 -0.1397 -0.0121 75  GLU B CG  
1288  C CD  . GLU B 67  ? 1.9725 2.0501 1.9249 -0.1004 -0.1363 0.0413  75  GLU B CD  
1289  O OE1 . GLU B 67  ? 1.7085 1.8262 1.6601 -0.1009 -0.1037 0.0577  75  GLU B OE1 
1290  O OE2 . GLU B 67  ? 2.0310 2.1059 2.0168 -0.1071 -0.1688 0.0674  75  GLU B OE2 
1291  N N   . CYS B 68  ? 1.4407 1.4636 1.1953 -0.0359 -0.0370 -0.1022 76  CYS B N   
1292  C CA  . CYS B 68  ? 1.7773 1.8093 1.5023 -0.0255 -0.0081 -0.1080 76  CYS B CA  
1293  C C   . CYS B 68  ? 1.9470 1.9878 1.6467 -0.0151 0.0063  -0.1294 76  CYS B C   
1294  O O   . CYS B 68  ? 1.4959 1.5490 1.1759 0.0040  0.0029  -0.1432 76  CYS B O   
1295  C CB  . CYS B 68  ? 1.7654 1.8088 1.4914 -0.0362 0.0220  -0.0860 76  CYS B CB  
1296  S SG  . CYS B 68  ? 1.8118 1.8634 1.5681 -0.0490 0.0077  -0.0533 76  CYS B SG  
1297  N N   . ALA B 74  ? 1.6620 1.8946 1.3613 0.0006  0.1437  -0.0202 82  ALA B N   
1298  C CA  . ALA B 74  ? 1.6618 1.9283 1.3842 -0.0033 0.1526  0.0133  82  ALA B CA  
1299  C C   . ALA B 74  ? 1.7150 1.9555 1.4733 -0.0281 0.1499  0.0331  82  ALA B C   
1300  O O   . ALA B 74  ? 1.7010 1.8902 1.4593 -0.0385 0.1421  0.0167  82  ALA B O   
1301  C CB  . ALA B 74  ? 1.6715 1.9344 1.3821 0.0039  0.1546  0.0096  82  ALA B CB  
1302  N N   . SER B 75  ? 1.6847 1.9674 1.4778 -0.0337 0.1518  0.0705  83  SER B N   
1303  C CA  . SER B 75  ? 1.6863 1.9494 1.5265 -0.0545 0.1396  0.0944  83  SER B CA  
1304  C C   . SER B 75  ? 1.7473 1.9984 1.6130 -0.0665 0.1290  0.1132  83  SER B C   
1305  O O   . SER B 75  ? 1.7404 1.9428 1.6248 -0.0770 0.1092  0.1055  83  SER B O   
1306  C CB  . SER B 75  ? 1.7293 2.0452 1.6032 -0.0571 0.1411  0.1316  83  SER B CB  
1307  O OG  . SER B 75  ? 1.8278 2.1258 1.7592 -0.0768 0.1221  0.1602  83  SER B OG  
1308  N N   . SER B 76  A 1.7150 2.0145 1.5823 -0.0612 0.1390  0.1368  83  SER B N   
1309  C CA  . SER B 76  A 1.7178 2.0115 1.6093 -0.0733 0.1293  0.1569  83  SER B CA  
1310  C C   . SER B 76  A 1.7599 2.0289 1.6067 -0.0647 0.1376  0.1272  83  SER B C   
1311  O O   . SER B 76  A 1.7482 2.0426 1.5599 -0.0446 0.1555  0.1124  83  SER B O   
1312  C CB  . SER B 76  A 1.7680 2.1384 1.7042 -0.0758 0.1335  0.2127  83  SER B CB  
1313  O OG  . SER B 76  A 1.8849 2.2817 1.8694 -0.0863 0.1230  0.2478  83  SER B OG  
1314  N N   . TRP B 77  ? 1.7160 1.9361 1.5651 -0.0770 0.1198  0.1173  84  TRP B N   
1315  C CA  . TRP B 77  ? 1.7071 1.9011 1.5153 -0.0721 0.1247  0.0920  84  TRP B CA  
1316  C C   . TRP B 77  ? 1.7101 1.8755 1.5339 -0.0860 0.1013  0.0978  84  TRP B C   
1317  O O   . TRP B 77  ? 1.7047 1.8530 1.5696 -0.0974 0.0722  0.1107  84  TRP B O   
1318  C CB  . TRP B 77  ? 1.6975 1.8538 1.4610 -0.0627 0.1276  0.0515  84  TRP B CB  
1319  C CG  . TRP B 77  ? 1.7179 1.8341 1.4880 -0.0676 0.1061  0.0361  84  TRP B CG  
1320  C CD1 . TRP B 77  ? 1.7620 1.8455 1.5233 -0.0685 0.0852  0.0219  84  TRP B CD1 
1321  C CD2 . TRP B 77  ? 1.7160 1.8264 1.4980 -0.0652 0.1029  0.0295  84  TRP B CD2 
1322  N NE1 . TRP B 77  ? 1.7562 1.8203 1.5277 -0.0629 0.0677  0.0085  84  TRP B NE1 
1323  C CE2 . TRP B 77  ? 1.7690 1.8458 1.5536 -0.0624 0.0803  0.0124  84  TRP B CE2 
1324  C CE3 . TRP B 77  ? 1.7308 1.8649 1.5195 -0.0619 0.1155  0.0347  84  TRP B CE3 
1325  C CZ2 . TRP B 77  ? 1.7580 1.8233 1.5549 -0.0560 0.0732  0.0007  84  TRP B CZ2 
1326  C CZ3 . TRP B 77  ? 1.7488 1.8648 1.5461 -0.0605 0.1089  0.0223  84  TRP B CZ3 
1327  C CH2 . TRP B 77  ? 1.7563 1.8377 1.5597 -0.0576 0.0894  0.0059  84  TRP B CH2 
1328  N N   . SER B 78  ? 1.6354 1.7931 1.4257 -0.0825 0.1100  0.0850  85  SER B N   
1329  C CA  . SER B 78  ? 1.6281 1.7590 1.4190 -0.0926 0.0886  0.0837  85  SER B CA  
1330  C C   . SER B 78  ? 1.6431 1.7249 1.3923 -0.0872 0.0715  0.0450  85  SER B C   
1331  O O   . SER B 78  ? 1.6451 1.7009 1.4019 -0.0917 0.0379  0.0396  85  SER B O   
1332  C CB  . SER B 78  ? 1.6739 1.8304 1.4487 -0.0894 0.1109  0.0917  85  SER B CB  
1333  O OG  . SER B 78  ? 1.7900 1.9538 1.5191 -0.0706 0.1403  0.0682  85  SER B OG  
1334  N N   . TYR B 79  ? 1.5654 1.6413 1.2734 -0.0752 0.0904  0.0206  86  TYR B N   
1335  C CA  . TYR B 79  ? 1.5485 1.5971 1.2176 -0.0668 0.0796  -0.0083 86  TYR B CA  
1336  C C   . TYR B 79  ? 1.5551 1.6088 1.2041 -0.0580 0.0986  -0.0199 86  TYR B C   
1337  O O   . TYR B 79  ? 1.5514 1.6228 1.2013 -0.0550 0.1202  -0.0145 86  TYR B O   
1338  C CB  . TYR B 79  ? 1.5646 1.5987 1.1940 -0.0663 0.0765  -0.0217 86  TYR B CB  
1339  C CG  . TYR B 79  ? 1.5732 1.6171 1.1773 -0.0645 0.1078  -0.0222 86  TYR B CG  
1340  C CD1 . TYR B 79  ? 1.5934 1.6569 1.2165 -0.0692 0.1198  -0.0038 86  TYR B CD1 
1341  C CD2 . TYR B 79  ? 1.5760 1.6123 1.1408 -0.0557 0.1213  -0.0397 86  TYR B CD2 
1342  C CE1 . TYR B 79  ? 1.5842 1.6601 1.1839 -0.0597 0.1472  -0.0083 86  TYR B CE1 
1343  C CE2 . TYR B 79  ? 1.5804 1.6206 1.1248 -0.0490 0.1444  -0.0444 86  TYR B CE2 
1344  C CZ  . TYR B 79  ? 1.6393 1.6993 1.1989 -0.0484 0.1583  -0.0318 86  TYR B CZ  
1345  O OH  . TYR B 79  ? 1.6148 1.6824 1.1549 -0.0344 0.1804  -0.0400 86  TYR B OH  
1346  N N   . ILE B 80  ? 1.4767 1.9215 1.4251 0.2660  -0.0924 -0.0173 87  ILE B N   
1347  C CA  . ILE B 80  ? 1.4267 1.8943 1.3723 0.2112  -0.0973 -0.0645 87  ILE B CA  
1348  C C   . ILE B 80  ? 1.4797 2.0552 1.4511 0.2032  -0.1355 -0.0952 87  ILE B C   
1349  O O   . ILE B 80  ? 1.4536 2.0881 1.4890 0.2223  -0.1451 -0.0957 87  ILE B O   
1350  C CB  . ILE B 80  ? 1.3973 1.8150 1.3851 0.1729  -0.0684 -0.0853 87  ILE B CB  
1351  C CG1 . ILE B 80  ? 1.4087 1.7275 1.3840 0.1784  -0.0361 -0.0547 87  ILE B CG1 
1352  C CG2 . ILE B 80  ? 1.3640 1.7945 1.3412 0.1189  -0.0700 -0.1272 87  ILE B CG2 
1353  C CD1 . ILE B 80  ? 1.4976 1.7799 1.5229 0.2037  -0.0243 -0.0364 87  ILE B CD1 
1354  N N   . VAL B 81  ? 1.4761 2.0773 1.4007 0.1746  -0.1571 -0.1220 88  VAL B N   
1355  C CA  . VAL B 81  ? 1.4874 2.1916 1.4397 0.1541  -0.1984 -0.1569 88  VAL B CA  
1356  C C   . VAL B 81  ? 1.5099 2.2061 1.4902 0.0889  -0.1870 -0.2005 88  VAL B C   
1357  O O   . VAL B 81  ? 1.5046 2.1161 1.4433 0.0633  -0.1593 -0.2068 88  VAL B O   
1358  C CB  . VAL B 81  ? 1.6166 2.3597 1.4938 0.1692  -0.2409 -0.1602 88  VAL B CB  
1359  C CG1 . VAL B 81  ? 1.6245 2.4969 1.5560 0.1643  -0.2926 -0.1840 88  VAL B CG1 
1360  C CG2 . VAL B 81  ? 1.6745 2.3812 1.4889 0.2323  -0.2359 -0.1080 88  VAL B CG2 
1361  N N   . GLU B 82  ? 1.4462 2.2326 1.5030 0.0648  -0.2051 -0.2257 89  GLU B N   
1362  C CA  . GLU B 82  ? 1.4154 2.2080 1.5099 0.0027  -0.1952 -0.2630 89  GLU B CA  
1363  C C   . GLU B 82  ? 1.4901 2.4013 1.6383 -0.0234 -0.2391 -0.2913 89  GLU B C   
1364  O O   . GLU B 82  ? 1.4828 2.4915 1.6893 0.0084  -0.2624 -0.2786 89  GLU B O   
1365  C CB  . GLU B 82  ? 1.3689 2.1404 1.5247 -0.0022 -0.1536 -0.2565 89  GLU B CB  
1366  C CG  . GLU B 82  ? 1.4941 2.2502 1.6738 -0.0630 -0.1337 -0.2861 89  GLU B CG  
1367  C CD  . GLU B 82  ? 1.6914 2.4877 1.9506 -0.0687 -0.1074 -0.2862 89  GLU B CD  
1368  O OE1 . GLU B 82  ? 1.4632 2.3611 1.7947 -0.0869 -0.1209 -0.2993 89  GLU B OE1 
1369  O OE2 . GLU B 82  ? 1.6726 2.4003 1.9214 -0.0553 -0.0729 -0.2735 89  GLU B OE2 
1370  N N   . THR B 83  ? 1.4754 2.3772 1.6067 -0.0808 -0.2516 -0.3292 90  THR B N   
1371  C CA  . THR B 83  ? 1.5001 2.5085 1.6911 -0.1201 -0.2946 -0.3613 90  THR B CA  
1372  C C   . THR B 83  ? 1.5000 2.5684 1.8060 -0.1458 -0.2669 -0.3613 90  THR B C   
1373  O O   . THR B 83  ? 1.4625 2.4555 1.7670 -0.1649 -0.2194 -0.3586 90  THR B O   
1374  C CB  . THR B 83  ? 1.6348 2.5890 1.7651 -0.1764 -0.3114 -0.4039 90  THR B CB  
1375  O OG1 . THR B 83  ? 1.6846 2.5607 1.6942 -0.1445 -0.3194 -0.3990 90  THR B OG1 
1376  C CG2 . THR B 83  ? 1.6592 2.7189 1.8452 -0.2218 -0.3664 -0.4419 90  THR B CG2 
1377  N N   . PRO B 84  A 1.4513 2.6569 1.8569 -0.1426 -0.2931 -0.3613 90  PRO B N   
1378  C CA  . PRO B 84  A 1.3981 2.6628 1.9115 -0.1655 -0.2589 -0.3589 90  PRO B CA  
1379  C C   . PRO B 84  A 1.4567 2.6918 1.9899 -0.2453 -0.2431 -0.3891 90  PRO B C   
1380  O O   . PRO B 84  A 1.4058 2.6126 1.9725 -0.2633 -0.1934 -0.3818 90  PRO B O   
1381  C CB  . PRO B 84  A 1.4261 2.8541 2.0407 -0.1457 -0.2975 -0.3535 90  PRO B CB  
1382  C CG  . PRO B 84  A 1.5452 3.0040 2.1097 -0.1442 -0.3634 -0.3696 90  PRO B CG  
1383  C CD  . PRO B 84  A 1.5148 2.8334 1.9410 -0.1173 -0.3542 -0.3621 90  PRO B CD  
1384  N N   . SER B 85  ? 1.4833 2.7118 1.9827 -0.2901 -0.2854 -0.4230 91  SER B N   
1385  C CA  . SER B 85  ? 1.5149 2.7021 2.0207 -0.3683 -0.2811 -0.4568 91  SER B CA  
1386  C C   . SER B 85  ? 1.5661 2.5952 1.9855 -0.3787 -0.2311 -0.4546 91  SER B C   
1387  O O   . SER B 85  ? 1.5654 2.5517 2.0030 -0.4364 -0.2084 -0.4706 91  SER B O   
1388  C CB  . SER B 85  ? 1.6395 2.8480 2.1114 -0.4007 -0.3468 -0.4968 91  SER B CB  
1389  O OG  . SER B 85  ? 1.7259 3.0819 2.2661 -0.3820 -0.4013 -0.4965 91  SER B OG  
1390  N N   . SER B 86  ? 1.5225 2.4678 1.8537 -0.3230 -0.2140 -0.4321 92  SER B N   
1391  C CA  . SER B 86  ? 1.5155 2.3224 1.7691 -0.3232 -0.1705 -0.4252 92  SER B CA  
1392  C C   . SER B 86  ? 1.5274 2.3178 1.8298 -0.3281 -0.1173 -0.4048 92  SER B C   
1393  O O   . SER B 86  ? 1.4739 2.3045 1.8122 -0.2856 -0.1014 -0.3790 92  SER B O   
1394  C CB  . SER B 86  ? 1.5572 2.2992 1.7210 -0.2638 -0.1701 -0.4037 92  SER B CB  
1395  O OG  . SER B 86  ? 1.6184 2.3798 1.8100 -0.2123 -0.1495 -0.3682 92  SER B OG  
1396  N N   . ASP B 87  ? 1.5235 2.2501 1.8212 -0.3781 -0.0901 -0.4171 93  ASP B N   
1397  C CA  . ASP B 87  ? 1.4953 2.1975 1.8252 -0.3877 -0.0391 -0.3989 93  ASP B CA  
1398  C C   . ASP B 87  ? 1.5562 2.1236 1.8033 -0.3840 -0.0066 -0.3911 93  ASP B C   
1399  O O   . ASP B 87  ? 1.5201 2.0554 1.7758 -0.3855 0.0336  -0.3741 93  ASP B O   
1400  C CB  . ASP B 87  ? 1.5412 2.3003 1.9548 -0.4506 -0.0304 -0.4114 93  ASP B CB  
1401  C CG  . ASP B 87  ? 1.6453 2.5558 2.1651 -0.4545 -0.0549 -0.4128 93  ASP B CG  
1402  O OD1 . ASP B 87  ? 1.6031 2.5777 2.1726 -0.4171 -0.0325 -0.3886 93  ASP B OD1 
1403  O OD2 . ASP B 87  ? 1.7510 2.7168 2.3075 -0.4959 -0.0960 -0.4394 93  ASP B OD2 
1404  N N   . ASN B 88  ? 1.5562 2.0495 1.7218 -0.3752 -0.0238 -0.4020 94  ASN B N   
1405  C CA  . ASN B 88  ? 1.5655 1.9380 1.6554 -0.3681 0.0034  -0.3946 94  ASN B CA  
1406  C C   . ASN B 88  ? 1.5541 1.8975 1.6244 -0.3162 0.0248  -0.3623 94  ASN B C   
1407  O O   . ASN B 88  ? 1.5389 1.8755 1.5750 -0.2761 0.0109  -0.3515 94  ASN B O   
1408  C CB  . ASN B 88  ? 1.6278 1.9395 1.6406 -0.3724 -0.0185 -0.4173 94  ASN B CB  
1409  C CG  . ASN B 88  ? 1.9746 2.2958 1.9990 -0.4286 -0.0423 -0.4560 94  ASN B CG  
1410  O OD1 . ASN B 88  ? 1.8620 2.2805 1.9470 -0.4493 -0.0746 -0.4712 94  ASN B OD1 
1411  N ND2 . ASN B 88  ? 1.9445 2.1644 1.9144 -0.4546 -0.0282 -0.4734 94  ASN B ND2 
1412  N N   . GLY B 89  ? 1.4663 1.7921 1.5585 -0.3194 0.0580  -0.3470 95  GLY B N   
1413  C CA  . GLY B 89  ? 1.4101 1.7071 1.4898 -0.2790 0.0759  -0.3222 95  GLY B CA  
1414  C C   . GLY B 89  ? 1.4348 1.6578 1.4891 -0.2884 0.1082  -0.3112 95  GLY B C   
1415  O O   . GLY B 89  ? 1.4428 1.5904 1.4475 -0.2823 0.1140  -0.3057 95  GLY B O   
1416  N N   . THR B 90  ? 1.3683 1.6161 1.4552 -0.2988 0.1308  -0.3053 96  THR B N   
1417  C CA  . THR B 90  ? 1.3686 1.5530 1.4276 -0.3036 0.1609  -0.2914 96  THR B CA  
1418  C C   . THR B 90  ? 1.4568 1.6020 1.5089 -0.3501 0.1773  -0.2976 96  THR B C   
1419  O O   . THR B 90  ? 1.4709 1.6578 1.5655 -0.3820 0.1916  -0.3002 96  THR B O   
1420  C CB  . THR B 90  ? 1.3978 1.6150 1.4758 -0.2834 0.1799  -0.2797 96  THR B CB  
1421  O OG1 . THR B 90  ? 1.3555 1.6367 1.4830 -0.3102 0.1976  -0.2823 96  THR B OG1 
1422  C CG2 . THR B 90  ? 1.3453 1.5920 1.4316 -0.2385 0.1622  -0.2781 96  THR B CG2 
1423  N N   . CYS B 91  ? 1.4264 1.4901 1.4281 -0.3531 0.1771  -0.2989 97  CYS B N   
1424  C CA  . CYS B 91  ? 1.4710 1.4718 1.4540 -0.3919 0.1932  -0.3054 97  CYS B CA  
1425  C C   . CYS B 91  ? 1.5197 1.4922 1.5014 -0.3993 0.2288  -0.2821 97  CYS B C   
1426  O O   . CYS B 91  ? 1.5628 1.5268 1.5645 -0.4397 0.2482  -0.2828 97  CYS B O   
1427  C CB  . CYS B 91  ? 1.4987 1.4161 1.4220 -0.3783 0.1891  -0.3089 97  CYS B CB  
1428  S SG  . CYS B 91  ? 1.5072 1.3830 1.3961 -0.3262 0.1977  -0.2787 97  CYS B SG  
1429  N N   . TYR B 92  ? 1.4294 1.3874 1.3869 -0.3608 0.2363  -0.2608 98  TYR B N   
1430  C CA  . TYR B 92  ? 1.4420 1.3795 1.3863 -0.3585 0.2664  -0.2374 98  TYR B CA  
1431  C C   . TYR B 92  ? 1.4223 1.4472 1.4096 -0.3542 0.2720  -0.2375 98  TYR B C   
1432  O O   . TYR B 92  ? 1.3734 1.4472 1.3766 -0.3267 0.2498  -0.2466 98  TYR B O   
1433  C CB  . TYR B 92  ? 1.4615 1.3480 1.3581 -0.3184 0.2647  -0.2184 98  TYR B CB  
1434  C CG  . TYR B 92  ? 1.5427 1.3929 1.4084 -0.3153 0.2935  -0.1929 98  TYR B CG  
1435  C CD1 . TYR B 92  ? 1.5737 1.4669 1.4404 -0.3017 0.3053  -0.1843 98  TYR B CD1 
1436  C CD2 . TYR B 92  ? 1.6098 1.3801 1.4397 -0.3224 0.3112  -0.1761 98  TYR B CD2 
1437  C CE1 . TYR B 92  ? 1.6584 1.5190 1.4860 -0.2960 0.3335  -0.1585 98  TYR B CE1 
1438  C CE2 . TYR B 92  ? 1.6750 1.4109 1.4712 -0.3165 0.3384  -0.1476 98  TYR B CE2 
1439  C CZ  . TYR B 92  ? 1.8089 1.5917 1.6014 -0.3036 0.3490  -0.1383 98  TYR B CZ  
1440  O OH  . TYR B 92  ? 1.9095 1.6598 1.6579 -0.2935 0.3766  -0.1080 98  TYR B OH  
1441  N N   . PRO B 93  ? 1.3751 1.4213 1.3848 -0.3800 0.3041  -0.2262 99  PRO B N   
1442  C CA  . PRO B 93  ? 1.3415 1.4780 1.3957 -0.3715 0.3152  -0.2252 99  PRO B CA  
1443  C C   . PRO B 93  ? 1.3658 1.5055 1.3828 -0.3202 0.3156  -0.2175 99  PRO B C   
1444  O O   . PRO B 93  ? 1.3782 1.4524 1.3356 -0.3007 0.3201  -0.2037 99  PRO B O   
1445  C CB  . PRO B 93  ? 1.4153 1.5574 1.4930 -0.4100 0.3577  -0.2070 99  PRO B CB  
1446  C CG  . PRO B 93  ? 1.5236 1.5600 1.5416 -0.4181 0.3724  -0.1899 99  PRO B CG  
1447  C CD  . PRO B 93  ? 1.4523 1.4406 1.4501 -0.4158 0.3363  -0.2103 99  PRO B CD  
1448  N N   . GLY B 94  ? 1.2966 1.5109 1.3487 -0.2976 0.3084  -0.2279 100 GLY B N   
1449  C CA  . GLY B 94  ? 1.2985 1.5120 1.3148 -0.2493 0.3074  -0.2275 100 GLY B CA  
1450  C C   . GLY B 94  ? 1.3421 1.6284 1.4000 -0.2211 0.2952  -0.2425 100 GLY B C   
1451  O O   . GLY B 94  ? 1.3161 1.6780 1.4406 -0.2381 0.2965  -0.2478 100 GLY B O   
1452  N N   . ASP B 95  ? 1.3294 1.5923 1.3499 -0.1772 0.2818  -0.2496 101 ASP B N   
1453  C CA  . ASP B 95  ? 1.3269 1.6415 1.3782 -0.1424 0.2712  -0.2634 101 ASP B CA  
1454  C C   . ASP B 95  ? 1.3449 1.6124 1.3767 -0.1167 0.2324  -0.2735 101 ASP B C   
1455  O O   . ASP B 95  ? 1.3648 1.5651 1.3436 -0.1030 0.2222  -0.2740 101 ASP B O   
1456  C CB  . ASP B 95  ? 1.4117 1.7490 1.4414 -0.1098 0.3030  -0.2641 101 ASP B CB  
1457  C CG  . ASP B 95  ? 1.7424 2.1389 1.8022 -0.1325 0.3494  -0.2482 101 ASP B CG  
1458  O OD1 . ASP B 95  ? 1.7627 2.2342 1.9013 -0.1598 0.3533  -0.2457 101 ASP B OD1 
1459  O OD2 . ASP B 95  ? 1.9032 2.2753 1.9093 -0.1216 0.3817  -0.2374 101 ASP B OD2 
1460  N N   . PHE B 96  ? 1.2428 1.5475 1.3203 -0.1117 0.2099  -0.2788 102 PHE B N   
1461  C CA  . PHE B 96  ? 1.2062 1.4707 1.2740 -0.0874 0.1780  -0.2825 102 PHE B CA  
1462  C C   . PHE B 96  ? 1.2781 1.5510 1.3454 -0.0426 0.1795  -0.2933 102 PHE B C   
1463  O O   . PHE B 96  ? 1.2844 1.6252 1.3951 -0.0248 0.1871  -0.2963 102 PHE B O   
1464  C CB  . PHE B 96  ? 1.1871 1.4825 1.2924 -0.0971 0.1555  -0.2795 102 PHE B CB  
1465  C CG  . PHE B 96  ? 1.1812 1.4171 1.2659 -0.0869 0.1301  -0.2733 102 PHE B CG  
1466  C CD1 . PHE B 96  ? 1.2162 1.4202 1.2957 -0.0520 0.1174  -0.2741 102 PHE B CD1 
1467  C CD2 . PHE B 96  ? 1.1821 1.3915 1.2543 -0.1119 0.1217  -0.2658 102 PHE B CD2 
1468  C CE1 . PHE B 96  ? 1.2120 1.3646 1.2831 -0.0466 0.0980  -0.2633 102 PHE B CE1 
1469  C CE2 . PHE B 96  ? 1.2015 1.3634 1.2598 -0.1006 0.1050  -0.2552 102 PHE B CE2 
1470  C CZ  . PHE B 96  ? 1.1791 1.3163 1.2417 -0.0701 0.0938  -0.2518 102 PHE B CZ  
1471  N N   . ILE B 97  ? 1.2447 1.4486 1.2631 -0.0238 0.1718  -0.3006 103 ILE B N   
1472  C CA  . ILE B 97  ? 1.2753 1.4615 1.2755 0.0190  0.1717  -0.3174 103 ILE B CA  
1473  C C   . ILE B 97  ? 1.3241 1.4975 1.3543 0.0422  0.1462  -0.3185 103 ILE B C   
1474  O O   . ILE B 97  ? 1.3010 1.4357 1.3356 0.0282  0.1224  -0.3085 103 ILE B O   
1475  C CB  . ILE B 97  ? 1.3526 1.4656 1.2841 0.0254  0.1664  -0.3285 103 ILE B CB  
1476  C CG1 . ILE B 97  ? 1.3639 1.4796 1.2608 -0.0016 0.1890  -0.3168 103 ILE B CG1 
1477  C CG2 . ILE B 97  ? 1.4230 1.5129 1.3203 0.0700  0.1702  -0.3532 103 ILE B CG2 
1478  C CD1 . ILE B 97  ? 1.4839 1.6623 1.3834 -0.0011 0.2339  -0.3115 103 ILE B CD1 
1479  N N   . ASP B 98  ? 1.3056 1.5118 1.3571 0.0808  0.1550  -0.3274 104 ASP B N   
1480  C CA  . ASP B 98  ? 1.3120 1.5070 1.3924 0.1113  0.1360  -0.3251 104 ASP B CA  
1481  C C   . ASP B 98  ? 1.3058 1.5348 1.4263 0.0898  0.1189  -0.3025 104 ASP B C   
1482  O O   . ASP B 98  ? 1.3009 1.4866 1.4258 0.0980  0.0975  -0.2919 104 ASP B O   
1483  C CB  . ASP B 98  ? 1.3832 1.4758 1.4274 0.1269  0.1141  -0.3376 104 ASP B CB  
1484  C CG  . ASP B 98  ? 1.6173 1.6626 1.6058 0.1490  0.1229  -0.3665 104 ASP B CG  
1485  O OD1 . ASP B 98  ? 1.6602 1.7489 1.6431 0.1779  0.1512  -0.3776 104 ASP B OD1 
1486  O OD2 . ASP B 98  ? 1.7297 1.6963 1.6811 0.1403  0.1007  -0.3786 104 ASP B OD2 
1487  N N   . TYR B 99  ? 1.2252 1.5275 1.3714 0.0608  0.1288  -0.2953 105 TYR B N   
1488  C CA  . TYR B 99  ? 1.1944 1.5289 1.3665 0.0403  0.1107  -0.2800 105 TYR B CA  
1489  C C   . TYR B 99  ? 1.2663 1.6432 1.4758 0.0777  0.0970  -0.2711 105 TYR B C   
1490  O O   . TYR B 99  ? 1.2594 1.6117 1.4654 0.0827  0.0763  -0.2560 105 TYR B O   
1491  C CB  . TYR B 99  ? 1.1883 1.5846 1.3788 -0.0019 0.1212  -0.2804 105 TYR B CB  
1492  C CG  . TYR B 99  ? 1.1923 1.6208 1.4002 -0.0220 0.0989  -0.2721 105 TYR B CG  
1493  C CD1 . TYR B 99  ? 1.2113 1.5811 1.3890 -0.0225 0.0801  -0.2614 105 TYR B CD1 
1494  C CD2 . TYR B 99  ? 1.2003 1.7192 1.4537 -0.0416 0.0967  -0.2757 105 TYR B CD2 
1495  C CE1 . TYR B 99  ? 1.2279 1.6239 1.4071 -0.0344 0.0608  -0.2554 105 TYR B CE1 
1496  C CE2 . TYR B 99  ? 1.2119 1.7571 1.4706 -0.0592 0.0707  -0.2737 105 TYR B CE2 
1497  C CZ  . TYR B 99  ? 1.3333 1.8139 1.5475 -0.0529 0.0537  -0.2643 105 TYR B CZ  
1498  O OH  . TYR B 99  ? 1.3741 1.8770 1.5793 -0.0654 0.0295  -0.2641 105 TYR B OH  
1499  N N   . GLU B 100 ? 1.2494 1.6892 1.4931 0.1085  0.1112  -0.2773 106 GLU B N   
1500  C CA  . GLU B 100 ? 1.2678 1.7544 1.5511 0.1537  0.1006  -0.2673 106 GLU B CA  
1501  C C   . GLU B 100 ? 1.3573 1.7471 1.6113 0.1880  0.0891  -0.2615 106 GLU B C   
1502  O O   . GLU B 100 ? 1.3623 1.7497 1.6274 0.2072  0.0698  -0.2414 106 GLU B O   
1503  C CB  . GLU B 100 ? 1.3065 1.8736 1.6327 0.1860  0.1251  -0.2752 106 GLU B CB  
1504  C CG  . GLU B 100 ? 1.4813 2.0895 1.8118 0.1561  0.1563  -0.2870 106 GLU B CG  
1505  C CD  . GLU B 100 ? 1.8919 2.4147 2.1590 0.1621  0.1785  -0.3035 106 GLU B CD  
1506  O OE1 . GLU B 100 ? 1.7501 2.2726 2.0109 0.2070  0.2008  -0.3146 106 GLU B OE1 
1507  O OE2 . GLU B 100 ? 1.9361 2.3927 2.1567 0.1249  0.1725  -0.3060 106 GLU B OE2 
1508  N N   . GLU B 101 ? 1.3446 1.6505 1.5583 0.1914  0.0991  -0.2784 107 GLU B N   
1509  C CA  . GLU B 101 ? 1.3891 1.5917 1.5780 0.2137  0.0871  -0.2783 107 GLU B CA  
1510  C C   . GLU B 101 ? 1.4203 1.5733 1.5999 0.1843  0.0666  -0.2569 107 GLU B C   
1511  O O   . GLU B 101 ? 1.4529 1.5464 1.6352 0.2046  0.0553  -0.2422 107 GLU B O   
1512  C CB  . GLU B 101 ? 1.4522 1.5846 1.5971 0.2175  0.0973  -0.3077 107 GLU B CB  
1513  C CG  . GLU B 101 ? 1.6688 1.8188 1.8125 0.2668  0.1193  -0.3279 107 GLU B CG  
1514  C CD  . GLU B 101 ? 1.8507 2.1000 2.0099 0.2667  0.1494  -0.3341 107 GLU B CD  
1515  O OE1 . GLU B 101 ? 1.7133 2.0429 1.9202 0.3005  0.1620  -0.3263 107 GLU B OE1 
1516  O OE2 . GLU B 101 ? 1.6964 1.9430 1.8221 0.2361  0.1622  -0.3449 107 GLU B OE2 
1517  N N   . LEU B 102 ? 1.3250 1.5019 1.4955 0.1389  0.0654  -0.2526 108 LEU B N   
1518  C CA  . LEU B 102 ? 1.3024 1.4438 1.4631 0.1134  0.0524  -0.2313 108 LEU B CA  
1519  C C   . LEU B 102 ? 1.3607 1.5460 1.5390 0.1299  0.0417  -0.2060 108 LEU B C   
1520  O O   . LEU B 102 ? 1.3649 1.5050 1.5370 0.1351  0.0338  -0.1815 108 LEU B O   
1521  C CB  . LEU B 102 ? 1.2612 1.4081 1.4011 0.0668  0.0577  -0.2369 108 LEU B CB  
1522  C CG  . LEU B 102 ? 1.2893 1.4054 1.4168 0.0433  0.0504  -0.2157 108 LEU B CG  
1523  C CD1 . LEU B 102 ? 1.3097 1.3465 1.4366 0.0474  0.0436  -0.2036 108 LEU B CD1 
1524  C CD2 . LEU B 102 ? 1.2732 1.3965 1.3806 0.0050  0.0587  -0.2236 108 LEU B CD2 
1525  N N   . ARG B 103 ? 1.3142 1.5913 1.5162 0.1386  0.0410  -0.2102 109 ARG B N   
1526  C CA  . ARG B 103 ? 1.3217 1.6543 1.5380 0.1585  0.0246  -0.1891 109 ARG B CA  
1527  C C   . ARG B 103 ? 1.4582 1.7512 1.6830 0.2096  0.0207  -0.1683 109 ARG B C   
1528  O O   . ARG B 103 ? 1.4796 1.7506 1.6916 0.2228  0.0102  -0.1391 109 ARG B O   
1529  C CB  . ARG B 103 ? 1.2663 1.7126 1.5200 0.1581  0.0212  -0.2010 109 ARG B CB  
1530  C CG  . ARG B 103 ? 1.2602 1.7442 1.5096 0.1044  0.0228  -0.2178 109 ARG B CG  
1531  C CD  . ARG B 103 ? 1.2767 1.8768 1.5790 0.1009  0.0188  -0.2282 109 ARG B CD  
1532  N NE  . ARG B 103 ? 1.2826 1.9444 1.5911 0.0969  -0.0120 -0.2207 109 ARG B NE  
1533  C CZ  . ARG B 103 ? 1.4026 2.0928 1.7035 0.0502  -0.0239 -0.2342 109 ARG B CZ  
1534  N NH1 . ARG B 103 ? 1.0842 1.7455 1.3758 0.0042  -0.0041 -0.2513 109 ARG B NH1 
1535  N NH2 . ARG B 103 ? 1.3582 2.1006 1.6553 0.0508  -0.0569 -0.2313 109 ARG B NH2 
1536  N N   . GLU B 104 ? 1.4632 1.7354 1.7030 0.2392  0.0323  -0.1829 110 GLU B N   
1537  C CA  . GLU B 104 ? 1.5310 1.7480 1.7782 0.2898  0.0319  -0.1683 110 GLU B CA  
1538  C C   . GLU B 104 ? 1.6101 1.7199 1.8354 0.2796  0.0278  -0.1478 110 GLU B C   
1539  O O   . GLU B 104 ? 1.6557 1.7350 1.8855 0.3111  0.0228  -0.1157 110 GLU B O   
1540  C CB  . GLU B 104 ? 1.5874 1.7835 1.8411 0.3179  0.0484  -0.1971 110 GLU B CB  
1541  C CG  . GLU B 104 ? 1.7650 2.0719 2.0549 0.3432  0.0589  -0.2081 110 GLU B CG  
1542  C CD  . GLU B 104 ? 2.1668 2.5319 2.4950 0.4008  0.0522  -0.1849 110 GLU B CD  
1543  O OE1 . GLU B 104 ? 2.2788 2.5693 2.6006 0.4447  0.0516  -0.1708 110 GLU B OE1 
1544  O OE2 . GLU B 104 ? 2.0444 2.5310 2.4133 0.4029  0.0476  -0.1813 110 GLU B OE2 
1545  N N   . GLN B 105 ? 1.5327 1.5919 1.7387 0.2354  0.0306  -0.1620 111 GLN B N   
1546  C CA  . GLN B 105 ? 1.5432 1.5136 1.7423 0.2176  0.0275  -0.1428 111 GLN B CA  
1547  C C   . GLN B 105 ? 1.5655 1.5567 1.7560 0.2035  0.0252  -0.1072 111 GLN B C   
1548  O O   . GLN B 105 ? 1.5894 1.5253 1.7840 0.2113  0.0267  -0.0736 111 GLN B O   
1549  C CB  . GLN B 105 ? 1.5448 1.4662 1.7317 0.1794  0.0278  -0.1703 111 GLN B CB  
1550  C CG  . GLN B 105 ? 1.8160 1.6920 1.9967 0.1971  0.0284  -0.2058 111 GLN B CG  
1551  C CD  . GLN B 105 ? 2.1838 1.9723 2.3776 0.2264  0.0232  -0.1976 111 GLN B CD  
1552  O OE1 . GLN B 105 ? 2.1589 1.8700 2.3619 0.2051  0.0140  -0.1894 111 GLN B OE1 
1553  N NE2 . GLN B 105 ? 2.1398 1.9389 2.3404 0.2758  0.0295  -0.1982 111 GLN B NE2 
1554  N N   . LEU B 106 ? 1.4839 1.5507 1.6604 0.1833  0.0234  -0.1144 112 LEU B N   
1555  C CA  . LEU B 106 ? 1.4818 1.5690 1.6360 0.1727  0.0212  -0.0881 112 LEU B CA  
1556  C C   . LEU B 106 ? 1.5986 1.7340 1.7480 0.2129  0.0106  -0.0619 112 LEU B C   
1557  O O   . LEU B 106 ? 1.6162 1.7625 1.7355 0.2127  0.0081  -0.0375 112 LEU B O   
1558  C CB  . LEU B 106 ? 1.4326 1.5619 1.5666 0.1313  0.0222  -0.1103 112 LEU B CB  
1559  C CG  . LEU B 106 ? 1.4675 1.5422 1.5903 0.0947  0.0329  -0.1121 112 LEU B CG  
1560  C CD1 . LEU B 106 ? 1.4314 1.5387 1.5411 0.0601  0.0360  -0.1419 112 LEU B CD1 
1561  C CD2 . LEU B 106 ? 1.5100 1.5597 1.6123 0.0935  0.0397  -0.0774 112 LEU B CD2 
1562  N N   . SER B 107 ? 1.5943 1.7570 1.7694 0.2522  0.0050  -0.0652 113 SER B N   
1563  C CA  . SER B 107 ? 1.6442 1.8579 1.8201 0.2982  -0.0084 -0.0382 113 SER B CA  
1564  C C   . SER B 107 ? 1.7990 1.9490 1.9506 0.3185  -0.0036 0.0103  113 SER B C   
1565  O O   . SER B 107 ? 1.8091 1.9916 1.9249 0.3225  -0.0114 0.0331  113 SER B O   
1566  C CB  . SER B 107 ? 1.7059 1.9349 1.9190 0.3433  -0.0083 -0.0450 113 SER B CB  
1567  O OG  . SER B 107 ? 1.7694 2.0576 2.0075 0.3275  -0.0053 -0.0857 113 SER B OG  
1568  N N   . SER B 108 ? 1.8287 1.8828 1.9972 0.3272  0.0105  0.0245  114 SER B N   
1569  C CA  . SER B 108 ? 1.8972 1.8759 2.0567 0.3425  0.0221  0.0746  114 SER B CA  
1570  C C   . SER B 108 ? 1.9503 1.8791 2.1028 0.2948  0.0368  0.0819  114 SER B C   
1571  O O   . SER B 108 ? 1.9369 1.7976 2.1189 0.2703  0.0438  0.0695  114 SER B O   
1572  C CB  . SER B 108 ? 1.9933 1.8923 2.1842 0.3754  0.0283  0.0848  114 SER B CB  
1573  O OG  . SER B 108 ? 2.0404 1.8918 2.2552 0.3489  0.0305  0.0415  114 SER B OG  
1574  N N   . VAL B 109 ? 1.9148 1.8811 2.0276 0.2831  0.0400  0.0993  115 VAL B N   
1575  C CA  . VAL B 109 ? 1.9000 1.8312 2.0059 0.2456  0.0582  0.1111  115 VAL B CA  
1576  C C   . VAL B 109 ? 2.0110 1.9430 2.0731 0.2656  0.0731  0.1630  115 VAL B C   
1577  O O   . VAL B 109 ? 2.0098 2.0033 2.0192 0.2795  0.0625  0.1605  115 VAL B O   
1578  C CB  . VAL B 109 ? 1.8773 1.8441 1.9751 0.2013  0.0543  0.0654  115 VAL B CB  
1579  C CG1 . VAL B 109 ? 1.8667 1.8029 1.9579 0.1725  0.0750  0.0837  115 VAL B CG1 
1580  C CG2 . VAL B 109 ? 1.8371 1.7906 1.9718 0.1820  0.0460  0.0218  115 VAL B CG2 
1581  N N   . SER B 110 ? 2.0189 1.8823 2.1028 0.2651  0.0979  0.2092  116 SER B N   
1582  C CA  . SER B 110 ? 2.0781 1.9326 2.1228 0.2851  0.1223  0.2667  116 SER B CA  
1583  C C   . SER B 110 ? 2.1021 1.9661 2.1319 0.2503  0.1417  0.2621  116 SER B C   
1584  O O   . SER B 110 ? 2.0869 2.0036 2.0579 0.2501  0.1341  0.2389  116 SER B O   
1585  C CB  . SER B 110 ? 2.1870 1.9634 2.2721 0.3011  0.1445  0.3238  116 SER B CB  
1586  O OG  . SER B 110 ? 2.3515 2.1205 2.3954 0.3255  0.1736  0.3868  116 SER B OG  
1587  N N   . SER B 111 A 2.0431 1.8569 2.1308 0.2204  0.1644  0.2808  116 SER B N   
1588  C CA  . SER B 111 A 2.0024 1.8231 2.0942 0.1902  0.1864  0.2819  116 SER B CA  
1589  C C   . SER B 111 A 1.9368 1.7829 2.0394 0.1542  0.1650  0.2182  116 SER B C   
1590  O O   . SER B 111 A 1.9013 1.7550 2.0156 0.1498  0.1368  0.1769  116 SER B O   
1591  C CB  . SER B 111 A 2.0793 1.8476 2.2453 0.1721  0.2150  0.3288  116 SER B CB  
1592  O OG  . SER B 111 A 2.1624 1.9448 2.3463 0.1460  0.2372  0.3332  116 SER B OG  
1593  N N   . PHE B 112 B 1.8407 1.6993 1.9369 0.1328  0.1819  0.2137  116 PHE B N   
1594  C CA  . PHE B 112 B 1.7643 1.6416 1.8651 0.1014  0.1670  0.1621  116 PHE B CA  
1595  C C   . PHE B 112 B 1.7563 1.6332 1.8675 0.0847  0.1940  0.1760  116 PHE B C   
1596  O O   . PHE B 112 B 1.7878 1.6778 1.8450 0.1029  0.2184  0.1958  116 PHE B O   
1597  C CB  . PHE B 112 B 1.7799 1.7017 1.8121 0.1095  0.1470  0.1205  116 PHE B CB  
1598  C CG  . PHE B 112 B 1.7469 1.6853 1.7915 0.0830  0.1234  0.0657  116 PHE B CG  
1599  C CD1 . PHE B 112 B 1.7743 1.7103 1.8526 0.0830  0.1017  0.0447  116 PHE B CD1 
1600  C CD2 . PHE B 112 B 1.7522 1.7070 1.7665 0.0625  0.1255  0.0361  116 PHE B CD2 
1601  C CE1 . PHE B 112 B 1.7463 1.7016 1.8288 0.0626  0.0854  -0.0020 116 PHE B CE1 
1602  C CE2 . PHE B 112 B 1.7502 1.7196 1.7724 0.0393  0.1079  -0.0087 116 PHE B CE2 
1603  C CZ  . PHE B 112 B 1.7114 1.6843 1.7672 0.0396  0.0891  -0.0261 116 PHE B CZ  
1604  N N   . GLU B 113 C 1.6300 1.4928 1.8078 0.0538  0.1890  0.1655  116 GLU B N   
1605  C CA  . GLU B 113 C 1.5868 1.4571 1.7876 0.0390  0.2108  0.1767  116 GLU B CA  
1606  C C   . GLU B 113 C 1.5201 1.4004 1.7180 0.0154  0.1890  0.1269  116 GLU B C   
1607  O O   . GLU B 113 C 1.4885 1.3572 1.7270 -0.0040 0.1620  0.1025  116 GLU B O   
1608  C CB  . GLU B 113 C 1.6143 1.4668 1.9098 0.0242  0.2256  0.2205  116 GLU B CB  
1609  C CG  . GLU B 113 C 1.6904 1.5639 2.0199 0.0149  0.2516  0.2400  116 GLU B CG  
1610  C CD  . GLU B 113 C 1.8771 1.7491 2.3209 -0.0132 0.2507  0.2655  116 GLU B CD  
1611  O OE1 . GLU B 113 C 1.8381 1.6813 2.3396 -0.0286 0.2326  0.2733  116 GLU B OE1 
1612  O OE2 . GLU B 113 C 1.6830 1.5826 2.1614 -0.0195 0.2670  0.2772  116 GLU B OE2 
1613  N N   . ARG B 114 ? 1.4220 1.3180 1.5652 0.0194  0.2020  0.1120  117 ARG B N   
1614  C CA  . ARG B 114 ? 1.3574 1.2574 1.4932 -0.0004 0.1891  0.0731  117 ARG B CA  
1615  C C   . ARG B 114 ? 1.3511 1.2517 1.5396 -0.0071 0.2088  0.0995  117 ARG B C   
1616  O O   . ARG B 114 ? 1.3865 1.2921 1.5674 0.0107  0.2431  0.1335  117 ARG B O   
1617  C CB  . ARG B 114 ? 1.3646 1.2727 1.4156 0.0066  0.1929  0.0434  117 ARG B CB  
1618  C CG  . ARG B 114 ? 1.4405 1.3435 1.4786 -0.0121 0.1884  0.0109  117 ARG B CG  
1619  C CD  . ARG B 114 ? 1.6004 1.5028 1.5590 -0.0092 0.1914  -0.0183 117 ARG B CD  
1620  N NE  . ARG B 114 ? 1.6837 1.5658 1.6206 -0.0180 0.2045  -0.0335 117 ARG B NE  
1621  C CZ  . ARG B 114 ? 1.8162 1.6805 1.7285 -0.0012 0.2349  -0.0171 117 ARG B CZ  
1622  N NH1 . ARG B 114 ? 1.6594 1.5285 1.5662 0.0241  0.2581  0.0174  117 ARG B NH1 
1623  N NH2 . ARG B 114 ? 1.5912 1.4302 1.4829 -0.0065 0.2460  -0.0322 117 ARG B NH2 
1624  N N   . PHE B 115 ? 1.2289 1.1282 1.4723 -0.0295 0.1871  0.0865  118 PHE B N   
1625  C CA  . PHE B 115 ? 1.2001 1.1112 1.5077 -0.0366 0.1980  0.1117  118 PHE B CA  
1626  C C   . PHE B 115 ? 1.2033 1.1168 1.5117 -0.0507 0.1773  0.0820  118 PHE B C   
1627  O O   . PHE B 115 ? 1.1912 1.0938 1.4772 -0.0627 0.1479  0.0456  118 PHE B O   
1628  C CB  . PHE B 115 ? 1.2236 1.1355 1.6265 -0.0499 0.1908  0.1442  118 PHE B CB  
1629  C CG  . PHE B 115 ? 1.2247 1.1178 1.6626 -0.0730 0.1466  0.1157  118 PHE B CG  
1630  C CD1 . PHE B 115 ? 1.2709 1.1381 1.6824 -0.0690 0.1323  0.0999  118 PHE B CD1 
1631  C CD2 . PHE B 115 ? 1.2355 1.1361 1.7315 -0.0949 0.1189  0.1054  118 PHE B CD2 
1632  C CE1 . PHE B 115 ? 1.2835 1.1255 1.7199 -0.0852 0.0949  0.0707  118 PHE B CE1 
1633  C CE2 . PHE B 115 ? 1.2751 1.1513 1.7903 -0.1135 0.0768  0.0741  118 PHE B CE2 
1634  C CZ  . PHE B 115 ? 1.2653 1.1088 1.7487 -0.1079 0.0672  0.0559  118 PHE B CZ  
1635  N N   . GLU B 116 ? 1.1439 1.0728 1.4786 -0.0455 0.1947  0.1011  119 GLU B N   
1636  C CA  . GLU B 116 ? 1.1241 1.0556 1.4616 -0.0537 0.1762  0.0816  119 GLU B CA  
1637  C C   . GLU B 116 ? 1.1549 1.0968 1.5678 -0.0762 0.1362  0.0794  119 GLU B C   
1638  O O   . GLU B 116 ? 1.1571 1.1255 1.6553 -0.0816 0.1355  0.1107  119 GLU B O   
1639  C CB  . GLU B 116 ? 1.1549 1.0998 1.5000 -0.0345 0.2081  0.1062  119 GLU B CB  
1640  C CG  . GLU B 116 ? 1.3119 1.2307 1.5782 -0.0260 0.2154  0.0786  119 GLU B CG  
1641  C CD  . GLU B 116 ? 1.6734 1.5916 1.9334 -0.0002 0.2511  0.0996  119 GLU B CD  
1642  O OE1 . GLU B 116 ? 1.5845 1.5170 1.8637 0.0202  0.2864  0.1318  119 GLU B OE1 
1643  O OE2 . GLU B 116 ? 1.6821 1.5810 1.9109 0.0031  0.2476  0.0847  119 GLU B OE2 
1644  N N   . ILE B 117 ? 1.1009 1.0226 1.4838 -0.0891 0.1033  0.0419  120 ILE B N   
1645  C CA  . ILE B 117 ? 1.1040 1.0223 1.5358 -0.1090 0.0604  0.0275  120 ILE B CA  
1646  C C   . ILE B 117 ? 1.1824 1.1218 1.6418 -0.1134 0.0399  0.0280  120 ILE B C   
1647  O O   . ILE B 117 ? 1.1876 1.1472 1.7287 -0.1276 0.0158  0.0423  120 ILE B O   
1648  C CB  . ILE B 117 ? 1.1440 1.0327 1.5228 -0.1131 0.0373  -0.0144 120 ILE B CB  
1649  C CG1 . ILE B 117 ? 1.1691 1.0428 1.5880 -0.1306 -0.0076 -0.0344 120 ILE B CG1 
1650  C CG2 . ILE B 117 ? 1.1373 1.0212 1.4310 -0.1053 0.0438  -0.0436 120 ILE B CG2 
1651  C CD1 . ILE B 117 ? 1.2601 1.0999 1.6425 -0.1293 -0.0240 -0.0682 120 ILE B CD1 
1652  N N   . PHE B 118 ? 1.1554 1.0909 1.5501 -0.1013 0.0498  0.0152  121 PHE B N   
1653  C CA  . PHE B 118 ? 1.1644 1.1162 1.5670 -0.0968 0.0357  0.0193  121 PHE B CA  
1654  C C   . PHE B 118 ? 1.2217 1.1717 1.5880 -0.0747 0.0790  0.0374  121 PHE B C   
1655  O O   . PHE B 118 ? 1.2280 1.1493 1.5153 -0.0692 0.0908  0.0166  121 PHE B O   
1656  C CB  . PHE B 118 ? 1.2044 1.1360 1.5465 -0.1017 0.0038  -0.0180 121 PHE B CB  
1657  C CG  . PHE B 118 ? 1.2396 1.1579 1.5902 -0.1180 -0.0367 -0.0469 121 PHE B CG  
1658  C CD1 . PHE B 118 ? 1.2946 1.2292 1.7147 -0.1320 -0.0781 -0.0447 121 PHE B CD1 
1659  C CD2 . PHE B 118 ? 1.2736 1.1631 1.5614 -0.1184 -0.0353 -0.0790 121 PHE B CD2 
1660  C CE1 . PHE B 118 ? 1.3344 1.2438 1.7525 -0.1463 -0.1173 -0.0779 121 PHE B CE1 
1661  C CE2 . PHE B 118 ? 1.3330 1.2024 1.6207 -0.1272 -0.0698 -0.1084 121 PHE B CE2 
1662  C CZ  . PHE B 118 ? 1.3295 1.2028 1.6769 -0.1411 -0.1108 -0.1098 121 PHE B CZ  
1663  N N   . PRO B 119 ? 1.1816 1.1586 1.6052 -0.0618 0.1063  0.0759  122 PRO B N   
1664  C CA  . PRO B 119 ? 1.1965 1.1623 1.5786 -0.0355 0.1512  0.0904  122 PRO B CA  
1665  C C   . PRO B 119 ? 1.2531 1.2033 1.5938 -0.0220 0.1496  0.0841  122 PRO B C   
1666  O O   . PRO B 119 ? 1.2446 1.2216 1.6293 -0.0212 0.1209  0.0937  122 PRO B O   
1667  C CB  . PRO B 119 ? 1.2217 1.2292 1.6884 -0.0220 0.1773  0.1362  122 PRO B CB  
1668  C CG  . PRO B 119 ? 1.2637 1.3121 1.8304 -0.0450 0.1368  0.1473  122 PRO B CG  
1669  C CD  . PRO B 119 ? 1.1978 1.2147 1.7274 -0.0701 0.1017  0.1088  122 PRO B CD  
1670  N N   . LYS B 120 ? 1.2271 1.1319 1.4831 -0.0111 0.1797  0.0690  123 LYS B N   
1671  C CA  . LYS B 120 ? 1.2551 1.1263 1.4579 0.0017  0.1874  0.0636  123 LYS B CA  
1672  C C   . LYS B 120 ? 1.3182 1.2146 1.5726 0.0299  0.1940  0.0996  123 LYS B C   
1673  O O   . LYS B 120 ? 1.3247 1.2133 1.5643 0.0379  0.1780  0.1020  123 LYS B O   
1674  C CB  . LYS B 120 ? 1.3178 1.1327 1.4350 0.0056  0.2233  0.0436  123 LYS B CB  
1675  C CG  . LYS B 120 ? 1.4252 1.1927 1.4727 -0.0040 0.2204  0.0203  123 LYS B CG  
1676  C CD  . LYS B 120 ? 1.5347 1.2548 1.5468 0.0213  0.2519  0.0330  123 LYS B CD  
1677  C CE  . LYS B 120 ? 1.5352 1.2013 1.4859 0.0247  0.2884  0.0151  123 LYS B CE  
1678  N NZ  . LYS B 120 ? 1.5919 1.2063 1.5150 0.0562  0.3221  0.0295  123 LYS B NZ  
1679  N N   . THR B 121 ? 1.2851 1.2167 1.6024 0.0475  0.2186  0.1311  124 THR B N   
1680  C CA  . THR B 121 ? 1.3023 1.2738 1.6874 0.0780  0.2294  0.1707  124 THR B CA  
1681  C C   . THR B 121 ? 1.3422 1.3683 1.8010 0.0675  0.1761  0.1813  124 THR B C   
1682  O O   . THR B 121 ? 1.3675 1.3821 1.7990 0.0807  0.1594  0.1813  124 THR B O   
1683  C CB  . THR B 121 ? 1.3455 1.3539 1.7916 0.0965  0.2697  0.2044  124 THR B CB  
1684  O OG1 . THR B 121 ? 1.2621 1.3095 1.7708 0.0669  0.2495  0.2081  124 THR B OG1 
1685  C CG2 . THR B 121 ? 1.3545 1.3056 1.7139 0.1180  0.3230  0.1946  124 THR B CG2 
1686  N N   . SER B 122 ? 1.2581 1.3374 1.8037 0.0429  0.1473  0.1885  125 SER B N   
1687  C CA  . SER B 122 ? 1.2429 1.3778 1.8683 0.0276  0.0906  0.1946  125 SER B CA  
1688  C C   . SER B 122 ? 1.3083 1.4139 1.8737 0.0035  0.0390  0.1535  125 SER B C   
1689  O O   . SER B 122 ? 1.3452 1.4481 1.8778 0.0170  0.0155  0.1511  125 SER B O   
1690  C CB  . SER B 122 ? 1.2459 1.4401 1.9905 0.0063  0.0820  0.2170  125 SER B CB  
1691  O OG  . SER B 122 ? 1.2967 1.4553 2.0119 -0.0193 0.0883  0.1955  125 SER B OG  
1692  N N   . SER B 123 ? 1.2316 1.3156 1.7811 -0.0274 0.0240  0.1242  126 SER B N   
1693  C CA  . SER B 123 ? 1.2306 1.2884 1.7309 -0.0502 -0.0206 0.0831  126 SER B CA  
1694  C C   . SER B 123 ? 1.3223 1.3578 1.7431 -0.0381 -0.0427 0.0663  126 SER B C   
1695  O O   . SER B 123 ? 1.3389 1.3845 1.7594 -0.0496 -0.0941 0.0468  126 SER B O   
1696  C CB  . SER B 123 ? 1.2460 1.2581 1.6877 -0.0646 -0.0004 0.0556  126 SER B CB  
1697  O OG  . SER B 123 ? 1.3140 1.3444 1.8283 -0.0792 0.0056  0.0689  126 SER B OG  
1698  N N   . TRP B 124 ? 1.2962 1.2955 1.6445 -0.0158 -0.0046 0.0724  127 TRP B N   
1699  C CA  . TRP B 124 ? 1.3335 1.3043 1.6011 -0.0035 -0.0171 0.0630  127 TRP B CA  
1700  C C   . TRP B 124 ? 1.4410 1.4234 1.7197 0.0313  -0.0049 0.1001  127 TRP B C   
1701  O O   . TRP B 124 ? 1.4606 1.4002 1.6934 0.0493  0.0420  0.1108  127 TRP B O   
1702  C CB  . TRP B 124 ? 1.3161 1.2264 1.4867 -0.0121 0.0141  0.0362  127 TRP B CB  
1703  C CG  . TRP B 124 ? 1.2897 1.1953 1.4650 -0.0379 0.0147  0.0087  127 TRP B CG  
1704  C CD1 . TRP B 124 ? 1.3010 1.1943 1.4798 -0.0437 0.0506  0.0075  127 TRP B CD1 
1705  C CD2 . TRP B 124 ? 1.2826 1.1974 1.4651 -0.0569 -0.0250 -0.0189 127 TRP B CD2 
1706  N NE1 . TRP B 124 ? 1.2700 1.1664 1.4580 -0.0637 0.0366  -0.0155 127 TRP B NE1 
1707  C CE2 . TRP B 124 ? 1.2995 1.2055 1.4916 -0.0719 -0.0080 -0.0327 127 TRP B CE2 
1708  C CE3 . TRP B 124 ? 1.3267 1.2512 1.5000 -0.0598 -0.0743 -0.0355 127 TRP B CE3 
1709  C CZ2 . TRP B 124 ? 1.2848 1.1877 1.4819 -0.0880 -0.0348 -0.0603 127 TRP B CZ2 
1710  C CZ3 . TRP B 124 ? 1.3429 1.2603 1.5157 -0.0776 -0.1014 -0.0681 127 TRP B CZ3 
1711  C CH2 . TRP B 124 ? 1.3165 1.2215 1.5039 -0.0908 -0.0800 -0.0790 127 TRP B CH2 
1712  N N   . PRO B 125 ? 1.4176 1.4575 1.7608 0.0422  -0.0481 0.1200  128 PRO B N   
1713  C CA  . PRO B 125 ? 1.4447 1.5048 1.8101 0.0817  -0.0370 0.1605  128 PRO B CA  
1714  C C   . PRO B 125 ? 1.5525 1.5860 1.8371 0.1058  -0.0543 0.1658  128 PRO B C   
1715  O O   . PRO B 125 ? 1.5813 1.5983 1.8508 0.1422  -0.0259 0.1973  128 PRO B O   
1716  C CB  . PRO B 125 ? 1.4475 1.5985 1.9440 0.0797  -0.0747 0.1834  128 PRO B CB  
1717  C CG  . PRO B 125 ? 1.4916 1.6575 2.0064 0.0383  -0.1275 0.1475  128 PRO B CG  
1718  C CD  . PRO B 125 ? 1.4328 1.5243 1.8408 0.0194  -0.1105 0.1068  128 PRO B CD  
1719  N N   . ASN B 126 ? 1.5380 1.5646 1.7680 0.0901  -0.0987 0.1376  129 ASN B N   
1720  C CA  . ASN B 126 ? 1.6101 1.6105 1.7514 0.1144  -0.1144 0.1446  129 ASN B CA  
1721  C C   . ASN B 126 ? 1.6787 1.5970 1.7058 0.1066  -0.0721 0.1259  129 ASN B C   
1722  O O   . ASN B 126 ? 1.7325 1.6247 1.6737 0.1161  -0.0851 0.1224  129 ASN B O   
1723  C CB  . ASN B 126 ? 1.6646 1.7115 1.8096 0.1092  -0.1898 0.1287  129 ASN B CB  
1724  C CG  . ASN B 126 ? 2.0734 2.2075 2.3345 0.1193  -0.2360 0.1535  129 ASN B CG  
1725  O OD1 . ASN B 126 ? 2.0699 2.2314 2.3762 0.1534  -0.2191 0.1967  129 ASN B OD1 
1726  N ND2 . ASN B 126 ? 1.9629 2.1425 2.2787 0.0900  -0.2958 0.1264  129 ASN B ND2 
1727  N N   . HIS B 127 ? 1.5934 1.4746 1.6213 0.0898  -0.0207 0.1160  130 HIS B N   
1728  C CA  . HIS B 127 ? 1.6020 1.4150 1.5447 0.0748  0.0210  0.0971  130 HIS B CA  
1729  C C   . HIS B 127 ? 1.6258 1.3932 1.5685 0.0770  0.0792  0.1060  130 HIS B C   
1730  O O   . HIS B 127 ? 1.5911 1.3824 1.6004 0.0847  0.0907  0.1178  130 HIS B O   
1731  C CB  . HIS B 127 ? 1.5774 1.3966 1.5087 0.0397  0.0063  0.0547  130 HIS B CB  
1732  C CG  . HIS B 127 ? 1.6471 1.4975 1.5654 0.0384  -0.0499 0.0381  130 HIS B CG  
1733  N ND1 . HIS B 127 ? 1.6428 1.5456 1.6380 0.0280  -0.0966 0.0278  130 HIS B ND1 
1734  C CD2 . HIS B 127 ? 1.7327 1.5654 1.5673 0.0486  -0.0654 0.0320  130 HIS B CD2 
1735  C CE1 . HIS B 127 ? 1.6828 1.5938 1.6349 0.0303  -0.1431 0.0090  130 HIS B CE1 
1736  N NE2 . HIS B 127 ? 1.7424 1.6136 1.5929 0.0454  -0.1252 0.0113  130 HIS B NE2 
1737  N N   . ASP B 128 ? 1.6034 1.3036 1.4695 0.0699  0.1162  0.1001  131 ASP B N   
1738  C CA  . ASP B 128 ? 1.6097 1.2518 1.4588 0.0669  0.1677  0.0997  131 ASP B CA  
1739  C C   . ASP B 128 ? 1.5860 1.2298 1.4378 0.0294  0.1772  0.0619  131 ASP B C   
1740  O O   . ASP B 128 ? 1.5703 1.2071 1.3841 0.0043  0.1743  0.0393  131 ASP B O   
1741  C CB  . ASP B 128 ? 1.7205 1.2865 1.4930 0.0746  0.1994  0.1144  131 ASP B CB  
1742  C CG  . ASP B 128 ? 1.9299 1.4204 1.6798 0.0735  0.2498  0.1138  131 ASP B CG  
1743  O OD1 . ASP B 128 ? 1.9121 1.3984 1.6735 0.0483  0.2638  0.0845  131 ASP B OD1 
1744  O OD2 . ASP B 128 ? 2.1030 1.5319 1.8157 0.0974  0.2745  0.1408  131 ASP B OD2 
1745  N N   . SER B 129 ? 1.3087 1.5708 1.5845 -0.1627 0.0518  -0.0874 132 SER B N   
1746  C CA  . SER B 129 ? 1.3099 1.5443 1.5556 -0.1819 0.0738  -0.0745 132 SER B CA  
1747  C C   . SER B 129 ? 1.3896 1.5960 1.5926 -0.1777 0.0884  -0.0620 132 SER B C   
1748  O O   . SER B 129 ? 1.3905 1.5683 1.5531 -0.1868 0.0945  -0.0493 132 SER B O   
1749  C CB  . SER B 129 ? 1.3451 1.5956 1.6303 -0.2027 0.0964  -0.0821 132 SER B CB  
1750  O OG  . SER B 129 ? 1.4162 1.7073 1.7600 -0.1990 0.1043  -0.0966 132 SER B OG  
1751  N N   . ASP B 130 ? 1.3605 1.5742 1.5712 -0.1627 0.0922  -0.0664 133 ASP B N   
1752  C CA  . ASP B 130 ? 1.3741 1.5565 1.5419 -0.1588 0.1066  -0.0571 133 ASP B CA  
1753  C C   . ASP B 130 ? 1.4100 1.5600 1.5226 -0.1527 0.0920  -0.0473 133 ASP B C   
1754  O O   . ASP B 130 ? 1.4256 1.5447 1.4960 -0.1595 0.1022  -0.0380 133 ASP B O   
1755  C CB  . ASP B 130 ? 1.4186 1.6158 1.6115 -0.1428 0.1193  -0.0657 133 ASP B CB  
1756  C CG  . ASP B 130 ? 1.6134 1.8520 1.8738 -0.1493 0.1366  -0.0780 133 ASP B CG  
1757  O OD1 . ASP B 130 ? 1.6328 1.8595 1.8914 -0.1693 0.1615  -0.0746 133 ASP B OD1 
1758  O OD2 . ASP B 130 ? 1.7200 2.0015 2.0340 -0.1340 0.1259  -0.0916 133 ASP B OD2 
1759  N N   . LYS B 131 A 1.3384 1.4910 1.4477 -0.1413 0.0693  -0.0500 133 LYS B N   
1760  C CA  . LYS B 131 A 1.3358 1.4547 1.3932 -0.1380 0.0608  -0.0416 133 LYS B CA  
1761  C C   . LYS B 131 A 1.3599 1.4715 1.4013 -0.1539 0.0577  -0.0318 133 LYS B C   
1762  O O   . LYS B 131 A 1.3605 1.4493 1.3660 -0.1561 0.0551  -0.0248 133 LYS B O   
1763  C CB  . LYS B 131 A 1.3756 1.4859 1.4214 -0.1148 0.0428  -0.0483 133 LYS B CB  
1764  C CG  . LYS B 131 A 1.5715 1.6437 1.5691 -0.1022 0.0481  -0.0458 133 LYS B CG  
1765  C CD  . LYS B 131 A 1.6494 1.6817 1.5922 -0.1173 0.0534  -0.0346 133 LYS B CD  
1766  C CE  . LYS B 131 A 1.6546 1.6477 1.5506 -0.1174 0.0664  -0.0315 133 LYS B CE  
1767  N NZ  . LYS B 131 A 1.6226 1.5941 1.4857 -0.1433 0.0731  -0.0221 133 LYS B NZ  
1768  N N   . GLY B 132 ? 1.2959 1.4252 1.3631 -0.1650 0.0611  -0.0314 134 GLY B N   
1769  C CA  . GLY B 132 ? 1.2793 1.4035 1.3338 -0.1754 0.0594  -0.0219 134 GLY B CA  
1770  C C   . GLY B 132 ? 1.3100 1.4213 1.3386 -0.1871 0.0677  -0.0111 134 GLY B C   
1771  O O   . GLY B 132 ? 1.3023 1.4151 1.3317 -0.1949 0.0719  -0.0057 134 GLY B O   
1772  N N   . VAL B 133 ? 1.2477 1.3420 1.2482 -0.1881 0.0686  -0.0085 135 VAL B N   
1773  C CA  . VAL B 133 ? 1.2352 1.3162 1.2083 -0.2009 0.0714  -0.0004 135 VAL B CA  
1774  C C   . VAL B 133 ? 1.2984 1.3710 1.2501 -0.2061 0.0650  0.0034  135 VAL B C   
1775  O O   . VAL B 133 ? 1.3097 1.3690 1.2500 -0.1987 0.0643  -0.0006 135 VAL B O   
1776  C CB  . VAL B 133 ? 1.2835 1.3442 1.2372 -0.2046 0.0832  -0.0017 135 VAL B CB  
1777  C CG1 . VAL B 133 ? 1.2785 1.3422 1.2456 -0.2070 0.0943  -0.0020 135 VAL B CG1 
1778  C CG2 . VAL B 133 ? 1.2897 1.3389 1.2388 -0.1926 0.0889  -0.0092 135 VAL B CG2 
1779  N N   . THR B 134 ? 1.2503 1.3296 1.1961 -0.2186 0.0607  0.0105  136 THR B N   
1780  C CA  . THR B 134 ? 1.2532 1.3326 1.1888 -0.2288 0.0571  0.0132  136 THR B CA  
1781  C C   . THR B 134 ? 1.3186 1.3950 1.2369 -0.2469 0.0518  0.0162  136 THR B C   
1782  O O   . THR B 134 ? 1.3166 1.3920 1.2295 -0.2482 0.0482  0.0184  136 THR B O   
1783  C CB  . THR B 134 ? 1.3389 1.4422 1.2995 -0.2237 0.0546  0.0171  136 THR B CB  
1784  O OG1 . THR B 134 ? 1.3573 1.4552 1.3094 -0.2310 0.0584  0.0174  136 THR B OG1 
1785  C CG2 . THR B 134 ? 1.3062 1.4359 1.2858 -0.2247 0.0485  0.0240  136 THR B CG2 
1786  N N   . ALA B 135 ? 1.2989 1.3699 1.2049 -0.2619 0.0513  0.0155  137 ALA B N   
1787  C CA  . ALA B 135 ? 1.3269 1.3974 1.2186 -0.2835 0.0426  0.0159  137 ALA B CA  
1788  C C   . ALA B 135 ? 1.3873 1.5032 1.3139 -0.2876 0.0289  0.0209  137 ALA B C   
1789  O O   . ALA B 135 ? 1.4031 1.5239 1.3213 -0.3003 0.0147  0.0211  137 ALA B O   
1790  C CB  . ALA B 135 ? 1.3658 1.4140 1.2347 -0.3013 0.0493  0.0117  137 ALA B CB  
1791  N N   . ALA B 136 ? 1.3407 1.4867 1.3028 -0.2744 0.0318  0.0248  138 ALA B N   
1792  C CA  . ALA B 136 ? 1.3373 1.5276 1.3346 -0.2706 0.0210  0.0304  138 ALA B CA  
1793  C C   . ALA B 136 ? 1.4231 1.6097 1.4096 -0.2595 0.0096  0.0341  138 ALA B C   
1794  O O   . ALA B 136 ? 1.4312 1.6458 1.4329 -0.2561 -0.0053 0.0382  138 ALA B O   
1795  C CB  . ALA B 136 ? 1.3217 1.5296 1.3464 -0.2549 0.0316  0.0340  138 ALA B CB  
1796  N N   . CYS B 137 ? 1.4004 1.5508 1.3596 -0.2527 0.0177  0.0321  139 CYS B N   
1797  C CA  . CYS B 137 ? 1.4228 1.5556 1.3620 -0.2439 0.0146  0.0348  139 CYS B CA  
1798  C C   . CYS B 137 ? 1.5046 1.5961 1.4006 -0.2539 0.0168  0.0309  139 CYS B C   
1799  O O   . CYS B 137 ? 1.4991 1.5643 1.3826 -0.2488 0.0328  0.0277  139 CYS B O   
1800  C CB  . CYS B 137 ? 1.4188 1.5453 1.3679 -0.2282 0.0281  0.0354  139 CYS B CB  
1801  S SG  . CYS B 137 ? 1.4961 1.6095 1.4289 -0.2149 0.0260  0.0416  139 CYS B SG  
1802  N N   . PRO B 138 ? 1.4949 1.5800 1.3682 -0.2685 0.0013  0.0300  140 PRO B N   
1803  C CA  . PRO B 138 ? 1.5322 1.5675 1.3544 -0.2775 0.0057  0.0264  140 PRO B CA  
1804  C C   . PRO B 138 ? 1.5995 1.5992 1.3816 -0.2695 0.0042  0.0294  140 PRO B C   
1805  O O   . PRO B 138 ? 1.6012 1.6143 1.3894 -0.2586 -0.0065 0.0345  140 PRO B O   
1806  C CB  . PRO B 138 ? 1.5805 1.6195 1.3922 -0.3003 -0.0105 0.0226  140 PRO B CB  
1807  C CG  . PRO B 138 ? 1.6151 1.7137 1.4767 -0.3020 -0.0279 0.0251  140 PRO B CG  
1808  C CD  . PRO B 138 ? 1.5213 1.6441 1.4150 -0.2784 -0.0209 0.0312  140 PRO B CD  
1809  N N   . HIS B 139 ? 1.5623 1.5100 1.2972 -0.2730 0.0177  0.0266  141 HIS B N   
1810  C CA  . HIS B 139 ? 1.5905 1.4867 1.2722 -0.2674 0.0237  0.0287  141 HIS B CA  
1811  C C   . HIS B 139 ? 1.6376 1.4800 1.2671 -0.2765 0.0353  0.0245  141 HIS B C   
1812  O O   . HIS B 139 ? 1.6070 1.4401 1.2445 -0.2722 0.0599  0.0213  141 HIS B O   
1813  C CB  . HIS B 139 ? 1.5844 1.4769 1.2817 -0.2518 0.0477  0.0307  141 HIS B CB  
1814  C CG  . HIS B 139 ? 1.6888 1.5197 1.3307 -0.2478 0.0669  0.0316  141 HIS B CG  
1815  N ND1 . HIS B 139 ? 1.7381 1.5352 1.3612 -0.2491 0.0938  0.0273  141 HIS B ND1 
1816  C CD2 . HIS B 139 ? 1.7626 1.5570 1.3622 -0.2404 0.0657  0.0363  141 HIS B CD2 
1817  C CE1 . HIS B 139 ? 1.7916 1.5332 1.3636 -0.2450 0.1108  0.0295  141 HIS B CE1 
1818  N NE2 . HIS B 139 ? 1.8148 1.5487 1.3665 -0.2401 0.0944  0.0349  141 HIS B NE2 
1819  N N   . ALA B 140 ? 1.6375 1.4440 1.2121 -0.2879 0.0157  0.0241  142 ALA B N   
1820  C CA  . ALA B 140 ? 1.6927 1.4361 1.2015 -0.2985 0.0226  0.0203  142 ALA B CA  
1821  C C   . ALA B 140 ? 1.7122 1.4644 1.2350 -0.3103 0.0286  0.0151  142 ALA B C   
1822  O O   . ALA B 140 ? 1.7419 1.4453 1.2245 -0.3093 0.0501  0.0126  142 ALA B O   
1823  C CB  . ALA B 140 ? 1.7414 1.4261 1.2073 -0.2848 0.0562  0.0218  142 ALA B CB  
1824  N N   . GLY B 141 ? 1.6200 1.4297 1.1955 -0.3198 0.0121  0.0138  143 GLY B N   
1825  C CA  . GLY B 141 ? 1.6081 1.4239 1.1944 -0.3318 0.0181  0.0091  143 GLY B CA  
1826  C C   . GLY B 141 ? 1.5960 1.4377 1.2275 -0.3141 0.0402  0.0095  143 GLY B C   
1827  O O   . GLY B 141 ? 1.5725 1.4386 1.2310 -0.3201 0.0397  0.0073  143 GLY B O   
1828  N N   . ALA B 142 ? 1.5231 1.3573 1.1612 -0.2930 0.0596  0.0114  144 ALA B N   
1829  C CA  . ALA B 142 ? 1.4685 1.3272 1.1499 -0.2743 0.0777  0.0100  144 ALA B CA  
1830  C C   . ALA B 142 ? 1.4319 1.3495 1.1744 -0.2700 0.0676  0.0119  144 ALA B C   
1831  O O   . ALA B 142 ? 1.4149 1.3562 1.1723 -0.2732 0.0533  0.0161  144 ALA B O   
1832  C CB  . ALA B 142 ? 1.4874 1.3278 1.1652 -0.2585 0.1001  0.0101  144 ALA B CB  
1833  N N   . LYS B 143 ? 1.3457 1.2816 1.1178 -0.2598 0.0748  0.0089  145 LYS B N   
1834  C CA  . LYS B 143 ? 1.2995 1.2813 1.1220 -0.2532 0.0685  0.0103  145 LYS B CA  
1835  C C   . LYS B 143 ? 1.3333 1.3282 1.1803 -0.2408 0.0760  0.0112  145 LYS B C   
1836  O O   . LYS B 143 ? 1.3328 1.3190 1.1856 -0.2299 0.0913  0.0067  145 LYS B O   
1837  C CB  . LYS B 143 ? 1.3274 1.3110 1.1608 -0.2430 0.0740  0.0059  145 LYS B CB  
1838  C CG  . LYS B 143 ? 1.5129 1.4893 1.3310 -0.2562 0.0691  0.0057  145 LYS B CG  
1839  C CD  . LYS B 143 ? 1.6127 1.5735 1.4243 -0.2415 0.0763  0.0014  145 LYS B CD  
1840  C CE  . LYS B 143 ? 1.6319 1.6189 1.4743 -0.2340 0.0725  0.0022  145 LYS B CE  
1841  N NZ  . LYS B 143 ? 1.7109 1.6951 1.5441 -0.2517 0.0731  0.0042  145 LYS B NZ  
1842  N N   . SER B 144 ? 1.2744 1.2872 1.1328 -0.2429 0.0667  0.0164  146 SER B N   
1843  C CA  . SER B 144 ? 1.2624 1.2777 1.1344 -0.2344 0.0760  0.0174  146 SER B CA  
1844  C C   . SER B 144 ? 1.2658 1.3160 1.1769 -0.2275 0.0699  0.0192  146 SER B C   
1845  O O   . SER B 144 ? 1.2490 1.3195 1.1795 -0.2261 0.0633  0.0182  146 SER B O   
1846  C CB  . SER B 144 ? 1.3542 1.3422 1.1882 -0.2385 0.0731  0.0225  146 SER B CB  
1847  O OG  . SER B 144 ? 1.4840 1.4565 1.3164 -0.2323 0.0902  0.0225  146 SER B OG  
1848  N N   . PHE B 145 ? 1.2021 1.2503 1.1168 -0.2230 0.0747  0.0218  147 PHE B N   
1849  C CA  . PHE B 145 ? 1.1638 1.2331 1.1047 -0.2158 0.0717  0.0238  147 PHE B CA  
1850  C C   . PHE B 145 ? 1.2012 1.2495 1.1219 -0.2126 0.0774  0.0284  147 PHE B C   
1851  O O   . PHE B 145 ? 1.2174 1.2344 1.1034 -0.2159 0.0834  0.0298  147 PHE B O   
1852  C CB  . PHE B 145 ? 1.1644 1.2462 1.1373 -0.2119 0.0796  0.0153  147 PHE B CB  
1853  C CG  . PHE B 145 ? 1.1634 1.2627 1.1571 -0.2053 0.0731  0.0163  147 PHE B CG  
1854  C CD1 . PHE B 145 ? 1.1912 1.3055 1.1883 -0.2020 0.0619  0.0209  147 PHE B CD1 
1855  C CD2 . PHE B 145 ? 1.1895 1.2860 1.1966 -0.2040 0.0805  0.0122  147 PHE B CD2 
1856  C CE1 . PHE B 145 ? 1.1943 1.3169 1.2033 -0.1940 0.0593  0.0226  147 PHE B CE1 
1857  C CE2 . PHE B 145 ? 1.2170 1.3199 1.2332 -0.1977 0.0747  0.0132  147 PHE B CE2 
1858  C CZ  . PHE B 145 ? 1.1841 1.2984 1.1991 -0.1911 0.0646  0.0190  147 PHE B CZ  
1859  N N   . TYR B 146 ? 1.1421 1.1983 1.0747 -0.2052 0.0767  0.0312  148 TYR B N   
1860  C CA  . TYR B 146 ? 1.1654 1.1925 1.0710 -0.2003 0.0843  0.0357  148 TYR B CA  
1861  C C   . TYR B 146 ? 1.2461 1.2470 1.1492 -0.2092 0.1092  0.0280  148 TYR B C   
1862  O O   . TYR B 146 ? 1.2153 1.2346 1.1550 -0.2143 0.1166  0.0191  148 TYR B O   
1863  C CB  . TYR B 146 ? 1.1521 1.1889 1.0674 -0.1893 0.0798  0.0402  148 TYR B CB  
1864  C CG  . TYR B 146 ? 1.1199 1.1903 1.0505 -0.1799 0.0610  0.0467  148 TYR B CG  
1865  C CD1 . TYR B 146 ? 1.1568 1.2298 1.0693 -0.1689 0.0471  0.0555  148 TYR B CD1 
1866  C CD2 . TYR B 146 ? 1.0888 1.1873 1.0518 -0.1803 0.0581  0.0438  148 TYR B CD2 
1867  C CE1 . TYR B 146 ? 1.1326 1.2452 1.0704 -0.1606 0.0326  0.0605  148 TYR B CE1 
1868  C CE2 . TYR B 146 ? 1.0828 1.2106 1.0617 -0.1729 0.0474  0.0495  148 TYR B CE2 
1869  C CZ  . TYR B 146 ? 1.1627 1.3022 1.1347 -0.1640 0.0357  0.0576  148 TYR B CZ  
1870  O OH  . TYR B 146 ? 1.1373 1.3149 1.1361 -0.1580 0.0273  0.0621  148 TYR B OH  
1871  N N   . LYS B 147 ? 1.2558 1.2137 1.1160 -0.2111 0.1222  0.0306  149 LYS B N   
1872  C CA  . LYS B 147 ? 1.2826 1.2125 1.1392 -0.2218 0.1522  0.0233  149 LYS B CA  
1873  C C   . LYS B 147 ? 1.3528 1.2799 1.2288 -0.2275 0.1674  0.0178  149 LYS B C   
1874  O O   . LYS B 147 ? 1.3529 1.2899 1.2632 -0.2400 0.1867  0.0067  149 LYS B O   
1875  C CB  . LYS B 147 ? 1.3715 1.2430 1.1643 -0.2215 0.1652  0.0284  149 LYS B CB  
1876  C CG  . LYS B 147 ? 1.5548 1.4084 1.3463 -0.2316 0.1917  0.0214  149 LYS B CG  
1877  C CD  . LYS B 147 ? 1.6553 1.4813 1.4500 -0.2432 0.2299  0.0144  149 LYS B CD  
1878  C CE  . LYS B 147 ? 1.6667 1.4863 1.4736 -0.2513 0.2589  0.0067  149 LYS B CE  
1879  N NZ  . LYS B 147 ? 1.7007 1.4930 1.5123 -0.2655 0.3011  -0.0006 149 LYS B NZ  
1880  N N   . ASN B 148 ? 1.3173 1.2326 1.1734 -0.2184 0.1583  0.0248  150 ASN B N   
1881  C CA  . ASN B 148 ? 1.3302 1.2290 1.1896 -0.2248 0.1728  0.0203  150 ASN B CA  
1882  C C   . ASN B 148 ? 1.3518 1.2938 1.2654 -0.2289 0.1626  0.0118  150 ASN B C   
1883  O O   . ASN B 148 ? 1.3652 1.2931 1.2844 -0.2394 0.1749  0.0049  150 ASN B O   
1884  C CB  . ASN B 148 ? 1.3519 1.2073 1.1549 -0.2099 0.1700  0.0318  150 ASN B CB  
1885  C CG  . ASN B 148 ? 1.6427 1.4468 1.3822 -0.2027 0.1764  0.0396  150 ASN B CG  
1886  O OD1 . ASN B 148 ? 1.5543 1.3331 1.2799 -0.2148 0.1971  0.0351  150 ASN B OD1 
1887  N ND2 . ASN B 148 ? 1.5907 1.3772 1.2886 -0.1806 0.1581  0.0514  150 ASN B ND2 
1888  N N   . LEU B 149 ? 1.2665 1.2532 1.2129 -0.2220 0.1410  0.0114  151 LEU B N   
1889  C CA  . LEU B 149 ? 1.2352 1.2530 1.2217 -0.2233 0.1300  0.0032  151 LEU B CA  
1890  C C   . LEU B 149 ? 1.2602 1.3165 1.2831 -0.2222 0.1185  -0.0033 151 LEU B C   
1891  O O   . LEU B 149 ? 1.2584 1.3214 1.2711 -0.2160 0.1111  0.0030  151 LEU B O   
1892  C CB  . LEU B 149 ? 1.2325 1.2469 1.2043 -0.2098 0.1160  0.0110  151 LEU B CB  
1893  C CG  . LEU B 149 ? 1.2929 1.3061 1.2378 -0.1926 0.1052  0.0258  151 LEU B CG  
1894  C CD1 . LEU B 149 ? 1.2617 1.3120 1.2296 -0.1879 0.0894  0.0273  151 LEU B CD1 
1895  C CD2 . LEU B 149 ? 1.3277 1.3245 1.2525 -0.1790 0.1030  0.0328  151 LEU B CD2 
1896  N N   . ILE B 150 ? 1.1970 1.2754 1.2595 -0.2281 0.1163  -0.0167 152 ILE B N   
1897  C CA  . ILE B 150 ? 1.1744 1.2845 1.2687 -0.2231 0.1051  -0.0246 152 ILE B CA  
1898  C C   . ILE B 150 ? 1.2438 1.3635 1.3370 -0.2107 0.0824  -0.0235 152 ILE B C   
1899  O O   . ILE B 150 ? 1.2580 1.3716 1.3514 -0.2109 0.0755  -0.0267 152 ILE B O   
1900  C CB  . ILE B 150 ? 1.2103 1.3430 1.3522 -0.2335 0.1135  -0.0416 152 ILE B CB  
1901  C CG1 . ILE B 150 ? 1.2409 1.3590 1.3839 -0.2483 0.1435  -0.0436 152 ILE B CG1 
1902  C CG2 . ILE B 150 ? 1.1988 1.3627 1.3707 -0.2222 0.1010  -0.0495 152 ILE B CG2 
1903  C CD1 . ILE B 150 ? 1.3161 1.4458 1.5000 -0.2673 0.1567  -0.0591 152 ILE B CD1 
1904  N N   . TRP B 151 ? 1.1885 1.3159 1.2749 -0.2010 0.0732  -0.0199 153 TRP B N   
1905  C CA  . TRP B 151 ? 1.1719 1.3003 1.2508 -0.1894 0.0567  -0.0193 153 TRP B CA  
1906  C C   . TRP B 151 ? 1.2146 1.3578 1.3199 -0.1838 0.0455  -0.0340 153 TRP B C   
1907  O O   . TRP B 151 ? 1.2065 1.3592 1.3205 -0.1784 0.0456  -0.0382 153 TRP B O   
1908  C CB  . TRP B 151 ? 1.1519 1.2765 1.2087 -0.1850 0.0554  -0.0101 153 TRP B CB  
1909  C CG  . TRP B 151 ? 1.1658 1.2829 1.2069 -0.1754 0.0456  -0.0077 153 TRP B CG  
1910  C CD1 . TRP B 151 ? 1.2112 1.3194 1.2491 -0.1667 0.0360  -0.0126 153 TRP B CD1 
1911  C CD2 . TRP B 151 ? 1.1662 1.2779 1.1875 -0.1753 0.0468  -0.0004 153 TRP B CD2 
1912  N NE1 . TRP B 151 ? 1.2136 1.3068 1.2271 -0.1593 0.0342  -0.0078 153 TRP B NE1 
1913  C CE2 . TRP B 151 ? 1.2284 1.3261 1.2350 -0.1661 0.0420  -0.0006 153 TRP B CE2 
1914  C CE3 . TRP B 151 ? 1.1824 1.2962 1.1942 -0.1842 0.0518  0.0056  153 TRP B CE3 
1915  C CZ2 . TRP B 151 ? 1.2344 1.3217 1.2209 -0.1670 0.0465  0.0050  153 TRP B CZ2 
1916  C CZ3 . TRP B 151 ? 1.2108 1.3190 1.2067 -0.1869 0.0523  0.0099  153 TRP B CZ3 
1917  C CH2 . TRP B 151 ? 1.2295 1.3255 1.2148 -0.1791 0.0519  0.0097  153 TRP B CH2 
1918  N N   . LEU B 152 ? 1.1723 1.3157 1.2886 -0.1840 0.0348  -0.0424 154 LEU B N   
1919  C CA  . LEU B 152 ? 1.1664 1.3279 1.3112 -0.1777 0.0179  -0.0584 154 LEU B CA  
1920  C C   . LEU B 152 ? 1.2149 1.3613 1.3333 -0.1581 -0.0018 -0.0590 154 LEU B C   
1921  O O   . LEU B 152 ? 1.2199 1.3393 1.3054 -0.1533 -0.0082 -0.0539 154 LEU B O   
1922  C CB  . LEU B 152 ? 1.1754 1.3438 1.3453 -0.1902 0.0125  -0.0706 154 LEU B CB  
1923  C CG  . LEU B 152 ? 1.2320 1.4256 1.4469 -0.2091 0.0295  -0.0799 154 LEU B CG  
1924  C CD1 . LEU B 152 ? 1.2482 1.4539 1.4940 -0.2220 0.0177  -0.0967 154 LEU B CD1 
1925  C CD2 . LEU B 152 ? 1.2713 1.4977 1.5224 -0.2025 0.0342  -0.0863 154 LEU B CD2 
1926  N N   . VAL B 153 ? 1.1635 1.3219 1.2918 -0.1449 -0.0093 -0.0656 155 VAL B N   
1927  C CA  . VAL B 153 ? 1.1792 1.3158 1.2756 -0.1231 -0.0270 -0.0676 155 VAL B CA  
1928  C C   . VAL B 153 ? 1.2503 1.4102 1.3784 -0.1080 -0.0513 -0.0858 155 VAL B C   
1929  O O   . VAL B 153 ? 1.2245 1.4262 1.4087 -0.1166 -0.0492 -0.0962 155 VAL B O   
1930  C CB  . VAL B 153 ? 1.2277 1.3440 1.2899 -0.1173 -0.0142 -0.0569 155 VAL B CB  
1931  C CG1 . VAL B 153 ? 1.2212 1.3148 1.2507 -0.1282 -0.0002 -0.0418 155 VAL B CG1 
1932  C CG2 . VAL B 153 ? 1.2118 1.3509 1.3002 -0.1226 0.0010  -0.0574 155 VAL B CG2 
1933  N N   . LYS B 154 ? 1.2579 1.3900 1.3498 -0.0853 -0.0742 -0.0901 156 LYS B N   
1934  C CA  . LYS B 154 ? 1.2866 1.4371 1.4009 -0.0650 -0.1053 -0.1079 156 LYS B CA  
1935  C C   . LYS B 154 ? 1.3632 1.5538 1.5214 -0.0522 -0.1037 -0.1157 156 LYS B C   
1936  O O   . LYS B 154 ? 1.3631 1.5362 1.4952 -0.0443 -0.0862 -0.1062 156 LYS B O   
1937  C CB  . LYS B 154 ? 1.3599 1.4560 1.4069 -0.0392 -0.1288 -0.1087 156 LYS B CB  
1938  C CG  . LYS B 154 ? 1.4183 1.4684 1.4048 -0.0219 -0.1166 -0.0977 156 LYS B CG  
1939  C CD  . LYS B 154 ? 1.4946 1.4819 1.4080 0.0036  -0.1372 -0.0995 156 LYS B CD  
1940  C CE  . LYS B 154 ? 1.5791 1.5202 1.4346 0.0232  -0.1269 -0.0928 156 LYS B CE  
1941  N NZ  . LYS B 154 ? 1.7235 1.5881 1.4933 0.0461  -0.1399 -0.0926 156 LYS B NZ  
1942  N N   . LYS B 155 ? 1.3384 1.5826 1.5640 -0.0506 -0.1214 -0.1337 157 LYS B N   
1943  C CA  . LYS B 155 ? 1.3406 1.6332 1.6213 -0.0360 -0.1199 -0.1436 157 LYS B CA  
1944  C C   . LYS B 155 ? 1.4543 1.7332 1.7088 0.0056  -0.1525 -0.1518 157 LYS B C   
1945  O O   . LYS B 155 ? 1.4657 1.7786 1.7587 0.0194  -0.1873 -0.1698 157 LYS B O   
1946  C CB  . LYS B 155 ? 1.3493 1.7119 1.7234 -0.0563 -0.1205 -0.1604 157 LYS B CB  
1947  C CG  . LYS B 155 ? 1.5261 1.9438 1.9676 -0.0498 -0.1023 -0.1676 157 LYS B CG  
1948  C CD  . LYS B 155 ? 1.6319 2.1208 2.1707 -0.0724 -0.1024 -0.1868 157 LYS B CD  
1949  C CE  . LYS B 155 ? 1.7431 2.2927 2.3574 -0.0626 -0.0838 -0.1961 157 LYS B CE  
1950  N NZ  . LYS B 155 ? 1.8526 2.4768 2.5694 -0.0867 -0.0842 -0.2175 157 LYS B NZ  
1951  N N   . GLY B 156 ? 1.4460 1.6708 1.6303 0.0245  -0.1420 -0.1389 158 GLY B N   
1952  C CA  . GLY B 156 ? 1.4991 1.6900 1.6354 0.0665  -0.1666 -0.1432 158 GLY B CA  
1953  C C   . GLY B 156 ? 1.5958 1.7550 1.6928 0.0827  -0.2060 -0.1514 158 GLY B C   
1954  O O   . GLY B 156 ? 1.5985 1.7954 1.7358 0.1032  -0.2426 -0.1695 158 GLY B O   
1955  N N   . ASN B 157 ? 1.5991 1.6887 1.6175 0.0738  -0.1983 -0.1388 159 ASN B N   
1956  C CA  . ASN B 157 ? 1.6642 1.6998 1.6208 0.0863  -0.2266 -0.1423 159 ASN B CA  
1957  C C   . ASN B 157 ? 1.7313 1.8115 1.7427 0.0783  -0.2616 -0.1603 159 ASN B C   
1958  O O   . ASN B 157 ? 1.7833 1.8447 1.7691 0.1048  -0.3032 -0.1735 159 ASN B O   
1959  C CB  . ASN B 157 ? 1.7778 1.7459 1.6504 0.1302  -0.2459 -0.1434 159 ASN B CB  
1960  C CG  . ASN B 157 ? 2.2095 2.2144 2.1156 0.1682  -0.2744 -0.1581 159 ASN B CG  
1961  O OD1 . ASN B 157 ? 2.1434 2.1391 2.0354 0.1857  -0.2574 -0.1527 159 ASN B OD1 
1962  N ND2 . ASN B 157 ? 2.1572 2.2014 2.1048 0.1834  -0.3198 -0.1775 159 ASN B ND2 
1963  N N   . SER B 158 ? 1.6348 1.7669 1.7141 0.0404  -0.2443 -0.1609 160 SER B N   
1964  C CA  . SER B 158 ? 1.6222 1.7949 1.7555 0.0218  -0.2686 -0.1773 160 SER B CA  
1965  C C   . SER B 158 ? 1.5788 1.7746 1.7504 -0.0217 -0.2350 -0.1701 160 SER B C   
1966  O O   . SER B 158 ? 1.5209 1.7746 1.7637 -0.0392 -0.2138 -0.1723 160 SER B O   
1967  C CB  . SER B 158 ? 1.6924 1.9416 1.9104 0.0359  -0.2997 -0.2001 160 SER B CB  
1968  O OG  . SER B 158 ? 1.8574 2.1396 2.1207 0.0177  -0.3295 -0.2188 160 SER B OG  
1969  N N   . TYR B 159 ? 1.5725 1.4850 1.5435 0.0014  0.0336  0.1829  161 TYR B N   
1970  C CA  . TYR B 159 ? 1.5038 1.4396 1.5164 -0.0173 0.0468  0.1549  161 TYR B CA  
1971  C C   . TYR B 159 ? 1.5159 1.5342 1.5814 -0.0370 0.0397  0.1421  161 TYR B C   
1972  O O   . TYR B 159 ? 1.5062 1.5466 1.5666 -0.0714 0.0340  0.1252  161 TYR B O   
1973  C CB  . TYR B 159 ? 1.5099 1.4085 1.4850 -0.0502 0.0529  0.1346  161 TYR B CB  
1974  C CG  . TYR B 159 ? 1.4696 1.3737 1.4760 -0.0585 0.0678  0.1103  161 TYR B CG  
1975  C CD1 . TYR B 159 ? 1.4422 1.4006 1.5025 -0.0691 0.0676  0.0913  161 TYR B CD1 
1976  C CD2 . TYR B 159 ? 1.4885 1.3412 1.4639 -0.0592 0.0813  0.1062  161 TYR B CD2 
1977  C CE1 . TYR B 159 ? 1.4093 1.3651 1.4934 -0.0734 0.0791  0.0712  161 TYR B CE1 
1978  C CE2 . TYR B 159 ? 1.4567 1.3190 1.4604 -0.0651 0.0933  0.0867  161 TYR B CE2 
1979  C CZ  . TYR B 159 ? 1.4561 1.3677 1.5142 -0.0699 0.0913  0.0699  161 TYR B CZ  
1980  O OH  . TYR B 159 ? 1.3718 1.2853 1.4523 -0.0727 0.1011  0.0528  161 TYR B OH  
1981  N N   . PRO B 160 ? 1.4518 1.5186 1.5644 -0.0195 0.0408  0.1481  162 PRO B N   
1982  C CA  . PRO B 160 ? 1.4167 1.5555 1.5696 -0.0453 0.0353  0.1351  162 PRO B CA  
1983  C C   . PRO B 160 ? 1.4184 1.5509 1.5940 -0.0685 0.0459  0.1047  162 PRO B C   
1984  O O   . PRO B 160 ? 1.4032 1.4900 1.5752 -0.0581 0.0574  0.0986  162 PRO B O   
1985  C CB  . PRO B 160 ? 1.4390 1.6322 1.6250 -0.0199 0.0330  0.1541  162 PRO B CB  
1986  C CG  . PRO B 160 ? 1.5296 1.6771 1.6953 0.0254  0.0376  0.1753  162 PRO B CG  
1987  C CD  . PRO B 160 ? 1.4820 1.5454 1.6104 0.0205  0.0475  0.1647  162 PRO B CD  
1988  N N   . LYS B 161 ? 1.3562 1.5322 1.5519 -0.0994 0.0419  0.0861  163 LYS B N   
1989  C CA  . LYS B 161 ? 1.3324 1.4969 1.5453 -0.1184 0.0501  0.0566  163 LYS B CA  
1990  C C   . LYS B 161 ? 1.3741 1.5291 1.6133 -0.1043 0.0587  0.0596  163 LYS B C   
1991  O O   . LYS B 161 ? 1.3671 1.5658 1.6280 -0.1072 0.0559  0.0685  163 LYS B O   
1992  C CB  . LYS B 161 ? 1.3577 1.5669 1.5815 -0.1533 0.0444  0.0369  163 LYS B CB  
1993  C CG  . LYS B 161 ? 1.4780 1.6633 1.7106 -0.1696 0.0520  0.0034  163 LYS B CG  
1994  C CD  . LYS B 161 ? 1.5868 1.8098 1.8308 -0.2022 0.0491  -0.0139 163 LYS B CD  
1995  C CE  . LYS B 161 ? 1.6735 1.9014 1.9363 -0.2067 0.0523  -0.0093 163 LYS B CE  
1996  N NZ  . LYS B 161 ? 1.7574 2.0255 2.0220 -0.2447 0.0495  -0.0224 163 LYS B NZ  
1997  N N   . LEU B 162 ? 1.3278 1.4319 1.5623 -0.0919 0.0687  0.0534  164 LEU B N   
1998  C CA  . LEU B 162 ? 1.3143 1.4046 1.5701 -0.0825 0.0766  0.0555  164 LEU B CA  
1999  C C   . LEU B 162 ? 1.3377 1.4197 1.6065 -0.1050 0.0776  0.0317  164 LEU B C   
2000  O O   . LEU B 162 ? 1.3409 1.4087 1.5994 -0.1167 0.0770  0.0100  164 LEU B O   
2001  C CB  . LEU B 162 ? 1.3165 1.3583 1.5594 -0.0607 0.0870  0.0622  164 LEU B CB  
2002  C CG  . LEU B 162 ? 1.3827 1.3858 1.6042 -0.0660 0.0921  0.0453  164 LEU B CG  
2003  C CD1 . LEU B 162 ? 1.3755 1.3537 1.6122 -0.0651 0.0998  0.0350  164 LEU B CD1 
2004  C CD2 . LEU B 162 ? 1.4372 1.4100 1.6238 -0.0530 0.0969  0.0580  164 LEU B CD2 
2005  N N   . SER B 163 ? 1.2738 1.3635 1.5611 -0.1114 0.0788  0.0347  165 SER B N   
2006  C CA  . SER B 163 ? 1.2827 1.3490 1.5728 -0.1332 0.0788  0.0141  165 SER B CA  
2007  C C   . SER B 163 ? 1.3172 1.3666 1.6176 -0.1346 0.0821  0.0218  165 SER B C   
2008  O O   . SER B 163 ? 1.3341 1.4033 1.6381 -0.1585 0.0785  0.0218  165 SER B O   
2009  C CB  . SER B 163 ? 1.3564 1.4571 1.6444 -0.1635 0.0722  0.0019  165 SER B CB  
2010  O OG  . SER B 163 ? 1.5045 1.5643 1.7827 -0.1806 0.0731  -0.0254 165 SER B OG  
2011  N N   . LYS B 164 ? 1.2437 1.2596 1.5454 -0.1137 0.0888  0.0288  166 LYS B N   
2012  C CA  . LYS B 164 ? 1.2386 1.2382 1.5485 -0.1177 0.0913  0.0364  166 LYS B CA  
2013  C C   . LYS B 164 ? 1.3177 1.2628 1.6180 -0.1313 0.0890  0.0187  166 LYS B C   
2014  O O   . LYS B 164 ? 1.3201 1.2361 1.6109 -0.1237 0.0892  0.0013  166 LYS B O   
2015  C CB  . LYS B 164 ? 1.2404 1.2307 1.5546 -0.0931 0.1000  0.0517  166 LYS B CB  
2016  C CG  . LYS B 164 ? 1.3838 1.4073 1.7129 -0.0941 0.1022  0.0686  166 LYS B CG  
2017  C CD  . LYS B 164 ? 1.5430 1.6299 1.8804 -0.0845 0.1002  0.0809  166 LYS B CD  
2018  C CE  . LYS B 164 ? 1.7086 1.8473 2.0626 -0.0930 0.1000  0.0917  166 LYS B CE  
2019  N NZ  . LYS B 164 ? 1.7969 2.0111 2.1607 -0.0840 0.0957  0.1021  166 LYS B NZ  
2020  N N   . SER B 165 ? 1.2939 1.2271 1.5928 -0.1524 0.0858  0.0225  167 SER B N   
2021  C CA  . SER B 165 ? 1.3303 1.1998 1.6120 -0.1658 0.0817  0.0086  167 SER B CA  
2022  C C   . SER B 165 ? 1.3764 1.2192 1.6567 -0.1739 0.0808  0.0227  167 SER B C   
2023  O O   . SER B 165 ? 1.3689 1.2512 1.6549 -0.1930 0.0799  0.0367  167 SER B O   
2024  C CB  . SER B 165 ? 1.4189 1.2868 1.6829 -0.1988 0.0756  -0.0061 167 SER B CB  
2025  O OG  . SER B 165 ? 1.5242 1.4247 1.7902 -0.1963 0.0761  -0.0185 167 SER B OG  
2026  N N   . TYR B 166 ? 1.3360 1.1186 1.6084 -0.1597 0.0804  0.0192  168 TYR B N   
2027  C CA  . TYR B 166 ? 1.3479 1.0990 1.6155 -0.1691 0.0777  0.0335  168 TYR B CA  
2028  C C   . TYR B 166 ? 1.4736 1.1510 1.7092 -0.1899 0.0676  0.0242  168 TYR B C   
2029  O O   . TYR B 166 ? 1.5123 1.1408 1.7339 -0.1743 0.0652  0.0057  168 TYR B O   
2030  C CB  . TYR B 166 ? 1.3292 1.0688 1.6085 -0.1395 0.0839  0.0422  168 TYR B CB  
2031  C CG  . TYR B 166 ? 1.3675 1.0725 1.6403 -0.1508 0.0798  0.0575  168 TYR B CG  
2032  C CD1 . TYR B 166 ? 1.3774 1.1202 1.6601 -0.1707 0.0820  0.0752  168 TYR B CD1 
2033  C CD2 . TYR B 166 ? 1.4160 1.0533 1.6716 -0.1410 0.0728  0.0541  168 TYR B CD2 
2034  C CE1 . TYR B 166 ? 1.4140 1.1289 1.6887 -0.1870 0.0772  0.0896  168 TYR B CE1 
2035  C CE2 . TYR B 166 ? 1.4519 1.0553 1.6982 -0.1532 0.0669  0.0711  168 TYR B CE2 
2036  C CZ  . TYR B 166 ? 1.5275 1.1700 1.7828 -0.1796 0.0689  0.0890  168 TYR B CZ  
2037  O OH  . TYR B 166 ? 1.5630 1.1762 1.8075 -0.1971 0.0623  0.1062  168 TYR B OH  
2038  N N   . ILE B 167 ? 1.4396 1.1067 1.6599 -0.2247 0.0615  0.0365  169 ILE B N   
2039  C CA  . ILE B 167 ? 1.5090 1.0942 1.6871 -0.2519 0.0506  0.0314  169 ILE B CA  
2040  C C   . ILE B 167 ? 1.5630 1.1047 1.7356 -0.2476 0.0458  0.0492  169 ILE B C   
2041  O O   . ILE B 167 ? 1.5129 1.1033 1.7028 -0.2598 0.0483  0.0679  169 ILE B O   
2042  C CB  . ILE B 167 ? 1.5798 1.1897 1.7347 -0.3054 0.0462  0.0319  169 ILE B CB  
2043  C CG1 . ILE B 167 ? 1.5647 1.2391 1.7321 -0.3087 0.0517  0.0182  169 ILE B CG1 
2044  C CG2 . ILE B 167 ? 1.6808 1.1901 1.7780 -0.3397 0.0349  0.0253  169 ILE B CG2 
2045  C CD1 . ILE B 167 ? 1.5899 1.3805 1.7993 -0.3008 0.0591  0.0321  169 ILE B CD1 
2046  N N   . ASN B 168 ? 1.5812 1.0360 1.7308 -0.2272 0.0390  0.0432  170 ASN B N   
2047  C CA  . ASN B 168 ? 1.6033 1.0133 1.7460 -0.2191 0.0325  0.0617  170 ASN B CA  
2048  C C   . ASN B 168 ? 1.7411 1.1125 1.8476 -0.2692 0.0208  0.0782  170 ASN B C   
2049  O O   . ASN B 168 ? 1.8307 1.1162 1.8871 -0.2915 0.0096  0.0717  170 ASN B O   
2050  C CB  . ASN B 168 ? 1.6247 0.9600 1.7536 -0.1766 0.0275  0.0514  170 ASN B CB  
2051  C CG  . ASN B 168 ? 1.8347 1.1522 1.9703 -0.1556 0.0235  0.0723  170 ASN B CG  
2052  O OD1 . ASN B 168 ? 1.6727 1.0201 1.8177 -0.1786 0.0234  0.0953  170 ASN B OD1 
2053  N ND2 . ASN B 168 ? 1.7994 1.0750 1.9310 -0.1110 0.0204  0.0643  170 ASN B ND2 
2054  N N   . ASP B 169 ? 1.6735 1.1065 1.8014 -0.2883 0.0238  0.0986  171 ASP B N   
2055  C CA  . ASP B 169 ? 1.7271 1.1458 1.8251 -0.3408 0.0135  0.1159  171 ASP B CA  
2056  C C   . ASP B 169 ? 1.8021 1.1845 1.8974 -0.3342 0.0067  0.1380  171 ASP B C   
2057  O O   . ASP B 169 ? 1.8492 1.1958 1.9091 -0.3777 -0.0058 0.1535  171 ASP B O   
2058  C CB  . ASP B 169 ? 1.6936 1.2240 1.8175 -0.3718 0.0218  0.1207  171 ASP B CB  
2059  C CG  . ASP B 169 ? 1.7484 1.3648 1.9271 -0.3403 0.0364  0.1284  171 ASP B CG  
2060  O OD1 . ASP B 169 ? 1.7534 1.4075 1.9413 -0.3603 0.0372  0.1444  171 ASP B OD1 
2061  O OD2 . ASP B 169 ? 1.7502 1.3931 1.9579 -0.2985 0.0473  0.1177  171 ASP B OD2 
2062  N N   . LYS B 170 ? 1.7195 1.1143 1.8484 -0.2838 0.0144  0.1399  172 LYS B N   
2063  C CA  . LYS B 170 ? 1.7187 1.0973 1.8531 -0.2715 0.0106  0.1610  172 LYS B CA  
2064  C C   . LYS B 170 ? 1.9027 1.1660 1.9876 -0.2726 -0.0094 0.1711  172 LYS B C   
2065  O O   . LYS B 170 ? 1.9194 1.1679 1.9991 -0.2798 -0.0170 0.1944  172 LYS B O   
2066  C CB  . LYS B 170 ? 1.6623 1.0886 1.8393 -0.2198 0.0251  0.1576  172 LYS B CB  
2067  C CG  . LYS B 170 ? 1.6300 1.1553 1.8481 -0.2152 0.0444  0.1504  172 LYS B CG  
2068  C CD  . LYS B 170 ? 1.6657 1.2555 1.9013 -0.2459 0.0511  0.1668  172 LYS B CD  
2069  C CE  . LYS B 170 ? 1.6593 1.3314 1.9231 -0.2443 0.0664  0.1568  172 LYS B CE  
2070  N NZ  . LYS B 170 ? 1.7252 1.4621 2.0053 -0.2703 0.0737  0.1689  172 LYS B NZ  
2071  N N   . GLY B 171 ? 1.9456 1.1266 1.9926 -0.2645 -0.0178 0.1538  173 GLY B N   
2072  C CA  . GLY B 171 ? 2.0635 1.1183 2.0552 -0.2587 -0.0371 0.1604  173 GLY B CA  
2073  C C   . GLY B 171 ? 2.1237 1.1514 2.1302 -0.1920 -0.0384 0.1602  173 GLY B C   
2074  O O   . GLY B 171 ? 2.2289 1.1509 2.1928 -0.1677 -0.0525 0.1574  173 GLY B O   
2075  N N   . LYS B 172 ? 1.9651 1.0900 2.0286 -0.1623 -0.0235 0.1629  174 LYS B N   
2076  C CA  . LYS B 172 ? 1.9364 1.0726 2.0226 -0.1030 -0.0210 0.1630  174 LYS B CA  
2077  C C   . LYS B 172 ? 1.9309 1.1076 2.0419 -0.0647 -0.0072 0.1311  174 LYS B C   
2078  O O   . LYS B 172 ? 1.8959 1.1022 2.0129 -0.0866 0.0014  0.1137  174 LYS B O   
2079  C CB  . LYS B 172 ? 1.8786 1.1010 2.0041 -0.1066 -0.0117 0.1861  174 LYS B CB  
2080  C CG  . LYS B 172 ? 2.0346 1.2238 2.1376 -0.1421 -0.0260 0.2187  174 LYS B CG  
2081  C CD  . LYS B 172 ? 2.0414 1.3198 2.1829 -0.1486 -0.0145 0.2387  174 LYS B CD  
2082  C CE  . LYS B 172 ? 2.1749 1.4194 2.2926 -0.1820 -0.0306 0.2714  174 LYS B CE  
2083  N NZ  . LYS B 172 ? 2.1791 1.5123 2.3328 -0.1917 -0.0180 0.2895  174 LYS B NZ  
2084  N N   . GLU B 173 ? 1.8759 1.0598 1.9998 -0.0093 -0.0060 0.1237  175 GLU B N   
2085  C CA  . GLU B 173 ? 1.8253 1.0568 1.9718 0.0262  0.0064  0.0934  175 GLU B CA  
2086  C C   . GLU B 173 ? 1.7504 1.0933 1.9395 0.0131  0.0254  0.0957  175 GLU B C   
2087  O O   . GLU B 173 ? 1.7017 1.0928 1.9099 0.0142  0.0305  0.1160  175 GLU B O   
2088  C CB  . GLU B 173 ? 1.8743 1.0947 2.0213 0.0877  0.0017  0.0860  175 GLU B CB  
2089  C CG  . GLU B 173 ? 2.1347 1.2346 2.2350 0.1117  -0.0170 0.0811  175 GLU B CG  
2090  C CD  . GLU B 173 ? 2.4834 1.5803 2.5865 0.1784  -0.0232 0.0787  175 GLU B CD  
2091  O OE1 . GLU B 173 ? 2.2805 1.4036 2.3946 0.1894  -0.0280 0.1073  175 GLU B OE1 
2092  O OE2 . GLU B 173 ? 2.5621 1.6357 2.6563 0.2200  -0.0232 0.0476  175 GLU B OE2 
2093  N N   . VAL B 174 ? 1.6614 1.0405 1.8607 -0.0017 0.0355  0.0763  176 VAL B N   
2094  C CA  . VAL B 174 ? 1.5673 1.0369 1.7983 -0.0136 0.0523  0.0790  176 VAL B CA  
2095  C C   . VAL B 174 ? 1.5709 1.0939 1.8177 0.0201  0.0630  0.0582  176 VAL B C   
2096  O O   . VAL B 174 ? 1.5871 1.1036 1.8286 0.0297  0.0629  0.0329  176 VAL B O   
2097  C CB  . VAL B 174 ? 1.5981 1.0848 1.8305 -0.0549 0.0559  0.0784  176 VAL B CB  
2098  C CG1 . VAL B 174 ? 1.5156 1.0847 1.7752 -0.0570 0.0726  0.0763  176 VAL B CG1 
2099  C CG2 . VAL B 174 ? 1.6189 1.0815 1.8396 -0.0929 0.0481  0.1020  176 VAL B CG2 
2100  N N   . LEU B 175 ? 1.4585 1.0371 1.7212 0.0332  0.0722  0.0688  177 LEU B N   
2101  C CA  . LEU B 175 ? 1.4020 1.0416 1.6741 0.0563  0.0830  0.0520  177 LEU B CA  
2102  C C   . LEU B 175 ? 1.3810 1.0682 1.6611 0.0319  0.0966  0.0487  177 LEU B C   
2103  O O   . LEU B 175 ? 1.3451 1.0508 1.6314 0.0090  0.1042  0.0674  177 LEU B O   
2104  C CB  . LEU B 175 ? 1.3798 1.0602 1.6578 0.0743  0.0873  0.0660  177 LEU B CB  
2105  C CG  . LEU B 175 ? 1.3805 1.1394 1.6628 0.0824  0.1018  0.0547  177 LEU B CG  
2106  C CD1 . LEU B 175 ? 1.3959 1.1690 1.6745 0.1120  0.0987  0.0236  177 LEU B CD1 
2107  C CD2 . LEU B 175 ? 1.3948 1.1980 1.6798 0.0886  0.1070  0.0731  177 LEU B CD2 
2108  N N   . VAL B 176 ? 1.3201 1.0249 1.5980 0.0379  0.0990  0.0247  178 VAL B N   
2109  C CA  . VAL B 176 ? 1.2705 1.0134 1.5506 0.0189  0.1091  0.0214  178 VAL B CA  
2110  C C   . VAL B 176 ? 1.2875 1.0819 1.5618 0.0312  0.1174  0.0061  178 VAL B C   
2111  O O   . VAL B 176 ? 1.3012 1.1014 1.5722 0.0507  0.1127  -0.0166 178 VAL B O   
2112  C CB  . VAL B 176 ? 1.3340 1.0543 1.6123 0.0040  0.1028  0.0099  178 VAL B CB  
2113  C CG1 . VAL B 176 ? 1.2908 1.0526 1.5705 -0.0100 0.1110  0.0082  178 VAL B CG1 
2114  C CG2 . VAL B 176 ? 1.3582 1.0359 1.6359 -0.0164 0.0950  0.0252  178 VAL B CG2 
2115  N N   . LEU B 177 ? 1.2011 1.0316 1.4697 0.0180  0.1299  0.0170  179 LEU B N   
2116  C CA  . LEU B 177 ? 1.1827 1.0614 1.4356 0.0195  0.1382  0.0046  179 LEU B CA  
2117  C C   . LEU B 177 ? 1.2357 1.1221 1.4757 0.0003  0.1434  0.0030  179 LEU B C   
2118  O O   . LEU B 177 ? 1.2361 1.1036 1.4794 -0.0123 0.1463  0.0191  179 LEU B O   
2119  C CB  . LEU B 177 ? 1.1638 1.0740 1.4072 0.0164  0.1492  0.0186  179 LEU B CB  
2120  C CG  . LEU B 177 ? 1.2342 1.1529 1.4874 0.0383  0.1441  0.0221  179 LEU B CG  
2121  C CD1 . LEU B 177 ? 1.2401 1.1271 1.5047 0.0310  0.1431  0.0481  179 LEU B CD1 
2122  C CD2 . LEU B 177 ? 1.2491 1.2308 1.4864 0.0383  0.1540  0.0196  179 LEU B CD2 
2123  N N   . TRP B 178 ? 1.1788 1.0959 1.4031 -0.0011 0.1437  -0.0162 180 TRP B N   
2124  C CA  . TRP B 178 ? 1.1636 1.0870 1.3693 -0.0188 0.1461  -0.0174 180 TRP B CA  
2125  C C   . TRP B 178 ? 1.2136 1.1802 1.3907 -0.0267 0.1499  -0.0331 180 TRP B C   
2126  O O   . TRP B 178 ? 1.2279 1.2276 1.4083 -0.0142 0.1479  -0.0507 180 TRP B O   
2127  C CB  . TRP B 178 ? 1.1542 1.0617 1.3741 -0.0200 0.1356  -0.0265 180 TRP B CB  
2128  C CG  . TRP B 178 ? 1.1791 1.1011 1.4040 -0.0104 0.1277  -0.0547 180 TRP B CG  
2129  C CD1 . TRP B 178 ? 1.2148 1.1710 1.4253 -0.0182 0.1260  -0.0751 180 TRP B CD1 
2130  C CD2 . TRP B 178 ? 1.1995 1.0985 1.4416 0.0086  0.1206  -0.0669 180 TRP B CD2 
2131  N NE1 . TRP B 178 ? 1.2267 1.1888 1.4480 -0.0037 0.1198  -0.1017 180 TRP B NE1 
2132  C CE2 . TRP B 178 ? 1.2621 1.1837 1.5009 0.0150  0.1164  -0.0972 180 TRP B CE2 
2133  C CE3 . TRP B 178 ? 1.2351 1.0924 1.4907 0.0199  0.1169  -0.0551 180 TRP B CE3 
2134  C CZ2 . TRP B 178 ? 1.2889 1.1867 1.5363 0.0370  0.1098  -0.1175 180 TRP B CZ2 
2135  C CZ3 . TRP B 178 ? 1.2918 1.1199 1.5521 0.0395  0.1086  -0.0722 180 TRP B CZ3 
2136  C CH2 . TRP B 178 ? 1.3165 1.1623 1.5723 0.0504  0.1057  -0.1038 180 TRP B CH2 
2137  N N   . GLY B 179 ? 1.1552 1.1218 1.3018 -0.0468 0.1542  -0.0274 181 GLY B N   
2138  C CA  . GLY B 179 ? 1.1555 1.1600 1.2644 -0.0642 0.1570  -0.0405 181 GLY B CA  
2139  C C   . GLY B 179 ? 1.2183 1.2284 1.3149 -0.0767 0.1484  -0.0516 181 GLY B C   
2140  O O   . GLY B 179 ? 1.2150 1.1967 1.3276 -0.0738 0.1422  -0.0438 181 GLY B O   
2141  N N   . ILE B 180 ? 1.1925 1.2477 1.2601 -0.0931 0.1476  -0.0702 182 ILE B N   
2142  C CA  . ILE B 180 ? 1.2105 1.2805 1.2579 -0.1127 0.1393  -0.0814 182 ILE B CA  
2143  C C   . ILE B 180 ? 1.3112 1.3936 1.2968 -0.1451 0.1449  -0.0771 182 ILE B C   
2144  O O   . ILE B 180 ? 1.3150 1.4472 1.2822 -0.1547 0.1502  -0.0911 182 ILE B O   
2145  C CB  . ILE B 180 ? 1.2448 1.3633 1.3165 -0.1049 0.1314  -0.1146 182 ILE B CB  
2146  C CG1 . ILE B 180 ? 1.2531 1.3459 1.3756 -0.0754 0.1266  -0.1200 182 ILE B CG1 
2147  C CG2 . ILE B 180 ? 1.2541 1.3959 1.3018 -0.1320 0.1231  -0.1261 182 ILE B CG2 
2148  C CD1 . ILE B 180 ? 1.3859 1.4325 1.5259 -0.0762 0.1212  -0.1031 182 ILE B CD1 
2149  N N   . HIS B 181 ? 1.3036 1.3391 1.2531 -0.1616 0.1438  -0.0567 183 HIS B N   
2150  C CA  . HIS B 181 ? 1.3437 1.3682 1.2209 -0.1965 0.1482  -0.0491 183 HIS B CA  
2151  C C   . HIS B 181 ? 1.4231 1.4877 1.2687 -0.2262 0.1374  -0.0665 183 HIS B C   
2152  O O   . HIS B 181 ? 1.4297 1.4897 1.2922 -0.2234 0.1256  -0.0672 183 HIS B O   
2153  C CB  . HIS B 181 ? 1.3823 1.3262 1.2294 -0.1953 0.1514  -0.0189 183 HIS B CB  
2154  C CG  . HIS B 181 ? 1.4755 1.3849 1.2368 -0.2315 0.1556  -0.0091 183 HIS B CG  
2155  N ND1 . HIS B 181 ? 1.5389 1.4109 1.2550 -0.2475 0.1447  0.0013  183 HIS B ND1 
2156  C CD2 . HIS B 181 ? 1.5132 1.4179 1.2218 -0.2568 0.1690  -0.0078 183 HIS B CD2 
2157  C CE1 . HIS B 181 ? 1.5817 1.4175 1.2154 -0.2818 0.1514  0.0085  183 HIS B CE1 
2158  N NE2 . HIS B 181 ? 1.5731 1.4287 1.1985 -0.2907 0.1669  0.0025  183 HIS B NE2 
2159  N N   . HIS B 182 ? 1.3773 1.4887 1.1760 -0.2581 0.1413  -0.0806 184 HIS B N   
2160  C CA  . HIS B 182 ? 1.3855 1.5445 1.1467 -0.2943 0.1316  -0.0986 184 HIS B CA  
2161  C C   . HIS B 182 ? 1.4669 1.5801 1.1342 -0.3401 0.1329  -0.0803 184 HIS B C   
2162  O O   . HIS B 182 ? 1.4757 1.6074 1.0948 -0.3669 0.1434  -0.0827 184 HIS B O   
2163  C CB  . HIS B 182 ? 1.3709 1.6333 1.1513 -0.2964 0.1335  -0.1340 184 HIS B CB  
2164  C CG  . HIS B 182 ? 1.3715 1.6609 1.2330 -0.2488 0.1323  -0.1515 184 HIS B CG  
2165  N ND1 . HIS B 182 ? 1.3820 1.7057 1.2779 -0.2410 0.1223  -0.1754 184 HIS B ND1 
2166  C CD2 . HIS B 182 ? 1.3682 1.6483 1.2746 -0.2107 0.1398  -0.1476 184 HIS B CD2 
2167  C CE1 . HIS B 182 ? 1.3492 1.6749 1.3049 -0.1978 0.1244  -0.1858 184 HIS B CE1 
2168  N NE2 . HIS B 182 ? 1.3445 1.6441 1.3087 -0.1780 0.1337  -0.1685 184 HIS B NE2 
2169  N N   . PRO B 183 ? 1.4590 1.5058 1.0960 -0.3482 0.1226  -0.0595 185 PRO B N   
2170  C CA  . PRO B 183 ? 1.5393 1.5214 1.0783 -0.3886 0.1226  -0.0397 185 PRO B CA  
2171  C C   . PRO B 183 ? 1.6527 1.6917 1.1250 -0.4466 0.1174  -0.0579 185 PRO B C   
2172  O O   . PRO B 183 ? 1.6356 1.7475 1.1335 -0.4561 0.1063  -0.0801 185 PRO B O   
2173  C CB  . PRO B 183 ? 1.5898 1.5016 1.1254 -0.3738 0.1090  -0.0154 185 PRO B CB  
2174  C CG  . PRO B 183 ? 1.5797 1.5151 1.2130 -0.3249 0.1065  -0.0190 185 PRO B CG  
2175  C CD  . PRO B 183 ? 1.4640 1.4925 1.1491 -0.3221 0.1100  -0.0524 185 PRO B CD  
2176  N N   . SER B 184 ? 1.6684 1.6758 1.0516 -0.4890 0.1259  -0.0499 186 SER B N   
2177  C CA  . SER B 184 ? 1.7035 1.7650 1.0081 -0.5542 0.1222  -0.0657 186 SER B CA  
2178  C C   . SER B 184 ? 1.7728 1.8185 1.0303 -0.5890 0.1014  -0.0615 186 SER B C   
2179  O O   . SER B 184 ? 1.7481 1.8903 1.0103 -0.6176 0.0927  -0.0880 186 SER B O   
2180  C CB  . SER B 184 ? 1.8256 1.8396 1.0353 -0.5961 0.1367  -0.0540 186 SER B CB  
2181  O OG  . SER B 184 ? 2.0293 1.9050 1.1948 -0.5841 0.1392  -0.0209 186 SER B OG  
2182  N N   . THR B 185 ? 1.7701 1.6988 0.9836 -0.5846 0.0930  -0.0288 187 THR B N   
2183  C CA  . THR B 185 ? 1.8064 1.7074 0.9721 -0.6140 0.0712  -0.0176 187 THR B CA  
2184  C C   . THR B 185 ? 1.8050 1.7027 1.0560 -0.5622 0.0594  -0.0090 187 THR B C   
2185  O O   . THR B 185 ? 1.7566 1.6317 1.0794 -0.5050 0.0681  -0.0014 187 THR B O   
2186  C CB  . THR B 185 ? 1.9469 1.7166 0.9903 -0.6474 0.0674  0.0148  187 THR B CB  
2187  O OG1 . THR B 185 ? 1.8998 1.5625 0.9597 -0.5925 0.0736  0.0431  187 THR B OG1 
2188  C CG2 . THR B 185 ? 1.9876 1.7546 0.9332 -0.7082 0.0800  0.0071  187 THR B CG2 
2189  N N   . SER B 186 ? 1.7719 1.6976 1.0126 -0.5870 0.0395  -0.0101 188 SER B N   
2190  C CA  . SER B 186 ? 1.7350 1.6650 1.0460 -0.5483 0.0268  -0.0007 188 SER B CA  
2191  C C   . SER B 186 ? 1.8272 1.6393 1.1220 -0.5083 0.0240  0.0403  188 SER B C   
2192  O O   . SER B 186 ? 1.7749 1.5883 1.1475 -0.4565 0.0241  0.0482  188 SER B O   
2193  C CB  . SER B 186 ? 1.7978 1.7813 1.0868 -0.5925 0.0061  -0.0082 188 SER B CB  
2194  O OG  . SER B 186 ? 2.0062 1.9453 1.1803 -0.6534 -0.0062 0.0060  188 SER B OG  
2195  N N   . ALA B 187 ? 1.8788 1.5896 1.0684 -0.5329 0.0228  0.0645  189 ALA B N   
2196  C CA  . ALA B 187 ? 1.9434 1.5290 1.0947 -0.4974 0.0211  0.1023  189 ALA B CA  
2197  C C   . ALA B 187 ? 1.9459 1.5086 1.1589 -0.4405 0.0418  0.1036  189 ALA B C   
2198  O O   . ALA B 187 ? 1.9546 1.4636 1.1953 -0.3890 0.0397  0.1269  189 ALA B O   
2199  C CB  . ALA B 187 ? 2.0736 1.5564 1.0877 -0.5451 0.0189  0.1194  189 ALA B CB  
2200  N N   . ASP B 188 ? 1.8534 1.4629 1.0870 -0.4503 0.0612  0.0791  190 ASP B N   
2201  C CA  . ASP B 188 ? 1.8054 1.4036 1.0969 -0.4042 0.0812  0.0783  190 ASP B CA  
2202  C C   . ASP B 188 ? 1.7771 1.4334 1.1861 -0.3515 0.0781  0.0738  190 ASP B C   
2203  O O   . ASP B 188 ? 1.7677 1.3835 1.2144 -0.3043 0.0848  0.0890  190 ASP B O   
2204  C CB  . ASP B 188 ? 1.7923 1.4408 1.0776 -0.4314 0.0999  0.0540  190 ASP B CB  
2205  C CG  . ASP B 188 ? 1.9232 1.4897 1.1025 -0.4666 0.1130  0.0642  190 ASP B CG  
2206  O OD1 . ASP B 188 ? 2.0199 1.4982 1.1023 -0.4941 0.1036  0.0835  190 ASP B OD1 
2207  O OD2 . ASP B 188 ? 1.9297 1.5206 1.1173 -0.4707 0.1324  0.0527  190 ASP B OD2 
2208  N N   . GLN B 189 ? 1.4912 1.2682 1.2750 -0.3817 0.2012  -0.1520 191 GLN B N   
2209  C CA  . GLN B 189 ? 1.4471 1.2572 1.2805 -0.3535 0.1278  -0.1302 191 GLN B CA  
2210  C C   . GLN B 189 ? 1.5417 1.3054 1.3362 -0.3176 0.1120  -0.0938 191 GLN B C   
2211  O O   . GLN B 189 ? 1.4909 1.2931 1.3419 -0.3041 0.0685  -0.0717 191 GLN B O   
2212  C CB  . GLN B 189 ? 1.4798 1.2846 1.3026 -0.3474 0.1049  -0.1529 191 GLN B CB  
2213  C CG  . GLN B 189 ? 1.6259 1.4593 1.4914 -0.3209 0.0380  -0.1369 191 GLN B CG  
2214  C CD  . GLN B 189 ? 1.7664 1.6800 1.7298 -0.3300 0.0019  -0.1354 191 GLN B CD  
2215  O OE1 . GLN B 189 ? 1.6467 1.6025 1.6465 -0.3513 0.0107  -0.1574 191 GLN B OE1 
2216  N NE2 . GLN B 189 ? 1.6688 1.6033 1.6730 -0.3115 -0.0382 -0.1123 191 GLN B NE2 
2217  N N   . GLN B 190 ? 1.6023 1.2809 1.2967 -0.3012 0.1518  -0.0904 192 GLN B N   
2218  C CA  . GLN B 190 ? 1.6711 1.2970 1.3072 -0.2583 0.1438  -0.0584 192 GLN B CA  
2219  C C   . GLN B 190 ? 1.7163 1.3417 1.3656 -0.2597 0.1650  -0.0313 192 GLN B C   
2220  O O   . GLN B 190 ? 1.7491 1.3579 1.3806 -0.2223 0.1423  -0.0035 192 GLN B O   
2221  C CB  . GLN B 190 ? 1.8109 1.3348 1.3219 -0.2376 0.1883  -0.0641 192 GLN B CB  
2222  C CG  . GLN B 190 ? 2.0519 1.5392 1.5042 -0.1801 0.1509  -0.0411 192 GLN B CG  
2223  C CD  . GLN B 190 ? 2.4606 1.8465 1.7943 -0.1471 0.2049  -0.0190 192 GLN B CD  
2224  O OE1 . GLN B 190 ? 2.4449 1.8294 1.7700 -0.1103 0.1881  0.0119  192 GLN B OE1 
2225  N NE2 . GLN B 190 ? 2.4630 1.7578 1.7001 -0.1585 0.2750  -0.0363 192 GLN B NE2 
2226  N N   . SER B 191 ? 1.6238 1.2713 1.3049 -0.3022 0.2086  -0.0417 193 SER B N   
2227  C CA  . SER B 191 ? 1.5994 1.2487 1.2988 -0.3126 0.2346  -0.0183 193 SER B CA  
2228  C C   . SER B 191 ? 1.5185 1.2561 1.3319 -0.3300 0.1869  -0.0108 193 SER B C   
2229  O O   . SER B 191 ? 1.4931 1.2341 1.3314 -0.3288 0.1864  0.0143  193 SER B O   
2230  C CB  . SER B 191 ? 1.6838 1.2978 1.3393 -0.3503 0.3221  -0.0361 193 SER B CB  
2231  O OG  . SER B 191 ? 1.7553 1.4300 1.4600 -0.3916 0.3316  -0.0755 193 SER B OG  
2232  N N   . LEU B 192 ? 1.3876 1.1894 1.2648 -0.3449 0.1504  -0.0324 194 LEU B N   
2233  C CA  . LEU B 192 ? 1.2868 1.1611 1.2602 -0.3583 0.1098  -0.0274 194 LEU B CA  
2234  C C   . LEU B 192 ? 1.3274 1.2219 1.3407 -0.3285 0.0429  -0.0176 194 LEU B C   
2235  O O   . LEU B 192 ? 1.2812 1.2046 1.3537 -0.3292 0.0152  -0.0038 194 LEU B O   
2236  C CB  . LEU B 192 ? 1.2324 1.1657 1.2486 -0.3877 0.1146  -0.0572 194 LEU B CB  
2237  C CG  . LEU B 192 ? 1.2799 1.2247 1.2821 -0.4250 0.1780  -0.0787 194 LEU B CG  
2238  C CD1 . LEU B 192 ? 1.2391 1.2400 1.2675 -0.4413 0.1767  -0.1173 194 LEU B CD1 
2239  C CD2 . LEU B 192 ? 1.2770 1.2522 1.3240 -0.4471 0.1916  -0.0619 194 LEU B CD2 
2240  N N   . TYR B 193 ? 1.3200 1.2003 1.3028 -0.3064 0.0204  -0.0293 195 TYR B N   
2241  C CA  . TYR B 193 ? 1.3006 1.2077 1.3226 -0.2827 -0.0373 -0.0291 195 TYR B CA  
2242  C C   . TYR B 193 ? 1.4509 1.3189 1.4104 -0.2435 -0.0526 -0.0248 195 TYR B C   
2243  O O   . TYR B 193 ? 1.4329 1.3280 1.4238 -0.2217 -0.0975 -0.0261 195 TYR B O   
2244  C CB  . TYR B 193 ? 1.2664 1.2167 1.3343 -0.2961 -0.0582 -0.0513 195 TYR B CB  
2245  C CG  . TYR B 193 ? 1.2262 1.2133 1.3336 -0.3275 -0.0370 -0.0597 195 TYR B CG  
2246  C CD1 . TYR B 193 ? 1.2580 1.2475 1.3395 -0.3458 -0.0045 -0.0830 195 TYR B CD1 
2247  C CD2 . TYR B 193 ? 1.1779 1.1989 1.3461 -0.3380 -0.0480 -0.0479 195 TYR B CD2 
2248  C CE1 . TYR B 193 ? 1.2101 1.2476 1.3289 -0.3705 0.0128  -0.0960 195 TYR B CE1 
2249  C CE2 . TYR B 193 ? 1.1460 1.2061 1.3450 -0.3617 -0.0305 -0.0559 195 TYR B CE2 
2250  C CZ  . TYR B 193 ? 1.1889 1.2631 1.3643 -0.3763 -0.0015 -0.0805 195 TYR B CZ  
2251  O OH  . TYR B 193 ? 1.0757 1.2022 1.2833 -0.3958 0.0132  -0.0932 195 TYR B OH  
2252  N N   . GLN B 194 ? 1.5109 1.3147 1.3785 -0.2341 -0.0113 -0.0225 196 GLN B N   
2253  C CA  . GLN B 194 ? 1.6087 1.3576 1.3888 -0.1926 -0.0127 -0.0166 196 GLN B CA  
2254  C C   . GLN B 194 ? 1.6861 1.4480 1.4608 -0.1790 -0.0489 -0.0363 196 GLN B C   
2255  O O   . GLN B 194 ? 1.7599 1.4643 1.4479 -0.1598 -0.0320 -0.0405 196 GLN B O   
2256  C CB  . GLN B 194 ? 1.6555 1.3975 1.4227 -0.1538 -0.0311 0.0078  196 GLN B CB  
2257  C CG  . GLN B 194 ? 2.0463 1.7052 1.6916 -0.1121 -0.0006 0.0218  196 GLN B CG  
2258  C CD  . GLN B 194 ? 2.3950 2.0329 2.0143 -0.0776 0.0043  0.0500  196 GLN B CD  
2259  O OE1 . GLN B 194 ? 2.3384 2.0337 2.0237 -0.0632 -0.0416 0.0538  196 GLN B OE1 
2260  N NE2 . GLN B 194 ? 2.3577 1.9084 1.8752 -0.0612 0.0633  0.0678  196 GLN B NE2 
2261  N N   . ASN B 195 ? 1.5826 1.4127 1.4443 -0.1899 -0.0929 -0.0487 197 ASN B N   
2262  C CA  . ASN B 195 ? 1.5867 1.4386 1.4590 -0.1840 -0.1251 -0.0689 197 ASN B CA  
2263  C C   . ASN B 195 ? 1.6436 1.4739 1.4953 -0.2125 -0.0959 -0.0880 197 ASN B C   
2264  O O   . ASN B 195 ? 1.5757 1.4414 1.4859 -0.2433 -0.0894 -0.0974 197 ASN B O   
2265  C CB  . ASN B 195 ? 1.5369 1.4616 1.5091 -0.1913 -0.1678 -0.0776 197 ASN B CB  
2266  C CG  . ASN B 195 ? 1.7063 1.6582 1.7037 -0.1650 -0.1975 -0.0700 197 ASN B CG  
2267  O OD1 . ASN B 195 ? 1.5995 1.5829 1.6080 -0.1432 -0.2320 -0.0846 197 ASN B OD1 
2268  N ND2 . ASN B 195 ? 1.5471 1.4930 1.5581 -0.1683 -0.1838 -0.0514 197 ASN B ND2 
2269  N N   . ALA B 196 ? 1.6840 1.4527 1.4467 -0.1999 -0.0754 -0.0950 198 ALA B N   
2270  C CA  . ALA B 196 ? 1.7090 1.4450 1.4394 -0.2263 -0.0423 -0.1190 198 ALA B CA  
2271  C C   . ALA B 196 ? 1.7232 1.5147 1.5257 -0.2460 -0.0725 -0.1400 198 ALA B C   
2272  O O   . ALA B 196 ? 1.6911 1.4981 1.5222 -0.2767 -0.0522 -0.1587 198 ALA B O   
2273  C CB  . ALA B 196 ? 1.8245 1.4753 1.4410 -0.2038 -0.0188 -0.1218 198 ALA B CB  
2274  N N   . ASP B 197 ? 1.6851 1.5113 1.5189 -0.2279 -0.1183 -0.1396 199 ASP B N   
2275  C CA  . ASP B 197 ? 1.6412 1.5175 1.5446 -0.2452 -0.1432 -0.1573 199 ASP B CA  
2276  C C   . ASP B 197 ? 1.6135 1.5540 1.6068 -0.2464 -0.1701 -0.1486 199 ASP B C   
2277  O O   . ASP B 197 ? 1.5920 1.5656 1.6176 -0.2317 -0.2021 -0.1502 199 ASP B O   
2278  C CB  . ASP B 197 ? 1.7143 1.5818 1.5896 -0.2322 -0.1651 -0.1702 199 ASP B CB  
2279  C CG  . ASP B 197 ? 1.8898 1.7891 1.8203 -0.2578 -0.1733 -0.1916 199 ASP B CG  
2280  O OD1 . ASP B 197 ? 1.9288 1.7951 1.8313 -0.2778 -0.1485 -0.2079 199 ASP B OD1 
2281  O OD2 . ASP B 197 ? 1.9456 1.9003 1.9475 -0.2587 -0.2002 -0.1943 199 ASP B OD2 
2282  N N   . ALA B 198 ? 1.5263 1.4829 1.5556 -0.2642 -0.1528 -0.1425 200 ALA B N   
2283  C CA  . ALA B 198 ? 1.4609 1.4644 1.5661 -0.2677 -0.1694 -0.1335 200 ALA B CA  
2284  C C   . ALA B 198 ? 1.4550 1.4930 1.6168 -0.2828 -0.1749 -0.1468 200 ALA B C   
2285  O O   . ALA B 198 ? 1.4493 1.4823 1.5987 -0.2962 -0.1584 -0.1609 200 ALA B O   
2286  C CB  . ALA B 198 ? 1.4557 1.4549 1.5612 -0.2760 -0.1464 -0.1176 200 ALA B CB  
2287  N N   . TYR B 199 ? 1.3701 1.4397 1.5916 -0.2794 -0.1948 -0.1449 201 TYR B N   
2288  C CA  . TYR B 199 ? 1.3355 1.4302 1.6072 -0.2873 -0.1964 -0.1535 201 TYR B CA  
2289  C C   . TYR B 199 ? 1.3094 1.4213 1.6287 -0.2867 -0.1968 -0.1410 201 TYR B C   
2290  O O   . TYR B 199 ? 1.3000 1.4080 1.6231 -0.2829 -0.2011 -0.1294 201 TYR B O   
2291  C CB  . TYR B 199 ? 1.3778 1.4814 1.6669 -0.2848 -0.2114 -0.1698 201 TYR B CB  
2292  C CG  . TYR B 199 ? 1.4221 1.5437 1.7471 -0.2769 -0.2273 -0.1728 201 TYR B CG  
2293  C CD1 . TYR B 199 ? 1.4794 1.6028 1.7806 -0.2634 -0.2434 -0.1758 201 TYR B CD1 
2294  C CD2 . TYR B 199 ? 1.4122 1.5480 1.7918 -0.2809 -0.2231 -0.1767 201 TYR B CD2 
2295  C CE1 . TYR B 199 ? 1.4898 1.6405 1.8300 -0.2571 -0.2577 -0.1878 201 TYR B CE1 
2296  C CE2 . TYR B 199 ? 1.4197 1.5705 1.8340 -0.2783 -0.2310 -0.1883 201 TYR B CE2 
2297  C CZ  . TYR B 199 ? 1.5338 1.6981 1.9329 -0.2679 -0.2496 -0.1967 201 TYR B CZ  
2298  O OH  . TYR B 199 ? 1.5395 1.7293 1.9784 -0.2661 -0.2573 -0.2168 201 TYR B OH  
2299  N N   . VAL B 200 ? 1.2140 1.3406 1.5661 -0.2882 -0.1912 -0.1436 202 VAL B N   
2300  C CA  . VAL B 200 ? 1.1747 1.3076 1.5644 -0.2841 -0.1884 -0.1326 202 VAL B CA  
2301  C C   . VAL B 200 ? 1.1947 1.3282 1.6143 -0.2787 -0.1857 -0.1422 202 VAL B C   
2302  O O   . VAL B 200 ? 1.1911 1.3290 1.6045 -0.2801 -0.1836 -0.1539 202 VAL B O   
2303  C CB  . VAL B 200 ? 1.2069 1.3533 1.5939 -0.2850 -0.1762 -0.1210 202 VAL B CB  
2304  C CG1 . VAL B 200 ? 1.1917 1.3328 1.6060 -0.2807 -0.1749 -0.1061 202 VAL B CG1 
2305  C CG2 . VAL B 200 ? 1.2079 1.3539 1.5583 -0.2957 -0.1667 -0.1190 202 VAL B CG2 
2306  N N   . PHE B 201 ? 1.1332 1.2558 1.5825 -0.2745 -0.1810 -0.1393 203 PHE B N   
2307  C CA  . PHE B 201 ? 1.1366 1.2479 1.6090 -0.2689 -0.1672 -0.1480 203 PHE B CA  
2308  C C   . PHE B 201 ? 1.1824 1.2700 1.6697 -0.2598 -0.1523 -0.1367 203 PHE B C   
2309  O O   . PHE B 201 ? 1.1828 1.2592 1.6812 -0.2662 -0.1542 -0.1359 203 PHE B O   
2310  C CB  . PHE B 201 ? 1.1689 1.2816 1.6579 -0.2783 -0.1685 -0.1718 203 PHE B CB  
2311  C CG  . PHE B 201 ? 1.2067 1.3013 1.7196 -0.2765 -0.1430 -0.1831 203 PHE B CG  
2312  C CD1 . PHE B 201 ? 1.2539 1.3290 1.7918 -0.2805 -0.1262 -0.1958 203 PHE B CD1 
2313  C CD2 . PHE B 201 ? 1.2443 1.3356 1.7526 -0.2705 -0.1300 -0.1820 203 PHE B CD2 
2314  C CE1 . PHE B 201 ? 1.2884 1.3349 1.8408 -0.2793 -0.0915 -0.2076 203 PHE B CE1 
2315  C CE2 . PHE B 201 ? 1.3008 1.3662 1.8248 -0.2663 -0.0987 -0.1896 203 PHE B CE2 
2316  C CZ  . PHE B 201 ? 1.2893 1.3292 1.8324 -0.2710 -0.0770 -0.2021 203 PHE B CZ  
2317  N N   . VAL B 202 ? 1.1326 1.2090 1.6167 -0.2428 -0.1360 -0.1290 204 VAL B N   
2318  C CA  . VAL B 202 ? 1.1399 1.1817 1.6251 -0.2278 -0.1169 -0.1169 204 VAL B CA  
2319  C C   . VAL B 202 ? 1.2395 1.2454 1.7302 -0.2179 -0.0875 -0.1267 204 VAL B C   
2320  O O   . VAL B 202 ? 1.2471 1.2583 1.7281 -0.2019 -0.0800 -0.1237 204 VAL B O   
2321  C CB  . VAL B 202 ? 1.1741 1.2312 1.6395 -0.2083 -0.1207 -0.0954 204 VAL B CB  
2322  C CG1 . VAL B 202 ? 1.2017 1.2143 1.6593 -0.1907 -0.1010 -0.0815 204 VAL B CG1 
2323  C CG2 . VAL B 202 ? 1.1338 1.2254 1.5947 -0.2243 -0.1402 -0.0902 204 VAL B CG2 
2324  N N   . GLY B 203 ? 1.2247 1.1948 1.7318 -0.2291 -0.0675 -0.1420 205 GLY B N   
2325  C CA  . GLY B 203 ? 1.2654 1.1937 1.7779 -0.2264 -0.0282 -0.1580 205 GLY B CA  
2326  C C   . GLY B 203 ? 1.3603 1.2196 1.8573 -0.2116 0.0098  -0.1521 205 GLY B C   
2327  O O   . GLY B 203 ? 1.3487 1.1842 1.8562 -0.2255 0.0159  -0.1619 205 GLY B O   
2328  N N   . SER B 204 ? 1.3690 1.1913 1.8377 -0.1816 0.0382  -0.1374 206 SER B N   
2329  C CA  . SER B 204 ? 1.4366 1.1774 1.8725 -0.1567 0.0837  -0.1280 206 SER B CA  
2330  C C   . SER B 204 ? 1.5411 1.2443 1.9708 -0.1499 0.1303  -0.1411 206 SER B C   
2331  O O   . SER B 204 ? 1.5058 1.2557 1.9599 -0.1653 0.1186  -0.1541 206 SER B O   
2332  C CB  . SER B 204 ? 1.4990 1.2403 1.8945 -0.1147 0.0692  -0.0908 206 SER B CB  
2333  O OG  . SER B 204 ? 1.6990 1.3589 2.0475 -0.0773 0.1138  -0.0762 206 SER B OG  
2334  N N   . SER B 205 ? 1.5843 1.1984 1.9784 -0.1283 0.1870  -0.1385 207 SER B N   
2335  C CA  . SER B 205 ? 1.6427 1.2145 2.0263 -0.1207 0.2399  -0.1491 207 SER B CA  
2336  C C   . SER B 205 ? 1.7013 1.2989 2.0604 -0.0794 0.2244  -0.1180 207 SER B C   
2337  O O   . SER B 205 ? 1.7032 1.3200 2.0791 -0.0876 0.2359  -0.1283 207 SER B O   
2338  C CB  . SER B 205 ? 1.7975 1.2546 2.1406 -0.1077 0.3143  -0.1563 207 SER B CB  
2339  O OG  . SER B 205 ? 1.9293 1.3687 2.3063 -0.1539 0.3383  -0.2000 207 SER B OG  
2340  N N   . ARG B 206 ? 1.6507 1.2585 1.9749 -0.0376 0.1958  -0.0840 208 ARG B N   
2341  C CA  . ARG B 206 ? 1.6493 1.2958 1.9532 0.0054  0.1759  -0.0599 208 ARG B CA  
2342  C C   . ARG B 206 ? 1.5922 1.3472 1.9350 -0.0147 0.1114  -0.0641 208 ARG B C   
2343  O O   . ARG B 206 ? 1.5740 1.3697 1.9245 -0.0044 0.1009  -0.0643 208 ARG B O   
2344  C CB  . ARG B 206 ? 1.7347 1.3395 1.9753 0.0688  0.1854  -0.0264 208 ARG B CB  
2345  C CG  . ARG B 206 ? 1.8716 1.4901 2.1012 0.0712  0.1536  -0.0140 208 ARG B CG  
2346  C CD  . ARG B 206 ? 2.0488 1.6703 2.2226 0.1383  0.1440  0.0178  208 ARG B CD  
2347  N NE  . ARG B 206 ? 2.2282 1.7336 2.3317 0.1847  0.2013  0.0358  208 ARG B NE  
2348  C CZ  . ARG B 206 ? 2.4201 1.9074 2.4592 0.2555  0.2050  0.0650  208 ARG B CZ  
2349  N NH1 . ARG B 206 ? 2.2061 1.7966 2.2503 0.2864  0.1530  0.0748  208 ARG B NH1 
2350  N NH2 . ARG B 206 ? 2.3240 1.6897 2.2897 0.2977  0.2636  0.0813  208 ARG B NH2 
2351  N N   . TYR B 207 ? 1.4847 1.2798 1.8501 -0.0451 0.0739  -0.0697 209 TYR B N   
2352  C CA  . TYR B 207 ? 1.4100 1.2936 1.8030 -0.0660 0.0221  -0.0753 209 TYR B CA  
2353  C C   . TYR B 207 ? 1.4185 1.3260 1.8515 -0.1170 0.0102  -0.1017 209 TYR B C   
2354  O O   . TYR B 207 ? 1.4162 1.2940 1.8629 -0.1416 0.0232  -0.1152 209 TYR B O   
2355  C CB  . TYR B 207 ? 1.3968 1.3104 1.7806 -0.0607 -0.0084 -0.0612 209 TYR B CB  
2356  C CG  . TYR B 207 ? 1.3565 1.3549 1.7580 -0.0762 -0.0509 -0.0673 209 TYR B CG  
2357  C CD1 . TYR B 207 ? 1.3325 1.3568 1.7598 -0.1195 -0.0716 -0.0818 209 TYR B CD1 
2358  C CD2 . TYR B 207 ? 1.3648 1.4164 1.7535 -0.0456 -0.0666 -0.0619 209 TYR B CD2 
2359  C CE1 . TYR B 207 ? 1.2976 1.3850 1.7316 -0.1339 -0.1003 -0.0892 209 TYR B CE1 
2360  C CE2 . TYR B 207 ? 1.3254 1.4506 1.7293 -0.0643 -0.0964 -0.0754 209 TYR B CE2 
2361  C CZ  . TYR B 207 ? 1.3522 1.4882 1.7755 -0.1095 -0.1099 -0.0881 209 TYR B CZ  
2362  O OH  . TYR B 207 ? 1.2920 1.4863 1.7209 -0.1278 -0.1297 -0.1027 209 TYR B OH  
2363  N N   . SER B 208 ? 1.3445 1.3081 1.7938 -0.1315 -0.0157 -0.1115 210 SER B N   
2364  C CA  . SER B 208 ? 1.3139 1.3050 1.7906 -0.1732 -0.0325 -0.1342 210 SER B CA  
2365  C C   . SER B 208 ? 1.3487 1.3962 1.8266 -0.1818 -0.0648 -0.1386 210 SER B C   
2366  O O   . SER B 208 ? 1.3522 1.4112 1.8306 -0.1748 -0.0597 -0.1432 210 SER B O   
2367  C CB  . SER B 208 ? 1.3922 1.3552 1.8870 -0.1915 -0.0002 -0.1555 210 SER B CB  
2368  O OG  . SER B 208 ? 1.5425 1.4719 2.0482 -0.2064 0.0200  -0.1687 210 SER B OG  
2369  N N   . LYS B 209 ? 1.2873 1.3646 1.7630 -0.1973 -0.0936 -0.1387 211 LYS B N   
2370  C CA  . LYS B 209 ? 1.2644 1.3849 1.7334 -0.2090 -0.1168 -0.1468 211 LYS B CA  
2371  C C   . LYS B 209 ? 1.2912 1.4216 1.7557 -0.2348 -0.1363 -0.1529 211 LYS B C   
2372  O O   . LYS B 209 ? 1.2752 1.3964 1.7406 -0.2369 -0.1404 -0.1439 211 LYS B O   
2373  C CB  . LYS B 209 ? 1.2947 1.4491 1.7509 -0.1856 -0.1237 -0.1386 211 LYS B CB  
2374  C CG  . LYS B 209 ? 1.5177 1.7049 1.9738 -0.1849 -0.1271 -0.1553 211 LYS B CG  
2375  C CD  . LYS B 209 ? 1.6230 1.8421 2.0689 -0.2096 -0.1421 -0.1720 211 LYS B CD  
2376  C CE  . LYS B 209 ? 1.7380 1.9777 2.1851 -0.2176 -0.1409 -0.1960 211 LYS B CE  
2377  N NZ  . LYS B 209 ? 1.7954 2.0503 2.2241 -0.2446 -0.1462 -0.2163 211 LYS B NZ  
2378  N N   . THR B 210 ? 1.2433 1.3875 1.6992 -0.2526 -0.1461 -0.1682 212 THR B N   
2379  C CA  . THR B 210 ? 1.2329 1.3797 1.6709 -0.2708 -0.1615 -0.1736 212 THR B CA  
2380  C C   . THR B 210 ? 1.2769 1.4428 1.6894 -0.2737 -0.1649 -0.1752 212 THR B C   
2381  O O   . THR B 210 ? 1.2760 1.4589 1.6882 -0.2704 -0.1593 -0.1854 212 THR B O   
2382  C CB  . THR B 210 ? 1.3365 1.4765 1.7727 -0.2869 -0.1649 -0.1917 212 THR B CB  
2383  O OG1 . THR B 210 ? 1.3218 1.4524 1.7878 -0.2867 -0.1513 -0.1981 212 THR B OG1 
2384  C CG2 . THR B 210 ? 1.3203 1.4574 1.7346 -0.2953 -0.1809 -0.1946 212 THR B CG2 
2385  N N   . PHE B 211 ? 1.2365 1.4006 1.6288 -0.2806 -0.1701 -0.1689 213 PHE B N   
2386  C CA  . PHE B 211 ? 1.2424 1.4211 1.6083 -0.2880 -0.1635 -0.1750 213 PHE B CA  
2387  C C   . PHE B 211 ? 1.3194 1.4730 1.6437 -0.3022 -0.1625 -0.1802 213 PHE B C   
2388  O O   . PHE B 211 ? 1.3259 1.4600 1.6437 -0.3003 -0.1727 -0.1712 213 PHE B O   
2389  C CB  . PHE B 211 ? 1.2501 1.4490 1.6246 -0.2810 -0.1595 -0.1605 213 PHE B CB  
2390  C CG  . PHE B 211 ? 1.2645 1.4777 1.6676 -0.2596 -0.1598 -0.1500 213 PHE B CG  
2391  C CD1 . PHE B 211 ? 1.3069 1.5550 1.7160 -0.2453 -0.1555 -0.1600 213 PHE B CD1 
2392  C CD2 . PHE B 211 ? 1.2927 1.4820 1.7123 -0.2511 -0.1620 -0.1322 213 PHE B CD2 
2393  C CE1 . PHE B 211 ? 1.3255 1.5803 1.7494 -0.2169 -0.1543 -0.1471 213 PHE B CE1 
2394  C CE2 . PHE B 211 ? 1.3367 1.5243 1.7698 -0.2281 -0.1560 -0.1214 213 PHE B CE2 
2395  C CZ  . PHE B 211 ? 1.3199 1.5384 1.7513 -0.2082 -0.1526 -0.1263 213 PHE B CZ  
2396  N N   . LYS B 212 ? 1.2838 1.4377 1.5770 -0.3142 -0.1471 -0.1976 214 LYS B N   
2397  C CA  . LYS B 212 ? 1.3125 1.4299 1.5510 -0.3252 -0.1353 -0.2037 214 LYS B CA  
2398  C C   . LYS B 212 ? 1.3426 1.4722 1.5606 -0.3385 -0.1070 -0.2185 214 LYS B C   
2399  O O   . LYS B 212 ? 1.3084 1.4791 1.5522 -0.3413 -0.1007 -0.2365 214 LYS B O   
2400  C CB  . LYS B 212 ? 1.3871 1.4747 1.5981 -0.3316 -0.1367 -0.2209 214 LYS B CB  
2401  C CG  . LYS B 212 ? 1.6359 1.6876 1.8122 -0.3234 -0.1492 -0.2100 214 LYS B CG  
2402  C CD  . LYS B 212 ? 1.8177 1.8414 1.9641 -0.3291 -0.1517 -0.2271 214 LYS B CD  
2403  C CE  . LYS B 212 ? 2.0047 2.0055 2.1166 -0.3140 -0.1685 -0.2178 214 LYS B CE  
2404  N NZ  . LYS B 212 ? 2.1421 2.1251 2.2324 -0.3188 -0.1750 -0.2342 214 LYS B NZ  
2405  N N   . PRO B 213 ? 1.1443 1.7038 1.1184 -0.2203 0.2199  -0.1857 215 PRO B N   
2406  C CA  . PRO B 213 ? 1.1680 1.6747 1.1448 -0.2156 0.1720  -0.1571 215 PRO B CA  
2407  C C   . PRO B 213 ? 1.1778 1.6969 1.2148 -0.2145 0.1538  -0.1243 215 PRO B C   
2408  O O   . PRO B 213 ? 1.1372 1.7110 1.2136 -0.2109 0.1664  -0.1222 215 PRO B O   
2409  C CB  . PRO B 213 ? 1.2084 1.7161 1.1527 -0.2019 0.1574  -0.1757 215 PRO B CB  
2410  C CG  . PRO B 213 ? 1.2356 1.8136 1.1850 -0.1910 0.1913  -0.2036 215 PRO B CG  
2411  C CD  . PRO B 213 ? 1.1551 1.7646 1.1115 -0.2057 0.2359  -0.2185 215 PRO B CD  
2412  N N   . GLU B 214 ? 1.1452 1.6158 1.1862 -0.2191 0.1245  -0.1034 216 GLU B N   
2413  C CA  . GLU B 214 ? 1.1270 1.6027 1.2143 -0.2227 0.1036  -0.0818 216 GLU B CA  
2414  C C   . GLU B 214 ? 1.1753 1.6263 1.2477 -0.2147 0.0780  -0.0736 216 GLU B C   
2415  O O   . GLU B 214 ? 1.2038 1.6100 1.2584 -0.2137 0.0547  -0.0666 216 GLU B O   
2416  C CB  . GLU B 214 ? 1.1687 1.6089 1.2608 -0.2283 0.0872  -0.0733 216 GLU B CB  
2417  C CG  . GLU B 214 ? 1.3378 1.7960 1.4473 -0.2358 0.1089  -0.0787 216 GLU B CG  
2418  C CD  . GLU B 214 ? 1.7093 2.1354 1.8270 -0.2360 0.0860  -0.0721 216 GLU B CD  
2419  O OE1 . GLU B 214 ? 1.7782 2.1454 1.8527 -0.2276 0.0656  -0.0692 216 GLU B OE1 
2420  O OE2 . GLU B 214 ? 1.5798 2.0448 1.7494 -0.2440 0.0872  -0.0727 216 GLU B OE2 
2421  N N   . ILE B 215 ? 1.1038 1.5839 1.1800 -0.2075 0.0846  -0.0759 217 ILE B N   
2422  C CA  . ILE B 215 ? 1.1287 1.5799 1.1828 -0.1984 0.0632  -0.0688 217 ILE B CA  
2423  C C   . ILE B 215 ? 1.1954 1.6317 1.2729 -0.2111 0.0461  -0.0516 217 ILE B C   
2424  O O   . ILE B 215 ? 1.1647 1.6344 1.2743 -0.2216 0.0528  -0.0475 217 ILE B O   
2425  C CB  . ILE B 215 ? 1.1658 1.6434 1.2016 -0.1809 0.0735  -0.0808 217 ILE B CB  
2426  C CG1 . ILE B 215 ? 1.1820 1.6684 1.1809 -0.1697 0.0851  -0.1101 217 ILE B CG1 
2427  C CG2 . ILE B 215 ? 1.2094 1.6485 1.2203 -0.1713 0.0502  -0.0697 217 ILE B CG2 
2428  C CD1 . ILE B 215 ? 1.2873 1.8305 1.2805 -0.1539 0.1108  -0.1349 217 ILE B CD1 
2429  N N   . ALA B 216 ? 1.1933 1.5850 1.2551 -0.2130 0.0258  -0.0463 218 ALA B N   
2430  C CA  . ALA B 216 ? 1.2053 1.5793 1.2773 -0.2263 0.0117  -0.0402 218 ALA B CA  
2431  C C   . ALA B 216 ? 1.2907 1.6218 1.3363 -0.2212 -0.0030 -0.0387 218 ALA B C   
2432  O O   . ALA B 216 ? 1.2911 1.6114 1.3274 -0.2134 -0.0065 -0.0413 218 ALA B O   
2433  C CB  . ALA B 216 ? 1.1904 1.5880 1.3001 -0.2404 0.0108  -0.0455 218 ALA B CB  
2434  N N   . ILE B 217 ? 1.2782 1.5867 1.3113 -0.2286 -0.0091 -0.0362 219 ILE B N   
2435  C CA  . ILE B 217 ? 1.3080 1.5855 1.3234 -0.2265 -0.0170 -0.0368 219 ILE B CA  
2436  C C   . ILE B 217 ? 1.3517 1.6390 1.3870 -0.2339 -0.0207 -0.0477 219 ILE B C   
2437  O O   . ILE B 217 ? 1.3499 1.6507 1.3983 -0.2495 -0.0206 -0.0588 219 ILE B O   
2438  C CB  . ILE B 217 ? 1.3878 1.6325 1.3734 -0.2324 -0.0163 -0.0333 219 ILE B CB  
2439  C CG1 . ILE B 217 ? 1.4200 1.6464 1.3772 -0.2142 -0.0195 -0.0252 219 ILE B CG1 
2440  C CG2 . ILE B 217 ? 1.4122 1.6375 1.3896 -0.2389 -0.0160 -0.0403 219 ILE B CG2 
2441  C CD1 . ILE B 217 ? 1.5731 1.7574 1.4900 -0.2167 -0.0191 -0.0189 219 ILE B CD1 
2442  N N   . ARG B 218 ? 1.2974 1.5808 1.3335 -0.2229 -0.0258 -0.0485 220 ARG B N   
2443  C CA  . ARG B 218 ? 1.2866 1.5771 1.3346 -0.2214 -0.0315 -0.0604 220 ARG B CA  
2444  C C   . ARG B 218 ? 1.3456 1.6287 1.3872 -0.2193 -0.0307 -0.0663 220 ARG B C   
2445  O O   . ARG B 218 ? 1.3532 1.6231 1.3839 -0.2193 -0.0272 -0.0576 220 ARG B O   
2446  C CB  . ARG B 218 ? 1.2635 1.5522 1.3116 -0.2101 -0.0360 -0.0570 220 ARG B CB  
2447  C CG  . ARG B 218 ? 1.3128 1.6149 1.3717 -0.2129 -0.0318 -0.0568 220 ARG B CG  
2448  C CD  . ARG B 218 ? 1.3648 1.6647 1.4095 -0.2108 -0.0214 -0.0490 220 ARG B CD  
2449  N NE  . ARG B 218 ? 1.3676 1.6830 1.4213 -0.2130 -0.0106 -0.0511 220 ARG B NE  
2450  C CZ  . ARG B 218 ? 1.4462 1.7733 1.4904 -0.2133 0.0060  -0.0526 220 ARG B CZ  
2451  N NH1 . ARG B 218 ? 1.1910 1.5156 1.2145 -0.2095 0.0086  -0.0547 220 ARG B NH1 
2452  N NH2 . ARG B 218 ? 1.2825 1.6282 1.3379 -0.2170 0.0214  -0.0565 220 ARG B NH2 
2453  N N   . PRO B 219 ? 1.2924 1.5884 1.3417 -0.2155 -0.0329 -0.0839 221 PRO B N   
2454  C CA  . PRO B 219 ? 1.2917 1.5931 1.3407 -0.2130 -0.0255 -0.0920 221 PRO B CA  
2455  C C   . PRO B 219 ? 1.3388 1.6366 1.3932 -0.2038 -0.0287 -0.0755 221 PRO B C   
2456  O O   . PRO B 219 ? 1.3369 1.6278 1.3896 -0.1970 -0.0388 -0.0661 221 PRO B O   
2457  C CB  . PRO B 219 ? 1.3112 1.6356 1.3671 -0.2048 -0.0287 -0.1190 221 PRO B CB  
2458  C CG  . PRO B 219 ? 1.3674 1.6876 1.4262 -0.1964 -0.0441 -0.1155 221 PRO B CG  
2459  C CD  . PRO B 219 ? 1.3068 1.6179 1.3660 -0.2109 -0.0421 -0.1009 221 PRO B CD  
2460  N N   . LYS B 220 ? 1.2877 1.5910 1.3477 -0.2075 -0.0193 -0.0748 222 LYS B N   
2461  C CA  . LYS B 220 ? 1.2659 1.5766 1.3406 -0.2047 -0.0244 -0.0637 222 LYS B CA  
2462  C C   . LYS B 220 ? 1.3011 1.6339 1.3930 -0.1954 -0.0291 -0.0688 222 LYS B C   
2463  O O   . LYS B 220 ? 1.2816 1.6448 1.3946 -0.1928 -0.0183 -0.0791 222 LYS B O   
2464  C CB  . LYS B 220 ? 1.2903 1.6052 1.3726 -0.2122 -0.0133 -0.0625 222 LYS B CB  
2465  C CG  . LYS B 220 ? 1.5261 1.8151 1.5917 -0.2145 -0.0221 -0.0499 222 LYS B CG  
2466  C CD  . LYS B 220 ? 1.6787 1.9723 1.7562 -0.2188 -0.0172 -0.0483 222 LYS B CD  
2467  C CE  . LYS B 220 ? 1.9011 2.1655 1.9547 -0.2154 -0.0299 -0.0409 222 LYS B CE  
2468  N NZ  . LYS B 220 ? 2.0206 2.2975 2.0808 -0.2116 -0.0517 -0.0426 222 LYS B NZ  
2469  N N   . VAL B 221 ? 1.2649 1.5813 1.3435 -0.1901 -0.0428 -0.0629 223 VAL B N   
2470  C CA  . VAL B 221 ? 1.2595 1.5800 1.3392 -0.1809 -0.0511 -0.0644 223 VAL B CA  
2471  C C   . VAL B 221 ? 1.2678 1.5910 1.3552 -0.1940 -0.0584 -0.0553 223 VAL B C   
2472  O O   . VAL B 221 ? 1.2798 1.5827 1.3484 -0.2035 -0.0644 -0.0510 223 VAL B O   
2473  C CB  . VAL B 221 ? 1.3454 1.6360 1.3961 -0.1708 -0.0609 -0.0649 223 VAL B CB  
2474  C CG1 . VAL B 221 ? 1.3605 1.6379 1.3968 -0.1618 -0.0714 -0.0631 223 VAL B CG1 
2475  C CG2 . VAL B 221 ? 1.3509 1.6502 1.4021 -0.1607 -0.0585 -0.0816 223 VAL B CG2 
2476  N N   . ARG B 222 ? 1.1657 1.5235 1.2850 -0.1965 -0.0563 -0.0576 224 ARG B N   
2477  C CA  . ARG B 222 ? 1.1254 1.5016 1.2660 -0.2148 -0.0649 -0.0548 224 ARG B CA  
2478  C C   . ARG B 222 ? 1.1451 1.5216 1.2912 -0.2253 -0.0650 -0.0541 224 ARG B C   
2479  O O   . ARG B 222 ? 1.1214 1.4920 1.2590 -0.2385 -0.0784 -0.0577 224 ARG B O   
2480  C CB  . ARG B 222 ? 1.1379 1.4881 1.2493 -0.2244 -0.0807 -0.0542 224 ARG B CB  
2481  C CG  . ARG B 222 ? 1.2256 1.5802 1.3369 -0.2140 -0.0830 -0.0538 224 ARG B CG  
2482  C CD  . ARG B 222 ? 1.2398 1.5648 1.3181 -0.2299 -0.0977 -0.0536 224 ARG B CD  
2483  N NE  . ARG B 222 ? 1.2721 1.6282 1.3780 -0.2618 -0.1066 -0.0604 224 ARG B NE  
2484  C CZ  . ARG B 222 ? 1.4298 1.8384 1.5864 -0.2735 -0.1091 -0.0620 224 ARG B CZ  
2485  N NH1 . ARG B 222 ? 1.2864 1.7236 1.4689 -0.2525 -0.0997 -0.0574 224 ARG B NH1 
2486  N NH2 . ARG B 222 ? 1.2408 1.6821 1.4264 -0.3066 -0.1209 -0.0727 224 ARG B NH2 
2487  N N   . ASP B 223 ? 1.1162 1.4963 1.2687 -0.2184 -0.0497 -0.0541 225 ASP B N   
2488  C CA  . ASP B 223 ? 1.1258 1.4945 1.2727 -0.2217 -0.0460 -0.0521 225 ASP B CA  
2489  C C   . ASP B 223 ? 1.2020 1.5391 1.3146 -0.2220 -0.0601 -0.0505 225 ASP B C   
2490  O O   . ASP B 223 ? 1.2005 1.5361 1.3116 -0.2251 -0.0685 -0.0531 225 ASP B O   
2491  C CB  . ASP B 223 ? 1.1119 1.5155 1.2997 -0.2312 -0.0424 -0.0541 225 ASP B CB  
2492  C CG  . ASP B 223 ? 1.1519 1.5708 1.3533 -0.2290 -0.0148 -0.0583 225 ASP B CG  
2493  O OD1 . ASP B 223 ? 1.0970 1.5476 1.3177 -0.2245 -0.0003 -0.0665 225 ASP B OD1 
2494  O OD2 . ASP B 223 ? 1.2510 1.6480 1.4370 -0.2312 -0.0062 -0.0567 225 ASP B OD2 
2495  N N   . ARG B 224 ? 1.1739 1.4894 1.2589 -0.2168 -0.0611 -0.0496 226 ARG B N   
2496  C CA  . ARG B 224 ? 1.1836 1.4785 1.2373 -0.2158 -0.0660 -0.0518 226 ARG B CA  
2497  C C   . ARG B 224 ? 1.2501 1.5285 1.2882 -0.2082 -0.0555 -0.0467 226 ARG B C   
2498  O O   . ARG B 224 ? 1.2425 1.5198 1.2832 -0.2049 -0.0517 -0.0464 226 ARG B O   
2499  C CB  . ARG B 224 ? 1.1451 1.4367 1.1823 -0.2239 -0.0741 -0.0604 226 ARG B CB  
2500  C CG  . ARG B 224 ? 1.1524 1.4625 1.1969 -0.2386 -0.0885 -0.0749 226 ARG B CG  
2501  C CD  . ARG B 224 ? 1.2037 1.5155 1.2304 -0.2363 -0.0945 -0.0893 226 ARG B CD  
2502  N NE  . ARG B 224 ? 1.2438 1.5818 1.2948 -0.2454 -0.1114 -0.1022 226 ARG B NE  
2503  C CZ  . ARG B 224 ? 1.4192 1.7627 1.4919 -0.2374 -0.1134 -0.0945 226 ARG B CZ  
2504  N NH1 . ARG B 224 ? 1.3219 1.6425 1.3875 -0.2230 -0.0984 -0.0756 226 ARG B NH1 
2505  N NH2 . ARG B 224 ? 1.2093 1.5804 1.3086 -0.2467 -0.1305 -0.1084 226 ARG B NH2 
2506  N N   . GLU B 225 ? 1.4394 1.5133 1.5483 -0.4559 0.1111  -0.0068 227 GLU B N   
2507  C CA  . GLU B 225 ? 1.4364 1.5551 1.5585 -0.4362 0.1438  0.0162  227 GLU B CA  
2508  C C   . GLU B 225 ? 1.4577 1.5900 1.5384 -0.3937 0.1428  0.0053  227 GLU B C   
2509  O O   . GLU B 225 ? 1.4537 1.6373 1.5569 -0.3764 0.1611  0.0121  227 GLU B O   
2510  C CB  . GLU B 225 ? 1.4948 1.5807 1.5978 -0.4406 0.1766  0.0440  227 GLU B CB  
2511  C CG  . GLU B 225 ? 1.6837 1.7632 1.8435 -0.4836 0.1861  0.0591  227 GLU B CG  
2512  C CD  . GLU B 225 ? 2.1346 2.2334 2.3187 -0.4878 0.2304  0.0978  227 GLU B CD  
2513  O OE1 . GLU B 225 ? 2.1630 2.2264 2.2920 -0.4680 0.2527  0.1182  227 GLU B OE1 
2514  O OE2 . GLU B 225 ? 2.1078 2.2592 2.3688 -0.5112 0.2427  0.1105  227 GLU B OE2 
2515  N N   . GLY B 226 ? 1.3858 1.4710 1.4117 -0.3782 0.1236  -0.0119 228 GLY B N   
2516  C CA  . GLY B 226 ? 1.3542 1.4422 1.3429 -0.3428 0.1178  -0.0258 228 GLY B CA  
2517  C C   . GLY B 226 ? 1.3524 1.4671 1.3669 -0.3366 0.0939  -0.0447 228 GLY B C   
2518  O O   . GLY B 226 ? 1.3477 1.4794 1.4021 -0.3599 0.0767  -0.0473 228 GLY B O   
2519  N N   . ARG B 227 ? 1.2656 1.3829 1.2567 -0.3056 0.0911  -0.0573 229 ARG B N   
2520  C CA  . ARG B 227 ? 1.2139 1.3521 1.2281 -0.2941 0.0712  -0.0709 229 ARG B CA  
2521  C C   . ARG B 227 ? 1.2349 1.3331 1.2061 -0.2726 0.0572  -0.0879 229 ARG B C   
2522  O O   . ARG B 227 ? 1.2240 1.2891 1.1522 -0.2628 0.0631  -0.0905 229 ARG B O   
2523  C CB  . ARG B 227 ? 1.1643 1.3612 1.2231 -0.2766 0.0890  -0.0657 229 ARG B CB  
2524  C CG  . ARG B 227 ? 1.1902 1.4394 1.3108 -0.2973 0.1047  -0.0456 229 ARG B CG  
2525  C CD  . ARG B 227 ? 1.1836 1.4697 1.3649 -0.3190 0.0761  -0.0428 229 ARG B CD  
2526  N NE  . ARG B 227 ? 1.2232 1.5706 1.4796 -0.3365 0.0917  -0.0225 229 ARG B NE  
2527  C CZ  . ARG B 227 ? 1.4363 1.7825 1.7143 -0.3726 0.0944  -0.0113 229 ARG B CZ  
2528  N NH1 . ARG B 227 ? 1.2356 1.5184 1.4621 -0.3926 0.0834  -0.0195 229 ARG B NH1 
2529  N NH2 . ARG B 227 ? 1.3741 1.7813 1.7317 -0.3887 0.1104  0.0093  229 ARG B NH2 
2530  N N   . MET B 228 ? 1.1856 1.2890 1.1723 -0.2662 0.0373  -0.0966 230 MET B N   
2531  C CA  . MET B 228 ? 1.1842 1.2531 1.1436 -0.2475 0.0257  -0.1099 230 MET B CA  
2532  C C   . MET B 228 ? 1.2166 1.3138 1.2068 -0.2259 0.0226  -0.1135 230 MET B C   
2533  O O   . MET B 228 ? 1.2061 1.3321 1.2303 -0.2319 0.0090  -0.1061 230 MET B O   
2534  C CB  . MET B 228 ? 1.2193 1.2510 1.1605 -0.2624 0.0067  -0.1126 230 MET B CB  
2535  C CG  . MET B 228 ? 1.2823 1.2644 1.1861 -0.2628 0.0096  -0.1156 230 MET B CG  
2536  S SD  . MET B 228 ? 1.3477 1.2841 1.2313 -0.2722 -0.0036 -0.1203 230 MET B SD  
2537  C CE  . MET B 228 ? 1.3232 1.2173 1.1845 -0.2829 0.0083  -0.1152 230 MET B CE  
2538  N N   . ASN B 229 ? 1.1733 1.2608 1.1518 -0.2009 0.0333  -0.1248 231 ASN B N   
2539  C CA  . ASN B 229 ? 1.1714 1.2753 1.1813 -0.1776 0.0334  -0.1286 231 ASN B CA  
2540  C C   . ASN B 229 ? 1.2110 1.2770 1.2098 -0.1724 0.0142  -0.1339 231 ASN B C   
2541  O O   . ASN B 229 ? 1.2231 1.2477 1.1874 -0.1756 0.0100  -0.1429 231 ASN B O   
2542  C CB  . ASN B 229 ? 1.2147 1.3208 1.2178 -0.1534 0.0577  -0.1416 231 ASN B CB  
2543  C CG  . ASN B 229 ? 1.7131 1.8666 1.7419 -0.1513 0.0841  -0.1317 231 ASN B CG  
2544  O OD1 . ASN B 229 ? 1.6339 1.8317 1.7097 -0.1650 0.0818  -0.1130 231 ASN B OD1 
2545  N ND2 . ASN B 229 ? 1.7174 1.8630 1.7162 -0.1346 0.1101  -0.1441 231 ASN B ND2 
2546  N N   . TYR B 230 ? 1.1258 1.2086 1.1569 -0.1650 0.0025  -0.1241 232 TYR B N   
2547  C CA  . TYR B 230 ? 1.1051 1.1536 1.1268 -0.1593 -0.0116 -0.1230 232 TYR B CA  
2548  C C   . TYR B 230 ? 1.1740 1.2143 1.2207 -0.1307 -0.0040 -0.1277 232 TYR B C   
2549  O O   . TYR B 230 ? 1.1806 1.2560 1.2690 -0.1150 -0.0006 -0.1176 232 TYR B O   
2550  C CB  . TYR B 230 ? 1.1113 1.1749 1.1367 -0.1732 -0.0323 -0.1060 232 TYR B CB  
2551  C CG  . TYR B 230 ? 1.1209 1.1889 1.1250 -0.2034 -0.0385 -0.1055 232 TYR B CG  
2552  C CD1 . TYR B 230 ? 1.1465 1.1689 1.1078 -0.2176 -0.0365 -0.1134 232 TYR B CD1 
2553  C CD2 . TYR B 230 ? 1.1308 1.2479 1.1654 -0.2177 -0.0444 -0.0967 232 TYR B CD2 
2554  C CE1 . TYR B 230 ? 1.1550 1.1728 1.0988 -0.2442 -0.0386 -0.1141 232 TYR B CE1 
2555  C CE2 . TYR B 230 ? 1.1541 1.2689 1.1732 -0.2483 -0.0491 -0.0981 232 TYR B CE2 
2556  C CZ  . TYR B 230 ? 1.2471 1.3082 1.2179 -0.2608 -0.0453 -0.1077 232 TYR B CZ  
2557  O OH  . TYR B 230 ? 1.2836 1.3338 1.2407 -0.2896 -0.0465 -0.1099 232 TYR B OH  
2558  N N   . TYR B 231 ? 1.1480 1.1420 1.1755 -0.1242 -0.0012 -0.1429 233 TYR B N   
2559  C CA  . TYR B 231 ? 1.1717 1.1432 1.2206 -0.1003 0.0067  -0.1527 233 TYR B CA  
2560  C C   . TYR B 231 ? 1.2548 1.1922 1.3111 -0.0977 -0.0030 -0.1423 233 TYR B C   
2561  O O   . TYR B 231 ? 1.2317 1.1505 1.2644 -0.1142 -0.0118 -0.1365 233 TYR B O   
2562  C CB  . TYR B 231 ? 1.2005 1.1443 1.2248 -0.0966 0.0166  -0.1816 233 TYR B CB  
2563  C CG  . TYR B 231 ? 1.2260 1.1978 1.2340 -0.0954 0.0325  -0.1907 233 TYR B CG  
2564  C CD1 . TYR B 231 ? 1.2367 1.2203 1.2126 -0.1155 0.0302  -0.1867 233 TYR B CD1 
2565  C CD2 . TYR B 231 ? 1.2671 1.2483 1.2904 -0.0724 0.0544  -0.2026 233 TYR B CD2 
2566  C CE1 . TYR B 231 ? 1.2530 1.2607 1.2122 -0.1141 0.0487  -0.1904 233 TYR B CE1 
2567  C CE2 . TYR B 231 ? 1.3001 1.3058 1.3044 -0.0697 0.0755  -0.2091 233 TYR B CE2 
2568  C CZ  . TYR B 231 ? 1.3692 1.3896 1.3412 -0.0913 0.0723  -0.2011 233 TYR B CZ  
2569  O OH  . TYR B 231 ? 1.4216 1.4654 1.3738 -0.0889 0.0964  -0.2024 233 TYR B OH  
2570  N N   . TRP B 232 ? 1.2645 1.1910 1.3556 -0.0751 0.0029  -0.1383 234 TRP B N   
2571  C CA  . TRP B 232 ? 1.2892 1.1827 1.3927 -0.0699 -0.0015 -0.1231 234 TRP B CA  
2572  C C   . TRP B 232 ? 1.3760 1.2327 1.5131 -0.0491 0.0105  -0.1341 234 TRP B C   
2573  O O   . TRP B 232 ? 1.3814 1.2469 1.5402 -0.0304 0.0230  -0.1458 234 TRP B O   
2574  C CB  . TRP B 232 ? 1.2831 1.2058 1.3955 -0.0660 -0.0124 -0.0889 234 TRP B CB  
2575  C CG  . TRP B 232 ? 1.3143 1.2690 1.4734 -0.0406 -0.0087 -0.0749 234 TRP B CG  
2576  C CD1 . TRP B 232 ? 1.3452 1.3537 1.5258 -0.0368 -0.0084 -0.0725 234 TRP B CD1 
2577  C CD2 . TRP B 232 ? 1.3420 1.2767 1.5416 -0.0138 -0.0013 -0.0593 234 TRP B CD2 
2578  N NE1 . TRP B 232 ? 1.3572 1.3843 1.5920 -0.0074 -0.0015 -0.0560 234 TRP B NE1 
2579  C CE2 . TRP B 232 ? 1.4002 1.3798 1.6456 0.0080  0.0028  -0.0479 234 TRP B CE2 
2580  C CE3 . TRP B 232 ? 1.3804 1.2631 1.5888 -0.0056 0.0045  -0.0514 234 TRP B CE3 
2581  C CZ2 . TRP B 232 ? 1.4235 1.3951 1.7209 0.0401  0.0121  -0.0287 234 TRP B CZ2 
2582  C CZ3 . TRP B 232 ? 1.4311 1.3027 1.6878 0.0236  0.0135  -0.0322 234 TRP B CZ3 
2583  C CH2 . TRP B 232 ? 1.4478 1.3626 1.7474 0.0473  0.0168  -0.0207 234 TRP B CH2 
2584  N N   . THR B 233 ? 1.3618 1.1755 1.5071 -0.0519 0.0095  -0.1287 235 THR B N   
2585  C CA  . THR B 233 ? 1.4008 1.1701 1.5840 -0.0363 0.0200  -0.1360 235 THR B CA  
2586  C C   . THR B 233 ? 1.4712 1.2102 1.6720 -0.0373 0.0207  -0.1075 235 THR B C   
2587  O O   . THR B 233 ? 1.4378 1.1823 1.6132 -0.0527 0.0147  -0.0905 235 THR B O   
2588  C CB  . THR B 233 ? 1.5210 1.2570 1.6979 -0.0434 0.0219  -0.1788 235 THR B CB  
2589  O OG1 . THR B 233 ? 1.5532 1.2463 1.7694 -0.0260 0.0340  -0.1894 235 THR B OG1 
2590  C CG2 . THR B 233 ? 1.4764 1.1924 1.6387 -0.0688 0.0094  -0.1867 235 THR B CG2 
2591  N N   . LEU B 234 ? 1.4879 1.1916 1.7321 -0.0193 0.0321  -0.1015 236 LEU B N   
2592  C CA  . LEU B 234 ? 1.5166 1.1842 1.7859 -0.0177 0.0388  -0.0728 236 LEU B CA  
2593  C C   . LEU B 234 ? 1.6134 1.2304 1.9102 -0.0310 0.0428  -0.1020 236 LEU B C   
2594  O O   . LEU B 234 ? 1.6333 1.2335 1.9379 -0.0291 0.0429  -0.1406 236 LEU B O   
2595  C CB  . LEU B 234 ? 1.5517 1.2123 1.8593 0.0125  0.0491  -0.0415 236 LEU B CB  
2596  C CG  . LEU B 234 ? 1.6048 1.3180 1.8948 0.0259  0.0391  -0.0047 236 LEU B CG  
2597  C CD1 . LEU B 234 ? 1.6357 1.3580 1.9731 0.0591  0.0466  0.0092  236 LEU B CD1 
2598  C CD2 . LEU B 234 ? 1.6564 1.3650 1.9220 0.0216  0.0360  0.0384  236 LEU B CD2 
2599  N N   . VAL B 235 ? 1.5775 1.1715 1.8870 -0.0459 0.0457  -0.0853 237 VAL B N   
2600  C CA  . VAL B 235 ? 1.5956 1.1463 1.9452 -0.0624 0.0460  -0.1077 237 VAL B CA  
2601  C C   . VAL B 235 ? 1.6875 1.1967 2.0886 -0.0541 0.0647  -0.0738 237 VAL B C   
2602  O O   . VAL B 235 ? 1.6834 1.1997 2.0760 -0.0516 0.0751  -0.0313 237 VAL B O   
2603  C CB  . VAL B 235 ? 1.6121 1.1768 1.9468 -0.0900 0.0336  -0.1198 237 VAL B CB  
2604  C CG1 . VAL B 235 ? 1.6336 1.1593 2.0245 -0.1087 0.0303  -0.1365 237 VAL B CG1 
2605  C CG2 . VAL B 235 ? 1.5840 1.1832 1.8695 -0.0965 0.0162  -0.1520 237 VAL B CG2 
2606  N N   . GLU B 236 ? 1.6881 1.1503 2.1378 -0.0485 0.0711  -0.0925 238 GLU B N   
2607  C CA  . GLU B 236 ? 1.7311 1.1441 2.2404 -0.0408 0.0912  -0.0625 238 GLU B CA  
2608  C C   . GLU B 236 ? 1.7640 1.1611 2.3078 -0.0683 0.0944  -0.0517 238 GLU B C   
2609  O O   . GLU B 236 ? 1.7440 1.1551 2.2826 -0.0929 0.0765  -0.0839 238 GLU B O   
2610  C CB  . GLU B 236 ? 1.8085 1.1677 2.3621 -0.0323 0.0964  -0.0968 238 GLU B CB  
2611  C CG  . GLU B 236 ? 2.0007 1.3746 2.5291 -0.0040 0.0981  -0.1140 238 GLU B CG  
2612  C CD  . GLU B 236 ? 2.3464 1.7130 2.8495 -0.0126 0.0862  -0.1787 238 GLU B CD  
2613  O OE1 . GLU B 236 ? 2.3193 1.6428 2.8437 0.0042  0.0988  -0.2056 238 GLU B OE1 
2614  O OE2 . GLU B 236 ? 2.2669 1.6680 2.7258 -0.0344 0.0661  -0.2016 238 GLU B OE2 
2615  N N   . PRO B 237 ? 1.7296 1.1010 2.3111 -0.0640 0.1181  -0.0036 239 PRO B N   
2616  C CA  . PRO B 237 ? 1.7228 1.0825 2.3486 -0.0898 0.1267  0.0089  239 PRO B CA  
2617  C C   . PRO B 237 ? 1.7773 1.1049 2.4681 -0.1171 0.1119  -0.0364 239 PRO B C   
2618  O O   . PRO B 237 ? 1.8245 1.1059 2.5514 -0.1130 0.1117  -0.0592 239 PRO B O   
2619  C CB  . PRO B 237 ? 1.7896 1.1181 2.4469 -0.0750 0.1599  0.0688  239 PRO B CB  
2620  C CG  . PRO B 237 ? 1.8840 1.1907 2.5399 -0.0452 0.1635  0.0763  239 PRO B CG  
2621  C CD  . PRO B 237 ? 1.7866 1.1398 2.3760 -0.0347 0.1395  0.0454  239 PRO B CD  
2622  N N   . GLY B 238 ? 1.6803 1.0329 2.3835 -0.1440 0.0977  -0.0506 240 GLY B N   
2623  C CA  . GLY B 238 ? 1.6827 1.0167 2.4457 -0.1748 0.0745  -0.0925 240 GLY B CA  
2624  C C   . GLY B 238 ? 1.6739 1.0323 2.3860 -0.1839 0.0369  -0.1486 240 GLY B C   
2625  O O   . GLY B 238 ? 1.6651 1.0322 2.4071 -0.2118 0.0100  -0.1767 240 GLY B O   
2626  N N   . ASP B 239 ? 1.5933 0.9653 2.2307 -0.1602 0.0349  -0.1622 241 ASP B N   
2627  C CA  . ASP B 239 ? 1.5734 0.9678 2.1492 -0.1626 0.0072  -0.2099 241 ASP B CA  
2628  C C   . ASP B 239 ? 1.5820 1.0343 2.1164 -0.1728 -0.0079 -0.2036 241 ASP B C   
2629  O O   . ASP B 239 ? 1.5408 1.0193 2.0673 -0.1668 0.0093  -0.1619 241 ASP B O   
2630  C CB  . ASP B 239 ? 1.5948 0.9871 2.1191 -0.1315 0.0188  -0.2170 241 ASP B CB  
2631  C CG  . ASP B 239 ? 1.6289 1.0378 2.0890 -0.1294 -0.0001 -0.2645 241 ASP B CG  
2632  O OD1 . ASP B 239 ? 1.6325 1.0352 2.0871 -0.1526 -0.0265 -0.3039 241 ASP B OD1 
2633  O OD2 . ASP B 239 ? 1.6852 1.1134 2.1026 -0.1045 0.0115  -0.2608 241 ASP B OD2 
2634  N N   . LYS B 240 ? 1.5479 1.0153 2.0528 -0.1877 -0.0393 -0.2452 242 LYS B N   
2635  C CA  . LYS B 240 ? 1.4969 1.0141 1.9665 -0.1974 -0.0569 -0.2427 242 LYS B CA  
2636  C C   . LYS B 240 ? 1.5153 1.0595 1.8977 -0.1835 -0.0635 -0.2614 242 LYS B C   
2637  O O   . LYS B 240 ? 1.5539 1.0808 1.9038 -0.1802 -0.0743 -0.3007 242 LYS B O   
2638  C CB  . LYS B 240 ? 1.5460 1.0661 2.0586 -0.2272 -0.0910 -0.2661 242 LYS B CB  
2639  C CG  . LYS B 240 ? 1.6327 1.2030 2.1168 -0.2355 -0.1114 -0.2610 242 LYS B CG  
2640  C CD  . LYS B 240 ? 1.7820 1.3563 2.2637 -0.2573 -0.1571 -0.3015 242 LYS B CD  
2641  C CE  . LYS B 240 ? 1.9781 1.5720 2.5458 -0.2819 -0.1777 -0.2871 242 LYS B CE  
2642  N NZ  . LYS B 240 ? 2.1828 1.7815 2.7499 -0.3055 -0.2303 -0.3270 242 LYS B NZ  
2643  N N   . ILE B 241 ? 1.4018 0.9857 1.7469 -0.1767 -0.0549 -0.2342 243 ILE B N   
2644  C CA  . ILE B 241 ? 1.3747 0.9888 1.6467 -0.1670 -0.0590 -0.2451 243 ILE B CA  
2645  C C   . ILE B 241 ? 1.4147 1.0590 1.6666 -0.1827 -0.0815 -0.2498 243 ILE B C   
2646  O O   . ILE B 241 ? 1.3878 1.0487 1.6617 -0.1893 -0.0772 -0.2220 243 ILE B O   
2647  C CB  . ILE B 241 ? 1.3757 1.0088 1.6187 -0.1475 -0.0349 -0.2150 243 ILE B CB  
2648  C CG1 . ILE B 241 ? 1.3545 1.0210 1.5331 -0.1409 -0.0387 -0.2264 243 ILE B CG1 
2649  C CG2 . ILE B 241 ? 1.3566 0.9988 1.6158 -0.1503 -0.0202 -0.1742 243 ILE B CG2 
2650  C CD1 . ILE B 241 ? 1.3345 1.0222 1.4918 -0.1239 -0.0217 -0.2040 243 ILE B CD1 
2651  N N   . THR B 242 ? 1.3947 1.0423 1.6051 -0.1873 -0.1041 -0.2842 244 THR B N   
2652  C CA  . THR B 242 ? 1.3844 1.0593 1.5701 -0.2000 -0.1299 -0.2887 244 THR B CA  
2653  C C   . THR B 242 ? 1.3969 1.1007 1.5134 -0.1890 -0.1207 -0.2818 244 THR B C   
2654  O O   . THR B 242 ? 1.4006 1.1020 1.4817 -0.1743 -0.1037 -0.2906 244 THR B O   
2655  C CB  . THR B 242 ? 1.5828 1.2401 1.7642 -0.2146 -0.1647 -0.3291 244 THR B CB  
2656  O OG1 . THR B 242 ? 1.6223 1.2524 1.8815 -0.2284 -0.1718 -0.3326 244 THR B OG1 
2657  C CG2 . THR B 242 ? 1.5744 1.2623 1.7306 -0.2270 -0.1978 -0.3302 244 THR B CG2 
2658  N N   . PHE B 243 ? 1.3207 1.0521 1.4267 -0.1956 -0.1297 -0.2634 245 PHE B N   
2659  C CA  . PHE B 243 ? 1.3006 1.0570 1.3491 -0.1891 -0.1209 -0.2531 245 PHE B CA  
2660  C C   . PHE B 243 ? 1.3875 1.1613 1.4048 -0.1971 -0.1474 -0.2570 245 PHE B C   
2661  O O   . PHE B 243 ? 1.3696 1.1582 1.4113 -0.2032 -0.1544 -0.2334 245 PHE B O   
2662  C CB  . PHE B 243 ? 1.2704 1.0375 1.3331 -0.1862 -0.0975 -0.2189 245 PHE B CB  
2663  C CG  . PHE B 243 ? 1.2721 1.0353 1.3280 -0.1747 -0.0729 -0.2119 245 PHE B CG  
2664  C CD1 . PHE B 243 ? 1.3111 1.0531 1.4074 -0.1700 -0.0631 -0.2076 245 PHE B CD1 
2665  C CD2 . PHE B 243 ? 1.2859 1.0689 1.3004 -0.1694 -0.0608 -0.2055 245 PHE B CD2 
2666  C CE1 . PHE B 243 ? 1.3160 1.0584 1.4062 -0.1576 -0.0445 -0.1960 245 PHE B CE1 
2667  C CE2 . PHE B 243 ? 1.3104 1.0973 1.3252 -0.1599 -0.0442 -0.1963 245 PHE B CE2 
2668  C CZ  . PHE B 243 ? 1.2914 1.0589 1.3416 -0.1527 -0.0376 -0.1909 245 PHE B CZ  
2669  N N   . GLU B 244 ? 1.3904 1.1610 1.3514 -0.1951 -0.1604 -0.2850 246 GLU B N   
2670  C CA  . GLU B 244 ? 1.4213 1.2076 1.3384 -0.2009 -0.1874 -0.2874 246 GLU B CA  
2671  C C   . GLU B 244 ? 1.4520 1.2586 1.3140 -0.1920 -0.1668 -0.2689 246 GLU B C   
2672  O O   . GLU B 244 ? 1.4516 1.2566 1.2829 -0.1817 -0.1410 -0.2772 246 GLU B O   
2673  C CB  . GLU B 244 ? 1.5168 1.2835 1.3905 -0.2044 -0.2122 -0.3293 246 GLU B CB  
2674  C CG  . GLU B 244 ? 1.7370 1.5170 1.5871 -0.2164 -0.2563 -0.3323 246 GLU B CG  
2675  C CD  . GLU B 244 ? 2.3107 2.0650 2.1215 -0.2251 -0.2885 -0.3790 246 GLU B CD  
2676  O OE1 . GLU B 244 ? 2.4442 2.2022 2.2900 -0.2429 -0.3320 -0.3856 246 GLU B OE1 
2677  O OE2 . GLU B 244 ? 2.3399 2.0702 2.0867 -0.2147 -0.2701 -0.4101 246 GLU B OE2 
2678  N N   . ALA B 245 ? 1.3880 1.2141 1.2467 -0.1958 -0.1761 -0.2412 247 ALA B N   
2679  C CA  . ALA B 245 ? 1.3743 1.2158 1.1881 -0.1903 -0.1564 -0.2200 247 ALA B CA  
2680  C C   . ALA B 245 ? 1.4295 1.2858 1.2265 -0.1929 -0.1763 -0.1958 247 ALA B C   
2681  O O   . ALA B 245 ? 1.4051 1.2663 1.2510 -0.1981 -0.1977 -0.1816 247 ALA B O   
2682  C CB  . ALA B 245 ? 1.3272 1.1699 1.1727 -0.1888 -0.1245 -0.1995 247 ALA B CB  
2683  N N   . THR B 246 ? 1.4197 1.2847 1.1527 -0.1880 -0.1664 -0.1870 248 THR B N   
2684  C CA  . THR B 246 ? 1.4469 1.3245 1.1535 -0.1872 -0.1795 -0.1574 248 THR B CA  
2685  C C   . THR B 246 ? 1.4799 1.3603 1.1766 -0.1850 -0.1431 -0.1295 248 THR B C   
2686  O O   . THR B 246 ? 1.5003 1.3867 1.1700 -0.1828 -0.1439 -0.1014 248 THR B O   
2687  C CB  . THR B 246 ? 1.6142 1.4956 1.2432 -0.1846 -0.2061 -0.1715 248 THR B CB  
2688  O OG1 . THR B 246 ? 1.6353 1.5094 1.2044 -0.1782 -0.1800 -0.1958 248 THR B OG1 
2689  C CG2 . THR B 246 ? 1.6148 1.4942 1.2603 -0.1921 -0.2531 -0.1944 248 THR B CG2 
2690  N N   . GLY B 247 ? 1.3952 1.2704 1.1186 -0.1869 -0.1138 -0.1361 249 GLY B N   
2691  C CA  . GLY B 247 ? 1.3728 1.2496 1.0975 -0.1901 -0.0819 -0.1162 249 GLY B CA  
2692  C C   . GLY B 247 ? 1.4018 1.2832 1.1328 -0.1906 -0.0580 -0.1331 249 GLY B C   
2693  O O   . GLY B 247 ? 1.4038 1.2858 1.1305 -0.1847 -0.0616 -0.1595 249 GLY B O   
2694  N N   . ASN B 248 ? 1.3282 1.2118 1.0748 -0.1984 -0.0349 -0.1174 250 ASN B N   
2695  C CA  . ASN B 248 ? 1.2963 1.1927 1.0564 -0.2016 -0.0144 -0.1248 250 ASN B CA  
2696  C C   . ASN B 248 ? 1.2993 1.1902 1.0963 -0.2002 -0.0185 -0.1398 250 ASN B C   
2697  O O   . ASN B 248 ? 1.2815 1.1850 1.0948 -0.2038 -0.0062 -0.1403 250 ASN B O   
2698  C CB  . ASN B 248 ? 1.3222 1.2396 1.0492 -0.1933 -0.0008 -0.1345 250 ASN B CB  
2699  C CG  . ASN B 248 ? 1.6948 1.6179 1.3804 -0.1945 0.0094  -0.1143 250 ASN B CG  
2700  O OD1 . ASN B 248 ? 1.6745 1.5915 1.3162 -0.1871 -0.0041 -0.1148 250 ASN B OD1 
2701  N ND2 . ASN B 248 ? 1.5830 1.5160 1.2824 -0.2057 0.0308  -0.0938 250 ASN B ND2 
2702  N N   . LEU B 249 ? 1.2312 1.1057 1.0453 -0.1959 -0.0361 -0.1486 251 LEU B N   
2703  C CA  . LEU B 249 ? 1.1940 1.0601 1.0420 -0.1936 -0.0366 -0.1579 251 LEU B CA  
2704  C C   . LEU B 249 ? 1.2277 1.0815 1.0956 -0.2023 -0.0284 -0.1430 251 LEU B C   
2705  O O   . LEU B 249 ? 1.2385 1.0787 1.1082 -0.2075 -0.0278 -0.1293 251 LEU B O   
2706  C CB  . LEU B 249 ? 1.1922 1.0441 1.0581 -0.1878 -0.0552 -0.1724 251 LEU B CB  
2707  C CG  . LEU B 249 ? 1.2032 1.0414 1.1085 -0.1846 -0.0540 -0.1777 251 LEU B CG  
2708  C CD1 . LEU B 249 ? 1.1981 1.0452 1.1035 -0.1761 -0.0423 -0.1870 251 LEU B CD1 
2709  C CD2 . LEU B 249 ? 1.2105 1.0344 1.1396 -0.1836 -0.0727 -0.1904 251 LEU B CD2 
2710  N N   . VAL B 250 ? 1.1572 1.0147 1.0366 -0.2025 -0.0213 -0.1454 252 VAL B N   
2711  C CA  . VAL B 250 ? 1.1436 0.9863 1.0294 -0.2099 -0.0145 -0.1364 252 VAL B CA  
2712  C C   . VAL B 250 ? 1.1847 1.0142 1.0936 -0.2002 -0.0176 -0.1398 252 VAL B C   
2713  O O   . VAL B 250 ? 1.1846 1.0235 1.1010 -0.1938 -0.0180 -0.1428 252 VAL B O   
2714  C CB  . VAL B 250 ? 1.1931 1.0542 1.0697 -0.2195 -0.0094 -0.1338 252 VAL B CB  
2715  C CG1 . VAL B 250 ? 1.1954 1.0340 1.0628 -0.2297 -0.0056 -0.1285 252 VAL B CG1 
2716  C CG2 . VAL B 250 ? 1.2008 1.0785 1.0652 -0.2293 -0.0037 -0.1295 252 VAL B CG2 
2717  N N   . VAL B 251 ? 1.1287 0.9388 1.0560 -0.1984 -0.0196 -0.1363 253 VAL B N   
2718  C CA  . VAL B 251 ? 1.1176 0.9128 1.0776 -0.1916 -0.0204 -0.1361 253 VAL B CA  
2719  C C   . VAL B 251 ? 1.1930 0.9750 1.1517 -0.1895 -0.0072 -0.1265 253 VAL B C   
2720  O O   . VAL B 251 ? 1.2049 0.9795 1.1367 -0.1961 0.0025  -0.1196 253 VAL B O   
2721  C CB  . VAL B 251 ? 1.1551 0.9387 1.1452 -0.1928 -0.0235 -0.1288 253 VAL B CB  
2722  C CG1 . VAL B 251 ? 1.1594 0.9577 1.1489 -0.1936 -0.0445 -0.1375 253 VAL B CG1 
2723  C CG2 . VAL B 251 ? 1.1532 0.9211 1.1367 -0.1967 -0.0063 -0.1133 253 VAL B CG2 
2724  N N   . PRO B 252 ? 1.1607 0.9348 1.1449 -0.1810 -0.0063 -0.1251 254 PRO B N   
2725  C CA  . PRO B 252 ? 1.1747 0.9345 1.1500 -0.1774 0.0070  -0.1102 254 PRO B CA  
2726  C C   . PRO B 252 ? 1.2301 0.9636 1.2117 -0.1793 0.0258  -0.0965 254 PRO B C   
2727  O O   . PRO B 252 ? 1.2067 0.9349 1.2268 -0.1798 0.0271  -0.0954 254 PRO B O   
2728  C CB  . PRO B 252 ? 1.1990 0.9560 1.2057 -0.1660 0.0041  -0.1098 254 PRO B CB  
2729  C CG  . PRO B 252 ? 1.2404 1.0085 1.2660 -0.1650 -0.0107 -0.1309 254 PRO B CG  
2730  C CD  . PRO B 252 ? 1.1759 0.9488 1.1944 -0.1749 -0.0168 -0.1366 254 PRO B CD  
2731  N N   . ARG B 253 ? 1.2191 0.9371 1.1616 -0.1802 0.0403  -0.0863 255 ARG B N   
2732  C CA  . ARG B 253 ? 1.2469 0.9349 1.1849 -0.1785 0.0666  -0.0731 255 ARG B CA  
2733  C C   . ARG B 253 ? 1.3272 1.0022 1.2629 -0.1690 0.0783  -0.0563 255 ARG B C   
2734  O O   . ARG B 253 ? 1.3303 0.9913 1.3079 -0.1630 0.0955  -0.0429 255 ARG B O   
2735  C CB  . ARG B 253 ? 1.2926 0.9628 1.1729 -0.1869 0.0777  -0.0771 255 ARG B CB  
2736  C CG  . ARG B 253 ? 1.4428 1.0764 1.3167 -0.1822 0.1122  -0.0664 255 ARG B CG  
2737  C CD  . ARG B 253 ? 1.5851 1.1922 1.4044 -0.1908 0.1246  -0.0767 255 ARG B CD  
2738  N NE  . ARG B 253 ? 1.7377 1.3037 1.5390 -0.1830 0.1639  -0.0680 255 ARG B NE  
2739  C CZ  . ARG B 253 ? 2.0668 1.5941 1.8034 -0.1882 0.1830  -0.0786 255 ARG B CZ  
2740  N NH1 . ARG B 253 ? 1.8803 1.4067 1.5705 -0.2047 0.1622  -0.0976 255 ARG B NH1 
2741  N NH2 . ARG B 253 ? 2.0596 1.5467 1.7785 -0.1776 0.2249  -0.0712 255 ARG B NH2 
2742  N N   . TYR B 254 ? 1.3032 0.9859 1.1962 -0.1676 0.0677  -0.0538 256 TYR B N   
2743  C CA  . TYR B 254 ? 1.3367 1.0090 1.2204 -0.1563 0.0754  -0.0328 256 TYR B CA  
2744  C C   . TYR B 254 ? 1.3613 1.0572 1.2763 -0.1478 0.0547  -0.0317 256 TYR B C   
2745  O O   . TYR B 254 ? 1.3343 1.0589 1.2443 -0.1513 0.0331  -0.0457 256 TYR B O   
2746  C CB  . TYR B 254 ? 1.4144 1.0737 1.2183 -0.1588 0.0794  -0.0253 256 TYR B CB  
2747  C CG  . TYR B 254 ? 1.4925 1.1157 1.2573 -0.1631 0.1088  -0.0261 256 TYR B CG  
2748  C CD1 . TYR B 254 ? 1.5275 1.1445 1.2601 -0.1767 0.1067  -0.0469 256 TYR B CD1 
2749  C CD2 . TYR B 254 ? 1.5479 1.1398 1.3077 -0.1524 0.1431  -0.0048 256 TYR B CD2 
2750  C CE1 . TYR B 254 ? 1.5901 1.1672 1.2865 -0.1780 0.1381  -0.0495 256 TYR B CE1 
2751  C CE2 . TYR B 254 ? 1.6059 1.1621 1.3283 -0.1530 0.1769  -0.0059 256 TYR B CE2 
2752  C CZ  . TYR B 254 ? 1.7121 1.2593 1.4026 -0.1651 0.1744  -0.0299 256 TYR B CZ  
2753  O OH  . TYR B 254 ? 1.7767 1.2823 1.4315 -0.1632 0.2118  -0.0330 256 TYR B OH  
2754  N N   . ALA B 255 ? 1.3341 1.0156 1.2859 -0.1359 0.0652  -0.0137 257 ALA B N   
2755  C CA  . ALA B 255 ? 1.3373 1.0296 1.3236 -0.1237 0.0527  -0.0092 257 ALA B CA  
2756  C C   . ALA B 255 ? 1.4583 1.1370 1.4226 -0.1099 0.0622  0.0246  257 ALA B C   
2757  O O   . ALA B 255 ? 1.4905 1.1486 1.4117 -0.1110 0.0808  0.0418  257 ALA B O   
2758  C CB  . ALA B 255 ? 1.3283 1.0084 1.3853 -0.1231 0.0556  -0.0194 257 ALA B CB  
2759  N N   . PHE B 256 ? 1.4411 1.1293 1.4311 -0.0949 0.0517  0.0357  258 PHE B N   
2760  C CA  . PHE B 256 ? 1.4971 1.1755 1.4649 -0.0793 0.0573  0.0735  258 PHE B CA  
2761  C C   . PHE B 256 ? 1.5765 1.2319 1.6072 -0.0627 0.0694  0.0934  258 PHE B C   
2762  O O   . PHE B 256 ? 1.5470 1.2143 1.6193 -0.0515 0.0570  0.0866  258 PHE B O   
2763  C CB  . PHE B 256 ? 1.5358 1.2516 1.4609 -0.0749 0.0297  0.0803  258 PHE B CB  
2764  C CG  . PHE B 256 ? 1.5429 1.2814 1.4175 -0.0949 0.0143  0.0557  258 PHE B CG  
2765  C CD1 . PHE B 256 ? 1.6223 1.3414 1.4255 -0.1064 0.0228  0.0585  258 PHE B CD1 
2766  C CD2 . PHE B 256 ? 1.5324 1.3063 1.4305 -0.1022 -0.0045 0.0292  258 PHE B CD2 
2767  C CE1 . PHE B 256 ? 1.6328 1.3645 1.3928 -0.1263 0.0100  0.0337  258 PHE B CE1 
2768  C CE2 . PHE B 256 ? 1.5657 1.3566 1.4239 -0.1224 -0.0164 0.0090  258 PHE B CE2 
2769  C CZ  . PHE B 256 ? 1.5818 1.3497 1.3730 -0.1351 -0.0103 0.0104  258 PHE B CZ  
2770  N N   . ALA B 257 ? 1.6012 1.2207 1.6402 -0.0604 0.0974  0.1193  259 ALA B N   
2771  C CA  . ALA B 257 ? 1.6468 1.2362 1.7460 -0.0465 0.1137  0.1446  259 ALA B CA  
2772  C C   . ALA B 257 ? 1.7912 1.3843 1.8487 -0.0253 0.1101  0.1877  259 ALA B C   
2773  O O   . ALA B 257 ? 1.8326 1.4210 1.8198 -0.0243 0.1190  0.2133  259 ALA B O   
2774  C CB  . ALA B 257 ? 1.6738 1.2278 1.8030 -0.0549 0.1475  0.1587  259 ALA B CB  
2775  N N   . MET B 258 ? 1.7756 1.3793 1.8709 -0.0075 0.0951  0.1943  260 MET B N   
2776  C CA  . MET B 258 ? 1.8348 1.4517 1.9005 0.0152  0.0842  0.2374  260 MET B CA  
2777  C C   . MET B 258 ? 1.9520 1.5377 2.0816 0.0395  0.0993  0.2726  260 MET B C   
2778  O O   . MET B 258 ? 1.9273 1.4898 2.1335 0.0405  0.1085  0.2512  260 MET B O   
2779  C CB  . MET B 258 ? 1.8390 1.5119 1.8864 0.0179  0.0472  0.2211  260 MET B CB  
2780  C CG  . MET B 258 ? 1.8378 1.5238 1.9565 0.0216  0.0404  0.1856  260 MET B CG  
2781  S SD  . MET B 258 ? 1.8725 1.6276 1.9901 0.0308  0.0053  0.1795  260 MET B SD  
2782  C CE  . MET B 258 ? 1.7813 1.5626 1.8465 -0.0031 -0.0072 0.1349  260 MET B CE  
2783  N N   . GLU B 259 ? 1.7530 1.3610 1.5425 0.2340  0.1337  -0.0749 261 GLU B N   
2784  C CA  . GLU B 259 ? 1.7711 1.3731 1.5487 0.2493  0.1305  -0.0789 261 GLU B CA  
2785  C C   . GLU B 259 ? 1.8446 1.4728 1.6014 0.2534  0.1209  -0.0845 261 GLU B C   
2786  O O   . GLU B 259 ? 1.8341 1.4614 1.5728 0.2482  0.1228  -0.0847 261 GLU B O   
2787  C CB  . GLU B 259 ? 1.8088 1.3717 1.5785 0.2550  0.1428  -0.0752 261 GLU B CB  
2788  C CG  . GLU B 259 ? 1.9705 1.5249 1.7464 0.2704  0.1408  -0.0756 261 GLU B CG  
2789  C CD  . GLU B 259 ? 2.3218 1.8542 2.0824 0.2800  0.1477  -0.0724 261 GLU B CD  
2790  O OE1 . GLU B 259 ? 2.4044 1.9061 2.1633 0.2775  0.1602  -0.0666 261 GLU B OE1 
2791  O OE2 . GLU B 259 ? 2.1781 1.7251 1.9308 0.2899  0.1411  -0.0746 261 GLU B OE2 
2792  N N   . ARG B 260 ? 1.8300 1.4824 1.5911 0.2616  0.1108  -0.0892 262 ARG B N   
2793  C CA  . ARG B 260 ? 1.8434 1.5221 1.5896 0.2659  0.1015  -0.0931 262 ARG B CA  
2794  C C   . ARG B 260 ? 1.9273 1.5934 1.6580 0.2762  0.1032  -0.0922 262 ARG B C   
2795  O O   . ARG B 260 ? 1.9325 1.5806 1.6717 0.2856  0.1077  -0.0913 262 ARG B O   
2796  C CB  . ARG B 260 ? 1.8425 1.5539 1.6014 0.2697  0.0914  -0.0990 262 ARG B CB  
2797  C CG  . ARG B 260 ? 1.9545 1.6905 1.7260 0.2581  0.0871  -0.0975 262 ARG B CG  
2798  C CD  . ARG B 260 ? 2.0188 1.7949 1.7891 0.2600  0.0761  -0.1018 262 ARG B CD  
2799  N NE  . ARG B 260 ? 2.0643 1.8627 1.8516 0.2598  0.0717  -0.1064 262 ARG B NE  
2800  C CZ  . ARG B 260 ? 2.2278 2.0484 2.0292 0.2490  0.0688  -0.1020 262 ARG B CZ  
2801  N NH1 . ARG B 260 ? 2.1001 1.9218 1.9056 0.2381  0.0705  -0.0925 262 ARG B NH1 
2802  N NH2 . ARG B 260 ? 2.0280 1.8715 1.8419 0.2484  0.0644  -0.1067 262 ARG B NH2 
2803  N N   . ASN B 261 ? 1.8931 1.5705 1.6034 0.2738  0.0991  -0.0909 263 ASN B N   
2804  C CA  . ASN B 261 ? 1.9044 1.5784 1.5993 0.2811  0.0986  -0.0873 263 ASN B CA  
2805  C C   . ASN B 261 ? 1.9420 1.6452 1.6435 0.2889  0.0882  -0.0895 263 ASN B C   
2806  O O   . ASN B 261 ? 1.9145 1.6366 1.6303 0.2890  0.0833  -0.0953 263 ASN B O   
2807  C CB  . ASN B 261 ? 1.9358 1.6072 1.6046 0.2713  0.0995  -0.0846 263 ASN B CB  
2808  C CG  . ASN B 261 ? 2.3331 1.9965 1.9836 0.2756  0.1014  -0.0784 263 ASN B CG  
2809  O OD1 . ASN B 261 ? 2.3056 1.9453 1.9548 0.2792  0.1107  -0.0747 263 ASN B OD1 
2810  N ND2 . ASN B 261 ? 2.2442 1.9287 1.8812 0.2751  0.0923  -0.0754 263 ASN B ND2 
2811  N N   . ALA B 262 ? 1.9198 1.6281 1.6129 0.2949  0.0856  -0.0843 264 ALA B N   
2812  C CA  . ALA B 262 ? 1.9179 1.6525 1.6200 0.3019  0.0773  -0.0850 264 ALA B CA  
2813  C C   . ALA B 262 ? 1.9888 1.7405 1.6702 0.2951  0.0696  -0.0798 264 ALA B C   
2814  O O   . ALA B 262 ? 1.9653 1.7381 1.6475 0.2913  0.0626  -0.0831 264 ALA B O   
2815  C CB  . ALA B 262 ? 1.9328 1.6626 1.6502 0.3143  0.0802  -0.0806 264 ALA B CB  
2816  N N   . GLY B 263 ? 1.9852 1.7282 1.6483 0.2929  0.0708  -0.0712 265 GLY B N   
2817  C CA  . GLY B 263 ? 2.0012 1.7579 1.6427 0.2856  0.0632  -0.0650 265 GLY B CA  
2818  C C   . GLY B 263 ? 2.0674 1.8201 1.6901 0.2722  0.0629  -0.0690 265 GLY B C   
2819  O O   . GLY B 263 ? 2.0853 1.8278 1.6850 0.2644  0.0650  -0.0660 265 GLY B O   
2820  N N   . SER B 264 ? 2.0066 1.7692 1.6408 0.2689  0.0604  -0.0758 266 SER B N   
2821  C CA  . SER B 264 ? 1.9988 1.7623 1.6258 0.2566  0.0599  -0.0792 266 SER B CA  
2822  C C   . SER B 264 ? 2.0158 1.8093 1.6551 0.2564  0.0496  -0.0796 266 SER B C   
2823  O O   . SER B 264 ? 1.9992 1.8075 1.6556 0.2647  0.0468  -0.0811 266 SER B O   
2824  C CB  . SER B 264 ? 2.0384 1.7804 1.6752 0.2518  0.0710  -0.0845 266 SER B CB  
2825  O OG  . SER B 264 ? 2.1675 1.8812 1.7959 0.2537  0.0815  -0.0835 266 SER B OG  
2826  N N   . GLY B 265 A 1.9545 1.7577 1.5861 0.2469  0.0444  -0.0788 266 GLY B N   
2827  C CA  . GLY B 265 A 1.9243 1.7572 1.5682 0.2463  0.0342  -0.0770 266 GLY B CA  
2828  C C   . GLY B 265 A 1.9388 1.7765 1.5842 0.2343  0.0324  -0.0778 266 GLY B C   
2829  O O   . GLY B 265 A 1.9414 1.7581 1.5831 0.2256  0.0414  -0.0823 266 GLY B O   
2830  N N   . ILE B 266 ? 1.8588 1.7246 1.5130 0.2341  0.0215  -0.0734 267 ILE B N   
2831  C CA  . ILE B 266 ? 1.8418 1.7177 1.5046 0.2239  0.0180  -0.0730 267 ILE B CA  
2832  C C   . ILE B 266 ? 1.9040 1.7946 1.5546 0.2233  0.0055  -0.0672 267 ILE B C   
2833  O O   . ILE B 266 ? 1.8933 1.8061 1.5489 0.2315  -0.0038 -0.0604 267 ILE B O   
2834  C CB  . ILE B 266 ? 1.8470 1.7458 1.5426 0.2227  0.0174  -0.0712 267 ILE B CB  
2835  C CG1 . ILE B 266 ? 1.8415 1.7233 1.5499 0.2202  0.0298  -0.0756 267 ILE B CG1 
2836  C CG2 . ILE B 266 ? 1.8465 1.7609 1.5584 0.2132  0.0126  -0.0685 267 ILE B CG2 
2837  C CD1 . ILE B 266 ? 1.8606 1.7653 1.5920 0.2246  0.0281  -0.0729 267 ILE B CD1 
2838  N N   . ILE B 267 ? 1.8819 1.7601 1.5174 0.2130  0.0058  -0.0702 268 ILE B N   
2839  C CA  . ILE B 267 ? 1.8920 1.7817 1.5149 0.2098  -0.0064 -0.0651 268 ILE B CA  
2840  C C   . ILE B 267 ? 1.9442 1.8496 1.5895 0.2019  -0.0109 -0.0660 268 ILE B C   
2841  O O   . ILE B 267 ? 1.9464 1.8398 1.6018 0.1924  -0.0016 -0.0743 268 ILE B O   
2842  C CB  . ILE B 267 ? 1.9602 1.8276 1.5488 0.2028  -0.0037 -0.0682 268 ILE B CB  
2843  C CG1 . ILE B 267 ? 1.9712 1.8340 1.5440 0.2124  -0.0041 -0.0610 268 ILE B CG1 
2844  C CG2 . ILE B 267 ? 1.9838 1.8593 1.5602 0.1933  -0.0145 -0.0669 268 ILE B CG2 
2845  C CD1 . ILE B 267 ? 2.0954 1.9388 1.6366 0.2064  0.0001  -0.0616 268 ILE B CD1 
2846  N N   . ILE B 268 ? 1.8936 1.8263 1.5509 0.2061  -0.0245 -0.0566 269 ILE B N   
2847  C CA  . ILE B 268 ? 1.8826 1.8332 1.5652 0.1997  -0.0303 -0.0553 269 ILE B CA  
2848  C C   . ILE B 268 ? 1.9620 1.9136 1.6259 0.1946  -0.0420 -0.0526 269 ILE B C   
2849  O O   . ILE B 268 ? 1.9578 1.9284 1.6225 0.2017  -0.0549 -0.0409 269 ILE B O   
2850  C CB  . ILE B 268 ? 1.8889 1.8733 1.6075 0.2074  -0.0360 -0.0457 269 ILE B CB  
2851  C CG1 . ILE B 268 ? 1.8820 1.8673 1.6115 0.2132  -0.0265 -0.0472 269 ILE B CG1 
2852  C CG2 . ILE B 268 ? 1.8793 1.8802 1.6322 0.1993  -0.0385 -0.0446 269 ILE B CG2 
2853  C CD1 . ILE B 268 ? 1.9862 1.9854 1.7095 0.2264  -0.0312 -0.0413 269 ILE B CD1 
2854  N N   . SER B 269 ? 1.9424 1.8726 1.5874 0.1820  -0.0370 -0.0635 270 SER B N   
2855  C CA  . SER B 269 ? 1.9625 1.8919 1.5852 0.1744  -0.0475 -0.0631 270 SER B CA  
2856  C C   . SER B 269 ? 2.0289 1.9461 1.6523 0.1587  -0.0420 -0.0781 270 SER B C   
2857  O O   . SER B 269 ? 2.0218 1.9192 1.6457 0.1524  -0.0263 -0.0906 270 SER B O   
2858  C CB  . SER B 269 ? 2.0291 1.9449 1.6119 0.1759  -0.0487 -0.0593 270 SER B CB  
2859  O OG  . SER B 269 ? 2.1559 2.0761 1.7181 0.1685  -0.0614 -0.0551 270 SER B OG  
2860  N N   . ASP B 270 ? 2.0061 1.9346 1.6302 0.1521  -0.0547 -0.0770 271 ASP B N   
2861  C CA  . ASP B 270 ? 2.0279 1.9479 1.6539 0.1363  -0.0514 -0.0927 271 ASP B CA  
2862  C C   . ASP B 270 ? 2.1278 2.0277 1.7045 0.1247  -0.0499 -0.1025 271 ASP B C   
2863  O O   . ASP B 270 ? 2.1488 2.0400 1.7208 0.1100  -0.0459 -0.1187 271 ASP B O   
2864  C CB  . ASP B 270 ? 2.0370 1.9813 1.6944 0.1350  -0.0662 -0.0872 271 ASP B CB  
2865  C CG  . ASP B 270 ? 2.1434 2.0974 1.8531 0.1313  -0.0590 -0.0934 271 ASP B CG  
2866  O OD1 . ASP B 270 ? 2.1636 2.1002 1.8776 0.1184  -0.0454 -0.1116 271 ASP B OD1 
2867  O OD2 . ASP B 270 ? 2.1810 2.1617 1.9293 0.1407  -0.0670 -0.0794 271 ASP B OD2 
2868  N N   . THR B 271 ? 2.0906 1.9849 1.6329 0.1307  -0.0520 -0.0929 272 THR B N   
2869  C CA  . THR B 271 ? 2.1202 2.0004 1.6157 0.1206  -0.0510 -0.0977 272 THR B CA  
2870  C C   . THR B 271 ? 2.1950 2.0496 1.6775 0.1103  -0.0306 -0.1180 272 THR B C   
2871  O O   . THR B 271 ? 2.1691 2.0139 1.6750 0.1156  -0.0168 -0.1225 272 THR B O   
2872  C CB  . THR B 271 ? 2.1224 2.0065 1.5955 0.1306  -0.0574 -0.0792 272 THR B CB  
2873  O OG1 . THR B 271 ? 2.0386 1.9171 1.5268 0.1441  -0.0470 -0.0753 272 THR B OG1 
2874  C CG2 . THR B 271 ? 2.0732 1.9802 1.5525 0.1362  -0.0775 -0.0602 272 THR B CG2 
2875  N N   . PRO B 272 ? 2.1958 2.0399 1.6428 0.0949  -0.0279 -0.1306 273 PRO B N   
2876  C CA  . PRO B 272 ? 2.2122 2.0319 1.6488 0.0853  -0.0069 -0.1506 273 PRO B CA  
2877  C C   . PRO B 272 ? 2.2513 2.0546 1.6697 0.0932  0.0058  -0.1456 273 PRO B C   
2878  O O   . PRO B 272 ? 2.2473 2.0588 1.6560 0.1044  -0.0024 -0.1274 273 PRO B O   
2879  C CB  . PRO B 272 ? 2.2794 2.0978 1.6808 0.0665  -0.0099 -0.1645 273 PRO B CB  
2880  C CG  . PRO B 272 ? 2.3464 2.1842 1.7240 0.0686  -0.0310 -0.1454 273 PRO B CG  
2881  C CD  . PRO B 272 ? 2.2481 2.1032 1.6632 0.0845  -0.0435 -0.1272 273 PRO B CD  
2882  N N   . VAL B 273 ? 2.1970 1.9771 1.6138 0.0873  0.0262  -0.1614 274 VAL B N   
2883  C CA  . VAL B 273 ? 2.1924 1.9539 1.5947 0.0941  0.0401  -0.1582 274 VAL B CA  
2884  C C   . VAL B 273 ? 2.3111 2.0554 1.6762 0.0795  0.0535  -0.1741 274 VAL B C   
2885  O O   . VAL B 273 ? 2.3198 2.0528 1.6917 0.0666  0.0651  -0.1945 274 VAL B O   
2886  C CB  . VAL B 273 ? 2.1925 1.9426 1.6346 0.1047  0.0524  -0.1572 274 VAL B CB  
2887  C CG1 . VAL B 273 ? 2.1732 1.9210 1.6528 0.0963  0.0599  -0.1711 274 VAL B CG1 
2888  C CG2 . VAL B 273 ? 2.1985 1.9241 1.6277 0.1086  0.0699  -0.1584 274 VAL B CG2 
2889  N N   . HIS B 274 ? 2.3125 2.0572 1.6402 0.0810  0.0521  -0.1645 275 HIS B N   
2890  C CA  . HIS B 274 ? 2.3660 2.0993 1.6531 0.0678  0.0636  -0.1763 275 HIS B CA  
2891  C C   . HIS B 274 ? 2.4472 2.1621 1.7258 0.0765  0.0795  -0.1708 275 HIS B C   
2892  O O   . HIS B 274 ? 2.4128 2.1249 1.7156 0.0931  0.0795  -0.1566 275 HIS B O   
2893  C CB  . HIS B 274 ? 2.4068 2.1621 1.6543 0.0576  0.0469  -0.1696 275 HIS B CB  
2894  C CG  . HIS B 274 ? 2.4568 2.2248 1.7071 0.0446  0.0350  -0.1811 275 HIS B CG  
2895  N ND1 . HIS B 274 ? 2.4463 2.2306 1.7274 0.0523  0.0182  -0.1703 275 HIS B ND1 
2896  C CD2 . HIS B 274 ? 2.5134 2.2799 1.7420 0.0248  0.0386  -0.2032 275 HIS B CD2 
2897  C CE1 . HIS B 274 ? 2.4536 2.2456 1.7323 0.0378  0.0111  -0.1844 275 HIS B CE1 
2898  N NE2 . HIS B 274 ? 2.4986 2.2801 1.7463 0.0206  0.0229  -0.2055 275 HIS B NE2 
2899  N N   . ASP B 275 ? 2.4648 2.1678 1.7094 0.0651  0.0932  -0.1823 276 ASP B N   
2900  C CA  . ASP B 275 ? 2.4829 2.1676 1.7180 0.0720  0.1099  -0.1780 276 ASP B CA  
2901  C C   . ASP B 275 ? 2.5489 2.2485 1.7700 0.0840  0.1001  -0.1521 276 ASP B C   
2902  O O   . ASP B 275 ? 2.5495 2.2356 1.7689 0.0924  0.1125  -0.1455 276 ASP B O   
2903  C CB  . ASP B 275 ? 2.5515 2.2210 1.7548 0.0554  0.1284  -0.1990 276 ASP B CB  
2904  C CG  . ASP B 275 ? 2.6867 2.3265 1.8994 0.0617  0.1522  -0.2026 276 ASP B CG  
2905  O OD1 . ASP B 275 ? 2.7201 2.3574 1.9034 0.0624  0.1598  -0.1965 276 ASP B OD1 
2906  O OD2 . ASP B 275 ? 2.7258 2.3461 1.9772 0.0659  0.1629  -0.2101 276 ASP B OD2 
2907  N N   . CYS B 276 ? 2.5028 2.2299 1.7190 0.0854  0.0784  -0.1363 277 CYS B N   
2908  C CA  . CYS B 276 ? 2.4931 2.2382 1.7042 0.0960  0.0679  -0.1098 277 CYS B CA  
2909  C C   . CYS B 276 ? 2.4609 2.1958 1.7086 0.1173  0.0727  -0.0972 277 CYS B C   
2910  O O   . CYS B 276 ? 2.4271 2.1466 1.7054 0.1241  0.0787  -0.1061 277 CYS B O   
2911  C CB  . CYS B 276 ? 2.5020 2.2766 1.7087 0.0925  0.0446  -0.0961 277 CYS B CB  
2912  S SG  . CYS B 276 ? 2.5197 2.2981 1.7625 0.0960  0.0327  -0.1026 277 CYS B SG  
2913  N N   . ASN B 277 ? 2.3812 2.1265 1.6275 0.1271  0.0700  -0.0759 278 ASN B N   
2914  C CA  . ASN B 277 ? 2.3303 2.0693 1.6114 0.1471  0.0729  -0.0631 278 ASN B CA  
2915  C C   . ASN B 277 ? 2.3169 2.0822 1.6150 0.1553  0.0546  -0.0429 278 ASN B C   
2916  O O   . ASN B 277 ? 2.3300 2.1182 1.6079 0.1460  0.0418  -0.0326 278 ASN B O   
2917  C CB  . ASN B 277 ? 2.3684 2.0995 1.6422 0.1531  0.0853  -0.0534 278 ASN B CB  
2918  C CG  . ASN B 277 ? 2.8069 2.5106 2.0654 0.1469  0.1056  -0.0704 278 ASN B CG  
2919  O OD1 . ASN B 277 ? 2.7483 2.4299 2.0201 0.1452  0.1151  -0.0884 278 ASN B OD1 
2920  N ND2 . ASN B 277 ? 2.7876 2.4949 2.0210 0.1439  0.1128  -0.0622 278 ASN B ND2 
2921  N N   . THR B 278 ? 2.2090 1.9716 1.5447 0.1720  0.0537  -0.0371 279 THR B N   
2922  C CA  . THR B 278 ? 2.1745 1.9602 1.5314 0.1810  0.0390  -0.0190 279 THR B CA  
2923  C C   . THR B 278 ? 2.1784 1.9585 1.5735 0.2002  0.0441  -0.0120 279 THR B C   
2924  O O   . THR B 278 ? 2.1644 1.9227 1.5737 0.2065  0.0555  -0.0241 279 THR B O   
2925  C CB  . THR B 278 ? 2.2288 2.0269 1.5896 0.1757  0.0255  -0.0238 279 THR B CB  
2926  O OG1 . THR B 278 ? 2.2104 2.0325 1.5851 0.1815  0.0114  -0.0038 279 THR B OG1 
2927  C CG2 . THR B 278 ? 2.1756 1.9603 1.5621 0.1820  0.0299  -0.0391 279 THR B CG2 
2928  N N   . THR B 279 ? 2.1090 1.9094 1.5227 0.2086  0.0356  0.0078  280 THR B N   
2929  C CA  . THR B 279 ? 2.0758 1.8750 1.5292 0.2264  0.0391  0.0145  280 THR B CA  
2930  C C   . THR B 279 ? 2.0802 1.8865 1.5571 0.2324  0.0314  0.0090  280 THR B C   
2931  O O   . THR B 279 ? 2.0497 1.8472 1.5543 0.2441  0.0368  0.0020  280 THR B O   
2932  C CB  . THR B 279 ? 2.2215 2.0412 1.6887 0.2317  0.0351  0.0391  280 THR B CB  
2933  O OG1 . THR B 279 ? 2.2398 2.0848 1.7007 0.2240  0.0203  0.0524  280 THR B OG1 
2934  C CG2 . THR B 279 ? 2.2423 2.0587 1.6913 0.2280  0.0434  0.0475  280 THR B CG2 
2935  N N   . CYS B 280 ? 2.0293 1.8529 1.4948 0.2238  0.0183  0.0129  281 CYS B N   
2936  C CA  . CYS B 280 ? 1.9999 1.8347 1.4843 0.2280  0.0094  0.0104  281 CYS B CA  
2937  C C   . CYS B 280 ? 1.9925 1.8270 1.4561 0.2156  0.0033  -0.0014 281 CYS B C   
2938  O O   . CYS B 280 ? 2.0075 1.8466 1.4423 0.2021  -0.0020 0.0011  281 CYS B O   
2939  C CB  . CYS B 280 ? 2.0137 1.8724 1.5147 0.2323  -0.0011 0.0312  281 CYS B CB  
2940  S SG  . CYS B 280 ? 2.0387 1.9122 1.5672 0.2401  -0.0102 0.0300  281 CYS B SG  
2941  N N   . GLN B 281 ? 1.8795 1.7111 1.3601 0.2196  0.0039  -0.0137 282 GLN B N   
2942  C CA  . GLN B 281 ? 1.8584 1.6912 1.3294 0.2095  -0.0011 -0.0245 282 GLN B CA  
2943  C C   . GLN B 281 ? 1.8700 1.7204 1.3649 0.2159  -0.0108 -0.0224 282 GLN B C   
2944  O O   . GLN B 281 ? 1.8387 1.6907 1.3589 0.2276  -0.0069 -0.0243 282 GLN B O   
2945  C CB  . GLN B 281 ? 1.8702 1.6804 1.3386 0.2051  0.0123  -0.0426 282 GLN B CB  
2946  C CG  . GLN B 281 ? 2.0311 1.8415 1.4951 0.1934  0.0098  -0.0548 282 GLN B CG  
2947  C CD  . GLN B 281 ? 2.3684 2.1828 1.8014 0.1787  0.0033  -0.0548 282 GLN B CD  
2948  O OE1 . GLN B 281 ? 2.3660 2.1664 1.7744 0.1695  0.0119  -0.0613 282 GLN B OE1 
2949  N NE2 . GLN B 281 ? 2.2944 2.1287 1.7277 0.1757  -0.0120 -0.0474 282 GLN B NE2 
2950  N N   . THR B 282 ? 1.8347 1.6993 1.3212 0.2080  -0.0234 -0.0184 283 THR B N   
2951  C CA  . THR B 282 ? 1.8136 1.6967 1.3211 0.2131  -0.0337 -0.0146 283 THR B CA  
2952  C C   . THR B 282 ? 1.8862 1.7713 1.3898 0.2025  -0.0384 -0.0243 283 THR B C   
2953  O O   . THR B 282 ? 1.9134 1.7901 1.3926 0.1895  -0.0383 -0.0297 283 THR B O   
2954  C CB  . THR B 282 ? 1.8772 1.7794 1.3873 0.2160  -0.0465 0.0051  283 THR B CB  
2955  O OG1 . THR B 282 ? 1.8510 1.7590 1.3385 0.2028  -0.0577 0.0108  283 THR B OG1 
2956  C CG2 . THR B 282 ? 1.8754 1.7774 1.3915 0.2237  -0.0420 0.0169  283 THR B CG2 
2957  N N   . PRO B 283 ? 1.8245 1.7234 1.3529 0.2073  -0.0431 -0.0259 284 PRO B N   
2958  C CA  . PRO B 283 ? 1.8232 1.7265 1.3551 0.1976  -0.0479 -0.0334 284 PRO B CA  
2959  C C   . PRO B 283 ? 1.8985 1.8081 1.4104 0.1865  -0.0608 -0.0279 284 PRO B C   
2960  O O   . PRO B 283 ? 1.9081 1.8141 1.4157 0.1749  -0.0614 -0.0385 284 PRO B O   
2961  C CB  . PRO B 283 ? 1.8118 1.7354 1.3767 0.2074  -0.0525 -0.0297 284 PRO B CB  
2962  C CG  . PRO B 283 ? 1.8528 1.7745 1.4290 0.2197  -0.0440 -0.0292 284 PRO B CG  
2963  C CD  . PRO B 283 ? 1.8157 1.7282 1.3721 0.2214  -0.0432 -0.0216 284 PRO B CD  
2964  N N   . LYS B 284 ? 1.8550 1.7742 1.3571 0.1892  -0.0706 -0.0113 285 LYS B N   
2965  C CA  . LYS B 284 ? 1.8736 1.8003 1.3553 0.1783  -0.0843 -0.0022 285 LYS B CA  
2966  C C   . LYS B 284 ? 1.9712 1.8826 1.4174 0.1643  -0.0785 -0.0100 285 LYS B C   
2967  O O   . LYS B 284 ? 1.9896 1.9027 1.4163 0.1502  -0.0860 -0.0138 285 LYS B O   
2968  C CB  . LYS B 284 ? 1.8980 1.8397 1.3853 0.1860  -0.0947 0.0209  285 LYS B CB  
2969  C CG  . LYS B 284 ? 2.0537 2.0108 1.5387 0.1798  -0.1128 0.0341  285 LYS B CG  
2970  C CD  . LYS B 284 ? 2.1232 2.0948 1.6228 0.1892  -0.1210 0.0578  285 LYS B CD  
2971  C CE  . LYS B 284 ? 2.2292 2.2150 1.7281 0.1831  -0.1394 0.0735  285 LYS B CE  
2972  N NZ  . LYS B 284 ? 2.3181 2.3174 1.8373 0.1932  -0.1459 0.0974  285 LYS B NZ  
2973  N N   . GLY B 285 ? 1.9407 1.8386 1.3798 0.1684  -0.0651 -0.0128 286 GLY B N   
2974  C CA  . GLY B 285 ? 1.9696 1.8539 1.3768 0.1574  -0.0571 -0.0191 286 GLY B CA  
2975  C C   . GLY B 285 ? 2.0225 1.9002 1.4285 0.1660  -0.0474 -0.0110 286 GLY B C   
2976  O O   . GLY B 285 ? 1.9980 1.8831 1.4275 0.1797  -0.0485 0.0009  286 GLY B O   
2977  N N   . ALA B 286 ? 2.0089 1.8732 1.3891 0.1580  -0.0374 -0.0176 287 ALA B N   
2978  C CA  . ALA B 286 ? 2.0173 1.8749 1.3976 0.1657  -0.0272 -0.0098 287 ALA B CA  
2979  C C   . ALA B 286 ? 2.1011 1.9778 1.4782 0.1667  -0.0367 0.0151  287 ALA B C   
2980  O O   . ALA B 286 ? 2.1146 2.0071 1.4756 0.1559  -0.0502 0.0251  287 ALA B O   
2981  C CB  . ALA B 286 ? 2.0513 1.8897 1.4061 0.1568  -0.0131 -0.0240 287 ALA B CB  
2982  N N   . ILE B 287 ? 2.0620 1.9382 1.4584 0.1794  -0.0298 0.0260  288 ILE B N   
2983  C CA  . ILE B 287 ? 2.0690 1.9642 1.4719 0.1814  -0.0363 0.0518  288 ILE B CA  
2984  C C   . ILE B 287 ? 2.1386 2.0282 1.5392 0.1846  -0.0246 0.0577  288 ILE B C   
2985  O O   . ILE B 287 ? 2.1213 1.9935 1.5378 0.1957  -0.0116 0.0473  288 ILE B O   
2986  C CB  . ILE B 287 ? 2.0789 1.9881 1.5210 0.1950  -0.0426 0.0664  288 ILE B CB  
2987  C CG1 . ILE B 287 ? 2.0527 1.9601 1.5097 0.2001  -0.0468 0.0539  288 ILE B CG1 
2988  C CG2 . ILE B 287 ? 2.1077 2.0413 1.5503 0.1888  -0.0558 0.0939  288 ILE B CG2 
2989  C CD1 . ILE B 287 ? 2.0567 1.9721 1.5530 0.2160  -0.0464 0.0609  288 ILE B CD1 
2990  N N   . ASN B 288 ? 2.1237 2.0301 1.5072 0.1752  -0.0298 0.0766  289 ASN B N   
2991  C CA  . ASN B 288 ? 2.1357 2.0437 1.5195 0.1779  -0.0205 0.0880  289 ASN B CA  
2992  C C   . ASN B 288 ? 2.1940 2.1307 1.6009 0.1797  -0.0301 0.1199  289 ASN B C   
2993  O O   . ASN B 288 ? 2.2155 2.1731 1.6002 0.1652  -0.0398 0.1367  289 ASN B O   
2994  C CB  . ASN B 288 ? 2.1812 2.0849 1.5188 0.1617  -0.0159 0.0797  289 ASN B CB  
2995  C CG  . ASN B 288 ? 2.4558 2.3618 1.7920 0.1647  -0.0053 0.0915  289 ASN B CG  
2996  O OD1 . ASN B 288 ? 2.3675 2.2625 1.7344 0.1807  0.0053  0.0928  289 ASN B OD1 
2997  N ND2 . ASN B 288 ? 2.3628 2.2843 1.6635 0.1489  -0.0080 0.1001  289 ASN B ND2 
2998  N N   . THR B 289 ? 2.1247 2.0635 1.5783 0.1965  -0.0275 0.1281  290 THR B N   
2999  C CA  . THR B 289 ? 2.1130 2.0780 1.6005 0.1999  -0.0345 0.1583  290 THR B CA  
3000  C C   . THR B 289 ? 2.1427 2.1070 1.6789 0.2178  -0.0234 0.1662  290 THR B C   
3001  O O   . THR B 289 ? 2.1247 2.0674 1.6752 0.2304  -0.0125 0.1462  290 THR B O   
3002  C CB  . THR B 289 ? 2.1629 2.1386 1.6631 0.1989  -0.0475 0.1641  290 THR B CB  
3003  O OG1 . THR B 289 ? 2.1304 2.1326 1.6612 0.1988  -0.0543 0.1962  290 THR B OG1 
3004  C CG2 . THR B 289 ? 2.1152 2.0754 1.6417 0.2138  -0.0424 0.1449  290 THR B CG2 
3005  N N   . SER B 290 ? 2.0936 2.0836 1.6581 0.2179  -0.0267 0.1966  291 SER B N   
3006  C CA  . SER B 290 ? 2.0678 2.0638 1.6870 0.2335  -0.0176 0.2095  291 SER B CA  
3007  C C   . SER B 290 ? 2.0974 2.1033 1.7636 0.2423  -0.0211 0.2173  291 SER B C   
3008  O O   . SER B 290 ? 2.0737 2.0817 1.7912 0.2567  -0.0126 0.2216  291 SER B O   
3009  C CB  . SER B 290 ? 2.1198 2.1415 1.7472 0.2275  -0.0183 0.2404  291 SER B CB  
3010  O OG  . SER B 290 ? 2.2299 2.2781 1.8390 0.2105  -0.0327 0.2637  291 SER B OG  
3011  N N   . LEU B 291 ? 2.0554 2.0670 1.7050 0.2337  -0.0332 0.2182  292 LEU B N   
3012  C CA  . LEU B 291 ? 2.0283 2.0495 1.7158 0.2399  -0.0375 0.2260  292 LEU B CA  
3013  C C   . LEU B 291 ? 2.0221 2.0241 1.7337 0.2564  -0.0276 0.1994  292 LEU B C   
3014  O O   . LEU B 291 ? 2.0158 1.9959 1.6990 0.2581  -0.0234 0.1723  292 LEU B O   
3015  C CB  . LEU B 291 ? 2.0433 2.0734 1.7014 0.2260  -0.0534 0.2329  292 LEU B CB  
3016  C CG  . LEU B 291 ? 2.1295 2.1848 1.7717 0.2086  -0.0655 0.2639  292 LEU B CG  
3017  C CD1 . LEU B 291 ? 2.1759 2.2319 1.7733 0.1933  -0.0805 0.2606  292 LEU B CD1 
3018  C CD2 . LEU B 291 ? 2.1229 2.2040 1.8194 0.2110  -0.0679 0.2983  292 LEU B CD2 
3019  N N   . PRO B 292 ? 1.9323 1.9434 1.6978 0.2679  -0.0231 0.2069  293 PRO B N   
3020  C CA  . PRO B 292 ? 1.9007 1.8965 1.6883 0.2826  -0.0134 0.1807  293 PRO B CA  
3021  C C   . PRO B 292 ? 1.9259 1.9166 1.6966 0.2823  -0.0193 0.1645  293 PRO B C   
3022  O O   . PRO B 292 ? 1.9033 1.8821 1.6826 0.2922  -0.0120 0.1405  293 PRO B O   
3023  C CB  . PRO B 292 ? 1.9069 1.9169 1.7600 0.2934  -0.0056 0.1952  293 PRO B CB  
3024  C CG  . PRO B 292 ? 1.9725 2.0070 1.8377 0.2833  -0.0153 0.2298  293 PRO B CG  
3025  C CD  . PRO B 292 ? 1.9425 1.9793 1.7542 0.2674  -0.0255 0.2395  293 PRO B CD  
3026  N N   . PHE B 293 ? 1.8873 1.8888 1.6365 0.2709  -0.0328 0.1785  294 PHE B N   
3027  C CA  . PHE B 293 ? 1.8781 1.8776 1.6143 0.2708  -0.0395 0.1667  294 PHE B CA  
3028  C C   . PHE B 293 ? 1.9399 1.9372 1.6262 0.2562  -0.0524 0.1663  294 PHE B C   
3029  O O   . PHE B 293 ? 1.9591 1.9624 1.6233 0.2440  -0.0587 0.1817  294 PHE B O   
3030  C CB  . PHE B 293 ? 1.8919 1.9076 1.6688 0.2760  -0.0416 0.1830  294 PHE B CB  
3031  C CG  . PHE B 293 ? 1.9012 1.9172 1.7289 0.2909  -0.0269 0.1764  294 PHE B CG  
3032  C CD1 . PHE B 293 ? 1.9335 1.9386 1.7669 0.3018  -0.0181 0.1477  294 PHE B CD1 
3033  C CD2 . PHE B 293 ? 1.9345 1.9630 1.8056 0.2931  -0.0216 0.1983  294 PHE B CD2 
3034  C CE1 . PHE B 293 ? 1.9351 1.9406 1.8144 0.3145  -0.0044 0.1387  294 PHE B CE1 
3035  C CE2 . PHE B 293 ? 1.9579 1.9864 1.8796 0.3067  -0.0072 0.1899  294 PHE B CE2 
3036  C CZ  . PHE B 293 ? 1.9226 1.9388 1.8466 0.3172  0.0013  0.1589  294 PHE B CZ  
3037  N N   . GLN B 294 ? 1.8814 1.8715 1.5510 0.2572  -0.0559 0.1480  295 GLN B N   
3038  C CA  . GLN B 294 ? 1.8917 1.8789 1.5192 0.2442  -0.0672 0.1439  295 GLN B CA  
3039  C C   . GLN B 294 ? 1.9216 1.9144 1.5531 0.2466  -0.0754 0.1404  295 GLN B C   
3040  O O   . GLN B 294 ? 1.8947 1.8856 1.5466 0.2584  -0.0686 0.1265  295 GLN B O   
3041  C CB  . GLN B 294 ? 1.9181 1.8860 1.5146 0.2407  -0.0600 0.1204  295 GLN B CB  
3042  C CG  . GLN B 294 ? 2.1043 2.0635 1.6756 0.2357  -0.0643 0.1008  295 GLN B CG  
3043  C CD  . GLN B 294 ? 2.2994 2.2502 1.8877 0.2477  -0.0549 0.0798  295 GLN B CD  
3044  O OE1 . GLN B 294 ? 2.2040 2.1628 1.8043 0.2524  -0.0594 0.0764  295 GLN B OE1 
3045  N NE2 . GLN B 294 ? 2.2083 2.1443 1.7984 0.2526  -0.0422 0.0662  295 GLN B NE2 
3046  N N   . ASN B 295 ? 1.8945 1.8957 1.5071 0.2352  -0.0902 0.1534  296 ASN B N   
3047  C CA  . ASN B 295 ? 1.8873 1.8950 1.5042 0.2372  -0.0995 0.1531  296 ASN B CA  
3048  C C   . ASN B 295 ? 1.9646 1.9644 1.5495 0.2290  -0.1056 0.1352  296 ASN B C   
3049  O O   . ASN B 295 ? 1.9509 1.9580 1.5373 0.2283  -0.1159 0.1377  296 ASN B O   
3050  C CB  . ASN B 295 ? 1.9009 1.9250 1.5308 0.2324  -0.1123 0.1832  296 ASN B CB  
3051  C CG  . ASN B 295 ? 2.2830 2.3114 1.8801 0.2147  -0.1280 0.1956  296 ASN B CG  
3052  O OD1 . ASN B 295 ? 2.2220 2.2433 1.7862 0.2037  -0.1278 0.1865  296 ASN B OD1 
3053  N ND2 . ASN B 295 ? 2.2215 2.2621 1.8275 0.2112  -0.1416 0.2165  296 ASN B ND2 
3054  N N   . ILE B 296 ? 1.9458 1.9309 1.5060 0.2235  -0.0981 0.1173  297 ILE B N   
3055  C CA  . ILE B 296 ? 1.9496 1.9258 1.4827 0.2142  -0.1010 0.0991  297 ILE B CA  
3056  C C   . ILE B 296 ? 1.9568 1.9312 1.5055 0.2234  -0.0970 0.0812  297 ILE B C   
3057  O O   . ILE B 296 ? 1.9444 1.9269 1.4943 0.2208  -0.1073 0.0819  297 ILE B O   
3058  C CB  . ILE B 296 ? 2.0098 1.9708 1.5139 0.2048  -0.0926 0.0872  297 ILE B CB  
3059  C CG1 . ILE B 296 ? 2.0377 2.0067 1.5239 0.1933  -0.0991 0.1072  297 ILE B CG1 
3060  C CG2 . ILE B 296 ? 2.0325 1.9827 1.5138 0.1951  -0.0928 0.0660  297 ILE B CG2 
3061  C CD1 . ILE B 296 ? 2.1550 2.1146 1.6270 0.1907  -0.0878 0.1038  297 ILE B CD1 
3062  N N   . HIS B 297 ? 1.8827 1.8482 1.4441 0.2331  -0.0830 0.0663  298 HIS B N   
3063  C CA  . HIS B 297 ? 1.8518 1.8187 1.4277 0.2401  -0.0790 0.0508  298 HIS B CA  
3064  C C   . HIS B 297 ? 1.8790 1.8436 1.4774 0.2534  -0.0660 0.0425  298 HIS B C   
3065  O O   . HIS B 297 ? 1.8894 1.8412 1.4844 0.2544  -0.0563 0.0385  298 HIS B O   
3066  C CB  . HIS B 297 ? 1.8651 1.8194 1.4224 0.2303  -0.0762 0.0333  298 HIS B CB  
3067  C CG  . HIS B 297 ? 1.8833 1.8454 1.4578 0.2341  -0.0762 0.0229  298 HIS B CG  
3068  N ND1 . HIS B 297 ? 1.8866 1.8465 1.4777 0.2424  -0.0651 0.0112  298 HIS B ND1 
3069  C CD2 . HIS B 297 ? 1.8952 1.8694 1.4752 0.2303  -0.0865 0.0247  298 HIS B CD2 
3070  C CE1 . HIS B 297 ? 1.8595 1.8322 1.4651 0.2429  -0.0689 0.0072  298 HIS B CE1 
3071  N NE2 . HIS B 297 ? 1.8679 1.8494 1.4692 0.2364  -0.0815 0.0151  298 HIS B NE2 
3072  N N   . PRO B 298 ? 1.7966 1.7748 1.4182 0.2632  -0.0657 0.0392  299 PRO B N   
3073  C CA  . PRO B 298 ? 1.7739 1.7517 1.4160 0.2747  -0.0536 0.0292  299 PRO B CA  
3074  C C   . PRO B 298 ? 1.8068 1.7680 1.4426 0.2735  -0.0425 0.0111  299 PRO B C   
3075  O O   . PRO B 298 ? 1.8048 1.7585 1.4512 0.2802  -0.0325 0.0056  299 PRO B O   
3076  C CB  . PRO B 298 ? 1.7772 1.7760 1.4396 0.2825  -0.0571 0.0291  299 PRO B CB  
3077  C CG  . PRO B 298 ? 1.8356 1.8418 1.4880 0.2749  -0.0690 0.0339  299 PRO B CG  
3078  C CD  . PRO B 298 ? 1.8023 1.7986 1.4334 0.2646  -0.0763 0.0452  299 PRO B CD  
3079  N N   . ILE B 299 ? 1.7439 1.6990 1.3659 0.2648  -0.0438 0.0024  300 ILE B N   
3080  C CA  . ILE B 299 ? 1.7315 1.6694 1.3490 0.2621  -0.0329 -0.0129 300 ILE B CA  
3081  C C   . ILE B 299 ? 1.8037 1.7203 1.4003 0.2562  -0.0279 -0.0117 300 ILE B C   
3082  O O   . ILE B 299 ? 1.8096 1.7239 1.3858 0.2465  -0.0344 -0.0053 300 ILE B O   
3083  C CB  . ILE B 299 ? 1.7579 1.6986 1.3753 0.2545  -0.0348 -0.0210 300 ILE B CB  
3084  C CG1 . ILE B 299 ? 1.7371 1.7040 1.3775 0.2608  -0.0402 -0.0195 300 ILE B CG1 
3085  C CG2 . ILE B 299 ? 1.7685 1.6894 1.3836 0.2507  -0.0226 -0.0346 300 ILE B CG2 
3086  C CD1 . ILE B 299 ? 1.8007 1.7782 1.4479 0.2530  -0.0457 -0.0213 300 ILE B CD1 
3087  N N   . THR B 300 ? 1.7728 1.6757 1.3752 0.2620  -0.0167 -0.0173 301 THR B N   
3088  C CA  . THR B 300 ? 1.7965 1.6810 1.3831 0.2585  -0.0105 -0.0149 301 THR B CA  
3089  C C   . THR B 300 ? 1.8558 1.7197 1.4453 0.2605  0.0026  -0.0280 301 THR B C   
3090  O O   . THR B 300 ? 1.8308 1.6966 1.4409 0.2684  0.0073  -0.0358 301 THR B O   
3091  C CB  . THR B 300 ? 1.9098 1.8013 1.5077 0.2656  -0.0114 -0.0006 301 THR B CB  
3092  O OG1 . THR B 300 ? 1.9380 1.8350 1.5655 0.2783  -0.0058 -0.0050 301 THR B OG1 
3093  C CG2 . THR B 300 ? 1.8783 1.7872 1.4717 0.2615  -0.0240 0.0163  301 THR B CG2 
3094  N N   . ILE B 301 ? 1.8434 1.6882 1.4121 0.2531  0.0086  -0.0298 302 ILE B N   
3095  C CA  . ILE B 301 ? 1.8468 1.6688 1.4170 0.2544  0.0217  -0.0397 302 ILE B CA  
3096  C C   . ILE B 301 ? 1.9420 1.7518 1.5013 0.2553  0.0274  -0.0318 302 ILE B C   
3097  O O   . ILE B 301 ? 1.9622 1.7727 1.4970 0.2462  0.0241  -0.0252 302 ILE B O   
3098  C CB  . ILE B 301 ? 1.8849 1.6945 1.4452 0.2437  0.0261  -0.0516 302 ILE B CB  
3099  C CG1 . ILE B 301 ? 1.8684 1.6946 1.4467 0.2438  0.0206  -0.0565 302 ILE B CG1 
3100  C CG2 . ILE B 301 ? 1.8947 1.6783 1.4573 0.2445  0.0405  -0.0594 302 ILE B CG2 
3101  C CD1 . ILE B 301 ? 1.9735 1.7956 1.5483 0.2321  0.0219  -0.0643 302 ILE B CD1 
3102  N N   . GLY B 302 ? 1.9045 1.7051 1.4832 0.2660  0.0357  -0.0324 303 GLY B N   
3103  C CA  . GLY B 302 ? 1.9203 1.7114 1.4971 0.2695  0.0420  -0.0234 303 GLY B CA  
3104  C C   . GLY B 302 ? 1.9756 1.7852 1.5721 0.2778  0.0369  -0.0083 303 GLY B C   
3105  O O   . GLY B 302 ? 1.9686 1.7954 1.5826 0.2823  0.0303  -0.0074 303 GLY B O   
3106  N N   . LYS B 303 ? 1.9374 1.7453 1.5346 0.2798  0.0406  0.0048  304 LYS B N   
3107  C CA  . LYS B 303 ? 1.9309 1.7581 1.5531 0.2868  0.0368  0.0225  304 LYS B CA  
3108  C C   . LYS B 303 ? 1.9894 1.8374 1.5974 0.2777  0.0241  0.0336  304 LYS B C   
3109  O O   . LYS B 303 ? 2.0009 1.8523 1.5790 0.2659  0.0196  0.0420  304 LYS B O   
3110  C CB  . LYS B 303 ? 1.9743 1.7982 1.6017 0.2897  0.0432  0.0367  304 LYS B CB  
3111  C CG  . LYS B 303 ? 2.1387 1.9507 1.8021 0.3045  0.0535  0.0321  304 LYS B CG  
3112  C CD  . LYS B 303 ? 2.2652 2.0755 1.9381 0.3086  0.0599  0.0479  304 LYS B CD  
3113  C CE  . LYS B 303 ? 2.3275 2.1212 2.0337 0.3227  0.0702  0.0407  304 LYS B CE  
3114  N NZ  . LYS B 303 ? 2.3998 2.1925 2.1189 0.3281  0.0767  0.0576  304 LYS B NZ  
3115  N N   . CYS B 304 ? 1.9370 1.7983 1.5644 0.2824  0.0183  0.0316  305 CYS B N   
3116  C CA  . CYS B 304 ? 1.9391 1.8186 1.5566 0.2750  0.0059  0.0408  305 CYS B CA  
3117  C C   . CYS B 304 ? 1.9511 1.8513 1.6019 0.2820  0.0015  0.0563  305 CYS B C   
3118  O O   . CYS B 304 ? 1.9240 1.8258 1.6089 0.2940  0.0076  0.0504  305 CYS B O   
3119  C CB  . CYS B 304 ? 1.9402 1.8171 1.5451 0.2715  0.0021  0.0245  305 CYS B CB  
3120  S SG  . CYS B 304 ? 2.0174 1.8764 1.5810 0.2572  0.0034  0.0119  305 CYS B SG  
3121  N N   . PRO B 305 ? 1.9057 1.8224 1.5473 0.2734  -0.0093 0.0754  306 PRO B N   
3122  C CA  . PRO B 305 ? 1.8898 1.8264 1.5654 0.2788  -0.0134 0.0925  306 PRO B CA  
3123  C C   . PRO B 305 ? 1.9067 1.8484 1.5909 0.2832  -0.0171 0.0816  306 PRO B C   
3124  O O   . PRO B 305 ? 1.8968 1.8383 1.5540 0.2755  -0.0253 0.0764  306 PRO B O   
3125  C CB  . PRO B 305 ? 1.9329 1.8840 1.5898 0.2656  -0.0250 0.1164  306 PRO B CB  
3126  C CG  . PRO B 305 ? 2.0120 1.9511 1.6257 0.2542  -0.0250 0.1102  306 PRO B CG  
3127  C CD  . PRO B 305 ? 1.9475 1.8659 1.5488 0.2577  -0.0181 0.0825  306 PRO B CD  
3128  N N   . LYS B 306 ? 1.8421 1.7890 1.5652 0.2957  -0.0102 0.0771  307 LYS B N   
3129  C CA  . LYS B 306 ? 1.8219 1.7765 1.5575 0.3016  -0.0114 0.0663  307 LYS B CA  
3130  C C   . LYS B 306 ? 1.8824 1.8510 1.6066 0.2946  -0.0246 0.0806  307 LYS B C   
3131  O O   . LYS B 306 ? 1.8792 1.8581 1.6110 0.2902  -0.0304 0.1037  307 LYS B O   
3132  C CB  . LYS B 306 ? 1.8352 1.7968 1.6176 0.3146  -0.0015 0.0633  307 LYS B CB  
3133  C CG  . LYS B 306 ? 1.9784 1.9260 1.7718 0.3224  0.0106  0.0431  307 LYS B CG  
3134  C CD  . LYS B 306 ? 2.0966 2.0484 1.9378 0.3326  0.0207  0.0464  307 LYS B CD  
3135  C CE  . LYS B 306 ? 2.2175 2.1538 2.0667 0.3397  0.0310  0.0255  307 LYS B CE  
3136  N NZ  . LYS B 306 ? 2.3050 2.2463 2.2056 0.3509  0.0417  0.0218  307 LYS B NZ  
3137  N N   . TYR B 307 ? 1.8489 1.8182 1.5556 0.2928  -0.0298 0.0685  308 TYR B N   
3138  C CA  . TYR B 307 ? 1.8554 1.8367 1.5511 0.2867  -0.0431 0.0804  308 TYR B CA  
3139  C C   . TYR B 307 ? 1.9138 1.9119 1.6418 0.2934  -0.0450 0.0954  308 TYR B C   
3140  O O   . TYR B 307 ? 1.8851 1.8878 1.6427 0.3044  -0.0355 0.0868  308 TYR B O   
3141  C CB  . TYR B 307 ? 1.8603 1.8406 1.5372 0.2845  -0.0472 0.0644  308 TYR B CB  
3142  C CG  . TYR B 307 ? 1.8857 1.8779 1.5529 0.2784  -0.0615 0.0765  308 TYR B CG  
3143  C CD1 . TYR B 307 ? 1.9301 1.9194 1.5708 0.2654  -0.0720 0.0872  308 TYR B CD1 
3144  C CD2 . TYR B 307 ? 1.8809 1.8882 1.5658 0.2857  -0.0647 0.0771  308 TYR B CD2 
3145  C CE1 . TYR B 307 ? 1.9421 1.9418 1.5758 0.2598  -0.0860 0.0980  308 TYR B CE1 
3146  C CE2 . TYR B 307 ? 1.8946 1.9127 1.5737 0.2812  -0.0783 0.0897  308 TYR B CE2 
3147  C CZ  . TYR B 307 ? 2.0112 2.0249 1.6657 0.2683  -0.0894 0.1002  308 TYR B CZ  
3148  O OH  . TYR B 307 ? 2.0262 2.0499 1.6767 0.2637  -0.1037 0.1125  308 TYR B OH  
3149  N N   . VAL B 308 ? 1.9051 1.9123 1.6272 0.2857  -0.0572 0.1177  309 VAL B N   
3150  C CA  . VAL B 308 ? 1.9094 1.9319 1.6589 0.2890  -0.0617 0.1376  309 VAL B CA  
3151  C C   . VAL B 308 ? 1.9816 2.0105 1.7093 0.2804  -0.0783 0.1493  309 VAL B C   
3152  O O   . VAL B 308 ? 1.9895 2.0118 1.6831 0.2693  -0.0862 0.1472  309 VAL B O   
3153  C CB  . VAL B 308 ? 1.9694 1.9980 1.7479 0.2885  -0.0586 0.1608  309 VAL B CB  
3154  C CG1 . VAL B 308 ? 1.9548 1.9826 1.7727 0.3011  -0.0419 0.1502  309 VAL B CG1 
3155  C CG2 . VAL B 308 ? 1.9887 2.0129 1.7426 0.2762  -0.0635 0.1723  309 VAL B CG2 
3156  N N   . LYS B 309 ? 1.9414 1.9828 1.6896 0.2857  -0.0828 0.1603  310 LYS B N   
3157  C CA  . LYS B 309 ? 1.9452 1.9934 1.6786 0.2792  -0.0989 0.1729  310 LYS B CA  
3158  C C   . LYS B 309 ? 1.9991 2.0542 1.7382 0.2702  -0.1099 0.2048  310 LYS B C   
3159  O O   . LYS B 309 ? 2.0017 2.0609 1.7250 0.2621  -0.1252 0.2171  310 LYS B O   
3160  C CB  . LYS B 309 ? 1.9629 2.0218 1.7136 0.2900  -0.0987 0.1675  310 LYS B CB  
3161  C CG  . LYS B 309 ? 2.2077 2.2643 1.9437 0.2935  -0.0948 0.1407  310 LYS B CG  
3162  C CD  . LYS B 309 ? 2.3619 2.4341 2.1120 0.3021  -0.0979 0.1397  310 LYS B CD  
3163  C CE  . LYS B 309 ? 2.5065 2.5862 2.2799 0.3149  -0.0830 0.1243  310 LYS B CE  
3164  N NZ  . LYS B 309 ? 2.5881 2.6835 2.3642 0.3210  -0.0850 0.1155  310 LYS B NZ  
3165  N N   . SER B 310 ? 1.9512 2.0086 1.7151 0.2711  -0.1024 0.2187  311 SER B N   
3166  C CA  . SER B 310 ? 1.9597 2.0267 1.7377 0.2625  -0.1104 0.2523  311 SER B CA  
3167  C C   . SER B 310 ? 2.0154 2.0827 1.7548 0.2446  -0.1261 0.2646  311 SER B C   
3168  O O   . SER B 310 ? 2.0171 2.0747 1.7213 0.2385  -0.1258 0.2462  311 SER B O   
3169  C CB  . SER B 310 ? 2.0108 2.0811 1.8257 0.2669  -0.0969 0.2612  311 SER B CB  
3170  O OG  . SER B 310 ? 2.1392 2.1987 1.9448 0.2707  -0.0850 0.2375  311 SER B OG  
3171  N N   . THR B 311 ? 1.9660 2.0450 1.7131 0.2356  -0.1395 0.2962  312 THR B N   
3172  C CA  . THR B 311 ? 1.9765 2.0602 1.6902 0.2167  -0.1563 0.3124  312 THR B CA  
3173  C C   . THR B 311 ? 2.0095 2.0962 1.7153 0.2080  -0.1513 0.3189  312 THR B C   
3174  O O   . THR B 311 ? 2.0237 2.1068 1.6875 0.1957  -0.1568 0.3099  312 THR B O   
3175  C CB  . THR B 311 ? 2.0783 2.1753 1.8109 0.2106  -0.1709 0.3474  312 THR B CB  
3176  O OG1 . THR B 311 ? 2.0544 2.1507 1.8128 0.2242  -0.1693 0.3455  312 THR B OG1 
3177  C CG2 . THR B 311 ? 2.0785 2.1794 1.7713 0.1918  -0.1914 0.3576  312 THR B CG2 
3178  N N   . LYS B 312 ? 1.9288 2.0233 1.6781 0.2147  -0.1402 0.3346  313 LYS B N   
3179  C CA  . LYS B 312 ? 1.9225 2.0237 1.6785 0.2097  -0.1334 0.3447  313 LYS B CA  
3180  C C   . LYS B 312 ? 1.9401 2.0459 1.7555 0.2236  -0.1168 0.3516  313 LYS B C   
3181  O O   . LYS B 312 ? 1.9160 2.0257 1.7700 0.2319  -0.1142 0.3612  313 LYS B O   
3182  C CB  . LYS B 312 ? 1.9681 2.0878 1.7116 0.1900  -0.1489 0.3788  313 LYS B CB  
3183  C CG  . LYS B 312 ? 2.0932 2.2156 1.8020 0.1786  -0.1484 0.3752  313 LYS B CG  
3184  C CD  . LYS B 312 ? 2.2009 2.3145 1.8470 0.1655  -0.1599 0.3561  313 LYS B CD  
3185  C CE  . LYS B 312 ? 2.3312 2.4541 1.9436 0.1499  -0.1622 0.3614  313 LYS B CE  
3186  N NZ  . LYS B 312 ? 2.4535 2.5707 2.0076 0.1344  -0.1742 0.3453  313 LYS B NZ  
3195  N N   . GLN C 3   ? 1.6222 2.0376 1.8771 -0.0580 0.0138  0.1740  3   GLN C N   
3196  C CA  . GLN C 3   ? 1.6236 2.0147 1.8191 -0.0696 0.0185  0.1370  3   GLN C CA  
3197  C C   . GLN C 3   ? 1.6693 2.0867 1.8152 -0.0663 -0.0073 0.1373  3   GLN C C   
3198  O O   . GLN C 3   ? 1.6594 2.0922 1.8191 -0.0631 -0.0076 0.1538  3   GLN C O   
3199  C CB  . GLN C 3   ? 1.6570 2.0133 1.8718 -0.0841 0.0563  0.1218  3   GLN C CB  
3200  C CG  . GLN C 3   ? 1.7824 2.1058 2.0572 -0.0887 0.0932  0.1227  3   GLN C CG  
3201  C CD  . GLN C 3   ? 1.9738 2.3096 2.3297 -0.0758 0.1088  0.1610  3   GLN C CD  
3202  O OE1 . GLN C 3   ? 1.9253 2.2586 2.3008 -0.0776 0.1265  0.1689  3   GLN C OE1 
3203  N NE2 . GLN C 3   ? 1.8358 2.1880 2.2437 -0.0629 0.1025  0.1884  3   GLN C NE2 
3204  N N   . LEU C 4   ? 1.6311 2.0521 1.7234 -0.0664 -0.0261 0.1208  4   LEU C N   
3205  C CA  . LEU C 4   ? 1.6272 2.0687 1.6768 -0.0630 -0.0449 0.1203  4   LEU C CA  
3206  C C   . LEU C 4   ? 1.7001 2.1292 1.7117 -0.0710 -0.0419 0.0967  4   LEU C C   
3207  O O   . LEU C 4   ? 1.6968 2.1090 1.6875 -0.0760 -0.0403 0.0796  4   LEU C O   
3208  C CB  . LEU C 4   ? 1.6204 2.0803 1.6442 -0.0570 -0.0660 0.1263  4   LEU C CB  
3209  C CG  . LEU C 4   ? 1.6729 2.1603 1.7207 -0.0548 -0.0780 0.1556  4   LEU C CG  
3210  C CD1 . LEU C 4   ? 1.6784 2.1771 1.7002 -0.0576 -0.0931 0.1552  4   LEU C CD1 
3211  C CD2 . LEU C 4   ? 1.6914 2.1981 1.7291 -0.0544 -0.0847 0.1692  4   LEU C CD2 
3212  N N   . VAL C 5   ? 1.6748 2.1144 1.6794 -0.0738 -0.0415 0.0981  5   VAL C N   
3213  C CA  . VAL C 5   ? 1.6887 2.1273 1.6636 -0.0841 -0.0416 0.0827  5   VAL C CA  
3214  C C   . VAL C 5   ? 1.7393 2.2018 1.6901 -0.0736 -0.0586 0.0895  5   VAL C C   
3215  O O   . VAL C 5   ? 1.7311 2.2088 1.6897 -0.0701 -0.0599 0.1000  5   VAL C O   
3216  C CB  . VAL C 5   ? 1.7601 2.1913 1.7497 -0.1009 -0.0230 0.0772  5   VAL C CB  
3217  C CG1 . VAL C 5   ? 1.7703 2.2070 1.7272 -0.1184 -0.0264 0.0635  5   VAL C CG1 
3218  C CG2 . VAL C 5   ? 1.7740 2.1751 1.7960 -0.1111 0.0034  0.0715  5   VAL C CG2 
3219  N N   . GLN C 6   ? 1.7027 2.1654 1.6270 -0.0687 -0.0675 0.0839  6   GLN C N   
3220  C CA  . GLN C 6   ? 1.6990 2.1787 1.6061 -0.0584 -0.0761 0.0902  6   GLN C CA  
3221  C C   . GLN C 6   ? 1.7527 2.2487 1.6568 -0.0639 -0.0783 0.0919  6   GLN C C   
3222  O O   . GLN C 6   ? 1.7553 2.2498 1.6608 -0.0801 -0.0754 0.0855  6   GLN C O   
3223  C CB  . GLN C 6   ? 1.7166 2.1875 1.6027 -0.0507 -0.0788 0.0852  6   GLN C CB  
3224  C CG  . GLN C 6   ? 1.8408 2.3084 1.7236 -0.0457 -0.0797 0.0880  6   GLN C CG  
3225  C CD  . GLN C 6   ? 2.0483 2.5052 1.9074 -0.0408 -0.0777 0.0799  6   GLN C CD  
3226  O OE1 . GLN C 6   ? 2.0054 2.4471 1.8604 -0.0429 -0.0768 0.0705  6   GLN C OE1 
3227  N NE2 . GLN C 6   ? 1.9222 2.3835 1.7666 -0.0348 -0.0728 0.0825  6   GLN C NE2 
3228  N N   . SER C 7   ? 1.7035 2.2156 1.6043 -0.0532 -0.0814 0.1012  7   SER C N   
3229  C CA  . SER C 7   ? 1.6988 2.2343 1.6055 -0.0555 -0.0851 0.1094  7   SER C CA  
3230  C C   . SER C 7   ? 1.7662 2.3054 1.6624 -0.0604 -0.0915 0.1100  7   SER C C   
3231  O O   . SER C 7   ? 1.7763 2.2971 1.6588 -0.0554 -0.0902 0.1038  7   SER C O   
3232  C CB  . SER C 7   ? 1.7251 2.2715 1.6380 -0.0405 -0.0810 0.1204  7   SER C CB  
3233  O OG  . SER C 7   ? 1.8024 2.3750 1.7308 -0.0398 -0.0840 0.1333  7   SER C OG  
3234  N N   . GLY C 8   ? 1.7178 2.2834 1.6202 -0.0718 -0.0990 0.1193  8   GLY C N   
3235  C CA  . GLY C 8   ? 1.7229 2.3013 1.6163 -0.0805 -0.1088 0.1269  8   GLY C CA  
3236  C C   . GLY C 8   ? 1.7567 2.3440 1.6607 -0.0584 -0.1085 0.1445  8   GLY C C   
3237  O O   . GLY C 8   ? 1.7463 2.3313 1.6649 -0.0392 -0.0981 0.1495  8   GLY C O   
3238  N N   . ALA C 9   ? 1.7087 2.3042 1.6052 -0.0631 -0.1166 0.1544  9   ALA C N   
3239  C CA  . ALA C 9   ? 1.7027 2.3057 1.6146 -0.0424 -0.1129 0.1750  9   ALA C CA  
3240  C C   . ALA C 9   ? 1.7334 2.3690 1.6861 -0.0281 -0.1097 0.2009  9   ALA C C   
3241  O O   . ALA C 9   ? 1.7250 2.3962 1.6931 -0.0418 -0.1222 0.2136  9   ALA C O   
3242  C CB  . ALA C 9   ? 1.7278 2.3433 1.6278 -0.0553 -0.1263 0.1874  9   ALA C CB  
3243  N N   . GLU C 10  ? 1.6838 2.3047 1.6539 -0.0031 -0.0891 0.2068  10  GLU C N   
3244  C CA  . GLU C 10  ? 1.6795 2.3222 1.6932 0.0124  -0.0771 0.2296  10  GLU C CA  
3245  C C   . GLU C 10  ? 1.7284 2.3739 1.7748 0.0339  -0.0604 0.2555  10  GLU C C   
3246  O O   . GLU C 10  ? 1.7345 2.3437 1.7645 0.0445  -0.0417 0.2433  10  GLU C O   
3247  C CB  . GLU C 10  ? 1.6937 2.3110 1.7015 0.0182  -0.0583 0.2102  10  GLU C CB  
3248  C CG  . GLU C 10  ? 1.8128 2.4336 1.8039 0.0010  -0.0712 0.1937  10  GLU C CG  
3249  C CD  . GLU C 10  ? 1.9907 2.6531 2.0082 -0.0094 -0.0846 0.2099  10  GLU C CD  
3250  O OE1 . GLU C 10  ? 1.8508 2.5353 1.9075 0.0023  -0.0760 0.2315  10  GLU C OE1 
3251  O OE2 . GLU C 10  ? 1.8369 2.5082 1.8373 -0.0309 -0.1005 0.2001  10  GLU C OE2 
3252  N N   . VAL C 11  ? 1.6744 2.3651 1.7712 0.0395  -0.0660 0.2936  11  VAL C N   
3253  C CA  . VAL C 11  ? 1.6829 2.3833 1.8279 0.0623  -0.0476 0.3280  11  VAL C CA  
3254  C C   . VAL C 11  ? 1.7294 2.4493 1.9344 0.0775  -0.0274 0.3508  11  VAL C C   
3255  O O   . VAL C 11  ? 1.7138 2.4806 1.9463 0.0680  -0.0478 0.3706  11  VAL C O   
3256  C CB  . VAL C 11  ? 1.7423 2.4854 1.9019 0.0551  -0.0743 0.3638  11  VAL C CB  
3257  C CG1 . VAL C 11  ? 1.7555 2.5066 1.9731 0.0825  -0.0511 0.4041  11  VAL C CG1 
3258  C CG2 . VAL C 11  ? 1.7442 2.4644 1.8409 0.0357  -0.0923 0.3380  11  VAL C CG2 
3259  N N   . LYS C 12  ? 1.7025 2.3839 1.9261 0.0981  0.0155  0.3460  12  LYS C N   
3260  C CA  . LYS C 12  ? 1.7091 2.3962 1.9909 0.1132  0.0462  0.3640  12  LYS C CA  
3261  C C   . LYS C 12  ? 1.7923 2.4499 2.1153 0.1376  0.0944  0.3796  12  LYS C C   
3262  O O   . LYS C 12  ? 1.8028 2.4147 2.0871 0.1392  0.1132  0.3562  12  LYS C O   
3263  C CB  . LYS C 12  ? 1.7338 2.3900 1.9815 0.1031  0.0585  0.3270  12  LYS C CB  
3264  C CG  . LYS C 12  ? 1.8599 2.5549 2.1056 0.0866  0.0254  0.3271  12  LYS C CG  
3265  C CD  . LYS C 12  ? 1.9506 2.6185 2.1792 0.0813  0.0441  0.3008  12  LYS C CD  
3266  C CE  . LYS C 12  ? 2.0256 2.7278 2.2508 0.0650  0.0145  0.2992  12  LYS C CE  
3267  N NZ  . LYS C 12  ? 2.1245 2.8048 2.3449 0.0627  0.0356  0.2817  12  LYS C NZ  
3268  N N   . LYS C 13  ? 1.7598 2.4428 2.1651 0.1559  0.1175  0.4196  13  LYS C N   
3269  C CA  . LYS C 13  ? 1.7856 2.4400 2.2465 0.1807  0.1728  0.4397  13  LYS C CA  
3270  C C   . LYS C 13  ? 1.8605 2.4440 2.2882 0.1771  0.2257  0.3955  13  LYS C C   
3271  O O   . LYS C 13  ? 1.8457 2.4214 2.2399 0.1613  0.2189  0.3681  13  LYS C O   
3272  C CB  . LYS C 13  ? 1.8178 2.5255 2.3866 0.2005  0.1817  0.5002  13  LYS C CB  
3273  C CG  . LYS C 13  ? 1.9514 2.7329 2.5540 0.2004  0.1317  0.5506  13  LYS C CG  
3274  C CD  . LYS C 13  ? 2.0498 2.8969 2.7612 0.2153  0.1322  0.6137  13  LYS C CD  
3275  C CE  . LYS C 13  ? 2.1303 3.0615 2.8600 0.2026  0.0711  0.6607  13  LYS C CE  
3276  N NZ  . LYS C 13  ? 2.1649 3.1361 2.9903 0.2148  0.0688  0.7066  13  LYS C NZ  
3277  N N   . PRO C 14  ? 1.8551 2.3853 2.2854 0.1873  0.2789  0.3867  14  PRO C N   
3278  C CA  . PRO C 14  ? 1.8872 2.3492 2.2725 0.1742  0.3291  0.3409  14  PRO C CA  
3279  C C   . PRO C 14  ? 1.9607 2.4135 2.3823 0.1730  0.3633  0.3412  14  PRO C C   
3280  O O   . PRO C 14  ? 1.9557 2.4438 2.4661 0.1925  0.3734  0.3845  14  PRO C O   
3281  C CB  . PRO C 14  ? 1.9470 2.3615 2.3450 0.1860  0.3837  0.3407  14  PRO C CB  
3282  C CG  . PRO C 14  ? 1.9820 2.4337 2.3936 0.1991  0.3453  0.3705  14  PRO C CG  
3283  C CD  . PRO C 14  ? 1.8909 2.4186 2.3576 0.2069  0.2964  0.4154  14  PRO C CD  
3284  N N   . GLY C 15  ? 1.9359 2.3441 2.2878 0.1481  0.3791  0.2943  15  GLY C N   
3285  C CA  . GLY C 15  ? 1.9533 2.3421 2.3168 0.1389  0.4119  0.2837  15  GLY C CA  
3286  C C   . GLY C 15  ? 1.9659 2.3889 2.2950 0.1239  0.3593  0.2733  15  GLY C C   
3287  O O   . GLY C 15  ? 1.9814 2.3758 2.2731 0.1041  0.3763  0.2457  15  GLY C O   
3288  N N   . GLU C 16  ? 1.8748 2.3572 2.2133 0.1302  0.2973  0.2949  16  GLU C N   
3289  C CA  . GLU C 16  ? 1.8406 2.3608 2.1540 0.1172  0.2459  0.2893  16  GLU C CA  
3290  C C   . GLU C 16  ? 1.8999 2.3898 2.1206 0.0910  0.2295  0.2447  16  GLU C C   
3291  O O   . GLU C 16  ? 1.9116 2.3609 2.0801 0.0809  0.2448  0.2190  16  GLU C O   
3292  C CB  . GLU C 16  ? 1.8197 2.4022 2.1554 0.1238  0.1906  0.3188  16  GLU C CB  
3293  C CG  . GLU C 16  ? 1.9440 2.5813 2.3742 0.1420  0.1884  0.3699  16  GLU C CG  
3294  C CD  . GLU C 16  ? 2.1735 2.8766 2.6133 0.1377  0.1301  0.3968  16  GLU C CD  
3295  O OE1 . GLU C 16  ? 2.1364 2.8581 2.5985 0.1477  0.1216  0.4237  16  GLU C OE1 
3296  O OE2 . GLU C 16  ? 2.0420 2.7759 2.4635 0.1212  0.0950  0.3901  16  GLU C OE2 
3297  N N   . SER C 17  ? 1.8478 2.3605 2.0521 0.0795  0.1987  0.2384  17  SER C N   
3298  C CA  . SER C 17  ? 1.8490 2.3436 1.9785 0.0565  0.1787  0.2056  17  SER C CA  
3299  C C   . SER C 17  ? 1.8511 2.3821 1.9619 0.0527  0.1240  0.2077  17  SER C C   
3300  O O   . SER C 17  ? 1.8131 2.3877 1.9597 0.0570  0.0986  0.2276  17  SER C O   
3301  C CB  . SER C 17  ? 1.9257 2.4117 2.0507 0.0453  0.1920  0.1966  17  SER C CB  
3302  O OG  . SER C 17  ? 2.0782 2.5479 2.1345 0.0230  0.1746  0.1705  17  SER C OG  
3303  N N   . LEU C 18  ? 1.8117 2.3241 1.8674 0.0420  0.1092  0.1869  18  LEU C N   
3304  C CA  . LEU C 18  ? 1.7820 2.3172 1.8163 0.0359  0.0659  0.1842  18  LEU C CA  
3305  C C   . LEU C 18  ? 1.8438 2.3583 1.8215 0.0178  0.0550  0.1592  18  LEU C C   
3306  O O   . LEU C 18  ? 1.8627 2.3443 1.8062 0.0091  0.0760  0.1433  18  LEU C O   
3307  C CB  . LEU C 18  ? 1.7760 2.3130 1.8133 0.0447  0.0592  0.1911  18  LEU C CB  
3308  C CG  . LEU C 18  ? 1.8037 2.3616 1.8239 0.0373  0.0200  0.1896  18  LEU C CG  
3309  C CD1 . LEU C 18  ? 1.7908 2.3952 1.8518 0.0399  -0.0014 0.2160  18  LEU C CD1 
3310  C CD2 . LEU C 18  ? 1.8278 2.3650 1.8239 0.0394  0.0209  0.1811  18  LEU C CD2 
3311  N N   . THR C 19  ? 1.7807 2.3153 1.7505 0.0101  0.0241  0.1578  19  THR C N   
3312  C CA  . THR C 19  ? 1.7749 2.2974 1.7044 -0.0046 0.0109  0.1424  19  THR C CA  
3313  C C   . THR C 19  ? 1.7740 2.3109 1.7018 -0.0072 -0.0176 0.1417  19  THR C C   
3314  O O   . THR C 19  ? 1.7594 2.3210 1.7105 -0.0072 -0.0312 0.1502  19  THR C O   
3315  C CB  . THR C 19  ? 1.9147 2.4362 1.8378 -0.0139 0.0155  0.1409  19  THR C CB  
3316  O OG1 . THR C 19  ? 1.9029 2.4204 1.7967 -0.0266 -0.0010 0.1342  19  THR C OG1 
3317  C CG2 . THR C 19  ? 1.8958 2.4447 1.8566 -0.0090 0.0093  0.1529  19  THR C CG2 
3318  N N   . ILE C 20  ? 1.6960 2.2169 1.5965 -0.0121 -0.0237 0.1309  20  ILE C N   
3319  C CA  . ILE C 20  ? 1.6583 2.1847 1.5574 -0.0158 -0.0440 0.1277  20  ILE C CA  
3320  C C   . ILE C 20  ? 1.6745 2.1959 1.5609 -0.0263 -0.0536 0.1226  20  ILE C C   
3321  O O   . ILE C 20  ? 1.6772 2.1872 1.5423 -0.0319 -0.0494 0.1193  20  ILE C O   
3322  C CB  . ILE C 20  ? 1.6952 2.2108 1.5857 -0.0110 -0.0438 0.1233  20  ILE C CB  
3323  C CG1 . ILE C 20  ? 1.7151 2.2056 1.5788 -0.0117 -0.0278 0.1130  20  ILE C CG1 
3324  C CG2 . ILE C 20  ? 1.7046 2.2366 1.6203 -0.0012 -0.0418 0.1374  20  ILE C CG2 
3325  C CD1 . ILE C 20  ? 1.8014 2.2773 1.6500 -0.0110 -0.0300 0.1040  20  ILE C CD1 
3326  N N   . SER C 21  ? 1.6047 2.1362 1.5062 -0.0312 -0.0647 0.1240  21  SER C N   
3327  C CA  . SER C 21  ? 1.5945 2.1231 1.4992 -0.0387 -0.0702 0.1246  21  SER C CA  
3328  C C   . SER C 21  ? 1.6370 2.1534 1.5385 -0.0415 -0.0755 0.1187  21  SER C C   
3329  O O   . SER C 21  ? 1.6314 2.1404 1.5239 -0.0391 -0.0760 0.1112  21  SER C O   
3330  C CB  . SER C 21  ? 1.6286 2.1683 1.5549 -0.0440 -0.0705 0.1277  21  SER C CB  
3331  O OG  . SER C 21  ? 1.7246 2.2712 1.6574 -0.0489 -0.0732 0.1228  21  SER C OG  
3332  N N   . CYS C 22  ? 1.5909 2.1060 1.5040 -0.0461 -0.0781 0.1248  22  CYS C N   
3333  C CA  . CYS C 22  ? 1.5846 2.0905 1.5066 -0.0486 -0.0809 0.1239  22  CYS C CA  
3334  C C   . CYS C 22  ? 1.6178 2.1288 1.5712 -0.0517 -0.0787 0.1381  22  CYS C C   
3335  O O   . CYS C 22  ? 1.6140 2.1368 1.5681 -0.0525 -0.0832 0.1536  22  CYS C O   
3336  C CB  . CYS C 22  ? 1.5960 2.1005 1.4956 -0.0492 -0.0858 0.1242  22  CYS C CB  
3337  S SG  . CYS C 22  ? 1.6550 2.1621 1.5753 -0.0542 -0.0930 0.1354  22  CYS C SG  
3338  N N   . LYS C 23  ? 1.5652 2.0663 1.5433 -0.0558 -0.0686 0.1334  23  LYS C N   
3339  C CA  . LYS C 23  ? 1.5629 2.0632 1.5782 -0.0582 -0.0577 0.1460  23  LYS C CA  
3340  C C   . LYS C 23  ? 1.6110 2.1018 1.6624 -0.0579 -0.0508 0.1554  23  LYS C C   
3341  O O   . LYS C 23  ? 1.5958 2.0664 1.6548 -0.0633 -0.0394 0.1409  23  LYS C O   
3342  C CB  . LYS C 23  ? 1.5970 2.0899 1.6181 -0.0674 -0.0430 0.1334  23  LYS C CB  
3343  C CG  . LYS C 23  ? 1.7303 2.2286 1.7753 -0.0681 -0.0323 0.1457  23  LYS C CG  
3344  C CD  . LYS C 23  ? 1.8430 2.3233 1.9313 -0.0731 -0.0088 0.1506  23  LYS C CD  
3345  C CE  . LYS C 23  ? 1.9496 2.4330 2.0625 -0.0733 0.0054  0.1631  23  LYS C CE  
3346  N NZ  . LYS C 23  ? 2.0726 2.5380 2.2388 -0.0739 0.0324  0.1755  23  LYS C NZ  
3347  N N   . GLY C 24  ? 1.5858 2.0926 1.6613 -0.0534 -0.0570 0.1821  24  GLY C N   
3348  C CA  . GLY C 24  ? 1.5918 2.0988 1.7153 -0.0511 -0.0517 0.2016  24  GLY C CA  
3349  C C   . GLY C 24  ? 1.6573 2.1458 1.8311 -0.0521 -0.0229 0.2055  24  GLY C C   
3350  O O   . GLY C 24  ? 1.6611 2.1529 1.8454 -0.0520 -0.0142 0.2137  24  GLY C O   
3351  N N   . SER C 25  ? 1.6174 2.0823 1.8218 -0.0549 -0.0036 0.1975  25  SER C N   
3352  C CA  . SER C 25  ? 1.6275 2.0648 1.8793 -0.0603 0.0339  0.1955  25  SER C CA  
3353  C C   . SER C 25  ? 1.6745 2.1037 1.9984 -0.0543 0.0533  0.2186  25  SER C C   
3354  O O   . SER C 25  ? 1.6608 2.0910 1.9887 -0.0521 0.0440  0.2184  25  SER C O   
3355  C CB  . SER C 25  ? 1.6822 2.0873 1.8989 -0.0780 0.0521  0.1556  25  SER C CB  
3356  O OG  . SER C 25  ? 1.7620 2.1802 1.9165 -0.0822 0.0294  0.1377  25  SER C OG  
3357  N N   . GLY C 26  ? 1.6422 2.0621 2.0266 -0.0517 0.0834  0.2387  26  GLY C N   
3358  C CA  . GLY C 26  ? 1.6481 2.0583 2.1184 -0.0445 0.1113  0.2661  26  GLY C CA  
3359  C C   . GLY C 26  ? 1.6791 2.1342 2.1951 -0.0290 0.0838  0.3151  26  GLY C C   
3360  O O   . GLY C 26  ? 1.6817 2.1339 2.2690 -0.0226 0.1010  0.3379  26  GLY C O   
3361  N N   . TYR C 27  ? 1.6121 2.1097 2.0892 -0.0257 0.0426  0.3332  27  TYR C N   
3362  C CA  . TYR C 27  ? 1.5989 2.1468 2.1055 -0.0191 0.0107  0.3812  27  TYR C CA  
3363  C C   . TYR C 27  ? 1.6464 2.2305 2.1189 -0.0206 -0.0181 0.4037  27  TYR C C   
3364  O O   . TYR C 27  ? 1.6386 2.2086 2.0538 -0.0253 -0.0180 0.3754  27  TYR C O   
3365  C CB  . TYR C 27  ? 1.5983 2.1591 2.0730 -0.0241 -0.0159 0.3697  27  TYR C CB  
3366  C CG  . TYR C 27  ? 1.6079 2.1820 1.9878 -0.0334 -0.0498 0.3449  27  TYR C CG  
3367  C CD1 . TYR C 27  ? 1.6283 2.1697 1.9438 -0.0381 -0.0431 0.2966  27  TYR C CD1 
3368  C CD2 . TYR C 27  ? 1.6170 2.2368 1.9736 -0.0403 -0.0860 0.3714  27  TYR C CD2 
3369  C CE1 . TYR C 27  ? 1.6289 2.1804 1.8684 -0.0445 -0.0679 0.2772  27  TYR C CE1 
3370  C CE2 . TYR C 27  ? 1.6246 2.2497 1.8964 -0.0511 -0.1083 0.3466  27  TYR C CE2 
3371  C CZ  . TYR C 27  ? 1.6828 2.2722 1.9009 -0.0507 -0.0973 0.3002  27  TYR C CZ  
3372  O OH  . TYR C 27  ? 1.6633 2.2562 1.8087 -0.0593 -0.1135 0.2793  27  TYR C OH  
3373  N N   . SER C 28  ? 1.6064 2.2392 2.1135 -0.0193 -0.0433 0.4560  28  SER C N   
3374  C CA  . SER C 28  ? 1.6127 2.2821 2.0852 -0.0261 -0.0718 0.4813  28  SER C CA  
3375  C C   . SER C 28  ? 1.6643 2.3428 2.0401 -0.0417 -0.1036 0.4507  28  SER C C   
3376  O O   . SER C 28  ? 1.6618 2.3755 2.0225 -0.0533 -0.1328 0.4686  28  SER C O   
3377  C CB  . SER C 28  ? 1.6678 2.3898 2.2082 -0.0248 -0.0894 0.5502  28  SER C CB  
3378  O OG  . SER C 28  ? 1.7909 2.5478 2.2881 -0.0371 -0.1183 0.5741  28  SER C OG  
3379  N N   . PHE C 29  ? 1.6262 2.2722 1.9402 -0.0433 -0.0944 0.4045  29  PHE C N   
3380  C CA  . PHE C 29  ? 1.6289 2.2714 1.8564 -0.0548 -0.1124 0.3697  29  PHE C CA  
3381  C C   . PHE C 29  ? 1.7003 2.3810 1.8854 -0.0723 -0.1433 0.3922  29  PHE C C   
3382  O O   . PHE C 29  ? 1.7010 2.3869 1.8351 -0.0852 -0.1584 0.3749  29  PHE C O   
3383  C CB  . PHE C 29  ? 1.6476 2.2590 1.8373 -0.0518 -0.0958 0.3334  29  PHE C CB  
3384  C CG  . PHE C 29  ? 1.6648 2.2679 1.7790 -0.0595 -0.1060 0.2988  29  PHE C CG  
3385  C CD1 . PHE C 29  ? 1.6913 2.2735 1.7833 -0.0580 -0.1020 0.2659  29  PHE C CD1 
3386  C CD2 . PHE C 29  ? 1.7039 2.3172 1.7729 -0.0683 -0.1155 0.2999  29  PHE C CD2 
3387  C CE1 . PHE C 29  ? 1.7038 2.2779 1.7360 -0.0625 -0.1069 0.2385  29  PHE C CE1 
3388  C CE2 . PHE C 29  ? 1.7414 2.3427 1.7507 -0.0740 -0.1172 0.2692  29  PHE C CE2 
3389  C CZ  . PHE C 29  ? 1.7043 2.2873 1.6989 -0.0698 -0.1127 0.2406  29  PHE C CZ  
3390  N N   . SER C 30  ? 2.0347 2.2270 1.7256 -0.1219 0.1778  0.3466  30  SER C N   
3391  C CA  . SER C 30  ? 2.0567 2.2565 1.7058 -0.1216 0.1466  0.3806  30  SER C CA  
3392  C C   . SER C 30  ? 2.0755 2.3185 1.7740 -0.0736 0.1085  0.3927  30  SER C C   
3393  O O   . SER C 30  ? 2.0501 2.3426 1.7297 -0.0807 0.0872  0.4065  30  SER C O   
3394  C CB  . SER C 30  ? 2.2319 2.3233 1.7964 -0.1398 0.1425  0.4150  30  SER C CB  
3395  O OG  . SER C 30  ? 2.3607 2.4236 1.8750 -0.1930 0.1785  0.4017  30  SER C OG  
3396  N N   . SER C 31  ? 2.0307 2.2606 1.7950 -0.0276 0.1024  0.3837  31  SER C N   
3397  C CA  . SER C 31  ? 2.0120 2.2933 1.8386 0.0209  0.0657  0.3905  31  SER C CA  
3398  C C   . SER C 31  ? 1.9237 2.3225 1.7953 0.0144  0.0672  0.3619  31  SER C C   
3399  O O   . SER C 31  ? 1.9066 2.3574 1.7760 0.0213  0.0358  0.3781  31  SER C O   
3400  C CB  . SER C 31  ? 2.1007 2.3459 1.9999 0.0709  0.0666  0.3785  31  SER C CB  
3401  O OG  . SER C 31  ? 2.3433 2.4736 2.2015 0.0905  0.0508  0.4152  31  SER C OG  
3402  N N   . TYR C 32  ? 1.7859 2.2192 1.6880 -0.0037 0.1035  0.3205  32  TYR C N   
3403  C CA  . TYR C 32  ? 1.6804 2.2065 1.6166 -0.0133 0.1103  0.2904  32  TYR C CA  
3404  C C   . TYR C 32  ? 1.6533 2.2043 1.5354 -0.0558 0.1217  0.2904  32  TYR C C   
3405  O O   . TYR C 32  ? 1.6524 2.1625 1.4917 -0.0842 0.1405  0.2937  32  TYR C O   
3406  C CB  . TYR C 32  ? 1.6637 2.2037 1.6538 -0.0128 0.1419  0.2465  32  TYR C CB  
3407  C CG  . TYR C 32  ? 1.7417 2.2637 1.8012 0.0294  0.1409  0.2341  32  TYR C CG  
3408  C CD1 . TYR C 32  ? 1.7448 2.3403 1.8796 0.0577  0.1300  0.2116  32  TYR C CD1 
3409  C CD2 . TYR C 32  ? 1.8236 2.2570 1.8779 0.0386  0.1561  0.2383  32  TYR C CD2 
3410  C CE1 . TYR C 32  ? 1.7973 2.3865 2.0119 0.0997  0.1321  0.1935  32  TYR C CE1 
3411  C CE2 . TYR C 32  ? 1.8812 2.2944 2.0078 0.0813  0.1598  0.2219  32  TYR C CE2 
3412  C CZ  . TYR C 32  ? 1.9412 2.4367 2.1538 0.1142  0.1472  0.1987  32  TYR C CZ  
3413  O OH  . TYR C 32  ? 1.9904 2.4769 2.2894 0.1605  0.1519  0.1777  32  TYR C OH  
3414  N N   . TRP C 33  ? 1.5535 2.1744 1.4425 -0.0607 0.1128  0.2823  33  TRP C N   
3415  C CA  . TRP C 33  ? 1.5138 2.1625 1.3634 -0.0942 0.1247  0.2774  33  TRP C CA  
3416  C C   . TRP C 33  ? 1.5001 2.1563 1.3620 -0.1119 0.1533  0.2469  33  TRP C C   
3417  O O   . TRP C 33  ? 1.4913 2.1528 1.3926 -0.1024 0.1629  0.2234  33  TRP C O   
3418  C CB  . TRP C 33  ? 1.4771 2.1899 1.3312 -0.0937 0.1103  0.2734  33  TRP C CB  
3419  C CG  . TRP C 33  ? 1.5498 2.2634 1.3740 -0.0895 0.0799  0.3055  33  TRP C CG  
3420  C CD1 . TRP C 33  ? 1.6388 2.3470 1.4844 -0.0592 0.0477  0.3264  33  TRP C CD1 
3421  C CD2 . TRP C 33  ? 1.5619 2.2857 1.3292 -0.1181 0.0774  0.3187  33  TRP C CD2 
3422  N NE1 . TRP C 33  ? 1.6795 2.3897 1.4752 -0.0703 0.0207  0.3570  33  TRP C NE1 
3423  C CE2 . TRP C 33  ? 1.6741 2.3936 1.4188 -0.1100 0.0418  0.3504  33  TRP C CE2 
3424  C CE3 . TRP C 33  ? 1.5514 2.2866 1.2865 -0.1497 0.1022  0.3058  33  TRP C CE3 
3425  C CZ2 . TRP C 33  ? 1.7025 2.4261 1.3830 -0.1407 0.0333  0.3682  33  TRP C CZ2 
3426  C CZ3 . TRP C 33  ? 1.6031 2.3446 1.2852 -0.1758 0.0984  0.3190  33  TRP C CZ3 
3427  C CH2 . TRP C 33  ? 1.6753 2.4095 1.3253 -0.1754 0.0658  0.3493  33  TRP C CH2 
3428  N N   . ILE C 34  ? 1.4097 2.0685 1.2387 -0.1388 0.1659  0.2461  34  ILE C N   
3429  C CA  . ILE C 34  ? 1.3546 2.0231 1.1896 -0.1559 0.1844  0.2231  34  ILE C CA  
3430  C C   . ILE C 34  ? 1.3513 2.0608 1.1759 -0.1652 0.1850  0.2155  34  ILE C C   
3431  O O   . ILE C 34  ? 1.3434 2.0620 1.1457 -0.1740 0.1843  0.2266  34  ILE C O   
3432  C CB  . ILE C 34  ? 1.4113 2.0444 1.2283 -0.1768 0.1984  0.2258  34  ILE C CB  
3433  C CG1 . ILE C 34  ? 1.4645 2.0431 1.2887 -0.1696 0.2045  0.2277  34  ILE C CG1 
3434  C CG2 . ILE C 34  ? 1.3799 2.0342 1.1990 -0.1965 0.2087  0.2073  34  ILE C CG2 
3435  C CD1 . ILE C 34  ? 1.5219 2.0984 1.3822 -0.1618 0.2152  0.2013  34  ILE C CD1 
3436  N N   . GLY C 35  ? 1.2871 2.0147 1.1244 -0.1657 0.1892  0.1945  35  GLY C N   
3437  C CA  . GLY C 35  ? 1.2649 2.0161 1.0888 -0.1723 0.1910  0.1859  35  GLY C CA  
3438  C C   . GLY C 35  ? 1.3147 2.0582 1.1324 -0.1845 0.1968  0.1776  35  GLY C C   
3439  O O   . GLY C 35  ? 1.3183 2.0447 1.1396 -0.1935 0.1998  0.1779  35  GLY C O   
3440  N N   . TRP C 36  ? 1.2681 2.0212 1.0738 -0.1855 0.1968  0.1707  36  TRP C N   
3441  C CA  . TRP C 36  ? 1.2734 2.0181 1.0726 -0.1917 0.1942  0.1669  36  TRP C CA  
3442  C C   . TRP C 36  ? 1.3098 2.0417 1.0863 -0.1924 0.1936  0.1556  36  TRP C C   
3443  O O   . TRP C 36  ? 1.3108 2.0499 1.0788 -0.1864 0.1982  0.1529  36  TRP C O   
3444  C CB  . TRP C 36  ? 1.2669 2.0313 1.0787 -0.1884 0.1936  0.1755  36  TRP C CB  
3445  C CG  . TRP C 36  ? 1.2948 2.0638 1.1184 -0.1989 0.1951  0.1830  36  TRP C CG  
3446  C CD1 . TRP C 36  ? 1.3469 2.1166 1.1695 -0.2031 0.2020  0.1921  36  TRP C CD1 
3447  C CD2 . TRP C 36  ? 1.3048 2.0739 1.1339 -0.2122 0.1899  0.1823  36  TRP C CD2 
3448  N NE1 . TRP C 36  ? 1.3565 2.1223 1.1824 -0.2190 0.2052  0.1949  36  TRP C NE1 
3449  C CE2 . TRP C 36  ? 1.3682 2.1393 1.2012 -0.2256 0.1981  0.1878  36  TRP C CE2 
3450  C CE3 . TRP C 36  ? 1.3304 2.0947 1.1540 -0.2184 0.1773  0.1787  36  TRP C CE3 
3451  C CZ2 . TRP C 36  ? 1.3731 2.1482 1.2085 -0.2467 0.1976  0.1861  36  TRP C CZ2 
3452  C CZ3 . TRP C 36  ? 1.3641 2.1357 1.1908 -0.2381 0.1722  0.1798  36  TRP C CZ3 
3453  C CH2 . TRP C 36  ? 1.3780 2.1583 1.2127 -0.2529 0.1839  0.1817  36  TRP C CH2 
3454  N N   . VAL C 37  ? 1.2566 1.9627 1.0140 -0.2056 0.1897  0.1481  37  VAL C N   
3455  C CA  . VAL C 37  ? 1.2684 1.9454 0.9882 -0.2138 0.1893  0.1380  37  VAL C CA  
3456  C C   . VAL C 37  ? 1.3425 1.9906 1.0401 -0.2171 0.1727  0.1468  37  VAL C C   
3457  O O   . VAL C 37  ? 1.3467 1.9872 1.0394 -0.2324 0.1646  0.1496  37  VAL C O   
3458  C CB  . VAL C 37  ? 1.3224 1.9907 1.0275 -0.2338 0.2010  0.1173  37  VAL C CB  
3459  C CG1 . VAL C 37  ? 1.3622 1.9907 1.0138 -0.2529 0.2034  0.1050  37  VAL C CG1 
3460  C CG2 . VAL C 37  ? 1.2945 1.9998 1.0284 -0.2241 0.2097  0.1105  37  VAL C CG2 
3461  N N   . ARG C 38  ? 1.3198 1.9502 1.0033 -0.2025 0.1667  0.1515  38  ARG C N   
3462  C CA  . ARG C 38  ? 1.3590 1.9579 1.0236 -0.1963 0.1444  0.1637  38  ARG C CA  
3463  C C   . ARG C 38  ? 1.4841 2.0176 1.0784 -0.2189 0.1417  0.1580  38  ARG C C   
3464  O O   . ARG C 38  ? 1.4971 2.0153 1.0642 -0.2322 0.1614  0.1415  38  ARG C O   
3465  C CB  . ARG C 38  ? 1.3584 1.9676 1.0517 -0.1633 0.1422  0.1691  38  ARG C CB  
3466  C CG  . ARG C 38  ? 1.5352 2.1000 1.2088 -0.1466 0.1177  0.1813  38  ARG C CG  
3467  C CD  . ARG C 38  ? 1.6449 2.2369 1.3732 -0.1085 0.1157  0.1835  38  ARG C CD  
3468  N NE  . ARG C 38  ? 1.7914 2.3290 1.4918 -0.0922 0.1260  0.1773  38  ARG C NE  
3469  C CZ  . ARG C 38  ? 1.9904 2.5331 1.7325 -0.0566 0.1279  0.1747  38  ARG C CZ  
3470  N NH1 . ARG C 38  ? 1.7287 2.3387 1.5477 -0.0340 0.1189  0.1763  38  ARG C NH1 
3471  N NH2 . ARG C 38  ? 1.9391 2.4197 1.6475 -0.0452 0.1420  0.1667  38  ARG C NH2 
3472  N N   . ARG C 39  ? 1.4960 1.9919 1.0567 -0.2273 0.1161  0.1717  39  ARG C N   
3473  C CA  . ARG C 39  ? 1.5755 1.9955 1.0538 -0.2545 0.1091  0.1708  39  ARG C CA  
3474  C C   . ARG C 39  ? 1.7136 2.0953 1.1752 -0.2333 0.0712  0.1976  39  ARG C C   
3475  O O   . ARG C 39  ? 1.7195 2.1252 1.2010 -0.2322 0.0441  0.2138  39  ARG C O   
3476  C CB  . ARG C 39  ? 1.5822 1.9939 1.0257 -0.3015 0.1165  0.1579  39  ARG C CB  
3477  C CG  . ARG C 39  ? 1.7243 2.0571 1.0742 -0.3400 0.0995  0.1635  39  ARG C CG  
3478  C CD  . ARG C 39  ? 1.7187 1.9927 0.9976 -0.3692 0.1217  0.1435  39  ARG C CD  
3479  N NE  . ARG C 39  ? 1.6691 1.9687 0.9482 -0.4084 0.1564  0.1087  39  ARG C NE  
3480  C CZ  . ARG C 39  ? 1.8875 2.1627 1.1224 -0.4404 0.1844  0.0802  39  ARG C CZ  
3481  N NH1 . ARG C 39  ? 1.8030 2.0171 0.9775 -0.4422 0.1834  0.0839  39  ARG C NH1 
3482  N NH2 . ARG C 39  ? 1.6963 2.0091 0.9500 -0.4712 0.2156  0.0451  39  ARG C NH2 
3483  N N   . MET C 40  ? 1.7301 2.0552 1.1600 -0.2144 0.0686  0.2021  40  MET C N   
3484  C CA  . MET C 40  ? 1.8009 2.0815 1.2187 -0.1858 0.0293  0.2292  40  MET C CA  
3485  C C   . MET C 40  ? 1.9556 2.1443 1.2682 -0.2228 0.0037  0.2439  40  MET C C   
3486  O O   . MET C 40  ? 1.9800 2.1213 1.2198 -0.2675 0.0283  0.2259  40  MET C O   
3487  C CB  . MET C 40  ? 1.8525 2.1064 1.2887 -0.1435 0.0389  0.2274  40  MET C CB  
3488  C CG  . MET C 40  ? 1.8322 2.1707 1.3764 -0.0976 0.0390  0.2270  40  MET C CG  
3489  S SD  . MET C 40  ? 1.9528 2.2494 1.5274 -0.0372 0.0261  0.2356  40  MET C SD  
3490  C CE  . MET C 40  ? 1.9975 2.2551 1.5514 -0.0219 -0.0406 0.2739  40  MET C CE  
3491  N N   . PRO C 41  ? 1.9800 2.1461 1.2808 -0.2099 -0.0462 0.2753  41  PRO C N   
3492  C CA  . PRO C 41  ? 2.0955 2.1660 1.2807 -0.2526 -0.0741 0.2928  41  PRO C CA  
3493  C C   . PRO C 41  ? 2.2346 2.1869 1.3183 -0.2679 -0.0614 0.2899  41  PRO C C   
3494  O O   . PRO C 41  ? 2.2803 2.1817 1.3655 -0.2237 -0.0730 0.3033  41  PRO C O   
3495  C CB  . PRO C 41  ? 2.1724 2.2485 1.3796 -0.2206 -0.1367 0.3316  41  PRO C CB  
3496  C CG  . PRO C 41  ? 2.1608 2.3126 1.4897 -0.1519 -0.1364 0.3308  41  PRO C CG  
3497  C CD  . PRO C 41  ? 1.9801 2.2112 1.3706 -0.1602 -0.0812 0.2955  41  PRO C CD  
3498  N N   . GLY C 42  ? 2.2090 2.1206 1.2083 -0.3328 -0.0327 0.2676  42  GLY C N   
3499  C CA  . GLY C 42  ? 2.2988 2.1009 1.1883 -0.3661 -0.0124 0.2569  42  GLY C CA  
3500  C C   . GLY C 42  ? 2.2823 2.1050 1.2091 -0.3475 0.0339  0.2279  42  GLY C C   
3501  O O   . GLY C 42  ? 2.3650 2.0950 1.2237 -0.3473 0.0422  0.2281  42  GLY C O   
3502  N N   . LYS C 43  ? 2.1003 2.0391 1.1290 -0.3344 0.0632  0.2039  43  LYS C N   
3503  C CA  . LYS C 43  ? 2.0365 2.0146 1.1077 -0.3210 0.1047  0.1765  43  LYS C CA  
3504  C C   . LYS C 43  ? 1.9877 2.0572 1.1044 -0.3506 0.1391  0.1436  43  LYS C C   
3505  O O   . LYS C 43  ? 1.9689 2.0668 1.0889 -0.3776 0.1342  0.1403  43  LYS C O   
3506  C CB  . LYS C 43  ? 2.0178 2.0423 1.1825 -0.2541 0.0964  0.1893  43  LYS C CB  
3507  C CG  . LYS C 43  ? 2.2765 2.2045 1.4009 -0.2215 0.0828  0.2061  43  LYS C CG  
3508  C CD  . LYS C 43  ? 2.4273 2.3360 1.5748 -0.1793 0.0289  0.2443  43  LYS C CD  
3509  C CE  . LYS C 43  ? 2.6731 2.4476 1.7409 -0.1610 0.0056  0.2667  43  LYS C CE  
3510  N NZ  . LYS C 43  ? 2.7846 2.5387 1.8914 -0.1143 0.0289  0.2560  43  LYS C NZ  
3511  N N   . GLY C 44  ? 1.8882 1.9989 1.0364 -0.3467 0.1728  0.1190  44  GLY C N   
3512  C CA  . GLY C 44  ? 1.7978 1.9967 0.9968 -0.3661 0.2009  0.0898  44  GLY C CA  
3513  C C   . GLY C 44  ? 1.7333 2.0279 1.0383 -0.3278 0.1940  0.0986  44  GLY C C   
3514  O O   . GLY C 44  ? 1.7222 2.0248 1.0664 -0.2884 0.1718  0.1234  44  GLY C O   
3515  N N   . LEU C 45  ? 1.6012 1.9684 0.9539 -0.3397 0.2133  0.0772  45  LEU C N   
3516  C CA  . LEU C 45  ? 1.5036 1.9505 0.9449 -0.3092 0.2093  0.0850  45  LEU C CA  
3517  C C   . LEU C 45  ? 1.5310 2.0147 1.0109 -0.2800 0.2170  0.0873  45  LEU C C   
3518  O O   . LEU C 45  ? 1.5249 2.0188 0.9904 -0.2934 0.2363  0.0684  45  LEU C O   
3519  C CB  . LEU C 45  ? 1.4559 1.9543 0.9323 -0.3285 0.2242  0.0635  45  LEU C CB  
3520  C CG  . LEU C 45  ? 1.5351 2.0077 0.9852 -0.3593 0.2216  0.0579  45  LEU C CG  
3521  C CD1 . LEU C 45  ? 1.5250 2.0348 0.9973 -0.3855 0.2477  0.0232  45  LEU C CD1 
3522  C CD2 . LEU C 45  ? 1.5185 2.0050 1.0039 -0.3401 0.2010  0.0820  45  LEU C CD2 
3523  N N   . GLU C 46  ? 1.4745 1.9803 1.0001 -0.2458 0.2033  0.1080  46  GLU C N   
3524  C CA  . GLU C 46  ? 1.4498 1.9887 1.0101 -0.2220 0.2121  0.1100  46  GLU C CA  
3525  C C   . GLU C 46  ? 1.4420 2.0497 1.0627 -0.2123 0.2117  0.1149  46  GLU C C   
3526  O O   . GLU C 46  ? 1.4116 2.0334 1.0604 -0.2058 0.1987  0.1267  46  GLU C O   
3527  C CB  . GLU C 46  ? 1.4979 2.0101 1.0672 -0.1922 0.2005  0.1254  46  GLU C CB  
3528  C CG  . GLU C 46  ? 1.7771 2.2046 1.2832 -0.1943 0.1963  0.1263  46  GLU C CG  
3529  C CD  . GLU C 46  ? 2.2183 2.6176 1.7416 -0.1598 0.1721  0.1462  46  GLU C CD  
3530  O OE1 . GLU C 46  ? 2.3248 2.6779 1.8129 -0.1648 0.1459  0.1612  46  GLU C OE1 
3531  O OE2 . GLU C 46  ? 2.1237 2.5485 1.6957 -0.1292 0.1789  0.1454  46  GLU C OE2 
3532  N N   . TRP C 47  ? 1.3959 2.0418 1.0300 -0.2146 0.2243  0.1069  47  TRP C N   
3533  C CA  . TRP C 47  ? 1.3597 2.0579 1.0399 -0.2053 0.2208  0.1160  47  TRP C CA  
3534  C C   . TRP C 47  ? 1.4082 2.1203 1.1088 -0.1886 0.2224  0.1274  47  TRP C C   
3535  O O   . TRP C 47  ? 1.4190 2.1204 1.1029 -0.1874 0.2345  0.1205  47  TRP C O   
3536  C CB  . TRP C 47  ? 1.3372 2.0715 1.0204 -0.2165 0.2267  0.1051  47  TRP C CB  
3537  C CG  . TRP C 47  ? 1.3265 2.1024 1.0474 -0.2055 0.2180  0.1189  47  TRP C CG  
3538  C CD1 . TRP C 47  ? 1.3512 2.1410 1.1038 -0.1994 0.2095  0.1231  47  TRP C CD1 
3539  C CD2 . TRP C 47  ? 1.3308 2.1309 1.0529 -0.2027 0.2178  0.1297  47  TRP C CD2 
3540  N NE1 . TRP C 47  ? 1.3409 2.1549 1.1126 -0.1890 0.2004  0.1402  47  TRP C NE1 
3541  C CE2 . TRP C 47  ? 1.3694 2.1918 1.1190 -0.1940 0.2043  0.1451  47  TRP C CE2 
3542  C CE3 . TRP C 47  ? 1.3640 2.1630 1.0615 -0.2098 0.2298  0.1267  47  TRP C CE3 
3543  C CZ2 . TRP C 47  ? 1.3698 2.2104 1.1143 -0.1949 0.1981  0.1613  47  TRP C CZ2 
3544  C CZ3 . TRP C 47  ? 1.3866 2.2107 1.0826 -0.2143 0.2282  0.1382  47  TRP C CZ3 
3545  C CH2 . TRP C 47  ? 1.3873 2.2306 1.1024 -0.2082 0.2103  0.1573  47  TRP C CH2 
3546  N N   . MET C 48  ? 1.3486 2.0824 1.0833 -0.1798 0.2144  0.1409  48  MET C N   
3547  C CA  . MET C 48  ? 1.3456 2.0995 1.1033 -0.1702 0.2192  0.1469  48  MET C CA  
3548  C C   . MET C 48  ? 1.4147 2.1980 1.1759 -0.1780 0.2257  0.1524  48  MET C C   
3549  O O   . MET C 48  ? 1.4199 2.2135 1.1759 -0.1815 0.2396  0.1471  48  MET C O   
3550  C CB  . MET C 48  ? 1.3638 2.1243 1.1507 -0.1626 0.2079  0.1556  48  MET C CB  
3551  C CG  . MET C 48  ? 1.4277 2.1601 1.2088 -0.1532 0.1959  0.1549  48  MET C CG  
3552  S SD  . MET C 48  ? 1.4728 2.2298 1.2922 -0.1479 0.1777  0.1654  48  MET C SD  
3553  C CE  . MET C 48  ? 1.4312 2.1697 1.2271 -0.1710 0.1697  0.1693  48  MET C CE  
3554  N N   . GLY C 49  ? 1.3830 2.1742 1.1504 -0.1816 0.2159  0.1630  49  GLY C N   
3555  C CA  . GLY C 49  ? 1.3940 2.2011 1.1558 -0.1886 0.2146  0.1751  49  GLY C CA  
3556  C C   . GLY C 49  ? 1.4443 2.2456 1.2169 -0.1848 0.2010  0.1884  49  GLY C C   
3557  O O   . GLY C 49  ? 1.4335 2.2225 1.2210 -0.1795 0.1972  0.1835  49  GLY C O   
3558  N N   . ILE C 50  ? 1.4147 2.2190 1.1752 -0.1888 0.1938  0.2046  50  ILE C N   
3559  C CA  . ILE C 50  ? 1.4337 2.2217 1.2031 -0.1802 0.1796  0.2206  50  ILE C CA  
3560  C C   . ILE C 50  ? 1.5421 2.3111 1.2862 -0.1923 0.1789  0.2411  50  ILE C C   
3561  O O   . ILE C 50  ? 1.5531 2.3326 1.2706 -0.2099 0.1872  0.2421  50  ILE C O   
3562  C CB  . ILE C 50  ? 1.4815 2.2862 1.2615 -0.1679 0.1625  0.2222  50  ILE C CB  
3563  C CG1 . ILE C 50  ? 1.5119 2.3437 1.2636 -0.1797 0.1564  0.2262  50  ILE C CG1 
3564  C CG2 . ILE C 50  ? 1.4599 2.2754 1.2679 -0.1608 0.1674  0.1983  50  ILE C CG2 
3565  C CD1 . ILE C 50  ? 1.6870 2.5388 1.4450 -0.1691 0.1287  0.2413  50  ILE C CD1 
3566  N N   . ILE C 51  ? 1.5390 2.2744 1.2861 -0.1875 0.1730  0.2546  51  ILE C N   
3567  C CA  . ILE C 51  ? 1.5954 2.2976 1.3069 -0.2041 0.1735  0.2748  51  ILE C CA  
3568  C C   . ILE C 51  ? 1.7011 2.3560 1.4097 -0.1879 0.1560  0.2961  51  ILE C C   
3569  O O   . ILE C 51  ? 1.6770 2.3187 1.4196 -0.1710 0.1577  0.2871  51  ILE C O   
3570  C CB  . ILE C 51  ? 1.6284 2.3320 1.3387 -0.2263 0.1963  0.2634  51  ILE C CB  
3571  C CG1 . ILE C 51  ? 1.6984 2.3738 1.3605 -0.2559 0.2035  0.2784  51  ILE C CG1 
3572  C CG2 . ILE C 51  ? 1.6132 2.3053 1.3528 -0.2208 0.2017  0.2529  51  ILE C CG2 
3573  C CD1 . ILE C 51  ? 1.7878 2.4965 1.4526 -0.2839 0.2294  0.2588  51  ILE C CD1 
3574  N N   . ASN C 52  ? 1.7347 2.3609 1.4007 -0.1930 0.1386  0.3239  52  ASN C N   
3575  C CA  . ASN C 52  ? 1.8054 2.3745 1.4629 -0.1737 0.1176  0.3499  52  ASN C CA  
3576  C C   . ASN C 52  ? 1.9269 2.4346 1.5406 -0.2002 0.1348  0.3587  52  ASN C C   
3577  O O   . ASN C 52  ? 1.9601 2.4549 1.5168 -0.2337 0.1401  0.3697  52  ASN C O   
3578  C CB  . ASN C 52  ? 1.8686 2.4332 1.4929 -0.1679 0.0835  0.3801  52  ASN C CB  
3579  C CG  . ASN C 52  ? 2.1905 2.6837 1.7970 -0.1460 0.0561  0.4142  52  ASN C CG  
3580  O OD1 . ASN C 52  ? 2.1339 2.6164 1.7949 -0.1067 0.0458  0.4118  52  ASN C OD1 
3581  N ND2 . ASN C 52  ? 2.1348 2.5728 1.6625 -0.1719 0.0446  0.4457  52  ASN C ND2 
3582  N N   . PRO C 53  ? 1.9094 2.3797 1.5441 -0.1929 0.1480  0.3503  53  PRO C N   
3583  C CA  . PRO C 53  ? 1.9688 2.3842 1.5575 -0.2266 0.1690  0.3540  53  PRO C CA  
3584  C C   . PRO C 53  ? 2.1455 2.4820 1.6561 -0.2438 0.1569  0.3892  53  PRO C C   
3585  O O   . PRO C 53  ? 2.1844 2.4929 1.6432 -0.2870 0.1785  0.3882  53  PRO C O   
3586  C CB  . PRO C 53  ? 1.9839 2.3698 1.6084 -0.2133 0.1823  0.3386  53  PRO C CB  
3587  C CG  . PRO C 53  ? 1.9511 2.4019 1.6424 -0.1863 0.1786  0.3155  53  PRO C CG  
3588  C CD  . PRO C 53  ? 1.8905 2.3705 1.5877 -0.1628 0.1506  0.3308  53  PRO C CD  
3589  N N   . ARG C 54  ? 2.1567 2.4622 1.6556 -0.2141 0.1212  0.4198  54  ARG C N   
3590  C CA  . ARG C 54  ? 2.2773 2.4990 1.6907 -0.2295 0.1008  0.4604  54  ARG C CA  
3591  C C   . ARG C 54  ? 2.3463 2.5942 1.6945 -0.2795 0.1073  0.4637  54  ARG C C   
3592  O O   . ARG C 54  ? 2.3932 2.6011 1.6775 -0.3280 0.1320  0.4626  54  ARG C O   
3593  C CB  . ARG C 54  ? 2.3245 2.5187 1.7522 -0.1794 0.0530  0.4936  54  ARG C CB  
3594  C CG  . ARG C 54  ? 2.4682 2.6054 1.9438 -0.1332 0.0483  0.4953  54  ARG C CG  
3595  C CD  . ARG C 54  ? 2.7568 2.7616 2.1574 -0.1336 0.0342  0.5347  54  ARG C CD  
3596  N NE  . ARG C 54  ? 2.8898 2.8393 2.3463 -0.0836 0.0328  0.5321  54  ARG C NE  
3597  C CZ  . ARG C 54  ? 3.1325 2.9948 2.5660 -0.0963 0.0650  0.5232  54  ARG C CZ  
3598  N NH1 . ARG C 54  ? 2.9877 2.8149 2.3444 -0.1588 0.0989  0.5167  54  ARG C NH1 
3599  N NH2 . ARG C 54  ? 2.9973 2.8113 2.4874 -0.0493 0.0669  0.5162  54  ARG C NH2 
3600  N N   . ASP C 55  ? 2.2582 2.5763 1.6236 -0.2722 0.0903  0.4621  55  ASP C N   
3601  C CA  . ASP C 55  ? 2.2660 2.6150 1.5756 -0.3187 0.0991  0.4599  55  ASP C CA  
3602  C C   . ASP C 55  ? 2.2226 2.6319 1.5580 -0.3499 0.1455  0.4169  55  ASP C C   
3603  O O   . ASP C 55  ? 2.2469 2.6692 1.5334 -0.3969 0.1657  0.4081  55  ASP C O   
3604  C CB  . ASP C 55  ? 2.2587 2.6694 1.5878 -0.3006 0.0709  0.4646  55  ASP C CB  
3605  C CG  . ASP C 55  ? 2.4971 2.8698 1.8072 -0.2698 0.0173  0.5077  55  ASP C CG  
3606  O OD1 . ASP C 55  ? 2.6338 2.9357 1.8527 -0.2961 -0.0039 0.5450  55  ASP C OD1 
3607  O OD2 . ASP C 55  ? 2.5093 2.9277 1.8941 -0.2219 -0.0050 0.5035  55  ASP C OD2 
3608  N N   . SER C 56  ? 2.0706 2.5205 1.4857 -0.3234 0.1611  0.3888  56  SER C N   
3609  C CA  . SER C 56  ? 1.9814 2.4969 1.4418 -0.3378 0.1955  0.3495  56  SER C CA  
3610  C C   . SER C 56  ? 1.9676 2.5536 1.4479 -0.3389 0.2004  0.3312  56  SER C C   
3611  O O   . SER C 56  ? 1.9198 2.5577 1.4316 -0.3515 0.2277  0.3004  56  SER C O   
3612  C CB  . SER C 56  ? 2.0659 2.5623 1.4878 -0.3861 0.2264  0.3390  56  SER C CB  
3613  O OG  . SER C 56  ? 2.2301 2.6552 1.6300 -0.3874 0.2255  0.3530  56  SER C OG  
3614  N N   . ASP C 57  ? 1.9212 2.5093 1.3861 -0.3241 0.1728  0.3493  57  ASP C N   
3615  C CA  . ASP C 57  ? 1.8754 2.5193 1.3470 -0.3291 0.1769  0.3336  57  ASP C CA  
3616  C C   . ASP C 57  ? 1.8149 2.5097 1.3615 -0.2958 0.1832  0.3066  57  ASP C C   
3617  O O   . ASP C 57  ? 1.7847 2.4747 1.3709 -0.2619 0.1665  0.3106  57  ASP C O   
3618  C CB  . ASP C 57  ? 1.9544 2.5858 1.3771 -0.3321 0.1432  0.3628  57  ASP C CB  
3619  C CG  . ASP C 57  ? 2.0206 2.6572 1.4839 -0.2855 0.1053  0.3792  57  ASP C CG  
3620  O OD1 . ASP C 57  ? 1.9911 2.6709 1.4608 -0.2802 0.0896  0.3773  57  ASP C OD1 
3621  O OD2 . ASP C 57  ? 2.1054 2.7049 1.5948 -0.2571 0.0939  0.3909  57  ASP C OD2 
3622  N N   . THR C 58  ? 1.7152 2.4530 1.2789 -0.3075 0.2096  0.2775  58  THR C N   
3623  C CA  . THR C 58  ? 1.6321 2.4063 1.2527 -0.2814 0.2168  0.2529  58  THR C CA  
3624  C C   . THR C 58  ? 1.6508 2.4491 1.2609 -0.2806 0.2126  0.2459  58  THR C C   
3625  O O   . THR C 58  ? 1.6845 2.4795 1.2462 -0.3024 0.2038  0.2592  58  THR C O   
3626  C CB  . THR C 58  ? 1.7127 2.5117 1.3669 -0.2877 0.2460  0.2260  58  THR C CB  
3627  O OG1 . THR C 58  ? 1.7307 2.5144 1.3711 -0.3101 0.2558  0.2309  58  THR C OG1 
3628  C CG2 . THR C 58  ? 1.6318 2.4453 1.3408 -0.2570 0.2430  0.2124  58  THR C CG2 
3629  N N   . ARG C 59  ? 1.6135 1.9194 1.4648 -0.0935 0.3023  0.1973  59  ARG C N   
3630  C CA  . ARG C 59  ? 1.6396 1.9165 1.4669 -0.0928 0.2926  0.1886  59  ARG C CA  
3631  C C   . ARG C 59  ? 1.7124 1.9702 1.5518 -0.0719 0.2924  0.1716  59  ARG C C   
3632  O O   . ARG C 59  ? 1.6872 1.9267 1.5461 -0.0661 0.2851  0.1817  59  ARG C O   
3633  C CB  . ARG C 59  ? 1.6260 1.8822 1.4591 -0.1082 0.2802  0.2158  59  ARG C CB  
3634  C CG  . ARG C 59  ? 1.7653 1.9935 1.5725 -0.1138 0.2651  0.2162  59  ARG C CG  
3635  C CD  . ARG C 59  ? 1.8014 2.0054 1.6226 -0.1281 0.2536  0.2528  59  ARG C CD  
3636  N NE  . ARG C 59  ? 1.8066 1.9738 1.6118 -0.1277 0.2341  0.2584  59  ARG C NE  
3637  C CZ  . ARG C 59  ? 1.8213 1.9549 1.6440 -0.1279 0.2215  0.2901  59  ARG C CZ  
3638  N NH1 . ARG C 59  ? 1.5328 1.6635 1.3864 -0.1285 0.2300  0.3157  59  ARG C NH1 
3639  N NH2 . ARG C 59  ? 1.5840 1.6850 1.3953 -0.1262 0.2002  0.2974  59  ARG C NH2 
3640  N N   . TYR C 60  ? 1.7102 1.9778 1.5442 -0.0608 0.3026  0.1491  60  TYR C N   
3641  C CA  . TYR C 60  ? 1.7133 1.9741 1.5708 -0.0443 0.3049  0.1361  60  TYR C CA  
3642  C C   . TYR C 60  ? 1.7868 2.0249 1.6475 -0.0376 0.2916  0.1272  60  TYR C C   
3643  O O   . TYR C 60  ? 1.8131 2.0378 1.6463 -0.0447 0.2838  0.1215  60  TYR C O   
3644  C CB  . TYR C 60  ? 1.7529 2.0311 1.6121 -0.0369 0.3231  0.1203  60  TYR C CB  
3645  C CG  . TYR C 60  ? 1.7950 2.0965 1.6584 -0.0392 0.3342  0.1322  60  TYR C CG  
3646  C CD1 . TYR C 60  ? 1.8529 2.1736 1.6941 -0.0457 0.3401  0.1366  60  TYR C CD1 
3647  C CD2 . TYR C 60  ? 1.7839 2.0919 1.6768 -0.0344 0.3380  0.1404  60  TYR C CD2 
3648  C CE1 . TYR C 60  ? 1.8732 2.2192 1.7278 -0.0445 0.3476  0.1517  60  TYR C CE1 
3649  C CE2 . TYR C 60  ? 1.7936 2.1201 1.6940 -0.0357 0.3445  0.1540  60  TYR C CE2 
3650  C CZ  . TYR C 60  ? 1.9363 2.2819 1.8206 -0.0391 0.3488  0.1605  60  TYR C CZ  
3651  O OH  . TYR C 60  ? 1.9523 2.3199 1.8529 -0.0374 0.3522  0.1786  60  TYR C OH  
3652  N N   . SER C 61  ? 1.7241 1.9619 1.6225 -0.0242 0.2876  0.1273  61  SER C N   
3653  C CA  . SER C 61  ? 1.7209 1.9462 1.6419 -0.0133 0.2733  0.1220  61  SER C CA  
3654  C C   . SER C 61  ? 1.8010 2.0341 1.7289 -0.0080 0.2854  0.0942  61  SER C C   
3655  O O   . SER C 61  ? 1.7905 2.0426 1.7251 -0.0077 0.3056  0.0876  61  SER C O   
3656  C CB  . SER C 61  ? 1.7182 1.9545 1.6869 -0.0005 0.2666  0.1365  61  SER C CB  
3657  O OG  . SER C 61  ? 1.8093 2.0466 1.8185 0.0134  0.2527  0.1345  61  SER C OG  
3658  N N   . PRO C 62  ? 1.7902 2.0070 1.7202 -0.0036 0.2739  0.0793  62  PRO C N   
3659  C CA  . PRO C 62  ? 1.8132 2.0353 1.7547 0.0019  0.2889  0.0497  62  PRO C CA  
3660  C C   . PRO C 62  ? 1.8259 2.0770 1.8300 0.0115  0.3049  0.0499  62  PRO C C   
3661  O O   . PRO C 62  ? 1.8355 2.0959 1.8425 0.0113  0.3292  0.0348  62  PRO C O   
3662  C CB  . PRO C 62  ? 1.8534 2.0524 1.8036 0.0070  0.2662  0.0388  62  PRO C CB  
3663  C CG  . PRO C 62  ? 1.9170 2.0926 1.8304 -0.0027 0.2435  0.0611  62  PRO C CG  
3664  C CD  . PRO C 62  ? 1.8181 2.0081 1.7433 -0.0034 0.2466  0.0902  62  PRO C CD  
3665  N N   . SER C 63  ? 1.7348 2.0026 1.7902 0.0187  0.2924  0.0709  63  SER C N   
3666  C CA  . SER C 63  ? 1.6899 1.9935 1.8123 0.0238  0.3035  0.0788  63  SER C CA  
3667  C C   . SER C 63  ? 1.7450 2.0630 1.8537 0.0144  0.3240  0.0891  63  SER C C   
3668  O O   . SER C 63  ? 1.7124 2.0579 1.8710 0.0134  0.3382  0.0953  63  SER C O   
3669  C CB  . SER C 63  ? 1.6783 2.0008 1.8527 0.0338  0.2818  0.1016  63  SER C CB  
3670  O OG  . SER C 63  ? 1.7594 2.0718 1.9606 0.0453  0.2598  0.0983  63  SER C OG  
3671  N N   . PHE C 64  ? 1.7338 2.0358 1.7833 0.0062  0.3240  0.0947  64  PHE C N   
3672  C CA  . PHE C 64  ? 1.7326 2.0456 1.7703 -0.0017 0.3374  0.1072  64  PHE C CA  
3673  C C   . PHE C 64  ? 1.8309 2.1349 1.8203 -0.0071 0.3516  0.1006  64  PHE C C   
3674  O O   . PHE C 64  ? 1.8176 2.1317 1.8046 -0.0113 0.3618  0.1134  64  PHE C O   
3675  C CB  . PHE C 64  ? 1.7351 2.0482 1.7657 -0.0049 0.3233  0.1260  64  PHE C CB  
3676  C CG  . PHE C 64  ? 1.7147 2.0463 1.7932 0.0015  0.3123  0.1376  64  PHE C CG  
3677  C CD1 . PHE C 64  ? 1.7455 2.0693 1.8345 0.0113  0.2935  0.1417  64  PHE C CD1 
3678  C CD2 . PHE C 64  ? 1.7114 2.0714 1.8266 -0.0026 0.3193  0.1490  64  PHE C CD2 
3679  C CE1 . PHE C 64  ? 1.7165 2.0655 1.8545 0.0204  0.2830  0.1563  64  PHE C CE1 
3680  C CE2 . PHE C 64  ? 1.7097 2.0968 1.8709 0.0025  0.3089  0.1619  64  PHE C CE2 
3681  C CZ  . PHE C 64  ? 1.6749 2.0587 1.8483 0.0156  0.2913  0.1652  64  PHE C CZ  
3682  N N   . GLN C 65  ? 1.8376 2.1253 1.7905 -0.0069 0.3504  0.0830  65  GLN C N   
3683  C CA  . GLN C 65  ? 1.8794 2.1665 1.7864 -0.0110 0.3631  0.0769  65  GLN C CA  
3684  C C   . GLN C 65  ? 1.9447 2.2422 1.8665 -0.0050 0.3898  0.0721  65  GLN C C   
3685  O O   . GLN C 65  ? 1.9418 2.2366 1.8936 0.0010  0.4001  0.0573  65  GLN C O   
3686  C CB  . GLN C 65  ? 1.9410 2.2102 1.8057 -0.0146 0.3539  0.0586  65  GLN C CB  
3687  C CG  . GLN C 65  ? 2.2635 2.5392 2.0798 -0.0184 0.3682  0.0490  65  GLN C CG  
3688  C CD  . GLN C 65  ? 2.5829 2.8760 2.3767 -0.0290 0.3628  0.0714  65  GLN C CD  
3689  O OE1 . GLN C 65  ? 2.5479 2.8354 2.3249 -0.0410 0.3450  0.0802  65  GLN C OE1 
3690  N NE2 . GLN C 65  ? 2.4880 2.8043 2.2870 -0.0252 0.3781  0.0843  65  GLN C NE2 
3691  N N   . GLY C 66  ? 1.9097 2.2199 1.8185 -0.0063 0.4007  0.0884  66  GLY C N   
3692  C CA  . GLY C 66  ? 1.9214 2.2398 1.8435 0.0003  0.4268  0.0940  66  GLY C CA  
3693  C C   . GLY C 66  ? 1.9361 2.2638 1.9104 -0.0013 0.4317  0.1178  66  GLY C C   
3694  O O   . GLY C 66  ? 1.9309 2.2671 1.9113 -0.0004 0.4418  0.1414  66  GLY C O   
3695  N N   . GLN C 67  ? 1.8595 2.1888 1.8747 -0.0042 0.4227  0.1154  67  GLN C N   
3696  C CA  . GLN C 67  ? 1.8179 2.1626 1.8873 -0.0101 0.4246  0.1382  67  GLN C CA  
3697  C C   . GLN C 67  ? 1.8676 2.2166 1.9255 -0.0175 0.4108  0.1623  67  GLN C C   
3698  O O   . GLN C 67  ? 1.8658 2.2197 1.9358 -0.0207 0.4203  0.1861  67  GLN C O   
3699  C CB  . GLN C 67  ? 1.7991 2.1543 1.9140 -0.0107 0.4128  0.1309  67  GLN C CB  
3700  C CG  . GLN C 67  ? 1.9460 2.2956 2.0779 -0.0026 0.4195  0.1045  67  GLN C CG  
3701  C CD  . GLN C 67  ? 2.1935 2.5483 2.3631 -0.0015 0.4503  0.1043  67  GLN C CD  
3702  O OE1 . GLN C 67  ? 2.1296 2.5079 2.3691 -0.0073 0.4600  0.1218  67  GLN C OE1 
3703  N NE2 . GLN C 67  ? 2.1179 2.4535 2.2445 0.0049  0.4681  0.0874  67  GLN C NE2 
3704  N N   . VAL C 68  ? 1.8146 2.1590 1.8508 -0.0199 0.3887  0.1574  68  VAL C N   
3705  C CA  . VAL C 68  ? 1.7988 2.1438 1.8236 -0.0267 0.3745  0.1734  68  VAL C CA  
3706  C C   . VAL C 68  ? 1.8750 2.2137 1.8588 -0.0255 0.3696  0.1710  68  VAL C C   
3707  O O   . VAL C 68  ? 1.8982 2.2310 1.8570 -0.0222 0.3703  0.1550  68  VAL C O   
3708  C CB  . VAL C 68  ? 1.8193 2.1665 1.8574 -0.0303 0.3574  0.1730  68  VAL C CB  
3709  C CG1 . VAL C 68  ? 1.8226 2.1565 1.8378 -0.0252 0.3453  0.1579  68  VAL C CG1 
3710  C CG2 . VAL C 68  ? 1.8085 2.1565 1.8429 -0.0389 0.3471  0.1883  68  VAL C CG2 
3711  N N   . THR C 69  ? 1.8144 2.1580 1.7971 -0.0296 0.3634  0.1889  69  THR C N   
3712  C CA  . THR C 69  ? 1.8145 2.1642 1.7768 -0.0300 0.3580  0.1935  69  THR C CA  
3713  C C   . THR C 69  ? 1.8319 2.1774 1.7973 -0.0380 0.3407  0.1979  69  THR C C   
3714  O O   . THR C 69  ? 1.8143 2.1573 1.7960 -0.0421 0.3342  0.2075  69  THR C O   
3715  C CB  . THR C 69  ? 1.9292 2.2941 1.8987 -0.0240 0.3678  0.2135  69  THR C CB  
3716  O OG1 . THR C 69  ? 1.9384 2.3014 1.9096 -0.0163 0.3882  0.2097  69  THR C OG1 
3717  C CG2 . THR C 69  ? 1.9199 2.3048 1.8761 -0.0222 0.3647  0.2194  69  THR C CG2 
3718  N N   . ILE C 70  ? 1.7790 2.1219 1.7292 -0.0418 0.3343  0.1915  70  ILE C N   
3719  C CA  . ILE C 70  ? 1.7599 2.0964 1.7165 -0.0494 0.3225  0.1958  70  ILE C CA  
3720  C C   . ILE C 70  ? 1.8112 2.1692 1.7826 -0.0537 0.3193  0.2113  70  ILE C C   
3721  O O   . ILE C 70  ? 1.8097 2.1860 1.7758 -0.0556 0.3223  0.2155  70  ILE C O   
3722  C CB  . ILE C 70  ? 1.7961 2.1156 1.7395 -0.0525 0.3179  0.1878  70  ILE C CB  
3723  C CG1 . ILE C 70  ? 1.8031 2.1097 1.7412 -0.0447 0.3189  0.1754  70  ILE C CG1 
3724  C CG2 . ILE C 70  ? 1.7891 2.0969 1.7430 -0.0584 0.3106  0.1932  70  ILE C CG2 
3725  C CD1 . ILE C 70  ? 1.8940 2.1850 1.8184 -0.0448 0.3132  0.1717  70  ILE C CD1 
3726  N N   . SER C 71  ? 1.7670 2.1263 1.7606 -0.0559 0.3116  0.2210  71  SER C N   
3727  C CA  . SER C 71  ? 1.7551 2.1387 1.7788 -0.0584 0.3048  0.2387  71  SER C CA  
3728  C C   . SER C 71  ? 1.7959 2.1717 1.8374 -0.0686 0.2971  0.2370  71  SER C C   
3729  O O   . SER C 71  ? 1.8026 2.1499 1.8294 -0.0710 0.2967  0.2233  71  SER C O   
3730  C CB  . SER C 71  ? 1.7981 2.1861 1.8410 -0.0531 0.2991  0.2538  71  SER C CB  
3731  O OG  . SER C 71  ? 1.9147 2.2984 1.9434 -0.0454 0.3094  0.2559  71  SER C OG  
3732  N N   . ALA C 72  ? 1.7251 2.1298 1.8040 -0.0739 0.2926  0.2526  72  ALA C N   
3733  C CA  . ALA C 72  ? 1.7048 2.1047 1.8133 -0.0847 0.2886  0.2533  72  ALA C CA  
3734  C C   . ALA C 72  ? 1.7118 2.1476 1.8805 -0.0870 0.2787  0.2729  72  ALA C C   
3735  O O   . ALA C 72  ? 1.6803 2.1604 1.8746 -0.0843 0.2777  0.2928  72  ALA C O   
3736  C CB  . ALA C 72  ? 1.7110 2.1092 1.8134 -0.0948 0.2968  0.2545  72  ALA C CB  
3737  N N   . ASP C 73  ? 1.6628 2.0820 1.8569 -0.0910 0.2707  0.2672  73  ASP C N   
3738  C CA  . ASP C 73  ? 1.6335 2.0839 1.8960 -0.0932 0.2583  0.2840  73  ASP C CA  
3739  C C   . ASP C 73  ? 1.6662 2.1075 1.9654 -0.1065 0.2622  0.2778  73  ASP C C   
3740  O O   . ASP C 73  ? 1.6793 2.0824 1.9692 -0.1082 0.2596  0.2583  73  ASP C O   
3741  C CB  . ASP C 73  ? 1.6684 2.1071 1.9353 -0.0847 0.2415  0.2858  73  ASP C CB  
3742  C CG  . ASP C 73  ? 1.7813 2.2656 2.1233 -0.0802 0.2247  0.3140  73  ASP C CG  
3743  O OD1 . ASP C 73  ? 1.7616 2.2693 2.1659 -0.0885 0.2213  0.3196  73  ASP C OD1 
3744  O OD2 . ASP C 73  ? 1.8735 2.3706 2.2190 -0.0679 0.2146  0.3337  73  ASP C OD2 
3745  N N   . LYS C 74  ? 1.5869 2.0647 1.9286 -0.1174 0.2702  0.2959  74  LYS C N   
3746  C CA  . LYS C 74  ? 1.5626 2.0404 1.9546 -0.1332 0.2788  0.2995  74  LYS C CA  
3747  C C   . LYS C 74  ? 1.5990 2.0868 2.0622 -0.1350 0.2675  0.2997  74  LYS C C   
3748  O O   . LYS C 74  ? 1.6017 2.0627 2.0864 -0.1442 0.2764  0.2883  74  LYS C O   
3749  C CB  . LYS C 74  ? 1.5505 2.0778 1.9833 -0.1482 0.2877  0.3284  74  LYS C CB  
3750  C CG  . LYS C 74  ? 1.6451 2.2434 2.1168 -0.1442 0.2774  0.3550  74  LYS C CG  
3751  C CD  . LYS C 74  ? 1.7173 2.3749 2.2437 -0.1642 0.2847  0.3866  74  LYS C CD  
3752  C CE  . LYS C 74  ? 1.8258 2.5454 2.3523 -0.1577 0.2788  0.4071  74  LYS C CE  
3753  N NZ  . LYS C 74  ? 1.8654 2.6502 2.4432 -0.1807 0.2847  0.4399  74  LYS C NZ  
3754  N N   . SER C 75  ? 1.5377 2.0618 2.0389 -0.1249 0.2480  0.3139  75  SER C N   
3755  C CA  . SER C 75  ? 1.5204 2.0584 2.0966 -0.1240 0.2304  0.3176  75  SER C CA  
3756  C C   . SER C 75  ? 1.6167 2.0873 2.1478 -0.1219 0.2250  0.2829  75  SER C C   
3757  O O   . SER C 75  ? 1.6089 2.0667 2.1863 -0.1295 0.2238  0.2708  75  SER C O   
3758  C CB  . SER C 75  ? 1.5375 2.1276 2.1573 -0.1099 0.2085  0.3470  75  SER C CB  
3759  O OG  . SER C 75  ? 1.6058 2.2630 2.2595 -0.1105 0.2139  0.3784  75  SER C OG  
3760  N N   . ILE C 76  ? 1.6166 2.0474 2.0605 -0.1131 0.2226  0.2674  76  ILE C N   
3761  C CA  . ILE C 76  ? 1.6627 2.0352 2.0523 -0.1130 0.2171  0.2366  76  ILE C CA  
3762  C C   . ILE C 76  ? 1.7349 2.0651 2.0667 -0.1184 0.2406  0.2111  76  ILE C C   
3763  O O   . ILE C 76  ? 1.7796 2.0653 2.0682 -0.1196 0.2406  0.1839  76  ILE C O   
3764  C CB  . ILE C 76  ? 1.7238 2.0830 2.0610 -0.1039 0.2028  0.2405  76  ILE C CB  
3765  C CG1 . ILE C 76  ? 1.6996 2.1070 2.0814 -0.0933 0.1882  0.2778  76  ILE C CG1 
3766  C CG2 . ILE C 76  ? 1.7724 2.0880 2.0840 -0.1082 0.1867  0.2191  76  ILE C CG2 
3767  C CD1 . ILE C 76  ? 1.8443 2.2410 2.1733 -0.0844 0.1846  0.2888  76  ILE C CD1 
3768  N N   . SER C 77  ? 1.6485 1.9945 1.9813 -0.1216 0.2593  0.2229  77  SER C N   
3769  C CA  . SER C 77  ? 1.6490 1.9603 1.9347 -0.1240 0.2803  0.2104  77  SER C CA  
3770  C C   . SER C 77  ? 1.6990 1.9778 1.9018 -0.1143 0.2790  0.1928  77  SER C C   
3771  O O   . SER C 77  ? 1.7220 1.9627 1.8853 -0.1128 0.2864  0.1721  77  SER C O   
3772  C CB  . SER C 77  ? 1.6951 1.9792 2.0089 -0.1323 0.2933  0.1973  77  SER C CB  
3773  O OG  . SER C 77  ? 1.8178 2.0641 2.1028 -0.1292 0.2863  0.1677  77  SER C OG  
3774  N N   . THR C 78  ? 1.6255 1.9247 1.8087 -0.1074 0.2702  0.2034  78  THR C N   
3775  C CA  . THR C 78  ? 1.6338 1.9144 1.7567 -0.1002 0.2683  0.1931  78  THR C CA  
3776  C C   . THR C 78  ? 1.6423 1.9411 1.7455 -0.0942 0.2745  0.2052  78  THR C C   
3777  O O   . THR C 78  ? 1.6151 1.9471 1.7452 -0.0930 0.2719  0.2234  78  THR C O   
3778  C CB  . THR C 78  ? 1.7575 2.0374 1.8793 -0.0994 0.2499  0.1935  78  THR C CB  
3779  O OG1 . THR C 78  ? 1.7627 2.0439 1.9303 -0.1047 0.2376  0.1929  78  THR C OG1 
3780  C CG2 . THR C 78  ? 1.7716 2.0242 1.8405 -0.0997 0.2484  0.1769  78  THR C CG2 
3781  N N   . ALA C 79  ? 1.5932 1.8728 1.6519 -0.0894 0.2818  0.1948  79  ALA C N   
3782  C CA  . ALA C 79  ? 1.5768 1.8672 1.6142 -0.0832 0.2872  0.2004  79  ALA C CA  
3783  C C   . ALA C 79  ? 1.6278 1.9178 1.6455 -0.0784 0.2824  0.1975  79  ALA C C   
3784  O O   . ALA C 79  ? 1.6368 1.9127 1.6452 -0.0813 0.2762  0.1891  79  ALA C O   
3785  C CB  . ALA C 79  ? 1.5890 1.8603 1.6039 -0.0807 0.2964  0.1951  79  ALA C CB  
3786  N N   . TYR C 80  ? 1.5799 1.8859 1.5928 -0.0730 0.2863  0.2053  80  TYR C N   
3787  C CA  . TYR C 80  ? 1.5866 1.8949 1.5915 -0.0704 0.2857  0.2084  80  TYR C CA  
3788  C C   . TYR C 80  ? 1.6481 1.9596 1.6385 -0.0638 0.2963  0.2039  80  TYR C C   
3789  O O   . TYR C 80  ? 1.6458 1.9598 1.6294 -0.0605 0.3021  0.2007  80  TYR C O   
3790  C CB  . TYR C 80  ? 1.5969 1.9213 1.6238 -0.0694 0.2803  0.2285  80  TYR C CB  
3791  C CG  . TYR C 80  ? 1.6185 1.9436 1.6713 -0.0743 0.2660  0.2354  80  TYR C CG  
3792  C CD1 . TYR C 80  ? 1.6633 1.9686 1.7121 -0.0824 0.2545  0.2283  80  TYR C CD1 
3793  C CD2 . TYR C 80  ? 1.6090 1.9583 1.6946 -0.0716 0.2629  0.2494  80  TYR C CD2 
3794  C CE1 . TYR C 80  ? 1.6809 1.9836 1.7565 -0.0869 0.2398  0.2312  80  TYR C CE1 
3795  C CE2 . TYR C 80  ? 1.6142 1.9685 1.7373 -0.0754 0.2481  0.2567  80  TYR C CE2 
3796  C CZ  . TYR C 80  ? 1.7256 2.0530 1.8430 -0.0828 0.2363  0.2458  80  TYR C CZ  
3797  O OH  . TYR C 80  ? 1.7268 2.0555 1.8833 -0.0867 0.2202  0.2496  80  TYR C OH  
3798  N N   . LEU C 81  ? 1.6082 1.9217 1.5991 -0.0639 0.2981  0.2052  81  LEU C N   
3799  C CA  . LEU C 81  ? 1.6022 1.9226 1.5933 -0.0579 0.3081  0.2016  81  LEU C CA  
3800  C C   . LEU C 81  ? 1.6695 2.0010 1.6783 -0.0600 0.3139  0.2172  81  LEU C C   
3801  O O   . LEU C 81  ? 1.6609 1.9988 1.6843 -0.0661 0.3138  0.2232  81  LEU C O   
3802  C CB  . LEU C 81  ? 1.5941 1.9120 1.5839 -0.0564 0.3057  0.1920  81  LEU C CB  
3803  C CG  . LEU C 81  ? 1.6414 1.9672 1.6404 -0.0479 0.3123  0.1865  81  LEU C CG  
3804  C CD1 . LEU C 81  ? 1.6482 1.9607 1.6300 -0.0415 0.3120  0.1785  81  LEU C CD1 
3805  C CD2 . LEU C 81  ? 1.6596 1.9974 1.6756 -0.0463 0.3079  0.1866  81  LEU C CD2 
3806  N N   . GLN C 82  ? 1.6433 1.9803 1.6551 -0.0557 0.3191  0.2286  82  GLN C N   
3807  C CA  . GLN C 82  ? 1.6461 1.9900 1.6761 -0.0550 0.3271  0.2505  82  GLN C CA  
3808  C C   . GLN C 82  ? 1.6856 2.0348 1.7255 -0.0509 0.3455  0.2468  82  GLN C C   
3809  O O   . GLN C 82  ? 1.6859 2.0350 1.7120 -0.0430 0.3538  0.2283  82  GLN C O   
3810  C CB  . GLN C 82  ? 1.6741 2.0266 1.7058 -0.0470 0.3273  0.2654  82  GLN C CB  
3811  C CG  . GLN C 82  ? 1.9358 2.2918 1.9908 -0.0451 0.3297  0.2987  82  GLN C CG  
3812  C CD  . GLN C 82  ? 2.1147 2.4804 2.1846 -0.0404 0.3152  0.3205  82  GLN C CD  
3813  O OE1 . GLN C 82  ? 2.0061 2.3872 2.0736 -0.0346 0.3116  0.3138  82  GLN C OE1 
3814  N NE2 . GLN C 82  ? 2.0140 2.3743 2.1072 -0.0436 0.3055  0.3517  82  GLN C NE2 
3815  N N   . TRP C 83  ? 1.6142 2.4239 1.5795 -0.0804 0.1032  0.2792  83  TRP C N   
3816  C CA  . TRP C 83  ? 1.6310 2.4404 1.5738 -0.0440 0.1058  0.2552  83  TRP C CA  
3817  C C   . TRP C 83  ? 1.6979 2.5886 1.6631 -0.0293 0.1241  0.2494  83  TRP C C   
3818  O O   . TRP C 83  ? 1.6768 2.6205 1.6917 -0.0362 0.1269  0.2559  83  TRP C O   
3819  C CB  . TRP C 83  ? 1.6082 2.3781 1.5512 -0.0266 0.0858  0.2390  83  TRP C CB  
3820  C CG  . TRP C 83  ? 1.6231 2.3172 1.5260 -0.0272 0.0713  0.2369  83  TRP C CG  
3821  C CD1 . TRP C 83  ? 1.6851 2.3406 1.5444 -0.0100 0.0634  0.2270  83  TRP C CD1 
3822  C CD2 . TRP C 83  ? 1.6045 2.2557 1.5087 -0.0450 0.0611  0.2465  83  TRP C CD2 
3823  N NE1 . TRP C 83  ? 1.6742 2.2688 1.5126 -0.0207 0.0503  0.2331  83  TRP C NE1 
3824  C CE2 . TRP C 83  ? 1.6672 2.2622 1.5320 -0.0415 0.0519  0.2436  83  TRP C CE2 
3825  C CE3 . TRP C 83  ? 1.5980 2.2536 1.5322 -0.0616 0.0562  0.2576  83  TRP C CE3 
3826  C CZ2 . TRP C 83  ? 1.6523 2.2060 1.5098 -0.0557 0.0448  0.2512  83  TRP C CZ2 
3827  C CZ3 . TRP C 83  ? 1.6109 2.2203 1.5318 -0.0706 0.0467  0.2617  83  TRP C CZ3 
3828  C CH2 . TRP C 83  ? 1.6331 2.1971 1.5174 -0.0683 0.0443  0.2581  83  TRP C CH2 
3829  N N   . SER C 84  ? 1.6859 2.5864 1.6145 -0.0068 0.1349  0.2372  84  SER C N   
3830  C CA  . SER C 84  ? 1.7016 2.6844 1.6413 0.0146  0.1558  0.2271  84  SER C CA  
3831  C C   . SER C 84  ? 1.7436 2.7519 1.7122 0.0461  0.1441  0.2000  84  SER C C   
3832  O O   . SER C 84  ? 1.7312 2.8110 1.7548 0.0420  0.1547  0.2029  84  SER C O   
3833  C CB  . SER C 84  ? 1.7812 2.7476 1.6618 0.0398  0.1619  0.2161  84  SER C CB  
3834  O OG  . SER C 84  ? 1.8648 2.7694 1.7098 0.0150  0.1598  0.2347  84  SER C OG  
3835  N N   . SER C 85  ? 1.6989 2.6422 1.6317 0.0739  0.1171  0.1753  85  SER C N   
3836  C CA  . SER C 85  ? 1.6951 2.6355 1.6420 0.1028  0.0942  0.1450  85  SER C CA  
3837  C C   . SER C 85  ? 1.7338 2.5732 1.6416 0.1020  0.0608  0.1398  85  SER C C   
3838  O O   . SER C 85  ? 1.7491 2.5353 1.6071 0.1048  0.0513  0.1435  85  SER C O   
3839  C CB  . SER C 85  ? 1.7714 2.7578 1.7023 0.1489  0.0930  0.1121  85  SER C CB  
3840  O OG  . SER C 85  ? 1.8697 2.8565 1.8202 0.1756  0.0668  0.0791  85  SER C OG  
3841  N N   . LEU C 86  ? 1.6588 2.4702 1.5894 0.0958  0.0427  0.1345  86  LEU C N   
3842  C CA  . LEU C 86  ? 1.6553 2.3767 1.5499 0.0899  0.0136  0.1328  86  LEU C CA  
3843  C C   . LEU C 86  ? 1.7225 2.4002 1.5745 0.1218  -0.0234 0.1016  86  LEU C C   
3844  O O   . LEU C 86  ? 1.7306 2.4420 1.5957 0.1515  -0.0353 0.0715  86  LEU C O   
3845  C CB  . LEU C 86  ? 1.6356 2.3355 1.5616 0.0709  0.0073  0.1407  86  LEU C CB  
3846  C CG  . LEU C 86  ? 1.6646 2.3669 1.6109 0.0366  0.0258  0.1741  86  LEU C CG  
3847  C CD1 . LEU C 86  ? 1.6555 2.3545 1.6413 0.0287  0.0174  0.1787  86  LEU C CD1 
3848  C CD2 . LEU C 86  ? 1.6974 2.3360 1.6009 0.0205  0.0207  0.1875  86  LEU C CD2 
3849  N N   . LYS C 87  ? 1.6848 2.2884 1.4873 0.1148  -0.0452 0.1091  87  LYS C N   
3850  C CA  . LYS C 87  ? 1.7207 2.2663 1.4744 0.1377  -0.0914 0.0866  87  LYS C CA  
3851  C C   . LYS C 87  ? 1.7658 2.2427 1.5047 0.1158  -0.1147 0.0917  87  LYS C C   
3852  O O   . LYS C 87  ? 1.7339 2.2031 1.4884 0.0855  -0.0921 0.1171  87  LYS C O   
3853  C CB  . LYS C 87  ? 1.7733 2.2833 1.4792 0.1433  -0.1027 0.0987  87  LYS C CB  
3854  C CG  . LYS C 87  ? 1.9461 2.5091 1.6509 0.1659  -0.0810 0.0961  87  LYS C CG  
3855  C CD  . LYS C 87  ? 2.0105 2.5843 1.7261 0.1358  -0.0423 0.1300  87  LYS C CD  
3856  C CE  . LYS C 87  ? 2.1113 2.6172 1.7826 0.1313  -0.0600 0.1476  87  LYS C CE  
3857  N NZ  . LYS C 87  ? 2.1630 2.6109 1.8305 0.1000  -0.0731 0.1667  87  LYS C NZ  
3858  N N   . ALA C 88  ? 1.7550 2.1790 1.4584 0.1312  -0.1630 0.0673  88  ALA C N   
3859  C CA  . ALA C 88  ? 1.7676 2.1189 1.4447 0.1088  -0.1891 0.0723  88  ALA C CA  
3860  C C   . ALA C 88  ? 1.8111 2.1212 1.4564 0.0801  -0.1850 0.1077  88  ALA C C   
3861  O O   . ALA C 88  ? 1.8043 2.0748 1.4375 0.0534  -0.1853 0.1234  88  ALA C O   
3862  C CB  . ALA C 88  ? 1.8303 2.1303 1.4699 0.1299  -0.2492 0.0380  88  ALA C CB  
3863  N N   . SER C 89  ? 1.7698 2.0916 1.4035 0.0870  -0.1797 0.1200  89  SER C N   
3864  C CA  . SER C 89  ? 1.7674 2.0576 1.3810 0.0629  -0.1752 0.1532  89  SER C CA  
3865  C C   . SER C 89  ? 1.7698 2.0940 1.4217 0.0355  -0.1243 0.1782  89  SER C C   
3866  O O   . SER C 89  ? 1.7691 2.0685 1.4125 0.0105  -0.1181 0.2035  89  SER C O   
3867  C CB  . SER C 89  ? 1.8323 2.1168 1.4227 0.0847  -0.1912 0.1548  89  SER C CB  
3868  O OG  . SER C 89  ? 1.9213 2.2672 1.5409 0.0994  -0.1541 0.1504  89  SER C OG  
3869  N N   . ASP C 90  ? 1.6793 2.0615 1.3746 0.0399  -0.0920 0.1711  90  ASP C N   
3870  C CA  . ASP C 90  ? 1.6276 2.0417 1.3591 0.0164  -0.0535 0.1915  90  ASP C CA  
3871  C C   . ASP C 90  ? 1.6569 2.0484 1.3932 -0.0031 -0.0512 0.1990  90  ASP C C   
3872  O O   . ASP C 90  ? 1.6117 2.0225 1.3727 -0.0201 -0.0272 0.2144  90  ASP C O   
3873  C CB  . ASP C 90  ? 1.6250 2.1073 1.3983 0.0252  -0.0274 0.1858  90  ASP C CB  
3874  C CG  . ASP C 90  ? 1.7666 2.2760 1.5340 0.0360  -0.0160 0.1879  90  ASP C CG  
3875  O OD1 . ASP C 90  ? 1.7861 2.2558 1.5215 0.0344  -0.0264 0.1975  90  ASP C OD1 
3876  O OD2 . ASP C 90  ? 1.8407 2.4096 1.6353 0.0449  0.0030  0.1820  90  ASP C OD2 
3877  N N   . THR C 91  ? 1.6544 2.0000 1.3616 0.0003  -0.0802 0.1872  91  THR C N   
3878  C CA  . THR C 91  ? 1.6622 1.9747 1.3598 -0.0152 -0.0818 0.1929  91  THR C CA  
3879  C C   . THR C 91  ? 1.7031 2.0002 1.3834 -0.0394 -0.0700 0.2192  91  THR C C   
3880  O O   . THR C 91  ? 1.7244 1.9842 1.3679 -0.0476 -0.0912 0.2267  91  THR C O   
3881  C CB  . THR C 91  ? 1.8383 2.0957 1.4990 -0.0074 -0.1215 0.1727  91  THR C CB  
3882  O OG1 . THR C 91  ? 1.8530 2.1301 1.5320 0.0193  -0.1368 0.1439  91  THR C OG1 
3883  C CG2 . THR C 91  ? 1.8333 2.0525 1.4813 -0.0193 -0.1231 0.1750  91  THR C CG2 
3884  N N   . ALA C 92  ? 1.6240 1.9534 1.3342 -0.0505 -0.0397 0.2332  92  ALA C N   
3885  C CA  . ALA C 92  ? 1.6146 1.9418 1.3196 -0.0710 -0.0253 0.2545  92  ALA C CA  
3886  C C   . ALA C 92  ? 1.6294 1.9841 1.3622 -0.0780 -0.0016 0.2608  92  ALA C C   
3887  O O   . ALA C 92  ? 1.6032 1.9772 1.3608 -0.0683 0.0014  0.2527  92  ALA C O   
3888  C CB  . ALA C 92  ? 1.6150 1.9518 1.3255 -0.0731 -0.0231 0.2632  92  ALA C CB  
3889  N N   . MET C 93  ? 1.5858 1.9434 1.3163 -0.0939 0.0111  0.2755  93  MET C N   
3890  C CA  . MET C 93  ? 1.5641 1.9479 1.3174 -0.0986 0.0285  0.2793  93  MET C CA  
3891  C C   . MET C 93  ? 1.5780 1.9892 1.3631 -0.1052 0.0374  0.2829  93  MET C C   
3892  O O   . MET C 93  ? 1.5860 1.9883 1.3670 -0.1141 0.0373  0.2913  93  MET C O   
3893  C CB  . MET C 93  ? 1.6201 1.9949 1.3504 -0.1102 0.0366  0.2898  93  MET C CB  
3894  C CG  . MET C 93  ? 1.6508 2.0573 1.4031 -0.1113 0.0525  0.2903  93  MET C CG  
3895  S SD  . MET C 93  ? 1.7022 2.1132 1.4625 -0.0907 0.0459  0.2774  93  MET C SD  
3896  C CE  . MET C 93  ? 1.6825 2.1048 1.4239 -0.0889 0.0597  0.2794  93  MET C CE  
3897  N N   . TYR C 94  ? 1.4900 1.9274 1.3046 -0.1018 0.0397  0.2777  94  TYR C N   
3898  C CA  . TYR C 94  ? 1.4525 1.9084 1.2918 -0.1109 0.0434  0.2797  94  TYR C CA  
3899  C C   . TYR C 94  ? 1.4891 1.9613 1.3492 -0.1184 0.0443  0.2786  94  TYR C C   
3900  O O   . TYR C 94  ? 1.4819 1.9647 1.3503 -0.1110 0.0368  0.2742  94  TYR C O   
3901  C CB  . TYR C 94  ? 1.4423 1.9168 1.2964 -0.1052 0.0401  0.2760  94  TYR C CB  
3902  C CG  . TYR C 94  ? 1.4624 1.9262 1.2971 -0.0932 0.0370  0.2719  94  TYR C CG  
3903  C CD1 . TYR C 94  ? 1.4999 1.9585 1.3262 -0.0788 0.0288  0.2630  94  TYR C CD1 
3904  C CD2 . TYR C 94  ? 1.4699 1.9230 1.2926 -0.0933 0.0371  0.2743  94  TYR C CD2 
3905  C CE1 . TYR C 94  ? 1.5190 1.9675 1.3269 -0.0646 0.0194  0.2538  94  TYR C CE1 
3906  C CE2 . TYR C 94  ? 1.4960 1.9387 1.2971 -0.0765 0.0277  0.2672  94  TYR C CE2 
3907  C CZ  . TYR C 94  ? 1.5682 2.0106 1.3622 -0.0621 0.0181  0.2557  94  TYR C CZ  
3908  O OH  . TYR C 94  ? 1.5714 2.0031 1.3435 -0.0426 0.0026  0.2438  94  TYR C OH  
3909  N N   . TYR C 95  ? 1.4392 1.9090 1.3076 -0.1308 0.0483  0.2811  95  TYR C N   
3910  C CA  . TYR C 95  ? 1.4220 1.9062 1.3122 -0.1374 0.0447  0.2747  95  TYR C CA  
3911  C C   . TYR C 95  ? 1.4653 1.9466 1.3736 -0.1502 0.0355  0.2723  95  TYR C C   
3912  O O   . TYR C 95  ? 1.4663 1.9305 1.3664 -0.1546 0.0386  0.2781  95  TYR C O   
3913  C CB  . TYR C 95  ? 1.4411 1.9249 1.3311 -0.1434 0.0555  0.2776  95  TYR C CB  
3914  C CG  . TYR C 95  ? 1.4895 1.9779 1.3570 -0.1358 0.0660  0.2818  95  TYR C CG  
3915  C CD1 . TYR C 95  ? 1.5194 2.0279 1.3861 -0.1238 0.0663  0.2725  95  TYR C CD1 
3916  C CD2 . TYR C 95  ? 1.5276 1.9968 1.3703 -0.1410 0.0719  0.2955  95  TYR C CD2 
3917  C CE1 . TYR C 95  ? 1.5583 2.0677 1.3967 -0.1172 0.0776  0.2768  95  TYR C CE1 
3918  C CE2 . TYR C 95  ? 1.5682 2.0376 1.3842 -0.1394 0.0800  0.3014  95  TYR C CE2 
3919  C CZ  . TYR C 95  ? 1.6468 2.1367 1.4593 -0.1277 0.0858  0.2921  95  TYR C CZ  
3920  O OH  . TYR C 95  ? 1.6636 2.1505 1.4424 -0.1260 0.0952  0.2981  95  TYR C OH  
3921  N N   . CYS C 96  ? 1.4133 1.9062 1.3413 -0.1553 0.0198  0.2628  96  CYS C N   
3922  C CA  . CYS C 96  ? 1.4056 1.8879 1.3468 -0.1722 0.0049  0.2586  96  CYS C CA  
3923  C C   . CYS C 96  ? 1.4081 1.8890 1.3668 -0.1765 -0.0041 0.2448  96  CYS C C   
3924  O O   . CYS C 96  ? 1.4008 1.9024 1.3628 -0.1635 -0.0021 0.2379  96  CYS C O   
3925  C CB  . CYS C 96  ? 1.4177 1.9137 1.3665 -0.1776 -0.0158 0.2595  96  CYS C CB  
3926  S SG  . CYS C 96  ? 1.4592 1.9708 1.4235 -0.1707 -0.0487 0.2469  96  CYS C SG  
3927  N N   . ALA C 97  ? 1.3349 1.7907 1.3036 -0.1925 -0.0138 0.2393  97  ALA C N   
3928  C CA  . ALA C 97  ? 1.3220 1.7785 1.3139 -0.1953 -0.0242 0.2223  97  ALA C CA  
3929  C C   . ALA C 97  ? 1.3742 1.7984 1.3782 -0.2142 -0.0523 0.2086  97  ALA C C   
3930  O O   . ALA C 97  ? 1.3939 1.7821 1.3849 -0.2276 -0.0534 0.2172  97  ALA C O   
3931  C CB  . ALA C 97  ? 1.3370 1.7934 1.3344 -0.1926 0.0000  0.2299  97  ALA C CB  
3932  N N   . ARG C 98  ? 1.3135 1.7473 1.3388 -0.2134 -0.0781 0.1851  98  ARG C N   
3933  C CA  . ARG C 98  ? 1.3104 1.7085 1.3479 -0.2317 -0.1144 0.1654  98  ARG C CA  
3934  C C   . ARG C 98  ? 1.3498 1.7168 1.4047 -0.2390 -0.1036 0.1622  98  ARG C C   
3935  O O   . ARG C 98  ? 1.3515 1.7464 1.4306 -0.2276 -0.0882 0.1561  98  ARG C O   
3936  C CB  . ARG C 98  ? 1.3132 1.7349 1.3679 -0.2221 -0.1507 0.1372  98  ARG C CB  
3937  C CG  . ARG C 98  ? 1.3965 1.7778 1.4541 -0.2433 -0.2031 0.1167  98  ARG C CG  
3938  C CD  . ARG C 98  ? 1.3881 1.7910 1.4636 -0.2284 -0.2452 0.0835  98  ARG C CD  
3939  N NE  . ARG C 98  ? 1.3982 1.8109 1.5067 -0.2185 -0.2394 0.0576  98  ARG C NE  
3940  C CZ  . ARG C 98  ? 1.6047 2.0336 1.7344 -0.2043 -0.2779 0.0200  98  ARG C CZ  
3941  N NH1 . ARG C 98  ? 1.4392 1.8684 1.5558 -0.1978 -0.3314 0.0047  98  ARG C NH1 
3942  N NH2 . ARG C 98  ? 1.4898 1.9361 1.6559 -0.1955 -0.2672 -0.0028 98  ARG C NH2 
3943  N N   . VAL C 99  ? 1.2941 1.6032 1.3354 -0.2574 -0.1114 0.1689  99  VAL C N   
3944  C CA  . VAL C 99  ? 1.2921 1.5550 1.3465 -0.2638 -0.1070 0.1701  99  VAL C CA  
3945  C C   . VAL C 99  ? 1.3318 1.5662 1.4185 -0.2746 -0.1424 0.1384  99  VAL C C   
3946  O O   . VAL C 99  ? 1.3285 1.5412 1.4085 -0.2876 -0.1804 0.1186  99  VAL C O   
3947  C CB  . VAL C 99  ? 1.3583 1.5642 1.3771 -0.2719 -0.1009 0.1912  99  VAL C CB  
3948  C CG1 . VAL C 99  ? 1.3668 1.5155 1.3977 -0.2743 -0.1022 0.1957  99  VAL C CG1 
3949  C CG2 . VAL C 99  ? 1.3566 1.5958 1.3478 -0.2573 -0.0697 0.2166  99  VAL C CG2 
3950  N N   . VAL C 100 ? 1.2910 1.5271 1.4146 -0.2700 -0.1323 0.1344  100 VAL C N   
3951  C CA  . VAL C 100 ? 1.2988 1.5120 1.4645 -0.2767 -0.1612 0.1034  100 VAL C CA  
3952  C C   . VAL C 100 ? 1.3707 1.4896 1.5302 -0.2937 -0.1775 0.1090  100 VAL C C   
3953  O O   . VAL C 100 ? 1.3669 1.4632 1.5182 -0.2906 -0.1544 0.1385  100 VAL C O   
3954  C CB  . VAL C 100 ? 1.3441 1.6203 1.5593 -0.2622 -0.1375 0.0993  100 VAL C CB  
3955  C CG1 . VAL C 100 ? 1.3433 1.6199 1.6069 -0.2633 -0.1711 0.0567  100 VAL C CG1 
3956  C CG2 . VAL C 100 ? 1.3317 1.6931 1.5370 -0.2422 -0.1070 0.1084  100 VAL C CG2 
3957  N N   . ALA C 101 ? 1.3444 1.4016 1.5041 -0.3107 -0.2229 0.0802  101 ALA C N   
3958  C CA  . ALA C 101 ? 1.3697 1.3223 1.5175 -0.3270 -0.2457 0.0809  101 ALA C CA  
3959  C C   . ALA C 101 ? 1.4446 1.3456 1.6270 -0.3402 -0.2950 0.0388  101 ALA C C   
3960  O O   . ALA C 101 ? 1.4301 1.3793 1.6403 -0.3365 -0.3162 0.0062  101 ALA C O   
3961  C CB  . ALA C 101 ? 1.4007 1.3042 1.4827 -0.3397 -0.2512 0.0974  101 ALA C CB  
3962  N N   . ASP C 102 ? 1.4417 1.2399 1.6212 -0.3527 -0.3172 0.0376  102 ASP C N   
3963  C CA  . ASP C 102 ? 1.4666 1.1947 1.6780 -0.3667 -0.3686 -0.0031 102 ASP C CA  
3964  C C   . ASP C 102 ? 1.5310 1.2210 1.7085 -0.3883 -0.4214 -0.0359 102 ASP C C   
3965  O O   . ASP C 102 ? 1.5458 1.2083 1.6602 -0.4024 -0.4237 -0.0181 102 ASP C O   
3966  C CB  . ASP C 102 ? 1.5293 1.1440 1.7397 -0.3731 -0.3805 0.0088  102 ASP C CB  
3967  C CG  . ASP C 102 ? 1.7259 1.2465 1.8570 -0.3857 -0.3894 0.0289  102 ASP C CG  
3968  O OD1 . ASP C 102 ? 1.7497 1.2914 1.8434 -0.3730 -0.3504 0.0682  102 ASP C OD1 
3969  O OD2 . ASP C 102 ? 1.8131 1.2405 1.9166 -0.4080 -0.4369 0.0038  102 ASP C OD2 
3970  N N   . ARG C 103 ? 1.1489 2.0835 1.4212 -0.3701 -0.0703 -0.0003 103 ARG C N   
3971  C CA  . ARG C 103 ? 1.1317 2.0752 1.4255 -0.3690 -0.0707 -0.0034 103 ARG C CA  
3972  C C   . ARG C 103 ? 1.1726 2.1104 1.4800 -0.3663 -0.0811 0.0016  103 ARG C C   
3973  O O   . ARG C 103 ? 1.1625 2.1078 1.4943 -0.3679 -0.0859 0.0005  103 ARG C O   
3974  C CB  . ARG C 103 ? 1.1225 2.0766 1.4422 -0.3792 -0.0608 -0.0163 103 ARG C CB  
3975  C CG  . ARG C 103 ? 1.2416 2.2074 1.5510 -0.3879 -0.0505 -0.0204 103 ARG C CG  
3976  C CD  . ARG C 103 ? 1.3721 2.3376 1.6599 -0.4016 -0.0453 -0.0217 103 ARG C CD  
3977  N NE  . ARG C 103 ? 1.4902 2.4670 1.7665 -0.4173 -0.0362 -0.0226 103 ARG C NE  
3978  C CZ  . ARG C 103 ? 1.7424 2.7205 1.9951 -0.4339 -0.0364 -0.0168 103 ARG C CZ  
3979  N NH1 . ARG C 103 ? 1.5996 2.5688 1.8398 -0.4338 -0.0461 -0.0110 103 ARG C NH1 
3980  N NH2 . ARG C 103 ? 1.6538 2.6424 1.8954 -0.4535 -0.0283 -0.0151 103 ARG C NH2 
3981  N N   . GLU C 104 ? 1.1252 2.0502 1.4171 -0.3656 -0.0854 0.0081  104 GLU C N   
3982  C CA  . GLU C 104 ? 1.1185 2.0369 1.4166 -0.3711 -0.0952 0.0153  104 GLU C CA  
3983  C C   . GLU C 104 ? 1.1741 2.0885 1.4486 -0.3715 -0.0980 0.0189  104 GLU C C   
3984  O O   . GLU C 104 ? 1.1676 2.0782 1.4424 -0.3827 -0.1061 0.0243  104 GLU C O   
3985  C CB  . GLU C 104 ? 1.1394 2.0461 1.4403 -0.3765 -0.0956 0.0196  104 GLU C CB  
3986  C CG  . GLU C 104 ? 1.2342 2.1446 1.5644 -0.3785 -0.0921 0.0133  104 GLU C CG  
3987  C CD  . GLU C 104 ? 1.4232 2.3439 1.7983 -0.3828 -0.0973 0.0110  104 GLU C CD  
3988  O OE1 . GLU C 104 ? 1.1542 2.0748 1.5418 -0.3890 -0.1107 0.0212  104 GLU C OE1 
3989  O OE2 . GLU C 104 ? 1.3957 2.3255 1.7959 -0.3829 -0.0883 -0.0016 104 GLU C OE2 
3990  N N   . GLY C 105 ? 1.1419 2.0579 1.3995 -0.3629 -0.0916 0.0159  105 GLY C N   
3991  C CA  . GLY C 105 ? 1.1496 2.0625 1.3913 -0.3621 -0.0906 0.0152  105 GLY C CA  
3992  C C   . GLY C 105 ? 1.2154 2.1150 1.4462 -0.3687 -0.0870 0.0161  105 GLY C C   
3993  O O   . GLY C 105 ? 1.2188 2.1157 1.4456 -0.3825 -0.0905 0.0168  105 GLY C O   
3994  N N   . PHE C 106 ? 1.1780 2.0701 1.4034 -0.3625 -0.0808 0.0169  106 PHE C N   
3995  C CA  . PHE C 106 ? 1.1894 2.0684 1.4042 -0.3674 -0.0755 0.0178  106 PHE C CA  
3996  C C   . PHE C 106 ? 1.2628 2.1375 1.4778 -0.3594 -0.0685 0.0146  106 PHE C C   
3997  O O   . PHE C 106 ? 1.2778 2.1429 1.4882 -0.3645 -0.0611 0.0118  106 PHE C O   
3998  C CB  . PHE C 106 ? 1.2098 2.0826 1.4212 -0.3690 -0.0773 0.0232  106 PHE C CB  
3999  C CG  . PHE C 106 ? 1.2246 2.0942 1.4398 -0.3817 -0.0830 0.0295  106 PHE C CG  
4000  C CD1 . PHE C 106 ? 1.2665 2.1235 1.4689 -0.3900 -0.0814 0.0364  106 PHE C CD1 
4001  C CD2 . PHE C 106 ? 1.2390 2.1184 1.4738 -0.3862 -0.0914 0.0307  106 PHE C CD2 
4002  C CE1 . PHE C 106 ? 1.2743 2.1277 1.4844 -0.4044 -0.0888 0.0466  106 PHE C CE1 
4003  C CE2 . PHE C 106 ? 1.2687 2.1452 1.5169 -0.4002 -0.1002 0.0398  106 PHE C CE2 
4004  C CZ  . PHE C 106 ? 1.2510 2.1142 1.4875 -0.4099 -0.0993 0.0488  106 PHE C CZ  
4005  N N   . GLY C 107 ? 1.2143 2.0960 1.4379 -0.3498 -0.0709 0.0161  107 GLY C N   
4006  C CA  . GLY C 107 ? 1.2202 2.0989 1.4549 -0.3434 -0.0685 0.0170  107 GLY C CA  
4007  C C   . GLY C 107 ? 1.2784 2.1543 1.5141 -0.3416 -0.0737 0.0240  107 GLY C C   
4008  O O   . GLY C 107 ? 1.2763 2.1479 1.5269 -0.3385 -0.0743 0.0266  107 GLY C O   
4009  N N   . TYR C 108 ? 1.2398 2.1188 1.4634 -0.3456 -0.0784 0.0263  108 TYR C N   
4010  C CA  . TYR C 108 ? 1.2440 2.1228 1.4628 -0.3491 -0.0854 0.0313  108 TYR C CA  
4011  C C   . TYR C 108 ? 1.2796 2.1694 1.5062 -0.3542 -0.0919 0.0371  108 TYR C C   
4012  O O   . TYR C 108 ? 1.2737 2.1728 1.4987 -0.3576 -0.0895 0.0347  108 TYR C O   
4013  C CB  . TYR C 108 ? 1.2621 2.1413 1.4664 -0.3549 -0.0859 0.0280  108 TYR C CB  
4014  C CG  . TYR C 108 ? 1.2935 2.1611 1.4868 -0.3543 -0.0818 0.0271  108 TYR C CG  
4015  C CD1 . TYR C 108 ? 1.3319 2.1895 1.5122 -0.3540 -0.0831 0.0302  108 TYR C CD1 
4016  C CD2 . TYR C 108 ? 1.2982 2.1656 1.4939 -0.3573 -0.0787 0.0253  108 TYR C CD2 
4017  C CE1 . TYR C 108 ? 1.3595 2.2060 1.5250 -0.3565 -0.0786 0.0320  108 TYR C CE1 
4018  C CE2 . TYR C 108 ? 1.3153 2.1719 1.5007 -0.3622 -0.0768 0.0289  108 TYR C CE2 
4019  C CZ  . TYR C 108 ? 1.4331 2.2787 1.6009 -0.3620 -0.0755 0.0323  108 TYR C CZ  
4020  O OH  . TYR C 108 ? 1.4475 2.2817 1.6009 -0.3694 -0.0727 0.0383  108 TYR C OH  
4021  N N   . TYR C 109 ? 1.2236 2.1127 1.4601 -0.3577 -0.1010 0.0464  109 TYR C N   
4022  C CA  . TYR C 109 ? 1.2139 2.1130 1.4567 -0.3696 -0.1097 0.0566  109 TYR C CA  
4023  C C   . TYR C 109 ? 1.2755 2.1789 1.5059 -0.3877 -0.1210 0.0606  109 TYR C C   
4024  O O   . TYR C 109 ? 1.2833 2.1803 1.5155 -0.3878 -0.1298 0.0643  109 TYR C O   
4025  C CB  . TYR C 109 ? 1.2243 2.1212 1.4952 -0.3651 -0.1147 0.0677  109 TYR C CB  
4026  C CG  . TYR C 109 ? 1.2354 2.1297 1.5154 -0.3507 -0.1029 0.0602  109 TYR C CG  
4027  C CD1 . TYR C 109 ? 1.2508 2.1532 1.5215 -0.3506 -0.0981 0.0589  109 TYR C CD1 
4028  C CD2 . TYR C 109 ? 1.2492 2.1337 1.5459 -0.3401 -0.0958 0.0528  109 TYR C CD2 
4029  C CE1 . TYR C 109 ? 1.2530 2.1545 1.5282 -0.3399 -0.0898 0.0513  109 TYR C CE1 
4030  C CE2 . TYR C 109 ? 1.2578 2.1415 1.5601 -0.3326 -0.0848 0.0431  109 TYR C CE2 
4031  C CZ  . TYR C 109 ? 1.3348 2.2272 1.6250 -0.3324 -0.0835 0.0428  109 TYR C CZ  
4032  O OH  . TYR C 109 ? 1.3343 2.2271 1.6267 -0.3274 -0.0753 0.0327  109 TYR C OH  
4033  N N   . TYR C 110 ? 1.2958 1.5693 1.0953 -0.0400 0.1662  0.3838  110 TYR C N   
4034  C CA  . TYR C 110 ? 1.2938 1.5848 1.0730 -0.0016 0.1789  0.3513  110 TYR C CA  
4035  C C   . TYR C 110 ? 1.3321 1.6321 1.0808 0.0161  0.1884  0.3183  110 TYR C C   
4036  O O   . TYR C 110 ? 1.3392 1.6613 1.0633 0.0392  0.1997  0.2925  110 TYR C O   
4037  C CB  . TYR C 110 ? 1.3426 1.6162 1.1667 0.0252  0.1509  0.3294  110 TYR C CB  
4038  C CG  . TYR C 110 ? 1.3774 1.6328 1.2406 0.0098  0.1302  0.3598  110 TYR C CG  
4039  C CD1 . TYR C 110 ? 1.3729 1.6504 1.2167 -0.0103 0.1522  0.3944  110 TYR C CD1 
4040  C CD2 . TYR C 110 ? 1.4323 1.6471 1.3526 0.0163  0.0855  0.3531  110 TYR C CD2 
4041  C CE1 . TYR C 110 ? 1.3913 1.6520 1.2713 -0.0269 0.1313  0.4241  110 TYR C CE1 
4042  C CE2 . TYR C 110 ? 1.4628 1.6565 1.4214 0.0006  0.0594  0.3825  110 TYR C CE2 
4043  C CZ  . TYR C 110 ? 1.5314 1.7491 1.4696 -0.0221 0.0830  0.4188  110 TYR C CZ  
4044  O OH  . TYR C 110 ? 1.5742 1.7702 1.5505 -0.0406 0.0552  0.4500  110 TYR C OH  
4045  N N   . GLY C 111 ? 1.2648 1.5516 1.0141 0.0015  0.1827  0.3198  111 GLY C N   
4046  C CA  . GLY C 111 ? 1.2558 1.5453 0.9815 0.0142  0.1865  0.2925  111 GLY C CA  
4047  C C   . GLY C 111 ? 1.3298 1.5881 1.0880 0.0163  0.1593  0.2776  111 GLY C C   
4048  O O   . GLY C 111 ? 1.3488 1.5845 1.1419 0.0004  0.1382  0.2947  111 GLY C O   
4049  N N   . MET C 112 ? 1.2887 1.5445 1.0342 0.0324  0.1568  0.2478  112 MET C N   
4050  C CA  . MET C 112 ? 1.3173 1.5433 1.0896 0.0346  0.1320  0.2331  112 MET C CA  
4051  C C   . MET C 112 ? 1.4003 1.6231 1.1767 0.0643  0.1232  0.1920  112 MET C C   
4052  O O   . MET C 112 ? 1.3924 1.6385 1.1349 0.0734  0.1387  0.1730  112 MET C O   
4053  C CB  . MET C 112 ? 1.3402 1.5647 1.1013 0.0143  0.1341  0.2410  112 MET C CB  
4054  C CG  . MET C 112 ? 1.3713 1.6209 1.0922 0.0146  0.1565  0.2370  112 MET C CG  
4055  S SD  . MET C 112 ? 1.3931 1.6655 1.1062 -0.0156 0.1726  0.2641  112 MET C SD  
4056  C CE  . MET C 112 ? 1.3566 1.6168 1.1005 -0.0370 0.1534  0.2640  112 MET C CE  
4057  N N   . ASP C 113 ? 1.4027 1.5980 1.2219 0.0767  0.0956  0.1776  113 ASP C N   
4058  C CA  . ASP C 113 ? 1.4368 1.6324 1.2724 0.1055  0.0846  0.1329  113 ASP C CA  
4059  C C   . ASP C 113 ? 1.5064 1.6860 1.3382 0.1080  0.0753  0.1112  113 ASP C C   
4060  O O   . ASP C 113 ? 1.4898 1.6947 1.2940 0.1162  0.0898  0.0850  113 ASP C O   
4061  C CB  . ASP C 113 ? 1.4954 1.6694 1.3861 0.1223  0.0555  0.1215  113 ASP C CB  
4062  C CG  . ASP C 113 ? 1.7135 1.8396 1.6404 0.1040  0.0218  0.1527  113 ASP C CG  
4063  O OD1 . ASP C 113 ? 1.7384 1.8437 1.6554 0.0818  0.0143  0.1704  113 ASP C OD1 
4064  O OD2 . ASP C 113 ? 1.8229 1.9332 1.7891 0.1101  -0.0008 0.1577  113 ASP C OD2 
4065  N N   . VAL C 114 ? 1.5015 1.6406 1.3594 0.0986  0.0490  0.1215  114 VAL C N   
4066  C CA  . VAL C 114 ? 1.5259 1.6462 1.3818 0.1000  0.0380  0.1033  114 VAL C CA  
4067  C C   . VAL C 114 ? 1.5579 1.6904 1.3755 0.0796  0.0566  0.1209  114 VAL C C   
4068  O O   . VAL C 114 ? 1.5286 1.6608 1.3421 0.0564  0.0595  0.1531  114 VAL C O   
4069  C CB  . VAL C 114 ? 1.6151 1.6866 1.5097 0.0958  -0.0007 0.1081  114 VAL C CB  
4070  C CG1 . VAL C 114 ? 1.6349 1.6893 1.5261 0.1016  -0.0106 0.0837  114 VAL C CG1 
4071  C CG2 . VAL C 114 ? 1.6424 1.6966 1.5840 0.1157  -0.0265 0.0944  114 VAL C CG2 
4072  N N   . TRP C 115 ? 1.5280 1.6745 1.3201 0.0864  0.0677  0.0978  115 TRP C N   
4073  C CA  . TRP C 115 ? 1.5115 1.6674 1.2719 0.0706  0.0802  0.1095  115 TRP C CA  
4074  C C   . TRP C 115 ? 1.6204 1.7560 1.3816 0.0691  0.0673  0.0954  115 TRP C C   
4075  O O   . TRP C 115 ? 1.6374 1.7621 1.4105 0.0834  0.0567  0.0681  115 TRP C O   
4076  C CB  . TRP C 115 ? 1.4709 1.6610 1.1930 0.0736  0.1017  0.1017  115 TRP C CB  
4077  C CG  . TRP C 115 ? 1.4498 1.6610 1.1592 0.0680  0.1178  0.1242  115 TRP C CG  
4078  C CD1 . TRP C 115 ? 1.4834 1.7058 1.2038 0.0768  0.1222  0.1256  115 TRP C CD1 
4079  C CD2 . TRP C 115 ? 1.4172 1.6429 1.0995 0.0537  0.1311  0.1451  115 TRP C CD2 
4080  N NE1 . TRP C 115 ? 1.4437 1.6859 1.1417 0.0664  0.1396  0.1499  115 TRP C NE1 
4081  C CE2 . TRP C 115 ? 1.4431 1.6872 1.1181 0.0526  0.1449  0.1611  115 TRP C CE2 
4082  C CE3 . TRP C 115 ? 1.4222 1.6466 1.0900 0.0425  0.1305  0.1501  115 TRP C CE3 
4083  C CZ2 . TRP C 115 ? 1.4069 1.6668 1.0579 0.0402  0.1588  0.1822  115 TRP C CZ2 
4084  C CZ3 . TRP C 115 ? 1.4160 1.6560 1.0659 0.0324  0.1414  0.1679  115 TRP C CZ3 
4085  C CH2 . TRP C 115 ? 1.4070 1.6639 1.0478 0.0308  0.1558  0.1841  115 TRP C CH2 
4086  N N   . GLY C 116 ? 1.5989 1.7331 1.3495 0.0516  0.0686  0.1117  116 GLY C N   
4087  C CA  . GLY C 116 ? 1.6253 1.7437 1.3730 0.0469  0.0582  0.1024  116 GLY C CA  
4088  C C   . GLY C 116 ? 1.7028 1.8337 1.4232 0.0530  0.0666  0.0826  116 GLY C C   
4089  O O   . GLY C 116 ? 1.6886 1.8430 1.3874 0.0562  0.0799  0.0795  116 GLY C O   
4090  N N   . GLN C 117 ? 1.6880 1.8033 1.4064 0.0505  0.0566  0.0713  117 GLN C N   
4091  C CA  . GLN C 117 ? 1.7005 1.8230 1.3942 0.0495  0.0591  0.0547  117 GLN C CA  
4092  C C   . GLN C 117 ? 1.7545 1.8939 1.4244 0.0390  0.0656  0.0675  117 GLN C C   
4093  O O   . GLN C 117 ? 1.7513 1.9046 1.3940 0.0358  0.0685  0.0590  117 GLN C O   
4094  C CB  . GLN C 117 ? 1.7364 1.8348 1.4365 0.0459  0.0455  0.0461  117 GLN C CB  
4095  C CG  . GLN C 117 ? 1.9198 2.0095 1.6268 0.0324  0.0385  0.0650  117 GLN C CG  
4096  C CD  . GLN C 117 ? 2.2598 2.3232 1.9777 0.0284  0.0229  0.0614  117 GLN C CD  
4097  O OE1 . GLN C 117 ? 2.2622 2.3058 1.9977 0.0321  0.0115  0.0613  117 GLN C OE1 
4098  N NE2 . GLN C 117 ? 2.1548 2.2155 1.8631 0.0193  0.0187  0.0605  117 GLN C NE2 
4099  N N   . GLY C 118 ? 1.7131 1.8530 1.3949 0.0312  0.0648  0.0860  118 GLY C N   
4100  C CA  . GLY C 118 ? 1.7013 1.8540 1.3733 0.0235  0.0656  0.0951  118 GLY C CA  
4101  C C   . GLY C 118 ? 1.7634 1.9080 1.4449 0.0163  0.0534  0.0918  118 GLY C C   
4102  O O   . GLY C 118 ? 1.7898 1.9207 1.4617 0.0157  0.0448  0.0805  118 GLY C O   
4103  N N   . THR C 119 ? 1.6883 1.8465 1.3904 0.0089  0.0532  0.0994  119 THR C N   
4104  C CA  . THR C 119 ? 1.6823 1.8425 1.3987 0.0020  0.0420  0.0927  119 THR C CA  
4105  C C   . THR C 119 ? 1.7004 1.8688 1.4147 0.0035  0.0341  0.0888  119 THR C C   
4106  O O   . THR C 119 ? 1.6717 1.8569 1.3905 0.0042  0.0393  0.0940  119 THR C O   
4107  C CB  . THR C 119 ? 1.8261 2.0046 1.5683 -0.0111 0.0438  0.0973  119 THR C CB  
4108  O OG1 . THR C 119 ? 1.8567 2.0186 1.5982 -0.0138 0.0437  0.1046  119 THR C OG1 
4109  C CG2 . THR C 119 ? 1.8216 2.0096 1.5787 -0.0198 0.0327  0.0864  119 THR C CG2 
4110  N N   . THR C 120 ? 1.6637 1.8172 1.3715 0.0030  0.0187  0.0804  120 THR C N   
4111  C CA  . THR C 120 ? 1.6601 1.8124 1.3677 0.0031  0.0015  0.0773  120 THR C CA  
4112  C C   . THR C 120 ? 1.6834 1.8541 1.4297 0.0024  -0.0086 0.0655  120 THR C C   
4113  O O   . THR C 120 ? 1.6939 1.8605 1.4502 -0.0007 -0.0175 0.0569  120 THR C O   
4114  C CB  . THR C 120 ? 1.7770 1.9045 1.4546 -0.0020 -0.0129 0.0765  120 THR C CB  
4115  O OG1 . THR C 120 ? 1.7557 1.8799 1.4047 -0.0026 0.0010  0.0792  120 THR C OG1 
4116  C CG2 . THR C 120 ? 1.7721 1.8913 1.4405 -0.0066 -0.0367 0.0798  120 THR C CG2 
4117  N N   . VAL C 121 ? 1.5939 1.7896 1.3632 0.0048  -0.0067 0.0623  121 VAL C N   
4118  C CA  . VAL C 121 ? 1.5670 1.7939 1.3804 0.0043  -0.0147 0.0433  121 VAL C CA  
4119  C C   . VAL C 121 ? 1.6225 1.8422 1.4526 0.0129  -0.0420 0.0326  121 VAL C C   
4120  O O   . VAL C 121 ? 1.6144 1.8304 1.4381 0.0171  -0.0457 0.0388  121 VAL C O   
4121  C CB  . VAL C 121 ? 1.5822 1.8523 1.4188 -0.0036 0.0061  0.0408  121 VAL C CB  
4122  C CG1 . VAL C 121 ? 1.5607 1.8766 1.4468 -0.0064 -0.0013 0.0133  121 VAL C CG1 
4123  C CG2 . VAL C 121 ? 1.5815 1.8529 1.4053 -0.0162 0.0224  0.0524  121 VAL C CG2 
4124  N N   . THR C 122 ? 1.5893 1.8053 1.4418 0.0148  -0.0642 0.0171  122 THR C N   
4125  C CA  . THR C 122 ? 1.5972 1.8021 1.4750 0.0231  -0.0991 0.0044  122 THR C CA  
4126  C C   . THR C 122 ? 1.6230 1.8763 1.5634 0.0291  -0.1037 -0.0289 122 THR C C   
4127  O O   . THR C 122 ? 1.6066 1.8859 1.5636 0.0234  -0.0954 -0.0423 122 THR C O   
4128  C CB  . THR C 122 ? 1.7109 1.8749 1.5691 0.0188  -0.1251 0.0113  122 THR C CB  
4129  O OG1 . THR C 122 ? 1.7067 1.8448 1.5106 0.0086  -0.1102 0.0342  122 THR C OG1 
4130  C CG2 . THR C 122 ? 1.7187 1.8541 1.5873 0.0222  -0.1685 0.0103  122 THR C CG2 
4131  N N   . VAL C 123 ? 1.5768 1.8469 1.5517 0.0389  -0.1167 -0.0448 123 VAL C N   
4132  C CA  . VAL C 123 ? 1.5610 1.8876 1.6031 0.0450  -0.1215 -0.0850 123 VAL C CA  
4133  C C   . VAL C 123 ? 1.6450 1.9546 1.7307 0.0624  -0.1681 -0.1071 123 VAL C C   
4134  O O   . VAL C 123 ? 1.6391 1.9537 1.7480 0.0719  -0.1802 -0.1173 123 VAL C O   
4135  C CB  . VAL C 123 ? 1.5795 1.9627 1.6397 0.0379  -0.0901 -0.0952 123 VAL C CB  
4136  C CG1 . VAL C 123 ? 1.5576 2.0159 1.6812 0.0340  -0.0866 -0.1400 123 VAL C CG1 
4137  C CG2 . VAL C 123 ? 1.5667 1.9476 1.5770 0.0208  -0.0534 -0.0636 123 VAL C CG2 
4138  N N   . SER C 124 ? 1.6341 1.9209 1.7315 0.0658  -0.1970 -0.1137 124 SER C N   
4139  C CA  . SER C 124 ? 1.6605 1.9227 1.8017 0.0808  -0.2497 -0.1326 124 SER C CA  
4140  C C   . SER C 124 ? 1.7013 1.9965 1.8988 0.0876  -0.2653 -0.1691 124 SER C C   
4141  O O   . SER C 124 ? 1.6823 1.9893 1.8596 0.0762  -0.2443 -0.1636 124 SER C O   
4142  C CB  . SER C 124 ? 1.7488 1.9333 1.8381 0.0733  -0.2817 -0.0944 124 SER C CB  
4143  O OG  . SER C 124 ? 1.8950 2.0475 2.0244 0.0834  -0.3404 -0.1074 124 SER C OG  
4144  N N   . SER C 125 ? 1.6722 1.9813 1.9417 0.1068  -0.3050 -0.2078 125 SER C N   
4145  C CA  . SER C 125 ? 1.6776 2.0242 2.0144 0.1176  -0.3269 -0.2514 125 SER C CA  
4146  C C   . SER C 125 ? 1.7865 2.0742 2.1073 0.1148  -0.3630 -0.2316 125 SER C C   
4147  O O   . SER C 125 ? 1.7826 2.1002 2.1420 0.1186  -0.3714 -0.2587 125 SER C O   
4148  C CB  . SER C 125 ? 1.7200 2.1003 2.1456 0.1418  -0.3611 -0.3033 125 SER C CB  
4149  O OG  . SER C 125 ? 1.8049 2.2495 2.2482 0.1404  -0.3247 -0.3253 125 SER C OG  
4150  N N   . ALA C 126 ? 1.7921 2.0018 2.0537 0.1043  -0.3832 -0.1846 126 ALA C N   
4151  C CA  . ALA C 126 ? 1.8376 1.9895 2.0744 0.0932  -0.4168 -0.1596 126 ALA C CA  
4152  C C   . ALA C 126 ? 1.8977 2.0641 2.0921 0.0770  -0.3763 -0.1453 126 ALA C C   
4153  O O   . ALA C 126 ? 1.8715 2.0544 2.0181 0.0662  -0.3276 -0.1281 126 ALA C O   
4154  C CB  . ALA C 126 ? 1.8833 1.9620 2.0593 0.0769  -0.4421 -0.1135 126 ALA C CB  
4155  N N   . SER C 127 ? 1.8877 2.0481 2.1033 0.0758  -0.3988 -0.1538 127 SER C N   
4156  C CA  . SER C 127 ? 1.8853 2.0561 2.0644 0.0604  -0.3673 -0.1421 127 SER C CA  
4157  C C   . SER C 127 ? 1.9689 2.0755 2.0712 0.0361  -0.3674 -0.0931 127 SER C C   
4158  O O   . SER C 127 ? 1.9900 2.0459 2.0700 0.0280  -0.3983 -0.0692 127 SER C O   
4159  C CB  . SER C 127 ? 1.9371 2.1386 2.1741 0.0692  -0.3886 -0.1761 127 SER C CB  
4160  O OG  . SER C 127 ? 2.0104 2.2939 2.3048 0.0830  -0.3695 -0.2243 127 SER C OG  
4161  N N   . THR C 128 ? 1.9241 2.0370 1.9853 0.0217  -0.3336 -0.0799 128 THR C N   
4162  C CA  . THR C 128 ? 1.9464 2.0120 1.9384 -0.0023 -0.3262 -0.0413 128 THR C CA  
4163  C C   . THR C 128 ? 2.0394 2.0574 2.0345 -0.0153 -0.3763 -0.0276 128 THR C C   
4164  O O   . THR C 128 ? 2.0433 2.0697 2.0770 -0.0106 -0.3968 -0.0440 128 THR C O   
4165  C CB  . THR C 128 ? 2.0565 2.1432 2.0151 -0.0113 -0.2821 -0.0374 128 THR C CB  
4166  O OG1 . THR C 128 ? 2.0439 2.1782 2.0117 -0.0018 -0.2461 -0.0529 128 THR C OG1 
4167  C CG2 . THR C 128 ? 2.0543 2.1019 1.9434 -0.0332 -0.2658 -0.0040 128 THR C CG2 
4168  N N   . LYS C 129 ? 2.0268 1.9977 1.9806 -0.0348 -0.3981 0.0025  129 LYS C N   
4169  C CA  . LYS C 129 ? 2.0729 1.9943 2.0201 -0.0573 -0.4507 0.0228  129 LYS C CA  
4170  C C   . LYS C 129 ? 2.1721 2.0617 2.0419 -0.0942 -0.4435 0.0597  129 LYS C C   
4171  O O   . LYS C 129 ? 2.1542 2.0466 1.9874 -0.0987 -0.4233 0.0698  129 LYS C O   
4172  C CB  . LYS C 129 ? 2.1185 2.0174 2.1153 -0.0463 -0.5103 0.0142  129 LYS C CB  
4173  C CG  . LYS C 129 ? 2.2337 2.0835 2.2449 -0.0663 -0.5761 0.0291  129 LYS C CG  
4174  C CD  . LYS C 129 ? 2.3125 2.1226 2.3513 -0.0662 -0.6420 0.0333  129 LYS C CD  
4175  C CE  . LYS C 129 ? 2.4145 2.1675 2.4553 -0.0962 -0.7121 0.0576  129 LYS C CE  
4176  N NZ  . LYS C 129 ? 2.4896 2.2084 2.4427 -0.1489 -0.7150 0.1045  129 LYS C NZ  
4177  N N   . GLY C 130 ? 1.9083 2.6147 2.0412 -0.4850 -0.3035 0.1001  130 GLY C N   
4178  C CA  . GLY C 130 ? 1.9415 2.5575 2.0719 -0.4796 -0.2990 0.0753  130 GLY C CA  
4179  C C   . GLY C 130 ? 1.9979 2.6064 2.0926 -0.4546 -0.3028 0.0400  130 GLY C C   
4180  O O   . GLY C 130 ? 1.9648 2.6276 2.0370 -0.4444 -0.3133 0.0264  130 GLY C O   
4181  N N   . PRO C 131 ? 1.9846 2.5315 2.0753 -0.4442 -0.2988 0.0240  131 PRO C N   
4182  C CA  . PRO C 131 ? 1.9608 2.5031 2.0214 -0.4245 -0.3006 -0.0017 131 PRO C CA  
4183  C C   . PRO C 131 ? 2.0074 2.5341 2.0450 -0.4241 -0.3046 -0.0371 131 PRO C C   
4184  O O   . PRO C 131 ? 2.0274 2.5244 2.0777 -0.4292 -0.3025 -0.0525 131 PRO C O   
4185  C CB  . PRO C 131 ? 1.9967 2.4960 2.0618 -0.4136 -0.2944 0.0007  131 PRO C CB  
4186  C CG  . PRO C 131 ? 2.0917 2.5546 2.1858 -0.4271 -0.2963 0.0121  131 PRO C CG  
4187  C CD  . PRO C 131 ? 2.0450 2.5324 2.1608 -0.4488 -0.2974 0.0291  131 PRO C CD  
4188  N N   . SER C 132 ? 1.9297 2.4789 1.9377 -0.4130 -0.3126 -0.0522 132 SER C N   
4189  C CA  . SER C 132 ? 1.9225 2.4566 1.8991 -0.4069 -0.3163 -0.0842 132 SER C CA  
4190  C C   . SER C 132 ? 1.9905 2.4889 1.9636 -0.3951 -0.3084 -0.0863 132 SER C C   
4191  O O   . SER C 132 ? 1.9783 2.4798 1.9394 -0.3869 -0.3123 -0.0829 132 SER C O   
4192  C CB  . SER C 132 ? 1.9219 2.4949 1.8684 -0.4007 -0.3360 -0.0978 132 SER C CB  
4193  O OG  . SER C 132 ? 1.9611 2.5898 1.9129 -0.4098 -0.3477 -0.0930 132 SER C OG  
4194  N N   . VAL C 133 ? 1.9662 2.4391 1.9584 -0.3940 -0.3008 -0.0912 133 VAL C N   
4195  C CA  . VAL C 133 ? 1.9684 2.4254 1.9605 -0.3823 -0.2970 -0.0951 133 VAL C CA  
4196  C C   . VAL C 133 ? 2.0324 2.4924 1.9964 -0.3692 -0.2953 -0.1126 133 VAL C C   
4197  O O   . VAL C 133 ? 2.0375 2.5016 1.9956 -0.3616 -0.2946 -0.1355 133 VAL C O   
4198  C CB  . VAL C 133 ? 2.0231 2.4681 2.0504 -0.3794 -0.3005 -0.1015 133 VAL C CB  
4199  C CG1 . VAL C 133 ? 2.0174 2.4647 2.0422 -0.3662 -0.3032 -0.1069 133 VAL C CG1 
4200  C CG2 . VAL C 133 ? 2.0316 2.4653 2.0848 -0.3936 -0.3035 -0.0806 133 VAL C CG2 
4201  N N   . PHE C 134 ? 1.9892 2.4482 1.9372 -0.3654 -0.2932 -0.1023 134 PHE C N   
4202  C CA  . PHE C 134 ? 1.9953 2.4561 1.9176 -0.3541 -0.2907 -0.1084 134 PHE C CA  
4203  C C   . PHE C 134 ? 2.0654 2.5373 1.9935 -0.3487 -0.2848 -0.0981 134 PHE C C   
4204  O O   . PHE C 134 ? 2.0558 2.5256 1.9922 -0.3578 -0.2839 -0.0849 134 PHE C O   
4205  C CB  . PHE C 134 ? 2.0165 2.4694 1.9117 -0.3580 -0.2999 -0.1032 134 PHE C CB  
4206  C CG  . PHE C 134 ? 2.0195 2.4804 1.9083 -0.3639 -0.3146 -0.1121 134 PHE C CG  
4207  C CD1 . PHE C 134 ? 2.0412 2.5170 1.9468 -0.3692 -0.3261 -0.0991 134 PHE C CD1 
4208  C CD2 . PHE C 134 ? 2.0445 2.5101 1.9110 -0.3596 -0.3187 -0.1383 134 PHE C CD2 
4209  C CE1 . PHE C 134 ? 2.0361 2.5418 1.9391 -0.3701 -0.3451 -0.1079 134 PHE C CE1 
4210  C CE2 . PHE C 134 ? 2.0680 2.5560 1.9243 -0.3660 -0.3361 -0.1487 134 PHE C CE2 
4211  C CZ  . PHE C 134 ? 2.0256 2.5385 1.9008 -0.3710 -0.3513 -0.1316 134 PHE C CZ  
4212  N N   . PRO C 135 ? 2.0427 2.5370 1.9661 -0.3306 -0.2807 -0.1064 135 PRO C N   
4213  C CA  . PRO C 135 ? 2.0441 2.5684 1.9723 -0.3259 -0.2782 -0.0951 135 PRO C CA  
4214  C C   . PRO C 135 ? 2.1025 2.6197 2.0093 -0.3375 -0.2720 -0.0684 135 PRO C C   
4215  O O   . PRO C 135 ? 2.1103 2.5975 1.9997 -0.3441 -0.2742 -0.0617 135 PRO C O   
4216  C CB  . PRO C 135 ? 2.0606 2.6310 2.0017 -0.2952 -0.2790 -0.1149 135 PRO C CB  
4217  C CG  . PRO C 135 ? 2.1172 2.6707 2.0549 -0.2837 -0.2769 -0.1386 135 PRO C CG  
4218  C CD  . PRO C 135 ? 2.0693 2.5745 1.9831 -0.3090 -0.2779 -0.1292 135 PRO C CD  
4219  N N   . LEU C 136 ? 2.0520 2.6001 1.9628 -0.3405 -0.2685 -0.0552 136 LEU C N   
4220  C CA  . LEU C 136 ? 2.0648 2.6112 1.9657 -0.3551 -0.2618 -0.0263 136 LEU C CA  
4221  C C   . LEU C 136 ? 2.1255 2.7363 2.0253 -0.3452 -0.2569 -0.0145 136 LEU C C   
4222  O O   . LEU C 136 ? 2.1046 2.7571 2.0136 -0.3442 -0.2614 -0.0247 136 LEU C O   
4223  C CB  . LEU C 136 ? 2.0560 2.5801 1.9690 -0.3756 -0.2613 -0.0221 136 LEU C CB  
4224  C CG  . LEU C 136 ? 2.0917 2.5766 2.0145 -0.3793 -0.2682 -0.0319 136 LEU C CG  
4225  C CD1 . LEU C 136 ? 2.0735 2.5589 2.0129 -0.3839 -0.2649 -0.0403 136 LEU C CD1 
4226  C CD2 . LEU C 136 ? 2.1220 2.5796 2.0436 -0.3844 -0.2773 -0.0196 136 LEU C CD2 
4227  N N   . ALA C 137 ? 2.1078 2.7343 1.9941 -0.3338 -0.2505 0.0044  137 ALA C N   
4228  C CA  . ALA C 137 ? 2.1114 2.8161 1.9983 -0.3176 -0.2449 0.0218  137 ALA C CA  
4229  C C   . ALA C 137 ? 2.1796 2.9174 2.0700 -0.3431 -0.2405 0.0502  137 ALA C C   
4230  O O   . ALA C 137 ? 2.2018 2.8861 2.0920 -0.3732 -0.2360 0.0699  137 ALA C O   
4231  C CB  . ALA C 137 ? 2.1473 2.8485 2.0137 -0.3001 -0.2359 0.0407  137 ALA C CB  
4232  N N   . PRO C 138 ? 2.1160 2.9508 2.0142 -0.3293 -0.2445 0.0493  138 PRO C N   
4233  C CA  . PRO C 138 ? 2.1248 3.0006 2.0218 -0.3562 -0.2403 0.0722  138 PRO C CA  
4234  C C   . PRO C 138 ? 2.2152 3.0955 2.1078 -0.3761 -0.2239 0.1286  138 PRO C C   
4235  O O   . PRO C 138 ? 2.2250 3.1295 2.1119 -0.3549 -0.2179 0.1523  138 PRO C O   
4236  C CB  . PRO C 138 ? 2.1098 3.1021 2.0145 -0.3299 -0.2578 0.0474  138 PRO C CB  
4237  C CG  . PRO C 138 ? 2.1429 3.1742 2.0619 -0.2844 -0.2647 0.0325  138 PRO C CG  
4238  C CD  . PRO C 138 ? 2.0961 3.0175 2.0104 -0.2861 -0.2579 0.0207  138 PRO C CD  
4239  N N   . SER C 139 ? 2.1865 3.0449 2.0850 -0.4149 -0.2166 0.1485  139 SER C N   
4240  C CA  . SER C 139 ? 2.4199 3.2733 2.3254 -0.4435 -0.2034 0.2056  139 SER C CA  
4241  C C   . SER C 139 ? 2.6371 3.5720 2.5470 -0.4276 -0.1931 0.2219  139 SER C C   
4242  O O   . SER C 139 ? 2.0824 3.0830 1.9911 -0.4609 -0.1862 0.2907  139 SER C O   
4243  C CB  . SER C 139 ? 2.4675 3.2410 2.3946 -0.4803 -0.2007 0.2070  139 SER C CB  
4244  O OG  . SER C 139 ? 2.5007 3.3051 2.4311 -0.4908 -0.2001 0.1724  139 SER C OG  
4245  N N   . THR C 147 ? 1.8490 3.4919 1.6726 -0.4429 -0.2897 0.0684  147 THR C N   
4246  C CA  . THR C 147 ? 1.8144 3.3752 1.6220 -0.4243 -0.3098 -0.0026 147 THR C CA  
4247  C C   . THR C 147 ? 1.8620 3.2452 1.6859 -0.4364 -0.2823 0.0101  147 THR C C   
4248  O O   . THR C 147 ? 1.8596 3.1512 1.6713 -0.4516 -0.2740 -0.0232 147 THR C O   
4249  C CB  . THR C 147 ? 1.9451 3.5436 1.7105 -0.4381 -0.3256 -0.0626 147 THR C CB  
4250  O OG1 . THR C 147 ? 1.9595 3.6966 1.7129 -0.4345 -0.3414 -0.0556 147 THR C OG1 
4251  C CG2 . THR C 147 ? 1.8740 3.4504 1.6173 -0.4030 -0.3650 -0.1400 147 THR C CG2 
4252  N N   . ALA C 148 ? 1.8302 3.1763 1.6806 -0.4249 -0.2700 0.0549  148 ALA C N   
4253  C CA  . ALA C 148 ? 1.8493 3.0474 1.7139 -0.4326 -0.2509 0.0671  148 ALA C CA  
4254  C C   . ALA C 148 ? 1.8710 3.0131 1.7341 -0.4026 -0.2703 0.0154  148 ALA C C   
4255  O O   . ALA C 148 ? 1.8384 3.0440 1.7085 -0.3654 -0.2947 -0.0059 148 ALA C O   
4256  C CB  . ALA C 148 ? 1.8881 3.0728 1.7706 -0.4294 -0.2348 0.1267  148 ALA C CB  
4257  N N   . ALA C 149 ? 1.8410 2.8716 1.7024 -0.4170 -0.2606 -0.0042 149 ALA C N   
4258  C CA  . ALA C 149 ? 1.8202 2.7873 1.6806 -0.3968 -0.2745 -0.0457 149 ALA C CA  
4259  C C   . ALA C 149 ? 1.8635 2.7588 1.7434 -0.3863 -0.2682 -0.0275 149 ALA C C   
4260  O O   . ALA C 149 ? 1.8685 2.7308 1.7574 -0.3994 -0.2506 0.0128  149 ALA C O   
4261  C CB  . ALA C 149 ? 1.8328 2.7347 1.6816 -0.4122 -0.2655 -0.0749 149 ALA C CB  
4262  N N   . LEU C 150 ? 1.8083 2.6788 1.6938 -0.3634 -0.2852 -0.0597 150 LEU C N   
4263  C CA  . LEU C 150 ? 1.8125 2.6207 1.7131 -0.3531 -0.2814 -0.0533 150 LEU C CA  
4264  C C   . LEU C 150 ? 1.8740 2.6021 1.7763 -0.3582 -0.2824 -0.0746 150 LEU C C   
4265  O O   . LEU C 150 ? 1.8612 2.5928 1.7565 -0.3536 -0.2960 -0.1054 150 LEU C O   
4266  C CB  . LEU C 150 ? 1.7949 2.6607 1.7136 -0.3178 -0.2979 -0.0653 150 LEU C CB  
4267  C CG  . LEU C 150 ? 1.8296 2.7678 1.7616 -0.2911 -0.3318 -0.1069 150 LEU C CG  
4268  C CD1 . LEU C 150 ? 1.8237 2.7006 1.7722 -0.2832 -0.3474 -0.1378 150 LEU C CD1 
4269  C CD2 . LEU C 150 ? 1.8524 2.8968 1.8105 -0.2526 -0.3460 -0.1097 150 LEU C CD2 
4270  N N   . GLY C 151 ? 1.8464 2.5101 1.7558 -0.3651 -0.2708 -0.0584 151 GLY C N   
4271  C CA  . GLY C 151 ? 1.8384 2.4403 1.7537 -0.3688 -0.2701 -0.0700 151 GLY C CA  
4272  C C   . GLY C 151 ? 1.8782 2.4591 1.8050 -0.3557 -0.2798 -0.0816 151 GLY C C   
4273  O O   . GLY C 151 ? 1.8633 2.4734 1.7977 -0.3395 -0.2870 -0.0866 151 GLY C O   
4274  N N   . CYS C 152 ? 1.8385 2.3759 1.7715 -0.3603 -0.2791 -0.0866 152 CYS C N   
4275  C CA  . CYS C 152 ? 1.8364 2.3510 1.7836 -0.3548 -0.2866 -0.0939 152 CYS C CA  
4276  C C   . CYS C 152 ? 1.8699 2.3509 1.8212 -0.3634 -0.2799 -0.0852 152 CYS C C   
4277  O O   . CYS C 152 ? 1.8651 2.3385 1.8175 -0.3622 -0.2785 -0.0908 152 CYS C O   
4278  C CB  . CYS C 152 ? 1.8437 2.3712 1.8033 -0.3436 -0.3048 -0.1161 152 CYS C CB  
4279  S SG  . CYS C 152 ? 1.8967 2.4113 1.8901 -0.3353 -0.3175 -0.1265 152 CYS C SG  
4280  N N   . LEU C 153 ? 1.8094 2.2796 1.7614 -0.3674 -0.2782 -0.0747 153 LEU C N   
4281  C CA  . LEU C 153 ? 1.7847 2.2469 1.7471 -0.3695 -0.2788 -0.0685 153 LEU C CA  
4282  C C   . LEU C 153 ? 1.8414 2.2997 1.8144 -0.3704 -0.2836 -0.0692 153 LEU C C   
4283  O O   . LEU C 153 ? 1.8531 2.3082 1.8251 -0.3718 -0.2878 -0.0757 153 LEU C O   
4284  C CB  . LEU C 153 ? 1.7745 2.2372 1.7335 -0.3713 -0.2850 -0.0619 153 LEU C CB  
4285  C CG  . LEU C 153 ? 1.7948 2.2715 1.7707 -0.3668 -0.2966 -0.0614 153 LEU C CG  
4286  C CD1 . LEU C 153 ? 1.7724 2.2654 1.7762 -0.3569 -0.2927 -0.0616 153 LEU C CD1 
4287  C CD2 . LEU C 153 ? 1.8054 2.2822 1.7710 -0.3666 -0.3144 -0.0638 153 LEU C CD2 
4288  N N   . VAL C 154 ? 1.7792 2.2426 1.7659 -0.3674 -0.2816 -0.0626 154 VAL C N   
4289  C CA  . VAL C 154 ? 1.7717 2.2387 1.7729 -0.3709 -0.2845 -0.0530 154 VAL C CA  
4290  C C   . VAL C 154 ? 1.7836 2.2876 1.7958 -0.3642 -0.2886 -0.0447 154 VAL C C   
4291  O O   . VAL C 154 ? 1.7647 2.2890 1.7913 -0.3491 -0.2837 -0.0420 154 VAL C O   
4292  C CB  . VAL C 154 ? 1.8313 2.2825 1.8397 -0.3671 -0.2812 -0.0498 154 VAL C CB  
4293  C CG1 . VAL C 154 ? 1.8396 2.2928 1.8676 -0.3745 -0.2836 -0.0305 154 VAL C CG1 
4294  C CG2 . VAL C 154 ? 1.8452 2.2746 1.8461 -0.3674 -0.2884 -0.0668 154 VAL C CG2 
4295  N N   . LYS C 155 ? 1.7148 2.2358 1.7207 -0.3696 -0.3008 -0.0478 155 LYS C N   
4296  C CA  . LYS C 155 ? 1.6760 2.2471 1.6940 -0.3590 -0.3164 -0.0474 155 LYS C CA  
4297  C C   . LYS C 155 ? 1.7189 2.3343 1.7453 -0.3636 -0.3251 -0.0380 155 LYS C C   
4298  O O   . LYS C 155 ? 1.7360 2.3358 1.7494 -0.3807 -0.3235 -0.0396 155 LYS C O   
4299  C CB  . LYS C 155 ? 1.6978 2.2658 1.6984 -0.3575 -0.3337 -0.0633 155 LYS C CB  
4300  C CG  . LYS C 155 ? 1.8012 2.4164 1.8293 -0.3381 -0.3559 -0.0689 155 LYS C CG  
4301  C CD  . LYS C 155 ? 1.8922 2.5077 1.9021 -0.3371 -0.3852 -0.0858 155 LYS C CD  
4302  C CE  . LYS C 155 ? 1.9297 2.6044 1.9806 -0.3132 -0.4188 -0.0967 155 LYS C CE  
4303  N NZ  . LYS C 155 ? 2.0120 2.6877 2.0426 -0.3107 -0.4583 -0.1172 155 LYS C NZ  
4304  N N   . ASP C 156 ? 1.6474 2.3293 1.7012 -0.3449 -0.3353 -0.0302 156 ASP C N   
4305  C CA  . ASP C 156 ? 1.6284 2.3851 1.6975 -0.3427 -0.3478 -0.0174 156 ASP C CA  
4306  C C   . ASP C 156 ? 1.6894 2.4316 1.7619 -0.3637 -0.3301 0.0098  156 ASP C C   
4307  O O   . ASP C 156 ? 1.7159 2.4311 1.7715 -0.3884 -0.3298 0.0056  156 ASP C O   
4308  C CB  . ASP C 156 ? 1.6454 2.4423 1.6939 -0.3462 -0.3789 -0.0400 156 ASP C CB  
4309  C CG  . ASP C 156 ? 1.8053 2.6306 1.8631 -0.3219 -0.4079 -0.0638 156 ASP C CG  
4310  O OD1 . ASP C 156 ? 1.7829 2.6866 1.8838 -0.2925 -0.4244 -0.0629 156 ASP C OD1 
4311  O OD2 . ASP C 156 ? 1.9052 2.6783 1.9328 -0.3290 -0.4161 -0.0835 156 ASP C OD2 
4312  N N   . TYR C 157 ? 1.6233 2.3848 1.7214 -0.3509 -0.3161 0.0359  157 TYR C N   
4313  C CA  . TYR C 157 ? 1.6495 2.3965 1.7586 -0.3687 -0.3022 0.0694  157 TYR C CA  
4314  C C   . TYR C 157 ? 1.6958 2.5141 1.8344 -0.3441 -0.2955 0.1010  157 TYR C C   
4315  O O   . TYR C 157 ? 1.6542 2.5235 1.8079 -0.3068 -0.2977 0.0893  157 TYR C O   
4316  C CB  . TYR C 157 ? 1.7015 2.3484 1.7999 -0.3831 -0.2885 0.0660  157 TYR C CB  
4317  C CG  . TYR C 157 ? 1.7153 2.3322 1.8095 -0.3594 -0.2768 0.0595  157 TYR C CG  
4318  C CD1 . TYR C 157 ? 1.7559 2.3720 1.8607 -0.3474 -0.2655 0.0837  157 TYR C CD1 
4319  C CD2 . TYR C 157 ? 1.7116 2.2976 1.7872 -0.3503 -0.2764 0.0281  157 TYR C CD2 
4320  C CE1 . TYR C 157 ? 1.7656 2.3546 1.8573 -0.3223 -0.2548 0.0679  157 TYR C CE1 
4321  C CE2 . TYR C 157 ? 1.7212 2.2846 1.7888 -0.3303 -0.2653 0.0158  157 TYR C CE2 
4322  C CZ  . TYR C 157 ? 1.8070 2.3714 1.8797 -0.3148 -0.2548 0.0312  157 TYR C CZ  
4323  O OH  . TYR C 157 ? 1.7850 2.3278 1.8409 -0.2918 -0.2440 0.0100  157 TYR C OH  
4324  N N   . PHE C 158 ? 1.6938 2.5186 1.8465 -0.3625 -0.2873 0.1412  158 PHE C N   
4325  C CA  . PHE C 158 ? 1.6917 2.5845 1.8715 -0.3413 -0.2774 0.1823  158 PHE C CA  
4326  C C   . PHE C 158 ? 1.8326 2.6831 2.0226 -0.3771 -0.2679 0.2279  158 PHE C C   
4327  O O   . PHE C 158 ? 1.8528 2.6992 2.0455 -0.4145 -0.2760 0.2333  158 PHE C O   
4328  C CB  . PHE C 158 ? 1.6516 2.6892 1.8553 -0.3185 -0.2952 0.1885  158 PHE C CB  
4329  C CG  . PHE C 158 ? 1.6388 2.7770 1.8773 -0.2771 -0.2862 0.2221  158 PHE C CG  
4330  C CD1 . PHE C 158 ? 1.7010 2.8872 1.9575 -0.2921 -0.2775 0.2794  158 PHE C CD1 
4331  C CD2 . PHE C 158 ? 1.6054 2.8019 1.8651 -0.2198 -0.2867 0.1961  158 PHE C CD2 
4332  C CE1 . PHE C 158 ? 1.6848 2.9766 1.9740 -0.2475 -0.2675 0.3137  158 PHE C CE1 
4333  C CE2 . PHE C 158 ? 1.6068 2.9116 1.9040 -0.1708 -0.2773 0.2219  158 PHE C CE2 
4334  C CZ  . PHE C 158 ? 1.6107 2.9657 1.9199 -0.1834 -0.2672 0.2822  158 PHE C CZ  
4335  N N   . PRO C 159 ? 1.8376 2.6539 2.0348 -0.3666 -0.2525 0.2587  159 PRO C N   
4336  C CA  . PRO C 159 ? 1.8232 2.6393 2.0127 -0.3198 -0.2387 0.2492  159 PRO C CA  
4337  C C   . PRO C 159 ? 1.8963 2.5977 2.0534 -0.3191 -0.2365 0.2097  159 PRO C C   
4338  O O   . PRO C 159 ? 1.9256 2.5455 2.0738 -0.3539 -0.2466 0.1993  159 PRO C O   
4339  C CB  . PRO C 159 ? 1.8821 2.7273 2.0909 -0.3134 -0.2256 0.3084  159 PRO C CB  
4340  C CG  . PRO C 159 ? 2.0003 2.7931 2.2229 -0.3714 -0.2332 0.3455  159 PRO C CG  
4341  C CD  . PRO C 159 ? 1.9258 2.6969 2.1410 -0.4027 -0.2490 0.3062  159 PRO C CD  
4342  N N   . GLU C 160 ? 1.8302 2.5375 1.9733 -0.2752 -0.2247 0.1835  160 GLU C N   
4343  C CA  . GLU C 160 ? 1.8479 2.4671 1.9552 -0.2689 -0.2229 0.1420  160 GLU C CA  
4344  C C   . GLU C 160 ? 1.9729 2.5111 2.0638 -0.2793 -0.2248 0.1610  160 GLU C C   
4345  O O   . GLU C 160 ? 1.9926 2.5540 2.0993 -0.2742 -0.2175 0.2070  160 GLU C O   
4346  C CB  . GLU C 160 ? 1.8166 2.4788 1.9178 -0.2165 -0.2079 0.1060  160 GLU C CB  
4347  C CG  . GLU C 160 ? 1.8917 2.5393 1.9820 -0.2176 -0.2133 0.0577  160 GLU C CG  
4348  C CD  . GLU C 160 ? 2.0690 2.7097 2.1409 -0.1785 -0.1984 0.0128  160 GLU C CD  
4349  O OE1 . GLU C 160 ? 1.7421 2.4537 1.8377 -0.1302 -0.1839 0.0057  160 GLU C OE1 
4350  O OE2 . GLU C 160 ? 2.0774 2.6514 2.1139 -0.1932 -0.2019 -0.0186 160 GLU C OE2 
4351  N N   . PRO C 161 ? 1.5979 2.2456 1.5708 -0.2857 -0.0234 0.0340  161 PRO C N   
4352  C CA  . PRO C 161 ? 1.6204 2.2302 1.5686 -0.2916 -0.0221 0.0246  161 PRO C CA  
4353  C C   . PRO C 161 ? 1.6994 2.2791 1.6298 -0.2999 -0.0289 0.0256  161 PRO C C   
4354  O O   . PRO C 161 ? 1.6893 2.2758 1.6257 -0.3024 -0.0373 0.0335  161 PRO C O   
4355  C CB  . PRO C 161 ? 1.6439 2.2476 1.5922 -0.2934 -0.0089 0.0251  161 PRO C CB  
4356  C CG  . PRO C 161 ? 1.6890 2.3101 1.6580 -0.2925 -0.0042 0.0361  161 PRO C CG  
4357  C CD  . PRO C 161 ? 1.6173 2.2650 1.6021 -0.2892 -0.0159 0.0425  161 PRO C CD  
4358  N N   . VAL C 162 ? 1.6878 2.2380 1.5966 -0.3049 -0.0261 0.0193  162 VAL C N   
4359  C CA  . VAL C 162 ? 1.7152 2.2383 1.6021 -0.3140 -0.0313 0.0184  162 VAL C CA  
4360  C C   . VAL C 162 ? 1.8046 2.3019 1.6724 -0.3161 -0.0206 0.0130  162 VAL C C   
4361  O O   . VAL C 162 ? 1.7969 2.2936 1.6624 -0.3121 -0.0136 0.0116  162 VAL C O   
4362  C CB  . VAL C 162 ? 1.7667 2.2885 1.6459 -0.3165 -0.0411 0.0202  162 VAL C CB  
4363  C CG1 . VAL C 162 ? 1.7548 2.2962 1.6462 -0.3163 -0.0519 0.0298  162 VAL C CG1 
4364  C CG2 . VAL C 162 ? 1.7570 2.2831 1.6416 -0.3098 -0.0383 0.0168  162 VAL C CG2 
4365  N N   . THR C 163 ? 1.7968 2.2730 1.6518 -0.3217 -0.0192 0.0108  163 THR C N   
4366  C CA  . THR C 163 ? 1.8241 2.2728 1.6570 -0.3211 -0.0075 0.0048  163 THR C CA  
4367  C C   . THR C 163 ? 1.9082 2.3412 1.7123 -0.3262 -0.0122 -0.0001 163 THR C C   
4368  O O   . THR C 163 ? 1.9221 2.3479 1.7135 -0.3362 -0.0243 -0.0020 163 THR C O   
4369  C CB  . THR C 163 ? 1.9144 2.3440 1.7468 -0.3244 -0.0044 0.0026  163 THR C CB  
4370  O OG1 . THR C 163 ? 1.8477 2.3023 1.7141 -0.3191 -0.0004 0.0119  163 THR C OG1 
4371  C CG2 . THR C 163 ? 1.9220 2.3193 1.7298 -0.3204 0.0105  -0.0051 163 THR C CG2 
4372  N N   . VAL C 164 ? 1.8678 2.3013 1.6646 -0.3199 -0.0037 0.0011  164 VAL C N   
4373  C CA  . VAL C 164 ? 1.8860 2.3133 1.6605 -0.3227 -0.0068 0.0003  164 VAL C CA  
4374  C C   . VAL C 164 ? 1.9788 2.3848 1.7249 -0.3176 0.0061  -0.0048 164 VAL C C   
4375  O O   . VAL C 164 ? 1.9706 2.3767 1.7218 -0.3075 0.0203  -0.0007 164 VAL C O   
4376  C CB  . VAL C 164 ? 1.9121 2.3597 1.7032 -0.3196 -0.0098 0.0091  164 VAL C CB  
4377  C CG1 . VAL C 164 ? 1.9248 2.3733 1.6999 -0.3232 -0.0144 0.0126  164 VAL C CG1 
4378  C CG2 . VAL C 164 ? 1.8849 2.3496 1.7016 -0.3208 -0.0196 0.0117  164 VAL C CG2 
4379  N N   . SER C 165 ? 1.9792 2.3690 1.6943 -0.3243 0.0014  -0.0130 165 SER C N   
4380  C CA  . SER C 165 ? 2.0227 2.3906 1.7033 -0.3183 0.0131  -0.0212 165 SER C CA  
4381  C C   . SER C 165 ? 2.1256 2.5002 1.7804 -0.3235 0.0060  -0.0222 165 SER C C   
4382  O O   . SER C 165 ? 2.1235 2.5072 1.7789 -0.3369 -0.0096 -0.0216 165 SER C O   
4383  C CB  . SER C 165 ? 2.0876 2.4215 1.7509 -0.3219 0.0157  -0.0360 165 SER C CB  
4384  O OG  . SER C 165 ? 2.1868 2.5128 1.8386 -0.3392 -0.0022 -0.0435 165 SER C OG  
4385  N N   . TRP C 166 ? 2.1172 2.4924 1.7507 -0.3122 0.0178  -0.0206 166 TRP C N   
4386  C CA  . TRP C 166 ? 2.1379 2.5271 1.7475 -0.3154 0.0125  -0.0194 166 TRP C CA  
4387  C C   . TRP C 166 ? 2.2021 2.5626 1.7628 -0.3172 0.0157  -0.0398 166 TRP C C   
4388  O O   . TRP C 166 ? 2.2206 2.5541 1.7628 -0.3049 0.0313  -0.0496 166 TRP C O   
4389  C CB  . TRP C 166 ? 2.1181 2.5349 1.7376 -0.3017 0.0212  -0.0011 166 TRP C CB  
4390  C CG  . TRP C 166 ? 2.0914 2.5327 1.7565 -0.3020 0.0161  0.0171  166 TRP C CG  
4391  C CD1 . TRP C 166 ? 2.1041 2.5449 1.7952 -0.2955 0.0228  0.0235  166 TRP C CD1 
4392  C CD2 . TRP C 166 ? 2.0691 2.5381 1.7583 -0.3091 0.0035  0.0310  166 TRP C CD2 
4393  N NE1 . TRP C 166 ? 2.0673 2.5300 1.7937 -0.2989 0.0140  0.0371  166 TRP C NE1 
4394  C CE2 . TRP C 166 ? 2.0874 2.5655 1.8147 -0.3063 0.0027  0.0420  166 TRP C CE2 
4395  C CE3 . TRP C 166 ? 2.0948 2.5830 1.7784 -0.3181 -0.0070 0.0360  166 TRP C CE3 
4396  C CZ2 . TRP C 166 ? 2.0562 2.5548 1.8152 -0.3108 -0.0076 0.0554  166 TRP C CZ2 
4397  C CZ3 . TRP C 166 ? 2.0857 2.5993 1.8048 -0.3219 -0.0159 0.0532  166 TRP C CZ3 
4398  C CH2 . TRP C 166 ? 2.0634 2.5787 1.8194 -0.3176 -0.0159 0.0617  166 TRP C CH2 
4399  N N   . ASN C 167 ? 2.1525 2.5195 1.6923 -0.3328 0.0009  -0.0456 167 ASN C N   
4400  C CA  . ASN C 167 ? 2.2018 2.5439 1.6911 -0.3400 -0.0014 -0.0674 167 ASN C CA  
4401  C C   . ASN C 167 ? 2.2798 2.5722 1.7559 -0.3439 0.0007  -0.0883 167 ASN C C   
4402  O O   . ASN C 167 ? 2.3310 2.5889 1.7685 -0.3361 0.0118  -0.1078 167 ASN C O   
4403  C CB  . ASN C 167 ? 2.2089 2.5594 1.6641 -0.3235 0.0126  -0.0694 167 ASN C CB  
4404  C CG  . ASN C 167 ? 2.3434 2.7466 1.8153 -0.3214 0.0087  -0.0460 167 ASN C CG  
4405  O OD1 . ASN C 167 ? 2.2598 2.6883 1.7301 -0.3375 -0.0066 -0.0410 167 ASN C OD1 
4406  N ND2 . ASN C 167 ? 2.1852 2.6084 1.6764 -0.3021 0.0220  -0.0281 167 ASN C ND2 
4407  N N   . SER C 168 ? 2.1966 2.4867 1.7073 -0.3546 -0.0096 -0.0826 168 SER C N   
4408  C CA  . SER C 168 ? 2.2066 2.4591 1.7216 -0.3601 -0.0107 -0.0946 168 SER C CA  
4409  C C   . SER C 168 ? 2.2597 2.4871 1.7783 -0.3390 0.0129  -0.0987 168 SER C C   
4410  O O   . SER C 168 ? 2.2804 2.4697 1.7944 -0.3406 0.0163  -0.1114 168 SER C O   
4411  C CB  . SER C 168 ? 2.3050 2.5260 1.7811 -0.3800 -0.0252 -0.1153 168 SER C CB  
4412  O OG  . SER C 168 ? 2.3927 2.6420 1.8723 -0.4013 -0.0474 -0.1058 168 SER C OG  
4413  N N   . GLY C 169 ? 2.1915 2.4428 1.7228 -0.3203 0.0284  -0.0844 169 GLY C N   
4414  C CA  . GLY C 169 ? 2.1931 2.4318 1.7309 -0.2993 0.0521  -0.0808 169 GLY C CA  
4415  C C   . GLY C 169 ? 2.2945 2.5179 1.7896 -0.2818 0.0699  -0.0893 169 GLY C C   
4416  O O   . GLY C 169 ? 2.3345 2.5221 1.8131 -0.2690 0.0875  -0.0999 169 GLY C O   
4417  N N   . ALA C 170 ? 2.2424 2.4951 1.7212 -0.2795 0.0665  -0.0830 170 ALA C N   
4418  C CA  . ALA C 170 ? 2.2776 2.5274 1.7157 -0.2609 0.0826  -0.0873 170 ALA C CA  
4419  C C   . ALA C 170 ? 2.2731 2.5671 1.7351 -0.2439 0.0931  -0.0580 170 ALA C C   
4420  O O   . ALA C 170 ? 2.2859 2.5760 1.7390 -0.2213 0.1151  -0.0504 170 ALA C O   
4421  C CB  . ALA C 170 ? 2.3269 2.5785 1.7226 -0.2731 0.0688  -0.1036 170 ALA C CB  
4422  N N   . LEU C 171 ? 2.1624 2.4977 1.6565 -0.2549 0.0773  -0.0398 171 LEU C N   
4423  C CA  . LEU C 171 ? 2.1101 2.4874 1.6335 -0.2439 0.0818  -0.0105 171 LEU C CA  
4424  C C   . LEU C 171 ? 2.1110 2.4896 1.6757 -0.2408 0.0880  0.0033  171 LEU C C   
4425  O O   . LEU C 171 ? 2.0696 2.4482 1.6636 -0.2555 0.0753  0.0018  171 LEU C O   
4426  C CB  . LEU C 171 ? 2.0770 2.4921 1.6197 -0.2579 0.0622  0.0016  171 LEU C CB  
4427  C CG  . LEU C 171 ? 2.0879 2.5451 1.6689 -0.2516 0.0614  0.0325  171 LEU C CG  
4428  C CD1 . LEU C 171 ? 2.1121 2.5923 1.6740 -0.2317 0.0750  0.0477  171 LEU C CD1 
4429  C CD2 . LEU C 171 ? 2.0782 2.5626 1.6849 -0.2678 0.0417  0.0414  171 LEU C CD2 
4430  N N   . THR C 172 ? 2.0714 2.4537 1.6369 -0.2210 0.1083  0.0180  172 THR C N   
4431  C CA  . THR C 172 ? 2.0332 2.4216 1.6344 -0.2168 0.1172  0.0342  172 THR C CA  
4432  C C   . THR C 172 ? 2.0237 2.4526 1.6502 -0.2080 0.1211  0.0667  172 THR C C   
4433  O O   . THR C 172 ? 1.9808 2.4261 1.6447 -0.2139 0.1177  0.0815  172 THR C O   
4434  C CB  . THR C 172 ? 2.2063 2.5607 1.7911 -0.2031 0.1393  0.0254  172 THR C CB  
4435  O OG1 . THR C 172 ? 2.2713 2.6148 1.8145 -0.1830 0.1566  0.0228  172 THR C OG1 
4436  C CG2 . THR C 172 ? 2.2026 2.5191 1.7812 -0.2165 0.1319  -0.0013 172 THR C CG2 
4437  N N   . SER C 173 ? 1.9709 2.4177 1.5769 -0.1945 0.1272  0.0785  173 SER C N   
4438  C CA  . SER C 173 ? 1.9335 2.4213 1.5630 -0.1855 0.1300  0.1135  173 SER C CA  
4439  C C   . SER C 173 ? 1.9030 2.4197 1.5676 -0.2027 0.1065  0.1251  173 SER C C   
4440  O O   . SER C 173 ? 1.9005 2.4180 1.5567 -0.2127 0.0927  0.1125  173 SER C O   
4441  C CB  . SER C 173 ? 2.0256 2.5265 1.6215 -0.1628 0.1452  0.1241  173 SER C CB  
4442  O OG  . SER C 173 ? 2.1976 2.6648 1.7565 -0.1451 0.1681  0.1091  173 SER C OG  
4443  N N   . GLY C 174 ? 1.7957 2.3348 1.4996 -0.2067 0.1023  0.1495  174 GLY C N   
4444  C CA  . GLY C 174 ? 1.7492 2.3112 1.4908 -0.2219 0.0814  0.1622  174 GLY C CA  
4445  C C   . GLY C 174 ? 1.7607 2.3052 1.5159 -0.2411 0.0644  0.1391  174 GLY C C   
4446  O O   . GLY C 174 ? 1.7324 2.2905 1.5136 -0.2520 0.0479  0.1455  174 GLY C O   
4447  N N   . VAL C 175 ? 1.7155 2.2307 1.4557 -0.2442 0.0690  0.1147  175 VAL C N   
4448  C CA  . VAL C 175 ? 1.6909 2.1908 1.4413 -0.2596 0.0551  0.0940  175 VAL C CA  
4449  C C   . VAL C 175 ? 1.7084 2.2156 1.4941 -0.2675 0.0491  0.0997  175 VAL C C   
4450  O O   . VAL C 175 ? 1.7015 2.2093 1.4919 -0.2627 0.0605  0.1055  175 VAL C O   
4451  C CB  . VAL C 175 ? 1.7570 2.2257 1.4776 -0.2594 0.0614  0.0688  175 VAL C CB  
4452  C CG1 . VAL C 175 ? 1.7335 2.1916 1.4703 -0.2730 0.0493  0.0536  175 VAL C CG1 
4453  C CG2 . VAL C 175 ? 1.7885 2.2492 1.4727 -0.2574 0.0610  0.0581  175 VAL C CG2 
4454  N N   . HIS C 176 ? 1.6396 2.1531 1.4493 -0.2790 0.0320  0.0984  176 HIS C N   
4455  C CA  A HIS C 176 ? 1.6106 2.1291 1.4499 -0.2873 0.0240  0.0990  176 HIS C CA  
4456  C CA  B HIS C 176 ? 1.6112 2.1296 1.4504 -0.2873 0.0240  0.0990  176 HIS C CA  
4457  C C   . HIS C 176 ? 1.6427 2.1491 1.4870 -0.2955 0.0134  0.0784  176 HIS C C   
4458  O O   . HIS C 176 ? 1.6338 2.1397 1.4839 -0.3002 0.0024  0.0758  176 HIS C O   
4459  C CB  A HIS C 176 ? 1.6112 2.1472 1.4777 -0.2916 0.0139  0.1189  176 HIS C CB  
4460  C CB  B HIS C 176 ? 1.6123 2.1483 1.4788 -0.2916 0.0138  0.1189  176 HIS C CB  
4461  C CG  A HIS C 176 ? 1.6565 2.2105 1.5276 -0.2855 0.0226  0.1441  176 HIS C CG  
4462  C CG  B HIS C 176 ? 1.6575 2.2113 1.5295 -0.2860 0.0223  0.1437  176 HIS C CG  
4463  N ND1 A HIS C 176 ? 1.6681 2.2301 1.5531 -0.2892 0.0252  0.1516  176 HIS C ND1 
4464  N ND1 B HIS C 176 ? 1.6937 2.2628 1.5581 -0.2763 0.0281  0.1644  176 HIS C ND1 
4465  C CD2 A HIS C 176 ? 1.6919 2.2620 1.5565 -0.2759 0.0288  0.1659  176 HIS C CD2 
4466  C CD2 B HIS C 176 ? 1.6706 2.2339 1.5560 -0.2889 0.0256  0.1533  176 HIS C CD2 
4467  C CE1 A HIS C 176 ? 1.6669 2.2484 1.5542 -0.2823 0.0330  0.1792  176 HIS C CE1 
4468  C CE1 B HIS C 176 ? 1.6837 2.2698 1.5576 -0.2727 0.0351  0.1875  176 HIS C CE1 
4469  N NE2 A HIS C 176 ? 1.6849 2.2719 1.5602 -0.2730 0.0357  0.1888  176 HIS C NE2 
4470  N NE2 B HIS C 176 ? 1.6746 2.2580 1.5614 -0.2812 0.0335  0.1821  176 HIS C NE2 
4471  N N   . THR C 177 ? 1.5831 2.0838 1.4271 -0.2961 0.0177  0.0670  177 THR C N   
4472  C CA  . THR C 177 ? 1.5652 2.0603 1.4154 -0.3015 0.0088  0.0509  177 THR C CA  
4473  C C   . THR C 177 ? 1.5939 2.1009 1.4682 -0.3052 0.0037  0.0503  177 THR C C   
4474  O O   . THR C 177 ? 1.5806 2.0973 1.4600 -0.3040 0.0114  0.0524  177 THR C O   
4475  C CB  . THR C 177 ? 1.6245 2.1071 1.4571 -0.2998 0.0151  0.0396  177 THR C CB  
4476  O OG1 . THR C 177 ? 1.6073 2.0769 1.4132 -0.2974 0.0192  0.0385  177 THR C OG1 
4477  C CG2 . THR C 177 ? 1.5896 2.0713 1.4294 -0.3049 0.0044  0.0281  177 THR C CG2 
4478  N N   . PHE C 178 ? 1.5478 2.0549 1.4371 -0.3096 -0.0087 0.0481  178 PHE C N   
4479  C CA  . PHE C 178 ? 1.5391 2.0526 1.4477 -0.3138 -0.0161 0.0437  178 PHE C CA  
4480  C C   . PHE C 178 ? 1.5803 2.0992 1.4911 -0.3124 -0.0172 0.0287  178 PHE C C   
4481  O O   . PHE C 178 ? 1.5798 2.0936 1.4837 -0.3095 -0.0185 0.0216  178 PHE C O   
4482  C CB  . PHE C 178 ? 1.5694 2.0748 1.4929 -0.3174 -0.0282 0.0448  178 PHE C CB  
4483  C CG  . PHE C 178 ? 1.5937 2.1021 1.5248 -0.3198 -0.0295 0.0641  178 PHE C CG  
4484  C CD1 . PHE C 178 ? 1.6333 2.1486 1.5792 -0.3259 -0.0334 0.0739  178 PHE C CD1 
4485  C CD2 . PHE C 178 ? 1.6228 2.1315 1.5471 -0.3166 -0.0277 0.0746  178 PHE C CD2 
4486  C CE1 . PHE C 178 ? 1.6491 2.1716 1.6058 -0.3279 -0.0357 0.0965  178 PHE C CE1 
4487  C CE2 . PHE C 178 ? 1.6618 2.1802 1.5957 -0.3170 -0.0288 0.0958  178 PHE C CE2 
4488  C CZ  . PHE C 178 ? 1.6382 2.1635 1.5898 -0.3222 -0.0329 0.1080  178 PHE C CZ  
4489  N N   . PRO C 179 ? 1.5188 2.0520 1.4401 -0.3149 -0.0179 0.0254  179 PRO C N   
4490  C CA  . PRO C 179 ? 1.5034 2.0494 1.4283 -0.3118 -0.0190 0.0127  179 PRO C CA  
4491  C C   . PRO C 179 ? 1.5405 2.0769 1.4682 -0.3084 -0.0289 -0.0001 179 PRO C C   
4492  O O   . PRO C 179 ? 1.5449 2.0655 1.4776 -0.3106 -0.0361 -0.0012 179 PRO C O   
4493  C CB  . PRO C 179 ? 1.5221 2.0889 1.4567 -0.3168 -0.0187 0.0135  179 PRO C CB  
4494  C CG  . PRO C 179 ? 1.5795 2.1463 1.5144 -0.3220 -0.0138 0.0314  179 PRO C CG  
4495  C CD  . PRO C 179 ? 1.5347 2.0782 1.4653 -0.3214 -0.0184 0.0353  179 PRO C CD  
4496  N N   . ALA C 180 ? 1.4786 2.0260 1.4058 -0.3020 -0.0285 -0.0067 180 ALA C N   
4497  C CA  . ALA C 180 ? 1.4791 2.0223 1.4086 -0.2954 -0.0353 -0.0155 180 ALA C CA  
4498  C C   . ALA C 180 ? 1.5334 2.0825 1.4690 -0.2925 -0.0401 -0.0295 180 ALA C C   
4499  O O   . ALA C 180 ? 1.5175 2.0847 1.4553 -0.2958 -0.0385 -0.0329 180 ALA C O   
4500  C CB  . ALA C 180 ? 1.4773 2.0347 1.4050 -0.2894 -0.0336 -0.0129 180 ALA C CB  
4501  N N   . VAL C 181 ? 1.5113 2.0456 1.4491 -0.2860 -0.0455 -0.0374 181 VAL C N   
4502  C CA  . VAL C 181 ? 1.5308 2.0632 1.4703 -0.2806 -0.0499 -0.0551 181 VAL C CA  
4503  C C   . VAL C 181 ? 1.5794 2.1170 1.5179 -0.2646 -0.0493 -0.0599 181 VAL C C   
4504  O O   . VAL C 181 ? 1.5655 2.0931 1.5063 -0.2607 -0.0487 -0.0494 181 VAL C O   
4505  C CB  . VAL C 181 ? 1.6107 2.1131 1.5560 -0.2881 -0.0569 -0.0613 181 VAL C CB  
4506  C CG1 . VAL C 181 ? 1.6081 2.1169 1.5544 -0.3026 -0.0592 -0.0591 181 VAL C CG1 
4507  C CG2 . VAL C 181 ? 1.6129 2.0923 1.5662 -0.2896 -0.0579 -0.0479 181 VAL C CG2 
4508  N N   . LEU C 182 ? 1.5480 2.1064 1.4830 -0.2549 -0.0489 -0.0734 182 LEU C N   
4509  C CA  . LEU C 182 ? 1.5550 2.1242 1.4886 -0.2363 -0.0471 -0.0761 182 LEU C CA  
4510  C C   . LEU C 182 ? 1.6627 2.1970 1.5965 -0.2284 -0.0488 -0.0873 182 LEU C C   
4511  O O   . LEU C 182 ? 1.6824 2.1964 1.6131 -0.2321 -0.0528 -0.1060 182 LEU C O   
4512  C CB  . LEU C 182 ? 1.5476 2.1555 1.4773 -0.2264 -0.0455 -0.0861 182 LEU C CB  
4513  C CG  . LEU C 182 ? 1.6082 2.2378 1.5371 -0.2042 -0.0425 -0.0842 182 LEU C CG  
4514  C CD1 . LEU C 182 ? 1.5791 2.2584 1.5159 -0.2001 -0.0403 -0.0686 182 LEU C CD1 
4515  C CD2 . LEU C 182 ? 1.6690 2.2944 1.5866 -0.1900 -0.0425 -0.1093 182 LEU C CD2 
4516  N N   . GLN C 183 ? 1.6438 2.1712 1.5827 -0.2186 -0.0461 -0.0743 183 GLN C N   
4517  C CA  . GLN C 183 ? 1.6828 2.1789 1.6269 -0.2084 -0.0449 -0.0793 183 GLN C CA  
4518  C C   . GLN C 183 ? 1.7749 2.2753 1.7103 -0.1864 -0.0411 -0.0976 183 GLN C C   
4519  O O   . GLN C 183 ? 1.7602 2.2957 1.6867 -0.1784 -0.0398 -0.1024 183 GLN C O   
4520  C CB  . GLN C 183 ? 1.6911 2.1862 1.6455 -0.2060 -0.0420 -0.0539 183 GLN C CB  
4521  C CG  . GLN C 183 ? 1.8286 2.3111 1.7905 -0.2253 -0.0454 -0.0395 183 GLN C CG  
4522  C CD  . GLN C 183 ? 2.0099 2.4981 1.9801 -0.2239 -0.0432 -0.0148 183 GLN C CD  
4523  O OE1 . GLN C 183 ? 1.9876 2.4598 1.9711 -0.2170 -0.0405 -0.0080 183 GLN C OE1 
4524  N NE2 . GLN C 183 ? 1.8425 2.3542 1.8060 -0.2312 -0.0445 0.0000  183 GLN C NE2 
4525  N N   . SER C 184 ? 1.7765 2.2426 1.7157 -0.1751 -0.0386 -0.1065 184 SER C N   
4526  C CA  . SER C 184 ? 1.8150 2.2768 1.7437 -0.1506 -0.0329 -0.1256 184 SER C CA  
4527  C C   . SER C 184 ? 1.8454 2.3482 1.7725 -0.1296 -0.0252 -0.1066 184 SER C C   
4528  O O   . SER C 184 ? 1.8453 2.3703 1.7592 -0.1101 -0.0212 -0.1192 184 SER C O   
4529  C CB  . SER C 184 ? 1.9189 2.3307 1.8571 -0.1429 -0.0299 -0.1332 184 SER C CB  
4530  O OG  . SER C 184 ? 2.0825 2.4585 2.0285 -0.1645 -0.0391 -0.1440 184 SER C OG  
4531  N N   . SER C 185 ? 1.7855 2.3024 1.7258 -0.1349 -0.0243 -0.0748 185 SER C N   
4532  C CA  . SER C 185 ? 1.7695 2.3271 1.7128 -0.1210 -0.0202 -0.0488 185 SER C CA  
4533  C C   . SER C 185 ? 1.7987 2.4026 1.7358 -0.1230 -0.0240 -0.0472 185 SER C C   
4534  O O   . SER C 185 ? 1.7802 2.4230 1.7187 -0.1061 -0.0210 -0.0314 185 SER C O   
4535  C CB  . SER C 185 ? 1.7943 2.3526 1.7518 -0.1339 -0.0218 -0.0173 185 SER C CB  
4536  O OG  . SER C 185 ? 1.8672 2.4213 1.8252 -0.1606 -0.0296 -0.0158 185 SER C OG  
4537  N N   . GLY C 186 ? 1.7498 2.3517 1.6835 -0.1431 -0.0300 -0.0600 186 GLY C N   
4538  C CA  . GLY C 186 ? 1.7199 2.3640 1.6528 -0.1479 -0.0328 -0.0576 186 GLY C CA  
4539  C C   . GLY C 186 ? 1.7329 2.3872 1.6751 -0.1676 -0.0371 -0.0353 186 GLY C C   
4540  O O   . GLY C 186 ? 1.7035 2.3934 1.6506 -0.1706 -0.0387 -0.0271 186 GLY C O   
4541  N N   . LEU C 187 ? 1.6865 2.3099 1.6318 -0.1804 -0.0388 -0.0252 187 LEU C N   
4542  C CA  . LEU C 187 ? 1.6614 2.2865 1.6103 -0.1991 -0.0429 -0.0072 187 LEU C CA  
4543  C C   . LEU C 187 ? 1.7126 2.3083 1.6578 -0.2183 -0.0443 -0.0168 187 LEU C C   
4544  O O   . LEU C 187 ? 1.7243 2.2898 1.6699 -0.2203 -0.0441 -0.0249 187 LEU C O   
4545  C CB  . LEU C 187 ? 1.6640 2.2879 1.6179 -0.1982 -0.0440 0.0165  187 LEU C CB  
4546  C CG  . LEU C 187 ? 1.7181 2.3791 1.6781 -0.1823 -0.0440 0.0359  187 LEU C CG  
4547  C CD1 . LEU C 187 ? 1.7763 2.4313 1.7403 -0.1666 -0.0392 0.0471  187 LEU C CD1 
4548  C CD2 . LEU C 187 ? 1.6992 2.3798 1.6634 -0.1967 -0.0514 0.0586  187 LEU C CD2 
4549  N N   . TYR C 188 ? 1.6542 2.2601 1.5983 -0.2313 -0.0453 -0.0134 188 TYR C N   
4550  C CA  . TYR C 188 ? 1.6543 2.2397 1.5944 -0.2474 -0.0450 -0.0184 188 TYR C CA  
4551  C C   . TYR C 188 ? 1.7217 2.2823 1.6592 -0.2574 -0.0467 -0.0078 188 TYR C C   
4552  O O   . TYR C 188 ? 1.7115 2.2767 1.6493 -0.2565 -0.0488 0.0063  188 TYR C O   
4553  C CB  . TYR C 188 ? 1.6484 2.2536 1.5893 -0.2549 -0.0429 -0.0141 188 TYR C CB  
4554  C CG  . TYR C 188 ? 1.6582 2.2973 1.6055 -0.2464 -0.0408 -0.0205 188 TYR C CG  
4555  C CD1 . TYR C 188 ? 1.6849 2.3280 1.6314 -0.2505 -0.0387 -0.0330 188 TYR C CD1 
4556  C CD2 . TYR C 188 ? 1.6537 2.3268 1.6094 -0.2353 -0.0417 -0.0109 188 TYR C CD2 
4557  C CE1 . TYR C 188 ? 1.6874 2.3687 1.6398 -0.2438 -0.0369 -0.0376 188 TYR C CE1 
4558  C CE2 . TYR C 188 ? 1.6525 2.3649 1.6161 -0.2266 -0.0395 -0.0144 188 TYR C CE2 
4559  C CZ  . TYR C 188 ? 1.7449 2.4621 1.7062 -0.2311 -0.0368 -0.0286 188 TYR C CZ  
4560  O OH  . TYR C 188 ? 1.7273 2.4898 1.6962 -0.2232 -0.0348 -0.0310 188 TYR C OH  
4561  N N   . SER C 189 ? 1.6975 2.2368 1.6335 -0.2671 -0.0464 -0.0123 189 SER C N   
4562  C CA  . SER C 189 ? 1.7016 2.2232 1.6363 -0.2760 -0.0476 -0.0017 189 SER C CA  
4563  C C   . SER C 189 ? 1.7566 2.2674 1.6882 -0.2864 -0.0461 -0.0031 189 SER C C   
4564  O O   . SER C 189 ? 1.7600 2.2653 1.6970 -0.2871 -0.0467 -0.0122 189 SER C O   
4565  C CB  . SER C 189 ? 1.7554 2.2636 1.7011 -0.2700 -0.0492 0.0011  189 SER C CB  
4566  O OG  . SER C 189 ? 1.8535 2.3517 1.8024 -0.2787 -0.0503 0.0135  189 SER C OG  
4567  N N   . LEU C 190 ? 1.7112 2.2197 1.6328 -0.2945 -0.0444 0.0067  190 LEU C N   
4568  C CA  . LEU C 190 ? 1.7124 2.2140 1.6299 -0.3013 -0.0411 0.0096  190 LEU C CA  
4569  C C   . LEU C 190 ? 1.7654 2.2599 1.6797 -0.3062 -0.0421 0.0217  190 LEU C C   
4570  O O   . LEU C 190 ? 1.7725 2.2685 1.6878 -0.3062 -0.0454 0.0283  190 LEU C O   
4571  C CB  . LEU C 190 ? 1.7043 2.2133 1.6110 -0.3033 -0.0343 0.0085  190 LEU C CB  
4572  C CG  . LEU C 190 ? 1.7586 2.2677 1.6508 -0.3055 -0.0321 0.0117  190 LEU C CG  
4573  C CD1 . LEU C 190 ? 1.7647 2.2622 1.6407 -0.3101 -0.0273 0.0173  190 LEU C CD1 
4574  C CD2 . LEU C 190 ? 1.7881 2.3091 1.6826 -0.3033 -0.0271 0.0084  190 LEU C CD2 
4575  N N   . SER C 191 ? 1.7006 2.1927 1.6124 -0.3099 -0.0389 0.0274  191 SER C N   
4576  C CA  . SER C 191 ? 1.6919 2.1842 1.6011 -0.3130 -0.0388 0.0407  191 SER C CA  
4577  C C   . SER C 191 ? 1.7206 2.2143 1.6095 -0.3135 -0.0305 0.0437  191 SER C C   
4578  O O   . SER C 191 ? 1.7050 2.1988 1.5911 -0.3120 -0.0248 0.0394  191 SER C O   
4579  C CB  . SER C 191 ? 1.7404 2.2305 1.6730 -0.3140 -0.0434 0.0489  191 SER C CB  
4580  O OG  . SER C 191 ? 1.8708 2.3564 1.8126 -0.3145 -0.0448 0.0406  191 SER C OG  
4581  N N   . SER C 192 ? 1.6844 2.1808 1.5587 -0.3147 -0.0288 0.0517  192 SER C N   
4582  C CA  . SER C 192 ? 1.6967 2.1919 1.5476 -0.3123 -0.0194 0.0536  192 SER C CA  
4583  C C   . SER C 192 ? 1.7827 2.2894 1.6296 -0.3114 -0.0192 0.0684  192 SER C C   
4584  O O   . SER C 192 ? 1.7960 2.3098 1.6393 -0.3152 -0.0245 0.0717  192 SER C O   
4585  C CB  . SER C 192 ? 1.7431 2.2275 1.5688 -0.3139 -0.0164 0.0412  192 SER C CB  
4586  O OG  . SER C 192 ? 1.8391 2.3152 1.6470 -0.3089 -0.0045 0.0385  192 SER C OG  
4587  N N   . VAL C 193 ? 1.7439 2.2583 1.5942 -0.3062 -0.0132 0.0808  193 VAL C N   
4588  C CA  . VAL C 193 ? 1.7499 2.2829 1.6006 -0.3029 -0.0125 0.0996  193 VAL C CA  
4589  C C   . VAL C 193 ? 1.8214 2.3571 1.6435 -0.2933 0.0009  0.1034  193 VAL C C   
4590  O O   . VAL C 193 ? 1.8184 2.3398 1.6264 -0.2892 0.0105  0.0941  193 VAL C O   
4591  C CB  . VAL C 193 ? 1.7842 2.3305 1.6733 -0.3046 -0.0202 0.1189  193 VAL C CB  
4592  C CG1 . VAL C 193 ? 1.7712 2.3122 1.6872 -0.3114 -0.0317 0.1152  193 VAL C CG1 
4593  C CG2 . VAL C 193 ? 1.7745 2.3182 1.6733 -0.3033 -0.0169 0.1234  193 VAL C CG2 
4594  N N   . VAL C 194 ? 1.7974 2.3544 1.6131 -0.2880 0.0027  0.1192  194 VAL C N   
4595  C CA  . VAL C 194 ? 1.8223 2.3862 1.6101 -0.2751 0.0165  0.1259  194 VAL C CA  
4596  C C   . VAL C 194 ? 1.8673 2.4676 1.6703 -0.2690 0.0147  0.1546  194 VAL C C   
4597  O O   . VAL C 194 ? 1.8500 2.4694 1.6601 -0.2735 0.0065  0.1609  194 VAL C O   
4598  C CB  . VAL C 194 ? 1.9113 2.4556 1.6521 -0.2723 0.0246  0.1032  194 VAL C CB  
4599  C CG1 . VAL C 194 ? 1.9208 2.4736 1.6502 -0.2816 0.0144  0.0968  194 VAL C CG1 
4600  C CG2 . VAL C 194 ? 1.9378 2.4846 1.6482 -0.2552 0.0417  0.1084  194 VAL C CG2 
4601  N N   . THR C 195 ? 2.2228 2.4124 1.9363 0.1770  -0.1429 -0.1728 195 THR C N   
4602  C CA  . THR C 195 ? 2.2492 2.4473 1.9786 0.1672  -0.1255 -0.1558 195 THR C CA  
4603  C C   . THR C 195 ? 2.3405 2.5478 2.0427 0.1693  -0.0917 -0.1593 195 THR C C   
4604  O O   . THR C 195 ? 2.3385 2.5664 2.0713 0.1731  -0.0693 -0.1640 195 THR C O   
4605  C CB  . THR C 195 ? 2.3372 2.5491 2.1360 0.1610  -0.1291 -0.1448 195 THR C CB  
4606  O OG1 . THR C 195 ? 2.3110 2.5051 2.1213 0.1623  -0.1649 -0.1462 195 THR C OG1 
4607  C CG2 . THR C 195 ? 2.3423 2.5636 2.1633 0.1469  -0.1144 -0.1226 195 THR C CG2 
4608  N N   . VAL C 196 ? 2.3281 2.5164 1.9710 0.1686  -0.0910 -0.1591 196 VAL C N   
4609  C CA  . VAL C 196 ? 2.3610 2.5450 1.9586 0.1712  -0.0648 -0.1630 196 VAL C CA  
4610  C C   . VAL C 196 ? 2.4515 2.6349 2.0351 0.1575  -0.0418 -0.1433 196 VAL C C   
4611  O O   . VAL C 196 ? 2.4502 2.6243 2.0394 0.1452  -0.0571 -0.1260 196 VAL C O   
4612  C CB  . VAL C 196 ? 2.4177 2.5756 1.9566 0.1785  -0.0808 -0.1752 196 VAL C CB  
4613  C CG1 . VAL C 196 ? 2.3859 2.5497 1.9353 0.1908  -0.0899 -0.1939 196 VAL C CG1 
4614  C CG2 . VAL C 196 ? 2.4132 2.5506 1.9355 0.1732  -0.1103 -0.1687 196 VAL C CG2 
4615  N N   . PRO C 197 ? 2.4438 2.6348 2.0058 0.1591  -0.0053 -0.1453 197 PRO C N   
4616  C CA  . PRO C 197 ? 2.4910 2.6808 2.0324 0.1433  0.0207  -0.1241 197 PRO C CA  
4617  C C   . PRO C 197 ? 2.5853 2.7320 2.0451 0.1359  0.0068  -0.1162 197 PRO C C   
4618  O O   . PRO C 197 ? 2.5772 2.6979 1.9889 0.1469  -0.0101 -0.1319 197 PRO C O   
4619  C CB  . PRO C 197 ? 2.5413 2.7540 2.0840 0.1510  0.0665  -0.1338 197 PRO C CB  
4620  C CG  . PRO C 197 ? 2.5808 2.7849 2.1039 0.1716  0.0566  -0.1614 197 PRO C CG  
4621  C CD  . PRO C 197 ? 2.4680 2.6669 2.0202 0.1753  0.0137  -0.1669 197 PRO C CD  
4622  N N   . SER C 198 ? 2.5899 2.7272 2.0371 0.1159  0.0117  -0.0905 198 SER C N   
4623  C CA  . SER C 198 ? 2.6470 2.7381 2.0175 0.1051  -0.0047 -0.0789 198 SER C CA  
4624  C C   . SER C 198 ? 2.7885 2.8572 2.0772 0.1074  0.0254  -0.0838 198 SER C C   
4625  O O   . SER C 198 ? 2.8397 2.8612 2.0536 0.1006  0.0084  -0.0776 198 SER C O   
4626  C CB  . SER C 198 ? 2.7116 2.7978 2.0965 0.0808  -0.0112 -0.0475 198 SER C CB  
4627  O OG  . SER C 198 ? 2.7622 2.8626 2.2169 0.0809  -0.0426 -0.0449 198 SER C OG  
4628  N N   . SER C 199 ? 2.7628 2.8613 2.0648 0.1182  0.0670  -0.0968 199 SER C N   
4629  C CA  . SER C 199 ? 2.8367 2.9164 2.0627 0.1246  0.1002  -0.1061 199 SER C CA  
4630  C C   . SER C 199 ? 2.9136 2.9519 2.0771 0.1423  0.0726  -0.1294 199 SER C C   
4631  O O   . SER C 199 ? 2.9839 2.9807 2.0580 0.1423  0.0810  -0.1309 199 SER C O   
4632  C CB  . SER C 199 ? 2.8763 3.0041 2.1486 0.1349  0.1493  -0.1177 199 SER C CB  
4633  O OG  . SER C 199 ? 2.9949 3.1582 2.3150 0.1163  0.1826  -0.0939 199 SER C OG  
4634  N N   . SER C 200 ? 2.8125 2.8600 2.0215 0.1562  0.0394  -0.1464 200 SER C N   
4635  C CA  . SER C 200 ? 2.8158 2.8308 1.9838 0.1719  0.0107  -0.1671 200 SER C CA  
4636  C C   . SER C 200 ? 2.8590 2.8426 2.0145 0.1664  -0.0377 -0.1619 200 SER C C   
4637  O O   . SER C 200 ? 2.9117 2.8463 1.9954 0.1627  -0.0546 -0.1587 200 SER C O   
4638  C CB  . SER C 200 ? 2.8023 2.8484 2.0255 0.1905  0.0101  -0.1898 200 SER C CB  
4639  O OG  . SER C 200 ? 2.9300 2.9443 2.1067 0.2051  -0.0083 -0.2087 200 SER C OG  
4640  N N   . LEU C 201 ? 2.7489 2.7585 1.9734 0.1665  -0.0605 -0.1620 201 LEU C N   
4641  C CA  . LEU C 201 ? 2.7264 2.7174 1.9572 0.1645  -0.1036 -0.1611 201 LEU C CA  
4642  C C   . LEU C 201 ? 2.7834 2.7461 1.9826 0.1769  -0.1304 -0.1786 201 LEU C C   
4643  O O   . LEU C 201 ? 2.7520 2.7290 1.9655 0.1898  -0.1247 -0.1948 201 LEU C O   
4644  C CB  . LEU C 201 ? 2.7679 2.7309 1.9713 0.1465  -0.1177 -0.1390 201 LEU C CB  
4645  C CG  . LEU C 201 ? 2.8263 2.8128 2.0631 0.1305  -0.0974 -0.1170 201 LEU C CG  
4646  C CD1 . LEU C 201 ? 2.8933 2.8402 2.0787 0.1107  -0.1079 -0.0935 201 LEU C CD1 
4647  C CD2 . LEU C 201 ? 2.7888 2.8062 2.1029 0.1324  -0.1154 -0.1178 201 LEU C CD2 
4648  N N   . GLY C 202 ? 2.7753 2.6969 1.9366 0.1720  -0.1621 -0.1743 202 GLY C N   
4649  C CA  . GLY C 202 ? 2.7839 2.6746 1.9224 0.1812  -0.1945 -0.1878 202 GLY C CA  
4650  C C   . GLY C 202 ? 2.8747 2.7390 1.9604 0.1910  -0.1878 -0.1994 202 GLY C C   
4651  O O   . GLY C 202 ? 2.8633 2.7128 1.9507 0.2005  -0.2145 -0.2124 202 GLY C O   
4652  N N   . THR C 203 ? 2.8768 2.7342 1.9161 0.1892  -0.1527 -0.1952 203 THR C N   
4653  C CA  . THR C 203 ? 2.9234 2.7538 1.9056 0.2011  -0.1423 -0.2089 203 THR C CA  
4654  C C   . THR C 203 ? 2.9060 2.7729 1.9430 0.2167  -0.1380 -0.2275 203 THR C C   
4655  O O   . THR C 203 ? 2.9229 2.7645 1.9373 0.2286  -0.1572 -0.2420 203 THR C O   
4656  C CB  . THR C 203 ? 3.0967 2.9183 2.0212 0.1958  -0.0990 -0.2009 203 THR C CB  
4657  O OG1 . THR C 203 ? 3.0428 2.9237 2.0320 0.1932  -0.0616 -0.1964 203 THR C OG1 
4658  C CG2 . THR C 203 ? 3.1578 2.9320 2.0122 0.1776  -0.1062 -0.1800 203 THR C CG2 
4659  N N   . GLN C 204 ? 2.7799 2.7019 1.8893 0.2155  -0.1177 -0.2258 204 GLN C N   
4660  C CA  . GLN C 204 ? 2.7104 2.6668 1.8760 0.2267  -0.1165 -0.2401 204 GLN C CA  
4661  C C   . GLN C 204 ? 2.6836 2.6507 1.8959 0.2251  -0.1503 -0.2410 204 GLN C C   
4662  O O   . GLN C 204 ? 2.6427 2.6216 1.8816 0.2158  -0.1586 -0.2305 204 GLN C O   
4663  C CB  . GLN C 204 ? 2.6886 2.6925 1.9082 0.2250  -0.0834 -0.2370 204 GLN C CB  
4664  C CG  . GLN C 204 ? 2.8043 2.8273 2.0490 0.2393  -0.0706 -0.2545 204 GLN C CG  
4665  C CD  . GLN C 204 ? 2.9366 2.9717 2.2264 0.2437  -0.0988 -0.2628 204 GLN C CD  
4666  O OE1 . GLN C 204 ? 2.8234 2.8891 2.1701 0.2379  -0.1030 -0.2575 204 GLN C OE1 
4667  N NE2 . GLN C 204 ? 2.8217 2.8304 2.0844 0.2533  -0.1195 -0.2751 204 GLN C NE2 
4668  N N   . THR C 205 ? 2.6242 2.5866 1.8461 0.2342  -0.1698 -0.2537 205 THR C N   
4669  C CA  . THR C 205 ? 2.5713 2.5475 1.8386 0.2325  -0.1972 -0.2552 205 THR C CA  
4670  C C   . THR C 205 ? 2.5385 2.5618 1.8690 0.2297  -0.1850 -0.2538 205 THR C C   
4671  O O   . THR C 205 ? 2.5263 2.5642 1.8753 0.2348  -0.1764 -0.2606 205 THR C O   
4672  C CB  . THR C 205 ? 2.7042 2.6560 1.9591 0.2405  -0.2230 -0.2659 205 THR C CB  
4673  O OG1 . THR C 205 ? 2.7719 2.6718 1.9573 0.2445  -0.2333 -0.2681 205 THR C OG1 
4674  C CG2 . THR C 205 ? 2.6402 2.6043 1.9402 0.2366  -0.2503 -0.2653 205 THR C CG2 
4675  N N   . TYR C 206 ? 2.4363 2.4780 1.7962 0.2221  -0.1874 -0.2456 206 TYR C N   
4676  C CA  . TYR C 206 ? 2.3684 2.4462 1.7790 0.2190  -0.1802 -0.2439 206 TYR C CA  
4677  C C   . TYR C 206 ? 2.3567 2.4479 1.7977 0.2182  -0.1988 -0.2478 206 TYR C C   
4678  O O   . TYR C 206 ? 2.3365 2.4288 1.7862 0.2161  -0.2102 -0.2463 206 TYR C O   
4679  C CB  . TYR C 206 ? 2.3729 2.4605 1.7947 0.2123  -0.1693 -0.2330 206 TYR C CB  
4680  C CG  . TYR C 206 ? 2.4138 2.5015 1.8230 0.2108  -0.1435 -0.2273 206 TYR C CG  
4681  C CD1 . TYR C 206 ? 2.4202 2.5304 1.8602 0.2138  -0.1263 -0.2307 206 TYR C CD1 
4682  C CD2 . TYR C 206 ? 2.4657 2.5318 1.8352 0.2054  -0.1361 -0.2178 206 TYR C CD2 
4683  C CE1 . TYR C 206 ? 2.4499 2.5669 1.8889 0.2133  -0.0991 -0.2269 206 TYR C CE1 
4684  C CE2 . TYR C 206 ? 2.5030 2.5744 1.8633 0.2026  -0.1065 -0.2113 206 TYR C CE2 
4685  C CZ  . TYR C 206 ? 2.5702 2.6704 1.9695 0.2074  -0.0863 -0.2168 206 TYR C CZ  
4686  O OH  . TYR C 206 ? 2.6028 2.7143 2.0028 0.2055  -0.0538 -0.2118 206 TYR C OH  
4687  N N   . ILE C 207 ? 2.2880 2.3894 1.7459 0.2197  -0.2015 -0.2530 207 ILE C N   
4688  C CA  . ILE C 207 ? 2.2558 2.3730 1.7421 0.2165  -0.2142 -0.2549 207 ILE C CA  
4689  C C   . ILE C 207 ? 2.2509 2.3936 1.7656 0.2114  -0.2055 -0.2520 207 ILE C C   
4690  O O   . ILE C 207 ? 2.2312 2.3773 1.7508 0.2109  -0.1968 -0.2508 207 ILE C O   
4691  C CB  . ILE C 207 ? 2.3083 2.4155 1.7926 0.2183  -0.2269 -0.2590 207 ILE C CB  
4692  C CG1 . ILE C 207 ? 2.3585 2.4296 1.8026 0.2255  -0.2370 -0.2633 207 ILE C CG1 
4693  C CG2 . ILE C 207 ? 2.2979 2.4219 1.8136 0.2123  -0.2394 -0.2579 207 ILE C CG2 
4694  C CD1 . ILE C 207 ? 2.4629 2.5163 1.8896 0.2320  -0.2408 -0.2699 207 ILE C CD1 
4695  N N   . CYS C 208 ? 2.1888 2.3469 1.7212 0.2085  -0.2090 -0.2522 208 CYS C N   
4696  C CA  . CYS C 208 ? 2.1683 2.3437 1.7164 0.2040  -0.2028 -0.2504 208 CYS C CA  
4697  C C   . CYS C 208 ? 2.2142 2.4052 1.7768 0.1978  -0.2051 -0.2507 208 CYS C C   
4698  O O   . CYS C 208 ? 2.2112 2.4156 1.7863 0.1981  -0.2061 -0.2543 208 CYS C O   
4699  C CB  . CYS C 208 ? 2.1676 2.3456 1.7178 0.2067  -0.2024 -0.2515 208 CYS C CB  
4700  S SG  . CYS C 208 ? 2.2056 2.3945 1.7635 0.2037  -0.1985 -0.2514 208 CYS C SG  
4701  N N   . ASN C 209 ? 2.1655 2.3550 1.7292 0.1918  -0.2065 -0.2467 209 ASN C N   
4702  C CA  . ASN C 209 ? 2.1601 2.3612 1.7344 0.1817  -0.2093 -0.2425 209 ASN C CA  
4703  C C   . ASN C 209 ? 2.2017 2.4126 1.7728 0.1743  -0.2014 -0.2394 209 ASN C C   
4704  O O   . ASN C 209 ? 2.1964 2.3957 1.7585 0.1717  -0.2033 -0.2363 209 ASN C O   
4705  C CB  . ASN C 209 ? 2.1786 2.3666 1.7526 0.1778  -0.2207 -0.2391 209 ASN C CB  
4706  C CG  . ASN C 209 ? 2.5122 2.6826 2.0782 0.1875  -0.2290 -0.2446 209 ASN C CG  
4707  O OD1 . ASN C 209 ? 2.4345 2.5938 1.9861 0.1968  -0.2230 -0.2492 209 ASN C OD1 
4708  N ND2 . ASN C 209 ? 2.4335 2.5985 2.0063 0.1849  -0.2435 -0.2433 209 ASN C ND2 
4709  N N   . VAL C 210 ? 2.1626 2.3933 1.7410 0.1717  -0.1930 -0.2412 210 VAL C N   
4710  C CA  . VAL C 210 ? 2.1748 2.4132 1.7407 0.1658  -0.1826 -0.2403 210 VAL C CA  
4711  C C   . VAL C 210 ? 2.2451 2.5026 1.8194 0.1519  -0.1753 -0.2332 210 VAL C C   
4712  O O   . VAL C 210 ? 2.2378 2.5143 1.8395 0.1521  -0.1737 -0.2346 210 VAL C O   
4713  C CB  . VAL C 210 ? 2.2240 2.4699 1.7882 0.1774  -0.1749 -0.2516 210 VAL C CB  
4714  C CG1 . VAL C 210 ? 2.2423 2.4875 1.7822 0.1738  -0.1656 -0.2528 210 VAL C CG1 
4715  C CG2 . VAL C 210 ? 2.2129 2.4409 1.7743 0.1882  -0.1840 -0.2549 210 VAL C CG2 
4716  N N   . ASN C 211 ? 2.2232 2.4736 1.7748 0.1383  -0.1727 -0.2242 211 ASN C N   
4717  C CA  . ASN C 211 ? 2.2396 2.5067 1.7939 0.1207  -0.1636 -0.2134 211 ASN C CA  
4718  C C   . ASN C 211 ? 2.3263 2.5917 1.8436 0.1114  -0.1484 -0.2104 211 ASN C C   
4719  O O   . ASN C 211 ? 2.3378 2.5736 1.8212 0.1116  -0.1575 -0.2098 211 ASN C O   
4720  C CB  . ASN C 211 ? 2.2540 2.5068 1.8151 0.1072  -0.1827 -0.1996 211 ASN C CB  
4721  C CG  . ASN C 211 ? 2.6403 2.8587 2.1742 0.1017  -0.1999 -0.1937 211 ASN C CG  
4722  O OD1 . ASN C 211 ? 2.5917 2.7919 2.1286 0.1137  -0.2128 -0.2004 211 ASN C OD1 
4723  N ND2 . ASN C 211 ? 2.5713 2.7793 2.0797 0.0826  -0.2009 -0.1805 211 ASN C ND2 
4724  N N   . HIS C 212 ? 2.2983 2.5945 1.8225 0.1035  -0.1252 -0.2089 212 HIS C N   
4725  C CA  . HIS C 212 ? 2.3380 2.6348 1.8201 0.0934  -0.1046 -0.2062 212 HIS C CA  
4726  C C   . HIS C 212 ? 2.4131 2.7096 1.8872 0.0656  -0.1043 -0.1834 212 HIS C C   
4727  O O   . HIS C 212 ? 2.3981 2.7258 1.9143 0.0564  -0.0970 -0.1757 212 HIS C O   
4728  C CB  . HIS C 212 ? 2.3508 2.6871 1.8503 0.1046  -0.0743 -0.2219 212 HIS C CB  
4729  C CG  . HIS C 212 ? 2.4422 2.7732 1.8884 0.1039  -0.0521 -0.2278 212 HIS C CG  
4730  N ND1 . HIS C 212 ? 2.5120 2.8506 1.9278 0.0817  -0.0303 -0.2136 212 HIS C ND1 
4731  C CD2 . HIS C 212 ? 2.4774 2.7947 1.8945 0.1231  -0.0490 -0.2468 212 HIS C CD2 
4732  C CE1 . HIS C 212 ? 2.5495 2.8764 1.9120 0.0889  -0.0132 -0.2255 212 HIS C CE1 
4733  N NE2 . HIS C 212 ? 2.5344 2.8474 1.8973 0.1147  -0.0257 -0.2464 212 HIS C NE2 
4734  N N   . LYS C 213 ? 2.4042 2.6614 1.8283 0.0513  -0.1181 -0.1711 213 LYS C N   
4735  C CA  . LYS C 213 ? 2.4354 2.6828 1.8454 0.0222  -0.1247 -0.1469 213 LYS C CA  
4736  C C   . LYS C 213 ? 2.5315 2.8096 1.9253 0.0037  -0.0880 -0.1371 213 LYS C C   
4737  O O   . LYS C 213 ? 2.5236 2.8288 1.9547 -0.0134 -0.0827 -0.1217 213 LYS C O   
4738  C CB  . LYS C 213 ? 2.4967 2.6879 1.8597 0.0121  -0.1557 -0.1370 213 LYS C CB  
4739  C CG  . LYS C 213 ? 2.6190 2.7873 2.0117 0.0255  -0.1903 -0.1428 213 LYS C CG  
4740  C CD  . LYS C 213 ? 2.7411 2.9004 2.1584 0.0097  -0.2156 -0.1269 213 LYS C CD  
4741  C CE  . LYS C 213 ? 2.8073 2.9446 2.2508 0.0255  -0.2460 -0.1364 213 LYS C CE  
4742  N NZ  . LYS C 213 ? 2.9023 3.0246 2.3650 0.0121  -0.2748 -0.1236 213 LYS C NZ  
4743  N N   . PRO C 214 ? 2.5368 2.8136 1.8799 0.0073  -0.0612 -0.1461 214 PRO C N   
4744  C CA  . PRO C 214 ? 2.5839 2.8944 1.9119 -0.0104 -0.0201 -0.1375 214 PRO C CA  
4745  C C   . PRO C 214 ? 2.6043 2.9821 2.0092 -0.0039 0.0091  -0.1448 214 PRO C C   
4746  O O   . PRO C 214 ? 2.6071 3.0123 2.0450 -0.0273 0.0183  -0.1244 214 PRO C O   
4747  C CB  . PRO C 214 ? 2.6570 2.9453 1.9111 0.0000  -0.0015 -0.1525 214 PRO C CB  
4748  C CG  . PRO C 214 ? 2.7031 2.9330 1.9246 0.0114  -0.0424 -0.1579 214 PRO C CG  
4749  C CD  . PRO C 214 ? 2.5706 2.8124 1.8645 0.0261  -0.0678 -0.1634 214 PRO C CD  
4750  N N   . SER C 215 ? 2.5214 2.9235 1.9597 0.0264  0.0191  -0.1727 215 SER C N   
4751  C CA  . SER C 215 ? 2.4917 2.9544 2.0083 0.0356  0.0420  -0.1832 215 SER C CA  
4752  C C   . SER C 215 ? 2.4981 2.9727 2.0881 0.0321  0.0145  -0.1733 215 SER C C   
4753  O O   . SER C 215 ? 2.4727 2.9942 2.1332 0.0352  0.0278  -0.1776 215 SER C O   
4754  C CB  . SER C 215 ? 2.5265 3.0025 2.0542 0.0691  0.0527  -0.2162 215 SER C CB  
4755  O OG  . SER C 215 ? 2.5749 3.0222 2.1151 0.0892  0.0163  -0.2272 215 SER C OG  
4756  N N   . ASN C 216 ? 2.4438 2.8739 2.0178 0.0270  -0.0252 -0.1616 216 ASN C N   
4757  C CA  . ASN C 216 ? 2.4036 2.8289 2.0285 0.0258  -0.0578 -0.1538 216 ASN C CA  
4758  C C   . ASN C 216 ? 2.4254 2.8640 2.1000 0.0536  -0.0674 -0.1759 216 ASN C C   
4759  O O   . ASN C 216 ? 2.3968 2.8324 2.1130 0.0549  -0.0924 -0.1720 216 ASN C O   
4760  C CB  . ASN C 216 ? 2.3983 2.8487 2.0629 -0.0023 -0.0552 -0.1287 216 ASN C CB  
4761  C CG  . ASN C 216 ? 2.5826 2.9938 2.2084 -0.0282 -0.0792 -0.1031 216 ASN C CG  
4762  O OD1 . ASN C 216 ? 2.4418 2.8099 2.0510 -0.0222 -0.1157 -0.1037 216 ASN C OD1 
4763  N ND2 . ASN C 216 ? 2.5025 2.9282 2.1157 -0.0583 -0.0595 -0.0799 216 ASN C ND2 
4764  N N   . THR C 217 ? 2.3890 2.8341 2.0521 0.0758  -0.0524 -0.1988 217 THR C N   
4765  C CA  . THR C 217 ? 2.3539 2.8051 2.0544 0.1013  -0.0632 -0.2196 217 THR C CA  
4766  C C   . THR C 217 ? 2.3907 2.7955 2.0659 0.1115  -0.0965 -0.2212 217 THR C C   
4767  O O   . THR C 217 ? 2.3912 2.7710 2.0249 0.1221  -0.0990 -0.2296 217 THR C O   
4768  C CB  . THR C 217 ? 2.4511 2.9235 2.1474 0.1198  -0.0375 -0.2427 217 THR C CB  
4769  O OG1 . THR C 217 ? 2.4792 2.9938 2.1882 0.1082  -0.0003 -0.2402 217 THR C OG1 
4770  C CG2 . THR C 217 ? 2.3930 2.8760 2.1381 0.1434  -0.0498 -0.2631 217 THR C CG2 
4771  N N   . LYS C 218 ? 2.0688 2.2848 2.0519 -0.2456 -0.2973 0.1126  218 LYS C N   
4772  C CA  . LYS C 218 ? 2.0656 2.2482 2.0472 -0.2422 -0.3058 0.1012  218 LYS C CA  
4773  C C   . LYS C 218 ? 2.1305 2.3111 2.1207 -0.2288 -0.2974 0.0981  218 LYS C C   
4774  O O   . LYS C 218 ? 2.1151 2.2984 2.1137 -0.2294 -0.3057 0.1069  218 LYS C O   
4775  C CB  . LYS C 218 ? 2.0868 2.2581 2.0679 -0.2561 -0.3326 0.1064  218 LYS C CB  
4776  C CG  . LYS C 218 ? 2.1406 2.3117 2.1128 -0.2738 -0.3457 0.1096  218 LYS C CG  
4777  C CD  . LYS C 218 ? 2.1920 2.3439 2.1620 -0.2864 -0.3789 0.1079  218 LYS C CD  
4778  C CE  . LYS C 218 ? 2.2470 2.3942 2.2071 -0.3074 -0.3958 0.1097  218 LYS C CE  
4779  N NZ  . LYS C 218 ? 2.3268 2.4452 2.2743 -0.3057 -0.3851 0.0897  218 LYS C NZ  
4780  N N   . VAL C 219 ? 2.1047 2.2780 2.0925 -0.2167 -0.2839 0.0866  219 VAL C N   
4781  C CA  . VAL C 219 ? 2.1061 2.2760 2.1001 -0.2063 -0.2778 0.0823  219 VAL C CA  
4782  C C   . VAL C 219 ? 2.1542 2.3006 2.1457 -0.2037 -0.2812 0.0743  219 VAL C C   
4783  O O   . VAL C 219 ? 2.1511 2.2851 2.1380 -0.2004 -0.2786 0.0667  219 VAL C O   
4784  C CB  . VAL C 219 ? 2.1651 2.3480 2.1602 -0.1951 -0.2671 0.0767  219 VAL C CB  
4785  C CG1 . VAL C 219 ? 2.1587 2.3348 2.1600 -0.1881 -0.2665 0.0714  219 VAL C CG1 
4786  C CG2 . VAL C 219 ? 2.1685 2.3836 2.1668 -0.1961 -0.2623 0.0840  219 VAL C CG2 
4787  N N   . ASP C 220 ? 2.1080 2.2495 2.1031 -0.2038 -0.2877 0.0772  220 ASP C N   
4788  C CA  . ASP C 220 ? 2.1040 2.2322 2.0969 -0.2001 -0.2904 0.0710  220 ASP C CA  
4789  C C   . ASP C 220 ? 2.1502 2.2776 2.1470 -0.1943 -0.2834 0.0705  220 ASP C C   
4790  O O   . ASP C 220 ? 2.1480 2.2767 2.1493 -0.1933 -0.2844 0.0755  220 ASP C O   
4791  C CB  . ASP C 220 ? 2.1280 2.2516 2.1192 -0.2014 -0.3066 0.0732  220 ASP C CB  
4792  C CG  . ASP C 220 ? 2.2487 2.3658 2.2359 -0.1954 -0.3105 0.0650  220 ASP C CG  
4793  O OD1 . ASP C 220 ? 2.2603 2.3749 2.2452 -0.1914 -0.3264 0.0651  220 ASP C OD1 
4794  O OD2 . ASP C 220 ? 2.3111 2.4276 2.2979 -0.1935 -0.3000 0.0593  220 ASP C OD2 
4795  N N   . LYS C 221 ? 2.1002 2.2235 2.0962 -0.1917 -0.2788 0.0654  221 LYS C N   
4796  C CA  . LYS C 221 ? 2.0943 2.2160 2.0932 -0.1897 -0.2769 0.0653  221 LYS C CA  
4797  C C   . LYS C 221 ? 2.1510 2.2711 2.1482 -0.1899 -0.2771 0.0649  221 LYS C C   
4798  O O   . LYS C 221 ? 2.1405 2.2604 2.1373 -0.1900 -0.2767 0.0632  221 LYS C O   
4799  C CB  . LYS C 221 ? 2.1163 2.2406 2.1182 -0.1870 -0.2766 0.0626  221 LYS C CB  
4800  C CG  . LYS C 221 ? 2.1605 2.2933 2.1660 -0.1854 -0.2756 0.0620  221 LYS C CG  
4801  C CD  . LYS C 221 ? 2.1879 2.3255 2.1956 -0.1792 -0.2799 0.0552  221 LYS C CD  
4802  C CE  . LYS C 221 ? 2.1703 2.2997 2.1817 -0.1810 -0.2882 0.0513  221 LYS C CE  
4803  N NZ  . LYS C 221 ? 2.1895 2.3233 2.2028 -0.1737 -0.2999 0.0423  221 LYS C NZ  
4804  N N   . ARG C 222 ? 2.1226 2.2416 2.1191 -0.1901 -0.2779 0.0670  222 ARG C N   
4805  C CA  . ARG C 222 ? 2.1305 2.2555 2.1249 -0.1907 -0.2771 0.0688  222 ARG C CA  
4806  C C   . ARG C 222 ? 2.1992 2.3260 2.1983 -0.1961 -0.2793 0.0725  222 ARG C C   
4807  O O   . ARG C 222 ? 2.1940 2.3137 2.1958 -0.1983 -0.2845 0.0716  222 ARG C O   
4808  C CB  . ARG C 222 ? 2.1445 2.2658 2.1335 -0.1879 -0.2785 0.0702  222 ARG C CB  
4809  C CG  . ARG C 222 ? 2.2565 2.3917 2.2403 -0.1854 -0.2767 0.0714  222 ARG C CG  
4810  C CD  . ARG C 222 ? 2.2830 2.4115 2.2595 -0.1822 -0.2783 0.0735  222 ARG C CD  
4811  N NE  . ARG C 222 ? 2.2438 2.3683 2.2218 -0.1931 -0.2783 0.0780  222 ARG C NE  
4812  C CZ  . ARG C 222 ? 2.3047 2.4458 2.2803 -0.1990 -0.2766 0.0839  222 ARG C CZ  
4813  N NH1 . ARG C 222 ? 2.1222 2.2887 2.0946 -0.1930 -0.2714 0.0851  222 ARG C NH1 
4814  N NH2 . ARG C 222 ? 2.0498 2.1845 2.0268 -0.2117 -0.2824 0.0885  222 ARG C NH2 
4815  N N   . VAL C 223 ? 2.1715 2.3084 2.1730 -0.1980 -0.2789 0.0768  223 VAL C N   
4816  C CA  . VAL C 223 ? 2.1789 2.3185 2.1869 -0.2040 -0.2867 0.0847  223 VAL C CA  
4817  C C   . VAL C 223 ? 2.2560 2.4047 2.2617 -0.2117 -0.2889 0.0912  223 VAL C C   
4818  O O   . VAL C 223 ? 2.2543 2.4188 2.2560 -0.2110 -0.2814 0.0936  223 VAL C O   
4819  C CB  . VAL C 223 ? 2.2265 2.3707 2.2410 -0.2031 -0.2873 0.0897  223 VAL C CB  
4820  C CG1 . VAL C 223 ? 2.2263 2.3713 2.2497 -0.2088 -0.3017 0.1021  223 VAL C CG1 
4821  C CG2 . VAL C 223 ? 2.2220 2.3512 2.2358 -0.1961 -0.2856 0.0819  223 VAL C CG2 
4822  N N   . GLU C 224 ? 2.2315 2.3703 2.2384 -0.2186 -0.3008 0.0924  224 GLU C N   
4823  C CA  . GLU C 224 ? 2.2424 2.3835 2.2456 -0.2292 -0.3063 0.0978  224 GLU C CA  
4824  C C   . GLU C 224 ? 2.3074 2.4576 2.3180 -0.2420 -0.3239 0.1111  224 GLU C C   
4825  O O   . GLU C 224 ? 2.3082 2.4486 2.3259 -0.2420 -0.3411 0.1109  224 GLU C O   
4826  C CB  . GLU C 224 ? 2.2616 2.3797 2.2600 -0.2304 -0.3106 0.0881  224 GLU C CB  
4827  C CG  . GLU C 224 ? 2.3915 2.4951 2.3957 -0.2301 -0.3249 0.0798  224 GLU C CG  
4828  C CD  . GLU C 224 ? 2.6278 2.7290 2.6339 -0.2175 -0.3163 0.0712  224 GLU C CD  
4829  O OE1 . GLU C 224 ? 2.6389 2.7285 2.6444 -0.2150 -0.3145 0.0630  224 GLU C OE1 
4830  O OE2 . GLU C 224 ? 2.4780 2.5883 2.4867 -0.2112 -0.3123 0.0735  224 GLU C OE2 
4831  N N   . PRO C 225 ? 2.2625 2.4334 2.2717 -0.2522 -0.3228 0.1238  225 PRO C N   
4832  C CA  . PRO C 225 ? 2.2838 2.4661 2.3020 -0.2672 -0.3437 0.1409  225 PRO C CA  
4833  C C   . PRO C 225 ? 2.2685 2.4342 2.2834 -0.2824 -0.3665 0.1403  225 PRO C C   
4834  O O   . PRO C 225 ? 1.6320 1.7747 1.6498 -0.2807 -0.3850 0.1304  225 PRO C O   
4835  C CB  . PRO C 225 ? 2.3058 2.5245 2.3240 -0.2720 -0.3306 0.1555  225 PRO C CB  
4836  C CG  . PRO C 225 ? 2.3535 2.5762 2.3594 -0.2579 -0.3058 0.1422  225 PRO C CG  
4837  C CD  . PRO C 225 ? 2.2905 2.4786 2.2898 -0.2495 -0.3055 0.1246  225 PRO C CD  
4838  N N   . GLU D 1   ? 1.9001 2.1519 1.2036 0.0495  0.0145  -0.0579 1   GLU D N   
4839  C CA  . GLU D 1   ? 1.9041 2.1140 1.2140 0.0172  0.0444  -0.0544 1   GLU D CA  
4840  C C   . GLU D 1   ? 1.9351 2.1309 1.2755 0.0140  0.0435  -0.0662 1   GLU D C   
4841  O O   . GLU D 1   ? 1.9309 2.1265 1.2804 0.0173  0.0209  -0.0826 1   GLU D O   
4842  C CB  . GLU D 1   ? 1.9295 2.1105 1.2126 -0.0130 0.0501  -0.0581 1   GLU D CB  
4843  C CG  . GLU D 1   ? 2.0568 2.2503 1.3096 -0.0167 0.0581  -0.0500 1   GLU D CG  
4844  C CD  . GLU D 1   ? 2.2464 2.4201 1.4731 -0.0430 0.0669  -0.0574 1   GLU D CD  
4845  O OE1 . GLU D 1   ? 2.1632 2.3147 1.4002 -0.0668 0.0933  -0.0567 1   GLU D OE1 
4846  O OE2 . GLU D 1   ? 2.1140 2.2986 1.3092 -0.0373 0.0474  -0.0649 1   GLU D OE2 
4847  N N   . ILE D 2   ? 1.8777 2.0612 1.2338 0.0070  0.0687  -0.0586 2   ILE D N   
4848  C CA  . ILE D 2   ? 1.8700 2.0420 1.2520 0.0020  0.0714  -0.0692 2   ILE D CA  
4849  C C   . ILE D 2   ? 1.9081 2.0382 1.2856 -0.0348 0.0808  -0.0719 2   ILE D C   
4850  O O   . ILE D 2   ? 1.9100 2.0197 1.2857 -0.0544 0.1050  -0.0625 2   ILE D O   
4851  C CB  . ILE D 2   ? 1.9107 2.0924 1.3055 0.0154  0.0937  -0.0594 2   ILE D CB  
4852  C CG1 . ILE D 2   ? 1.9154 2.1441 1.3120 0.0571  0.0888  -0.0518 2   ILE D CG1 
4853  C CG2 . ILE D 2   ? 1.9148 2.0905 1.3325 0.0117  0.0946  -0.0735 2   ILE D CG2 
4854  C CD1 . ILE D 2   ? 2.0373 2.2690 1.4147 0.0604  0.1060  -0.0285 2   ILE D CD1 
4855  N N   . VAL D 3   ? 1.8441 1.9642 1.2200 -0.0416 0.0619  -0.0843 3   VAL D N   
4856  C CA  . VAL D 3   ? 1.8362 1.9225 1.2064 -0.0699 0.0689  -0.0857 3   VAL D CA  
4857  C C   . VAL D 3   ? 1.8500 1.9167 1.2431 -0.0877 0.0848  -0.0860 3   VAL D C   
4858  O O   . VAL D 3   ? 1.8463 1.9154 1.2643 -0.0830 0.0765  -0.0972 3   VAL D O   
4859  C CB  . VAL D 3   ? 1.8983 1.9776 1.2635 -0.0675 0.0462  -0.0974 3   VAL D CB  
4860  C CG1 . VAL D 3   ? 1.9068 1.9526 1.2690 -0.0922 0.0570  -0.0963 3   VAL D CG1 
4861  C CG2 . VAL D 3   ? 1.8967 1.9951 1.2304 -0.0522 0.0309  -0.0960 3   VAL D CG2 
4862  N N   . LEU D 4   ? 1.7772 1.8287 1.1630 -0.1076 0.1072  -0.0757 4   LEU D N   
4863  C CA  . LEU D 4   ? 1.7599 1.7950 1.1633 -0.1257 0.1218  -0.0743 4   LEU D CA  
4864  C C   . LEU D 4   ? 1.8192 1.8352 1.2219 -0.1434 0.1215  -0.0760 4   LEU D C   
4865  O O   . LEU D 4   ? 1.8222 1.8367 1.2048 -0.1493 0.1268  -0.0725 4   LEU D O   
4866  C CB  . LEU D 4   ? 1.7480 1.7817 1.1479 -0.1346 0.1459  -0.0633 4   LEU D CB  
4867  C CG  . LEU D 4   ? 1.7920 1.8392 1.1945 -0.1169 0.1540  -0.0572 4   LEU D CG  
4868  C CD1 . LEU D 4   ? 1.7917 1.8312 1.1912 -0.1283 0.1795  -0.0466 4   LEU D CD1 
4869  C CD2 . LEU D 4   ? 1.8080 1.8594 1.2282 -0.1082 0.1508  -0.0631 4   LEU D CD2 
4870  N N   . THR D 5   ? 1.7773 1.7819 1.2020 -0.1496 0.1160  -0.0821 5   THR D N   
4871  C CA  . THR D 5   ? 1.7863 1.7720 1.2145 -0.1636 0.1181  -0.0807 5   THR D CA  
4872  C C   . THR D 5   ? 1.8580 1.8364 1.3064 -0.1803 0.1313  -0.0761 5   THR D C   
4873  O O   . THR D 5   ? 1.8451 1.8221 1.3161 -0.1820 0.1270  -0.0826 5   THR D O   
4874  C CB  . THR D 5   ? 1.8870 1.8636 1.3233 -0.1560 0.1000  -0.0908 5   THR D CB  
4875  O OG1 . THR D 5   ? 1.9220 1.9127 1.3784 -0.1429 0.0863  -0.1042 5   THR D OG1 
4876  C CG2 . THR D 5   ? 1.8527 1.8310 1.2590 -0.1450 0.0905  -0.0906 5   THR D CG2 
4877  N N   . GLN D 6   ? 1.8455 1.8253 1.2859 -0.1911 0.1472  -0.0668 6   GLN D N   
4878  C CA  . GLN D 6   ? 1.8523 1.8320 1.3097 -0.2052 0.1591  -0.0610 6   GLN D CA  
4879  C C   . GLN D 6   ? 1.9567 1.9246 1.4306 -0.2132 0.1589  -0.0575 6   GLN D C   
4880  O O   . GLN D 6   ? 1.9687 1.9287 1.4340 -0.2099 0.1585  -0.0547 6   GLN D O   
4881  C CB  . GLN D 6   ? 1.8536 1.8469 1.3022 -0.2110 0.1754  -0.0558 6   GLN D CB  
4882  C CG  . GLN D 6   ? 1.9394 1.9393 1.3879 -0.2100 0.1823  -0.0563 6   GLN D CG  
4883  C CD  . GLN D 6   ? 2.1399 2.1526 1.5872 -0.2175 0.1993  -0.0550 6   GLN D CD  
4884  O OE1 . GLN D 6   ? 2.0466 2.0668 1.4798 -0.2143 0.2055  -0.0577 6   GLN D OE1 
4885  N NE2 . GLN D 6   ? 2.0939 2.1127 1.5582 -0.2274 0.2069  -0.0527 6   GLN D NE2 
4886  N N   . SER D 7   ? 1.9345 1.9018 1.4306 -0.2228 0.1606  -0.0565 7   SER D N   
4887  C CA  . SER D 7   ? 1.9472 1.9050 1.4645 -0.2320 0.1627  -0.0511 7   SER D CA  
4888  C C   . SER D 7   ? 1.9714 1.9439 1.5006 -0.2423 0.1723  -0.0425 7   SER D C   
4889  O O   . SER D 7   ? 1.9558 1.9375 1.4856 -0.2445 0.1714  -0.0467 7   SER D O   
4890  C CB  . SER D 7   ? 2.0253 1.9710 1.5634 -0.2331 0.1512  -0.0631 7   SER D CB  
4891  O OG  . SER D 7   ? 2.2027 2.1316 1.7606 -0.2404 0.1542  -0.0578 7   SER D OG  
4892  N N   . PRO D 8   ? 1.9147 1.8930 1.4520 -0.2456 0.1818  -0.0299 8   PRO D N   
4893  C CA  . PRO D 8   ? 1.9238 1.8931 1.4577 -0.2394 0.1876  -0.0216 8   PRO D CA  
4894  C C   . PRO D 8   ? 1.9615 1.9450 1.4684 -0.2284 0.1945  -0.0218 8   PRO D C   
4895  O O   . PRO D 8   ? 1.9516 1.9464 1.4451 -0.2275 0.1934  -0.0299 8   PRO D O   
4896  C CB  . PRO D 8   ? 1.9413 1.9210 1.4982 -0.2447 0.1971  -0.0068 8   PRO D CB  
4897  C CG  . PRO D 8   ? 1.9711 1.9787 1.5316 -0.2494 0.1984  -0.0076 8   PRO D CG  
4898  C CD  . PRO D 8   ? 1.9131 1.9128 1.4640 -0.2526 0.1882  -0.0221 8   PRO D CD  
4899  N N   . GLY D 9   ? 1.9131 1.8968 1.4120 -0.2191 0.2033  -0.0133 9   GLY D N   
4900  C CA  . GLY D 9   ? 1.8951 1.8992 1.3667 -0.2067 0.2117  -0.0158 9   GLY D CA  
4901  C C   . GLY D 9   ? 1.8876 1.9316 1.3683 -0.2062 0.2243  -0.0147 9   GLY D C   
4902  O O   . GLY D 9   ? 1.8634 1.9298 1.3309 -0.2040 0.2285  -0.0257 9   GLY D O   
4903  N N   . THR D 10  ? 1.8160 1.8714 1.3230 -0.2084 0.2302  -0.0024 10  THR D N   
4904  C CA  . THR D 10  ? 1.7766 1.8758 1.3007 -0.2058 0.2398  -0.0007 10  THR D CA  
4905  C C   . THR D 10  ? 1.8057 1.9050 1.3601 -0.2159 0.2354  0.0104  10  THR D C   
4906  O O   . THR D 10  ? 1.8132 1.8873 1.3779 -0.2191 0.2335  0.0220  10  THR D O   
4907  C CB  . THR D 10  ? 1.8576 1.9915 1.3750 -0.1849 0.2562  0.0046  10  THR D CB  
4908  O OG1 . THR D 10  ? 1.9159 2.0220 1.4228 -0.1756 0.2600  0.0181  10  THR D OG1 
4909  C CG2 . THR D 10  ? 1.8059 1.9680 1.3004 -0.1762 0.2629  -0.0137 10  THR D CG2 
4910  N N   . LEU D 11  ? 1.7359 1.8640 1.3053 -0.2213 0.2341  0.0057  11  LEU D N   
4911  C CA  . LEU D 11  ? 1.7242 1.8608 1.3187 -0.2298 0.2282  0.0146  11  LEU D CA  
4912  C C   . LEU D 11  ? 1.7696 1.9597 1.3852 -0.2172 0.2369  0.0227  11  LEU D C   
4913  O O   . LEU D 11  ? 1.7581 1.9852 1.3760 -0.2107 0.2417  0.0106  11  LEU D O   
4914  C CB  . LEU D 11  ? 1.7120 1.8409 1.3052 -0.2433 0.2178  0.0028  11  LEU D CB  
4915  C CG  . LEU D 11  ? 1.7837 1.8740 1.3724 -0.2550 0.2061  0.0004  11  LEU D CG  
4916  C CD1 . LEU D 11  ? 1.7810 1.8680 1.3608 -0.2610 0.2006  -0.0113 11  LEU D CD1 
4917  C CD2 . LEU D 11  ? 1.8052 1.8955 1.4146 -0.2615 0.2017  0.0119  11  LEU D CD2 
4918  N N   . SER D 12  ? 1.7175 1.9155 1.3518 -0.2123 0.2400  0.0423  12  SER D N   
4919  C CA  . SER D 12  ? 1.6830 1.9389 1.3408 -0.1958 0.2475  0.0531  12  SER D CA  
4920  C C   . SER D 12  ? 1.7153 1.9857 1.3948 -0.2075 0.2343  0.0577  12  SER D C   
4921  O O   . SER D 12  ? 1.7359 1.9827 1.4241 -0.2175 0.2295  0.0711  12  SER D O   
4922  C CB  . SER D 12  ? 1.7332 1.9927 1.3967 -0.1780 0.2624  0.0755  12  SER D CB  
4923  O OG  . SER D 12  ? 1.8322 2.0776 1.4694 -0.1657 0.2737  0.0703  12  SER D OG  
4924  N N   . LEU D 13  ? 1.6305 1.9378 1.3179 -0.2074 0.2282  0.0441  13  LEU D N   
4925  C CA  . LEU D 13  ? 1.6060 1.9291 1.3079 -0.2172 0.2137  0.0455  13  LEU D CA  
4926  C C   . LEU D 13  ? 1.6169 2.0118 1.3453 -0.2010 0.2129  0.0438  13  LEU D C   
4927  O O   . LEU D 13  ? 1.6004 2.0301 1.3340 -0.1869 0.2225  0.0304  13  LEU D O   
4928  C CB  . LEU D 13  ? 1.6112 1.8984 1.2937 -0.2354 0.2036  0.0277  13  LEU D CB  
4929  C CG  . LEU D 13  ? 1.6965 1.9233 1.3581 -0.2501 0.1995  0.0270  13  LEU D CG  
4930  C CD1 . LEU D 13  ? 1.7000 1.8968 1.3381 -0.2548 0.2012  0.0097  13  LEU D CD1 
4931  C CD2 . LEU D 13  ? 1.7342 1.9523 1.3985 -0.2627 0.1862  0.0307  13  LEU D CD2 
4932  N N   . SER D 14  ? 1.5537 1.9758 1.3004 -0.2020 0.2007  0.0552  14  SER D N   
4933  C CA  . SER D 14  ? 1.5109 2.0074 1.2865 -0.1853 0.1953  0.0535  14  SER D CA  
4934  C C   . SER D 14  ? 1.5294 2.0278 1.3016 -0.1968 0.1830  0.0309  14  SER D C   
4935  O O   . SER D 14  ? 1.5390 1.9902 1.2898 -0.2166 0.1732  0.0285  14  SER D O   
4936  C CB  . SER D 14  ? 1.5643 2.0906 1.3598 -0.1801 0.1864  0.0779  14  SER D CB  
4937  O OG  . SER D 14  ? 1.7300 2.2717 1.5383 -0.1618 0.2018  0.1009  14  SER D OG  
4938  N N   . PRO D 15  ? 1.4547 2.0078 1.2489 -0.1834 0.1851  0.0127  15  PRO D N   
4939  C CA  . PRO D 15  ? 1.4450 1.9948 1.2388 -0.1946 0.1763  -0.0087 15  PRO D CA  
4940  C C   . PRO D 15  ? 1.4892 2.0411 1.2808 -0.2029 0.1552  -0.0007 15  PRO D C   
4941  O O   . PRO D 15  ? 1.4638 2.0775 1.2818 -0.1893 0.1434  0.0039  15  PRO D O   
4942  C CB  . PRO D 15  ? 1.4347 2.0556 1.2636 -0.1755 0.1831  -0.0298 15  PRO D CB  
4943  C CG  . PRO D 15  ? 1.4901 2.1375 1.3250 -0.1559 0.1997  -0.0238 15  PRO D CG  
4944  C CD  . PRO D 15  ? 1.4513 2.0742 1.2734 -0.1556 0.1972  0.0084  15  PRO D CD  
4945  N N   . GLY D 16  ? 1.4706 1.9589 1.2291 -0.2227 0.1505  0.0004  16  GLY D N   
4946  C CA  . GLY D 16  ? 1.4739 1.9559 1.2191 -0.2316 0.1320  0.0059  16  GLY D CA  
4947  C C   . GLY D 16  ? 1.5802 2.0017 1.2933 -0.2473 0.1313  0.0145  16  GLY D C   
4948  O O   . GLY D 16  ? 1.5848 1.9864 1.2750 -0.2566 0.1202  0.0115  16  GLY D O   
4949  N N   . GLU D 17  ? 1.5726 1.9671 1.2838 -0.2485 0.1438  0.0228  17  GLU D N   
4950  C CA  . GLU D 17  ? 1.6094 1.9500 1.2982 -0.2620 0.1448  0.0273  17  GLU D CA  
4951  C C   . GLU D 17  ? 1.7047 1.9953 1.3634 -0.2706 0.1489  0.0108  17  GLU D C   
4952  O O   . GLU D 17  ? 1.6993 1.9916 1.3551 -0.2674 0.1540  -0.0014 17  GLU D O   
4953  C CB  . GLU D 17  ? 1.6388 1.9683 1.3387 -0.2582 0.1574  0.0406  17  GLU D CB  
4954  C CG  . GLU D 17  ? 1.7417 2.1039 1.4659 -0.2527 0.1548  0.0624  17  GLU D CG  
4955  C CD  . GLU D 17  ? 1.9584 2.3015 1.6921 -0.2487 0.1700  0.0779  17  GLU D CD  
4956  O OE1 . GLU D 17  ? 1.9476 2.2633 1.6833 -0.2604 0.1694  0.0869  17  GLU D OE1 
4957  O OE2 . GLU D 17  ? 1.7633 2.1206 1.5031 -0.2331 0.1836  0.0798  17  GLU D OE2 
4958  N N   . GLY D 18  ? 1.6960 1.9466 1.3362 -0.2799 0.1476  0.0101  18  GLY D N   
4959  C CA  . GLY D 18  ? 1.7197 1.9287 1.3322 -0.2835 0.1514  -0.0034 18  GLY D CA  
4960  C C   . GLY D 18  ? 1.7997 1.9753 1.4083 -0.2835 0.1618  -0.0052 18  GLY D C   
4961  O O   . GLY D 18  ? 1.8058 1.9678 1.4208 -0.2875 0.1612  0.0000  18  GLY D O   
4962  N N   . ALA D 19  ? 1.7698 1.9320 1.3690 -0.2790 0.1714  -0.0132 19  ALA D N   
4963  C CA  . ALA D 19  ? 1.7849 1.9189 1.3763 -0.2770 0.1796  -0.0160 19  ALA D CA  
4964  C C   . ALA D 19  ? 1.8380 1.9390 1.4072 -0.2773 0.1774  -0.0249 19  ALA D C   
4965  O O   . ALA D 19  ? 1.8282 1.9260 1.3823 -0.2752 0.1768  -0.0309 19  ALA D O   
4966  C CB  . ALA D 19  ? 1.7877 1.9300 1.3808 -0.2716 0.1912  -0.0212 19  ALA D CB  
4967  N N   . THR D 20  ? 1.8089 1.8887 1.3770 -0.2771 0.1768  -0.0263 20  THR D N   
4968  C CA  . THR D 20  ? 1.8270 1.8841 1.3800 -0.2733 0.1737  -0.0370 20  THR D CA  
4969  C C   . THR D 20  ? 1.8817 1.9215 1.4320 -0.2681 0.1774  -0.0382 20  THR D C   
4970  O O   . THR D 20  ? 1.8829 1.9167 1.4453 -0.2708 0.1762  -0.0340 20  THR D O   
4971  C CB  . THR D 20  ? 1.9744 2.0318 1.5347 -0.2790 0.1644  -0.0424 20  THR D CB  
4972  O OG1 . THR D 20  ? 1.9925 2.0707 1.5520 -0.2834 0.1600  -0.0399 20  THR D OG1 
4973  C CG2 . THR D 20  ? 1.9706 2.0167 1.5187 -0.2710 0.1610  -0.0586 20  THR D CG2 
4974  N N   . LEU D 21  ? 1.8373 1.8694 1.3711 -0.2598 0.1827  -0.0428 21  LEU D N   
4975  C CA  . LEU D 21  ? 1.8454 1.8659 1.3722 -0.2536 0.1848  -0.0441 21  LEU D CA  
4976  C C   . LEU D 21  ? 1.9353 1.9438 1.4508 -0.2428 0.1791  -0.0534 21  LEU D C   
4977  O O   . LEU D 21  ? 1.9382 1.9486 1.4425 -0.2346 0.1819  -0.0570 21  LEU D O   
4978  C CB  . LEU D 21  ? 1.8348 1.8634 1.3556 -0.2522 0.1965  -0.0420 21  LEU D CB  
4979  C CG  . LEU D 21  ? 1.8754 1.9264 1.4112 -0.2579 0.2024  -0.0368 21  LEU D CG  
4980  C CD1 . LEU D 21  ? 1.8625 1.9287 1.4050 -0.2616 0.2067  -0.0377 21  LEU D CD1 
4981  C CD2 . LEU D 21  ? 1.9100 1.9696 1.4414 -0.2539 0.2112  -0.0389 21  LEU D CD2 
4982  N N   . SER D 22  ? 1.9162 1.9149 1.4354 -0.2399 0.1717  -0.0573 22  SER D N   
4983  C CA  . SER D 22  ? 1.9309 1.9256 1.4455 -0.2268 0.1630  -0.0687 22  SER D CA  
4984  C C   . SER D 22  ? 1.9720 1.9639 1.4704 -0.2160 0.1636  -0.0674 22  SER D C   
4985  O O   . SER D 22  ? 1.9693 1.9579 1.4624 -0.2205 0.1679  -0.0608 22  SER D O   
4986  C CB  . SER D 22  ? 2.0046 1.9923 1.5388 -0.2305 0.1527  -0.0776 22  SER D CB  
4987  O OG  . SER D 22  ? 2.1550 2.1476 1.7054 -0.2411 0.1519  -0.0806 22  SER D OG  
4988  N N   . CYS D 23  ? 1.9163 1.9146 1.4065 -0.1993 0.1593  -0.0745 23  CYS D N   
4989  C CA  . CYS D 23  ? 1.9111 1.9119 1.3859 -0.1859 0.1577  -0.0734 23  CYS D CA  
4990  C C   . CYS D 23  ? 1.9680 1.9814 1.4471 -0.1655 0.1443  -0.0861 23  CYS D C   
4991  O O   . CYS D 23  ? 1.9642 1.9922 1.4398 -0.1500 0.1482  -0.0882 23  CYS D O   
4992  C CB  . CYS D 23  ? 1.9082 1.9121 1.3690 -0.1837 0.1735  -0.0639 23  CYS D CB  
4993  S SG  . CYS D 23  ? 1.9602 1.9713 1.4026 -0.1666 0.1736  -0.0609 23  CYS D SG  
4994  N N   . ARG D 24  ? 1.9295 1.9400 1.4181 -0.1633 0.1295  -0.0956 24  ARG D N   
4995  C CA  . ARG D 24  ? 1.9286 1.9576 1.4283 -0.1428 0.1141  -0.1124 24  ARG D CA  
4996  C C   . ARG D 24  ? 1.9846 2.0260 1.4687 -0.1230 0.1055  -0.1107 24  ARG D C   
4997  O O   . ARG D 24  ? 1.9831 2.0124 1.4560 -0.1279 0.1001  -0.1064 24  ARG D O   
4998  C CB  . ARG D 24  ? 1.9347 1.9559 1.4616 -0.1512 0.1026  -0.1280 24  ARG D CB  
4999  C CG  . ARG D 24  ? 2.0614 2.0893 1.6088 -0.1587 0.1064  -0.1389 24  ARG D CG  
5000  C CD  . ARG D 24  ? 2.2016 2.2132 1.7779 -0.1762 0.1019  -0.1488 24  ARG D CD  
5001  N NE  . ARG D 24  ? 2.2650 2.2716 1.8502 -0.1949 0.1121  -0.1448 24  ARG D NE  
5002  C CZ  . ARG D 24  ? 2.3937 2.3817 1.9722 -0.2130 0.1226  -0.1244 24  ARG D CZ  
5003  N NH1 . ARG D 24  ? 2.2261 2.1989 1.7886 -0.2148 0.1262  -0.1082 24  ARG D NH1 
5004  N NH2 . ARG D 24  ? 2.1881 2.1780 1.7757 -0.2273 0.1290  -0.1216 24  ARG D NH2 
5005  N N   . ALA D 25  ? 1.9455 2.0142 1.4266 -0.0982 0.1050  -0.1134 25  ALA D N   
5006  C CA  . ALA D 25  ? 1.9447 2.0340 1.4125 -0.0745 0.0973  -0.1100 25  ALA D CA  
5007  C C   . ALA D 25  ? 2.0026 2.1137 1.4863 -0.0557 0.0724  -0.1292 25  ALA D C   
5008  O O   . ALA D 25  ? 1.9999 2.1221 1.5105 -0.0522 0.0642  -0.1494 25  ALA D O   
5009  C CB  . ALA D 25  ? 1.9507 2.0628 1.4113 -0.0522 0.1106  -0.1018 25  ALA D CB  
5010  N N   . SER D 26  ? 1.9228 1.8166 1.3324 -0.1416 -0.0336 0.0549  26  SER D N   
5011  C CA  . SER D 26  ? 1.9464 1.8266 1.3206 -0.1097 -0.0847 0.0514  26  SER D CA  
5012  C C   . SER D 26  ? 2.0199 1.8805 1.4038 -0.0902 -0.0876 0.0767  26  SER D C   
5013  O O   . SER D 26  ? 2.0215 1.8465 1.3869 -0.0768 -0.1336 0.0955  26  SER D O   
5014  C CB  . SER D 26  ? 1.9833 1.8968 1.3411 -0.0884 -0.0839 0.0205  26  SER D CB  
5015  O OG  . SER D 26  ? 2.0957 2.0076 1.4199 -0.0503 -0.1335 0.0134  26  SER D OG  
5016  N N   . GLN D 27  ? 1.9914 1.8680 1.4029 -0.0911 -0.0418 0.0783  27  GLN D N   
5017  C CA  . GLN D 27  ? 1.9991 1.8485 1.4227 -0.0777 -0.0359 0.0964  27  GLN D CA  
5018  C C   . GLN D 27  ? 2.0497 1.8969 1.5099 -0.1076 0.0088  0.1025  27  GLN D C   
5019  O O   . GLN D 27  ? 2.0379 1.9143 1.5128 -0.1320 0.0351  0.0930  27  GLN D O   
5020  C CB  . GLN D 27  ? 2.0191 1.8871 1.4303 -0.0476 -0.0361 0.0862  27  GLN D CB  
5021  C CG  . GLN D 27  ? 2.1323 2.0590 1.5490 -0.0581 -0.0014 0.0640  27  GLN D CG  
5022  C CD  . GLN D 27  ? 2.3522 2.3170 1.7386 -0.0282 -0.0276 0.0428  27  GLN D CD  
5023  O OE1 . GLN D 27  ? 2.3130 2.3069 1.6931 -0.0082 -0.0233 0.0376  27  GLN D OE1 
5024  N NE2 . GLN D 27  ? 2.2248 2.1924 1.5899 -0.0257 -0.0578 0.0267  27  GLN D NE2 
5025  N N   . SER D 28  ? 2.0087 1.8162 1.4813 -0.1034 0.0123  0.1162  28  SER D N   
5026  C CA  . SER D 28  ? 1.9915 1.7919 1.4938 -0.1293 0.0444  0.1153  28  SER D CA  
5027  C C   . SER D 28  ? 2.0391 1.8718 1.5496 -0.1412 0.0752  0.0985  28  SER D C   
5028  O O   . SER D 28  ? 2.0387 1.8745 1.5370 -0.1270 0.0752  0.0942  28  SER D O   
5029  C CB  . SER D 28  ? 2.0366 1.7751 1.5460 -0.1206 0.0348  0.1290  28  SER D CB  
5030  O OG  . SER D 28  ? 2.1369 1.8685 1.6720 -0.1461 0.0578  0.1221  28  SER D OG  
5031  N N   . VAL D 29  ? 1.9870 1.8473 1.5160 -0.1666 0.0970  0.0910  29  VAL D N   
5032  C CA  . VAL D 29  ? 1.9732 1.8630 1.5087 -0.1813 0.1176  0.0797  29  VAL D CA  
5033  C C   . VAL D 29  ? 2.0113 1.8838 1.5659 -0.2012 0.1241  0.0744  29  VAL D C   
5034  O O   . VAL D 29  ? 2.0109 1.8680 1.5783 -0.2053 0.1204  0.0770  29  VAL D O   
5035  C CB  . VAL D 29  ? 2.0112 1.9488 1.5461 -0.1866 0.1283  0.0743  29  VAL D CB  
5036  C CG1 . VAL D 29  ? 2.0054 1.9736 1.5344 -0.1909 0.1389  0.0693  29  VAL D CG1 
5037  C CG2 . VAL D 29  ? 2.0173 1.9610 1.5353 -0.1716 0.1137  0.0734  29  VAL D CG2 
5038  N N   . ASP D 30  ? 1.9540 1.8318 1.5074 -0.2146 0.1284  0.0654  30  ASP D N   
5039  C CA  . ASP D 30  ? 1.9409 1.8016 1.5049 -0.2333 0.1235  0.0532  30  ASP D CA  
5040  C C   . ASP D 30  ? 1.9505 1.8470 1.5310 -0.2396 0.1266  0.0508  30  ASP D C   
5041  O O   . ASP D 30  ? 1.9326 1.8669 1.5132 -0.2363 0.1349  0.0575  30  ASP D O   
5042  C CB  . ASP D 30  ? 1.9735 1.8337 1.5237 -0.2494 0.1167  0.0455  30  ASP D CB  
5043  C CG  . ASP D 30  ? 2.1410 1.9613 1.6905 -0.2688 0.0981  0.0265  30  ASP D CG  
5044  O OD1 . ASP D 30  ? 2.1634 1.9604 1.7270 -0.2674 0.0935  0.0161  30  ASP D OD1 
5045  O OD2 . ASP D 30  ? 2.2001 2.0133 1.7326 -0.2872 0.0846  0.0201  30  ASP D OD2 
5046  N N   . SER D 31  ? 1.8930 1.7763 1.4872 -0.2462 0.1191  0.0396  31  SER D N   
5047  C CA  . SER D 31  ? 1.8717 1.7933 1.4824 -0.2488 0.1191  0.0348  31  SER D CA  
5048  C C   . SER D 31  ? 1.8816 1.8308 1.4884 -0.2532 0.1102  0.0307  31  SER D C   
5049  O O   . SER D 31  ? 1.8665 1.8511 1.4808 -0.2469 0.1167  0.0385  31  SER D O   
5050  C CB  . SER D 31  ? 1.9309 1.8376 1.5544 -0.2536 0.1085  0.0180  31  SER D CB  
5051  O OG  . SER D 31  ? 2.0812 1.9502 1.6951 -0.2633 0.0889  -0.0036 31  SER D OG  
5052  N N   . SER D 32  ? 1.8188 1.7456 1.4108 -0.2647 0.0915  0.0206  32  SER D N   
5053  C CA  . SER D 32  ? 1.7996 1.7456 1.3811 -0.2722 0.0711  0.0205  32  SER D CA  
5054  C C   . SER D 32  ? 1.7992 1.7736 1.3744 -0.2681 0.0855  0.0425  32  SER D C   
5055  O O   . SER D 32  ? 1.7966 1.7910 1.3666 -0.2703 0.0694  0.0499  32  SER D O   
5056  C CB  . SER D 32  ? 1.8695 1.7785 1.4306 -0.2922 0.0405  0.0037  32  SER D CB  
5057  O OG  . SER D 32  ? 2.0317 1.9036 1.5814 -0.2988 0.0516  0.0049  32  SER D OG  
5058  N N   . SER D 33  ? 1.7112 1.6865 1.2853 -0.2599 0.1106  0.0522  33  SER D N   
5059  C CA  . SER D 33  ? 1.6849 1.6883 1.2525 -0.2542 0.1240  0.0663  33  SER D CA  
5060  C C   . SER D 33  ? 1.6719 1.6929 1.2529 -0.2404 0.1381  0.0716  33  SER D C   
5061  O O   . SER D 33  ? 1.6624 1.7008 1.2396 -0.2350 0.1466  0.0796  33  SER D O   
5062  C CB  . SER D 33  ? 1.7399 1.7386 1.2940 -0.2496 0.1352  0.0680  33  SER D CB  
5063  O OG  . SER D 33  ? 1.8213 1.8097 1.3798 -0.2339 0.1454  0.0673  33  SER D OG  
5064  N N   . LEU D 34  ? 1.5906 1.6063 1.1864 -0.2364 0.1396  0.0662  34  LEU D N   
5065  C CA  . LEU D 34  ? 1.5643 1.5917 1.1710 -0.2277 0.1514  0.0697  34  LEU D CA  
5066  C C   . LEU D 34  ? 1.5781 1.6219 1.1969 -0.2216 0.1444  0.0724  34  LEU D C   
5067  O O   . LEU D 34  ? 1.5652 1.6149 1.1888 -0.2228 0.1249  0.0664  34  LEU D O   
5068  C CB  . LEU D 34  ? 1.5659 1.5857 1.1797 -0.2294 0.1547  0.0663  34  LEU D CB  
5069  C CG  . LEU D 34  ? 1.6375 1.6357 1.2374 -0.2278 0.1553  0.0687  34  LEU D CG  
5070  C CD1 . LEU D 34  ? 1.6463 1.6268 1.2526 -0.2318 0.1481  0.0682  34  LEU D CD1 
5071  C CD2 . LEU D 34  ? 1.6623 1.6618 1.2520 -0.2229 0.1590  0.0714  34  LEU D CD2 
5072  N N   . ALA D 35  ? 1.5213 1.5673 1.1429 -0.2126 0.1558  0.0793  35  ALA D N   
5073  C CA  . ALA D 35  ? 1.5060 1.5594 1.1389 -0.2000 0.1490  0.0855  35  ALA D CA  
5074  C C   . ALA D 35  ? 1.5768 1.6225 1.2169 -0.1936 0.1660  0.0859  35  ALA D C   
5075  O O   . ALA D 35  ? 1.5797 1.6088 1.2095 -0.1989 0.1793  0.0822  35  ALA D O   
5076  C CB  . ALA D 35  ? 1.5101 1.5599 1.1349 -0.1947 0.1371  0.0985  35  ALA D CB  
5077  N N   . TRP D 36  ? 1.5433 1.6000 1.1980 -0.1816 0.1607  0.0880  36  TRP D N   
5078  C CA  . TRP D 36  ? 1.5479 1.5948 1.2094 -0.1765 0.1743  0.0884  36  TRP D CA  
5079  C C   . TRP D 36  ? 1.5907 1.6170 1.2575 -0.1533 0.1691  0.1000  36  TRP D C   
5080  O O   . TRP D 36  ? 1.5812 1.6219 1.2545 -0.1358 0.1464  0.1081  36  TRP D O   
5081  C CB  . TRP D 36  ? 1.5346 1.6163 1.2098 -0.1798 0.1731  0.0825  36  TRP D CB  
5082  C CG  . TRP D 36  ? 1.5649 1.6555 1.2350 -0.2032 0.1804  0.0763  36  TRP D CG  
5083  C CD1 . TRP D 36  ? 1.6074 1.7237 1.2824 -0.2119 0.1730  0.0709  36  TRP D CD1 
5084  C CD2 . TRP D 36  ? 1.5772 1.6470 1.2346 -0.2203 0.1895  0.0756  36  TRP D CD2 
5085  N NE1 . TRP D 36  ? 1.6192 1.7321 1.2871 -0.2314 0.1782  0.0724  36  TRP D NE1 
5086  C CE2 . TRP D 36  ? 1.6435 1.7294 1.2981 -0.2376 0.1846  0.0754  36  TRP D CE2 
5087  C CE3 . TRP D 36  ? 1.5961 1.6286 1.2411 -0.2230 0.1958  0.0734  36  TRP D CE3 
5088  C CZ2 . TRP D 36  ? 1.6515 1.7218 1.2892 -0.2574 0.1803  0.0773  36  TRP D CZ2 
5089  C CZ3 . TRP D 36  ? 1.6331 1.6485 1.2594 -0.2447 0.1911  0.0688  36  TRP D CZ3 
5090  C CH2 . TRP D 36  ? 1.6546 1.6907 1.2762 -0.2616 0.1808  0.0729  36  TRP D CH2 
5091  N N   . TYR D 37  ? 1.5470 1.5336 1.2085 -0.1517 0.1845  0.0998  37  TYR D N   
5092  C CA  . TYR D 37  ? 1.5372 1.4872 1.2032 -0.1283 0.1823  0.1118  37  TYR D CA  
5093  C C   . TYR D 37  ? 1.5902 1.5099 1.2619 -0.1234 0.1948  0.1065  37  TYR D C   
5094  O O   . TYR D 37  ? 1.6050 1.5193 1.2684 -0.1460 0.2070  0.0914  37  TYR D O   
5095  C CB  . TYR D 37  ? 1.5657 1.4838 1.2185 -0.1298 0.1881  0.1139  37  TYR D CB  
5096  C CG  . TYR D 37  ? 1.6239 1.5723 1.2684 -0.1374 0.1760  0.1213  37  TYR D CG  
5097  C CD1 . TYR D 37  ? 1.6488 1.5975 1.2936 -0.1241 0.1547  0.1431  37  TYR D CD1 
5098  C CD2 . TYR D 37  ? 1.6597 1.6316 1.2931 -0.1585 0.1820  0.1082  37  TYR D CD2 
5099  C CE1 . TYR D 37  ? 1.6808 1.6571 1.3139 -0.1377 0.1408  0.1502  37  TYR D CE1 
5100  C CE2 . TYR D 37  ? 1.6816 1.6779 1.3060 -0.1671 0.1715  0.1142  37  TYR D CE2 
5101  C CZ  . TYR D 37  ? 1.7861 1.7863 1.4095 -0.1597 0.1516  0.1342  37  TYR D CZ  
5102  O OH  . TYR D 37  ? 1.8295 1.8542 1.4401 -0.1746 0.1385  0.1401  37  TYR D OH  
5103  N N   . GLN D 38  ? 1.5201 1.4161 1.2033 -0.0938 0.1866  0.1204  38  GLN D N   
5104  C CA  . GLN D 38  ? 1.5033 1.3614 1.1921 -0.0853 0.1974  0.1170  38  GLN D CA  
5105  C C   . GLN D 38  ? 1.5263 1.3068 1.2129 -0.0637 0.1995  0.1257  38  GLN D C   
5106  O O   . GLN D 38  ? 1.5045 1.2765 1.1980 -0.0342 0.1804  0.1485  38  GLN D O   
5107  C CB  . GLN D 38  ? 1.5039 1.4047 1.2105 -0.0625 0.1838  0.1250  38  GLN D CB  
5108  C CG  . GLN D 38  ? 1.6521 1.5193 1.3648 -0.0533 0.1951  0.1227  38  GLN D CG  
5109  C CD  . GLN D 38  ? 1.8363 1.7296 1.5668 -0.0113 0.1752  0.1366  38  GLN D CD  
5110  O OE1 . GLN D 38  ? 1.8265 1.7145 1.5620 0.0257  0.1473  0.1549  38  GLN D OE1 
5111  N NE2 . GLN D 38  ? 1.6250 1.5451 1.3629 -0.0146 0.1844  0.1293  38  GLN D NE2 
5112  N N   . GLN D 39  ? 1.4828 1.2024 1.1569 -0.0792 0.2172  0.1070  39  GLN D N   
5113  C CA  . GLN D 39  ? 1.4735 1.1080 1.1451 -0.0600 0.2211  0.1095  39  GLN D CA  
5114  C C   . GLN D 39  ? 1.5464 1.1180 1.2213 -0.0517 0.2287  0.1025  39  GLN D C   
5115  O O   . GLN D 39  ? 1.5736 1.1384 1.2362 -0.0819 0.2376  0.0790  39  GLN D O   
5116  C CB  . GLN D 39  ? 1.5000 1.1036 1.1508 -0.0813 0.2301  0.0871  39  GLN D CB  
5117  C CG  . GLN D 39  ? 1.5396 1.0579 1.1891 -0.0602 0.2333  0.0884  39  GLN D CG  
5118  C CD  . GLN D 39  ? 1.7718 1.2967 1.4081 -0.0687 0.2350  0.0794  39  GLN D CD  
5119  O OE1 . GLN D 39  ? 1.7473 1.3269 1.3701 -0.0928 0.2353  0.0635  39  GLN D OE1 
5120  N NE2 . GLN D 39  ? 1.6536 1.1235 1.2937 -0.0468 0.2347  0.0903  39  GLN D NE2 
5121  N N   . LYS D 40  ? 1.7797 1.6538 1.5564 -0.2320 0.1125  0.1258  40  LYS D N   
5122  C CA  . LYS D 40  ? 1.8361 1.6576 1.5553 -0.2434 0.0864  0.1304  40  LYS D CA  
5123  C C   . LYS D 40  ? 1.9072 1.7150 1.6686 -0.2489 0.0485  0.1474  40  LYS D C   
5124  O O   . LYS D 40  ? 1.8649 1.6992 1.6966 -0.2434 0.0436  0.1538  40  LYS D O   
5125  C CB  . LYS D 40  ? 1.9011 1.6889 1.5642 -0.2492 0.0816  0.1253  40  LYS D CB  
5126  C CG  . LYS D 40  ? 1.9917 1.7726 1.6021 -0.2484 0.1162  0.1114  40  LYS D CG  
5127  C CD  . LYS D 40  ? 2.0704 1.8407 1.6572 -0.2501 0.1244  0.1064  40  LYS D CD  
5128  C CE  . LYS D 40  ? 2.1120 1.8689 1.6546 -0.2510 0.1596  0.0951  40  LYS D CE  
5129  N NZ  . LYS D 40  ? 2.2675 1.9504 1.7276 -0.2658 0.1562  0.0934  40  LYS D NZ  
5130  N N   . PRO D 41  ? 1.9260 1.6909 1.6512 -0.2600 0.0219  0.1559  41  PRO D N   
5131  C CA  . PRO D 41  ? 1.9381 1.6911 1.7146 -0.2663 -0.0180 0.1755  41  PRO D CA  
5132  C C   . PRO D 41  ? 2.0074 1.7455 1.8077 -0.2703 -0.0513 0.1849  41  PRO D C   
5133  O O   . PRO D 41  ? 2.0467 1.7454 1.7807 -0.2789 -0.0654 0.1814  41  PRO D O   
5134  C CB  . PRO D 41  ? 2.0227 1.7233 1.7348 -0.2794 -0.0411 0.1811  41  PRO D CB  
5135  C CG  . PRO D 41  ? 2.0831 1.7820 1.7305 -0.2756 -0.0019 0.1627  41  PRO D CG  
5136  C CD  . PRO D 41  ? 2.0002 1.7214 1.6390 -0.2679 0.0269  0.1487  41  PRO D CD  
5137  N N   . GLY D 42  ? 1.9315 1.6992 1.8279 -0.2645 -0.0594 0.1961  42  GLY D N   
5138  C CA  . GLY D 42  ? 1.9347 1.6950 1.8752 -0.2657 -0.0891 0.2056  42  GLY D CA  
5139  C C   . GLY D 42  ? 1.9564 1.7356 1.8826 -0.2569 -0.0653 0.1904  42  GLY D C   
5140  O O   . GLY D 42  ? 1.9740 1.7293 1.8827 -0.2621 -0.0899 0.1930  42  GLY D O   
5141  N N   . GLN D 43  ? 1.8712 1.6915 1.8028 -0.2448 -0.0181 0.1752  43  GLN D N   
5142  C CA  . GLN D 43  ? 1.8435 1.6873 1.7650 -0.2355 0.0094  0.1605  43  GLN D CA  
5143  C C   . GLN D 43  ? 1.8311 1.7214 1.8110 -0.2227 0.0475  0.1536  43  GLN D C   
5144  O O   . GLN D 43  ? 1.8186 1.7225 1.8145 -0.2222 0.0644  0.1545  43  GLN D O   
5145  C CB  . GLN D 43  ? 1.8857 1.7150 1.7169 -0.2393 0.0280  0.1474  43  GLN D CB  
5146  C CG  . GLN D 43  ? 2.2778 2.0552 2.0401 -0.2524 0.0014  0.1496  43  GLN D CG  
5147  C CD  . GLN D 43  ? 2.6289 2.3882 2.3108 -0.2562 0.0288  0.1364  43  GLN D CD  
5148  O OE1 . GLN D 43  ? 2.5671 2.3608 2.2561 -0.2464 0.0643  0.1250  43  GLN D OE1 
5149  N NE2 . GLN D 43  ? 2.5862 2.2851 2.1903 -0.2718 0.0129  0.1385  43  GLN D NE2 
5150  N N   . ALA D 44  ? 1.7440 1.6542 1.7491 -0.2138 0.0622  0.1462  44  ALA D N   
5151  C CA  . ALA D 44  ? 1.6839 1.6278 1.7308 -0.2038 0.0987  0.1383  44  ALA D CA  
5152  C C   . ALA D 44  ? 1.6904 1.6515 1.6835 -0.2029 0.1291  0.1261  44  ALA D C   
5153  O O   . ALA D 44  ? 1.7137 1.6636 1.6461 -0.2066 0.1256  0.1214  44  ALA D O   
5154  C CB  . ALA D 44  ? 1.6751 1.6282 1.7527 -0.1952 0.1031  0.1332  44  ALA D CB  
5155  N N   . PRO D 45  ? 1.5827 1.5657 1.5960 -0.1998 0.1592  0.1216  45  PRO D N   
5156  C CA  . PRO D 45  ? 1.5629 1.5606 1.5297 -0.2003 0.1826  0.1122  45  PRO D CA  
5157  C C   . PRO D 45  ? 1.5976 1.6061 1.5350 -0.1962 0.1920  0.1030  45  PRO D C   
5158  O O   . PRO D 45  ? 1.5754 1.5860 1.5317 -0.1911 0.1880  0.1014  45  PRO D O   
5159  C CB  . PRO D 45  ? 1.5594 1.5713 1.5574 -0.2005 0.2088  0.1115  45  PRO D CB  
5160  C CG  . PRO D 45  ? 1.6168 1.6168 1.6738 -0.2018 0.2005  0.1219  45  PRO D CG  
5161  C CD  . PRO D 45  ? 1.5747 1.5632 1.6520 -0.1980 0.1744  0.1257  45  PRO D CD  
5162  N N   . ARG D 46  ? 1.5628 1.5777 1.4584 -0.1983 0.2054  0.0975  46  ARG D N   
5163  C CA  . ARG D 46  ? 1.5532 1.5786 1.4252 -0.1959 0.2169  0.0909  46  ARG D CA  
5164  C C   . ARG D 46  ? 1.5597 1.6073 1.4321 -0.1959 0.2389  0.0872  46  ARG D C   
5165  O O   . ARG D 46  ? 1.5477 1.5957 1.4130 -0.1999 0.2449  0.0882  46  ARG D O   
5166  C CB  . ARG D 46  ? 1.5980 1.5998 1.4207 -0.2010 0.2116  0.0900  46  ARG D CB  
5167  C CG  . ARG D 46  ? 1.7511 1.7531 1.5563 -0.1999 0.2197  0.0861  46  ARG D CG  
5168  C CD  . ARG D 46  ? 1.9553 1.9217 1.7298 -0.2055 0.2023  0.0882  46  ARG D CD  
5169  N NE  . ARG D 46  ? 2.1745 2.1011 1.9009 -0.2151 0.1947  0.0899  46  ARG D NE  
5170  C CZ  . ARG D 46  ? 2.4505 2.3511 2.1304 -0.2214 0.2105  0.0859  46  ARG D CZ  
5171  N NH1 . ARG D 46  ? 2.3573 2.2717 2.0400 -0.2192 0.2341  0.0819  46  ARG D NH1 
5172  N NH2 . ARG D 46  ? 2.2956 2.1525 1.9279 -0.2305 0.2046  0.0864  46  ARG D NH2 
5173  N N   . LEU D 47  ? 1.4885 1.5530 1.3684 -0.1925 0.2494  0.0838  47  LEU D N   
5174  C CA  . LEU D 47  ? 1.4658 1.5473 1.3438 -0.1950 0.2647  0.0823  47  LEU D CA  
5175  C C   . LEU D 47  ? 1.5353 1.6200 1.3901 -0.1969 0.2700  0.0818  47  LEU D C   
5176  O O   . LEU D 47  ? 1.5352 1.6163 1.3829 -0.1947 0.2696  0.0810  47  LEU D O   
5177  C CB  . LEU D 47  ? 1.4440 1.5363 1.3406 -0.1919 0.2712  0.0802  47  LEU D CB  
5178  C CG  . LEU D 47  ? 1.4870 1.5898 1.3782 -0.1974 0.2816  0.0806  47  LEU D CG  
5179  C CD1 . LEU D 47  ? 1.4867 1.5778 1.3798 -0.2042 0.2894  0.0812  47  LEU D CD1 
5180  C CD2 . LEU D 47  ? 1.5123 1.6237 1.4117 -0.1941 0.2844  0.0790  47  LEU D CD2 
5181  N N   . LEU D 48  ? 1.5063 1.5944 1.3515 -0.2015 0.2772  0.0824  48  LEU D N   
5182  C CA  . LEU D 48  ? 1.5158 1.6036 1.3480 -0.2033 0.2856  0.0822  48  LEU D CA  
5183  C C   . LEU D 48  ? 1.5363 1.6454 1.3851 -0.2060 0.2919  0.0852  48  LEU D C   
5184  O O   . LEU D 48  ? 1.5420 1.6588 1.4015 -0.2053 0.2965  0.0874  48  LEU D O   
5185  C CB  . LEU D 48  ? 1.5338 1.6079 1.3465 -0.2062 0.2888  0.0809  48  LEU D CB  
5186  C CG  . LEU D 48  ? 1.6165 1.6674 1.4118 -0.2063 0.2787  0.0802  48  LEU D CG  
5187  C CD1 . LEU D 48  ? 1.6178 1.6687 1.4086 -0.2089 0.2822  0.0800  48  LEU D CD1 
5188  C CD2 . LEU D 48  ? 1.6937 1.7139 1.4575 -0.2075 0.2783  0.0781  48  LEU D CD2 
5189  N N   . ILE D 49  ? 1.4500 1.5651 1.3003 -0.2110 0.2920  0.0864  49  ILE D N   
5190  C CA  . ILE D 49  ? 1.4281 1.5561 1.2870 -0.2174 0.2925  0.0908  49  ILE D CA  
5191  C C   . ILE D 49  ? 1.4680 1.5914 1.3250 -0.2215 0.2908  0.0907  49  ILE D C   
5192  O O   . ILE D 49  ? 1.4705 1.5823 1.3219 -0.2227 0.2942  0.0883  49  ILE D O   
5193  C CB  . ILE D 49  ? 1.4671 1.5966 1.3210 -0.2232 0.2965  0.0926  49  ILE D CB  
5194  C CG1 . ILE D 49  ? 1.4761 1.6002 1.3311 -0.2187 0.3039  0.0909  49  ILE D CG1 
5195  C CG2 . ILE D 49  ? 1.4752 1.6139 1.3369 -0.2327 0.2912  0.0995  49  ILE D CG2 
5196  C CD1 . ILE D 49  ? 1.5659 1.6953 1.4437 -0.2167 0.3081  0.0951  49  ILE D CD1 
5197  N N   . PHE D 50  ? 1.4067 1.5351 1.2700 -0.2240 0.2873  0.0935  50  PHE D N   
5198  C CA  . PHE D 50  ? 1.4042 1.5189 1.2590 -0.2300 0.2885  0.0929  50  PHE D CA  
5199  C C   . PHE D 50  ? 1.4809 1.5954 1.3262 -0.2425 0.2815  0.1001  50  PHE D C   
5200  O O   . PHE D 50  ? 1.4708 1.6026 1.3313 -0.2423 0.2745  0.1059  50  PHE D O   
5201  C CB  . PHE D 50  ? 1.4117 1.5261 1.2789 -0.2210 0.2888  0.0892  50  PHE D CB  
5202  C CG  . PHE D 50  ? 1.4211 1.5524 1.3008 -0.2181 0.2833  0.0928  50  PHE D CG  
5203  C CD1 . PHE D 50  ? 1.4484 1.5961 1.3435 -0.2108 0.2834  0.0941  50  PHE D CD1 
5204  C CD2 . PHE D 50  ? 1.4630 1.5888 1.3376 -0.2240 0.2798  0.0955  50  PHE D CD2 
5205  C CE1 . PHE D 50  ? 1.4537 1.6170 1.3670 -0.2089 0.2824  0.0988  50  PHE D CE1 
5206  C CE2 . PHE D 50  ? 1.4914 1.6346 1.3834 -0.2215 0.2745  0.1006  50  PHE D CE2 
5207  C CZ  . PHE D 50  ? 1.4495 1.6139 1.3649 -0.2136 0.2769  0.1026  50  PHE D CZ  
5208  N N   . ALA D 51  ? 1.4637 1.5538 1.2846 -0.2551 0.2836  0.1007  51  ALA D N   
5209  C CA  . ALA D 51  ? 1.4856 1.5650 1.2872 -0.2716 0.2726  0.1088  51  ALA D CA  
5210  C C   . ALA D 51  ? 1.5524 1.6420 1.3542 -0.2790 0.2663  0.1148  51  ALA D C   
5211  O O   . ALA D 51  ? 1.5647 1.6531 1.3636 -0.2910 0.2509  0.1244  51  ALA D O   
5212  C CB  . ALA D 51  ? 1.4919 1.5813 1.3073 -0.2704 0.2591  0.1147  51  ALA D CB  
5213  N N   . GLY D 52  ? 1.5093 1.6070 1.3163 -0.2721 0.2771  0.1097  52  GLY D N   
5214  C CA  . GLY D 52  ? 1.5151 1.6208 1.3224 -0.2764 0.2766  0.1124  52  GLY D CA  
5215  C C   . GLY D 52  ? 1.5690 1.6984 1.4087 -0.2689 0.2703  0.1165  52  GLY D C   
5216  O O   . GLY D 52  ? 1.5637 1.6986 1.4077 -0.2667 0.2764  0.1147  52  GLY D O   
5217  N N   . SER D 53  ? 1.5322 1.6729 1.3970 -0.2655 0.2611  0.1221  53  SER D N   
5218  C CA  . SER D 53  ? 1.5256 1.6836 1.4289 -0.2599 0.2599  0.1276  53  SER D CA  
5219  C C   . SER D 53  ? 1.5767 1.7441 1.5022 -0.2476 0.2666  0.1256  53  SER D C   
5220  O O   . SER D 53  ? 1.5621 1.7329 1.5066 -0.2397 0.2782  0.1238  53  SER D O   
5221  C CB  . SER D 53  ? 1.5859 1.7478 1.5093 -0.2729 0.2407  0.1418  53  SER D CB  
5222  O OG  . SER D 53  ? 1.7278 1.8765 1.6246 -0.2873 0.2329  0.1444  53  SER D OG  
5223  N N   . SER D 54  ? 1.5478 1.7142 1.4668 -0.2469 0.2618  0.1253  54  SER D N   
5224  C CA  . SER D 54  ? 1.5352 1.7108 1.4727 -0.2367 0.2674  0.1239  54  SER D CA  
5225  C C   . SER D 54  ? 1.5866 1.7568 1.5145 -0.2253 0.2818  0.1135  54  SER D C   
5226  O O   . SER D 54  ? 1.5937 1.7523 1.4965 -0.2235 0.2836  0.1060  54  SER D O   
5227  C CB  . SER D 54  ? 1.5723 1.7440 1.4989 -0.2386 0.2601  0.1238  54  SER D CB  
5228  O OG  . SER D 54  ? 1.6710 1.8362 1.5919 -0.2528 0.2438  0.1334  54  SER D OG  
5229  N N   . ARG D 55  ? 1.5322 1.7061 1.4801 -0.2195 0.2923  0.1145  55  ARG D N   
5230  C CA  . ARG D 55  ? 1.5359 1.6956 1.4671 -0.2121 0.3039  0.1061  55  ARG D CA  
5231  C C   . ARG D 55  ? 1.5844 1.7450 1.5088 -0.2061 0.3019  0.1017  55  ARG D C   
5232  O O   . ARG D 55  ? 1.5757 1.7501 1.5197 -0.2050 0.3012  0.1058  55  ARG D O   
5233  C CB  . ARG D 55  ? 1.5495 1.7018 1.4982 -0.2115 0.3206  0.1089  55  ARG D CB  
5234  C CG  . ARG D 55  ? 1.6566 1.7797 1.5734 -0.2095 0.3318  0.1006  55  ARG D CG  
5235  C CD  . ARG D 55  ? 1.7253 1.8287 1.6525 -0.2108 0.3545  0.1021  55  ARG D CD  
5236  N NE  . ARG D 55  ? 1.8397 1.9448 1.7993 -0.2141 0.3639  0.1079  55  ARG D NE  
5237  C CZ  . ARG D 55  ? 2.0368 2.1496 2.0448 -0.2165 0.3759  0.1175  55  ARG D CZ  
5238  N NH1 . ARG D 55  ? 1.8952 2.0158 1.9209 -0.2160 0.3820  0.1220  55  ARG D NH1 
5239  N NH2 . ARG D 55  ? 1.8718 1.9844 1.9160 -0.2194 0.3826  0.1236  55  ARG D NH2 
5240  N N   . ALA D 56  ? 1.4377 1.5125 1.3646 -0.2324 0.1996  0.0880  56  ALA D N   
5241  C CA  . ALA D 56  ? 1.4601 1.5053 1.3907 -0.2463 0.1973  0.0915  56  ALA D CA  
5242  C C   . ALA D 56  ? 1.5679 1.5646 1.5253 -0.2443 0.2042  0.0716  56  ALA D C   
5243  O O   . ALA D 56  ? 1.5652 1.5549 1.5332 -0.2289 0.2128  0.0487  56  ALA D O   
5244  C CB  . ALA D 56  ? 1.4500 1.5096 1.3465 -0.2652 0.1943  0.0804  56  ALA D CB  
5245  N N   . THR D 57  ? 1.5815 1.5471 1.5527 -0.2603 0.1998  0.0799  57  THR D N   
5246  C CA  . THR D 57  ? 1.6470 1.5553 1.6496 -0.2646 0.2027  0.0603  57  THR D CA  
5247  C C   . THR D 57  ? 1.7261 1.6308 1.7077 -0.2724 0.2088  0.0062  57  THR D C   
5248  O O   . THR D 57  ? 1.7248 1.6434 1.6824 -0.2962 0.2048  -0.0064 57  THR D O   
5249  C CB  . THR D 57  ? 1.7755 1.6614 1.7989 -0.2874 0.1937  0.0906  57  THR D CB  
5250  O OG1 . THR D 57  ? 1.7276 1.6495 1.7544 -0.2820 0.1878  0.1426  57  THR D OG1 
5251  C CG2 . THR D 57  ? 1.8317 1.6455 1.9052 -0.2895 0.1944  0.0834  57  THR D CG2 
5252  N N   . GLY D 58  ? 1.7002 1.5984 1.6906 -0.2505 0.2187  -0.0235 58  GLY D N   
5253  C CA  . GLY D 58  ? 1.7116 1.6208 1.6826 -0.2527 0.2261  -0.0756 58  GLY D CA  
5254  C C   . GLY D 58  ? 1.6985 1.6736 1.6273 -0.2541 0.2297  -0.0784 58  GLY D C   
5255  O O   . GLY D 58  ? 1.6845 1.6853 1.5843 -0.2728 0.2282  -0.0958 58  GLY D O   
5256  N N   . ILE D 59  ? 1.6199 1.6248 1.5491 -0.2353 0.2337  -0.0584 59  ILE D N   
5257  C CA  . ILE D 59  ? 1.5746 1.6367 1.4746 -0.2364 0.2367  -0.0536 59  ILE D CA  
5258  C C   . ILE D 59  ? 1.6412 1.7305 1.5552 -0.2123 0.2482  -0.0647 59  ILE D C   
5259  O O   . ILE D 59  ? 1.6522 1.7251 1.5966 -0.1929 0.2494  -0.0527 59  ILE D O   
5260  C CB  . ILE D 59  ? 1.5638 1.6404 1.4527 -0.2443 0.2265  -0.0136 59  ILE D CB  
5261  C CG1 . ILE D 59  ? 1.5560 1.6220 1.4284 -0.2653 0.2170  -0.0037 59  ILE D CG1 
5262  C CG2 . ILE D 59  ? 1.5309 1.6535 1.4031 -0.2440 0.2283  -0.0046 59  ILE D CG2 
5263  C CD1 . ILE D 59  ? 1.5984 1.6873 1.4411 -0.2824 0.2176  -0.0224 59  ILE D CD1 
5264  N N   . PRO D 60  ? 1.5967 1.7359 1.4912 -0.2120 0.2571  -0.0836 60  PRO D N   
5265  C CA  . PRO D 60  ? 1.6047 1.7826 1.5142 -0.1891 0.2692  -0.0924 60  PRO D CA  
5266  C C   . PRO D 60  ? 1.6321 1.8360 1.5561 -0.1830 0.2666  -0.0554 60  PRO D C   
5267  O O   . PRO D 60  ? 1.6071 1.8093 1.5213 -0.1993 0.2557  -0.0264 60  PRO D O   
5268  C CB  . PRO D 60  ? 1.6267 1.8650 1.5085 -0.1959 0.2779  -0.1130 60  PRO D CB  
5269  C CG  . PRO D 60  ? 1.6580 1.8965 1.5116 -0.2226 0.2682  -0.0964 60  PRO D CG  
5270  C CD  . PRO D 60  ? 1.6086 1.7818 1.4689 -0.2313 0.2571  -0.0941 60  PRO D CD  
5271  N N   . ASP D 61  ? 1.5928 1.8262 1.5412 -0.1586 0.2766  -0.0602 61  ASP D N   
5272  C CA  . ASP D 61  ? 1.5610 1.8317 1.5300 -0.1507 0.2752  -0.0302 61  ASP D CA  
5273  C C   . ASP D 61  ? 1.5580 1.8752 1.5119 -0.1744 0.2702  -0.0054 61  ASP D C   
5274  O O   . ASP D 61  ? 1.5193 1.8509 1.4876 -0.1789 0.2618  0.0211  61  ASP D O   
5275  C CB  . ASP D 61  ? 1.6108 1.9192 1.6067 -0.1188 0.2899  -0.0461 61  ASP D CB  
5276  C CG  . ASP D 61  ? 1.8181 2.0747 1.8452 -0.0892 0.2926  -0.0594 61  ASP D CG  
5277  O OD1 . ASP D 61  ? 1.8595 2.0526 1.8822 -0.0933 0.2897  -0.0794 61  ASP D OD1 
5278  O OD2 . ASP D 61  ? 1.9248 2.2057 1.9845 -0.0620 0.2975  -0.0484 61  ASP D OD2 
5279  N N   . ARG D 62  ? 1.5127 1.8555 1.4409 -0.1897 0.2748  -0.0133 62  ARG D N   
5280  C CA  . ARG D 62  ? 1.4786 1.8587 1.3975 -0.2127 0.2707  0.0134  62  ARG D CA  
5281  C C   . ARG D 62  ? 1.4952 1.8336 1.4084 -0.2313 0.2534  0.0354  62  ARG D C   
5282  O O   . ARG D 62  ? 1.4669 1.8224 1.3929 -0.2431 0.2459  0.0577  62  ARG D O   
5283  C CB  . ARG D 62  ? 1.4575 1.8757 1.3515 -0.2222 0.2793  0.0053  62  ARG D CB  
5284  C CG  . ARG D 62  ? 1.5198 1.9005 1.3865 -0.2277 0.2764  -0.0158 62  ARG D CG  
5285  C CD  . ARG D 62  ? 1.5979 2.0363 1.4422 -0.2319 0.2863  -0.0273 62  ARG D CD  
5286  N NE  . ARG D 62  ? 1.7586 2.1981 1.5959 -0.2163 0.2951  -0.0748 62  ARG D NE  
5287  C CZ  . ARG D 62  ? 1.9466 2.3702 1.7615 -0.2245 0.2921  -0.1001 62  ARG D CZ  
5288  N NH1 . ARG D 62  ? 1.7548 2.1672 1.5508 -0.2451 0.2820  -0.0781 62  ARG D NH1 
5289  N NH2 . ARG D 62  ? 1.8148 2.2353 1.6281 -0.2118 0.2987  -0.1496 62  ARG D NH2 
5290  N N   . PHE D 63  ? 1.4562 1.7438 1.3531 -0.2334 0.2468  0.0266  63  PHE D N   
5291  C CA  . PHE D 63  ? 1.4425 1.6972 1.3308 -0.2460 0.2319  0.0421  63  PHE D CA  
5292  C C   . PHE D 63  ? 1.5229 1.7699 1.4320 -0.2384 0.2231  0.0535  63  PHE D C   
5293  O O   . PHE D 63  ? 1.5386 1.7701 1.4611 -0.2223 0.2253  0.0491  63  PHE D O   
5294  C CB  . PHE D 63  ? 1.4649 1.6827 1.3319 -0.2497 0.2290  0.0313  63  PHE D CB  
5295  C CG  . PHE D 63  ? 1.4817 1.7154 1.3251 -0.2598 0.2341  0.0233  63  PHE D CG  
5296  C CD1 . PHE D 63  ? 1.5002 1.7373 1.3285 -0.2726 0.2275  0.0404  63  PHE D CD1 
5297  C CD2 . PHE D 63  ? 1.5269 1.7747 1.3643 -0.2546 0.2447  -0.0026 63  PHE D CD2 
5298  C CE1 . PHE D 63  ? 1.5129 1.7739 1.3211 -0.2798 0.2318  0.0391  63  PHE D CE1 
5299  C CE2 . PHE D 63  ? 1.5660 1.8425 1.3797 -0.2643 0.2482  -0.0096 63  PHE D CE2 
5300  C CZ  . PHE D 63  ? 1.5218 1.8077 1.3213 -0.2767 0.2419  0.0150  63  PHE D CZ  
5301  N N   . SER D 64  ? 1.4800 1.7396 1.3941 -0.2503 0.2123  0.0683  64  SER D N   
5302  C CA  . SER D 64  ? 1.4772 1.7457 1.4082 -0.2460 0.2016  0.0777  64  SER D CA  
5303  C C   . SER D 64  ? 1.5213 1.7781 1.4410 -0.2599 0.1858  0.0809  64  SER D C   
5304  O O   . SER D 64  ? 1.5085 1.7582 1.4207 -0.2753 0.1826  0.0807  64  SER D O   
5305  C CB  . SER D 64  ? 1.5295 1.8458 1.4885 -0.2438 0.2045  0.0850  64  SER D CB  
5306  O OG  . SER D 64  ? 1.6410 1.9789 1.6034 -0.2644 0.2035  0.0911  64  SER D OG  
5307  N N   . GLY D 65  ? 1.4923 1.7495 1.4125 -0.2523 0.1765  0.0843  65  GLY D N   
5308  C CA  . GLY D 65  ? 1.4996 1.7555 1.4082 -0.2602 0.1615  0.0808  65  GLY D CA  
5309  C C   . GLY D 65  ? 1.5824 1.8780 1.5099 -0.2644 0.1497  0.0814  65  GLY D C   
5310  O O   . GLY D 65  ? 1.5855 1.9132 1.5294 -0.2521 0.1498  0.0924  65  GLY D O   
5311  N N   . LYS D 66  ? 1.5584 1.8524 1.4870 -0.2820 0.1386  0.0700  66  LYS D N   
5312  C CA  . LYS D 66  ? 1.5717 1.9038 1.5188 -0.2930 0.1240  0.0634  66  LYS D CA  
5313  C C   . LYS D 66  ? 1.6583 1.9802 1.5890 -0.2976 0.1079  0.0411  66  LYS D C   
5314  O O   . LYS D 66  ? 1.6717 1.9500 1.5919 -0.3044 0.1067  0.0301  66  LYS D O   
5315  C CB  . LYS D 66  ? 1.6120 1.9514 1.5849 -0.3146 0.1248  0.0668  66  LYS D CB  
5316  C CG  . LYS D 66  ? 1.7637 2.1474 1.7627 -0.3325 0.1087  0.0599  66  LYS D CG  
5317  C CD  . LYS D 66  ? 1.8060 2.1885 1.8330 -0.3608 0.1081  0.0664  66  LYS D CD  
5318  C CE  . LYS D 66  ? 1.7723 2.1945 1.8290 -0.3861 0.0894  0.0564  66  LYS D CE  
5319  N NZ  . LYS D 66  ? 1.7762 2.1871 1.8641 -0.4190 0.0871  0.0662  66  LYS D NZ  
5320  N N   . THR D 67  ? 1.6284 1.9954 1.5566 -0.2907 0.0961  0.0348  67  THR D N   
5321  C CA  . THR D 67  ? 1.6510 2.0220 1.5618 -0.2914 0.0807  0.0070  67  THR D CA  
5322  C C   . THR D 67  ? 1.7393 2.1313 1.6708 -0.3137 0.0628  -0.0183 67  THR D C   
5323  O O   . THR D 67  ? 1.7397 2.1948 1.6765 -0.3142 0.0504  -0.0262 67  THR D O   
5324  C CB  . THR D 67  ? 1.7387 2.1523 1.6292 -0.2701 0.0792  0.0147  67  THR D CB  
5325  O OG1 . THR D 67  ? 1.7238 2.1924 1.6313 -0.2624 0.0804  0.0398  67  THR D OG1 
5326  C CG2 . THR D 67  ? 1.6901 2.0682 1.5599 -0.2562 0.0926  0.0297  67  THR D CG2 
5327  N N   . SER D 68  ? 1.7249 2.0658 1.6711 -0.3339 0.0611  -0.0283 68  SER D N   
5328  C CA  . SER D 68  ? 1.7597 2.1005 1.7347 -0.3629 0.0445  -0.0501 68  SER D CA  
5329  C C   . SER D 68  ? 1.8439 2.1948 1.8110 -0.3661 0.0230  -0.0966 68  SER D C   
5330  O O   . SER D 68  ? 1.8266 2.1897 1.7623 -0.3427 0.0221  -0.1111 68  SER D O   
5331  C CB  . SER D 68  ? 1.8279 2.1032 1.8219 -0.3813 0.0499  -0.0407 68  SER D CB  
5332  O OG  . SER D 68  ? 1.9178 2.2062 1.9267 -0.3854 0.0663  -0.0036 68  SER D OG  
5333  N N   . GLY D 69  ? 1.8507 2.2003 1.8485 -0.3963 0.0055  -0.1208 69  GLY D N   
5334  C CA  . GLY D 69  ? 1.9044 2.2574 1.9018 -0.4050 -0.0176 -0.1754 69  GLY D CA  
5335  C C   . GLY D 69  ? 2.0011 2.2729 1.9865 -0.3939 -0.0184 -0.2025 69  GLY D C   
5336  O O   . GLY D 69  ? 2.0340 2.3102 2.0054 -0.3851 -0.0330 -0.2521 69  GLY D O   
5337  N N   . THR D 70  ? 1.9543 2.1586 1.9454 -0.3916 -0.0022 -0.1697 70  THR D N   
5338  C CA  . THR D 70  ? 1.9785 2.1058 1.9615 -0.3766 0.0015  -0.1804 70  THR D CA  
5339  C C   . THR D 70  ? 1.9907 2.1483 1.9270 -0.3384 0.0087  -0.1899 70  THR D C   
5340  O O   . THR D 70  ? 2.0156 2.1715 1.9377 -0.3234 -0.0025 -0.2351 70  THR D O   
5341  C CB  . THR D 70  ? 2.0636 2.1397 2.0627 -0.3835 0.0187  -0.1313 70  THR D CB  
5342  O OG1 . THR D 70  ? 1.9666 2.0852 1.9451 -0.3709 0.0380  -0.0913 70  THR D OG1 
5343  C CG2 . THR D 70  ? 2.0915 2.1413 2.1411 -0.4229 0.0113  -0.1177 70  THR D CG2 
5344  N N   . ASP D 71  ? 1.8890 2.0804 1.8044 -0.3240 0.0267  -0.1481 71  ASP D N   
5345  C CA  . ASP D 71  ? 1.8514 2.0824 1.7291 -0.2943 0.0367  -0.1383 71  ASP D CA  
5346  C C   . ASP D 71  ? 1.8209 2.0516 1.6925 -0.2892 0.0573  -0.0888 71  ASP D C   
5347  O O   . ASP D 71  ? 1.7941 2.0709 1.6474 -0.2745 0.0636  -0.0722 71  ASP D O   
5348  C CB  . ASP D 71  ? 1.9031 2.1127 1.7574 -0.2697 0.0351  -0.1663 71  ASP D CB  
5349  C CG  . ASP D 71  ? 2.0198 2.2908 1.8550 -0.2558 0.0207  -0.2094 71  ASP D CG  
5350  O OD1 . ASP D 71  ? 1.9796 2.3277 1.7976 -0.2479 0.0224  -0.1941 71  ASP D OD1 
5351  O OD2 . ASP D 71  ? 2.1505 2.3948 1.9892 -0.2515 0.0078  -0.2580 71  ASP D OD2 
5352  N N   . PHE D 72  ? 1.7362 1.9195 1.6249 -0.3018 0.0672  -0.0653 72  PHE D N   
5353  C CA  . PHE D 72  ? 1.6813 1.8664 1.5632 -0.2967 0.0860  -0.0278 72  PHE D CA  
5354  C C   . PHE D 72  ? 1.6982 1.8552 1.6031 -0.3144 0.0948  -0.0047 72  PHE D C   
5355  O O   . PHE D 72  ? 1.7324 1.8488 1.6538 -0.3263 0.0896  -0.0089 72  PHE D O   
5356  C CB  . PHE D 72  ? 1.6945 1.8670 1.5474 -0.2757 0.0950  -0.0224 72  PHE D CB  
5357  C CG  . PHE D 72  ? 1.6820 1.8806 1.5207 -0.2657 0.1078  0.0024  72  PHE D CG  
5358  C CD1 . PHE D 72  ? 1.7121 1.9022 1.5298 -0.2535 0.1162  0.0114  72  PHE D CD1 
5359  C CD2 . PHE D 72  ? 1.6950 1.9263 1.5457 -0.2687 0.1107  0.0170  72  PHE D CD2 
5360  C CE1 . PHE D 72  ? 1.7019 1.9090 1.5127 -0.2490 0.1262  0.0325  72  PHE D CE1 
5361  C CE2 . PHE D 72  ? 1.7111 1.9541 1.5556 -0.2592 0.1218  0.0388  72  PHE D CE2 
5362  C CZ  . PHE D 72  ? 1.6801 1.9081 1.5054 -0.2515 0.1287  0.0452  72  PHE D CZ  
5363  N N   . THR D 73  ? 1.5857 1.7662 1.4927 -0.3139 0.1086  0.0206  73  THR D N   
5364  C CA  . THR D 73  ? 1.5570 1.7328 1.4814 -0.3267 0.1201  0.0441  73  THR D CA  
5365  C C   . THR D 73  ? 1.5465 1.7400 1.4587 -0.3142 0.1377  0.0611  73  THR D C   
5366  O O   . THR D 73  ? 1.5160 1.7395 1.4299 -0.3051 0.1406  0.0625  73  THR D O   
5367  C CB  . THR D 73  ? 1.6006 1.8013 1.5601 -0.3493 0.1133  0.0479  73  THR D CB  
5368  O OG1 . THR D 73  ? 1.5421 1.7798 1.5059 -0.3481 0.1013  0.0313  73  THR D OG1 
5369  C CG2 . THR D 73  ? 1.6145 1.7789 1.5989 -0.3723 0.1036  0.0473  73  THR D CG2 
5370  N N   . LEU D 74  ? 1.4966 1.6731 1.3991 -0.3135 0.1489  0.0733  74  LEU D N   
5371  C CA  . LEU D 74  ? 1.4818 1.6740 1.3736 -0.3045 0.1650  0.0819  74  LEU D CA  
5372  C C   . LEU D 74  ? 1.5634 1.7805 1.4738 -0.3164 0.1743  0.0981  74  LEU D C   
5373  O O   . LEU D 74  ? 1.5701 1.7779 1.4904 -0.3301 0.1721  0.1116  74  LEU D O   
5374  C CB  . LEU D 74  ? 1.4801 1.6519 1.3453 -0.2964 0.1700  0.0816  74  LEU D CB  
5375  C CG  . LEU D 74  ? 1.5268 1.7128 1.3801 -0.2906 0.1845  0.0828  74  LEU D CG  
5376  C CD1 . LEU D 74  ? 1.5229 1.7045 1.3686 -0.2790 0.1852  0.0730  74  LEU D CD1 
5377  C CD2 . LEU D 74  ? 1.5475 1.7287 1.3825 -0.2919 0.1886  0.0889  74  LEU D CD2 
5378  N N   . THR D 75  ? 1.5412 1.7932 1.4594 -0.3094 0.1851  0.0989  75  THR D N   
5379  C CA  . THR D 75  ? 1.5549 1.8489 1.4908 -0.3173 0.1959  0.1136  75  THR D CA  
5380  C C   . THR D 75  ? 1.6117 1.9310 1.5349 -0.3012 0.2133  0.1063  75  THR D C   
5381  O O   . THR D 75  ? 1.6061 1.9193 1.5256 -0.2836 0.2167  0.0905  75  THR D O   
5382  C CB  . THR D 75  ? 1.7062 2.0344 1.6744 -0.3262 0.1902  0.1193  75  THR D CB  
5383  O OG1 . THR D 75  ? 1.7323 2.0344 1.7092 -0.3395 0.1715  0.1140  75  THR D OG1 
5384  C CG2 . THR D 75  ? 1.7122 2.0898 1.7044 -0.3414 0.1985  0.1417  75  THR D CG2 
5385  N N   . ILE D 76  ? 1.5743 1.9244 1.4934 -0.3071 0.2239  0.1181  76  ILE D N   
5386  C CA  . ILE D 76  ? 1.5739 1.9600 1.4800 -0.2931 0.2405  0.1052  76  ILE D CA  
5387  C C   . ILE D 76  ? 1.6437 2.1010 1.5708 -0.2974 0.2514  0.1217  76  ILE D C   
5388  O O   . ILE D 76  ? 1.6481 2.1267 1.5879 -0.3174 0.2491  0.1520  76  ILE D O   
5389  C CB  . ILE D 76  ? 1.6114 1.9906 1.4876 -0.2943 0.2438  0.1019  76  ILE D CB  
5390  C CG1 . ILE D 76  ? 1.6077 1.9264 1.4675 -0.2943 0.2317  0.0946  76  ILE D CG1 
5391  C CG2 . ILE D 76  ? 1.6263 2.0398 1.4875 -0.2795 0.2584  0.0755  76  ILE D CG2 
5392  C CD1 . ILE D 76  ? 1.7330 2.0481 1.5754 -0.3020 0.2292  0.1088  76  ILE D CD1 
5393  N N   . SER D 77  ? 1.6044 2.1000 1.5389 -0.2779 0.2636  0.1041  77  SER D N   
5394  C CA  . SER D 77  ? 1.6082 2.1863 1.5627 -0.2775 0.2761  0.1179  77  SER D CA  
5395  C C   . SER D 77  ? 1.6625 2.2979 1.5983 -0.2793 0.2896  0.1233  77  SER D C   
5396  O O   . SER D 77  ? 1.6642 2.3474 1.6124 -0.2992 0.2910  0.1603  77  SER D O   
5397  C CB  . SER D 77  ? 1.6628 2.2663 1.6331 -0.2499 0.2853  0.0955  77  SER D CB  
5398  O OG  . SER D 77  ? 1.7884 2.3577 1.7393 -0.2253 0.2916  0.0575  77  SER D OG  
5399  N N   . ARG D 78  ? 1.6132 2.2460 1.5210 -0.2606 0.2982  0.0877  78  ARG D N   
5400  C CA  . ARG D 78  ? 1.6130 2.3087 1.4969 -0.2598 0.3101  0.0841  78  ARG D CA  
5401  C C   . ARG D 78  ? 1.6403 2.2873 1.4944 -0.2686 0.3014  0.0784  78  ARG D C   
5402  O O   . ARG D 78  ? 1.6461 2.2325 1.4875 -0.2594 0.2963  0.0449  78  ARG D O   
5403  C CB  . ARG D 78  ? 1.6259 2.3698 1.5021 -0.2309 0.3266  0.0385  78  ARG D CB  
5404  C CG  . ARG D 78  ? 1.7220 2.5457 1.6250 -0.2179 0.3397  0.0460  78  ARG D CG  
5405  C CD  . ARG D 78  ? 1.8472 2.7077 1.7432 -0.1827 0.3558  -0.0078 78  ARG D CD  
5406  N NE  . ARG D 78  ? 1.9329 2.8930 1.8519 -0.1669 0.3712  0.0004  78  ARG D NE  
5407  C CZ  . ARG D 78  ? 2.1339 3.1340 2.0575 -0.1299 0.3866  -0.0441 78  ARG D CZ  
5408  N NH1 . ARG D 78  ? 2.0424 2.9805 1.9524 -0.1071 0.3874  -0.1015 78  ARG D NH1 
5409  N NH2 . ARG D 78  ? 1.9376 3.0402 1.8833 -0.1152 0.4011  -0.0318 78  ARG D NH2 
5410  N N   . LEU D 79  ? 1.5654 2.2407 1.4129 -0.2865 0.2991  0.1158  79  LEU D N   
5411  C CA  . LEU D 79  ? 1.5472 2.1909 1.3686 -0.2926 0.2916  0.1156  79  LEU D CA  
5412  C C   . LEU D 79  ? 1.5847 2.2940 1.3758 -0.2833 0.3025  0.0868  79  LEU D C   
5413  O O   . LEU D 79  ? 1.5935 2.3938 1.3794 -0.2860 0.3125  0.1081  79  LEU D O   
5414  C CB  . LEU D 79  ? 1.5427 2.1832 1.3745 -0.3117 0.2836  0.1699  79  LEU D CB  
5415  C CG  . LEU D 79  ? 1.5866 2.1395 1.4384 -0.3208 0.2675  0.1833  79  LEU D CG  
5416  C CD1 . LEU D 79  ? 1.5952 2.1558 1.4758 -0.3397 0.2628  0.2355  79  LEU D CD1 
5417  C CD2 . LEU D 79  ? 1.6132 2.1031 1.4430 -0.3166 0.2570  0.1676  79  LEU D CD2 
5418  N N   . GLU D 80  ? 1.5216 2.1901 1.2952 -0.2735 0.3005  0.0376  80  GLU D N   
5419  C CA  . GLU D 80  ? 1.5319 2.2538 1.2770 -0.2670 0.3079  -0.0026 80  GLU D CA  
5420  C C   . GLU D 80  ? 1.5633 2.3010 1.2847 -0.2814 0.3002  0.0173  80  GLU D C   
5421  O O   . GLU D 80  ? 1.5278 2.2079 1.2563 -0.2910 0.2885  0.0493  80  GLU D O   
5422  C CB  . GLU D 80  ? 1.5646 2.2265 1.3092 -0.2543 0.3068  -0.0624 80  GLU D CB  
5423  C CG  . GLU D 80  ? 1.6586 2.3105 1.4289 -0.2337 0.3155  -0.0826 80  GLU D CG  
5424  C CD  . GLU D 80  ? 1.7302 2.4789 1.4983 -0.2161 0.3332  -0.1046 80  GLU D CD  
5425  O OE1 . GLU D 80  ? 1.5843 2.3791 1.3288 -0.2103 0.3392  -0.1484 80  GLU D OE1 
5426  O OE2 . GLU D 80  ? 1.4868 2.2692 1.2782 -0.2075 0.3407  -0.0819 80  GLU D OE2 
5427  N N   . PRO D 81  ? 1.5505 2.3715 1.2443 -0.2815 0.3060  -0.0011 81  PRO D N   
5428  C CA  . PRO D 81  ? 1.5473 2.3928 1.2209 -0.2938 0.2980  0.0236  81  PRO D CA  
5429  C C   . PRO D 81  ? 1.5786 2.3347 1.2494 -0.3009 0.2832  0.0122  81  PRO D C   
5430  O O   . PRO D 81  ? 1.5631 2.3165 1.2294 -0.3080 0.2750  0.0488  81  PRO D O   
5431  C CB  . PRO D 81  ? 1.6037 2.5539 1.2470 -0.2912 0.3058  -0.0136 81  PRO D CB  
5432  C CG  . PRO D 81  ? 1.6758 2.6822 1.3260 -0.2767 0.3213  -0.0334 81  PRO D CG  
5433  C CD  . PRO D 81  ? 1.6051 2.5112 1.2847 -0.2686 0.3200  -0.0460 81  PRO D CD  
5434  N N   . GLU D 82  ? 1.5431 2.2297 1.2201 -0.2971 0.2805  -0.0348 82  GLU D N   
5435  C CA  . GLU D 82  ? 1.5381 2.1431 1.2169 -0.3043 0.2677  -0.0478 82  GLU D CA  
5436  C C   . GLU D 82  ? 1.5421 2.0795 1.2397 -0.3047 0.2594  -0.0048 82  GLU D C   
5437  O O   . GLU D 82  ? 1.5235 2.0234 1.2174 -0.3109 0.2489  0.0037  82  GLU D O   
5438  C CB  . GLU D 82  ? 1.5815 2.1323 1.2711 -0.2989 0.2686  -0.1023 82  GLU D CB  
5439  C CG  . GLU D 82  ? 1.7629 2.3693 1.4403 -0.2933 0.2779  -0.1574 82  GLU D CG  
5440  C CD  . GLU D 82  ? 1.8767 2.5141 1.5663 -0.2728 0.2924  -0.1707 82  GLU D CD  
5441  O OE1 . GLU D 82  ? 1.5524 2.2877 1.2253 -0.2677 0.3029  -0.1767 82  GLU D OE1 
5442  O OE2 . GLU D 82  ? 1.8300 2.4032 1.5462 -0.2605 0.2938  -0.1752 82  GLU D OE2 
5443  N N   . ASP D 83  ? 1.4774 2.0053 1.1957 -0.2983 0.2637  0.0187  83  ASP D N   
5444  C CA  . ASP D 83  ? 1.4438 1.9125 1.1825 -0.2989 0.2555  0.0511  83  ASP D CA  
5445  C C   . ASP D 83  ? 1.4688 1.9426 1.2064 -0.3046 0.2489  0.0956  83  ASP D C   
5446  O O   . ASP D 83  ? 1.4494 1.8671 1.1998 -0.3043 0.2396  0.1119  83  ASP D O   
5447  C CB  . ASP D 83  ? 1.4617 1.9323 1.2253 -0.2939 0.2615  0.0597  83  ASP D CB  
5448  C CG  . ASP D 83  ? 1.5742 2.0301 1.3472 -0.2818 0.2675  0.0212  83  ASP D CG  
5449  O OD1 . ASP D 83  ? 1.6117 2.0798 1.3712 -0.2769 0.2724  -0.0175 83  ASP D OD1 
5450  O OD2 . ASP D 83  ? 1.5914 2.0276 1.3881 -0.2767 0.2673  0.0293  83  ASP D OD2 
5451  N N   . PHE D 84  ? 1.4327 1.9759 1.1569 -0.3076 0.2536  0.1152  84  PHE D N   
5452  C CA  . PHE D 84  ? 1.4328 1.9826 1.1615 -0.3092 0.2482  0.1630  84  PHE D CA  
5453  C C   . PHE D 84  ? 1.4960 2.0155 1.2115 -0.3066 0.2381  0.1588  84  PHE D C   
5454  O O   . PHE D 84  ? 1.5016 2.0719 1.1953 -0.3083 0.2384  0.1517  84  PHE D O   
5455  C CB  . PHE D 84  ? 1.4679 2.1131 1.1908 -0.3117 0.2571  0.1949  84  PHE D CB  
5456  C CG  . PHE D 84  ? 1.4875 2.1650 1.2313 -0.3152 0.2664  0.2138  84  PHE D CG  
5457  C CD1 . PHE D 84  ? 1.5259 2.1758 1.3025 -0.3215 0.2629  0.2619  84  PHE D CD1 
5458  C CD2 . PHE D 84  ? 1.5174 2.2527 1.2513 -0.3122 0.2782  0.1812  84  PHE D CD2 
5459  C CE1 . PHE D 84  ? 1.5426 2.2285 1.3427 -0.3288 0.2707  0.2822  84  PHE D CE1 
5460  C CE2 . PHE D 84  ? 1.5555 2.3315 1.3104 -0.3142 0.2876  0.2005  84  PHE D CE2 
5461  C CZ  . PHE D 84  ? 1.5308 2.2854 1.3191 -0.3246 0.2837  0.2535  84  PHE D CZ  
5462  N N   . ALA D 85  ? 1.4520 1.8967 1.1806 -0.3024 0.2290  0.1603  85  ALA D N   
5463  C CA  . ALA D 85  ? 1.4478 1.8656 1.1672 -0.2971 0.2198  0.1571  85  ALA D CA  
5464  C C   . ALA D 85  ? 1.4867 1.8414 1.2251 -0.2881 0.2113  0.1738  85  ALA D C   
5465  O O   . ALA D 85  ? 1.4932 1.8257 1.2537 -0.2895 0.2111  0.1910  85  ALA D O   
5466  C CB  . ALA D 85  ? 1.4496 1.8509 1.1566 -0.3020 0.2181  0.1153  85  ALA D CB  
5467  N N   . VAL D 86  ? 1.4200 1.7522 1.1512 -0.2797 0.2038  0.1672  86  VAL D N   
5468  C CA  . VAL D 86  ? 1.4128 1.6923 1.1581 -0.2671 0.1953  0.1731  86  VAL D CA  
5469  C C   . VAL D 86  ? 1.4391 1.6797 1.1868 -0.2694 0.1915  0.1440  86  VAL D C   
5470  O O   . VAL D 86  ? 1.4214 1.6711 1.1563 -0.2741 0.1922  0.1240  86  VAL D O   
5471  C CB  . VAL D 86  ? 1.4632 1.7537 1.2003 -0.2514 0.1905  0.1840  86  VAL D CB  
5472  C CG1 . VAL D 86  ? 1.4765 1.7150 1.2312 -0.2335 0.1828  0.1884  86  VAL D CG1 
5473  C CG2 . VAL D 86  ? 1.4723 1.8194 1.2044 -0.2492 0.1948  0.2147  86  VAL D CG2 
5474  N N   . TYR D 87  ? 1.4006 1.6009 1.1677 -0.2677 0.1866  0.1437  87  TYR D N   
5475  C CA  . TYR D 87  ? 1.3892 1.5636 1.1609 -0.2690 0.1822  0.1209  87  TYR D CA  
5476  C C   . TYR D 87  ? 1.4606 1.6067 1.2345 -0.2557 0.1719  0.1115  87  TYR D C   
5477  O O   . TYR D 87  ? 1.4844 1.6048 1.2728 -0.2492 0.1663  0.1182  87  TYR D O   
5478  C CB  . TYR D 87  ? 1.4000 1.5687 1.1912 -0.2801 0.1845  0.1217  87  TYR D CB  
5479  C CG  . TYR D 87  ? 1.4094 1.6123 1.1945 -0.2881 0.1955  0.1174  87  TYR D CG  
5480  C CD1 . TYR D 87  ? 1.4391 1.6811 1.2195 -0.2928 0.2039  0.1332  87  TYR D CD1 
5481  C CD2 . TYR D 87  ? 1.4108 1.6113 1.1951 -0.2883 0.1977  0.0966  87  TYR D CD2 
5482  C CE1 . TYR D 87  ? 1.4507 1.7307 1.2228 -0.2972 0.2141  0.1206  87  TYR D CE1 
5483  C CE2 . TYR D 87  ? 1.4238 1.6505 1.2049 -0.2915 0.2079  0.0856  87  TYR D CE2 
5484  C CZ  . TYR D 87  ? 1.5359 1.8033 1.3093 -0.2958 0.2161  0.0937  87  TYR D CZ  
5485  O OH  . TYR D 87  ? 1.5808 1.8796 1.3492 -0.2964 0.2261  0.0747  87  TYR D OH  
5486  N N   . TYR D 88  ? 1.4083 1.5615 1.1699 -0.2512 0.1693  0.0961  88  TYR D N   
5487  C CA  . TYR D 88  ? 1.4194 1.5646 1.1779 -0.2362 0.1607  0.0839  88  TYR D CA  
5488  C C   . TYR D 88  ? 1.4566 1.5999 1.2196 -0.2387 0.1556  0.0687  88  TYR D C   
5489  O O   . TYR D 88  ? 1.4208 1.5745 1.1843 -0.2483 0.1599  0.0702  88  TYR D O   
5490  C CB  . TYR D 88  ? 1.4363 1.6132 1.1765 -0.2274 0.1619  0.0868  88  TYR D CB  
5491  C CG  . TYR D 88  ? 1.4811 1.6699 1.2169 -0.2172 0.1641  0.1018  88  TYR D CG  
5492  C CD1 . TYR D 88  ? 1.5361 1.7126 1.2765 -0.1944 0.1590  0.1001  88  TYR D CD1 
5493  C CD2 . TYR D 88  ? 1.4805 1.6983 1.2086 -0.2281 0.1708  0.1159  88  TYR D CD2 
5494  C CE1 . TYR D 88  ? 1.5706 1.7610 1.3112 -0.1806 0.1613  0.1189  88  TYR D CE1 
5495  C CE2 . TYR D 88  ? 1.5015 1.7427 1.2263 -0.2175 0.1723  0.1343  88  TYR D CE2 
5496  C CZ  . TYR D 88  ? 1.6257 1.8522 1.3582 -0.1927 0.1679  0.1391  88  TYR D CZ  
5497  O OH  . TYR D 88  ? 1.6457 1.8971 1.3792 -0.1780 0.1696  0.1621  88  TYR D OH  
5498  N N   . CYS D 89  ? 1.4442 1.5774 1.2114 -0.2281 0.1460  0.0529  89  CYS D N   
5499  C CA  . CYS D 89  ? 1.4460 1.5937 1.2146 -0.2279 0.1395  0.0391  89  CYS D CA  
5500  C C   . CYS D 89  ? 1.4542 1.6342 1.2053 -0.2106 0.1359  0.0314  89  CYS D C   
5501  O O   . CYS D 89  ? 1.4528 1.6344 1.1954 -0.1965 0.1364  0.0298  89  CYS D O   
5502  C CB  . CYS D 89  ? 1.4897 1.6158 1.2766 -0.2326 0.1300  0.0224  89  CYS D CB  
5503  S SG  . CYS D 89  ? 1.5940 1.6861 1.3873 -0.2178 0.1199  0.0006  89  CYS D SG  
5504  N N   . GLN D 90  ? 1.3808 1.5949 1.1282 -0.2100 0.1331  0.0310  90  GLN D N   
5505  C CA  . GLN D 90  ? 1.3728 1.6341 1.1043 -0.1945 0.1304  0.0288  90  GLN D CA  
5506  C C   . GLN D 90  ? 1.4192 1.7192 1.1510 -0.1913 0.1227  0.0212  90  GLN D C   
5507  O O   . GLN D 90  ? 1.4085 1.7085 1.1528 -0.2034 0.1231  0.0332  90  GLN D O   
5508  C CB  . GLN D 90  ? 1.3679 1.6529 1.0930 -0.2007 0.1387  0.0555  90  GLN D CB  
5509  C CG  . GLN D 90  ? 1.5486 1.8934 1.2598 -0.1868 0.1374  0.0610  90  GLN D CG  
5510  C CD  . GLN D 90  ? 1.8015 2.1781 1.5179 -0.2009 0.1413  0.0920  90  GLN D CD  
5511  O OE1 . GLN D 90  ? 1.7160 2.0712 1.4475 -0.2160 0.1430  0.1050  90  GLN D OE1 
5512  N NE2 . GLN D 90  ? 1.7509 2.1812 1.4587 -0.1952 0.1426  0.1061  90  GLN D NE2 
5513  N N   . GLN D 91  ? 1.3860 1.7261 1.1044 -0.1724 0.1158  0.0008  91  GLN D N   
5514  C CA  . GLN D 91  ? 1.3915 1.7892 1.1055 -0.1667 0.1077  -0.0072 91  GLN D CA  
5515  C C   . GLN D 91  ? 1.4439 1.9141 1.1443 -0.1573 0.1117  0.0173  91  GLN D C   
5516  O O   . GLN D 91  ? 1.4463 1.9290 1.1357 -0.1469 0.1167  0.0203  91  GLN D O   
5517  C CB  . GLN D 91  ? 1.4436 1.8432 1.1538 -0.1538 0.0953  -0.0551 91  GLN D CB  
5518  C CG  . GLN D 91  ? 1.6538 2.0592 1.3494 -0.1282 0.0945  -0.0828 91  GLN D CG  
5519  C CD  . GLN D 91  ? 1.8112 2.3097 1.4847 -0.1066 0.0930  -0.0889 91  GLN D CD  
5520  O OE1 . GLN D 91  ? 1.7243 2.2877 1.3929 -0.1099 0.0891  -0.0793 91  GLN D OE1 
5521  N NE2 . GLN D 91  ? 1.7236 2.2391 1.3846 -0.0820 0.0967  -0.1020 91  GLN D NE2 
5522  N N   . CYS D 92  ? 1.6454 2.0616 0.9962 -0.3098 -0.0899 0.1280  92  CYS D N   
5523  C CA  . CYS D 92  ? 1.6237 2.1393 1.0200 -0.3069 -0.0842 0.1708  92  CYS D CA  
5524  C C   . CYS D 92  ? 1.7221 2.3016 1.0838 -0.3034 -0.0794 0.1829  92  CYS D C   
5525  O O   . CYS D 92  ? 1.6940 2.3710 1.1010 -0.3046 -0.0759 0.2277  92  CYS D O   
5526  C CB  . CYS D 92  ? 1.5595 2.1008 1.0544 -0.3353 -0.0985 0.2089  92  CYS D CB  
5527  S SG  . CYS D 92  ? 1.5804 2.0463 1.1065 -0.3345 -0.1083 0.1900  92  CYS D SG  
5528  N N   . GLY D 93  ? 1.7435 2.2705 1.0279 -0.2962 -0.0826 0.1448  93  GLY D N   
5529  C CA  . GLY D 93  ? 1.7903 2.3626 1.0243 -0.2880 -0.0822 0.1456  93  GLY D CA  
5530  C C   . GLY D 93  ? 1.9115 2.5256 1.0809 -0.2386 -0.0671 0.1251  93  GLY D C   
5531  O O   . GLY D 93  ? 1.9412 2.4889 1.0532 -0.2135 -0.0701 0.0765  93  GLY D O   
5532  N N   . ASN D 94  ? 1.8964 2.6252 1.0788 -0.2224 -0.0521 0.1633  94  ASN D N   
5533  C CA  . ASN D 94  ? 1.9571 2.7479 1.0818 -0.1697 -0.0325 0.1530  94  ASN D CA  
5534  C C   . ASN D 94  ? 2.0090 2.7751 1.1426 -0.1435 -0.0190 0.1403  94  ASN D C   
5535  O O   . ASN D 94  ? 1.9781 2.6496 1.1203 -0.1566 -0.0284 0.1111  94  ASN D O   
5536  C CB  . ASN D 94  ? 2.0379 2.8009 1.0545 -0.1403 -0.0401 0.0999  94  ASN D CB  
5537  C CG  . ASN D 94  ? 2.1686 3.0339 1.1532 -0.1283 -0.0351 0.1245  94  ASN D CG  
5538  O OD1 . ASN D 94  ? 2.1434 3.0732 1.0647 -0.0779 -0.0201 0.1120  94  ASN D OD1 
5539  N ND2 . ASN D 94  ? 1.9602 2.8429 0.9847 -0.1729 -0.0481 0.1581  94  ASN D ND2 
5540  N N   . SER D 95  ? 1.9857 2.8442 1.1208 -0.1063 0.0038  0.1683  95  SER D N   
5541  C CA  . SER D 95  ? 1.9799 2.8289 1.1292 -0.0807 0.0192  0.1676  95  SER D CA  
5542  C C   . SER D 95  ? 2.0976 2.8640 1.1668 -0.0513 0.0196  0.0950  95  SER D C   
5543  O O   . SER D 95  ? 2.1660 2.9409 1.1554 -0.0204 0.0191  0.0562  95  SER D O   
5544  C CB  . SER D 95  ? 2.0168 2.9933 1.1947 -0.0474 0.0433  0.2265  95  SER D CB  
5545  O OG  . SER D 95  ? 2.0874 3.0508 1.2910 -0.0275 0.0569  0.2357  95  SER D OG  
5546  N N   . PRO D 96  ? 2.0274 2.7152 1.1211 -0.0602 0.0162  0.0753  96  PRO D N   
5547  C CA  . PRO D 96  ? 1.9457 2.6121 1.1234 -0.0909 0.0129  0.1120  96  PRO D CA  
5548  C C   . PRO D 96  ? 1.9281 2.5118 1.1290 -0.1338 -0.0109 0.0961  96  PRO D C   
5549  O O   . PRO D 96  ? 1.9509 2.4846 1.1059 -0.1411 -0.0248 0.0579  96  PRO D O   
5550  C CB  . PRO D 96  ? 1.9826 2.6145 1.1555 -0.0681 0.0250  0.0931  96  PRO D CB  
5551  C CG  . PRO D 96  ? 2.1086 2.6908 1.2013 -0.0441 0.0203  0.0239  96  PRO D CG  
5552  C CD  . PRO D 96  ? 2.0976 2.7133 1.1365 -0.0363 0.0124  0.0115  96  PRO D CD  
5553  N N   . TRP D 97  ? 1.8069 2.3767 1.0805 -0.1591 -0.0178 0.1271  97  TRP D N   
5554  C CA  . TRP D 97  ? 1.7665 2.2622 1.0627 -0.1934 -0.0372 0.1128  97  TRP D CA  
5555  C C   . TRP D 97  ? 1.8099 2.2275 1.0883 -0.1874 -0.0381 0.0751  97  TRP D C   
5556  O O   . TRP D 97  ? 1.7953 2.2173 1.0938 -0.1746 -0.0291 0.0851  97  TRP D O   
5557  C CB  . TRP D 97  ? 1.6925 2.2146 1.0756 -0.2189 -0.0491 0.1600  97  TRP D CB  
5558  C CG  . TRP D 97  ? 1.6866 2.2917 1.1097 -0.2321 -0.0535 0.2034  97  TRP D CG  
5559  C CD1 . TRP D 97  ? 1.7539 2.4181 1.1371 -0.2223 -0.0443 0.2080  97  TRP D CD1 
5560  C CD2 . TRP D 97  ? 1.6288 2.2719 1.1467 -0.2576 -0.0720 0.2496  97  TRP D CD2 
5561  N NE1 . TRP D 97  ? 1.7100 2.4518 1.1601 -0.2437 -0.0533 0.2586  97  TRP D NE1 
5562  C CE2 . TRP D 97  ? 1.6722 2.4032 1.2116 -0.2661 -0.0719 0.2853  97  TRP D CE2 
5563  C CE3 . TRP D 97  ? 1.6038 2.2150 1.1931 -0.2730 -0.0927 0.2624  97  TRP D CE3 
5564  C CZ2 . TRP D 97  ? 1.6082 2.4005 1.2502 -0.2928 -0.0924 0.3370  97  TRP D CZ2 
5565  C CZ3 . TRP D 97  ? 1.5732 2.2392 1.2597 -0.2949 -0.1157 0.3085  97  TRP D CZ3 
5566  C CH2 . TRP D 97  ? 1.5668 2.3237 1.2848 -0.3066 -0.1159 0.3467  97  TRP D CH2 
5567  N N   . THR D 98  ? 1.7760 2.1268 1.0207 -0.1961 -0.0501 0.0361  98  THR D N   
5568  C CA  . THR D 98  ? 1.7746 2.0621 1.0108 -0.1918 -0.0538 0.0041  98  THR D CA  
5569  C C   . THR D 98  ? 1.7876 2.0222 1.0537 -0.2174 -0.0671 0.0043  98  THR D C   
5570  O O   . THR D 98  ? 1.7777 2.0049 1.0517 -0.2363 -0.0765 0.0132  98  THR D O   
5571  C CB  . THR D 98  ? 1.8919 2.1540 1.0736 -0.1712 -0.0602 -0.0399 98  THR D CB  
5572  O OG1 . THR D 98  ? 1.8761 2.1299 1.0298 -0.1786 -0.0746 -0.0474 98  THR D OG1 
5573  C CG2 . THR D 98  ? 1.9189 2.2272 1.0716 -0.1366 -0.0437 -0.0483 98  THR D CG2 
5574  N N   . PHE D 99  ? 1.7136 1.9156 0.9975 -0.2172 -0.0669 -0.0030 99  PHE D N   
5575  C CA  . PHE D 99  ? 1.6759 1.8339 0.9815 -0.2339 -0.0775 -0.0051 99  PHE D CA  
5576  C C   . PHE D 99  ? 1.7237 1.8397 1.0098 -0.2301 -0.0861 -0.0346 99  PHE D C   
5577  O O   . PHE D 99  ? 1.7157 1.8308 0.9867 -0.2151 -0.0846 -0.0548 99  PHE D O   
5578  C CB  . PHE D 99  ? 1.6737 1.8280 1.0157 -0.2357 -0.0759 0.0105  99  PHE D CB  
5579  C CG  . PHE D 99  ? 1.6681 1.8580 1.0510 -0.2416 -0.0797 0.0450  99  PHE D CG  
5580  C CD1 . PHE D 99  ? 1.6788 1.8566 1.0906 -0.2560 -0.0938 0.0534  99  PHE D CD1 
5581  C CD2 . PHE D 99  ? 1.6945 1.9349 1.0951 -0.2306 -0.0717 0.0721  99  PHE D CD2 
5582  C CE1 . PHE D 99  ? 1.6661 1.8788 1.1310 -0.2618 -0.1055 0.0854  99  PHE D CE1 
5583  C CE2 . PHE D 99  ? 1.7020 1.9831 1.1583 -0.2363 -0.0821 0.1120  99  PHE D CE2 
5584  C CZ  . PHE D 99  ? 1.6503 1.9157 1.1420 -0.2532 -0.1017 0.1169  99  PHE D CZ  
5585  N N   . GLY D 100 ? 1.6937 1.7797 0.9880 -0.2422 -0.0970 -0.0340 100 GLY D N   
5586  C CA  . GLY D 100 ? 1.7130 1.7667 1.0067 -0.2399 -0.1105 -0.0498 100 GLY D CA  
5587  C C   . GLY D 100 ? 1.7920 1.8377 1.1058 -0.2366 -0.1090 -0.0571 100 GLY D C   
5588  O O   . GLY D 100 ? 1.7770 1.8335 1.1006 -0.2364 -0.0972 -0.0506 100 GLY D O   
5589  N N   . GLN D 101 ? 1.7749 1.8031 1.1030 -0.2353 -0.1245 -0.0659 101 GLN D N   
5590  C CA  . GLN D 101 ? 1.7644 1.7908 1.1214 -0.2358 -0.1268 -0.0703 101 GLN D CA  
5591  C C   . GLN D 101 ? 1.7886 1.8152 1.1585 -0.2435 -0.1188 -0.0532 101 GLN D C   
5592  O O   . GLN D 101 ? 1.7804 1.8088 1.1607 -0.2456 -0.1111 -0.0535 101 GLN D O   
5593  C CB  . GLN D 101 ? 1.7851 1.8029 1.1698 -0.2327 -0.1524 -0.0778 101 GLN D CB  
5594  C CG  . GLN D 101 ? 2.0500 2.0591 1.4173 -0.2205 -0.1694 -0.0995 101 GLN D CG  
5595  C CD  . GLN D 101 ? 2.3908 2.3943 1.7969 -0.2132 -0.1985 -0.1172 101 GLN D CD  
5596  O OE1 . GLN D 101 ? 2.3802 2.3803 1.8327 -0.2176 -0.2231 -0.1020 101 GLN D OE1 
5597  N NE2 . GLN D 101 ? 2.2807 2.2874 1.6741 -0.1992 -0.1991 -0.1475 101 GLN D NE2 
5598  N N   . GLY D 102 ? 1.7322 1.7553 1.0996 -0.2458 -0.1214 -0.0389 102 GLY D N   
5599  C CA  . GLY D 102 ? 1.7177 1.7421 1.0895 -0.2461 -0.1161 -0.0276 102 GLY D CA  
5600  C C   . GLY D 102 ? 1.7623 1.7950 1.1551 -0.2427 -0.1238 -0.0162 102 GLY D C   
5601  O O   . GLY D 102 ? 1.7574 1.7993 1.1752 -0.2442 -0.1305 -0.0183 102 GLY D O   
5602  N N   . THR D 103 ? 1.7015 1.7376 1.0908 -0.2373 -0.1229 -0.0003 103 THR D N   
5603  C CA  . THR D 103 ? 1.6741 1.7312 1.0852 -0.2287 -0.1279 0.0205  103 THR D CA  
5604  C C   . THR D 103 ? 1.6992 1.7674 1.0940 -0.2169 -0.1176 0.0223  103 THR D C   
5605  O O   . THR D 103 ? 1.7010 1.7613 1.0767 -0.2104 -0.1116 0.0226  103 THR D O   
5606  C CB  . THR D 103 ? 1.7436 1.8004 1.1713 -0.2264 -0.1385 0.0450  103 THR D CB  
5607  O OG1 . THR D 103 ? 1.7053 1.7808 1.1353 -0.2132 -0.1317 0.0699  103 THR D OG1 
5608  C CG2 . THR D 103 ? 1.7402 1.7690 1.1484 -0.2353 -0.1400 0.0383  103 THR D CG2 
5609  N N   . LYS D 104 ? 1.6326 1.7197 1.0372 -0.2134 -0.1181 0.0222  104 LYS D N   
5610  C CA  . LYS D 104 ? 1.6342 1.7333 1.0180 -0.1975 -0.1125 0.0204  104 LYS D CA  
5611  C C   . LYS D 104 ? 1.6707 1.8047 1.0583 -0.1777 -0.1087 0.0469  104 LYS D C   
5612  O O   . LYS D 104 ? 1.6414 1.8076 1.0665 -0.1778 -0.1146 0.0754  104 LYS D O   
5613  C CB  . LYS D 104 ? 1.6567 1.7651 1.0495 -0.2024 -0.1156 0.0146  104 LYS D CB  
5614  C CG  . LYS D 104 ? 1.7559 1.8962 1.1356 -0.1830 -0.1139 0.0220  104 LYS D CG  
5615  C CD  . LYS D 104 ? 1.7964 1.9114 1.1298 -0.1643 -0.1144 -0.0011 104 LYS D CD  
5616  C CE  . LYS D 104 ? 1.7100 1.8587 1.0211 -0.1390 -0.1140 0.0016  104 LYS D CE  
5617  N NZ  . LYS D 104 ? 1.7141 1.8332 0.9809 -0.1156 -0.1217 -0.0270 104 LYS D NZ  
5618  N N   . VAL D 105 ? 1.6442 1.7744 0.9997 -0.1587 -0.1015 0.0398  105 VAL D N   
5619  C CA  . VAL D 105 ? 1.6453 1.8109 0.9972 -0.1330 -0.0933 0.0643  105 VAL D CA  
5620  C C   . VAL D 105 ? 1.7078 1.9073 1.0378 -0.1091 -0.0906 0.0592  105 VAL D C   
5621  O O   . VAL D 105 ? 1.7332 1.9088 1.0272 -0.0988 -0.0938 0.0267  105 VAL D O   
5622  C CB  . VAL D 105 ? 1.7033 1.8452 1.0373 -0.1257 -0.0874 0.0587  105 VAL D CB  
5623  C CG1 . VAL D 105 ? 1.7101 1.8901 1.0437 -0.0970 -0.0758 0.0892  105 VAL D CG1 
5624  C CG2 . VAL D 105 ? 1.6823 1.7919 1.0357 -0.1529 -0.0919 0.0631  105 VAL D CG2 
5625  N N   . GLU D 106 ? 1.6322 1.8889 0.9906 -0.1017 -0.0896 0.0929  106 GLU D N   
5626  C CA  . GLU D 106 ? 1.6392 1.9425 0.9813 -0.0799 -0.0869 0.0956  106 GLU D CA  
5627  C C   . GLU D 106 ? 1.7019 2.0679 1.0337 -0.0402 -0.0736 0.1270  106 GLU D C   
5628  O O   . GLU D 106 ? 1.6632 2.0516 1.0274 -0.0357 -0.0690 0.1659  106 GLU D O   
5629  C CB  . GLU D 106 ? 1.6205 1.9549 1.0097 -0.1023 -0.0967 0.1124  106 GLU D CB  
5630  C CG  . GLU D 106 ? 1.7176 2.1059 1.1801 -0.1099 -0.1038 0.1636  106 GLU D CG  
5631  C CD  . GLU D 106 ? 1.9236 2.3546 1.4471 -0.1306 -0.1176 0.1827  106 GLU D CD  
5632  O OE1 . GLU D 106 ? 1.7621 2.1531 1.2851 -0.1566 -0.1237 0.1521  106 GLU D OE1 
5633  O OE2 . GLU D 106 ? 1.8711 2.3788 1.4539 -0.1222 -0.1241 0.2336  106 GLU D OE2 
5634  N N   . ILE D 107 ? 1.6874 2.0817 0.9736 -0.0088 -0.0689 0.1118  107 ILE D N   
5635  C CA  . ILE D 107 ? 1.7095 2.1732 0.9746 0.0381  -0.0535 0.1380  107 ILE D CA  
5636  C C   . ILE D 107 ? 1.7321 2.2859 1.0593 0.0380  -0.0518 0.2018  107 ILE D C   
5637  O O   . ILE D 107 ? 1.7163 2.2970 1.0655 0.0217  -0.0614 0.2057  107 ILE D O   
5638  C CB  . ILE D 107 ? 1.8093 2.2746 1.0011 0.0747  -0.0541 0.0952  107 ILE D CB  
5639  C CG1 . ILE D 107 ? 1.8558 2.2289 1.0066 0.0703  -0.0677 0.0337  107 ILE D CG1 
5640  C CG2 . ILE D 107 ? 1.8587 2.4003 1.0197 0.1314  -0.0351 0.1185  107 ILE D CG2 
5641  C CD1 . ILE D 107 ? 2.0360 2.3740 1.1449 0.0745  -0.0881 -0.0118 107 ILE D CD1 
5642  N N   . LYS D 108 ? 1.6719 2.2720 1.0383 0.0536  -0.0431 0.2565  108 LYS D N   
5643  C CA  . LYS D 108 ? 1.6287 2.3219 1.0738 0.0564  -0.0475 0.3299  108 LYS D CA  
5644  C C   . LYS D 108 ? 1.7194 2.5151 1.1417 0.1012  -0.0332 0.3551  108 LYS D C   
5645  O O   . LYS D 108 ? 1.7620 2.5793 1.1262 0.1477  -0.0126 0.3509  108 LYS D O   
5646  C CB  . LYS D 108 ? 1.6359 2.3348 1.1326 0.0599  -0.0472 0.3836  108 LYS D CB  
5647  C CG  . LYS D 108 ? 1.7730 2.5415 1.3790 0.0484  -0.0677 0.4601  108 LYS D CG  
5648  C CD  . LYS D 108 ? 1.9391 2.6765 1.5969 0.0409  -0.0784 0.5024  108 LYS D CD  
5649  C CE  . LYS D 108 ? 2.2092 2.9778 1.8478 0.0833  -0.0540 0.5436  108 LYS D CE  
5650  N NZ  . LYS D 108 ? 2.3272 3.0350 2.0014 0.0677  -0.0648 0.5704  108 LYS D NZ  
5651  N N   . ARG D 109 ? 1.6494 2.5103 1.1175 0.0875  -0.0448 0.3794  109 ARG D N   
5652  C CA  . ARG D 109 ? 1.6587 2.6293 1.1132 0.1244  -0.0344 0.4079  109 ARG D CA  
5653  C C   . ARG D 109 ? 1.6518 2.7313 1.2215 0.1079  -0.0501 0.4861  109 ARG D C   
5654  O O   . ARG D 109 ? 1.5965 2.6547 1.2556 0.0667  -0.0734 0.5091  109 ARG D O   
5655  C CB  . ARG D 109 ? 1.6696 2.6006 1.0371 0.1275  -0.0348 0.3382  109 ARG D CB  
5656  C CG  . ARG D 109 ? 1.7127 2.5956 1.1146 0.0716  -0.0569 0.3130  109 ARG D CG  
5657  C CD  . ARG D 109 ? 1.8266 2.7295 1.1758 0.0809  -0.0593 0.2853  109 ARG D CD  
5658  N NE  . ARG D 109 ? 1.9076 2.9446 1.3136 0.0895  -0.0586 0.3494  109 ARG D NE  
5659  C CZ  . ARG D 109 ? 2.0248 3.1261 1.3793 0.1202  -0.0534 0.3470  109 ARG D CZ  
5660  N NH1 . ARG D 109 ? 1.9062 2.9417 1.1475 0.1487  -0.0518 0.2790  109 ARG D NH1 
5661  N NH2 . ARG D 109 ? 1.7469 2.9819 1.1669 0.1242  -0.0534 0.4139  109 ARG D NH2 
5662  N N   . THR D 110 ? 1.4802 1.6872 1.4762 -0.2133 -0.0734 0.2611  110 THR D N   
5663  C CA  . THR D 110 ? 1.4913 1.7246 1.5065 -0.2234 -0.0556 0.2924  110 THR D CA  
5664  C C   . THR D 110 ? 1.5665 1.7759 1.5395 -0.2335 -0.0680 0.3071  110 THR D C   
5665  O O   . THR D 110 ? 1.5740 1.7635 1.4917 -0.2316 -0.0760 0.2955  110 THR D O   
5666  C CB  . THR D 110 ? 1.6238 1.9066 1.6312 -0.2191 -0.0179 0.3002  110 THR D CB  
5667  O OG1 . THR D 110 ? 1.6149 1.8929 1.5539 -0.2107 -0.0136 0.2827  110 THR D OG1 
5668  C CG2 . THR D 110 ? 1.6507 1.9695 1.7195 -0.2103 0.0005  0.2930  110 THR D CG2 
5669  N N   . VAL D 111 ? 1.5376 1.7489 1.5423 -0.2439 -0.0716 0.3324  111 VAL D N   
5670  C CA  . VAL D 111 ? 1.5444 1.7357 1.5211 -0.2523 -0.0846 0.3466  111 VAL D CA  
5671  C C   . VAL D 111 ? 1.6641 1.8716 1.5858 -0.2540 -0.0665 0.3540  111 VAL D C   
5672  O O   . VAL D 111 ? 1.6694 1.9119 1.5942 -0.2558 -0.0412 0.3690  111 VAL D O   
5673  C CB  . VAL D 111 ? 1.5808 1.7735 1.6095 -0.2618 -0.0937 0.3723  111 VAL D CB  
5674  C CG1 . VAL D 111 ? 1.5674 1.7242 1.5765 -0.2642 -0.1203 0.3724  111 VAL D CG1 
5675  C CG2 . VAL D 111 ? 1.5715 1.7660 1.6707 -0.2601 -0.1020 0.3708  111 VAL D CG2 
5676  N N   . ALA D 112 ? 1.6535 1.8362 1.5246 -0.2530 -0.0793 0.3433  112 ALA D N   
5677  C CA  . ALA D 112 ? 1.6909 1.8813 1.5089 -0.2541 -0.0692 0.3479  112 ALA D CA  
5678  C C   . ALA D 112 ? 1.7706 1.9458 1.5754 -0.2627 -0.0827 0.3636  112 ALA D C   
5679  O O   . ALA D 112 ? 1.7493 1.8980 1.5521 -0.2624 -0.1026 0.3547  112 ALA D O   
5680  C CB  . ALA D 112 ? 1.7096 1.8865 1.4854 -0.2451 -0.0741 0.3218  112 ALA D CB  
5681  N N   . ALA D 113 ? 1.7694 1.9620 1.5659 -0.2700 -0.0721 0.3874  113 ALA D N   
5682  C CA  . ALA D 113 ? 1.7756 1.9554 1.5629 -0.2778 -0.0862 0.4031  113 ALA D CA  
5683  C C   . ALA D 113 ? 1.8549 2.0195 1.5895 -0.2746 -0.0936 0.3899  113 ALA D C   
5684  O O   . ALA D 113 ? 1.8772 2.0491 1.5756 -0.2692 -0.0829 0.3797  113 ALA D O   
5685  C CB  . ALA D 113 ? 1.8067 2.0085 1.6008 -0.2878 -0.0744 0.4347  113 ALA D CB  
5686  N N   . PRO D 114 ? 1.8042 1.9484 1.5368 -0.2767 -0.1127 0.3885  114 PRO D N   
5687  C CA  . PRO D 114 ? 1.8062 1.9387 1.4987 -0.2747 -0.1202 0.3778  114 PRO D CA  
5688  C C   . PRO D 114 ? 1.8823 2.0210 1.5416 -0.2789 -0.1178 0.3920  114 PRO D C   
5689  O O   . PRO D 114 ? 1.8867 2.0347 1.5551 -0.2859 -0.1149 0.4147  114 PRO D O   
5690  C CB  . PRO D 114 ? 1.8074 1.9227 1.5165 -0.2750 -0.1378 0.3739  114 PRO D CB  
5691  C CG  . PRO D 114 ? 1.8615 1.9787 1.6094 -0.2785 -0.1428 0.3892  114 PRO D CG  
5692  C CD  . PRO D 114 ? 1.8093 1.9409 1.5783 -0.2792 -0.1292 0.3948  114 PRO D CD  
5693  N N   . SER D 115 ? 1.8581 1.9889 1.4793 -0.2750 -0.1221 0.3795  115 SER D N   
5694  C CA  . SER D 115 ? 1.8915 2.0205 1.4747 -0.2773 -0.1261 0.3890  115 SER D CA  
5695  C C   . SER D 115 ? 1.9553 2.0686 1.5507 -0.2817 -0.1470 0.3914  115 SER D C   
5696  O O   . SER D 115 ? 1.9470 2.0496 1.5406 -0.2788 -0.1568 0.3762  115 SER D O   
5697  C CB  . SER D 115 ? 1.9447 2.0702 1.4850 -0.2685 -0.1244 0.3706  115 SER D CB  
5698  O OG  . SER D 115 ? 2.0169 2.1581 1.5562 -0.2610 -0.1053 0.3610  115 SER D OG  
5699  N N   . VAL D 116 ? 1.9202 2.0341 1.5363 -0.2887 -0.1538 0.4109  116 VAL D N   
5700  C CA  . VAL D 116 ? 1.9080 2.0107 1.5450 -0.2910 -0.1731 0.4126  116 VAL D CA  
5701  C C   . VAL D 116 ? 2.0144 2.1081 1.6242 -0.2944 -0.1876 0.4203  116 VAL D C   
5702  O O   . VAL D 116 ? 2.0550 2.1496 1.6408 -0.2992 -0.1870 0.4379  116 VAL D O   
5703  C CB  . VAL D 116 ? 1.9361 2.0401 1.6169 -0.2942 -0.1791 0.4251  116 VAL D CB  
5704  C CG1 . VAL D 116 ? 1.9193 2.0141 1.6242 -0.2928 -0.1984 0.4216  116 VAL D CG1 
5705  C CG2 . VAL D 116 ? 1.9105 2.0188 1.6179 -0.2899 -0.1696 0.4161  116 VAL D CG2 
5706  N N   . PHE D 117 ? 1.9682 2.0530 1.5827 -0.2923 -0.2012 0.4086  117 PHE D N   
5707  C CA  . PHE D 117 ? 1.9948 2.0679 1.5930 -0.2949 -0.2203 0.4132  117 PHE D CA  
5708  C C   . PHE D 117 ? 2.0395 2.1112 1.6789 -0.2948 -0.2353 0.4093  117 PHE D C   
5709  O O   . PHE D 117 ? 2.0020 2.0808 1.6662 -0.2907 -0.2285 0.3965  117 PHE D O   
5710  C CB  . PHE D 117 ? 2.0378 2.1029 1.5969 -0.2909 -0.2227 0.4004  117 PHE D CB  
5711  C CG  . PHE D 117 ? 2.0802 2.1498 1.5992 -0.2864 -0.2059 0.3965  117 PHE D CG  
5712  C CD1 . PHE D 117 ? 2.1016 2.1759 1.6209 -0.2803 -0.1941 0.3786  117 PHE D CD1 
5713  C CD2 . PHE D 117 ? 2.1508 2.2212 1.6320 -0.2878 -0.2017 0.4110  117 PHE D CD2 
5714  C CE1 . PHE D 117 ? 2.1364 2.2174 1.6240 -0.2737 -0.1786 0.3719  117 PHE D CE1 
5715  C CE2 . PHE D 117 ? 2.2109 2.2912 1.6563 -0.2814 -0.1821 0.4060  117 PHE D CE2 
5716  C CZ  . PHE D 117 ? 2.1658 2.2522 1.6173 -0.2734 -0.1708 0.3849  117 PHE D CZ  
5717  N N   . ILE D 118 ? 2.0380 2.1010 1.6839 -0.2986 -0.2556 0.4203  118 ILE D N   
5718  C CA  . ILE D 118 ? 2.0323 2.0970 1.7221 -0.2971 -0.2705 0.4160  118 ILE D CA  
5719  C C   . ILE D 118 ? 2.1185 2.1727 1.7989 -0.2990 -0.2893 0.4142  118 ILE D C   
5720  O O   . ILE D 118 ? 2.1480 2.1861 1.7919 -0.3025 -0.3028 0.4236  118 ILE D O   
5721  C CB  . ILE D 118 ? 2.0749 2.1388 1.7999 -0.2982 -0.2828 0.4270  118 ILE D CB  
5722  C CG1 . ILE D 118 ? 2.0579 2.1293 1.8345 -0.2924 -0.2942 0.4167  118 ILE D CG1 
5723  C CG2 . ILE D 118 ? 2.1341 2.1825 1.8351 -0.3065 -0.2997 0.4490  118 ILE D CG2 
5724  C CD1 . ILE D 118 ? 2.1116 2.1874 1.9313 -0.2866 -0.2995 0.4154  118 ILE D CD1 
5725  N N   . PHE D 119 ? 2.0710 2.1344 1.7829 -0.2965 -0.2900 0.4028  119 PHE D N   
5726  C CA  . PHE D 119 ? 2.0915 2.1468 1.8080 -0.2988 -0.3096 0.4013  119 PHE D CA  
5727  C C   . PHE D 119 ? 2.1354 2.1981 1.9071 -0.2986 -0.3258 0.4034  119 PHE D C   
5728  O O   . PHE D 119 ? 2.0977 2.1822 1.9126 -0.2943 -0.3133 0.3962  119 PHE D O   
5729  C CB  . PHE D 119 ? 2.1076 2.1678 1.8209 -0.2984 -0.3012 0.3904  119 PHE D CB  
5730  C CG  . PHE D 119 ? 2.1492 2.1977 1.8093 -0.2971 -0.2938 0.3852  119 PHE D CG  
5731  C CD1 . PHE D 119 ? 2.1721 2.2303 1.8236 -0.2942 -0.2702 0.3784  119 PHE D CD1 
5732  C CD2 . PHE D 119 ? 2.2190 2.2457 1.8379 -0.2969 -0.3123 0.3851  119 PHE D CD2 
5733  C CE1 . PHE D 119 ? 2.2013 2.2510 1.8100 -0.2913 -0.2637 0.3712  119 PHE D CE1 
5734  C CE2 . PHE D 119 ? 2.2773 2.2956 1.8476 -0.2923 -0.3047 0.3766  119 PHE D CE2 
5735  C CZ  . PHE D 119 ? 2.2307 2.2622 1.7994 -0.2895 -0.2798 0.3695  119 PHE D CZ  
5736  N N   . PRO D 120 ? 2.1266 2.1712 1.8971 -0.3021 -0.3544 0.4120  120 PRO D N   
5737  C CA  . PRO D 120 ? 2.1171 2.1692 1.9479 -0.3012 -0.3726 0.4126  120 PRO D CA  
5738  C C   . PRO D 120 ? 2.1446 2.2128 2.0167 -0.3013 -0.3728 0.4053  120 PRO D C   
5739  O O   . PRO D 120 ? 2.1492 2.2103 1.9947 -0.3045 -0.3716 0.4031  120 PRO D O   
5740  C CB  . PRO D 120 ? 2.1823 2.2046 1.9914 -0.3060 -0.4060 0.4252  120 PRO D CB  
5741  C CG  . PRO D 120 ? 2.2700 2.2710 2.0083 -0.3087 -0.4069 0.4275  120 PRO D CG  
5742  C CD  . PRO D 120 ? 2.1917 2.2078 1.9047 -0.3059 -0.3724 0.4208  120 PRO D CD  
5743  N N   . PRO D 121 ? 2.0704 2.1621 2.0101 -0.2976 -0.3739 0.4018  121 PRO D N   
5744  C CA  . PRO D 121 ? 2.0499 2.1624 2.0343 -0.2996 -0.3711 0.3993  121 PRO D CA  
5745  C C   . PRO D 121 ? 2.1175 2.2074 2.1049 -0.3068 -0.4051 0.4059  121 PRO D C   
5746  O O   . PRO D 121 ? 2.1404 2.2042 2.1172 -0.3079 -0.4346 0.4113  121 PRO D O   
5747  C CB  . PRO D 121 ? 2.0510 2.1961 2.1068 -0.2918 -0.3639 0.3938  121 PRO D CB  
5748  C CG  . PRO D 121 ? 2.1069 2.2465 2.1518 -0.2843 -0.3616 0.3901  121 PRO D CG  
5749  C CD  . PRO D 121 ? 2.0793 2.1811 2.0615 -0.2909 -0.3785 0.3999  121 PRO D CD  
5750  N N   . SER D 122 ? 2.0649 2.1620 2.0668 -0.3120 -0.4042 0.4065  122 SER D N   
5751  C CA  . SER D 122 ? 2.0887 2.1629 2.0999 -0.3183 -0.4401 0.4116  122 SER D CA  
5752  C C   . SER D 122 ? 2.1255 2.2111 2.2126 -0.3186 -0.4622 0.4159  122 SER D C   
5753  O O   . SER D 122 ? 2.0887 2.2132 2.2359 -0.3146 -0.4414 0.4139  122 SER D O   
5754  C CB  . SER D 122 ? 2.1295 2.2115 2.1501 -0.3245 -0.4346 0.4127  122 SER D CB  
5755  O OG  . SER D 122 ? 2.2754 2.3318 2.3083 -0.3300 -0.4742 0.4169  122 SER D OG  
5756  N N   . ASP D 123 ? 2.1129 2.1640 2.1966 -0.3218 -0.5053 0.4203  123 ASP D N   
5757  C CA  . ASP D 123 ? 2.1149 2.1707 2.2732 -0.3225 -0.5339 0.4243  123 ASP D CA  
5758  C C   . ASP D 123 ? 2.1469 2.2368 2.3903 -0.3278 -0.5311 0.4285  123 ASP D C   
5759  O O   . ASP D 123 ? 2.1268 2.2380 2.4516 -0.3269 -0.5426 0.4308  123 ASP D O   
5760  C CB  . ASP D 123 ? 2.1883 2.1917 2.3103 -0.3243 -0.5839 0.4283  123 ASP D CB  
5761  C CG  . ASP D 123 ? 2.3104 2.2878 2.3614 -0.3207 -0.5850 0.4295  123 ASP D CG  
5762  O OD1 . ASP D 123 ? 2.3002 2.2875 2.3847 -0.3175 -0.5862 0.4309  123 ASP D OD1 
5763  O OD2 . ASP D 123 ? 2.4058 2.3548 2.3708 -0.3208 -0.5844 0.4295  123 ASP D OD2 
5764  N N   . GLU D 124 ? 2.1059 2.2034 2.3343 -0.3334 -0.5149 0.4306  124 GLU D N   
5765  C CA  . GLU D 124 ? 2.0886 2.2213 2.3916 -0.3413 -0.5065 0.4394  124 GLU D CA  
5766  C C   . GLU D 124 ? 2.0932 2.2842 2.4393 -0.3367 -0.4568 0.4385  124 GLU D C   
5767  O O   . GLU D 124 ? 2.0726 2.3059 2.5034 -0.3396 -0.4469 0.4460  124 GLU D O   
5768  C CB  . GLU D 124 ? 2.1175 2.2321 2.3800 -0.3490 -0.5090 0.4425  124 GLU D CB  
5769  C CG  . GLU D 124 ? 2.3004 2.3683 2.5553 -0.3540 -0.5623 0.4447  124 GLU D CG  
5770  C CD  . GLU D 124 ? 2.5731 2.5848 2.7321 -0.3467 -0.5891 0.4337  124 GLU D CD  
5771  O OE1 . GLU D 124 ? 2.6168 2.5946 2.7773 -0.3454 -0.6327 0.4338  124 GLU D OE1 
5772  O OE2 . GLU D 124 ? 2.3902 2.3917 2.4729 -0.3421 -0.5674 0.4255  124 GLU D OE2 
5773  N N   . GLN D 125 ? 2.0311 2.2241 2.3179 -0.3287 -0.4260 0.4289  125 GLN D N   
5774  C CA  . GLN D 125 ? 1.9936 2.2322 2.2996 -0.3206 -0.3810 0.4234  125 GLN D CA  
5775  C C   . GLN D 125 ? 2.0181 2.2787 2.3815 -0.3095 -0.3828 0.4161  125 GLN D C   
5776  O O   . GLN D 125 ? 1.9903 2.2986 2.4021 -0.3018 -0.3516 0.4120  125 GLN D O   
5777  C CB  . GLN D 125 ? 2.0047 2.2275 2.2273 -0.3154 -0.3583 0.4147  125 GLN D CB  
5778  C CG  . GLN D 125 ? 2.1153 2.3777 2.3438 -0.3071 -0.3140 0.4084  125 GLN D CG  
5779  C CD  . GLN D 125 ? 2.3219 2.5647 2.4735 -0.3032 -0.2972 0.4007  125 GLN D CD  
5780  O OE1 . GLN D 125 ? 2.2872 2.4962 2.3913 -0.3009 -0.3125 0.3965  125 GLN D OE1 
5781  N NE2 . GLN D 125 ? 2.1755 2.4407 2.3157 -0.3024 -0.2650 0.4000  125 GLN D NE2 
5782  N N   . LEU D 126 ? 1.9831 2.2081 2.3397 -0.3078 -0.4206 0.4141  126 LEU D N   
5783  C CA  . LEU D 126 ? 1.9716 2.2078 2.3839 -0.2979 -0.4335 0.4072  126 LEU D CA  
5784  C C   . LEU D 126 ? 1.9775 2.2542 2.4948 -0.2987 -0.4368 0.4113  126 LEU D C   
5785  O O   . LEU D 126 ? 1.9586 2.2711 2.5382 -0.2865 -0.4252 0.4017  126 LEU D O   
5786  C CB  . LEU D 126 ? 2.0076 2.1896 2.3842 -0.3002 -0.4797 0.4095  126 LEU D CB  
5787  C CG  . LEU D 126 ? 2.0755 2.2373 2.4013 -0.2925 -0.4783 0.4032  126 LEU D CG  
5788  C CD1 . LEU D 126 ? 2.0834 2.2200 2.3127 -0.2968 -0.4628 0.4056  126 LEU D CD1 
5789  C CD2 . LEU D 126 ? 2.1424 2.2660 2.4730 -0.2937 -0.5257 0.4076  126 LEU D CD2 
5790  N N   . LYS D 127 ? 1.9189 2.1914 2.4590 -0.3122 -0.4526 0.4250  127 LYS D N   
5791  C CA  . LYS D 127 ? 1.9042 2.2147 2.5489 -0.3169 -0.4580 0.4342  127 LYS D CA  
5792  C C   . LYS D 127 ? 1.9256 2.3061 2.6209 -0.3123 -0.4041 0.4350  127 LYS D C   
5793  O O   . LYS D 127 ? 1.9201 2.3467 2.7125 -0.3099 -0.3982 0.4381  127 LYS D O   
5794  C CB  . LYS D 127 ? 1.9483 2.2300 2.5957 -0.3335 -0.4914 0.4499  127 LYS D CB  
5795  C CG  . LYS D 127 ? 2.0128 2.3089 2.7675 -0.3392 -0.5233 0.4597  127 LYS D CG  
5796  C CD  . LYS D 127 ? 2.0679 2.3474 2.8378 -0.3560 -0.5481 0.4768  127 LYS D CD  
5797  C CE  . LYS D 127 ? 2.1075 2.4123 2.9997 -0.3629 -0.5735 0.4894  127 LYS D CE  
5798  N NZ  . LYS D 127 ? 2.2113 2.4952 3.1224 -0.3797 -0.6042 0.5069  127 LYS D NZ  
5799  N N   . SER D 128 ? 1.8624 2.2517 2.4925 -0.3104 -0.3649 0.4321  128 SER D N   
5800  C CA  . SER D 128 ? 1.8403 2.2913 2.5004 -0.3054 -0.3128 0.4333  128 SER D CA  
5801  C C   . SER D 128 ? 1.8773 2.3636 2.5635 -0.2830 -0.2881 0.4126  128 SER D C   
5802  O O   . SER D 128 ? 1.8630 2.4092 2.6221 -0.2759 -0.2595 0.4125  128 SER D O   
5803  C CB  . SER D 128 ? 1.8814 2.3233 2.4619 -0.3119 -0.2860 0.4382  128 SER D CB  
5804  O OG  . SER D 128 ? 1.9879 2.4004 2.4865 -0.3009 -0.2793 0.4214  128 SER D OG  
5805  N N   . GLY D 129 ? 1.8377 2.2877 2.4669 -0.2718 -0.3000 0.3957  129 GLY D N   
5806  C CA  . GLY D 129 ? 1.8303 2.3020 2.4769 -0.2492 -0.2855 0.3733  129 GLY D CA  
5807  C C   . GLY D 129 ? 1.8710 2.3342 2.4390 -0.2385 -0.2582 0.3602  129 GLY D C   
5808  O O   . GLY D 129 ? 1.8649 2.3429 2.4422 -0.2181 -0.2475 0.3397  129 GLY D O   
5809  N N   . THR D 130 ? 1.8189 2.2574 2.3128 -0.2513 -0.2493 0.3708  130 THR D N   
5810  C CA  . THR D 130 ? 1.8070 2.2314 2.2235 -0.2445 -0.2273 0.3614  130 THR D CA  
5811  C C   . THR D 130 ? 1.8473 2.2172 2.1909 -0.2600 -0.2494 0.3718  130 THR D C   
5812  O O   . THR D 130 ? 1.8436 2.2073 2.1763 -0.2758 -0.2515 0.3871  130 THR D O   
5813  C CB  . THR D 130 ? 1.8967 2.3667 2.3109 -0.2404 -0.1805 0.3622  130 THR D CB  
5814  O OG1 . THR D 130 ? 1.8844 2.4070 2.3654 -0.2228 -0.1596 0.3501  130 THR D OG1 
5815  C CG2 . THR D 130 ? 1.8764 2.3285 2.2111 -0.2334 -0.1612 0.3524  130 THR D CG2 
5816  N N   . ALA D 131 ? 1.7973 2.1291 2.0960 -0.2552 -0.2674 0.3637  131 ALA D N   
5817  C CA  . ALA D 131 ? 1.7977 2.0814 2.0270 -0.2669 -0.2860 0.3718  131 ALA D CA  
5818  C C   . ALA D 131 ? 1.8319 2.1009 1.9981 -0.2610 -0.2687 0.3638  131 ALA D C   
5819  O O   . ALA D 131 ? 1.8244 2.1001 1.9974 -0.2467 -0.2624 0.3508  131 ALA D O   
5820  C CB  . ALA D 131 ? 1.8241 2.0735 2.0575 -0.2704 -0.3269 0.3758  131 ALA D CB  
5821  N N   . SER D 132 ? 1.7815 2.0291 1.8903 -0.2711 -0.2641 0.3706  132 SER D N   
5822  C CA  . SER D 132 ? 1.7705 2.0040 1.8232 -0.2672 -0.2486 0.3645  132 SER D CA  
5823  C C   . SER D 132 ? 1.8217 2.0153 1.8220 -0.2738 -0.2672 0.3699  132 SER D C   
5824  O O   . SER D 132 ? 1.8272 2.0017 1.8128 -0.2839 -0.2859 0.3789  132 SER D O   
5825  C CB  . SER D 132 ? 1.8096 2.0567 1.8412 -0.2710 -0.2225 0.3660  132 SER D CB  
5826  O OG  . SER D 132 ? 1.9164 2.2042 1.9920 -0.2658 -0.2013 0.3645  132 SER D OG  
5827  N N   . VAL D 133 ? 1.7791 1.9610 1.7516 -0.2675 -0.2620 0.3646  133 VAL D N   
5828  C CA  . VAL D 133 ? 1.7946 1.9458 1.7195 -0.2731 -0.2731 0.3714  133 VAL D CA  
5829  C C   . VAL D 133 ? 1.8479 1.9959 1.7316 -0.2730 -0.2516 0.3675  133 VAL D C   
5830  O O   . VAL D 133 ? 1.8272 1.9893 1.7190 -0.2646 -0.2341 0.3578  133 VAL D O   
5831  C CB  . VAL D 133 ? 1.8537 1.9932 1.7902 -0.2685 -0.2897 0.3733  133 VAL D CB  
5832  C CG1 . VAL D 133 ? 1.8687 1.9814 1.7573 -0.2765 -0.2982 0.3856  133 VAL D CG1 
5833  C CG2 . VAL D 133 ? 1.8604 2.0024 1.8436 -0.2676 -0.3138 0.3756  133 VAL D CG2 
5834  N N   . VAL D 134 ? 1.8292 1.9580 1.6685 -0.2809 -0.2541 0.3733  134 VAL D N   
5835  C CA  . VAL D 134 ? 1.8258 1.9501 1.6296 -0.2811 -0.2370 0.3689  134 VAL D CA  
5836  C C   . VAL D 134 ? 1.9004 2.0087 1.6730 -0.2817 -0.2378 0.3735  134 VAL D C   
5837  O O   . VAL D 134 ? 1.9173 2.0127 1.6724 -0.2864 -0.2514 0.3829  134 VAL D O   
5838  C CB  . VAL D 134 ? 1.8768 1.9973 1.6615 -0.2877 -0.2358 0.3687  134 VAL D CB  
5839  C CG1 . VAL D 134 ? 1.8642 1.9829 1.6238 -0.2864 -0.2189 0.3620  134 VAL D CG1 
5840  C CG2 . VAL D 134 ? 1.8700 2.0077 1.6928 -0.2905 -0.2379 0.3704  134 VAL D CG2 
5841  N N   . CYS D 135 ? 1.8549 1.9647 1.6210 -0.2771 -0.2234 0.3680  135 CYS D N   
5842  C CA  . CYS D 135 ? 1.8628 1.9632 1.6095 -0.2780 -0.2204 0.3733  135 CYS D CA  
5843  C C   . CYS D 135 ? 1.8946 1.9921 1.6127 -0.2787 -0.2064 0.3671  135 CYS D C   
5844  O O   . CYS D 135 ? 1.8815 1.9810 1.6049 -0.2741 -0.1965 0.3588  135 CYS D O   
5845  C CB  . CYS D 135 ? 1.8669 1.9692 1.6411 -0.2713 -0.2214 0.3716  135 CYS D CB  
5846  S SG  . CYS D 135 ? 1.9303 2.0239 1.6958 -0.2745 -0.2196 0.3827  135 CYS D SG  
5847  N N   . LEU D 136 ? 1.8506 1.9413 1.5381 -0.2830 -0.2084 0.3691  136 LEU D N   
5848  C CA  . LEU D 136 ? 1.8407 1.9277 1.5028 -0.2823 -0.1990 0.3609  136 LEU D CA  
5849  C C   . LEU D 136 ? 1.8833 1.9714 1.5366 -0.2806 -0.1877 0.3634  136 LEU D C   
5850  O O   . LEU D 136 ? 1.8956 1.9847 1.5409 -0.2830 -0.1883 0.3755  136 LEU D O   
5851  C CB  . LEU D 136 ? 1.8612 1.9393 1.4953 -0.2844 -0.2089 0.3590  136 LEU D CB  
5852  C CG  . LEU D 136 ? 1.9308 2.0032 1.5321 -0.2811 -0.2029 0.3502  136 LEU D CG  
5853  C CD1 . LEU D 136 ? 1.9177 1.9885 1.5262 -0.2798 -0.1989 0.3382  136 LEU D CD1 
5854  C CD2 . LEU D 136 ? 1.9932 2.0539 1.5623 -0.2803 -0.2169 0.3485  136 LEU D CD2 
5855  N N   . LEU D 137 ? 1.8223 1.9105 1.4785 -0.2773 -0.1781 0.3536  137 LEU D N   
5856  C CA  . LEU D 137 ? 1.8175 1.9086 1.4755 -0.2753 -0.1675 0.3543  137 LEU D CA  
5857  C C   . LEU D 137 ? 1.8702 1.9589 1.5071 -0.2725 -0.1617 0.3421  137 LEU D C   
5858  O O   . LEU D 137 ? 1.8565 1.9402 1.5013 -0.2699 -0.1604 0.3315  137 LEU D O   
5859  C CB  . LEU D 137 ? 1.7985 1.8877 1.4851 -0.2719 -0.1670 0.3507  137 LEU D CB  
5860  C CG  . LEU D 137 ? 1.8542 1.9451 1.5676 -0.2720 -0.1728 0.3617  137 LEU D CG  
5861  C CD1 . LEU D 137 ? 1.8535 1.9449 1.5764 -0.2718 -0.1835 0.3638  137 LEU D CD1 
5862  C CD2 . LEU D 137 ? 1.8736 1.9583 1.6098 -0.2663 -0.1744 0.3546  137 LEU D CD2 
5863  N N   . ASN D 138 ? 1.8404 1.9302 1.4484 -0.2717 -0.1609 0.3421  138 ASN D N   
5864  C CA  . ASN D 138 ? 1.8459 1.9325 1.4340 -0.2661 -0.1585 0.3268  138 ASN D CA  
5865  C C   . ASN D 138 ? 1.8820 1.9790 1.4799 -0.2615 -0.1432 0.3228  138 ASN D C   
5866  O O   . ASN D 138 ? 1.8769 1.9874 1.4840 -0.2631 -0.1317 0.3361  138 ASN D O   
5867  C CB  . ASN D 138 ? 1.8939 1.9762 1.4445 -0.2633 -0.1652 0.3240  138 ASN D CB  
5868  C CG  . ASN D 138 ? 2.2325 2.3004 1.7703 -0.2595 -0.1794 0.3067  138 ASN D CG  
5869  O OD1 . ASN D 138 ? 2.1425 2.2083 1.6808 -0.2537 -0.1770 0.2919  138 ASN D OD1 
5870  N ND2 . ASN D 138 ? 2.1637 2.2199 1.6933 -0.2628 -0.1976 0.3085  138 ASN D ND2 
5871  N N   . ASN D 139 ? 1.8308 1.9211 1.4322 -0.2566 -0.1452 0.3059  139 ASN D N   
5872  C CA  . ASN D 139 ? 1.8250 1.9220 1.4408 -0.2504 -0.1353 0.2958  139 ASN D CA  
5873  C C   . ASN D 139 ? 1.8399 1.9511 1.4885 -0.2524 -0.1225 0.3084  139 ASN D C   
5874  O O   . ASN D 139 ? 1.8508 1.9806 1.4982 -0.2533 -0.1086 0.3215  139 ASN D O   
5875  C CB  . ASN D 139 ? 1.8932 1.9980 1.4823 -0.2407 -0.1288 0.2829  139 ASN D CB  
5876  C CG  . ASN D 139 ? 2.2692 2.3551 1.8335 -0.2369 -0.1476 0.2665  139 ASN D CG  
5877  O OD1 . ASN D 139 ? 2.2311 2.3151 1.7621 -0.2328 -0.1520 0.2636  139 ASN D OD1 
5878  N ND2 . ASN D 139 ? 2.1677 2.2370 1.7473 -0.2384 -0.1619 0.2565  139 ASN D ND2 
5879  N N   . PHE D 140 ? 1.7569 1.8579 1.4345 -0.2533 -0.1291 0.3052  140 PHE D N   
5880  C CA  . PHE D 140 ? 1.7353 1.8431 1.4508 -0.2547 -0.1245 0.3149  140 PHE D CA  
5881  C C   . PHE D 140 ? 1.7516 1.8459 1.4922 -0.2509 -0.1328 0.3020  140 PHE D C   
5882  O O   . PHE D 140 ? 1.7389 1.8150 1.4650 -0.2491 -0.1443 0.2882  140 PHE D O   
5883  C CB  . PHE D 140 ? 1.7490 1.8531 1.4752 -0.2606 -0.1312 0.3309  140 PHE D CB  
5884  C CG  . PHE D 140 ? 1.7567 1.8418 1.4751 -0.2606 -0.1456 0.3246  140 PHE D CG  
5885  C CD1 . PHE D 140 ? 1.7810 1.8508 1.5169 -0.2575 -0.1555 0.3178  140 PHE D CD1 
5886  C CD2 . PHE D 140 ? 1.7846 1.8683 1.4789 -0.2633 -0.1493 0.3264  140 PHE D CD2 
5887  C CE1 . PHE D 140 ? 1.7836 1.8400 1.5073 -0.2562 -0.1647 0.3126  140 PHE D CE1 
5888  C CE2 . PHE D 140 ? 1.8054 1.8784 1.4971 -0.2631 -0.1584 0.3222  140 PHE D CE2 
5889  C CZ  . PHE D 140 ? 1.7687 1.8298 1.4726 -0.2592 -0.1640 0.3154  140 PHE D CZ  
5890  N N   . TYR D 141 ? 1.6981 1.8001 1.4783 -0.2506 -0.1293 0.3082  141 TYR D N   
5891  C CA  . TYR D 141 ? 1.6916 1.7781 1.5007 -0.2468 -0.1410 0.2972  141 TYR D CA  
5892  C C   . TYR D 141 ? 1.7734 1.8599 1.6263 -0.2490 -0.1465 0.3102  141 TYR D C   
5893  O O   . TYR D 141 ? 1.7699 1.8805 1.6475 -0.2528 -0.1332 0.3267  141 TYR D O   
5894  C CB  . TYR D 141 ? 1.7051 1.8019 1.5265 -0.2404 -0.1337 0.2831  141 TYR D CB  
5895  C CG  . TYR D 141 ? 1.7099 1.7853 1.5585 -0.2364 -0.1510 0.2694  141 TYR D CG  
5896  C CD1 . TYR D 141 ? 1.7387 1.7860 1.5624 -0.2348 -0.1687 0.2543  141 TYR D CD1 
5897  C CD2 . TYR D 141 ? 1.7082 1.7906 1.6097 -0.2351 -0.1515 0.2733  141 TYR D CD2 
5898  C CE1 . TYR D 141 ? 1.7407 1.7643 1.5852 -0.2317 -0.1878 0.2429  141 TYR D CE1 
5899  C CE2 . TYR D 141 ? 1.7149 1.7738 1.6422 -0.2311 -0.1715 0.2601  141 TYR D CE2 
5900  C CZ  . TYR D 141 ? 1.7850 1.8131 1.6806 -0.2291 -0.1900 0.2445  141 TYR D CZ  
5901  O OH  . TYR D 141 ? 1.7749 1.7759 1.6921 -0.2257 -0.2128 0.2329  141 TYR D OH  
5902  N N   . PRO D 142 ? 1.7628 1.8216 1.6256 -0.2466 -0.1673 0.3041  142 PRO D N   
5903  C CA  . PRO D 142 ? 1.7774 1.8072 1.6097 -0.2431 -0.1829 0.2883  142 PRO D CA  
5904  C C   . PRO D 142 ? 1.8517 1.8755 1.6456 -0.2448 -0.1841 0.2908  142 PRO D C   
5905  O O   . PRO D 142 ? 1.8443 1.8827 1.6393 -0.2479 -0.1769 0.3032  142 PRO D O   
5906  C CB  . PRO D 142 ? 1.8035 1.8095 1.6656 -0.2387 -0.2033 0.2835  142 PRO D CB  
5907  C CG  . PRO D 142 ? 1.8515 1.8688 1.7518 -0.2407 -0.2034 0.2995  142 PRO D CG  
5908  C CD  . PRO D 142 ? 1.7850 1.8388 1.6922 -0.2472 -0.1787 0.3143  142 PRO D CD  
5909  N N   . ARG D 143 ? 1.8306 1.8342 1.5936 -0.2434 -0.1934 0.2806  143 ARG D N   
5910  C CA  . ARG D 143 ? 1.8367 1.8381 1.5678 -0.2447 -0.1928 0.2827  143 ARG D CA  
5911  C C   . ARG D 143 ? 1.8928 1.8927 1.6336 -0.2404 -0.1973 0.2874  143 ARG D C   
5912  O O   . ARG D 143 ? 1.8848 1.8938 1.6127 -0.2409 -0.1926 0.2917  143 ARG D O   
5913  C CB  . ARG D 143 ? 1.8585 1.8383 1.5612 -0.2444 -0.2025 0.2741  143 ARG D CB  
5914  C CG  . ARG D 143 ? 1.9921 1.9776 1.6652 -0.2484 -0.1970 0.2785  143 ARG D CG  
5915  C CD  . ARG D 143 ? 2.1361 2.1021 1.7824 -0.2504 -0.2057 0.2751  143 ARG D CD  
5916  N NE  . ARG D 143 ? 2.1991 2.1759 1.8266 -0.2580 -0.1993 0.2828  143 ARG D NE  
5917  C CZ  . ARG D 143 ? 2.3434 2.3084 1.9496 -0.2640 -0.2052 0.2858  143 ARG D CZ  
5918  N NH1 . ARG D 143 ? 2.1619 2.1012 1.7570 -0.2629 -0.2187 0.2806  143 ARG D NH1 
5919  N NH2 . ARG D 143 ? 2.1741 2.1522 1.7726 -0.2723 -0.1998 0.2958  143 ARG D NH2 
5920  N N   . GLU D 144 ? 1.8565 1.8441 1.6249 -0.2353 -0.2093 0.2855  144 GLU D N   
5921  C CA  . GLU D 144 ? 1.8576 1.8367 1.6429 -0.2287 -0.2213 0.2865  144 GLU D CA  
5922  C C   . GLU D 144 ? 1.8914 1.8923 1.6984 -0.2333 -0.2143 0.3016  144 GLU D C   
5923  O O   . GLU D 144 ? 1.8732 1.8850 1.7143 -0.2385 -0.2124 0.3134  144 GLU D O   
5924  C CB  . GLU D 144 ? 1.8827 1.8402 1.6985 -0.2233 -0.2403 0.2812  144 GLU D CB  
5925  C CG  . GLU D 144 ? 2.0079 1.9383 1.8001 -0.2187 -0.2521 0.2668  144 GLU D CG  
5926  C CD  . GLU D 144 ? 2.1302 2.0631 1.9284 -0.2246 -0.2474 0.2647  144 GLU D CD  
5927  O OE1 . GLU D 144 ? 1.9678 1.9137 1.7409 -0.2304 -0.2333 0.2655  144 GLU D OE1 
5928  O OE2 . GLU D 144 ? 1.9415 1.8610 1.7714 -0.2224 -0.2611 0.2606  144 GLU D OE2 
5929  N N   . ALA D 145 ? 1.8554 1.8639 1.6435 -0.2323 -0.2103 0.3026  145 ALA D N   
5930  C CA  . ALA D 145 ? 1.8525 1.8774 1.6555 -0.2366 -0.2076 0.3161  145 ALA D CA  
5931  C C   . ALA D 145 ? 1.9209 1.9440 1.7150 -0.2285 -0.2136 0.3094  145 ALA D C   
5932  O O   . ALA D 145 ? 1.9296 1.9459 1.6979 -0.2215 -0.2121 0.2961  145 ALA D O   
5933  C CB  . ALA D 145 ? 1.8543 1.8993 1.6419 -0.2468 -0.1907 0.3262  145 ALA D CB  
5934  N N   . LYS D 146 ? 1.8744 1.9048 1.6910 -0.2294 -0.2203 0.3190  146 LYS D N   
5935  C CA  . LYS D 146 ? 1.8795 1.9112 1.6963 -0.2201 -0.2269 0.3110  146 LYS D CA  
5936  C C   . LYS D 146 ? 1.9546 2.0013 1.7838 -0.2275 -0.2269 0.3252  146 LYS D C   
5937  O O   . LYS D 146 ? 1.9507 1.9987 1.8019 -0.2360 -0.2332 0.3423  146 LYS D O   
5938  C CB  . LYS D 146 ? 1.9178 1.9298 1.7552 -0.2052 -0.2488 0.2985  146 LYS D CB  
5939  C CG  . LYS D 146 ? 2.0436 2.0578 1.8807 -0.1903 -0.2553 0.2840  146 LYS D CG  
5940  C CD  . LYS D 146 ? 2.1317 2.1544 1.9301 -0.1830 -0.2378 0.2697  146 LYS D CD  
5941  C CE  . LYS D 146 ? 2.1844 2.2212 1.9885 -0.1705 -0.2370 0.2589  146 LYS D CE  
5942  N NZ  . LYS D 146 ? 2.2378 2.2898 2.0085 -0.1664 -0.2156 0.2507  146 LYS D NZ  
5943  N N   . VAL D 147 ? 1.9387 1.9967 1.7555 -0.2246 -0.2207 0.3195  147 VAL D N   
5944  C CA  . VAL D 147 ? 1.9494 2.0192 1.7775 -0.2302 -0.2239 0.3301  147 VAL D CA  
5945  C C   . VAL D 147 ? 2.0470 2.1171 1.8992 -0.2162 -0.2374 0.3182  147 VAL D C   
5946  O O   . VAL D 147 ? 2.0505 2.1234 1.8939 -0.2030 -0.2320 0.3000  147 VAL D O   
5947  C CB  . VAL D 147 ? 1.9913 2.0746 1.7944 -0.2387 -0.2091 0.3337  147 VAL D CB  
5948  C CG1 . VAL D 147 ? 1.9916 2.0819 1.8051 -0.2459 -0.2167 0.3468  147 VAL D CG1 
5949  C CG2 . VAL D 147 ? 1.9855 2.0667 1.7633 -0.2476 -0.1974 0.3383  147 VAL D CG2 
5950  N N   . GLN D 148 ? 2.0338 2.1013 1.9159 -0.2185 -0.2554 0.3286  148 GLN D N   
5951  C CA  . GLN D 148 ? 2.0510 2.1178 1.9636 -0.2044 -0.2731 0.3165  148 GLN D CA  
5952  C C   . GLN D 148 ? 2.1023 2.1791 2.0296 -0.2119 -0.2796 0.3281  148 GLN D C   
5953  O O   . GLN D 148 ? 2.0977 2.1673 2.0351 -0.2248 -0.2923 0.3493  148 GLN D O   
5954  C CB  . GLN D 148 ? 2.0848 2.1310 2.0294 -0.1983 -0.2995 0.3168  148 GLN D CB  
5955  C CG  . GLN D 148 ? 2.3496 2.3806 2.2856 -0.1872 -0.3010 0.3018  148 GLN D CG  
5956  C CD  . GLN D 148 ? 2.6245 2.6352 2.5945 -0.1905 -0.3262 0.3132  148 GLN D CD  
5957  O OE1 . GLN D 148 ? 2.5622 2.5707 2.5316 -0.2047 -0.3205 0.3310  148 GLN D OE1 
5958  N NE2 . GLN D 148 ? 2.5420 2.5383 2.5468 -0.1772 -0.3556 0.3034  148 GLN D NE2 
5959  N N   . TRP D 149 ? 2.3467 2.0663 2.4570 -0.1731 -0.1563 0.1255  149 TRP D N   
5960  C CA  . TRP D 149 ? 2.3482 2.0677 2.4529 -0.1717 -0.1540 0.1270  149 TRP D CA  
5961  C C   . TRP D 149 ? 2.4098 2.1304 2.5154 -0.1716 -0.1498 0.1272  149 TRP D C   
5962  O O   . TRP D 149 ? 2.4052 2.1271 2.5112 -0.1728 -0.1490 0.1271  149 TRP D O   
5963  C CB  . TRP D 149 ? 2.3305 2.0505 2.4289 -0.1728 -0.1583 0.1293  149 TRP D CB  
5964  C CG  . TRP D 149 ? 2.3403 2.0590 2.4343 -0.1723 -0.1634 0.1303  149 TRP D CG  
5965  C CD1 . TRP D 149 ? 2.3769 2.0974 2.4716 -0.1743 -0.1706 0.1288  149 TRP D CD1 
5966  C CD2 . TRP D 149 ? 2.3400 2.0542 2.4273 -0.1710 -0.1625 0.1337  149 TRP D CD2 
5967  N NE1 . TRP D 149 ? 2.3683 2.0874 2.4575 -0.1728 -0.1744 0.1306  149 TRP D NE1 
5968  C CE2 . TRP D 149 ? 2.3872 2.1014 2.4705 -0.1707 -0.1687 0.1339  149 TRP D CE2 
5969  C CE3 . TRP D 149 ? 2.3575 2.0660 2.4410 -0.1718 -0.1576 0.1369  149 TRP D CE3 
5970  C CZ2 . TRP D 149 ? 2.3807 2.0890 2.4544 -0.1700 -0.1689 0.1378  149 TRP D CZ2 
5971  C CZ3 . TRP D 149 ? 2.3800 2.0809 2.4539 -0.1729 -0.1578 0.1411  149 TRP D CZ3 
5972  C CH2 . TRP D 149 ? 2.3883 2.0889 2.4565 -0.1714 -0.1627 0.1417  149 TRP D CH2 
5973  N N   . LYS D 150 ? 2.3730 2.0923 2.4790 -0.1715 -0.1475 0.1271  150 LYS D N   
5974  C CA  . LYS D 150 ? 2.3690 2.0899 2.4773 -0.1726 -0.1457 0.1269  150 LYS D CA  
5975  C C   . LYS D 150 ? 2.4138 2.1315 2.5220 -0.1756 -0.1461 0.1306  150 LYS D C   
5976  O O   . LYS D 150 ? 2.4086 2.1208 2.5135 -0.1789 -0.1465 0.1321  150 LYS D O   
5977  C CB  . LYS D 150 ? 2.4011 2.1229 2.5104 -0.1727 -0.1449 0.1237  150 LYS D CB  
5978  C CG  . LYS D 150 ? 2.5857 2.3097 2.6960 -0.1701 -0.1449 0.1226  150 LYS D CG  
5979  C CD  . LYS D 150 ? 2.7042 2.4295 2.8145 -0.1698 -0.1448 0.1202  150 LYS D CD  
5980  C CE  . LYS D 150 ? 2.8292 2.5550 2.9398 -0.1675 -0.1454 0.1218  150 LYS D CE  
5981  N NZ  . LYS D 150 ? 2.9375 2.6652 3.0471 -0.1668 -0.1458 0.1200  150 LYS D NZ  
5982  N N   . VAL D 151 ? 2.3668 2.0862 2.4787 -0.1757 -0.1457 0.1328  151 VAL D N   
5983  C CA  . VAL D 151 ? 2.3623 2.0781 2.4776 -0.1790 -0.1466 0.1382  151 VAL D CA  
5984  C C   . VAL D 151 ? 2.4031 2.1216 2.5281 -0.1814 -0.1464 0.1367  151 VAL D C   
5985  O O   . VAL D 151 ? 2.3987 2.1216 2.5300 -0.1795 -0.1441 0.1351  151 VAL D O   
5986  C CB  . VAL D 151 ? 2.4107 2.1268 2.5257 -0.1775 -0.1466 0.1419  151 VAL D CB  
5987  C CG1 . VAL D 151 ? 2.4074 2.1191 2.5290 -0.1810 -0.1474 0.1491  151 VAL D CG1 
5988  C CG2 . VAL D 151 ? 2.4108 2.1250 2.5147 -0.1759 -0.1495 0.1432  151 VAL D CG2 
5989  N N   . ASP D 152 ? 2.3488 2.0643 2.4742 -0.1867 -0.1492 0.1364  152 ASP D N   
5990  C CA  . ASP D 152 ? 2.3367 2.0549 2.4703 -0.1910 -0.1521 0.1345  152 ASP D CA  
5991  C C   . ASP D 152 ? 2.3748 2.1016 2.5083 -0.1854 -0.1507 0.1288  152 ASP D C   
5992  O O   . ASP D 152 ? 2.3669 2.0975 2.5080 -0.1840 -0.1495 0.1287  152 ASP D O   
5993  C CB  . ASP D 152 ? 2.3543 2.0701 2.5012 -0.1956 -0.1540 0.1402  152 ASP D CB  
5994  C CG  . ASP D 152 ? 2.4333 2.1379 2.5787 -0.2023 -0.1562 0.1489  152 ASP D CG  
5995  O OD1 . ASP D 152 ? 2.4397 2.1410 2.5758 -0.1985 -0.1539 0.1522  152 ASP D OD1 
5996  O OD2 . ASP D 152 ? 2.4783 2.1766 2.6317 -0.2122 -0.1613 0.1533  152 ASP D OD2 
5997  N N   . ASN D 153 ? 2.3252 2.0535 2.4497 -0.1826 -0.1502 0.1252  153 ASN D N   
5998  C CA  . ASN D 153 ? 2.3188 2.0523 2.4391 -0.1780 -0.1495 0.1224  153 ASN D CA  
5999  C C   . ASN D 153 ? 2.3689 2.1019 2.4874 -0.1738 -0.1450 0.1238  153 ASN D C   
6000  O O   . ASN D 153 ? 2.3597 2.0924 2.4719 -0.1714 -0.1442 0.1237  153 ASN D O   
6001  C CB  . ASN D 153 ? 2.3201 2.0588 2.4429 -0.1798 -0.1538 0.1205  153 ASN D CB  
6002  C CG  . ASN D 153 ? 2.5855 2.3278 2.6996 -0.1754 -0.1542 0.1195  153 ASN D CG  
6003  O OD1 . ASN D 153 ? 2.5035 2.2455 2.6152 -0.1724 -0.1509 0.1214  153 ASN D OD1 
6004  N ND2 . ASN D 153 ? 2.4818 2.2261 2.5898 -0.1761 -0.1582 0.1173  153 ASN D ND2 
6005  N N   . ALA D 154 ? 2.3322 2.0642 2.4565 -0.1745 -0.1425 0.1256  154 ALA D N   
6006  C CA  . ALA D 154 ? 2.3353 2.0656 2.4576 -0.1734 -0.1381 0.1259  154 ALA D CA  
6007  C C   . ALA D 154 ? 2.3771 2.1046 2.4933 -0.1732 -0.1389 0.1264  154 ALA D C   
6008  O O   . ALA D 154 ? 2.3665 2.0927 2.4832 -0.1735 -0.1405 0.1280  154 ALA D O   
6009  C CB  . ALA D 154 ? 2.3465 2.0769 2.4783 -0.1748 -0.1351 0.1270  154 ALA D CB  
6010  N N   . LEU D 155 ? 2.3354 2.0609 2.4454 -0.1733 -0.1389 0.1260  155 LEU D N   
6011  C CA  . LEU D 155 ? 2.3355 2.0581 2.4421 -0.1746 -0.1414 0.1263  155 LEU D CA  
6012  C C   . LEU D 155 ? 2.3879 2.1087 2.4930 -0.1781 -0.1409 0.1261  155 LEU D C   
6013  O O   . LEU D 155 ? 2.3881 2.1064 2.4915 -0.1815 -0.1371 0.1254  155 LEU D O   
6014  C CB  . LEU D 155 ? 2.3367 2.0559 2.4396 -0.1758 -0.1424 0.1277  155 LEU D CB  
6015  C CG  . LEU D 155 ? 2.3890 2.1101 2.4929 -0.1724 -0.1439 0.1279  155 LEU D CG  
6016  C CD1 . LEU D 155 ? 2.3850 2.1079 2.4850 -0.1710 -0.1429 0.1287  155 LEU D CD1 
6017  C CD2 . LEU D 155 ? 2.4189 2.1360 2.5239 -0.1736 -0.1466 0.1301  155 LEU D CD2 
6018  N N   . GLN D 156 ? 2.3377 2.0595 2.4424 -0.1777 -0.1445 0.1265  156 GLN D N   
6019  C CA  . GLN D 156 ? 2.3326 2.0540 2.4344 -0.1809 -0.1460 0.1262  156 GLN D CA  
6020  C C   . GLN D 156 ? 2.3766 2.0957 2.4738 -0.1861 -0.1519 0.1249  156 GLN D C   
6021  O O   . GLN D 156 ? 2.3676 2.0867 2.4660 -0.1850 -0.1565 0.1254  156 GLN D O   
6022  C CB  . GLN D 156 ? 2.3460 2.0693 2.4476 -0.1780 -0.1481 0.1292  156 GLN D CB  
6023  C CG  . GLN D 156 ? 2.4865 2.2103 2.5952 -0.1760 -0.1438 0.1317  156 GLN D CG  
6024  C CD  . GLN D 156 ? 2.6803 2.4046 2.7948 -0.1778 -0.1382 0.1302  156 GLN D CD  
6025  O OE1 . GLN D 156 ? 2.6068 2.3308 2.7188 -0.1806 -0.1373 0.1287  156 GLN D OE1 
6026  N NE2 . GLN D 156 ? 2.5731 2.2984 2.6960 -0.1768 -0.1345 0.1300  156 GLN D NE2 
6027  N N   . SER D 157 ? 2.7067 2.6841 2.0441 -0.0795 -0.0510 0.0413  157 SER D N   
6028  C CA  . SER D 157 ? 2.6442 2.6574 2.0014 -0.1291 -0.0407 0.0274  157 SER D CA  
6029  C C   . SER D 157 ? 2.6522 2.7408 2.0779 -0.1270 -0.0414 0.0078  157 SER D C   
6030  O O   . SER D 157 ? 2.6810 2.7777 2.1358 -0.0935 -0.0328 0.0000  157 SER D O   
6031  C CB  . SER D 157 ? 2.7165 2.6669 2.0309 -0.1597 -0.0048 0.0227  157 SER D CB  
6032  O OG  . SER D 157 ? 2.7806 2.7587 2.1033 -0.2082 -0.0001 0.0127  157 SER D OG  
6033  N N   . GLY D 158 ? 2.5391 2.6791 1.9863 -0.1628 -0.0502 -0.0018 158 GLY D N   
6034  C CA  . GLY D 158 ? 2.4956 2.7039 1.9969 -0.1722 -0.0490 -0.0250 158 GLY D CA  
6035  C C   . GLY D 158 ? 2.4868 2.7680 2.0217 -0.1596 -0.0785 -0.0263 158 GLY D C   
6036  O O   . GLY D 158 ? 2.4401 2.7656 1.9882 -0.1911 -0.0828 -0.0394 158 GLY D O   
6037  N N   . ASN D 159 ? 2.4457 2.7358 1.9884 -0.1146 -0.0981 -0.0128 159 ASN D N   
6038  C CA  . ASN D 159 ? 2.4103 2.7692 1.9810 -0.0991 -0.1275 -0.0107 159 ASN D CA  
6039  C C   . ASN D 159 ? 2.4061 2.7632 1.9451 -0.1308 -0.1431 0.0032  159 ASN D C   
6040  O O   . ASN D 159 ? 2.3681 2.7871 1.9271 -0.1423 -0.1575 -0.0027 159 ASN D O   
6041  C CB  . ASN D 159 ? 2.4501 2.8024 2.0240 -0.0433 -0.1459 0.0049  159 ASN D CB  
6042  C CG  . ASN D 159 ? 2.7188 2.9728 2.2330 -0.0268 -0.1400 0.0273  159 ASN D CG  
6043  O OD1 . ASN D 159 ? 2.6051 2.8055 2.0703 -0.0571 -0.1348 0.0385  159 ASN D OD1 
6044  N ND2 . ASN D 159 ? 2.6711 2.8978 2.1854 0.0218  -0.1387 0.0318  159 ASN D ND2 
6045  N N   . SER D 160 ? 2.3542 2.6407 1.8426 -0.1464 -0.1375 0.0193  160 SER D N   
6046  C CA  . SER D 160 ? 2.3124 2.5876 1.7696 -0.1753 -0.1486 0.0318  160 SER D CA  
6047  C C   . SER D 160 ? 2.3001 2.5949 1.7586 -0.2186 -0.1389 0.0180  160 SER D C   
6048  O O   . SER D 160 ? 2.2991 2.5781 1.7582 -0.2349 -0.1185 0.0045  160 SER D O   
6049  C CB  . SER D 160 ? 2.3810 2.5774 1.7861 -0.1765 -0.1436 0.0483  160 SER D CB  
6050  O OG  . SER D 160 ? 2.4881 2.6415 1.8761 -0.1909 -0.1171 0.0401  160 SER D OG  
6051  N N   . GLN D 161 ? 2.2075 2.5306 1.6605 -0.2377 -0.1530 0.0223  161 GLN D N   
6052  C CA  . GLN D 161 ? 2.1663 2.4998 1.6087 -0.2758 -0.1473 0.0124  161 GLN D CA  
6053  C C   . GLN D 161 ? 2.1982 2.5087 1.6084 -0.2901 -0.1585 0.0302  161 GLN D C   
6054  O O   . GLN D 161 ? 2.1964 2.5179 1.6053 -0.2789 -0.1736 0.0436  161 GLN D O   
6055  C CB  . GLN D 161 ? 2.1590 2.5567 1.6273 -0.2854 -0.1485 -0.0065 161 GLN D CB  
6056  C CG  . GLN D 161 ? 2.2812 2.7015 1.7812 -0.2828 -0.1322 -0.0320 161 GLN D CG  
6057  C CD  . GLN D 161 ? 2.4303 2.9225 1.9603 -0.2867 -0.1339 -0.0540 161 GLN D CD  
6058  O OE1 . GLN D 161 ? 2.3362 2.8484 1.8482 -0.3159 -0.1340 -0.0622 161 GLN D OE1 
6059  N NE2 . GLN D 161 ? 2.3129 2.8453 1.8870 -0.2582 -0.1330 -0.0667 161 GLN D NE2 
6060  N N   . GLU D 162 ? 2.1364 2.4150 1.5213 -0.3144 -0.1512 0.0301  162 GLU D N   
6061  C CA  . GLU D 162 ? 2.1153 2.3731 1.4739 -0.3270 -0.1598 0.0438  162 GLU D CA  
6062  C C   . GLU D 162 ? 2.1080 2.3828 1.4550 -0.3515 -0.1622 0.0398  162 GLU D C   
6063  O O   . GLU D 162 ? 2.1000 2.3841 1.4461 -0.3662 -0.1542 0.0250  162 GLU D O   
6064  C CB  . GLU D 162 ? 2.1512 2.3610 1.4872 -0.3322 -0.1517 0.0473  162 GLU D CB  
6065  C CG  . GLU D 162 ? 2.3462 2.5217 1.6713 -0.3115 -0.1515 0.0569  162 GLU D CG  
6066  C CD  . GLU D 162 ? 2.6957 2.8237 1.9913 -0.3216 -0.1386 0.0559  162 GLU D CD  
6067  O OE1 . GLU D 162 ? 2.5699 2.6908 1.8499 -0.3403 -0.1415 0.0570  162 GLU D OE1 
6068  O OE2 . GLU D 162 ? 2.7136 2.8121 2.0004 -0.3110 -0.1241 0.0527  162 GLU D OE2 
6069  N N   . SER D 163 ? 2.0273 2.2994 1.3601 -0.3569 -0.1719 0.0525  163 SER D N   
6070  C CA  . SER D 163 ? 1.9994 2.2772 1.3131 -0.3768 -0.1733 0.0524  163 SER D CA  
6071  C C   . SER D 163 ? 2.0286 2.2823 1.3264 -0.3812 -0.1793 0.0659  163 SER D C   
6072  O O   . SER D 163 ? 2.0265 2.2691 1.3277 -0.3720 -0.1842 0.0760  163 SER D O   
6073  C CB  . SER D 163 ? 2.0296 2.3454 1.3467 -0.3811 -0.1746 0.0495  163 SER D CB  
6074  O OG  . SER D 163 ? 2.1213 2.4328 1.4094 -0.4018 -0.1708 0.0469  163 SER D OG  
6075  N N   . VAL D 164 ? 1.9736 2.2163 1.2520 -0.3949 -0.1788 0.0647  164 VAL D N   
6076  C CA  . VAL D 164 ? 1.9630 2.1880 1.2310 -0.3989 -0.1831 0.0735  164 VAL D CA  
6077  C C   . VAL D 164 ? 2.0059 2.2304 1.2522 -0.4096 -0.1832 0.0759  164 VAL D C   
6078  O O   . VAL D 164 ? 2.0145 2.2383 1.2432 -0.4161 -0.1803 0.0680  164 VAL D O   
6079  C CB  . VAL D 164 ? 2.0176 2.2238 1.2855 -0.3990 -0.1827 0.0690  164 VAL D CB  
6080  C CG1 . VAL D 164 ? 2.0221 2.2133 1.2974 -0.3916 -0.1805 0.0709  164 VAL D CG1 
6081  C CG2 . VAL D 164 ? 2.0261 2.2314 1.2892 -0.4036 -0.1788 0.0578  164 VAL D CG2 
6082  N N   . THR D 165 ? 1.9468 2.1644 1.1892 -0.4127 -0.1850 0.0860  165 THR D N   
6083  C CA  . THR D 165 ? 1.9441 2.1534 1.1629 -0.4208 -0.1824 0.0902  165 THR D CA  
6084  C C   . THR D 165 ? 1.9764 2.1715 1.1942 -0.4167 -0.1872 0.0879  165 THR D C   
6085  O O   . THR D 165 ? 1.9659 2.1605 1.2028 -0.4129 -0.1905 0.0848  165 THR D O   
6086  C CB  . THR D 165 ? 2.0860 2.2958 1.3020 -0.4290 -0.1787 0.1019  165 THR D CB  
6087  O OG1 . THR D 165 ? 2.0902 2.2920 1.3254 -0.4266 -0.1829 0.1059  165 THR D OG1 
6088  C CG2 . THR D 165 ? 2.0794 2.3118 1.2912 -0.4356 -0.1744 0.1035  165 THR D CG2 
6089  N N   . GLU D 166 ? 1.9335 2.1164 1.1254 -0.4172 -0.1870 0.0881  166 GLU D N   
6090  C CA  . GLU D 166 ? 1.9318 2.1075 1.1237 -0.4091 -0.1944 0.0858  166 GLU D CA  
6091  C C   . GLU D 166 ? 1.9505 2.1278 1.1621 -0.4088 -0.1935 0.0894  166 GLU D C   
6092  O O   . GLU D 166 ? 1.9297 2.1066 1.1494 -0.4174 -0.1871 0.0954  166 GLU D O   
6093  C CB  . GLU D 166 ? 1.9765 2.1313 1.1278 -0.4059 -0.1953 0.0863  166 GLU D CB  
6094  C CG  . GLU D 166 ? 2.1706 2.3198 1.3080 -0.4030 -0.2038 0.0774  166 GLU D CG  
6095  C CD  . GLU D 166 ? 2.5323 2.6779 1.6539 -0.4148 -0.1975 0.0700  166 GLU D CD  
6096  O OE1 . GLU D 166 ? 2.4876 2.6530 1.6367 -0.4194 -0.1921 0.0678  166 GLU D OE1 
6097  O OE2 . GLU D 166 ? 2.5069 2.6278 1.5873 -0.4191 -0.1983 0.0647  166 GLU D OE2 
6098  N N   . GLN D 167 ? 1.8957 2.0765 1.1153 -0.4000 -0.2004 0.0840  167 GLN D N   
6099  C CA  . GLN D 167 ? 1.8738 2.0593 1.1149 -0.4009 -0.1985 0.0815  167 GLN D CA  
6100  C C   . GLN D 167 ? 1.9074 2.0748 1.1331 -0.4065 -0.1878 0.0927  167 GLN D C   
6101  O O   . GLN D 167 ? 1.9265 2.0775 1.1202 -0.4012 -0.1852 0.0994  167 GLN D O   
6102  C CB  . GLN D 167 ? 1.8942 2.0960 1.1474 -0.3875 -0.2094 0.0709  167 GLN D CB  
6103  C CG  . GLN D 167 ? 1.9312 2.1521 1.2181 -0.3932 -0.2076 0.0573  167 GLN D CG  
6104  C CD  . GLN D 167 ? 2.0579 2.3084 1.3627 -0.3802 -0.2191 0.0432  167 GLN D CD  
6105  O OE1 . GLN D 167 ? 2.0148 2.2664 1.3072 -0.3617 -0.2299 0.0472  167 GLN D OE1 
6106  N NE2 . GLN D 167 ? 1.8871 2.1615 1.2180 -0.3902 -0.2169 0.0250  167 GLN D NE2 
6107  N N   . ASP D 168 ? 1.8334 1.9975 1.0741 -0.4204 -0.1794 0.0942  168 ASP D N   
6108  C CA  . ASP D 168 ? 1.8295 1.9751 1.0557 -0.4320 -0.1659 0.1051  168 ASP D CA  
6109  C C   . ASP D 168 ? 1.8825 2.0204 1.1070 -0.4218 -0.1624 0.1034  168 ASP D C   
6110  O O   . ASP D 168 ? 1.8730 2.0276 1.1246 -0.4112 -0.1701 0.0904  168 ASP D O   
6111  C CB  . ASP D 168 ? 1.8396 1.9793 1.0799 -0.4525 -0.1592 0.1062  168 ASP D CB  
6112  C CG  . ASP D 168 ? 1.9887 2.1111 1.2069 -0.4709 -0.1451 0.1209  168 ASP D CG  
6113  O OD1 . ASP D 168 ? 2.0056 2.1321 1.2102 -0.4779 -0.1451 0.1294  168 ASP D OD1 
6114  O OD2 . ASP D 168 ? 2.0756 2.1828 1.2907 -0.4793 -0.1330 0.1230  168 ASP D OD2 
6115  N N   . SER D 169 ? 1.8519 1.9651 1.0422 -0.4246 -0.1496 0.1152  169 SER D N   
6116  C CA  . SER D 169 ? 1.8691 1.9656 1.0494 -0.4119 -0.1431 0.1163  169 SER D CA  
6117  C C   . SER D 169 ? 1.9109 2.0094 1.1244 -0.4231 -0.1330 0.1104  169 SER D C   
6118  O O   . SER D 169 ? 1.9074 2.0111 1.1388 -0.4065 -0.1345 0.1020  169 SER D O   
6119  C CB  . SER D 169 ? 1.9334 1.9935 1.0569 -0.4173 -0.1262 0.1304  169 SER D CB  
6120  O OG  . SER D 169 ? 1.9916 2.0425 1.1045 -0.4474 -0.1076 0.1398  169 SER D OG  
6121  N N   . LYS D 170 ? 1.8603 1.9542 1.0810 -0.4515 -0.1230 0.1136  170 LYS D N   
6122  C CA  . LYS D 170 ? 1.8525 1.9389 1.0967 -0.4711 -0.1102 0.1072  170 LYS D CA  
6123  C C   . LYS D 170 ? 1.8908 1.9998 1.1758 -0.4749 -0.1201 0.0863  170 LYS D C   
6124  O O   . LYS D 170 ? 1.8952 2.0123 1.2080 -0.4743 -0.1155 0.0704  170 LYS D O   
6125  C CB  . LYS D 170 ? 1.8788 1.9399 1.0998 -0.5049 -0.0926 0.1219  170 LYS D CB  
6126  C CG  . LYS D 170 ? 2.0236 2.0637 1.1965 -0.5089 -0.0779 0.1403  170 LYS D CG  
6127  C CD  . LYS D 170 ? 2.1163 2.1237 1.2709 -0.5309 -0.0500 0.1484  170 LYS D CD  
6128  C CE  . LYS D 170 ? 2.2223 2.2042 1.3204 -0.5299 -0.0326 0.1626  170 LYS D CE  
6129  N NZ  . LYS D 170 ? 2.3232 2.2683 1.4013 -0.5466 -0.0026 0.1693  170 LYS D NZ  
6130  N N   . ASP D 171 ? 1.8304 1.9480 1.1166 -0.4796 -0.1312 0.0842  171 ASP D N   
6131  C CA  . ASP D 171 ? 1.8187 1.9475 1.1301 -0.4882 -0.1360 0.0633  171 ASP D CA  
6132  C C   . ASP D 171 ? 1.8378 1.9948 1.1593 -0.4693 -0.1522 0.0520  171 ASP D C   
6133  O O   . ASP D 171 ? 1.8268 1.9881 1.1586 -0.4799 -0.1529 0.0348  171 ASP D O   
6134  C CB  . ASP D 171 ? 1.8510 1.9517 1.1487 -0.5168 -0.1300 0.0672  171 ASP D CB  
6135  C CG  . ASP D 171 ? 2.0135 2.1096 1.2887 -0.5130 -0.1384 0.0844  171 ASP D CG  
6136  O OD1 . ASP D 171 ? 2.0076 2.1104 1.2684 -0.5022 -0.1394 0.0999  171 ASP D OD1 
6137  O OD2 . ASP D 171 ? 2.1456 2.2281 1.4142 -0.5223 -0.1423 0.0812  171 ASP D OD2 
6138  N N   . SER D 172 ? 1.7878 1.9590 1.1007 -0.4450 -0.1628 0.0600  172 SER D N   
6139  C CA  . SER D 172 ? 1.7807 1.9769 1.0995 -0.4291 -0.1772 0.0513  172 SER D CA  
6140  C C   . SER D 172 ? 1.8241 2.0161 1.1385 -0.4400 -0.1783 0.0478  172 SER D C   
6141  O O   . SER D 172 ? 1.8175 2.0274 1.1426 -0.4393 -0.1824 0.0317  172 SER D O   
6142  C CB  . SER D 172 ? 1.8181 2.0473 1.1659 -0.4186 -0.1833 0.0303  172 SER D CB  
6143  O OG  . SER D 172 ? 1.9138 2.1449 1.2650 -0.4020 -0.1836 0.0342  172 SER D OG  
6144  N N   . THR D 173 ? 1.7818 1.9506 1.0779 -0.4494 -0.1740 0.0627  173 THR D N   
6145  C CA  . THR D 173 ? 1.7821 1.9405 1.0704 -0.4546 -0.1751 0.0620  173 THR D CA  
6146  C C   . THR D 173 ? 1.8364 1.9963 1.1112 -0.4442 -0.1799 0.0766  173 THR D C   
6147  O O   . THR D 173 ? 1.8274 1.9850 1.0908 -0.4445 -0.1780 0.0903  173 THR D O   
6148  C CB  . THR D 173 ? 1.8746 2.0036 1.1548 -0.4752 -0.1673 0.0622  173 THR D CB  
6149  O OG1 . THR D 173 ? 1.8372 1.9553 1.1080 -0.4824 -0.1634 0.0797  173 THR D OG1 
6150  C CG2 . THR D 173 ? 1.8731 1.9970 1.1637 -0.4915 -0.1596 0.0408  173 THR D CG2 
6151  N N   . TYR D 174 ? 1.8018 1.9649 1.0761 -0.4379 -0.1832 0.0712  174 TYR D N   
6152  C CA  . TYR D 174 ? 1.7994 1.9671 1.0666 -0.4283 -0.1864 0.0791  174 TYR D CA  
6153  C C   . TYR D 174 ? 1.8685 2.0211 1.1295 -0.4303 -0.1853 0.0876  174 TYR D C   
6154  O O   . TYR D 174 ? 1.8735 2.0038 1.1295 -0.4394 -0.1827 0.0856  174 TYR D O   
6155  C CB  . TYR D 174 ? 1.8083 1.9846 1.0785 -0.4216 -0.1881 0.0681  174 TYR D CB  
6156  C CG  . TYR D 174 ? 1.8098 2.0036 1.0847 -0.4185 -0.1930 0.0596  174 TYR D CG  
6157  C CD1 . TYR D 174 ? 1.8296 2.0305 1.0949 -0.4106 -0.1989 0.0641  174 TYR D CD1 
6158  C CD2 . TYR D 174 ? 1.8205 2.0235 1.1062 -0.4238 -0.1923 0.0453  174 TYR D CD2 
6159  C CE1 . TYR D 174 ? 1.8385 2.0517 1.1034 -0.4044 -0.2069 0.0579  174 TYR D CE1 
6160  C CE2 . TYR D 174 ? 1.8302 2.0569 1.1235 -0.4175 -0.2001 0.0373  174 TYR D CE2 
6161  C CZ  . TYR D 174 ? 1.9211 2.1510 1.2031 -0.4059 -0.2090 0.0454  174 TYR D CZ  
6162  O OH  . TYR D 174 ? 1.9493 2.1987 1.2341 -0.3966 -0.2201 0.0391  174 TYR D OH  
6163  N N   . SER D 175 ? 1.8344 1.9988 1.0939 -0.4221 -0.1877 0.0951  175 SER D N   
6164  C CA  . SER D 175 ? 1.8489 2.0084 1.1063 -0.4180 -0.1903 0.1033  175 SER D CA  
6165  C C   . SER D 175 ? 1.9219 2.0966 1.1867 -0.4028 -0.1917 0.1001  175 SER D C   
6166  O O   . SER D 175 ? 1.9156 2.1092 1.1832 -0.4018 -0.1901 0.0953  175 SER D O   
6167  C CB  . SER D 175 ? 1.8873 2.0561 1.1392 -0.4273 -0.1907 0.1158  175 SER D CB  
6168  O OG  . SER D 175 ? 1.9989 2.1522 1.2445 -0.4435 -0.1859 0.1180  175 SER D OG  
6169  N N   . LEU D 176 ? 1.9006 2.0626 1.1652 -0.3913 -0.1938 0.1020  176 LEU D N   
6170  C CA  . LEU D 176 ? 1.9058 2.0808 1.1810 -0.3747 -0.1931 0.0978  176 LEU D CA  
6171  C C   . LEU D 176 ? 1.9706 2.1623 1.2535 -0.3614 -0.2010 0.1062  176 LEU D C   
6172  O O   . LEU D 176 ? 1.9843 2.1593 1.2565 -0.3614 -0.2079 0.1164  176 LEU D O   
6173  C CB  . LEU D 176 ? 1.9298 2.0731 1.1963 -0.3682 -0.1860 0.0901  176 LEU D CB  
6174  C CG  . LEU D 176 ? 1.9956 2.1474 1.2725 -0.3566 -0.1790 0.0820  176 LEU D CG  
6175  C CD1 . LEU D 176 ? 2.0095 2.1374 1.2736 -0.3650 -0.1671 0.0717  176 LEU D CD1 
6176  C CD2 . LEU D 176 ? 2.0529 2.1981 1.3337 -0.3335 -0.1811 0.0865  176 LEU D CD2 
6177  N N   . SER D 177 ? 1.9274 2.1528 1.2286 -0.3510 -0.2003 0.1001  177 SER D N   
6178  C CA  . SER D 177 ? 1.9376 2.1936 1.2543 -0.3349 -0.2084 0.1035  177 SER D CA  
6179  C C   . SER D 177 ? 2.0148 2.2818 1.3511 -0.3149 -0.2037 0.0922  177 SER D C   
6180  O O   . SER D 177 ? 2.0035 2.2946 1.3515 -0.3222 -0.1953 0.0786  177 SER D O   
6181  C CB  . SER D 177 ? 1.9560 2.2570 1.2774 -0.3496 -0.2094 0.1031  177 SER D CB  
6182  O OG  . SER D 177 ? 2.0558 2.4019 1.3983 -0.3354 -0.2159 0.1003  177 SER D OG  
6183  N N   . SER D 178 ? 2.0035 2.2453 1.3379 -0.2907 -0.2073 0.0970  178 SER D N   
6184  C CA  . SER D 178 ? 2.0188 2.2646 1.3711 -0.2682 -0.2007 0.0874  178 SER D CA  
6185  C C   . SER D 178 ? 2.0871 2.3774 1.4659 -0.2425 -0.2135 0.0887  178 SER D C   
6186  O O   . SER D 178 ? 2.1038 2.3846 1.4719 -0.2288 -0.2288 0.1031  178 SER D O   
6187  C CB  . SER D 178 ? 2.0925 2.2749 1.4183 -0.2570 -0.1924 0.0904  178 SER D CB  
6188  O OG  . SER D 178 ? 2.1901 2.3700 1.5292 -0.2433 -0.1786 0.0792  178 SER D OG  
6189  N N   . THR D 179 ? 2.0361 2.3772 1.4487 -0.2384 -0.2079 0.0721  179 THR D N   
6190  C CA  . THR D 179 ? 2.0429 2.4432 1.4895 -0.2150 -0.2192 0.0673  179 THR D CA  
6191  C C   . THR D 179 ? 2.1461 2.5426 1.6158 -0.1802 -0.2141 0.0589  179 THR D C   
6192  O O   . THR D 179 ? 2.1367 2.5300 1.6181 -0.1876 -0.1954 0.0423  179 THR D O   
6193  C CB  . THR D 179 ? 2.0660 2.5332 1.5318 -0.2397 -0.2153 0.0506  179 THR D CB  
6194  O OG1 . THR D 179 ? 2.0237 2.4778 1.4591 -0.2716 -0.2152 0.0597  179 THR D OG1 
6195  C CG2 . THR D 179 ? 2.0375 2.5783 1.5369 -0.2217 -0.2285 0.0444  179 THR D CG2 
6196  N N   . LEU D 180 ? 2.1543 2.5480 1.6276 -0.1424 -0.2306 0.0707  180 LEU D N   
6197  C CA  . LEU D 180 ? 2.1976 2.5825 1.6893 -0.1010 -0.2276 0.0659  180 LEU D CA  
6198  C C   . LEU D 180 ? 2.2492 2.7245 1.7978 -0.0776 -0.2376 0.0500  180 LEU D C   
6199  O O   . LEU D 180 ? 2.2668 2.7694 1.8254 -0.0461 -0.2612 0.0603  180 LEU D O   
6200  C CB  . LEU D 180 ? 2.2565 2.5685 1.7058 -0.0708 -0.2391 0.0885  180 LEU D CB  
6201  C CG  . LEU D 180 ? 2.3722 2.6478 1.8217 -0.0256 -0.2324 0.0874  180 LEU D CG  
6202  C CD1 . LEU D 180 ? 2.3874 2.5968 1.8100 -0.0411 -0.2010 0.0806  180 LEU D CD1 
6203  C CD2 . LEU D 180 ? 2.4620 2.6830 1.8701 0.0093  -0.2528 0.1095  180 LEU D CD2 
6204  N N   . THR D 181 ? 2.1810 2.7032 1.7650 -0.0950 -0.2196 0.0229  181 THR D N   
6205  C CA  . THR D 181 ? 2.1688 2.7834 1.8101 -0.0807 -0.2229 -0.0014 181 THR D CA  
6206  C C   . THR D 181 ? 2.2696 2.8840 1.9418 -0.0271 -0.2243 -0.0050 181 THR D C   
6207  O O   . THR D 181 ? 2.2777 2.8435 1.9469 -0.0227 -0.2019 -0.0117 181 THR D O   
6208  C CB  . THR D 181 ? 2.2088 2.8612 1.8667 -0.1237 -0.2002 -0.0322 181 THR D CB  
6209  O OG1 . THR D 181 ? 2.2040 2.7929 1.8458 -0.1372 -0.1760 -0.0375 181 THR D OG1 
6210  C CG2 . THR D 181 ? 2.1366 2.8039 1.7660 -0.1689 -0.2021 -0.0305 181 THR D CG2 
6211  N N   . LEU D 182 ? 2.2064 2.2560 2.5852 -0.0389 -0.3530 0.3929  182 LEU D N   
6212  C CA  . LEU D 182 ? 2.2216 2.2684 2.5856 -0.0276 -0.3519 0.4122  182 LEU D CA  
6213  C C   . LEU D 182 ? 2.2644 2.3329 2.6960 -0.0325 -0.3630 0.4438  182 LEU D C   
6214  O O   . LEU D 182 ? 2.2464 2.3247 2.7279 -0.0546 -0.3847 0.4385  182 LEU D O   
6215  C CB  . LEU D 182 ? 2.2365 2.2613 2.5361 -0.0449 -0.3659 0.3824  182 LEU D CB  
6216  C CG  . LEU D 182 ? 2.3170 2.3205 2.5540 -0.0253 -0.3536 0.3785  182 LEU D CG  
6217  C CD1 . LEU D 182 ? 2.3325 2.3416 2.5747 0.0061  -0.3395 0.4156  182 LEU D CD1 
6218  C CD2 . LEU D 182 ? 2.3539 2.3404 2.5558 -0.0153 -0.3436 0.3563  182 LEU D CD2 
6219  N N   . SER D 183 ? 2.2360 2.3095 2.6666 -0.0106 -0.3510 0.4766  183 SER D N   
6220  C CA  . SER D 183 ? 2.2391 2.3331 2.7310 -0.0130 -0.3594 0.5112  183 SER D CA  
6221  C C   . SER D 183 ? 2.3090 2.3951 2.7794 -0.0403 -0.3852 0.4878  183 SER D C   
6222  O O   . SER D 183 ? 2.3133 2.3790 2.7129 -0.0474 -0.3875 0.4562  183 SER D O   
6223  C CB  . SER D 183 ? 2.2981 2.3990 2.7841 0.0247  -0.3349 0.5573  183 SER D CB  
6224  O OG  . SER D 183 ? 2.4421 2.5199 2.8408 0.0341  -0.3301 0.5435  183 SER D OG  
6225  N N   . LYS D 184 ? 2.2711 2.3734 2.8067 -0.0522 -0.4045 0.5042  184 LYS D N   
6226  C CA  . LYS D 184 ? 2.2793 2.3757 2.8005 -0.0711 -0.4295 0.4828  184 LYS D CA  
6227  C C   . LYS D 184 ? 2.3485 2.4395 2.8083 -0.0598 -0.4138 0.4917  184 LYS D C   
6228  O O   . LYS D 184 ? 2.3505 2.4296 2.7627 -0.0700 -0.4237 0.4626  184 LYS D O   
6229  C CB  . LYS D 184 ? 2.3045 2.4179 2.9177 -0.0823 -0.4570 0.4988  184 LYS D CB  
6230  C CG  . LYS D 184 ? 2.4507 2.5525 3.0527 -0.0994 -0.4925 0.4615  184 LYS D CG  
6231  C CD  . LYS D 184 ? 2.5244 2.6396 3.2151 -0.1058 -0.5225 0.4786  184 LYS D CD  
6232  C CE  . LYS D 184 ? 2.6009 2.7012 3.2708 -0.1129 -0.5582 0.4390  184 LYS D CE  
6233  N NZ  . LYS D 184 ? 2.6324 2.7474 3.3316 -0.0991 -0.5518 0.4181  184 LYS D NZ  
6234  N N   . ALA D 185 ? 2.3127 2.4120 2.7717 -0.0345 -0.3885 0.5336  185 ALA D N   
6235  C CA  . ALA D 185 ? 2.3249 2.4182 2.7224 -0.0187 -0.3724 0.5488  185 ALA D CA  
6236  C C   . ALA D 185 ? 2.3854 2.4520 2.6936 -0.0177 -0.3661 0.5130  185 ALA D C   
6237  O O   . ALA D 185 ? 2.3857 2.4441 2.6451 -0.0230 -0.3670 0.5000  185 ALA D O   
6238  C CB  . ALA D 185 ? 2.3385 2.4433 2.7512 0.0165  -0.3482 0.6036  185 ALA D CB  
6239  N N   . ASP D 186 ? 2.3446 2.3984 2.6367 -0.0108 -0.3599 0.4975  186 ASP D N   
6240  C CA  . ASP D 186 ? 2.3543 2.3819 2.5761 -0.0102 -0.3572 0.4650  186 ASP D CA  
6241  C C   . ASP D 186 ? 2.4082 2.4292 2.6217 -0.0398 -0.3749 0.4234  186 ASP D C   
6242  O O   . ASP D 186 ? 2.4102 2.4133 2.5729 -0.0428 -0.3742 0.4005  186 ASP D O   
6243  C CB  . ASP D 186 ? 2.3785 2.3950 2.5902 0.0119  -0.3449 0.4650  186 ASP D CB  
6244  C CG  . ASP D 186 ? 2.5080 2.5251 2.7113 0.0546  -0.3261 0.5055  186 ASP D CG  
6245  O OD1 . ASP D 186 ? 2.5341 2.5269 2.6804 0.0803  -0.3202 0.4992  186 ASP D OD1 
6246  O OD2 . ASP D 186 ? 2.5681 2.6090 2.8243 0.0659  -0.3190 0.5454  186 ASP D OD2 
6247  N N   . TYR D 187 ? 2.3610 2.3954 2.6264 -0.0577 -0.3922 0.4163  187 TYR D N   
6248  C CA  . TYR D 187 ? 2.3601 2.3880 2.6175 -0.0773 -0.4119 0.3812  187 TYR D CA  
6249  C C   . TYR D 187 ? 2.4387 2.4660 2.6713 -0.0808 -0.4188 0.3708  187 TYR D C   
6250  O O   . TYR D 187 ? 2.4348 2.4513 2.6336 -0.0852 -0.4243 0.3445  187 TYR D O   
6251  C CB  . TYR D 187 ? 2.3613 2.3999 2.6795 -0.0889 -0.4329 0.3780  187 TYR D CB  
6252  C CG  . TYR D 187 ? 2.3784 2.4052 2.6772 -0.1009 -0.4527 0.3432  187 TYR D CG  
6253  C CD1 . TYR D 187 ? 2.3972 2.4139 2.6747 -0.1042 -0.4475 0.3284  187 TYR D CD1 
6254  C CD2 . TYR D 187 ? 2.3955 2.4205 2.6943 -0.1042 -0.4768 0.3266  187 TYR D CD2 
6255  C CE1 . TYR D 187 ? 2.4087 2.4145 2.6630 -0.1117 -0.4650 0.3019  187 TYR D CE1 
6256  C CE2 . TYR D 187 ? 2.4125 2.4251 2.6872 -0.1064 -0.4955 0.2991  187 TYR D CE2 
6257  C CZ  . TYR D 187 ? 2.4931 2.4965 2.7448 -0.1109 -0.4891 0.2890  187 TYR D CZ  
6258  O OH  . TYR D 187 ? 2.5017 2.4929 2.7241 -0.1097 -0.5065 0.2671  187 TYR D OH  
6259  N N   . GLU D 188 ? 2.4179 2.4583 2.6684 -0.0758 -0.4168 0.3936  188 GLU D N   
6260  C CA  . GLU D 188 ? 2.4315 2.4740 2.6585 -0.0759 -0.4200 0.3847  188 GLU D CA  
6261  C C   . GLU D 188 ? 2.5022 2.5334 2.6630 -0.0677 -0.3988 0.3819  188 GLU D C   
6262  O O   . GLU D 188 ? 2.4996 2.5302 2.6328 -0.0670 -0.3981 0.3661  188 GLU D O   
6263  C CB  . GLU D 188 ? 2.4505 2.5114 2.7226 -0.0746 -0.4263 0.4102  188 GLU D CB  
6264  C CG  . GLU D 188 ? 2.5824 2.6482 2.8950 -0.0819 -0.4572 0.3909  188 GLU D CG  
6265  C CD  . GLU D 188 ? 2.8034 2.8670 3.1684 -0.0905 -0.4837 0.3796  188 GLU D CD  
6266  O OE1 . GLU D 188 ? 2.7033 2.7768 3.1229 -0.0934 -0.4828 0.4055  188 GLU D OE1 
6267  O OE2 . GLU D 188 ? 2.7042 2.7565 3.0560 -0.0908 -0.5055 0.3469  188 GLU D OE2 
6268  N N   . LYS D 189 ? 2.4769 2.4980 2.6138 -0.0578 -0.3829 0.3964  189 LYS D N   
6269  C CA  . LYS D 189 ? 2.4920 2.4971 2.5700 -0.0481 -0.3683 0.3943  189 LYS D CA  
6270  C C   . LYS D 189 ? 2.5485 2.5389 2.6030 -0.0560 -0.3713 0.3629  189 LYS D C   
6271  O O   . LYS D 189 ? 2.5469 2.5310 2.5674 -0.0533 -0.3636 0.3557  189 LYS D O   
6272  C CB  . LYS D 189 ? 2.5361 2.5296 2.5975 -0.0283 -0.3578 0.4165  189 LYS D CB  
6273  C CG  . LYS D 189 ? 2.7048 2.7102 2.7697 -0.0103 -0.3481 0.4568  189 LYS D CG  
6274  C CD  . LYS D 189 ? 2.7984 2.7866 2.8300 0.0208  -0.3381 0.4777  189 LYS D CD  
6275  C CE  . LYS D 189 ? 2.8688 2.8680 2.8954 0.0458  -0.3266 0.5242  189 LYS D CE  
6276  N NZ  . LYS D 189 ? 2.9770 2.9557 2.9624 0.0867  -0.3189 0.5453  189 LYS D NZ  
6277  N N   . HIS D 190 ? 2.5012 2.4876 2.5763 -0.0643 -0.3811 0.3476  190 HIS D N   
6278  C CA  . HIS D 190 ? 2.4965 2.4706 2.5562 -0.0704 -0.3842 0.3239  190 HIS D CA  
6279  C C   . HIS D 190 ? 2.5347 2.5182 2.6101 -0.0763 -0.3979 0.3079  190 HIS D C   
6280  O O   . HIS D 190 ? 2.5318 2.5284 2.6344 -0.0775 -0.4092 0.3114  190 HIS D O   
6281  C CB  . HIS D 190 ? 2.5048 2.4656 2.5666 -0.0712 -0.3849 0.3191  190 HIS D CB  
6282  C CG  . HIS D 190 ? 2.5572 2.5055 2.6019 -0.0556 -0.3756 0.3333  190 HIS D CG  
6283  N ND1 . HIS D 190 ? 2.5928 2.5211 2.6033 -0.0470 -0.3720 0.3300  190 HIS D ND1 
6284  C CD2 . HIS D 190 ? 2.5791 2.5315 2.6373 -0.0419 -0.3708 0.3525  190 HIS D CD2 
6285  C CE1 . HIS D 190 ? 2.5972 2.5146 2.5940 -0.0263 -0.3683 0.3442  190 HIS D CE1 
6286  N NE2 . HIS D 190 ? 2.5936 2.5263 2.6174 -0.0204 -0.3649 0.3599  190 HIS D NE2 
6287  N N   . LYS D 191 ? 2.4820 2.4576 2.5418 -0.0760 -0.3987 0.2926  191 LYS D N   
6288  C CA  . LYS D 191 ? 2.4787 2.4598 2.5429 -0.0710 -0.4123 0.2793  191 LYS D CA  
6289  C C   . LYS D 191 ? 2.5178 2.4893 2.5756 -0.0725 -0.4193 0.2692  191 LYS D C   
6290  O O   . LYS D 191 ? 2.5129 2.4859 2.5779 -0.0694 -0.4378 0.2608  191 LYS D O   
6291  C CB  . LYS D 191 ? 2.5181 2.5054 2.5645 -0.0561 -0.4033 0.2767  191 LYS D CB  
6292  C CG  . LYS D 191 ? 2.6974 2.6979 2.7510 -0.0517 -0.4043 0.2813  191 LYS D CG  
6293  C CD  . LYS D 191 ? 2.8117 2.8133 2.8473 -0.0535 -0.3836 0.2964  191 LYS D CD  
6294  C CE  . LYS D 191 ? 2.9174 2.9327 2.9617 -0.0519 -0.3844 0.3068  191 LYS D CE  
6295  N NZ  . LYS D 191 ? 3.0163 3.0306 3.0338 -0.0508 -0.3648 0.3249  191 LYS D NZ  
6296  N N   . VAL D 192 ? 2.4703 2.4306 2.5144 -0.0754 -0.4072 0.2707  192 VAL D N   
6297  C CA  . VAL D 192 ? 2.4665 2.4184 2.5032 -0.0767 -0.4113 0.2652  192 VAL D CA  
6298  C C   . VAL D 192 ? 2.4882 2.4301 2.5282 -0.0904 -0.4105 0.2632  192 VAL D C   
6299  O O   . VAL D 192 ? 2.4799 2.4127 2.5183 -0.0925 -0.4010 0.2666  192 VAL D O   
6300  C CB  . VAL D 192 ? 2.5241 2.4726 2.5508 -0.0656 -0.3998 0.2703  192 VAL D CB  
6301  C CG1 . VAL D 192 ? 2.5238 2.4645 2.5440 -0.0657 -0.4030 0.2709  192 VAL D CG1 
6302  C CG2 . VAL D 192 ? 2.5280 2.4884 2.5495 -0.0442 -0.3977 0.2715  192 VAL D CG2 
6303  N N   . TYR D 193 ? 2.4259 2.3680 2.4670 -0.0957 -0.4217 0.2565  193 TYR D N   
6304  C CA  . TYR D 193 ? 2.4074 2.3429 2.4499 -0.1056 -0.4189 0.2523  193 TYR D CA  
6305  C C   . TYR D 193 ? 2.4379 2.3649 2.4604 -0.1084 -0.4207 0.2467  193 TYR D C   
6306  O O   . TYR D 193 ? 2.4416 2.3714 2.4525 -0.1031 -0.4323 0.2455  193 TYR D O   
6307  C CB  . TYR D 193 ? 2.4121 2.3579 2.4779 -0.1101 -0.4276 0.2522  193 TYR D CB  
6308  C CG  . TYR D 193 ? 2.4258 2.3827 2.5169 -0.1062 -0.4269 0.2637  193 TYR D CG  
6309  C CD1 . TYR D 193 ? 2.4557 2.4224 2.5619 -0.1032 -0.4419 0.2645  193 TYR D CD1 
6310  C CD2 . TYR D 193 ? 2.4297 2.3860 2.5279 -0.1014 -0.4125 0.2750  193 TYR D CD2 
6311  C CE1 . TYR D 193 ? 2.4667 2.4445 2.5980 -0.1005 -0.4409 0.2776  193 TYR D CE1 
6312  C CE2 . TYR D 193 ? 2.4410 2.4084 2.5599 -0.0954 -0.4104 0.2916  193 TYR D CE2 
6313  C CZ  . TYR D 193 ? 2.5392 2.5185 2.6767 -0.0976 -0.4238 0.2935  193 TYR D CZ  
6314  O OH  . TYR D 193 ? 2.5545 2.5457 2.7140 -0.0926 -0.4212 0.3122  193 TYR D OH  
6315  N N   . ALA D 194 ? 2.3670 2.2820 2.3831 -0.1132 -0.4109 0.2440  194 ALA D N   
6316  C CA  . ALA D 194 ? 2.3522 2.2588 2.3508 -0.1169 -0.4102 0.2416  194 ALA D CA  
6317  C C   . ALA D 194 ? 2.3746 2.2729 2.3679 -0.1240 -0.4040 0.2308  194 ALA D C   
6318  O O   . ALA D 194 ? 2.3604 2.2574 2.3646 -0.1209 -0.3986 0.2269  194 ALA D O   
6319  C CB  . ALA D 194 ? 2.3665 2.2655 2.3682 -0.1121 -0.4049 0.2512  194 ALA D CB  
6320  N N   . CYS D 195 ? 2.3228 2.2158 2.2964 -0.1293 -0.4035 0.2277  195 CYS D N   
6321  C CA  . CYS D 195 ? 2.3106 2.1952 2.2735 -0.1341 -0.3956 0.2153  195 CYS D CA  
6322  C C   . CYS D 195 ? 2.3599 2.2322 2.3102 -0.1378 -0.3937 0.2178  195 CYS D C   
6323  O O   . CYS D 195 ? 2.3627 2.2389 2.2955 -0.1389 -0.3970 0.2286  195 CYS D O   
6324  C CB  . CYS D 195 ? 2.3020 2.1972 2.2545 -0.1387 -0.3953 0.2073  195 CYS D CB  
6325  S SG  . CYS D 195 ? 2.3534 2.2547 2.2769 -0.1419 -0.4095 0.2132  195 CYS D SG  
6326  N N   . GLU D 196 ? 2.3056 2.1615 2.2668 -0.1357 -0.3908 0.2103  196 GLU D N   
6327  C CA  . GLU D 196 ? 2.2977 2.1401 2.2598 -0.1397 -0.3916 0.2135  196 GLU D CA  
6328  C C   . GLU D 196 ? 2.3168 2.1567 2.2505 -0.1452 -0.3845 0.1998  196 GLU D C   
6329  O O   . GLU D 196 ? 2.3022 2.1369 2.2302 -0.1395 -0.3787 0.1801  196 GLU D O   
6330  C CB  . GLU D 196 ? 2.3264 2.1480 2.3172 -0.1333 -0.3983 0.2091  196 GLU D CB  
6331  C CG  . GLU D 196 ? 2.4426 2.2521 2.4548 -0.1382 -0.4039 0.2206  196 GLU D CG  
6332  C CD  . GLU D 196 ? 2.6040 2.3873 2.6482 -0.1319 -0.4174 0.2119  196 GLU D CD  
6333  O OE1 . GLU D 196 ? 2.5752 2.3549 2.6561 -0.1320 -0.4245 0.2294  196 GLU D OE1 
6334  O OE2 . GLU D 196 ? 2.4140 2.1791 2.4477 -0.1234 -0.4219 0.1877  196 GLU D OE2 
6335  N N   . VAL D 197 ? 2.2579 2.1024 2.1705 -0.1521 -0.3833 0.2124  197 VAL D N   
6336  C CA  . VAL D 197 ? 2.2376 2.0812 2.1151 -0.1586 -0.3752 0.2025  197 VAL D CA  
6337  C C   . VAL D 197 ? 2.2695 2.0975 2.1554 -0.1621 -0.3753 0.2064  197 VAL D C   
6338  O O   . VAL D 197 ? 2.2745 2.1019 2.1790 -0.1622 -0.3803 0.2322  197 VAL D O   
6339  C CB  . VAL D 197 ? 2.2812 2.1393 2.1200 -0.1610 -0.3759 0.2142  197 VAL D CB  
6340  C CG1 . VAL D 197 ? 2.2693 2.1258 2.0646 -0.1680 -0.3668 0.2083  197 VAL D CG1 
6341  C CG2 . VAL D 197 ? 2.2751 2.1454 2.1152 -0.1588 -0.3798 0.2053  197 VAL D CG2 
6342  N N   . THR D 198 ? 2.1991 2.0149 2.0762 -0.1616 -0.3698 0.1818  198 THR D N   
6343  C CA  . THR D 198 ? 2.1911 1.9890 2.0793 -0.1640 -0.3730 0.1791  198 THR D CA  
6344  C C   . THR D 198 ? 2.2305 2.0319 2.0706 -0.1701 -0.3589 0.1681  198 THR D C   
6345  O O   . THR D 198 ? 2.2126 2.0148 2.0292 -0.1637 -0.3477 0.1405  198 THR D O   
6346  C CB  . THR D 198 ? 2.2411 2.0155 2.1619 -0.1508 -0.3839 0.1557  198 THR D CB  
6347  O OG1 . THR D 198 ? 2.2312 2.0076 2.1292 -0.1368 -0.3739 0.1293  198 THR D OG1 
6348  C CG2 . THR D 198 ? 2.2003 1.9687 2.1666 -0.1464 -0.3991 0.1700  198 THR D CG2 
6349  N N   . HIS D 199 ? 2.1960 2.0011 2.0201 -0.1795 -0.3570 0.1929  199 HIS D N   
6350  C CA  . HIS D 199 ? 2.1879 1.9972 1.9579 -0.1863 -0.3429 0.1880  199 HIS D CA  
6351  C C   . HIS D 199 ? 2.2521 2.0538 2.0285 -0.1927 -0.3448 0.2124  199 HIS D C   
6352  O O   . HIS D 199 ? 2.2561 2.0547 2.0804 -0.1915 -0.3562 0.2423  199 HIS D O   
6353  C CB  . HIS D 199 ? 2.1917 2.0206 1.9109 -0.1881 -0.3365 0.1990  199 HIS D CB  
6354  C CG  . HIS D 199 ? 2.2226 2.0566 1.8777 -0.1941 -0.3214 0.1903  199 HIS D CG  
6355  N ND1 . HIS D 199 ? 2.2479 2.0864 1.8586 -0.1967 -0.3199 0.2201  199 HIS D ND1 
6356  C CD2 . HIS D 199 ? 2.2308 2.0666 1.8585 -0.1945 -0.3056 0.1571  199 HIS D CD2 
6357  C CE1 . HIS D 199 ? 2.2283 2.0702 1.7825 -0.2022 -0.3047 0.2023  199 HIS D CE1 
6358  N NE2 . HIS D 199 ? 2.2202 2.0617 1.7849 -0.2015 -0.2944 0.1636  199 HIS D NE2 
6359  N N   . GLN D 200 ? 2.2093 2.0094 1.9406 -0.1984 -0.3318 0.2015  200 GLN D N   
6360  C CA  . GLN D 200 ? 2.2132 2.0075 1.9444 -0.2051 -0.3309 0.2253  200 GLN D CA  
6361  C C   . GLN D 200 ? 2.2814 2.0910 1.9888 -0.2038 -0.3288 0.2771  200 GLN D C   
6362  O O   . GLN D 200 ? 2.2835 2.0907 2.0251 -0.2033 -0.3334 0.3147  200 GLN D O   
6363  C CB  . GLN D 200 ? 2.2168 2.0070 1.8958 -0.2095 -0.3146 0.1963  200 GLN D CB  
6364  C CG  . GLN D 200 ? 2.4005 2.1780 2.0982 -0.2158 -0.3178 0.2104  200 GLN D CG  
6365  C CD  . GLN D 200 ? 2.6256 2.4018 2.2610 -0.2198 -0.2985 0.1852  200 GLN D CD  
6366  O OE1 . GLN D 200 ? 2.5913 2.3759 2.1699 -0.2166 -0.2804 0.1534  200 GLN D OE1 
6367  N NE2 . GLN D 200 ? 2.4622 2.2289 2.1110 -0.2261 -0.3010 0.2006  200 GLN D NE2 
6368  N N   . GLY D 201 ? 2.2511 2.0750 1.9040 -0.1991 -0.3239 0.2803  201 GLY D N   
6369  C CA  . GLY D 201 ? 2.2712 2.1065 1.8879 -0.1875 -0.3250 0.3256  201 GLY D CA  
6370  C C   . GLY D 201 ? 2.3678 2.2068 2.0410 -0.1728 -0.3366 0.3605  201 GLY D C   
6371  O O   . GLY D 201 ? 2.3810 2.2273 2.0390 -0.1555 -0.3363 0.4074  201 GLY D O   
6372  N N   . LEU D 202 ? 2.3384 2.1726 2.0742 -0.1753 -0.3454 0.3394  202 LEU D N   
6373  C CA  . LEU D 202 ? 2.3509 2.1890 2.1453 -0.1625 -0.3542 0.3654  202 LEU D CA  
6374  C C   . LEU D 202 ? 2.4182 2.2482 2.2880 -0.1647 -0.3580 0.3901  202 LEU D C   
6375  O O   . LEU D 202 ? 2.4085 2.2228 2.3097 -0.1788 -0.3629 0.3646  202 LEU D O   
6376  C CB  . LEU D 202 ? 2.3486 2.1854 2.1677 -0.1642 -0.3617 0.3316  202 LEU D CB  
6377  C CG  . LEU D 202 ? 2.4076 2.2559 2.1828 -0.1551 -0.3641 0.3245  202 LEU D CG  
6378  C CD1 . LEU D 202 ? 2.4001 2.2463 2.1788 -0.1647 -0.3653 0.2812  202 LEU D CD1 
6379  C CD2 . LEU D 202 ? 2.4495 2.3065 2.2494 -0.1348 -0.3704 0.3536  202 LEU D CD2 
6380  N N   . SER D 203 ? 2.3931 2.2336 2.2961 -0.1465 -0.3569 0.4404  203 SER D N   
6381  C CA  . SER D 203 ? 2.3975 2.2346 2.3871 -0.1453 -0.3605 0.4743  203 SER D CA  
6382  C C   . SER D 203 ? 2.4536 2.2807 2.5133 -0.1511 -0.3735 0.4498  203 SER D C   
6383  O O   . SER D 203 ? 2.4492 2.2602 2.5756 -0.1621 -0.3855 0.4444  203 SER D O   
6384  C CB  . SER D 203 ? 2.4527 2.3081 2.4533 -0.1161 -0.3506 0.5393  203 SER D CB  
6385  O OG  . SER D 203 ? 2.5743 2.4412 2.5618 -0.0943 -0.3497 0.5420  203 SER D OG  
6386  N N   . SER D 204 ? 2.4172 2.2519 2.4591 -0.1425 -0.3736 0.4345  204 SER D N   
6387  C CA  . SER D 204 ? 2.4212 2.2486 2.5120 -0.1449 -0.3837 0.4125  204 SER D CA  
6388  C C   . SER D 204 ? 2.4803 2.3071 2.5182 -0.1491 -0.3849 0.3679  204 SER D C   
6389  O O   . SER D 204 ? 2.4707 2.3105 2.4496 -0.1421 -0.3780 0.3688  204 SER D O   
6390  C CB  . SER D 204 ? 2.4712 2.3142 2.6061 -0.1242 -0.3785 0.4522  204 SER D CB  
6391  O OG  . SER D 204 ? 2.5747 2.4363 2.6534 -0.1024 -0.3677 0.4711  204 SER D OG  
6392  N N   . PRO D 205 ? 2.4525 2.2637 2.5118 -0.1570 -0.3952 0.3314  205 PRO D N   
6393  C CA  . PRO D 205 ? 2.4523 2.2659 2.4694 -0.1575 -0.3939 0.2968  205 PRO D CA  
6394  C C   . PRO D 205 ? 2.5164 2.3468 2.5311 -0.1463 -0.3915 0.3088  205 PRO D C   
6395  O O   . PRO D 205 ? 2.5184 2.3456 2.5676 -0.1426 -0.3967 0.3051  205 PRO D O   
6396  C CB  . PRO D 205 ? 2.4800 2.2705 2.5245 -0.1599 -0.4060 0.2640  205 PRO D CB  
6397  C CG  . PRO D 205 ? 2.5407 2.3132 2.6347 -0.1639 -0.4172 0.2744  205 PRO D CG  
6398  C CD  . PRO D 205 ? 2.4817 2.2707 2.6045 -0.1615 -0.4108 0.3223  205 PRO D CD  
6399  N N   . VAL D 206 ? 2.4763 2.3227 2.4470 -0.1381 -0.3853 0.3229  206 VAL D N   
6400  C CA  . VAL D 206 ? 2.4812 2.3422 2.4440 -0.1223 -0.3856 0.3335  206 VAL D CA  
6401  C C   . VAL D 206 ? 2.5292 2.3916 2.4799 -0.1276 -0.3901 0.3017  206 VAL D C   
6402  O O   . VAL D 206 ? 2.5109 2.3679 2.4413 -0.1393 -0.3900 0.2759  206 VAL D O   
6403  C CB  . VAL D 206 ? 2.5386 2.4110 2.4569 -0.1037 -0.3833 0.3598  206 VAL D CB  
6404  C CG1 . VAL D 206 ? 2.5330 2.4063 2.3911 -0.1088 -0.3884 0.3373  206 VAL D CG1 
6405  C CG2 . VAL D 206 ? 2.5484 2.4331 2.4787 -0.0758 -0.3826 0.3839  206 VAL D CG2 
6406  N N   . THR D 207 ? 2.3496 2.1955 2.1814 0.0244  -0.2549 0.3080  207 THR D N   
6407  C CA  . THR D 207 ? 2.3553 2.1972 2.1695 0.0282  -0.2470 0.2699  207 THR D CA  
6408  C C   . THR D 207 ? 2.3951 2.2603 2.2201 0.0470  -0.2307 0.2502  207 THR D C   
6409  O O   . THR D 207 ? 2.3881 2.2652 2.2224 0.0586  -0.2319 0.2587  207 THR D O   
6410  C CB  . THR D 207 ? 2.4944 2.3114 2.2782 0.0254  -0.2632 0.2600  207 THR D CB  
6411  O OG1 . THR D 207 ? 2.5008 2.2910 2.2710 0.0081  -0.2831 0.2859  207 THR D OG1 
6412  C CG2 . THR D 207 ? 2.4899 2.2959 2.2529 0.0269  -0.2551 0.2293  207 THR D CG2 
6413  N N   . LYS D 208 ? 2.3434 2.2143 2.1671 0.0495  -0.2172 0.2262  208 LYS D N   
6414  C CA  . LYS D 208 ? 2.3310 2.2174 2.1595 0.0640  -0.2044 0.2087  208 LYS D CA  
6415  C C   . LYS D 208 ? 2.3993 2.2830 2.2136 0.0672  -0.2033 0.1820  208 LYS D C   
6416  O O   . LYS D 208 ? 2.3926 2.2723 2.2025 0.0620  -0.2005 0.1716  208 LYS D O   
6417  C CB  . LYS D 208 ? 2.3468 2.2433 2.1893 0.0661  -0.1894 0.2125  208 LYS D CB  
6418  C CG  . LYS D 208 ? 2.4712 2.3715 2.3299 0.0661  -0.1859 0.2442  208 LYS D CG  
6419  C CD  . LYS D 208 ? 2.5674 2.4728 2.4294 0.0803  -0.1879 0.2578  208 LYS D CD  
6420  C CE  . LYS D 208 ? 2.6465 2.5551 2.5261 0.0808  -0.1864 0.2967  208 LYS D CE  
6421  N NZ  . LYS D 208 ? 2.7102 2.6258 2.5954 0.0941  -0.1938 0.3136  208 LYS D NZ  
6422  N N   . SER D 209 ? 2.3716 2.2593 2.1817 0.0760  -0.2053 0.1738  209 SER D N   
6423  C CA  . SER D 209 ? 2.3785 2.2649 2.1780 0.0795  -0.2037 0.1550  209 SER D CA  
6424  C C   . SER D 209 ? 2.4378 2.3367 2.2426 0.0869  -0.1946 0.1432  209 SER D C   
6425  O O   . SER D 209 ? 2.4298 2.3358 2.2419 0.0919  -0.1904 0.1475  209 SER D O   
6426  C CB  . SER D 209 ? 2.4284 2.3090 2.2195 0.0809  -0.2132 0.1564  209 SER D CB  
6427  O OG  . SER D 209 ? 2.5242 2.4189 2.3285 0.0868  -0.2166 0.1649  209 SER D OG  
6428  N N   . PHE D 210 ? 2.4076 2.3057 2.2063 0.0878  -0.1920 0.1312  210 PHE D N   
6429  C CA  . PHE D 210 ? 2.4065 2.3125 2.2077 0.0913  -0.1870 0.1234  210 PHE D CA  
6430  C C   . PHE D 210 ? 2.4806 2.3877 2.2788 0.0924  -0.1866 0.1191  210 PHE D C   
6431  O O   . PHE D 210 ? 2.4780 2.3769 2.2684 0.0922  -0.1861 0.1186  210 PHE D O   
6432  C CB  . PHE D 210 ? 2.4263 2.3326 2.2286 0.0900  -0.1833 0.1200  210 PHE D CB  
6433  C CG  . PHE D 210 ? 2.4423 2.3485 2.2433 0.0890  -0.1833 0.1163  210 PHE D CG  
6434  C CD1 . PHE D 210 ? 2.4792 2.3812 2.2792 0.0865  -0.1840 0.1171  210 PHE D CD1 
6435  C CD2 . PHE D 210 ? 2.4669 2.3767 2.2683 0.0905  -0.1831 0.1151  210 PHE D CD2 
6436  C CE1 . PHE D 210 ? 2.4893 2.3925 2.2892 0.0887  -0.1832 0.1157  210 PHE D CE1 
6437  C CE2 . PHE D 210 ? 2.5002 2.4121 2.3035 0.0920  -0.1833 0.1171  210 PHE D CE2 
6438  C CZ  . PHE D 210 ? 2.4755 2.3849 2.2784 0.0926  -0.1826 0.1168  210 PHE D CZ  
6439  N N   . ASN D 211 ? 2.4549 2.3708 2.2586 0.0935  -0.1855 0.1177  211 ASN D N   
6440  C CA  . ASN D 211 ? 2.4587 2.3794 2.2649 0.0928  -0.1833 0.1172  211 ASN D CA  
6441  C C   . ASN D 211 ? 2.5215 2.4424 2.3282 0.0907  -0.1802 0.1189  211 ASN D C   
6442  O O   . ASN D 211 ? 2.5202 2.4404 2.3261 0.0886  -0.1820 0.1183  211 ASN D O   
6443  C CB  . ASN D 211 ? 2.4725 2.4058 2.2889 0.0925  -0.1849 0.1173  211 ASN D CB  
6444  C CG  . ASN D 211 ? 2.8136 2.7502 2.6323 0.0921  -0.1850 0.1163  211 ASN D CG  
6445  O OD1 . ASN D 211 ? 2.7509 2.6804 2.5635 0.0951  -0.1848 0.1166  211 ASN D OD1 
6446  N ND2 . ASN D 211 ? 2.7159 2.6612 2.5418 0.0882  -0.1843 0.1163  211 ASN D ND2 
6447  N N   . ARG D 212 ? 2.4847 2.4038 2.2905 0.0923  -0.1760 0.1236  212 ARG D N   
6448  C CA  . ARG D 212 ? 2.4857 2.4066 2.2952 0.0915  -0.1742 0.1321  212 ARG D CA  
6449  C C   . ARG D 212 ? 2.5318 2.4595 2.3491 0.0841  -0.1765 0.1381  212 ARG D C   
6450  O O   . ARG D 212 ? 2.5174 2.4522 2.3416 0.0806  -0.1742 0.1388  212 ARG D O   
6451  C CB  . ARG D 212 ? 2.4977 2.4148 2.3049 0.0975  -0.1662 0.1406  212 ARG D CB  
6452  C CG  . ARG D 212 ? 2.6286 2.5402 2.4315 0.1037  -0.1653 0.1450  212 ARG D CG  
6453  C CD  . ARG D 212 ? 2.7632 2.6676 2.5606 0.1128  -0.1545 0.1565  212 ARG D CD  
6454  N NE  . ARG D 212 ? 2.8732 2.7881 2.6850 0.1125  -0.1506 0.1757  212 ARG D NE  
6455  C CZ  . ARG D 212 ? 3.0605 2.9730 2.8730 0.1181  -0.1381 0.1902  212 ARG D CZ  
6456  N NH1 . ARG D 212 ? 2.9040 2.8006 2.6987 0.1256  -0.1287 0.1847  212 ARG D NH1 
6457  N NH2 . ARG D 212 ? 2.8936 2.8172 2.7230 0.1156  -0.1353 0.2129  212 ARG D NH2 
6458  N N   . GLY D 213 ? 2.4964 2.4207 2.3119 0.0804  -0.1826 0.1428  213 GLY D N   
6459  C CA  . GLY D 213 ? 2.4977 2.4205 2.3141 0.0707  -0.1883 0.1513  213 GLY D CA  
6460  C C   . GLY D 213 ? 2.5470 2.4647 2.3560 0.0662  -0.1909 0.1419  213 GLY D C   
6461  O O   . GLY D 213 ? 2.5574 2.4611 2.3518 0.0638  -0.1972 0.1391  213 GLY D O   
6462  N N   . GLU D 214 ? 2.4868 2.4151 2.3048 0.0660  -0.1861 0.1383  214 GLU D N   
6463  C CA  . GLU D 214 ? 2.4807 2.4089 2.2961 0.0640  -0.1874 0.1312  214 GLU D CA  
6464  C C   . GLU D 214 ? 2.5390 2.4580 2.3418 0.0730  -0.1876 0.1213  214 GLU D C   
6465  O O   . GLU D 214 ? 2.5309 2.4519 2.3352 0.0801  -0.1855 0.1183  214 GLU D O   
6466  C CB  . GLU D 214 ? 2.4760 2.4240 2.3103 0.0633  -0.1831 0.1307  214 GLU D CB  
6467  C CG  . GLU D 214 ? 2.5637 2.5219 2.4131 0.0524  -0.1805 0.1435  214 GLU D CG  
6468  C CD  . GLU D 214 ? 2.6777 2.6573 2.5481 0.0521  -0.1744 0.1439  214 GLU D CD  
6469  O OE1 . GLU D 214 ? 2.5108 2.4926 2.3809 0.0617  -0.1709 0.1392  214 GLU D OE1 
6470  O OE2 . GLU D 214 ? 2.5411 2.5334 2.4273 0.0409  -0.1736 0.1504  214 GLU D OE2 
6471  N N   . CYS D 215 ? 2.5089 2.4148 2.2973 0.0725  -0.1894 0.1187  215 CYS D N   
6472  C CA  . CYS D 215 ? 2.8665 2.7610 2.6416 0.0826  -0.1865 0.1138  215 CYS D CA  
6473  C C   . CYS D 215 ? 2.9831 2.8937 2.7723 0.0914  -0.1831 0.1133  215 CYS D C   
6474  O O   . CYS D 215 ? 2.4144 2.3246 2.2039 0.1000  -0.1803 0.1149  215 CYS D O   
6475  C CB  . CYS D 215 ? 2.8982 2.7662 2.6463 0.0809  -0.1881 0.1131  215 CYS D CB  
6476  S SG  . CYS D 215 ? 2.9697 2.8144 2.6976 0.0704  -0.1974 0.1173  215 CYS D SG  
6477  N N   . ILE E 10  ? 2.5462 1.9368 2.1104 0.4168  0.3026  0.4172  10  ILE E N   
6478  C CA  . ILE E 10  ? 2.5507 1.9267 2.1049 0.3967  0.2881  0.4006  10  ILE E CA  
6479  C C   . ILE E 10  ? 2.6358 1.9814 2.1562 0.3845  0.2725  0.3898  10  ILE E C   
6480  O O   . ILE E 10  ? 2.6092 1.9754 2.1495 0.3755  0.2648  0.3890  10  ILE E O   
6481  C CB  . ILE E 10  ? 2.5410 1.9570 2.1439 0.3803  0.2786  0.3989  10  ILE E CB  
6482  C CG1 . ILE E 10  ? 2.5124 1.9631 2.1493 0.3760  0.2720  0.4023  10  ILE E CG1 
6483  C CG2 . ILE E 10  ? 2.5373 1.9633 2.1593 0.3837  0.2881  0.4081  10  ILE E CG2 
6484  C CD1 . ILE E 10  ? 2.5908 2.0504 2.2373 0.3594  0.2588  0.3932  10  ILE E CD1 
6485  N N   . GLU E 11  ? 2.6485 1.9419 2.1169 0.3823  0.2652  0.3843  11  GLU E N   
6486  C CA  . GLU E 11  ? 2.6872 1.9396 2.1171 0.3656  0.2433  0.3809  11  GLU E CA  
6487  C C   . GLU E 11  ? 2.7109 1.9989 2.1859 0.3402  0.2239  0.3838  11  GLU E C   
6488  O O   . GLU E 11  ? 2.6969 1.9894 2.1814 0.3240  0.2115  0.3888  11  GLU E O   
6489  C CB  . GLU E 11  ? 2.7801 1.9567 2.1330 0.3708  0.2356  0.3785  11  GLU E CB  
6490  C CG  . GLU E 11  ? 2.9395 2.0672 2.2526 0.3458  0.2014  0.3816  11  GLU E CG  
6491  C CD  . GLU E 11  ? 3.2217 2.3347 2.5252 0.3303  0.1891  0.3865  11  GLU E CD  
6492  O OE1 . GLU E 11  ? 3.3114 2.3934 2.5762 0.3459  0.2025  0.3827  11  GLU E OE1 
6493  O OE2 . GLU E 11  ? 3.0872 2.2210 2.4242 0.3028  0.1668  0.3974  11  GLU E OE2 
6494  N N   . GLY E 12  ? 2.6545 1.9686 2.1588 0.3383  0.2238  0.3837  12  GLY E N   
6495  C CA  . GLY E 12  ? 2.6209 1.9709 2.1683 0.3223  0.2112  0.3905  12  GLY E CA  
6496  C C   . GLY E 12  ? 2.6324 2.0322 2.2286 0.3253  0.2239  0.3906  12  GLY E C   
6497  O O   . GLY E 12  ? 2.6053 2.0275 2.2231 0.3345  0.2360  0.3872  12  GLY E O   
6498  N N   . GLY E 13  ? 2.5789 1.9901 2.1885 0.3160  0.2191  0.3964  13  GLY E N   
6499  C CA  . GLY E 13  ? 2.5326 1.9837 2.1805 0.3182  0.2278  0.3972  13  GLY E CA  
6500  C C   . GLY E 13  ? 2.5492 2.0264 2.2265 0.3183  0.2299  0.4032  13  GLY E C   
6501  O O   . GLY E 13  ? 2.5405 2.0225 2.2286 0.3090  0.2222  0.4173  13  GLY E O   
6502  N N   . TRP E 14  ? 2.4880 1.9788 2.1764 0.3295  0.2396  0.3972  14  TRP E N   
6503  C CA  . TRP E 14  ? 2.4710 1.9746 2.1744 0.3341  0.2438  0.4006  14  TRP E CA  
6504  C C   . TRP E 14  ? 2.4917 2.0099 2.2102 0.3330  0.2458  0.4121  14  TRP E C   
6505  O O   . TRP E 14  ? 2.4782 2.0034 2.2032 0.3268  0.2442  0.4152  14  TRP E O   
6506  C CB  . TRP E 14  ? 2.4533 1.9556 2.1561 0.3423  0.2486  0.3953  14  TRP E CB  
6507  C CG  . TRP E 14  ? 2.4752 1.9673 2.1717 0.3436  0.2507  0.3923  14  TRP E CG  
6508  C CD1 . TRP E 14  ? 2.5123 2.0003 2.2086 0.3412  0.2511  0.3904  14  TRP E CD1 
6509  C CD2 . TRP E 14  ? 2.4775 1.9663 2.1728 0.3484  0.2536  0.3960  14  TRP E CD2 
6510  N NE1 . TRP E 14  ? 2.5083 1.9886 2.2018 0.3426  0.2559  0.3905  14  TRP E NE1 
6511  C CE2 . TRP E 14  ? 2.5309 2.0112 2.2240 0.3481  0.2587  0.3970  14  TRP E CE2 
6512  C CE3 . TRP E 14  ? 2.4904 1.9866 2.1907 0.3536  0.2520  0.4031  14  TRP E CE3 
6513  C CZ2 . TRP E 14  ? 2.5261 2.0032 2.2216 0.3537  0.2656  0.4085  14  TRP E CZ2 
6514  C CZ3 . TRP E 14  ? 2.5116 2.0069 2.2155 0.3605  0.2563  0.4161  14  TRP E CZ3 
6515  C CH2 . TRP E 14  ? 2.5272 2.0119 2.2284 0.3609  0.2647  0.4206  14  TRP E CH2 
6516  N N   . THR E 15  ? 2.4337 1.9569 2.1586 0.3402  0.2512  0.4211  15  THR E N   
6517  C CA  . THR E 15  ? 2.4199 1.9550 2.1574 0.3453  0.2590  0.4393  15  THR E CA  
6518  C C   . THR E 15  ? 2.4351 1.9612 2.1605 0.3637  0.2712  0.4401  15  THR E C   
6519  O O   . THR E 15  ? 2.4312 1.9542 2.1509 0.3732  0.2805  0.4460  15  THR E O   
6520  C CB  . THR E 15  ? 2.5609 2.1077 2.3167 0.3374  0.2527  0.4646  15  THR E CB  
6521  O OG1 . THR E 15  ? 2.5569 2.1021 2.3117 0.3397  0.2464  0.4648  15  THR E OG1 
6522  C CG2 . THR E 15  ? 2.5681 2.1106 2.3260 0.3168  0.2382  0.4699  15  THR E CG2 
6523  N N   . GLY E 16  ? 2.3697 1.8873 2.0875 0.3685  0.2706  0.4347  16  GLY E N   
6524  C CA  . GLY E 16  ? 2.3732 1.8722 2.0711 0.3850  0.2803  0.4353  16  GLY E CA  
6525  C C   . GLY E 16  ? 2.4090 1.8758 2.0749 0.3892  0.2788  0.4226  16  GLY E C   
6526  O O   . GLY E 16  ? 2.4364 1.8744 2.0722 0.4051  0.2867  0.4262  16  GLY E O   
6527  N N   . MET E 17  ? 2.3245 1.7911 1.9926 0.3767  0.2669  0.4115  17  MET E N   
6528  C CA  . MET E 17  ? 2.3253 1.7633 1.9680 0.3773  0.2573  0.4068  17  MET E CA  
6529  C C   . MET E 17  ? 2.3682 1.7954 1.9939 0.3869  0.2588  0.4107  17  MET E C   
6530  O O   . MET E 17  ? 2.3433 1.7988 1.9921 0.3847  0.2635  0.4140  17  MET E O   
6531  C CB  . MET E 17  ? 2.3337 1.7823 1.9915 0.3644  0.2449  0.4033  17  MET E CB  
6532  C CG  . MET E 17  ? 2.3980 1.8170 2.0350 0.3620  0.2289  0.4084  17  MET E CG  
6533  S SD  . MET E 17  ? 2.4351 1.8655 2.0943 0.3505  0.2182  0.4180  17  MET E SD  
6534  C CE  . MET E 17  ? 2.3719 1.8371 2.0543 0.3528  0.2154  0.4190  17  MET E CE  
6535  N N   . VAL E 18  ? 2.3474 1.7280 1.9288 0.3964  0.2534  0.4115  18  VAL E N   
6536  C CA  . VAL E 18  ? 2.3632 1.7187 1.9137 0.4082  0.2525  0.4148  18  VAL E CA  
6537  C C   . VAL E 18  ? 2.4080 1.7185 1.9208 0.4030  0.2251  0.4144  18  VAL E C   
6538  O O   . VAL E 18  ? 2.4324 1.7098 1.9084 0.4120  0.2171  0.4167  18  VAL E O   
6539  C CB  . VAL E 18  ? 2.4543 1.7825 1.9713 0.4330  0.2759  0.4236  18  VAL E CB  
6540  C CG1 . VAL E 18  ? 2.4196 1.7984 1.9818 0.4368  0.2978  0.4362  18  VAL E CG1 
6541  C CG2 . VAL E 18  ? 2.4876 1.7760 1.9698 0.4419  0.2801  0.4237  18  VAL E CG2 
6542  N N   . ASP E 19  ? 2.3316 1.6392 1.8536 0.3879  0.2090  0.4160  19  ASP E N   
6543  C CA  . ASP E 19  ? 2.3435 1.6103 1.8379 0.3780  0.1779  0.4262  19  ASP E CA  
6544  C C   . ASP E 19  ? 2.3137 1.6155 1.8408 0.3697  0.1584  0.4334  19  ASP E C   
6545  O O   . ASP E 19  ? 2.3334 1.6022 1.8316 0.3682  0.1308  0.4438  19  ASP E O   
6546  C CB  . ASP E 19  ? 2.3687 1.6246 1.8698 0.3637  0.1715  0.4332  19  ASP E CB  
6547  C CG  . ASP E 19  ? 2.5202 1.7683 2.0135 0.3695  0.1940  0.4239  19  ASP E CG  
6548  O OD1 . ASP E 19  ? 2.5890 1.7801 2.0274 0.3799  0.1951  0.4234  19  ASP E OD1 
6549  O OD2 . ASP E 19  ? 2.5398 1.8358 2.0783 0.3652  0.2092  0.4185  19  ASP E OD2 
6550  N N   . GLY E 20  ? 2.1838 1.5478 1.7665 0.3653  0.1707  0.4294  20  GLY E N   
6551  C CA  . GLY E 20  ? 2.1313 1.5362 1.7509 0.3603  0.1571  0.4364  20  GLY E CA  
6552  C C   . GLY E 20  ? 2.0948 1.5546 1.7596 0.3592  0.1769  0.4274  20  GLY E C   
6553  O O   . GLY E 20  ? 2.0868 1.5569 1.7550 0.3620  0.1980  0.4154  20  GLY E O   
6554  N N   . TRP E 21  ? 1.9884 1.4791 1.6847 0.3558  0.1688  0.4380  21  TRP E N   
6555  C CA  . TRP E 21  ? 1.9409 1.4708 1.6678 0.3561  0.1842  0.4314  21  TRP E CA  
6556  C C   . TRP E 21  ? 1.9705 1.5009 1.7033 0.3573  0.1957  0.4367  21  TRP E C   
6557  O O   . TRP E 21  ? 1.9560 1.4930 1.6902 0.3574  0.2127  0.4249  21  TRP E O   
6558  C CB  . TRP E 21  ? 1.8961 1.4612 1.6513 0.3572  0.1702  0.4401  21  TRP E CB  
6559  C CG  . TRP E 21  ? 1.8977 1.4739 1.6563 0.3547  0.1620  0.4321  21  TRP E CG  
6560  C CD1 . TRP E 21  ? 1.9441 1.5073 1.6869 0.3537  0.1743  0.4188  21  TRP E CD1 
6561  C CD2 . TRP E 21  ? 1.8664 1.4749 1.6514 0.3539  0.1420  0.4401  21  TRP E CD2 
6562  N NE1 . TRP E 21  ? 1.9200 1.5017 1.6750 0.3518  0.1647  0.4173  21  TRP E NE1 
6563  C CE2 . TRP E 21  ? 1.9106 1.5217 1.6925 0.3505  0.1430  0.4279  21  TRP E CE2 
6564  C CE3 . TRP E 21  ? 1.8581 1.4969 1.6725 0.3573  0.1232  0.4607  21  TRP E CE3 
6565  C CZ2 . TRP E 21  ? 1.8712 1.5137 1.6778 0.3475  0.1239  0.4308  21  TRP E CZ2 
6566  C CZ3 . TRP E 21  ? 1.8456 1.5181 1.6865 0.3555  0.1020  0.4654  21  TRP E CZ3 
6567  C CH2 . TRP E 21  ? 1.8471 1.5209 1.6835 0.3492  0.1013  0.4483  21  TRP E CH2 
6568  N N   . TYR E 22  ? 1.9330 1.4530 1.6676 0.3572  0.1847  0.4582  22  TYR E N   
6569  C CA  . TYR E 22  ? 1.9286 1.4508 1.6723 0.3601  0.1974  0.4700  22  TYR E CA  
6570  C C   . TYR E 22  ? 1.9992 1.4920 1.7297 0.3522  0.1992  0.4744  22  TYR E C   
6571  O O   . TYR E 22  ? 2.0101 1.4777 1.7291 0.3444  0.1802  0.4880  22  TYR E O   
6572  C CB  . TYR E 22  ? 1.9225 1.4674 1.6925 0.3677  0.1880  0.5026  22  TYR E CB  
6573  C CG  . TYR E 22  ? 1.9031 1.4810 1.6911 0.3750  0.1818  0.5016  22  TYR E CG  
6574  C CD1 . TYR E 22  ? 1.9135 1.5003 1.7102 0.3707  0.1545  0.5103  22  TYR E CD1 
6575  C CD2 . TYR E 22  ? 1.8997 1.4954 1.6924 0.3856  0.2010  0.4931  22  TYR E CD2 
6576  C CE1 . TYR E 22  ? 1.8858 1.5094 1.7057 0.3755  0.1476  0.5089  22  TYR E CE1 
6577  C CE2 . TYR E 22  ? 1.8861 1.5128 1.6972 0.3905  0.1950  0.4923  22  TYR E CE2 
6578  C CZ  . TYR E 22  ? 1.9225 1.5687 1.7527 0.3849  0.1687  0.5001  22  TYR E CZ  
6579  O OH  . TYR E 22  ? 1.8405 1.5237 1.6956 0.3881  0.1615  0.4992  22  TYR E OH  
6580  N N   . GLY E 23  ? 1.9503 1.4430 1.6800 0.3533  0.2193  0.4642  23  GLY E N   
6581  C CA  . GLY E 23  ? 2.2499 1.7241 1.9755 0.3451  0.2244  0.4666  23  GLY E CA  
6582  C C   . GLY E 23  ? 2.5815 2.0298 2.2861 0.3370  0.2172  0.4540  23  GLY E C   
6583  O O   . GLY E 23  ? 2.0814 1.5077 1.7813 0.3269  0.2118  0.4640  23  GLY E O   
6584  N N   . ALA E 36  ? 1.4887 1.8739 2.4009 0.3372  -0.0531 0.2692  36  ALA E N   
6585  C CA  . ALA E 36  ? 1.5174 1.8736 2.3846 0.3148  -0.0576 0.2545  36  ALA E CA  
6586  C C   . ALA E 36  ? 1.5959 1.9568 2.4326 0.3013  -0.0511 0.2440  36  ALA E C   
6587  O O   . ALA E 36  ? 1.6012 1.9665 2.4261 0.3060  -0.0486 0.2468  36  ALA E O   
6588  C CB  . ALA E 36  ? 1.5447 1.8665 2.3860 0.3135  -0.0658 0.2617  36  ALA E CB  
6589  N N   . ASP E 37  ? 1.5631 1.9204 2.3864 0.2864  -0.0494 0.2339  37  ASP E N   
6590  C CA  . ASP E 37  ? 1.5703 1.9287 2.3695 0.2744  -0.0452 0.2301  37  ASP E CA  
6591  C C   . ASP E 37  ? 1.6242 1.9582 2.3905 0.2686  -0.0532 0.2265  37  ASP E C   
6592  O O   . ASP E 37  ? 1.6203 1.9383 2.3766 0.2650  -0.0582 0.2235  37  ASP E O   
6593  C CB  . ASP E 37  ? 1.5991 1.9600 2.3982 0.2652  -0.0389 0.2275  37  ASP E CB  
6594  C CG  . ASP E 37  ? 1.7666 2.1272 2.5471 0.2550  -0.0345 0.2321  37  ASP E CG  
6595  O OD1 . ASP E 37  ? 1.7634 2.1421 2.5527 0.2532  -0.0289 0.2392  37  ASP E OD1 
6596  O OD2 . ASP E 37  ? 1.8671 2.2111 2.6276 0.2504  -0.0371 0.2314  37  ASP E OD2 
6597  N N   . LEU E 38  ? 1.5840 1.9179 2.3370 0.2677  -0.0541 0.2269  38  LEU E N   
6598  C CA  . LEU E 38  ? 1.5955 1.9104 2.3255 0.2627  -0.0602 0.2236  38  LEU E CA  
6599  C C   . LEU E 38  ? 1.6275 1.9377 2.3497 0.2524  -0.0629 0.2212  38  LEU E C   
6600  O O   . LEU E 38  ? 1.6244 1.9255 2.3417 0.2498  -0.0653 0.2199  38  LEU E O   
6601  C CB  . LEU E 38  ? 1.6078 1.9223 2.3264 0.2659  -0.0623 0.2225  38  LEU E CB  
6602  C CG  . LEU E 38  ? 1.6869 1.9795 2.3876 0.2675  -0.0655 0.2206  38  LEU E CG  
6603  C CD1 . LEU E 38  ? 1.6968 1.9866 2.3880 0.2817  -0.0645 0.2227  38  LEU E CD1 
6604  C CD2 . LEU E 38  ? 1.7313 2.0160 2.4230 0.2560  -0.0716 0.2144  38  LEU E CD2 
6605  N N   . LYS E 39  ? 1.5646 1.8836 2.2898 0.2481  -0.0607 0.2250  39  LYS E N   
6606  C CA  . LYS E 39  ? 1.5585 1.8736 2.2803 0.2442  -0.0630 0.2295  39  LYS E CA  
6607  C C   . LYS E 39  ? 1.5881 1.9002 2.3087 0.2473  -0.0615 0.2272  39  LYS E C   
6608  O O   . LYS E 39  ? 1.5850 1.8969 2.3053 0.2485  -0.0646 0.2294  39  LYS E O   
6609  C CB  . LYS E 39  ? 1.5879 1.9090 2.3133 0.2404  -0.0587 0.2417  39  LYS E CB  
6610  C CG  . LYS E 39  ? 1.7920 2.1066 2.5175 0.2399  -0.0644 0.2536  39  LYS E CG  
6611  C CD  . LYS E 39  ? 1.9231 2.2380 2.6513 0.2376  -0.0570 0.2736  39  LYS E CD  
6612  C CE  . LYS E 39  ? 2.0597 2.3664 2.7926 0.2433  -0.0628 0.2923  39  LYS E CE  
6613  N NZ  . LYS E 39  ? 2.1641 2.4695 2.8938 0.2556  -0.0594 0.2915  39  LYS E NZ  
6614  N N   . SER E 40  ? 1.5256 1.8384 2.2497 0.2498  -0.0576 0.2231  40  SER E N   
6615  C CA  . SER E 40  ? 1.5216 1.8290 2.2410 0.2525  -0.0588 0.2183  40  SER E CA  
6616  C C   . SER E 40  ? 1.5631 1.8661 2.2806 0.2512  -0.0644 0.2154  40  SER E C   
6617  O O   . SER E 40  ? 1.5561 1.8620 2.2692 0.2516  -0.0656 0.2155  40  SER E O   
6618  C CB  . SER E 40  ? 1.5545 1.8625 2.2834 0.2551  -0.0556 0.2142  40  SER E CB  
6619  O OG  . SER E 40  ? 1.6286 1.9407 2.3748 0.2576  -0.0572 0.2143  40  SER E OG  
6620  N N   . THR E 41  ? 1.5159 1.8143 2.2393 0.2508  -0.0656 0.2167  41  THR E N   
6621  C CA  . THR E 41  ? 1.5147 1.8059 2.2374 0.2477  -0.0673 0.2207  41  THR E CA  
6622  C C   . THR E 41  ? 1.5718 1.8681 2.2930 0.2429  -0.0646 0.2229  41  THR E C   
6623  O O   . THR E 41  ? 1.5620 1.8624 2.2870 0.2381  -0.0624 0.2267  41  THR E O   
6624  C CB  . THR E 41  ? 1.5950 1.8757 2.3251 0.2526  -0.0678 0.2287  41  THR E CB  
6625  O OG1 . THR E 41  ? 1.5769 1.8567 2.3031 0.2560  -0.0646 0.2310  41  THR E OG1 
6626  C CG2 . THR E 41  ? 1.5765 1.8588 2.3230 0.2605  -0.0710 0.2289  41  THR E CG2 
6627  N N   . GLN E 42  ? 1.5396 1.8382 2.2598 0.2436  -0.0649 0.2214  42  GLN E N   
6628  C CA  . GLN E 42  ? 1.5403 1.8437 2.2661 0.2401  -0.0650 0.2224  42  GLN E CA  
6629  C C   . GLN E 42  ? 1.5764 1.8973 2.3157 0.2412  -0.0648 0.2255  42  GLN E C   
6630  O O   . GLN E 42  ? 1.5639 1.8971 2.3190 0.2384  -0.0610 0.2290  42  GLN E O   
6631  C CB  . GLN E 42  ? 1.5688 1.8684 2.2903 0.2409  -0.0697 0.2199  42  GLN E CB  
6632  C CG  . GLN E 42  ? 1.8617 2.1631 2.5930 0.2378  -0.0735 0.2195  42  GLN E CG  
6633  C CD  . GLN E 42  ? 2.1179 2.4295 2.8635 0.2396  -0.0803 0.2253  42  GLN E CD  
6634  O OE1 . GLN E 42  ? 2.0494 2.3560 2.7890 0.2392  -0.0861 0.2277  42  GLN E OE1 
6635  N NE2 . GLN E 42  ? 2.0153 2.3435 2.7837 0.2428  -0.0790 0.2318  42  GLN E NE2 
6636  N N   . ASN E 43  ? 1.5208 1.8450 2.2567 0.2470  -0.0666 0.2268  43  ASN E N   
6637  C CA  . ASN E 43  ? 1.5003 1.8406 2.2468 0.2549  -0.0660 0.2333  43  ASN E CA  
6638  C C   . ASN E 43  ? 1.5147 1.8641 2.2600 0.2555  -0.0627 0.2308  43  ASN E C   
6639  O O   . ASN E 43  ? 1.4938 1.8657 2.2545 0.2628  -0.0604 0.2369  43  ASN E O   
6640  C CB  . ASN E 43  ? 1.5220 1.8567 2.2602 0.2627  -0.0666 0.2398  43  ASN E CB  
6641  C CG  . ASN E 43  ? 1.8536 2.1853 2.6006 0.2623  -0.0707 0.2501  43  ASN E CG  
6642  O OD1 . ASN E 43  ? 1.7945 2.1359 2.5633 0.2643  -0.0757 0.2565  43  ASN E OD1 
6643  N ND2 . ASN E 43  ? 1.7689 2.0892 2.5041 0.2593  -0.0688 0.2537  43  ASN E ND2 
6644  N N   . ALA E 44  ? 1.4578 1.7926 2.1892 0.2493  -0.0633 0.2243  44  ALA E N   
6645  C CA  . ALA E 44  ? 1.4458 1.7842 2.1745 0.2467  -0.0633 0.2233  44  ALA E CA  
6646  C C   . ALA E 44  ? 1.4426 1.7937 2.1885 0.2371  -0.0567 0.2317  44  ALA E C   
6647  O O   . ALA E 44  ? 1.4227 1.7984 2.1819 0.2372  -0.0523 0.2366  44  ALA E O   
6648  C CB  . ALA E 44  ? 1.4711 1.7874 2.1867 0.2442  -0.0688 0.2176  44  ALA E CB  
6649  N N   . ILE E 45  ? 1.3670 1.7038 2.1141 0.2303  -0.0539 0.2352  45  ILE E N   
6650  C CA  . ILE E 45  ? 1.3329 1.6757 2.0948 0.2205  -0.0439 0.2460  45  ILE E CA  
6651  C C   . ILE E 45  ? 1.3355 1.7128 2.1270 0.2216  -0.0371 0.2490  45  ILE E C   
6652  O O   . ILE E 45  ? 1.3043 1.7062 2.1177 0.2148  -0.0265 0.2590  45  ILE E O   
6653  C CB  . ILE E 45  ? 1.3775 1.6945 2.1291 0.2194  -0.0425 0.2478  45  ILE E CB  
6654  C CG1 . ILE E 45  ? 1.3926 1.6836 2.1296 0.2208  -0.0459 0.2543  45  ILE E CG1 
6655  C CG2 . ILE E 45  ? 1.3748 1.6971 2.1413 0.2113  -0.0300 0.2568  45  ILE E CG2 
6656  C CD1 . ILE E 45  ? 1.4988 1.7693 2.2240 0.2294  -0.0480 0.2536  45  ILE E CD1 
6657  N N   . ASP E 46  ? 1.5494 1.7061 1.8974 -0.0078 -0.1130 -0.0261 46  ASP E N   
6658  C CA  . ASP E 46  ? 1.5674 1.6927 1.9021 -0.0476 -0.1514 -0.0514 46  ASP E CA  
6659  C C   . ASP E 46  ? 1.5500 1.6676 1.9369 -0.0890 -0.1338 -0.0535 46  ASP E C   
6660  O O   . ASP E 46  ? 1.5721 1.6463 1.9324 -0.1057 -0.1458 -0.0725 46  ASP E O   
6661  C CB  . ASP E 46  ? 1.6127 1.7656 1.9636 -0.0560 -0.1836 -0.0515 46  ASP E CB  
6662  C CG  . ASP E 46  ? 1.8103 1.9618 2.0926 -0.0150 -0.2158 -0.0590 46  ASP E CG  
6663  O OD1 . ASP E 46  ? 1.8468 1.9789 2.0678 0.0278  -0.2039 -0.0567 46  ASP E OD1 
6664  O OD2 . ASP E 46  ? 1.9067 2.0758 2.1980 -0.0223 -0.2519 -0.0649 46  ASP E OD2 
6665  N N   . GLU E 47  ? 1.4205 1.5791 1.8788 -0.1020 -0.1022 -0.0334 47  GLU E N   
6666  C CA  . GLU E 47  ? 1.3687 1.5167 1.8674 -0.1346 -0.0838 -0.0350 47  GLU E CA  
6667  C C   . GLU E 47  ? 1.3800 1.5013 1.8579 -0.1262 -0.0672 -0.0448 47  GLU E C   
6668  O O   . GLU E 47  ? 1.3707 1.4636 1.8459 -0.1475 -0.0670 -0.0561 47  GLU E O   
6669  C CB  . GLU E 47  ? 1.3343 1.5282 1.9095 -0.1489 -0.0534 -0.0118 47  GLU E CB  
6670  C CG  . GLU E 47  ? 1.4716 1.6454 2.0783 -0.1851 -0.0475 -0.0121 47  GLU E CG  
6671  C CD  . GLU E 47  ? 1.7959 2.0038 2.4720 -0.1994 -0.0101 0.0100  47  GLU E CD  
6672  O OE1 . GLU E 47  ? 1.7760 2.0286 2.4939 -0.1983 -0.0005 0.0323  47  GLU E OE1 
6673  O OE2 . GLU E 47  ? 1.7434 1.9323 2.4302 -0.2111 0.0098  0.0053  47  GLU E OE2 
6674  N N   . ILE E 48  ? 1.3134 1.4425 1.7792 -0.0917 -0.0528 -0.0379 48  ILE E N   
6675  C CA  . ILE E 48  ? 1.2922 1.3951 1.7458 -0.0811 -0.0399 -0.0441 48  ILE E CA  
6676  C C   . ILE E 48  ? 1.3730 1.4220 1.7546 -0.0856 -0.0656 -0.0625 48  ILE E C   
6677  O O   . ILE E 48  ? 1.3678 1.3926 1.7443 -0.1049 -0.0656 -0.0744 48  ILE E O   
6678  C CB  . ILE E 48  ? 1.3115 1.4343 1.7882 -0.0394 -0.0137 -0.0255 48  ILE E CB  
6679  C CG1 . ILE E 48  ? 1.2547 1.4356 1.8222 -0.0358 0.0202  -0.0076 48  ILE E CG1 
6680  C CG2 . ILE E 48  ? 1.3244 1.4105 1.7860 -0.0266 -0.0073 -0.0301 48  ILE E CG2 
6681  C CD1 . ILE E 48  ? 1.2866 1.4773 1.9113 -0.0655 0.0350  -0.0167 48  ILE E CD1 
6682  N N   . THR E 49  ? 1.3604 1.3918 1.6861 -0.0661 -0.0864 -0.0651 49  THR E N   
6683  C CA  . THR E 49  ? 1.4018 1.3821 1.6596 -0.0679 -0.1090 -0.0826 49  THR E CA  
6684  C C   . THR E 49  ? 1.4456 1.4092 1.7101 -0.1059 -0.1259 -0.1008 49  THR E C   
6685  O O   . THR E 49  ? 1.4504 1.3779 1.6840 -0.1134 -0.1285 -0.1122 49  THR E O   
6686  C CB  . THR E 49  ? 1.5276 1.4939 1.7253 -0.0384 -0.1303 -0.0847 49  THR E CB  
6687  O OG1 . THR E 49  ? 1.5208 1.5210 1.7394 -0.0434 -0.1496 -0.0855 49  THR E OG1 
6688  C CG2 . THR E 49  ? 1.5133 1.4765 1.6899 0.0093  -0.1065 -0.0629 49  THR E CG2 
6689  N N   . ASN E 50  ? 1.3885 1.3784 1.7005 -0.1273 -0.1321 -0.0990 50  ASN E N   
6690  C CA  . ASN E 50  ? 1.3917 1.3661 1.7271 -0.1580 -0.1414 -0.1089 50  ASN E CA  
6691  C C   . ASN E 50  ? 1.4083 1.3790 1.7673 -0.1701 -0.1138 -0.1047 50  ASN E C   
6692  O O   . ASN E 50  ? 1.4242 1.3680 1.7774 -0.1823 -0.1141 -0.1134 50  ASN E O   
6693  C CB  . ASN E 50  ? 1.4136 1.4115 1.7967 -0.1737 -0.1567 -0.1029 50  ASN E CB  
6694  C CG  . ASN E 50  ? 1.8673 1.8552 2.2259 -0.1685 -0.1972 -0.1181 50  ASN E CG  
6695  O OD1 . ASN E 50  ? 1.8643 1.8353 2.2488 -0.1877 -0.2197 -0.1294 50  ASN E OD1 
6696  N ND2 . ASN E 50  ? 1.7977 1.7926 2.1076 -0.1385 -0.2079 -0.1193 50  ASN E ND2 
6697  N N   . LYS E 51  ? 1.3071 1.3050 1.6939 -0.1631 -0.0896 -0.0926 51  LYS E N   
6698  C CA  . LYS E 51  ? 1.2650 1.2588 1.6680 -0.1698 -0.0681 -0.0934 51  LYS E CA  
6699  C C   . LYS E 51  ? 1.2998 1.2665 1.6606 -0.1579 -0.0670 -0.1031 51  LYS E C   
6700  O O   . LYS E 51  ? 1.2925 1.2423 1.6454 -0.1642 -0.0600 -0.1097 51  LYS E O   
6701  C CB  . LYS E 51  ? 1.2473 1.2785 1.7009 -0.1664 -0.0454 -0.0819 51  LYS E CB  
6702  C CG  . LYS E 51  ? 1.4004 1.4373 1.8925 -0.1865 -0.0307 -0.0759 51  LYS E CG  
6703  C CD  . LYS E 51  ? 1.5076 1.5547 2.0280 -0.2023 -0.0381 -0.0621 51  LYS E CD  
6704  C CE  . LYS E 51  ? 1.5311 1.5770 2.0923 -0.2199 -0.0174 -0.0487 51  LYS E CE  
6705  N NZ  . LYS E 51  ? 1.5240 1.5903 2.1304 -0.2341 -0.0203 -0.0281 51  LYS E NZ  
6706  N N   . VAL E 52  ? 1.2560 1.2162 1.5876 -0.1378 -0.0726 -0.1011 52  VAL E N   
6707  C CA  . VAL E 52  ? 1.2646 1.1955 1.5584 -0.1252 -0.0702 -0.1038 52  VAL E CA  
6708  C C   . VAL E 52  ? 1.3664 1.2636 1.6205 -0.1385 -0.0803 -0.1152 52  VAL E C   
6709  O O   . VAL E 52  ? 1.3575 1.2401 1.6015 -0.1421 -0.0716 -0.1186 52  VAL E O   
6710  C CB  . VAL E 52  ? 1.3159 1.2422 1.5905 -0.0957 -0.0684 -0.0919 52  VAL E CB  
6711  C CG1 . VAL E 52  ? 1.3386 1.2228 1.5654 -0.0850 -0.0672 -0.0908 52  VAL E CG1 
6712  C CG2 . VAL E 52  ? 1.2737 1.2332 1.6046 -0.0776 -0.0485 -0.0778 52  VAL E CG2 
6713  N N   . ASN E 53  ? 1.3707 1.2586 1.6087 -0.1445 -0.0986 -0.1219 53  ASN E N   
6714  C CA  . ASN E 53  ? 1.4062 1.2655 1.6233 -0.1568 -0.1068 -0.1339 53  ASN E CA  
6715  C C   . ASN E 53  ? 1.4444 1.3068 1.6969 -0.1737 -0.0957 -0.1350 53  ASN E C   
6716  O O   . ASN E 53  ? 1.4580 1.3005 1.6999 -0.1778 -0.0880 -0.1393 53  ASN E O   
6717  C CB  . ASN E 53  ? 1.4827 1.3341 1.6884 -0.1581 -0.1338 -0.1449 53  ASN E CB  
6718  C CG  . ASN E 53  ? 1.9008 1.7284 2.0465 -0.1362 -0.1427 -0.1473 53  ASN E CG  
6719  O OD1 . ASN E 53  ? 1.8006 1.6388 1.9317 -0.1135 -0.1406 -0.1359 53  ASN E OD1 
6720  N ND2 . ASN E 53  ? 1.8579 1.6507 1.9692 -0.1392 -0.1480 -0.1594 53  ASN E ND2 
6721  N N   . SER E 54  ? 1.3648 1.2513 1.6598 -0.1803 -0.0900 -0.1276 54  SER E N   
6722  C CA  . SER E 54  ? 1.3453 1.2300 1.6715 -0.1897 -0.0749 -0.1232 54  SER E CA  
6723  C C   . SER E 54  ? 1.3575 1.2399 1.6671 -0.1805 -0.0551 -0.1224 54  SER E C   
6724  O O   . SER E 54  ? 1.3599 1.2285 1.6693 -0.1791 -0.0412 -0.1209 54  SER E O   
6725  C CB  . SER E 54  ? 1.3807 1.2857 1.7558 -0.1995 -0.0742 -0.1123 54  SER E CB  
6726  O OG  . SER E 54  ? 1.5311 1.4380 1.9257 -0.2078 -0.0974 -0.1142 54  SER E OG  
6727  N N   . VAL E 55  ? 1.2790 1.1745 1.5791 -0.1708 -0.0539 -0.1231 55  VAL E N   
6728  C CA  . VAL E 55  ? 1.2649 1.1588 1.5534 -0.1612 -0.0431 -0.1269 55  VAL E CA  
6729  C C   . VAL E 55  ? 1.3336 1.2054 1.5815 -0.1545 -0.0425 -0.1299 55  VAL E C   
6730  O O   . VAL E 55  ? 1.3353 1.2011 1.5681 -0.1475 -0.0339 -0.1328 55  VAL E O   
6731  C CB  . VAL E 55  ? 1.2856 1.2022 1.5995 -0.1533 -0.0420 -0.1277 55  VAL E CB  
6732  C CG1 . VAL E 55  ? 1.2787 1.1957 1.5871 -0.1419 -0.0484 -0.1230 55  VAL E CG1 
6733  C CG2 . VAL E 55  ? 1.2844 1.1996 1.5957 -0.1451 -0.0367 -0.1375 55  VAL E CG2 
6734  N N   . ILE E 56  ? 1.3075 1.1665 1.5351 -0.1549 -0.0505 -0.1282 56  ILE E N   
6735  C CA  . ILE E 56  ? 1.3278 1.1638 1.5197 -0.1515 -0.0457 -0.1272 56  ILE E CA  
6736  C C   . ILE E 56  ? 1.4314 1.2595 1.6258 -0.1580 -0.0349 -0.1290 56  ILE E C   
6737  O O   . ILE E 56  ? 1.4386 1.2607 1.6167 -0.1517 -0.0204 -0.1263 56  ILE E O   
6738  C CB  . ILE E 56  ? 1.3751 1.1934 1.5415 -0.1479 -0.0543 -0.1240 56  ILE E CB  
6739  C CG1 . ILE E 56  ? 1.3620 1.1835 1.5310 -0.1319 -0.0549 -0.1145 56  ILE E CG1 
6740  C CG2 . ILE E 56  ? 1.4017 1.1927 1.5346 -0.1499 -0.0456 -0.1223 56  ILE E CG2 
6741  C CD1 . ILE E 56  ? 1.4659 1.2753 1.6156 -0.1196 -0.0617 -0.1080 56  ILE E CD1 
6742  N N   . GLU E 57  ? 1.4119 1.2423 1.6354 -0.1679 -0.0404 -0.1313 57  GLU E N   
6743  C CA  . GLU E 57  ? 1.4273 1.2503 1.6769 -0.1713 -0.0279 -0.1295 57  GLU E CA  
6744  C C   . GLU E 57  ? 1.4698 1.2977 1.7249 -0.1594 -0.0067 -0.1218 57  GLU E C   
6745  O O   . GLU E 57  ? 1.4726 1.2928 1.7249 -0.1489 0.0144  -0.1163 57  GLU E O   
6746  C CB  . GLU E 57  ? 1.4521 1.2769 1.7456 -0.1837 -0.0434 -0.1319 57  GLU E CB  
6747  C CG  . GLU E 57  ? 1.6599 1.4737 2.0011 -0.1860 -0.0314 -0.1284 57  GLU E CG  
6748  C CD  . GLU E 57  ? 1.9917 1.8058 2.3675 -0.1774 -0.0074 -0.1122 57  GLU E CD  
6749  O OE1 . GLU E 57  ? 1.9194 1.7417 2.3144 -0.1821 -0.0125 -0.1055 57  GLU E OE1 
6750  O OE2 . GLU E 57  ? 1.9381 1.7432 2.3213 -0.1630 0.0202  -0.1035 57  GLU E OE2 
6751  N N   . LYS E 58  ? 1.4120 1.2523 1.6736 -0.1578 -0.0102 -0.1212 58  LYS E N   
6752  C CA  . LYS E 58  ? 1.4136 1.2537 1.6711 -0.1436 0.0067  -0.1172 58  LYS E CA  
6753  C C   . LYS E 58  ? 1.4582 1.2968 1.6722 -0.1265 0.0122  -0.1224 58  LYS E C   
6754  O O   . LYS E 58  ? 1.4755 1.3077 1.6742 -0.1075 0.0294  -0.1186 58  LYS E O   
6755  C CB  . LYS E 58  ? 1.4413 1.2948 1.7186 -0.1484 0.0013  -0.1177 58  LYS E CB  
6756  C CG  . LYS E 58  ? 1.7316 1.5743 2.0206 -0.1384 0.0222  -0.1075 58  LYS E CG  
6757  C CD  . LYS E 58  ? 1.8836 1.7383 2.2060 -0.1500 0.0213  -0.1028 58  LYS E CD  
6758  C CE  . LYS E 58  ? 2.0888 1.9227 2.4263 -0.1410 0.0465  -0.0855 58  LYS E CE  
6759  N NZ  . LYS E 58  ? 2.2040 2.0488 2.5792 -0.1553 0.0504  -0.0762 58  LYS E NZ  
6760  N N   . MET E 59  ? 1.3950 1.2371 1.5891 -0.1298 -0.0013 -0.1283 59  MET E N   
6761  C CA  . MET E 59  ? 1.3989 1.2398 1.5589 -0.1158 0.0004  -0.1309 59  MET E CA  
6762  C C   . MET E 59  ? 1.4570 1.2886 1.6013 -0.1113 0.0192  -0.1213 59  MET E C   
6763  O O   . MET E 59  ? 1.4714 1.3041 1.5927 -0.0926 0.0334  -0.1180 59  MET E O   
6764  C CB  . MET E 59  ? 1.4137 1.2578 1.5726 -0.1199 -0.0176 -0.1346 59  MET E CB  
6765  C CG  . MET E 59  ? 1.4445 1.3029 1.6278 -0.1176 -0.0309 -0.1445 59  MET E CG  
6766  S SD  . MET E 59  ? 1.4723 1.3332 1.6794 -0.1201 -0.0440 -0.1400 59  MET E SD  
6767  C CE  . MET E 59  ? 1.4362 1.2908 1.6337 -0.1065 -0.0519 -0.1426 59  MET E CE  
6768  N N   . ASN E 60  ? 1.4008 1.2243 1.5584 -0.1263 0.0200  -0.1176 60  ASN E N   
6769  C CA  . ASN E 60  ? 1.4017 1.2173 1.5583 -0.1257 0.0405  -0.1096 60  ASN E CA  
6770  C C   . ASN E 60  ? 1.4428 1.2607 1.6240 -0.1109 0.0673  -0.1012 60  ASN E C   
6771  O O   . ASN E 60  ? 1.4397 1.2604 1.6137 -0.0960 0.0936  -0.0909 60  ASN E O   
6772  C CB  . ASN E 60  ? 1.4144 1.2179 1.5841 -0.1443 0.0304  -0.1136 60  ASN E CB  
6773  C CG  . ASN E 60  ? 1.7142 1.5056 1.8507 -0.1497 0.0186  -0.1131 60  ASN E CG  
6774  O OD1 . ASN E 60  ? 1.5836 1.3780 1.7047 -0.1445 0.0074  -0.1118 60  ASN E OD1 
6775  N ND2 . ASN E 60  ? 1.6697 1.4438 1.8000 -0.1582 0.0217  -0.1135 60  ASN E ND2 
6776  N N   . THR E 61  ? 1.3889 1.2053 1.6028 -0.1118 0.0648  -0.1012 61  THR E N   
6777  C CA  . THR E 61  ? 1.3925 1.2041 1.6368 -0.0924 0.0940  -0.0872 61  THR E CA  
6778  C C   . THR E 61  ? 1.4572 1.2709 1.6592 -0.0623 0.1085  -0.0825 61  THR E C   
6779  O O   . THR E 61  ? 1.4801 1.2900 1.6868 -0.0341 0.1415  -0.0669 61  THR E O   
6780  C CB  . THR E 61  ? 1.4710 1.2747 1.7718 -0.1038 0.0884  -0.0836 61  THR E CB  
6781  O OG1 . THR E 61  ? 1.4981 1.2915 1.8461 -0.0842 0.1222  -0.0648 61  THR E OG1 
6782  C CG2 . THR E 61  ? 1.4330 1.2381 1.7237 -0.1056 0.0752  -0.0857 61  THR E CG2 
6783  N N   . GLN E 62  ? 1.4047 1.2244 1.5681 -0.0645 0.0841  -0.0965 62  GLN E N   
6784  C CA  . GLN E 62  ? 1.4287 1.2492 1.5467 -0.0362 0.0873  -0.1003 62  GLN E CA  
6785  C C   . GLN E 62  ? 1.4774 1.3067 1.5577 -0.0193 0.0951  -0.0981 62  GLN E C   
6786  O O   . GLN E 62  ? 1.5016 1.3307 1.5471 0.0147  0.1107  -0.0939 62  GLN E O   
6787  C CB  . GLN E 62  ? 1.4437 1.2689 1.5501 -0.0453 0.0570  -0.1193 62  GLN E CB  
6788  C CG  . GLN E 62  ? 1.7239 1.5441 1.7895 -0.0154 0.0572  -0.1285 62  GLN E CG  
6789  C CD  . GLN E 62  ? 2.0799 1.8803 2.1426 0.0105  0.0885  -0.1123 62  GLN E CD  
6790  O OE1 . GLN E 62  ? 2.0236 1.8139 2.1281 -0.0022 0.0988  -0.1005 62  GLN E OE1 
6791  N NE2 . GLN E 62  ? 2.0579 1.8505 2.0717 0.0511  0.1057  -0.1085 62  GLN E NE2 
6792  N N   . PHE E 63  ? 1.4079 1.2431 1.4920 -0.0401 0.0862  -0.0985 63  PHE E N   
6793  C CA  . PHE E 63  ? 1.4155 1.2594 1.4712 -0.0281 0.0973  -0.0908 63  PHE E CA  
6794  C C   . PHE E 63  ? 1.4755 1.3233 1.5445 -0.0064 0.1410  -0.0704 63  PHE E C   
6795  O O   . PHE E 63  ? 1.4931 1.3517 1.5314 0.0235  0.1601  -0.0608 63  PHE E O   
6796  C CB  . PHE E 63  ? 1.4185 1.2601 1.4795 -0.0558 0.0834  -0.0904 63  PHE E CB  
6797  C CG  . PHE E 63  ? 1.4410 1.2890 1.4840 -0.0499 0.1020  -0.0753 63  PHE E CG  
6798  C CD1 . PHE E 63  ? 1.4661 1.3119 1.5303 -0.0602 0.1301  -0.0610 63  PHE E CD1 
6799  C CD2 . PHE E 63  ? 1.4844 1.3414 1.4944 -0.0345 0.0908  -0.0756 63  PHE E CD2 
6800  C CE1 . PHE E 63  ? 1.4779 1.3313 1.5295 -0.0562 0.1530  -0.0433 63  PHE E CE1 
6801  C CE2 . PHE E 63  ? 1.5200 1.3851 1.5170 -0.0298 0.1099  -0.0571 63  PHE E CE2 
6802  C CZ  . PHE E 63  ? 1.4808 1.3445 1.4981 -0.0413 0.1439  -0.0392 63  PHE E CZ  
6803  N N   . THR E 64  ? 1.4193 1.2594 1.5410 -0.0187 0.1566  -0.0636 64  THR E N   
6804  C CA  . THR E 64  ? 1.4206 1.2631 1.5836 0.0009  0.2010  -0.0433 64  THR E CA  
6805  C C   . THR E 64  ? 1.5033 1.3409 1.6547 0.0436  0.2247  -0.0313 64  THR E C   
6806  O O   . THR E 64  ? 1.5130 1.3591 1.6657 0.0801  0.2658  -0.0108 64  THR E O   
6807  C CB  . THR E 64  ? 1.5017 1.3339 1.7343 -0.0261 0.2000  -0.0452 64  THR E CB  
6808  O OG1 . THR E 64  ? 1.4736 1.3029 1.6966 -0.0614 0.1705  -0.0603 64  THR E OG1 
6809  C CG2 . THR E 64  ? 1.4800 1.3170 1.7756 -0.0102 0.2458  -0.0261 64  THR E CG2 
6810  N N   . ALA E 65  ? 1.4763 1.2995 1.6143 0.0422  0.2020  -0.0419 65  ALA E N   
6811  C CA  . ALA E 65  ? 1.5152 1.3239 1.6308 0.0825  0.2211  -0.0320 65  ALA E CA  
6812  C C   . ALA E 65  ? 1.6086 1.4260 1.6453 0.1195  0.2208  -0.0368 65  ALA E C   
6813  O O   . ALA E 65  ? 1.6453 1.4581 1.6628 0.1684  0.2580  -0.0174 65  ALA E O   
6814  C CB  . ALA E 65  ? 1.5248 1.3166 1.6453 0.0648  0.1952  -0.0437 65  ALA E CB  
6815  N N   . VAL E 66  ? 1.5587 1.3877 1.5538 0.1007  0.1791  -0.0614 66  VAL E N   
6816  C CA  . VAL E 66  ? 1.5926 1.4318 1.5184 0.1314  0.1669  -0.0716 66  VAL E CA  
6817  C C   . VAL E 66  ? 1.6649 1.5257 1.5857 0.1510  0.1992  -0.0501 66  VAL E C   
6818  O O   . VAL E 66  ? 1.7034 1.5746 1.5692 0.1913  0.2047  -0.0481 66  VAL E O   
6819  C CB  . VAL E 66  ? 1.6221 1.4666 1.5281 0.1049  0.1126  -0.1024 66  VAL E CB  
6820  C CG1 . VAL E 66  ? 1.6618 1.5151 1.5041 0.1384  0.0937  -0.1162 66  VAL E CG1 
6821  C CG2 . VAL E 66  ? 1.6135 1.4426 1.5354 0.0873  0.0897  -0.1201 66  VAL E CG2 
6822  N N   . GLY E 67  ? 1.5872 1.4545 1.5673 0.1256  0.2226  -0.0340 67  GLY E N   
6823  C CA  . GLY E 67  ? 1.5743 1.4631 1.5714 0.1368  0.2618  -0.0105 67  GLY E CA  
6824  C C   . GLY E 67  ? 1.6595 1.5566 1.6477 0.1963  0.3139  0.0158  67  GLY E C   
6825  O O   . GLY E 67  ? 1.6439 1.5653 1.6475 0.2130  0.3532  0.0385  67  GLY E O   
6826  N N   . LYS E 68  ? 1.6559 1.5319 1.6186 0.2323  0.3181  0.0156  68  LYS E N   
6827  C CA  . LYS E 68  ? 1.7018 1.5755 1.6409 0.3011  0.3664  0.0414  68  LYS E CA  
6828  C C   . LYS E 68  ? 1.8201 1.7039 1.6560 0.3425  0.3459  0.0288  68  LYS E C   
6829  O O   . LYS E 68  ? 1.8786 1.7473 1.6604 0.4021  0.3641  0.0365  68  LYS E O   
6830  C CB  . LYS E 68  ? 1.7451 1.5816 1.7125 0.3193  0.3846  0.0520  68  LYS E CB  
6831  C CG  . LYS E 68  ? 1.8429 1.6506 1.7529 0.3148  0.3410  0.0251  68  LYS E CG  
6832  C CD  . LYS E 68  ? 1.9100 1.6791 1.8581 0.3314  0.3685  0.0448  68  LYS E CD  
6833  C CE  . LYS E 68  ? 2.0357 1.7729 1.9022 0.3678  0.3568  0.0342  68  LYS E CE  
6834  N NZ  . LYS E 68  ? 2.1334 1.8286 2.0277 0.4080  0.4057  0.0695  68  LYS E NZ  
6835  N N   . GLU E 69  ? 1.8369 1.7027 1.4634 -0.1193 0.0347  -0.2735 69  GLU E N   
6836  C CA  . GLU E 69  ? 2.0145 1.8814 1.6446 -0.1206 0.0320  -0.2688 69  GLU E CA  
6837  C C   . GLU E 69  ? 1.9680 1.8372 1.5946 -0.1200 0.0281  -0.2719 69  GLU E C   
6838  O O   . GLU E 69  ? 1.3426 1.2080 0.9719 -0.1188 0.0270  -0.2706 69  GLU E O   
6839  C CB  . GLU E 69  ? 2.0316 1.9030 1.6645 -0.1239 0.0311  -0.2638 69  GLU E CB  
6840  C CG  . GLU E 69  ? 2.1616 2.0292 1.8004 -0.1244 0.0333  -0.2592 69  GLU E CG  
6841  C CD  . GLU E 69  ? 2.3761 2.2417 2.0150 -0.1236 0.0359  -0.2610 69  GLU E CD  
6842  O OE1 . GLU E 69  ? 2.2451 2.1060 1.8885 -0.1209 0.0377  -0.2605 69  GLU E OE1 
6843  O OE2 . GLU E 69  ? 2.2636 2.1332 1.8988 -0.1254 0.0359  -0.2631 69  GLU E OE2 
6844  N N   . LYS E 83  ? 2.3195 2.1769 1.9882 -0.1217 0.0234  -0.2388 83  LYS E N   
6845  C CA  . LYS E 83  ? 2.3197 2.1772 1.9869 -0.1227 0.0251  -0.2382 83  LYS E CA  
6846  C C   . LYS E 83  ? 2.3666 2.2243 2.0303 -0.1226 0.0268  -0.2403 83  LYS E C   
6847  O O   . LYS E 83  ? 2.3602 2.2190 2.0211 -0.1221 0.0260  -0.2431 83  LYS E O   
6848  C CB  . LYS E 83  ? 2.3549 2.2101 2.0252 -0.1226 0.0262  -0.2358 83  LYS E CB  
6849  C CG  . LYS E 83  ? 2.5735 2.4284 2.2457 -0.1230 0.0248  -0.2343 83  LYS E CG  
6850  C CD  . LYS E 83  ? 2.7059 2.5586 2.3797 -0.1230 0.0252  -0.2330 83  LYS E CD  
6851  C CE  . LYS E 83  ? 2.8373 2.6891 2.5119 -0.1233 0.0239  -0.2321 83  LYS E CE  
6852  N NZ  . LYS E 83  ? 2.9408 2.7902 2.6159 -0.1233 0.0233  -0.2317 83  LYS E NZ  
6853  N N   . VAL E 84  ? 2.3174 2.1740 1.9815 -0.1228 0.0284  -0.2396 84  VAL E N   
6854  C CA  . VAL E 84  ? 2.3069 2.1634 1.9687 -0.1223 0.0301  -0.2418 84  VAL E CA  
6855  C C   . VAL E 84  ? 2.3338 2.1890 1.9957 -0.1198 0.0317  -0.2437 84  VAL E C   
6856  O O   . VAL E 84  ? 2.3257 2.1811 1.9839 -0.1192 0.0324  -0.2470 84  VAL E O   
6857  C CB  . VAL E 84  ? 2.3550 2.2104 2.0185 -0.1228 0.0304  -0.2404 84  VAL E CB  
6858  C CG1 . VAL E 84  ? 2.3550 2.2123 2.0168 -0.1257 0.0289  -0.2389 84  VAL E CG1 
6859  C CG2 . VAL E 84  ? 2.3508 2.2045 2.0188 -0.1216 0.0299  -0.2384 84  VAL E CG2 
6860  N N   . ASP E 85  ? 2.2747 2.1292 1.9405 -0.1184 0.0323  -0.2419 85  ASP E N   
6861  C CA  . ASP E 85  ? 2.2621 2.1166 1.9288 -0.1161 0.0339  -0.2426 85  ASP E CA  
6862  C C   . ASP E 85  ? 2.2959 2.1499 1.9612 -0.1167 0.0325  -0.2430 85  ASP E C   
6863  O O   . ASP E 85  ? 2.2904 2.1435 1.9523 -0.1159 0.0328  -0.2459 85  ASP E O   
6864  C CB  . ASP E 85  ? 2.2796 2.1359 1.9512 -0.1144 0.0344  -0.2402 85  ASP E CB  
6865  C CG  . ASP E 85  ? 2.3502 2.2072 2.0240 -0.1130 0.0344  -0.2404 85  ASP E CG  
6866  O OD1 . ASP E 85  ? 2.3451 2.2020 2.0183 -0.1111 0.0356  -0.2428 85  ASP E OD1 
6867  O OD2 . ASP E 85  ? 2.4041 2.2617 2.0806 -0.1134 0.0328  -0.2386 85  ASP E OD2 
6868  N N   . ASP E 86  ? 2.2379 2.0920 1.9059 -0.1180 0.0306  -0.2403 86  ASP E N   
6869  C CA  . ASP E 86  ? 2.2286 2.0820 1.8972 -0.1186 0.0283  -0.2399 86  ASP E CA  
6870  C C   . ASP E 86  ? 2.2624 2.1155 1.9269 -0.1189 0.0255  -0.2434 86  ASP E C   
6871  O O   . ASP E 86  ? 2.2560 2.1078 1.9197 -0.1186 0.0234  -0.2445 86  ASP E O   
6872  C CB  . ASP E 86  ? 2.2521 2.1059 1.9251 -0.1196 0.0266  -0.2367 86  ASP E CB  
6873  C CG  . ASP E 86  ? 2.3709 2.2241 2.0468 -0.1200 0.0245  -0.2350 86  ASP E CG  
6874  O OD1 . ASP E 86  ? 2.3750 2.2275 2.0523 -0.1205 0.0210  -0.2352 86  ASP E OD1 
6875  O OD2 . ASP E 86  ? 2.4405 2.2943 2.1177 -0.1196 0.0259  -0.2332 86  ASP E OD2 
6876  N N   . GLY E 87  ? 2.2109 2.0657 1.8729 -0.1195 0.0251  -0.2450 87  GLY E N   
6877  C CA  . GLY E 87  ? 2.2037 2.0606 1.8615 -0.1196 0.0223  -0.2487 87  GLY E CA  
6878  C C   . GLY E 87  ? 2.2313 2.0872 1.8839 -0.1186 0.0231  -0.2529 87  GLY E C   
6879  O O   . GLY E 87  ? 2.2260 2.0817 1.8760 -0.1180 0.0199  -0.2561 87  GLY E O   
6880  N N   . PHE E 88  ? 2.2149 1.8877 1.9208 0.5505  0.2551  0.0668  88  PHE E N   
6881  C CA  . PHE E 88  ? 2.1618 1.7664 1.8957 0.5045  0.2745  0.0557  88  PHE E CA  
6882  C C   . PHE E 88  ? 2.1123 1.7343 1.9016 0.4522  0.2439  0.0266  88  PHE E C   
6883  O O   . PHE E 88  ? 2.0798 1.6798 1.8887 0.4151  0.2355  0.0054  88  PHE E O   
6884  C CB  . PHE E 88  ? 2.2028 1.7411 1.9329 0.5155  0.3334  0.0844  88  PHE E CB  
6885  C CG  . PHE E 88  ? 2.1678 1.6620 1.9427 0.4649  0.3521  0.0692  88  PHE E CG  
6886  C CD1 . PHE E 88  ? 2.1696 1.6717 1.9885 0.4410  0.3578  0.0707  88  PHE E CD1 
6887  C CD2 . PHE E 88  ? 2.1759 1.6270 1.9503 0.4402  0.3630  0.0509  88  PHE E CD2 
6888  C CE1 . PHE E 88  ? 2.1334 1.6080 1.9935 0.3943  0.3743  0.0552  88  PHE E CE1 
6889  C CE2 . PHE E 88  ? 2.1633 1.5879 1.9786 0.3967  0.3792  0.0350  88  PHE E CE2 
6890  C CZ  . PHE E 88  ? 2.1041 1.5442 1.9612 0.3745  0.3847  0.0376  88  PHE E CZ  
6891  N N   . LEU E 89  ? 2.0206 1.6770 1.8344 0.4501  0.2309  0.0270  89  LEU E N   
6892  C CA  . LEU E 89  ? 1.9487 1.6167 1.8115 0.4030  0.2061  0.0012  89  LEU E CA  
6893  C C   . LEU E 89  ? 1.9551 1.6553 1.8296 0.3795  0.1693  -0.0337 89  LEU E C   
6894  O O   . LEU E 89  ? 1.9148 1.5875 1.8171 0.3401  0.1661  -0.0479 89  LEU E O   
6895  C CB  . LEU E 89  ? 1.9369 1.6376 1.8198 0.4077  0.1975  0.0039  89  LEU E CB  
6896  C CG  . LEU E 89  ? 1.9900 1.6501 1.8891 0.4056  0.2381  0.0314  89  LEU E CG  
6897  C CD1 . LEU E 89  ? 1.9999 1.6956 1.9043 0.4299  0.2348  0.0429  89  LEU E CD1 
6898  C CD2 . LEU E 89  ? 1.9705 1.5984 1.9148 0.3500  0.2444  0.0180  89  LEU E CD2 
6899  N N   . ASP E 90  ? 1.9193 1.6797 1.7731 0.4049  0.1470  -0.0472 90  ASP E N   
6900  C CA  . ASP E 90  ? 1.8913 1.6912 1.7603 0.3833  0.1201  -0.0846 90  ASP E CA  
6901  C C   . ASP E 90  ? 1.8939 1.6440 1.7738 0.3521  0.1277  -0.0904 90  ASP E C   
6902  O O   . ASP E 90  ? 1.8459 1.5983 1.7608 0.3161  0.1148  -0.1156 90  ASP E O   
6903  C CB  . ASP E 90  ? 1.9520 1.8253 1.7902 0.4201  0.1068  -0.0942 90  ASP E CB  
6904  C CG  . ASP E 90  ? 2.1176 2.0673 1.9566 0.4438  0.0882  -0.1074 90  ASP E CG  
6905  O OD1 . ASP E 90  ? 2.0938 2.0523 1.9695 0.4167  0.0758  -0.1308 90  ASP E OD1 
6906  O OD2 . ASP E 90  ? 2.2400 2.2457 2.0429 0.4894  0.0851  -0.0981 90  ASP E OD2 
6907  N N   . ILE E 91  ? 1.8649 1.5667 1.7153 0.3671  0.1525  -0.0669 91  ILE E N   
6908  C CA  . ILE E 91  ? 1.8457 1.4967 1.7021 0.3425  0.1631  -0.0717 91  ILE E CA  
6909  C C   . ILE E 91  ? 1.8225 1.4352 1.7167 0.3058  0.1686  -0.0728 91  ILE E C   
6910  O O   . ILE E 91  ? 1.7725 1.3936 1.6999 0.2747  0.1513  -0.0929 91  ILE E O   
6911  C CB  . ILE E 91  ? 1.9340 1.5386 1.7460 0.3704  0.1938  -0.0500 91  ILE E CB  
6912  C CG1 . ILE E 91  ? 1.9848 1.6309 1.7510 0.4164  0.1919  -0.0392 91  ILE E CG1 
6913  C CG2 . ILE E 91  ? 1.9424 1.5025 1.7601 0.3449  0.2003  -0.0637 91  ILE E CG2 
6914  C CD1 . ILE E 91  ? 2.0767 1.6723 1.7930 0.4573  0.2327  -0.0055 91  ILE E CD1 
6915  N N   . TRP E 92  ? 1.7810 1.3578 1.6721 0.3105  0.1959  -0.0516 92  TRP E N   
6916  C CA  . TRP E 92  ? 1.7471 1.2966 1.6717 0.2780  0.2068  -0.0516 92  TRP E CA  
6917  C C   . TRP E 92  ? 1.7856 1.3633 1.7485 0.2480  0.1786  -0.0672 92  TRP E C   
6918  O O   . TRP E 92  ? 1.7559 1.3196 1.7443 0.2186  0.1749  -0.0755 92  TRP E O   
6919  C CB  . TRP E 92  ? 1.7338 1.2599 1.6547 0.2891  0.2442  -0.0299 92  TRP E CB  
6920  C CG  . TRP E 92  ? 1.7006 1.2296 1.6627 0.2563  0.2479  -0.0316 92  TRP E CG  
6921  C CD1 . TRP E 92  ? 1.7219 1.2716 1.7012 0.2542  0.2458  -0.0247 92  TRP E CD1 
6922  C CD2 . TRP E 92  ? 1.6588 1.1752 1.6508 0.2202  0.2527  -0.0423 92  TRP E CD2 
6923  N NE1 . TRP E 92  ? 1.6747 1.2226 1.6928 0.2160  0.2505  -0.0305 92  TRP E NE1 
6924  C CE2 . TRP E 92  ? 1.6774 1.2095 1.7027 0.1964  0.2537  -0.0407 92  TRP E CE2 
6925  C CE3 . TRP E 92  ? 1.6666 1.1642 1.6611 0.2062  0.2551  -0.0540 92  TRP E CE3 
6926  C CZ2 . TRP E 92  ? 1.6319 1.1668 1.6900 0.1607  0.2579  -0.0489 92  TRP E CZ2 
6927  C CZ3 . TRP E 92  ? 1.6482 1.1507 1.6754 0.1742  0.2580  -0.0618 92  TRP E CZ3 
6928  C CH2 . TRP E 92  ? 1.6278 1.1512 1.6849 0.1525  0.2597  -0.0586 92  TRP E CH2 
6929  N N   . THR E 93  ? 1.7542 1.3712 1.7196 0.2575  0.1609  -0.0722 93  THR E N   
6930  C CA  . THR E 93  ? 1.7249 1.3647 1.7229 0.2312  0.1382  -0.0915 93  THR E CA  
6931  C C   . THR E 93  ? 1.7522 1.3993 1.7668 0.2112  0.1218  -0.1149 93  THR E C   
6932  O O   . THR E 93  ? 1.7169 1.3581 1.7604 0.1832  0.1146  -0.1252 93  THR E O   
6933  C CB  . THR E 93  ? 1.9045 1.5866 1.8985 0.2492  0.1251  -0.0984 93  THR E CB  
6934  O OG1 . THR E 93  ? 1.9963 1.7176 1.9632 0.2799  0.1158  -0.1066 93  THR E OG1 
6935  C CG2 . THR E 93  ? 1.8921 1.5626 1.8811 0.2635  0.1452  -0.0730 93  THR E CG2 
6936  N N   . TYR E 94  ? 1.7305 1.3887 1.7284 0.2249  0.1197  -0.1224 94  TYR E N   
6937  C CA  . TYR E 94  ? 1.7208 1.3842 1.7403 0.2045  0.1118  -0.1438 94  TYR E CA  
6938  C C   . TYR E 94  ? 1.7306 1.3466 1.7593 0.1875  0.1230  -0.1320 94  TYR E C   
6939  O O   . TYR E 94  ? 1.7107 1.3194 1.7682 0.1644  0.1196  -0.1410 94  TYR E O   
6940  C CB  . TYR E 94  ? 1.7719 1.4752 1.7775 0.2202  0.1066  -0.1611 94  TYR E CB  
6941  C CG  . TYR E 94  ? 1.8066 1.5211 1.8445 0.1952  0.1049  -0.1873 94  TYR E CG  
6942  C CD1 . TYR E 94  ? 1.8219 1.5636 1.8930 0.1766  0.1008  -0.2146 94  TYR E CD1 
6943  C CD2 . TYR E 94  ? 1.8274 1.5223 1.8656 0.1889  0.1123  -0.1868 94  TYR E CD2 
6944  C CE1 . TYR E 94  ? 1.8287 1.5777 1.9343 0.1536  0.1090  -0.2383 94  TYR E CE1 
6945  C CE2 . TYR E 94  ? 1.8289 1.5339 1.9036 0.1644  0.1162  -0.2098 94  TYR E CE2 
6946  C CZ  . TYR E 94  ? 1.9059 1.6383 2.0153 0.1475  0.1169  -0.2343 94  TYR E CZ  
6947  O OH  . TYR E 94  ? 1.8831 1.6233 2.0331 0.1236  0.1300  -0.2569 94  TYR E OH  
6948  N N   . ASN E 95  ? 1.6740 1.2588 1.6786 0.2005  0.1398  -0.1134 95  ASN E N   
6949  C CA  . ASN E 95  ? 1.6538 1.1990 1.6649 0.1870  0.1530  -0.1075 95  ASN E CA  
6950  C C   . ASN E 95  ? 1.6556 1.1939 1.6935 0.1649  0.1548  -0.1012 95  ASN E C   
6951  O O   . ASN E 95  ? 1.6411 1.1668 1.6977 0.1484  0.1549  -0.1028 95  ASN E O   
6952  C CB  . ASN E 95  ? 1.6853 1.2001 1.6633 0.2071  0.1774  -0.0961 95  ASN E CB  
6953  C CG  . ASN E 95  ? 2.0669 1.5469 2.0427 0.1994  0.1884  -0.1031 95  ASN E CG  
6954  O OD1 . ASN E 95  ? 2.0586 1.5387 2.0584 0.1807  0.1761  -0.1140 95  ASN E OD1 
6955  N ND2 . ASN E 95  ? 1.9576 1.4043 1.9050 0.2149  0.2157  -0.0982 95  ASN E ND2 
6956  N N   . ALA E 96  ? 1.5820 1.1327 1.6229 0.1648  0.1560  -0.0941 96  ALA E N   
6957  C CA  . ALA E 96  ? 1.5408 1.0925 1.6074 0.1415  0.1576  -0.0894 96  ALA E CA  
6958  C C   . ALA E 96  ? 1.5375 1.1004 1.6278 0.1237  0.1374  -0.1000 96  ALA E C   
6959  O O   . ALA E 96  ? 1.5076 1.0654 1.6172 0.1058  0.1374  -0.0959 96  ALA E O   
6960  C CB  . ALA E 96  ? 1.5485 1.1095 1.6144 0.1444  0.1663  -0.0812 96  ALA E CB  
6961  N N   . GLU E 97  ? 1.4926 1.0740 1.5815 0.1303  0.1239  -0.1155 97  GLU E N   
6962  C CA  . GLU E 97  ? 1.4823 1.0712 1.5944 0.1147  0.1138  -0.1319 97  GLU E CA  
6963  C C   . GLU E 97  ? 1.5325 1.1073 1.6573 0.1086  0.1178  -0.1323 97  GLU E C   
6964  O O   . GLU E 97  ? 1.5159 1.0807 1.6621 0.0937  0.1190  -0.1304 97  GLU E O   
6965  C CB  . GLU E 97  ? 1.5104 1.1315 1.6199 0.1237  0.1049  -0.1570 97  GLU E CB  
6966  C CG  . GLU E 97  ? 1.6662 1.2997 1.7786 0.1197  0.0982  -0.1640 97  GLU E CG  
6967  C CD  . GLU E 97  ? 2.0163 1.6916 2.1243 0.1325  0.0891  -0.1926 97  GLU E CD  
6968  O OE1 . GLU E 97  ? 2.0167 1.7012 2.1437 0.1175  0.0859  -0.2198 97  GLU E OE1 
6969  O OE2 . GLU E 97  ? 2.0099 1.7106 2.0941 0.1590  0.0869  -0.1888 97  GLU E OE2 
6970  N N   . LEU E 98  ? 1.5150 1.0864 1.6261 0.1210  0.1218  -0.1327 98  LEU E N   
6971  C CA  . LEU E 98  ? 1.5246 1.0815 1.6490 0.1153  0.1268  -0.1345 98  LEU E CA  
6972  C C   . LEU E 98  ? 1.5657 1.1012 1.7025 0.1056  0.1313  -0.1173 98  LEU E C   
6973  O O   . LEU E 98  ? 1.5593 1.0883 1.7202 0.0965  0.1335  -0.1164 98  LEU E O   
6974  C CB  . LEU E 98  ? 1.5435 1.0959 1.6447 0.1294  0.1308  -0.1373 98  LEU E CB  
6975  C CG  . LEU E 98  ? 1.6047 1.1520 1.7223 0.1217  0.1345  -0.1491 98  LEU E CG  
6976  C CD1 . LEU E 98  ? 1.6248 1.1952 1.7247 0.1328  0.1334  -0.1644 98  LEU E CD1 
6977  C CD2 . LEU E 98  ? 1.6228 1.1354 1.7404 0.1185  0.1416  -0.1388 98  LEU E CD2 
6978  N N   . LEU E 99  ? 1.5178 1.0478 1.6404 0.1085  0.1364  -0.1050 99  LEU E N   
6979  C CA  . LEU E 99  ? 1.5062 1.0322 1.6399 0.1004  0.1418  -0.0935 99  LEU E CA  
6980  C C   . LEU E 99  ? 1.5338 1.0705 1.6884 0.0876  0.1357  -0.0849 99  LEU E C   
6981  O O   . LEU E 99  ? 1.5164 1.0543 1.6852 0.0844  0.1367  -0.0754 99  LEU E O   
6982  C CB  . LEU E 99  ? 1.5059 1.0331 1.6246 0.1033  0.1562  -0.0902 99  LEU E CB  
6983  C CG  . LEU E 99  ? 1.5764 1.0870 1.6847 0.1100  0.1708  -0.0966 99  LEU E CG  
6984  C CD1 . LEU E 99  ? 1.5807 1.0852 1.6697 0.1169  0.1946  -0.0992 99  LEU E CD1 
6985  C CD2 . LEU E 99  ? 1.6039 1.1248 1.7321 0.1014  0.1713  -0.0953 99  LEU E CD2 
6986  N N   . VAL E 100 ? 1.4961 1.0405 1.6512 0.0820  0.1300  -0.0887 100 VAL E N   
6987  C CA  . VAL E 100 ? 1.4952 1.0429 1.6663 0.0686  0.1262  -0.0839 100 VAL E CA  
6988  C C   . VAL E 100 ? 1.5654 1.1002 1.7532 0.0688  0.1289  -0.0878 100 VAL E C   
6989  O O   . VAL E 100 ? 1.5700 1.1002 1.7703 0.0660  0.1327  -0.0729 100 VAL E O   
6990  C CB  . VAL E 100 ? 1.5403 1.0951 1.7079 0.0603  0.1212  -0.0927 100 VAL E CB  
6991  C CG1 . VAL E 100 ? 1.5374 1.0857 1.7196 0.0457  0.1189  -0.0954 100 VAL E CG1 
6992  C CG2 . VAL E 100 ? 1.5224 1.0896 1.6844 0.0553  0.1267  -0.0842 100 VAL E CG2 
6993  N N   . LEU E 101 ? 1.5212 1.0547 1.7110 0.0731  0.1309  -0.1077 101 LEU E N   
6994  C CA  . LEU E 101 ? 1.5231 1.0477 1.7361 0.0703  0.1430  -0.1182 101 LEU E CA  
6995  C C   . LEU E 101 ? 1.5442 1.0560 1.7703 0.0745  0.1504  -0.1016 101 LEU E C   
6996  O O   . LEU E 101 ? 1.5485 1.0472 1.7981 0.0724  0.1650  -0.0958 101 LEU E O   
6997  C CB  . LEU E 101 ? 1.5312 1.0729 1.7461 0.0720  0.1457  -0.1483 101 LEU E CB  
6998  C CG  . LEU E 101 ? 1.5940 1.1583 1.7964 0.0725  0.1373  -0.1701 101 LEU E CG  
6999  C CD1 . LEU E 101 ? 1.6047 1.1993 1.7952 0.0836  0.1331  -0.1892 101 LEU E CD1 
7000  C CD2 . LEU E 101 ? 1.6296 1.1929 1.8524 0.0605  0.1491  -0.1932 101 LEU E CD2 
7001  N N   . LEU E 102 ? 1.4650 0.9786 1.6764 0.0812  0.1438  -0.0951 102 LEU E N   
7002  C CA  . LEU E 102 ? 1.4492 0.9527 1.6708 0.0852  0.1483  -0.0845 102 LEU E CA  
7003  C C   . LEU E 102 ? 1.4503 0.9595 1.6756 0.0882  0.1470  -0.0610 102 LEU E C   
7004  O O   . LEU E 102 ? 1.4496 0.9523 1.6945 0.0926  0.1541  -0.0482 102 LEU E O   
7005  C CB  . LEU E 102 ? 1.4505 0.9510 1.6525 0.0904  0.1450  -0.0934 102 LEU E CB  
7006  C CG  . LEU E 102 ? 1.5232 1.0089 1.7409 0.0891  0.1517  -0.1002 102 LEU E CG  
7007  C CD1 . LEU E 102 ? 1.5305 1.0166 1.7364 0.0884  0.1520  -0.1212 102 LEU E CD1 
7008  C CD2 . LEU E 102 ? 1.5675 1.0453 1.7817 0.0936  0.1516  -0.0931 102 LEU E CD2 
7009  N N   . GLU E 103 ? 1.3746 0.9012 1.5839 0.0861  0.1400  -0.0554 103 GLU E N   
7010  C CA  . GLU E 103 ? 1.3646 0.9121 1.5777 0.0875  0.1388  -0.0365 103 GLU E CA  
7011  C C   . GLU E 103 ? 1.4197 0.9643 1.6447 0.0866  0.1416  -0.0201 103 GLU E C   
7012  O O   . GLU E 103 ? 1.4233 0.9823 1.6554 0.0948  0.1432  0.0006  103 GLU E O   
7013  C CB  . GLU E 103 ? 1.3638 0.9382 1.5631 0.0809  0.1369  -0.0400 103 GLU E CB  
7014  C CG  . GLU E 103 ? 1.4919 1.1022 1.6963 0.0837  0.1391  -0.0318 103 GLU E CG  
7015  C CD  . GLU E 103 ? 1.8072 1.4159 2.0148 0.0949  0.1428  -0.0382 103 GLU E CD  
7016  O OE1 . GLU E 103 ? 1.7610 1.3448 1.9590 0.0959  0.1475  -0.0557 103 GLU E OE1 
7017  O OE2 . GLU E 103 ? 1.7698 1.4038 1.9886 0.1035  0.1413  -0.0262 103 GLU E OE2 
7018  N N   . ASN E 104 ? 1.3786 0.9053 1.6047 0.0786  0.1446  -0.0309 104 ASN E N   
7019  C CA  . ASN E 104 ? 1.3902 0.9023 1.6261 0.0766  0.1544  -0.0215 104 ASN E CA  
7020  C C   . ASN E 104 ? 1.4675 0.9581 1.7253 0.0878  0.1733  -0.0119 104 ASN E C   
7021  O O   . ASN E 104 ? 1.4863 0.9691 1.7513 0.0961  0.1851  0.0111  104 ASN E O   
7022  C CB  . ASN E 104 ? 1.3697 0.8684 1.6028 0.0638  0.1561  -0.0458 104 ASN E CB  
7023  C CG  . ASN E 104 ? 1.5547 1.0684 1.7735 0.0508  0.1429  -0.0487 104 ASN E CG  
7024  O OD1 . ASN E 104 ? 1.4060 0.9396 1.6204 0.0474  0.1372  -0.0304 104 ASN E OD1 
7025  N ND2 . ASN E 104 ? 1.4685 0.9782 1.6832 0.0422  0.1395  -0.0740 104 ASN E ND2 
7026  N N   . GLU E 105 ? 1.4216 0.9038 1.6912 0.0880  0.1788  -0.0281 105 GLU E N   
7027  C CA  . GLU E 105 ? 1.4398 0.9035 1.7383 0.0941  0.2006  -0.0224 105 GLU E CA  
7028  C C   . GLU E 105 ? 1.4938 0.9673 1.7954 0.1102  0.1968  0.0084  105 GLU E C   
7029  O O   . GLU E 105 ? 1.4950 0.9553 1.8162 0.1219  0.2161  0.0306  105 GLU E O   
7030  C CB  . GLU E 105 ? 1.4501 0.9126 1.7594 0.0859  0.2032  -0.0496 105 GLU E CB  
7031  C CG  . GLU E 105 ? 1.6273 1.0722 1.9765 0.0818  0.2344  -0.0564 105 GLU E CG  
7032  C CD  . GLU E 105 ? 1.9155 1.3563 2.2808 0.0696  0.2581  -0.0844 105 GLU E CD  
7033  O OE1 . GLU E 105 ? 1.7377 1.1980 2.1008 0.0586  0.2534  -0.1176 105 GLU E OE1 
7034  O OE2 . GLU E 105 ? 1.8942 1.3147 2.2733 0.0724  0.2835  -0.0751 105 GLU E OE2 
7035  N N   . ARG E 106 ? 1.4532 0.9527 1.7356 0.1122  0.1753  0.0083  106 ARG E N   
7036  C CA  . ARG E 106 ? 1.4588 0.9821 1.7419 0.1268  0.1689  0.0279  106 ARG E CA  
7037  C C   . ARG E 106 ? 1.5353 1.0863 1.8105 0.1376  0.1661  0.0555  106 ARG E C   
7038  O O   . ARG E 106 ? 1.5481 1.1185 1.8312 0.1562  0.1679  0.0785  106 ARG E O   
7039  C CB  . ARG E 106 ? 1.4309 0.9737 1.6983 0.1227  0.1547  0.0086  106 ARG E CB  
7040  C CG  . ARG E 106 ? 1.5674 1.0865 1.8461 0.1204  0.1588  -0.0087 106 ARG E CG  
7041  C CD  . ARG E 106 ? 1.7305 1.2646 1.9953 0.1213  0.1512  -0.0250 106 ARG E CD  
7042  N NE  . ARG E 106 ? 1.9162 1.4447 2.1560 0.1113  0.1485  -0.0473 106 ARG E NE  
7043  C CZ  . ARG E 106 ? 2.1523 1.6817 2.3767 0.1103  0.1504  -0.0674 106 ARG E CZ  
7044  N NH1 . ARG E 106 ? 2.0188 1.5571 2.2508 0.1159  0.1524  -0.0741 106 ARG E NH1 
7045  N NH2 . ARG E 106 ? 1.9966 1.5170 2.1978 0.1052  0.1535  -0.0820 106 ARG E NH2 
7046  N N   . THR E 107 ? 1.4959 1.0519 1.7557 0.1262  0.1615  0.0530  107 THR E N   
7047  C CA  . THR E 107 ? 1.5095 1.0926 1.7601 0.1315  0.1591  0.0768  107 THR E CA  
7048  C C   . THR E 107 ? 1.6205 1.1737 1.8816 0.1473  0.1803  0.1039  107 THR E C   
7049  O O   . THR E 107 ? 1.6257 1.2035 1.8858 0.1684  0.1825  0.1353  107 THR E O   
7050  C CB  . THR E 107 ? 1.5849 1.1766 1.8202 0.1092  0.1498  0.0616  107 THR E CB  
7051  O OG1 . THR E 107 ? 1.5687 1.1867 1.7971 0.0981  0.1386  0.0404  107 THR E OG1 
7052  C CG2 . THR E 107 ? 1.5483 1.1689 1.7753 0.1090  0.1476  0.0832  107 THR E CG2 
7053  N N   . LEU E 108 ? 1.6223 1.1260 1.8938 0.1387  0.1995  0.0901  108 LEU E N   
7054  C CA  . LEU E 108 ? 1.6773 1.1417 1.9623 0.1508  0.2317  0.1084  108 LEU E CA  
7055  C C   . LEU E 108 ? 1.7993 1.2563 2.1089 0.1739  0.2505  0.1324  108 LEU E C   
7056  O O   . LEU E 108 ? 1.8404 1.2809 2.1563 0.1954  0.2754  0.1650  108 LEU E O   
7057  C CB  . LEU E 108 ? 1.6794 1.1014 1.9746 0.1318  0.2524  0.0753  108 LEU E CB  
7058  C CG  . LEU E 108 ? 1.7266 1.1469 2.0005 0.1123  0.2409  0.0555  108 LEU E CG  
7059  C CD1 . LEU E 108 ? 1.7145 1.1205 1.9961 0.0921  0.2444  0.0104  108 LEU E CD1 
7060  C CD2 . LEU E 108 ? 1.7963 1.1883 2.0628 0.1183  0.2631  0.0739  108 LEU E CD2 
7061  N N   . ASP E 109 ? 1.7614 1.2284 2.0845 0.1702  0.2403  0.1174  109 ASP E N   
7062  C CA  . ASP E 109 ? 1.7876 1.2501 2.1379 0.1880  0.2545  0.1359  109 ASP E CA  
7063  C C   . ASP E 109 ? 1.8328 1.3438 2.1703 0.2133  0.2353  0.1665  109 ASP E C   
7064  O O   . ASP E 109 ? 1.8606 1.3713 2.2168 0.2382  0.2505  0.1959  109 ASP E O   
7065  C CB  . ASP E 109 ? 1.7979 1.2519 2.1666 0.1705  0.2503  0.1036  109 ASP E CB  
7066  C CG  . ASP E 109 ? 2.0117 1.4286 2.4068 0.1507  0.2788  0.0766  109 ASP E CG  
7067  O OD1 . ASP E 109 ? 2.0410 1.4441 2.4285 0.1412  0.2900  0.0642  109 ASP E OD1 
7068  O OD2 . ASP E 109 ? 2.0906 1.4969 2.5154 0.1421  0.2903  0.0629  109 ASP E OD2 
7069  N N   . TYR E 110 ? 1.7515 1.3094 2.0602 0.2071  0.2054  0.1581  110 TYR E N   
7070  C CA  . TYR E 110 ? 1.7472 1.3693 2.0439 0.2273  0.1876  0.1777  110 TYR E CA  
7071  C C   . TYR E 110 ? 1.8782 1.5144 2.1645 0.2514  0.1981  0.2197  110 TYR E C   
7072  O O   . TYR E 110 ? 1.9011 1.5754 2.1901 0.2826  0.1981  0.2504  110 TYR E O   
7073  C CB  . TYR E 110 ? 1.7038 1.3740 1.9804 0.2076  0.1620  0.1485  110 TYR E CB  
7074  C CG  . TYR E 110 ? 1.6972 1.4463 1.9608 0.2210  0.1486  0.1631  110 TYR E CG  
7075  C CD1 . TYR E 110 ? 1.7206 1.5229 1.9914 0.2428  0.1418  0.1676  110 TYR E CD1 
7076  C CD2 . TYR E 110 ? 1.6934 1.4705 1.9398 0.2099  0.1434  0.1681  110 TYR E CD2 
7077  C CE1 . TYR E 110 ? 1.7218 1.6125 1.9828 0.2554  0.1307  0.1759  110 TYR E CE1 
7078  C CE2 . TYR E 110 ? 1.6962 1.5579 1.9340 0.2191  0.1329  0.1784  110 TYR E CE2 
7079  C CZ  . TYR E 110 ? 1.7762 1.6995 2.0212 0.2426  0.1268  0.1813  110 TYR E CZ  
7080  O OH  . TYR E 110 ? 1.7686 1.7902 2.0070 0.2521  0.1177  0.1868  110 TYR E OH  
7081  N N   . HIS E 111 ? 1.8717 1.4788 2.1445 0.2381  0.2070  0.2199  111 HIS E N   
7082  C CA  . HIS E 111 ? 1.9235 1.5308 2.1817 0.2574  0.2210  0.2571  111 HIS E CA  
7083  C C   . HIS E 111 ? 2.0384 1.6015 2.3155 0.2891  0.2579  0.2928  111 HIS E C   
7084  O O   . HIS E 111 ? 2.0642 1.6543 2.3331 0.3245  0.2650  0.3364  111 HIS E O   
7085  C CB  . HIS E 111 ? 1.9359 1.5050 2.1797 0.2304  0.2268  0.2391  111 HIS E CB  
7086  C CG  . HIS E 111 ? 1.9480 1.5674 2.1721 0.2061  0.1973  0.2207  111 HIS E CG  
7087  N ND1 . HIS E 111 ? 1.9829 1.6581 2.1886 0.2153  0.1874  0.2451  111 HIS E ND1 
7088  C CD2 . HIS E 111 ? 1.9318 1.5536 2.1549 0.1731  0.1806  0.1813  111 HIS E CD2 
7089  C CE1 . HIS E 111 ? 1.9350 1.6451 2.1343 0.1834  0.1670  0.2170  111 HIS E CE1 
7090  N NE2 . HIS E 111 ? 1.9087 1.5854 2.1176 0.1591  0.1632  0.1801  111 HIS E NE2 
7091  N N   . ASP E 112 ? 2.0135 1.5147 2.3187 0.2767  0.2839  0.2734  112 ASP E N   
7092  C CA  . ASP E 112 ? 2.0607 1.5126 2.3968 0.2978  0.3289  0.2973  112 ASP E CA  
7093  C C   . ASP E 112 ? 2.1306 1.6201 2.4807 0.3321  0.3242  0.3311  112 ASP E C   
7094  O O   . ASP E 112 ? 2.1762 1.6522 2.5345 0.3679  0.3551  0.3763  112 ASP E O   
7095  C CB  . ASP E 112 ? 2.0662 1.4689 2.4350 0.2673  0.3498  0.2553  112 ASP E CB  
7096  C CG  . ASP E 112 ? 2.2500 1.6095 2.6642 0.2799  0.3992  0.2698  112 ASP E CG  
7097  O OD1 . ASP E 112 ? 2.2291 1.5919 2.6735 0.2689  0.3960  0.2524  112 ASP E OD1 
7098  O OD2 . ASP E 112 ? 2.3941 1.7137 2.8156 0.2990  0.4453  0.2973  112 ASP E OD2 
7099  N N   . SER E 113 ? 2.0529 1.5890 2.4045 0.3226  0.2878  0.3082  113 SER E N   
7100  C CA  . SER E 113 ? 2.0612 1.6409 2.4260 0.3504  0.2770  0.3277  113 SER E CA  
7101  C C   . SER E 113 ? 2.1548 1.8059 2.4924 0.3876  0.2614  0.3667  113 SER E C   
7102  O O   . SER E 113 ? 2.1871 1.8663 2.5371 0.4248  0.2667  0.3997  113 SER E O   
7103  C CB  . SER E 113 ? 2.0485 1.6539 2.4181 0.3257  0.2456  0.2830  113 SER E CB  
7104  O OG  . SER E 113 ? 2.1225 1.6706 2.5235 0.3008  0.2628  0.2559  113 SER E OG  
7105  N N   . ASN E 114 ? 1.8683 1.3602 2.2930 0.3253  0.3551  0.2831  114 ASN E N   
7106  C CA  . ASN E 114 ? 1.8550 1.3480 2.2883 0.3190  0.3717  0.2760  114 ASN E CA  
7107  C C   . ASN E 114 ? 1.9154 1.4057 2.3482 0.3085  0.3611  0.2723  114 ASN E C   
7108  O O   . ASN E 114 ? 1.9017 1.3864 2.3244 0.3039  0.3659  0.2646  114 ASN E O   
7109  C CB  . ASN E 114 ? 1.8576 1.3620 2.3203 0.3175  0.3955  0.2833  114 ASN E CB  
7110  C CG  . ASN E 114 ? 2.1581 1.6655 2.6232 0.3294  0.4150  0.2858  114 ASN E CG  
7111  O OD1 . ASN E 114 ? 2.1022 1.6209 2.5945 0.3323  0.4299  0.2989  114 ASN E OD1 
7112  N ND2 . ASN E 114 ? 2.0552 1.5504 2.4954 0.3372  0.4188  0.2736  114 ASN E ND2 
7113  N N   . VAL E 115 ? 1.8938 1.3882 2.3380 0.3052  0.3474  0.2775  115 VAL E N   
7114  C CA  . VAL E 115 ? 1.9010 1.3899 2.3461 0.2974  0.3410  0.2723  115 VAL E CA  
7115  C C   . VAL E 115 ? 1.9559 1.4351 2.3722 0.2975  0.3335  0.2642  115 VAL E C   
7116  O O   . VAL E 115 ? 1.9495 1.4214 2.3586 0.2943  0.3382  0.2592  115 VAL E O   
7117  C CB  . VAL E 115 ? 1.9607 1.4577 2.4290 0.2948  0.3297  0.2771  115 VAL E CB  
7118  C CG1 . VAL E 115 ? 1.9653 1.4536 2.4313 0.2888  0.3262  0.2674  115 VAL E CG1 
7119  C CG2 . VAL E 115 ? 1.9501 1.4535 2.4571 0.2932  0.3413  0.2873  115 VAL E CG2 
7120  N N   . LYS E 116 ? 1.9220 1.3987 2.3220 0.3003  0.3239  0.2644  116 LYS E N   
7121  C CA  . LYS E 116 ? 1.9311 1.3943 2.3083 0.2982  0.3218  0.2588  116 LYS E CA  
7122  C C   . LYS E 116 ? 1.9754 1.4304 2.3460 0.3020  0.3312  0.2554  116 LYS E C   
7123  O O   . LYS E 116 ? 1.9747 1.4235 2.3399 0.2995  0.3328  0.2533  116 LYS E O   
7124  C CB  . LYS E 116 ? 1.9861 1.4407 2.3448 0.2966  0.3136  0.2598  116 LYS E CB  
7125  C CG  . LYS E 116 ? 2.2491 1.7147 2.6112 0.2893  0.3007  0.2614  116 LYS E CG  
7126  C CD  . LYS E 116 ? 2.4587 1.9117 2.7927 0.2825  0.2925  0.2614  116 LYS E CD  
7127  C CE  . LYS E 116 ? 2.6834 2.1435 3.0153 0.2876  0.2803  0.2707  116 LYS E CE  
7128  N NZ  . LYS E 116 ? 2.8383 2.2853 3.1642 0.3003  0.2909  0.2733  116 LYS E NZ  
7129  N N   . ASN E 117 ? 1.9219 1.3789 2.2963 0.3080  0.3390  0.2552  117 ASN E N   
7130  C CA  . ASN E 117 ? 1.9142 1.3672 2.2867 0.3111  0.3481  0.2495  117 ASN E CA  
7131  C C   . ASN E 117 ? 1.9750 1.4383 2.3543 0.3057  0.3513  0.2489  117 ASN E C   
7132  O O   . ASN E 117 ? 1.9735 1.4359 2.3497 0.3057  0.3521  0.2454  117 ASN E O   
7133  C CB  . ASN E 117 ? 1.8963 1.3476 2.2704 0.3191  0.3603  0.2461  117 ASN E CB  
7134  C CG  . ASN E 117 ? 2.1675 1.5964 2.5253 0.3249  0.3593  0.2438  117 ASN E CG  
7135  O OD1 . ASN E 117 ? 2.0547 1.4745 2.4000 0.3209  0.3480  0.2481  117 ASN E OD1 
7136  N ND2 . ASN E 117 ? 2.1055 1.5219 2.4611 0.3331  0.3734  0.2353  117 ASN E ND2 
7137  N N   . LEU E 118 ? 1.9392 1.4090 2.3277 0.2999  0.3531  0.2524  118 LEU E N   
7138  C CA  . LEU E 118 ? 1.9460 1.4158 2.3333 0.2918  0.3576  0.2515  118 LEU E CA  
7139  C C   . LEU E 118 ? 2.0252 1.4874 2.4018 0.2912  0.3483  0.2523  118 LEU E C   
7140  O O   . LEU E 118 ? 2.0273 1.4882 2.3943 0.2885  0.3476  0.2524  118 LEU E O   
7141  C CB  . LEU E 118 ? 1.9450 1.4140 2.3473 0.2841  0.3681  0.2543  118 LEU E CB  
7142  C CG  . LEU E 118 ? 2.0105 1.4726 2.4067 0.2715  0.3799  0.2519  118 LEU E CG  
7143  C CD1 . LEU E 118 ? 2.0078 1.4722 2.4211 0.2631  0.4017  0.2534  118 LEU E CD1 
7144  C CD2 . LEU E 118 ? 2.0517 1.4955 2.4416 0.2658  0.3775  0.2517  118 LEU E CD2 
7145  N N   . TYR E 119 ? 1.9995 1.4581 2.3775 0.2934  0.3427  0.2532  119 TYR E N   
7146  C CA  . TYR E 119 ? 2.0129 1.4646 2.3834 0.2935  0.3409  0.2533  119 TYR E CA  
7147  C C   . TYR E 119 ? 2.0716 1.5216 2.4359 0.2970  0.3393  0.2560  119 TYR E C   
7148  O O   . TYR E 119 ? 2.0707 1.5182 2.4313 0.2980  0.3407  0.2597  119 TYR E O   
7149  C CB  . TYR E 119 ? 2.0355 1.4863 2.4111 0.2919  0.3395  0.2508  119 TYR E CB  
7150  C CG  . TYR E 119 ? 2.0680 1.5129 2.4365 0.2913  0.3441  0.2497  119 TYR E CG  
7151  C CD1 . TYR E 119 ? 2.0991 1.5372 2.4646 0.2927  0.3527  0.2487  119 TYR E CD1 
7152  C CD2 . TYR E 119 ? 2.0828 1.5256 2.4461 0.2882  0.3441  0.2496  119 TYR E CD2 
7153  C CE1 . TYR E 119 ? 2.1175 1.5513 2.4798 0.2930  0.3635  0.2487  119 TYR E CE1 
7154  C CE2 . TYR E 119 ? 2.1018 1.5384 2.4614 0.2846  0.3555  0.2490  119 TYR E CE2 
7155  C CZ  . TYR E 119 ? 2.2023 1.6368 2.5639 0.2881  0.3664  0.2489  119 TYR E CZ  
7156  O OH  . TYR E 119 ? 2.2183 1.6478 2.5795 0.2855  0.3838  0.2493  119 TYR E OH  
7157  N N   . GLU E 120 ? 2.0358 1.4842 2.4011 0.2994  0.3383  0.2547  120 GLU E N   
7158  C CA  . GLU E 120 ? 2.0437 1.4838 2.4095 0.3018  0.3398  0.2560  120 GLU E CA  
7159  C C   . GLU E 120 ? 2.1051 1.5536 2.4764 0.3043  0.3381  0.2565  120 GLU E C   
7160  O O   . GLU E 120 ? 2.1023 1.5463 2.4814 0.3063  0.3380  0.2599  120 GLU E O   
7161  C CB  . GLU E 120 ? 2.0658 1.4918 2.4275 0.3030  0.3422  0.2519  120 GLU E CB  
7162  C CG  . GLU E 120 ? 2.2231 1.6299 2.5778 0.2970  0.3467  0.2534  120 GLU E CG  
7163  C CD  . GLU E 120 ? 2.5202 1.9322 2.8688 0.2899  0.3455  0.2542  120 GLU E CD  
7164  O OE1 . GLU E 120 ? 2.4090 1.8234 2.7502 0.2876  0.3394  0.2519  120 GLU E OE1 
7165  O OE2 . GLU E 120 ? 2.4958 1.9104 2.8488 0.2873  0.3517  0.2571  120 GLU E OE2 
7166  N N   . LYS E 121 ? 2.0709 1.5312 2.4403 0.3020  0.3379  0.2537  121 LYS E N   
7167  C CA  . LYS E 121 ? 2.0778 1.5491 2.4478 0.3000  0.3355  0.2527  121 LYS E CA  
7168  C C   . LYS E 121 ? 2.1667 1.6395 2.5288 0.2978  0.3284  0.2615  121 LYS E C   
7169  O O   . LYS E 121 ? 2.1764 1.6563 2.5429 0.2995  0.3211  0.2667  121 LYS E O   
7170  C CB  . LYS E 121 ? 2.1015 1.5813 2.4690 0.2936  0.3439  0.2461  121 LYS E CB  
7171  C CG  . LYS E 121 ? 2.2133 1.7066 2.5806 0.2886  0.3443  0.2409  121 LYS E CG  
7172  C CD  . LYS E 121 ? 2.2739 1.7727 2.6340 0.2757  0.3573  0.2359  121 LYS E CD  
7173  C CE  . LYS E 121 ? 2.3530 1.8668 2.7073 0.2660  0.3565  0.2301  121 LYS E CE  
7174  N NZ  . LYS E 121 ? 2.4381 1.9521 2.7801 0.2474  0.3728  0.2259  121 LYS E NZ  
7175  N N   . VAL E 122 ? 2.1359 1.6006 2.4883 0.2951  0.3313  0.2632  122 VAL E N   
7176  C CA  . VAL E 122 ? 2.1505 1.6090 2.4906 0.2948  0.3297  0.2700  122 VAL E CA  
7177  C C   . VAL E 122 ? 2.1994 1.6562 2.5481 0.3026  0.3306  0.2788  122 VAL E C   
7178  O O   . VAL E 122 ? 2.2045 1.6646 2.5509 0.3059  0.3264  0.2891  122 VAL E O   
7179  C CB  . VAL E 122 ? 2.2049 1.6481 2.5364 0.2904  0.3383  0.2651  122 VAL E CB  
7180  C CG1 . VAL E 122 ? 2.2206 1.6496 2.5362 0.2923  0.3414  0.2695  122 VAL E CG1 
7181  C CG2 . VAL E 122 ? 2.2039 1.6450 2.5320 0.2798  0.3431  0.2591  122 VAL E CG2 
7182  N N   . ARG E 123 ? 2.1459 1.5971 2.5044 0.3040  0.3376  0.2761  123 ARG E N   
7183  C CA  . ARG E 123 ? 2.1465 1.5919 2.5149 0.3067  0.3464  0.2830  123 ARG E CA  
7184  C C   . ARG E 123 ? 2.2116 1.6600 2.5971 0.3095  0.3432  0.2917  123 ARG E C   
7185  O O   . ARG E 123 ? 2.2152 1.6614 2.6129 0.3121  0.3510  0.3036  123 ARG E O   
7186  C CB  . ARG E 123 ? 2.1360 1.5725 2.5051 0.3020  0.3546  0.2756  123 ARG E CB  
7187  C CG  . ARG E 123 ? 2.2364 1.6650 2.6091 0.2996  0.3717  0.2790  123 ARG E CG  
7188  C CD  . ARG E 123 ? 2.3397 1.7552 2.7165 0.2917  0.3799  0.2777  123 ARG E CD  
7189  N NE  . ARG E 123 ? 2.4518 1.8601 2.8421 0.2936  0.3785  0.2847  123 ARG E NE  
7190  C CZ  . ARG E 123 ? 2.5928 1.9883 2.9822 0.2912  0.3748  0.2789  123 ARG E CZ  
7191  N NH1 . ARG E 123 ? 2.4133 1.8038 2.7861 0.2871  0.3706  0.2692  123 ARG E NH1 
7192  N NH2 . ARG E 123 ? 2.3798 1.7657 2.7864 0.2937  0.3761  0.2831  123 ARG E NH2 
7193  N N   . SER E 124 ? 2.1719 1.6245 2.5626 0.3092  0.3350  0.2857  124 SER E N   
7194  C CA  . SER E 124 ? 2.1756 1.6293 2.5881 0.3119  0.3320  0.2903  124 SER E CA  
7195  C C   . SER E 124 ? 2.2577 1.7310 2.6750 0.3145  0.3186  0.3005  124 SER E C   
7196  O O   . SER E 124 ? 2.2585 1.7356 2.7013 0.3178  0.3154  0.3098  124 SER E O   
7197  C CB  . SER E 124 ? 2.2085 1.6572 2.6243 0.3118  0.3321  0.2764  124 SER E CB  
7198  O OG  . SER E 124 ? 2.3089 1.7354 2.7193 0.3097  0.3430  0.2702  124 SER E OG  
7199  N N   . GLN E 125 ? 2.2348 1.7179 2.6283 0.3118  0.3109  0.2993  125 GLN E N   
7200  C CA  . GLN E 125 ? 2.2546 1.7536 2.6408 0.3112  0.2963  0.3089  125 GLN E CA  
7201  C C   . GLN E 125 ? 2.3265 1.8222 2.7095 0.3175  0.2987  0.3268  125 GLN E C   
7202  O O   . GLN E 125 ? 2.3433 1.8519 2.7251 0.3198  0.2854  0.3406  125 GLN E O   
7203  C CB  . GLN E 125 ? 2.2814 1.7831 2.6380 0.3014  0.2921  0.2985  125 GLN E CB  
7204  C CG  . GLN E 125 ? 2.4999 2.0124 2.8617 0.2948  0.2915  0.2838  125 GLN E CG  
7205  C CD  . GLN E 125 ? 2.8210 2.3297 3.1577 0.2824  0.2983  0.2735  125 GLN E CD  
7206  O OE1 . GLN E 125 ? 2.7879 2.2806 3.1164 0.2811  0.3096  0.2701  125 GLN E OE1 
7207  N NE2 . GLN E 125 ? 2.7435 2.2663 3.0707 0.2711  0.2936  0.2680  125 GLN E NE2 
7208  N N   . LEU E 126 ? 2.2734 1.7528 2.6548 0.3202  0.3167  0.3262  126 LEU E N   
7209  C CA  . LEU E 126 ? 2.5370 2.0103 2.9160 0.3272  0.3284  0.3397  126 LEU E CA  
7210  C C   . LEU E 126 ? 2.6194 2.0866 3.0280 0.3298  0.3480  0.3475  126 LEU E C   
7211  O O   . LEU E 126 ? 2.1068 1.5748 2.5277 0.3365  0.3599  0.3645  126 LEU E O   
7212  C CB  . LEU E 126 ? 2.5449 2.0016 2.8954 0.3259  0.3395  0.3284  126 LEU E CB  
7213  C CG  . LEU E 126 ? 2.6214 2.0730 2.9417 0.3187  0.3278  0.3189  126 LEU E CG  
7214  C CD1 . LEU E 126 ? 2.6199 2.0521 2.9281 0.3147  0.3413  0.3028  126 LEU E CD1 
7215  C CD2 . LEU E 126 ? 2.6855 2.1347 2.9822 0.3213  0.3193  0.3314  126 LEU E CD2 
7216  N N   . CYS E 148 ? 2.3879 2.3423 2.5129 0.3650  -0.3138 0.2754  148 CYS E N   
7217  C CA  . CYS E 148 ? 2.3862 2.3419 2.5121 0.3643  -0.3145 0.2771  148 CYS E CA  
7218  C C   . CYS E 148 ? 2.4524 2.4055 2.5774 0.3633  -0.3138 0.2782  148 CYS E C   
7219  O O   . CYS E 148 ? 2.4445 2.3970 2.5695 0.3626  -0.3139 0.2775  148 CYS E O   
7220  C CB  . CYS E 148 ? 2.3861 2.3448 2.5129 0.3659  -0.3159 0.2799  148 CYS E CB  
7221  S SG  . CYS E 148 ? 2.4316 2.3907 2.5602 0.3655  -0.3184 0.2827  148 CYS E SG  
7222  N N   . MET E 149 ? 2.4241 2.3758 2.5483 0.3635  -0.3130 0.2800  149 MET E N   
7223  C CA  . MET E 149 ? 2.4269 2.3764 2.5507 0.3621  -0.3121 0.2815  149 MET E CA  
7224  C C   . MET E 149 ? 2.4800 2.4295 2.6054 0.3610  -0.3106 0.2799  149 MET E C   
7225  O O   . MET E 149 ? 2.4727 2.4221 2.5989 0.3599  -0.3098 0.2805  149 MET E O   
7226  C CB  . MET E 149 ? 2.4581 2.4061 2.5811 0.3624  -0.3119 0.2852  149 MET E CB  
7227  C CG  . MET E 149 ? 2.5068 2.4518 2.6292 0.3611  -0.3123 0.2880  149 MET E CG  
7228  S SD  . MET E 149 ? 2.5619 2.5058 2.6844 0.3625  -0.3159 0.2925  149 MET E SD  
7229  C CE  . MET E 149 ? 2.5215 2.4598 2.6428 0.3607  -0.3162 0.2960  149 MET E CE  
7230  N N   . GLU E 150 ? 2.4395 2.3896 2.5660 0.3615  -0.3106 0.2782  150 GLU E N   
7231  C CA  . GLU E 150 ? 2.4349 2.3855 2.5647 0.3607  -0.3104 0.2771  150 GLU E CA  
7232  C C   . GLU E 150 ? 2.4748 2.4271 2.6075 0.3602  -0.3106 0.2769  150 GLU E C   
7233  O O   . GLU E 150 ? 2.4657 2.4198 2.6029 0.3595  -0.3106 0.2775  150 GLU E O   
7234  C CB  . GLU E 150 ? 2.4541 2.4039 2.5839 0.3622  -0.3118 0.2753  150 GLU E CB  
7235  C CG  . GLU E 150 ? 2.5806 2.5293 2.7083 0.3632  -0.3112 0.2760  150 GLU E CG  
7236  C CD  . GLU E 150 ? 2.8144 2.7632 2.9381 0.3650  -0.3106 0.2779  150 GLU E CD  
7237  O OE1 . GLU E 150 ? 2.7113 2.6609 2.8334 0.3670  -0.3117 0.2769  150 GLU E OE1 
7238  O OE2 . GLU E 150 ? 2.7224 2.6707 2.8455 0.3643  -0.3094 0.2811  150 GLU E OE2 
7239  N N   . SER E 151 ? 2.4253 2.3777 2.5564 0.3608  -0.3109 0.2765  151 SER E N   
7240  C CA  . SER E 151 ? 2.4169 2.3708 2.5498 0.3610  -0.3107 0.2770  151 SER E CA  
7241  C C   . SER E 151 ? 2.4495 2.4050 2.5826 0.3611  -0.3095 0.2786  151 SER E C   
7242  O O   . SER E 151 ? 2.4392 2.3975 2.5759 0.3617  -0.3090 0.2801  151 SER E O   
7243  C CB  . SER E 151 ? 2.4617 2.4149 2.5923 0.3615  -0.3112 0.2762  151 SER E CB  
7244  O OG  . SER E 151 ? 2.5651 2.5177 2.6925 0.3617  -0.3115 0.2760  151 SER E OG  
7245  N N   . VAL E 152 ? 2.3998 2.3536 2.5295 0.3609  -0.3092 0.2789  152 VAL E N   
7246  C CA  . VAL E 152 ? 2.3946 2.3488 2.5234 0.3611  -0.3083 0.2801  152 VAL E CA  
7247  C C   . VAL E 152 ? 2.4455 2.4022 2.5790 0.3595  -0.3071 0.2814  152 VAL E C   
7248  O O   . VAL E 152 ? 2.4358 2.3959 2.5720 0.3598  -0.3061 0.2827  152 VAL E O   
7249  C CB  . VAL E 152 ? 2.4402 2.3905 2.5643 0.3612  -0.3095 0.2805  152 VAL E CB  
7250  C CG1 . VAL E 152 ? 2.4373 2.3869 2.5593 0.3621  -0.3093 0.2814  152 VAL E CG1 
7251  C CG2 . VAL E 152 ? 2.4382 2.3871 2.5599 0.3624  -0.3115 0.2794  152 VAL E CG2 
7252  N N   . LYS E 153 ? 2.4095 2.3650 2.5442 0.3579  -0.3072 0.2812  153 LYS E N   
7253  C CA  . LYS E 153 ? 2.4087 2.3664 2.5484 0.3560  -0.3064 0.2822  153 LYS E CA  
7254  C C   . LYS E 153 ? 2.4669 2.4296 2.6138 0.3563  -0.3071 0.2824  153 LYS E C   
7255  O O   . LYS E 153 ? 2.4605 2.4278 2.6133 0.3551  -0.3064 0.2841  153 LYS E O   
7256  C CB  . LYS E 153 ? 2.4387 2.3936 2.5772 0.3554  -0.3067 0.2817  153 LYS E CB  
7257  C CG  . LYS E 153 ? 2.5808 2.5317 2.7141 0.3552  -0.3061 0.2833  153 LYS E CG  
7258  C CD  . LYS E 153 ? 2.6701 2.6191 2.8014 0.3562  -0.3065 0.2834  153 LYS E CD  
7259  C CE  . LYS E 153 ? 2.7599 2.7060 2.8873 0.3568  -0.3065 0.2864  153 LYS E CE  
7260  N NZ  . LYS E 153 ? 2.8584 2.8041 2.9836 0.3591  -0.3068 0.2869  153 LYS E NZ  
7261  N N   . ASN E 154 ? 2.4259 2.3880 2.5731 0.3578  -0.3088 0.2814  154 ASN E N   
7262  C CA  . ASN E 154 ? 2.7428 2.7085 2.8971 0.3584  -0.3106 0.2826  154 ASN E CA  
7263  C C   . ASN E 154 ? 2.8838 2.8525 3.0389 0.3602  -0.3099 0.2848  154 ASN E C   
7264  O O   . ASN E 154 ? 2.3059 2.2769 2.4595 0.3607  -0.3080 0.2859  154 ASN E O   
7265  C CB  . ASN E 154 ? 2.7537 2.7158 2.9075 0.3591  -0.3132 0.2809  154 ASN E CB  
7266  C CG  . ASN E 154 ? 3.0410 3.0052 3.2033 0.3592  -0.3166 0.2822  154 ASN E CG  
7267  O OD1 . ASN E 154 ? 2.9749 2.9429 3.1434 0.3600  -0.3177 0.2854  154 ASN E OD1 
7268  N ND2 . ASN E 154 ? 2.9325 2.8942 3.0953 0.3590  -0.3187 0.2802  154 ASN E ND2 
7269  N N   . TYR E 159 ? 2.8167 2.4619 2.5550 0.3399  -0.0573 0.3905  159 TYR E N   
7270  C CA  . TYR E 159 ? 2.7948 2.4640 2.5555 0.3440  -0.0260 0.3851  159 TYR E CA  
7271  C C   . TYR E 159 ? 2.8535 2.5221 2.6227 0.3482  -0.0225 0.3940  159 TYR E C   
7272  O O   . TYR E 159 ? 2.8426 2.5109 2.6151 0.3578  -0.0023 0.3839  159 TYR E O   
7273  C CB  . TYR E 159 ? 2.7838 2.4909 2.5684 0.3342  -0.0145 0.3859  159 TYR E CB  
7274  C CG  . TYR E 159 ? 2.7813 2.5044 2.5792 0.3429  0.0131  0.3771  159 TYR E CG  
7275  C CD1 . TYR E 159 ? 2.7991 2.5102 2.5917 0.3498  0.0273  0.3626  159 TYR E CD1 
7276  C CD2 . TYR E 159 ? 2.7788 2.5281 2.5934 0.3451  0.0216  0.3856  159 TYR E CD2 
7277  C CE1 . TYR E 159 ? 2.7914 2.5118 2.5939 0.3584  0.0448  0.3570  159 TYR E CE1 
7278  C CE2 . TYR E 159 ? 2.7777 2.5378 2.5986 0.3555  0.0408  0.3768  159 TYR E CE2 
7279  C CZ  . TYR E 159 ? 2.8550 2.5985 2.6695 0.3620  0.0501  0.3627  159 TYR E CZ  
7280  O OH  . TYR E 159 ? 2.8487 2.5977 2.6673 0.3728  0.0615  0.3566  159 TYR E OH  
7281  N N   . PRO E 160 ? 2.8202 2.4875 2.5945 0.3406  -0.0429 0.4138  160 PRO E N   
7282  C CA  . PRO E 160 ? 2.8168 2.4808 2.6004 0.3433  -0.0372 0.4211  160 PRO E CA  
7283  C C   . PRO E 160 ? 2.8719 2.4953 2.6354 0.3567  -0.0351 0.4107  160 PRO E C   
7284  O O   . PRO E 160 ? 2.8566 2.4810 2.6303 0.3588  -0.0226 0.4090  160 PRO E O   
7285  C CB  . PRO E 160 ? 2.8503 2.5156 2.6425 0.3312  -0.0649 0.4493  160 PRO E CB  
7286  C CG  . PRO E 160 ? 2.9030 2.5934 2.7015 0.3205  -0.0780 0.4567  160 PRO E CG  
7287  C CD  . PRO E 160 ? 2.8502 2.5207 2.6255 0.3274  -0.0741 0.4332  160 PRO E CD  
7288  N N   . LYS E 161 ? 2.8464 2.4357 2.5803 0.3672  -0.0476 0.4039  161 LYS E N   
7289  C CA  . LYS E 161 ? 2.8603 2.4127 2.5715 0.3849  -0.0456 0.3957  161 LYS E CA  
7290  C C   . LYS E 161 ? 2.8975 2.4701 2.6198 0.3931  -0.0144 0.3796  161 LYS E C   
7291  O O   . LYS E 161 ? 2.8913 2.4507 2.6119 0.4025  -0.0062 0.3751  161 LYS E O   
7292  C CB  . LYS E 161 ? 2.9182 2.4318 2.5898 0.3988  -0.0694 0.3953  161 LYS E CB  
7293  C CG  . LYS E 161 ? 3.0459 2.5141 2.6876 0.4215  -0.0751 0.3931  161 LYS E CG  
7294  C CD  . LYS E 161 ? 3.1423 2.5779 2.7394 0.4429  -0.0932 0.3897  161 LYS E CD  
7295  C CE  . LYS E 161 ? 3.2000 2.5968 2.7661 0.4718  -0.0930 0.3870  161 LYS E CE  
7296  N NZ  . LYS E 161 ? 3.2167 2.6441 2.7993 0.4813  -0.0566 0.3765  161 LYS E NZ  
7297  N N   . TYR E 162 ? 2.8464 2.4491 2.5810 0.3888  -0.0002 0.3725  162 TYR E N   
7298  C CA  . TYR E 162 ? 2.8314 2.4520 2.5778 0.3952  0.0228  0.3620  162 TYR E CA  
7299  C C   . TYR E 162 ? 2.8596 2.5148 2.6333 0.3856  0.0366  0.3595  162 TYR E C   
7300  O O   . TYR E 162 ? 2.8464 2.5134 2.6291 0.3902  0.0494  0.3531  162 TYR E O   
7301  C CB  . TYR E 162 ? 2.8534 2.4686 2.5850 0.4036  0.0251  0.3579  162 TYR E CB  
7302  C CG  . TYR E 162 ? 2.9036 2.4879 2.6039 0.4222  0.0159  0.3593  162 TYR E CG  
7303  C CD1 . TYR E 162 ? 2.9571 2.5128 2.6281 0.4253  -0.0086 0.3631  162 TYR E CD1 
7304  C CD2 . TYR E 162 ? 2.9122 2.4967 2.6102 0.4390  0.0291  0.3586  162 TYR E CD2 
7305  C CE1 . TYR E 162 ? 2.9969 2.5198 2.6310 0.4485  -0.0197 0.3642  162 TYR E CE1 
7306  C CE2 . TYR E 162 ? 2.9490 2.5075 2.6148 0.4618  0.0219  0.3615  162 TYR E CE2 
7307  C CZ  . TYR E 162 ? 3.0575 2.5828 2.6883 0.4683  -0.0023 0.3632  162 TYR E CZ  
7308  O OH  . TYR E 162 ? 3.0720 2.5672 2.6632 0.4963  -0.0121 0.3658  162 TYR E OH  
7309  N N   . SER E 163 ? 2.8042 2.4749 2.5892 0.3748  0.0313  0.3674  163 SER E N   
7310  C CA  . SER E 163 ? 2.7798 2.4833 2.5840 0.3711  0.0424  0.3669  163 SER E CA  
7311  C C   . SER E 163 ? 2.8092 2.5195 2.6221 0.3770  0.0532  0.3593  163 SER E C   
7312  O O   . SER E 163 ? 2.7941 2.5211 2.6137 0.3814  0.0611  0.3531  163 SER E O   
7313  C CB  . SER E 163 ? 2.8225 2.5449 2.6364 0.3615  0.0338  0.3824  163 SER E CB  
7314  O OG  . SER E 163 ? 2.9160 2.6722 2.7434 0.3634  0.0449  0.3831  163 SER E OG  
7315  N N   . GLU E 164 ? 2.7604 2.4543 2.5712 0.3773  0.0502  0.3595  164 GLU E N   
7316  C CA  . GLU E 164 ? 2.7397 2.4380 2.5587 0.3801  0.0571  0.3508  164 GLU E CA  
7317  C C   . GLU E 164 ? 2.7591 2.4541 2.5778 0.3887  0.0619  0.3414  164 GLU E C   
7318  O O   . GLU E 164 ? 2.7388 2.4472 2.5668 0.3908  0.0644  0.3345  164 GLU E O   
7319  C CB  . GLU E 164 ? 2.7628 2.4406 2.5809 0.3758  0.0516  0.3542  164 GLU E CB  
7320  C CG  . GLU E 164 ? 2.8962 2.5369 2.6986 0.3822  0.0453  0.3535  164 GLU E CG  
7321  C CD  . GLU E 164 ? 3.0968 2.7149 2.8798 0.3853  0.0321  0.3630  164 GLU E CD  
7322  O OE1 . GLU E 164 ? 3.0234 2.6317 2.8040 0.3775  0.0178  0.3763  164 GLU E OE1 
7323  O OE2 . GLU E 164 ? 2.9459 2.5559 2.7154 0.3960  0.0334  0.3590  164 GLU E OE2 
7324  N N   . GLU E 165 ? 2.7079 2.3864 2.5151 0.3945  0.0605  0.3438  165 GLU E N   
7325  C CA  . GLU E 165 ? 2.6922 2.3707 2.5004 0.4038  0.0646  0.3424  165 GLU E CA  
7326  C C   . GLU E 165 ? 2.7046 2.3995 2.5222 0.4035  0.0670  0.3425  165 GLU E C   
7327  O O   . GLU E 165 ? 2.6893 2.3921 2.5173 0.4077  0.0666  0.3431  165 GLU E O   
7328  C CB  . GLU E 165 ? 2.7278 2.3854 2.5164 0.4131  0.0622  0.3476  165 GLU E CB  
7329  C CG  . GLU E 165 ? 2.8709 2.5315 2.6603 0.4262  0.0674  0.3517  165 GLU E CG  
7330  C CD  . GLU E 165 ? 3.1843 2.8281 2.9497 0.4392  0.0657  0.3576  165 GLU E CD  
7331  O OE1 . GLU E 165 ? 3.1574 2.7784 2.9019 0.4505  0.0603  0.3585  165 GLU E OE1 
7332  O OE2 . GLU E 165 ? 3.1297 2.7794 2.8942 0.4393  0.0680  0.3612  165 GLU E OE2 
7333  N N   . ALA E 166 ? 2.6428 2.3407 2.4569 0.3984  0.0667  0.3435  166 ALA E N   
7334  C CA  . ALA E 166 ? 2.6249 2.3296 2.4437 0.3989  0.0678  0.3434  166 ALA E CA  
7335  C C   . ALA E 166 ? 2.6344 2.3520 2.4612 0.4022  0.0652  0.3395  166 ALA E C   
7336  O O   . ALA E 166 ? 2.6209 2.3353 2.4512 0.4075  0.0608  0.3409  166 ALA E O   
7337  C CB  . ALA E 166 ? 2.6396 2.3448 2.4525 0.3923  0.0674  0.3446  166 ALA E CB  
7338  N N   . LYS E 167 ? 2.5723 2.3019 2.4002 0.4004  0.0652  0.3364  167 LYS E N   
7339  C CA  . LYS E 167 ? 2.5590 2.3012 2.3882 0.4066  0.0609  0.3314  167 LYS E CA  
7340  C C   . LYS E 167 ? 2.5764 2.3152 2.4113 0.4102  0.0521  0.3273  167 LYS E C   
7341  O O   . LYS E 167 ? 2.5736 2.3139 2.4060 0.4183  0.0412  0.3250  167 LYS E O   
7342  C CB  . LYS E 167 ? 2.5941 2.3521 2.4231 0.4039  0.0639  0.3315  167 LYS E CB  
7343  C CG  . LYS E 167 ? 2.7951 2.5705 2.6180 0.4153  0.0612  0.3291  167 LYS E CG  
7344  C CD  . LYS E 167 ? 2.9258 2.7210 2.7502 0.4137  0.0652  0.3324  167 LYS E CD  
7345  C CE  . LYS E 167 ? 3.0482 2.8632 2.8612 0.4305  0.0627  0.3307  167 LYS E CE  
7346  N NZ  . LYS E 167 ? 3.1564 2.9855 2.9638 0.4401  0.0676  0.3404  167 LYS E NZ  
7347  N N   . LEU E 168 ? 2.5043 2.2373 2.3455 0.4058  0.0538  0.3279  168 LEU E N   
7348  C CA  . LEU E 168 ? 2.4797 2.2146 2.3310 0.4074  0.0448  0.3272  168 LEU E CA  
7349  C C   . LEU E 168 ? 2.5042 2.2355 2.3610 0.4129  0.0369  0.3381  168 LEU E C   
7350  O O   . LEU E 168 ? 2.4888 2.2241 2.3537 0.4158  0.0208  0.3410  168 LEU E O   
7351  C CB  . LEU E 168 ? 2.4755 2.2047 2.3304 0.4043  0.0511  0.3275  168 LEU E CB  
7352  C CG  . LEU E 168 ? 2.5186 2.2552 2.3865 0.4034  0.0427  0.3244  168 LEU E CG  
7353  C CD1 . LEU E 168 ? 2.5165 2.2523 2.3840 0.3958  0.0426  0.3111  168 LEU E CD1 
7354  C CD2 . LEU E 168 ? 2.5409 2.2739 2.4130 0.4085  0.0479  0.3335  168 LEU E CD2 
7355  N N   . ASN E 169 ? 2.4523 2.1745 2.3047 0.4136  0.0453  0.3456  169 ASN E N   
7356  C CA  . ASN E 169 ? 2.4431 2.1581 2.3010 0.4174  0.0400  0.3588  169 ASN E CA  
7357  C C   . ASN E 169 ? 2.4855 2.1893 2.3374 0.4206  0.0311  0.3584  169 ASN E C   
7358  O O   . ASN E 169 ? 2.4751 2.1681 2.3333 0.4241  0.0186  0.3705  169 ASN E O   
7359  C CB  . ASN E 169 ? 2.4388 2.1470 2.2919 0.4173  0.0526  0.3657  169 ASN E CB  
7360  C CG  . ASN E 169 ? 2.6397 2.3549 2.4962 0.4220  0.0573  0.3718  169 ASN E CG  
7361  O OD1 . ASN E 169 ? 2.5373 2.2611 2.4068 0.4275  0.0532  0.3870  169 ASN E OD1 
7362  N ND2 . ASN E 169 ? 2.5190 2.2299 2.3637 0.4214  0.0642  0.3628  169 ASN E ND2 
7363  N N   . ARG E 170 ? 2.4446 2.1503 2.2844 0.4210  0.0359  0.3474  170 ARG E N   
7364  C CA  . ARG E 170 ? 2.4508 2.1459 2.2801 0.4288  0.0284  0.3459  170 ARG E CA  
7365  C C   . ARG E 170 ? 2.5179 2.2120 2.3418 0.4397  0.0077  0.3432  170 ARG E C   
7366  O O   . ARG E 170 ? 2.5237 2.1971 2.3404 0.4496  -0.0096 0.3486  170 ARG E O   
7367  C CB  . ARG E 170 ? 2.4332 2.1377 2.2528 0.4277  0.0413  0.3391  170 ARG E CB  
7368  C CG  . ARG E 170 ? 2.4972 2.1931 2.3170 0.4195  0.0517  0.3421  170 ARG E CG  
7369  C CD  . ARG E 170 ? 2.5224 2.2318 2.3363 0.4178  0.0596  0.3390  170 ARG E CD  
7370  N NE  . ARG E 170 ? 2.5197 2.2451 2.3372 0.4075  0.0663  0.3397  170 ARG E NE  
7371  C CZ  . ARG E 170 ? 2.6145 2.3593 2.4332 0.4082  0.0675  0.3399  170 ARG E CZ  
7372  N NH1 . ARG E 170 ? 2.4498 2.2046 2.2645 0.4200  0.0641  0.3371  170 ARG E NH1 
7373  N NH2 . ARG E 170 ? 2.3760 2.1272 2.1979 0.3983  0.0695  0.3441  170 ARG E NH2 
7374  N N   . GLU E 171 ? 2.4770 2.1890 2.3025 0.4381  0.0065  0.3349  171 GLU E N   
7375  C CA  . GLU E 171 ? 2.4839 2.1975 2.3018 0.4472  -0.0155 0.3292  171 GLU E CA  
7376  C C   . GLU E 171 ? 2.5398 2.2432 2.3694 0.4471  -0.0406 0.3400  171 GLU E C   
7377  O O   . GLU E 171 ? 2.5516 2.2403 2.3694 0.4590  -0.0685 0.3419  171 GLU E O   
7378  C CB  . GLU E 171 ? 2.4915 2.2263 2.3102 0.4419  -0.0083 0.3170  171 GLU E CB  
7379  C CG  . GLU E 171 ? 2.6097 2.3573 2.4142 0.4479  0.0051  0.3112  171 GLU E CG  
7380  C CD  . GLU E 171 ? 2.6996 2.4655 2.5050 0.4427  0.0108  0.3024  171 GLU E CD  
7381  O OE1 . GLU E 171 ? 2.4425 2.2105 2.2430 0.4464  -0.0061 0.2935  171 GLU E OE1 
7382  O OE2 . GLU E 171 ? 2.5650 2.3419 2.3753 0.4349  0.0293  0.3056  171 GLU E OE2 
7383  N N   . GLU E 172 ? 2.4827 2.1941 2.3341 0.4359  -0.0335 0.3497  172 GLU E N   
7384  C CA  . GLU E 172 ? 2.4748 2.1856 2.3443 0.4346  -0.0561 0.3668  172 GLU E CA  
7385  C C   . GLU E 172 ? 2.5352 2.2216 2.4061 0.4401  -0.0701 0.3867  172 GLU E C   
7386  O O   . GLU E 172 ? 2.5276 2.2082 2.4103 0.4417  -0.0994 0.4047  172 GLU E O   
7387  C CB  . GLU E 172 ? 2.4745 2.2057 2.3653 0.4253  -0.0414 0.3735  172 GLU E CB  
7388  C CG  . GLU E 172 ? 2.5944 2.3437 2.4916 0.4196  -0.0459 0.3610  172 GLU E CG  
7389  C CD  . GLU E 172 ? 2.8034 2.5660 2.7216 0.4170  -0.0739 0.3740  172 GLU E CD  
7390  O OE1 . GLU E 172 ? 2.6874 2.4411 2.6027 0.4213  -0.1067 0.3796  172 GLU E OE1 
7391  O OE2 . GLU E 172 ? 2.7197 2.5011 2.6559 0.4118  -0.0658 0.3789  172 GLU E OE2 
7392  N N   . ILE E 173 ? 2.5009 2.1717 2.3610 0.4416  -0.0519 0.3850  173 ILE E N   
7393  C CA  . ILE E 173 ? 2.5067 2.1480 2.3665 0.4453  -0.0617 0.4015  173 ILE E CA  
7394  C C   . ILE E 173 ? 2.5759 2.1866 2.4106 0.4602  -0.0831 0.3957  173 ILE E C   
7395  O O   . ILE E 173 ? 2.5868 2.1673 2.4207 0.4670  -0.1128 0.4126  173 ILE E O   
7396  C CB  . ILE E 173 ? 2.5374 2.1774 2.4002 0.4374  -0.0318 0.4027  173 ILE E CB  
7397  C CG1 . ILE E 173 ? 2.5278 2.1786 2.4133 0.4315  -0.0279 0.4247  173 ILE E CG1 
7398  C CG2 . ILE E 173 ? 2.5595 2.1665 2.4084 0.4411  -0.0315 0.4021  173 ILE E CG2 
7399  C CD1 . ILE E 173 ? 2.5811 2.2656 2.4775 0.4283  -0.0155 0.4227  173 ILE E CD1 
7400  N N   . ASP E 174 ? 2.5306 2.1484 2.3441 0.4674  -0.0707 0.3749  174 ASP E N   
7401  C CA  . ASP E 174 ? 2.7602 2.3527 2.5441 0.4877  -0.0881 0.3686  174 ASP E CA  
7402  C C   . ASP E 174 ? 2.6731 2.2623 2.4429 0.5010  -0.1230 0.3659  174 ASP E C   
7403  O O   . ASP E 174 ? 1.9742 1.5936 1.7492 0.4954  -0.1199 0.3556  174 ASP E O   
7404  C CB  . ASP E 174 ? 2.7840 2.3929 2.5525 0.4926  -0.0608 0.3524  174 ASP E CB  
7405  C CG  . ASP E 174 ? 2.8647 2.4756 2.6439 0.4792  -0.0324 0.3536  174 ASP E CG  
7406  O OD1 . ASP E 174 ? 2.8660 2.4489 2.6518 0.4748  -0.0365 0.3647  174 ASP E OD1 
7407  O OD2 . ASP E 174 ? 2.9164 2.5556 2.6972 0.4728  -0.0088 0.3446  174 ASP E OD2 
7408  N N   . ASN F 11  ? 1.3700 1.8079 1.9992 0.1158  0.3525  0.1609  20  ASN F N   
7409  C CA  . ASN F 11  ? 1.3567 1.7580 2.0022 0.1117  0.3583  0.1584  20  ASN F CA  
7410  C C   . ASN F 11  ? 1.4159 1.7660 2.0597 0.1145  0.3594  0.1465  20  ASN F C   
7411  O O   . ASN F 11  ? 1.4056 1.7283 2.0552 0.1054  0.3589  0.1397  20  ASN F O   
7412  C CB  . ASN F 11  ? 1.3483 1.7727 2.0282 0.1253  0.3817  0.1804  20  ASN F CB  
7413  C CG  . ASN F 11  ? 1.6432 2.1137 2.3294 0.1196  0.3840  0.2001  20  ASN F CG  
7414  O OD1 . ASN F 11  ? 1.5518 2.0743 2.2417 0.1319  0.3893  0.2167  20  ASN F OD1 
7415  N ND2 . ASN F 11  ? 1.5677 2.0167 2.2555 0.1013  0.3802  0.1998  20  ASN F ND2 
7416  N N   . ASN F 12  ? 1.3889 1.7258 2.0241 0.1266  0.3608  0.1461  21  ASN F N   
7417  C CA  . ASN F 12  ? 1.3902 1.6746 2.0244 0.1320  0.3634  0.1411  21  ASN F CA  
7418  C C   . ASN F 12  ? 1.4373 1.6862 2.0606 0.1089  0.3551  0.1301  21  ASN F C   
7419  O O   . ASN F 12  ? 1.4260 1.6395 2.0582 0.1130  0.3591  0.1309  21  ASN F O   
7420  C CB  . ASN F 12  ? 1.4269 1.6987 2.0435 0.1411  0.3633  0.1436  21  ASN F CB  
7421  C CG  . ASN F 12  ? 1.8222 2.0304 2.4361 0.1457  0.3672  0.1439  21  ASN F CG  
7422  O OD1 . ASN F 12  ? 1.7773 1.9540 2.3684 0.1248  0.3634  0.1401  21  ASN F OD1 
7423  N ND2 . ASN F 12  ? 1.7252 1.9121 2.3658 0.1733  0.3795  0.1500  21  ASN F ND2 
7424  N N   . SER F 13  ? 1.3914 1.6546 2.0005 0.0876  0.3465  0.1211  22  SER F N   
7425  C CA  . SER F 13  ? 1.3803 1.6225 1.9844 0.0697  0.3452  0.1125  22  SER F CA  
7426  C C   . SER F 13  ? 1.3906 1.6191 2.0113 0.0718  0.3459  0.1141  22  SER F C   
7427  O O   . SER F 13  ? 1.3723 1.6145 2.0074 0.0785  0.3467  0.1161  22  SER F O   
7428  C CB  . SER F 13  ? 1.4242 1.6904 2.0203 0.0548  0.3411  0.1008  22  SER F CB  
7429  O OG  . SER F 13  ? 1.5110 1.7610 2.1057 0.0414  0.3489  0.0926  22  SER F OG  
7430  N N   . THR F 14  ? 1.3325 1.5375 1.9523 0.0638  0.3493  0.1150  23  THR F N   
7431  C CA  . THR F 14  ? 1.3154 1.5145 1.9483 0.0630  0.3490  0.1167  23  THR F CA  
7432  C C   . THR F 14  ? 1.3731 1.5869 2.0073 0.0534  0.3473  0.1103  23  THR F C   
7433  O O   . THR F 14  ? 1.3628 1.5826 2.0061 0.0533  0.3442  0.1089  23  THR F O   
7434  C CB  . THR F 14  ? 1.3644 1.5343 1.9998 0.0628  0.3551  0.1280  23  THR F CB  
7435  O OG1 . THR F 14  ? 1.3294 1.5062 1.9774 0.0603  0.3530  0.1291  23  THR F OG1 
7436  C CG2 . THR F 14  ? 1.3421 1.4979 1.9672 0.0496  0.3666  0.1351  23  THR F CG2 
7437  N N   . ASP F 15  ? 1.3423 1.5616 1.9697 0.0461  0.3530  0.1051  24  ASP F N   
7438  C CA  . ASP F 15  ? 1.3330 1.5637 1.9669 0.0432  0.3579  0.0977  24  ASP F CA  
7439  C C   . ASP F 15  ? 1.3542 1.5899 1.9945 0.0480  0.3476  0.0942  24  ASP F C   
7440  O O   . ASP F 15  ? 1.3584 1.5950 1.9968 0.0497  0.3396  0.0926  24  ASP F O   
7441  C CB  . ASP F 15  ? 1.3672 1.6073 1.9965 0.0385  0.3648  0.0850  24  ASP F CB  
7442  C CG  . ASP F 15  ? 1.5571 1.7925 2.1797 0.0275  0.3820  0.0850  24  ASP F CG  
7443  O OD1 . ASP F 15  ? 1.5680 1.7869 2.1933 0.0235  0.3947  0.0992  24  ASP F OD1 
7444  O OD2 . ASP F 15  ? 1.6485 1.8963 2.2636 0.0203  0.3854  0.0716  24  ASP F OD2 
7445  N N   . THR F 16  ? 1.2805 1.5208 1.9295 0.0492  0.3510  0.0961  25  THR F N   
7446  C CA  . THR F 16  ? 1.2669 1.5077 1.9194 0.0508  0.3432  0.0928  25  THR F CA  
7447  C C   . THR F 16  ? 1.2755 1.5168 1.9350 0.0588  0.3486  0.0862  25  THR F C   
7448  O O   . THR F 16  ? 1.2552 1.5088 1.9249 0.0645  0.3636  0.0876  25  THR F O   
7449  C CB  . THR F 16  ? 1.4043 1.6535 2.0603 0.0464  0.3406  0.0986  25  THR F CB  
7450  O OG1 . THR F 16  ? 1.4091 1.6583 2.0659 0.0430  0.3358  0.0929  25  THR F OG1 
7451  C CG2 . THR F 16  ? 1.3962 1.6621 2.0593 0.0472  0.3495  0.1094  25  THR F CG2 
7452  N N   . VAL F 17  ? 1.2194 1.4443 1.8775 0.0606  0.3413  0.0813  26  VAL F N   
7453  C CA  . VAL F 17  ? 1.2091 1.4214 1.8753 0.0726  0.3453  0.0747  26  VAL F CA  
7454  C C   . VAL F 17  ? 1.2579 1.4593 1.9223 0.0713  0.3399  0.0770  26  VAL F C   
7455  O O   . VAL F 17  ? 1.2618 1.4619 1.9189 0.0570  0.3343  0.0808  26  VAL F O   
7456  C CB  . VAL F 17  ? 1.2633 1.4552 1.9300 0.0765  0.3434  0.0681  26  VAL F CB  
7457  C CG1 . VAL F 17  ? 1.2624 1.4722 1.9293 0.0742  0.3503  0.0615  26  VAL F CG1 
7458  C CG2 . VAL F 17  ? 1.2715 1.4442 1.9302 0.0663  0.3333  0.0770  26  VAL F CG2 
7459  N N   . ASP F 18  ? 1.2032 1.3974 1.8764 0.0866  0.3455  0.0734  27  ASP F N   
7460  C CA  . ASP F 18  ? 1.2083 1.3904 1.8768 0.0847  0.3410  0.0747  27  ASP F CA  
7461  C C   . ASP F 18  ? 1.2513 1.3839 1.9222 0.0963  0.3415  0.0716  27  ASP F C   
7462  O O   . ASP F 18  ? 1.2438 1.3664 1.9291 0.1179  0.3498  0.0655  27  ASP F O   
7463  C CB  . ASP F 18  ? 1.2299 1.4513 1.9069 0.0954  0.3479  0.0777  27  ASP F CB  
7464  C CG  . ASP F 18  ? 1.4312 1.6944 2.1037 0.0792  0.3444  0.0848  27  ASP F CG  
7465  O OD1 . ASP F 18  ? 1.4550 1.7388 2.1342 0.0798  0.3514  0.0911  27  ASP F OD1 
7466  O OD2 . ASP F 18  ? 1.5117 1.7860 2.1754 0.0658  0.3370  0.0839  27  ASP F OD2 
7467  N N   . THR F 19  ? 1.2034 1.3015 1.8632 0.0815  0.3369  0.0760  28  THR F N   
7468  C CA  . THR F 19  ? 1.1935 1.2303 1.8546 0.0900  0.3385  0.0786  28  THR F CA  
7469  C C   . THR F 19  ? 1.2294 1.2499 1.8851 0.0935  0.3401  0.0775  28  THR F C   
7470  O O   . THR F 19  ? 1.2187 1.2880 1.8726 0.0928  0.3394  0.0739  28  THR F O   
7471  C CB  . THR F 19  ? 1.2783 1.2788 1.9341 0.0695  0.3390  0.0910  28  THR F CB  
7472  O OG1 . THR F 19  ? 1.2705 1.2743 1.9171 0.0417  0.3447  0.0970  28  THR F OG1 
7473  C CG2 . THR F 19  ? 1.2465 1.2724 1.9067 0.0685  0.3364  0.0927  28  THR F CG2 
7474  N N   . VAL F 20  ? 1.1855 1.1379 1.8388 0.0972  0.3428  0.0826  29  VAL F N   
7475  C CA  . VAL F 20  ? 1.1887 1.1163 1.8337 0.1000  0.3451  0.0819  29  VAL F CA  
7476  C C   . VAL F 20  ? 1.2618 1.1940 1.8880 0.0582  0.3478  0.0849  29  VAL F C   
7477  O O   . VAL F 20  ? 1.2637 1.2212 1.8797 0.0505  0.3473  0.0784  29  VAL F O   
7478  C CB  . VAL F 20  ? 1.2319 1.0720 1.8823 0.1217  0.3498  0.0871  29  VAL F CB  
7479  C CG1 . VAL F 20  ? 1.2304 1.0574 1.8770 0.1399  0.3526  0.0831  29  VAL F CG1 
7480  C CG2 . VAL F 20  ? 1.2073 1.0358 1.8813 0.1556  0.3517  0.0821  29  VAL F CG2 
7481  N N   . LEU F 21  ? 1.7015 0.8620 2.1016 -0.1115 0.1824  -0.0905 30  LEU F N   
7482  C CA  . LEU F 21  ? 1.7226 0.8712 2.1204 -0.1419 0.2276  -0.0864 30  LEU F CA  
7483  C C   . LEU F 21  ? 1.7772 0.9819 2.1519 -0.1437 0.2250  -0.0935 30  LEU F C   
7484  O O   . LEU F 21  ? 1.7714 1.0156 2.1253 -0.1677 0.2218  -0.1133 30  LEU F O   
7485  C CB  . LEU F 21  ? 1.7399 0.8494 2.1649 -0.1268 0.2579  -0.0619 30  LEU F CB  
7486  C CG  . LEU F 21  ? 1.7981 0.8625 2.2597 -0.1204 0.2648  -0.0536 30  LEU F CG  
7487  C CD1 . LEU F 21  ? 1.8057 0.8700 2.2955 -0.0815 0.2729  -0.0254 30  LEU F CD1 
7488  C CD2 . LEU F 21  ? 1.8666 0.8694 2.3273 -0.1667 0.3135  -0.0591 30  LEU F CD2 
7489  N N   . GLU F 22  ? 1.7417 0.9521 2.1195 -0.1171 0.2261  -0.0788 31  GLU F N   
7490  C CA  . GLU F 22  ? 1.7474 0.9940 2.1049 -0.1158 0.2299  -0.0857 31  GLU F CA  
7491  C C   . GLU F 22  ? 1.7780 1.0802 2.1307 -0.0925 0.1791  -0.0929 31  GLU F C   
7492  O O   . GLU F 22  ? 1.7593 1.0584 2.1201 -0.0598 0.1470  -0.0800 31  GLU F O   
7493  C CB  . GLU F 22  ? 1.7885 1.0005 2.1436 -0.0891 0.2492  -0.0632 31  GLU F CB  
7494  C CG  . GLU F 22  ? 1.9539 1.1628 2.2770 -0.1026 0.2870  -0.0739 31  GLU F CG  
7495  C CD  . GLU F 22  ? 2.2764 1.4423 2.5826 -0.0672 0.3030  -0.0497 31  GLU F CD  
7496  O OE1 . GLU F 22  ? 2.2066 1.3247 2.5187 -0.0488 0.3275  -0.0237 31  GLU F OE1 
7497  O OE2 . GLU F 22  ? 2.2293 1.4071 2.5132 -0.0566 0.2945  -0.0564 31  GLU F OE2 
7498  N N   . LYS F 23  ? 1.7381 1.0949 2.0769 -0.1104 0.1759  -0.1144 32  LYS F N   
7499  C CA  . LYS F 23  ? 1.7185 1.1288 2.0513 -0.0847 0.1353  -0.1183 32  LYS F CA  
7500  C C   . LYS F 23  ? 1.7882 1.2236 2.1159 -0.0770 0.1381  -0.1223 32  LYS F C   
7501  O O   . LYS F 23  ? 1.8092 1.2455 2.1303 -0.1043 0.1748  -0.1372 32  LYS F O   
7502  C CB  . LYS F 23  ? 1.7456 1.2108 2.0681 -0.0979 0.1233  -0.1362 32  LYS F CB  
7503  C CG  . LYS F 23  ? 1.8844 1.3118 2.2001 -0.0997 0.1162  -0.1328 32  LYS F CG  
7504  C CD  . LYS F 23  ? 1.9403 1.3487 2.2431 -0.0574 0.0839  -0.1214 32  LYS F CD  
7505  C CE  . LYS F 23  ? 2.0148 1.3910 2.2946 -0.0590 0.0798  -0.1268 32  LYS F CE  
7506  N NZ  . LYS F 23  ? 2.0721 1.3740 2.3667 -0.0826 0.1016  -0.1265 32  LYS F NZ  
7507  N N   . ASN F 24  ? 1.7374 1.1829 2.0626 -0.0436 0.1066  -0.1113 33  ASN F N   
7508  C CA  . ASN F 24  ? 1.7439 1.2008 2.0621 -0.0329 0.1046  -0.1124 33  ASN F CA  
7509  C C   . ASN F 24  ? 1.8209 1.2226 2.1301 -0.0373 0.1329  -0.1050 33  ASN F C   
7510  O O   . ASN F 24  ? 1.8455 1.2446 2.1425 -0.0589 0.1669  -0.1229 33  ASN F O   
7511  C CB  . ASN F 24  ? 1.7809 1.3110 2.1006 -0.0450 0.1066  -0.1377 33  ASN F CB  
7512  C CG  . ASN F 24  ? 2.2132 1.7739 2.5310 -0.0132 0.0775  -0.1298 33  ASN F CG  
7513  O OD1 . ASN F 24  ? 2.1631 1.6916 2.4722 0.0131  0.0579  -0.1083 33  ASN F OD1 
7514  N ND2 . ASN F 24  ? 2.1724 1.7941 2.4970 -0.0145 0.0783  -0.1475 33  ASN F ND2 
7515  N N   . VAL F 25  ? 1.7778 1.1366 2.0886 -0.0151 0.1214  -0.0801 34  VAL F N   
7516  C CA  . VAL F 25  ? 1.8109 1.1182 2.1090 -0.0035 0.1408  -0.0630 34  VAL F CA  
7517  C C   . VAL F 25  ? 1.8706 1.1718 2.1516 0.0188  0.1177  -0.0521 34  VAL F C   
7518  O O   . VAL F 25  ? 1.8437 1.1663 2.1315 0.0311  0.0839  -0.0459 34  VAL F O   
7519  C CB  . VAL F 25  ? 1.8607 1.1420 2.1772 0.0093  0.1403  -0.0421 34  VAL F CB  
7520  C CG1 . VAL F 25  ? 1.9053 1.1374 2.2051 0.0263  0.1702  -0.0217 34  VAL F CG1 
7521  C CG2 . VAL F 25  ? 1.8465 1.1305 2.1812 -0.0158 0.1557  -0.0531 34  VAL F CG2 
7522  N N   . THR F 26  ? 1.8618 1.1239 2.1128 0.0211  0.1424  -0.0512 35  THR F N   
7523  C CA  . THR F 26  ? 1.8691 1.1116 2.0946 0.0376  0.1263  -0.0413 35  THR F CA  
7524  C C   . THR F 26  ? 1.8852 1.1227 2.1125 0.0653  0.0987  -0.0122 35  THR F C   
7525  O O   . THR F 26  ? 1.8970 1.1207 2.1318 0.0791  0.1097  0.0032  35  THR F O   
7526  C CB  . THR F 26  ? 2.0611 1.2483 2.2444 0.0315  0.1679  -0.0517 35  THR F CB  
7527  O OG1 . THR F 26  ? 2.0841 1.2882 2.2719 -0.0013 0.2023  -0.0856 35  THR F OG1 
7528  C CG2 . THR F 26  ? 2.0505 1.2142 2.2044 0.0380  0.1545  -0.0506 35  THR F CG2 
7529  N N   . VAL F 27  ? 1.7990 1.0535 2.0209 0.0711  0.0661  -0.0064 36  VAL F N   
7530  C CA  . VAL F 27  ? 1.7878 1.0573 2.0113 0.0893  0.0378  0.0134  36  VAL F CA  
7531  C C   . VAL F 27  ? 1.8570 1.1122 2.0432 0.0901  0.0234  0.0197  36  VAL F C   
7532  O O   . VAL F 27  ? 1.8417 1.0904 2.0170 0.0732  0.0255  0.0071  36  VAL F O   
7533  C CB  . VAL F 27  ? 1.7845 1.0976 2.0439 0.0837  0.0183  0.0070  36  VAL F CB  
7534  C CG1 . VAL F 27  ? 1.7767 1.1168 2.0293 0.0836  -0.0082 0.0098  36  VAL F CG1 
7535  C CG2 . VAL F 27  ? 1.7786 1.0964 2.0692 0.0926  0.0270  0.0132  36  VAL F CG2 
7536  N N   . THR F 28  ? 1.8482 1.0974 2.0125 0.1110  0.0114  0.0405  37  THR F N   
7537  C CA  . THR F 28  ? 1.8752 1.1053 1.9949 0.1107  -0.0016 0.0490  37  THR F CA  
7538  C C   . THR F 28  ? 1.8724 1.1410 1.9960 0.0876  -0.0248 0.0416  37  THR F C   
7539  O O   . THR F 28  ? 1.8726 1.1128 1.9702 0.0673  -0.0184 0.0345  37  THR F O   
7540  C CB  . THR F 28  ? 2.0268 1.2486 2.1175 0.1451  -0.0092 0.0757  37  THR F CB  
7541  O OG1 . THR F 28  ? 1.9839 1.2776 2.1130 0.1604  -0.0351 0.0856  37  THR F OG1 
7542  C CG2 . THR F 28  ? 2.0522 1.2098 2.1175 0.1681  0.0295  0.0837  37  THR F CG2 
7543  N N   . HIS F 29  ? 1.7897 1.1173 1.9424 0.0883  -0.0444 0.0409  38  HIS F N   
7544  C CA  . HIS F 29  ? 1.7665 1.1253 1.9152 0.0617  -0.0539 0.0281  38  HIS F CA  
7545  C C   . HIS F 29  ? 1.7378 1.1129 1.9220 0.0541  -0.0442 0.0104  38  HIS F C   
7546  O O   . HIS F 29  ? 1.7108 1.1073 1.9311 0.0681  -0.0469 0.0099  38  HIS F O   
7547  C CB  . HIS F 29  ? 1.8045 1.2228 1.9502 0.0632  -0.0797 0.0334  38  HIS F CB  
7548  C CG  . HIS F 29  ? 1.9087 1.3162 2.0156 0.0815  -0.0936 0.0558  38  HIS F CG  
7549  N ND1 . HIS F 29  ? 1.9639 1.3438 2.0673 0.1210  -0.0895 0.0768  38  HIS F ND1 
7550  C CD2 . HIS F 29  ? 1.9738 1.3908 2.0371 0.0657  -0.1074 0.0601  38  HIS F CD2 
7551  C CE1 . HIS F 29  ? 2.0163 1.3842 2.0704 0.1338  -0.1019 0.0946  38  HIS F CE1 
7552  N NE2 . HIS F 29  ? 2.0260 1.4204 2.0567 0.1000  -0.1167 0.0853  38  HIS F NE2 
7553  N N   . SER F 30  ? 1.6602 1.0168 1.8293 0.0349  -0.0287 -0.0019 39  SER F N   
7554  C CA  . SER F 30  ? 1.6172 0.9768 1.8029 0.0320  -0.0155 -0.0174 39  SER F CA  
7555  C C   . SER F 30  ? 1.6544 0.9915 1.8048 0.0153  0.0058  -0.0254 39  SER F C   
7556  O O   . SER F 30  ? 1.6668 0.9762 1.7907 0.0086  0.0147  -0.0173 39  SER F O   
7557  C CB  . SER F 30  ? 1.6322 0.9787 1.8406 0.0462  -0.0082 -0.0170 39  SER F CB  
7558  O OG  . SER F 30  ? 1.7404 1.0621 1.9325 0.0460  0.0004  -0.0122 39  SER F OG  
7559  N N   . VAL F 31  ? 1.5858 0.9245 1.7313 0.0093  0.0209  -0.0416 40  VAL F N   
7560  C CA  . VAL F 31  ? 1.5968 0.9020 1.6974 -0.0027 0.0539  -0.0485 40  VAL F CA  
7561  C C   . VAL F 31  ? 1.6039 0.8855 1.6998 0.0190  0.0727  -0.0513 40  VAL F C   
7562  O O   . VAL F 31  ? 1.5703 0.8622 1.6909 0.0295  0.0647  -0.0603 40  VAL F O   
7563  C CB  . VAL F 31  ? 1.6768 0.9924 1.7505 -0.0336 0.0693  -0.0686 40  VAL F CB  
7564  C CG1 . VAL F 31  ? 1.6685 0.9934 1.7554 -0.0337 0.0776  -0.0936 40  VAL F CG1 
7565  C CG2 . VAL F 31  ? 1.7197 0.9899 1.7326 -0.0553 0.1117  -0.0700 40  VAL F CG2 
7566  N N   . ASN F 32  ? 1.5660 0.8157 1.6282 0.0275  0.0987  -0.0417 41  ASN F N   
7567  C CA  . ASN F 32  ? 1.5662 0.7984 1.6135 0.0567  0.1177  -0.0388 41  ASN F CA  
7568  C C   . ASN F 32  ? 1.6482 0.8374 1.6452 0.0534  0.1562  -0.0543 41  ASN F C   
7569  O O   . ASN F 32  ? 1.6741 0.8520 1.6486 0.0217  0.1725  -0.0695 41  ASN F O   
7570  C CB  . ASN F 32  ? 1.5712 0.7922 1.6038 0.0722  0.1332  -0.0202 41  ASN F CB  
7571  C CG  . ASN F 32  ? 1.8477 1.0794 1.8786 0.1126  0.1405  -0.0119 41  ASN F CG  
7572  O OD1 . ASN F 32  ? 1.7685 1.0225 1.8159 0.1287  0.1252  -0.0188 41  ASN F OD1 
7573  N ND2 . ASN F 32  ? 1.7593 0.9794 1.7702 0.1306  0.1641  0.0043  41  ASN F ND2 
7574  N N   . LEU F 33  ? 1.6008 0.7671 1.5753 0.0848  0.1733  -0.0535 42  LEU F N   
7575  C CA  . LEU F 33  ? 1.6389 0.7439 1.5501 0.0883  0.2204  -0.0694 42  LEU F CA  
7576  C C   . LEU F 33  ? 1.7328 0.7979 1.5908 0.1328  0.2557  -0.0494 42  LEU F C   
7577  O O   . LEU F 33  ? 1.7837 0.7778 1.5669 0.1392  0.3130  -0.0548 42  LEU F O   
7578  C CB  . LEU F 33  ? 1.6193 0.7235 1.5477 0.0874  0.2072  -0.0919 42  LEU F CB  
7579  C CG  . LEU F 33  ? 1.6295 0.7755 1.6128 0.0528  0.1761  -0.1109 42  LEU F CG  
7580  C CD1 . LEU F 33  ? 1.6121 0.7599 1.6259 0.0594  0.1587  -0.1236 42  LEU F CD1 
7581  C CD2 . LEU F 33  ? 1.6848 0.8145 1.6369 0.0151  0.2074  -0.1382 42  LEU F CD2 
7582  N N   . LEU F 34  ? 1.6713 0.7852 1.5660 0.1647  0.2250  -0.0278 43  LEU F N   
7583  C CA  . LEU F 34  ? 1.7134 0.8206 1.5743 0.2170  0.2449  -0.0053 43  LEU F CA  
7584  C C   . LEU F 34  ? 1.7620 0.8713 1.6165 0.2274  0.2649  0.0189  43  LEU F C   
7585  O O   . LEU F 34  ? 1.7142 0.8647 1.6201 0.2023  0.2370  0.0205  43  LEU F O   
7586  C CB  . LEU F 34  ? 1.6792 0.8589 1.5911 0.2402  0.1968  -0.0030 43  LEU F CB  
7587  C CG  . LEU F 34  ? 1.7949 0.9870 1.6731 0.2996  0.2060  0.0151  43  LEU F CG  
7588  C CD1 . LEU F 34  ? 1.7914 0.9959 1.6726 0.3068  0.1823  0.0017  43  LEU F CD1 
7589  C CD2 . LEU F 34  ? 1.8259 1.1048 1.7517 0.3211  0.1819  0.0324  43  LEU F CD2 
7590  N N   . GLU F 35  ? 1.7701 0.8266 1.5563 0.2679  0.3184  0.0385  44  GLU F N   
7591  C CA  . GLU F 35  ? 1.7831 0.8337 1.5580 0.2880  0.3477  0.0661  44  GLU F CA  
7592  C C   . GLU F 35  ? 1.8368 0.9353 1.6134 0.3592  0.3417  0.0911  44  GLU F C   
7593  O O   . GLU F 35  ? 1.8912 0.9502 1.6045 0.4058  0.3717  0.1005  44  GLU F O   
7594  C CB  . GLU F 35  ? 1.8773 0.8230 1.5670 0.2730  0.4270  0.0714  44  GLU F CB  
7595  C CG  . GLU F 35  ? 2.0453 0.9763 1.7280 0.2845  0.4614  0.1007  44  GLU F CG  
7596  C CD  . GLU F 35  ? 2.2974 1.2546 2.0348 0.2307  0.4350  0.0957  44  GLU F CD  
7597  O OE1 . GLU F 35  ? 2.3536 1.2461 2.0499 0.2054  0.4880  0.1061  44  GLU F OE1 
7598  O OE2 . GLU F 35  ? 2.0998 1.1336 1.9136 0.2149  0.3678  0.0825  44  GLU F OE2 
7599  N N   . ASP F 36  ? 0.9587 1.2782 1.4131 0.0031  0.2364  -0.0120 45  ASP F N   
7600  C CA  . ASP F 36  ? 0.9980 1.2513 1.3869 -0.0074 0.2128  -0.0336 45  ASP F CA  
7601  C C   . ASP F 36  ? 1.0017 1.2915 1.4168 -0.0232 0.1708  -0.0450 45  ASP F C   
7602  O O   . ASP F 36  ? 1.0231 1.2710 1.4020 -0.0356 0.1457  -0.0564 45  ASP F O   
7603  C CB  . ASP F 36  ? 1.0711 1.2725 1.4225 -0.0009 0.2205  -0.0355 45  ASP F CB  
7604  C CG  . ASP F 36  ? 1.2251 1.4860 1.6373 0.0101  0.2311  -0.0238 45  ASP F CG  
7605  O OD1 . ASP F 36  ? 1.2518 1.5250 1.6840 0.0262  0.2700  -0.0051 45  ASP F OD1 
7606  O OD2 . ASP F 36  ? 1.2696 1.5657 1.7144 0.0041  0.2028  -0.0296 45  ASP F OD2 
7607  N N   . LYS F 37  ? 0.9022 1.2637 1.3773 -0.0228 0.1646  -0.0383 46  LYS F N   
7608  C CA  . LYS F 37  ? 0.8654 1.2561 1.3637 -0.0319 0.1365  -0.0444 46  LYS F CA  
7609  C C   . LYS F 37  ? 0.9037 1.3095 1.4029 -0.0430 0.1256  -0.0480 46  LYS F C   
7610  O O   . LYS F 37  ? 0.8899 1.3227 1.4052 -0.0439 0.1343  -0.0399 46  LYS F O   
7611  C CB  . LYS F 37  ? 0.8640 1.3025 1.4060 -0.0239 0.1378  -0.0358 46  LYS F CB  
7612  C CG  . LYS F 37  ? 1.1079 1.5326 1.6521 -0.0131 0.1468  -0.0334 46  LYS F CG  
7613  C CD  . LYS F 37  ? 1.2626 1.7356 1.8494 -0.0030 0.1543  -0.0225 46  LYS F CD  
7614  C CE  . LYS F 37  ? 1.4689 1.9279 2.0596 0.0077  0.1621  -0.0214 46  LYS F CE  
7615  N NZ  . LYS F 37  ? 1.5487 2.0542 2.1811 0.0184  0.1678  -0.0115 46  LYS F NZ  
7616  N N   . HIS F 38  ? 0.8611 1.2494 1.3488 -0.0520 0.1055  -0.0561 47  HIS F N   
7617  C CA  . HIS F 38  ? 0.8510 1.2453 1.3348 -0.0623 0.0960  -0.0603 47  HIS F CA  
7618  C C   . HIS F 38  ? 0.8899 1.2763 1.3832 -0.0662 0.0800  -0.0596 47  HIS F C   
7619  O O   . HIS F 38  ? 0.8843 1.2549 1.3875 -0.0640 0.0713  -0.0548 47  HIS F O   
7620  C CB  . HIS F 38  ? 0.8916 1.2527 1.3407 -0.0682 0.0995  -0.0661 47  HIS F CB  
7621  C CG  . HIS F 38  ? 0.9681 1.2808 1.3872 -0.0761 0.0824  -0.0713 47  HIS F CG  
7622  N ND1 . HIS F 38  ? 1.0274 1.3002 1.4254 -0.0749 0.0763  -0.0703 47  HIS F ND1 
7623  C CD2 . HIS F 38  ? 0.9963 1.2944 1.4066 -0.0875 0.0664  -0.0740 47  HIS F CD2 
7624  C CE1 . HIS F 38  ? 1.0480 1.2813 1.4245 -0.0884 0.0514  -0.0708 47  HIS F CE1 
7625  N NE2 . HIS F 38  ? 1.0318 1.2823 1.4191 -0.0954 0.0460  -0.0719 47  HIS F NE2 
7626  N N   . ASN F 39  ? 0.8400 1.2341 1.3328 -0.0719 0.0777  -0.0604 48  ASN F N   
7627  C CA  . ASN F 39  ? 0.8302 1.2139 1.3354 -0.0731 0.0720  -0.0536 48  ASN F CA  
7628  C C   . ASN F 39  ? 0.9162 1.2760 1.4082 -0.0850 0.0605  -0.0557 48  ASN F C   
7629  O O   . ASN F 39  ? 0.9365 1.2901 1.4016 -0.0912 0.0619  -0.0658 48  ASN F O   
7630  C CB  . ASN F 39  ? 0.7774 1.1683 1.2746 -0.0716 0.0817  -0.0524 48  ASN F CB  
7631  C CG  . ASN F 39  ? 0.8665 1.2607 1.3367 -0.0828 0.0811  -0.0616 48  ASN F CG  
7632  O OD1 . ASN F 39  ? 0.6150 1.0180 1.0809 -0.0879 0.0789  -0.0671 48  ASN F OD1 
7633  N ND2 . ASN F 39  ? 0.8227 1.2043 1.2723 -0.0858 0.0858  -0.0609 48  ASN F ND2 
7634  N N   . GLY F 40  ? 0.8704 1.2168 1.3858 -0.0878 0.0498  -0.0421 49  GLY F N   
7635  C CA  . GLY F 40  ? 0.8856 1.2086 1.3925 -0.1015 0.0338  -0.0393 49  GLY F CA  
7636  C C   . GLY F 40  ? 0.9257 1.2551 1.4234 -0.1052 0.0446  -0.0429 49  GLY F C   
7637  O O   . GLY F 40  ? 0.9533 1.2665 1.4436 -0.1162 0.0335  -0.0411 49  GLY F O   
7638  N N   . LYS F 41  ? 0.8405 1.1872 1.3322 -0.0976 0.0641  -0.0476 50  LYS F N   
7639  C CA  . LYS F 41  ? 0.8333 1.1778 1.3074 -0.1013 0.0757  -0.0511 50  LYS F CA  
7640  C C   . LYS F 41  ? 0.8775 1.2273 1.3215 -0.1104 0.0733  -0.0682 50  LYS F C   
7641  O O   . LYS F 41  ? 0.8672 1.2279 1.3045 -0.1091 0.0718  -0.0753 50  LYS F O   
7642  C CB  . LYS F 41  ? 0.8735 1.2149 1.3365 -0.0918 0.0937  -0.0477 50  LYS F CB  
7643  C CG  . LYS F 41  ? 1.0265 1.3569 1.5204 -0.0769 0.1069  -0.0261 50  LYS F CG  
7644  C CD  . LYS F 41  ? 1.1087 1.4202 1.5714 -0.0653 0.1269  -0.0249 50  LYS F CD  
7645  C CE  . LYS F 41  ? 1.1989 1.5256 1.6730 -0.0564 0.1226  -0.0256 50  LYS F CE  
7646  N NZ  . LYS F 41  ? 1.3492 1.6545 1.7746 -0.0521 0.1321  -0.0301 50  LYS F NZ  
7647  N N   . LEU F 42  ? 0.8432 1.1855 1.2749 -0.1180 0.0764  -0.0708 51  LEU F N   
7648  C CA  . LEU F 42  ? 0.8484 1.1958 1.2579 -0.1259 0.0769  -0.0833 51  LEU F CA  
7649  C C   . LEU F 42  ? 0.9546 1.3023 1.3454 -0.1295 0.0846  -0.0851 51  LEU F C   
7650  O O   . LEU F 42  ? 0.9641 1.2963 1.3407 -0.1338 0.0923  -0.0846 51  LEU F O   
7651  C CB  . LEU F 42  ? 0.8448 1.1785 1.2484 -0.1331 0.0731  -0.0852 51  LEU F CB  
7652  C CG  . LEU F 42  ? 0.9005 1.2135 1.2994 -0.1351 0.0591  -0.0843 51  LEU F CG  
7653  C CD1 . LEU F 42  ? 0.9076 1.2028 1.2991 -0.1442 0.0521  -0.0821 51  LEU F CD1 
7654  C CD2 . LEU F 42  ? 0.9336 1.2402 1.3093 -0.1312 0.0633  -0.0940 51  LEU F CD2 
7655  N N   . CYS F 43  ? 0.9359 1.2941 1.3222 -0.1288 0.0812  -0.0851 52  CYS F N   
7656  C CA  . CYS F 43  ? 0.9658 1.3107 1.3211 -0.1364 0.0795  -0.0849 52  CYS F CA  
7657  C C   . CYS F 43  ? 0.9687 1.3166 1.3113 -0.1515 0.0717  -0.0895 52  CYS F C   
7658  O O   . CYS F 43  ? 0.9243 1.2943 1.2907 -0.1526 0.0703  -0.0912 52  CYS F O   
7659  C CB  . CYS F 43  ? 0.9908 1.3461 1.3487 -0.1342 0.0711  -0.0797 52  CYS F CB  
7660  S SG  . CYS F 43  ? 1.0382 1.3921 1.4160 -0.1151 0.0813  -0.0733 52  CYS F SG  
7661  N N   . LYS F 44  ? 0.9463 1.2633 1.2457 -0.1627 0.0681  -0.0899 53  LYS F N   
7662  C CA  . LYS F 44  ? 0.9482 1.2644 1.2354 -0.1803 0.0559  -0.0916 53  LYS F CA  
7663  C C   . LYS F 44  ? 0.9712 1.3174 1.2852 -0.1913 0.0325  -0.0808 53  LYS F C   
7664  O O   . LYS F 44  ? 0.9877 1.3224 1.2840 -0.1981 0.0165  -0.0732 53  LYS F O   
7665  C CB  . LYS F 44  ? 1.0383 1.2978 1.2596 -0.1909 0.0592  -0.0950 53  LYS F CB  
7666  C CG  . LYS F 44  ? 1.2657 1.4696 1.4239 -0.1927 0.0575  -0.0916 53  LYS F CG  
7667  C CD  . LYS F 44  ? 1.4373 1.5695 1.5238 -0.1930 0.0798  -0.0948 53  LYS F CD  
7668  C CE  . LYS F 44  ? 1.6065 1.6571 1.6003 -0.1995 0.0765  -0.0921 53  LYS F CE  
7669  N NZ  . LYS F 44  ? 1.7212 1.6901 1.6424 -0.1898 0.1144  -0.0915 53  LYS F NZ  
7670  N N   . LEU F 45  ? 0.8939 1.2766 1.2542 -0.1913 0.0329  -0.0761 54  LEU F N   
7671  C CA  . LEU F 45  ? 0.8825 1.3010 1.2904 -0.1979 0.0181  -0.0565 54  LEU F CA  
7672  C C   . LEU F 45  ? 0.9815 1.3884 1.3753 -0.2245 -0.0151 -0.0427 54  LEU F C   
7673  O O   . LEU F 45  ? 0.9936 1.3851 1.3709 -0.2390 -0.0236 -0.0445 54  LEU F O   
7674  C CB  . LEU F 45  ? 0.8505 1.2966 1.3046 -0.1880 0.0352  -0.0511 54  LEU F CB  
7675  C CG  . LEU F 45  ? 0.8978 1.3817 1.4159 -0.1895 0.0304  -0.0221 54  LEU F CG  
7676  C CD1 . LEU F 45  ? 0.8814 1.3806 1.4281 -0.1680 0.0522  -0.0147 54  LEU F CD1 
7677  C CD2 . LEU F 45  ? 0.9306 1.4263 1.4807 -0.1914 0.0379  -0.0118 54  LEU F CD2 
7678  N N   . ARG F 46  ? 0.9607 1.3727 1.3608 -0.2326 -0.0370 -0.0270 55  ARG F N   
7679  C CA  . ARG F 46  ? 1.0150 1.4091 1.3979 -0.2623 -0.0796 -0.0081 55  ARG F CA  
7680  C C   . ARG F 46  ? 1.1294 1.4555 1.4250 -0.2818 -0.0931 -0.0227 55  ARG F C   
7681  O O   . ARG F 46  ? 1.1657 1.4811 1.4588 -0.3076 -0.1227 -0.0102 55  ARG F O   
7682  C CB  . ARG F 46  ? 1.0384 1.4867 1.5111 -0.2745 -0.1000 0.0280  55  ARG F CB  
7683  C CG  . ARG F 46  ? 1.2782 1.7540 1.8004 -0.2699 -0.0832 0.0328  55  ARG F CG  
7684  C CD  . ARG F 46  ? 1.4728 2.0094 2.0996 -0.2566 -0.0683 0.0668  55  ARG F CD  
7685  N NE  . ARG F 46  ? 1.6071 2.1586 2.2702 -0.2451 -0.0420 0.0690  55  ARG F NE  
7686  C CZ  . ARG F 46  ? 1.7416 2.3271 2.4764 -0.2224 -0.0085 0.0915  55  ARG F CZ  
7687  N NH1 . ARG F 46  ? 1.5219 2.1334 2.3043 -0.2087 0.0045  0.1147  55  ARG F NH1 
7688  N NH2 . ARG F 46  ? 1.5650 2.1517 2.3189 -0.2112 0.0169  0.0919  55  ARG F NH2 
7689  N N   . GLY F 47  A 1.1033 1.3806 1.3301 -0.2680 -0.0681 -0.0460 55  GLY F N   
7690  C CA  . GLY F 47  A 1.1701 1.3689 1.3022 -0.2792 -0.0668 -0.0596 55  GLY F CA  
7691  C C   . GLY F 47  A 1.1861 1.3854 1.3200 -0.2688 -0.0361 -0.0748 55  GLY F C   
7692  O O   . GLY F 47  A 1.2079 1.3634 1.2923 -0.2544 -0.0053 -0.0877 55  GLY F O   
7693  N N   . VAL F 48  ? 1.0834 1.3300 1.2770 -0.2752 -0.0423 -0.0693 56  VAL F N   
7694  C CA  . VAL F 48  ? 1.0487 1.2994 1.2479 -0.2669 -0.0162 -0.0822 56  VAL F CA  
7695  C C   . VAL F 48  ? 1.0442 1.3226 1.2757 -0.2378 0.0195  -0.0925 56  VAL F C   
7696  O O   . VAL F 48  ? 0.9925 1.3155 1.2781 -0.2250 0.0224  -0.0871 56  VAL F O   
7697  C CB  . VAL F 48  ? 1.0709 1.3582 1.3219 -0.2799 -0.0303 -0.0720 56  VAL F CB  
7698  C CG1 . VAL F 48  ? 1.1394 1.3746 1.3333 -0.3107 -0.0597 -0.0684 56  VAL F CG1 
7699  C CG2 . VAL F 48  ? 1.0280 1.3777 1.3650 -0.2785 -0.0446 -0.0485 56  VAL F CG2 
7700  N N   . ALA F 49  ? 1.0170 1.2614 1.2117 -0.2289 0.0456  -0.1037 57  ALA F N   
7701  C CA  . ALA F 49  ? 0.9737 1.2338 1.1953 -0.2066 0.0728  -0.1079 57  ALA F CA  
7702  C C   . ALA F 49  ? 0.9654 1.2649 1.2348 -0.2007 0.0800  -0.1113 57  ALA F C   
7703  O O   . ALA F 49  ? 0.9623 1.2663 1.2334 -0.2109 0.0761  -0.1131 57  ALA F O   
7704  C CB  . ALA F 49  ? 1.0204 1.2275 1.1938 -0.1996 0.0989  -0.1088 57  ALA F CB  
7705  N N   . PRO F 50  ? 0.8762 1.1956 1.1776 -0.1852 0.0894  -0.1112 58  PRO F N   
7706  C CA  . PRO F 50  ? 0.8477 1.1857 1.1747 -0.1805 0.0950  -0.1147 58  PRO F CA  
7707  C C   . PRO F 50  ? 0.9220 1.2441 1.2372 -0.1819 0.1083  -0.1179 58  PRO F C   
7708  O O   . PRO F 50  ? 0.9541 1.2498 1.2425 -0.1852 0.1180  -0.1161 58  PRO F O   
7709  C CB  . PRO F 50  ? 0.8482 1.1930 1.1939 -0.1680 0.0948  -0.1123 58  PRO F CB  
7710  C CG  . PRO F 50  ? 0.9108 1.2419 1.2488 -0.1643 0.0965  -0.1071 58  PRO F CG  
7711  C CD  . PRO F 50  ? 0.8823 1.2007 1.1926 -0.1730 0.0925  -0.1068 58  PRO F CD  
7712  N N   . LEU F 51  ? 0.8685 1.1993 1.1981 -0.1784 0.1116  -0.1208 59  LEU F N   
7713  C CA  . LEU F 51  ? 0.8745 1.1948 1.1995 -0.1802 0.1226  -0.1212 59  LEU F CA  
7714  C C   . LEU F 51  ? 0.9336 1.2486 1.2724 -0.1745 0.1190  -0.1146 59  LEU F C   
7715  O O   . LEU F 51  ? 0.9456 1.2580 1.2830 -0.1720 0.1119  -0.1182 59  LEU F O   
7716  C CB  . LEU F 51  ? 0.8747 1.2035 1.1998 -0.1845 0.1259  -0.1281 59  LEU F CB  
7717  C CG  . LEU F 51  ? 0.9382 1.2575 1.2559 -0.1882 0.1390  -0.1292 59  LEU F CG  
7718  C CD1 . LEU F 51  ? 0.9542 1.2598 1.2479 -0.1989 0.1453  -0.1314 59  LEU F CD1 
7719  C CD2 . LEU F 51  ? 0.9880 1.3147 1.3132 -0.1852 0.1418  -0.1342 59  LEU F CD2 
7720  N N   . HIS F 52  ? 0.8882 1.1940 1.2382 -0.1728 0.1237  -0.1012 60  HIS F N   
7721  C CA  . HIS F 52  ? 0.8897 1.1905 1.2631 -0.1720 0.1123  -0.0868 60  HIS F CA  
7722  C C   . HIS F 52  ? 0.9679 1.2642 1.3512 -0.1774 0.1151  -0.0783 60  HIS F C   
7723  O O   . HIS F 52  ? 0.9742 1.2698 1.3600 -0.1775 0.1365  -0.0731 60  HIS F O   
7724  C CB  . HIS F 52  ? 0.8969 1.1945 1.2951 -0.1662 0.1159  -0.0677 60  HIS F CB  
7725  C CG  . HIS F 52  ? 0.9353 1.2297 1.3669 -0.1684 0.0950  -0.0480 60  HIS F CG  
7726  N ND1 . HIS F 52  ? 0.9549 1.2475 1.4277 -0.1709 0.0969  -0.0192 60  HIS F ND1 
7727  C CD2 . HIS F 52  ? 0.9593 1.2478 1.3885 -0.1701 0.0706  -0.0499 60  HIS F CD2 
7728  C CE1 . HIS F 52  ? 0.9523 1.2397 1.4498 -0.1772 0.0669  -0.0033 60  HIS F CE1 
7729  N NE2 . HIS F 52  ? 0.9628 1.2430 1.4282 -0.1770 0.0507  -0.0233 60  HIS F NE2 
7730  N N   . LEU F 53  ? 0.9380 1.2232 1.3188 -0.1826 0.0938  -0.0762 61  LEU F N   
7731  C CA  . LEU F 53  ? 0.9438 1.2213 1.3326 -0.1902 0.0887  -0.0655 61  LEU F CA  
7732  C C   . LEU F 53  ? 1.0205 1.2850 1.4384 -0.1986 0.0599  -0.0382 61  LEU F C   
7733  O O   . LEU F 53  ? 1.0443 1.2797 1.4335 -0.2058 0.0308  -0.0415 61  LEU F O   
7734  C CB  . LEU F 53  ? 0.9599 1.2207 1.3068 -0.1914 0.0844  -0.0851 61  LEU F CB  
7735  C CG  . LEU F 53  ? 1.0070 1.2767 1.3297 -0.1830 0.1024  -0.1082 61  LEU F CG  
7736  C CD1 . LEU F 53  ? 1.0266 1.2679 1.3110 -0.1793 0.1004  -0.1192 61  LEU F CD1 
7737  C CD2 . LEU F 53  ? 1.0375 1.3293 1.3712 -0.1834 0.1251  -0.1123 61  LEU F CD2 
7738  N N   . GLY F 54  ? 0.9845 1.2637 1.4565 -0.1972 0.0692  -0.0088 62  GLY F N   
7739  C CA  . GLY F 54  ? 1.0060 1.2814 1.5299 -0.2055 0.0428  0.0284  62  GLY F CA  
7740  C C   . GLY F 54  ? 1.1245 1.3742 1.6398 -0.2248 -0.0006 0.0399  62  GLY F C   
7741  O O   . GLY F 54  ? 1.1543 1.3713 1.6276 -0.2329 -0.0332 0.0289  62  GLY F O   
7742  N N   . LYS F 55  ? 1.1058 1.3620 1.6543 -0.2330 -0.0011 0.0638  63  LYS F N   
7743  C CA  . LYS F 55  ? 1.1472 1.3732 1.6835 -0.2546 -0.0456 0.0785  63  LYS F CA  
7744  C C   . LYS F 55  ? 1.2091 1.4187 1.6775 -0.2524 -0.0330 0.0439  63  LYS F C   
7745  O O   . LYS F 55  ? 1.2143 1.4194 1.6906 -0.2625 -0.0416 0.0580  63  LYS F O   
7746  C CB  . LYS F 55  ? 1.1753 1.4212 1.8050 -0.2668 -0.0590 0.1362  63  LYS F CB  
7747  C CG  . LYS F 55  ? 1.3169 1.6020 2.0009 -0.2522 -0.0057 0.1529  63  LYS F CG  
7748  C CD  . LYS F 55  ? 1.4314 1.7207 2.1572 -0.2677 -0.0211 0.1881  63  LYS F CD  
7749  C CE  . LYS F 55  ? 1.5514 1.8591 2.3898 -0.2788 -0.0416 0.2589  63  LYS F CE  
7750  N NZ  . LYS F 55  ? 1.6432 1.9558 2.5248 -0.2970 -0.0629 0.2965  63  LYS F NZ  
7751  N N   . CYS F 56  ? 1.1607 1.3639 1.5699 -0.2383 -0.0110 0.0025  64  CYS F N   
7752  C CA  . CYS F 56  ? 1.1632 1.3558 1.5178 -0.2310 0.0092  -0.0286 64  CYS F CA  
7753  C C   . CYS F 56  ? 1.2190 1.3765 1.5037 -0.2224 0.0094  -0.0590 64  CYS F C   
7754  O O   . CYS F 56  ? 1.2168 1.3776 1.5030 -0.2172 0.0084  -0.0632 64  CYS F O   
7755  C CB  . CYS F 56  ? 1.1237 1.3614 1.5073 -0.2182 0.0543  -0.0373 64  CYS F CB  
7756  S SG  . CYS F 56  ? 1.1732 1.4138 1.5394 -0.2170 0.0749  -0.0489 64  CYS F SG  
7757  N N   . ASN F 57  ? 1.1817 1.3059 1.4089 -0.2180 0.0170  -0.0777 65  ASN F N   
7758  C CA  . ASN F 57  ? 1.2051 1.2951 1.3722 -0.2037 0.0318  -0.1014 65  ASN F CA  
7759  C C   . ASN F 57  ? 1.2424 1.3715 1.4253 -0.1884 0.0723  -0.1175 65  ASN F C   
7760  O O   . ASN F 57  ? 1.1971 1.3672 1.4218 -0.1915 0.0838  -0.1132 65  ASN F O   
7761  C CB  . ASN F 57  ? 1.2396 1.2409 1.3179 -0.2080 0.0116  -0.1050 65  ASN F CB  
7762  C CG  . ASN F 57  ? 1.4468 1.4219 1.4992 -0.2145 0.0064  -0.1021 65  ASN F CG  
7763  O OD1 . ASN F 57  ? 1.2963 1.2981 1.3599 -0.2023 0.0388  -0.1127 65  ASN F OD1 
7764  N ND2 . ASN F 57  ? 1.4118 1.3279 1.4247 -0.2353 -0.0379 -0.0863 65  ASN F ND2 
7765  N N   . ILE F 58  ? 1.2396 1.3552 1.3947 -0.1724 0.0944  -0.1316 66  ILE F N   
7766  C CA  . ILE F 58  ? 1.2132 1.3671 1.3943 -0.1602 0.1273  -0.1402 66  ILE F CA  
7767  C C   . ILE F 58  ? 1.2838 1.4289 1.4533 -0.1589 0.1391  -0.1431 66  ILE F C   
7768  O O   . ILE F 58  ? 1.2411 1.4317 1.4508 -0.1589 0.1554  -0.1452 66  ILE F O   
7769  C CB  . ILE F 58  ? 1.2698 1.4138 1.4400 -0.1428 0.1487  -0.1441 66  ILE F CB  
7770  C CG1 . ILE F 58  ? 1.2604 1.4240 1.4515 -0.1452 0.1372  -0.1406 66  ILE F CG1 
7771  C CG2 . ILE F 58  ? 1.2410 1.4269 1.4520 -0.1337 0.1760  -0.1447 66  ILE F CG2 
7772  C CD1 . ILE F 58  ? 1.4137 1.5472 1.5805 -0.1300 0.1515  -0.1392 66  ILE F CD1 
7773  N N   . ALA F 59  ? 1.2984 1.3793 1.4077 -0.1600 0.1281  -0.1425 67  ALA F N   
7774  C CA  . ALA F 59  ? 1.3036 1.3704 1.3965 -0.1586 0.1376  -0.1444 67  ALA F CA  
7775  C C   . ALA F 59  ? 1.2746 1.3901 1.4206 -0.1750 0.1259  -0.1346 67  ALA F C   
7776  O O   . ALA F 59  ? 1.2371 1.3931 1.4176 -0.1713 0.1488  -0.1383 67  ALA F O   
7777  C CB  . ALA F 59  ? 1.4068 1.3794 1.4090 -0.1589 0.1228  -0.1443 67  ALA F CB  
7778  N N   . GLY F 60  ? 1.2006 1.3121 1.3587 -0.1921 0.0932  -0.1185 68  GLY F N   
7779  C CA  . GLY F 60  ? 1.1457 1.3003 1.3634 -0.2049 0.0875  -0.1000 68  GLY F CA  
7780  C C   . GLY F 60  ? 1.1091 1.3241 1.3813 -0.1992 0.1167  -0.1031 68  GLY F C   
7781  O O   . GLY F 60  ? 1.0785 1.3217 1.3845 -0.2020 0.1326  -0.0952 68  GLY F O   
7782  N N   . TRP F 61  ? 1.0336 1.2608 1.3068 -0.1917 0.1244  -0.1140 69  TRP F N   
7783  C CA  . TRP F 61  ? 0.9887 1.2564 1.2947 -0.1892 0.1461  -0.1177 69  TRP F CA  
7784  C C   . TRP F 61  ? 1.0161 1.2990 1.3207 -0.1839 0.1706  -0.1314 69  TRP F C   
7785  O O   . TRP F 61  ? 0.9975 1.2995 1.3208 -0.1879 0.1870  -0.1291 69  TRP F O   
7786  C CB  . TRP F 61  ? 0.9692 1.2423 1.2748 -0.1853 0.1416  -0.1228 69  TRP F CB  
7787  C CG  . TRP F 61  ? 0.9613 1.2609 1.2819 -0.1851 0.1590  -0.1285 69  TRP F CG  
7788  C CD1 . TRP F 61  ? 0.9880 1.2957 1.3222 -0.1900 0.1712  -0.1206 69  TRP F CD1 
7789  C CD2 . TRP F 61  ? 0.9577 1.2685 1.2753 -0.1815 0.1654  -0.1396 69  TRP F CD2 
7790  N NE1 . TRP F 61  ? 0.9822 1.2958 1.3069 -0.1921 0.1805  -0.1301 69  TRP F NE1 
7791  C CE2 . TRP F 61  ? 0.9993 1.3209 1.3216 -0.1889 0.1730  -0.1399 69  TRP F CE2 
7792  C CE3 . TRP F 61  ? 0.9888 1.2963 1.3011 -0.1724 0.1668  -0.1446 69  TRP F CE3 
7793  C CZ2 . TRP F 61  ? 0.9938 1.3257 1.3178 -0.1928 0.1714  -0.1445 69  TRP F CZ2 
7794  C CZ3 . TRP F 61  ? 1.0007 1.3289 1.3315 -0.1727 0.1711  -0.1448 69  TRP F CZ3 
7795  C CH2 . TRP F 61  ? 0.9997 1.3415 1.3373 -0.1855 0.1683  -0.1446 69  TRP F CH2 
7796  N N   . ILE F 62  ? 0.9612 1.2310 1.2441 -0.1738 0.1759  -0.1426 70  ILE F N   
7797  C CA  . ILE F 62  ? 0.9293 1.2153 1.2219 -0.1676 0.1971  -0.1505 70  ILE F CA  
7798  C C   . ILE F 62  ? 0.9783 1.2623 1.2692 -0.1682 0.2087  -0.1510 70  ILE F C   
7799  O O   . ILE F 62  ? 0.9646 1.2718 1.2752 -0.1697 0.2248  -0.1545 70  ILE F O   
7800  C CB  . ILE F 62  ? 0.9773 1.2496 1.2603 -0.1527 0.2056  -0.1532 70  ILE F CB  
7801  C CG1 . ILE F 62  ? 0.9619 1.2660 1.2813 -0.1502 0.2214  -0.1523 70  ILE F CG1 
7802  C CG2 . ILE F 62  ? 1.0164 1.2363 1.2523 -0.1400 0.2111  -0.1544 70  ILE F CG2 
7803  C CD1 . ILE F 62  ? 1.0177 1.3510 1.3641 -0.1618 0.2096  -0.1489 70  ILE F CD1 
7804  N N   . LEU F 63  ? 0.9438 1.1967 1.2091 -0.1693 0.1973  -0.1458 71  LEU F N   
7805  C CA  . LEU F 63  ? 0.9264 1.1746 1.1886 -0.1704 0.2054  -0.1436 71  LEU F CA  
7806  C C   . LEU F 63  ? 0.9340 1.2143 1.2349 -0.1819 0.2110  -0.1323 71  LEU F C   
7807  O O   . LEU F 63  ? 0.9229 1.2160 1.2350 -0.1814 0.2295  -0.1330 71  LEU F O   
7808  C CB  . LEU F 63  ? 0.9675 1.1625 1.1828 -0.1721 0.1842  -0.1378 71  LEU F CB  
7809  C CG  . LEU F 63  ? 1.0713 1.2100 1.2260 -0.1563 0.1909  -0.1479 71  LEU F CG  
7810  C CD1 . LEU F 63  ? 1.1442 1.2117 1.2338 -0.1646 0.1592  -0.1409 71  LEU F CD1 
7811  C CD2 . LEU F 63  ? 1.0904 1.2296 1.2426 -0.1413 0.2225  -0.1555 71  LEU F CD2 
7812  N N   . GLY F 64  ? 0.8576 1.1460 1.1780 -0.1900 0.1996  -0.1195 72  GLY F N   
7813  C CA  . GLY F 64  ? 0.8194 1.1275 1.1757 -0.1967 0.2127  -0.1018 72  GLY F CA  
7814  C C   . GLY F 64  ? 0.8332 1.1348 1.2127 -0.2053 0.1948  -0.0738 72  GLY F C   
7815  O O   . GLY F 64  ? 0.7915 1.1070 1.2024 -0.2081 0.2116  -0.0559 72  GLY F O   
7816  N N   . ASN F 65  ? 0.8300 1.1070 1.1951 -0.2109 0.1590  -0.0665 73  ASN F N   
7817  C CA  . ASN F 65  ? 0.8648 1.1283 1.2518 -0.2250 0.1265  -0.0345 73  ASN F CA  
7818  C C   . ASN F 65  ? 0.9145 1.2107 1.3743 -0.2279 0.1427  0.0006  73  ASN F C   
7819  O O   . ASN F 65  ? 0.9020 1.2103 1.3767 -0.2211 0.1604  0.0002  73  ASN F O   
7820  C CB  . ASN F 65  ? 0.9148 1.1402 1.2685 -0.2319 0.0854  -0.0341 73  ASN F CB  
7821  C CG  . ASN F 65  ? 1.2540 1.4595 1.6311 -0.2520 0.0400  0.0033  73  ASN F CG  
7822  O OD1 . ASN F 65  ? 1.1905 1.3826 1.5708 -0.2641 0.0217  0.0218  73  ASN F OD1 
7823  N ND2 . ASN F 65  ? 1.1929 1.3931 1.5867 -0.2580 0.0162  0.0172  73  ASN F ND2 
7824  N N   . PRO F 66  ? 0.8711 1.1783 1.3756 -0.2358 0.1430  0.0330  74  PRO F N   
7825  C CA  . PRO F 66  ? 0.8519 1.1864 1.4304 -0.2334 0.1714  0.0724  74  PRO F CA  
7826  C C   . PRO F 66  ? 0.9358 1.2730 1.5586 -0.2345 0.1598  0.1018  74  PRO F C   
7827  O O   . PRO F 66  ? 0.9263 1.2765 1.5945 -0.2240 0.1990  0.1267  74  PRO F O   
7828  C CB  . PRO F 66  ? 0.8775 1.2209 1.5007 -0.2446 0.1610  0.1083  74  PRO F CB  
7829  C CG  . PRO F 66  ? 0.9690 1.2795 1.5372 -0.2580 0.1112  0.0924  74  PRO F CG  
7830  C CD  . PRO F 66  ? 0.9160 1.2079 1.4051 -0.2453 0.1227  0.0381  74  PRO F CD  
7831  N N   . GLU F 67  ? 0.9291 1.2463 1.5325 -0.2452 0.1108  0.0990  75  GLU F N   
7832  C CA  . GLU F 67  ? 0.9328 1.2525 1.5784 -0.2465 0.0964  0.1255  75  GLU F CA  
7833  C C   . GLU F 67  ? 0.9755 1.2949 1.5866 -0.2297 0.1250  0.0934  75  GLU F C   
7834  O O   . GLU F 67  ? 0.9822 1.3045 1.6266 -0.2262 0.1234  0.1130  75  GLU F O   
7835  C CB  . GLU F 67  ? 0.9895 1.2804 1.6239 -0.2674 0.0297  0.1377  75  GLU F CB  
7836  C CG  . GLU F 67  ? 1.2028 1.4876 1.8773 -0.2897 -0.0095 0.1804  75  GLU F CG  
7837  C CD  . GLU F 67  ? 1.5750 1.9000 2.3673 -0.2906 0.0086  0.2444  75  GLU F CD  
7838  O OE1 . GLU F 67  ? 1.7404 2.0765 2.6031 -0.2937 -0.0041 0.2858  75  GLU F OE1 
7839  O OE2 . GLU F 67  ? 1.4787 1.8233 2.2971 -0.2866 0.0389  0.2563  75  GLU F OE2 
7840  N N   . CYS F 68  ? 0.9083 1.2241 1.4573 -0.2205 0.1494  0.0481  76  CYS F N   
7841  C CA  . CYS F 68  ? 1.0476 1.3606 1.5584 -0.2088 0.1708  0.0176  76  CYS F CA  
7842  C C   . CYS F 68  ? 1.1392 1.4542 1.6283 -0.2006 0.2149  0.0015  76  CYS F C   
7843  O O   . CYS F 68  ? 0.7477 1.0538 1.2050 -0.1941 0.2328  -0.0172 76  CYS F O   
7844  C CB  . CYS F 68  ? 1.0634 1.3624 1.5191 -0.2103 0.1430  -0.0173 76  CYS F CB  
7845  S SG  . CYS F 68  ? 1.1473 1.4198 1.5980 -0.2242 0.0872  -0.0033 76  CYS F SG  
7846  N N   . ALA F 74  ? 1.2541 1.4504 1.4273 -0.2242 0.1964  -0.1344 82  ALA F N   
7847  C CA  . ALA F 74  ? 1.2895 1.4613 1.4254 -0.2364 0.1732  -0.1371 82  ALA F CA  
7848  C C   . ALA F 74  ? 1.3207 1.5130 1.4684 -0.2540 0.1430  -0.1417 82  ALA F C   
7849  O O   . ALA F 74  ? 1.2670 1.5089 1.4702 -0.2489 0.1389  -0.1422 82  ALA F O   
7850  C CB  . ALA F 74  ? 1.2761 1.4683 1.4364 -0.2264 0.1621  -0.1323 82  ALA F CB  
7851  N N   . SER F 75  ? 1.3083 1.4552 1.4019 -0.2752 0.1214  -0.1410 83  SER F N   
7852  C CA  . SER F 75  ? 1.2966 1.4576 1.4070 -0.2971 0.0859  -0.1363 83  SER F CA  
7853  C C   . SER F 75  ? 1.2718 1.4921 1.4528 -0.2946 0.0608  -0.1250 83  SER F C   
7854  O O   . SER F 75  ? 1.2484 1.5067 1.4838 -0.3014 0.0451  -0.1147 83  SER F O   
7855  C CB  . SER F 75  ? 1.4286 1.5111 1.4515 -0.3248 0.0622  -0.1349 83  SER F CB  
7856  O OG  . SER F 75  ? 1.5277 1.6268 1.5785 -0.3503 0.0161  -0.1220 83  SER F OG  
7857  N N   . SER F 76  A 1.1931 1.4179 1.3749 -0.2844 0.0595  -0.1232 83  SER F N   
7858  C CA  . SER F 76  A 1.1418 1.4173 1.3866 -0.2797 0.0418  -0.1107 83  SER F CA  
7859  C C   . SER F 76  A 1.1576 1.4467 1.4124 -0.2577 0.0582  -0.1147 83  SER F C   
7860  O O   . SER F 76  A 1.1803 1.4344 1.3909 -0.2508 0.0744  -0.1223 83  SER F O   
7861  C CB  . SER F 76  A 1.2092 1.4707 1.4449 -0.3053 -0.0002 -0.0946 83  SER F CB  
7862  O OG  . SER F 76  A 1.3530 1.5386 1.4943 -0.3218 -0.0108 -0.1011 83  SER F OG  
7863  N N   . TRP F 77  ? 1.0552 1.3909 1.3697 -0.2454 0.0571  -0.1064 84  TRP F N   
7864  C CA  . TRP F 77  ? 1.0213 1.3684 1.3469 -0.2270 0.0675  -0.1085 84  TRP F CA  
7865  C C   . TRP F 77  ? 1.0649 1.4488 1.4429 -0.2215 0.0588  -0.0931 84  TRP F C   
7866  O O   . TRP F 77  ? 1.0690 1.4771 1.4899 -0.2250 0.0544  -0.0788 84  TRP F O   
7867  C CB  . TRP F 77  ? 0.9730 1.3205 1.3004 -0.2099 0.0921  -0.1188 84  TRP F CB  
7868  C CG  . TRP F 77  ? 0.9622 1.3299 1.3205 -0.2023 0.1023  -0.1181 84  TRP F CG  
7869  C CD1 . TRP F 77  ? 0.9853 1.3672 1.3703 -0.1873 0.1103  -0.1132 84  TRP F CD1 
7870  C CD2 . TRP F 77  ? 0.9585 1.3243 1.3158 -0.2070 0.1103  -0.1218 84  TRP F CD2 
7871  N NE1 . TRP F 77  ? 0.9760 1.3602 1.3727 -0.1810 0.1244  -0.1130 84  TRP F NE1 
7872  C CE2 . TRP F 77  ? 0.9965 1.3768 1.3822 -0.1932 0.1232  -0.1185 84  TRP F CE2 
7873  C CE3 . TRP F 77  ? 0.9921 1.3382 1.3213 -0.2205 0.1109  -0.1272 84  TRP F CE3 
7874  C CZ2 . TRP F 77  ? 0.9857 1.3677 1.3788 -0.1919 0.1353  -0.1204 84  TRP F CZ2 
7875  C CZ3 . TRP F 77  ? 1.0028 1.3551 1.3429 -0.2209 0.1213  -0.1296 84  TRP F CZ3 
7876  C CH2 . TRP F 77  ? 0.9893 1.3627 1.3644 -0.2066 0.1325  -0.1261 84  TRP F CH2 
7877  N N   . SER F 78  ? 1.0043 1.3918 1.3840 -0.2115 0.0594  -0.0923 85  SER F N   
7878  C CA  . SER F 78  ? 0.9851 1.4030 1.4116 -0.2036 0.0569  -0.0758 85  SER F CA  
7879  C C   . SER F 78  ? 1.0181 1.4431 1.4645 -0.1810 0.0830  -0.0771 85  SER F C   
7880  O O   . SER F 78  ? 1.0101 1.4543 1.4979 -0.1716 0.0917  -0.0592 85  SER F O   
7881  C CB  . SER F 78  ? 1.0358 1.4490 1.4491 -0.2051 0.0443  -0.0734 85  SER F CB  
7882  O OG  . SER F 78  ? 1.1551 1.5402 1.5259 -0.1980 0.0542  -0.0899 85  SER F OG  
7883  N N   . TYR F 79  ? 0.9730 1.3747 1.3865 -0.1729 0.0956  -0.0947 86  TYR F N   
7884  C CA  . TYR F 79  ? 0.9687 1.3539 1.3739 -0.1561 0.1138  -0.0993 86  TYR F CA  
7885  C C   . TYR F 79  ? 1.0098 1.3705 1.3817 -0.1581 0.1142  -0.1138 86  TYR F C   
7886  O O   . TYR F 79  ? 0.9912 1.3503 1.3528 -0.1674 0.1067  -0.1177 86  TYR F O   
7887  C CB  . TYR F 79  ? 0.9875 1.3674 1.3939 -0.1443 0.1171  -0.0947 86  TYR F CB  
7888  C CG  . TYR F 79  ? 1.0015 1.3802 1.3963 -0.1487 0.1028  -0.1000 86  TYR F CG  
7889  C CD1 . TYR F 79  ? 1.0188 1.4161 1.4254 -0.1577 0.0895  -0.0938 86  TYR F CD1 
7890  C CD2 . TYR F 79  ? 1.0159 1.3699 1.3882 -0.1438 0.1014  -0.1072 86  TYR F CD2 
7891  C CE1 . TYR F 79  ? 1.0154 1.4053 1.4085 -0.1578 0.0822  -0.0968 86  TYR F CE1 
7892  C CE2 . TYR F 79  ? 1.0156 1.3705 1.3886 -0.1448 0.0919  -0.1067 86  TYR F CE2 
7893  C CZ  . TYR F 79  ? 1.0686 1.4410 1.4508 -0.1495 0.0861  -0.1023 86  TYR F CZ  
7894  O OH  . TYR F 79  ? 1.0610 1.4280 1.4405 -0.1471 0.0823  -0.1004 86  TYR F OH  
7895  N N   . ILE F 80  ? 0.9874 1.3227 1.3401 -0.1494 0.1241  -0.1181 87  ILE F N   
7896  C CA  . ILE F 80  ? 0.9916 1.3059 1.3214 -0.1543 0.1189  -0.1254 87  ILE F CA  
7897  C C   . ILE F 80  ? 1.0508 1.3396 1.3636 -0.1522 0.1070  -0.1242 87  ILE F C   
7898  O O   . ILE F 80  ? 1.0824 1.3452 1.3748 -0.1437 0.1096  -0.1238 87  ILE F O   
7899  C CB  . ILE F 80  ? 1.0487 1.3452 1.3624 -0.1518 0.1296  -0.1296 87  ILE F CB  
7900  C CG1 . ILE F 80  ? 1.0472 1.3645 1.3839 -0.1485 0.1446  -0.1258 87  ILE F CG1 
7901  C CG2 . ILE F 80  ? 1.0533 1.3458 1.3617 -0.1616 0.1236  -0.1320 87  ILE F CG2 
7902  C CD1 . ILE F 80  ? 1.1559 1.4430 1.4740 -0.1338 0.1643  -0.1243 87  ILE F CD1 
7903  N N   . VAL F 81  ? 0.9774 1.2683 1.2989 -0.1597 0.0958  -0.1200 88  VAL F N   
7904  C CA  . VAL F 81  ? 0.9757 1.2457 1.2942 -0.1613 0.0787  -0.1124 88  VAL F CA  
7905  C C   . VAL F 81  ? 1.0204 1.2662 1.3298 -0.1699 0.0665  -0.1063 88  VAL F C   
7906  O O   . VAL F 81  ? 0.9954 1.2566 1.3276 -0.1750 0.0708  -0.0990 88  VAL F O   
7907  C CB  . VAL F 81  ? 1.0001 1.2891 1.3478 -0.1610 0.0754  -0.1029 88  VAL F CB  
7908  C CG1 . VAL F 81  ? 1.0134 1.2826 1.3645 -0.1618 0.0560  -0.0930 88  VAL F CG1 
7909  C CG2 . VAL F 81  ? 0.9830 1.2950 1.3358 -0.1558 0.0851  -0.1081 88  VAL F CG2 
7910  N N   . GLU F 82  ? 1.0055 1.2056 1.2750 -0.1718 0.0523  -0.1077 89  GLU F N   
7911  C CA  . GLU F 82  ? 1.0320 1.1967 1.2811 -0.1835 0.0321  -0.1001 89  GLU F CA  
7912  C C   . GLU F 82  ? 1.1236 1.2525 1.3641 -0.1946 -0.0025 -0.0857 89  GLU F C   
7913  O O   . GLU F 82  ? 1.1504 1.2469 1.3548 -0.1902 -0.0065 -0.0922 89  GLU F O   
7914  C CB  . GLU F 82  ? 1.0921 1.2132 1.2815 -0.1778 0.0431  -0.1138 89  GLU F CB  
7915  C CG  . GLU F 82  ? 1.2472 1.3280 1.4055 -0.1897 0.0247  -0.1085 89  GLU F CG  
7916  C CD  . GLU F 82  ? 1.5459 1.5600 1.6250 -0.1811 0.0366  -0.1211 89  GLU F CD  
7917  O OE1 . GLU F 82  ? 1.6952 1.6305 1.7050 -0.1901 0.0111  -0.1182 89  GLU F OE1 
7918  O OE2 . GLU F 82  ? 1.3036 1.3364 1.3864 -0.1652 0.0715  -0.1313 89  GLU F OE2 
7919  N N   . THR F 83  ? 1.0776 1.2130 1.3579 -0.2090 -0.0268 -0.0619 90  THR F N   
7920  C CA  . THR F 83  ? 1.1105 1.2147 1.3973 -0.2243 -0.0678 -0.0399 90  THR F CA  
7921  C C   . THR F 83  ? 1.2726 1.2926 1.4705 -0.2368 -0.0965 -0.0468 90  THR F C   
7922  O O   . THR F 83  ? 1.3015 1.3012 1.4665 -0.2394 -0.0928 -0.0530 90  THR F O   
7923  C CB  . THR F 83  ? 1.1792 1.3157 1.5455 -0.2359 -0.0828 -0.0039 90  THR F CB  
7924  O OG1 . THR F 83  ? 1.1479 1.3434 1.5718 -0.2201 -0.0439 -0.0012 90  THR F OG1 
7925  C CG2 . THR F 83  ? 1.1863 1.3033 1.5861 -0.2527 -0.1272 0.0287  90  THR F CG2 
7926  N N   . PRO F 84  A 1.2971 1.2573 1.4438 -0.2439 -0.1227 -0.0470 90  PRO F N   
7927  C CA  . PRO F 84  A 1.4084 1.2640 1.4466 -0.2569 -0.1497 -0.0532 90  PRO F CA  
7928  C C   . PRO F 84  A 1.5190 1.3456 1.5615 -0.2855 -0.1992 -0.0268 90  PRO F C   
7929  O O   . PRO F 84  A 1.5706 1.3293 1.5332 -0.2931 -0.2096 -0.0339 90  PRO F O   
7930  C CB  . PRO F 84  A 1.4836 1.2835 1.4749 -0.2605 -0.1684 -0.0543 90  PRO F CB  
7931  C CG  . PRO F 84  A 1.4546 1.3339 1.5517 -0.2598 -0.1727 -0.0361 90  PRO F CG  
7932  C CD  . PRO F 84  A 1.2987 1.2732 1.4749 -0.2411 -0.1291 -0.0406 90  PRO F CD  
7933  N N   . SER F 85  ? 1.4632 1.3452 1.6072 -0.2994 -0.2255 0.0076  91  SER F N   
7934  C CA  . SER F 85  ? 1.4956 1.3737 1.6850 -0.3273 -0.2735 0.0470  91  SER F CA  
7935  C C   . SER F 85  ? 1.5361 1.4521 1.7528 -0.3229 -0.2500 0.0479  91  SER F C   
7936  O O   . SER F 85  ? 1.5669 1.4601 1.7926 -0.3467 -0.2898 0.0758  91  SER F O   
7937  C CB  . SER F 85  ? 1.4993 1.4392 1.8108 -0.3340 -0.2906 0.0885  91  SER F CB  
7938  O OG  . SER F 85  ? 1.6596 1.5771 1.9561 -0.3339 -0.3043 0.0853  91  SER F OG  
7939  N N   . SER F 86  ? 1.4481 1.4198 1.6789 -0.2946 -0.1889 0.0201  92  SER F N   
7940  C CA  . SER F 86  ? 1.4162 1.4253 1.6702 -0.2876 -0.1597 0.0167  92  SER F CA  
7941  C C   . SER F 86  ? 1.5509 1.4887 1.7057 -0.2926 -0.1681 -0.0022 92  SER F C   
7942  O O   . SER F 86  ? 1.5801 1.4721 1.6505 -0.2779 -0.1465 -0.0342 92  SER F O   
7943  C CB  . SER F 86  ? 1.3890 1.4647 1.6760 -0.2601 -0.0996 -0.0066 92  SER F CB  
7944  O OG  . SER F 86  ? 1.5125 1.5628 1.7264 -0.2436 -0.0729 -0.0436 92  SER F OG  
7945  N N   . ASP F 87  ? 1.5485 1.4741 1.7162 -0.3123 -0.1976 0.0223  93  ASP F N   
7946  C CA  . ASP F 87  ? 1.6322 1.4849 1.7069 -0.3196 -0.2103 0.0104  93  ASP F CA  
7947  C C   . ASP F 87  ? 1.6222 1.5305 1.7443 -0.3114 -0.1784 0.0116  93  ASP F C   
7948  O O   . ASP F 87  ? 1.6772 1.5348 1.7328 -0.3152 -0.1837 0.0032  93  ASP F O   
7949  C CB  . ASP F 87  ? 1.7656 1.5349 1.7958 -0.3567 -0.2863 0.0411  93  ASP F CB  
7950  C CG  . ASP F 87  ? 2.0446 1.7330 1.9997 -0.3682 -0.3225 0.0373  93  ASP F CG  
7951  O OD1 . ASP F 87  ? 2.1413 1.7432 1.9711 -0.3563 -0.3067 0.0037  93  ASP F OD1 
7952  O OD2 . ASP F 87  ? 2.1247 1.8294 2.1450 -0.3891 -0.3661 0.0717  93  ASP F OD2 
7953  N N   . ASN F 88  ? 1.4663 1.4697 1.6933 -0.2990 -0.1422 0.0211  94  ASN F N   
7954  C CA  . ASN F 88  ? 1.4042 1.4593 1.6780 -0.2911 -0.1082 0.0237  94  ASN F CA  
7955  C C   . ASN F 88  ? 1.3999 1.4636 1.6291 -0.2663 -0.0570 -0.0182 94  ASN F C   
7956  O O   . ASN F 88  ? 1.3301 1.4420 1.5897 -0.2487 -0.0183 -0.0337 94  ASN F O   
7957  C CB  . ASN F 88  ? 1.3531 1.4845 1.7430 -0.2890 -0.0894 0.0564  94  ASN F CB  
7958  C CG  . ASN F 88  ? 1.7060 1.8433 2.1614 -0.3118 -0.1250 0.1078  94  ASN F CG  
7959  O OD1 . ASN F 88  ? 1.5798 1.7721 2.1338 -0.3085 -0.1043 0.1434  94  ASN F OD1 
7960  N ND2 . ASN F 88  ? 1.7085 1.7791 2.1018 -0.3350 -0.1784 0.1140  94  ASN F ND2 
7961  N N   . GLY F 89  ? 1.3962 1.4068 1.5528 -0.2669 -0.0611 -0.0318 95  GLY F N   
7962  C CA  . GLY F 89  ? 1.3825 1.3868 1.4933 -0.2449 -0.0181 -0.0644 95  GLY F CA  
7963  C C   . GLY F 89  ? 1.4878 1.4200 1.5207 -0.2506 -0.0333 -0.0667 95  GLY F C   
7964  O O   . GLY F 89  ? 1.5812 1.4320 1.5449 -0.2680 -0.0782 -0.0570 95  GLY F O   
7965  N N   . THR F 90  ? 1.3862 1.3413 1.4249 -0.2374 0.0018  -0.0783 96  THR F N   
7966  C CA  . THR F 90  ? 1.4309 1.3261 1.4028 -0.2386 -0.0030 -0.0811 96  THR F CA  
7967  C C   . THR F 90  ? 1.4823 1.3595 1.4677 -0.2699 -0.0569 -0.0468 96  THR F C   
7968  O O   . THR F 90  ? 1.5641 1.3467 1.4615 -0.2866 -0.1008 -0.0398 96  THR F O   
7969  C CB  . THR F 90  ? 1.5798 1.3709 1.4282 -0.2230 0.0071  -0.1032 96  THR F CB  
7970  O OG1 . THR F 90  ? 1.6807 1.3850 1.4542 -0.2413 -0.0406 -0.0946 96  THR F OG1 
7971  C CG2 . THR F 90  ? 1.4969 1.3141 1.3538 -0.1924 0.0609  -0.1260 96  THR F CG2 
7972  N N   . CYS F 91  ? 1.3504 1.3137 1.4458 -0.2779 -0.0523 -0.0220 97  CYS F N   
7973  C CA  . CYS F 91  ? 1.3468 1.3207 1.4952 -0.3048 -0.0933 0.0212  97  CYS F CA  
7974  C C   . CYS F 91  ? 1.4220 1.3315 1.4966 -0.3126 -0.1112 0.0202  97  CYS F C   
7975  O O   . CYS F 91  ? 1.4814 1.3379 1.5318 -0.3415 -0.1704 0.0501  97  CYS F O   
7976  C CB  . CYS F 91  ? 1.2588 1.3326 1.5292 -0.2993 -0.0579 0.0423  97  CYS F CB  
7977  S SG  . CYS F 91  ? 1.2507 1.3717 1.5269 -0.2707 0.0140  0.0081  97  CYS F SG  
7978  N N   . TYR F 92  ? 1.3420 1.2520 1.3800 -0.2876 -0.0623 -0.0119 98  TYR F N   
7979  C CA  . TYR F 92  ? 1.4032 1.2435 1.3581 -0.2883 -0.0695 -0.0182 98  TYR F CA  
7980  C C   . TYR F 92  ? 1.5755 1.2996 1.3917 -0.2800 -0.0778 -0.0439 98  TYR F C   
7981  O O   . TYR F 92  ? 1.5512 1.2842 1.3570 -0.2560 -0.0392 -0.0696 98  TYR F O   
7982  C CB  . TYR F 92  ? 1.3407 1.2339 1.3256 -0.2629 -0.0090 -0.0378 98  TYR F CB  
7983  C CG  . TYR F 92  ? 1.4038 1.2374 1.3230 -0.2655 -0.0175 -0.0363 98  TYR F CG  
7984  C CD1 . TYR F 92  ? 1.5255 1.2530 1.3151 -0.2506 -0.0103 -0.0607 98  TYR F CD1 
7985  C CD2 . TYR F 92  ? 1.3767 1.2527 1.3599 -0.2816 -0.0304 -0.0070 98  TYR F CD2 
7986  C CE1 . TYR F 92  ? 1.6067 1.2662 1.3230 -0.2524 -0.0187 -0.0588 98  TYR F CE1 
7987  C CE2 . TYR F 92  ? 1.4492 1.2678 1.3692 -0.2853 -0.0417 -0.0043 98  TYR F CE2 
7988  C CZ  . TYR F 92  ? 1.6377 1.3453 1.4198 -0.2709 -0.0371 -0.0317 98  TYR F CZ  
7989  O OH  . TYR F 92  ? 1.7279 1.3670 1.4350 -0.2727 -0.0461 -0.0298 98  TYR F OH  
7990  N N   . PRO F 93  ? 1.6640 1.2714 1.3697 -0.3008 -0.1292 -0.0339 99  PRO F N   
7991  C CA  . PRO F 93  ? 1.7870 1.2634 1.3430 -0.2914 -0.1317 -0.0569 99  PRO F CA  
7992  C C   . PRO F 93  ? 1.8563 1.3020 1.3509 -0.2491 -0.0600 -0.0909 99  PRO F C   
7993  O O   . PRO F 93  ? 1.8285 1.3082 1.3490 -0.2355 -0.0282 -0.0953 99  PRO F O   
7994  C CB  . PRO F 93  ? 1.9482 1.3011 1.3957 -0.3261 -0.2037 -0.0353 99  PRO F CB  
7995  C CG  . PRO F 93  ? 1.9493 1.3672 1.4760 -0.3393 -0.2143 -0.0116 99  PRO F CG  
7996  C CD  . PRO F 93  ? 1.7290 1.3078 1.4331 -0.3347 -0.1877 0.0014  99  PRO F CD  
7997  N N   . GLY F 94  ? 1.2130 1.5016 1.2691 -0.3432 -0.0461 -0.3139 100 GLY F N   
7998  C CA  . GLY F 94  ? 1.2030 1.4880 1.2366 -0.3008 -0.0148 -0.3174 100 GLY F CA  
7999  C C   . GLY F 94  ? 1.2637 1.4790 1.2612 -0.2765 0.0042  -0.3358 100 GLY F C   
8000  O O   . GLY F 94  ? 1.3307 1.4771 1.2931 -0.2932 -0.0101 -0.3555 100 GLY F O   
8001  N N   . ASP F 95  ? 1.1612 1.3952 1.1691 -0.2371 0.0360  -0.3260 101 ASP F N   
8002  C CA  . ASP F 95  ? 1.1943 1.3734 1.1753 -0.2059 0.0592  -0.3365 101 ASP F CA  
8003  C C   . ASP F 95  ? 1.1241 1.3495 1.1783 -0.1877 0.0794  -0.3093 101 ASP F C   
8004  O O   . ASP F 95  ? 1.0475 1.3392 1.1411 -0.1748 0.0912  -0.2854 101 ASP F O   
8005  C CB  . ASP F 95  ? 1.3107 1.4566 1.2120 -0.1680 0.0805  -0.3518 101 ASP F CB  
8006  C CG  . ASP F 95  ? 1.5431 1.6256 1.3521 -0.1847 0.0579  -0.3838 101 ASP F CG  
8007  O OD1 . ASP F 95  ? 1.6093 1.6202 1.3871 -0.2128 0.0336  -0.4057 101 ASP F OD1 
8008  O OD2 . ASP F 95  ? 1.6458 1.7474 1.4100 -0.1703 0.0635  -0.3857 101 ASP F OD2 
8009  N N   . PHE F 96  ? 1.0695 1.2592 1.1415 -0.1904 0.0798  -0.3111 102 PHE F N   
8010  C CA  . PHE F 96  ? 1.0029 1.2291 1.1364 -0.1754 0.0947  -0.2864 102 PHE F CA  
8011  C C   . PHE F 96  ? 1.1287 1.3361 1.2366 -0.1302 0.1249  -0.2841 102 PHE F C   
8012  O O   . PHE F 96  ? 1.2122 1.3463 1.2714 -0.1149 0.1327  -0.3029 102 PHE F O   
8013  C CB  . PHE F 96  ? 1.0014 1.2027 1.1640 -0.1968 0.0824  -0.2855 102 PHE F CB  
8014  C CG  . PHE F 96  ? 0.9338 1.1885 1.1636 -0.1963 0.0854  -0.2587 102 PHE F CG  
8015  C CD1 . PHE F 96  ? 0.9560 1.2326 1.2082 -0.1668 0.1048  -0.2401 102 PHE F CD1 
8016  C CD2 . PHE F 96  ? 0.9037 1.1864 1.1712 -0.2243 0.0682  -0.2501 102 PHE F CD2 
8017  C CE1 . PHE F 96  ? 0.9027 1.2233 1.2096 -0.1712 0.1012  -0.2161 102 PHE F CE1 
8018  C CE2 . PHE F 96  ? 0.8824 1.2018 1.1966 -0.2228 0.0691  -0.2293 102 PHE F CE2 
8019  C CZ  . PHE F 96  ? 0.8468 1.1821 1.1782 -0.1992 0.0828  -0.2137 102 PHE F CZ  
8020  N N   . ILE F 97  ? 1.0551 1.3281 1.1948 -0.1079 0.1423  -0.2583 103 ILE F N   
8021  C CA  . ILE F 97  ? 1.0919 1.3720 1.2201 -0.0604 0.1753  -0.2447 103 ILE F CA  
8022  C C   . ILE F 97  ? 1.1086 1.3918 1.2827 -0.0475 0.1842  -0.2255 103 ILE F C   
8023  O O   . ILE F 97  ? 1.0241 1.3518 1.2614 -0.0702 0.1693  -0.2053 103 ILE F O   
8024  C CB  . ILE F 97  ? 1.0966 1.4580 1.2521 -0.0476 0.1874  -0.2164 103 ILE F CB  
8025  C CG1 . ILE F 97  ? 1.1104 1.4798 1.2348 -0.0711 0.1703  -0.2305 103 ILE F CG1 
8026  C CG2 . ILE F 97  ? 1.1504 1.5264 1.2875 0.0059  0.2256  -0.1991 103 ILE F CG2 
8027  C CD1 . ILE F 97  ? 1.3437 1.6448 1.3699 -0.0627 0.1709  -0.2672 103 ILE F CD1 
8028  N N   . ASP F 98  ? 1.1266 1.3543 1.2613 -0.0106 0.2070  -0.2333 104 ASP F N   
8029  C CA  . ASP F 98  ? 1.1112 1.3333 1.2801 0.0086  0.2183  -0.2146 104 ASP F CA  
8030  C C   . ASP F 98  ? 1.1003 1.2939 1.2932 -0.0297 0.1916  -0.2223 104 ASP F C   
8031  O O   . ASP F 98  ? 1.0406 1.2621 1.2843 -0.0275 0.1916  -0.1975 104 ASP F O   
8032  C CB  . ASP F 98  ? 1.0739 1.3924 1.3176 0.0264  0.2315  -0.1668 104 ASP F CB  
8033  C CG  . ASP F 98  ? 1.2735 1.6408 1.5127 0.0690  0.2631  -0.1441 104 ASP F CG  
8034  O OD1 . ASP F 98  ? 1.3817 1.6947 1.5501 0.1079  0.2890  -0.1634 104 ASP F OD1 
8035  O OD2 . ASP F 98  ? 1.2896 1.7472 1.5950 0.0657  0.2629  -0.1042 104 ASP F OD2 
8036  N N   . TYR F 99  ? 1.0818 1.2257 1.2399 -0.0650 0.1683  -0.2523 105 TYR F N   
8037  C CA  . TYR F 99  ? 1.0576 1.1817 1.2397 -0.1012 0.1450  -0.2553 105 TYR F CA  
8038  C C   . TYR F 99  ? 1.1726 1.2483 1.3544 -0.0826 0.1555  -0.2495 105 TYR F C   
8039  O O   . TYR F 99  ? 1.1219 1.2235 1.3517 -0.0942 0.1481  -0.2299 105 TYR F O   
8040  C CB  . TYR F 99  ? 1.0910 1.1727 1.2364 -0.1399 0.1198  -0.2831 105 TYR F CB  
8041  C CG  . TYR F 99  ? 1.0755 1.1355 1.2431 -0.1744 0.0994  -0.2824 105 TYR F CG  
8042  C CD1 . TYR F 99  ? 1.0124 1.1298 1.2408 -0.1890 0.0926  -0.2595 105 TYR F CD1 
8043  C CD2 . TYR F 99  ? 1.1552 1.1352 1.2792 -0.1932 0.0860  -0.3031 105 TYR F CD2 
8044  C CE1 . TYR F 99  ? 1.0038 1.1062 1.2507 -0.2153 0.0787  -0.2547 105 TYR F CE1 
8045  C CE2 . TYR F 99  ? 1.1480 1.1163 1.2987 -0.2255 0.0686  -0.2955 105 TYR F CE2 
8046  C CZ  . TYR F 99  ? 1.1384 1.1724 1.3515 -0.2342 0.0674  -0.2703 105 TYR F CZ  
8047  O OH  . TYR F 99  ? 1.1668 1.1946 1.4044 -0.2613 0.0546  -0.2591 105 TYR F OH  
8048  N N   . GLU F 100 ? 1.2368 1.2399 1.3594 -0.0502 0.1740  -0.2658 106 GLU F N   
8049  C CA  . GLU F 100 ? 1.3011 1.2410 1.4084 -0.0229 0.1890  -0.2627 106 GLU F CA  
8050  C C   . GLU F 100 ? 1.2828 1.2933 1.4535 0.0078  0.2079  -0.2220 106 GLU F C   
8051  O O   . GLU F 100 ? 1.2702 1.2682 1.4669 0.0105  0.2076  -0.2060 106 GLU F O   
8052  C CB  . GLU F 100 ? 1.4528 1.3000 1.4718 0.0148  0.2093  -0.2898 106 GLU F CB  
8053  C CG  . GLU F 100 ? 1.7090 1.5253 1.6615 0.0003  0.1984  -0.3232 106 GLU F CG  
8054  C CD  . GLU F 100 ? 2.0859 1.9762 2.0409 0.0248  0.2165  -0.3133 106 GLU F CD  
8055  O OE1 . GLU F 100 ? 2.0945 1.9838 2.0260 0.0803  0.2521  -0.3040 106 GLU F OE1 
8056  O OE2 . GLU F 100 ? 1.9901 1.9395 1.9700 -0.0097 0.1966  -0.3124 106 GLU F OE2 
8057  N N   . GLU F 101 ? 1.1980 1.2870 1.3960 0.0278  0.2219  -0.2017 107 GLU F N   
8058  C CA  . GLU F 101 ? 1.1441 1.3141 1.4082 0.0513  0.2349  -0.1576 107 GLU F CA  
8059  C C   . GLU F 101 ? 1.0814 1.3102 1.4074 0.0089  0.2059  -0.1399 107 GLU F C   
8060  O O   . GLU F 101 ? 1.0560 1.3240 1.4292 0.0169  0.2060  -0.1080 107 GLU F O   
8061  C CB  . GLU F 101 ? 1.1615 1.3975 1.4356 0.0822  0.2574  -0.1380 107 GLU F CB  
8062  C CG  . GLU F 101 ? 1.4459 1.6446 1.6735 0.1450  0.2980  -0.1367 107 GLU F CG  
8063  C CD  . GLU F 101 ? 1.8462 1.9755 1.9823 0.1615  0.3110  -0.1761 107 GLU F CD  
8064  O OE1 . GLU F 101 ? 1.9957 2.0296 2.0618 0.1961  0.3301  -0.1987 107 GLU F OE1 
8065  O OE2 . GLU F 101 ? 1.6766 1.8427 1.8062 0.1416  0.3018  -0.1838 107 GLU F OE2 
8066  N N   . LEU F 102 ? 0.9863 1.2182 1.3079 -0.0341 0.1810  -0.1597 108 LEU F N   
8067  C CA  . LEU F 102 ? 0.9152 1.1898 1.2812 -0.0714 0.1548  -0.1480 108 LEU F CA  
8068  C C   . LEU F 102 ? 0.9831 1.2155 1.3490 -0.0864 0.1442  -0.1508 108 LEU F C   
8069  O O   . LEU F 102 ? 0.9351 1.2020 1.3381 -0.0953 0.1334  -0.1284 108 LEU F O   
8070  C CB  . LEU F 102 ? 0.8777 1.1712 1.2387 -0.1041 0.1369  -0.1642 108 LEU F CB  
8071  C CG  . LEU F 102 ? 0.8679 1.1985 1.2641 -0.1370 0.1128  -0.1545 108 LEU F CG  
8072  C CD1 . LEU F 102 ? 0.8388 1.2272 1.2805 -0.1319 0.1084  -0.1212 108 LEU F CD1 
8073  C CD2 . LEU F 102 ? 0.8538 1.2004 1.2432 -0.1595 0.1009  -0.1678 108 LEU F CD2 
8074  N N   . ARG F 103 ? 0.9984 1.1545 1.3200 -0.0908 0.1453  -0.1766 109 ARG F N   
8075  C CA  . ARG F 103 ? 1.0118 1.1218 1.3311 -0.1054 0.1370  -0.1771 109 ARG F CA  
8076  C C   . ARG F 103 ? 1.0936 1.2130 1.4393 -0.0779 0.1487  -0.1479 109 ARG F C   
8077  O O   . ARG F 103 ? 1.0617 1.1963 1.4332 -0.0927 0.1373  -0.1315 109 ARG F O   
8078  C CB  . ARG F 103 ? 1.0728 1.0927 1.3375 -0.1110 0.1368  -0.2057 109 ARG F CB  
8079  C CG  . ARG F 103 ? 1.1997 1.2155 1.4475 -0.1497 0.1164  -0.2280 109 ARG F CG  
8080  C CD  . ARG F 103 ? 1.4923 1.4168 1.6845 -0.1627 0.1087  -0.2545 109 ARG F CD  
8081  N NE  . ARG F 103 ? 1.6702 1.5526 1.8710 -0.1843 0.0978  -0.2468 109 ARG F NE  
8082  C CZ  . ARG F 103 ? 1.9596 1.7686 2.1372 -0.1665 0.1069  -0.2459 109 ARG F CZ  
8083  N NH1 . ARG F 103 ? 1.9317 1.6984 2.0723 -0.1226 0.1293  -0.2541 109 ARG F NH1 
8084  N NH2 . ARG F 103 ? 1.7601 1.5374 1.9510 -0.1900 0.0956  -0.2341 109 ARG F NH2 
8085  N N   . GLU F 104 ? 1.1104 1.2293 1.4510 -0.0353 0.1725  -0.1377 110 GLU F N   
8086  C CA  . GLU F 104 ? 1.1240 1.2651 1.4958 -0.0017 0.1870  -0.1032 110 GLU F CA  
8087  C C   . GLU F 104 ? 1.0804 1.3125 1.5116 -0.0187 0.1693  -0.0707 110 GLU F C   
8088  O O   . GLU F 104 ? 1.0714 1.3110 1.5247 -0.0237 0.1602  -0.0501 110 GLU F O   
8089  C CB  . GLU F 104 ? 1.1977 1.3371 1.5543 0.0504  0.2192  -0.0963 110 GLU F CB  
8090  C CG  . GLU F 104 ? 1.3749 1.5548 1.7724 0.0926  0.2385  -0.0526 110 GLU F CG  
8091  C CD  . GLU F 104 ? 1.7000 1.9466 2.1208 0.1339  0.2640  -0.0255 110 GLU F CD  
8092  O OE1 . GLU F 104 ? 1.8108 2.0455 2.1948 0.1452  0.2776  -0.0468 110 GLU F OE1 
8093  O OE2 . GLU F 104 ? 1.5232 1.8379 2.0002 0.1558  0.2706  0.0210  110 GLU F OE2 
8094  N N   . GLN F 105 ? 0.9622 1.2559 1.4131 -0.0303 0.1616  -0.0671 111 GLN F N   
8095  C CA  . GLN F 105 ? 0.8886 1.2575 1.3866 -0.0496 0.1405  -0.0391 111 GLN F CA  
8096  C C   . GLN F 105 ? 0.9223 1.2807 1.4184 -0.0847 0.1150  -0.0451 111 GLN F C   
8097  O O   . GLN F 105 ? 0.8952 1.2898 1.4180 -0.0921 0.0994  -0.0191 111 GLN F O   
8098  C CB  . GLN F 105 ? 0.8603 1.2789 1.3710 -0.0614 0.1345  -0.0393 111 GLN F CB  
8099  C CG  . GLN F 105 ? 1.0155 1.4474 1.5202 -0.0272 0.1621  -0.0357 111 GLN F CG  
8100  C CD  . GLN F 105 ? 1.2403 1.7246 1.7854 0.0107  0.1809  0.0077  111 GLN F CD  
8101  O OE1 . GLN F 105 ? 1.1649 1.7241 1.7637 0.0009  0.1665  0.0455  111 GLN F OE1 
8102  N NE2 . GLN F 105 ? 1.1634 1.6094 1.6819 0.0558  0.2136  0.0050  111 GLN F NE2 
8103  N N   . LEU F 106 ? 0.8965 1.2073 1.3592 -0.1055 0.1108  -0.0767 112 LEU F N   
8104  C CA  . LEU F 106 ? 0.8824 1.1858 1.3400 -0.1345 0.0921  -0.0816 112 LEU F CA  
8105  C C   . LEU F 106 ? 1.0165 1.2782 1.4651 -0.1327 0.0952  -0.0762 112 LEU F C   
8106  O O   . LEU F 106 ? 1.0034 1.2618 1.4457 -0.1539 0.0832  -0.0776 112 LEU F O   
8107  C CB  . LEU F 106 ? 0.8614 1.1520 1.2983 -0.1582 0.0858  -0.1096 112 LEU F CB  
8108  C CG  . LEU F 106 ? 0.8772 1.2125 1.3255 -0.1706 0.0735  -0.1092 112 LEU F CG  
8109  C CD1 . LEU F 106 ? 0.8789 1.2051 1.3102 -0.1783 0.0770  -0.1327 112 LEU F CD1 
8110  C CD2 . LEU F 106 ? 0.8910 1.2375 1.3385 -0.1907 0.0549  -0.1051 112 LEU F CD2 
8111  N N   . SER F 107 ? 1.0451 1.2756 1.4922 -0.1048 0.1124  -0.0669 113 SER F N   
8112  C CA  . SER F 107 ? 1.0901 1.2743 1.5293 -0.1015 0.1162  -0.0584 113 SER F CA  
8113  C C   . SER F 107 ? 1.1125 1.3270 1.5666 -0.1165 0.1003  -0.0362 113 SER F C   
8114  O O   . SER F 107 ? 1.1092 1.3041 1.5500 -0.1387 0.0936  -0.0431 113 SER F O   
8115  C CB  . SER F 107 ? 1.1990 1.3539 1.6390 -0.0621 0.1374  -0.0441 113 SER F CB  
8116  O OG  . SER F 107 ? 1.3582 1.4694 1.7940 -0.0592 0.1395  -0.0311 113 SER F OG  
8117  N N   . SER F 108 ? 1.0399 1.3052 1.5199 -0.1050 0.0934  -0.0075 114 SER F N   
8118  C CA  . SER F 108 ? 1.0180 1.3116 1.5027 -0.1179 0.0750  0.0137  114 SER F CA  
8119  C C   . SER F 108 ? 1.0208 1.3702 1.5163 -0.1312 0.0538  0.0193  114 SER F C   
8120  O O   . SER F 108 ? 0.9993 1.3795 1.5171 -0.1214 0.0563  0.0248  114 SER F O   
8121  C CB  . SER F 108 ? 1.0952 1.3912 1.5976 -0.0946 0.0804  0.0481  114 SER F CB  
8122  O OG  . SER F 108 ? 1.2174 1.5262 1.7123 -0.1079 0.0641  0.0658  114 SER F OG  
8123  N N   . VAL F 109 ? 0.9692 1.3277 1.4450 -0.1532 0.0331  0.0185  115 VAL F N   
8124  C CA  . VAL F 109 ? 0.9466 1.3405 1.4205 -0.1706 0.0076  0.0206  115 VAL F CA  
8125  C C   . VAL F 109 ? 1.0158 1.4184 1.4672 -0.1821 -0.0172 0.0375  115 VAL F C   
8126  O O   . VAL F 109 ? 1.0239 1.4006 1.4464 -0.1829 -0.0129 0.0346  115 VAL F O   
8127  C CB  . VAL F 109 ? 0.9717 1.3523 1.4265 -0.1864 0.0073  -0.0119 115 VAL F CB  
8128  C CG1 . VAL F 109 ? 0.9738 1.3528 1.3954 -0.2065 -0.0165 -0.0193 115 VAL F CG1 
8129  C CG2 . VAL F 109 ? 0.9466 1.3507 1.4285 -0.1816 0.0126  -0.0145 115 VAL F CG2 
8130  N N   . SER F 110 ? 0.9750 1.4157 1.4390 -0.1922 -0.0447 0.0577  116 SER F N   
8131  C CA  . SER F 110 ? 1.0033 1.4527 1.4403 -0.2074 -0.0770 0.0740  116 SER F CA  
8132  C C   . SER F 110 ? 1.0926 1.5149 1.4780 -0.2306 -0.0986 0.0473  116 SER F C   
8133  O O   . SER F 110 ? 1.1331 1.5292 1.4652 -0.2363 -0.1108 0.0419  116 SER F O   
8134  C CB  . SER F 110 ? 1.0327 1.5379 1.5135 -0.2095 -0.0995 0.1140  116 SER F CB  
8135  O OG  . SER F 110 ? 1.1001 1.6270 1.6241 -0.1811 -0.0764 0.1411  116 SER F OG  
8136  N N   . SER F 111 A 1.0345 1.4598 1.4318 -0.2409 -0.1016 0.0318  116 SER F N   
8137  C CA  . SER F 111 A 1.0473 1.4401 1.3992 -0.2592 -0.1184 0.0055  116 SER F CA  
8138  C C   . SER F 111 A 1.0589 1.4482 1.4305 -0.2558 -0.0967 -0.0165 116 SER F C   
8139  O O   . SER F 111 A 1.0178 1.4407 1.4399 -0.2490 -0.0850 -0.0052 116 SER F O   
8140  C CB  . SER F 111 A 1.1156 1.5196 1.4608 -0.2852 -0.1627 0.0211  116 SER F CB  
8141  O OG  . SER F 111 A 1.2344 1.5900 1.5234 -0.3007 -0.1799 -0.0059 116 SER F OG  
8142  N N   . PHE F 112 B 1.0266 1.3776 1.3566 -0.2572 -0.0895 -0.0455 116 PHE F N   
8143  C CA  . PHE F 112 B 0.9943 1.3423 1.3383 -0.2544 -0.0705 -0.0653 116 PHE F CA  
8144  C C   . PHE F 112 B 1.0832 1.3954 1.3823 -0.2621 -0.0796 -0.0873 116 PHE F C   
8145  O O   . PHE F 112 B 1.0892 1.3780 1.3592 -0.2518 -0.0618 -0.1038 116 PHE F O   
8146  C CB  . PHE F 112 B 0.9903 1.3361 1.3481 -0.2384 -0.0372 -0.0734 116 PHE F CB  
8147  C CG  . PHE F 112 B 0.9722 1.3246 1.3533 -0.2362 -0.0199 -0.0877 116 PHE F CG  
8148  C CD1 . PHE F 112 B 0.9873 1.3654 1.4072 -0.2304 -0.0128 -0.0789 116 PHE F CD1 
8149  C CD2 . PHE F 112 B 0.9910 1.3265 1.3534 -0.2371 -0.0091 -0.1075 116 PHE F CD2 
8150  C CE1 . PHE F 112 B 0.9760 1.3566 1.4071 -0.2275 0.0025  -0.0932 116 PHE F CE1 
8151  C CE2 . PHE F 112 B 1.0003 1.3440 1.3819 -0.2369 0.0037  -0.1189 116 PHE F CE2 
8152  C CZ  . PHE F 112 B 0.9599 1.3228 1.3716 -0.2329 0.0086  -0.1135 116 PHE F CZ  
8153  N N   . GLU F 113 C 1.0630 1.3721 1.3597 -0.2795 -0.1067 -0.0841 116 GLU F N   
8154  C CA  . GLU F 113 C 1.1003 1.3655 1.3515 -0.2864 -0.1187 -0.1033 116 GLU F CA  
8155  C C   . GLU F 113 C 1.1075 1.3839 1.3870 -0.2833 -0.1013 -0.1133 116 GLU F C   
8156  O O   . GLU F 113 C 1.0630 1.3753 1.3901 -0.2916 -0.1043 -0.1001 116 GLU F O   
8157  C CB  . GLU F 113 C 1.1719 1.4180 1.4020 -0.3120 -0.1627 -0.0932 116 GLU F CB  
8158  C CG  . GLU F 113 C 1.4331 1.6138 1.6015 -0.3186 -0.1792 -0.1147 116 GLU F CG  
8159  C CD  . GLU F 113 C 1.8303 1.9895 1.9917 -0.3509 -0.2238 -0.1047 116 GLU F CD  
8160  O OE1 . GLU F 113 C 1.7608 1.9638 1.9667 -0.3723 -0.2479 -0.0758 116 GLU F OE1 
8161  O OE2 . GLU F 113 C 1.8090 1.9070 1.9217 -0.3547 -0.2351 -0.1230 116 GLU F OE2 
8162  N N   . ARG F 114 ? 1.0783 1.3295 1.3294 -0.2696 -0.0820 -0.1328 117 ARG F N   
8163  C CA  . ARG F 114 ? 1.0492 1.3083 1.3196 -0.2665 -0.0681 -0.1416 117 ARG F CA  
8164  C C   . ARG F 114 ? 1.1310 1.3442 1.3615 -0.2744 -0.0901 -0.1491 117 ARG F C   
8165  O O   . ARG F 114 ? 1.1784 1.3413 1.3480 -0.2671 -0.0966 -0.1603 117 ARG F O   
8166  C CB  . ARG F 114 ? 1.0471 1.3103 1.3141 -0.2483 -0.0374 -0.1522 117 ARG F CB  
8167  C CG  . ARG F 114 ? 1.2227 1.4943 1.5036 -0.2444 -0.0254 -0.1595 117 ARG F CG  
8168  C CD  . ARG F 114 ? 1.5423 1.8268 1.8259 -0.2306 0.0004  -0.1628 117 ARG F CD  
8169  N NE  . ARG F 114 ? 1.8345 2.1178 2.1134 -0.2214 0.0097  -0.1673 117 ARG F NE  
8170  C CZ  . ARG F 114 ? 2.1173 2.3694 2.3546 -0.2042 0.0148  -0.1712 117 ARG F CZ  
8171  N NH1 . ARG F 114 ? 1.9660 2.1802 2.1543 -0.1959 0.0096  -0.1744 117 ARG F NH1 
8172  N NH2 . ARG F 114 ? 2.0080 2.2651 2.2481 -0.1925 0.0258  -0.1709 117 ARG F NH2 
8173  N N   . PHE F 115 ? 1.0640 1.2898 1.3240 -0.2887 -0.1021 -0.1415 118 PHE F N   
8174  C CA  . PHE F 115 ? 1.1116 1.2874 1.3371 -0.3002 -0.1264 -0.1458 118 PHE F CA  
8175  C C   . PHE F 115 ? 1.1313 1.3211 1.3857 -0.3000 -0.1176 -0.1441 118 PHE F C   
8176  O O   . PHE F 115 ? 1.0694 1.3162 1.3781 -0.3009 -0.1039 -0.1330 118 PHE F O   
8177  C CB  . PHE F 115 ? 1.1673 1.3337 1.3922 -0.3298 -0.1675 -0.1290 118 PHE F CB  
8178  C CG  . PHE F 115 ? 1.1304 1.3635 1.4290 -0.3475 -0.1747 -0.1002 118 PHE F CG  
8179  C CD1 . PHE F 115 ? 1.1234 1.4147 1.4659 -0.3421 -0.1628 -0.0842 118 PHE F CD1 
8180  C CD2 . PHE F 115 ? 1.1577 1.3942 1.4802 -0.3674 -0.1927 -0.0855 118 PHE F CD2 
8181  C CE1 . PHE F 115 ? 1.0951 1.4502 1.5028 -0.3510 -0.1644 -0.0545 118 PHE F CE1 
8182  C CE2 . PHE F 115 ? 1.1531 1.4594 1.5451 -0.3800 -0.1955 -0.0535 118 PHE F CE2 
8183  C CZ  . PHE F 115 ? 1.0866 1.4528 1.5196 -0.3695 -0.1799 -0.0383 118 PHE F CZ  
8184  N N   . GLU F 116 ? 1.1335 1.2670 1.3465 -0.2969 -0.1255 -0.1545 119 GLU F N   
8185  C CA  . GLU F 116 ? 1.1109 1.2522 1.3476 -0.2968 -0.1201 -0.1497 119 GLU F CA  
8186  C C   . GLU F 116 ? 1.1789 1.3402 1.4543 -0.3279 -0.1482 -0.1261 119 GLU F C   
8187  O O   . GLU F 116 ? 1.2469 1.3551 1.4934 -0.3484 -0.1815 -0.1222 119 GLU F O   
8188  C CB  . GLU F 116 ? 1.1864 1.2554 1.3646 -0.2800 -0.1191 -0.1650 119 GLU F CB  
8189  C CG  . GLU F 116 ? 1.1860 1.2815 1.3811 -0.2540 -0.0860 -0.1678 119 GLU F CG  
8190  C CD  . GLU F 116 ? 1.2604 1.2924 1.4018 -0.2276 -0.0771 -0.1789 119 GLU F CD  
8191  O OE1 . GLU F 116 ? 1.0771 1.0412 1.1504 -0.2154 -0.0828 -0.1934 119 GLU F OE1 
8192  O OE2 . GLU F 116 ? 1.0770 1.1285 1.2414 -0.2152 -0.0619 -0.1720 119 GLU F OE2 
8193  N N   . ILE F 117 ? 1.0631 1.3002 1.4013 -0.3313 -0.1356 -0.1086 120 ILE F N   
8194  C CA  . ILE F 117 ? 1.0434 1.3216 1.4309 -0.3553 -0.1540 -0.0783 120 ILE F CA  
8195  C C   . ILE F 117 ? 1.1122 1.3710 1.5038 -0.3658 -0.1645 -0.0687 120 ILE F C   
8196  O O   . ILE F 117 ? 1.1632 1.4024 1.5600 -0.3942 -0.1977 -0.0490 120 ILE F O   
8197  C CB  . ILE F 117 ? 1.0159 1.3755 1.4593 -0.3459 -0.1300 -0.0635 120 ILE F CB  
8198  C CG1 . ILE F 117 ? 1.0112 1.4238 1.5094 -0.3661 -0.1452 -0.0249 120 ILE F CG1 
8199  C CG2 . ILE F 117 ? 0.9812 1.3647 1.4308 -0.3223 -0.0952 -0.0781 120 ILE F CG2 
8200  C CD1 . ILE F 117 ? 1.0423 1.5262 1.5861 -0.3531 -0.1244 -0.0068 120 ILE F CD1 
8201  N N   . PHE F 118 ? 1.0147 1.2774 1.4035 -0.3446 -0.1385 -0.0804 121 PHE F N   
8202  C CA  . PHE F 118 ? 1.0149 1.2594 1.4054 -0.3474 -0.1424 -0.0720 121 PHE F CA  
8203  C C   . PHE F 118 ? 1.0761 1.2714 1.4196 -0.3205 -0.1255 -0.0977 121 PHE F C   
8204  O O   . PHE F 118 ? 1.0300 1.2646 1.3885 -0.3002 -0.0975 -0.1031 121 PHE F O   
8205  C CB  . PHE F 118 ? 0.9757 1.2969 1.4208 -0.3449 -0.1238 -0.0515 121 PHE F CB  
8206  C CG  . PHE F 118 ? 0.9589 1.3453 1.4552 -0.3602 -0.1285 -0.0224 121 PHE F CG  
8207  C CD1 . PHE F 118 ? 1.0246 1.4132 1.5465 -0.3897 -0.1580 0.0096  121 PHE F CD1 
8208  C CD2 . PHE F 118 ? 0.9307 1.3771 1.4508 -0.3437 -0.1023 -0.0234 121 PHE F CD2 
8209  C CE1 . PHE F 118 ? 1.0079 1.4702 1.5854 -0.4001 -0.1586 0.0444  121 PHE F CE1 
8210  C CE2 . PHE F 118 ? 0.9455 1.4544 1.5117 -0.3495 -0.1007 0.0067  121 PHE F CE2 
8211  C CZ  . PHE F 118 ? 0.9448 1.4680 1.5434 -0.3764 -0.1273 0.0427  121 PHE F CZ  
8212  N N   . PRO F 119 ? 1.0998 1.2092 1.3830 -0.3188 -0.1423 -0.1125 122 PRO F N   
8213  C CA  . PRO F 119 ? 1.1304 1.1957 1.3672 -0.2857 -0.1213 -0.1331 122 PRO F CA  
8214  C C   . PRO F 119 ? 1.1532 1.2318 1.4076 -0.2692 -0.1041 -0.1248 122 PRO F C   
8215  O O   . PRO F 119 ? 1.1730 1.2361 1.4399 -0.2838 -0.1201 -0.1083 122 PRO F O   
8216  C CB  . PRO F 119 ? 1.2566 1.2172 1.4182 -0.2882 -0.1467 -0.1477 122 PRO F CB  
8217  C CG  . PRO F 119 ? 1.3317 1.2780 1.5086 -0.3297 -0.1870 -0.1297 122 PRO F CG  
8218  C CD  . PRO F 119 ? 1.1856 1.2324 1.4349 -0.3454 -0.1816 -0.1105 122 PRO F CD  
8219  N N   . LYS F 120 ? 1.0582 1.1683 1.3158 -0.2401 -0.0728 -0.1326 123 LYS F N   
8220  C CA  . LYS F 120 ? 1.0370 1.1737 1.3141 -0.2205 -0.0535 -0.1229 123 LYS F CA  
8221  C C   . LYS F 120 ? 1.1614 1.2254 1.4060 -0.2111 -0.0633 -0.1176 123 LYS F C   
8222  O O   . LYS F 120 ? 1.1549 1.2420 1.4300 -0.2136 -0.0631 -0.0988 123 LYS F O   
8223  C CB  . LYS F 120 ? 1.0467 1.2139 1.3212 -0.1916 -0.0239 -0.1308 123 LYS F CB  
8224  C CG  . LYS F 120 ? 1.0163 1.2541 1.3352 -0.1825 -0.0059 -0.1161 123 LYS F CG  
8225  C CD  . LYS F 120 ? 1.0025 1.2682 1.3205 -0.1579 0.0187  -0.1185 123 LYS F CD  
8226  C CE  . LYS F 120 ? 1.0319 1.3414 1.3770 -0.1396 0.0339  -0.0997 123 LYS F CE  
8227  N NZ  . LYS F 120 ? 1.1060 1.4282 1.4437 -0.1093 0.0578  -0.0956 123 LYS F NZ  
8228  N N   . THR F 121 ? 1.1997 1.1707 1.3778 -0.2010 -0.0733 -0.1337 124 THR F N   
8229  C CA  . THR F 121 ? 1.3010 1.1772 1.4301 -0.1891 -0.0841 -0.1339 124 THR F CA  
8230  C C   . THR F 121 ? 1.3575 1.2177 1.5116 -0.2250 -0.1153 -0.1138 124 THR F C   
8231  O O   . THR F 121 ? 1.3257 1.2090 1.5118 -0.2193 -0.1080 -0.0939 124 THR F O   
8232  C CB  . THR F 121 ? 1.6396 1.4097 1.6789 -0.1750 -0.0932 -0.1598 124 THR F CB  
8233  O OG1 . THR F 121 ? 1.7317 1.4917 1.7633 -0.2128 -0.1244 -0.1665 124 THR F OG1 
8234  C CG2 . THR F 121 ? 1.6320 1.4121 1.6420 -0.1303 -0.0566 -0.1731 124 THR F CG2 
8235  N N   . SER F 122 ? 1.3575 1.1863 1.5018 -0.2632 -0.1506 -0.1143 125 SER F N   
8236  C CA  . SER F 122 ? 1.3914 1.2036 1.5604 -0.3034 -0.1854 -0.0901 125 SER F CA  
8237  C C   . SER F 122 ? 1.3618 1.2894 1.6194 -0.3258 -0.1811 -0.0594 125 SER F C   
8238  O O   . SER F 122 ? 1.3452 1.2975 1.6354 -0.3238 -0.1746 -0.0373 125 SER F O   
8239  C CB  . SER F 122 ? 1.5229 1.2629 1.6491 -0.3378 -0.2279 -0.0979 125 SER F CB  
8240  O OG  . SER F 122 ? 1.6122 1.4126 1.7573 -0.3474 -0.2263 -0.1041 125 SER F OG  
8241  N N   . SER F 123 ? 1.2727 1.2671 1.5646 -0.3441 -0.1838 -0.0567 126 SER F N   
8242  C CA  . SER F 123 ? 1.1937 1.2928 1.5593 -0.3620 -0.1786 -0.0298 126 SER F CA  
8243  C C   . SER F 123 ? 1.1815 1.3431 1.5922 -0.3531 -0.1588 -0.0071 126 SER F C   
8244  O O   . SER F 123 ? 1.1691 1.3791 1.6271 -0.3760 -0.1686 0.0253  126 SER F O   
8245  C CB  . SER F 123 ? 1.1924 1.3539 1.5728 -0.3518 -0.1587 -0.0439 126 SER F CB  
8246  O OG  . SER F 123 ? 1.3931 1.5189 1.7488 -0.3691 -0.1825 -0.0521 126 SER F OG  
8247  N N   . TRP F 124 ? 1.0925 1.2618 1.4917 -0.3206 -0.1313 -0.0198 127 TRP F N   
8248  C CA  . TRP F 124 ? 1.0448 1.2759 1.4813 -0.3116 -0.1141 0.0011  127 TRP F CA  
8249  C C   . TRP F 124 ? 1.1391 1.3134 1.5534 -0.2954 -0.1143 0.0077  127 TRP F C   
8250  O O   . TRP F 124 ? 1.1403 1.3098 1.5356 -0.2639 -0.0931 -0.0062 127 TRP F O   
8251  C CB  . TRP F 124 ? 0.9620 1.2676 1.4133 -0.2919 -0.0846 -0.0124 127 TRP F CB  
8252  C CG  . TRP F 124 ? 0.9453 1.2770 1.4008 -0.2996 -0.0829 -0.0270 127 TRP F CG  
8253  C CD1 . TRP F 124 ? 0.9809 1.2914 1.4088 -0.2880 -0.0757 -0.0542 127 TRP F CD1 
8254  C CD2 . TRP F 124 ? 0.9186 1.2977 1.4078 -0.3195 -0.0893 -0.0103 127 TRP F CD2 
8255  N NE1 . TRP F 124 ? 0.9465 1.2866 1.3887 -0.2999 -0.0778 -0.0568 127 TRP F NE1 
8256  C CE2 . TRP F 124 ? 0.9522 1.3351 1.4322 -0.3175 -0.0854 -0.0300 127 TRP F CE2 
8257  C CE3 . TRP F 124 ? 0.9304 1.3555 1.4596 -0.3359 -0.0953 0.0237  127 TRP F CE3 
8258  C CZ2 . TRP F 124 ? 0.9226 1.3513 1.4316 -0.3287 -0.0866 -0.0176 127 TRP F CZ2 
8259  C CZ3 . TRP F 124 ? 0.9262 1.4022 1.4853 -0.3460 -0.0946 0.0373  127 TRP F CZ3 
8260  C CH2 . TRP F 124 ? 0.9198 1.3957 1.4686 -0.3414 -0.0903 0.0164  127 TRP F CH2 
8261  N N   . PRO F 125 ? 1.1365 1.2658 1.5543 -0.3164 -0.1386 0.0322  128 PRO F N   
8262  C CA  . PRO F 125 ? 1.1991 1.2584 1.5898 -0.2986 -0.1396 0.0386  128 PRO F CA  
8263  C C   . PRO F 125 ? 1.2137 1.3305 1.6444 -0.2898 -0.1261 0.0702  128 PRO F C   
8264  O O   . PRO F 125 ? 1.2462 1.3286 1.6583 -0.2613 -0.1148 0.0723  128 PRO F O   
8265  C CB  . PRO F 125 ? 1.3109 1.2725 1.6745 -0.3297 -0.1785 0.0459  128 PRO F CB  
8266  C CG  . PRO F 125 ? 1.3266 1.3500 1.7366 -0.3706 -0.1973 0.0648  128 PRO F CG  
8267  C CD  . PRO F 125 ? 1.1684 1.3019 1.6142 -0.3577 -0.1681 0.0576  128 PRO F CD  
8268  N N   . ASN F 126 ? 1.2117 1.1508 2.1517 0.0540  0.1100  0.0947  129 ASN F N   
8269  C CA  . ASN F 126 ? 1.2138 1.1653 2.1617 0.0761  0.1505  0.1469  129 ASN F CA  
8270  C C   . ASN F 126 ? 1.2701 1.2487 2.0851 0.0768  0.1816  0.1532  129 ASN F C   
8271  O O   . ASN F 126 ? 1.2703 1.2552 2.0680 0.0953  0.2181  0.2012  129 ASN F O   
8272  C CB  . ASN F 126 ? 1.2200 1.1468 2.2860 0.0878  0.1728  0.2136  129 ASN F CB  
8273  C CG  . ASN F 126 ? 1.5013 1.4039 2.7248 0.0929  0.1396  0.2120  129 ASN F CG  
8274  O OD1 . ASN F 126 ? 1.4180 1.3289 2.6785 0.1017  0.1173  0.1839  129 ASN F OD1 
8275  N ND2 . ASN F 126 ? 1.4054 1.2760 2.7378 0.0881  0.1341  0.2426  129 ASN F ND2 
8276  N N   . HIS F 127 ? 1.2377 1.2337 1.9613 0.0597  0.1652  0.1039  130 HIS F N   
8277  C CA  . HIS F 127 ? 1.2323 1.2544 1.8446 0.0575  0.1838  0.0992  130 HIS F CA  
8278  C C   . HIS F 127 ? 1.2609 1.3098 1.8079 0.0512  0.1635  0.0478  130 HIS F C   
8279  O O   . HIS F 127 ? 1.2460 1.2928 1.8121 0.0443  0.1366  0.0099  130 HIS F O   
8280  C CB  . HIS F 127 ? 1.2315 1.2473 1.8202 0.0408  0.1967  0.1120  130 HIS F CB  
8281  C CG  . HIS F 127 ? 1.2830 1.2716 1.9387 0.0491  0.2233  0.1663  130 HIS F CG  
8282  N ND1 . HIS F 127 ? 1.2966 1.2557 2.0509 0.0379  0.2089  0.1775  130 HIS F ND1 
8283  C CD2 . HIS F 127 ? 1.3254 1.3123 1.9668 0.0718  0.2629  0.2134  130 HIS F CD2 
8284  C CE1 . HIS F 127 ? 1.3007 1.2417 2.1069 0.0523  0.2446  0.2352  130 HIS F CE1 
8285  N NE2 . HIS F 127 ? 1.3253 1.2833 2.0597 0.0746  0.2806  0.2589  130 HIS F NE2 
8286  N N   . ASP F 128 ? 1.2172 1.2902 1.6898 0.0571  0.1765  0.0475  131 ASP F N   
8287  C CA  . ASP F 128 ? 1.2134 1.3139 1.6340 0.0539  0.1641  0.0098  131 ASP F CA  
8288  C C   . ASP F 128 ? 1.2371 1.3534 1.6140 0.0348  0.1625  -0.0053 131 ASP F C   
8289  O O   . ASP F 128 ? 1.2236 1.3451 1.5703 0.0317  0.1766  0.0115  131 ASP F O   
8290  C CB  . ASP F 128 ? 1.2567 1.3729 1.6397 0.0711  0.1728  0.0209  131 ASP F CB  
8291  C CG  . ASP F 128 ? 1.4119 1.5538 1.7649 0.0714  0.1610  -0.0107 131 ASP F CG  
8292  O OD1 . ASP F 128 ? 1.4069 1.5656 1.7353 0.0582  0.1558  -0.0343 131 ASP F OD1 
8293  O OD2 . ASP F 128 ? 1.4963 1.6435 1.8548 0.0859  0.1590  -0.0060 131 ASP F OD2 
8294  N N   . SER F 129 ? 1.1839 1.3090 1.5599 0.0243  0.1452  -0.0365 132 SER F N   
8295  C CA  . SER F 129 ? 1.1576 1.3042 1.5022 0.0070  0.1425  -0.0471 132 SER F CA  
8296  C C   . SER F 129 ? 1.1998 1.3841 1.5042 0.0115  0.1440  -0.0660 132 SER F C   
8297  O O   . SER F 129 ? 1.1860 1.3965 1.4720 0.0011  0.1488  -0.0625 132 SER F O   
8298  C CB  . SER F 129 ? 1.1969 1.3311 1.5624 -0.0038 0.1216  -0.0639 132 SER F CB  
8299  O OG  . SER F 129 ? 1.2919 1.4089 1.6833 0.0092  0.1038  -0.0885 132 SER F OG  
8300  N N   . ASP F 130 ? 1.1562 1.3437 1.4612 0.0276  0.1411  -0.0824 133 ASP F N   
8301  C CA  . ASP F 130 ? 1.1459 1.3653 1.4291 0.0356  0.1449  -0.0973 133 ASP F CA  
8302  C C   . ASP F 130 ? 1.1640 1.3998 1.4391 0.0395  0.1514  -0.0817 133 ASP F C   
8303  O O   . ASP F 130 ? 1.1487 1.4153 1.4193 0.0408  0.1543  -0.0864 133 ASP F O   
8304  C CB  . ASP F 130 ? 1.1989 1.4118 1.4958 0.0519  0.1406  -0.1210 133 ASP F CB  
8305  C CG  . ASP F 130 ? 1.3775 1.5691 1.6868 0.0528  0.1257  -0.1456 133 ASP F CG  
8306  O OD1 . ASP F 130 ? 1.3880 1.5910 1.6681 0.0476  0.1199  -0.1603 133 ASP F OD1 
8307  O OD2 . ASP F 130 ? 1.5089 1.6735 1.8618 0.0602  0.1169  -0.1498 133 ASP F OD2 
8308  N N   . LYS F 131 A 1.1145 1.3307 1.3901 0.0445  0.1526  -0.0624 133 LYS F N   
8309  C CA  . LYS F 131 A 1.1036 1.3305 1.3632 0.0521  0.1503  -0.0537 133 LYS F CA  
8310  C C   . LYS F 131 A 1.1261 1.3616 1.3714 0.0414  0.1524  -0.0470 133 LYS F C   
8311  O O   . LYS F 131 A 1.1157 1.3604 1.3504 0.0483  0.1443  -0.0474 133 LYS F O   
8312  C CB  . LYS F 131 A 1.1484 1.3546 1.4034 0.0697  0.1486  -0.0376 133 LYS F CB  
8313  C CG  . LYS F 131 A 1.1189 1.3370 1.3806 0.0830  0.1368  -0.0430 133 LYS F CG  
8314  C CD  . LYS F 131 A 1.0713 1.3056 1.3165 0.0862  0.1226  -0.0464 133 LYS F CD  
8315  C CE  . LYS F 131 A 0.8970 1.1491 1.1738 0.0924  0.1105  -0.0556 133 LYS F CE  
8316  N NZ  . LYS F 131 A 0.7692 1.0434 1.0599 0.0896  0.0972  -0.0628 133 LYS F NZ  
8317  N N   . GLY F 132 ? 1.0701 1.3032 1.3224 0.0248  0.1593  -0.0436 134 GLY F N   
8318  C CA  . GLY F 132 ? 1.0544 1.2963 1.3071 0.0120  0.1634  -0.0368 134 GLY F CA  
8319  C C   . GLY F 132 ? 1.0848 1.3671 1.3569 0.0035  0.1579  -0.0450 134 GLY F C   
8320  O O   . GLY F 132 ? 1.0676 1.3661 1.3593 -0.0142 0.1621  -0.0396 134 GLY F O   
8321  N N   . VAL F 133 ? 1.0360 1.3363 1.3150 0.0164  0.1481  -0.0534 135 VAL F N   
8322  C CA  . VAL F 133 ? 1.0105 1.3516 1.3294 0.0131  0.1431  -0.0551 135 VAL F CA  
8323  C C   . VAL F 133 ? 1.0660 1.4094 1.3992 0.0246  0.1241  -0.0619 135 VAL F C   
8324  O O   . VAL F 133 ? 1.0915 1.4109 1.3960 0.0406  0.1131  -0.0670 135 VAL F O   
8325  C CB  . VAL F 133 ? 1.0596 1.4274 1.3959 0.0186  0.1500  -0.0560 135 VAL F CB  
8326  C CG1 . VAL F 133 ? 1.0538 1.4334 1.3806 0.0068  0.1626  -0.0519 135 VAL F CG1 
8327  C CG2 . VAL F 133 ? 1.0865 1.4336 1.4056 0.0355  0.1479  -0.0649 135 VAL F CG2 
8328  N N   . THR F 134 ? 0.9950 1.3683 1.3787 0.0175  0.1169  -0.0616 136 THR F N   
8329  C CA  . THR F 134 ? 1.0006 1.3757 1.4105 0.0286  0.0904  -0.0744 136 THR F CA  
8330  C C   . THR F 134 ? 1.0079 1.4275 1.5106 0.0275  0.0804  -0.0690 136 THR F C   
8331  O O   . THR F 134 ? 0.9650 1.4195 1.5073 0.0164  0.1003  -0.0507 136 THR F O   
8332  C CB  . THR F 134 ? 1.1581 1.5134 1.5426 0.0254  0.0875  -0.0838 136 THR F CB  
8333  O OG1 . THR F 134 ? 1.2370 1.5779 1.6110 0.0451  0.0568  -0.1049 136 THR F OG1 
8334  C CG2 . THR F 134 ? 1.0927 1.4771 1.5350 0.0038  0.0974  -0.0765 136 THR F CG2 
8335  N N   . ALA F 135 ? 0.9792 1.3981 1.5207 0.0416  0.0481  -0.0825 137 ALA F N   
8336  C CA  . ALA F 135 ? 0.9463 1.4045 1.5993 0.0440  0.0332  -0.0751 137 ALA F CA  
8337  C C   . ALA F 135 ? 0.9672 1.4539 1.6908 0.0305  0.0295  -0.0744 137 ALA F C   
8338  O O   . ALA F 135 ? 0.9286 1.4601 1.7607 0.0281  0.0299  -0.0552 137 ALA F O   
8339  C CB  . ALA F 135 ? 0.9877 1.4286 1.6660 0.0639  -0.0089 -0.0926 137 ALA F CB  
8340  N N   . ALA F 136 ? 0.9368 1.4001 1.6090 0.0228  0.0293  -0.0911 138 ALA F N   
8341  C CA  . ALA F 136 ? 0.9067 1.3932 1.6459 0.0082  0.0280  -0.0926 138 ALA F CA  
8342  C C   . ALA F 136 ? 0.9331 1.4623 1.7157 -0.0134 0.0629  -0.0560 138 ALA F C   
8343  O O   . ALA F 136 ? 0.8920 1.4587 1.7684 -0.0263 0.0631  -0.0445 138 ALA F O   
8344  C CB  . ALA F 136 ? 0.9505 1.3968 1.6119 0.0078  0.0286  -0.1160 138 ALA F CB  
8345  N N   . CYS F 137 ? 0.9202 1.4444 1.6367 -0.0156 0.0898  -0.0386 139 CYS F N   
8346  C CA  . CYS F 137 ? 0.9025 1.4631 1.6347 -0.0301 0.1193  -0.0066 139 CYS F CA  
8347  C C   . CYS F 137 ? 0.9704 1.5568 1.7149 -0.0149 0.1320  0.0119  139 CYS F C   
8348  O O   . CYS F 137 ? 1.0015 1.5680 1.6674 -0.0095 0.1466  0.0098  139 CYS F O   
8349  C CB  . CYS F 137 ? 0.9265 1.4547 1.5695 -0.0434 0.1364  -0.0074 139 CYS F CB  
8350  S SG  . CYS F 137 ? 0.9783 1.4786 1.6177 -0.0600 0.1330  -0.0198 139 CYS F SG  
8351  N N   . PRO F 138 ? 0.9016 1.5311 1.7516 -0.0051 0.1277  0.0301  140 PRO F N   
8352  C CA  . PRO F 138 ? 0.9047 1.5568 1.7662 0.0133  0.1471  0.0512  140 PRO F CA  
8353  C C   . PRO F 138 ? 0.9271 1.6287 1.7963 0.0121  0.1835  0.0891  140 PRO F C   
8354  O O   . PRO F 138 ? 0.8709 1.6010 1.7691 -0.0048 0.1897  0.1071  140 PRO F O   
8355  C CB  . PRO F 138 ? 0.9138 1.5857 1.8966 0.0272  0.1246  0.0569  140 PRO F CB  
8356  C CG  . PRO F 138 ? 0.9488 1.6271 2.0047 0.0138  0.0962  0.0450  140 PRO F CG  
8357  C CD  . PRO F 138 ? 0.8925 1.5516 1.8674 -0.0077 0.1055  0.0334  140 PRO F CD  
8358  N N   . HIS F 139 ? 0.9317 1.6432 1.7710 0.0325  0.2080  0.1013  141 HIS F N   
8359  C CA  . HIS F 139 ? 0.9501 1.7075 1.7763 0.0432  0.2455  0.1358  141 HIS F CA  
8360  C C   . HIS F 139 ? 1.0271 1.7920 1.8576 0.0734  0.2680  0.1452  141 HIS F C   
8361  O O   . HIS F 139 ? 1.0548 1.7756 1.8025 0.0813  0.2667  0.1145  141 HIS F O   
8362  C CB  . HIS F 139 ? 0.9927 1.7277 1.7000 0.0313  0.2510  0.1205  141 HIS F CB  
8363  C CG  . HIS F 139 ? 1.0820 1.8462 1.7312 0.0508  0.2829  0.1390  141 HIS F CG  
8364  N ND1 . HIS F 139 ? 1.1015 1.9349 1.8122 0.0665  0.3129  0.1892  141 HIS F ND1 
8365  C CD2 . HIS F 139 ? 1.1633 1.8961 1.6986 0.0594  0.2873  0.1124  141 HIS F CD2 
8366  C CE1 . HIS F 139 ? 1.1579 1.9983 1.7739 0.0870  0.3362  0.1896  141 HIS F CE1 
8367  N NE2 . HIS F 139 ? 1.2007 1.9801 1.7112 0.0827  0.3187  0.1401  141 HIS F NE2 
8368  N N   . ALA F 140 ? 0.9729 1.7940 1.9161 0.0907  0.2891  0.1905  142 ALA F N   
8369  C CA  . ALA F 140 ? 1.0030 1.8403 1.9842 0.1223  0.3175  0.2122  142 ALA F CA  
8370  C C   . ALA F 140 ? 1.0648 1.8518 2.0667 0.1255  0.2886  0.1810  142 ALA F C   
8371  O O   . ALA F 140 ? 1.1014 1.8728 2.0754 0.1460  0.3075  0.1767  142 ALA F O   
8372  C CB  . ALA F 140 ? 1.0747 1.9174 1.9400 0.1435  0.3580  0.2134  142 ALA F CB  
8373  N N   . GLY F 141 ? 0.9830 1.7460 2.0337 0.1067  0.2424  0.1594  143 GLY F N   
8374  C CA  . GLY F 141 ? 0.9804 1.6961 2.0475 0.1087  0.2048  0.1295  143 GLY F CA  
8375  C C   . GLY F 141 ? 1.0299 1.6837 1.9629 0.0971  0.1851  0.0823  143 GLY F C   
8376  O O   . GLY F 141 ? 1.0234 1.6389 1.9548 0.0921  0.1445  0.0549  143 GLY F O   
8377  N N   . ALA F 142 ? 0.9921 1.6372 1.8155 0.0955  0.2124  0.0739  144 ALA F N   
8378  C CA  . ALA F 142 ? 1.0025 1.5943 1.7106 0.0866  0.2010  0.0367  144 ALA F CA  
8379  C C   . ALA F 142 ? 0.9865 1.5544 1.6607 0.0644  0.1742  0.0180  144 ALA F C   
8380  O O   . ALA F 142 ? 0.9391 1.5352 1.6466 0.0515  0.1755  0.0316  144 ALA F O   
8381  C CB  . ALA F 142 ? 1.0455 1.6398 1.6684 0.0926  0.2334  0.0336  144 ALA F CB  
8382  N N   . LYS F 143 ? 0.9565 1.4742 1.5676 0.0616  0.1537  -0.0095 145 LYS F N   
8383  C CA  . LYS F 143 ? 0.9550 1.4443 1.5209 0.0458  0.1357  -0.0257 145 LYS F CA  
8384  C C   . LYS F 143 ? 1.0081 1.4976 1.5160 0.0332  0.1580  -0.0232 145 LYS F C   
8385  O O   . LYS F 143 ? 1.0456 1.5153 1.4979 0.0387  0.1691  -0.0322 145 LYS F O   
8386  C CB  . LYS F 143 ? 1.0157 1.4555 1.5271 0.0526  0.1150  -0.0467 145 LYS F CB  
8387  C CG  . LYS F 143 ? 1.0918 1.5218 1.6411 0.0621  0.0793  -0.0559 145 LYS F CG  
8388  C CD  . LYS F 143 ? 1.2349 1.6207 1.7195 0.0727  0.0626  -0.0696 145 LYS F CD  
8389  C CE  . LYS F 143 ? 1.3720 1.7434 1.8707 0.0843  0.0207  -0.0833 145 LYS F CE  
8390  N NZ  . LYS F 143 ? 1.4894 1.8410 1.9329 0.0825  0.0105  -0.0980 145 LYS F NZ  
8391  N N   . SER F 144 ? 0.9138 1.4280 1.4466 0.0172  0.1619  -0.0106 146 SER F N   
8392  C CA  . SER F 144 ? 0.9053 1.4207 1.3932 0.0039  0.1764  -0.0055 146 SER F CA  
8393  C C   . SER F 144 ? 0.9458 1.4318 1.4147 -0.0154 0.1659  -0.0128 146 SER F C   
8394  O O   . SER F 144 ? 0.9525 1.4084 1.4131 -0.0125 0.1512  -0.0270 146 SER F O   
8395  C CB  . SER F 144 ? 0.9183 1.4916 1.4528 0.0026  0.1947  0.0239  146 SER F CB  
8396  O OG  . SER F 144 ? 1.0475 1.6223 1.5270 -0.0044 0.2052  0.0274  146 SER F OG  
8397  N N   . PHE F 145 ? 0.8838 1.3777 1.3436 -0.0325 0.1739  -0.0016 147 PHE F N   
8398  C CA  . PHE F 145 ? 0.8637 1.3314 1.3164 -0.0519 0.1700  -0.0020 147 PHE F CA  
8399  C C   . PHE F 145 ? 0.8968 1.3925 1.3677 -0.0708 0.1772  0.0194  147 PHE F C   
8400  O O   . PHE F 145 ? 0.8932 1.4292 1.3706 -0.0647 0.1854  0.0337  147 PHE F O   
8401  C CB  . PHE F 145 ? 0.9166 1.3274 1.3059 -0.0473 0.1673  -0.0177 147 PHE F CB  
8402  C CG  . PHE F 145 ? 0.9312 1.3086 1.3180 -0.0585 0.1679  -0.0161 147 PHE F CG  
8403  C CD1 . PHE F 145 ? 0.9597 1.3322 1.3605 -0.0535 0.1635  -0.0228 147 PHE F CD1 
8404  C CD2 . PHE F 145 ? 0.9601 1.3092 1.3335 -0.0713 0.1722  -0.0083 147 PHE F CD2 
8405  C CE1 . PHE F 145 ? 0.9758 1.3182 1.3686 -0.0590 0.1705  -0.0208 147 PHE F CE1 
8406  C CE2 . PHE F 145 ? 0.9918 1.3106 1.3720 -0.0793 0.1796  -0.0007 147 PHE F CE2 
8407  C CZ  . PHE F 145 ? 0.9677 1.2843 1.3529 -0.0720 0.1822  -0.0066 147 PHE F CZ  
8408  N N   . TYR F 146 ? 0.8393 1.3155 1.3202 -0.0916 0.1757  0.0250  148 TYR F N   
8409  C CA  . TYR F 146 ? 0.8153 1.3126 1.3182 -0.1126 0.1777  0.0474  148 TYR F CA  
8410  C C   . TYR F 146 ? 0.8703 1.3466 1.3103 -0.1086 0.1717  0.0412  148 TYR F C   
8411  O O   . TYR F 146 ? 0.8774 1.3028 1.2783 -0.1039 0.1655  0.0232  148 TYR F O   
8412  C CB  . TYR F 146 ? 0.8121 1.2866 1.3507 -0.1353 0.1782  0.0544  148 TYR F CB  
8413  C CG  . TYR F 146 ? 0.8079 1.2917 1.4007 -0.1361 0.1801  0.0493  148 TYR F CG  
8414  C CD1 . TYR F 146 ? 0.7947 1.3306 1.4743 -0.1482 0.1810  0.0672  148 TYR F CD1 
8415  C CD2 . TYR F 146 ? 0.8373 1.2771 1.3981 -0.1235 0.1797  0.0270  148 TYR F CD2 
8416  C CE1 . TYR F 146 ? 0.7908 1.3316 1.5293 -0.1484 0.1770  0.0555  148 TYR F CE1 
8417  C CE2 . TYR F 146 ? 0.8387 1.2826 1.4392 -0.1205 0.1765  0.0148  148 TYR F CE2 
8418  C CZ  . TYR F 146 ? 0.9170 1.4094 1.6091 -0.1336 0.1732  0.0254  148 TYR F CZ  
8419  O OH  . TYR F 146 ? 0.9682 1.4623 1.7065 -0.1285 0.1644  0.0059  148 TYR F OH  
8420  N N   . LYS F 147 ? 0.8292 1.3456 1.2624 -0.1074 0.1723  0.0562  149 LYS F N   
8421  C CA  . LYS F 147 ? 0.8764 1.3763 1.2437 -0.0985 0.1609  0.0434  149 LYS F CA  
8422  C C   . LYS F 147 ? 0.8951 1.3484 1.2576 -0.1177 0.1412  0.0398  149 LYS F C   
8423  O O   . LYS F 147 ? 0.9313 1.3447 1.2497 -0.1078 0.1254  0.0155  149 LYS F O   
8424  C CB  . LYS F 147 ? 0.9495 1.5078 1.3022 -0.0883 0.1674  0.0638  149 LYS F CB  
8425  C CG  . LYS F 147 ? 1.3507 1.9065 1.6246 -0.0567 0.1684  0.0396  149 LYS F CG  
8426  C CD  . LYS F 147 ? 1.6000 2.1280 1.8098 -0.0552 0.1420  0.0207  149 LYS F CD  
8427  C CE  . LYS F 147 ? 1.8734 2.3925 2.0055 -0.0205 0.1421  -0.0136 149 LYS F CE  
8428  N NZ  . LYS F 147 ? 2.0647 2.5587 2.1328 -0.0143 0.1095  -0.0386 149 LYS F NZ  
8429  N N   . ASN F 148 ? 0.7894 1.2463 1.2096 -0.1444 0.1414  0.0641  150 ASN F N   
8430  C CA  . ASN F 148 ? 0.7901 1.2050 1.2261 -0.1650 0.1239  0.0692  150 ASN F CA  
8431  C C   . ASN F 148 ? 0.8477 1.1998 1.2961 -0.1663 0.1270  0.0585  150 ASN F C   
8432  O O   . ASN F 148 ? 0.8605 1.1722 1.3293 -0.1789 0.1124  0.0638  150 ASN F O   
8433  C CB  . ASN F 148 ? 0.6992 1.1456 1.2010 -0.1934 0.1251  0.1044  150 ASN F CB  
8434  C CG  . ASN F 148 ? 0.8439 1.3571 1.3408 -0.1903 0.1246  0.1257  150 ASN F CG  
8435  O OD1 . ASN F 148 ? 0.8676 1.3942 1.2960 -0.1685 0.1160  0.1139  150 ASN F OD1 
8436  N ND2 . ASN F 148 ? 0.6116 1.1707 1.1843 -0.2091 0.1363  0.1590  150 ASN F ND2 
8437  N N   . LEU F 149 ? 0.7821 1.1260 1.2215 -0.1511 0.1446  0.0469  151 LEU F N   
8438  C CA  . LEU F 149 ? 0.7813 1.0712 1.2240 -0.1458 0.1520  0.0432  151 LEU F CA  
8439  C C   . LEU F 149 ? 0.8819 1.1609 1.2814 -0.1184 0.1576  0.0219  151 LEU F C   
8440  O O   . LEU F 149 ? 0.8792 1.1914 1.2646 -0.1075 0.1631  0.0137  151 LEU F O   
8441  C CB  . LEU F 149 ? 0.7436 1.0230 1.2338 -0.1601 0.1711  0.0625  151 LEU F CB  
8442  C CG  . LEU F 149 ? 0.7532 1.0781 1.2761 -0.1686 0.1816  0.0682  151 LEU F CG  
8443  C CD1 . LEU F 149 ? 0.7491 1.0810 1.2450 -0.1458 0.1891  0.0488  151 LEU F CD1 
8444  C CD2 . LEU F 149 ? 0.7768 1.0882 1.3587 -0.1890 0.1955  0.0878  151 LEU F CD2 
8445  N N   . ILE F 150 ? 0.8765 1.1097 1.2679 -0.1075 0.1544  0.0169  152 ILE F N   
8446  C CA  . ILE F 150 ? 0.9039 1.1230 1.2646 -0.0827 0.1578  0.0019  152 ILE F CA  
8447  C C   . ILE F 150 ? 0.9786 1.1776 1.3390 -0.0725 0.1781  0.0149  152 ILE F C   
8448  O O   . ILE F 150 ? 0.9733 1.1423 1.3609 -0.0778 0.1901  0.0359  152 ILE F O   
8449  C CB  . ILE F 150 ? 0.9813 1.1658 1.3470 -0.0742 0.1407  -0.0092 152 ILE F CB  
8450  C CG1 . ILE F 150 ? 1.0110 1.2088 1.3642 -0.0796 0.1158  -0.0279 152 ILE F CG1 
8451  C CG2 . ILE F 150 ? 1.0101 1.1845 1.3570 -0.0498 0.1441  -0.0218 152 ILE F CG2 
8452  C CD1 . ILE F 150 ? 1.1420 1.2966 1.5319 -0.0846 0.0898  -0.0313 152 ILE F CD1 
8453  N N   . TRP F 151 ? 0.9632 1.1769 1.2918 -0.0545 0.1816  0.0034  153 TRP F N   
8454  C CA  . TRP F 151 ? 0.9919 1.1878 1.3009 -0.0375 0.1957  0.0111  153 TRP F CA  
8455  C C   . TRP F 151 ? 1.0902 1.2549 1.3926 -0.0188 0.1980  0.0185  153 TRP F C   
8456  O O   . TRP F 151 ? 1.0996 1.2720 1.3865 -0.0058 0.1877  0.0044  153 TRP F O   
8457  C CB  . TRP F 151 ? 0.9763 1.2012 1.2616 -0.0263 0.1887  -0.0060 153 TRP F CB  
8458  C CG  . TRP F 151 ? 1.0173 1.2271 1.2695 -0.0059 0.1954  -0.0050 153 TRP F CG  
8459  C CD1 . TRP F 151 ? 1.0875 1.2637 1.3194 0.0079  0.2144  0.0138  153 TRP F CD1 
8460  C CD2 . TRP F 151 ? 1.0263 1.2546 1.2612 0.0069  0.1812  -0.0234 153 TRP F CD2 
8461  N NE1 . TRP F 151 ? 1.1121 1.2855 1.2985 0.0307  0.2138  0.0060  153 TRP F NE1 
8462  C CE2 . TRP F 151 ? 1.1164 1.3194 1.3061 0.0293  0.1890  -0.0201 153 TRP F CE2 
8463  C CE3 . TRP F 151 ? 1.0218 1.2856 1.2811 0.0039  0.1618  -0.0405 153 TRP F CE3 
8464  C CZ2 . TRP F 151 ? 1.1397 1.3487 1.2995 0.0484  0.1706  -0.0407 153 TRP F CZ2 
8465  C CZ3 . TRP F 151 ? 1.0626 1.3318 1.3114 0.0204  0.1437  -0.0573 153 TRP F CZ3 
8466  C CH2 . TRP F 151 ? 1.1213 1.3620 1.3168 0.0421  0.1443  -0.0610 153 TRP F CH2 
8467  N N   . LEU F 152 ? 1.0657 1.1967 1.3943 -0.0175 0.2128  0.0444  154 LEU F N   
8468  C CA  . LEU F 152 ? 1.0867 1.1904 1.4334 0.0005  0.2169  0.0602  154 LEU F CA  
8469  C C   . LEU F 152 ? 1.1676 1.2652 1.4765 0.0291  0.2348  0.0771  154 LEU F C   
8470  O O   . LEU F 152 ? 1.1843 1.2721 1.4730 0.0385  0.2580  0.0967  154 LEU F O   
8471  C CB  . LEU F 152 ? 1.0830 1.1539 1.4964 -0.0082 0.2227  0.0863  154 LEU F CB  
8472  C CG  . LEU F 152 ? 1.1242 1.1890 1.5815 -0.0243 0.1927  0.0681  154 LEU F CG  
8473  C CD1 . LEU F 152 ? 1.1390 1.1650 1.6772 -0.0248 0.1937  0.0966  154 LEU F CD1 
8474  C CD2 . LEU F 152 ? 1.1595 1.2353 1.6018 -0.0125 0.1724  0.0384  154 LEU F CD2 
8475  N N   . VAL F 153 ? 1.1198 1.2228 1.4193 0.0449  0.2241  0.0700  155 VAL F N   
8476  C CA  . VAL F 153 ? 1.1452 1.2459 1.4092 0.0740  0.2342  0.0876  155 VAL F CA  
8477  C C   . VAL F 153 ? 1.2060 1.2903 1.5229 0.0888  0.2392  0.1144  155 VAL F C   
8478  O O   . VAL F 153 ? 1.1736 1.2499 1.5525 0.0758  0.2263  0.1057  155 VAL F O   
8479  C CB  . VAL F 153 ? 1.1896 1.3158 1.4027 0.0803  0.2144  0.0592  155 VAL F CB  
8480  C CG1 . VAL F 153 ? 1.1812 1.3192 1.3531 0.0759  0.2133  0.0439  155 VAL F CG1 
8481  C CG2 . VAL F 153 ? 1.1582 1.3024 1.3973 0.0661  0.1924  0.0295  155 VAL F CG2 
8482  N N   . LYS F 154 ? 1.2131 1.2932 1.5094 0.1180  0.2566  0.1479  156 LYS F N   
8483  C CA  . LYS F 154 ? 1.2381 1.3080 1.5978 0.1359  0.2663  0.1850  156 LYS F CA  
8484  C C   . LYS F 154 ? 1.2949 1.3745 1.7014 0.1305  0.2395  0.1612  156 LYS F C   
8485  O O   . LYS F 154 ? 1.2872 1.3855 1.6507 0.1292  0.2212  0.1316  156 LYS F O   
8486  C CB  . LYS F 154 ? 1.3257 1.3969 1.6404 0.1724  0.2923  0.2303  156 LYS F CB  
8487  C CG  . LYS F 154 ? 1.4872 1.5784 1.7196 0.1873  0.2744  0.2123  156 LYS F CG  
8488  C CD  . LYS F 154 ? 1.6525 1.7444 1.8329 0.2274  0.2975  0.2594  156 LYS F CD  
8489  C CE  . LYS F 154 ? 1.7812 1.8909 1.9036 0.2420  0.2702  0.2456  156 LYS F CE  
8490  N NZ  . LYS F 154 ? 1.9771 2.0889 2.0249 0.2850  0.2885  0.2882  156 LYS F NZ  
8491  N N   . LYS F 155 ? 1.2703 1.3354 1.7752 0.1289  0.2369  0.1744  157 LYS F N   
8492  C CA  . LYS F 155 ? 1.2724 1.3423 1.8373 0.1264  0.2129  0.1499  157 LYS F CA  
8493  C C   . LYS F 155 ? 1.3737 1.4534 1.9681 0.1523  0.2229  0.1884  157 LYS F C   
8494  O O   . LYS F 155 ? 1.3849 1.4552 2.0741 0.1648  0.2332  0.2280  157 LYS F O   
8495  C CB  . LYS F 155 ? 1.2972 1.3444 1.9618 0.1141  0.1980  0.1399  157 LYS F CB  
8496  C CG  . LYS F 155 ? 1.4527 1.5023 2.1625 0.1084  0.1670  0.0925  157 LYS F CG  
8497  C CD  . LYS F 155 ? 1.5652 1.5875 2.3774 0.1013  0.1451  0.0807  157 LYS F CD  
8498  C CE  . LYS F 155 ? 1.6628 1.6839 2.5244 0.1025  0.1137  0.0307  157 LYS F CE  
8499  N NZ  . LYS F 155 ? 1.7556 1.7463 2.7259 0.0997  0.0845  0.0166  157 LYS F NZ  
8500  N N   . GLY F 156 ? 1.3547 1.4543 1.8760 0.1606  0.2183  0.1807  158 GLY F N   
8501  C CA  . GLY F 156 ? 1.3867 1.5000 1.9197 0.1846  0.2229  0.2164  158 GLY F CA  
8502  C C   . GLY F 156 ? 1.4942 1.6045 2.0349 0.2127  0.2551  0.2850  158 GLY F C   
8503  O O   . GLY F 156 ? 1.5041 1.6122 2.1502 0.2238  0.2664  0.3252  158 GLY F O   
8504  N N   . ASN F 157 ? 1.4805 1.5916 1.9142 0.2273  0.2710  0.2991  159 ASN F N   
8505  C CA  . ASN F 157 ? 1.5279 1.6373 1.9309 0.2612  0.3084  0.3625  159 ASN F CA  
8506  C C   . ASN F 157 ? 1.5654 1.6578 2.0749 0.2653  0.3401  0.4098  159 ASN F C   
8507  O O   . ASN F 157 ? 1.5917 1.6902 2.1533 0.2953  0.3693  0.4772  159 ASN F O   
8508  C CB  . ASN F 157 ? 1.5558 1.6863 1.9300 0.2945  0.3105  0.4041  159 ASN F CB  
8509  C CG  . ASN F 157 ? 1.7426 1.8870 2.2345 0.2950  0.3005  0.4260  159 ASN F CG  
8510  O OD1 . ASN F 157 ? 1.6858 1.8428 2.1778 0.2855  0.2697  0.3963  159 ASN F OD1 
8511  N ND2 . ASN F 157 ? 1.5748 1.7179 2.1807 0.3080  0.3271  0.4822  159 ASN F ND2 
8512  N N   . SER F 158 ? 1.4733 1.5455 2.0192 0.2363  0.3338  0.3780  160 SER F N   
8513  C CA  . SER F 158 ? 1.4525 1.5026 2.1078 0.2342  0.3547  0.4140  160 SER F CA  
8514  C C   . SER F 158 ? 1.4524 1.4822 2.0993 0.2016  0.3428  0.3713  160 SER F C   
8515  O O   . SER F 158 ? 1.4029 1.4274 2.0913 0.1733  0.3069  0.3222  160 SER F O   
8516  C CB  . SER F 158 ? 1.4763 1.5252 2.2846 0.2329  0.3397  0.4290  160 SER F CB  
8517  O OG  . SER F 158 ? 1.5790 1.6061 2.5106 0.2368  0.3588  0.4740  160 SER F OG  
8518  N N   . TYR F 159 ? 1.3300 1.5907 1.2287 0.0106  0.5109  0.2446  161 TYR F N   
8519  C CA  . TYR F 159 ? 1.2953 1.5559 1.2280 -0.0142 0.4802  0.2138  161 TYR F CA  
8520  C C   . TYR F 159 ? 1.3436 1.5789 1.3180 -0.0220 0.5055  0.1997  161 TYR F C   
8521  O O   . TYR F 159 ? 1.3441 1.5810 1.3166 -0.0179 0.5122  0.1941  161 TYR F O   
8522  C CB  . TYR F 159 ? 1.3018 1.5933 1.2122 -0.0155 0.4481  0.2028  161 TYR F CB  
8523  C CG  . TYR F 159 ? 1.2957 1.5926 1.2354 -0.0380 0.4140  0.1757  161 TYR F CG  
8524  C CD1 . TYR F 159 ? 1.3038 1.6221 1.2281 -0.0426 0.3798  0.1690  161 TYR F CD1 
8525  C CD2 . TYR F 159 ? 1.2971 1.5793 1.2807 -0.0526 0.4178  0.1573  161 TYR F CD2 
8526  C CE1 . TYR F 159 ? 1.2865 1.6089 1.2363 -0.0599 0.3526  0.1458  161 TYR F CE1 
8527  C CE2 . TYR F 159 ? 1.2765 1.5667 1.2873 -0.0704 0.3880  0.1358  161 TYR F CE2 
8528  C CZ  . TYR F 159 ? 1.3368 1.6467 1.3289 -0.0731 0.3565  0.1306  161 TYR F CZ  
8529  O OH  . TYR F 159 ? 1.3081 1.6254 1.3249 -0.0873 0.3311  0.1111  161 TYR F OH  
8530  N N   . PRO F 160 ? 1.2947 1.5058 1.3084 -0.0346 0.5208  0.1924  162 PRO F N   
8531  C CA  . PRO F 160 ? 1.2980 1.4876 1.3572 -0.0427 0.5442  0.1766  162 PRO F CA  
8532  C C   . PRO F 160 ? 1.3120 1.5117 1.4074 -0.0642 0.5101  0.1500  162 PRO F C   
8533  O O   . PRO F 160 ? 1.2758 1.4944 1.3653 -0.0748 0.4709  0.1425  162 PRO F O   
8534  C CB  . PRO F 160 ? 1.3295 1.4950 1.4163 -0.0500 0.5723  0.1771  162 PRO F CB  
8535  C CG  . PRO F 160 ? 1.3848 1.5563 1.4372 -0.0457 0.5641  0.1959  162 PRO F CG  
8536  C CD  . PRO F 160 ? 1.3069 1.5078 1.3268 -0.0437 0.5194  0.1966  162 PRO F CD  
8537  N N   . LYS F 161 ? 1.2799 1.4659 1.4144 -0.0693 0.5273  0.1370  163 LYS F N   
8538  C CA  . LYS F 161 ? 1.2579 1.4536 1.4335 -0.0881 0.5004  0.1150  163 LYS F CA  
8539  C C   . LYS F 161 ? 1.3185 1.5206 1.5279 -0.1091 0.4737  0.0996  163 LYS F C   
8540  O O   . LYS F 161 ? 1.3270 1.5133 1.5708 -0.1178 0.4926  0.0922  163 LYS F O   
8541  C CB  . LYS F 161 ? 1.2964 1.4710 1.5127 -0.0887 0.5303  0.1064  163 LYS F CB  
8542  C CG  . LYS F 161 ? 1.4061 1.5918 1.6668 -0.1059 0.5062  0.0879  163 LYS F CG  
8543  C CD  . LYS F 161 ? 1.4832 1.6452 1.8024 -0.1114 0.5355  0.0766  163 LYS F CD  
8544  C CE  . LYS F 161 ? 1.5094 1.6752 1.8872 -0.1307 0.5259  0.0586  163 LYS F CE  
8545  N NZ  . LYS F 161 ? 1.5242 1.6650 1.9592 -0.1340 0.5612  0.0473  163 LYS F NZ  
8546  N N   . LEU F 162 ? 1.2623 1.4868 1.4595 -0.1168 0.4317  0.0943  164 LEU F N   
8547  C CA  . LEU F 162 ? 1.2405 1.4717 1.4624 -0.1352 0.4018  0.0802  164 LEU F CA  
8548  C C   . LEU F 162 ? 1.2668 1.5083 1.5434 -0.1496 0.3872  0.0616  164 LEU F C   
8549  O O   . LEU F 162 ? 1.2565 1.5056 1.5404 -0.1456 0.3877  0.0608  164 LEU F O   
8550  C CB  . LEU F 162 ? 1.2254 1.4710 1.4088 -0.1340 0.3672  0.0839  164 LEU F CB  
8551  C CG  . LEU F 162 ? 1.2666 1.5341 1.4327 -0.1287 0.3450  0.0820  164 LEU F CG  
8552  C CD1 . LEU F 162 ? 1.2347 1.5161 1.4255 -0.1416 0.3102  0.0664  164 LEU F CD1 
8553  C CD2 . LEU F 162 ? 1.3044 1.5787 1.4162 -0.1153 0.3396  0.0956  164 LEU F CD2 
8554  N N   . SER F 163 ? 1.2146 1.4573 1.5300 -0.1668 0.3754  0.0470  165 SER F N   
8555  C CA  . SER F 163 ? 1.2040 1.4617 1.5762 -0.1801 0.3594  0.0307  165 SER F CA  
8556  C C   . SER F 163 ? 1.2204 1.4915 1.6134 -0.1975 0.3268  0.0168  165 SER F C   
8557  O O   . SER F 163 ? 1.2224 1.4938 1.6601 -0.2120 0.3317  0.0027  165 SER F O   
8558  C CB  . SER F 163 ? 1.2931 1.5367 1.7122 -0.1818 0.3944  0.0248  165 SER F CB  
8559  O OG  . SER F 163 ? 1.4478 1.7059 1.9162 -0.1886 0.3833  0.0156  165 SER F OG  
8560  N N   . LYS F 164 ? 1.1502 1.4325 1.5109 -0.1959 0.2939  0.0194  166 LYS F N   
8561  C CA  . LYS F 164 ? 1.1408 1.4339 1.5127 -0.2099 0.2610  0.0077  166 LYS F CA  
8562  C C   . LYS F 164 ? 1.1830 1.5039 1.6018 -0.2153 0.2373  -0.0019 166 LYS F C   
8563  O O   . LYS F 164 ? 1.1706 1.5020 1.5933 -0.2057 0.2375  0.0039  166 LYS F O   
8564  C CB  . LYS F 164 ? 1.1647 1.4520 1.4827 -0.2041 0.2392  0.0147  166 LYS F CB  
8565  C CG  . LYS F 164 ? 1.3987 1.6610 1.6889 -0.2112 0.2484  0.0170  166 LYS F CG  
8566  C CD  . LYS F 164 ? 1.5570 1.8210 1.8616 -0.2302 0.2234  0.0019  166 LYS F CD  
8567  C CE  . LYS F 164 ? 1.7293 1.9641 2.0091 -0.2407 0.2396  0.0035  166 LYS F CE  
8568  N NZ  . LYS F 164 ? 1.8552 2.0848 2.1224 -0.2550 0.2092  -0.0068 166 LYS F NZ  
8569  N N   . SER F 165 ? 1.1410 1.4753 1.5962 -0.2313 0.2183  -0.0163 167 SER F N   
8570  C CA  . SER F 165 ? 1.1250 1.4906 1.6303 -0.2362 0.1945  -0.0237 167 SER F CA  
8571  C C   . SER F 165 ? 1.1866 1.5691 1.6900 -0.2455 0.1556  -0.0326 167 SER F C   
8572  O O   . SER F 165 ? 1.2156 1.5902 1.7149 -0.2600 0.1525  -0.0431 167 SER F O   
8573  C CB  . SER F 165 ? 1.1669 1.5394 1.7376 -0.2462 0.2137  -0.0337 167 SER F CB  
8574  O OG  . SER F 165 ? 1.2687 1.6195 1.8383 -0.2366 0.2527  -0.0256 167 SER F OG  
8575  N N   . TYR F 166 ? 1.1111 1.5154 1.6161 -0.2371 0.1288  -0.0282 168 TYR F N   
8576  C CA  . TYR F 166 ? 1.1027 1.5238 1.6039 -0.2420 0.0913  -0.0347 168 TYR F CA  
8577  C C   . TYR F 166 ? 1.1126 1.5742 1.6792 -0.2479 0.0724  -0.0406 168 TYR F C   
8578  O O   . TYR F 166 ? 1.0864 1.5645 1.6870 -0.2392 0.0796  -0.0326 168 TYR F O   
8579  C CB  . TYR F 166 ? 1.1110 1.5252 1.5623 -0.2255 0.0753  -0.0250 168 TYR F CB  
8580  C CG  . TYR F 166 ? 1.1386 1.5682 1.5852 -0.2265 0.0383  -0.0298 168 TYR F CG  
8581  C CD1 . TYR F 166 ? 1.1857 1.5972 1.5998 -0.2380 0.0236  -0.0383 168 TYR F CD1 
8582  C CD2 . TYR F 166 ? 1.1326 1.5936 1.6067 -0.2157 0.0205  -0.0249 168 TYR F CD2 
8583  C CE1 . TYR F 166 ? 1.2031 1.6267 1.6083 -0.2384 -0.0105 -0.0429 168 TYR F CE1 
8584  C CE2 . TYR F 166 ? 1.1511 1.6271 1.6184 -0.2135 -0.0128 -0.0275 168 TYR F CE2 
8585  C CZ  . TYR F 166 ? 1.2634 1.7204 1.6946 -0.2248 -0.0295 -0.0371 168 TYR F CZ  
8586  O OH  . TYR F 166 ? 1.2898 1.7593 1.7093 -0.2220 -0.0625 -0.0397 168 TYR F OH  
8587  N N   . ILE F 167 ? 1.0650 1.5435 1.6478 -0.2630 0.0478  -0.0541 169 ILE F N   
8588  C CA  . ILE F 167 ? 1.0547 1.5781 1.7002 -0.2698 0.0243  -0.0606 169 ILE F CA  
8589  C C   . ILE F 167 ? 1.0782 1.6194 1.6984 -0.2622 -0.0144 -0.0572 169 ILE F C   
8590  O O   . ILE F 167 ? 1.0815 1.6044 1.6537 -0.2683 -0.0286 -0.0638 169 ILE F O   
8591  C CB  . ILE F 167 ? 1.1190 1.6523 1.8064 -0.2943 0.0276  -0.0816 169 ILE F CB  
8592  C CG1 . ILE F 167 ? 1.1291 1.6341 1.8327 -0.2986 0.0737  -0.0845 169 ILE F CG1 
8593  C CG2 . ILE F 167 ? 1.1312 1.7174 1.8905 -0.3016 0.0016  -0.0889 169 ILE F CG2 
8594  C CD1 . ILE F 167 ? 1.2480 1.7075 1.8948 -0.3037 0.0998  -0.0870 169 ILE F CD1 
8595  N N   . ASN F 168 ? 1.0213 1.5942 1.6714 -0.2477 -0.0276 -0.0454 170 ASN F N   
8596  C CA  . ASN F 168 ? 1.0280 1.6182 1.6556 -0.2348 -0.0601 -0.0390 170 ASN F CA  
8597  C C   . ASN F 168 ? 1.1189 1.7412 1.7627 -0.2486 -0.0973 -0.0518 170 ASN F C   
8598  O O   . ASN F 168 ? 1.1217 1.7899 1.8296 -0.2541 -0.1113 -0.0540 170 ASN F O   
8599  C CB  . ASN F 168 ? 1.0082 1.6228 1.6654 -0.2141 -0.0568 -0.0208 170 ASN F CB  
8600  C CG  . ASN F 168 ? 1.2282 1.8465 1.8477 -0.1941 -0.0774 -0.0110 170 ASN F CG  
8601  O OD1 . ASN F 168 ? 1.0937 1.6988 1.6662 -0.1950 -0.1001 -0.0177 170 ASN F OD1 
8602  N ND2 . ASN F 168 ? 1.1441 1.7770 1.7832 -0.1751 -0.0661 0.0051  170 ASN F ND2 
8603  N N   . ASP F 169 ? 1.0987 1.6963 1.6831 -0.2541 -0.1133 -0.0600 171 ASP F N   
8604  C CA  . ASP F 169 ? 1.1292 1.7503 1.7123 -0.2689 -0.1489 -0.0740 171 ASP F CA  
8605  C C   . ASP F 169 ? 1.1900 1.8168 1.7329 -0.2492 -0.1795 -0.0638 171 ASP F C   
8606  O O   . ASP F 169 ? 1.2150 1.8712 1.7603 -0.2562 -0.2139 -0.0717 171 ASP F O   
8607  C CB  . ASP F 169 ? 1.1817 1.7658 1.7274 -0.2940 -0.1400 -0.0928 171 ASP F CB  
8608  C CG  . ASP F 169 ? 1.3727 1.8969 1.8403 -0.2859 -0.1258 -0.0862 171 ASP F CG  
8609  O OD1 . ASP F 169 ? 1.4061 1.9108 1.8241 -0.2909 -0.1456 -0.0918 171 ASP F OD1 
8610  O OD2 . ASP F 169 ? 1.4723 1.9690 1.9285 -0.2747 -0.0949 -0.0754 171 ASP F OD2 
8611  N N   . LYS F 170 ? 1.1230 1.7221 1.6295 -0.2241 -0.1653 -0.0473 172 LYS F N   
8612  C CA  . LYS F 170 ? 1.1225 1.7150 1.5859 -0.2006 -0.1839 -0.0367 172 LYS F CA  
8613  C C   . LYS F 170 ? 1.1695 1.8194 1.6759 -0.1846 -0.2094 -0.0252 172 LYS F C   
8614  O O   . LYS F 170 ? 1.1906 1.8410 1.6621 -0.1683 -0.2316 -0.0196 172 LYS F O   
8615  C CB  . LYS F 170 ? 1.1245 1.6754 1.5487 -0.1791 -0.1555 -0.0247 172 LYS F CB  
8616  C CG  . LYS F 170 ? 1.3125 1.8086 1.6909 -0.1905 -0.1316 -0.0320 172 LYS F CG  
8617  C CD  . LYS F 170 ? 1.4676 1.9229 1.7838 -0.2000 -0.1463 -0.0417 172 LYS F CD  
8618  C CE  . LYS F 170 ? 1.5955 2.0085 1.8861 -0.2182 -0.1218 -0.0487 172 LYS F CE  
8619  N NZ  . LYS F 170 ? 1.7584 2.1284 1.9920 -0.2303 -0.1320 -0.0571 172 LYS F NZ  
8620  N N   . GLY F 171 ? 1.0919 1.7874 1.6730 -0.1877 -0.2042 -0.0202 173 GLY F N   
8621  C CA  . GLY F 171 ? 1.0789 1.8331 1.7105 -0.1725 -0.2250 -0.0059 173 GLY F CA  
8622  C C   . GLY F 171 ? 1.0801 1.8341 1.7153 -0.1413 -0.2042 0.0177  173 GLY F C   
8623  O O   . GLY F 171 ? 1.0599 1.8614 1.7519 -0.1287 -0.2076 0.0339  173 GLY F O   
8624  N N   . LYS F 172 ? 1.0172 1.7180 1.5936 -0.1292 -0.1807 0.0195  174 LYS F N   
8625  C CA  . LYS F 172 ? 0.9845 1.6748 1.5543 -0.1019 -0.1537 0.0367  174 LYS F CA  
8626  C C   . LYS F 172 ? 0.9824 1.6567 1.5755 -0.1090 -0.1136 0.0378  174 LYS F C   
8627  O O   . LYS F 172 ? 0.9806 1.6419 1.5802 -0.1318 -0.1072 0.0252  174 LYS F O   
8628  C CB  . LYS F 172 ? 1.0230 1.6627 1.5131 -0.0865 -0.1520 0.0336  174 LYS F CB  
8629  C CG  . LYS F 172 ? 1.2126 1.8600 1.6706 -0.0722 -0.1860 0.0359  174 LYS F CG  
8630  C CD  . LYS F 172 ? 1.3357 1.9242 1.7166 -0.0558 -0.1786 0.0327  174 LYS F CD  
8631  C CE  . LYS F 172 ? 1.4595 1.9999 1.7859 -0.0782 -0.1883 0.0141  174 LYS F CE  
8632  N NZ  . LYS F 172 ? 1.5396 2.0180 1.7989 -0.0627 -0.1739 0.0119  174 LYS F NZ  
8633  N N   . GLU F 173 ? 0.8954 1.5695 1.4996 -0.0897 -0.0841 0.0523  175 GLU F N   
8634  C CA  . GLU F 173 ? 0.8600 1.5162 1.4775 -0.0953 -0.0445 0.0531  175 GLU F CA  
8635  C C   . GLU F 173 ? 0.8914 1.4948 1.4393 -0.0991 -0.0341 0.0397  175 GLU F C   
8636  O O   . GLU F 173 ? 0.8990 1.4789 1.3972 -0.0834 -0.0371 0.0388  175 GLU F O   
8637  C CB  . GLU F 173 ? 0.8582 1.5274 1.5010 -0.0746 -0.0145 0.0706  175 GLU F CB  
8638  C CG  . GLU F 173 ? 1.0016 1.7028 1.7205 -0.0816 0.0046  0.0829  175 GLU F CG  
8639  C CD  . GLU F 173 ? 1.2599 1.9731 2.0079 -0.0638 0.0396  0.1014  175 GLU F CD  
8640  O OE1 . GLU F 173 ? 1.0637 1.7719 1.7818 -0.0414 0.0448  0.1070  175 GLU F OE1 
8641  O OE2 . GLU F 173 ? 1.2510 1.9771 2.0542 -0.0722 0.0647  0.1106  175 GLU F OE2 
8642  N N   . VAL F 174 ? 0.8229 1.4072 1.3676 -0.1188 -0.0224 0.0300  176 VAL F N   
8643  C CA  . VAL F 174 ? 0.8127 1.3510 1.2964 -0.1230 -0.0125 0.0198  176 VAL F CA  
8644  C C   . VAL F 174 ? 0.8195 1.3426 1.2957 -0.1179 0.0248  0.0229  176 VAL F C   
8645  O O   . VAL F 174 ? 0.8093 1.3407 1.3199 -0.1278 0.0448  0.0251  176 VAL F O   
8646  C CB  . VAL F 174 ? 0.8785 1.4035 1.3547 -0.1461 -0.0232 0.0077  176 VAL F CB  
8647  C CG1 . VAL F 174 ? 0.8783 1.3594 1.3016 -0.1501 -0.0050 0.0020  176 VAL F CG1 
8648  C CG2 . VAL F 174 ? 0.9001 1.4316 1.3640 -0.1516 -0.0593 0.0009  176 VAL F CG2 
8649  N N   . LEU F 175 ? 0.7417 1.2419 1.1728 -0.1025 0.0346  0.0218  177 LEU F N   
8650  C CA  . LEU F 175 ? 0.7097 1.1966 1.1262 -0.0983 0.0679  0.0210  177 LEU F CA  
8651  C C   . LEU F 175 ? 0.7833 1.2400 1.1589 -0.1098 0.0725  0.0128  177 LEU F C   
8652  O O   . LEU F 175 ? 0.8037 1.2349 1.1369 -0.1093 0.0566  0.0072  177 LEU F O   
8653  C CB  . LEU F 175 ? 0.6929 1.1708 1.0837 -0.0771 0.0780  0.0208  177 LEU F CB  
8654  C CG  . LEU F 175 ? 0.7297 1.1889 1.0906 -0.0739 0.1080  0.0137  177 LEU F CG  
8655  C CD1 . LEU F 175 ? 0.7252 1.2033 1.1217 -0.0810 0.1392  0.0178  177 LEU F CD1 
8656  C CD2 . LEU F 175 ? 0.7343 1.1809 1.0701 -0.0534 0.1165  0.0097  177 LEU F CD2 
8657  N N   . VAL F 176 ? 0.7406 1.1987 1.1289 -0.1194 0.0957  0.0135  178 VAL F N   
8658  C CA  . VAL F 176 ? 0.7510 1.1853 1.1044 -0.1280 0.1041  0.0092  178 VAL F CA  
8659  C C   . VAL F 176 ? 0.8474 1.2774 1.1808 -0.1232 0.1322  0.0081  178 VAL F C   
8660  O O   . VAL F 176 ? 0.8416 1.2875 1.2058 -0.1251 0.1535  0.0115  178 VAL F O   
8661  C CB  . VAL F 176 ? 0.7982 1.2364 1.1815 -0.1441 0.1059  0.0104  178 VAL F CB  
8662  C CG1 . VAL F 176 ? 0.8006 1.2148 1.1481 -0.1495 0.1202  0.0092  178 VAL F CG1 
8663  C CG2 . VAL F 176 ? 0.8053 1.2510 1.2082 -0.1519 0.0779  0.0075  178 VAL F CG2 
8664  N N   . LEU F 177 ? 0.8443 1.2533 1.1276 -0.1183 0.1331  0.0031  179 LEU F N   
8665  C CA  . LEU F 177 ? 0.8530 1.2614 1.1130 -0.1149 0.1568  -0.0007 179 LEU F CA  
8666  C C   . LEU F 177 ? 0.9554 1.3506 1.1852 -0.1213 0.1622  0.0011  179 LEU F C   
8667  O O   . LEU F 177 ? 0.9738 1.3511 1.1843 -0.1236 0.1474  0.0033  179 LEU F O   
8668  C CB  . LEU F 177 ? 0.8448 1.2442 1.0748 -0.1016 0.1560  -0.0090 179 LEU F CB  
8669  C CG  . LEU F 177 ? 0.8905 1.3019 1.1450 -0.0908 0.1598  -0.0104 179 LEU F CG  
8670  C CD1 . LEU F 177 ? 0.9017 1.2996 1.1490 -0.0822 0.1330  -0.0093 179 LEU F CD1 
8671  C CD2 . LEU F 177 ? 0.9031 1.3141 1.1392 -0.0817 0.1818  -0.0211 179 LEU F CD2 
8672  N N   . TRP F 178 ? 0.9289 1.3323 1.1534 -0.1239 0.1854  0.0011  180 TRP F N   
8673  C CA  . TRP F 178 ? 0.9581 1.3531 1.1526 -0.1266 0.1941  0.0051  180 TRP F CA  
8674  C C   . TRP F 178 ? 1.0649 1.4720 1.2390 -0.1251 0.2153  0.0003  180 TRP F C   
8675  O O   . TRP F 178 ? 1.0556 1.4763 1.2497 -0.1268 0.2298  -0.0052 180 TRP F O   
8676  C CB  . TRP F 178 ? 0.9550 1.3468 1.1754 -0.1356 0.2014  0.0132  180 TRP F CB  
8677  C CG  . TRP F 178 ? 0.9630 1.3672 1.2202 -0.1413 0.2220  0.0143  180 TRP F CG  
8678  C CD1 . TRP F 178 ? 1.0105 1.4154 1.2577 -0.1436 0.2470  0.0162  180 TRP F CD1 
8679  C CD2 . TRP F 178 ? 0.9513 1.3670 1.2613 -0.1455 0.2204  0.0149  180 TRP F CD2 
8680  N NE1 . TRP F 178 ? 0.9985 1.4097 1.2889 -0.1502 0.2633  0.0175  180 TRP F NE1 
8681  C CE2 . TRP F 178 ? 1.0007 1.4204 1.3330 -0.1511 0.2475  0.0176  180 TRP F CE2 
8682  C CE3 . TRP F 178 ? 0.9557 1.3797 1.2959 -0.1445 0.1988  0.0145  180 TRP F CE3 
8683  C CZ2 . TRP F 178 ? 0.9832 1.4137 1.3711 -0.1560 0.2552  0.0212  180 TRP F CZ2 
8684  C CZ3 . TRP F 178 ? 0.9636 1.4040 1.3581 -0.1479 0.2038  0.0183  180 TRP F CZ3 
8685  C CH2 . TRP F 178 ? 0.9726 1.4158 1.3925 -0.1537 0.2325  0.0221  180 TRP F CH2 
8686  N N   . GLY F 179 ? 1.0680 1.4712 1.2034 -0.1228 0.2187  0.0031  181 GLY F N   
8687  C CA  . GLY F 179 ? 1.0852 1.5032 1.1950 -0.1223 0.2359  -0.0024 181 GLY F CA  
8688  C C   . GLY F 179 ? 1.1811 1.5995 1.2796 -0.1255 0.2524  0.0070  181 GLY F C   
8689  O O   . GLY F 179 ? 1.1948 1.5989 1.2993 -0.1256 0.2508  0.0184  181 GLY F O   
8690  N N   . ILE F 180 ? 1.1503 1.5839 1.2319 -0.1283 0.2709  0.0012  182 ILE F N   
8691  C CA  . ILE F 180 ? 1.1786 1.6126 1.2397 -0.1295 0.2888  0.0091  182 ILE F CA  
8692  C C   . ILE F 180 ? 1.2572 1.7118 1.2714 -0.1255 0.2890  0.0026  182 ILE F C   
8693  O O   . ILE F 180 ? 1.2595 1.7312 1.2709 -0.1312 0.2966  -0.0132 182 ILE F O   
8694  C CB  . ILE F 180 ? 1.2264 1.6568 1.3161 -0.1400 0.3138  0.0081  182 ILE F CB  
8695  C CG1 . ILE F 180 ? 1.2239 1.6392 1.3687 -0.1443 0.3118  0.0136  182 ILE F CG1 
8696  C CG2 . ILE F 180 ? 1.2682 1.6941 1.3291 -0.1397 0.3342  0.0158  182 ILE F CG2 
8697  C CD1 . ILE F 180 ? 1.3346 1.7317 1.4897 -0.1407 0.3042  0.0254  182 ILE F CD1 
8698  N N   . HIS F 181 ? 1.2319 1.6868 1.2122 -0.1158 0.2816  0.0144  183 HIS F N   
8699  C CA  . HIS F 181 ? 1.2442 1.7234 1.1806 -0.1102 0.2782  0.0109  183 HIS F CA  
8700  C C   . HIS F 181 ? 1.3331 1.8255 1.2430 -0.1128 0.2985  0.0127  183 HIS F C   
8701  O O   . HIS F 181 ? 1.3534 1.8300 1.2607 -0.1091 0.3110  0.0282  183 HIS F O   
8702  C CB  . HIS F 181 ? 1.2583 1.7327 1.1730 -0.0973 0.2626  0.0265  183 HIS F CB  
8703  C CG  . HIS F 181 ? 1.3141 1.8169 1.1876 -0.0898 0.2566  0.0261  183 HIS F CG  
8704  N ND1 . HIS F 181 ? 1.3663 1.8791 1.2070 -0.0797 0.2631  0.0444  183 HIS F ND1 
8705  C CD2 . HIS F 181 ? 1.3248 1.8492 1.1880 -0.0903 0.2459  0.0094  183 HIS F CD2 
8706  C CE1 . HIS F 181 ? 1.3637 1.9076 1.1755 -0.0749 0.2528  0.0392  183 HIS F CE1 
8707  N NE2 . HIS F 181 ? 1.3427 1.8942 1.1683 -0.0819 0.2425  0.0169  183 HIS F NE2 
8708  N N   . HIS F 182 ? 1.2914 1.8109 1.1812 -0.1195 0.3038  -0.0046 184 HIS F N   
8709  C CA  . HIS F 182 ? 1.3193 1.8532 1.1768 -0.1241 0.3222  -0.0060 184 HIS F CA  
8710  C C   . HIS F 182 ? 1.3809 1.9495 1.1902 -0.1151 0.3091  -0.0059 184 HIS F C   
8711  O O   . HIS F 182 ? 1.3744 1.9708 1.1759 -0.1208 0.3022  -0.0263 184 HIS F O   
8712  C CB  . HIS F 182 ? 1.3222 1.8606 1.1957 -0.1427 0.3435  -0.0268 184 HIS F CB  
8713  C CG  . HIS F 182 ? 1.3435 1.8526 1.2687 -0.1501 0.3555  -0.0244 184 HIS F CG  
8714  N ND1 . HIS F 182 ? 1.3834 1.8695 1.3201 -0.1560 0.3784  -0.0154 184 HIS F ND1 
8715  C CD2 . HIS F 182 ? 1.3281 1.8288 1.2954 -0.1512 0.3473  -0.0293 184 HIS F CD2 
8716  C CE1 . HIS F 182 ? 1.3497 1.8179 1.3388 -0.1613 0.3822  -0.0149 184 HIS F CE1 
8717  N NE2 . HIS F 182 ? 1.3214 1.7992 1.3289 -0.1581 0.3632  -0.0225 184 HIS F NE2 
8718  N N   . PRO F 183 ? 1.3439 1.9118 1.1247 -0.0996 0.3059  0.0176  185 PRO F N   
8719  C CA  . PRO F 183 ? 1.3570 1.9615 1.0953 -0.0885 0.2917  0.0221  185 PRO F CA  
8720  C C   . PRO F 183 ? 1.4436 2.0835 1.1453 -0.0973 0.2998  0.0065  185 PRO F C   
8721  O O   . PRO F 183 ? 1.4614 2.0896 1.1536 -0.1047 0.3214  0.0061  185 PRO F O   
8722  C CB  . PRO F 183 ? 1.4021 1.9923 1.1231 -0.0692 0.2950  0.0544  185 PRO F CB  
8723  C CG  . PRO F 183 ? 1.4426 1.9877 1.2033 -0.0714 0.3064  0.0628  185 PRO F CG  
8724  C CD  . PRO F 183 ? 1.3733 1.9086 1.1616 -0.0905 0.3179  0.0414  185 PRO F CD  
8725  N N   . SER F 184 ? 1.4154 2.0972 1.0969 -0.0973 0.2835  -0.0073 186 SER F N   
8726  C CA  . SER F 184 ? 1.4479 2.1718 1.0931 -0.1079 0.2880  -0.0267 186 SER F CA  
8727  C C   . SER F 184 ? 1.5598 2.2959 1.1549 -0.0978 0.2955  -0.0072 186 SER F C   
8728  O O   . SER F 184 ? 1.5846 2.3208 1.1597 -0.1111 0.3151  -0.0179 186 SER F O   
8729  C CB  . SER F 184 ? 1.4786 2.2465 1.1181 -0.1082 0.2668  -0.0452 186 SER F CB  
8730  O OG  . SER F 184 ? 1.5823 2.3552 1.2179 -0.0871 0.2453  -0.0215 186 SER F OG  
8731  N N   . THR F 185 ? 1.5343 2.2776 1.1093 -0.0740 0.2830  0.0225  187 THR F N   
8732  C CA  . THR F 185 ? 1.5808 2.3349 1.1069 -0.0583 0.2911  0.0460  187 THR F CA  
8733  C C   . THR F 185 ? 1.6140 2.3159 1.1523 -0.0444 0.3107  0.0746  187 THR F C   
8734  O O   . THR F 185 ? 1.5589 2.2272 1.1399 -0.0426 0.3097  0.0814  187 THR F O   
8735  C CB  . THR F 185 ? 1.7540 2.5583 1.2473 -0.0388 0.2680  0.0617  187 THR F CB  
8736  O OG1 . THR F 185 ? 1.7464 2.5331 1.2655 -0.0216 0.2582  0.0856  187 THR F OG1 
8737  C CG2 . THR F 185 ? 1.7509 2.6108 1.2353 -0.0526 0.2483  0.0310  187 THR F CG2 
8738  N N   . SER F 186 ? 1.6244 2.3188 1.1243 -0.0347 0.3301  0.0900  188 SER F N   
8739  C CA  . SER F 186 ? 1.6421 2.2871 1.1508 -0.0197 0.3541  0.1161  188 SER F CA  
8740  C C   . SER F 186 ? 1.6873 2.3321 1.2024 0.0050  0.3460  0.1461  188 SER F C   
8741  O O   . SER F 186 ? 1.6695 2.2713 1.2186 0.0104  0.3596  0.1593  188 SER F O   
8742  C CB  . SER F 186 ? 1.7537 2.3928 1.2125 -0.0112 0.3774  0.1264  188 SER F CB  
8743  O OG  . SER F 186 ? 1.9134 2.5112 1.3755 0.0108  0.4006  0.1558  188 SER F OG  
8744  N N   . ALA F 187 ? 1.6738 2.3827 1.3058 -0.2273 0.0696  0.0401  189 ALA F N   
8745  C CA  . ALA F 187 ? 1.6695 2.4008 1.3373 -0.1874 0.0574  0.0674  189 ALA F CA  
8746  C C   . ALA F 187 ? 1.6638 2.3745 1.3849 -0.1776 0.0722  0.0555  189 ALA F C   
8747  O O   . ALA F 187 ? 1.6605 2.3447 1.4018 -0.1465 0.0791  0.0763  189 ALA F O   
8748  C CB  . ALA F 187 ? 1.6974 2.5202 1.3761 -0.1831 0.0254  0.0764  189 ALA F CB  
8749  N N   . ASP F 188 ? 1.5775 2.2955 1.3161 -0.2052 0.0796  0.0221  190 ASP F N   
8750  C CA  . ASP F 188 ? 1.5269 2.2216 1.3075 -0.2011 0.0937  0.0076  190 ASP F CA  
8751  C C   . ASP F 188 ? 1.5432 2.1606 1.3190 -0.1928 0.1158  0.0110  190 ASP F C   
8752  O O   . ASP F 188 ? 1.5242 2.1177 1.3284 -0.1742 0.1240  0.0177  190 ASP F O   
8753  C CB  . ASP F 188 ? 1.5258 2.2377 1.3139 -0.2335 0.0991  -0.0284 190 ASP F CB  
8754  C CG  . ASP F 188 ? 1.5941 2.3798 1.4122 -0.2383 0.0838  -0.0377 190 ASP F CG  
8755  O OD1 . ASP F 188 ? 1.6120 2.4576 1.4354 -0.2245 0.0611  -0.0177 190 ASP F OD1 
8756  O OD2 . ASP F 188 ? 1.6222 2.4076 1.4568 -0.2569 0.0948  -0.0655 190 ASP F OD2 
8757  N N   . GLN F 189 ? 1.4894 2.0700 1.2293 -0.2079 0.1263  0.0064  191 GLN F N   
8758  C CA  . GLN F 189 ? 1.4711 1.9875 1.2070 -0.2036 0.1466  0.0077  191 GLN F CA  
8759  C C   . GLN F 189 ? 1.5293 2.0235 1.2635 -0.1742 0.1492  0.0374  191 GLN F C   
8760  O O   . GLN F 189 ? 1.4953 1.9508 1.2476 -0.1642 0.1635  0.0391  191 GLN F O   
8761  C CB  . GLN F 189 ? 1.5061 1.9977 1.2054 -0.2259 0.1575  -0.0025 191 GLN F CB  
8762  C CG  . GLN F 189 ? 1.6077 2.0416 1.3045 -0.2237 0.1785  -0.0021 191 GLN F CG  
8763  C CD  . GLN F 189 ? 1.6553 2.0685 1.3841 -0.2291 0.1892  -0.0215 191 GLN F CD  
8764  O OE1 . GLN F 189 ? 1.5276 1.9507 1.2622 -0.2449 0.1905  -0.0417 191 GLN F OE1 
8765  N NE2 . GLN F 189 ? 1.5364 1.9177 1.2818 -0.2172 0.1987  -0.0156 191 GLN F NE2 
8766  N N   . GLN F 190 ? 1.5402 2.0577 1.2493 -0.1609 0.1362  0.0610  192 GLN F N   
8767  C CA  . GLN F 190 ? 1.5803 2.0731 1.2798 -0.1298 0.1411  0.0926  192 GLN F CA  
8768  C C   . GLN F 190 ? 1.6251 2.1322 1.3685 -0.1040 0.1399  0.1040  192 GLN F C   
8769  O O   . GLN F 190 ? 1.6430 2.1059 1.3884 -0.0833 0.1575  0.1206  192 GLN F O   
8770  C CB  . GLN F 190 ? 1.6537 2.1718 1.3111 -0.1203 0.1244  0.1168  192 GLN F CB  
8771  C CG  . GLN F 190 ? 1.9352 2.3929 1.5489 -0.1046 0.1415  0.1406  192 GLN F CG  
8772  C CD  . GLN F 190 ? 2.2445 2.6806 1.8689 -0.0653 0.1501  0.1713  192 GLN F CD  
8773  O OE1 . GLN F 190 ? 2.2080 2.5776 1.8201 -0.0585 0.1782  0.1767  192 GLN F OE1 
8774  N NE2 . GLN F 190 ? 2.1645 2.6559 1.8109 -0.0389 0.1287  0.1921  192 GLN F NE2 
8775  N N   . SER F 191 ? 1.5474 2.1122 1.3249 -0.1076 0.1234  0.0929  193 SER F N   
8776  C CA  . SER F 191 ? 1.5281 2.1099 1.3505 -0.0847 0.1241  0.1017  193 SER F CA  
8777  C C   . SER F 191 ? 1.5365 2.0756 1.3853 -0.0939 0.1442  0.0815  193 SER F C   
8778  O O   . SER F 191 ? 1.5378 2.0628 1.4136 -0.0741 0.1552  0.0919  193 SER F O   
8779  C CB  . SER F 191 ? 1.5661 2.2319 1.4160 -0.0846 0.0993  0.0983  193 SER F CB  
8780  O OG  . SER F 191 ? 1.6616 2.3485 1.5130 -0.1202 0.0952  0.0638  193 SER F OG  
8781  N N   . LEU F 192 ? 1.4494 1.9669 1.2889 -0.1232 0.1498  0.0536  194 LEU F N   
8782  C CA  . LEU F 192 ? 1.4039 1.8827 1.2617 -0.1338 0.1650  0.0341  194 LEU F CA  
8783  C C   . LEU F 192 ? 1.4662 1.8828 1.3068 -0.1361 0.1839  0.0359  194 LEU F C   
8784  O O   . LEU F 192 ? 1.4494 1.8307 1.3036 -0.1340 0.1980  0.0331  194 LEU F O   
8785  C CB  . LEU F 192 ? 1.3678 1.8610 1.2271 -0.1615 0.1603  0.0035  194 LEU F CB  
8786  C CG  . LEU F 192 ? 1.4070 1.9569 1.2851 -0.1685 0.1473  -0.0085 194 LEU F CG  
8787  C CD1 . LEU F 192 ? 1.3945 1.9501 1.2562 -0.1977 0.1474  -0.0358 194 LEU F CD1 
8788  C CD2 . LEU F 192 ? 1.4185 1.9666 1.3321 -0.1601 0.1539  -0.0130 194 LEU F CD2 
8789  N N   . TYR F 193 ? 1.4528 1.8564 1.2631 -0.1445 0.1857  0.0374  195 TYR F N   
8790  C CA  . TYR F 193 ? 1.4629 1.8148 1.2600 -0.1516 0.2044  0.0342  195 TYR F CA  
8791  C C   . TYR F 193 ? 1.5846 1.9112 1.3487 -0.1418 0.2146  0.0546  195 TYR F C   
8792  O O   . TYR F 193 ? 1.5924 1.8763 1.3467 -0.1491 0.2336  0.0505  195 TYR F O   
8793  C CB  . TYR F 193 ? 1.4451 1.7942 1.2421 -0.1764 0.2045  0.0086  195 TYR F CB  
8794  C CG  . TYR F 193 ? 1.4227 1.7954 1.2398 -0.1861 0.1946  -0.0105 195 TYR F CG  
8795  C CD1 . TYR F 193 ? 1.4273 1.7845 1.2660 -0.1848 0.1983  -0.0179 195 TYR F CD1 
8796  C CD2 . TYR F 193 ? 1.4231 1.8291 1.2321 -0.1985 0.1846  -0.0217 195 TYR F CD2 
8797  C CE1 . TYR F 193 ? 1.4068 1.7779 1.2574 -0.1938 0.1923  -0.0354 195 TYR F CE1 
8798  C CE2 . TYR F 193 ? 1.4071 1.8282 1.2294 -0.2086 0.1806  -0.0404 195 TYR F CE2 
8799  C CZ  . TYR F 193 ? 1.4451 1.8473 1.2877 -0.2051 0.1845  -0.0467 195 TYR F CZ  
8800  O OH  . TYR F 193 ? 1.3954 1.8043 1.2449 -0.2154 0.1836  -0.0654 195 TYR F OH  
8801  N N   . GLN F 194 ? 1.5818 1.9353 1.3272 -0.1261 0.2023  0.0758  196 GLN F N   
8802  C CA  . GLN F 194 ? 1.6385 1.9698 1.3435 -0.1119 0.2089  0.1003  196 GLN F CA  
8803  C C   . GLN F 194 ? 1.7179 2.0177 1.3878 -0.1330 0.2210  0.0900  196 GLN F C   
8804  O O   . GLN F 194 ? 1.7650 2.0559 1.3933 -0.1272 0.2208  0.1068  196 GLN F O   
8805  C CB  . GLN F 194 ? 1.6895 1.9777 1.3917 -0.0860 0.2296  0.1238  196 GLN F CB  
8806  C CG  . GLN F 194 ? 1.9527 2.1758 1.6456 -0.0980 0.2611  0.1140  196 GLN F CG  
8807  C CD  . GLN F 194 ? 2.2437 2.4134 1.9117 -0.0755 0.2878  0.1393  196 GLN F CD  
8808  O OE1 . GLN F 194 ? 2.2181 2.3958 1.8775 -0.0445 0.2836  0.1687  196 GLN F OE1 
8809  N NE2 . GLN F 194 ? 2.1366 2.2508 1.7924 -0.0906 0.3177  0.1282  196 GLN F NE2 
8810  N N   . ASN F 195 ? 1.6424 1.9257 1.3283 -0.1561 0.2318  0.0638  197 ASN F N   
8811  C CA  . ASN F 195 ? 1.6533 1.9101 1.3175 -0.1764 0.2464  0.0509  197 ASN F CA  
8812  C C   . ASN F 195 ? 1.6890 1.9802 1.3456 -0.1943 0.2322  0.0372  197 ASN F C   
8813  O O   . ASN F 195 ? 1.6429 1.9556 1.3279 -0.2063 0.2259  0.0171  197 ASN F O   
8814  C CB  . ASN F 195 ? 1.6293 1.8595 1.3207 -0.1899 0.2641  0.0309  197 ASN F CB  
8815  C CG  . ASN F 195 ? 1.8968 2.0877 1.5880 -0.1791 0.2834  0.0413  197 ASN F CG  
8816  O OD1 . ASN F 195 ? 1.8897 2.0396 1.5548 -0.1817 0.3063  0.0458  197 ASN F OD1 
8817  N ND2 . ASN F 195 ? 1.7320 1.9297 1.4485 -0.1685 0.2784  0.0445  197 ASN F ND2 
8818  N N   . ALA F 196 ? 1.6844 1.9780 1.2972 -0.1959 0.2281  0.0491  198 ALA F N   
8819  C CA  . ALA F 196 ? 1.6863 2.0078 1.2806 -0.2169 0.2181  0.0366  198 ALA F CA  
8820  C C   . ALA F 196 ? 1.7153 2.0178 1.3221 -0.2414 0.2364  0.0093  198 ALA F C   
8821  O O   . ALA F 196 ? 1.6832 2.0105 1.3021 -0.2563 0.2309  -0.0083 198 ALA F O   
8822  C CB  . ALA F 196 ? 1.7614 2.0765 1.2980 -0.2167 0.2146  0.0549  198 ALA F CB  
8823  N N   . ASP F 197 ? 1.6915 1.9504 1.2978 -0.2449 0.2601  0.0054  199 ASP F N   
8824  C CA  . ASP F 197 ? 1.6732 1.9185 1.3015 -0.2637 0.2784  -0.0187 199 ASP F CA  
8825  C C   . ASP F 197 ? 1.6590 1.9027 1.3365 -0.2564 0.2812  -0.0268 199 ASP F C   
8826  O O   . ASP F 197 ? 1.6560 1.8724 1.3423 -0.2573 0.2987  -0.0291 199 ASP F O   
8827  C CB  . ASP F 197 ? 1.7544 1.9598 1.3511 -0.2776 0.3039  -0.0218 199 ASP F CB  
8828  C CG  . ASP F 197 ? 1.9976 2.1992 1.6159 -0.2978 0.3217  -0.0465 199 ASP F CG  
8829  O OD1 . ASP F 197 ? 2.0378 2.2470 1.6348 -0.3131 0.3225  -0.0542 199 ASP F OD1 
8830  O OD2 . ASP F 197 ? 2.0923 2.2854 1.7502 -0.2987 0.3355  -0.0584 199 ASP F OD2 
8831  N N   . ALA F 198 ? 1.5638 1.8367 1.2693 -0.2508 0.2639  -0.0315 200 ALA F N   
8832  C CA  . ALA F 198 ? 1.5144 1.7886 1.2606 -0.2451 0.2619  -0.0389 200 ALA F CA  
8833  C C   . ALA F 198 ? 1.5096 1.7901 1.2830 -0.2562 0.2670  -0.0595 200 ALA F C   
8834  O O   . ALA F 198 ? 1.4977 1.7877 1.2621 -0.2655 0.2680  -0.0681 200 ALA F O   
8835  C CB  . ALA F 198 ? 1.5040 1.8001 1.2603 -0.2324 0.2429  -0.0318 200 ALA F CB  
8836  N N   . TYR F 199 ? 1.4408 1.7156 1.2461 -0.2554 0.2713  -0.0669 201 TYR F N   
8837  C CA  . TYR F 199 ? 1.4164 1.7004 1.2534 -0.2602 0.2742  -0.0829 201 TYR F CA  
8838  C C   . TYR F 199 ? 1.4272 1.7191 1.2911 -0.2528 0.2609  -0.0855 201 TYR F C   
8839  O O   . TYR F 199 ? 1.4264 1.7112 1.2866 -0.2478 0.2553  -0.0772 201 TYR F O   
8840  C CB  . TYR F 199 ? 1.4513 1.7262 1.3028 -0.2698 0.2944  -0.0915 201 TYR F CB  
8841  C CG  . TYR F 199 ? 1.4774 1.7464 1.3476 -0.2712 0.2990  -0.0924 201 TYR F CG  
8842  C CD1 . TYR F 199 ? 1.5348 1.7785 1.3785 -0.2734 0.3108  -0.0832 201 TYR F CD1 
8843  C CD2 . TYR F 199 ? 1.4666 1.7539 1.3774 -0.2716 0.2933  -0.1029 201 TYR F CD2 
8844  C CE1 . TYR F 199 ? 1.5642 1.7974 1.4203 -0.2793 0.3207  -0.0870 201 TYR F CE1 
8845  C CE2 . TYR F 199 ? 1.4882 1.7733 1.4134 -0.2786 0.2982  -0.1067 201 TYR F CE2 
8846  C CZ  . TYR F 199 ? 1.6382 1.8944 1.5356 -0.2842 0.3141  -0.1003 201 TYR F CZ  
8847  O OH  . TYR F 199 ? 1.6729 1.9221 1.5802 -0.2955 0.3245  -0.1069 201 TYR F OH  
8848  N N   . VAL F 200 ? 1.3574 1.6601 1.2455 -0.2517 0.2578  -0.0961 202 VAL F N   
8849  C CA  . VAL F 200 ? 1.3312 1.6397 1.2410 -0.2457 0.2446  -0.0992 202 VAL F CA  
8850  C C   . VAL F 200 ? 1.3730 1.6953 1.3175 -0.2458 0.2486  -0.1086 202 VAL F C   
8851  O O   . VAL F 200 ? 1.3766 1.7020 1.3279 -0.2475 0.2620  -0.1136 202 VAL F O   
8852  C CB  . VAL F 200 ? 1.3639 1.6712 1.2626 -0.2390 0.2323  -0.0995 202 VAL F CB  
8853  C CG1 . VAL F 200 ? 1.3482 1.6515 1.2567 -0.2350 0.2193  -0.0995 202 VAL F CG1 
8854  C CG2 . VAL F 200 ? 1.3691 1.6752 1.2397 -0.2397 0.2303  -0.0929 202 VAL F CG2 
8855  N N   . PHE F 201 ? 1.3139 1.6463 1.2810 -0.2448 0.2382  -0.1110 203 PHE F N   
8856  C CA  . PHE F 201 ? 1.3049 1.6616 1.3111 -0.2425 0.2366  -0.1184 203 PHE F CA  
8857  C C   . PHE F 201 ? 1.3115 1.6778 1.3276 -0.2372 0.2155  -0.1180 203 PHE F C   
8858  O O   . PHE F 201 ? 1.3099 1.6686 1.3150 -0.2458 0.2088  -0.1169 203 PHE F O   
8859  C CB  . PHE F 201 ? 1.3430 1.7125 1.3723 -0.2553 0.2512  -0.1254 203 PHE F CB  
8860  C CG  . PHE F 201 ? 1.3699 1.7766 1.4485 -0.2528 0.2464  -0.1337 203 PHE F CG  
8861  C CD1 . PHE F 201 ? 1.4137 1.8431 1.5128 -0.2616 0.2348  -0.1389 203 PHE F CD1 
8862  C CD2 . PHE F 201 ? 1.4121 1.8334 1.5168 -0.2408 0.2531  -0.1358 203 PHE F CD2 
8863  C CE1 . PHE F 201 ? 1.4277 1.9026 1.5760 -0.2582 0.2256  -0.1457 203 PHE F CE1 
8864  C CE2 . PHE F 201 ? 1.4503 1.9128 1.6066 -0.2333 0.2467  -0.1407 203 PHE F CE2 
8865  C CZ  . PHE F 201 ? 1.4227 1.9161 1.6022 -0.2417 0.2306  -0.1454 203 PHE F CZ  
8866  N N   . VAL F 202 ? 1.2352 1.6141 1.2685 -0.2231 0.2071  -0.1182 204 VAL F N   
8867  C CA  . VAL F 202 ? 1.2209 1.6084 1.2593 -0.2161 0.1852  -0.1163 204 VAL F CA  
8868  C C   . VAL F 202 ? 1.2630 1.6926 1.3490 -0.2086 0.1787  -0.1190 204 VAL F C   
8869  O O   . VAL F 202 ? 1.2617 1.6992 1.3667 -0.1923 0.1859  -0.1172 204 VAL F O   
8870  C CB  . VAL F 202 ? 1.2684 1.6273 1.2752 -0.2031 0.1787  -0.1112 204 VAL F CB  
8871  C CG1 . VAL F 202 ? 1.2762 1.6369 1.2791 -0.1976 0.1561  -0.1082 204 VAL F CG1 
8872  C CG2 . VAL F 202 ? 1.2615 1.5902 1.2308 -0.2115 0.1854  -0.1102 204 VAL F CG2 
8873  N N   . GLY F 203 ? 1.2142 1.6715 1.3201 -0.2217 0.1675  -0.1241 205 GLY F N   
8874  C CA  . GLY F 203 ? 1.2147 1.7251 1.3724 -0.2183 0.1583  -0.1286 205 GLY F CA  
8875  C C   . GLY F 203 ? 1.2826 1.8181 1.4453 -0.2142 0.1279  -0.1252 205 GLY F C   
8876  O O   . GLY F 203 ? 1.2966 1.8281 1.4394 -0.2341 0.1175  -0.1294 205 GLY F O   
8877  N N   . SER F 204 ? 1.2249 1.7848 1.4124 -0.1880 0.1151  -0.1170 206 SER F N   
8878  C CA  . SER F 204 ? 1.2235 1.8139 1.4193 -0.1761 0.0833  -0.1098 206 SER F CA  
8879  C C   . SER F 204 ? 1.2663 1.9234 1.5322 -0.1597 0.0797  -0.1096 206 SER F C   
8880  O O   . SER F 204 ? 1.2470 1.9122 1.5453 -0.1591 0.1055  -0.1158 206 SER F O   
8881  C CB  . SER F 204 ? 1.2583 1.8020 1.4101 -0.1515 0.0766  -0.0955 206 SER F CB  
8882  O OG  . SER F 204 ? 1.3204 1.8901 1.4794 -0.1310 0.0481  -0.0842 206 SER F OG  
8883  N N   . SER F 205 ? 1.2437 1.9498 1.5339 -0.1467 0.0486  -0.1026 207 SER F N   
8884  C CA  . SER F 205 ? 1.2487 2.0257 1.6136 -0.1264 0.0444  -0.1006 207 SER F CA  
8885  C C   . SER F 205 ? 1.3296 2.0799 1.7009 -0.0863 0.0616  -0.0852 207 SER F C   
8886  O O   . SER F 205 ? 1.3150 2.0930 1.7406 -0.0753 0.0830  -0.0882 207 SER F O   
8887  C CB  . SER F 205 ? 1.3144 2.1591 1.7047 -0.1222 0.0031  -0.0957 207 SER F CB  
8888  O OG  . SER F 205 ? 1.4359 2.3164 1.8337 -0.1640 -0.0054 -0.1149 207 SER F OG  
8889  N N   . ARG F 206 ? 1.3223 2.0117 1.6343 -0.0679 0.0580  -0.0709 208 ARG F N   
8890  C CA  . ARG F 206 ? 1.3381 1.9880 1.6422 -0.0332 0.0794  -0.0575 208 ARG F CA  
8891  C C   . ARG F 206 ? 1.3585 1.9435 1.6260 -0.0472 0.1181  -0.0666 208 ARG F C   
8892  O O   . ARG F 206 ? 1.3604 1.9305 1.6442 -0.0306 0.1473  -0.0643 208 ARG F O   
8893  C CB  . ARG F 206 ? 1.3864 2.0048 1.6464 -0.0036 0.0588  -0.0375 208 ARG F CB  
8894  C CG  . ARG F 206 ? 1.5328 2.0935 1.7148 -0.0230 0.0466  -0.0393 208 ARG F CG  
8895  C CD  . ARG F 206 ? 1.6666 2.1703 1.7954 0.0077  0.0445  -0.0216 208 ARG F CD  
8896  N NE  . ARG F 206 ? 1.7354 2.2748 1.8708 0.0325  0.0074  -0.0038 208 ARG F NE  
8897  C CZ  . ARG F 206 ? 1.8909 2.3860 1.9813 0.0642  0.0015  0.0152  208 ARG F CZ  
8898  N NH1 . ARG F 206 ? 1.7503 2.1623 1.7867 0.0723  0.0333  0.0161  208 ARG F NH1 
8899  N NH2 . ARG F 206 ? 1.6893 2.2227 1.7854 0.0870  -0.0358 0.0331  208 ARG F NH2 
8900  N N   . TYR F 207 ? 1.2854 1.8349 1.5053 -0.0780 0.1190  -0.0767 209 TYR F N   
8901  C CA  . TYR F 207 ? 1.2646 1.7614 1.4482 -0.0930 0.1494  -0.0845 209 TYR F CA  
8902  C C   . TYR F 207 ? 1.2707 1.7855 1.4747 -0.1217 0.1639  -0.0990 209 TYR F C   
8903  O O   . TYR F 207 ? 1.2430 1.7857 1.4576 -0.1416 0.1488  -0.1057 209 TYR F O   
8904  C CB  . TYR F 207 ? 1.2833 1.7256 1.3989 -0.1032 0.1427  -0.0837 209 TYR F CB  
8905  C CG  . TYR F 207 ? 1.2931 1.6871 1.3711 -0.1144 0.1705  -0.0900 209 TYR F CG  
8906  C CD1 . TYR F 207 ? 1.2935 1.6851 1.3631 -0.1409 0.1788  -0.0996 209 TYR F CD1 
8907  C CD2 . TYR F 207 ? 1.3234 1.6744 1.3715 -0.0991 0.1891  -0.0864 209 TYR F CD2 
8908  C CE1 . TYR F 207 ? 1.2983 1.6552 1.3353 -0.1509 0.2004  -0.1043 209 TYR F CE1 
8909  C CE2 . TYR F 207 ? 1.3300 1.6445 1.3441 -0.1136 0.2135  -0.0945 209 TYR F CE2 
8910  C CZ  . TYR F 207 ? 1.3910 1.7129 1.4013 -0.1391 0.2165  -0.1029 209 TYR F CZ  
8911  O OH  . TYR F 207 ? 1.4054 1.6996 1.3829 -0.1531 0.2364  -0.1098 209 TYR F OH  
8912  N N   . SER F 208 ? 1.2242 1.7157 1.4251 -0.1261 0.1955  -0.1043 210 SER F N   
8913  C CA  . SER F 208 ? 1.2058 1.7005 1.4127 -0.1522 0.2133  -0.1163 210 SER F CA  
8914  C C   . SER F 208 ? 1.2686 1.7192 1.4427 -0.1577 0.2431  -0.1190 210 SER F C   
8915  O O   . SER F 208 ? 1.2834 1.7295 1.4751 -0.1465 0.2662  -0.1193 210 SER F O   
8916  C CB  . SER F 208 ? 1.2376 1.7864 1.5095 -0.1554 0.2183  -0.1242 210 SER F CB  
8917  O OG  . SER F 208 ? 1.3099 1.8942 1.5962 -0.1715 0.1961  -0.1296 210 SER F OG  
8918  N N   . LYS F 209 ? 1.1163 1.5740 1.4524 -0.0602 0.3497  -0.0111 211 LYS F N   
8919  C CA  . LYS F 209 ? 1.1474 1.5924 1.4333 -0.0642 0.3611  -0.0231 211 LYS F CA  
8920  C C   . LYS F 209 ? 1.2184 1.6617 1.4736 -0.0833 0.3509  -0.0067 211 LYS F C   
8921  O O   . LYS F 209 ? 1.1879 1.6187 1.4530 -0.0896 0.3298  0.0069  211 LYS F O   
8922  C CB  . LYS F 209 ? 1.1863 1.5952 1.4495 -0.0546 0.3555  -0.0437 211 LYS F CB  
8923  C CG  . LYS F 209 ? 1.4290 1.8341 1.6604 -0.0512 0.3798  -0.0674 211 LYS F CG  
8924  C CD  . LYS F 209 ? 1.5545 1.9206 1.7502 -0.0522 0.3715  -0.0864 211 LYS F CD  
8925  C CE  . LYS F 209 ? 1.6867 2.0500 1.8428 -0.0553 0.3952  -0.1129 211 LYS F CE  
8926  N NZ  . LYS F 209 ? 1.8009 2.1272 1.9202 -0.0621 0.3856  -0.1320 211 LYS F NZ  
8927  N N   . THR F 210 ? 1.2246 1.6814 1.4428 -0.0920 0.3668  -0.0079 212 THR F N   
8928  C CA  . THR F 210 ? 1.2395 1.6998 1.4256 -0.1094 0.3587  0.0119  212 THR F CA  
8929  C C   . THR F 210 ? 1.3120 1.7545 1.4480 -0.1121 0.3525  -0.0026 212 THR F C   
8930  O O   . THR F 210 ? 1.3374 1.7757 1.4536 -0.1064 0.3669  -0.0292 212 THR F O   
8931  C CB  . THR F 210 ? 1.3924 1.8916 1.5728 -0.1212 0.3804  0.0265  212 THR F CB  
8932  O OG1 . THR F 210 ? 1.3761 1.8980 1.6064 -0.1168 0.3917  0.0316  212 THR F OG1 
8933  C CG2 . THR F 210 ? 1.3977 1.9015 1.5615 -0.1393 0.3685  0.0589  212 THR F CG2 
8934  N N   . PHE F 211 ? 1.2574 1.6898 1.3766 -0.1210 0.3314  0.0143  213 PHE F N   
8935  C CA  . PHE F 211 ? 1.2710 1.6938 1.3475 -0.1265 0.3213  0.0049  213 PHE F CA  
8936  C C   . PHE F 211 ? 1.3125 1.7558 1.3574 -0.1424 0.3140  0.0304  213 PHE F C   
8937  O O   . PHE F 211 ? 1.2919 1.7422 1.3565 -0.1464 0.3076  0.0607  213 PHE F O   
8938  C CB  . PHE F 211 ? 1.2727 1.6666 1.3637 -0.1190 0.2990  0.0005  213 PHE F CB  
8939  C CG  . PHE F 211 ? 1.2813 1.6566 1.4059 -0.1046 0.3006  -0.0158 213 PHE F CG  
8940  C CD1 . PHE F 211 ? 1.3445 1.7052 1.4595 -0.0980 0.3097  -0.0421 213 PHE F CD1 
8941  C CD2 . PHE F 211 ? 1.2875 1.6591 1.4531 -0.0989 0.2918  -0.0042 213 PHE F CD2 
8942  C CE1 . PHE F 211 ? 1.3397 1.6850 1.4884 -0.0841 0.3092  -0.0507 213 PHE F CE1 
8943  C CE2 . PHE F 211 ? 1.3080 1.6691 1.5023 -0.0874 0.2905  -0.0154 213 PHE F CE2 
8944  C CZ  . PHE F 211 ? 1.2962 1.6455 1.4831 -0.0791 0.2987  -0.0358 213 PHE F CZ  
8945  N N   . LYS F 212 ? 1.2866 1.7389 1.2832 -0.1525 0.3134  0.0191  214 LYS F N   
8946  C CA  . LYS F 212 ? 1.3101 1.7882 1.2706 -0.1690 0.3030  0.0438  214 LYS F CA  
8947  C C   . LYS F 212 ? 1.3741 1.8470 1.3033 -0.1752 0.2864  0.0294  214 LYS F C   
8948  O O   . LYS F 212 ? 1.3730 1.8278 1.2907 -0.1729 0.2937  -0.0061 214 LYS F O   
8949  C CB  . LYS F 212 ? 1.3863 1.9005 1.3103 -0.1831 0.3253  0.0462  214 LYS F CB  
8950  C CG  . LYS F 212 ? 1.5729 2.1116 1.5048 -0.1926 0.3215  0.0923  214 LYS F CG  
8951  C CD  . LYS F 212 ? 1.7451 2.3258 1.6391 -0.2085 0.3457  0.0967  214 LYS F CD  
8952  C CE  . LYS F 212 ? 1.8708 2.4743 1.7750 -0.2200 0.3415  0.1478  214 LYS F CE  
8953  N NZ  . LYS F 212 ? 1.9957 2.6455 1.8647 -0.2368 0.3682  0.1534  214 LYS F NZ  
8954  N N   . PRO F 213 ? 1.3411 1.8285 1.2619 -0.1826 0.2632  0.0575  215 PRO F N   
8955  C CA  . PRO F 213 ? 1.3443 1.8328 1.2420 -0.1899 0.2457  0.0451  215 PRO F CA  
8956  C C   . PRO F 213 ? 1.4441 1.9571 1.2797 -0.2118 0.2511  0.0254  215 PRO F C   
8957  O O   . PRO F 213 ? 1.4710 2.0185 1.2727 -0.2260 0.2565  0.0415  215 PRO F O   
8958  C CB  . PRO F 213 ? 1.3532 1.8549 1.2726 -0.1873 0.2204  0.0851  215 PRO F CB  
8959  C CG  . PRO F 213 ? 1.4260 1.9442 1.3518 -0.1892 0.2256  0.1205  215 PRO F CG  
8960  C CD  . PRO F 213 ? 1.3627 1.8657 1.3011 -0.1838 0.2513  0.1034  215 PRO F CD  
8961  N N   . GLU F 214 ? 1.4161 1.9110 1.2355 -0.2166 0.2495  -0.0096 216 GLU F N   
8962  C CA  . GLU F 214 ? 1.4754 1.9850 1.2356 -0.2399 0.2531  -0.0374 216 GLU F CA  
8963  C C   . GLU F 214 ? 1.5133 2.0536 1.2574 -0.2563 0.2221  -0.0161 216 GLU F C   
8964  O O   . GLU F 214 ? 1.4920 2.0181 1.2433 -0.2597 0.2082  -0.0305 216 GLU F O   
8965  C CB  . GLU F 214 ? 1.5088 1.9753 1.2674 -0.2370 0.2672  -0.0860 216 GLU F CB  
8966  C CG  . GLU F 214 ? 1.7232 2.1657 1.4969 -0.2206 0.2990  -0.1092 216 GLU F CG  
8967  C CD  . GLU F 214 ? 2.1592 2.5590 1.9281 -0.2179 0.3148  -0.1563 216 GLU F CD  
8968  O OE1 . GLU F 214 ? 2.2268 2.5950 2.0184 -0.2139 0.3010  -0.1626 216 GLU F OE1 
8969  O OE2 . GLU F 214 ? 2.1002 2.4973 1.8455 -0.2188 0.3426  -0.1862 216 GLU F OE2 
8970  N N   . ILE F 215 ? 1.4744 2.0596 1.2024 -0.2657 0.2105  0.0231  217 ILE F N   
8971  C CA  . ILE F 215 ? 1.4763 2.1010 1.1956 -0.2790 0.1793  0.0524  217 ILE F CA  
8972  C C   . ILE F 215 ? 1.5928 2.2435 1.2478 -0.3112 0.1736  0.0241  217 ILE F C   
8973  O O   . ILE F 215 ? 1.6489 2.3292 1.2488 -0.3311 0.1836  0.0188  217 ILE F O   
8974  C CB  . ILE F 215 ? 1.5119 2.1727 1.2449 -0.2751 0.1665  0.1104  217 ILE F CB  
8975  C CG1 . ILE F 215 ? 1.4571 2.0850 1.2605 -0.2449 0.1669  0.1342  217 ILE F CG1 
8976  C CG2 . ILE F 215 ? 1.5398 2.2518 1.2591 -0.2905 0.1340  0.1426  217 ILE F CG2 
8977  C CD1 . ILE F 215 ? 1.5584 2.1972 1.3763 -0.2394 0.1709  0.1771  217 ILE F CD1 
8978  N N   . ALA F 216 ? 1.5340 2.1741 1.1957 -0.3183 0.1582  0.0045  218 ALA F N   
8979  C CA  . ALA F 216 ? 1.5813 2.2395 1.1894 -0.3517 0.1490  -0.0262 218 ALA F CA  
8980  C C   . ALA F 216 ? 1.5952 2.2555 1.2319 -0.3565 0.1237  -0.0246 218 ALA F C   
8981  O O   . ALA F 216 ? 1.5377 2.1597 1.2257 -0.3346 0.1266  -0.0277 218 ALA F O   
8982  C CB  . ALA F 216 ? 1.6271 2.2410 1.2013 -0.3589 0.1790  -0.0850 218 ALA F CB  
8983  N N   . ILE F 217 ? 1.5833 2.2932 1.1854 -0.3875 0.0990  -0.0199 219 ILE F N   
8984  C CA  . ILE F 217 ? 1.5577 2.2806 1.1836 -0.3984 0.0744  -0.0191 219 ILE F CA  
8985  C C   . ILE F 217 ? 1.6105 2.2811 1.2165 -0.4149 0.0884  -0.0766 219 ILE F C   
8986  O O   . ILE F 217 ? 1.6673 2.3332 1.2128 -0.4432 0.0974  -0.1148 219 ILE F O   
8987  C CB  . ILE F 217 ? 1.6316 2.4348 1.2337 -0.4265 0.0401  0.0117  219 ILE F CB  
8988  C CG1 . ILE F 217 ? 1.5974 2.4441 1.2476 -0.4012 0.0222  0.0768  219 ILE F CG1 
8989  C CG2 . ILE F 217 ? 1.6521 2.4701 1.2594 -0.4520 0.0188  -0.0050 219 ILE F CG2 
8990  C CD1 . ILE F 217 ? 1.7370 2.6691 1.3625 -0.4247 -0.0104 0.1176  219 ILE F CD1 
8991  N N   . ARG F 218 ? 1.5110 2.1403 1.1678 -0.3970 0.0916  -0.0825 220 ARG F N   
8992  C CA  . ARG F 218 ? 1.5261 2.0990 1.1771 -0.4085 0.1037  -0.1287 220 ARG F CA  
8993  C C   . ARG F 218 ? 1.5722 2.1655 1.2423 -0.4302 0.0783  -0.1251 220 ARG F C   
8994  O O   . ARG F 218 ? 1.5331 2.1841 1.2308 -0.4275 0.0544  -0.0847 220 ARG F O   
8995  C CB  . ARG F 218 ? 1.4715 1.9810 1.1631 -0.3730 0.1292  -0.1372 220 ARG F CB  
8996  C CG  . ARG F 218 ? 1.5841 2.0655 1.2481 -0.3624 0.1588  -0.1593 220 ARG F CG  
8997  C CD  . ARG F 218 ? 1.6056 2.0539 1.3177 -0.3237 0.1767  -0.1466 220 ARG F CD  
8998  N NE  . ARG F 218 ? 1.6614 2.1476 1.4026 -0.3048 0.1662  -0.0998 220 ARG F NE  
8999  C CZ  . ARG F 218 ? 1.8288 2.3218 1.5703 -0.2894 0.1802  -0.0850 220 ARG F CZ  
9000  N NH1 . ARG F 218 ? 1.6865 2.1584 1.4014 -0.2891 0.2066  -0.1131 220 ARG F NH1 
9001  N NH2 . ARG F 218 ? 1.6092 2.1300 1.3807 -0.2743 0.1690  -0.0420 220 ARG F NH2 
9002  N N   . PRO F 219 ? 1.5644 2.1151 1.2227 -0.4531 0.0824  -0.1647 221 PRO F N   
9003  C CA  . PRO F 219 ? 1.5574 2.1332 1.2367 -0.4768 0.0582  -0.1578 221 PRO F CA  
9004  C C   . PRO F 219 ? 1.5130 2.0983 1.2619 -0.4469 0.0524  -0.1214 221 PRO F C   
9005  O O   . PRO F 219 ? 1.4747 2.0177 1.2529 -0.4128 0.0716  -0.1181 221 PRO F O   
9006  C CB  . PRO F 219 ? 1.6335 2.1430 1.2912 -0.5014 0.0707  -0.2076 221 PRO F CB  
9007  C CG  . PRO F 219 ? 1.6901 2.1314 1.3450 -0.4727 0.1037  -0.2305 221 PRO F CG  
9008  C CD  . PRO F 219 ? 1.6299 2.1072 1.2614 -0.4575 0.1097  -0.2151 221 PRO F CD  
9009  N N   . LYS F 220 ? 1.4244 2.0699 1.1999 -0.4600 0.0265  -0.0948 222 LYS F N   
9010  C CA  . LYS F 220 ? 1.3442 2.0087 1.1848 -0.4331 0.0220  -0.0621 222 LYS F CA  
9011  C C   . LYS F 220 ? 1.3518 1.9612 1.2175 -0.4309 0.0352  -0.0800 222 LYS F C   
9012  O O   . LYS F 220 ? 1.3674 1.9907 1.2452 -0.4569 0.0236  -0.0832 222 LYS F O   
9013  C CB  . LYS F 220 ? 1.3736 2.1249 1.2401 -0.4455 -0.0075 -0.0279 222 LYS F CB  
9014  C CG  . LYS F 220 ? 1.5851 2.3862 1.4746 -0.4160 -0.0158 0.0146  222 LYS F CG  
9015  C CD  . LYS F 220 ? 1.7102 2.5926 1.6483 -0.4158 -0.0409 0.0528  222 LYS F CD  
9016  C CE  . LYS F 220 ? 1.8531 2.7823 1.8180 -0.3861 -0.0506 0.0977  222 LYS F CE  
9017  N NZ  . LYS F 220 ? 1.8984 2.7878 1.9061 -0.3392 -0.0299 0.1092  222 LYS F NZ  
9018  N N   . VAL F 221 ? 1.2612 1.8107 1.1351 -0.4014 0.0590  -0.0893 223 VAL F N   
9019  C CA  . VAL F 221 ? 1.2281 1.7244 1.1272 -0.3931 0.0726  -0.0998 223 VAL F CA  
9020  C C   . VAL F 221 ? 1.1972 1.7249 1.1489 -0.3626 0.0707  -0.0663 223 VAL F C   
9021  O O   . VAL F 221 ? 1.1576 1.6909 1.1216 -0.3320 0.0771  -0.0510 223 VAL F O   
9022  C CB  . VAL F 221 ? 1.2856 1.7078 1.1668 -0.3778 0.0976  -0.1263 223 VAL F CB  
9023  C CG1 . VAL F 221 ? 1.2575 1.6330 1.1713 -0.3640 0.1088  -0.1265 223 VAL F CG1 
9024  C CG2 . VAL F 221 ? 1.3564 1.7460 1.1863 -0.4079 0.1026  -0.1651 223 VAL F CG2 
9025  N N   . ARG F 222 ? 1.1392 1.6920 1.1215 -0.3736 0.0617  -0.0553 224 ARG F N   
9026  C CA  . ARG F 222 ? 1.0829 1.6754 1.1150 -0.3490 0.0603  -0.0271 224 ARG F CA  
9027  C C   . ARG F 222 ? 1.1040 1.7595 1.1503 -0.3350 0.0473  -0.0010 224 ARG F C   
9028  O O   . ARG F 222 ? 1.0539 1.7195 1.1300 -0.3013 0.0531  0.0171  224 ARG F O   
9029  C CB  . ARG F 222 ? 1.0553 1.6023 1.1062 -0.3178 0.0800  -0.0279 224 ARG F CB  
9030  C CG  . ARG F 222 ? 1.1916 1.6964 1.2434 -0.3328 0.0874  -0.0403 224 ARG F CG  
9031  C CD  . ARG F 222 ? 1.2195 1.6962 1.2931 -0.3058 0.1022  -0.0349 224 ARG F CD  
9032  N NE  . ARG F 222 ? 1.2800 1.8071 1.3903 -0.2868 0.1014  -0.0140 224 ARG F NE  
9033  C CZ  . ARG F 222 ? 1.4984 2.0613 1.6328 -0.2975 0.0985  -0.0030 224 ARG F CZ  
9034  N NH1 . ARG F 222 ? 1.3684 1.9211 1.4948 -0.3298 0.0942  -0.0075 224 ARG F NH1 
9035  N NH2 . ARG F 222 ? 1.3377 1.9467 1.5055 -0.2768 0.1014  0.0118  224 ARG F NH2 
9036  N N   . ASP F 223 ? 1.1097 1.8047 1.1320 -0.3639 0.0286  -0.0001 225 ASP F N   
9037  C CA  . ASP F 223 ? 1.1248 1.8850 1.1510 -0.3619 0.0102  0.0262  225 ASP F CA  
9038  C C   . ASP F 223 ? 1.1514 1.8994 1.1793 -0.3269 0.0189  0.0413  225 ASP F C   
9039  O O   . ASP F 223 ? 1.1296 1.9244 1.1907 -0.3064 0.0094  0.0738  225 ASP F O   
9040  C CB  . ASP F 223 ? 1.1425 1.9791 1.2198 -0.3619 -0.0067 0.0549  225 ASP F CB  
9041  C CG  . ASP F 223 ? 1.4424 2.3295 1.5038 -0.4074 -0.0301 0.0526  225 ASP F CG  
9042  O OD1 . ASP F 223 ? 1.5007 2.3603 1.5469 -0.4382 -0.0278 0.0279  225 ASP F OD1 
9043  O OD2 . ASP F 223 ? 1.5581 2.5123 1.6231 -0.4138 -0.0519 0.0770  225 ASP F OD2 
9044  N N   . ARG F 224 ? 1.1071 1.7921 1.1011 -0.3215 0.0373  0.0182  226 ARG F N   
9045  C CA  . ARG F 224 ? 1.0840 1.7507 1.0733 -0.2950 0.0479  0.0283  226 ARG F CA  
9046  C C   . ARG F 224 ? 1.1862 1.8341 1.1164 -0.3148 0.0524  0.0083  226 ARG F C   
9047  O O   . ARG F 224 ? 1.2034 1.8056 1.1030 -0.3309 0.0643  -0.0266 226 ARG F O   
9048  C CB  . ARG F 224 ? 1.0093 1.6237 1.0242 -0.2648 0.0694  0.0212  226 ARG F CB  
9049  C CG  . ARG F 224 ? 0.9929 1.6302 1.0636 -0.2373 0.0682  0.0445  226 ARG F CG  
9050  C CD  . ARG F 224 ? 1.0940 1.7571 1.1861 -0.2142 0.0631  0.0750  226 ARG F CD  
9051  N NE  . ARG F 224 ? 1.1946 1.9037 1.3391 -0.1979 0.0539  0.0991  226 ARG F NE  
9052  C CZ  . ARG F 224 ? 1.4391 2.2110 1.5972 -0.2072 0.0336  0.1224  226 ARG F CZ  
9053  N NH1 . ARG F 224 ? 1.3720 2.1688 1.4894 -0.2360 0.0182  0.1245  226 ARG F NH1 
9054  N NH2 . ARG F 224 ? 1.2578 2.0713 1.4711 -0.1878 0.0286  0.1432  226 ARG F NH2 
9055  N N   . GLU F 225 ? 1.1661 1.8504 1.0806 -0.3137 0.0434  0.0311  227 GLU F N   
9056  C CA  . GLU F 225 ? 1.2178 1.8960 1.0726 -0.3328 0.0486  0.0150  227 GLU F CA  
9057  C C   . GLU F 225 ? 1.2613 1.8840 1.1083 -0.3114 0.0761  0.0007  227 GLU F C   
9058  O O   . GLU F 225 ? 1.3010 1.8951 1.1033 -0.3257 0.0909  -0.0311 227 GLU F O   
9059  C CB  . GLU F 225 ? 1.2628 2.0081 1.1021 -0.3424 0.0272  0.0499  227 GLU F CB  
9060  C CG  . GLU F 225 ? 1.4365 2.2440 1.2735 -0.3716 -0.0015 0.0596  227 GLU F CG  
9061  C CD  . GLU F 225 ? 1.8170 2.6751 1.5958 -0.4056 -0.0187 0.0636  227 GLU F CD  
9062  O OE1 . GLU F 225 ? 1.8078 2.7008 1.5815 -0.3959 -0.0260 0.0996  227 GLU F OE1 
9063  O OE2 . GLU F 225 ? 1.7661 2.6297 1.5035 -0.4441 -0.0258 0.0315  227 GLU F OE2 
9064  N N   . GLY F 226 ? 1.1647 1.7740 1.0572 -0.2780 0.0833  0.0222  228 GLY F N   
9065  C CA  . GLY F 226 ? 1.1443 1.7079 1.0397 -0.2572 0.1069  0.0133  228 GLY F CA  
9066  C C   . GLY F 226 ? 1.1483 1.6582 1.0586 -0.2488 0.1230  -0.0160 228 GLY F C   
9067  O O   . GLY F 226 ? 1.1401 1.6453 1.0598 -0.2587 0.1164  -0.0273 228 GLY F O   
9068  N N   . ARG F 227 ? 1.0716 1.5441 0.9858 -0.2319 0.1437  -0.0256 229 ARG F N   
9069  C CA  . ARG F 227 ? 1.0481 1.4725 0.9790 -0.2215 0.1582  -0.0483 229 ARG F CA  
9070  C C   . ARG F 227 ? 1.0689 1.4759 1.0357 -0.1938 0.1689  -0.0361 229 ARG F C   
9071  O O   . ARG F 227 ? 1.0397 1.4631 1.0128 -0.1845 0.1695  -0.0153 229 ARG F O   
9072  C CB  . ARG F 227 ? 1.0844 1.4755 0.9787 -0.2343 0.1749  -0.0839 229 ARG F CB  
9073  C CG  . ARG F 227 ? 1.2082 1.6069 1.0625 -0.2662 0.1663  -0.1049 229 ARG F CG  
9074  C CD  . ARG F 227 ? 1.2143 1.5879 1.0822 -0.2767 0.1602  -0.1186 229 ARG F CD  
9075  N NE  . ARG F 227 ? 1.2892 1.6619 1.1161 -0.3107 0.1546  -0.1447 229 ARG F NE  
9076  C CZ  . ARG F 227 ? 1.3797 1.7975 1.1936 -0.3358 0.1323  -0.1352 229 ARG F CZ  
9077  N NH1 . ARG F 227 ? 1.1857 1.6531 1.0291 -0.3268 0.1147  -0.0986 229 ARG F NH1 
9078  N NH2 . ARG F 227 ? 1.1176 1.5320 0.8916 -0.3702 0.1275  -0.1630 229 ARG F NH2 
9079  N N   . MET F 228 ? 1.0295 1.4041 1.0197 -0.1829 0.1761  -0.0475 230 MET F N   
9080  C CA  . MET F 228 ? 1.0056 1.3645 1.0282 -0.1605 0.1846  -0.0400 230 MET F CA  
9081  C C   . MET F 228 ? 1.1187 1.4404 1.1428 -0.1555 0.1996  -0.0610 230 MET F C   
9082  O O   . MET F 228 ? 1.1324 1.4350 1.1593 -0.1604 0.1976  -0.0720 230 MET F O   
9083  C CB  . MET F 228 ? 0.9958 1.3634 1.0529 -0.1504 0.1742  -0.0266 230 MET F CB  
9084  C CG  . MET F 228 ? 1.0213 1.4087 1.1016 -0.1372 0.1693  -0.0037 230 MET F CG  
9085  S SD  . MET F 228 ? 1.0375 1.4284 1.1583 -0.1223 0.1642  0.0020  230 MET F SD  
9086  C CE  . MET F 228 ? 1.0009 1.4240 1.1413 -0.1141 0.1536  0.0282  230 MET F CE  
9087  N N   . ASN F 229 ? 1.1072 1.4202 1.1335 -0.1456 0.2147  -0.0641 231 ASN F N   
9088  C CA  . ASN F 229 ? 1.1230 1.4053 1.1607 -0.1362 0.2289  -0.0803 231 ASN F CA  
9089  C C   . ASN F 229 ? 1.1550 1.4337 1.2317 -0.1201 0.2254  -0.0675 231 ASN F C   
9090  O O   . ASN F 229 ? 1.1273 1.4232 1.2195 -0.1137 0.2217  -0.0515 231 ASN F O   
9091  C CB  . ASN F 229 ? 1.1638 1.4447 1.1882 -0.1334 0.2487  -0.0918 231 ASN F CB  
9092  C CG  . ASN F 229 ? 1.6437 1.9195 1.6257 -0.1500 0.2564  -0.1151 231 ASN F CG  
9093  O OD1 . ASN F 229 ? 1.6429 1.9042 1.6089 -0.1637 0.2486  -0.1282 231 ASN F OD1 
9094  N ND2 . ASN F 229 ? 1.5714 1.8602 1.5332 -0.1513 0.2729  -0.1223 231 ASN F ND2 
9095  N N   . TYR F 230 ? 1.1136 1.3698 1.2049 -0.1157 0.2253  -0.0736 232 TYR F N   
9096  C CA  . TYR F 230 ? 1.0765 1.3338 1.1991 -0.1039 0.2202  -0.0622 232 TYR F CA  
9097  C C   . TYR F 230 ? 1.0981 1.3435 1.2416 -0.0905 0.2320  -0.0652 232 TYR F C   
9098  O O   . TYR F 230 ? 1.1049 1.3261 1.2492 -0.0879 0.2394  -0.0755 232 TYR F O   
9099  C CB  . TYR F 230 ? 1.0929 1.3444 1.2184 -0.1100 0.2087  -0.0592 232 TYR F CB  
9100  C CG  . TYR F 230 ? 1.1248 1.3938 1.2342 -0.1235 0.1984  -0.0567 232 TYR F CG  
9101  C CD1 . TYR F 230 ? 1.1328 1.4288 1.2513 -0.1201 0.1910  -0.0449 232 TYR F CD1 
9102  C CD2 . TYR F 230 ? 1.1623 1.4216 1.2505 -0.1398 0.1961  -0.0664 232 TYR F CD2 
9103  C CE1 . TYR F 230 ? 1.1479 1.4663 1.2588 -0.1296 0.1815  -0.0398 232 TYR F CE1 
9104  C CE2 . TYR F 230 ? 1.1732 1.4572 1.2504 -0.1536 0.1849  -0.0620 232 TYR F CE2 
9105  C CZ  . TYR F 230 ? 1.2152 1.5315 1.3058 -0.1469 0.1776  -0.0471 232 TYR F CZ  
9106  O OH  . TYR F 230 ? 1.1645 1.5110 1.2514 -0.1574 0.1665  -0.0399 232 TYR F OH  
9107  N N   . TYR F 231 ? 1.0278 1.2905 1.1917 -0.0822 0.2340  -0.0557 233 TYR F N   
9108  C CA  . TYR F 231 ? 1.0274 1.2910 1.2183 -0.0696 0.2438  -0.0548 233 TYR F CA  
9109  C C   . TYR F 231 ? 1.0451 1.3183 1.2641 -0.0643 0.2322  -0.0426 233 TYR F C   
9110  O O   . TYR F 231 ? 1.0274 1.3107 1.2447 -0.0700 0.2203  -0.0365 233 TYR F O   
9111  C CB  . TYR F 231 ? 1.0512 1.3329 1.2444 -0.0684 0.2563  -0.0533 233 TYR F CB  
9112  C CG  . TYR F 231 ? 1.1181 1.3976 1.2791 -0.0753 0.2693  -0.0654 233 TYR F CG  
9113  C CD1 . TYR F 231 ? 1.1485 1.4367 1.2804 -0.0882 0.2620  -0.0614 233 TYR F CD1 
9114  C CD2 . TYR F 231 ? 1.1611 1.4344 1.3216 -0.0685 0.2894  -0.0805 233 TYR F CD2 
9115  C CE1 . TYR F 231 ? 1.1905 1.4833 1.2879 -0.0978 0.2718  -0.0714 233 TYR F CE1 
9116  C CE2 . TYR F 231 ? 1.2096 1.4843 1.3345 -0.0773 0.3028  -0.0954 233 TYR F CE2 
9117  C CZ  . TYR F 231 ? 1.3082 1.5938 1.3986 -0.0938 0.2927  -0.0904 233 TYR F CZ  
9118  O OH  . TYR F 231 ? 1.3767 1.6695 1.4269 -0.1058 0.3035  -0.1041 233 TYR F OH  
9119  N N   . TRP F 232 ? 0.9920 1.2644 1.2376 -0.0532 0.2360  -0.0394 234 TRP F N   
9120  C CA  . TRP F 232 ? 0.9668 1.2543 1.2373 -0.0502 0.2232  -0.0264 234 TRP F CA  
9121  C C   . TRP F 232 ? 1.0379 1.3430 1.3454 -0.0383 0.2290  -0.0194 234 TRP F C   
9122  O O   . TRP F 232 ? 1.0629 1.3600 1.3819 -0.0270 0.2446  -0.0248 234 TRP F O   
9123  C CB  . TRP F 232 ? 0.9485 1.2214 1.2139 -0.0517 0.2126  -0.0210 234 TRP F CB  
9124  C CG  . TRP F 232 ? 0.9780 1.2280 1.2575 -0.0406 0.2201  -0.0202 234 TRP F CG  
9125  C CD1 . TRP F 232 ? 1.0438 1.2613 1.3076 -0.0410 0.2310  -0.0336 234 TRP F CD1 
9126  C CD2 . TRP F 232 ? 0.9798 1.2367 1.2953 -0.0270 0.2176  -0.0055 234 TRP F CD2 
9127  N NE1 . TRP F 232 ? 1.0616 1.2586 1.3508 -0.0268 0.2373  -0.0300 234 TRP F NE1 
9128  C CE2 . TRP F 232 ? 1.0644 1.2871 1.3881 -0.0164 0.2290  -0.0103 234 TRP F CE2 
9129  C CE3 . TRP F 232 ? 0.9738 1.2642 1.3170 -0.0233 0.2061  0.0114  234 TRP F CE3 
9130  C CZ2 . TRP F 232 ? 1.0729 1.2923 1.4362 0.0014  0.2295  0.0047  234 TRP F CZ2 
9131  C CZ3 . TRP F 232 ? 1.0058 1.3003 1.3856 -0.0082 0.2041  0.0280  234 TRP F CZ3 
9132  C CH2 . TRP F 232 ? 1.0485 1.3072 1.4407 0.0060  0.2161  0.0261  234 TRP F CH2 
9133  N N   . THR F 233 ? 0.9771 1.3082 1.3048 -0.0412 0.2165  -0.0085 235 THR F N   
9134  C CA  . THR F 233 ? 0.9761 1.3345 1.3441 -0.0327 0.2167  0.0022  235 THR F CA  
9135  C C   . THR F 233 ? 1.0193 1.4018 1.3994 -0.0395 0.1956  0.0148  235 THR F C   
9136  O O   . THR F 233 ? 1.0082 1.3885 1.3642 -0.0522 0.1841  0.0111  235 THR F O   
9137  C CB  . THR F 233 ? 1.0817 1.4599 1.4649 -0.0338 0.2299  -0.0005 235 THR F CB  
9138  O OG1 . THR F 233 ? 1.0548 1.4617 1.4825 -0.0225 0.2331  0.0102  235 THR F OG1 
9139  C CG2 . THR F 233 ? 1.0707 1.4607 1.4471 -0.0507 0.2206  -0.0004 235 THR F CG2 
9140  N N   . LEU F 234 ? 0.9820 1.3918 1.4005 -0.0309 0.1912  0.0292  236 LEU F N   
9141  C CA  . LEU F 234 ? 0.9729 1.4158 1.4053 -0.0390 0.1698  0.0433  236 LEU F CA  
9142  C C   . LEU F 234 ? 1.0154 1.4948 1.4752 -0.0471 0.1684  0.0440  236 LEU F C   
9143  O O   . LEU F 234 ? 1.0250 1.5147 1.5126 -0.0376 0.1836  0.0450  236 LEU F O   
9144  C CB  . LEU F 234 ? 0.9857 1.4381 1.4459 -0.0241 0.1620  0.0655  236 LEU F CB  
9145  C CG  . LEU F 234 ? 1.0592 1.4696 1.5033 -0.0140 0.1674  0.0673  236 LEU F CG  
9146  C CD1 . LEU F 234 ? 1.0829 1.4974 1.5684 0.0062  0.1650  0.0907  236 LEU F CD1 
9147  C CD2 . LEU F 234 ? 1.0810 1.4799 1.4835 -0.0306 0.1544  0.0661  236 LEU F CD2 
9148  N N   . VAL F 235 ? 0.9427 1.4411 1.3933 -0.0665 0.1519  0.0412  237 VAL F N   
9149  C CA  . VAL F 235 ? 0.9243 1.4553 1.4000 -0.0801 0.1477  0.0407  237 VAL F CA  
9150  C C   . VAL F 235 ? 1.0026 1.5790 1.4995 -0.0876 0.1249  0.0560  237 VAL F C   
9151  O O   . VAL F 235 ? 1.0142 1.5935 1.4848 -0.0979 0.1086  0.0551  237 VAL F O   
9152  C CB  . VAL F 235 ? 0.9560 1.4672 1.4061 -0.0992 0.1492  0.0213  237 VAL F CB  
9153  C CG1 . VAL F 235 ? 0.9522 1.4939 1.4291 -0.1181 0.1421  0.0209  237 VAL F CG1 
9154  C CG2 . VAL F 235 ? 0.9490 1.4242 1.3829 -0.0912 0.1699  0.0132  237 VAL F CG2 
9155  N N   . GLU F 236 ? 0.9703 1.5875 1.5155 -0.0821 0.1241  0.0717  238 GLU F N   
9156  C CA  . GLU F 236 ? 0.9826 1.6544 1.5568 -0.0889 0.1006  0.0913  238 GLU F CA  
9157  C C   . GLU F 236 ? 1.0491 1.7405 1.6068 -0.1223 0.0835  0.0767  238 GLU F C   
9158  O O   . GLU F 236 ? 1.0391 1.7079 1.5865 -0.1350 0.0943  0.0571  238 GLU F O   
9159  C CB  . GLU F 236 ? 0.9987 1.7134 1.6366 -0.0738 0.1075  0.1105  238 GLU F CB  
9160  C CG  . GLU F 236 ? 1.1153 1.8069 1.7736 -0.0398 0.1300  0.1180  238 GLU F CG  
9161  C CD  . GLU F 236 ? 1.3071 1.9910 1.9825 -0.0312 0.1593  0.1062  238 GLU F CD  
9162  O OE1 . GLU F 236 ? 1.2994 2.0127 2.0262 -0.0103 0.1718  0.1189  238 GLU F OE1 
9163  O OE2 . GLU F 236 ? 1.1606 1.8114 1.7991 -0.0444 0.1705  0.0858  238 GLU F OE2 
9164  N N   . PRO F 237 ? 1.0351 1.7660 1.5882 -0.1384 0.0570  0.0851  239 PRO F N   
9165  C CA  . PRO F 237 ? 1.0486 1.7956 1.5837 -0.1727 0.0420  0.0651  239 PRO F CA  
9166  C C   . PRO F 237 ? 1.0860 1.8568 1.6607 -0.1877 0.0448  0.0619  239 PRO F C   
9167  O O   . PRO F 237 ? 1.0697 1.8850 1.6961 -0.1783 0.0436  0.0852  239 PRO F O   
9168  C CB  . PRO F 237 ? 1.0941 1.8931 1.6240 -0.1849 0.0127  0.0814  239 PRO F CB  
9169  C CG  . PRO F 237 ? 1.1484 1.9727 1.7187 -0.1563 0.0108  0.1187  239 PRO F CG  
9170  C CD  . PRO F 237 ? 1.0753 1.8392 1.6392 -0.1278 0.0390  0.1141  239 PRO F CD  
9171  N N   . GLY F 238 ? 1.0504 1.7901 1.6039 -0.2096 0.0501  0.0344  240 GLY F N   
9172  C CA  . GLY F 238 ? 1.0489 1.8017 1.6353 -0.2296 0.0535  0.0298  240 GLY F CA  
9173  C C   . GLY F 238 ? 1.0652 1.7787 1.6612 -0.2161 0.0816  0.0287  240 GLY F C   
9174  O O   . GLY F 238 ? 1.0750 1.7750 1.6798 -0.2362 0.0874  0.0187  240 GLY F O   
9175  N N   . ASP F 239 ? 0.9803 1.6751 1.5734 -0.1839 0.0990  0.0397  241 ASP F N   
9176  C CA  . ASP F 239 ? 0.9543 1.6170 1.5495 -0.1690 0.1261  0.0399  241 ASP F CA  
9177  C C   . ASP F 239 ? 0.9900 1.5910 1.5406 -0.1746 0.1346  0.0193  241 ASP F C   
9178  O O   . ASP F 239 ? 0.9954 1.5723 1.5098 -0.1770 0.1250  0.0051  241 ASP F O   
9179  C CB  . ASP F 239 ? 0.9610 1.6246 1.5645 -0.1351 0.1398  0.0539  241 ASP F CB  
9180  C CG  . ASP F 239 ? 1.0747 1.7153 1.6791 -0.1193 0.1685  0.0535  241 ASP F CG  
9181  O OD1 . ASP F 239 ? 1.0760 1.7185 1.6907 -0.1335 0.1788  0.0522  241 ASP F OD1 
9182  O OD2 . ASP F 239 ? 1.1844 1.8067 1.7792 -0.0946 0.1806  0.0550  241 ASP F OD2 
9183  N N   . LYS F 240 ? 0.9342 1.5145 1.4901 -0.1765 0.1529  0.0200  242 LYS F N   
9184  C CA  . LYS F 240 ? 0.9400 1.4661 1.4637 -0.1802 0.1614  0.0074  242 LYS F CA  
9185  C C   . LYS F 240 ? 0.9743 1.4753 1.4783 -0.1573 0.1813  0.0127  242 LYS F C   
9186  O O   . LYS F 240 ? 0.9724 1.4923 1.4950 -0.1488 0.1971  0.0253  242 LYS F O   
9187  C CB  . LYS F 240 ? 0.9944 1.5138 1.5376 -0.2058 0.1632  0.0070  242 LYS F CB  
9188  C CG  . LYS F 240 ? 1.1524 1.6153 1.6712 -0.2083 0.1716  -0.0004 242 LYS F CG  
9189  C CD  . LYS F 240 ? 1.2588 1.7189 1.8016 -0.2230 0.1834  0.0147  242 LYS F CD  
9190  C CE  . LYS F 240 ? 1.4569 1.8920 2.0118 -0.2519 0.1736  0.0044  242 LYS F CE  
9191  N NZ  . LYS F 240 ? 1.6118 2.0466 2.1943 -0.2696 0.1843  0.0240  242 LYS F NZ  
9192  N N   . ILE F 241 ? 0.9178 1.3795 1.3842 -0.1493 0.1812  0.0018  243 ILE F N   
9193  C CA  . ILE F 241 ? 0.9078 1.3456 1.3506 -0.1324 0.1964  0.0046  243 ILE F CA  
9194  C C   . ILE F 241 ? 0.9840 1.3881 1.4137 -0.1407 0.2018  0.0039  243 ILE F C   
9195  O O   . ILE F 241 ? 0.9914 1.3702 1.4094 -0.1468 0.1927  -0.0077 243 ILE F O   
9196  C CB  . ILE F 241 ? 0.9336 1.3600 1.3495 -0.1160 0.1927  -0.0015 243 ILE F CB  
9197  C CG1 . ILE F 241 ? 0.9353 1.3393 1.3264 -0.1027 0.2076  -0.0004 243 ILE F CG1 
9198  C CG2 . ILE F 241 ? 0.9402 1.3528 1.3362 -0.1229 0.1774  -0.0152 243 ILE F CG2 
9199  C CD1 . ILE F 241 ? 1.0020 1.3963 1.3725 -0.0887 0.2065  -0.0045 243 ILE F CD1 
9200  N N   . THR F 242 ? 0.9451 1.3519 1.3797 -0.1409 0.2170  0.0176  244 THR F N   
9201  C CA  . THR F 242 ? 0.9574 1.3372 1.3839 -0.1485 0.2223  0.0259  244 THR F CA  
9202  C C   . THR F 242 ? 1.0313 1.3949 1.4238 -0.1338 0.2295  0.0284  244 THR F C   
9203  O O   . THR F 242 ? 1.0171 1.3948 1.3967 -0.1216 0.2373  0.0262  244 THR F O   
9204  C CB  . THR F 242 ? 0.9658 1.3657 1.4194 -0.1636 0.2326  0.0435  244 THR F CB  
9205  O OG1 . THR F 242 ? 0.9490 1.3668 1.4352 -0.1799 0.2226  0.0395  244 THR F OG1 
9206  C CG2 . THR F 242 ? 0.9389 1.3107 1.3879 -0.1735 0.2368  0.0589  244 THR F CG2 
9207  N N   . PHE F 243 ? 1.0241 1.3579 1.4045 -0.1351 0.2262  0.0325  245 PHE F N   
9208  C CA  . PHE F 243 ? 1.0340 1.3570 1.3845 -0.1243 0.2294  0.0376  245 PHE F CA  
9209  C C   . PHE F 243 ? 1.1109 1.4229 1.4612 -0.1311 0.2337  0.0604  245 PHE F C   
9210  O O   . PHE F 243 ? 1.1207 1.4054 1.4784 -0.1315 0.2260  0.0646  245 PHE F O   
9211  C CB  . PHE F 243 ? 1.0534 1.3578 1.3904 -0.1148 0.2183  0.0226  245 PHE F CB  
9212  C CG  . PHE F 243 ? 1.0615 1.3781 1.3836 -0.1056 0.2164  0.0085  245 PHE F CG  
9213  C CD1 . PHE F 243 ? 1.0934 1.4224 1.4292 -0.1074 0.2108  -0.0020 245 PHE F CD1 
9214  C CD2 . PHE F 243 ? 1.0932 1.4089 1.3884 -0.0969 0.2183  0.0075  245 PHE F CD2 
9215  C CE1 . PHE F 243 ? 1.0952 1.4326 1.4197 -0.0989 0.2081  -0.0097 245 PHE F CE1 
9216  C CE2 . PHE F 243 ? 1.1212 1.4420 1.4051 -0.0904 0.2164  -0.0038 245 PHE F CE2 
9217  C CZ  . PHE F 243 ? 1.0874 1.4174 1.3868 -0.0904 0.2117  -0.0107 245 PHE F CZ  
9218  N N   . GLU F 244 ? 1.0778 1.4121 1.4203 -0.1358 0.2467  0.0761  246 GLU F N   
9219  C CA  . GLU F 244 ? 1.1058 1.4379 1.4434 -0.1444 0.2514  0.1038  246 GLU F CA  
9220  C C   . GLU F 244 ? 1.1506 1.4847 1.4514 -0.1358 0.2502  0.1102  246 GLU F C   
9221  O O   . GLU F 244 ? 1.1314 1.4842 1.4063 -0.1303 0.2571  0.0976  246 GLU F O   
9222  C CB  . GLU F 244 ? 1.1385 1.5019 1.4848 -0.1572 0.2676  0.1182  246 GLU F CB  
9223  C CG  . GLU F 244 ? 1.3002 1.6580 1.6869 -0.1741 0.2659  0.1279  246 GLU F CG  
9224  C CD  . GLU F 244 ? 1.5798 1.9751 1.9828 -0.1889 0.2824  0.1433  246 GLU F CD  
9225  O OE1 . GLU F 244 ? 1.6164 2.0357 1.9961 -0.1907 0.2967  0.1590  246 GLU F OE1 
9226  O OE2 . GLU F 244 ? 1.4450 1.8492 1.8843 -0.2009 0.2808  0.1401  246 GLU F OE2 
9227  N N   . ALA F 245 ? 1.1232 1.4380 1.4242 -0.1347 0.2407  0.1293  247 ALA F N   
9228  C CA  . ALA F 245 ? 1.1283 1.4518 1.3979 -0.1285 0.2358  0.1394  247 ALA F CA  
9229  C C   . ALA F 245 ? 1.2063 1.5206 1.4827 -0.1310 0.2285  0.1752  247 ALA F C   
9230  O O   . ALA F 245 ? 1.2026 1.4866 1.5133 -0.1301 0.2228  0.1846  247 ALA F O   
9231  C CB  . ALA F 245 ? 1.1124 1.4272 1.3747 -0.1147 0.2259  0.1158  247 ALA F CB  
9232  N N   . THR F 246 ? 1.1884 1.5286 1.4318 -0.1344 0.2279  0.1947  248 THR F N   
9233  C CA  . THR F 246 ? 1.2195 1.5613 1.4638 -0.1361 0.2183  0.2351  248 THR F CA  
9234  C C   . THR F 246 ? 1.2625 1.6219 1.4823 -0.1273 0.2055  0.2354  248 THR F C   
9235  O O   . THR F 246 ? 1.2936 1.6665 1.5085 -0.1281 0.1950  0.2704  248 THR F O   
9236  C CB  . THR F 246 ? 1.3691 1.7365 1.5961 -0.1546 0.2285  0.2667  248 THR F CB  
9237  O OG1 . THR F 246 ? 1.3866 1.7909 1.5694 -0.1622 0.2414  0.2483  248 THR F OG1 
9238  C CG2 . THR F 246 ? 1.3544 1.7031 1.6170 -0.1653 0.2376  0.2771  248 THR F CG2 
9239  N N   . GLY F 247 ? 1.1709 1.5312 1.3797 -0.1197 0.2050  0.1992  249 GLY F N   
9240  C CA  . GLY F 247 ? 1.1521 1.5298 1.3408 -0.1140 0.1933  0.1930  249 GLY F CA  
9241  C C   . GLY F 247 ? 1.1584 1.5435 1.3199 -0.1160 0.1994  0.1549  249 GLY F C   
9242  O O   . GLY F 247 ? 1.1521 1.5333 1.3074 -0.1204 0.2137  0.1355  249 GLY F O   
9243  N N   . ASN F 248 ? 1.0785 1.4744 1.2290 -0.1122 0.1882  0.1456  250 ASN F N   
9244  C CA  . ASN F 248 ? 1.0460 1.4468 1.1709 -0.1158 0.1905  0.1135  250 ASN F CA  
9245  C C   . ASN F 248 ? 1.0251 1.4005 1.1696 -0.1071 0.1965  0.0846  250 ASN F C   
9246  O O   . ASN F 248 ? 1.0143 1.3899 1.1440 -0.1088 0.1958  0.0627  250 ASN F O   
9247  C CB  . ASN F 248 ? 1.0798 1.4981 1.1602 -0.1311 0.2019  0.1044  250 ASN F CB  
9248  C CG  . ASN F 248 ? 1.5010 1.9523 1.5527 -0.1435 0.1940  0.1318  250 ASN F CG  
9249  O OD1 . ASN F 248 ? 1.4397 1.9005 1.4905 -0.1485 0.1983  0.1582  250 ASN F OD1 
9250  N ND2 . ASN F 248 ? 1.4533 1.9255 1.4842 -0.1500 0.1801  0.1302  250 ASN F ND2 
9251  N N   . LEU F 249 ? 0.9354 1.2900 1.1122 -0.1002 0.2009  0.0855  251 LEU F N   
9252  C CA  . LEU F 249 ? 0.8959 1.2332 1.0885 -0.0943 0.2044  0.0608  251 LEU F CA  
9253  C C   . LEU F 249 ? 0.9276 1.2596 1.1355 -0.0852 0.1945  0.0530  251 LEU F C   
9254  O O   . LEU F 249 ? 0.9302 1.2609 1.1571 -0.0782 0.1875  0.0676  251 LEU F O   
9255  C CB  . LEU F 249 ? 0.8917 1.2150 1.1106 -0.0947 0.2118  0.0619  251 LEU F CB  
9256  C CG  . LEU F 249 ? 0.9233 1.2349 1.1602 -0.0911 0.2129  0.0400  251 LEU F CG  
9257  C CD1 . LEU F 249 ? 0.9105 1.2294 1.1303 -0.0913 0.2188  0.0227  251 LEU F CD1 
9258  C CD2 . LEU F 249 ? 0.9650 1.2690 1.2281 -0.0959 0.2174  0.0445  251 LEU F CD2 
9259  N N   . VAL F 250 ? 0.8735 1.2037 1.0741 -0.0848 0.1949  0.0313  252 VAL F N   
9260  C CA  . VAL F 250 ? 0.8545 1.1842 1.0658 -0.0786 0.1886  0.0201  252 VAL F CA  
9261  C C   . VAL F 250 ? 0.8957 1.2111 1.1222 -0.0766 0.1927  0.0057  252 VAL F C   
9262  O O   . VAL F 250 ? 0.8794 1.1940 1.0970 -0.0796 0.1952  -0.0058 252 VAL F O   
9263  C CB  . VAL F 250 ? 0.8949 1.2372 1.0840 -0.0844 0.1847  0.0115  252 VAL F CB  
9264  C CG1 . VAL F 250 ? 0.8785 1.2276 1.0810 -0.0793 0.1795  0.0046  252 VAL F CG1 
9265  C CG2 . VAL F 250 ? 0.9089 1.2698 1.0777 -0.0918 0.1796  0.0243  252 VAL F CG2 
9266  N N   . VAL F 251 ? 0.8565 1.1601 1.1072 -0.0727 0.1928  0.0083  253 VAL F N   
9267  C CA  . VAL F 251 ? 0.8471 1.1398 1.1138 -0.0745 0.1946  -0.0040 253 VAL F CA  
9268  C C   . VAL F 251 ? 0.8743 1.1729 1.1368 -0.0739 0.1915  -0.0223 253 VAL F C   
9269  O O   . VAL F 251 ? 0.8600 1.1666 1.1177 -0.0694 0.1889  -0.0260 253 VAL F O   
9270  C CB  . VAL F 251 ? 0.9121 1.1860 1.2050 -0.0725 0.1946  -0.0003 253 VAL F CB  
9271  C CG1 . VAL F 251 ? 0.9268 1.1951 1.2255 -0.0767 0.1978  0.0224  253 VAL F CG1 
9272  C CG2 . VAL F 251 ? 0.9175 1.1875 1.2220 -0.0611 0.1920  -0.0036 253 VAL F CG2 
9273  N N   . PRO F 252 ? 0.8293 1.1292 1.0957 -0.0792 0.1910  -0.0313 254 PRO F N   
9274  C CA  . PRO F 252 ? 0.8252 1.1348 1.0851 -0.0805 0.1866  -0.0445 254 PRO F CA  
9275  C C   . PRO F 252 ? 0.9127 1.2184 1.1820 -0.0795 0.1857  -0.0591 254 PRO F C   
9276  O O   . PRO F 252 ? 0.9256 1.2154 1.2119 -0.0807 0.1874  -0.0623 254 PRO F O   
9277  C CB  . PRO F 252 ? 0.8405 1.1572 1.1047 -0.0864 0.1845  -0.0445 254 PRO F CB  
9278  C CG  . PRO F 252 ? 0.8970 1.2093 1.1705 -0.0870 0.1906  -0.0334 254 PRO F CG  
9279  C CD  . PRO F 252 ? 0.8533 1.1524 1.1313 -0.0854 0.1936  -0.0276 254 PRO F CD  
9280  N N   . ARG F 253 ? 0.8839 1.2033 1.1425 -0.0782 0.1847  -0.0690 255 ARG F N   
9281  C CA  . ARG F 253 ? 0.9083 1.2290 1.1713 -0.0772 0.1871  -0.0885 255 ARG F CA  
9282  C C   . ARG F 253 ? 1.0081 1.3461 1.2566 -0.0886 0.1818  -0.0986 255 ARG F C   
9283  O O   . ARG F 253 ? 1.0274 1.3619 1.2801 -0.0964 0.1802  -0.1137 255 ARG F O   
9284  C CB  . ARG F 253 ? 0.8955 1.2289 1.1576 -0.0676 0.1918  -0.0910 255 ARG F CB  
9285  C CG  . ARG F 253 ? 0.9560 1.2901 1.2262 -0.0631 0.1989  -0.1151 255 ARG F CG  
9286  C CD  . ARG F 253 ? 0.9273 1.2774 1.2072 -0.0498 0.2059  -0.1154 255 ARG F CD  
9287  N NE  . ARG F 253 ? 0.9914 1.3473 1.2766 -0.0449 0.2164  -0.1429 255 ARG F NE  
9288  C CZ  . ARG F 253 ? 1.1822 1.5641 1.4738 -0.0349 0.2255  -0.1494 255 ARG F CZ  
9289  N NH1 . ARG F 253 ? 1.0462 1.4518 1.3412 -0.0310 0.2228  -0.1284 255 ARG F NH1 
9290  N NH2 . ARG F 253 ? 1.0109 1.3982 1.3061 -0.0302 0.2382  -0.1787 255 ARG F NH2 
9291  N N   . TYR F 254 ? 0.9745 1.3311 1.2065 -0.0914 0.1780  -0.0886 256 TYR F N   
9292  C CA  . TYR F 254 ? 0.9896 1.3669 1.2079 -0.1020 0.1708  -0.0898 256 TYR F CA  
9293  C C   . TYR F 254 ? 1.0475 1.4248 1.2693 -0.1038 0.1642  -0.0709 256 TYR F C   
9294  O O   . TYR F 254 ? 1.0456 1.4122 1.2685 -0.0978 0.1670  -0.0582 256 TYR F O   
9295  C CB  . TYR F 254 ? 1.0126 1.4128 1.2121 -0.1044 0.1721  -0.0905 256 TYR F CB  
9296  C CG  . TYR F 254 ? 1.0624 1.4711 1.2599 -0.1017 0.1811  -0.1124 256 TYR F CG  
9297  C CD1 . TYR F 254 ? 1.0903 1.4963 1.2984 -0.0901 0.1898  -0.1129 256 TYR F CD1 
9298  C CD2 . TYR F 254 ? 1.0946 1.5181 1.2803 -0.1108 0.1814  -0.1334 256 TYR F CD2 
9299  C CE1 . TYR F 254 ? 1.1242 1.5404 1.3373 -0.0837 0.2006  -0.1334 256 TYR F CE1 
9300  C CE2 . TYR F 254 ? 1.1291 1.5599 1.3134 -0.1067 0.1935  -0.1583 256 TYR F CE2 
9301  C CZ  . TYR F 254 ? 1.2247 1.6510 1.4257 -0.0911 0.2041  -0.1580 256 TYR F CZ  
9302  O OH  . TYR F 254 ? 1.2503 1.6854 1.4568 -0.0831 0.2184  -0.1827 256 TYR F OH  
9303  N N   . ALA F 255 ? 0.9975 1.3890 1.2225 -0.1123 0.1557  -0.0705 257 ALA F N   
9304  C CA  . ALA F 255 ? 0.9737 1.3722 1.2095 -0.1118 0.1491  -0.0518 257 ALA F CA  
9305  C C   . ALA F 255 ? 1.0050 1.4316 1.2286 -0.1199 0.1376  -0.0431 257 ALA F C   
9306  O O   . ALA F 255 ? 1.0121 1.4548 1.2158 -0.1287 0.1358  -0.0548 257 ALA F O   
9307  C CB  . ALA F 255 ? 0.9820 1.3805 1.2406 -0.1148 0.1473  -0.0532 257 ALA F CB  
9308  N N   . PHE F 256 ? 0.9406 1.3750 1.1768 -0.1164 0.1307  -0.0215 258 PHE F N   
9309  C CA  . PHE F 256 ? 0.9453 1.4072 1.1722 -0.1235 0.1179  -0.0055 258 PHE F CA  
9310  C C   . PHE F 256 ? 0.9939 1.4820 1.2429 -0.1258 0.1044  0.0099  258 PHE F C   
9311  O O   . PHE F 256 ? 0.9832 1.4647 1.2593 -0.1133 0.1051  0.0273  258 PHE F O   
9312  C CB  . PHE F 256 ? 0.9693 1.4175 1.1897 -0.1175 0.1202  0.0130  258 PHE F CB  
9313  C CG  . PHE F 256 ? 0.9818 1.4079 1.1869 -0.1156 0.1327  0.0006  258 PHE F CG  
9314  C CD1 . PHE F 256 ? 1.0304 1.4720 1.2124 -0.1246 0.1350  -0.0111 258 PHE F CD1 
9315  C CD2 . PHE F 256 ? 0.9926 1.3877 1.2071 -0.1054 0.1426  -0.0001 258 PHE F CD2 
9316  C CE1 . PHE F 256 ? 1.0351 1.4639 1.2098 -0.1220 0.1455  -0.0199 258 PHE F CE1 
9317  C CE2 . PHE F 256 ? 1.0228 1.4049 1.2245 -0.1058 0.1510  -0.0094 258 PHE F CE2 
9318  C CZ  . PHE F 256 ? 1.0078 1.4080 1.1927 -0.1133 0.1518  -0.0176 258 PHE F CZ  
9319  N N   . ALA F 257 ? 0.9689 1.4900 1.2070 -0.1422 0.0924  0.0018  259 ALA F N   
9320  C CA  . ALA F 257 ? 0.9841 1.5431 1.2406 -0.1497 0.0750  0.0169  259 ALA F CA  
9321  C C   . ALA F 257 ? 1.0610 1.6425 1.3123 -0.1485 0.0624  0.0490  259 ALA F C   
9322  O O   . ALA F 257 ? 1.0786 1.6830 1.2970 -0.1627 0.0550  0.0495  259 ALA F O   
9323  C CB  . ALA F 257 ? 1.0131 1.5983 1.2519 -0.1723 0.0662  -0.0070 259 ALA F CB  
9324  N N   . MET F 258 ? 1.0185 1.5905 1.3023 -0.1308 0.0621  0.0758  260 MET F N   
9325  C CA  . MET F 258 ? 1.0358 1.6171 1.3231 -0.1257 0.0519  0.1109  260 MET F CA  
9326  C C   . MET F 258 ? 1.1293 1.7457 1.4558 -0.1189 0.0347  0.1436  260 MET F C   
9327  O O   . MET F 258 ? 1.1186 1.7403 1.4831 -0.1088 0.0371  0.1422  260 MET F O   
9328  C CB  . MET F 258 ? 1.0573 1.5882 1.3489 -0.1091 0.0679  0.1160  260 MET F CB  
9329  C CG  . MET F 258 ? 1.0845 1.5839 1.4071 -0.0908 0.0837  0.1052  260 MET F CG  
9330  S SD  . MET F 258 ? 1.1544 1.6044 1.4936 -0.0707 0.0961  0.1201  260 MET F SD  
9331  C CE  . MET F 258 ? 1.1041 1.5190 1.4033 -0.0796 0.1109  0.0929  260 MET F CE  
9332  N N   . GLU F 259 ? 1.1239 1.7671 1.4434 -0.1240 0.0174  0.1767  261 GLU F N   
9333  C CA  . GLU F 259 ? 1.1398 1.8218 1.4969 -0.1169 -0.0030 0.2178  261 GLU F CA  
9334  C C   . GLU F 259 ? 1.2108 1.8573 1.5836 -0.0985 0.0006  0.2507  261 GLU F C   
9335  O O   . GLU F 259 ? 1.2256 1.8658 1.5642 -0.1097 -0.0023 0.2623  261 GLU F O   
9336  C CB  . GLU F 259 ? 1.1797 1.9260 1.5071 -0.1438 -0.0286 0.2299  261 GLU F CB  
9337  C CG  . GLU F 259 ? 1.2944 2.0979 1.6618 -0.1415 -0.0544 0.2689  261 GLU F CG  
9338  C CD  . GLU F 259 ? 1.5358 2.4055 1.8663 -0.1707 -0.0817 0.2852  261 GLU F CD  
9339  O OE1 . GLU F 259 ? 1.3978 2.2875 1.6845 -0.1973 -0.0826 0.2483  261 GLU F OE1 
9340  O OE2 . GLU F 259 ? 1.4583 2.3600 1.8036 -0.1672 -0.1021 0.3352  261 GLU F OE2 
9341  N N   . ARG F 260 ? 1.0651 1.6908 2.2212 -0.2500 0.1614  -0.1996 262 ARG F N   
9342  C CA  . ARG F 260 ? 1.0413 1.6850 2.1450 -0.2371 0.1625  -0.1823 262 ARG F CA  
9343  C C   . ARG F 260 ? 1.0888 1.7906 2.2328 -0.2269 0.1163  -0.2024 262 ARG F C   
9344  O O   . ARG F 260 ? 1.0843 1.8146 2.3318 -0.2341 0.0975  -0.2295 262 ARG F O   
9345  C CB  . ARG F 260 ? 1.0514 1.6643 2.1628 -0.2465 0.2242  -0.1605 262 ARG F CB  
9346  C CG  . ARG F 260 ? 1.1699 1.7126 2.1664 -0.2401 0.2578  -0.1298 262 ARG F CG  
9347  C CD  . ARG F 260 ? 1.2143 1.7239 2.1812 -0.2380 0.3048  -0.1064 262 ARG F CD  
9348  N NE  . ARG F 260 ? 1.2825 1.7567 2.3179 -0.2553 0.3681  -0.1046 262 ARG F NE  
9349  C CZ  . ARG F 260 ? 1.4825 1.8714 2.4692 -0.2602 0.4188  -0.0886 262 ARG F CZ  
9350  N NH1 . ARG F 260 ? 1.3041 1.6363 2.1740 -0.2474 0.4059  -0.0752 262 ARG F NH1 
9351  N NH2 . ARG F 260 ? 1.3617 1.7170 2.4172 -0.2766 0.4842  -0.0865 262 ARG F NH2 
9352  N N   . ASN F 261 ? 1.0489 1.7630 2.1109 -0.2094 0.0966  -0.1900 263 ASN F N   
9353  C CA  . ASN F 261 ? 1.0325 1.7876 2.1019 -0.1960 0.0574  -0.2034 263 ASN F CA  
9354  C C   . ASN F 261 ? 1.0908 1.8512 2.1556 -0.1970 0.0886  -0.1839 263 ASN F C   
9355  O O   . ASN F 261 ? 1.0976 1.8226 2.1345 -0.2045 0.1353  -0.1599 263 ASN F O   
9356  C CB  . ASN F 261 ? 1.0506 1.8054 2.0247 -0.1761 0.0225  -0.2002 263 ASN F CB  
9357  C CG  . ASN F 261 ? 1.4439 2.2241 2.4053 -0.1591 -0.0188 -0.2152 263 ASN F CG  
9358  O OD1 . ASN F 261 ? 1.3622 2.1475 2.2624 -0.1495 -0.0178 -0.1989 263 ASN F OD1 
9359  N ND2 . ASN F 261 ? 1.3940 2.1826 2.4073 -0.1532 -0.0592 -0.2476 263 ASN F ND2 
9360  N N   . ALA F 262 ? 1.0476 1.8427 2.1343 -0.1873 0.0625  -0.1954 264 ALA F N   
9361  C CA  . ALA F 262 ? 1.0406 1.8428 2.1220 -0.1849 0.0853  -0.1801 264 ALA F CA  
9362  C C   . ALA F 262 ? 1.1033 1.8682 2.0788 -0.1816 0.1137  -0.1447 264 ALA F C   
9363  O O   . ALA F 262 ? 1.0925 1.8584 1.9890 -0.1697 0.0888  -0.1357 264 ALA F O   
9364  C CB  . ALA F 262 ? 1.0347 1.8700 2.1125 -0.1683 0.0391  -0.1964 264 ALA F CB  
9365  N N   . GLY F 263 ? 1.0919 1.8170 2.0672 -0.1915 0.1652  -0.1263 265 GLY F N   
9366  C CA  . GLY F 263 ? 1.1219 1.7937 1.9957 -0.1863 0.1899  -0.0950 265 GLY F CA  
9367  C C   . GLY F 263 ? 1.1676 1.8419 1.9769 -0.1732 0.1783  -0.0792 265 GLY F C   
9368  O O   . GLY F 263 ? 1.1819 1.8392 1.9913 -0.1714 0.2078  -0.0681 265 GLY F O   
9369  N N   . SER F 264 ? 1.0991 1.7911 1.8537 -0.1638 0.1383  -0.0778 266 SER F N   
9370  C CA  . SER F 264 ? 1.0847 1.7788 1.7795 -0.1531 0.1235  -0.0636 266 SER F CA  
9371  C C   . SER F 264 ? 1.1549 1.7945 1.7621 -0.1477 0.1319  -0.0365 266 SER F C   
9372  O O   . SER F 264 ? 1.1999 1.7889 1.7790 -0.1463 0.1638  -0.0210 266 SER F O   
9373  C CB  . SER F 264 ? 1.0886 1.8263 1.7788 -0.1457 0.0809  -0.0776 266 SER F CB  
9374  O OG  . SER F 264 ? 1.1310 1.9018 1.8701 -0.1422 0.0679  -0.0959 266 SER F OG  
9375  N N   . GLY F 265 A 1.0777 1.7209 1.6442 -0.1429 0.1046  -0.0319 266 GLY F N   
9376  C CA  . GLY F 265 A 1.0957 1.6883 1.5920 -0.1360 0.1023  -0.0104 266 GLY F CA  
9377  C C   . GLY F 265 A 1.1208 1.7091 1.6009 -0.1332 0.0821  -0.0098 266 GLY F C   
9378  O O   . GLY F 265 A 1.0930 1.7175 1.6098 -0.1361 0.0730  -0.0248 266 GLY F O   
9379  N N   . ILE F 266 ? 1.0826 1.6205 1.5057 -0.1247 0.0728  0.0068  267 ILE F N   
9380  C CA  . ILE F 266 ? 1.0682 1.5940 1.4778 -0.1186 0.0496  0.0087  267 ILE F CA  
9381  C C   . ILE F 266 ? 1.0578 1.5956 1.4525 -0.1137 0.0211  0.0180  267 ILE F C   
9382  O O   . ILE F 266 ? 1.0796 1.5767 1.4285 -0.1080 0.0151  0.0315  267 ILE F O   
9383  C CB  . ILE F 266 ? 1.1735 1.6172 1.5325 -0.1099 0.0559  0.0164  267 ILE F CB  
9384  C CG1 . ILE F 266 ? 1.2129 1.6321 1.5829 -0.1169 0.0938  0.0103  267 ILE F CG1 
9385  C CG2 . ILE F 266 ? 1.1779 1.6178 1.5387 -0.1020 0.0271  0.0130  267 ILE F CG2 
9386  C CD1 . ILE F 266 ? 1.4430 1.8036 1.7750 -0.1157 0.1302  0.0222  267 ILE F CD1 
9387  N N   . ILE F 267 ? 0.9391 1.5283 1.3728 -0.1156 0.0063  0.0109  268 ILE F N   
9388  C CA  . ILE F 267 ? 0.8970 1.5061 1.3370 -0.1143 -0.0154 0.0179  268 ILE F CA  
9389  C C   . ILE F 267 ? 0.9752 1.5548 1.4167 -0.1061 -0.0400 0.0219  268 ILE F C   
9390  O O   . ILE F 267 ? 0.9636 1.5572 1.4369 -0.1035 -0.0410 0.0130  268 ILE F O   
9391  C CB  . ILE F 267 ? 0.8758 1.5470 1.3540 -0.1194 -0.0088 0.0086  268 ILE F CB  
9392  C CG1 . ILE F 267 ? 0.8555 1.5414 1.3177 -0.1229 -0.0009 0.0077  268 ILE F CG1 
9393  C CG2 . ILE F 267 ? 0.8736 1.5657 1.3791 -0.1188 -0.0214 0.0134  268 ILE F CG2 
9394  C CD1 . ILE F 267 ? 0.8830 1.6085 1.3597 -0.1231 0.0046  -0.0036 268 ILE F CD1 
9395  N N   . ILE F 268 ? 0.9719 1.5040 1.3761 -0.0995 -0.0633 0.0337  269 ILE F N   
9396  C CA  . ILE F 268 ? 1.0073 1.5019 1.4127 -0.0883 -0.0989 0.0352  269 ILE F CA  
9397  C C   . ILE F 268 ? 1.0396 1.5750 1.4948 -0.0936 -0.1200 0.0382  269 ILE F C   
9398  O O   . ILE F 268 ? 1.0709 1.5731 1.4991 -0.0907 -0.1449 0.0475  269 ILE F O   
9399  C CB  . ILE F 268 ? 1.1264 1.5203 1.4463 -0.0728 -0.1156 0.0438  269 ILE F CB  
9400  C CG1 . ILE F 268 ? 1.1732 1.5265 1.4461 -0.0713 -0.0789 0.0433  269 ILE F CG1 
9401  C CG2 . ILE F 268 ? 1.1767 1.5221 1.4945 -0.0564 -0.1612 0.0403  269 ILE F CG2 
9402  C CD1 . ILE F 268 ? 1.3803 1.7113 1.6070 -0.0744 -0.0496 0.0531  269 ILE F CD1 
9403  N N   . SER F 269 ? 0.9443 1.5475 1.4690 -0.1015 -0.1053 0.0309  270 SER F N   
9404  C CA  . SER F 269 ? 0.9188 1.5626 1.4993 -0.1090 -0.1117 0.0342  270 SER F CA  
9405  C C   . SER F 269 ? 0.9594 1.6437 1.6241 -0.1079 -0.1103 0.0259  270 SER F C   
9406  O O   . SER F 269 ? 0.9412 1.6434 1.6186 -0.1043 -0.0904 0.0166  270 SER F O   
9407  C CB  . SER F 269 ? 0.9328 1.6125 1.5011 -0.1198 -0.0819 0.0374  270 SER F CB  
9408  O OG  . SER F 269 ? 1.0606 1.7649 1.6694 -0.1277 -0.0842 0.0435  270 SER F OG  
9409  N N   . ASP F 270 ? 0.9220 1.6206 1.6501 -0.1112 -0.1302 0.0289  271 ASP F N   
9410  C CA  . ASP F 270 ? 0.9040 1.6448 1.7332 -0.1107 -0.1263 0.0217  271 ASP F CA  
9411  C C   . ASP F 270 ? 0.8935 1.6880 1.7613 -0.1218 -0.0759 0.0243  271 ASP F C   
9412  O O   . ASP F 270 ? 0.8744 1.7043 1.8262 -0.1211 -0.0585 0.0198  271 ASP F O   
9413  C CB  . ASP F 270 ? 0.9584 1.6838 1.8519 -0.1080 -0.1759 0.0212  271 ASP F CB  
9414  C CG  . ASP F 270 ? 1.1937 1.8945 2.1209 -0.0903 -0.2155 0.0083  271 ASP F CG  
9415  O OD1 . ASP F 270 ? 1.2004 1.9403 2.1934 -0.0861 -0.1959 -0.0013 271 ASP F OD1 
9416  O OD2 . ASP F 270 ? 1.3292 1.9658 2.2160 -0.0782 -0.2685 0.0071  271 ASP F OD2 
9417  N N   . THR F 271 ? 0.8308 1.6241 1.6327 -0.1291 -0.0511 0.0309  272 THR F N   
9418  C CA  . THR F 271 ? 0.8107 1.6324 1.6162 -0.1351 -0.0047 0.0334  272 THR F CA  
9419  C C   . THR F 271 ? 0.8468 1.6870 1.6610 -0.1256 0.0296  0.0232  272 THR F C   
9420  O O   . THR F 271 ? 0.8454 1.6751 1.6360 -0.1172 0.0183  0.0144  272 THR F O   
9421  C CB  . THR F 271 ? 0.8735 1.6780 1.5955 -0.1399 0.0023  0.0395  272 THR F CB  
9422  O OG1 . THR F 271 ? 0.8622 1.6473 1.5198 -0.1336 -0.0075 0.0335  272 THR F OG1 
9423  C CG2 . THR F 271 ? 0.8598 1.6477 1.5792 -0.1492 -0.0225 0.0513  272 THR F CG2 
9424  N N   . PRO F 272 ? 0.8082 1.6677 1.6525 -0.1253 0.0731  0.0244  273 PRO F N   
9425  C CA  . PRO F 272 ? 0.8208 1.6869 1.6638 -0.1123 0.1040  0.0147  273 PRO F CA  
9426  C C   . PRO F 272 ? 0.9073 1.7511 1.6551 -0.1043 0.1121  0.0069  273 PRO F C   
9427  O O   . PRO F 272 ? 0.9092 1.7372 1.5968 -0.1091 0.1010  0.0091  273 PRO F O   
9428  C CB  . PRO F 272 ? 0.8660 1.7458 1.7593 -0.1129 0.1531  0.0209  273 PRO F CB  
9429  C CG  . PRO F 272 ? 0.9293 1.7987 1.8009 -0.1263 0.1565  0.0330  273 PRO F CG  
9430  C CD  . PRO F 272 ? 0.8438 1.7107 1.7194 -0.1355 0.1001  0.0353  273 PRO F CD  
9431  N N   . VAL F 273 ? 0.8874 1.7287 1.6264 -0.0910 0.1288  -0.0039 274 VAL F N   
9432  C CA  . VAL F 273 ? 0.9082 1.7258 1.5685 -0.0813 0.1312  -0.0153 274 VAL F CA  
9433  C C   . VAL F 273 ? 1.0077 1.8087 1.6432 -0.0650 0.1737  -0.0193 274 VAL F C   
9434  O O   . VAL F 273 ? 1.0093 1.8209 1.6927 -0.0568 0.1945  -0.0204 274 VAL F O   
9435  C CB  . VAL F 273 ? 0.9452 1.7589 1.5998 -0.0798 0.1012  -0.0261 274 VAL F CB  
9436  C CG1 . VAL F 273 ? 0.9354 1.7627 1.6547 -0.0762 0.0944  -0.0272 274 VAL F CG1 
9437  C CG2 . VAL F 273 ? 0.9683 1.7606 1.5660 -0.0686 0.1051  -0.0412 274 VAL F CG2 
9438  N N   . HIS F 274 ? 1.0118 1.7796 1.5678 -0.0576 0.1865  -0.0217 275 HIS F N   
9439  C CA  . HIS F 274 ? 1.0803 1.8086 1.5815 -0.0372 0.2273  -0.0252 275 HIS F CA  
9440  C C   . HIS F 274 ? 1.1633 1.8496 1.5765 -0.0193 0.2091  -0.0438 275 HIS F C   
9441  O O   . HIS F 274 ? 1.1191 1.8138 1.5246 -0.0262 0.1676  -0.0538 275 HIS F O   
9442  C CB  . HIS F 274 ? 1.1326 1.8384 1.6074 -0.0386 0.2628  -0.0116 275 HIS F CB  
9443  C CG  . HIS F 274 ? 1.1596 1.9014 1.7339 -0.0528 0.2902  0.0042  275 HIS F CG  
9444  N ND1 . HIS F 274 ? 1.1243 1.9073 1.7696 -0.0747 0.2580  0.0118  275 HIS F ND1 
9445  C CD2 . HIS F 274 ? 1.2274 1.9666 1.8459 -0.0465 0.3452  0.0119  275 HIS F CD2 
9446  C CE1 . HIS F 274 ? 1.1221 1.9289 1.8586 -0.0820 0.2876  0.0220  275 HIS F CE1 
9447  N NE2 . HIS F 274 ? 1.1813 1.9675 1.9131 -0.0668 0.3438  0.0228  275 HIS F NE2 
9448  N N   . ASP F 275 ? 1.2050 1.8404 1.5533 0.0050  0.2407  -0.0491 276 ASP F N   
9449  C CA  . ASP F 275 ? 1.2693 1.8526 1.5305 0.0269  0.2195  -0.0694 276 ASP F CA  
9450  C C   . ASP F 275 ? 1.3694 1.9147 1.5510 0.0324  0.1904  -0.0790 276 ASP F C   
9451  O O   . ASP F 275 ? 1.4298 1.9329 1.5494 0.0503  0.1604  -0.0997 276 ASP F O   
9452  C CB  . ASP F 275 ? 1.3872 1.9138 1.5915 0.0561  0.2620  -0.0719 276 ASP F CB  
9453  C CG  . ASP F 275 ? 1.6129 2.1024 1.7668 0.0763  0.2332  -0.0940 276 ASP F CG  
9454  O OD1 . ASP F 275 ? 1.7218 2.1335 1.7666 0.1033  0.2283  -0.1067 276 ASP F OD1 
9455  O OD2 . ASP F 275 ? 1.6495 2.1804 1.8685 0.0665  0.2130  -0.0993 276 ASP F OD2 
9456  N N   . CYS F 276 ? 1.2922 1.8512 1.4795 0.0179  0.1934  -0.0660 277 CYS F N   
9457  C CA  . CYS F 276 ? 1.3113 1.8382 1.4299 0.0231  0.1645  -0.0745 277 CYS F CA  
9458  C C   . CYS F 276 ? 1.3166 1.8673 1.4570 0.0171  0.1072  -0.0939 277 CYS F C   
9459  O O   . CYS F 276 ? 1.2485 1.8474 1.4642 0.0016  0.0941  -0.0948 277 CYS F O   
9460  C CB  . CYS F 276 ? 1.2892 1.8337 1.4236 0.0056  0.1796  -0.0549 277 CYS F CB  
9461  S SG  . CYS F 276 ? 1.2279 1.8597 1.4933 -0.0292 0.1752  -0.0367 277 CYS F SG  
9462  N N   . ASN F 277 ? 1.3106 1.8231 1.3870 0.0305  0.0747  -0.1100 278 ASN F N   
9463  C CA  . ASN F 277 ? 1.2714 1.8069 1.3806 0.0250  0.0234  -0.1298 278 ASN F CA  
9464  C C   . ASN F 277 ? 1.2778 1.8377 1.4000 0.0112  0.0109  -0.1220 278 ASN F C   
9465  O O   . ASN F 277 ? 1.3017 1.8347 1.3713 0.0157  0.0309  -0.1093 278 ASN F O   
9466  C CB  . ASN F 277 ? 1.3800 1.8515 1.4168 0.0545  -0.0136 -0.1595 278 ASN F CB  
9467  C CG  . ASN F 277 ? 1.8806 2.3153 1.8909 0.0725  -0.0104 -0.1713 278 ASN F CG  
9468  O OD1 . ASN F 277 ? 1.7193 2.1953 1.7968 0.0582  0.0022  -0.1657 278 ASN F OD1 
9469  N ND2 . ASN F 277 ? 2.0471 2.3928 1.9474 0.1078  -0.0264 -0.1895 278 ASN F ND2 
9470  N N   . THR F 278 ? 1.1747 1.7801 1.3643 -0.0048 -0.0178 -0.1287 279 THR F N   
9471  C CA  . THR F 278 ? 1.1433 1.7691 1.3444 -0.0152 -0.0298 -0.1224 279 THR F CA  
9472  C C   . THR F 278 ? 1.1702 1.8206 1.4245 -0.0190 -0.0669 -0.1425 279 THR F C   
9473  O O   . THR F 278 ? 1.1474 1.8187 1.4597 -0.0263 -0.0737 -0.1523 279 THR F O   
9474  C CB  . THR F 278 ? 1.1769 1.8398 1.4177 -0.0382 -0.0019 -0.0930 279 THR F CB  
9475  O OG1 . THR F 278 ? 1.1528 1.8159 1.3743 -0.0418 -0.0105 -0.0859 279 THR F OG1 
9476  C CG2 . THR F 278 ? 1.0952 1.8022 1.4167 -0.0576 -0.0003 -0.0869 279 THR F CG2 
9477  N N   . THR F 279 ? 1.1220 1.7676 1.3599 -0.0136 -0.0883 -0.1489 280 THR F N   
9478  C CA  . THR F 279 ? 1.0839 1.7557 1.3836 -0.0164 -0.1191 -0.1678 280 THR F CA  
9479  C C   . THR F 279 ? 1.0394 1.7570 1.4006 -0.0411 -0.0974 -0.1462 280 THR F C   
9480  O O   . THR F 279 ? 0.9945 1.7408 1.4303 -0.0518 -0.1008 -0.1539 280 THR F O   
9481  C CB  . THR F 279 ? 1.2751 1.9160 1.5256 0.0049  -0.1529 -0.1854 280 THR F CB  
9482  O OG1 . THR F 279 ? 1.2843 1.9148 1.4797 0.0026  -0.1336 -0.1624 280 THR F OG1 
9483  C CG2 . THR F 279 ? 1.3829 1.9598 1.5581 0.0356  -0.1830 -0.2110 280 THR F CG2 
9484  N N   . CYS F 280 ? 0.9757 1.6921 1.3022 -0.0489 -0.0740 -0.1194 281 CYS F N   
9485  C CA  . CYS F 280 ? 0.9254 1.6668 1.2841 -0.0673 -0.0569 -0.0968 281 CYS F CA  
9486  C C   . CYS F 280 ? 0.9318 1.6747 1.2858 -0.0789 -0.0311 -0.0727 281 CYS F C   
9487  O O   . CYS F 280 ? 0.9639 1.6889 1.2754 -0.0739 -0.0205 -0.0652 281 CYS F O   
9488  C CB  . CYS F 280 ? 0.9454 1.6793 1.2708 -0.0629 -0.0659 -0.0913 281 CYS F CB  
9489  S SG  . CYS F 280 ? 0.9622 1.7112 1.3125 -0.0796 -0.0499 -0.0658 281 CYS F SG  
9490  N N   . GLN F 281 ? 0.8180 1.5768 1.2167 -0.0929 -0.0204 -0.0614 282 GLN F N   
9491  C CA  . GLN F 281 ? 0.7855 1.5450 1.1916 -0.1018 -0.0049 -0.0425 282 GLN F CA  
9492  C C   . GLN F 281 ? 0.8138 1.5694 1.2282 -0.1119 -0.0034 -0.0238 282 GLN F C   
9493  O O   . GLN F 281 ? 0.8008 1.5535 1.2329 -0.1147 -0.0025 -0.0259 282 GLN F O   
9494  C CB  . GLN F 281 ? 0.7899 1.5549 1.2275 -0.1020 0.0013  -0.0513 282 GLN F CB  
9495  C CG  . GLN F 281 ? 0.8255 1.5924 1.2794 -0.1074 0.0132  -0.0364 282 GLN F CG  
9496  C CD  . GLN F 281 ? 0.9964 1.7612 1.4319 -0.1034 0.0251  -0.0287 282 GLN F CD  
9497  O OE1 . GLN F 281 ? 0.9921 1.7498 1.4115 -0.0931 0.0355  -0.0381 282 GLN F OE1 
9498  N NE2 . GLN F 281 ? 0.8052 1.5696 1.2408 -0.1108 0.0257  -0.0114 282 GLN F NE2 
9499  N N   . THR F 282 ? 0.7716 1.5201 1.1723 -0.1162 -0.0023 -0.0058 283 THR F N   
9500  C CA  . THR F 282 ? 0.7622 1.4931 1.1583 -0.1221 -0.0087 0.0120  283 THR F CA  
9501  C C   . THR F 282 ? 0.7763 1.5051 1.1979 -0.1264 -0.0109 0.0218  283 THR F C   
9502  O O   . THR F 282 ? 0.7539 1.4991 1.1931 -0.1267 -0.0020 0.0198  283 THR F O   
9503  C CB  . THR F 282 ? 0.8954 1.6135 1.2528 -0.1218 -0.0171 0.0224  283 THR F CB  
9504  O OG1 . THR F 282 ? 0.8452 1.5646 1.2001 -0.1258 -0.0165 0.0315  283 THR F OG1 
9505  C CG2 . THR F 282 ? 0.9177 1.6403 1.2528 -0.1142 -0.0188 0.0100  283 THR F CG2 
9506  N N   . PRO F 283 ? 0.7496 1.4521 1.1713 -0.1274 -0.0229 0.0320  284 PRO F N   
9507  C CA  . PRO F 283 ? 0.7701 1.4691 1.2244 -0.1287 -0.0343 0.0378  284 PRO F CA  
9508  C C   . PRO F 283 ? 0.8774 1.5927 1.3560 -0.1344 -0.0369 0.0451  284 PRO F C   
9509  O O   . PRO F 283 ? 0.8723 1.6048 1.4028 -0.1359 -0.0348 0.0439  284 PRO F O   
9510  C CB  . PRO F 283 ? 0.8163 1.4652 1.2411 -0.1241 -0.0546 0.0472  284 PRO F CB  
9511  C CG  . PRO F 283 ? 0.8668 1.4979 1.2560 -0.1210 -0.0395 0.0443  284 PRO F CG  
9512  C CD  . PRO F 283 ? 0.7843 1.4500 1.1726 -0.1241 -0.0265 0.0377  284 PRO F CD  
9513  N N   . LYS F 284 ? 0.8662 1.5751 1.3115 -0.1374 -0.0385 0.0522  285 LYS F N   
9514  C CA  . LYS F 284 ? 0.8738 1.5906 1.3351 -0.1448 -0.0358 0.0604  285 LYS F CA  
9515  C C   . LYS F 284 ? 0.9571 1.6993 1.4317 -0.1444 -0.0029 0.0530  285 LYS F C   
9516  O O   . LYS F 284 ? 0.9558 1.7083 1.4708 -0.1504 0.0117  0.0582  285 LYS F O   
9517  C CB  . LYS F 284 ? 0.9067 1.6004 1.3133 -0.1458 -0.0461 0.0689  285 LYS F CB  
9518  C CG  . LYS F 284 ? 1.0237 1.7050 1.4478 -0.1548 -0.0609 0.0818  285 LYS F CG  
9519  C CD  . LYS F 284 ? 1.1554 1.8055 1.5155 -0.1534 -0.0756 0.0903  285 LYS F CD  
9520  C CE  . LYS F 284 ? 1.4088 2.0446 1.7865 -0.1641 -0.0902 0.1023  285 LYS F CE  
9521  N NZ  . LYS F 284 ? 1.5940 2.1921 1.9020 -0.1607 -0.1088 0.1109  285 LYS F NZ  
9522  N N   . GLY F 285 ? 0.9415 1.6872 1.3826 -0.1359 0.0085  0.0402  286 GLY F N   
9523  C CA  . GLY F 285 ? 0.9685 1.7199 1.3978 -0.1290 0.0347  0.0306  286 GLY F CA  
9524  C C   . GLY F 285 ? 1.0626 1.8040 1.4384 -0.1178 0.0315  0.0158  286 GLY F C   
9525  O O   . GLY F 285 ? 1.0510 1.7874 1.4058 -0.1174 0.0135  0.0142  286 GLY F O   
9526  N N   . ALA F 286 ? 1.0651 1.7988 1.4191 -0.1064 0.0477  0.0035  287 ALA F N   
9527  C CA  . ALA F 286 ? 1.0883 1.8067 1.3961 -0.0921 0.0364  -0.0157 287 ALA F CA  
9528  C C   . ALA F 286 ? 1.1618 1.8528 1.4057 -0.0847 0.0296  -0.0164 287 ALA F C   
9529  O O   . ALA F 286 ? 1.1711 1.8462 1.3928 -0.0888 0.0453  -0.0020 287 ALA F O   
9530  C CB  . ALA F 286 ? 1.1313 1.8359 1.4249 -0.0783 0.0504  -0.0293 287 ALA F CB  
9531  N N   . ILE F 287 ? 1.2823 1.2742 1.4027 -0.3258 -0.1519 -0.0790 288 ILE F N   
9532  C CA  . ILE F 287 ? 1.3253 1.2975 1.4034 -0.3011 -0.1708 -0.0863 288 ILE F CA  
9533  C C   . ILE F 287 ? 1.4284 1.4331 1.5243 -0.2695 -0.1928 -0.1226 288 ILE F C   
9534  O O   . ILE F 287 ? 1.3998 1.4398 1.5727 -0.2682 -0.1964 -0.1552 288 ILE F O   
9535  C CB  . ILE F 287 ? 1.3646 1.3179 1.4422 -0.3012 -0.1689 -0.0852 288 ILE F CB  
9536  C CG1 . ILE F 287 ? 1.3414 1.2923 1.4329 -0.3219 -0.1495 -0.0694 288 ILE F CG1 
9537  C CG2 . ILE F 287 ? 1.4210 1.3381 1.4415 -0.2881 -0.1770 -0.0722 288 ILE F CG2 
9538  C CD1 . ILE F 287 ? 1.3522 1.2998 1.4561 -0.3107 -0.1449 -0.0741 288 ILE F CD1 
9539  N N   . ASN F 288 ? 1.4566 1.4537 1.4908 -0.2379 -0.2061 -0.1174 289 ASN F N   
9540  C CA  . ASN F 288 ? 1.4935 1.5289 1.5249 -0.1938 -0.2328 -0.1543 289 ASN F CA  
9541  C C   . ASN F 288 ? 1.5764 1.5956 1.5606 -0.1660 -0.2376 -0.1419 289 ASN F C   
9542  O O   . ASN F 288 ? 1.6087 1.6152 1.5298 -0.1373 -0.2301 -0.1104 289 ASN F O   
9543  C CB  . ASN F 288 ? 1.5914 1.6471 1.5839 -0.1662 -0.2388 -0.1543 289 ASN F CB  
9544  C CG  . ASN F 288 ? 2.2098 2.3193 2.1955 -0.1096 -0.2729 -0.2036 289 ASN F CG  
9545  O OD1 . ASN F 288 ? 2.1023 2.2488 2.1582 -0.1038 -0.2977 -0.2589 289 ASN F OD1 
9546  N ND2 . ASN F 288 ? 2.3391 2.4565 2.2453 -0.0612 -0.2735 -0.1832 289 ASN F ND2 
9547  N N   . THR F 289 ? 1.5216 1.5389 1.5444 -0.1737 -0.2427 -0.1590 290 THR F N   
9548  C CA  . THR F 289 ? 1.5504 1.5506 1.5392 -0.1535 -0.2436 -0.1469 290 THR F CA  
9549  C C   . THR F 289 ? 1.5766 1.6040 1.6134 -0.1368 -0.2651 -0.1866 290 THR F C   
9550  O O   . THR F 289 ? 1.5410 1.5863 1.6595 -0.1528 -0.2707 -0.2168 290 THR F O   
9551  C CB  . THR F 289 ? 1.6907 1.6372 1.6643 -0.1857 -0.2188 -0.1091 290 THR F CB  
9552  O OG1 . THR F 289 ? 1.7476 1.6773 1.6908 -0.1640 -0.2151 -0.0938 290 THR F OG1 
9553  C CG2 . THR F 289 ? 1.6343 1.5717 1.6590 -0.2189 -0.2117 -0.1185 290 THR F CG2 
9554  N N   . SER F 290 ? 1.5439 1.5740 1.5399 -0.1024 -0.2719 -0.1809 291 SER F N   
9555  C CA  . SER F 290 ? 1.5308 1.5830 1.5635 -0.0823 -0.2921 -0.2122 291 SER F CA  
9556  C C   . SER F 290 ? 1.5310 1.5341 1.5663 -0.1075 -0.2705 -0.1833 291 SER F C   
9557  O O   . SER F 290 ? 1.5149 1.5238 1.5919 -0.1006 -0.2803 -0.2014 291 SER F O   
9558  C CB  . SER F 290 ? 1.6260 1.7209 1.6059 -0.0209 -0.3125 -0.2228 291 SER F CB  
9559  O OG  . SER F 290 ? 1.7672 1.8396 1.6668 -0.0019 -0.2850 -0.1681 291 SER F OG  
9560  N N   . LEU F 291 ? 1.4615 1.4172 1.4596 -0.1350 -0.2428 -0.1424 292 LEU F N   
9561  C CA  . LEU F 291 ? 1.4473 1.3563 1.4408 -0.1563 -0.2234 -0.1195 292 LEU F CA  
9562  C C   . LEU F 291 ? 1.4415 1.3437 1.4926 -0.1764 -0.2205 -0.1328 292 LEU F C   
9563  O O   . LEU F 291 ? 1.4100 1.3292 1.5035 -0.1903 -0.2192 -0.1440 292 LEU F O   
9564  C CB  . LEU F 291 ? 1.4554 1.3258 1.4159 -0.1780 -0.2022 -0.0878 292 LEU F CB  
9565  C CG  . LEU F 291 ? 1.5545 1.4076 1.4795 -0.1584 -0.1861 -0.0560 292 LEU F CG  
9566  C CD1 . LEU F 291 ? 1.5768 1.4333 1.4936 -0.1320 -0.1845 -0.0520 292 LEU F CD1 
9567  C CD2 . LEU F 291 ? 1.6237 1.5026 1.5236 -0.1305 -0.1848 -0.0420 292 LEU F CD2 
9568  N N   . PRO F 292 ? 1.3835 1.2617 1.4413 -0.1740 -0.2134 -0.1259 293 PRO F N   
9569  C CA  . PRO F 292 ? 1.3491 1.2220 1.4654 -0.1812 -0.2031 -0.1290 293 PRO F CA  
9570  C C   . PRO F 292 ? 1.3686 1.2174 1.4682 -0.1989 -0.1817 -0.1100 293 PRO F C   
9571  O O   . PRO F 292 ? 1.3413 1.1958 1.4894 -0.1950 -0.1662 -0.1054 293 PRO F O   
9572  C CB  . PRO F 292 ? 1.3926 1.2478 1.5141 -0.1657 -0.2027 -0.1247 293 PRO F CB  
9573  C CG  . PRO F 292 ? 1.4860 1.3197 1.5352 -0.1626 -0.2008 -0.1081 293 PRO F CG  
9574  C CD  . PRO F 292 ? 1.4359 1.2932 1.4554 -0.1594 -0.2093 -0.1103 293 PRO F CD  
9575  N N   . PHE F 293 ? 1.3333 1.1595 1.3736 -0.2119 -0.1793 -0.0989 294 PHE F N   
9576  C CA  . PHE F 293 ? 1.3259 1.1373 1.3474 -0.2228 -0.1676 -0.0913 294 PHE F CA  
9577  C C   . PHE F 293 ? 1.3365 1.1513 1.3374 -0.2413 -0.1712 -0.0901 294 PHE F C   
9578  O O   . PHE F 293 ? 1.3522 1.1662 1.3403 -0.2438 -0.1780 -0.0869 294 PHE F O   
9579  C CB  . PHE F 293 ? 1.3875 1.1621 1.3759 -0.2166 -0.1626 -0.0875 294 PHE F CB  
9580  C CG  . PHE F 293 ? 1.4151 1.1836 1.4258 -0.1967 -0.1541 -0.0821 294 PHE F CG  
9581  C CD1 . PHE F 293 ? 1.4468 1.2274 1.4885 -0.1801 -0.1373 -0.0732 294 PHE F CD1 
9582  C CD2 . PHE F 293 ? 1.4622 1.2164 1.4717 -0.1897 -0.1584 -0.0800 294 PHE F CD2 
9583  C CE1 . PHE F 293 ? 1.4667 1.2385 1.5441 -0.1584 -0.1245 -0.0616 294 PHE F CE1 
9584  C CE2 . PHE F 293 ? 1.5005 1.2474 1.5398 -0.1722 -0.1506 -0.0732 294 PHE F CE2 
9585  C CZ  . PHE F 293 ? 1.4695 1.2221 1.5460 -0.1574 -0.1335 -0.0636 294 PHE F CZ  
9586  N N   . GLN F 294 ? 1.2391 1.0616 1.2386 -0.2480 -0.1642 -0.0889 295 GLN F N   
9587  C CA  . GLN F 294 ? 1.2120 1.0389 1.2003 -0.2667 -0.1675 -0.0872 295 GLN F CA  
9588  C C   . GLN F 294 ? 1.2433 1.0664 1.2117 -0.2663 -0.1677 -0.0938 295 GLN F C   
9589  O O   . GLN F 294 ? 1.2340 1.0735 1.2013 -0.2464 -0.1574 -0.0929 295 GLN F O   
9590  C CB  . GLN F 294 ? 1.1852 1.0477 1.2065 -0.2734 -0.1621 -0.0833 295 GLN F CB  
9591  C CG  . GLN F 294 ? 1.1972 1.0792 1.2215 -0.2862 -0.1532 -0.0761 295 GLN F CG  
9592  C CD  . GLN F 294 ? 1.1774 1.0915 1.2350 -0.2703 -0.1314 -0.0684 295 GLN F CD  
9593  O OE1 . GLN F 294 ? 0.9129 0.8337 0.9479 -0.2572 -0.1242 -0.0643 295 GLN F OE1 
9594  N NE2 . GLN F 294 ? 1.1727 1.1122 1.2937 -0.2646 -0.1186 -0.0669 295 GLN F NE2 
9595  N N   . ASN F 295 ? 1.1952 1.0007 1.1552 -0.2815 -0.1786 -0.1009 296 ASN F N   
9596  C CA  . ASN F 295 ? 1.2128 1.0215 1.1616 -0.2784 -0.1885 -0.1203 296 ASN F CA  
9597  C C   . ASN F 295 ? 1.2735 1.1079 1.2292 -0.2922 -0.1895 -0.1162 296 ASN F C   
9598  O O   . ASN F 295 ? 1.3155 1.1564 1.2679 -0.2902 -0.2041 -0.1376 296 ASN F O   
9599  C CB  . ASN F 295 ? 1.2112 0.9833 1.1711 -0.2829 -0.2025 -0.1415 296 ASN F CB  
9600  C CG  . ASN F 295 ? 1.3786 1.1314 1.3775 -0.3059 -0.2063 -0.1376 296 ASN F CG  
9601  O OD1 . ASN F 295 ? 1.2199 0.9762 1.2257 -0.3174 -0.1963 -0.1109 296 ASN F OD1 
9602  N ND2 . ASN F 295 ? 1.3122 1.0444 1.3477 -0.3091 -0.2195 -0.1652 296 ASN F ND2 
9603  N N   . ILE F 296 ? 1.1804 1.0331 1.1496 -0.3036 -0.1758 -0.0933 297 ILE F N   
9604  C CA  . ILE F 296 ? 1.1509 1.0255 1.1296 -0.3200 -0.1716 -0.0824 297 ILE F CA  
9605  C C   . ILE F 296 ? 1.1969 1.1171 1.1681 -0.3020 -0.1607 -0.0811 297 ILE F C   
9606  O O   . ILE F 296 ? 1.2180 1.1496 1.1782 -0.3016 -0.1730 -0.0936 297 ILE F O   
9607  C CB  . ILE F 296 ? 1.1548 1.0341 1.1517 -0.3340 -0.1605 -0.0620 297 ILE F CB  
9608  C CG1 . ILE F 296 ? 1.1841 1.0271 1.1775 -0.3376 -0.1684 -0.0573 297 ILE F CG1 
9609  C CG2 . ILE F 296 ? 1.1360 1.0369 1.1439 -0.3518 -0.1518 -0.0471 297 ILE F CG2 
9610  C CD1 . ILE F 296 ? 1.2811 1.1351 1.2778 -0.3294 -0.1644 -0.0502 297 ILE F CD1 
9611  N N   . HIS F 297 ? 1.1299 1.0806 1.1176 -0.2828 -0.1354 -0.0645 298 HIS F N   
9612  C CA  . HIS F 297 ? 1.1225 1.1238 1.1125 -0.2549 -0.1117 -0.0496 298 HIS F CA  
9613  C C   . HIS F 297 ? 1.1632 1.1839 1.1822 -0.2193 -0.0814 -0.0316 298 HIS F C   
9614  O O   . HIS F 297 ? 1.1312 1.1420 1.1998 -0.2298 -0.0721 -0.0259 298 HIS F O   
9615  C CB  . HIS F 297 ? 1.0947 1.1261 1.1151 -0.2755 -0.0935 -0.0279 298 HIS F CB  
9616  C CG  . HIS F 297 ? 1.1437 1.2312 1.1598 -0.2458 -0.0693 -0.0097 298 HIS F CG  
9617  N ND1 . HIS F 297 ? 1.1502 1.2808 1.2076 -0.2102 -0.0250 0.0211  298 HIS F ND1 
9618  C CD2 . HIS F 297 ? 1.1934 1.3044 1.1755 -0.2408 -0.0818 -0.0168 298 HIS F CD2 
9619  C CE1 . HIS F 297 ? 1.1578 1.3400 1.1951 -0.1805 -0.0077 0.0374  298 HIS F CE1 
9620  N NE2 . HIS F 297 ? 1.1867 1.3611 1.1744 -0.1982 -0.0448 0.0117  298 HIS F NE2 
9621  N N   . PRO F 298 ? 1.1442 1.1968 1.1399 -0.1710 -0.0646 -0.0222 299 PRO F N   
9622  C CA  . PRO F 298 ? 1.1442 1.2123 1.1793 -0.1298 -0.0275 0.0050  299 PRO F CA  
9623  C C   . PRO F 298 ? 1.1745 1.2751 1.3099 -0.1313 0.0170  0.0393  299 PRO F C   
9624  O O   . PRO F 298 ? 1.1771 1.2697 1.3800 -0.1202 0.0364  0.0501  299 PRO F O   
9625  C CB  . PRO F 298 ? 1.2155 1.3190 1.1937 -0.0681 -0.0166 0.0121  299 PRO F CB  
9626  C CG  . PRO F 298 ? 1.2837 1.4127 1.2173 -0.0782 -0.0394 -0.0063 299 PRO F CG  
9627  C CD  . PRO F 298 ? 1.2103 1.2883 1.1445 -0.1433 -0.0805 -0.0384 299 PRO F CD  
9628  N N   . ILE F 299 ? 1.1033 1.2404 1.2618 -0.1455 0.0334  0.0541  300 ILE F N   
9629  C CA  . ILE F 299 ? 1.0522 1.2230 1.3233 -0.1506 0.0775  0.0823  300 ILE F CA  
9630  C C   . ILE F 299 ? 1.0739 1.2110 1.3862 -0.2021 0.0493  0.0520  300 ILE F C   
9631  O O   . ILE F 299 ? 1.0740 1.1855 1.3284 -0.2389 0.0127  0.0297  300 ILE F O   
9632  C CB  . ILE F 299 ? 1.0801 1.3053 1.3611 -0.1443 0.1096  0.1120  300 ILE F CB  
9633  C CG1 . ILE F 299 ? 1.1393 1.4117 1.3689 -0.0773 0.1369  0.1412  300 ILE F CG1 
9634  C CG2 . ILE F 299 ? 1.0320 1.2901 1.4489 -0.1543 0.1579  0.1379  300 ILE F CG2 
9635  C CD1 . ILE F 299 ? 1.2941 1.6233 1.4941 -0.0675 0.1533  0.1621  300 ILE F CD1 
9636  N N   . THR F 300 ? 1.0092 1.1487 1.4254 -0.1976 0.0656  0.0501  301 THR F N   
9637  C CA  . THR F 300 ? 0.9826 1.1025 1.4422 -0.2315 0.0355  0.0134  301 THR F CA  
9638  C C   . THR F 300 ? 0.9802 1.1375 1.5992 -0.2282 0.0692  0.0145  301 THR F C   
9639  O O   . THR F 300 ? 0.9814 1.1640 1.6953 -0.1938 0.1160  0.0445  301 THR F O   
9640  C CB  . THR F 300 ? 1.1161 1.1937 1.5376 -0.2277 -0.0002 -0.0128 301 THR F CB  
9641  O OG1 . THR F 300 ? 1.1703 1.2523 1.6507 -0.1904 0.0283  0.0059  301 THR F OG1 
9642  C CG2 . THR F 300 ? 1.1238 1.1612 1.4123 -0.2379 -0.0363 -0.0229 301 THR F CG2 
9643  N N   . ILE F 301 ? 0.9003 1.0621 1.5579 -0.2585 0.0466  -0.0193 302 ILE F N   
9644  C CA  . ILE F 301 ? 0.8587 1.0580 1.6823 -0.2596 0.0688  -0.0357 302 ILE F CA  
9645  C C   . ILE F 301 ? 0.9212 1.1098 1.7666 -0.2704 0.0160  -0.0982 302 ILE F C   
9646  O O   . ILE F 301 ? 0.9403 1.1108 1.6836 -0.2888 -0.0246 -0.1207 302 ILE F O   
9647  C CB  . ILE F 301 ? 0.8674 1.1021 1.7285 -0.2772 0.1025  -0.0141 302 ILE F CB  
9648  C CG1 . ILE F 301 ? 0.8726 1.1401 1.7670 -0.2479 0.1682  0.0493  302 ILE F CG1 
9649  C CG2 . ILE F 301 ? 0.8284 1.0961 1.8453 -0.2899 0.1081  -0.0506 302 ILE F CG2 
9650  C CD1 . ILE F 301 ? 0.9919 1.2740 1.8036 -0.2609 0.1823  0.0806  302 ILE F CD1 
9651  N N   . GLY F 302 ? 0.8729 1.0762 1.8543 -0.2525 0.0183  -0.1239 303 GLY F N   
9652  C CA  . GLY F 302 ? 0.8868 1.0928 1.9032 -0.2516 -0.0346 -0.1905 303 GLY F CA  
9653  C C   . GLY F 302 ? 0.9884 1.1584 1.9202 -0.2369 -0.0677 -0.1981 303 GLY F C   
9654  O O   . GLY F 302 ? 1.0004 1.1425 1.8727 -0.2271 -0.0450 -0.1532 303 GLY F O   
9655  N N   . LYS F 303 ? 0.9725 1.1474 1.8965 -0.2298 -0.1216 -0.2559 304 LYS F N   
9656  C CA  . LYS F 303 ? 1.0113 1.1565 1.8546 -0.2146 -0.1524 -0.2623 304 LYS F CA  
9657  C C   . LYS F 303 ? 1.0988 1.2016 1.7586 -0.2258 -0.1548 -0.2224 304 LYS F C   
9658  O O   . LYS F 303 ? 1.1086 1.2089 1.6742 -0.2327 -0.1791 -0.2319 304 LYS F O   
9659  C CB  . LYS F 303 ? 1.0628 1.2350 1.9308 -0.1960 -0.2086 -0.3317 304 LYS F CB  
9660  C CG  . LYS F 303 ? 1.1907 1.3893 2.2423 -0.1780 -0.2124 -0.3705 304 LYS F CG  
9661  C CD  . LYS F 303 ? 1.3151 1.5328 2.3608 -0.1508 -0.2716 -0.4315 304 LYS F CD  
9662  C CE  . LYS F 303 ? 1.4413 1.6787 2.6834 -0.1348 -0.2730 -0.4655 304 LYS F CE  
9663  N NZ  . LYS F 303 ? 1.5775 1.8458 2.8290 -0.1043 -0.3363 -0.5348 304 LYS F NZ  
9664  N N   . CYS F 304 ? 1.0703 1.1428 1.6932 -0.2239 -0.1247 -0.1764 305 CYS F N   
9665  C CA  . CYS F 304 ? 1.1005 1.1366 1.5802 -0.2341 -0.1237 -0.1439 305 CYS F CA  
9666  C C   . CYS F 304 ? 1.1639 1.1612 1.5762 -0.2218 -0.1300 -0.1310 305 CYS F C   
9667  O O   . CYS F 304 ? 1.1600 1.1536 1.6324 -0.2033 -0.1120 -0.1206 305 CYS F O   
9668  C CB  . CYS F 304 ? 1.0940 1.1387 1.5747 -0.2412 -0.0848 -0.1062 305 CYS F CB  
9669  S SG  . CYS F 304 ? 1.1198 1.1949 1.6180 -0.2661 -0.0807 -0.1113 305 CYS F SG  
9670  N N   . PRO F 305 ? 1.1297 1.0962 1.4252 -0.2307 -0.1487 -0.1257 306 PRO F N   
9671  C CA  . PRO F 305 ? 1.1538 1.0825 1.3892 -0.2215 -0.1513 -0.1138 306 PRO F CA  
9672  C C   . PRO F 305 ? 1.2218 1.1385 1.4366 -0.2159 -0.1243 -0.0864 306 PRO F C   
9673  O O   . PRO F 305 ? 1.2245 1.1461 1.4031 -0.2273 -0.1183 -0.0770 306 PRO F O   
9674  C CB  . PRO F 305 ? 1.2018 1.1091 1.3482 -0.2316 -0.1719 -0.1154 306 PRO F CB  
9675  C CG  . PRO F 305 ? 1.2488 1.1833 1.4046 -0.2391 -0.1825 -0.1277 306 PRO F CG  
9676  C CD  . PRO F 305 ? 1.1568 1.1201 1.3845 -0.2471 -0.1633 -0.1271 306 PRO F CD  
9677  N N   . LYS F 306 ? 1.1901 1.0959 1.4303 -0.1924 -0.1078 -0.0735 307 LYS F N   
9678  C CA  . LYS F 306 ? 1.2041 1.1054 1.4207 -0.1693 -0.0804 -0.0469 307 LYS F CA  
9679  C C   . LYS F 306 ? 1.2925 1.1748 1.4066 -0.1784 -0.0956 -0.0520 307 LYS F C   
9680  O O   . LYS F 306 ? 1.3208 1.1719 1.3856 -0.1931 -0.1196 -0.0673 307 LYS F O   
9681  C CB  . LYS F 306 ? 1.2493 1.1303 1.4906 -0.1396 -0.0657 -0.0325 307 LYS F CB  
9682  C CG  . LYS F 306 ? 1.3181 1.2227 1.6930 -0.1224 -0.0405 -0.0219 307 LYS F CG  
9683  C CD  . LYS F 306 ? 1.4209 1.2983 1.8290 -0.1078 -0.0437 -0.0213 307 LYS F CD  
9684  C CE  . LYS F 306 ? 1.5157 1.4160 2.0830 -0.0912 -0.0213 -0.0163 307 LYS F CE  
9685  N NZ  . LYS F 306 ? 1.6157 1.4864 2.2214 -0.0696 -0.0154 -0.0045 307 LYS F NZ  
9686  N N   . TYR F 307 ? 1.2456 1.1520 1.3410 -0.1677 -0.0806 -0.0405 308 TYR F N   
9687  C CA  . TYR F 307 ? 1.2767 1.1743 1.2951 -0.1737 -0.0995 -0.0548 308 TYR F CA  
9688  C C   . TYR F 307 ? 1.3761 1.2439 1.3386 -0.1527 -0.1107 -0.0672 308 TYR F C   
9689  O O   . TYR F 307 ? 1.3919 1.2586 1.3561 -0.1160 -0.0914 -0.0519 308 TYR F O   
9690  C CB  . TYR F 307 ? 1.2930 1.2345 1.3073 -0.1592 -0.0824 -0.0420 308 TYR F CB  
9691  C CG  . TYR F 307 ? 1.3536 1.2933 1.3039 -0.1650 -0.1088 -0.0660 308 TYR F CG  
9692  C CD1 . TYR F 307 ? 1.3713 1.2938 1.3179 -0.2072 -0.1333 -0.0826 308 TYR F CD1 
9693  C CD2 . TYR F 307 ? 1.4082 1.3668 1.3097 -0.1220 -0.1096 -0.0741 308 TYR F CD2 
9694  C CE1 . TYR F 307 ? 1.4111 1.3316 1.3258 -0.2130 -0.1580 -0.1078 308 TYR F CE1 
9695  C CE2 . TYR F 307 ? 1.4533 1.4160 1.3123 -0.1249 -0.1414 -0.1090 308 TYR F CE2 
9696  C CZ  . TYR F 307 ? 1.5303 1.4720 1.4055 -0.1738 -0.1656 -0.1265 308 TYR F CZ  
9697  O OH  . TYR F 307 ? 1.5736 1.5185 1.4328 -0.1775 -0.1973 -0.1637 308 TYR F OH  
9698  N N   . VAL F 308 ? 1.3593 1.2021 1.2832 -0.1746 -0.1394 -0.0943 309 VAL F N   
9699  C CA  . VAL F 308 ? 1.4071 1.2217 1.2901 -0.1626 -0.1562 -0.1191 309 VAL F CA  
9700  C C   . VAL F 308 ? 1.4854 1.3051 1.3527 -0.1755 -0.1818 -0.1512 309 VAL F C   
9701  O O   . VAL F 308 ? 1.4595 1.2874 1.3480 -0.2044 -0.1865 -0.1480 309 VAL F O   
9702  C CB  . VAL F 308 ? 1.4569 1.2277 1.3479 -0.1778 -0.1614 -0.1211 309 VAL F CB  
9703  C CG1 . VAL F 308 ? 1.4515 1.2149 1.3501 -0.1514 -0.1414 -0.0995 309 VAL F CG1 
9704  C CG2 . VAL F 308 ? 1.4242 1.1878 1.3443 -0.2122 -0.1664 -0.1140 309 VAL F CG2 
9705  N N   . LYS F 309 ? 1.4885 1.3056 1.3254 -0.1510 -0.1995 -0.1851 310 LYS F N   
9706  C CA  . LYS F 309 ? 1.5115 1.3377 1.3525 -0.1587 -0.2297 -0.2273 310 LYS F CA  
9707  C C   . LYS F 309 ? 1.5948 1.3755 1.4806 -0.1906 -0.2476 -0.2544 310 LYS F C   
9708  O O   . LYS F 309 ? 1.6022 1.3835 1.5247 -0.2055 -0.2707 -0.2878 310 LYS F O   
9709  C CB  . LYS F 309 ? 1.5885 1.4529 1.3803 -0.1042 -0.2440 -0.2596 310 LYS F CB  
9710  C CG  . LYS F 309 ? 1.6922 1.6158 1.4553 -0.0703 -0.2242 -0.2315 310 LYS F CG  
9711  C CD  . LYS F 309 ? 1.8773 1.8507 1.5818 -0.0027 -0.2391 -0.2635 310 LYS F CD  
9712  C CE  . LYS F 309 ? 2.0607 2.0753 1.7672 -0.0036 -0.2715 -0.3029 310 LYS F CE  
9713  N NZ  . LYS F 309 ? 2.2679 2.3454 1.9087 0.0755  -0.2891 -0.3382 310 LYS F NZ  
9714  N N   . SER F 310 ? 1.5605 1.3042 1.4558 -0.1989 -0.2328 -0.2363 311 SER F N   
9715  C CA  . SER F 310 ? 1.5747 1.2768 1.5202 -0.2215 -0.2350 -0.2475 311 SER F CA  
9716  C C   . SER F 310 ? 1.6124 1.3036 1.6182 -0.2555 -0.2333 -0.2364 311 SER F C   
9717  O O   . SER F 310 ? 1.5747 1.2823 1.5719 -0.2673 -0.2249 -0.2067 311 SER F O   
9718  C CB  . SER F 310 ? 1.6051 1.2813 1.5405 -0.2188 -0.2127 -0.2167 311 SER F CB  
9719  O OG  . SER F 310 ? 1.6512 1.3445 1.5623 -0.2155 -0.1963 -0.1780 311 SER F OG  
9720  N N   . THR F 311 ? 1.5950 1.2583 1.6721 -0.2675 -0.2375 -0.2588 312 THR F N   
9721  C CA  . THR F 311 ? 1.5820 1.2286 1.7386 -0.2914 -0.2274 -0.2426 312 THR F CA  
9722  C C   . THR F 311 ? 1.5827 1.2179 1.7298 -0.2941 -0.1943 -0.1830 312 THR F C   
9723  O O   . THR F 311 ? 1.5450 1.1862 1.7004 -0.3025 -0.1837 -0.1510 312 THR F O   
9724  C CB  . THR F 311 ? 1.8139 1.4344 2.0745 -0.2963 -0.2332 -0.2817 312 THR F CB  
9725  O OG1 . THR F 311 ? 1.8963 1.5325 2.1464 -0.2800 -0.2692 -0.3489 312 THR F OG1 
9726  C CG2 . THR F 311 ? 1.8146 1.4235 2.1799 -0.3155 -0.2271 -0.2743 312 THR F CG2 
9727  N N   . LYS F 312 ? 1.5419 1.1642 1.6687 -0.2819 -0.1795 -0.1703 313 LYS F N   
9728  C CA  . LYS F 312 ? 1.5213 1.1424 1.6306 -0.2735 -0.1532 -0.1222 313 LYS F CA  
9729  C C   . LYS F 312 ? 1.5479 1.1620 1.6195 -0.2592 -0.1479 -0.1211 313 LYS F C   
9730  O O   . LYS F 312 ? 1.5580 1.1552 1.6390 -0.2565 -0.1545 -0.1511 313 LYS F O   
9731  C CB  . LYS F 312 ? 1.5711 1.1744 1.7572 -0.2719 -0.1236 -0.0908 313 LYS F CB  
9732  C CG  . LYS F 312 ? 1.8226 1.4446 1.9822 -0.2573 -0.1047 -0.0410 313 LYS F CG  
9733  C CD  . LYS F 312 ? 1.9835 1.6117 2.1636 -0.2673 -0.1079 -0.0320 313 LYS F CD  
9734  C CE  . LYS F 312 ? 2.1600 1.8020 2.3286 -0.2416 -0.0818 0.0206  313 LYS F CE  
9735  N NZ  . LYS F 312 ? 2.3091 1.9480 2.5098 -0.2489 -0.0774 0.0371  313 LYS F NZ  
9736  N N   . LEU F 313 ? 1.4707 1.1000 1.5033 -0.2474 -0.1381 -0.0899 314 LEU F N   
9737  C CA  . LEU F 313 ? 1.4620 1.0865 1.4663 -0.2330 -0.1314 -0.0814 314 LEU F CA  
9738  C C   . LEU F 313 ? 1.4995 1.1322 1.5120 -0.2173 -0.1094 -0.0437 314 LEU F C   
9739  O O   . LEU F 313 ? 1.4747 1.1360 1.4711 -0.2077 -0.1118 -0.0276 314 LEU F O   
9740  C CB  . LEU F 313 ? 1.4352 1.0811 1.3957 -0.2259 -0.1452 -0.0865 314 LEU F CB  
9741  C CG  . LEU F 313 ? 1.4945 1.1419 1.4364 -0.2245 -0.1583 -0.1127 314 LEU F CG  
9742  C CD1 . LEU F 313 ? 1.4666 1.1421 1.3926 -0.2145 -0.1598 -0.1041 314 LEU F CD1 
9743  C CD2 . LEU F 313 ? 1.5671 1.1877 1.4990 -0.2122 -0.1558 -0.1276 314 LEU F CD2 
9744  N N   . ARG F 314 ? 1.4639 1.0764 1.5011 -0.2091 -0.0870 -0.0299 315 ARG F N   
9745  C CA  . ARG F 314 ? 1.4600 1.0874 1.5048 -0.1839 -0.0597 0.0116  315 ARG F CA  
9746  C C   . ARG F 314 ? 1.5045 1.1259 1.5330 -0.1712 -0.0492 0.0221  315 ARG F C   
9747  O O   . ARG F 314 ? 1.5249 1.1134 1.5723 -0.1830 -0.0428 0.0086  315 ARG F O   
9748  C CB  . ARG F 314 ? 1.4591 1.0741 1.5780 -0.1797 -0.0255 0.0367  315 ARG F CB  
9749  C CG  . ARG F 314 ? 1.5168 1.1606 1.6384 -0.1391 0.0091  0.0907  315 ARG F CG  
9750  C CD  . ARG F 314 ? 1.5084 1.1504 1.6983 -0.1274 0.0410  0.1232  315 ARG F CD  
9751  N NE  . ARG F 314 ? 1.5362 1.2210 1.6772 -0.0874 0.0460  0.1574  315 ARG F NE  
9752  C CZ  . ARG F 314 ? 1.7013 1.3985 1.8106 -0.0940 0.0210  0.1448  315 ARG F CZ  
9753  N NH1 . ARG F 314 ? 1.4593 1.1314 1.5828 -0.1389 -0.0076 0.1042  315 ARG F NH1 
9754  N NH2 . ARG F 314 ? 1.6269 1.3659 1.6887 -0.0506 0.0249  0.1724  315 ARG F NH2 
9755  N N   . LEU F 315 ? 1.4325 1.0883 1.4281 -0.1439 -0.0492 0.0431  316 LEU F N   
9756  C CA  . LEU F 315 ? 1.4316 1.0882 1.4141 -0.1283 -0.0401 0.0565  316 LEU F CA  
9757  C C   . LEU F 315 ? 1.5233 1.1985 1.5248 -0.0959 -0.0013 0.1016  316 LEU F C   
9758  O O   . LEU F 315 ? 1.5419 1.2580 1.5320 -0.0643 0.0046  0.1228  316 LEU F O   
9759  C CB  . LEU F 315 ? 1.4082 1.0975 1.3556 -0.1153 -0.0710 0.0418  316 LEU F CB  
9760  C CG  . LEU F 315 ? 1.4354 1.1063 1.3789 -0.1374 -0.0958 0.0106  316 LEU F CG  
9761  C CD1 . LEU F 315 ? 1.4137 1.1239 1.3573 -0.1226 -0.1226 -0.0046 316 LEU F CD1 
9762  C CD2 . LEU F 315 ? 1.4668 1.0943 1.4127 -0.1459 -0.0834 0.0128  316 LEU F CD2 
9763  N N   . ALA F 316 ? 1.4888 1.1377 1.5189 -0.0975 0.0288  0.1192  317 ALA F N   
9764  C CA  . ALA F 316 ? 1.5079 1.1748 1.5692 -0.0637 0.0777  0.1705  317 ALA F CA  
9765  C C   . ALA F 316 ? 1.5632 1.2828 1.5715 -0.0203 0.0719  0.1905  317 ALA F C   
9766  O O   . ALA F 316 ? 1.5348 1.2553 1.5075 -0.0280 0.0384  0.1646  317 ALA F O   
9767  C CB  . ALA F 316 ? 1.5283 1.1503 1.6444 -0.0828 0.1104  0.1772  317 ALA F CB  
9768  N N   . THR F 317 ? 1.5640 1.3316 1.5739 0.0317  0.1053  0.2368  318 THR F N   
9769  C CA  . THR F 317 ? 1.5940 1.4280 1.5519 0.0890  0.1000  0.2550  318 THR F CA  
9770  C C   . THR F 317 ? 1.7120 1.5653 1.7010 0.1313  0.1658  0.3208  318 THR F C   
9771  O O   . THR F 317 ? 1.7232 1.6101 1.6810 0.1607  0.1644  0.3316  318 THR F O   
9772  C CB  . THR F 317 ? 1.6883 1.5793 1.5993 0.1278  0.0705  0.2426  318 THR F CB  
9773  O OG1 . THR F 317 ? 1.6077 1.4749 1.5080 0.0813  0.0181  0.1849  318 THR F OG1 
9774  C CG2 . THR F 317 ? 1.7158 1.6886 1.5697 0.1969  0.0526  0.2452  318 THR F CG2 
9775  N N   . GLY F 318 ? 1.6978 1.5296 1.7617 0.1331  0.2241  0.3634  319 GLY F N   
9776  C CA  . GLY F 318 ? 1.7319 1.5787 1.8553 0.1720  0.3003  0.4332  319 GLY F CA  
9777  C C   . GLY F 318 ? 1.7917 1.5711 2.0329 0.1249  0.3449  0.4407  319 GLY F C   
9778  O O   . GLY F 318 ? 1.7617 1.4873 2.0298 0.0671  0.3121  0.3885  319 GLY F O   
9779  N N   . LEU F 319 ? 1.7803 1.5668 2.1018 0.1525  0.4203  0.5023  320 LEU F N   
9780  C CA  . LEU F 319 ? 1.7846 1.5108 2.2442 0.1100  0.4646  0.5027  320 LEU F CA  
9781  C C   . LEU F 319 ? 1.8314 1.5439 2.4083 0.1120  0.4989  0.5180  320 LEU F C   
9782  O O   . LEU F 319 ? 1.8203 1.5565 2.3513 0.1324  0.4754  0.5175  320 LEU F O   
9783  C CB  . LEU F 319 ? 1.8118 1.5483 2.3368 0.1348  0.5379  0.5622  320 LEU F CB  
9784  C CG  . LEU F 319 ? 1.8725 1.5804 2.3480 0.1002  0.5139  0.5342  320 LEU F CG  
9785  C CD1 . LEU F 319 ? 1.8994 1.6428 2.4109 0.1449  0.5882  0.6093  320 LEU F CD1 
9786  C CD2 . LEU F 319 ? 1.8813 1.5087 2.4242 0.0278  0.4948  0.4718  320 LEU F CD2 
9787  N N   . ARG F 320 ? 1.8070 1.4804 2.5468 0.0908  0.5543  0.5292  321 ARG F N   
9788  C CA  . ARG F 320 ? 1.8151 1.4678 2.7165 0.0885  0.5956  0.5422  321 ARG F CA  
9789  C C   . ARG F 320 ? 1.9103 1.6135 2.9071 0.1700  0.6975  0.6527  321 ARG F C   
9790  O O   . ARG F 320 ? 1.9186 1.6846 2.7986 0.2356  0.7051  0.7040  321 ARG F O   
9791  C CB  . ARG F 320 ? 1.7854 1.3729 2.8314 0.0246  0.5946  0.4815  321 ARG F CB  
9792  C CG  . ARG F 320 ? 1.9445 1.5180 3.0440 0.0160  0.6351  0.4924  321 ARG F CG  
9793  C CD  . ARG F 320 ? 1.9912 1.5452 2.9362 -0.0190 0.5680  0.4374  321 ARG F CD  
9794  N NE  . ARG F 320 ? 1.9525 1.4507 2.9023 -0.0807 0.5020  0.3386  321 ARG F NE  
9795  C CZ  . ARG F 320 ? 1.9531 1.4194 2.8343 -0.1112 0.4651  0.2915  321 ARG F CZ  
9796  N NH1 . ARG F 320 ? 1.7115 1.1899 2.5226 -0.0945 0.4867  0.3332  321 ARG F NH1 
9797  N NH2 . ARG F 320 ? 1.6963 1.1213 2.5787 -0.1525 0.4081  0.2045  321 ARG F NH2 
9806  N N   . GLU G 1   ? 2.0275 1.9718 2.3014 0.4581  0.1337  -0.1048 1   GLU H N   
9807  C CA  . GLU G 1   ? 2.0210 1.9163 2.1695 0.4025  0.1142  -0.1270 1   GLU H CA  
9808  C C   . GLU G 1   ? 1.9466 1.8625 2.1175 0.3131  0.0379  -0.0959 1   GLU H C   
9809  O O   . GLU G 1   ? 1.8469 1.8448 2.1362 0.2853  0.0110  -0.0555 1   GLU H O   
9810  C CB  . GLU G 1   ? 1.9856 1.9828 2.1239 0.4002  0.1795  -0.1252 1   GLU H CB  
9811  C CG  . GLU G 1   ? 2.2779 2.2202 2.3152 0.4649  0.2443  -0.1726 1   GLU H CG  
9812  C CD  . GLU G 1   ? 2.7246 2.5135 2.5835 0.4434  0.2253  -0.2199 1   GLU H CD  
9813  O OE1 . GLU G 1   ? 2.6864 2.3685 2.4435 0.5038  0.2599  -0.2687 1   GLU H OE1 
9814  O OE2 . GLU G 1   ? 2.5895 2.3653 2.4075 0.3664  0.1785  -0.2060 1   GLU H OE2 
9815  N N   . VAL G 2   ? 1.9090 1.7565 1.9658 0.2657  0.0046  -0.1109 2   VAL H N   
9816  C CA  . VAL G 2   ? 1.8003 1.6751 1.8636 0.1858  -0.0614 -0.0828 2   VAL H CA  
9817  C C   . VAL G 2   ? 1.7375 1.6667 1.7658 0.1460  -0.0396 -0.0807 2   VAL H C   
9818  O O   . VAL G 2   ? 1.8156 1.6587 1.7294 0.1261  -0.0552 -0.0946 2   VAL H O   
9819  C CB  . VAL G 2   ? 1.9454 1.6890 1.9223 0.1599  -0.1458 -0.0840 2   VAL H CB  
9820  C CG1 . VAL G 2   ? 1.9431 1.6825 2.0058 0.1694  -0.1915 -0.0666 2   VAL H CG1 
9821  C CG2 . VAL G 2   ? 2.1294 1.7026 1.9426 0.1913  -0.1429 -0.1240 2   VAL H CG2 
9822  N N   . GLN G 3   ? 1.5095 1.5732 1.6342 0.1325  -0.0076 -0.0593 3   GLN H N   
9823  C CA  . GLN G 3   ? 1.4237 1.5363 1.5283 0.1009  0.0094  -0.0577 3   GLN H CA  
9824  C C   . GLN G 3   ? 1.2746 1.4949 1.4625 0.0559  -0.0068 -0.0304 3   GLN H C   
9825  O O   . GLN G 3   ? 1.1828 1.4711 1.4585 0.0521  -0.0088 -0.0092 3   GLN H O   
9826  C CB  . GLN G 3   ? 1.4691 1.6122 1.5620 0.1366  0.0728  -0.0700 3   GLN H CB  
9827  C CG  . GLN G 3   ? 1.6920 1.8589 1.8300 0.2014  0.1196  -0.0719 3   GLN H CG  
9828  C CD  . GLN G 3   ? 1.7450 2.0377 2.0126 0.2007  0.1323  -0.0295 3   GLN H CD  
9829  O OE1 . GLN G 3   ? 1.5538 1.9304 1.8616 0.1635  0.1308  -0.0049 3   GLN H OE1 
9830  N NE2 . GLN G 3   ? 1.6469 1.9482 1.9793 0.2424  0.1438  -0.0168 3   GLN H NE2 
9831  N N   . LEU G 4   ? 1.1877 1.4177 1.3440 0.0211  -0.0175 -0.0306 4   LEU H N   
9832  C CA  . LEU G 4   ? 1.0738 1.3894 1.2898 -0.0137 -0.0285 -0.0152 4   LEU H CA  
9833  C C   . LEU G 4   ? 1.0978 1.4583 1.3290 -0.0103 0.0034  -0.0153 4   LEU H C   
9834  O O   . LEU G 4   ? 1.1333 1.4573 1.3089 -0.0107 0.0136  -0.0253 4   LEU H O   
9835  C CB  . LEU G 4   ? 1.0586 1.3601 1.2413 -0.0515 -0.0701 -0.0098 4   LEU H CB  
9836  C CG  . LEU G 4   ? 1.1023 1.4028 1.2905 -0.0736 -0.1172 0.0043  4   LEU H CG  
9837  C CD1 . LEU G 4   ? 1.1252 1.3979 1.2553 -0.1060 -0.1581 0.0191  4   LEU H CD1 
9838  C CD2 . LEU G 4   ? 1.0238 1.4245 1.2985 -0.0941 -0.1223 0.0156  4   LEU H CD2 
9839  N N   . VAL G 5   ? 0.9966 1.4325 1.2978 -0.0145 0.0125  0.0010  5   VAL H N   
9840  C CA  . VAL G 5   ? 0.9802 1.4612 1.2982 -0.0174 0.0285  0.0106  5   VAL H CA  
9841  C C   . VAL G 5   ? 0.9868 1.4977 1.3302 -0.0479 0.0041  0.0118  5   VAL H C   
9842  O O   . VAL G 5   ? 0.9598 1.5077 1.3446 -0.0605 -0.0032 0.0228  5   VAL H O   
9843  C CB  . VAL G 5   ? 1.0327 1.5684 1.3985 0.0022  0.0543  0.0383  5   VAL H CB  
9844  C CG1 . VAL G 5   ? 1.0154 1.6003 1.3875 -0.0077 0.0593  0.0583  5   VAL H CG1 
9845  C CG2 . VAL G 5   ? 1.1002 1.6091 1.4510 0.0459  0.0841  0.0326  5   VAL H CG2 
9846  N N   . GLN G 6   ? 0.9362 1.4275 1.2540 -0.0605 -0.0086 0.0008  6   GLN H N   
9847  C CA  . GLN G 6   ? 0.8898 1.4018 1.2325 -0.0778 -0.0292 -0.0037 6   GLN H CA  
9848  C C   . GLN G 6   ? 0.9391 1.4769 1.3038 -0.0837 -0.0342 0.0074  6   GLN H C   
9849  O O   . GLN G 6   ? 0.9428 1.4962 1.3046 -0.0797 -0.0235 0.0263  6   GLN H O   
9850  C CB  . GLN G 6   ? 0.9140 1.3959 1.2337 -0.0886 -0.0451 -0.0107 6   GLN H CB  
9851  C CG  . GLN G 6   ? 0.8544 1.3275 1.1610 -0.0945 -0.0578 -0.0112 6   GLN H CG  
9852  C CD  . GLN G 6   ? 1.0021 1.4560 1.2958 -0.1102 -0.0757 -0.0031 6   GLN H CD  
9853  O OE1 . GLN G 6   ? 0.9794 1.3806 1.2223 -0.1233 -0.0802 0.0065  6   GLN H OE1 
9854  N NE2 . GLN G 6   ? 0.8545 1.3483 1.1931 -0.1099 -0.0854 -0.0049 6   GLN H NE2 
9855  N N   . SER G 7   ? 0.9038 1.4464 1.2861 -0.0923 -0.0534 -0.0023 7   SER H N   
9856  C CA  . SER G 7   ? 0.9251 1.4691 1.3144 -0.1017 -0.0734 0.0070  7   SER H CA  
9857  C C   . SER G 7   ? 1.0350 1.5661 1.4171 -0.1105 -0.0925 0.0148  7   SER H C   
9858  O O   . SER G 7   ? 1.0442 1.5588 1.4188 -0.1120 -0.0911 0.0064  7   SER H O   
9859  C CB  . SER G 7   ? 0.9791 1.5131 1.3774 -0.1009 -0.0878 -0.0165 7   SER H CB  
9860  O OG  . SER G 7   ? 1.1241 1.6333 1.5153 -0.1090 -0.1176 -0.0119 7   SER H OG  
9861  N N   . GLY G 8   ? 1.0195 1.5583 1.4007 -0.1253 -0.1177 0.0378  8   GLY H N   
9862  C CA  . GLY G 8   ? 1.0352 1.5736 1.4141 -0.1460 -0.1488 0.0529  8   GLY H CA  
9863  C C   . GLY G 8   ? 1.0886 1.5876 1.4875 -0.1513 -0.1844 0.0333  8   GLY H C   
9864  O O   . GLY G 8   ? 1.0937 1.5697 1.5058 -0.1318 -0.1826 0.0066  8   GLY H O   
9865  N N   . ALA G 9   ? 1.0304 1.5286 1.4363 -0.1790 -0.2174 0.0487  9   ALA H N   
9866  C CA  . ALA G 9   ? 1.0284 1.4919 1.4690 -0.1893 -0.2593 0.0404  9   ALA H CA  
9867  C C   . ALA G 9   ? 1.0634 1.4877 1.5167 -0.1741 -0.2958 0.0266  9   ALA H C   
9868  O O   . ALA G 9   ? 1.0736 1.4941 1.5003 -0.1852 -0.3214 0.0446  9   ALA H O   
9869  C CB  . ALA G 9   ? 1.0487 1.5268 1.4942 -0.2365 -0.2992 0.0705  9   ALA H CB  
9870  N N   . GLU G 10  ? 1.0132 1.4071 1.5010 -0.1473 -0.2972 -0.0029 10  GLU H N   
9871  C CA  . GLU G 10  ? 1.0559 1.3993 1.5469 -0.1214 -0.3238 -0.0291 10  GLU H CA  
9872  C C   . GLU G 10  ? 1.1088 1.4142 1.6568 -0.1140 -0.3686 -0.0374 10  GLU H C   
9873  O O   . GLU G 10  ? 1.0895 1.4166 1.6869 -0.1050 -0.3506 -0.0385 10  GLU H O   
9874  C CB  . GLU G 10  ? 1.0762 1.4279 1.5527 -0.0820 -0.2717 -0.0653 10  GLU H CB  
9875  C CG  . GLU G 10  ? 1.2180 1.5958 1.6472 -0.0924 -0.2398 -0.0549 10  GLU H CG  
9876  C CD  . GLU G 10  ? 1.6651 2.0080 2.0468 -0.1134 -0.2739 -0.0355 10  GLU H CD  
9877  O OE1 . GLU G 10  ? 1.6903 1.9683 2.0500 -0.1034 -0.3066 -0.0564 10  GLU H OE1 
9878  O OE2 . GLU G 10  ? 1.6097 1.9879 1.9727 -0.1390 -0.2684 0.0036  10  GLU H OE2 
9879  N N   . VAL G 11  ? 1.0971 1.3424 1.6389 -0.1213 -0.4339 -0.0360 11  VAL H N   
9880  C CA  . VAL G 11  ? 1.1298 1.3250 1.7317 -0.1114 -0.4887 -0.0440 11  VAL H CA  
9881  C C   . VAL G 11  ? 1.2840 1.3954 1.8564 -0.0646 -0.5073 -0.0879 11  VAL H C   
9882  O O   . VAL G 11  ? 1.3318 1.3916 1.8340 -0.0828 -0.5465 -0.0808 11  VAL H O   
9883  C CB  . VAL G 11  ? 1.1651 1.3547 1.7893 -0.1743 -0.5701 0.0031  11  VAL H CB  
9884  C CG1 . VAL G 11  ? 1.2063 1.3422 1.9093 -0.1655 -0.6319 -0.0020 11  VAL H CG1 
9885  C CG2 . VAL G 11  ? 1.0855 1.3537 1.7165 -0.2242 -0.5456 0.0415  11  VAL H CG2 
9886  N N   . LYS G 12  ? 1.2516 1.3508 1.8706 -0.0050 -0.4781 -0.1302 12  LYS H N   
9887  C CA  . LYS G 12  ? 1.3448 1.3610 1.9325 0.0512  -0.4842 -0.1845 12  LYS H CA  
9888  C C   . LYS G 12  ? 1.4179 1.4145 2.0980 0.1053  -0.4938 -0.2096 12  LYS H C   
9889  O O   . LYS G 12  ? 1.3296 1.4060 2.0929 0.1119  -0.4598 -0.1912 12  LYS H O   
9890  C CB  . LYS G 12  ? 1.3694 1.4145 1.8952 0.0817  -0.4070 -0.2222 12  LYS H CB  
9891  C CG  . LYS G 12  ? 1.5050 1.5159 1.9257 0.0417  -0.4176 -0.2092 12  LYS H CG  
9892  C CD  . LYS G 12  ? 1.6116 1.6295 1.9714 0.0672  -0.3555 -0.2508 12  LYS H CD  
9893  C CE  . LYS G 12  ? 1.6743 1.6634 1.9398 0.0171  -0.3681 -0.2237 12  LYS H CE  
9894  N NZ  . LYS G 12  ? 1.8831 1.8573 2.0806 0.0312  -0.3220 -0.2649 12  LYS H NZ  
9895  N N   . LYS G 13  ? 1.4973 1.3830 2.1609 0.1442  -0.5427 -0.2475 13  LYS H N   
9896  C CA  . LYS G 13  ? 1.5624 1.4154 2.3178 0.2091  -0.5552 -0.2768 13  LYS H CA  
9897  C C   . LYS G 13  ? 1.6210 1.5390 2.3944 0.2879  -0.4575 -0.3268 13  LYS H C   
9898  O O   . LYS G 13  ? 1.6126 1.5440 2.2948 0.2953  -0.4041 -0.3576 13  LYS H O   
9899  C CB  . LYS G 13  ? 1.7455 1.4412 2.4597 0.2288  -0.6434 -0.3065 13  LYS H CB  
9900  C CG  . LYS G 13  ? 2.0146 1.6656 2.7308 0.1454  -0.7543 -0.2457 13  LYS H CG  
9901  C CD  . LYS G 13  ? 2.3584 1.8432 3.0040 0.1527  -0.8540 -0.2678 13  LYS H CD  
9902  C CE  . LYS G 13  ? 2.5432 2.0500 3.1228 0.0466  -0.9030 -0.1862 13  LYS H CE  
9903  N NZ  . LYS G 13  ? 2.7267 2.2226 3.1527 0.0238  -0.8191 -0.1658 13  LYS H NZ  
9904  N N   . PRO G 14  ? 1.5633 1.5370 2.4571 0.3399  -0.4339 -0.3266 14  PRO H N   
9905  C CA  . PRO G 14  ? 1.5574 1.6247 2.4732 0.4099  -0.3403 -0.3622 14  PRO H CA  
9906  C C   . PRO G 14  ? 1.7349 1.7363 2.5620 0.4804  -0.3054 -0.4465 14  PRO H C   
9907  O O   . PRO G 14  ? 1.8551 1.7127 2.6336 0.5055  -0.3597 -0.4870 14  PRO H O   
9908  C CB  . PRO G 14  ? 1.5702 1.6949 2.6407 0.4500  -0.3421 -0.3337 14  PRO H CB  
9909  C CG  . PRO G 14  ? 1.5703 1.6708 2.6957 0.3695  -0.4209 -0.2647 14  PRO H CG  
9910  C CD  . PRO G 14  ? 1.5719 1.5443 2.5950 0.3287  -0.4921 -0.2821 14  PRO H CD  
9911  N N   . GLY G 15  ? 1.6709 1.7762 2.4690 0.5041  -0.2199 -0.4694 15  GLY H N   
9912  C CA  . GLY G 15  ? 1.7918 1.8645 2.4955 0.5596  -0.1705 -0.5480 15  GLY H CA  
9913  C C   . GLY G 15  ? 1.8287 1.8793 2.3957 0.4935  -0.1614 -0.5520 15  GLY H C   
9914  O O   . GLY G 15  ? 1.8602 1.9567 2.3618 0.5103  -0.0995 -0.5936 15  GLY H O   
9915  N N   . GLU G 16  ? 1.7227 1.7145 2.2526 0.4139  -0.2238 -0.5024 16  GLU H N   
9916  C CA  . GLU G 16  ? 1.6959 1.6630 2.1127 0.3431  -0.2290 -0.4865 16  GLU H CA  
9917  C C   . GLU G 16  ? 1.6372 1.7470 2.0551 0.3118  -0.1608 -0.4661 16  GLU H C   
9918  O O   . GLU G 16  ? 1.5401 1.7732 2.0473 0.3298  -0.1212 -0.4475 16  GLU H O   
9919  C CB  . GLU G 16  ? 1.6660 1.5750 2.0748 0.2722  -0.3081 -0.4251 16  GLU H CB  
9920  C CG  . GLU G 16  ? 1.9337 1.6762 2.2806 0.2729  -0.3938 -0.4395 16  GLU H CG  
9921  C CD  . GLU G 16  ? 2.0220 1.7319 2.3501 0.1927  -0.4730 -0.3703 16  GLU H CD  
9922  O OE1 . GLU G 16  ? 1.6703 1.3818 2.0812 0.1804  -0.5275 -0.3368 16  GLU H OE1 
9923  O OE2 . GLU G 16  ? 2.0143 1.7083 2.2497 0.1379  -0.4809 -0.3436 16  GLU H OE2 
9924  N N   . SER G 17  ? 1.6069 1.6955 1.9249 0.2592  -0.1555 -0.4622 17  SER H N   
9925  C CA  . SER G 17  ? 1.5072 1.7127 1.8184 0.2184  -0.1058 -0.4398 17  SER H CA  
9926  C C   . SER G 17  ? 1.4346 1.6497 1.7463 0.1476  -0.1368 -0.3722 17  SER H C   
9927  O O   . SER G 17  ? 1.4771 1.6017 1.7255 0.1093  -0.1831 -0.3523 17  SER H O   
9928  C CB  . SER G 17  ? 1.6606 1.8442 1.8683 0.2080  -0.0746 -0.4826 17  SER H CB  
9929  O OG  . SER G 17  ? 1.7408 2.0448 1.9541 0.1649  -0.0336 -0.4591 17  SER H OG  
9930  N N   . LEU G 18  ? 1.2407 1.5651 1.6202 0.1321  -0.1130 -0.3343 18  LEU H N   
9931  C CA  . LEU G 18  ? 1.1286 1.4744 1.5151 0.0777  -0.1300 -0.2767 18  LEU H CA  
9932  C C   . LEU G 18  ? 1.1057 1.5538 1.5010 0.0537  -0.0881 -0.2594 18  LEU H C   
9933  O O   . LEU G 18  ? 1.0848 1.6130 1.5171 0.0782  -0.0558 -0.2724 18  LEU H O   
9934  C CB  . LEU G 18  ? 1.0734 1.4223 1.5303 0.0809  -0.1585 -0.2453 18  LEU H CB  
9935  C CG  . LEU G 18  ? 1.0437 1.4041 1.5008 0.0310  -0.1772 -0.1924 18  LEU H CG  
9936  C CD1 . LEU G 18  ? 1.0917 1.3738 1.5114 0.0039  -0.2320 -0.1735 18  LEU H CD1 
9937  C CD2 . LEU G 18  ? 0.9898 1.3914 1.5117 0.0288  -0.1791 -0.1651 18  LEU H CD2 
9938  N N   . THR G 19  ? 1.0209 1.4706 1.3867 0.0055  -0.0936 -0.2244 19  THR H N   
9939  C CA  . THR G 19  ? 0.9469 1.4782 1.3235 -0.0222 -0.0670 -0.2025 19  THR H CA  
9940  C C   . THR G 19  ? 0.9437 1.4712 1.3320 -0.0496 -0.0811 -0.1552 19  THR H C   
9941  O O   . THR G 19  ? 0.9604 1.4404 1.3214 -0.0707 -0.1024 -0.1333 19  THR H O   
9942  C CB  . THR G 19  ? 1.0544 1.6044 1.3847 -0.0497 -0.0493 -0.2171 19  THR H CB  
9943  O OG1 . THR G 19  ? 0.9355 1.5588 1.2858 -0.0838 -0.0375 -0.1873 19  THR H OG1 
9944  C CG2 . THR G 19  ? 1.1080 1.5702 1.3726 -0.0793 -0.0731 -0.2100 19  THR H CG2 
9945  N N   . ILE G 20  ? 0.8426 1.4182 1.2652 -0.0483 -0.0713 -0.1371 20  ILE H N   
9946  C CA  . ILE G 20  ? 0.8059 1.3729 1.2303 -0.0662 -0.0779 -0.1015 20  ILE H CA  
9947  C C   . ILE G 20  ? 0.8453 1.4538 1.2669 -0.0860 -0.0628 -0.0844 20  ILE H C   
9948  O O   . ILE G 20  ? 0.8327 1.4898 1.2647 -0.0869 -0.0554 -0.0898 20  ILE H O   
9949  C CB  . ILE G 20  ? 0.8345 1.3886 1.2815 -0.0569 -0.0895 -0.0903 20  ILE H CB  
9950  C CG1 . ILE G 20  ? 0.8316 1.4297 1.3072 -0.0424 -0.0812 -0.0943 20  ILE H CG1 
9951  C CG2 . ILE G 20  ? 0.8763 1.3797 1.3295 -0.0516 -0.1189 -0.0938 20  ILE H CG2 
9952  C CD1 . ILE G 20  ? 0.9004 1.4887 1.3854 -0.0525 -0.0923 -0.0659 20  ILE H CD1 
9953  N N   . SER G 21  ? 0.8012 1.3956 1.2130 -0.1024 -0.0628 -0.0590 21  SER H N   
9954  C CA  . SER G 21  ? 0.7738 1.3943 1.1912 -0.1185 -0.0541 -0.0392 21  SER H CA  
9955  C C   . SER G 21  ? 0.8258 1.4346 1.2396 -0.1081 -0.0519 -0.0284 21  SER H C   
9956  O O   . SER G 21  ? 0.8479 1.4297 1.2513 -0.0962 -0.0553 -0.0310 21  SER H O   
9957  C CB  . SER G 21  ? 0.8212 1.4364 1.2384 -0.1373 -0.0534 -0.0114 21  SER H CB  
9958  O OG  . SER G 21  ? 0.9637 1.5527 1.3723 -0.1290 -0.0588 0.0066  21  SER H OG  
9959  N N   . CYS G 22  ? 0.7577 1.3790 1.1759 -0.1174 -0.0512 -0.0153 22  CYS H N   
9960  C CA  . CYS G 22  ? 0.7691 1.3608 1.1677 -0.1084 -0.0539 -0.0078 22  CYS H CA  
9961  C C   . CYS G 22  ? 0.7810 1.3848 1.2012 -0.1179 -0.0555 0.0091  22  CYS H C   
9962  O O   . CYS G 22  ? 0.7724 1.4141 1.2111 -0.1438 -0.0729 0.0130  22  CYS H O   
9963  C CB  . CYS G 22  ? 0.7893 1.3866 1.1710 -0.1154 -0.0731 -0.0118 22  CYS H CB  
9964  S SG  . CYS G 22  ? 0.8827 1.4402 1.2265 -0.1229 -0.0978 0.0042  22  CYS H SG  
9965  N N   . LYS G 23  ? 0.7176 1.3015 1.1440 -0.0994 -0.0379 0.0230  23  LYS H N   
9966  C CA  . LYS G 23  ? 0.6989 1.2962 1.1641 -0.1022 -0.0365 0.0467  23  LYS H CA  
9967  C C   . LYS G 23  ? 0.8089 1.3577 1.2580 -0.0785 -0.0415 0.0439  23  LYS H C   
9968  O O   . LYS G 23  ? 0.8723 1.3794 1.2895 -0.0423 -0.0188 0.0355  23  LYS H O   
9969  C CB  . LYS G 23  ? 0.7003 1.3216 1.1943 -0.0946 -0.0134 0.0746  23  LYS H CB  
9970  C CG  . LYS G 23  ? 0.6787 1.3407 1.2293 -0.1243 -0.0201 0.1123  23  LYS H CG  
9971  C CD  . LYS G 23  ? 0.7744 1.4366 1.3685 -0.0990 -0.0085 0.1382  23  LYS H CD  
9972  C CE  . LYS G 23  ? 0.8360 1.5436 1.4993 -0.1375 -0.0194 0.1881  23  LYS H CE  
9973  N NZ  . LYS G 23  ? 0.9584 1.6646 1.6805 -0.1111 -0.0151 0.2122  23  LYS H NZ  
9974  N N   . GLY G 24  ? 0.7516 1.3047 1.2182 -0.1019 -0.0747 0.0512  24  GLY H N   
9975  C CA  . GLY G 24  ? 0.8160 1.3090 1.2643 -0.0849 -0.0957 0.0503  24  GLY H CA  
9976  C C   . GLY G 24  ? 0.9318 1.4192 1.4303 -0.0537 -0.0740 0.0673  24  GLY H C   
9977  O O   . GLY G 24  ? 0.8933 1.4408 1.4655 -0.0772 -0.0738 0.0982  24  GLY H O   
9978  N N   . SER G 25  ? 0.9879 1.4042 1.4454 -0.0010 -0.0536 0.0500  25  SER H N   
9979  C CA  . SER G 25  ? 1.0250 1.4424 1.5331 0.0453  -0.0222 0.0643  25  SER H CA  
9980  C C   . SER G 25  ? 1.1521 1.4743 1.6332 0.0863  -0.0388 0.0468  25  SER H C   
9981  O O   . SER G 25  ? 1.2208 1.4493 1.6026 0.1001  -0.0515 0.0134  25  SER H O   
9982  C CB  . SER G 25  ? 1.1067 1.5519 1.6004 0.0834  0.0362  0.0615  25  SER H CB  
9983  O OG  . SER G 25  ? 1.1872 1.6862 1.6747 0.0480  0.0400  0.0679  25  SER H OG  
9984  N N   . GLY G 26  ? 1.1115 1.4522 1.6800 0.1041  -0.0408 0.0735  26  GLY H N   
9985  C CA  . GLY G 26  ? 1.2183 1.4672 1.7816 0.1526  -0.0572 0.0594  26  GLY H CA  
9986  C C   . GLY G 26  ? 1.2998 1.4679 1.8239 0.1156  -0.1398 0.0525  26  GLY H C   
9987  O O   . GLY G 26  ? 1.4136 1.4657 1.8876 0.1583  -0.1617 0.0286  26  GLY H O   
9988  N N   . TYR G 27  ? 1.1635 1.3924 1.7055 0.0358  -0.1895 0.0750  27  TYR H N   
9989  C CA  . TYR G 27  ? 1.1861 1.3706 1.6968 -0.0151 -0.2778 0.0822  27  TYR H CA  
9990  C C   . TYR G 27  ? 1.1200 1.4238 1.7090 -0.1025 -0.3207 0.1218  27  TYR H C   
9991  O O   . TYR G 27  ? 1.0213 1.4229 1.6589 -0.1239 -0.2785 0.1342  27  TYR H O   
9992  C CB  . TYR G 27  ? 1.2639 1.3625 1.6332 -0.0175 -0.2975 0.0535  27  TYR H CB  
9993  C CG  . TYR G 27  ? 1.1795 1.3633 1.5291 -0.0692 -0.2938 0.0603  27  TYR H CG  
9994  C CD1 . TYR G 27  ? 1.1431 1.3768 1.4928 -0.0503 -0.2239 0.0459  27  TYR H CD1 
9995  C CD2 . TYR G 27  ? 1.1601 1.3797 1.4941 -0.1357 -0.3633 0.0839  27  TYR H CD2 
9996  C CE1 . TYR G 27  ? 1.0586 1.3619 1.3971 -0.0895 -0.2218 0.0493  27  TYR H CE1 
9997  C CE2 . TYR G 27  ? 1.0937 1.3996 1.4183 -0.1726 -0.3534 0.0891  27  TYR H CE2 
9998  C CZ  . TYR G 27  ? 1.1133 1.4530 1.4411 -0.1456 -0.2817 0.0688  27  TYR H CZ  
9999  O OH  . TYR G 27  ? 1.0520 1.4675 1.3762 -0.1745 -0.2744 0.0713  27  TYR H OH  
10000 N N   . SER G 28  ? 1.2161 1.2715 1.7180 -0.0175 -0.0410 0.0663  28  SER H N   
10001 C CA  . SER G 28  ? 1.2098 1.2837 1.6747 -0.0486 -0.0770 0.1209  28  SER H CA  
10002 C C   . SER G 28  ? 1.2288 1.3081 1.5727 -0.0668 -0.0720 0.0923  28  SER H C   
10003 O O   . SER G 28  ? 1.2286 1.2867 1.5487 -0.0753 -0.0708 0.0764  28  SER H O   
10004 C CB  . SER G 28  ? 1.2871 1.3378 1.8277 -0.0574 -0.0985 0.1584  28  SER H CB  
10005 O OG  . SER G 28  ? 1.4043 1.4776 1.9003 -0.0955 -0.1328 0.2096  28  SER H OG  
10006 N N   . PHE G 29  ? 1.1599 1.2677 1.4350 -0.0716 -0.0677 0.0847  29  PHE H N   
10007 C CA  . PHE G 29  ? 1.1359 1.2529 1.3091 -0.0852 -0.0603 0.0575  29  PHE H CA  
10008 C C   . PHE G 29  ? 1.1739 1.2922 1.3075 -0.1154 -0.0759 0.0733  29  PHE H C   
10009 O O   . PHE G 29  ? 1.1542 1.2632 1.2365 -0.1177 -0.0642 0.0391  29  PHE H O   
10010 C CB  . PHE G 29  ? 1.1406 1.2898 1.2688 -0.0911 -0.0600 0.0646  29  PHE H CB  
10011 C CG  . PHE G 29  ? 1.1410 1.2989 1.1800 -0.1021 -0.0501 0.0367  29  PHE H CG  
10012 C CD1 . PHE G 29  ? 1.1701 1.3175 1.1790 -0.0830 -0.0290 -0.0085 29  PHE H CD1 
10013 C CD2 . PHE G 29  ? 1.1606 1.3397 1.1509 -0.1346 -0.0613 0.0564  29  PHE H CD2 
10014 C CE1 . PHE G 29  ? 1.1614 1.3166 1.1038 -0.0916 -0.0224 -0.0287 29  PHE H CE1 
10015 C CE2 . PHE G 29  ? 1.1795 1.3650 1.1035 -0.1427 -0.0484 0.0280  29  PHE H CE2 
10016 C CZ  . PHE G 29  ? 1.1399 1.3122 1.0459 -0.1186 -0.0306 -0.0119 29  PHE H CZ  
10017 N N   . SER G 30  ? 1.1451 1.2789 1.3045 -0.1415 -0.1030 0.1268  30  SER H N   
10018 C CA  . SER G 30  ? 1.1602 1.3029 1.2837 -0.1794 -0.1200 0.1485  30  SER H CA  
10019 C C   . SER G 30  ? 1.2245 1.3346 1.3746 -0.1770 -0.1211 0.1387  30  SER H C   
10020 O O   . SER G 30  ? 1.2206 1.3356 1.3220 -0.2032 -0.1244 0.1342  30  SER H O   
10021 C CB  . SER G 30  ? 1.2323 1.4076 1.3734 -0.2156 -0.1514 0.2134  30  SER H CB  
10022 O OG  . SER G 30  ? 1.3651 1.5435 1.5875 -0.1972 -0.1627 0.2468  30  SER H OG  
10023 N N   . SER G 31  ? 1.1908 1.2683 1.4194 -0.1475 -0.1154 0.1320  31  SER H N   
10024 C CA  . SER G 31  ? 1.2060 1.2477 1.4664 -0.1445 -0.1137 0.1196  31  SER H CA  
10025 C C   . SER G 31  ? 1.2402 1.2688 1.4355 -0.1384 -0.0898 0.0617  31  SER H C   
10026 O O   . SER G 31  ? 1.2525 1.2749 1.4213 -0.1580 -0.0957 0.0598  31  SER H O   
10027 C CB  . SER G 31  ? 1.2614 1.2710 1.6282 -0.1152 -0.1071 0.1196  31  SER H CB  
10028 O OG  . SER G 31  ? 1.3738 1.3906 1.8218 -0.1244 -0.1366 0.1835  31  SER H OG  
10029 N N   . TYR G 32  ? 1.1616 1.1901 1.3328 -0.1146 -0.0651 0.0183  32  TYR H N   
10030 C CA  . TYR G 32  ? 1.1448 1.1659 1.2616 -0.1094 -0.0453 -0.0315 32  TYR H CA  
10031 C C   . TYR G 32  ? 1.1570 1.2079 1.1963 -0.1227 -0.0452 -0.0385 32  TYR H C   
10032 O O   . TYR G 32  ? 1.1376 1.2119 1.1604 -0.1246 -0.0480 -0.0239 32  TYR H O   
10033 C CB  . TYR G 32  ? 1.1597 1.1678 1.2940 -0.0831 -0.0202 -0.0722 32  TYR H CB  
10034 C CG  . TYR G 32  ? 1.2194 1.1967 1.4396 -0.0683 -0.0106 -0.0778 32  TYR H CG  
10035 C CD1 . TYR G 32  ? 1.2792 1.2262 1.5140 -0.0681 0.0046  -0.1120 32  TYR H CD1 
10036 C CD2 . TYR G 32  ? 1.2355 1.2152 1.5275 -0.0547 -0.0135 -0.0530 32  TYR H CD2 
10037 C CE1 . TYR G 32  ? 1.3398 1.2554 1.6609 -0.0551 0.0198  -0.1250 32  TYR H CE1 
10038 C CE2 . TYR G 32  ? 1.2812 1.2319 1.6680 -0.0387 -0.0002 -0.0624 32  TYR H CE2 
10039 C CZ  . TYR G 32  ? 1.4338 1.3505 1.8360 -0.0389 0.0183  -0.1009 32  TYR H CZ  
10040 O OH  . TYR G 32  ? 1.4987 1.3840 2.0025 -0.0242 0.0366  -0.1158 32  TYR H OH  
10041 N N   . TRP G 33  ? 1.0977 1.1477 1.0957 -0.1318 -0.0402 -0.0626 33  TRP H N   
10042 C CA  . TRP G 33  ? 1.0704 1.1454 1.0101 -0.1423 -0.0362 -0.0755 33  TRP H CA  
10043 C C   . TRP G 33  ? 1.1174 1.1982 1.0368 -0.1216 -0.0217 -0.1023 33  TRP H C   
10044 O O   . TRP G 33  ? 1.1337 1.1986 1.0674 -0.1058 -0.0119 -0.1243 33  TRP H O   
10045 C CB  . TRP G 33  ? 1.0574 1.1290 0.9772 -0.1542 -0.0347 -0.0937 33  TRP H CB  
10046 C CG  . TRP G 33  ? 1.0893 1.1692 1.0050 -0.1844 -0.0477 -0.0707 33  TRP H CG  
10047 C CD1 . TRP G 33  ? 1.1514 1.2138 1.0994 -0.1967 -0.0612 -0.0477 33  TRP H CD1 
10048 C CD2 . TRP G 33  ? 1.0759 1.1841 0.9547 -0.2093 -0.0462 -0.0725 33  TRP H CD2 
10049 N NE1 . TRP G 33  ? 1.1509 1.2322 1.0768 -0.2309 -0.0713 -0.0309 33  TRP H NE1 
10050 C CE2 . TRP G 33  ? 1.1458 1.2564 1.0286 -0.2399 -0.0598 -0.0492 33  TRP H CE2 
10051 C CE3 . TRP G 33  ? 1.0724 1.2042 0.9208 -0.2104 -0.0333 -0.0924 33  TRP H CE3 
10052 C CZ2 . TRP G 33  ? 1.1398 1.2798 0.9909 -0.2747 -0.0583 -0.0485 33  TRP H CZ2 
10053 C CZ3 . TRP G 33  ? 1.0933 1.2509 0.9196 -0.2413 -0.0294 -0.0937 33  TRP H CZ3 
10054 C CH2 . TRP G 33  ? 1.1243 1.2877 0.9487 -0.2746 -0.0406 -0.0741 33  TRP H CH2 
10055 N N   . ILE G 34  ? 1.0525 1.1562 0.9388 -0.1255 -0.0194 -0.1017 34  ILE H N   
10056 C CA  . ILE G 34  ? 1.0310 1.1417 0.8975 -0.1096 -0.0093 -0.1215 34  ILE H CA  
10057 C C   . ILE G 34  ? 1.0668 1.1901 0.9057 -0.1153 -0.0057 -0.1378 34  ILE H C   
10058 O O   . ILE G 34  ? 1.0728 1.2104 0.9002 -0.1314 -0.0057 -0.1316 34  ILE H O   
10059 C CB  . ILE G 34  ? 1.0613 1.1850 0.9251 -0.1059 -0.0092 -0.1057 34  ILE H CB  
10060 C CG1 . ILE G 34  ? 1.0848 1.1991 0.9910 -0.0958 -0.0122 -0.0896 34  ILE H CG1 
10061 C CG2 . ILE G 34  ? 1.0450 1.1778 0.8830 -0.0949 -0.0009 -0.1231 34  ILE H CG2 
10062 C CD1 . ILE G 34  ? 1.2130 1.3112 1.1417 -0.0758 0.0001  -0.1151 34  ILE H CD1 
10063 N N   . GLY G 35  ? 1.0198 1.1403 0.8524 -0.1053 -0.0022 -0.1582 35  GLY H N   
10064 C CA  . GLY G 35  ? 1.0170 1.1512 0.8379 -0.1081 -0.0019 -0.1693 35  GLY H CA  
10065 C C   . GLY G 35  ? 1.0816 1.2267 0.8921 -0.0987 -0.0003 -0.1718 35  GLY H C   
10066 O O   . GLY G 35  ? 1.0997 1.2431 0.9047 -0.0913 0.0019  -0.1667 35  GLY H O   
10067 N N   . TRP G 36  ? 1.0178 1.1753 0.8316 -0.0994 -0.0025 -0.1773 36  TRP H N   
10068 C CA  . TRP G 36  ? 0.9998 1.1672 0.8121 -0.0922 -0.0048 -0.1751 36  TRP H CA  
10069 C C   . TRP G 36  ? 1.0406 1.2201 0.8633 -0.0938 -0.0150 -0.1769 36  TRP H C   
10070 O O   . TRP G 36  ? 1.0416 1.2288 0.8848 -0.0987 -0.0160 -0.1794 36  TRP H O   
10071 C CB  . TRP G 36  ? 0.9704 1.1439 0.7913 -0.0938 0.0034  -0.1716 36  TRP H CB  
10072 C CG  . TRP G 36  ? 0.9805 1.1493 0.7851 -0.0948 0.0092  -0.1642 36  TRP H CG  
10073 C CD1 . TRP G 36  ? 1.0186 1.1863 0.8180 -0.1067 0.0135  -0.1581 36  TRP H CD1 
10074 C CD2 . TRP G 36  ? 0.9730 1.1419 0.7653 -0.0872 0.0090  -0.1583 36  TRP H CD2 
10075 N NE1 . TRP G 36  ? 1.0142 1.1829 0.8011 -0.1067 0.0153  -0.1474 36  TRP H NE1 
10076 C CE2 . TRP G 36  ? 1.0278 1.1963 0.8097 -0.0936 0.0140  -0.1494 36  TRP H CE2 
10077 C CE3 . TRP G 36  ? 0.9875 1.1595 0.7758 -0.0792 0.0030  -0.1567 36  TRP H CE3 
10078 C CZ2 . TRP G 36  ? 1.0145 1.1853 0.7835 -0.0896 0.0152  -0.1418 36  TRP H CZ2 
10079 C CZ3 . TRP G 36  ? 1.0048 1.1774 0.7774 -0.0761 0.0048  -0.1502 36  TRP H CZ3 
10080 C CH2 . TRP G 36  ? 1.0105 1.1822 0.7742 -0.0800 0.0118  -0.1443 36  TRP H CH2 
10081 N N   . VAL G 37  ? 0.9877 1.1728 0.7969 -0.0936 -0.0236 -0.1740 37  VAL H N   
10082 C CA  . VAL G 37  ? 0.9959 1.1985 0.8115 -0.1018 -0.0387 -0.1684 37  VAL H CA  
10083 C C   . VAL G 37  ? 1.0940 1.3095 0.9164 -0.0999 -0.0501 -0.1515 37  VAL H C   
10084 O O   . VAL G 37  ? 1.0964 1.3099 0.8932 -0.1004 -0.0493 -0.1501 37  VAL H O   
10085 C CB  . VAL G 37  ? 1.0511 1.2537 0.8400 -0.1160 -0.0410 -0.1800 37  VAL H CB  
10086 C CG1 . VAL G 37  ? 1.0605 1.2883 0.8482 -0.1327 -0.0600 -0.1696 37  VAL H CG1 
10087 C CG2 . VAL G 37  ? 1.0495 1.2371 0.8421 -0.1182 -0.0322 -0.1935 37  VAL H CG2 
10088 N N   . ARG G 38  ? 1.0673 1.2967 0.9312 -0.0981 -0.0605 -0.1377 38  ARG H N   
10089 C CA  . ARG G 38  ? 1.0699 1.3110 0.9577 -0.0967 -0.0754 -0.1156 38  ARG H CA  
10090 C C   . ARG G 38  ? 1.1766 1.4423 1.0578 -0.1155 -0.1012 -0.0968 38  ARG H C   
10091 O O   . ARG G 38  ? 1.1846 1.4609 1.0619 -0.1271 -0.1066 -0.1010 38  ARG H O   
10092 C CB  . ARG G 38  ? 1.0271 1.2696 0.9804 -0.0849 -0.0706 -0.1113 38  ARG H CB  
10093 C CG  . ARG G 38  ? 1.1157 1.3716 1.1194 -0.0831 -0.0904 -0.0831 38  ARG H CG  
10094 C CD  . ARG G 38  ? 1.2534 1.5026 1.3274 -0.0689 -0.0759 -0.0873 38  ARG H CD  
10095 N NE  . ARG G 38  ? 1.4971 1.7663 1.6474 -0.0669 -0.0876 -0.0740 38  ARG H NE  
10096 C CZ  . ARG G 38  ? 1.8222 2.0906 2.0564 -0.0551 -0.0761 -0.0765 38  ARG H CZ  
10097 N NH1 . ARG G 38  ? 1.7158 1.9629 1.9605 -0.0476 -0.0512 -0.0942 38  ARG H NH1 
10098 N NH2 . ARG G 38  ? 1.7352 2.0256 2.0477 -0.0525 -0.0876 -0.0628 38  ARG H NH2 
10099 N N   . ARG G 39  ? 1.1688 1.4458 1.0465 -0.1231 -0.1182 -0.0744 39  ARG H N   
10100 C CA  . ARG G 39  ? 1.2032 1.5100 1.0724 -0.1490 -0.1473 -0.0488 39  ARG H CA  
10101 C C   . ARG G 39  ? 1.2802 1.5963 1.1967 -0.1457 -0.1684 -0.0130 39  ARG H C   
10102 O O   . ARG G 39  ? 1.2679 1.5728 1.1684 -0.1415 -0.1646 -0.0100 39  ARG H O   
10103 C CB  . ARG G 39  ? 1.2271 1.5393 1.0221 -0.1729 -0.1437 -0.0632 39  ARG H CB  
10104 C CG  . ARG G 39  ? 1.3631 1.7087 1.1337 -0.2078 -0.1723 -0.0352 39  ARG H CG  
10105 C CD  . ARG G 39  ? 1.4993 1.8760 1.2628 -0.2396 -0.1925 -0.0241 39  ARG H CD  
10106 N NE  . ARG G 39  ? 1.6283 2.0041 1.3303 -0.2617 -0.1728 -0.0615 39  ARG H NE  
10107 C CZ  . ARG G 39  ? 1.8729 2.2713 1.5549 -0.2932 -0.1813 -0.0646 39  ARG H CZ  
10108 N NH1 . ARG G 39  ? 1.7474 2.1749 1.4661 -0.3060 -0.2126 -0.0282 39  ARG H NH1 
10109 N NH2 . ARG G 39  ? 1.7557 2.1479 1.3868 -0.3130 -0.1576 -0.1046 39  ARG H NH2 
10110 N N   . MET G 40  ? 1.2642 1.5994 1.2472 -0.1462 -0.1900 0.0149  40  MET H N   
10111 C CA  . MET G 40  ? 1.2800 1.6229 1.3260 -0.1425 -0.2126 0.0536  40  MET H CA  
10112 C C   . MET G 40  ? 1.3836 1.7593 1.4013 -0.1782 -0.2509 0.0940  40  MET H C   
10113 O O   . MET G 40  ? 1.4099 1.8115 1.3837 -0.2075 -0.2634 0.0955  40  MET H O   
10114 C CB  . MET G 40  ? 1.2989 1.6476 1.4476 -0.1246 -0.2165 0.0663  40  MET H CB  
10115 C CG  . MET G 40  ? 1.3231 1.6398 1.5173 -0.0941 -0.1825 0.0386  40  MET H CG  
10116 S SD  . MET G 40  ? 1.3833 1.7047 1.7217 -0.0749 -0.1898 0.0635  40  MET H SD  
10117 C CE  . MET G 40  ? 1.3680 1.6902 1.7229 -0.0838 -0.2228 0.1120  40  MET H CE  
10118 N N   . PRO G 41  ? 1.3469 1.7234 1.3836 -0.1819 -0.2694 0.1260  41  PRO H N   
10119 C CA  . PRO G 41  ? 1.3777 1.7904 1.3808 -0.2241 -0.3082 0.1676  41  PRO H CA  
10120 C C   . PRO G 41  ? 1.4314 1.8869 1.4728 -0.2507 -0.3467 0.2090  41  PRO H C   
10121 O O   . PRO G 41  ? 1.4121 1.8744 1.5546 -0.2355 -0.3662 0.2432  41  PRO H O   
10122 C CB  . PRO G 41  ? 1.4082 1.8093 1.4500 -0.2167 -0.3218 0.1988  41  PRO H CB  
10123 C CG  . PRO G 41  ? 1.4368 1.8022 1.5625 -0.1715 -0.2968 0.1822  41  PRO H CG  
10124 C CD  . PRO G 41  ? 1.3522 1.6980 1.4383 -0.1535 -0.2559 0.1259  41  PRO H CD  
10125 N N   . GLY G 42  ? 1.4210 1.9059 1.3844 -0.2915 -0.3546 0.2027  42  GLY H N   
10126 C CA  . GLY G 42  ? 1.4535 1.9857 1.4317 -0.3280 -0.3911 0.2395  42  GLY H CA  
10127 C C   . GLY G 42  ? 1.4898 2.0187 1.5168 -0.3056 -0.3789 0.2222  42  GLY H C   
10128 O O   . GLY G 42  ? 1.5077 2.0700 1.6020 -0.3160 -0.4116 0.2645  42  GLY H O   
10129 N N   . LYS G 43  ? 1.4079 1.8990 1.4051 -0.2763 -0.3335 0.1632  43  LYS H N   
10130 C CA  . LYS G 43  ? 1.3799 1.8640 1.4108 -0.2563 -0.3160 0.1389  43  LYS H CA  
10131 C C   . LYS G 43  ? 1.4236 1.8874 1.3684 -0.2615 -0.2812 0.0830  43  LYS H C   
10132 O O   . LYS G 43  ? 1.4273 1.8821 1.2969 -0.2771 -0.2684 0.0618  43  LYS H O   
10133 C CB  . LYS G 43  ? 1.3701 1.8245 1.4913 -0.2072 -0.2962 0.1305  43  LYS H CB  
10134 C CG  . LYS G 43  ? 1.4707 1.9495 1.7096 -0.1998 -0.3277 0.1811  43  LYS H CG  
10135 C CD  . LYS G 43  ? 1.5424 2.0088 1.8279 -0.1880 -0.3392 0.2101  43  LYS H CD  
10136 C CE  . LYS G 43  ? 1.6531 2.1538 2.0434 -0.1968 -0.3854 0.2769  43  LYS H CE  
10137 N NZ  . LYS G 43  ? 1.7275 2.2247 2.2471 -0.1622 -0.3749 0.2765  43  LYS H NZ  
10138 N N   . GLY G 44  ? 1.3730 1.8313 1.3351 -0.2504 -0.2667 0.0609  44  GLY H N   
10139 C CA  . GLY G 44  ? 1.3768 1.8133 1.2736 -0.2539 -0.2359 0.0121  44  GLY H CA  
10140 C C   . GLY G 44  ? 1.4062 1.7963 1.2974 -0.2168 -0.1982 -0.0258 44  GLY H C   
10141 O O   . GLY G 44  ? 1.3861 1.7610 1.3213 -0.1889 -0.1928 -0.0185 44  GLY H O   
10142 N N   . LEU G 45  ? 1.3554 1.7236 1.1954 -0.2193 -0.1724 -0.0653 45  LEU H N   
10143 C CA  . LEU G 45  ? 1.3204 1.6488 1.1537 -0.1902 -0.1405 -0.0963 45  LEU H CA  
10144 C C   . LEU G 45  ? 1.3442 1.6626 1.2271 -0.1680 -0.1301 -0.1028 45  LEU H C   
10145 O O   . LEU G 45  ? 1.3482 1.6765 1.2388 -0.1779 -0.1329 -0.1073 45  LEU H O   
10146 C CB  . LEU G 45  ? 1.3342 1.6434 1.1083 -0.2017 -0.1189 -0.1313 45  LEU H CB  
10147 C CG  . LEU G 45  ? 1.4129 1.7283 1.1377 -0.2219 -0.1176 -0.1370 45  LEU H CG  
10148 C CD1 . LEU G 45  ? 1.4446 1.7512 1.1249 -0.2434 -0.0981 -0.1727 45  LEU H CD1 
10149 C CD2 . LEU G 45  ? 1.4170 1.7126 1.1429 -0.1977 -0.1051 -0.1389 45  LEU H CD2 
10150 N N   . GLU G 46  ? 1.2728 1.5741 1.1871 -0.1425 -0.1168 -0.1048 46  GLU H N   
10151 C CA  . GLU G 46  ? 1.2493 1.5437 1.2091 -0.1262 -0.1019 -0.1151 46  GLU H CA  
10152 C C   . GLU G 46  ? 1.2962 1.5605 1.2223 -0.1178 -0.0759 -0.1416 46  GLU H C   
10153 O O   . GLU G 46  ? 1.2873 1.5358 1.1889 -0.1108 -0.0679 -0.1445 46  GLU H O   
10154 C CB  . GLU G 46  ? 1.2537 1.5539 1.2794 -0.1100 -0.1034 -0.0997 46  GLU H CB  
10155 C CG  . GLU G 46  ? 1.4130 1.7442 1.4911 -0.1166 -0.1336 -0.0644 46  GLU H CG  
10156 C CD  . GLU G 46  ? 1.6310 1.9618 1.7698 -0.1022 -0.1387 -0.0442 46  GLU H CD  
10157 O OE1 . GLU G 46  ? 1.5803 1.9195 1.7078 -0.1114 -0.1617 -0.0165 46  GLU H OE1 
10158 O OE2 . GLU G 46  ? 1.4847 1.8077 1.6844 -0.0849 -0.1190 -0.0570 46  GLU H OE2 
10159 N N   . TRP G 47  ? 1.1410 1.7465 1.3612 -0.3005 -0.1757 -0.2635 47  TRP H N   
10160 C CA  . TRP G 47  ? 1.1162 1.7324 1.3231 -0.2944 -0.1336 -0.2750 47  TRP H CA  
10161 C C   . TRP G 47  ? 1.0843 1.7467 1.3632 -0.2881 -0.1031 -0.2768 47  TRP H C   
10162 O O   . TRP G 47  ? 1.0610 1.7474 1.4201 -0.2932 -0.1100 -0.2732 47  TRP H O   
10163 C CB  . TRP G 47  ? 1.1269 1.7314 1.3340 -0.3048 -0.1390 -0.2823 47  TRP H CB  
10164 C CG  . TRP G 47  ? 1.1185 1.7374 1.3198 -0.3013 -0.0984 -0.2908 47  TRP H CG  
10165 C CD1 . TRP G 47  ? 1.1703 1.7654 1.3039 -0.2995 -0.0785 -0.2945 47  TRP H CD1 
10166 C CD2 . TRP G 47  ? 1.0768 1.7335 1.3448 -0.3010 -0.0729 -0.2940 47  TRP H CD2 
10167 N NE1 . TRP G 47  ? 1.1305 1.7514 1.2887 -0.2996 -0.0463 -0.2983 47  TRP H NE1 
10168 C CE2 . TRP G 47  ? 1.1168 1.7741 1.3507 -0.3000 -0.0424 -0.2990 47  TRP H CE2 
10169 C CE3 . TRP G 47  ? 1.0722 1.7588 1.4267 -0.3014 -0.0696 -0.2912 47  TRP H CE3 
10170 C CZ2 . TRP G 47  ? 1.0755 1.7628 1.3506 -0.2997 -0.0128 -0.3016 47  TRP H CZ2 
10171 C CZ3 . TRP G 47  ? 1.0623 1.7735 1.4535 -0.2989 -0.0346 -0.2952 47  TRP H CZ3 
10172 C CH2 . TRP G 47  ? 1.0616 1.7734 1.4091 -0.2982 -0.0085 -0.3006 47  TRP H CH2 
10173 N N   . MET G 48  ? 0.9986 1.6676 1.2489 -0.2779 -0.0697 -0.2810 48  MET H N   
10174 C CA  . MET G 48  ? 0.9484 1.6498 1.2457 -0.2724 -0.0416 -0.2853 48  MET H CA  
10175 C C   . MET G 48  ? 0.9889 1.7010 1.2941 -0.2758 -0.0123 -0.2940 48  MET H C   
10176 O O   . MET G 48  ? 0.9801 1.7133 1.3418 -0.2772 0.0030  -0.2979 48  MET H O   
10177 C CB  . MET G 48  ? 0.9629 1.6633 1.2321 -0.2595 -0.0301 -0.2820 48  MET H CB  
10178 C CG  . MET G 48  ? 1.0159 1.7173 1.2976 -0.2535 -0.0532 -0.2718 48  MET H CG  
10179 S SD  . MET G 48  ? 1.0536 1.7578 1.3205 -0.2346 -0.0378 -0.2657 48  MET H SD  
10180 C CE  . MET G 48  ? 1.0529 1.7093 1.2305 -0.2286 -0.0378 -0.2566 48  MET H CE  
10181 N N   . GLY G 49  ? 0.9361 1.6323 1.1873 -0.2769 -0.0010 -0.2953 49  GLY H N   
10182 C CA  . GLY G 49  ? 0.9078 1.6150 1.1623 -0.2812 0.0256  -0.3003 49  GLY H CA  
10183 C C   . GLY G 49  ? 0.9254 1.6151 1.1260 -0.2841 0.0360  -0.2968 49  GLY H C   
10184 O O   . GLY G 49  ? 0.9400 1.6028 1.0972 -0.2817 0.0257  -0.2912 49  GLY H O   
10185 N N   . ILE G 50  ? 0.8347 1.5372 1.0393 -0.2894 0.0595  -0.2980 50  ILE H N   
10186 C CA  . ILE G 50  ? 0.8187 1.5106 0.9888 -0.2955 0.0732  -0.2910 50  ILE H CA  
10187 C C   . ILE G 50  ? 0.8693 1.5744 1.0379 -0.2999 0.0965  -0.2876 50  ILE H C   
10188 O O   . ILE G 50  ? 0.8755 1.5993 1.0697 -0.3002 0.1074  -0.2944 50  ILE H O   
10189 C CB  . ILE G 50  ? 0.8517 1.5414 1.0279 -0.3033 0.0696  -0.2923 50  ILE H CB  
10190 C CG1 . ILE G 50  ? 0.8384 1.5549 1.0721 -0.3050 0.0694  -0.2987 50  ILE H CG1 
10191 C CG2 . ILE G 50  ? 0.8885 1.5444 1.0303 -0.3024 0.0479  -0.2926 50  ILE H CG2 
10192 C CD1 . ILE G 50  ? 0.8631 1.5876 1.1164 -0.3122 0.0732  -0.2983 50  ILE H CD1 
10193 N N   . ILE G 51  ? 0.8274 1.5179 0.9665 -0.3043 0.1047  -0.2749 51  ILE H N   
10194 C CA  . ILE G 51  ? 0.8326 1.5293 0.9649 -0.3127 0.1198  -0.2670 51  ILE H CA  
10195 C C   . ILE G 51  ? 0.9101 1.6037 1.0396 -0.3247 0.1305  -0.2517 51  ILE H C   
10196 O O   . ILE G 51  ? 0.9147 1.5852 1.0319 -0.3239 0.1292  -0.2421 51  ILE H O   
10197 C CB  . ILE G 51  ? 0.8800 1.5603 0.9919 -0.3088 0.1151  -0.2604 51  ILE H CB  
10198 C CG1 . ILE G 51  ? 0.8909 1.5757 1.0120 -0.2974 0.1074  -0.2752 51  ILE H CG1 
10199 C CG2 . ILE G 51  ? 0.8944 1.5746 0.9930 -0.3220 0.1241  -0.2506 51  ILE H CG2 
10200 C CD1 . ILE G 51  ? 0.8965 1.5677 1.0023 -0.2947 0.1031  -0.2720 51  ILE H CD1 
10201 N N   . ASN G 52  ? 0.8807 1.5949 1.0224 -0.3359 0.1442  -0.2476 52  ASN H N   
10202 C CA  . ASN G 52  ? 0.8787 1.5951 1.0284 -0.3501 0.1557  -0.2290 52  ASN H CA  
10203 C C   . ASN G 52  ? 0.9511 1.6513 1.0811 -0.3577 0.1531  -0.2114 52  ASN H C   
10204 O O   . ASN G 52  ? 0.9721 1.6802 1.0900 -0.3618 0.1535  -0.2146 52  ASN H O   
10205 C CB  . ASN G 52  ? 0.8930 1.6436 1.0727 -0.3582 0.1698  -0.2302 52  ASN H CB  
10206 C CG  . ASN G 52  ? 1.1822 1.9426 1.3835 -0.3743 0.1828  -0.2097 52  ASN H CG  
10207 O OD1 . ASN G 52  ? 1.1406 1.9228 1.3546 -0.3856 0.1931  -0.1988 52  ASN H OD1 
10208 N ND2 . ASN G 52  ? 1.0193 1.7624 1.2264 -0.3766 0.1851  -0.2032 52  ASN H ND2 
10209 N N   . PRO G 53  ? 0.9080 1.5793 1.0333 -0.3586 0.1495  -0.1926 53  PRO H N   
10210 C CA  . PRO G 53  ? 0.9217 1.5731 1.0376 -0.3654 0.1402  -0.1728 53  PRO H CA  
10211 C C   . PRO G 53  ? 0.9927 1.6552 1.1120 -0.3867 0.1419  -0.1561 53  PRO H C   
10212 O O   . PRO G 53  ? 1.0144 1.6610 1.1123 -0.3921 0.1269  -0.1495 53  PRO H O   
10213 C CB  . PRO G 53  ? 0.9406 1.5594 1.0687 -0.3622 0.1430  -0.1500 53  PRO H CB  
10214 C CG  . PRO G 53  ? 0.9986 1.6127 1.1185 -0.3472 0.1485  -0.1676 53  PRO H CG  
10215 C CD  . PRO G 53  ? 0.9306 1.5786 1.0578 -0.3524 0.1543  -0.1871 53  PRO H CD  
10216 N N   . ARG G 54  ? 0.9356 1.6233 1.0806 -0.3996 0.1577  -0.1486 54  ARG H N   
10217 C CA  . ARG G 54  ? 0.9380 1.6396 1.0872 -0.4209 0.1589  -0.1303 54  ARG H CA  
10218 C C   . ARG G 54  ? 0.9898 1.7073 1.1062 -0.4182 0.1603  -0.1514 54  ARG H C   
10219 O O   . ARG G 54  ? 1.0138 1.7195 1.0993 -0.4312 0.1509  -0.1417 54  ARG H O   
10220 C CB  . ARG G 54  ? 0.9429 1.6689 1.1415 -0.4364 0.1772  -0.1105 54  ARG H CB  
10221 C CG  . ARG G 54  ? 1.1590 1.9125 1.3819 -0.4258 0.1942  -0.1315 54  ARG H CG  
10222 C CD  . ARG G 54  ? 1.4089 2.1997 1.6803 -0.4415 0.2119  -0.1173 54  ARG H CD  
10223 N NE  . ARG G 54  ? 1.6730 2.4965 1.9622 -0.4294 0.2214  -0.1416 54  ARG H NE  
10224 C CZ  . ARG G 54  ? 1.8992 2.7641 2.2322 -0.4368 0.2362  -0.1355 54  ARG H CZ  
10225 N NH1 . ARG G 54  ? 1.7678 2.6497 2.1288 -0.4584 0.2436  -0.1058 54  ARG H NH1 
10226 N NH2 . ARG G 54  ? 1.7121 2.6025 2.0690 -0.4229 0.2423  -0.1560 54  ARG H NH2 
10227 N N   . ASP G 55  ? 0.9264 1.6638 1.0487 -0.4017 0.1718  -0.1786 55  ASP H N   
10228 C CA  . ASP G 55  ? 0.9367 1.6856 1.0398 -0.3947 0.1822  -0.1986 55  ASP H CA  
10229 C C   . ASP G 55  ? 1.0016 1.7234 1.0654 -0.3826 0.1727  -0.2180 55  ASP H C   
10230 O O   . ASP G 55  ? 1.0201 1.7379 1.0574 -0.3795 0.1839  -0.2318 55  ASP H O   
10231 C CB  . ASP G 55  ? 0.9303 1.7111 1.0772 -0.3828 0.1983  -0.2132 55  ASP H CB  
10232 C CG  . ASP G 55  ? 1.0061 1.8218 1.1931 -0.3926 0.2149  -0.1994 55  ASP H CG  
10233 O OD1 . ASP G 55  ? 1.0372 1.8591 1.2080 -0.4043 0.2235  -0.1869 55  ASP H OD1 
10234 O OD2 . ASP G 55  ? 1.0056 1.8416 1.2391 -0.3880 0.2190  -0.2024 55  ASP H OD2 
10235 N N   . SER G 56  ? 0.9569 1.6588 1.0197 -0.3751 0.1556  -0.2182 56  SER H N   
10236 C CA  . SER G 56  ? 0.9813 1.6619 1.0218 -0.3625 0.1444  -0.2341 56  SER H CA  
10237 C C   . SER G 56  ? 1.0528 1.7456 1.1012 -0.3484 0.1581  -0.2605 56  SER H C   
10238 O O   . SER G 56  ? 1.0662 1.7431 1.0944 -0.3418 0.1569  -0.2749 56  SER H O   
10239 C CB  . SER G 56  ? 1.0800 1.7303 1.0768 -0.3731 0.1303  -0.2265 56  SER H CB  
10240 O OG  . SER G 56  ? 1.2918 1.9413 1.2547 -0.3849 0.1425  -0.2291 56  SER H OG  
10241 N N   . ASP G 57  ? 1.0200 1.7392 1.1058 -0.3440 0.1710  -0.2650 57  ASP H N   
10242 C CA  . ASP G 57  ? 1.0407 1.7715 1.1535 -0.3315 0.1839  -0.2833 57  ASP H CA  
10243 C C   . ASP G 57  ? 1.0799 1.8127 1.2230 -0.3196 0.1679  -0.2908 57  ASP H C   
10244 O O   . ASP G 57  ? 1.0551 1.7879 1.2049 -0.3204 0.1537  -0.2827 57  ASP H O   
10245 C CB  . ASP G 57  ? 1.0666 1.8225 1.2121 -0.3329 0.2045  -0.2807 57  ASP H CB  
10246 C CG  . ASP G 57  ? 1.2076 1.9850 1.3956 -0.3340 0.1969  -0.2730 57  ASP H CG  
10247 O OD1 . ASP G 57  ? 1.2252 1.9975 1.4012 -0.3426 0.1852  -0.2608 57  ASP H OD1 
10248 O OD2 . ASP G 57  ? 1.2140 2.0098 1.4500 -0.3266 0.2041  -0.2779 57  ASP H OD2 
10249 N N   . THR G 58  ? 1.0455 1.7767 1.2065 -0.3096 0.1720  -0.3050 58  THR H N   
10250 C CA  . THR G 58  ? 1.0249 1.7586 1.2175 -0.3001 0.1543  -0.3100 58  THR H CA  
10251 C C   . THR G 58  ? 1.0595 1.8079 1.3099 -0.2949 0.1608  -0.3154 58  THR H C   
10252 O O   . THR G 58  ? 1.0683 1.8187 1.3369 -0.2929 0.1862  -0.3204 58  THR H O   
10253 C CB  . THR G 58  ? 1.1549 1.8751 1.3344 -0.2941 0.1481  -0.3168 58  THR H CB  
10254 O OG1 . THR G 58  ? 1.2166 1.9190 1.3478 -0.2998 0.1456  -0.3113 58  THR H OG1 
10255 C CG2 . THR G 58  ? 1.1008 1.8222 1.3004 -0.2860 0.1241  -0.3147 58  THR H CG2 
10256 N N   . ARG G 59  ? 0.9970 1.7498 1.2756 -0.2928 0.1375  -0.3125 59  ARG H N   
10257 C CA  . ARG G 59  ? 0.9912 1.7539 1.3339 -0.2895 0.1316  -0.3129 59  ARG H CA  
10258 C C   . ARG G 59  ? 1.0667 1.8232 1.4246 -0.2861 0.1041  -0.3131 59  ARG H C   
10259 O O   . ARG G 59  ? 1.0673 1.8143 1.4033 -0.2879 0.0774  -0.3093 59  ARG H O   
10260 C CB  . ARG G 59  ? 0.9598 1.7301 1.3202 -0.2938 0.1224  -0.3072 59  ARG H CB  
10261 C CG  . ARG G 59  ? 1.0317 1.8127 1.3745 -0.2984 0.1468  -0.3034 59  ARG H CG  
10262 C CD  . ARG G 59  ? 1.1547 1.9518 1.5448 -0.2994 0.1467  -0.2985 59  ARG H CD  
10263 N NE  . ARG G 59  ? 1.3368 2.1499 1.7214 -0.3027 0.1753  -0.2927 59  ARG H NE  
10264 C CZ  . ARG G 59  ? 1.5892 2.4134 2.0065 -0.2968 0.2043  -0.2904 59  ARG H CZ  
10265 N NH1 . ARG G 59  ? 1.4518 2.2715 1.9184 -0.2869 0.2116  -0.2927 59  ARG H NH1 
10266 N NH2 . ARG G 59  ? 1.4608 2.2985 1.8651 -0.3008 0.2281  -0.2830 59  ARG H NH2 
10267 N N   . TYR G 60  ? 1.0434 1.8024 1.4345 -0.2817 0.1134  -0.3169 60  TYR H N   
10268 C CA  . TYR G 60  ? 1.0496 1.8087 1.4666 -0.2791 0.0898  -0.3146 60  TYR H CA  
10269 C C   . TYR G 60  ? 1.1083 1.8719 1.5951 -0.2823 0.0674  -0.3059 60  TYR H C   
10270 O O   . TYR G 60  ? 1.1167 1.8851 1.6542 -0.2833 0.0799  -0.3027 60  TYR H O   
10271 C CB  . TYR G 60  ? 1.0750 1.8370 1.5114 -0.2746 0.1110  -0.3215 60  TYR H CB  
10272 C CG  . TYR G 60  ? 1.1256 1.8779 1.4990 -0.2725 0.1265  -0.3297 60  TYR H CG  
10273 C CD1 . TYR G 60  ? 1.1816 1.9250 1.5263 -0.2749 0.1576  -0.3369 60  TYR H CD1 
10274 C CD2 . TYR G 60  ? 1.1290 1.8783 1.4772 -0.2677 0.1094  -0.3286 60  TYR H CD2 
10275 C CE1 . TYR G 60  ? 1.2221 1.9503 1.5080 -0.2758 0.1651  -0.3431 60  TYR H CE1 
10276 C CE2 . TYR G 60  ? 1.1518 1.8889 1.4526 -0.2661 0.1185  -0.3337 60  TYR H CE2 
10277 C CZ  . TYR G 60  ? 1.3050 2.0301 1.5728 -0.2717 0.1436  -0.3412 60  TYR H CZ  
10278 O OH  . TYR G 60  ? 1.3680 2.0749 1.5856 -0.2731 0.1457  -0.3446 60  TYR H OH  
10279 N N   . SER G 61  ? 1.0559 1.8159 1.5496 -0.2836 0.0334  -0.2996 61  SER H N   
10280 C CA  . SER G 61  ? 1.0535 1.8132 1.6125 -0.2898 0.0019  -0.2878 61  SER H CA  
10281 C C   . SER G 61  ? 1.0680 1.8424 1.7142 -0.2889 0.0197  -0.2829 61  SER H C   
10282 O O   . SER G 61  ? 1.0476 1.8292 1.6830 -0.2835 0.0413  -0.2901 61  SER H O   
10283 C CB  . SER G 61  ? 1.1123 1.8579 1.6315 -0.2925 -0.0400 -0.2818 61  SER H CB  
10284 O OG  . SER G 61  ? 1.2362 1.9785 1.8149 -0.3012 -0.0775 -0.2677 61  SER H OG  
10285 N N   . PRO G 62  ? 1.0148 1.7912 1.7539 -0.2944 0.0118  -0.2692 62  PRO H N   
10286 C CA  . PRO G 62  ? 1.0023 1.7893 1.8353 -0.2945 0.0343  -0.2613 62  PRO H CA  
10287 C C   . PRO G 62  ? 1.0516 1.8500 1.8953 -0.2959 0.0204  -0.2584 62  PRO H C   
10288 O O   . PRO G 62  ? 1.0367 1.8446 1.9179 -0.2923 0.0549  -0.2629 62  PRO H O   
10289 C CB  . PRO G 62  ? 1.0303 1.8127 1.9634 -0.3025 0.0111  -0.2397 62  PRO H CB  
10290 C CG  . PRO G 62  ? 1.0993 1.8712 1.9915 -0.3018 -0.0009 -0.2432 62  PRO H CG  
10291 C CD  . PRO G 62  ? 1.0467 1.8132 1.8185 -0.3009 -0.0177 -0.2584 62  PRO H CD  
10292 N N   . SER G 63  ? 1.0255 1.8206 1.8337 -0.3006 -0.0280 -0.2512 63  SER H N   
10293 C CA  . SER G 63  ? 1.0165 1.8243 1.8318 -0.3007 -0.0467 -0.2449 63  SER H CA  
10294 C C   . SER G 63  ? 1.0718 1.8866 1.8202 -0.2877 -0.0203 -0.2618 63  SER H C   
10295 O O   . SER G 63  ? 1.0655 1.8975 1.8415 -0.2847 -0.0234 -0.2576 63  SER H O   
10296 C CB  . SER G 63  ? 1.0765 1.8693 1.8538 -0.3081 -0.1036 -0.2323 63  SER H CB  
10297 O OG  . SER G 63  ? 1.1994 1.9821 2.0434 -0.3225 -0.1379 -0.2141 63  SER H OG  
10298 N N   . PHE G 64  ? 1.0252 1.8275 1.6937 -0.2808 0.0027  -0.2781 64  PHE H N   
10299 C CA  . PHE G 64  ? 1.0046 1.8067 1.6091 -0.2701 0.0215  -0.2908 64  PHE H CA  
10300 C C   . PHE G 64  ? 1.0316 1.8295 1.6205 -0.2671 0.0660  -0.3070 64  PHE H C   
10301 O O   . PHE G 64  ? 1.0148 1.8096 1.5597 -0.2603 0.0785  -0.3166 64  PHE H O   
10302 C CB  . PHE G 64  ? 1.0398 1.8230 1.5528 -0.2663 0.0009  -0.2900 64  PHE H CB  
10303 C CG  . PHE G 64  ? 1.0698 1.8466 1.5721 -0.2668 -0.0389 -0.2759 64  PHE H CG  
10304 C CD1 . PHE G 64  ? 1.1376 1.8973 1.6330 -0.2769 -0.0699 -0.2680 64  PHE H CD1 
10305 C CD2 . PHE G 64  ? 1.0835 1.8677 1.5796 -0.2568 -0.0463 -0.2700 64  PHE H CD2 
10306 C CE1 . PHE G 64  ? 1.1760 1.9206 1.6466 -0.2790 -0.1082 -0.2554 64  PHE H CE1 
10307 C CE2 . PHE G 64  ? 1.1415 1.9156 1.6196 -0.2565 -0.0809 -0.2554 64  PHE H CE2 
10308 C CZ  . PHE G 64  ? 1.1557 1.9072 1.6146 -0.2685 -0.1119 -0.2487 64  PHE H CZ  
10309 N N   . GLN G 65  ? 0.9959 1.7898 1.6199 -0.2719 0.0886  -0.3084 65  GLN H N   
10310 C CA  . GLN G 65  ? 1.0112 1.7941 1.6149 -0.2698 0.1334  -0.3222 65  GLN H CA  
10311 C C   . GLN G 65  ? 1.0959 1.8803 1.7315 -0.2668 0.1617  -0.3315 65  GLN H C   
10312 O O   . GLN G 65  ? 1.0831 1.8799 1.8054 -0.2691 0.1636  -0.3233 65  GLN H O   
10313 C CB  . GLN G 65  ? 1.0318 1.8095 1.6793 -0.2729 0.1522  -0.3167 65  GLN H CB  
10314 C CG  . GLN G 65  ? 1.0451 1.8066 1.6788 -0.2698 0.2048  -0.3282 65  GLN H CG  
10315 C CD  . GLN G 65  ? 1.1479 1.8981 1.6860 -0.2695 0.2127  -0.3375 65  GLN H CD  
10316 O OE1 . GLN G 65  ? 1.0172 1.7706 1.5416 -0.2712 0.2040  -0.3312 65  GLN H OE1 
10317 N NE2 . GLN G 65  ? 1.0951 1.8306 1.5707 -0.2687 0.2293  -0.3515 65  GLN H NE2 
10318 N N   . GLY G 66  ? 1.0889 1.8586 1.6564 -0.2633 0.1809  -0.3474 66  GLY H N   
10319 C CA  . GLY G 66  ? 1.1051 1.8682 1.6849 -0.2607 0.2078  -0.3610 66  GLY H CA  
10320 C C   . GLY G 66  ? 1.1391 1.9186 1.7237 -0.2552 0.1818  -0.3603 66  GLY H C   
10321 O O   . GLY G 66  ? 1.1601 1.9268 1.7019 -0.2514 0.1894  -0.3737 66  GLY H O   
10322 N N   . GLN G 67  ? 1.0507 1.8559 1.6874 -0.2545 0.1489  -0.3432 67  GLN H N   
10323 C CA  . GLN G 67  ? 1.0135 1.8389 1.6673 -0.2471 0.1226  -0.3366 67  GLN H CA  
10324 C C   . GLN G 67  ? 1.0711 1.8833 1.6395 -0.2386 0.1060  -0.3388 67  GLN H C   
10325 O O   . GLN G 67  ? 1.0650 1.8740 1.6215 -0.2317 0.1117  -0.3477 67  GLN H O   
10326 C CB  . GLN G 67  ? 0.9991 1.8463 1.7085 -0.2504 0.0881  -0.3147 67  GLN H CB  
10327 C CG  . GLN G 67  ? 0.9091 1.7657 1.7129 -0.2614 0.0968  -0.3049 67  GLN H CG  
10328 C CD  . GLN G 67  ? 1.0241 1.8958 1.9127 -0.2622 0.1263  -0.3087 67  GLN H CD  
10329 O OE1 . GLN G 67  ? 0.9497 1.8485 1.8949 -0.2605 0.1109  -0.2990 67  GLN H OE1 
10330 N NE2 . GLN G 67  ? 0.8986 1.7510 1.7963 -0.2643 0.1725  -0.3229 67  GLN H NE2 
10331 N N   . VAL G 68  ? 1.0316 1.8330 1.5467 -0.2398 0.0865  -0.3297 68  VAL H N   
10332 C CA  . VAL G 68  ? 1.0272 1.8115 1.4701 -0.2334 0.0737  -0.3259 68  VAL H CA  
10333 C C   . VAL G 68  ? 1.1042 1.8650 1.4861 -0.2412 0.0909  -0.3343 68  VAL H C   
10334 O O   . VAL G 68  ? 1.1100 1.8696 1.4994 -0.2497 0.1062  -0.3388 68  VAL H O   
10335 C CB  . VAL G 68  ? 1.0635 1.8472 1.4907 -0.2290 0.0441  -0.3080 68  VAL H CB  
10336 C CG1 . VAL G 68  ? 1.0762 1.8501 1.4833 -0.2396 0.0383  -0.3052 68  VAL H CG1 
10337 C CG2 . VAL G 68  ? 1.0603 1.8264 1.4366 -0.2181 0.0360  -0.2993 68  VAL H CG2 
10338 N N   . THR G 69  ? 1.0644 1.8066 1.3937 -0.2382 0.0877  -0.3333 69  THR H N   
10339 C CA  . THR G 69  ? 1.0815 1.8015 1.3526 -0.2474 0.0993  -0.3368 69  THR H CA  
10340 C C   . THR G 69  ? 1.1056 1.8133 1.3375 -0.2470 0.0828  -0.3194 69  THR H C   
10341 O O   . THR G 69  ? 1.0804 1.7815 1.3107 -0.2371 0.0678  -0.3077 69  THR H O   
10342 C CB  . THR G 69  ? 1.1826 1.8838 1.4296 -0.2495 0.1117  -0.3505 69  THR H CB  
10343 O OG1 . THR G 69  ? 1.1542 1.8648 1.4468 -0.2477 0.1303  -0.3658 69  THR H OG1 
10344 C CG2 . THR G 69  ? 1.1815 1.8584 1.3680 -0.2624 0.1263  -0.3551 69  THR H CG2 
10345 N N   . ILE G 70  ? 1.0635 1.7678 1.2724 -0.2565 0.0886  -0.3160 70  ILE H N   
10346 C CA  . ILE G 70  ? 1.0546 1.7451 1.2313 -0.2586 0.0799  -0.2997 70  ILE H CA  
10347 C C   . ILE G 70  ? 1.1358 1.8091 1.2752 -0.2686 0.0869  -0.2953 70  ILE H C   
10348 O O   . ILE G 70  ? 1.1499 1.8253 1.2756 -0.2793 0.1019  -0.3030 70  ILE H O   
10349 C CB  . ILE G 70  ? 1.0874 1.7837 1.2664 -0.2637 0.0789  -0.2972 70  ILE H CB  
10350 C CG1 . ILE G 70  ? 1.0895 1.8001 1.3077 -0.2585 0.0669  -0.3015 70  ILE H CG1 
10351 C CG2 . ILE G 70  ? 1.0905 1.7667 1.2388 -0.2638 0.0733  -0.2807 70  ILE H CG2 
10352 C CD1 . ILE G 70  ? 1.1564 1.8729 1.3886 -0.2663 0.0642  -0.3036 70  ILE H CD1 
10353 N N   . SER G 71  ? 1.1060 1.7601 1.2329 -0.2649 0.0752  -0.2798 71  SER H N   
10354 C CA  . SER G 71  ? 1.1270 1.7597 1.2245 -0.2764 0.0732  -0.2689 71  SER H CA  
10355 C C   . SER G 71  ? 1.1813 1.8020 1.2730 -0.2819 0.0729  -0.2447 71  SER H C   
10356 O O   . SER G 71  ? 1.1642 1.7838 1.2679 -0.2724 0.0729  -0.2367 71  SER H O   
10357 C CB  . SER G 71  ? 1.1796 1.7945 1.2814 -0.2691 0.0572  -0.2645 71  SER H CB  
10358 O OG  . SER G 71  ? 1.2754 1.9030 1.3973 -0.2594 0.0583  -0.2850 71  SER H OG  
10359 N N   . ALA G 72  ? 1.1603 1.7690 1.2328 -0.2986 0.0742  -0.2322 72  ALA H N   
10360 C CA  . ALA G 72  ? 1.1552 1.7520 1.2330 -0.3068 0.0777  -0.2062 72  ALA H CA  
10361 C C   . ALA G 72  ? 1.2438 1.8177 1.3150 -0.3225 0.0666  -0.1830 72  ALA H C   
10362 O O   . ALA G 72  ? 1.2755 1.8493 1.3199 -0.3363 0.0627  -0.1907 72  ALA H O   
10363 C CB  . ALA G 72  ? 1.1567 1.7742 1.2336 -0.3160 0.0948  -0.2124 72  ALA H CB  
10364 N N   . ASP G 73  ? 1.1887 1.7381 1.2846 -0.3208 0.0617  -0.1523 73  ASP H N   
10365 C CA  . ASP G 73  ? 1.1943 1.7178 1.2996 -0.3374 0.0470  -0.1216 73  ASP H CA  
10366 C C   . ASP G 73  ? 1.2051 1.7203 1.3402 -0.3478 0.0631  -0.0909 73  ASP H C   
10367 O O   . ASP G 73  ? 1.1902 1.6815 1.3574 -0.3363 0.0698  -0.0678 73  ASP H O   
10368 C CB  . ASP G 73  ? 1.2284 1.7229 1.3534 -0.3255 0.0229  -0.1073 73  ASP H CB  
10369 C CG  . ASP G 73  ? 1.4515 1.9183 1.5735 -0.3462 -0.0046 -0.0851 73  ASP H CG  
10370 O OD1 . ASP G 73  ? 1.4553 1.9116 1.5951 -0.3660 -0.0039 -0.0546 73  ASP H OD1 
10371 O OD2 . ASP G 73  ? 1.6109 2.0636 1.7161 -0.3436 -0.0288 -0.0962 73  ASP H OD2 
10372 N N   . LYS G 74  ? 1.1379 1.6722 1.2652 -0.3689 0.0733  -0.0902 74  LYS H N   
10373 C CA  . LYS G 74  ? 1.1042 1.6380 1.2647 -0.3836 0.0919  -0.0634 74  LYS H CA  
10374 C C   . LYS G 74  ? 1.1280 1.6260 1.3321 -0.3951 0.0817  -0.0171 74  LYS H C   
10375 O O   . LYS G 74  ? 1.1057 1.5902 1.3504 -0.3981 0.1034  0.0086  74  LYS H O   
10376 C CB  . LYS G 74  ? 1.1351 1.7029 1.2848 -0.4037 0.1014  -0.0719 74  LYS H CB  
10377 C CG  . LYS G 74  ? 1.3544 1.9255 1.4676 -0.4181 0.0809  -0.0779 74  LYS H CG  
10378 C CD  . LYS G 74  ? 1.4386 2.0394 1.5502 -0.4388 0.0931  -0.0749 74  LYS H CD  
10379 C CE  . LYS G 74  ? 1.5468 2.1517 1.6029 -0.4445 0.0845  -0.0951 74  LYS H CE  
10380 N NZ  . LYS G 74  ? 1.6364 2.2708 1.6943 -0.4623 0.0990  -0.0885 74  LYS H NZ  
10381 N N   . SER G 75  ? 1.0949 1.5728 1.2931 -0.4021 0.0487  -0.0057 75  SER H N   
10382 C CA  . SER G 75  ? 1.0904 1.5298 1.3371 -0.4148 0.0284  0.0419  75  SER H CA  
10383 C C   . SER G 75  ? 1.0857 1.4929 1.3806 -0.3910 0.0381  0.0640  75  SER H C   
10384 O O   . SER G 75  ? 1.0692 1.4496 1.4243 -0.3985 0.0494  0.1072  75  SER H O   
10385 C CB  . SER G 75  ? 1.1879 1.6094 1.4049 -0.4267 -0.0148 0.0420  75  SER H CB  
10386 O OG  . SER G 75  ? 1.3655 1.8095 1.5271 -0.4468 -0.0193 0.0214  75  SER H OG  
10387 N N   . ILE G 76  ? 1.0148 1.4237 1.2878 -0.3620 0.0370  0.0366  76  ILE H N   
10388 C CA  . ILE G 76  ? 0.9872 1.3680 1.2974 -0.3339 0.0488  0.0534  76  ILE H CA  
10389 C C   . ILE G 76  ? 1.0209 1.4088 1.3170 -0.3207 0.0905  0.0400  76  ILE H C   
10390 O O   . ILE G 76  ? 1.0265 1.3848 1.3450 -0.2988 0.1101  0.0564  76  ILE H O   
10391 C CB  . ILE G 76  ? 1.0214 1.4028 1.3203 -0.3096 0.0249  0.0330  76  ILE H CB  
10392 C CG1 . ILE G 76  ? 1.0478 1.4328 1.3210 -0.3253 -0.0152 0.0202  76  ILE H CG1 
10393 C CG2 . ILE G 76  ? 1.0158 1.3594 1.3748 -0.2847 0.0273  0.0679  76  ILE H CG2 
10394 C CD1 . ILE G 76  ? 1.1501 1.5479 1.4005 -0.3043 -0.0312 -0.0144 76  ILE H CD1 
10395 N N   . SER G 77  ? 0.9543 1.3768 1.2122 -0.3339 0.1034  0.0116  77  SER H N   
10396 C CA  . SER G 77  ? 0.9390 1.3697 1.1729 -0.3259 0.1347  -0.0080 77  SER H CA  
10397 C C   . SER G 77  ? 0.9838 1.4135 1.1881 -0.2968 0.1333  -0.0330 77  SER H C   
10398 O O   . SER G 77  ? 1.0018 1.4044 1.2003 -0.2808 0.1560  -0.0274 77  SER H O   
10399 C CB  . SER G 77  ? 0.9654 1.3633 1.2347 -0.3323 0.1686  0.0251  77  SER H CB  
10400 O OG  . SER G 77  ? 1.0533 1.4032 1.3517 -0.3119 0.1813  0.0543  77  SER H OG  
10401 N N   . THR G 78  ? 0.9083 1.3644 1.0939 -0.2910 0.1074  -0.0590 78  THR H N   
10402 C CA  . THR G 78  ? 0.8946 1.3579 1.0642 -0.2664 0.1009  -0.0807 78  THR H CA  
10403 C C   . THR G 78  ? 0.9389 1.4437 1.0787 -0.2698 0.0899  -0.1206 78  THR H C   
10404 O O   . THR G 78  ? 0.9456 1.4677 1.0793 -0.2841 0.0774  -0.1307 78  THR H O   
10405 C CB  . THR G 78  ? 0.9276 1.3747 1.1295 -0.2505 0.0814  -0.0642 78  THR H CB  
10406 O OG1 . THR G 78  ? 0.9172 1.3309 1.1606 -0.2587 0.0797  -0.0235 78  THR H OG1 
10407 C CG2 . THR G 78  ? 0.8875 1.3247 1.0940 -0.2208 0.0876  -0.0644 78  THR H CG2 
10408 N N   . ALA G 79  ? 0.8843 1.3995 1.0062 -0.2564 0.0944  -0.1409 79  ALA H N   
10409 C CA  . ALA G 79  ? 0.8760 1.4270 0.9844 -0.2571 0.0854  -0.1743 79  ALA H CA  
10410 C C   . ALA G 79  ? 0.9110 1.4686 1.0346 -0.2377 0.0713  -0.1810 79  ALA H C   
10411 O O   . ALA G 79  ? 0.9202 1.4556 1.0564 -0.2204 0.0718  -0.1624 79  ALA H O   
10412 C CB  . ALA G 79  ? 0.8952 1.4508 0.9828 -0.2583 0.0945  -0.1877 79  ALA H CB  
10413 N N   . TYR G 80  ? 0.8337 1.4205 0.9618 -0.2396 0.0623  -0.2056 80  TYR H N   
10414 C CA  . TYR G 80  ? 0.8138 1.4131 0.9665 -0.2233 0.0507  -0.2135 80  TYR H CA  
10415 C C   . TYR G 80  ? 0.8632 1.4930 1.0238 -0.2232 0.0497  -0.2379 80  TYR H C   
10416 O O   . TYR G 80  ? 0.8655 1.5074 1.0146 -0.2368 0.0567  -0.2515 80  TYR H O   
10417 C CB  . TYR G 80  ? 0.8244 1.4207 0.9895 -0.2253 0.0399  -0.2145 80  TYR H CB  
10418 C CG  . TYR G 80  ? 0.8440 1.4080 1.0110 -0.2292 0.0342  -0.1864 80  TYR H CG  
10419 C CD1 . TYR G 80  ? 0.8632 1.4040 1.0577 -0.2118 0.0324  -0.1583 80  TYR H CD1 
10420 C CD2 . TYR G 80  ? 0.8687 1.4225 1.0141 -0.2507 0.0310  -0.1842 80  TYR H CD2 
10421 C CE1 . TYR G 80  ? 0.8894 1.3970 1.1000 -0.2161 0.0278  -0.1268 80  TYR H CE1 
10422 C CE2 . TYR G 80  ? 0.8848 1.4075 1.0412 -0.2578 0.0217  -0.1532 80  TYR H CE2 
10423 C CZ  . TYR G 80  ? 0.9749 1.4742 1.1692 -0.2406 0.0200  -0.1236 80  TYR H CZ  
10424 O OH  . TYR G 80  ? 1.0076 1.4729 1.2279 -0.2472 0.0112  -0.0875 80  TYR H OH  
10425 N N   . LEU G 81  ? 0.8183 1.4612 1.0082 -0.2078 0.0408  -0.2403 81  LEU H N   
10426 C CA  . LEU G 81  ? 0.8188 1.4911 1.0336 -0.2083 0.0374  -0.2580 81  LEU H CA  
10427 C C   . LEU G 81  ? 0.8818 1.5720 1.1395 -0.1988 0.0328  -0.2648 81  LEU H C   
10428 O O   . LEU G 81  ? 0.8605 1.5620 1.1511 -0.1836 0.0239  -0.2573 81  LEU H O   
10429 C CB  . LEU G 81  ? 0.8235 1.4929 1.0332 -0.2015 0.0289  -0.2502 81  LEU H CB  
10430 C CG  . LEU G 81  ? 0.8738 1.5682 1.1100 -0.2084 0.0203  -0.2632 81  LEU H CG  
10431 C CD1 . LEU G 81  ? 0.8895 1.5824 1.1082 -0.2253 0.0254  -0.2732 81  LEU H CD1 
10432 C CD2 . LEU G 81  ? 0.8895 1.5784 1.1235 -0.1994 0.0039  -0.2518 81  LEU H CD2 
10433 N N   . GLN G 82  ? 1.2355 1.4013 1.3528 -0.0245 -0.0463 -0.2113 82  GLN H N   
10434 C CA  . GLN G 82  ? 1.3006 1.4219 1.3931 0.0124  -0.0730 -0.2293 82  GLN H CA  
10435 C C   . GLN G 82  ? 1.4030 1.5569 1.4999 0.0506  -0.0798 -0.2462 82  GLN H C   
10436 O O   . GLN G 82  ? 1.3830 1.6098 1.4905 0.0596  -0.0548 -0.2502 82  GLN H O   
10437 C CB  . GLN G 82  ? 1.3420 1.4526 1.4051 0.0243  -0.0662 -0.2422 82  GLN H CB  
10438 C CG  . GLN G 82  ? 1.6961 1.7333 1.7249 0.0557  -0.1023 -0.2582 82  GLN H CG  
10439 C CD  . GLN G 82  ? 2.0464 2.0398 2.0502 0.0440  -0.1036 -0.2565 82  GLN H CD  
10440 O OE1 . GLN G 82  ? 1.9972 2.0296 2.0013 0.0291  -0.0733 -0.2545 82  GLN H OE1 
10441 N NE2 . GLN G 82  ? 1.9897 1.8993 1.9717 0.0496  -0.1426 -0.2550 82  GLN H NE2 
10442 N N   . TRP G 83  ? 1.4195 1.5208 1.5091 0.0724  -0.1169 -0.2532 83  TRP H N   
10443 C CA  . TRP G 83  ? 1.4587 1.5776 1.5490 0.1131  -0.1311 -0.2714 83  TRP H CA  
10444 C C   . TRP G 83  ? 1.5661 1.6433 1.6162 0.1639  -0.1589 -0.3007 83  TRP H C   
10445 O O   . TRP G 83  ? 1.5974 1.5912 1.6257 0.1656  -0.1959 -0.3018 83  TRP H O   
10446 C CB  . TRP G 83  ? 1.4487 1.5412 1.5629 0.1018  -0.1575 -0.2581 83  TRP H CB  
10447 C CG  . TRP G 83  ? 1.4126 1.5689 1.5636 0.0758  -0.1304 -0.2415 83  TRP H CG  
10448 C CD1 . TRP G 83  ? 1.4412 1.6647 1.6078 0.0922  -0.1114 -0.2484 83  TRP H CD1 
10449 C CD2 . TRP G 83  ? 1.3671 1.5258 1.5416 0.0310  -0.1222 -0.2146 83  TRP H CD2 
10450 N NE1 . TRP G 83  ? 1.3883 1.6486 1.5865 0.0575  -0.0939 -0.2275 83  TRP H NE1 
10451 C CE2 . TRP G 83  ? 1.3881 1.6096 1.5896 0.0222  -0.1000 -0.2089 83  TRP H CE2 
10452 C CE3 . TRP G 83  ? 1.3718 1.4895 1.5455 0.0000  -0.1324 -0.1937 83  TRP H CE3 
10453 C CZ2 . TRP G 83  ? 1.3397 1.5776 1.5632 -0.0136 -0.0899 -0.1874 83  TRP H CZ2 
10454 C CZ3 . TRP G 83  ? 1.3494 1.4929 1.5456 -0.0329 -0.1195 -0.1717 83  TRP H CZ3 
10455 C CH2 . TRP G 83  ? 1.3296 1.5291 1.5486 -0.0381 -0.0997 -0.1708 83  TRP H CH2 
10456 N N   . SER G 84  ? 1.5327 1.6712 1.5718 0.2073  -0.1436 -0.3229 84  SER H N   
10457 C CA  . SER G 84  ? 1.5984 1.7148 1.5940 0.2686  -0.1669 -0.3568 84  SER H CA  
10458 C C   . SER G 84  ? 1.6908 1.7297 1.6760 0.2962  -0.2216 -0.3701 84  SER H C   
10459 O O   . SER G 84  ? 1.7394 1.6862 1.6932 0.3094  -0.2658 -0.3803 84  SER H O   
10460 C CB  . SER G 84  ? 1.6389 1.8625 1.6329 0.3078  -0.1342 -0.3706 84  SER H CB  
10461 O OG  . SER G 84  ? 1.6459 1.9531 1.6668 0.2697  -0.0872 -0.3468 84  SER H OG  
10462 N N   . SER G 85  ? 1.6217 1.6949 1.6357 0.2993  -0.2217 -0.3660 85  SER H N   
10463 C CA  . SER G 85  ? 1.6580 1.6700 1.6731 0.3184  -0.2719 -0.3734 85  SER H CA  
10464 C C   . SER G 85  ? 1.6102 1.6654 1.6761 0.2794  -0.2551 -0.3467 85  SER H C   
10465 O O   . SER G 85  ? 1.5505 1.6964 1.6388 0.2749  -0.2116 -0.3412 85  SER H O   
10466 C CB  . SER G 85  ? 1.7868 1.8071 1.7685 0.3940  -0.2927 -0.4130 85  SER H CB  
10467 O OG  . SER G 85  ? 1.9571 1.9029 1.9359 0.4132  -0.3507 -0.4219 85  SER H OG  
10468 N N   . LEU G 86  ? 1.5549 1.5481 1.6397 0.2486  -0.2909 -0.3262 86  LEU H N   
10469 C CA  . LEU G 86  ? 1.4943 1.5227 1.6256 0.2102  -0.2794 -0.2993 86  LEU H CA  
10470 C C   . LEU G 86  ? 1.5740 1.6254 1.7195 0.2410  -0.2933 -0.3120 86  LEU H C   
10471 O O   . LEU G 86  ? 1.6428 1.6433 1.7652 0.2849  -0.3379 -0.3357 86  LEU H O   
10472 C CB  . LEU G 86  ? 1.4786 1.4484 1.6272 0.1640  -0.3099 -0.2667 86  LEU H CB  
10473 C CG  . LEU G 86  ? 1.4836 1.4618 1.6367 0.1183  -0.2814 -0.2418 86  LEU H CG  
10474 C CD1 . LEU G 86  ? 1.5001 1.4137 1.6583 0.0877  -0.3226 -0.2123 86  LEU H CD1 
10475 C CD2 . LEU G 86  ? 1.4356 1.4915 1.6213 0.0857  -0.2336 -0.2246 86  LEU H CD2 
10476 N N   . LYS G 87  ? 1.4735 1.5989 1.6556 0.2187  -0.2574 -0.2966 87  LYS H N   
10477 C CA  . LYS G 87  ? 1.4770 1.6362 1.6804 0.2390  -0.2631 -0.3024 87  LYS H CA  
10478 C C   . LYS G 87  ? 1.4996 1.6474 1.7434 0.1919  -0.2753 -0.2713 87  LYS H C   
10479 O O   . LYS G 87  ? 1.4569 1.6048 1.7135 0.1461  -0.2605 -0.2458 87  LYS H O   
10480 C CB  . LYS G 87  ? 1.4643 1.7274 1.6800 0.2480  -0.2112 -0.3040 87  LYS H CB  
10481 C CG  . LYS G 87  ? 1.6413 1.9457 1.8229 0.2931  -0.1913 -0.3279 87  LYS H CG  
10482 C CD  . LYS G 87  ? 1.7363 2.0826 1.9178 0.2602  -0.1494 -0.3124 87  LYS H CD  
10483 C CE  . LYS G 87  ? 1.8230 2.2713 2.0344 0.2409  -0.1053 -0.2927 87  LYS H CE  
10484 N NZ  . LYS G 87  ? 1.8923 2.3399 2.1410 0.1857  -0.0975 -0.2643 87  LYS H NZ  
10485 N N   . ALA G 88  ? 1.4688 1.6139 1.7326 0.2047  -0.3009 -0.2730 88  ALA H N   
10486 C CA  . ALA G 88  ? 1.4271 1.5731 1.7317 0.1625  -0.3123 -0.2426 88  ALA H CA  
10487 C C   . ALA G 88  ? 1.3905 1.6152 1.7221 0.1277  -0.2589 -0.2236 88  ALA H C   
10488 O O   . ALA G 88  ? 1.3386 1.5701 1.6971 0.0870  -0.2583 -0.1962 88  ALA H O   
10489 C CB  . ALA G 88  ? 1.4739 1.6054 1.7935 0.1873  -0.3495 -0.2513 88  ALA H CB  
10490 N N   . SER G 89  ? 1.3358 1.6209 1.6582 0.1449  -0.2178 -0.2367 89  SER H N   
10491 C CA  . SER G 89  ? 1.2757 1.6309 1.6184 0.1151  -0.1726 -0.2200 89  SER H CA  
10492 C C   . SER G 89  ? 1.2907 1.6367 1.6253 0.0784  -0.1540 -0.2053 89  SER H C   
10493 O O   . SER G 89  ? 1.2479 1.6311 1.5996 0.0461  -0.1292 -0.1878 89  SER H O   
10494 C CB  . SER G 89  ? 1.3297 1.7539 1.6659 0.1455  -0.1429 -0.2330 89  SER H CB  
10495 O OG  . SER G 89  ? 1.4887 1.9094 1.7912 0.1691  -0.1349 -0.2494 89  SER H OG  
10496 N N   . ASP G 90  ? 1.2633 1.5564 1.5699 0.0847  -0.1691 -0.2129 90  ASP H N   
10497 C CA  . ASP G 90  ? 1.2307 1.5101 1.5270 0.0536  -0.1545 -0.2002 90  ASP H CA  
10498 C C   . ASP G 90  ? 1.2674 1.5237 1.5814 0.0161  -0.1689 -0.1733 90  ASP H C   
10499 O O   . ASP G 90  ? 1.2504 1.5017 1.5573 -0.0091 -0.1564 -0.1607 90  ASP H O   
10500 C CB  . ASP G 90  ? 1.2847 1.5194 1.5449 0.0744  -0.1649 -0.2165 90  ASP H CB  
10501 C CG  . ASP G 90  ? 1.3982 1.6759 1.6387 0.1031  -0.1381 -0.2367 90  ASP H CG  
10502 O OD1 . ASP G 90  ? 1.3782 1.7264 1.6354 0.0979  -0.1072 -0.2315 90  ASP H OD1 
10503 O OD2 . ASP G 90  ? 1.4897 1.7338 1.6985 0.1295  -0.1497 -0.2546 90  ASP H OD2 
10504 N N   . THR G 91  ? 1.2181 1.4683 1.5560 0.0136  -0.1949 -0.1629 91  THR H N   
10505 C CA  . THR G 91  ? 1.1862 1.4323 1.5453 -0.0189 -0.2098 -0.1334 91  THR H CA  
10506 C C   . THR G 91  ? 1.1625 1.4627 1.5331 -0.0430 -0.1732 -0.1233 91  THR H C   
10507 O O   . THR G 91  ? 1.1430 1.4814 1.5334 -0.0430 -0.1627 -0.1239 91  THR H O   
10508 C CB  . THR G 91  ? 1.3634 1.5986 1.7480 -0.0141 -0.2467 -0.1252 91  THR H CB  
10509 O OG1 . THR G 91  ? 1.4667 1.6489 1.8353 0.0177  -0.2828 -0.1436 91  THR H OG1 
10510 C CG2 . THR G 91  ? 1.3353 1.5696 1.7421 -0.0461 -0.2696 -0.0893 91  THR H CG2 
10511 N N   . ALA G 92  ? 1.0811 1.3813 1.4364 -0.0610 -0.1556 -0.1160 92  ALA H N   
10512 C CA  . ALA G 92  ? 1.0351 1.3754 1.3934 -0.0802 -0.1270 -0.1101 92  ALA H CA  
10513 C C   . ALA G 92  ? 1.0526 1.3837 1.3953 -0.0987 -0.1214 -0.0971 92  ALA H C   
10514 O O   . ALA G 92  ? 1.0614 1.3582 1.3920 -0.0990 -0.1361 -0.0905 92  ALA H O   
10515 C CB  . ALA G 92  ? 1.0424 1.4084 1.3931 -0.0717 -0.1002 -0.1276 92  ALA H CB  
10516 N N   . MET G 93  ? 0.9727 1.3333 1.3141 -0.1123 -0.1028 -0.0935 93  MET H N   
10517 C CA  . MET G 93  ? 0.9502 1.3097 1.2734 -0.1250 -0.0947 -0.0855 93  MET H CA  
10518 C C   . MET G 93  ? 0.9804 1.3321 1.2837 -0.1263 -0.0742 -0.1021 93  MET H C   
10519 O O   . MET G 93  ? 0.9686 1.3409 1.2769 -0.1269 -0.0626 -0.1113 93  MET H O   
10520 C CB  . MET G 93  ? 0.9583 1.3523 1.2885 -0.1329 -0.0931 -0.0751 93  MET H CB  
10521 C CG  . MET G 93  ? 0.9906 1.3878 1.2969 -0.1385 -0.0849 -0.0723 93  MET H CG  
10522 S SD  . MET G 93  ? 1.0348 1.4242 1.3308 -0.1404 -0.0960 -0.0496 93  MET H SD  
10523 C CE  . MET G 93  ? 0.9807 1.4134 1.2659 -0.1374 -0.0943 -0.0389 93  MET H CE  
10524 N N   . TYR G 94  ? 0.9214 1.2461 1.2048 -0.1287 -0.0722 -0.1022 94  TYR H N   
10525 C CA  . TYR G 94  ? 0.9124 1.2305 1.1792 -0.1318 -0.0555 -0.1153 94  TYR H CA  
10526 C C   . TYR G 94  ? 0.9568 1.2689 1.2049 -0.1447 -0.0491 -0.1115 94  TYR H C   
10527 O O   . TYR G 94  ? 0.9601 1.2579 1.1983 -0.1466 -0.0556 -0.1000 94  TYR H O   
10528 C CB  . TYR G 94  ? 0.9443 1.2344 1.2012 -0.1201 -0.0580 -0.1239 94  TYR H CB  
10529 C CG  . TYR G 94  ? 0.9849 1.2815 1.2538 -0.0996 -0.0651 -0.1340 94  TYR H CG  
10530 C CD1 . TYR G 94  ? 1.0226 1.2971 1.2997 -0.0886 -0.0900 -0.1291 94  TYR H CD1 
10531 C CD2 . TYR G 94  ? 0.9983 1.3267 1.2709 -0.0902 -0.0502 -0.1462 94  TYR H CD2 
10532 C CE1 . TYR G 94  ? 1.0357 1.3125 1.3209 -0.0653 -0.1003 -0.1414 94  TYR H CE1 
10533 C CE2 . TYR G 94  ? 1.0241 1.3649 1.3048 -0.0653 -0.0562 -0.1565 94  TYR H CE2 
10534 C CZ  . TYR G 94  ? 1.0965 1.4083 1.3822 -0.0514 -0.0814 -0.1566 94  TYR H CZ  
10535 O OH  . TYR G 94  ? 1.1110 1.4320 1.4020 -0.0228 -0.0904 -0.1698 94  TYR H OH  
10536 N N   . TYR G 95  ? 0.8964 1.2208 1.1399 -0.1532 -0.0399 -0.1189 95  TYR H N   
10537 C CA  . TYR G 95  ? 0.8868 1.2008 1.1098 -0.1629 -0.0382 -0.1198 95  TYR H CA  
10538 C C   . TYR G 95  ? 0.9448 1.2478 1.1589 -0.1722 -0.0292 -0.1275 95  TYR H C   
10539 O O   . TYR G 95  ? 0.9407 1.2604 1.1671 -0.1720 -0.0232 -0.1310 95  TYR H O   
10540 C CB  . TYR G 95  ? 0.8957 1.2258 1.1187 -0.1665 -0.0448 -0.1214 95  TYR H CB  
10541 C CG  . TYR G 95  ? 0.9088 1.2569 1.1380 -0.1574 -0.0535 -0.1136 95  TYR H CG  
10542 C CD1 . TYR G 95  ? 0.9448 1.2949 1.1569 -0.1500 -0.0587 -0.1072 95  TYR H CD1 
10543 C CD2 . TYR G 95  ? 0.9054 1.2760 1.1576 -0.1554 -0.0565 -0.1113 95  TYR H CD2 
10544 C CE1 . TYR G 95  ? 0.9765 1.3554 1.1952 -0.1406 -0.0667 -0.0971 95  TYR H CE1 
10545 C CE2 . TYR G 95  ? 0.9128 1.3043 1.1722 -0.1487 -0.0651 -0.1030 95  TYR H CE2 
10546 C CZ  . TYR G 95  ? 1.0595 1.4574 1.3023 -0.1413 -0.0702 -0.0954 95  TYR H CZ  
10547 O OH  . TYR G 95  ? 1.0739 1.5038 1.3248 -0.1335 -0.0785 -0.0842 95  TYR H OH  
10548 N N   . CYS G 96  ? 0.9104 1.1917 1.1039 -0.1794 -0.0287 -0.1284 96  CYS H N   
10549 C CA  . CYS G 96  ? 0.9135 1.1852 1.0991 -0.1923 -0.0230 -0.1334 96  CYS H CA  
10550 C C   . CYS G 96  ? 0.9450 1.2073 1.1165 -0.2016 -0.0342 -0.1360 96  CYS H C   
10551 O O   . CYS G 96  ? 0.9479 1.2053 1.1071 -0.1920 -0.0422 -0.1359 96  CYS H O   
10552 C CB  . CYS G 96  ? 0.9239 1.1701 1.0964 -0.1918 -0.0159 -0.1330 96  CYS H CB  
10553 S SG  . CYS G 96  ? 0.9795 1.1997 1.1271 -0.1925 -0.0204 -0.1277 96  CYS H SG  
10554 N N   . ALA G 97  ? 0.8884 1.1508 1.0611 -0.2184 -0.0388 -0.1370 97  ALA H N   
10555 C CA  . ALA G 97  ? 0.9043 1.1472 1.0607 -0.2261 -0.0587 -0.1408 97  ALA H CA  
10556 C C   . ALA G 97  ? 0.9900 1.2189 1.1424 -0.2473 -0.0667 -0.1396 97  ALA H C   
10557 O O   . ALA G 97  ? 1.0002 1.2532 1.1718 -0.2615 -0.0596 -0.1311 97  ALA H O   
10558 C CB  . ALA G 97  ? 0.9209 1.1779 1.0864 -0.2267 -0.0744 -0.1390 97  ALA H CB  
10559 N N   . ARG G 98  ? 0.9511 1.1448 1.0779 -0.2475 -0.0832 -0.1474 98  ARG H N   
10560 C CA  . ARG G 98  ? 0.9509 1.1229 1.0717 -0.2684 -0.0980 -0.1466 98  ARG H CA  
10561 C C   . ARG G 98  ? 1.0298 1.2067 1.1629 -0.2877 -0.1266 -0.1383 98  ARG H C   
10562 O O   . ARG G 98  ? 1.0598 1.2190 1.1794 -0.2787 -0.1501 -0.1449 98  ARG H O   
10563 C CB  . ARG G 98  ? 0.9297 1.0607 1.0161 -0.2560 -0.1100 -0.1596 98  ARG H CB  
10564 C CG  . ARG G 98  ? 0.9482 1.0541 1.0284 -0.2757 -0.1188 -0.1592 98  ARG H CG  
10565 C CD  . ARG G 98  ? 0.9862 1.0516 1.0300 -0.2593 -0.1360 -0.1740 98  ARG H CD  
10566 N NE  . ARG G 98  ? 1.1220 1.1586 1.1483 -0.2560 -0.1769 -0.1838 98  ARG H NE  
10567 C CZ  . ARG G 98  ? 1.3231 1.3183 1.3139 -0.2403 -0.2035 -0.2001 98  ARG H CZ  
10568 N NH1 . ARG G 98  ? 1.0975 1.0821 1.0693 -0.2280 -0.1896 -0.2058 98  ARG H NH1 
10569 N NH2 . ARG G 98  ? 1.2448 1.2070 1.2167 -0.2350 -0.2470 -0.2107 98  ARG H NH2 
10570 N N   . VAL G 99  ? 0.9759 1.1817 1.1350 -0.3134 -0.1262 -0.1213 99  VAL H N   
10571 C CA  . VAL G 99  ? 0.9957 1.2188 1.1745 -0.3380 -0.1547 -0.1029 99  VAL H CA  
10572 C C   . VAL G 99  ? 1.0923 1.2701 1.2568 -0.3588 -0.1970 -0.1014 99  VAL H C   
10573 O O   . VAL G 99  ? 1.0882 1.2462 1.2439 -0.3670 -0.1963 -0.1048 99  VAL H O   
10574 C CB  . VAL G 99  ? 1.0207 1.3117 1.2363 -0.3539 -0.1365 -0.0792 99  VAL H CB  
10575 C CG1 . VAL G 99  ? 1.0411 1.3605 1.2808 -0.3814 -0.1679 -0.0520 99  VAL H CG1 
10576 C CG2 . VAL G 99  ? 0.9881 1.3143 1.2128 -0.3279 -0.1015 -0.0851 99  VAL H CG2 
10577 N N   . VAL G 100 ? 1.0895 1.2466 1.2504 -0.3669 -0.2375 -0.0966 100 VAL H N   
10578 C CA  . VAL G 100 ? 1.1422 1.2476 1.2881 -0.3859 -0.2915 -0.0944 100 VAL H CA  
10579 C C   . VAL G 100 ? 1.2160 1.3603 1.4006 -0.4298 -0.3133 -0.0563 100 VAL H C   
10580 O O   . VAL G 100 ? 1.2047 1.4000 1.4181 -0.4402 -0.3097 -0.0333 100 VAL H O   
10581 C CB  . VAL G 100 ? 1.2406 1.2989 1.3582 -0.3683 -0.3300 -0.1094 100 VAL H CB  
10582 C CG1 . VAL G 100 ? 1.3029 1.2877 1.3892 -0.3741 -0.3880 -0.1197 100 VAL H CG1 
10583 C CG2 . VAL G 100 ? 1.2232 1.2789 1.3154 -0.3244 -0.2995 -0.1367 100 VAL H CG2 
10584 N N   . ALA G 101 ? 1.2012 1.3273 1.3883 -0.4560 -0.3372 -0.0463 101 ALA H N   
10585 C CA  . ALA G 101 ? 1.2098 1.3813 1.4366 -0.5015 -0.3615 -0.0037 101 ALA H CA  
10586 C C   . ALA G 101 ? 1.3115 1.4241 1.5289 -0.5304 -0.4225 0.0039  101 ALA H C   
10587 O O   . ALA G 101 ? 1.3254 1.3618 1.5023 -0.5101 -0.4398 -0.0290 101 ALA H O   
10588 C CB  . ALA G 101 ? 1.1711 1.4190 1.4265 -0.5076 -0.3115 0.0110  101 ALA H CB  
10589 N N   . ASP G 102 ? 1.2994 1.4512 1.5551 -0.5773 -0.4583 0.0499  102 ASP H N   
10590 C CA  . ASP G 102 ? 1.3560 1.4590 1.6124 -0.6141 -0.5253 0.0673  102 ASP H CA  
10591 C C   . ASP G 102 ? 1.4193 1.5041 1.6673 -0.6170 -0.5109 0.0536  102 ASP H C   
10592 O O   . ASP G 102 ? 1.3587 1.5074 1.6250 -0.6142 -0.4545 0.0575  102 ASP H O   
10593 C CB  . ASP G 102 ? 1.3868 1.5546 1.6944 -0.6673 -0.5649 0.1298  102 ASP H CB  
10594 C CG  . ASP G 102 ? 1.4693 1.7540 1.8237 -0.6873 -0.5190 0.1658  102 ASP H CG  
10595 O OD1 . ASP G 102 ? 1.4268 1.7874 1.7972 -0.6682 -0.4676 0.1704  102 ASP H OD1 
10596 O OD2 . ASP G 102 ? 1.5822 1.8827 1.9547 -0.7186 -0.5344 0.1872  102 ASP H OD2 
10597 N N   . ARG G 103 ? 1.2294 1.6461 1.5277 -0.2833 -0.0004 -0.1668 103 ARG H N   
10598 C CA  . ARG G 103 ? 1.2369 1.6525 1.5377 -0.2811 -0.0010 -0.1689 103 ARG H CA  
10599 C C   . ARG G 103 ? 1.2855 1.6911 1.5899 -0.2806 -0.0037 -0.1663 103 ARG H C   
10600 O O   . ARG G 103 ? 1.2781 1.6801 1.5873 -0.2813 -0.0070 -0.1675 103 ARG H O   
10601 C CB  . ARG G 103 ? 1.2743 1.7009 1.5817 -0.2793 -0.0022 -0.1782 103 ARG H CB  
10602 C CG  . ARG G 103 ? 1.4624 1.9040 1.7659 -0.2822 0.0003  -0.1800 103 ARG H CG  
10603 C CD  . ARG G 103 ? 1.5840 2.0382 1.8821 -0.2879 0.0013  -0.1812 103 ARG H CD  
10604 N NE  . ARG G 103 ? 1.6438 2.1174 1.9374 -0.2937 0.0017  -0.1817 103 ARG H NE  
10605 C CZ  . ARG G 103 ? 1.8247 2.3103 2.1109 -0.3040 -0.0005 -0.1779 103 ARG H CZ  
10606 N NH1 . ARG G 103 ? 1.7424 2.2195 2.0267 -0.3088 -0.0028 -0.1739 103 ARG H NH1 
10607 N NH2 . ARG G 103 ? 1.5896 2.0964 1.8710 -0.3112 -0.0022 -0.1767 103 ARG H NH2 
10608 N N   . GLU G 104 ? 1.2427 1.6451 1.5456 -0.2814 -0.0035 -0.1622 104 GLU H N   
10609 C CA  . GLU G 104 ? 1.2387 1.6372 1.5432 -0.2842 -0.0069 -0.1583 104 GLU H CA  
10610 C C   . GLU G 104 ? 1.2908 1.6889 1.5892 -0.2865 -0.0018 -0.1547 104 GLU H C   
10611 O O   . GLU G 104 ? 1.2786 1.6778 1.5765 -0.2915 -0.0037 -0.1517 104 GLU H O   
10612 C CB  . GLU G 104 ? 1.2533 1.6531 1.5617 -0.2839 -0.0125 -0.1563 104 GLU H CB  
10613 C CG  . GLU G 104 ? 1.3718 1.7712 1.6869 -0.2806 -0.0198 -0.1617 104 GLU H CG  
10614 C CD  . GLU G 104 ? 1.5488 1.9463 1.8731 -0.2811 -0.0280 -0.1668 104 GLU H CD  
10615 O OE1 . GLU G 104 ? 1.5202 1.9137 1.8466 -0.2873 -0.0338 -0.1621 104 GLU H OE1 
10616 O OE2 . GLU G 104 ? 1.3669 1.7681 1.6974 -0.2766 -0.0293 -0.1762 104 GLU H OE2 
10617 N N   . GLY G 105 ? 1.2576 1.6555 1.5518 -0.2839 0.0026  -0.1557 105 GLY H N   
10618 C CA  . GLY G 105 ? 1.2615 1.6589 1.5516 -0.2835 0.0061  -0.1555 105 GLY H CA  
10619 C C   . GLY G 105 ? 1.3162 1.7207 1.6100 -0.2834 0.0084  -0.1560 105 GLY H C   
10620 O O   . GLY G 105 ? 1.3186 1.7285 1.6108 -0.2873 0.0099  -0.1553 105 GLY H O   
10621 N N   . PHE G 106 ? 1.2722 1.6780 1.5715 -0.2808 0.0080  -0.1566 106 PHE H N   
10622 C CA  . PHE G 106 ? 1.2766 1.6888 1.5820 -0.2802 0.0098  -0.1563 106 PHE H CA  
10623 C C   . PHE G 106 ? 1.3299 1.7416 1.6429 -0.2768 0.0096  -0.1606 106 PHE H C   
10624 O O   . PHE G 106 ? 1.3325 1.7518 1.6530 -0.2751 0.0121  -0.1633 106 PHE H O   
10625 C CB  . PHE G 106 ? 1.3011 1.7119 1.6090 -0.2815 0.0065  -0.1509 106 PHE H CB  
10626 C CG  . PHE G 106 ? 1.3240 1.7383 1.6296 -0.2850 0.0025  -0.1460 106 PHE H CG  
10627 C CD1 . PHE G 106 ? 1.3612 1.7799 1.6693 -0.2865 -0.0007 -0.1395 106 PHE H CD1 
10628 C CD2 . PHE G 106 ? 1.3560 1.7680 1.6585 -0.2878 -0.0013 -0.1466 106 PHE H CD2 
10629 C CE1 . PHE G 106 ? 1.3758 1.7978 1.6822 -0.2912 -0.0095 -0.1332 106 PHE H CE1 
10630 C CE2 . PHE G 106 ? 1.3928 1.8070 1.6964 -0.2930 -0.0102 -0.1417 106 PHE H CE2 
10631 C CZ  . PHE G 106 ? 1.3682 1.7877 1.6732 -0.2949 -0.0153 -0.1348 106 PHE H CZ  
10632 N N   . GLY G 107 ? 1.2840 1.6886 1.5970 -0.2769 0.0046  -0.1612 107 GLY H N   
10633 C CA  . GLY G 107 ? 1.2851 1.6871 1.6078 -0.2758 -0.0014 -0.1646 107 GLY H CA  
10634 C C   . GLY G 107 ? 1.3396 1.7364 1.6696 -0.2811 -0.0074 -0.1606 107 GLY H C   
10635 O O   . GLY G 107 ? 1.3339 1.7276 1.6766 -0.2821 -0.0147 -0.1629 107 GLY H O   
10636 N N   . TYR G 108 ? 1.3015 1.6969 1.6250 -0.2853 -0.0058 -0.1554 108 TYR H N   
10637 C CA  . TYR G 108 ? 1.3023 1.6925 1.6296 -0.2929 -0.0111 -0.1509 108 TYR H CA  
10638 C C   . TYR G 108 ? 1.3754 1.7670 1.6988 -0.3002 -0.0191 -0.1503 108 TYR H C   
10639 O O   . TYR G 108 ? 1.3748 1.7723 1.6880 -0.2995 -0.0167 -0.1511 108 TYR H O   
10640 C CB  . TYR G 108 ? 1.3152 1.7045 1.6355 -0.2939 -0.0069 -0.1472 108 TYR H CB  
10641 C CG  . TYR G 108 ? 1.3388 1.7275 1.6611 -0.2892 -0.0029 -0.1440 108 TYR H CG  
10642 C CD1 . TYR G 108 ? 1.3700 1.7523 1.7001 -0.2913 -0.0046 -0.1384 108 TYR H CD1 
10643 C CD2 . TYR G 108 ? 1.3451 1.7392 1.6614 -0.2849 0.0000  -0.1446 108 TYR H CD2 
10644 C CE1 . TYR G 108 ? 1.3880 1.7718 1.7184 -0.2881 -0.0026 -0.1329 108 TYR H CE1 
10645 C CE2 . TYR G 108 ? 1.3547 1.7508 1.6718 -0.2835 0.0000  -0.1393 108 TYR H CE2 
10646 C CZ  . TYR G 108 ? 1.4553 1.8475 1.7786 -0.2846 -0.0010 -0.1331 108 TYR H CZ  
10647 O OH  . TYR G 108 ? 1.4775 1.8738 1.8003 -0.2840 -0.0027 -0.1256 108 TYR H OH  
10648 N N   . TYR G 109 ? 1.4196 1.5146 0.8812 -0.5232 0.0544  -0.0893 109 TYR H N   
10649 C CA  . TYR G 109 ? 1.4016 1.4762 0.8948 -0.4810 0.0745  -0.0993 109 TYR H CA  
10650 C C   . TYR G 109 ? 1.4815 1.5227 0.9618 -0.4607 0.0677  -0.0883 109 TYR H C   
10651 O O   . TYR G 109 ? 1.4803 1.5472 0.9680 -0.4679 0.0677  -0.0792 109 TYR H O   
10652 C CB  . TYR G 109 ? 1.3715 1.4982 0.9221 -0.4666 0.1092  -0.1153 109 TYR H CB  
10653 C CG  . TYR G 109 ? 1.3883 1.5370 0.9423 -0.4865 0.1160  -0.1265 109 TYR H CG  
10654 C CD1 . TYR G 109 ? 1.4147 1.5268 0.9608 -0.4823 0.1106  -0.1318 109 TYR H CD1 
10655 C CD2 . TYR G 109 ? 1.4024 1.6075 0.9662 -0.5109 0.1274  -0.1312 109 TYR H CD2 
10656 C CE1 . TYR G 109 ? 1.4310 1.5546 0.9738 -0.5044 0.1136  -0.1403 109 TYR H CE1 
10657 C CE2 . TYR G 109 ? 1.4235 1.6428 0.9816 -0.5316 0.1344  -0.1421 109 TYR H CE2 
10658 C CZ  . TYR G 109 ? 1.5077 1.6820 1.0525 -0.5296 0.1260  -0.1461 109 TYR H CZ  
10659 O OH  . TYR G 109 ? 1.4817 1.6615 1.0147 -0.5535 0.1296  -0.1551 109 TYR H OH  
10660 N N   . TYR G 110 ? 1.4540 1.4367 0.9130 -0.4368 0.0608  -0.0884 110 TYR H N   
10661 C CA  . TYR G 110 ? 1.4756 1.4121 0.9079 -0.4180 0.0531  -0.0789 110 TYR H CA  
10662 C C   . TYR G 110 ? 1.4991 1.4409 0.9700 -0.3850 0.0813  -0.0857 110 TYR H C   
10663 O O   . TYR G 110 ? 1.5276 1.4305 0.9739 -0.3719 0.0769  -0.0780 110 TYR H O   
10664 C CB  . TYR G 110 ? 1.5367 1.4027 0.9165 -0.4096 0.0295  -0.0760 110 TYR H CB  
10665 C CG  . TYR G 110 ? 1.5908 1.4383 0.9269 -0.4413 -0.0044 -0.0698 110 TYR H CG  
10666 C CD1 . TYR G 110 ? 1.6291 1.4917 0.9360 -0.4786 -0.0270 -0.0551 110 TYR H CD1 
10667 C CD2 . TYR G 110 ? 1.6207 1.4317 0.9420 -0.4349 -0.0176 -0.0764 110 TYR H CD2 
10668 C CE1 . TYR G 110 ? 1.6664 1.5083 0.9267 -0.5119 -0.0620 -0.0477 110 TYR H CE1 
10669 C CE2 . TYR G 110 ? 1.6684 1.4545 0.9447 -0.4660 -0.0543 -0.0702 110 TYR H CE2 
10670 C CZ  . TYR G 110 ? 1.7626 1.5632 1.0058 -0.5059 -0.0767 -0.0560 110 TYR H CZ  
10671 O OH  . TYR G 110 ? 1.8079 1.5819 1.0020 -0.5406 -0.1160 -0.0486 110 TYR H OH  
10672 N N   . GLY G 111 ? 1.3949 1.3791 0.9190 -0.3744 0.1070  -0.0991 111 GLY H N   
10673 C CA  . GLY G 111 ? 1.3556 1.3458 0.9158 -0.3468 0.1305  -0.1056 111 GLY H CA  
10674 C C   . GLY G 111 ? 1.3571 1.3467 0.9420 -0.3295 0.1454  -0.1164 111 GLY H C   
10675 O O   . GLY G 111 ? 1.3565 1.3497 0.9386 -0.3412 0.1388  -0.1200 111 GLY H O   
10676 N N   . MET G 112 ? 1.2742 1.2585 0.8823 -0.3046 0.1632  -0.1199 112 MET H N   
10677 C CA  . MET G 112 ? 1.2484 1.2356 0.8835 -0.2895 0.1762  -0.1265 112 MET H CA  
10678 C C   . MET G 112 ? 1.3053 1.2577 0.9306 -0.2644 0.1839  -0.1233 112 MET H C   
10679 O O   . MET G 112 ? 1.2939 1.2376 0.9170 -0.2540 0.1926  -0.1209 112 MET H O   
10680 C CB  . MET G 112 ? 1.2402 1.2692 0.9220 -0.2881 0.1922  -0.1350 112 MET H CB  
10681 C CG  . MET G 112 ? 1.2707 1.3175 0.9709 -0.2830 0.2002  -0.1365 112 MET H CG  
10682 S SD  . MET G 112 ? 1.2998 1.3987 1.0285 -0.2979 0.2033  -0.1459 112 MET H SD  
10683 C CE  . MET G 112 ? 1.2388 1.3548 0.9941 -0.2956 0.2143  -0.1574 112 MET H CE  
10684 N N   . ASP G 113 ? 1.2830 1.2153 0.9019 -0.2555 0.1802  -0.1233 113 ASP H N   
10685 C CA  . ASP G 113 ? 1.3095 1.2120 0.9188 -0.2300 0.1890  -0.1215 113 ASP H CA  
10686 C C   . ASP G 113 ? 1.3443 1.2707 0.9984 -0.2127 0.2118  -0.1225 113 ASP H C   
10687 O O   . ASP G 113 ? 1.3652 1.2862 1.0174 -0.2002 0.2268  -0.1210 113 ASP H O   
10688 C CB  . ASP G 113 ? 1.3716 1.2403 0.9542 -0.2252 0.1720  -0.1211 113 ASP H CB  
10689 C CG  . ASP G 113 ? 1.5096 1.3916 1.1108 -0.2398 0.1576  -0.1227 113 ASP H CG  
10690 O OD1 . ASP G 113 ? 1.4874 1.4053 1.1314 -0.2455 0.1676  -0.1243 113 ASP H OD1 
10691 O OD2 . ASP G 113 ? 1.6135 1.4638 1.1824 -0.2460 0.1338  -0.1218 113 ASP H OD2 
10692 N N   . VAL G 114 ? 1.2636 1.2118 0.9532 -0.2139 0.2123  -0.1230 114 VAL H N   
10693 C CA  . VAL G 114 ? 1.2360 1.2081 0.9686 -0.2011 0.2296  -0.1200 114 VAL H CA  
10694 C C   . VAL G 114 ? 1.2499 1.2498 1.0052 -0.2109 0.2365  -0.1215 114 VAL H C   
10695 O O   . VAL G 114 ? 1.2296 1.2433 0.9894 -0.2282 0.2277  -0.1259 114 VAL H O   
10696 C CB  . VAL G 114 ? 1.2813 1.2621 1.0434 -0.2006 0.2231  -0.1166 114 VAL H CB  
10697 C CG1 . VAL G 114 ? 1.2636 1.2692 1.0693 -0.1865 0.2403  -0.1092 114 VAL H CG1 
10698 C CG2 . VAL G 114 ? 1.3137 1.2628 1.0517 -0.1920 0.2094  -0.1173 114 VAL H CG2 
10699 N N   . TRP G 115 ? 1.1960 1.2017 0.9620 -0.2001 0.2514  -0.1186 115 TRP H N   
10700 C CA  . TRP G 115 ? 1.1713 1.1969 0.9568 -0.2070 0.2544  -0.1202 115 TRP H CA  
10701 C C   . TRP G 115 ? 1.2511 1.2959 1.0714 -0.2015 0.2633  -0.1129 115 TRP H C   
10702 O O   . TRP G 115 ? 1.2572 1.3024 1.0852 -0.1892 0.2738  -0.1056 115 TRP H O   
10703 C CB  . TRP G 115 ? 1.1587 1.1691 0.9212 -0.2054 0.2571  -0.1213 115 TRP H CB  
10704 C CG  . TRP G 115 ? 1.1716 1.1727 0.9094 -0.2165 0.2448  -0.1258 115 TRP H CG  
10705 C CD1 . TRP G 115 ? 1.2318 1.2088 0.9341 -0.2193 0.2356  -0.1245 115 TRP H CD1 
10706 C CD2 . TRP G 115 ? 1.1556 1.1707 0.9021 -0.2259 0.2390  -0.1303 115 TRP H CD2 
10707 N NE1 . TRP G 115 ? 1.2220 1.2015 0.9116 -0.2334 0.2242  -0.1258 115 TRP H NE1 
10708 C CE2 . TRP G 115 ? 1.2193 1.2248 0.9392 -0.2361 0.2277  -0.1299 115 TRP H CE2 
10709 C CE3 . TRP G 115 ? 1.1519 1.1870 0.9273 -0.2263 0.2402  -0.1346 115 TRP H CE3 
10710 C CZ2 . TRP G 115 ? 1.2069 1.2297 0.9351 -0.2462 0.2205  -0.1328 115 TRP H CZ2 
10711 C CZ3 . TRP G 115 ? 1.1692 1.2169 0.9513 -0.2331 0.2327  -0.1403 115 TRP H CZ3 
10712 C CH2 . TRP G 115 ? 1.1896 1.2352 0.9519 -0.2428 0.2245  -0.1390 115 TRP H CH2 
10713 N N   . GLY G 116 ? 1.2155 1.2763 1.0554 -0.2106 0.2584  -0.1147 116 GLY H N   
10714 C CA  . GLY G 116 ? 1.2119 1.2877 1.0802 -0.2102 0.2608  -0.1058 116 GLY H CA  
10715 C C   . GLY G 116 ? 1.2891 1.3627 1.1540 -0.2051 0.2688  -0.1013 116 GLY H C   
10716 O O   . GLY G 116 ? 1.2839 1.3416 1.1246 -0.2033 0.2705  -0.1068 116 GLY H O   
10717 N N   . GLN G 117 ? 1.2702 1.3576 1.1568 -0.2060 0.2714  -0.0894 117 GLN H N   
10718 C CA  . GLN G 117 ? 1.2864 1.3712 1.1662 -0.2057 0.2775  -0.0835 117 GLN H CA  
10719 C C   . GLN G 117 ? 1.3716 1.4436 1.2415 -0.2135 0.2633  -0.0913 117 GLN H C   
10720 O O   . GLN G 117 ? 1.3797 1.4375 1.2320 -0.2149 0.2648  -0.0907 117 GLN H O   
10721 C CB  . GLN G 117 ? 1.2961 1.4035 1.2014 -0.2074 0.2835  -0.0657 117 GLN H CB  
10722 C CG  . GLN G 117 ? 1.3337 1.4490 1.2571 -0.2203 0.2662  -0.0574 117 GLN H CG  
10723 C CD  . GLN G 117 ? 1.4823 1.6030 1.4241 -0.2245 0.2548  -0.0559 117 GLN H CD  
10724 O OE1 . GLN G 117 ? 1.3781 1.5021 1.3260 -0.2191 0.2597  -0.0580 117 GLN H OE1 
10725 N NE2 . GLN G 117 ? 1.3887 1.5047 1.3350 -0.2354 0.2367  -0.0518 117 GLN H NE2 
10726 N N   . GLY G 118 ? 1.3342 1.4089 1.2139 -0.2181 0.2496  -0.0992 118 GLY H N   
10727 C CA  . GLY G 118 ? 1.3331 1.3983 1.2096 -0.2212 0.2353  -0.1090 118 GLY H CA  
10728 C C   . GLY G 118 ? 1.3732 1.4386 1.2619 -0.2270 0.2209  -0.1034 118 GLY H C   
10729 O O   . GLY G 118 ? 1.3779 1.4448 1.2697 -0.2322 0.2197  -0.0885 118 GLY H O   
10730 N N   . THR G 119 ? 1.3096 1.3726 1.2022 -0.2270 0.2094  -0.1148 119 THR H N   
10731 C CA  . THR G 119 ? 1.3143 1.3678 1.2103 -0.2316 0.1915  -0.1114 119 THR H CA  
10732 C C   . THR G 119 ? 1.3681 1.4049 1.2580 -0.2282 0.1758  -0.1217 119 THR H C   
10733 O O   . THR G 119 ? 1.3624 1.3996 1.2529 -0.2202 0.1761  -0.1392 119 THR H O   
10734 C CB  . THR G 119 ? 1.4161 1.4693 1.3132 -0.2334 0.1880  -0.1176 119 THR H CB  
10735 O OG1 . THR G 119 ? 1.3917 1.4577 1.2958 -0.2376 0.1998  -0.1073 119 THR H OG1 
10736 C CG2 . THR G 119 ? 1.4255 1.4604 1.3184 -0.2392 0.1673  -0.1114 119 THR H CG2 
10737 N N   . THR G 120 ? 1.3283 1.3516 1.2138 -0.2355 0.1603  -0.1096 120 THR H N   
10738 C CA  . THR G 120 ? 1.3378 1.3389 1.2162 -0.2343 0.1392  -0.1172 120 THR H CA  
10739 C C   . THR G 120 ? 1.4094 1.3915 1.2846 -0.2303 0.1160  -0.1264 120 THR H C   
10740 O O   . THR G 120 ? 1.4147 1.3840 1.2820 -0.2400 0.1000  -0.1123 120 THR H O   
10741 C CB  . THR G 120 ? 1.3907 1.3833 1.2589 -0.2474 0.1336  -0.0995 120 THR H CB  
10742 O OG1 . THR G 120 ? 1.3494 1.3588 1.2165 -0.2486 0.1597  -0.0918 120 THR H OG1 
10743 C CG2 . THR G 120 ? 1.3842 1.3500 1.2428 -0.2484 0.1116  -0.1074 120 THR H CG2 
10744 N N   . VAL G 121 ? 1.3763 1.3566 1.2566 -0.2157 0.1144  -0.1498 121 VAL H N   
10745 C CA  . VAL G 121 ? 1.3999 1.3602 1.2741 -0.2064 0.0961  -0.1644 121 VAL H CA  
10746 C C   . VAL G 121 ? 1.4900 1.4264 1.3645 -0.1972 0.0704  -0.1763 121 VAL H C   
10747 O O   . VAL G 121 ? 1.4768 1.4242 1.3672 -0.1869 0.0751  -0.1900 121 VAL H O   
10748 C CB  . VAL G 121 ? 1.4384 1.4159 1.3171 -0.1960 0.1144  -0.1832 121 VAL H CB  
10749 C CG1 . VAL G 121 ? 1.4670 1.4211 1.3349 -0.1831 0.0985  -0.2020 121 VAL H CG1 
10750 C CG2 . VAL G 121 ? 1.4213 1.4122 1.2960 -0.2082 0.1311  -0.1697 121 VAL H CG2 
10751 N N   . THR G 122 ? 1.4920 1.3937 1.3487 -0.2020 0.0399  -0.1697 122 THR H N   
10752 C CA  . THR G 122 ? 1.5314 1.4006 1.3839 -0.1942 0.0072  -0.1802 122 THR H CA  
10753 C C   . THR G 122 ? 1.6375 1.4818 1.4791 -0.1760 -0.0086 -0.2004 122 THR H C   
10754 O O   . THR G 122 ? 1.6474 1.4731 1.4659 -0.1831 -0.0161 -0.1914 122 THR H O   
10755 C CB  . THR G 122 ? 1.6736 1.5159 1.5066 -0.2163 -0.0203 -0.1565 122 THR H CB  
10756 O OG1 . THR G 122 ? 1.6703 1.5390 1.5067 -0.2343 0.0026  -0.1353 122 THR H OG1 
10757 C CG2 . THR G 122 ? 1.6788 1.4891 1.5096 -0.2132 -0.0536 -0.1649 122 THR H CG2 
10758 N N   . VAL G 123 ? 1.6328 1.4771 1.4912 -0.1521 -0.0125 -0.2273 123 VAL H N   
10759 C CA  . VAL G 123 ? 1.6826 1.5037 1.5305 -0.1292 -0.0239 -0.2516 123 VAL H CA  
10760 C C   . VAL G 123 ? 1.7986 1.5829 1.6485 -0.1130 -0.0625 -0.2661 123 VAL H C   
10761 O O   . VAL G 123 ? 1.7861 1.5872 1.6667 -0.0897 -0.0584 -0.2893 123 VAL H O   
10762 C CB  . VAL G 123 ? 1.7203 1.5799 1.5857 -0.1111 0.0120  -0.2751 123 VAL H CB  
10763 C CG1 . VAL G 123 ? 1.7670 1.5961 1.6051 -0.0945 0.0049  -0.2945 123 VAL H CG1 
10764 C CG2 . VAL G 123 ? 1.6740 1.5720 1.5432 -0.1292 0.0469  -0.2603 123 VAL H CG2 
10765 N N   . SER G 124 ? 1.8218 1.5560 1.6396 -0.1266 -0.1024 -0.2508 124 SER H N   
10766 C CA  . SER G 124 ? 1.8791 1.5663 1.6898 -0.1161 -0.1484 -0.2607 124 SER H CA  
10767 C C   . SER G 124 ? 2.0155 1.6404 1.7778 -0.1167 -0.1876 -0.2583 124 SER H C   
10768 O O   . SER G 124 ? 2.0200 1.6342 1.7519 -0.1401 -0.1890 -0.2341 124 SER H O   
10769 C CB  . SER G 124 ? 1.9124 1.5942 1.7286 -0.1399 -0.1674 -0.2403 124 SER H CB  
10770 O OG  . SER G 124 ? 2.0661 1.6973 1.8731 -0.1333 -0.2172 -0.2485 124 SER H OG  
10771 N N   . SER G 125 ? 2.0276 1.6097 1.7834 -0.0905 -0.2218 -0.2826 125 SER H N   
10772 C CA  . SER G 125 ? 2.0946 1.6059 1.7989 -0.0857 -0.2658 -0.2851 125 SER H CA  
10773 C C   . SER G 125 ? 2.1847 1.6489 1.8543 -0.1194 -0.3161 -0.2543 125 SER H C   
10774 O O   . SER G 125 ? 2.2196 1.6277 1.8384 -0.1286 -0.3521 -0.2435 125 SER H O   
10775 C CB  . SER G 125 ? 2.1741 1.6567 1.8860 -0.0423 -0.2847 -0.3243 125 SER H CB  
10776 O OG  . SER G 125 ? 2.2079 1.7380 1.9502 -0.0127 -0.2370 -0.3525 125 SER H OG  
10777 N N   . ALA G 126 ? 2.1410 1.6267 1.8347 -0.1396 -0.3187 -0.2395 126 ALA H N   
10778 C CA  . ALA G 126 ? 2.1769 1.6301 1.8462 -0.1749 -0.3607 -0.2115 126 ALA H CA  
10779 C C   . ALA G 126 ? 2.2886 1.7094 1.9067 -0.2088 -0.3873 -0.1782 126 ALA H C   
10780 O O   . ALA G 126 ? 2.3464 1.7084 1.9270 -0.2236 -0.4438 -0.1683 126 ALA H O   
10781 C CB  . ALA G 126 ? 2.1327 1.6352 1.8340 -0.1965 -0.3322 -0.1961 126 ALA H CB  
10782 N N   . SER G 127 ? 2.2252 1.6840 1.8427 -0.2234 -0.3505 -0.1586 127 SER H N   
10783 C CA  . SER G 127 ? 2.2482 1.6912 1.8278 -0.2579 -0.3686 -0.1218 127 SER H CA  
10784 C C   . SER G 127 ? 2.3002 1.7641 1.8792 -0.3005 -0.3754 -0.0859 127 SER H C   
10785 O O   . SER G 127 ? 2.2988 1.7581 1.8859 -0.3065 -0.3886 -0.0898 127 SER H O   
10786 C CB  . SER G 127 ? 2.3693 1.7326 1.8929 -0.2553 -0.4257 -0.1224 127 SER H CB  
10787 O OG  . SER G 127 ? 2.4981 1.8308 2.0190 -0.2114 -0.4280 -0.1628 127 SER H OG  
10788 N N   . THR G 128 ? 2.2576 1.7438 1.8264 -0.3308 -0.3669 -0.0505 128 THR H N   
10789 C CA  . THR G 128 ? 2.2484 1.7653 1.8179 -0.3720 -0.3654 -0.0139 128 THR H CA  
10790 C C   . THR G 128 ? 2.3699 1.8365 1.9010 -0.3997 -0.4241 0.0002  128 THR H C   
10791 O O   . THR G 128 ? 2.4205 1.8292 1.9077 -0.4097 -0.4767 0.0101  128 THR H O   
10792 C CB  . THR G 128 ? 2.3578 1.9058 1.9265 -0.3950 -0.3508 0.0209  128 THR H CB  
10793 O OG1 . THR G 128 ? 2.3403 1.9148 1.9332 -0.3695 -0.3102 0.0060  128 THR H OG1 
10794 C CG2 . THR G 128 ? 2.3028 1.9090 1.8916 -0.4276 -0.3254 0.0525  128 THR H CG2 
10795 N N   . LYS G 129 ? 2.3356 1.8200 1.8787 -0.4142 -0.4169 0.0019  129 LYS H N   
10796 C CA  . LYS G 129 ? 2.3976 1.8396 1.9052 -0.4470 -0.4683 0.0169  129 LYS H CA  
10797 C C   . LYS G 129 ? 2.4496 1.9395 1.9682 -0.4793 -0.4383 0.0382  129 LYS H C   
10798 O O   . LYS G 129 ? 2.3889 1.9209 1.9430 -0.4633 -0.3891 0.0238  129 LYS H O   
10799 C CB  . LYS G 129 ? 2.4678 1.8511 1.9686 -0.4234 -0.5072 -0.0162 129 LYS H CB  
10800 C CG  . LYS G 129 ? 2.7032 2.0222 2.1554 -0.4579 -0.5774 -0.0007 129 LYS H CG  
10801 C CD  . LYS G 129 ? 2.8228 2.0959 2.2799 -0.4400 -0.6092 -0.0301 129 LYS H CD  
10802 C CE  . LYS G 129 ? 2.9280 2.1396 2.3367 -0.4810 -0.6775 -0.0121 129 LYS H CE  
10803 N NZ  . LYS G 129 ? 2.9489 2.1929 2.3548 -0.5245 -0.6583 0.0120  129 LYS H NZ  
10804 N N   . GLY G 130 ? 2.3425 1.8803 2.0981 -0.1571 -0.4165 0.2918  130 GLY H N   
10805 C CA  . GLY G 130 ? 2.3380 1.8958 2.1136 -0.1248 -0.4240 0.3055  130 GLY H CA  
10806 C C   . GLY G 130 ? 2.4230 1.9417 2.2039 -0.0967 -0.4130 0.3077  130 GLY H C   
10807 O O   . GLY G 130 ? 2.4312 1.9087 2.2055 -0.1042 -0.3947 0.3014  130 GLY H O   
10808 N N   . PRO G 131 ? 2.3894 1.9204 2.1836 -0.0676 -0.4207 0.3194  131 PRO H N   
10809 C CA  . PRO G 131 ? 2.3869 1.8897 2.1836 -0.0450 -0.4119 0.3233  131 PRO H CA  
10810 C C   . PRO G 131 ? 2.4585 1.9555 2.2679 -0.0434 -0.3930 0.3254  131 PRO H C   
10811 O O   . PRO G 131 ? 2.4476 1.9646 2.2682 -0.0436 -0.3926 0.3266  131 PRO H O   
10812 C CB  . PRO G 131 ? 2.3889 1.9104 2.1916 -0.0205 -0.4252 0.3329  131 PRO H CB  
10813 C CG  . PRO G 131 ? 2.4413 2.0014 2.2560 -0.0283 -0.4346 0.3402  131 PRO H CG  
10814 C CD  . PRO G 131 ? 2.4011 1.9713 2.2100 -0.0577 -0.4346 0.3326  131 PRO H CD  
10815 N N   . SER G 132 ? 2.4409 1.9101 2.2524 -0.0396 -0.3757 0.3286  132 SER H N   
10816 C CA  . SER G 132 ? 2.4479 1.9162 2.2787 -0.0338 -0.3525 0.3349  132 SER H CA  
10817 C C   . SER G 132 ? 2.5041 1.9830 2.3383 -0.0075 -0.3642 0.3473  132 SER H C   
10818 O O   . SER G 132 ? 2.4910 1.9598 2.3232 0.0024  -0.3628 0.3579  132 SER H O   
10819 C CB  . SER G 132 ? 2.5029 1.9420 2.3417 -0.0451 -0.3233 0.3400  132 SER H CB  
10820 O OG  . SER G 132 ? 2.6315 2.0526 2.4613 -0.0754 -0.3109 0.3272  132 SER H OG  
10821 N N   . VAL G 133 ? 2.4754 1.9734 2.3133 -0.0001 -0.3759 0.3468  133 VAL H N   
10822 C CA  . VAL G 133 ? 2.4721 1.9777 2.3112 0.0172  -0.3838 0.3563  133 VAL H CA  
10823 C C   . VAL G 133 ? 2.5456 2.0517 2.3997 0.0273  -0.3670 0.3651  133 VAL H C   
10824 O O   . VAL G 133 ? 2.5444 2.0516 2.4162 0.0272  -0.3511 0.3613  133 VAL H O   
10825 C CB  . VAL G 133 ? 2.5150 2.0314 2.3583 0.0176  -0.3951 0.3567  133 VAL H CB  
10826 C CG1 . VAL G 133 ? 2.5030 2.0203 2.3452 0.0281  -0.3977 0.3658  133 VAL H CG1 
10827 C CG2 . VAL G 133 ? 2.5132 2.0415 2.3510 0.0067  -0.4077 0.3537  133 VAL H CG2 
10828 N N   . PHE G 134 ? 2.5112 2.0214 2.3602 0.0360  -0.3685 0.3771  134 PHE H N   
10829 C CA  . PHE G 134 ? 2.5077 2.0293 2.3725 0.0452  -0.3544 0.3912  134 PHE H CA  
10830 C C   . PHE G 134 ? 2.5547 2.0878 2.4075 0.0500  -0.3654 0.3980  134 PHE H C   
10831 O O   . PHE G 134 ? 2.5500 2.0844 2.3827 0.0464  -0.3768 0.3969  134 PHE H O   
10832 C CB  . PHE G 134 ? 2.5315 2.0547 2.4077 0.0439  -0.3375 0.4070  134 PHE H CB  
10833 C CG  . PHE G 134 ? 2.5605 2.0632 2.4430 0.0312  -0.3223 0.4021  134 PHE H CG  
10834 C CD1 . PHE G 134 ? 2.6005 2.1022 2.5061 0.0249  -0.2957 0.3954  134 PHE H CD1 
10835 C CD2 . PHE G 134 ? 2.5968 2.0781 2.4635 0.0243  -0.3294 0.4038  134 PHE H CD2 
10836 C CE1 . PHE G 134 ? 2.6226 2.1034 2.5325 0.0055  -0.2752 0.3900  134 PHE H CE1 
10837 C CE2 . PHE G 134 ? 2.6421 2.0959 2.5132 0.0080  -0.3124 0.3995  134 PHE H CE2 
10838 C CZ  . PHE G 134 ? 2.6205 2.0749 2.5124 -0.0043 -0.2841 0.3931  134 PHE H CZ  
10839 N N   . PRO G 135 ? 2.5051 2.0453 2.3699 0.0569  -0.3588 0.4036  135 PRO H N   
10840 C CA  . PRO G 135 ? 2.4986 2.0470 2.3487 0.0538  -0.3656 0.4093  135 PRO H CA  
10841 C C   . PRO G 135 ? 2.5212 2.0977 2.3661 0.0516  -0.3633 0.4274  135 PRO H C   
10842 O O   . PRO G 135 ? 2.5116 2.0995 2.3718 0.0557  -0.3541 0.4406  135 PRO H O   
10843 C CB  . PRO G 135 ? 2.5199 2.0572 2.3850 0.0610  -0.3591 0.4075  135 PRO H CB  
10844 C CG  . PRO G 135 ? 2.5724 2.1038 2.4636 0.0722  -0.3464 0.4014  135 PRO H CG  
10845 C CD  . PRO G 135 ? 2.5186 2.0587 2.4115 0.0672  -0.3412 0.4031  135 PRO H CD  
10846 N N   . LEU G 136 ? 2.4602 2.0488 2.2848 0.0413  -0.3683 0.4301  136 LEU H N   
10847 C CA  . LEU G 136 ? 2.4477 2.0711 2.2629 0.0341  -0.3681 0.4483  136 LEU H CA  
10848 C C   . LEU G 136 ? 2.5000 2.1372 2.3053 0.0222  -0.3656 0.4520  136 LEU H C   
10849 O O   . LEU G 136 ? 2.5033 2.1271 2.2870 0.0071  -0.3656 0.4387  136 LEU H O   
10850 C CB  . LEU G 136 ? 2.4445 2.0708 2.2353 0.0264  -0.3756 0.4433  136 LEU H CB  
10851 C CG  . LEU G 136 ? 2.4877 2.0925 2.2837 0.0358  -0.3788 0.4385  136 LEU H CG  
10852 C CD1 . LEU G 136 ? 2.4843 2.0800 2.2567 0.0330  -0.3852 0.4222  136 LEU H CD1 
10853 C CD2 . LEU G 136 ? 2.5066 2.1233 2.3200 0.0400  -0.3725 0.4633  136 LEU H CD2 
10854 N N   . ALA G 137 ? 2.4482 2.1110 2.2733 0.0282  -0.3588 0.4710  137 ALA H N   
10855 C CA  . ALA G 137 ? 2.4504 2.1266 2.2696 0.0178  -0.3556 0.4768  137 ALA H CA  
10856 C C   . ALA G 137 ? 2.5077 2.2139 2.2916 -0.0117 -0.3593 0.4812  137 ALA H C   
10857 O O   . ALA G 137 ? 2.5023 2.2417 2.2777 -0.0173 -0.3638 0.4936  137 ALA H O   
10858 C CB  . ALA G 137 ? 2.4476 2.1565 2.3025 0.0345  -0.3451 0.5000  137 ALA H CB  
10859 N N   . PRO G 138 ? 2.4735 2.1665 2.2368 -0.0335 -0.3544 0.4717  138 PRO H N   
10860 C CA  . PRO G 138 ? 2.5292 2.2535 2.2565 -0.0686 -0.3513 0.4724  138 PRO H CA  
10861 C C   . PRO G 138 ? 2.7220 2.5133 2.4469 -0.0804 -0.3550 0.5008  138 PRO H C   
10862 O O   . PRO G 138 ? 2.1530 1.9613 1.9026 -0.0682 -0.3543 0.5187  138 PRO H O   
10863 C CB  . PRO G 138 ? 2.5596 2.2407 2.2713 -0.0913 -0.3377 0.4549  138 PRO H CB  
10864 C CG  . PRO G 138 ? 2.5931 2.2359 2.3340 -0.0668 -0.3387 0.4558  138 PRO H CG  
10865 C CD  . PRO G 138 ? 2.5066 2.1493 2.2780 -0.0303 -0.3478 0.4589  138 PRO H CD  
10866 N N   . ALA G 148 ? 2.5235 2.2985 2.0677 -0.3116 -0.2389 0.4114  148 ALA H N   
10867 C CA  . ALA G 148 ? 2.4990 2.2886 2.0695 -0.2591 -0.2715 0.4237  148 ALA H CA  
10868 C C   . ALA G 148 ? 2.5338 2.2609 2.1365 -0.2215 -0.2716 0.4126  148 ALA H C   
10869 O O   . ALA G 148 ? 2.5231 2.1964 2.1425 -0.2170 -0.2654 0.4110  148 ALA H O   
10870 C CB  . ALA G 148 ? 2.5058 2.3267 2.0925 -0.2395 -0.2999 0.4529  148 ALA H CB  
10871 N N   . ALA G 149 ? 2.4849 2.2193 2.0956 -0.1960 -0.2784 0.4060  149 ALA H N   
10872 C CA  . ALA G 149 ? 2.4671 2.1569 2.1055 -0.1634 -0.2795 0.3964  149 ALA H CA  
10873 C C   . ALA G 149 ? 2.5188 2.1969 2.1852 -0.1220 -0.3098 0.4102  149 ALA H C   
10874 O O   . ALA G 149 ? 2.5157 2.2278 2.1840 -0.1121 -0.3283 0.4283  149 ALA H O   
10875 C CB  . ALA G 149 ? 2.4621 2.1666 2.0945 -0.1582 -0.2686 0.3805  149 ALA H CB  
10876 N N   . LEU G 150 ? 2.4747 2.1086 2.1656 -0.1005 -0.3104 0.4037  150 LEU H N   
10877 C CA  . LEU G 150 ? 2.4667 2.0861 2.1839 -0.0657 -0.3319 0.4113  150 LEU H CA  
10878 C C   . LEU G 150 ? 2.5043 2.1116 2.2326 -0.0456 -0.3369 0.4016  150 LEU H C   
10879 O O   . LEU G 150 ? 2.4966 2.0901 2.2260 -0.0525 -0.3213 0.3900  150 LEU H O   
10880 C CB  . LEU G 150 ? 2.4721 2.0529 2.2088 -0.0588 -0.3317 0.4146  150 LEU H CB  
10881 C CG  . LEU G 150 ? 2.5417 2.0758 2.2826 -0.0748 -0.3120 0.4066  150 LEU H CG  
10882 C CD1 . LEU G 150 ? 2.5303 2.0378 2.2946 -0.0555 -0.3150 0.4024  150 LEU H CD1 
10883 C CD2 . LEU G 150 ? 2.5917 2.0927 2.3388 -0.0791 -0.3088 0.4121  150 LEU H CD2 
10884 N N   . GLY G 151 ? 2.4476 2.0613 2.1876 -0.0226 -0.3544 0.4083  151 GLY H N   
10885 C CA  . GLY G 151 ? 2.4274 2.0293 2.1753 -0.0053 -0.3615 0.4000  151 GLY H CA  
10886 C C   . GLY G 151 ? 2.4489 2.0235 2.2198 0.0097  -0.3679 0.3979  151 GLY H C   
10887 O O   . GLY G 151 ? 2.4473 2.0085 2.2312 0.0113  -0.3669 0.4023  151 GLY H O   
10888 N N   . CYS G 152 ? 2.3748 1.9416 2.1499 0.0201  -0.3739 0.3900  152 CYS H N   
10889 C CA  . CYS G 152 ? 2.3570 1.9055 2.1495 0.0290  -0.3801 0.3864  152 CYS H CA  
10890 C C   . CYS G 152 ? 2.3478 1.8940 2.1368 0.0370  -0.3878 0.3801  152 CYS H C   
10891 O O   . CYS G 152 ? 2.3312 1.8799 2.1153 0.0385  -0.3860 0.3714  152 CYS H O   
10892 C CB  . CYS G 152 ? 2.3635 1.9009 2.1662 0.0228  -0.3729 0.3835  152 CYS H CB  
10893 S SG  . CYS G 152 ? 2.4178 1.9377 2.2427 0.0280  -0.3804 0.3845  152 CYS H SG  
10894 N N   . LEU G 153 ? 2.2714 1.8113 2.0658 0.0418  -0.3915 0.3853  153 LEU H N   
10895 C CA  . LEU G 153 ? 2.2511 1.7769 2.0419 0.0457  -0.3961 0.3806  153 LEU H CA  
10896 C C   . LEU G 153 ? 2.2795 1.7933 2.0786 0.0428  -0.3997 0.3709  153 LEU H C   
10897 O O   . LEU G 153 ? 2.2820 1.7957 2.0941 0.0387  -0.3962 0.3719  153 LEU H O   
10898 C CB  . LEU G 153 ? 2.2519 1.7727 2.0485 0.0466  -0.3905 0.3957  153 LEU H CB  
10899 C CG  . LEU G 153 ? 2.3062 1.7977 2.1023 0.0464  -0.3898 0.3941  153 LEU H CG  
10900 C CD1 . LEU G 153 ? 2.2997 1.7802 2.0771 0.0538  -0.3982 0.3877  153 LEU H CD1 
10901 C CD2 . LEU G 153 ? 2.3393 1.8246 2.1544 0.0428  -0.3736 0.4150  153 LEU H CD2 
10902 N N   . VAL G 154 ? 2.2079 1.7140 1.9996 0.0450  -0.4060 0.3610  154 VAL H N   
10903 C CA  . VAL G 154 ? 2.1947 1.6958 1.9906 0.0384  -0.4113 0.3529  154 VAL H CA  
10904 C C   . VAL G 154 ? 2.2337 1.7054 2.0204 0.0369  -0.4115 0.3488  154 VAL H C   
10905 O O   . VAL G 154 ? 2.2214 1.6828 1.9984 0.0469  -0.4160 0.3425  154 VAL H O   
10906 C CB  . VAL G 154 ? 2.2236 1.7448 2.0240 0.0422  -0.4150 0.3489  154 VAL H CB  
10907 C CG1 . VAL G 154 ? 2.2229 1.7500 2.0286 0.0324  -0.4225 0.3451  154 VAL H CG1 
10908 C CG2 . VAL G 154 ? 2.2141 1.7534 2.0262 0.0408  -0.4078 0.3574  154 VAL H CG2 
10909 N N   . LYS G 155 ? 2.1882 1.6427 1.9810 0.0249  -0.4012 0.3528  155 LYS H N   
10910 C CA  . LYS G 155 ? 2.1863 1.6028 1.9745 0.0184  -0.3938 0.3534  155 LYS H CA  
10911 C C   . LYS G 155 ? 2.2449 1.6438 2.0307 -0.0030 -0.3893 0.3421  155 LYS H C   
10912 O O   . LYS G 155 ? 2.2511 1.6681 2.0449 -0.0175 -0.3828 0.3383  155 LYS H O   
10913 C CB  . LYS G 155 ? 2.2112 1.6181 2.0134 0.0172  -0.3746 0.3728  155 LYS H CB  
10914 C CG  . LYS G 155 ? 2.3196 1.6856 2.1181 0.0182  -0.3690 0.3824  155 LYS H CG  
10915 C CD  . LYS G 155 ? 2.4598 1.8157 2.2831 0.0098  -0.3411 0.4081  155 LYS H CD  
10916 C CE  . LYS G 155 ? 2.6194 1.9243 2.4426 0.0073  -0.3328 0.4217  155 LYS H CE  
10917 N NZ  . LYS G 155 ? 2.7470 2.0420 2.6041 -0.0046 -0.2970 0.4535  155 LYS H NZ  
10918 N N   . ASP G 156 ? 2.1933 1.5537 1.9670 -0.0063 -0.3914 0.3360  156 ASP H N   
10919 C CA  . ASP G 156 ? 2.1970 1.5290 1.9625 -0.0313 -0.3858 0.3247  156 ASP H CA  
10920 C C   . ASP G 156 ? 2.2195 1.5902 1.9808 -0.0447 -0.3984 0.3126  156 ASP H C   
10921 O O   . ASP G 156 ? 2.2238 1.6189 1.9928 -0.0628 -0.3892 0.3118  156 ASP H O   
10922 C CB  . ASP G 156 ? 2.2366 1.5371 2.0137 -0.0569 -0.3529 0.3324  156 ASP H CB  
10923 C CG  . ASP G 156 ? 2.3456 1.6034 2.1317 -0.0484 -0.3375 0.3515  156 ASP H CG  
10924 O OD1 . ASP G 156 ? 2.3538 1.5612 2.1279 -0.0470 -0.3417 0.3495  156 ASP H OD1 
10925 O OD2 . ASP G 156 ? 2.4074 1.6822 2.2149 -0.0429 -0.3207 0.3705  156 ASP H OD2 
10926 N N   . TYR G 157 ? 2.1404 1.5188 1.8927 -0.0349 -0.4174 0.3048  157 TYR H N   
10927 C CA  . TYR G 157 ? 2.1236 1.5460 1.8763 -0.0467 -0.4305 0.3003  157 TYR H CA  
10928 C C   . TYR G 157 ? 2.1632 1.5741 1.9059 -0.0439 -0.4419 0.2910  157 TYR H C   
10929 O O   . TYR G 157 ? 2.1530 1.5217 1.8896 -0.0235 -0.4419 0.2862  157 TYR H O   
10930 C CB  . TYR G 157 ? 2.1067 1.5842 1.8766 -0.0296 -0.4393 0.3109  157 TYR H CB  
10931 C CG  . TYR G 157 ? 2.0802 1.5690 1.8574 0.0030  -0.4445 0.3139  157 TYR H CG  
10932 C CD1 . TYR G 157 ? 2.0831 1.6008 1.8689 0.0127  -0.4517 0.3135  157 TYR H CD1 
10933 C CD2 . TYR G 157 ? 2.0714 1.5509 1.8507 0.0222  -0.4380 0.3182  157 TYR H CD2 
10934 C CE1 . TYR G 157 ? 2.0530 1.5843 1.8510 0.0425  -0.4467 0.3143  157 TYR H CE1 
10935 C CE2 . TYR G 157 ? 2.0525 1.5455 1.8377 0.0471  -0.4361 0.3179  157 TYR H CE2 
10936 C CZ  . TYR G 157 ? 2.0948 1.6125 1.8908 0.0580  -0.4377 0.3148  157 TYR H CZ  
10937 O OH  . TYR G 157 ? 2.0516 1.5860 1.8590 0.0824  -0.4265 0.3126  157 TYR H OH  
10938 N N   . PHE G 158 ? 2.1171 1.5674 1.8596 -0.0637 -0.4512 0.2896  158 PHE H N   
10939 C CA  . PHE G 158 ? 2.1083 1.5616 1.8455 -0.0625 -0.4624 0.2830  158 PHE H CA  
10940 C C   . PHE G 158 ? 2.1727 1.7038 1.9232 -0.0770 -0.4742 0.2940  158 PHE H C   
10941 O O   . PHE G 158 ? 2.1961 1.7531 1.9445 -0.1080 -0.4723 0.2981  158 PHE H O   
10942 C CB  . PHE G 158 ? 2.1545 1.5434 1.8673 -0.0915 -0.4544 0.2684  158 PHE H CB  
10943 C CG  . PHE G 158 ? 2.1584 1.5257 1.8639 -0.0800 -0.4645 0.2585  158 PHE H CG  
10944 C CD1 . PHE G 158 ? 2.2012 1.6023 1.9002 -0.1070 -0.4740 0.2557  158 PHE H CD1 
10945 C CD2 . PHE G 158 ? 2.1619 1.4768 1.8676 -0.0417 -0.4639 0.2520  158 PHE H CD2 
10946 C CE1 . PHE G 158 ? 2.2007 1.5817 1.8952 -0.0940 -0.4824 0.2462  158 PHE H CE1 
10947 C CE2 . PHE G 158 ? 2.1853 1.4753 1.8867 -0.0261 -0.4713 0.2401  158 PHE H CE2 
10948 C CZ  . PHE G 158 ? 2.1690 1.4916 1.8658 -0.0511 -0.4803 0.2372  158 PHE H CZ  
10949 N N   . PRO G 159 ? 2.1061 1.6814 1.8756 -0.0549 -0.4831 0.3021  159 PRO H N   
10950 C CA  . PRO G 159 ? 2.0755 1.6320 1.8534 -0.0148 -0.4815 0.2952  159 PRO H CA  
10951 C C   . PRO G 159 ? 2.0846 1.6434 1.8806 0.0232  -0.4706 0.2999  159 PRO H C   
10952 O O   . PRO G 159 ? 2.0949 1.6066 1.8763 0.0263  -0.4653 0.2936  159 PRO H O   
10953 C CB  . PRO G 159 ? 2.0833 1.7039 1.8811 -0.0149 -0.4891 0.3055  159 PRO H CB  
10954 C CG  . PRO G 159 ? 2.1459 1.8388 1.9607 -0.0405 -0.4933 0.3294  159 PRO H CG  
10955 C CD  . PRO G 159 ? 2.1235 1.7803 1.9125 -0.0719 -0.4921 0.3215  159 PRO H CD  
10956 N N   . GLU G 160 ? 1.9944 1.6083 1.8235 0.0492  -0.4628 0.3120  160 GLU H N   
10957 C CA  . GLU G 160 ? 1.9690 1.5821 1.8124 0.0792  -0.4460 0.3126  160 GLU H CA  
10958 C C   . GLU G 160 ? 2.0179 1.6871 1.8919 0.0762  -0.4336 0.3369  160 GLU H C   
10959 O O   . GLU G 160 ? 2.0203 1.6693 1.8881 0.0801  -0.4253 0.3357  160 GLU H O   
10960 C CB  . GLU G 160 ? 1.9512 1.5603 1.8082 0.1179  -0.4332 0.2995  160 GLU H CB  
10961 C CG  . GLU G 160 ? 2.0659 1.6715 1.9329 0.1461  -0.4107 0.2939  160 GLU H CG  
10962 C CD  . GLU G 160 ? 2.3708 1.9154 2.2051 0.1460  -0.4146 0.2812  160 GLU H CD  
10963 O OE1 . GLU G 160 ? 2.2649 1.8102 2.0912 0.1259  -0.4174 0.2920  160 GLU H OE1 
10964 O OE2 . GLU G 160 ? 2.3250 1.8245 2.1459 0.1684  -0.4128 0.2624  160 GLU H OE2 
10965 N N   . PRO G 161 ? 1.9680 1.7038 1.8764 0.0688  -0.4298 0.3615  161 PRO H N   
10966 C CA  . PRO G 161 ? 1.9576 1.7315 1.8984 0.0667  -0.4122 0.3872  161 PRO H CA  
10967 C C   . PRO G 161 ? 2.0548 1.8028 1.9779 0.0452  -0.4203 0.3909  161 PRO H C   
10968 O O   . PRO G 161 ? 2.0782 1.8315 1.9909 0.0194  -0.4377 0.3964  161 PRO H O   
10969 C CB  . PRO G 161 ? 1.9607 1.8084 1.9423 0.0580  -0.4095 0.4182  161 PRO H CB  
10970 C CG  . PRO G 161 ? 2.0342 1.8821 1.9921 0.0431  -0.4349 0.4070  161 PRO H CG  
10971 C CD  . PRO G 161 ? 1.9808 1.7623 1.9049 0.0621  -0.4380 0.3713  161 PRO H CD  
10972 N N   . VAL G 162 ? 2.0103 1.7326 1.9311 0.0562  -0.4046 0.3865  162 VAL H N   
10973 C CA  . VAL G 162 ? 2.0242 1.7202 1.9328 0.0433  -0.4066 0.3893  162 VAL H CA  
10974 C C   . VAL G 162 ? 2.0507 1.7572 1.9851 0.0500  -0.3783 0.4034  162 VAL H C   
10975 O O   . VAL G 162 ? 2.0234 1.7216 1.9555 0.0655  -0.3597 0.3916  162 VAL H O   
10976 C CB  . VAL G 162 ? 2.0942 1.7372 1.9636 0.0437  -0.4181 0.3659  162 VAL H CB  
10977 C CG1 . VAL G 162 ? 2.1019 1.7244 1.9656 0.0401  -0.4119 0.3689  162 VAL H CG1 
10978 C CG2 . VAL G 162 ? 2.1175 1.7462 1.9670 0.0249  -0.4371 0.3576  162 VAL H CG2 
10979 N N   . THR G 163 ? 2.0171 1.7394 1.9764 0.0357  -0.3720 0.4288  163 THR H N   
10980 C CA  . THR G 163 ? 2.0054 1.7295 1.9922 0.0346  -0.3400 0.4461  163 THR H CA  
10981 C C   . THR G 163 ? 2.0982 1.7765 2.0614 0.0256  -0.3447 0.4392  163 THR H C   
10982 O O   . THR G 163 ? 2.1144 1.7778 2.0684 0.0157  -0.3653 0.4418  163 THR H O   
10983 C CB  . THR G 163 ? 2.0677 1.8342 2.1052 0.0250  -0.3237 0.4849  163 THR H CB  
10984 O OG1 . THR G 163 ? 2.0341 1.8498 2.0893 0.0313  -0.3301 0.4921  163 THR H OG1 
10985 C CG2 . THR G 163 ? 2.0199 1.7923 2.0966 0.0240  -0.2761 0.5050  163 THR H CG2 
10986 N N   . VAL G 164 ? 2.0687 1.7281 2.0225 0.0288  -0.3238 0.4291  164 VAL H N   
10987 C CA  . VAL G 164 ? 2.0970 1.7179 2.0290 0.0204  -0.3258 0.4231  164 VAL H CA  
10988 C C   . VAL G 164 ? 2.1773 1.7894 2.1344 0.0066  -0.2905 0.4417  164 VAL H C   
10989 O O   . VAL G 164 ? 2.1522 1.7826 2.1275 0.0057  -0.2557 0.4444  164 VAL H O   
10990 C CB  . VAL G 164 ? 2.1530 1.7582 2.0472 0.0285  -0.3339 0.3978  164 VAL H CB  
10991 C CG1 . VAL G 164 ? 2.1699 1.7453 2.0449 0.0200  -0.3386 0.3957  164 VAL H CG1 
10992 C CG2 . VAL G 164 ? 2.1555 1.7606 2.0306 0.0394  -0.3609 0.3834  164 VAL H CG2 
10993 N N   . SER G 165 ? 2.1826 1.7632 2.1429 -0.0047 -0.2950 0.4536  165 SER H N   
10994 C CA  . SER G 165 ? 2.1975 1.7527 2.1804 -0.0220 -0.2619 0.4730  165 SER H CA  
10995 C C   . SER G 165 ? 2.2959 1.8028 2.2543 -0.0281 -0.2729 0.4649  165 SER H C   
10996 O O   . SER G 165 ? 2.2967 1.7926 2.2399 -0.0184 -0.3045 0.4565  165 SER H O   
10997 C CB  . SER G 165 ? 2.2471 1.8109 2.2763 -0.0291 -0.2513 0.5080  165 SER H CB  
10998 O OG  . SER G 165 ? 2.4051 1.9545 2.4290 -0.0263 -0.2854 0.5116  165 SER H OG  
10999 N N   . TRP G 166 ? 2.2861 1.7656 2.2427 -0.0456 -0.2428 0.4670  166 TRP H N   
11000 C CA  . TRP G 166 ? 2.3190 1.7530 2.2542 -0.0520 -0.2505 0.4605  166 TRP H CA  
11001 C C   . TRP G 166 ? 2.3731 1.7576 2.3371 -0.0645 -0.2349 0.4848  166 TRP H C   
11002 O O   . TRP G 166 ? 2.3531 1.7303 2.3492 -0.0826 -0.1968 0.5072  166 TRP H O   
11003 C CB  . TRP G 166 ? 2.3213 1.7544 2.2284 -0.0675 -0.2311 0.4453  166 TRP H CB  
11004 C CG  . TRP G 166 ? 2.3388 1.8140 2.2171 -0.0552 -0.2469 0.4238  166 TRP H CG  
11005 C CD1 . TRP G 166 ? 2.3611 1.8735 2.2422 -0.0521 -0.2315 0.4167  166 TRP H CD1 
11006 C CD2 . TRP G 166 ? 2.3513 1.8330 2.1984 -0.0438 -0.2771 0.4095  166 TRP H CD2 
11007 N NE1 . TRP G 166 ? 2.3606 1.8950 2.2107 -0.0398 -0.2535 0.3980  166 TRP H NE1 
11008 C CE2 . TRP G 166 ? 2.3965 1.9147 2.2272 -0.0361 -0.2807 0.3963  166 TRP H CE2 
11009 C CE3 . TRP G 166 ? 2.3835 1.8446 2.2203 -0.0374 -0.2980 0.4087  166 TRP H CE3 
11010 C CZ2 . TRP G 166 ? 2.3965 1.9289 2.2017 -0.0257 -0.3046 0.3870  166 TRP H CZ2 
11011 C CZ3 . TRP G 166 ? 2.4085 1.8922 2.2238 -0.0262 -0.3182 0.3998  166 TRP H CZ3 
11012 C CH2 . TRP G 166 ? 2.4111 1.9289 2.2111 -0.0222 -0.3215 0.3914  166 TRP H CH2 
11013 N N   . ASN G 167 ? 2.3581 2.3411 2.5560 -0.0385 0.1072  0.1993  167 ASN H N   
11014 C CA  . ASN G 167 ? 2.3838 2.4360 2.6480 -0.0468 0.1606  0.1982  167 ASN H CA  
11015 C C   . ASN G 167 ? 2.3731 2.4854 2.7919 -0.0157 0.1596  0.2035  167 ASN H C   
11016 O O   . ASN G 167 ? 2.3928 2.5520 2.8924 0.0023  0.2119  0.1795  167 ASN H O   
11017 C CB  . ASN G 167 ? 2.5041 2.5415 2.7053 -0.0542 0.2299  0.1611  167 ASN H CB  
11018 C CG  . ASN G 167 ? 2.9047 2.8655 2.9492 -0.0964 0.2223  0.1606  167 ASN H CG  
11019 O OD1 . ASN G 167 ? 2.8461 2.8107 2.8436 -0.1401 0.2080  0.1834  167 ASN H OD1 
11020 N ND2 . ASN G 167 ? 2.8682 2.7488 2.8264 -0.0873 0.2229  0.1369  167 ASN H ND2 
11021 N N   . SER G 168 ? 2.2557 2.3571 2.7135 -0.0113 0.0969  0.2340  168 SER H N   
11022 C CA  . SER G 168 ? 2.2021 2.3292 2.7908 0.0079  0.0703  0.2484  168 SER H CA  
11023 C C   . SER G 168 ? 2.2413 2.3605 2.8917 0.0443  0.0762  0.2107  168 SER H C   
11024 O O   . SER G 168 ? 2.2159 2.3604 2.9927 0.0594  0.0624  0.2131  168 SER H O   
11025 C CB  . SER G 168 ? 2.2428 2.4398 2.9344 -0.0047 0.0910  0.2750  168 SER H CB  
11026 O OG  . SER G 168 ? 2.3346 2.5301 2.9660 -0.0393 0.0661  0.3163  168 SER H OG  
11027 N N   . GLY G 169 ? 2.2146 2.2892 2.7735 0.0557  0.0854  0.1797  169 GLY H N   
11028 C CA  . GLY G 169 ? 2.2189 2.2738 2.8069 0.0891  0.0826  0.1440  169 GLY H CA  
11029 C C   . GLY G 169 ? 2.3158 2.3902 2.9049 0.1081  0.1518  0.1027  169 GLY H C   
11030 O O   . GLY G 169 ? 2.3209 2.4210 3.0111 0.1389  0.1642  0.0749  169 GLY H O   
11031 N N   . ALA G 170 ? 2.3116 2.3651 2.7845 0.0875  0.1947  0.0965  170 ALA H N   
11032 C CA  . ALA G 170 ? 2.3899 2.4418 2.8269 0.0967  0.2677  0.0570  170 ALA H CA  
11033 C C   . ALA G 170 ? 2.4772 2.4323 2.7608 0.0968  0.2594  0.0410  170 ALA H C   
11034 O O   . ALA G 170 ? 2.5261 2.4500 2.7957 0.1278  0.2787  0.0059  170 ALA H O   
11035 C CB  . ALA G 170 ? 2.4395 2.5370 2.8618 0.0607  0.3273  0.0652  170 ALA H CB  
11036 N N   . LEU G 171 ? 2.4092 2.3113 2.5824 0.0632  0.2246  0.0682  171 LEU H N   
11037 C CA  . LEU G 171 ? 2.4497 2.2515 2.4831 0.0561  0.2037  0.0643  171 LEU H CA  
11038 C C   . LEU G 171 ? 2.4269 2.2014 2.4795 0.0837  0.1386  0.0705  171 LEU H C   
11039 O O   . LEU G 171 ? 2.3431 2.1364 2.4332 0.0767  0.0894  0.0971  171 LEU H O   
11040 C CB  . LEU G 171 ? 2.4615 2.2222 2.3947 0.0071  0.1854  0.0908  171 LEU H CB  
11041 C CG  . LEU G 171 ? 2.5683 2.2186 2.3699 -0.0083 0.1492  0.0964  171 LEU H CG  
11042 C CD1 . LEU G 171 ? 2.6988 2.2683 2.3889 -0.0155 0.1948  0.0702  171 LEU H CD1 
11043 C CD2 . LEU G 171 ? 2.5848 2.2103 2.3329 -0.0526 0.1132  0.1239  171 LEU H CD2 
11044 N N   . THR G 172 ? 2.4181 2.1459 2.4403 0.1136  0.1389  0.0451  172 THR H N   
11045 C CA  . THR G 172 ? 2.3709 2.0700 2.4034 0.1379  0.0756  0.0485  172 THR H CA  
11046 C C   . THR G 172 ? 2.4619 2.0572 2.3602 0.1361  0.0493  0.0526  172 THR H C   
11047 O O   . THR G 172 ? 2.4158 1.9837 2.2993 0.1377  -0.0118 0.0721  172 THR H O   
11048 C CB  . THR G 172 ? 2.4662 2.2056 2.6060 0.1779  0.0771  0.0188  172 THR H CB  
11049 O OG1 . THR G 172 ? 2.5494 2.2805 2.6718 0.1967  0.1431  -0.0186 172 THR H OG1 
11050 C CG2 . THR G 172 ? 2.3706 2.1963 2.6565 0.1765  0.0696  0.0280  172 THR H CG2 
11051 N N   . SER G 173 ? 2.5112 2.0429 2.3088 0.1291  0.0945  0.0363  173 SER H N   
11052 C CA  . SER G 173 ? 2.5865 1.9977 2.2442 0.1239  0.0688  0.0438  173 SER H CA  
11053 C C   . SER G 173 ? 2.6103 1.9711 2.1978 0.0814  0.0323  0.0808  173 SER H C   
11054 O O   . SER G 173 ? 2.6047 1.9876 2.1890 0.0472  0.0567  0.0876  173 SER H O   
11055 C CB  . SER G 173 ? 2.7677 2.1123 2.3307 0.1259  0.1319  0.0126  173 SER H CB  
11056 O OG  . SER G 173 ? 2.9055 2.3068 2.5529 0.1686  0.1720  -0.0277 173 SER H OG  
11057 N N   . GLY G 174 ? 2.5451 1.8405 2.0849 0.0835  -0.0306 0.1049  174 GLY H N   
11058 C CA  . GLY G 174 ? 2.5227 1.7637 2.0118 0.0485  -0.0744 0.1395  174 GLY H CA  
11059 C C   . GLY G 174 ? 2.4287 1.7551 2.0105 0.0340  -0.0920 0.1561  174 GLY H C   
11060 O O   . GLY G 174 ? 2.4066 1.6977 1.9602 0.0038  -0.1192 0.1777  174 GLY H O   
11061 N N   . VAL G 175 ? 2.2972 1.7264 1.9889 0.0549  -0.0815 0.1460  175 VAL H N   
11062 C CA  . VAL G 175 ? 2.1991 1.7039 1.9737 0.0446  -0.0956 0.1599  175 VAL H CA  
11063 C C   . VAL G 175 ? 2.1930 1.6962 1.9895 0.0491  -0.1498 0.1795  175 VAL H C   
11064 O O   . VAL G 175 ? 2.1854 1.6922 1.9997 0.0702  -0.1719 0.1757  175 VAL H O   
11065 C CB  . VAL G 175 ? 2.2017 1.7966 2.0745 0.0595  -0.0644 0.1447  175 VAL H CB  
11066 C CG1 . VAL G 175 ? 2.1088 1.7623 2.0573 0.0531  -0.0904 0.1618  175 VAL H CG1 
11067 C CG2 . VAL G 175 ? 2.2451 1.8578 2.1075 0.0457  -0.0080 0.1319  175 VAL H CG2 
11068 N N   . HIS G 176 ? 2.1050 1.6032 1.9017 0.0272  -0.1722 0.1988  176 HIS H N   
11069 C CA  . HIS G 176 ? 2.0459 1.5513 1.8707 0.0265  -0.2136 0.2166  176 HIS H CA  
11070 C C   . HIS G 176 ? 1.9924 1.5637 1.8847 0.0180  -0.2112 0.2196  176 HIS H C   
11071 O O   . HIS G 176 ? 1.9764 1.5444 1.8661 0.0013  -0.2095 0.2240  176 HIS H O   
11072 C CB  . HIS G 176 ? 2.0992 1.5269 1.8688 0.0109  -0.2460 0.2366  176 HIS H CB  
11073 C CG  . HIS G 176 ? 2.2044 1.5586 1.9090 0.0210  -0.2703 0.2454  176 HIS H CG  
11074 N ND1 . HIS G 176 ? 2.3226 1.5886 1.9348 0.0158  -0.2600 0.2418  176 HIS H ND1 
11075 C CD2 . HIS G 176 ? 2.2153 1.5639 1.9249 0.0321  -0.3081 0.2600  176 HIS H CD2 
11076 C CE1 . HIS G 176 ? 2.3579 1.5633 1.9210 0.0286  -0.2934 0.2548  176 HIS H CE1 
11077 N NE2 . HIS G 176 ? 2.2969 1.5529 1.9187 0.0385  -0.3263 0.2676  176 HIS H NE2 
11078 N N   . THR G 177 ? 1.8923 1.5119 1.8365 0.0267  -0.2164 0.2170  177 THR H N   
11079 C CA  . THR G 177 ? 1.8390 1.5042 1.8316 0.0175  -0.2154 0.2207  177 THR H CA  
11080 C C   . THR G 177 ? 1.8606 1.5282 1.8640 0.0114  -0.2405 0.2297  177 THR H C   
11081 O O   . THR G 177 ? 1.8465 1.5187 1.8551 0.0126  -0.2577 0.2296  177 THR H O   
11082 C CB  . THR G 177 ? 1.9605 1.6632 1.9959 0.0221  -0.2015 0.2137  177 THR H CB  
11083 O OG1 . THR G 177 ? 1.9992 1.7057 2.0302 0.0274  -0.1729 0.2057  177 THR H OG1 
11084 C CG2 . THR G 177 ? 1.9178 1.6460 1.9828 0.0097  -0.2023 0.2219  177 THR H CG2 
11085 N N   . PHE G 178 ? 1.8157 1.4788 1.8245 0.0025  -0.2450 0.2366  178 PHE H N   
11086 C CA  . PHE G 178 ? 1.8006 1.4733 1.8316 -0.0045 -0.2601 0.2443  178 PHE H CA  
11087 C C   . PHE G 178 ? 1.8290 1.5407 1.8884 -0.0131 -0.2499 0.2389  178 PHE H C   
11088 O O   . PHE G 178 ? 1.8237 1.5485 1.8915 -0.0143 -0.2342 0.2327  178 PHE H O   
11089 C CB  . PHE G 178 ? 1.8307 1.4859 1.8762 -0.0094 -0.2678 0.2494  178 PHE H CB  
11090 C CG  . PHE G 178 ? 1.8941 1.4864 1.8999 -0.0111 -0.2895 0.2610  178 PHE H CG  
11091 C CD1 . PHE G 178 ? 1.9467 1.5101 1.9484 -0.0125 -0.3176 0.2794  178 PHE H CD1 
11092 C CD2 . PHE G 178 ? 1.9584 1.5111 1.9217 -0.0162 -0.2846 0.2565  178 PHE H CD2 
11093 C CE1 . PHE G 178 ? 2.0126 1.4962 1.9636 -0.0172 -0.3438 0.2950  178 PHE H CE1 
11094 C CE2 . PHE G 178 ? 2.0537 1.5272 1.9606 -0.0248 -0.3053 0.2675  178 PHE H CE2 
11095 C CZ  . PHE G 178 ? 2.0470 1.4803 1.9457 -0.0243 -0.3365 0.2876  178 PHE H CZ  
11096 N N   . PRO G 179 ? 1.7729 1.4961 1.8391 -0.0241 -0.2607 0.2436  179 PRO H N   
11097 C CA  . PRO G 179 ? 1.7584 1.5038 1.8336 -0.0413 -0.2484 0.2370  179 PRO H CA  
11098 C C   . PRO G 179 ? 1.8028 1.5645 1.9042 -0.0413 -0.2236 0.2290  179 PRO H C   
11099 O O   . PRO G 179 ? 1.7859 1.5505 1.9149 -0.0317 -0.2237 0.2293  179 PRO H O   
11100 C CB  . PRO G 179 ? 1.7886 1.5403 1.8571 -0.0588 -0.2667 0.2450  179 PRO H CB  
11101 C CG  . PRO G 179 ? 1.8573 1.5847 1.9072 -0.0459 -0.2971 0.2576  179 PRO H CG  
11102 C CD  . PRO G 179 ? 1.8046 1.5141 1.8608 -0.0264 -0.2874 0.2578  179 PRO H CD  
11103 N N   . ALA G 180 ? 1.7832 1.5447 1.8733 -0.0528 -0.2083 0.2217  180 ALA H N   
11104 C CA  . ALA G 180 ? 1.7931 1.5608 1.8963 -0.0505 -0.1859 0.2112  180 ALA H CA  
11105 C C   . ALA G 180 ? 1.8550 1.6469 1.9829 -0.0607 -0.1654 0.2018  180 ALA H C   
11106 O O   . ALA G 180 ? 1.8665 1.6666 1.9842 -0.0810 -0.1672 0.2059  180 ALA H O   
11107 C CB  . ALA G 180 ? 1.8208 1.5618 1.8883 -0.0607 -0.1810 0.2115  180 ALA H CB  
11108 N N   . VAL G 181 ? 1.7970 1.6018 1.9606 -0.0477 -0.1477 0.1879  181 VAL H N   
11109 C CA  . VAL G 181 ? 1.7980 1.6341 2.0037 -0.0525 -0.1181 0.1727  181 VAL H CA  
11110 C C   . VAL G 181 ? 1.8442 1.6688 2.0379 -0.0478 -0.0893 0.1513  181 VAL H C   
11111 O O   . VAL G 181 ? 1.8264 1.6310 2.0162 -0.0291 -0.1040 0.1487  181 VAL H O   
11112 C CB  . VAL G 181 ? 1.8273 1.6929 2.1148 -0.0380 -0.1288 0.1749  181 VAL H CB  
11113 C CG1 . VAL G 181 ? 1.8138 1.6880 2.1024 -0.0514 -0.1491 0.1975  181 VAL H CG1 
11114 C CG2 . VAL G 181 ? 1.8114 1.6537 2.1189 -0.0167 -0.1598 0.1768  181 VAL H CG2 
11115 N N   . LEU G 182 ? 1.8292 1.6591 2.0054 -0.0681 -0.0503 0.1366  182 LEU H N   
11116 C CA  . LEU G 182 ? 1.8732 1.6797 2.0233 -0.0644 -0.0181 0.1138  182 LEU H CA  
11117 C C   . LEU G 182 ? 1.9148 1.7597 2.1560 -0.0323 -0.0046 0.0896  182 LEU H C   
11118 O O   . LEU G 182 ? 1.9047 1.8022 2.2257 -0.0311 0.0129  0.0818  182 LEU H O   
11119 C CB  . LEU G 182 ? 1.9385 1.7273 2.0284 -0.1029 0.0237  0.1031  182 LEU H CB  
11120 C CG  . LEU G 182 ? 2.0759 1.8154 2.1076 -0.1046 0.0591  0.0806  182 LEU H CG  
11121 C CD1 . LEU G 182 ? 2.1378 1.7923 2.0481 -0.1465 0.0522  0.0949  182 LEU H CD1 
11122 C CD2 . LEU G 182 ? 2.1590 1.9411 2.2352 -0.1057 0.1218  0.0463  182 LEU H CD2 
11123 N N   . GLN G 183 ? 1.8702 1.6866 2.1044 -0.0076 -0.0202 0.0798  183 GLN H N   
11124 C CA  . GLN G 183 ? 1.8638 1.7041 2.1839 0.0239  -0.0213 0.0535  183 GLN H CA  
11125 C C   . GLN G 183 ? 1.9705 1.8245 2.3078 0.0278  0.0387  0.0165  183 GLN H C   
11126 O O   . GLN G 183 ? 2.0101 1.8398 2.2683 0.0013  0.0798  0.0135  183 GLN H O   
11127 C CB  . GLN G 183 ? 1.8765 1.6746 2.1695 0.0440  -0.0695 0.0570  183 GLN H CB  
11128 C CG  . GLN G 183 ? 2.0083 1.8021 2.3088 0.0425  -0.1238 0.0843  183 GLN H CG  
11129 C CD  . GLN G 183 ? 2.2178 1.9722 2.4828 0.0537  -0.1700 0.0886  183 GLN H CD  
11130 O OE1 . GLN G 183 ? 2.1598 1.9121 2.4761 0.0712  -0.1992 0.0702  183 GLN H OE1 
11131 N NE2 . GLN G 183 ? 2.0954 1.8167 2.2763 0.0413  -0.1829 0.1141  183 GLN H NE2 
11132 N N   . SER G 184 ? 1.9353 1.8212 2.3755 0.0586  0.0422  -0.0137 184 SER H N   
11133 C CA  . SER G 184 ? 1.9936 1.8997 2.4721 0.0713  0.1033  -0.0574 184 SER H CA  
11134 C C   . SER G 184 ? 2.1220 1.9521 2.4754 0.0725  0.1188  -0.0696 184 SER H C   
11135 O O   . SER G 184 ? 2.1919 2.0105 2.5030 0.0612  0.1840  -0.0954 184 SER H O   
11136 C CB  . SER G 184 ? 2.0149 1.9619 2.6406 0.1092  0.0853  -0.0866 184 SER H CB  
11137 O OG  . SER G 184 ? 2.0382 2.0322 2.7697 0.1049  0.0555  -0.0663 184 SER H OG  
11138 N N   . SER G 185 ? 2.0683 1.8396 2.3525 0.0806  0.0575  -0.0468 185 SER H N   
11139 C CA  . SER G 185 ? 2.1332 1.8174 2.2906 0.0803  0.0504  -0.0434 185 SER H CA  
11140 C C   . SER G 185 ? 2.2322 1.8631 2.2662 0.0360  0.0802  -0.0208 185 SER H C   
11141 O O   . SER G 185 ? 2.3140 1.8628 2.2388 0.0273  0.0954  -0.0244 185 SER H O   
11142 C CB  . SER G 185 ? 2.1386 1.7869 2.2675 0.0929  -0.0299 -0.0147 185 SER H CB  
11143 O OG  . SER G 185 ? 2.1699 1.8349 2.2959 0.0714  -0.0613 0.0245  185 SER H OG  
11144 N N   . GLY G 186 ? 2.1403 1.8066 2.1886 0.0067  0.0805  0.0028  186 GLY H N   
11145 C CA  . GLY G 186 ? 2.1733 1.7913 2.1203 -0.0409 0.0937  0.0250  186 GLY H CA  
11146 C C   . GLY G 186 ? 2.1803 1.7585 2.0771 -0.0533 0.0336  0.0690  186 GLY H C   
11147 O O   . GLY G 186 ? 2.2016 1.7222 2.0140 -0.0923 0.0295  0.0896  186 GLY H O   
11148 N N   . LEU G 187 ? 2.0791 1.6852 2.0308 -0.0237 -0.0145 0.0827  187 LEU H N   
11149 C CA  . LEU G 187 ? 2.0415 1.6253 1.9650 -0.0301 -0.0659 0.1209  187 LEU H CA  
11150 C C   . LEU G 187 ? 2.0372 1.6850 2.0316 -0.0295 -0.0812 0.1315  187 LEU H C   
11151 O O   . LEU G 187 ? 1.9973 1.6979 2.0722 -0.0092 -0.0820 0.1170  187 LEU H O   
11152 C CB  . LEU G 187 ? 2.0384 1.5961 1.9508 -0.0040 -0.1092 0.1301  187 LEU H CB  
11153 C CG  . LEU G 187 ? 2.1775 1.6480 1.9946 -0.0056 -0.1139 0.1344  187 LEU H CG  
11154 C CD1 . LEU G 187 ? 2.1997 1.6692 2.0374 0.0304  -0.1268 0.1092  187 LEU H CD1 
11155 C CD2 . LEU G 187 ? 2.2086 1.6220 1.9620 -0.0220 -0.1598 0.1802  187 LEU H CD2 
11156 N N   . TYR G 188 ? 1.9954 1.6291 1.9596 -0.0520 -0.0982 0.1570  188 TYR H N   
11157 C CA  . TYR G 188 ? 1.9470 1.6259 1.9594 -0.0513 -0.1149 0.1683  188 TYR H CA  
11158 C C   . TYR G 188 ? 1.9994 1.6930 2.0425 -0.0281 -0.1483 0.1786  188 TYR H C   
11159 O O   . TYR G 188 ? 2.0092 1.6736 2.0237 -0.0207 -0.1677 0.1872  188 TYR H O   
11160 C CB  . TYR G 188 ? 1.9620 1.6139 1.9332 -0.0801 -0.1277 0.1878  188 TYR H CB  
11161 C CG  . TYR G 188 ? 2.0356 1.6599 1.9603 -0.1161 -0.1047 0.1799  188 TYR H CG  
11162 C CD1 . TYR G 188 ? 2.0517 1.7145 1.9995 -0.1321 -0.0939 0.1734  188 TYR H CD1 
11163 C CD2 . TYR G 188 ? 2.1152 1.6641 1.9613 -0.1405 -0.0991 0.1826  188 TYR H CD2 
11164 C CE1 . TYR G 188 ? 2.1184 1.7539 2.0135 -0.1747 -0.0756 0.1669  188 TYR H CE1 
11165 C CE2 . TYR G 188 ? 2.1917 1.7006 1.9778 -0.1842 -0.0790 0.1747  188 TYR H CE2 
11166 C CZ  . TYR G 188 ? 2.2692 1.8256 2.0804 -0.2031 -0.0666 0.1658  188 TYR H CZ  
11167 O OH  . TYR G 188 ? 2.3440 1.8599 2.0872 -0.2547 -0.0491 0.1584  188 TYR H OH  
11168 N N   . SER G 189 ? 1.9444 1.6748 2.0359 -0.0212 -0.1581 0.1799  189 SER H N   
11169 C CA  . SER G 189 ? 1.9261 1.6608 2.0345 -0.0093 -0.1876 0.1882  189 SER H CA  
11170 C C   . SER G 189 ? 1.9521 1.7019 2.0783 -0.0122 -0.1951 0.1969  189 SER H C   
11171 O O   . SER G 189 ? 1.9360 1.7038 2.0945 -0.0135 -0.1875 0.1918  189 SER H O   
11172 C CB  . SER G 189 ? 1.9880 1.7265 2.1349 0.0061  -0.2010 0.1716  189 SER H CB  
11173 O OG  . SER G 189 ? 2.1022 1.8325 2.2547 0.0068  -0.2353 0.1795  189 SER H OG  
11174 N N   . LEU G 190 ? 1.9048 1.6448 2.0084 -0.0135 -0.2097 0.2107  190 LEU H N   
11175 C CA  . LEU G 190 ? 1.8946 1.6351 1.9995 -0.0140 -0.2161 0.2170  190 LEU H CA  
11176 C C   . LEU G 190 ? 1.9621 1.6846 2.0533 -0.0140 -0.2332 0.2211  190 LEU H C   
11177 O O   . LEU G 190 ? 1.9627 1.6779 2.0455 -0.0161 -0.2454 0.2207  190 LEU H O   
11178 C CB  . LEU G 190 ? 1.8886 1.6304 1.9762 -0.0192 -0.2104 0.2243  190 LEU H CB  
11179 C CG  . LEU G 190 ? 1.9414 1.6782 2.0150 -0.0211 -0.2103 0.2330  190 LEU H CG  
11180 C CD1 . LEU G 190 ? 1.9431 1.6812 2.0131 -0.0150 -0.2104 0.2356  190 LEU H CD1 
11181 C CD2 . LEU G 190 ? 1.9705 1.6994 2.0405 -0.0325 -0.2116 0.2361  190 LEU H CD2 
11182 N N   . SER G 191 ? 1.9367 1.6437 2.0152 -0.0153 -0.2375 0.2255  191 SER H N   
11183 C CA  . SER G 191 ? 1.9668 1.6402 2.0131 -0.0233 -0.2499 0.2286  191 SER H CA  
11184 C C   . SER G 191 ? 2.0498 1.7174 2.0654 -0.0207 -0.2340 0.2315  191 SER H C   
11185 O O   . SER G 191 ? 2.0346 1.7139 2.0594 -0.0116 -0.2278 0.2317  191 SER H O   
11186 C CB  . SER G 191 ? 2.0203 1.6559 2.0755 -0.0292 -0.2756 0.2301  191 SER H CB  
11187 O OG  . SER G 191 ? 2.0707 1.7210 2.1612 -0.0213 -0.2743 0.2329  191 SER H OG  
11188 N N   . SER G 192 ? 2.0524 1.7015 2.0308 -0.0304 -0.2280 0.2314  192 SER H N   
11189 C CA  . SER G 192 ? 2.0825 1.7265 2.0350 -0.0257 -0.2049 0.2280  192 SER H CA  
11190 C C   . SER G 192 ? 2.2189 1.8090 2.1077 -0.0452 -0.2039 0.2263  192 SER H C   
11191 O O   . SER G 192 ? 2.2348 1.8212 2.1041 -0.0660 -0.2074 0.2277  192 SER H O   
11192 C CB  . SER G 192 ? 2.0916 1.7847 2.0758 -0.0191 -0.1823 0.2277  192 SER H CB  
11193 O OG  . SER G 192 ? 2.1832 1.8840 2.1763 -0.0045 -0.1638 0.2197  192 SER H OG  
11194 N N   . VAL G 193 ? 2.2265 1.7634 2.0711 -0.0433 -0.2051 0.2252  193 VAL H N   
11195 C CA  . VAL G 193 ? 2.3063 1.7651 2.0678 -0.0678 -0.2056 0.2242  193 VAL H CA  
11196 C C   . VAL G 193 ? 2.4304 1.8706 2.1464 -0.0572 -0.1678 0.2120  193 VAL H C   
11197 O O   . VAL G 193 ? 2.3938 1.8770 2.1511 -0.0274 -0.1529 0.2050  193 VAL H O   
11198 C CB  . VAL G 193 ? 2.3819 1.7578 2.1125 -0.0832 -0.2519 0.2378  193 VAL H CB  
11199 C CG1 . VAL G 193 ? 2.3367 1.7281 2.1197 -0.0941 -0.2872 0.2431  193 VAL H CG1 
11200 C CG2 . VAL G 193 ? 2.3706 1.7317 2.1100 -0.0600 -0.2646 0.2469  193 VAL H CG2 
11201 N N   . VAL G 194 ? 2.1429 2.4100 2.2064 -0.0793 0.0651  -0.1815 194 VAL H N   
11202 C CA  . VAL G 194 ? 2.1388 2.4143 2.2218 -0.0644 0.0593  -0.1776 194 VAL H CA  
11203 C C   . VAL G 194 ? 2.1857 2.4858 2.2791 -0.0285 0.0622  -0.1953 194 VAL H C   
11204 O O   . VAL G 194 ? 2.1791 2.4830 2.2580 -0.0112 0.0699  -0.1950 194 VAL H O   
11205 C CB  . VAL G 194 ? 2.1883 2.4564 2.2689 -0.0676 0.0539  -0.1531 194 VAL H CB  
11206 C CG1 . VAL G 194 ? 2.1867 2.4565 2.2575 -0.0608 0.0607  -0.1394 194 VAL H CG1 
11207 C CG2 . VAL G 194 ? 2.1777 2.4618 2.2720 -0.0502 0.0410  -0.1524 194 VAL H CG2 
11208 N N   . THR G 195 ? 2.1413 2.4553 2.2593 -0.0146 0.0551  -0.2123 195 THR H N   
11209 C CA  . THR G 195 ? 2.1263 2.4665 2.2629 0.0285  0.0553  -0.2338 195 THR H CA  
11210 C C   . THR G 195 ? 2.1738 2.5319 2.3177 0.0580  0.0479  -0.2142 195 THR H C   
11211 O O   . THR G 195 ? 2.1560 2.5286 2.3201 0.0694  0.0289  -0.2083 195 THR H O   
11212 C CB  . THR G 195 ? 2.2188 2.5687 2.3864 0.0336  0.0468  -0.2594 195 THR H CB  
11213 O OG1 . THR G 195 ? 2.2295 2.5649 2.3880 -0.0026 0.0552  -0.2706 195 THR H OG1 
11214 C CG2 . THR G 195 ? 2.1757 2.5535 2.3665 0.0844  0.0486  -0.2910 195 THR H CG2 
11215 N N   . VAL G 196 ? 2.1445 2.5018 2.2680 0.0687  0.0606  -0.2030 196 VAL H N   
11216 C CA  . VAL G 196 ? 2.1383 2.5157 2.2655 0.0938  0.0588  -0.1810 196 VAL H CA  
11217 C C   . VAL G 196 ? 2.1654 2.5698 2.3048 0.1510  0.0635  -0.1974 196 VAL H C   
11218 O O   . VAL G 196 ? 2.1652 2.5610 2.2936 0.1677  0.0760  -0.2257 196 VAL H O   
11219 C CB  . VAL G 196 ? 2.2106 2.5694 2.3120 0.0695  0.0699  -0.1541 196 VAL H CB  
11220 C CG1 . VAL G 196 ? 2.2150 2.5594 2.3150 0.0294  0.0608  -0.1361 196 VAL H CG1 
11221 C CG2 . VAL G 196 ? 2.2266 2.5588 2.2972 0.0617  0.0844  -0.1655 196 VAL H CG2 
11222 N N   . PRO G 197 ? 2.0977 2.5376 2.2574 0.1866  0.0528  -0.1830 197 PRO H N   
11223 C CA  . PRO G 197 ? 2.0784 2.5460 2.2520 0.2503  0.0577  -0.1986 197 PRO H CA  
11224 C C   . PRO G 197 ? 2.1391 2.5927 2.2796 0.2639  0.0833  -0.1892 197 PRO H C   
11225 O O   . PRO G 197 ? 2.1535 2.5913 2.2721 0.2298  0.0911  -0.1592 197 PRO H O   
11226 C CB  . PRO G 197 ? 2.0758 2.5914 2.2811 0.2830  0.0321  -0.1825 197 PRO H CB  
11227 C CG  . PRO G 197 ? 2.1450 2.6552 2.3352 0.2353  0.0241  -0.1509 197 PRO H CG  
11228 C CD  . PRO G 197 ? 2.1105 2.5710 2.2781 0.1759  0.0342  -0.1552 197 PRO H CD  
11229 N N   . SER G 198 ? 2.0871 2.5443 2.2232 0.3168  0.0957  -0.2173 198 SER H N   
11230 C CA  . SER G 198 ? 2.1106 2.5482 2.2070 0.3392  0.1199  -0.2139 198 SER H CA  
11231 C C   . SER G 198 ? 2.1724 2.6420 2.2794 0.3689  0.1226  -0.1768 198 SER H C   
11232 O O   . SER G 198 ? 2.1962 2.6469 2.2692 0.3818  0.1438  -0.1644 198 SER H O   
11233 C CB  . SER G 198 ? 2.1462 2.5757 2.2287 0.3930  0.1321  -0.2633 198 SER H CB  
11234 O OG  . SER G 198 ? 2.2361 2.6454 2.3099 0.3653  0.1292  -0.2993 198 SER H OG  
11235 N N   . SER G 199 ? 2.1095 2.6282 2.2595 0.3791  0.0993  -0.1591 199 SER H N   
11236 C CA  . SER G 199 ? 2.1022 2.6679 2.2673 0.4084  0.0954  -0.1246 199 SER H CA  
11237 C C   . SER G 199 ? 2.2009 2.7545 2.3430 0.3560  0.1069  -0.0828 199 SER H C   
11238 O O   . SER G 199 ? 2.2057 2.7839 2.3452 0.3797  0.1186  -0.0558 199 SER H O   
11239 C CB  . SER G 199 ? 2.0946 2.7182 2.3052 0.4338  0.0588  -0.1234 199 SER H CB  
11240 O OG  . SER G 199 ? 2.1501 2.7961 2.3921 0.4990  0.0474  -0.1580 199 SER H OG  
11241 N N   . SER G 200 ? 2.1852 2.7041 2.3144 0.2883  0.1038  -0.0776 200 SER H N   
11242 C CA  . SER G 200 ? 2.2138 2.7201 2.3280 0.2394  0.1131  -0.0435 200 SER H CA  
11243 C C   . SER G 200 ? 2.3109 2.7550 2.3960 0.1862  0.1230  -0.0491 200 SER H C   
11244 O O   . SER G 200 ? 2.3036 2.7363 2.3925 0.1393  0.1136  -0.0417 200 SER H O   
11245 C CB  . SER G 200 ? 2.2337 2.7829 2.3706 0.2209  0.0903  -0.0261 200 SER H CB  
11246 O OG  . SER G 200 ? 2.3498 2.8971 2.4783 0.1829  0.1014  0.0038  200 SER H OG  
11247 N N   . LEU G 201 ? 2.3104 2.7157 2.3628 0.1998  0.1396  -0.0650 201 LEU H N   
11248 C CA  . LEU G 201 ? 2.3449 2.6954 2.3628 0.1599  0.1439  -0.0725 201 LEU H CA  
11249 C C   . LEU G 201 ? 2.4546 2.7781 2.4487 0.1375  0.1572  -0.0414 201 LEU H C   
11250 O O   . LEU G 201 ? 2.4746 2.7996 2.4538 0.1680  0.1736  -0.0289 201 LEU H O   
11251 C CB  . LEU G 201 ? 2.3519 2.6751 2.3379 0.1850  0.1479  -0.1139 201 LEU H CB  
11252 C CG  . LEU G 201 ? 2.4018 2.7427 2.3855 0.2526  0.1576  -0.1405 201 LEU H CG  
11253 C CD1 . LEU G 201 ? 2.4369 2.7626 2.3872 0.2842  0.1786  -0.1250 201 LEU H CD1 
11254 C CD2 . LEU G 201 ? 2.4321 2.7527 2.3920 0.2671  0.1567  -0.1902 201 LEU H CD2 
11255 N N   . GLY G 202 ? 2.4310 2.7301 2.4244 0.0870  0.1498  -0.0287 202 GLY H N   
11256 C CA  . GLY G 202 ? 2.4703 2.7417 2.4496 0.0593  0.1576  0.0003  202 GLY H CA  
11257 C C   . GLY G 202 ? 2.5270 2.8351 2.5411 0.0449  0.1627  0.0338  202 GLY H C   
11258 O O   . GLY G 202 ? 2.5331 2.8297 2.5596 0.0048  0.1594  0.0509  202 GLY H O   
11259 N N   . THR G 203 ? 2.4714 2.8291 2.5029 0.0817  0.1688  0.0407  203 THR H N   
11260 C CA  . THR G 203 ? 2.4601 2.8702 2.5219 0.0779  0.1711  0.0692  203 THR H CA  
11261 C C   . THR G 203 ? 2.4866 2.9169 2.5749 0.0439  0.1519  0.0644  203 THR H C   
11262 O O   . THR G 203 ? 2.4877 2.9331 2.5912 0.0144  0.1541  0.0836  203 THR H O   
11263 C CB  . THR G 203 ? 2.5116 2.9767 2.5848 0.1357  0.1731  0.0706  203 THR H CB  
11264 O OG1 . THR G 203 ? 2.4502 2.9332 2.5358 0.1610  0.1530  0.0397  203 THR H OG1 
11265 C CG2 . THR G 203 ? 2.5188 2.9625 2.5625 0.1757  0.1963  0.0757  203 THR H CG2 
11266 N N   . GLN G 204 ? 2.4186 2.8455 2.5094 0.0485  0.1343  0.0360  204 GLN H N   
11267 C CA  . GLN G 204 ? 2.3970 2.8303 2.5016 0.0209  0.1162  0.0258  204 GLN H CA  
11268 C C   . GLN G 204 ? 2.4619 2.8410 2.5575 -0.0176 0.1170  0.0205  204 GLN H C   
11269 O O   . GLN G 204 ? 2.4668 2.8091 2.5434 -0.0149 0.1190  0.0080  204 GLN H O   
11270 C CB  . GLN G 204 ? 2.3837 2.8333 2.4929 0.0443  0.0969  0.0003  204 GLN H CB  
11271 C CG  . GLN G 204 ? 2.6118 3.0940 2.7307 0.0371  0.0751  -0.0045 204 GLN H CG  
11272 C CD  . GLN G 204 ? 2.9008 3.3484 3.0141 -0.0041 0.0709  -0.0129 204 GLN H CD  
11273 O OE1 . GLN G 204 ? 2.8516 3.2647 2.9578 -0.0145 0.0652  -0.0308 204 GLN H OE1 
11274 N NE2 . GLN G 204 ? 2.8104 3.2691 2.9282 -0.0256 0.0744  -0.0015 204 GLN H NE2 
11275 N N   . THR G 205 ? 2.4159 2.7942 2.5249 -0.0489 0.1137  0.0274  205 THR H N   
11276 C CA  . THR G 205 ? 2.4204 2.7543 2.5291 -0.0788 0.1107  0.0229  205 THR H CA  
11277 C C   . THR G 205 ? 2.4400 2.7584 2.5440 -0.0803 0.0962  -0.0026 205 THR H C   
11278 O O   . THR G 205 ? 2.4199 2.7551 2.5301 -0.0826 0.0866  -0.0132 205 THR H O   
11279 C CB  . THR G 205 ? 2.5309 2.8727 2.6614 -0.1048 0.1137  0.0356  205 THR H CB  
11280 O OG1 . THR G 205 ? 2.5468 2.9131 2.6831 -0.1030 0.1288  0.0611  205 THR H OG1 
11281 C CG2 . THR G 205 ? 2.5219 2.8189 2.6592 -0.1280 0.1093  0.0342  205 THR H CG2 
11282 N N   . TYR G 206 ? 2.3912 2.6783 2.4789 -0.0779 0.0940  -0.0134 206 TYR H N   
11283 C CA  . TYR G 206 ? 2.3691 2.6420 2.4521 -0.0811 0.0831  -0.0345 206 TYR H CA  
11284 C C   . TYR G 206 ? 2.3956 2.6374 2.4809 -0.1008 0.0761  -0.0355 206 TYR H C   
11285 O O   . TYR G 206 ? 2.4001 2.6202 2.4717 -0.1020 0.0728  -0.0349 206 TYR H O   
11286 C CB  . TYR G 206 ? 2.3861 2.6574 2.4525 -0.0620 0.0839  -0.0507 206 TYR H CB  
11287 C CG  . TYR G 206 ? 2.4044 2.7092 2.4775 -0.0349 0.0850  -0.0562 206 TYR H CG  
11288 C CD1 . TYR G 206 ? 2.4121 2.7334 2.4959 -0.0322 0.0730  -0.0667 206 TYR H CD1 
11289 C CD2 . TYR G 206 ? 2.4256 2.7434 2.4920 -0.0070 0.0953  -0.0525 206 TYR H CD2 
11290 C CE1 . TYR G 206 ? 2.4083 2.7633 2.5016 -0.0021 0.0668  -0.0723 206 TYR H CE1 
11291 C CE2 . TYR G 206 ? 2.4232 2.7768 2.5016 0.0270  0.0929  -0.0586 206 TYR H CE2 
11292 C CZ  . TYR G 206 ? 2.4999 2.8743 2.5944 0.0296  0.0763  -0.0682 206 TYR H CZ  
11293 O OH  . TYR G 206 ? 2.4996 2.9121 2.6092 0.0678  0.0671  -0.0746 206 TYR H OH  
11294 N N   . ILE G 207 ? 2.3232 2.5643 2.4231 -0.1112 0.0711  -0.0396 207 ILE H N   
11295 C CA  . ILE G 207 ? 2.3090 2.5255 2.4189 -0.1212 0.0632  -0.0427 207 ILE H CA  
11296 C C   . ILE G 207 ? 2.3193 2.5225 2.4192 -0.1183 0.0559  -0.0592 207 ILE H C   
11297 O O   . ILE G 207 ? 2.3073 2.5172 2.3998 -0.1155 0.0564  -0.0702 207 ILE H O   
11298 C CB  . ILE G 207 ? 2.3465 2.5694 2.4776 -0.1283 0.0647  -0.0426 207 ILE H CB  
11299 C CG1 . ILE G 207 ? 2.3625 2.6096 2.5039 -0.1335 0.0751  -0.0250 207 ILE H CG1 
11300 C CG2 . ILE G 207 ? 2.3547 2.5533 2.5047 -0.1308 0.0561  -0.0459 207 ILE H CG2 
11301 C CD1 . ILE G 207 ? 2.4391 2.7168 2.5870 -0.1345 0.0774  -0.0322 207 ILE H CD1 
11302 N N   . CYS G 208 ? 2.2531 2.4391 2.3513 -0.1181 0.0466  -0.0601 208 CYS H N   
11303 C CA  . CYS G 208 ? 2.2332 2.4110 2.3233 -0.1154 0.0406  -0.0722 208 CYS H CA  
11304 C C   . CYS G 208 ? 2.2677 2.4303 2.3746 -0.1102 0.0319  -0.0743 208 CYS H C   
11305 O O   . CYS G 208 ? 2.2626 2.4201 2.3781 -0.1043 0.0184  -0.0686 208 CYS H O   
11306 C CB  . CYS G 208 ? 2.2349 2.4160 2.3055 -0.1127 0.0346  -0.0752 208 CYS H CB  
11307 S SG  . CYS G 208 ? 2.2726 2.4540 2.3342 -0.1121 0.0283  -0.0878 208 CYS H SG  
11308 N N   . ASN G 209 ? 2.2083 2.3629 2.3173 -0.1075 0.0371  -0.0852 209 ASN H N   
11309 C CA  . ASN G 209 ? 2.1897 2.3277 2.3130 -0.0943 0.0322  -0.0938 209 ASN H CA  
11310 C C   . ASN G 209 ? 2.2052 2.3327 2.3192 -0.0843 0.0277  -0.0989 209 ASN H C   
11311 O O   . ASN G 209 ? 2.2060 2.3257 2.2985 -0.0887 0.0353  -0.1065 209 ASN H O   
11312 C CB  . ASN G 209 ? 2.2127 2.3446 2.3326 -0.0916 0.0399  -0.1092 209 ASN H CB  
11313 C CG  . ASN G 209 ? 2.5559 2.7085 2.6826 -0.1023 0.0451  -0.1038 209 ASN H CG  
11314 O OD1 . ASN G 209 ? 2.5091 2.6798 2.6241 -0.1116 0.0488  -0.0947 209 ASN H OD1 
11315 N ND2 . ASN G 209 ? 2.4578 2.6115 2.6056 -0.0984 0.0457  -0.1109 209 ASN H ND2 
11316 N N   . VAL G 210 ? 2.1307 2.2600 2.2610 -0.0699 0.0130  -0.0936 210 VAL H N   
11317 C CA  . VAL G 210 ? 2.1138 2.2426 2.2392 -0.0556 0.0059  -0.0952 210 VAL H CA  
11318 C C   . VAL G 210 ? 2.1217 2.2392 2.2733 -0.0243 -0.0034 -0.1017 210 VAL H C   
11319 O O   . VAL G 210 ? 2.1041 2.2245 2.2841 -0.0142 -0.0163 -0.0991 210 VAL H O   
11320 C CB  . VAL G 210 ? 2.1621 2.3143 2.2786 -0.0587 -0.0096 -0.0857 210 VAL H CB  
11321 C CG1 . VAL G 210 ? 2.1542 2.3162 2.2637 -0.0462 -0.0155 -0.0866 210 VAL H CG1 
11322 C CG2 . VAL G 210 ? 2.1735 2.3358 2.2672 -0.0823 0.0002  -0.0854 210 VAL H CG2 
11323 N N   . ASN G 211 ? 2.0612 2.1640 2.2043 -0.0064 0.0031  -0.1110 211 ASN H N   
11324 C CA  . ASN G 211 ? 2.0335 2.1247 2.2004 0.0334  -0.0041 -0.1217 211 ASN H CA  
11325 C C   . ASN G 211 ? 2.0530 2.1473 2.2142 0.0584  -0.0081 -0.1185 211 ASN H C   
11326 O O   . ASN G 211 ? 2.0669 2.1533 2.1965 0.0428  0.0069  -0.1166 211 ASN H O   
11327 C CB  . ASN G 211 ? 2.0546 2.1165 2.2157 0.0419  0.0120  -0.1456 211 ASN H CB  
11328 C CG  . ASN G 211 ? 2.3646 2.3995 2.4795 0.0326  0.0312  -0.1573 211 ASN H CG  
11329 O OD1 . ASN G 211 ? 2.3161 2.3510 2.4055 0.0011  0.0394  -0.1553 211 ASN H OD1 
11330 N ND2 . ASN G 211 ? 2.2548 2.2643 2.3570 0.0638  0.0369  -0.1703 211 ASN H ND2 
11331 N N   . HIS G 212 ? 1.9662 2.0742 2.1605 0.0988  -0.0300 -0.1169 212 HIS H N   
11332 C CA  . HIS G 212 ? 1.9448 2.0643 2.1408 0.1337  -0.0377 -0.1124 212 HIS H CA  
11333 C C   . HIS G 212 ? 1.9870 2.0747 2.1950 0.1792  -0.0279 -0.1344 212 HIS H C   
11334 O O   . HIS G 212 ? 1.9595 2.0452 2.2055 0.2082  -0.0407 -0.1471 212 HIS H O   
11335 C CB  . HIS G 212 ? 1.9186 2.0814 2.1429 0.1571  -0.0764 -0.0978 212 HIS H CB  
11336 C CG  . HIS G 212 ? 1.9453 2.1385 2.1640 0.1832  -0.0880 -0.0869 212 HIS H CG  
11337 N ND1 . HIS G 212 ? 1.9491 2.1401 2.1886 0.2390  -0.0917 -0.0923 212 HIS H ND1 
11338 C CD2 . HIS G 212 ? 1.9645 2.1955 2.1602 0.1640  -0.0980 -0.0728 212 HIS H CD2 
11339 C CE1 . HIS G 212 ? 1.9322 2.1618 2.1613 0.2501  -0.1030 -0.0769 212 HIS H CE1 
11340 N NE2 . HIS G 212 ? 1.9458 2.2019 2.1480 0.2040  -0.1073 -0.0660 212 HIS H NE2 
11341 N N   . LYS G 213 ? 1.9683 2.0267 2.1411 0.1846  -0.0038 -0.1424 213 LYS H N   
11342 C CA  . LYS G 213 ? 1.9734 1.9932 2.1431 0.2314  0.0090  -0.1695 213 LYS H CA  
11343 C C   . LYS G 213 ? 1.9931 2.0323 2.2045 0.2999  -0.0109 -0.1702 213 LYS H C   
11344 O O   . LYS G 213 ? 1.9613 1.9901 2.2060 0.3414  -0.0181 -0.1942 213 LYS H O   
11345 C CB  . LYS G 213 ? 2.0533 2.0273 2.1629 0.2185  0.0388  -0.1789 213 LYS H CB  
11346 C CG  . LYS G 213 ? 2.2463 2.1962 2.3174 0.1676  0.0530  -0.1884 213 LYS H CG  
11347 C CD  . LYS G 213 ? 2.3114 2.2209 2.3626 0.1886  0.0625  -0.2272 213 LYS H CD  
11348 C CE  . LYS G 213 ? 2.3648 2.2593 2.3745 0.1427  0.0702  -0.2352 213 LYS H CE  
11349 N NZ  . LYS G 213 ? 2.4420 2.3007 2.4202 0.1649  0.0768  -0.2776 213 LYS H NZ  
11350 N N   . PRO G 214 ? 1.9519 2.0254 2.1674 0.3164  -0.0234 -0.1463 214 PRO H N   
11351 C CA  . PRO G 214 ? 1.9152 2.0139 2.1741 0.3908  -0.0476 -0.1472 214 PRO H CA  
11352 C C   . PRO G 214 ? 1.9284 2.0606 2.2482 0.4173  -0.0878 -0.1484 214 PRO H C   
11353 O O   . PRO G 214 ? 1.9051 2.0220 2.2622 0.4698  -0.0936 -0.1735 214 PRO H O   
11354 C CB  . PRO G 214 ? 1.9354 2.0745 2.1797 0.3908  -0.0540 -0.1177 214 PRO H CB  
11355 C CG  . PRO G 214 ? 2.0390 2.1526 2.2277 0.3248  -0.0210 -0.1102 214 PRO H CG  
11356 C CD  . PRO G 214 ? 1.9933 2.0874 2.1756 0.2739  -0.0162 -0.1204 214 PRO H CD  
11357 N N   . SER G 215 ? 1.8766 2.0498 2.2038 0.3824  -0.1156 -0.1253 215 SER H N   
11358 C CA  . SER G 215 ? 1.8423 2.0430 2.2199 0.4029  -0.1586 -0.1232 215 SER H CA  
11359 C C   . SER G 215 ? 1.9225 2.0904 2.3215 0.3824  -0.1497 -0.1424 215 SER H C   
11360 O O   . SER G 215 ? 1.8862 2.0684 2.3327 0.4022  -0.1830 -0.1433 215 SER H O   
11361 C CB  . SER G 215 ? 1.8687 2.1155 2.2321 0.3719  -0.1907 -0.0970 215 SER H CB  
11362 O OG  . SER G 215 ? 1.9834 2.2147 2.3089 0.3001  -0.1701 -0.0919 215 SER H OG  
11363 N N   . ASN G 216 ? 1.9438 2.0705 2.3072 0.3434  -0.1077 -0.1574 216 ASN H N   
11364 C CA  . ASN G 216 ? 1.9688 2.0688 2.3411 0.3175  -0.0925 -0.1767 216 ASN H CA  
11365 C C   . ASN G 216 ? 2.0520 2.1698 2.4324 0.2679  -0.1085 -0.1565 216 ASN H C   
11366 O O   . ASN G 216 ? 2.0541 2.1588 2.4504 0.2475  -0.1005 -0.1673 216 ASN H O   
11367 C CB  . ASN G 216 ? 1.9563 2.0411 2.3775 0.3760  -0.0968 -0.2103 216 ASN H CB  
11368 C CG  . ASN G 216 ? 2.2141 2.2567 2.6020 0.3976  -0.0613 -0.2456 216 ASN H CG  
11369 O OD1 . ASN G 216 ? 2.1615 2.1781 2.5002 0.3537  -0.0326 -0.2552 216 ASN H OD1 
11370 N ND2 . ASN G 216 ? 2.0833 2.1177 2.4947 0.4711  -0.0654 -0.2685 216 ASN H ND2 
11371 N N   . THR G 217 ? 2.0303 2.1773 2.3928 0.2480  -0.1287 -0.1291 217 THR H N   
11372 C CA  . THR G 217 ? 2.0493 2.2088 2.4054 0.2059  -0.1442 -0.1110 217 THR H CA  
11373 C C   . THR G 217 ? 2.1546 2.2961 2.4675 0.1475  -0.1076 -0.1099 217 THR H C   
11374 O O   . THR G 217 ? 2.1703 2.3194 2.4419 0.1220  -0.0962 -0.1006 217 THR H O   
11375 C CB  . THR G 217 ? 2.1529 2.3503 2.4962 0.2148  -0.1815 -0.0910 217 THR H CB  
11376 O OG1 . THR G 217 ? 2.1221 2.3414 2.5047 0.2783  -0.2158 -0.0933 217 THR H OG1 
11377 C CG2 . THR G 217 ? 2.1408 2.3451 2.4746 0.1846  -0.2057 -0.0773 217 THR H CG2 
11378 N N   . LYS G 218 ? 2.3417 2.0539 2.2643 -0.5504 -0.3304 0.2486  218 LYS H N   
11379 C CA  . LYS G 218 ? 2.3228 2.0503 2.2748 -0.5046 -0.3400 0.2468  218 LYS H CA  
11380 C C   . LYS G 218 ? 2.3794 2.1041 2.3170 -0.4560 -0.3181 0.2380  218 LYS H C   
11381 O O   . LYS G 218 ? 2.3753 2.0881 2.3081 -0.4454 -0.3102 0.2543  218 LYS H O   
11382 C CB  . LYS G 218 ? 2.3453 2.0697 2.3346 -0.5183 -0.3596 0.2747  218 LYS H CB  
11383 C CG  . LYS G 218 ? 2.4976 2.2239 2.5071 -0.5754 -0.3884 0.2876  218 LYS H CG  
11384 C CD  . LYS G 218 ? 2.5966 2.3252 2.6638 -0.5833 -0.4123 0.3128  218 LYS H CD  
11385 C CE  . LYS G 218 ? 2.7303 2.4621 2.8239 -0.6457 -0.4484 0.3275  218 LYS H CE  
11386 N NZ  . LYS G 218 ? 2.8379 2.5981 2.9380 -0.6436 -0.4698 0.3009  218 LYS H NZ  
11387 N N   . VAL G 219 ? 2.3451 2.0799 2.2758 -0.4307 -0.3112 0.2139  219 VAL H N   
11388 C CA  . VAL G 219 ? 2.3526 2.0852 2.2737 -0.3927 -0.2962 0.2049  219 VAL H CA  
11389 C C   . VAL G 219 ? 2.3936 2.1344 2.3285 -0.3606 -0.3041 0.2002  219 VAL H C   
11390 O O   . VAL G 219 ? 2.3854 2.1360 2.3253 -0.3542 -0.3123 0.1893  219 VAL H O   
11391 C CB  . VAL G 219 ? 2.4146 2.1467 2.3255 -0.3922 -0.2817 0.1861  219 VAL H CB  
11392 C CG1 . VAL G 219 ? 2.4144 2.1442 2.3246 -0.3588 -0.2732 0.1805  219 VAL H CG1 
11393 C CG2 . VAL G 219 ? 2.4271 2.1466 2.3211 -0.4286 -0.2677 0.1884  219 VAL H CG2 
11394 N N   . ASP G 220 ? 2.3450 2.0798 2.2822 -0.3437 -0.3004 0.2087  220 ASP H N   
11395 C CA  . ASP G 220 ? 2.3360 2.0729 2.2820 -0.3204 -0.3020 0.2031  220 ASP H CA  
11396 C C   . ASP G 220 ? 2.3888 2.1185 2.3152 -0.3014 -0.2929 0.1958  220 ASP H C   
11397 O O   . ASP G 220 ? 2.3866 2.1100 2.3023 -0.2985 -0.2872 0.2015  220 ASP H O   
11398 C CB  . ASP G 220 ? 2.3537 2.0886 2.3246 -0.3224 -0.3039 0.2147  220 ASP H CB  
11399 C CG  . ASP G 220 ? 2.4580 2.2004 2.4608 -0.3452 -0.3196 0.2248  220 ASP H CG  
11400 O OD1 . ASP G 220 ? 2.4650 2.2057 2.5021 -0.3482 -0.3224 0.2358  220 ASP H OD1 
11401 O OD2 . ASP G 220 ? 2.5082 2.2584 2.5060 -0.3626 -0.3306 0.2212  220 ASP H OD2 
11402 N N   . LYS G 221 ? 2.3462 2.0763 2.2677 -0.2919 -0.2953 0.1860  221 LYS H N   
11403 C CA  . LYS G 221 ? 2.3533 2.0755 2.2627 -0.2822 -0.2933 0.1819  221 LYS H CA  
11404 C C   . LYS G 221 ? 2.4287 2.1423 2.3315 -0.2769 -0.2953 0.1796  221 LYS H C   
11405 O O   . LYS G 221 ? 2.4176 2.1321 2.3227 -0.2761 -0.2990 0.1792  221 LYS H O   
11406 C CB  . LYS G 221 ? 2.3772 2.1009 2.2918 -0.2831 -0.2942 0.1772  221 LYS H CB  
11407 C CG  . LYS G 221 ? 2.4882 2.2134 2.4036 -0.2900 -0.2862 0.1766  221 LYS H CG  
11408 C CD  . LYS G 221 ? 2.5627 2.2882 2.4951 -0.2905 -0.2830 0.1687  221 LYS H CD  
11409 C CE  . LYS G 221 ? 2.6283 2.3482 2.5689 -0.2827 -0.2887 0.1697  221 LYS H CE  
11410 N NZ  . LYS G 221 ? 2.7000 2.4199 2.6731 -0.2838 -0.2855 0.1633  221 LYS H NZ  
11411 N N   . ARG G 222 ? 2.4149 2.1190 2.3049 -0.2774 -0.2935 0.1782  222 ARG H N   
11412 C CA  . ARG G 222 ? 2.4347 2.1245 2.3110 -0.2826 -0.2927 0.1753  222 ARG H CA  
11413 C C   . ARG G 222 ? 2.4974 2.1768 2.3673 -0.2883 -0.3030 0.1801  222 ARG H C   
11414 O O   . ARG G 222 ? 2.4836 2.1657 2.3626 -0.2887 -0.3106 0.1825  222 ARG H O   
11415 C CB  . ARG G 222 ? 2.4577 2.1410 2.3204 -0.2891 -0.2885 0.1703  222 ARG H CB  
11416 C CG  . ARG G 222 ? 2.6499 2.3162 2.4977 -0.3022 -0.2803 0.1630  222 ARG H CG  
11417 C CD  . ARG G 222 ? 2.8286 2.4875 2.6567 -0.3163 -0.2804 0.1554  222 ARG H CD  
11418 N NE  . ARG G 222 ? 3.0001 2.6493 2.8112 -0.3338 -0.2982 0.1590  222 ARG H NE  
11419 C CZ  . ARG G 222 ? 3.2319 2.8590 3.0220 -0.3607 -0.3009 0.1582  222 ARG H CZ  
11420 N NH1 . ARG G 222 ? 3.1056 2.7170 2.8839 -0.3715 -0.2823 0.1508  222 ARG H NH1 
11421 N NH2 . ARG G 222 ? 3.0681 2.6862 2.8511 -0.3814 -0.3227 0.1663  222 ARG H NH2 
11422 N N   . VAL G 223 ? 2.4764 2.1419 2.3335 -0.2944 -0.3034 0.1838  223 VAL H N   
11423 C CA  . VAL G 223 ? 2.4888 2.1382 2.3385 -0.3043 -0.3148 0.1957  223 VAL H CA  
11424 C C   . VAL G 223 ? 2.5843 2.2126 2.4155 -0.3285 -0.3195 0.1978  223 VAL H C   
11425 O O   . VAL G 223 ? 2.6016 2.2164 2.4097 -0.3418 -0.3091 0.1918  223 VAL H O   
11426 C CB  . VAL G 223 ? 2.5359 2.1772 2.3721 -0.3023 -0.3155 0.2041  223 VAL H CB  
11427 C CG1 . VAL G 223 ? 2.5437 2.1645 2.3722 -0.3142 -0.3289 0.2232  223 VAL H CG1 
11428 C CG2 . VAL G 223 ? 2.5094 2.1745 2.3623 -0.2846 -0.3162 0.1995  223 VAL H CG2 
11429 N N   . GLU G 224 ? 2.5486 2.1744 2.3937 -0.3379 -0.3354 0.2049  224 GLU H N   
11430 C CA  . GLU G 224 ? 2.5643 2.1724 2.3959 -0.3683 -0.3486 0.2085  224 GLU H CA  
11431 C C   . GLU G 224 ? 2.6159 2.1969 2.4476 -0.3949 -0.3665 0.2314  224 GLU H C   
11432 O O   . GLU G 224 ? 2.5961 2.1804 2.4601 -0.3850 -0.3760 0.2442  224 GLU H O   
11433 C CB  . GLU G 224 ? 2.5695 2.1949 2.4184 -0.3658 -0.3596 0.2012  224 GLU H CB  
11434 C CG  . GLU G 224 ? 2.6876 2.3275 2.5791 -0.3507 -0.3688 0.2066  224 GLU H CG  
11435 C CD  . GLU G 224 ? 2.8948 2.5569 2.7994 -0.3209 -0.3514 0.1970  224 GLU H CD  
11436 O OE1 . GLU G 224 ? 2.6927 2.3693 2.6031 -0.3132 -0.3507 0.1902  224 GLU H OE1 
11437 O OE2 . GLU G 224 ? 2.8575 2.5213 2.7637 -0.3095 -0.3406 0.1978  224 GLU H OE2 
11438 N N   . PRO G 225 ? 2.5928 2.1437 2.3895 -0.4332 -0.3703 0.2384  225 PRO H N   
11439 C CA  . PRO G 225 ? 2.6330 2.1519 2.4273 -0.4661 -0.3898 0.2674  225 PRO H CA  
11440 C C   . PRO G 225 ? 2.7717 2.2868 2.5968 -0.4942 -0.4209 0.2786  225 PRO H C   
11441 O O   . PRO G 225 ? 2.2207 1.7537 2.0973 -0.4746 -0.4328 0.2835  225 PRO H O   
11442 C CB  . PRO G 225 ? 2.6880 2.1727 2.4257 -0.5022 -0.3776 0.2693  225 PRO H CB  
11443 C CG  . PRO G 225 ? 2.7359 2.2377 2.4572 -0.4889 -0.3525 0.2368  225 PRO H CG  
11444 C CD  . PRO G 225 ? 2.6405 2.1814 2.3989 -0.4536 -0.3557 0.2212  225 PRO H CD  
11445 N N   . GLU H 1   ? 1.0037 3.2031 1.5253 -0.3206 0.2239  -0.7272 1   GLU L N   
11446 C CA  . GLU H 1   ? 1.0240 3.0018 1.4769 -0.3067 0.2158  -0.6520 1   GLU L CA  
11447 C C   . GLU H 1   ? 1.0644 2.9675 1.4924 -0.3101 0.1848  -0.5953 1   GLU L C   
11448 O O   . GLU H 1   ? 1.0635 2.9843 1.5190 -0.2782 0.1644  -0.6311 1   GLU L O   
11449 C CB  . GLU H 1   ? 1.0865 2.8894 1.5217 -0.2352 0.2152  -0.6888 1   GLU L CB  
11450 C CG  . GLU H 1   ? 1.2863 3.1207 1.7262 -0.2394 0.2453  -0.7285 1   GLU L CG  
11451 C CD  . GLU H 1   ? 1.7499 3.4068 2.1634 -0.1817 0.2405  -0.7569 1   GLU L CD  
11452 O OE1 . GLU H 1   ? 1.8015 3.2957 2.1532 -0.1753 0.2354  -0.6997 1   GLU L OE1 
11453 O OE2 . GLU H 1   ? 1.7292 3.3642 2.1696 -0.1403 0.2372  -0.8101 1   GLU L OE2 
11454 N N   . ILE H 2   ? 1.0176 2.8371 1.3950 -0.3468 0.1794  -0.5097 2   ILE L N   
11455 C CA  . ILE H 2   ? 1.0318 2.7618 1.3784 -0.3545 0.1489  -0.4520 2   ILE L CA  
11456 C C   . ILE H 2   ? 1.1290 2.6495 1.4388 -0.2876 0.1393  -0.4516 2   ILE L C   
11457 O O   . ILE H 2   ? 1.1360 2.5287 1.3993 -0.2825 0.1435  -0.4082 2   ILE L O   
11458 C CB  . ILE H 2   ? 1.0627 2.7965 1.3767 -0.4219 0.1412  -0.3658 2   ILE L CB  
11459 C CG1 . ILE H 2   ? 1.0354 2.9887 1.3828 -0.4984 0.1506  -0.3616 2   ILE L CG1 
11460 C CG2 . ILE H 2   ? 1.0971 2.7357 1.3811 -0.4311 0.1056  -0.3133 2   ILE L CG2 
11461 C CD1 . ILE H 2   ? 1.0543 3.0732 1.4082 -0.5162 0.1839  -0.3702 2   ILE L CD1 
11462 N N   . VAL H 3   ? 1.1136 2.6131 1.4474 -0.2364 0.1257  -0.5040 3   VAL L N   
11463 C CA  . VAL H 3   ? 1.1541 2.4754 1.4593 -0.1753 0.1119  -0.5107 3   VAL L CA  
11464 C C   . VAL H 3   ? 1.2213 2.4053 1.4724 -0.1810 0.0938  -0.4447 3   VAL L C   
11465 O O   . VAL H 3   ? 1.2236 2.4268 1.4763 -0.1977 0.0727  -0.4238 3   VAL L O   
11466 C CB  . VAL H 3   ? 1.2322 2.5767 1.5821 -0.1228 0.0933  -0.5768 3   VAL L CB  
11467 C CG1 . VAL H 3   ? 1.2787 2.4382 1.5947 -0.0692 0.0713  -0.5706 3   VAL L CG1 
11468 C CG2 . VAL H 3   ? 1.2249 2.6786 1.6282 -0.1041 0.1094  -0.6536 3   VAL L CG2 
11469 N N   . LEU H 4   ? 1.1852 2.2386 1.3882 -0.1686 0.1022  -0.4161 4   LEU L N   
11470 C CA  . LEU H 4   ? 1.2037 2.1236 1.3560 -0.1653 0.0872  -0.3660 4   LEU L CA  
11471 C C   . LEU H 4   ? 1.2898 2.0927 1.4240 -0.1148 0.0711  -0.3871 4   LEU L C   
11472 O O   . LEU H 4   ? 1.3070 2.0636 1.4340 -0.0873 0.0788  -0.4140 4   LEU L O   
11473 C CB  . LEU H 4   ? 1.1958 2.0621 1.3090 -0.1801 0.1042  -0.3273 4   LEU L CB  
11474 C CG  . LEU H 4   ? 1.2309 2.1869 1.3534 -0.2323 0.1115  -0.2887 4   LEU L CG  
11475 C CD1 . LEU H 4   ? 1.2280 2.1350 1.3177 -0.2348 0.1283  -0.2601 4   LEU L CD1 
11476 C CD2 . LEU H 4   ? 1.2870 2.2292 1.4032 -0.2599 0.0828  -0.2459 4   LEU L CD2 
11477 N N   . THR H 5   ? 1.2466 2.0062 1.3732 -0.1076 0.0458  -0.3740 5   THR L N   
11478 C CA  . THR H 5   ? 1.2663 1.9239 1.3757 -0.0664 0.0257  -0.3868 5   THR L CA  
11479 C C   . THR H 5   ? 1.3101 1.8564 1.3665 -0.0706 0.0147  -0.3450 5   THR L C   
11480 O O   . THR H 5   ? 1.3009 1.8519 1.3544 -0.0890 0.0000  -0.3235 5   THR L O   
11481 C CB  . THR H 5   ? 1.3680 2.0909 1.5241 -0.0460 0.0051  -0.4230 5   THR L CB  
11482 O OG1 . THR H 5   ? 1.3434 2.1856 1.5271 -0.0838 0.0041  -0.4150 5   THR L OG1 
11483 C CG2 . THR H 5   ? 1.3456 2.1144 1.5447 -0.0126 0.0082  -0.4800 5   THR L CG2 
11484 N N   . GLN H 6   ? 1.2814 1.7351 1.2947 -0.0571 0.0218  -0.3363 6   GLN L N   
11485 C CA  . GLN H 6   ? 1.3064 1.6661 1.2694 -0.0576 0.0148  -0.3072 6   GLN L CA  
11486 C C   . GLN H 6   ? 1.4026 1.6972 1.3493 -0.0393 -0.0118 -0.3095 6   GLN L C   
11487 O O   . GLN H 6   ? 1.4137 1.6923 1.3700 -0.0167 -0.0250 -0.3302 6   GLN L O   
11488 C CB  . GLN H 6   ? 1.3241 1.6363 1.2469 -0.0551 0.0332  -0.3001 6   GLN L CB  
11489 C CG  . GLN H 6   ? 1.4474 1.7980 1.3689 -0.0772 0.0530  -0.2784 6   GLN L CG  
11490 C CD  . GLN H 6   ? 1.6777 1.9980 1.5605 -0.0748 0.0719  -0.2728 6   GLN L CD  
11491 O OE1 . GLN H 6   ? 1.5758 1.9355 1.4637 -0.0810 0.0921  -0.2828 6   GLN L OE1 
11492 N NE2 . GLN H 6   ? 1.6210 1.8812 1.4645 -0.0678 0.0662  -0.2597 6   GLN L NE2 
11493 N N   . SER H 7   ? 1.3801 1.6348 1.3025 -0.0496 -0.0227 -0.2884 7   SER L N   
11494 C CA  . SER H 7   ? 1.4109 1.6107 1.3129 -0.0403 -0.0464 -0.2870 7   SER L CA  
11495 C C   . SER H 7   ? 1.4810 1.6104 1.3329 -0.0440 -0.0458 -0.2729 7   SER L C   
11496 O O   . SER H 7   ? 1.4746 1.6034 1.3215 -0.0562 -0.0385 -0.2611 7   SER L O   
11497 C CB  . SER H 7   ? 1.4554 1.7000 1.3855 -0.0529 -0.0636 -0.2854 7   SER L CB  
11498 O OG  . SER H 7   ? 1.5926 1.8076 1.5156 -0.0399 -0.0868 -0.2905 7   SER L OG  
11499 N N   . PRO H 8   ? 1.4640 1.5392 1.2793 -0.0344 -0.0556 -0.2752 8   PRO L N   
11500 C CA  . PRO H 8   ? 1.4873 1.5440 1.3023 -0.0211 -0.0734 -0.2819 8   PRO L CA  
11501 C C   . PRO H 8   ? 1.5490 1.5971 1.3574 -0.0141 -0.0633 -0.2880 8   PRO L C   
11502 O O   . PRO H 8   ? 1.5169 1.5925 1.3292 -0.0199 -0.0383 -0.2895 8   PRO L O   
11503 C CB  . PRO H 8   ? 1.5466 1.5524 1.3158 -0.0272 -0.0894 -0.2736 8   PRO L CB  
11504 C CG  . PRO H 8   ? 1.5959 1.5914 1.3322 -0.0363 -0.0696 -0.2717 8   PRO L CG  
11505 C CD  . PRO H 8   ? 1.5039 1.5351 1.2737 -0.0384 -0.0536 -0.2708 8   PRO L CD  
11506 N N   . GLY H 9   ? 1.5523 1.5600 1.3501 -0.0043 -0.0863 -0.2894 9   GLY L N   
11507 C CA  . GLY H 9   ? 1.5741 1.5540 1.3577 -0.0019 -0.0854 -0.2936 9   GLY L CA  
11508 C C   . GLY H 9   ? 1.6339 1.5823 1.3535 -0.0247 -0.0739 -0.2771 9   GLY L C   
11509 O O   . GLY H 9   ? 1.6244 1.5808 1.3293 -0.0332 -0.0531 -0.2792 9   GLY L O   
11510 N N   . THR H 10  ? 1.6013 1.5268 1.2830 -0.0368 -0.0867 -0.2634 10  THR L N   
11511 C CA  . THR H 10  ? 1.6129 1.5294 1.2335 -0.0601 -0.0787 -0.2530 10  THR L CA  
11512 C C   . THR H 10  ? 1.6442 1.5731 1.2515 -0.0646 -0.0801 -0.2545 10  THR L C   
11513 O O   . THR H 10  ? 1.6487 1.5679 1.2726 -0.0599 -0.1010 -0.2530 10  THR L O   
11514 C CB  . THR H 10  ? 1.7898 1.6581 1.3634 -0.0800 -0.1062 -0.2360 10  THR L CB  
11515 O OG1 . THR H 10  ? 1.8238 1.6543 1.4213 -0.0675 -0.1435 -0.2301 10  THR L OG1 
11516 C CG2 . THR H 10  ? 1.7841 1.6401 1.3415 -0.0892 -0.0962 -0.2356 10  THR L CG2 
11517 N N   . LEU H 11  ? 1.5818 1.5361 1.1613 -0.0720 -0.0588 -0.2613 11  LEU L N   
11518 C CA  . LEU H 11  ? 1.5864 1.5526 1.1532 -0.0732 -0.0600 -0.2728 11  LEU L CA  
11519 C C   . LEU H 11  ? 1.6801 1.6616 1.1862 -0.0975 -0.0649 -0.2740 11  LEU L C   
11520 O O   . LEU H 11  ? 1.6795 1.6878 1.1554 -0.1075 -0.0487 -0.2754 11  LEU L O   
11521 C CB  . LEU H 11  ? 1.5531 1.5420 1.1435 -0.0567 -0.0375 -0.2870 11  LEU L CB  
11522 C CG  . LEU H 11  ? 1.5927 1.5717 1.2296 -0.0449 -0.0437 -0.2886 11  LEU L CG  
11523 C CD1 . LEU H 11  ? 1.5768 1.5693 1.2342 -0.0335 -0.0280 -0.2929 11  LEU L CD1 
11524 C CD2 . LEU H 11  ? 1.6497 1.6112 1.2775 -0.0489 -0.0632 -0.2985 11  LEU L CD2 
11525 N N   . SER H 12  ? 1.6603 1.6370 1.1471 -0.1118 -0.0874 -0.2728 12  SER L N   
11526 C CA  . SER H 12  ? 1.6892 1.6989 1.1176 -0.1432 -0.0948 -0.2745 12  SER L CA  
11527 C C   . SER H 12  ? 1.7197 1.7692 1.1477 -0.1343 -0.0839 -0.3103 12  SER L C   
11528 O O   . SER H 12  ? 1.7284 1.7649 1.1736 -0.1299 -0.0966 -0.3190 12  SER L O   
11529 C CB  . SER H 12  ? 1.7857 1.7705 1.1923 -0.1700 -0.1309 -0.2475 12  SER L CB  
11530 O OG  . SER H 12  ? 1.9276 1.8631 1.3407 -0.1708 -0.1475 -0.2195 12  SER L OG  
11531 N N   . LEU H 13  ? 1.6521 1.7504 1.0640 -0.1285 -0.0615 -0.3346 13  LEU L N   
11532 C CA  . LEU H 13  ? 1.6548 1.7900 1.0727 -0.1102 -0.0529 -0.3786 13  LEU L CA  
11533 C C   . LEU H 13  ? 1.7285 1.9516 1.0985 -0.1289 -0.0440 -0.4053 13  LEU L C   
11534 O O   . LEU H 13  ? 1.7222 1.9789 1.0591 -0.1497 -0.0354 -0.3889 13  LEU L O   
11535 C CB  . LEU H 13  ? 1.6270 1.7397 1.0923 -0.0694 -0.0370 -0.3911 13  LEU L CB  
11536 C CG  . LEU H 13  ? 1.6828 1.7296 1.1970 -0.0544 -0.0465 -0.3741 13  LEU L CG  
11537 C CD1 . LEU H 13  ? 1.6498 1.6835 1.1968 -0.0384 -0.0315 -0.3555 13  LEU L CD1 
11538 C CD2 . LEU H 13  ? 1.7639 1.7887 1.2990 -0.0379 -0.0578 -0.4033 13  LEU L CD2 
11539 N N   . SER H 14  ? 1.7062 1.9741 1.0716 -0.1239 -0.0468 -0.4499 14  SER L N   
11540 C CA  . SER H 14  ? 1.7201 2.0967 1.0458 -0.1387 -0.0380 -0.4891 14  SER L CA  
11541 C C   . SER H 14  ? 1.7303 2.1388 1.0838 -0.0913 -0.0170 -0.5296 14  SER L C   
11542 O O   . SER H 14  ? 1.7200 2.0675 1.1237 -0.0474 -0.0189 -0.5459 14  SER L O   
11543 C CB  . SER H 14  ? 1.8110 2.2312 1.1249 -0.1527 -0.0511 -0.5273 14  SER L CB  
11544 O OG  . SER H 14  ? 1.9641 2.3889 1.2397 -0.2063 -0.0719 -0.4899 14  SER L OG  
11545 N N   . PRO H 15  ? 1.6674 2.1714 0.9889 -0.1012 -0.0006 -0.5436 15  PRO L N   
11546 C CA  . PRO H 15  ? 1.6442 2.1853 0.9966 -0.0512 0.0167  -0.5818 15  PRO L CA  
11547 C C   . PRO H 15  ? 1.7112 2.2657 1.1004 -0.0040 0.0094  -0.6498 15  PRO L C   
11548 O O   . PRO H 15  ? 1.7352 2.3916 1.1033 -0.0095 0.0098  -0.7036 15  PRO L O   
11549 C CB  . PRO H 15  ? 1.6646 2.3290 0.9651 -0.0826 0.0329  -0.5864 15  PRO L CB  
11550 C CG  . PRO H 15  ? 1.7331 2.3843 0.9789 -0.1501 0.0225  -0.5309 15  PRO L CG  
11551 C CD  . PRO H 15  ? 1.7019 2.2869 0.9562 -0.1615 -0.0008 -0.5221 15  PRO L CD  
11552 N N   . GLY H 16  ? 1.6676 2.1186 1.1108 0.0382  -0.0002 -0.6473 16  GLY L N   
11553 C CA  . GLY H 16  ? 1.7125 2.1374 1.1956 0.0848  -0.0156 -0.7055 16  GLY L CA  
11554 C C   . GLY H 16  ? 1.7883 2.0808 1.3057 0.0912  -0.0357 -0.6776 16  GLY L C   
11555 O O   . GLY H 16  ? 1.8300 2.0626 1.3881 0.1325  -0.0530 -0.7079 16  GLY L O   
11556 N N   . GLU H 17  ? 1.7208 1.9677 1.2221 0.0495  -0.0371 -0.6196 17  GLU L N   
11557 C CA  . GLU H 17  ? 1.7231 1.8647 1.2519 0.0459  -0.0545 -0.5873 17  GLU L CA  
11558 C C   . GLU H 17  ? 1.7425 1.8177 1.3132 0.0703  -0.0551 -0.5542 17  GLU L C   
11559 O O   . GLU H 17  ? 1.6954 1.8035 1.2729 0.0892  -0.0407 -0.5514 17  GLU L O   
11560 C CB  . GLU H 17  ? 1.7206 1.8540 1.2224 -0.0014 -0.0571 -0.5413 17  GLU L CB  
11561 C CG  . GLU H 17  ? 1.9005 2.0693 1.3723 -0.0296 -0.0686 -0.5654 17  GLU L CG  
11562 C CD  . GLU H 17  ? 2.1826 2.3336 1.6345 -0.0715 -0.0792 -0.5167 17  GLU L CD  
11563 O OE1 . GLU H 17  ? 1.9876 2.0948 1.4526 -0.0787 -0.0956 -0.5130 17  GLU L OE1 
11564 O OE2 . GLU H 17  ? 2.1634 2.3431 1.5864 -0.0973 -0.0743 -0.4826 17  GLU L OE2 
11565 N N   . GLY H 18  ? 1.7292 1.7220 1.3255 0.0650  -0.0729 -0.5292 18  GLY L N   
11566 C CA  . GLY H 18  ? 1.7236 1.6597 1.3575 0.0758  -0.0787 -0.4934 18  GLY L CA  
11567 C C   . GLY H 18  ? 1.7405 1.6687 1.3780 0.0455  -0.0708 -0.4385 18  GLY L C   
11568 O O   . GLY H 18  ? 1.7404 1.6463 1.3746 0.0217  -0.0812 -0.4238 18  GLY L O   
11569 N N   . ALA H 19  ? 1.6595 1.6124 1.3067 0.0481  -0.0531 -0.4116 19  ALA L N   
11570 C CA  . ALA H 19  ? 1.6151 1.5714 1.2715 0.0247  -0.0440 -0.3688 19  ALA L CA  
11571 C C   . ALA H 19  ? 1.6789 1.5976 1.3757 0.0199  -0.0575 -0.3410 19  ALA L C   
11572 O O   . ALA H 19  ? 1.6983 1.5954 1.4157 0.0361  -0.0672 -0.3413 19  ALA L O   
11573 C CB  . ALA H 19  ? 1.5855 1.5938 1.2295 0.0242  -0.0180 -0.3578 19  ALA L CB  
11574 N N   . THR H 20  ? 1.6175 1.5349 1.3257 -0.0039 -0.0613 -0.3165 20  THR L N   
11575 C CA  . THR H 20  ? 1.6051 1.5118 1.3478 -0.0206 -0.0737 -0.2883 20  THR L CA  
11576 C C   . THR H 20  ? 1.5768 1.5328 1.3335 -0.0358 -0.0580 -0.2686 20  THR L C   
11577 O O   . THR H 20  ? 1.5636 1.5266 1.3137 -0.0424 -0.0608 -0.2720 20  THR L O   
11578 C CB  . THR H 20  ? 1.8049 1.6654 1.5489 -0.0338 -0.1023 -0.2924 20  THR L CB  
11579 O OG1 . THR H 20  ? 1.8782 1.6918 1.6088 -0.0145 -0.1166 -0.3221 20  THR L OG1 
11580 C CG2 . THR H 20  ? 1.8071 1.6629 1.5801 -0.0604 -0.1199 -0.2610 20  THR L CG2 
11581 N N   . LEU H 21  ? 1.4884 1.4811 1.2660 -0.0396 -0.0436 -0.2510 21  LEU L N   
11582 C CA  . LEU H 21  ? 1.4407 1.4867 1.2351 -0.0503 -0.0272 -0.2422 21  LEU L CA  
11583 C C   . LEU H 21  ? 1.4950 1.5837 1.3287 -0.0746 -0.0333 -0.2215 21  LEU L C   
11584 O O   . LEU H 21  ? 1.4889 1.5836 1.3367 -0.0860 -0.0384 -0.2018 21  LEU L O   
11585 C CB  . LEU H 21  ? 1.4122 1.4872 1.1940 -0.0413 -0.0006 -0.2445 21  LEU L CB  
11586 C CG  . LEU H 21  ? 1.4839 1.5396 1.2217 -0.0277 0.0063  -0.2631 21  LEU L CG  
11587 C CD1 . LEU H 21  ? 1.5010 1.5519 1.2246 -0.0114 0.0096  -0.2719 21  LEU L CD1 
11588 C CD2 . LEU H 21  ? 1.5053 1.5886 1.2287 -0.0330 0.0252  -0.2634 21  LEU L CD2 
11589 N N   . SER H 22  ? 1.4578 1.5845 1.3103 -0.0837 -0.0353 -0.2263 22  SER L N   
11590 C CA  . SER H 22  ? 1.4449 1.6399 1.3354 -0.1106 -0.0405 -0.2142 22  SER L CA  
11591 C C   . SER H 22  ? 1.4640 1.7379 1.3811 -0.1123 -0.0172 -0.2220 22  SER L C   
11592 O O   . SER H 22  ? 1.4434 1.7101 1.3518 -0.0906 -0.0034 -0.2416 22  SER L O   
11593 C CB  . SER H 22  ? 1.5092 1.7135 1.4086 -0.1173 -0.0599 -0.2220 22  SER L CB  
11594 O OG  . SER H 22  ? 1.6906 1.8275 1.5656 -0.1216 -0.0820 -0.2170 22  SER L OG  
11595 N N   . CYS H 23  ? 1.4205 1.7719 1.3688 -0.1430 -0.0159 -0.2068 23  CYS L N   
11596 C CA  . CYS H 23  ? 1.3862 1.8341 1.3658 -0.1520 0.0059  -0.2181 23  CYS L CA  
11597 C C   . CYS H 23  ? 1.4384 1.9881 1.4545 -0.1912 -0.0051 -0.2101 23  CYS L C   
11598 O O   . CYS H 23  ? 1.4333 2.0138 1.4536 -0.2291 -0.0128 -0.1765 23  CYS L O   
11599 C CB  . CYS H 23  ? 1.3794 1.8330 1.3501 -0.1561 0.0263  -0.2028 23  CYS L CB  
11600 S SG  . CYS H 23  ? 1.3768 1.9607 1.3852 -0.1766 0.0549  -0.2162 23  CYS L SG  
11601 N N   . ARG H 24  ? 1.4030 2.0081 1.4447 -0.1838 -0.0100 -0.2396 24  ARG L N   
11602 C CA  . ARG H 24  ? 1.3910 2.1172 1.4679 -0.2218 -0.0203 -0.2398 24  ARG L CA  
11603 C C   . ARG H 24  ? 1.3764 2.2398 1.4970 -0.2308 0.0018  -0.2688 24  ARG L C   
11604 O O   . ARG H 24  ? 1.3443 2.2236 1.4853 -0.1923 0.0141  -0.3135 24  ARG L O   
11605 C CB  . ARG H 24  ? 1.4185 2.1454 1.5009 -0.2117 -0.0419 -0.2560 24  ARG L CB  
11606 C CG  . ARG H 24  ? 1.6174 2.2705 1.6661 -0.2380 -0.0687 -0.2192 24  ARG L CG  
11607 C CD  . ARG H 24  ? 1.8081 2.4297 1.8498 -0.2197 -0.0870 -0.2344 24  ARG L CD  
11608 N NE  . ARG H 24  ? 2.0067 2.4983 2.0033 -0.2168 -0.1027 -0.2132 24  ARG L NE  
11609 C CZ  . ARG H 24  ? 2.1902 2.5820 2.1599 -0.1774 -0.0964 -0.2232 24  ARG L CZ  
11610 N NH1 . ARG H 24  ? 2.0080 2.4013 1.9861 -0.1409 -0.0779 -0.2471 24  ARG L NH1 
11611 N NH2 . ARG H 24  ? 2.0343 2.3280 1.9671 -0.1775 -0.1108 -0.2112 24  ARG L NH2 
11612 N N   . ALA H 25  ? 1.3198 2.2806 1.4540 -0.2844 0.0033  -0.2427 25  ALA L N   
11613 C CA  . ALA H 25  ? 1.2806 2.3948 1.4557 -0.3071 0.0245  -0.2667 25  ALA L CA  
11614 C C   . ALA H 25  ? 1.3121 2.5781 1.5322 -0.3212 0.0181  -0.3049 25  ALA L C   
11615 O O   . ALA H 25  ? 1.3248 2.6034 1.5395 -0.3436 -0.0069 -0.2888 25  ALA L O   
11616 C CB  . ALA H 25  ? 1.2896 2.4508 1.4573 -0.3659 0.0245  -0.2155 25  ALA L CB  
11617 N N   . SER H 26  ? 1.2273 2.4470 1.3744 -0.2579 -0.1649 -0.4527 26  SER L N   
11618 C CA  . SER H 26  ? 1.2108 2.6017 1.3783 -0.2504 -0.1842 -0.5081 26  SER L CA  
11619 C C   . SER H 26  ? 1.2733 2.7817 1.4630 -0.3233 -0.1617 -0.4872 26  SER L C   
11620 O O   . SER H 26  ? 1.2889 2.8844 1.4874 -0.3450 -0.1663 -0.5197 26  SER L O   
11621 C CB  . SER H 26  ? 1.2191 2.6806 1.3993 -0.2017 -0.2083 -0.5326 26  SER L CB  
11622 O OG  . SER H 26  ? 1.2800 2.9289 1.4800 -0.1897 -0.2312 -0.5882 26  SER L OG  
11623 N N   . GLN H 27  ? 1.2220 2.7225 1.4166 -0.3631 -0.1383 -0.4321 27  GLN L N   
11624 C CA  . GLN H 27  ? 1.2374 2.8226 1.4418 -0.4412 -0.1173 -0.3968 27  GLN L CA  
11625 C C   . GLN H 27  ? 1.3182 2.7485 1.4953 -0.4845 -0.0993 -0.3301 27  GLN L C   
11626 O O   . GLN H 27  ? 1.3081 2.5954 1.4658 -0.4479 -0.1000 -0.3161 27  GLN L O   
11627 C CB  . GLN H 27  ? 1.2282 2.9800 1.4566 -0.4441 -0.1143 -0.4024 27  GLN L CB  
11628 C CG  . GLN H 27  ? 1.4284 3.1339 1.6586 -0.3905 -0.1174 -0.3931 27  GLN L CG  
11629 C CD  . GLN H 27  ? 1.6677 3.5157 1.9236 -0.3255 -0.1474 -0.4511 27  GLN L CD  
11630 O OE1 . GLN H 27  ? 1.5818 3.5643 1.8591 -0.3238 -0.1461 -0.4512 27  GLN L OE1 
11631 N NE2 . GLN H 27  ? 1.5808 3.3988 1.8305 -0.2658 -0.1805 -0.5031 27  GLN L NE2 
11632 N N   . SER H 28  ? 1.3157 2.7734 1.4868 -0.5625 -0.0884 -0.2912 28  SER L N   
11633 C CA  . SER H 28  ? 1.3592 2.6679 1.4944 -0.6031 -0.0839 -0.2335 28  SER L CA  
11634 C C   . SER H 28  ? 1.3788 2.6382 1.4975 -0.5903 -0.0719 -0.2041 28  SER L C   
11635 O O   . SER H 28  ? 1.3504 2.7249 1.4837 -0.5999 -0.0614 -0.2024 28  SER L O   
11636 C CB  . SER H 28  ? 1.4788 2.8249 1.6062 -0.6929 -0.0855 -0.2004 28  SER L CB  
11637 O OG  . SER H 28  ? 1.6719 2.8578 1.7559 -0.7255 -0.0956 -0.1516 28  SER L OG  
11638 N N   . VAL H 29  ? 1.3436 2.4403 1.4333 -0.5622 -0.0743 -0.1862 29  VAL L N   
11639 C CA  . VAL H 29  ? 1.3371 2.3634 1.4079 -0.5435 -0.0645 -0.1642 29  VAL L CA  
11640 C C   . VAL H 29  ? 1.4523 2.3381 1.4701 -0.5836 -0.0725 -0.1225 29  VAL L C   
11641 O O   . VAL H 29  ? 1.4899 2.3092 1.4903 -0.6031 -0.0900 -0.1157 29  VAL L O   
11642 C CB  . VAL H 29  ? 1.3366 2.3091 1.4210 -0.4655 -0.0638 -0.1891 29  VAL L CB  
11643 C CG1 . VAL H 29  ? 1.3077 2.2983 1.4008 -0.4406 -0.0526 -0.1842 29  VAL L CG1 
11644 C CG2 . VAL H 29  ? 1.2962 2.3423 1.4130 -0.4219 -0.0750 -0.2350 29  VAL L CG2 
11645 N N   . ASP H 30  ? 1.4160 2.2551 1.4053 -0.5905 -0.0655 -0.0993 30  ASP L N   
11646 C CA  . ASP H 30  ? 1.4789 2.1790 1.4060 -0.6216 -0.0817 -0.0672 30  ASP L CA  
11647 C C   . ASP H 30  ? 1.5123 2.0848 1.4214 -0.5744 -0.0952 -0.0786 30  ASP L C   
11648 O O   . ASP H 30  ? 1.4454 2.0194 1.3825 -0.5152 -0.0821 -0.1029 30  ASP L O   
11649 C CB  . ASP H 30  ? 1.5194 2.1988 1.4177 -0.6252 -0.0712 -0.0514 30  ASP L CB  
11650 C CG  . ASP H 30  ? 1.7316 2.2883 1.5523 -0.6739 -0.0951 -0.0179 30  ASP L CG  
11651 O OD1 . ASP H 30  ? 1.7951 2.2750 1.5834 -0.7056 -0.1260 -0.0044 30  ASP L OD1 
11652 O OD2 . ASP H 30  ? 1.7938 2.3269 1.5827 -0.6769 -0.0882 -0.0074 30  ASP L OD2 
11653 N N   . SER H 31  ? 1.5343 2.0028 1.3963 -0.6012 -0.1257 -0.0607 31  SER L N   
11654 C CA  . SER H 31  ? 1.5358 1.8936 1.3745 -0.5580 -0.1450 -0.0707 31  SER L CA  
11655 C C   . SER H 31  ? 1.5278 1.8205 1.3438 -0.5148 -0.1358 -0.0792 31  SER L C   
11656 O O   . SER H 31  ? 1.4777 1.7514 1.3103 -0.4618 -0.1267 -0.0983 31  SER L O   
11657 C CB  . SER H 31  ? 1.6883 1.9541 1.4765 -0.5946 -0.1906 -0.0508 31  SER L CB  
11658 O OG  . SER H 31  ? 1.9294 2.1360 1.6589 -0.6402 -0.2108 -0.0255 31  SER L OG  
11659 N N   . SER H 32  ? 1.4962 1.7608 1.2747 -0.5389 -0.1369 -0.0659 32  SER L N   
11660 C CA  . SER H 32  ? 1.4770 1.6811 1.2306 -0.5008 -0.1293 -0.0786 32  SER L CA  
11661 C C   . SER H 32  ? 1.4189 1.6979 1.2338 -0.4532 -0.0911 -0.0990 32  SER L C   
11662 O O   . SER H 32  ? 1.3911 1.6240 1.1988 -0.4131 -0.0832 -0.1148 32  SER L O   
11663 C CB  . SER H 32  ? 1.5879 1.7373 1.2788 -0.5390 -0.1442 -0.0614 32  SER L CB  
11664 O OG  . SER H 32  ? 1.6902 1.9316 1.3990 -0.5893 -0.1299 -0.0391 32  SER L OG  
11665 N N   . SER H 33  ? 1.3167 1.7098 1.1907 -0.4546 -0.0734 -0.1027 33  SER L N   
11666 C CA  . SER H 33  ? 1.2406 1.7020 1.1716 -0.4064 -0.0506 -0.1239 33  SER L CA  
11667 C C   . SER H 33  ? 1.2623 1.7084 1.2193 -0.3654 -0.0507 -0.1405 33  SER L C   
11668 O O   . SER H 33  ? 1.2162 1.6883 1.2109 -0.3238 -0.0401 -0.1563 33  SER L O   
11669 C CB  . SER H 33  ? 1.2463 1.8436 1.2200 -0.4208 -0.0408 -0.1261 33  SER L CB  
11670 O OG  . SER H 33  ? 1.3320 1.9968 1.3330 -0.4293 -0.0470 -0.1355 33  SER L OG  
11671 N N   . LEU H 34  ? 1.2400 1.6402 1.1746 -0.3762 -0.0665 -0.1357 34  LEU L N   
11672 C CA  . LEU H 34  ? 1.2110 1.5946 1.1611 -0.3404 -0.0673 -0.1480 34  LEU L CA  
11673 C C   . LEU H 34  ? 1.2532 1.5513 1.1771 -0.3097 -0.0682 -0.1490 34  LEU L C   
11674 O O   . LEU H 34  ? 1.2803 1.5129 1.1588 -0.3194 -0.0816 -0.1430 34  LEU L O   
11675 C CB  . LEU H 34  ? 1.2336 1.6269 1.1801 -0.3586 -0.0832 -0.1473 34  LEU L CB  
11676 C CG  . LEU H 34  ? 1.2734 1.7720 1.2580 -0.3718 -0.0803 -0.1607 34  LEU L CG  
11677 C CD1 . LEU H 34  ? 1.3117 1.8136 1.2870 -0.4029 -0.0978 -0.1579 34  LEU L CD1 
11678 C CD2 . LEU H 34  ? 1.2581 1.7918 1.2752 -0.3253 -0.0751 -0.1860 34  LEU L CD2 
11679 N N   . ALA H 35  ? 1.1728 1.4751 1.1217 -0.2733 -0.0578 -0.1582 35  ALA L N   
11680 C CA  . ALA H 35  ? 1.1692 1.4158 1.1010 -0.2459 -0.0541 -0.1591 35  ALA L CA  
11681 C C   . ALA H 35  ? 1.1933 1.4408 1.1368 -0.2217 -0.0522 -0.1599 35  ALA L C   
11682 O O   . ALA H 35  ? 1.1594 1.4472 1.1321 -0.2159 -0.0512 -0.1658 35  ALA L O   
11683 C CB  . ALA H 35  ? 1.1553 1.4011 1.1038 -0.2304 -0.0382 -0.1658 35  ALA L CB  
11684 N N   . TRP H 36  ? 1.1696 1.3750 1.0849 -0.2051 -0.0551 -0.1562 36  TRP L N   
11685 C CA  . TRP H 36  ? 1.1745 1.3748 1.0899 -0.1824 -0.0521 -0.1521 36  TRP L CA  
11686 C C   . TRP H 36  ? 1.1793 1.3724 1.0985 -0.1676 -0.0359 -0.1479 36  TRP L C   
11687 O O   . TRP H 36  ? 1.1705 1.3490 1.0698 -0.1644 -0.0345 -0.1525 36  TRP L O   
11688 C CB  . TRP H 36  ? 1.2026 1.3770 1.0832 -0.1729 -0.0708 -0.1501 36  TRP L CB  
11689 C CG  . TRP H 36  ? 1.2430 1.4265 1.1278 -0.1822 -0.0862 -0.1540 36  TRP L CG  
11690 C CD1 . TRP H 36  ? 1.2989 1.4694 1.1675 -0.2015 -0.1091 -0.1543 36  TRP L CD1 
11691 C CD2 . TRP H 36  ? 1.2341 1.4375 1.1366 -0.1714 -0.0846 -0.1612 36  TRP L CD2 
11692 N NE1 . TRP H 36  ? 1.2993 1.4898 1.1824 -0.2054 -0.1176 -0.1609 36  TRP L NE1 
11693 C CE2 . TRP H 36  ? 1.2994 1.5115 1.2020 -0.1842 -0.1024 -0.1691 36  TRP L CE2 
11694 C CE3 . TRP H 36  ? 1.2500 1.4586 1.1632 -0.1523 -0.0746 -0.1634 36  TRP L CE3 
11695 C CZ2 . TRP H 36  ? 1.2930 1.5257 1.2082 -0.1735 -0.1071 -0.1855 36  TRP L CZ2 
11696 C CZ3 . TRP H 36  ? 1.2763 1.4946 1.1932 -0.1407 -0.0839 -0.1789 36  TRP L CZ3 
11697 C CH2 . TRP H 36  ? 1.2911 1.5251 1.2104 -0.1489 -0.0982 -0.1930 36  TRP L CH2 
11698 N N   . TYR H 37  ? 1.1162 1.3184 1.0571 -0.1593 -0.0281 -0.1414 37  TYR L N   
11699 C CA  . TYR H 37  ? 1.1106 1.3099 1.0609 -0.1536 -0.0140 -0.1322 37  TYR L CA  
11700 C C   . TYR H 37  ? 1.1874 1.3773 1.1191 -0.1448 -0.0125 -0.1157 37  TYR L C   
11701 O O   . TYR H 37  ? 1.2037 1.3843 1.1261 -0.1383 -0.0236 -0.1150 37  TYR L O   
11702 C CB  . TYR H 37  ? 1.1019 1.3128 1.0951 -0.1555 -0.0130 -0.1349 37  TYR L CB  
11703 C CG  . TYR H 37  ? 1.0978 1.3251 1.1115 -0.1592 -0.0122 -0.1501 37  TYR L CG  
11704 C CD1 . TYR H 37  ? 1.1092 1.3327 1.1361 -0.1554 -0.0004 -0.1567 37  TYR L CD1 
11705 C CD2 . TYR H 37  ? 1.0963 1.3490 1.1170 -0.1656 -0.0228 -0.1592 37  TYR L CD2 
11706 C CE1 . TYR H 37  ? 1.1024 1.3365 1.1440 -0.1542 0.0003  -0.1710 37  TYR L CE1 
11707 C CE2 . TYR H 37  ? 1.0827 1.3568 1.1184 -0.1706 -0.0208 -0.1691 37  TYR L CE2 
11708 C CZ  . TYR H 37  ? 1.1862 1.4459 1.2303 -0.1629 -0.0095 -0.1744 37  TYR L CZ  
11709 O OH  . TYR H 37  ? 1.2516 1.5278 1.3052 -0.1639 -0.0077 -0.1845 37  TYR L OH  
11710 N N   . GLN H 38  ? 1.1394 1.3357 1.0634 -0.1446 0.0013  -0.1041 38  GLN L N   
11711 C CA  . GLN H 38  ? 1.1657 1.3613 1.0688 -0.1410 0.0063  -0.0825 38  GLN L CA  
11712 C C   . GLN H 38  ? 1.2405 1.4366 1.1663 -0.1582 0.0164  -0.0647 38  GLN L C   
11713 O O   . GLN H 38  ? 1.2335 1.4515 1.1769 -0.1659 0.0296  -0.0687 38  GLN L O   
11714 C CB  . GLN H 38  ? 1.1914 1.4127 1.0600 -0.1263 0.0103  -0.0828 38  GLN L CB  
11715 C CG  . GLN H 38  ? 1.3919 1.6272 1.2353 -0.1207 0.0180  -0.0580 38  GLN L CG  
11716 C CD  . GLN H 38  ? 1.6115 1.9018 1.4314 -0.1088 0.0263  -0.0584 38  GLN L CD  
11717 O OE1 . GLN H 38  ? 1.5343 1.8566 1.3644 -0.1164 0.0356  -0.0705 38  GLN L OE1 
11718 N NE2 . GLN H 38  ? 1.5181 1.8275 1.3055 -0.0859 0.0219  -0.0480 38  GLN L NE2 
11719 N N   . GLN H 39  ? 1.2255 1.3921 1.1481 -0.1637 0.0052  -0.0475 39  GLN L N   
11720 C CA  . GLN H 39  ? 1.2468 1.4011 1.1859 -0.1843 0.0049  -0.0251 39  GLN L CA  
11721 C C   . GLN H 39  ? 1.3716 1.5185 1.2720 -0.1957 0.0108  0.0079  39  GLN L C   
11722 O O   . GLN H 39  ? 1.3987 1.5148 1.2635 -0.1835 -0.0018 0.0126  39  GLN L O   
11723 C CB  . GLN H 39  ? 1.2594 1.3774 1.2229 -0.1825 -0.0249 -0.0325 39  GLN L CB  
11724 C CG  . GLN H 39  ? 1.3127 1.4091 1.2978 -0.2034 -0.0356 -0.0101 39  GLN L CG  
11725 C CD  . GLN H 39  ? 1.4297 1.5138 1.4591 -0.1920 -0.0650 -0.0290 39  GLN L CD  
11726 O OE1 . GLN H 39  ? 1.3457 1.4376 1.3828 -0.1690 -0.0820 -0.0571 39  GLN L OE1 
11727 N NE2 . GLN H 39  ? 1.2947 1.3668 1.3561 -0.2065 -0.0742 -0.0146 39  GLN L NE2 
11728 N N   . LYS H 40  ? 1.3592 1.5397 1.2652 -0.2185 0.0306  0.0291  40  LYS L N   
11729 C CA  . LYS H 40  ? 1.4242 1.6129 1.2939 -0.2371 0.0400  0.0668  40  LYS L CA  
11730 C C   . LYS H 40  ? 1.5536 1.6888 1.4299 -0.2702 0.0206  0.0971  40  LYS L C   
11731 O O   . LYS H 40  ? 1.5328 1.6517 1.4539 -0.2767 0.0072  0.0859  40  LYS L O   
11732 C CB  . LYS H 40  ? 1.4379 1.7118 1.3078 -0.2456 0.0707  0.0708  40  LYS L CB  
11733 C CG  . LYS H 40  ? 1.4359 1.7556 1.2760 -0.2089 0.0769  0.0495  40  LYS L CG  
11734 C CD  . LYS H 40  ? 1.4427 1.8448 1.2919 -0.2043 0.0941  0.0279  40  LYS L CD  
11735 C CE  . LYS H 40  ? 1.4742 1.9214 1.2875 -0.1634 0.0878  0.0061  40  LYS L CE  
11736 N NZ  . LYS H 40  ? 1.6378 2.1457 1.4156 -0.1602 0.0984  0.0338  40  LYS L NZ  
11737 N N   . PRO H 41  ? 1.6001 1.6999 1.4297 -0.2887 0.0123  0.1346  41  PRO L N   
11738 C CA  . PRO H 41  ? 1.6666 1.6993 1.4941 -0.3231 -0.0181 0.1647  41  PRO L CA  
11739 C C   . PRO H 41  ? 1.7206 1.7895 1.5948 -0.3635 -0.0060 0.1840  41  PRO L C   
11740 O O   . PRO H 41  ? 1.7207 1.8663 1.5957 -0.3864 0.0304  0.2020  41  PRO L O   
11741 C CB  . PRO H 41  ? 1.7808 1.7765 1.5371 -0.3376 -0.0227 0.2039  41  PRO L CB  
11742 C CG  . PRO H 41  ? 1.8108 1.8365 1.5377 -0.2944 -0.0050 0.1817  41  PRO L CG  
11743 C CD  . PRO H 41  ? 1.6647 1.7782 1.4377 -0.2772 0.0248  0.1515  41  PRO L CD  
11744 N N   . GLY H 42  ? 1.6660 1.6871 1.5811 -0.3667 -0.0396 0.1748  42  GLY L N   
11745 C CA  . GLY H 42  ? 1.6535 1.6953 1.6229 -0.3985 -0.0373 0.1866  42  GLY L CA  
11746 C C   . GLY H 42  ? 1.5941 1.7224 1.6125 -0.3824 0.0027  0.1517  42  GLY L C   
11747 O O   . GLY H 42  ? 1.5957 1.7794 1.6419 -0.4123 0.0270  0.1627  42  GLY L O   
11748 N N   . GLN H 43  ? 1.4575 1.5969 1.4817 -0.3365 0.0073  0.1078  43  GLN L N   
11749 C CA  . GLN H 43  ? 1.3755 1.5777 1.4306 -0.3146 0.0365  0.0689  43  GLN L CA  
11750 C C   . GLN H 43  ? 1.3792 1.5555 1.4601 -0.2752 0.0184  0.0290  43  GLN L C   
11751 O O   . GLN H 43  ? 1.3933 1.5285 1.4545 -0.2582 -0.0068 0.0252  43  GLN L O   
11752 C CB  . GLN H 43  ? 1.3795 1.6410 1.3911 -0.3035 0.0668  0.0621  43  GLN L CB  
11753 C CG  . GLN H 43  ? 1.5735 1.9088 1.5734 -0.3344 0.0956  0.0852  43  GLN L CG  
11754 C CD  . GLN H 43  ? 1.8683 2.2722 1.8272 -0.3101 0.1159  0.0691  43  GLN L CD  
11755 O OE1 . GLN H 43  ? 1.8067 2.2245 1.7646 -0.2742 0.1160  0.0270  43  GLN L OE1 
11756 N NE2 . GLN H 43  ? 1.8026 2.2519 1.7242 -0.3283 0.1289  0.1027  43  GLN L NE2 
11757 N N   . ALA H 44  ? 1.2730 1.4796 1.3942 -0.2600 0.0320  -0.0032 44  ALA L N   
11758 C CA  . ALA H 44  ? 1.2099 1.4060 1.3538 -0.2251 0.0211  -0.0398 44  ALA L CA  
11759 C C   . ALA H 44  ? 1.2194 1.4286 1.3198 -0.2074 0.0315  -0.0568 44  ALA L C   
11760 O O   . ALA H 44  ? 1.2356 1.4742 1.3000 -0.2134 0.0512  -0.0522 44  ALA L O   
11761 C CB  . ALA H 44  ? 1.1771 1.3981 1.3650 -0.2142 0.0356  -0.0682 44  ALA L CB  
11762 N N   . PRO H 45  ? 1.1251 1.3202 1.2285 -0.1857 0.0155  -0.0766 45  PRO L N   
11763 C CA  . PRO H 45  ? 1.1064 1.3101 1.1704 -0.1757 0.0213  -0.0890 45  PRO L CA  
11764 C C   . PRO H 45  ? 1.1105 1.3378 1.1576 -0.1690 0.0403  -0.1110 45  PRO L C   
11765 O O   . PRO H 45  ? 1.0778 1.3163 1.1479 -0.1659 0.0506  -0.1272 45  PRO L O   
11766 C CB  . PRO H 45  ? 1.1084 1.3041 1.1884 -0.1609 0.0000  -0.1050 45  PRO L CB  
11767 C CG  . PRO H 45  ? 1.1753 1.3544 1.2907 -0.1581 -0.0247 -0.0981 45  PRO L CG  
11768 C CD  . PRO H 45  ? 1.1233 1.3024 1.2653 -0.1693 -0.0124 -0.0883 45  PRO L CD  
11769 N N   . ARG H 46  ? 1.0723 1.3025 1.0759 -0.1631 0.0389  -0.1151 46  ARG L N   
11770 C CA  . ARG H 46  ? 1.0696 1.3118 1.0413 -0.1523 0.0423  -0.1385 46  ARG L CA  
11771 C C   . ARG H 46  ? 1.1093 1.3287 1.0602 -0.1466 0.0254  -0.1504 46  ARG L C   
11772 O O   . ARG H 46  ? 1.1098 1.3205 1.0566 -0.1492 0.0153  -0.1378 46  ARG L O   
11773 C CB  . ARG H 46  ? 1.1289 1.4007 1.0624 -0.1485 0.0464  -0.1297 46  ARG L CB  
11774 C CG  . ARG H 46  ? 1.3104 1.6112 1.2135 -0.1330 0.0460  -0.1599 46  ARG L CG  
11775 C CD  . ARG H 46  ? 1.4882 1.8485 1.3954 -0.1392 0.0654  -0.1552 46  ARG L CD  
11776 N NE  . ARG H 46  ? 1.8172 2.2071 1.7070 -0.1446 0.0697  -0.1226 46  ARG L NE  
11777 C CZ  . ARG H 46  ? 2.2073 2.6382 2.0540 -0.1227 0.0603  -0.1286 46  ARG L CZ  
11778 N NH1 . ARG H 46  ? 2.1292 2.5723 1.9426 -0.0943 0.0398  -0.1682 46  ARG L NH1 
11779 N NH2 . ARG H 46  ? 2.1189 2.5763 1.9512 -0.1251 0.0661  -0.0968 46  ARG L NH2 
11780 N N   . LEU H 47  ? 1.5714 1.4386 0.7927 -0.2851 0.0904  -0.1987 47  LEU L N   
11781 C CA  . LEU H 47  ? 1.5571 1.4311 0.8257 -0.2786 0.0939  -0.1996 47  LEU L CA  
11782 C C   . LEU H 47  ? 1.5595 1.4620 0.9010 -0.2458 0.0776  -0.1999 47  LEU L C   
11783 O O   . LEU H 47  ? 1.5437 1.4673 0.9069 -0.2442 0.0635  -0.1802 47  LEU L O   
11784 C CB  . LEU H 47  ? 1.5920 1.4636 0.8365 -0.3213 0.0893  -0.1718 47  LEU L CB  
11785 C CG  . LEU H 47  ? 1.6499 1.5216 0.9301 -0.3217 0.0949  -0.1735 47  LEU L CG  
11786 C CD1 . LEU H 47  ? 1.6962 1.5234 0.9406 -0.3323 0.1314  -0.1949 47  LEU L CD1 
11787 C CD2 . LEU H 47  ? 1.6915 1.5737 0.9670 -0.3577 0.0742  -0.1385 47  LEU L CD2 
11788 N N   . LEU H 48  ? 1.4979 1.3959 0.8755 -0.2220 0.0826  -0.2198 48  LEU L N   
11789 C CA  . LEU H 48  ? 1.4720 1.3778 0.8979 -0.1987 0.0715  -0.2224 48  LEU L CA  
11790 C C   . LEU H 48  ? 1.5304 1.4478 0.9911 -0.2032 0.0711  -0.2134 48  LEU L C   
11791 O O   . LEU H 48  ? 1.5276 1.4555 1.0144 -0.2010 0.0650  -0.1968 48  LEU L O   
11792 C CB  . LEU H 48  ? 1.4648 1.3521 0.8970 -0.1783 0.0693  -0.2462 48  LEU L CB  
11793 C CG  . LEU H 48  ? 1.5305 1.3993 0.9252 -0.1730 0.0709  -0.2607 48  LEU L CG  
11794 C CD1 . LEU H 48  ? 1.5363 1.3949 0.9467 -0.1618 0.0713  -0.2743 48  LEU L CD1 
11795 C CD2 . LEU H 48  ? 1.5699 1.4228 0.9523 -0.1643 0.0619  -0.2653 48  LEU L CD2 
11796 N N   . ILE H 49  ? 1.4823 1.3950 0.9477 -0.2074 0.0814  -0.2243 49  ILE L N   
11797 C CA  . ILE H 49  ? 1.4737 1.3938 0.9663 -0.2140 0.0836  -0.2202 49  ILE L CA  
11798 C C   . ILE H 49  ? 1.5837 1.4909 1.0463 -0.2409 0.1027  -0.2182 49  ILE L C   
11799 O O   . ILE H 49  ? 1.6034 1.4914 1.0428 -0.2437 0.1227  -0.2292 49  ILE L O   
11800 C CB  . ILE H 49  ? 1.4915 1.4126 1.0234 -0.1966 0.0800  -0.2337 49  ILE L CB  
11801 C CG1 . ILE H 49  ? 1.4867 1.3975 1.0228 -0.1809 0.0635  -0.2367 49  ILE L CG1 
11802 C CG2 . ILE H 49  ? 1.4989 1.4278 1.0563 -0.2053 0.0835  -0.2308 49  ILE L CG2 
11803 C CD1 . ILE H 49  ? 1.5681 1.4726 1.1057 -0.1795 0.0611  -0.2237 49  ILE L CD1 
11804 N N   . PHE H 50  ? 1.5658 1.4740 1.0212 -0.2638 0.0992  -0.2027 50  PHE L N   
11805 C CA  . PHE H 50  ? 1.6072 1.4871 1.0203 -0.2998 0.1176  -0.2001 50  PHE L CA  
11806 C C   . PHE H 50  ? 1.6512 1.5352 1.0963 -0.3017 0.1191  -0.2028 50  PHE L C   
11807 O O   . PHE H 50  ? 1.6161 1.5253 1.1024 -0.2819 0.1007  -0.1983 50  PHE L O   
11808 C CB  . PHE H 50  ? 1.6620 1.5331 1.0222 -0.3375 0.1028  -0.1725 50  PHE L CB  
11809 C CG  . PHE H 50  ? 1.6666 1.5660 1.0579 -0.3423 0.0734  -0.1435 50  PHE L CG  
11810 C CD1 . PHE H 50  ? 1.6683 1.6025 1.1073 -0.3136 0.0552  -0.1296 50  PHE L CD1 
11811 C CD2 . PHE H 50  ? 1.7240 1.6081 1.0963 -0.3767 0.0679  -0.1285 50  PHE L CD2 
11812 C CE1 . PHE H 50  ? 1.6737 1.6312 1.1527 -0.3139 0.0364  -0.0983 50  PHE L CE1 
11813 C CE2 . PHE H 50  ? 1.7487 1.6595 1.1576 -0.3788 0.0409  -0.0971 50  PHE L CE2 
11814 C CZ  . PHE H 50  ? 1.6864 1.6357 1.1538 -0.3451 0.0272  -0.0805 50  PHE L CZ  
11815 N N   . ALA H 51  ? 1.6438 1.4950 1.0643 -0.3268 0.1461  -0.2116 51  ALA L N   
11816 C CA  . ALA H 51  ? 1.6463 1.4952 1.0905 -0.3329 0.1526  -0.2177 51  ALA L CA  
11817 C C   . ALA H 51  ? 1.6596 1.5403 1.1758 -0.2968 0.1512  -0.2313 51  ALA L C   
11818 O O   . ALA H 51  ? 1.6482 1.5371 1.1871 -0.2980 0.1462  -0.2331 51  ALA L O   
11819 C CB  . ALA H 51  ? 1.6613 1.5158 1.0919 -0.3527 0.1252  -0.1964 51  ALA L CB  
11820 N N   . GLY H 52  ? 1.5996 1.4943 1.1451 -0.2702 0.1530  -0.2383 52  GLY L N   
11821 C CA  . GLY H 52  ? 1.5707 1.4922 1.1799 -0.2443 0.1450  -0.2441 52  GLY L CA  
11822 C C   . GLY H 52  ? 1.6103 1.5504 1.2315 -0.2277 0.1108  -0.2388 52  GLY L C   
11823 O O   . GLY H 52  ? 1.5823 1.5316 1.2287 -0.2108 0.0980  -0.2405 52  GLY L O   
11824 N N   . SER H 53  ? 1.6008 1.5386 1.2016 -0.2350 0.0983  -0.2303 53  SER L N   
11825 C CA  . SER H 53  ? 1.6064 1.5445 1.2100 -0.2218 0.0787  -0.2248 53  SER L CA  
11826 C C   . SER H 53  ? 1.6528 1.5853 1.2348 -0.2197 0.0732  -0.2092 53  SER L C   
11827 O O   . SER H 53  ? 1.6458 1.5671 1.2270 -0.2058 0.0679  -0.2061 53  SER L O   
11828 C CB  . SER H 53  ? 1.6943 1.6315 1.3105 -0.2272 0.0754  -0.2258 53  SER L CB  
11829 O OG  . SER H 53  ? 1.9025 1.8367 1.5065 -0.2435 0.0834  -0.2212 53  SER L OG  
11830 N N   . SER H 54  ? 1.6076 1.5432 1.1727 -0.2374 0.0757  -0.1957 54  SER L N   
11831 C CA  . SER H 54  ? 1.5927 1.5341 1.1544 -0.2394 0.0668  -0.1699 54  SER L CA  
11832 C C   . SER H 54  ? 1.6010 1.5454 1.1572 -0.2270 0.0645  -0.1686 54  SER L C   
11833 O O   . SER H 54  ? 1.6011 1.5421 1.1342 -0.2328 0.0687  -0.1806 54  SER L O   
11834 C CB  . SER H 54  ? 1.6448 1.5861 1.1837 -0.2724 0.0619  -0.1510 54  SER L CB  
11835 O OG  . SER H 54  ? 1.7117 1.6420 1.2461 -0.2875 0.0667  -0.1578 54  SER L OG  
11836 N N   . ARG H 55  ? 1.5223 1.4664 1.0981 -0.2096 0.0635  -0.1549 55  ARG L N   
11837 C CA  . ARG H 55  ? 1.4993 1.4420 1.0708 -0.1981 0.0642  -0.1541 55  ARG L CA  
11838 C C   . ARG H 55  ? 1.5105 1.4766 1.0792 -0.2164 0.0545  -0.1257 55  ARG L C   
11839 O O   . ARG H 55  ? 1.5118 1.4948 1.1043 -0.2284 0.0463  -0.0935 55  ARG L O   
11840 C CB  . ARG H 55  ? 1.5087 1.4292 1.0998 -0.1760 0.0764  -0.1505 55  ARG L CB  
11841 C CG  . ARG H 55  ? 1.6086 1.5047 1.1786 -0.1641 0.0812  -0.1691 55  ARG L CG  
11842 C CD  . ARG H 55  ? 1.6963 1.5544 1.2756 -0.1486 0.1030  -0.1634 55  ARG L CD  
11843 N NE  . ARG H 55  ? 1.7995 1.6135 1.3598 -0.1485 0.1123  -0.1767 55  ARG L NE  
11844 C CZ  . ARG H 55  ? 2.0074 1.7964 1.5816 -0.1429 0.1343  -0.1616 55  ARG L CZ  
11845 N NH1 . ARG H 55  ? 1.8289 1.6394 1.4527 -0.1326 0.1487  -0.1288 55  ARG L NH1 
11846 N NH2 . ARG H 55  ? 1.9010 1.6414 1.4400 -0.1499 0.1422  -0.1751 55  ARG L NH2 
11847 N N   . ALA H 56  ? 1.4397 1.4050 0.9769 -0.2220 0.0528  -0.1339 56  ALA L N   
11848 C CA  . ALA H 56  ? 1.4450 1.4273 0.9638 -0.2483 0.0407  -0.1063 56  ALA L CA  
11849 C C   . ALA H 56  ? 1.5023 1.5114 1.0706 -0.2417 0.0333  -0.0680 56  ALA L C   
11850 O O   . ALA H 56  ? 1.4869 1.4914 1.0996 -0.2119 0.0471  -0.0679 56  ALA L O   
11851 C CB  . ALA H 56  ? 1.4619 1.4284 0.9256 -0.2556 0.0457  -0.1276 56  ALA L CB  
11852 N N   . THR H 57  ? 1.4886 1.5204 1.0471 -0.2742 0.0137  -0.0318 57  THR L N   
11853 C CA  . THR H 57  ? 1.4868 1.5565 1.1031 -0.2771 0.0007  0.0183  57  THR L CA  
11854 C C   . THR H 57  ? 1.5230 1.5919 1.1550 -0.2495 0.0167  0.0065  57  THR L C   
11855 O O   . THR H 57  ? 1.5247 1.5902 1.1060 -0.2648 0.0113  -0.0029 57  THR L O   
11856 C CB  . THR H 57  ? 1.6223 1.7102 1.2046 -0.3326 -0.0321 0.0605  57  THR L CB  
11857 O OG1 . THR H 57  ? 1.6242 1.6861 1.1546 -0.3645 -0.0390 0.0532  57  THR L OG1 
11858 C CG2 . THR H 57  ? 1.6197 1.7585 1.2856 -0.3420 -0.0555 0.1289  57  THR L CG2 
11859 N N   . GLY H 58  ? 1.4774 1.5384 1.1687 -0.2121 0.0408  0.0048  58  GLY L N   
11860 C CA  . GLY H 58  ? 1.4796 1.5245 1.1844 -0.1872 0.0637  -0.0079 58  GLY L CA  
11861 C C   . GLY H 58  ? 1.5483 1.5417 1.1859 -0.1734 0.0776  -0.0669 58  GLY L C   
11862 O O   . GLY H 58  ? 1.5441 1.5277 1.1397 -0.1769 0.0763  -0.0856 58  GLY L O   
11863 N N   . ILE H 59  ? 1.5210 1.4808 1.1475 -0.1607 0.0881  -0.0933 59  ILE L N   
11864 C CA  . ILE H 59  ? 1.5290 1.4406 1.1014 -0.1518 0.0944  -0.1408 59  ILE L CA  
11865 C C   . ILE H 59  ? 1.6451 1.5070 1.2301 -0.1342 0.1203  -0.1493 59  ILE L C   
11866 O O   . ILE H 59  ? 1.6494 1.5168 1.2694 -0.1310 0.1277  -0.1302 59  ILE L O   
11867 C CB  . ILE H 59  ? 1.5514 1.4696 1.0875 -0.1657 0.0768  -0.1605 59  ILE L CB  
11868 C CG1 . ILE H 59  ? 1.5516 1.4934 1.0519 -0.1878 0.0630  -0.1565 59  ILE L CG1 
11869 C CG2 . ILE H 59  ? 1.5618 1.4398 1.0662 -0.1571 0.0779  -0.1973 59  ILE L CG2 
11870 C CD1 . ILE H 59  ? 1.6357 1.5627 1.0915 -0.1869 0.0640  -0.1747 59  ILE L CD1 
11871 N N   . PRO H 60  ? 1.6565 1.4599 1.2031 -0.1276 0.1358  -0.1768 60  PRO L N   
11872 C CA  . PRO H 60  ? 1.7101 1.4456 1.2472 -0.1209 0.1657  -0.1839 60  PRO L CA  
11873 C C   . PRO H 60  ? 1.8053 1.5202 1.3173 -0.1296 0.1556  -0.1966 60  PRO L C   
11874 O O   . PRO H 60  ? 1.7782 1.5237 1.2768 -0.1387 0.1253  -0.2086 60  PRO L O   
11875 C CB  . PRO H 60  ? 1.7673 1.4371 1.2494 -0.1233 0.1782  -0.2121 60  PRO L CB  
11876 C CG  . PRO H 60  ? 1.7887 1.4923 1.2423 -0.1304 0.1444  -0.2291 60  PRO L CG  
11877 C CD  . PRO H 60  ? 1.6831 1.4682 1.1827 -0.1307 0.1288  -0.2018 60  PRO L CD  
11878 N N   . ASP H 61  ? 1.8254 1.4824 1.3303 -0.1279 0.1862  -0.1926 61  ASP L N   
11879 C CA  . ASP H 61  ? 1.8569 1.4814 1.3314 -0.1399 0.1833  -0.2004 61  ASP L CA  
11880 C C   . ASP H 61  ? 1.9232 1.5207 1.3378 -0.1609 0.1523  -0.2283 61  ASP L C   
11881 O O   . ASP H 61  ? 1.9212 1.5280 1.3296 -0.1725 0.1344  -0.2298 61  ASP L O   
11882 C CB  . ASP H 61  ? 1.9550 1.4972 1.4119 -0.1380 0.2330  -0.1925 61  ASP L CB  
11883 C CG  . ASP H 61  ? 2.1399 1.7145 1.6735 -0.1163 0.2622  -0.1555 61  ASP L CG  
11884 O OD1 . ASP H 61  ? 2.1123 1.7508 1.7117 -0.1020 0.2570  -0.1325 61  ASP L OD1 
11885 O OD2 . ASP H 61  ? 2.2831 1.8166 1.8098 -0.1161 0.2896  -0.1461 61  ASP L OD2 
11886 N N   . ARG H 62  ? 1.8934 1.4579 1.2682 -0.1671 0.1448  -0.2468 62  ARG L N   
11887 C CA  . ARG H 62  ? 1.9091 1.4475 1.2347 -0.1882 0.1108  -0.2661 62  ARG L CA  
11888 C C   . ARG H 62  ? 1.9162 1.5353 1.2825 -0.1853 0.0736  -0.2646 62  ARG L C   
11889 O O   . ARG H 62  ? 1.9267 1.5404 1.2825 -0.2020 0.0483  -0.2664 62  ARG L O   
11890 C CB  . ARG H 62  ? 1.9153 1.3994 1.1905 -0.1950 0.1114  -0.2842 62  ARG L CB  
11891 C CG  . ARG H 62  ? 1.8992 1.4332 1.2065 -0.1740 0.1155  -0.2848 62  ARG L CG  
11892 C CD  . ARG H 62  ? 1.9615 1.4217 1.2139 -0.1808 0.1326  -0.3023 62  ARG L CD  
11893 N NE  . ARG H 62  ? 1.9596 1.4656 1.2283 -0.1669 0.1269  -0.3064 62  ARG L NE  
11894 C CZ  . ARG H 62  ? 2.1202 1.6295 1.4105 -0.1543 0.1575  -0.2991 62  ARG L CZ  
11895 N NH1 . ARG H 62  ? 2.0087 1.4800 1.3198 -0.1485 0.2012  -0.2852 62  ARG L NH1 
11896 N NH2 . ARG H 62  ? 1.8946 1.4444 1.1890 -0.1480 0.1473  -0.3024 62  ARG L NH2 
11897 N N   . PHE H 63  ? 1.8281 1.5159 1.2394 -0.1682 0.0733  -0.2578 63  PHE L N   
11898 C CA  . PHE H 63  ? 1.7921 1.5425 1.2359 -0.1663 0.0529  -0.2567 63  PHE L CA  
11899 C C   . PHE H 63  ? 1.8564 1.6377 1.3333 -0.1695 0.0539  -0.2448 63  PHE L C   
11900 O O   . PHE H 63  ? 1.8518 1.6463 1.3473 -0.1646 0.0701  -0.2303 63  PHE L O   
11901 C CB  . PHE H 63  ? 1.7822 1.5728 1.2373 -0.1570 0.0578  -0.2534 63  PHE L CB  
11902 C CG  . PHE H 63  ? 1.8097 1.5769 1.2300 -0.1545 0.0546  -0.2679 63  PHE L CG  
11903 C CD1 . PHE H 63  ? 1.8413 1.6145 1.2504 -0.1551 0.0383  -0.2800 63  PHE L CD1 
11904 C CD2 . PHE H 63  ? 1.8532 1.5923 1.2566 -0.1504 0.0715  -0.2676 63  PHE L CD2 
11905 C CE1 . PHE H 63  ? 1.8642 1.6123 1.2353 -0.1533 0.0349  -0.2942 63  PHE L CE1 
11906 C CE2 . PHE H 63  ? 1.9020 1.6164 1.2673 -0.1500 0.0692  -0.2837 63  PHE L CE2 
11907 C CZ  . PHE H 63  ? 1.8721 1.5902 1.2164 -0.1522 0.0489  -0.2980 63  PHE L CZ  
11908 N N   . SER H 64  ? 1.8236 1.6177 1.3132 -0.1784 0.0359  -0.2478 64  SER L N   
11909 C CA  . SER H 64  ? 1.8181 1.6385 1.3362 -0.1841 0.0366  -0.2400 64  SER L CA  
11910 C C   . SER H 64  ? 1.8513 1.7135 1.4081 -0.1857 0.0264  -0.2413 64  SER L C   
11911 O O   . SER H 64  ? 1.8580 1.7206 1.4234 -0.1855 0.0114  -0.2444 64  SER L O   
11912 C CB  . SER H 64  ? 1.9145 1.6910 1.4065 -0.1990 0.0334  -0.2379 64  SER L CB  
11913 O OG  . SER H 64  ? 2.0753 1.8244 1.5469 -0.2151 0.0086  -0.2414 64  SER L OG  
11914 N N   . GLY H 65  ? 1.7904 1.6819 1.3726 -0.1885 0.0370  -0.2368 65  GLY L N   
11915 C CA  . GLY H 65  ? 1.7754 1.6979 1.3978 -0.1904 0.0407  -0.2377 65  GLY L CA  
11916 C C   . GLY H 65  ? 1.8295 1.7633 1.4806 -0.2012 0.0357  -0.2334 65  GLY L C   
11917 O O   . GLY H 65  ? 1.8349 1.7600 1.4694 -0.2085 0.0397  -0.2314 65  GLY L O   
11918 N N   . LYS H 66  ? 1.7809 1.7359 1.4807 -0.2023 0.0275  -0.2286 66  LYS L N   
11919 C CA  . LYS H 66  ? 1.7830 1.7568 1.5223 -0.2148 0.0204  -0.2205 66  LYS L CA  
11920 C C   . LYS H 66  ? 1.8159 1.8242 1.6266 -0.2090 0.0408  -0.2163 66  LYS L C   
11921 O O   . LYS H 66  ? 1.8039 1.8169 1.6358 -0.1955 0.0520  -0.2158 66  LYS L O   
11922 C CB  . LYS H 66  ? 1.8425 1.8046 1.5802 -0.2291 -0.0167 -0.2075 66  LYS L CB  
11923 C CG  . LYS H 66  ? 2.0346 1.9422 1.6927 -0.2407 -0.0274 -0.2117 66  LYS L CG  
11924 C CD  . LYS H 66  ? 2.1959 2.0765 1.8348 -0.2686 -0.0639 -0.1970 66  LYS L CD  
11925 C CE  . LYS H 66  ? 2.3616 2.1683 1.9080 -0.2871 -0.0617 -0.2021 66  LYS L CE  
11926 N NZ  . LYS H 66  ? 2.5041 2.2726 2.0128 -0.3282 -0.0954 -0.1857 66  LYS L NZ  
11927 N N   . THR H 67  ? 1.7790 1.8052 1.6251 -0.2191 0.0519  -0.2138 67  THR L N   
11928 C CA  . THR H 67  ? 1.7809 1.8333 1.7036 -0.2146 0.0813  -0.2084 67  THR L CA  
11929 C C   . THR H 67  ? 1.8524 1.9287 1.8212 -0.2296 0.0773  -0.1998 67  THR L C   
11930 O O   . THR H 67  ? 1.8613 1.9222 1.7813 -0.2441 0.0745  -0.2097 67  THR L O   
11931 C CB  . THR H 67  ? 1.8776 1.9063 1.7743 -0.2128 0.1299  -0.2245 67  THR L CB  
11932 O OG1 . THR H 67  ? 1.8915 1.8929 1.7150 -0.2101 0.1268  -0.2338 67  THR L OG1 
11933 C CG2 . THR H 67  ? 1.8492 1.8852 1.8152 -0.2012 0.1697  -0.2182 67  THR L CG2 
11934 N N   . SER H 68  ? 1.8044 1.9196 1.8729 -0.2259 0.0786  -0.1783 68  SER L N   
11935 C CA  . SER H 68  ? 1.8042 1.9523 1.9381 -0.2404 0.0758  -0.1639 68  SER L CA  
11936 C C   . SER H 68  ? 1.8613 2.0516 2.1253 -0.2262 0.0989  -0.1385 68  SER L C   
11937 O O   . SER H 68  ? 1.8513 2.0705 2.1765 -0.2188 0.0689  -0.1097 68  SER L O   
11938 C CB  . SER H 68  ? 1.8518 2.0073 1.9625 -0.2635 0.0187  -0.1470 68  SER L CB  
11939 O OG  . SER H 68  ? 1.9658 2.1274 2.0906 -0.2624 -0.0210 -0.1252 68  SER L OG  
11940 N N   . GLY H 69  ? 1.8404 2.0273 2.1445 -0.2235 0.1555  -0.1481 69  GLY L N   
11941 C CA  . GLY H 69  ? 1.8496 2.0670 2.2847 -0.2071 0.1975  -0.1249 69  GLY L CA  
11942 C C   . GLY H 69  ? 1.9233 2.1058 2.3553 -0.1838 0.2481  -0.1333 69  GLY L C   
11943 O O   . GLY H 69  ? 1.9458 2.0756 2.3308 -0.1870 0.3102  -0.1595 69  GLY L O   
11944 N N   . THR H 70  ? 1.8746 2.0782 2.3474 -0.1651 0.2217  -0.1102 70  THR L N   
11945 C CA  . THR H 70  ? 1.8880 2.0584 2.3552 -0.1420 0.2650  -0.1149 70  THR L CA  
11946 C C   . THR H 70  ? 1.9111 2.0858 2.3392 -0.1338 0.2087  -0.1076 70  THR L C   
11947 O O   . THR H 70  ? 1.9273 2.0793 2.3521 -0.1144 0.2348  -0.1080 70  THR L O   
11948 C CB  . THR H 70  ? 2.0069 2.1983 2.6219 -0.1191 0.3240  -0.0846 70  THR L CB  
11949 O OG1 . THR H 70  ? 1.9851 2.2207 2.7031 -0.1276 0.3309  -0.0645 70  THR L OG1 
11950 C CG2 . THR H 70  ? 2.0321 2.1494 2.6039 -0.1102 0.4157  -0.1086 70  THR L CG2 
11951 N N   . ASP H 71  ? 1.8343 2.0265 2.2206 -0.1516 0.1371  -0.1033 71  ASP L N   
11952 C CA  . ASP H 71  ? 1.8239 2.0119 2.1695 -0.1516 0.0814  -0.0958 71  ASP L CA  
11953 C C   . ASP H 71  ? 1.8557 1.9892 2.0743 -0.1472 0.0904  -0.1312 71  ASP L C   
11954 O O   . ASP H 71  ? 1.8591 1.9811 2.0767 -0.1310 0.0928  -0.1281 71  ASP L O   
11955 C CB  . ASP H 71  ? 1.8526 2.0590 2.1842 -0.1803 0.0116  -0.0788 71  ASP L CB  
11956 C CG  . ASP H 71  ? 1.9895 2.2572 2.4552 -0.1889 -0.0095 -0.0328 71  ASP L CG  
11957 O OD1 . ASP H 71  ? 2.0186 2.3153 2.5568 -0.1886 -0.0485 0.0063  71  ASP L OD1 
11958 O OD2 . ASP H 71  ? 2.0367 2.3248 2.5423 -0.1960 0.0151  -0.0332 71  ASP L OD2 
11959 N N   . PHE H 72  ? 1.7905 1.8934 1.9097 -0.1618 0.0933  -0.1602 72  PHE L N   
11960 C CA  . PHE H 72  ? 1.7804 1.8397 1.7893 -0.1615 0.0994  -0.1873 72  PHE L CA  
11961 C C   . PHE H 72  ? 1.7751 1.8210 1.7406 -0.1587 0.0562  -0.1859 72  PHE L C   
11962 O O   . PHE H 72  ? 1.7679 1.8154 1.7617 -0.1444 0.0550  -0.1766 72  PHE L O   
11963 C CB  . PHE H 72  ? 1.8308 1.8613 1.8204 -0.1528 0.1590  -0.2010 72  PHE L CB  
11964 C CG  . PHE H 72  ? 1.8740 1.8641 1.7539 -0.1609 0.1663  -0.2230 72  PHE L CG  
11965 C CD1 . PHE H 72  ? 1.9180 1.9003 1.7371 -0.1771 0.1469  -0.2326 72  PHE L CD1 
11966 C CD2 . PHE H 72  ? 1.9332 1.8926 1.7743 -0.1542 0.1955  -0.2301 72  PHE L CD2 
11967 C CE1 . PHE H 72  ? 1.9413 1.8952 1.6769 -0.1860 0.1507  -0.2435 72  PHE L CE1 
11968 C CE2 . PHE H 72  ? 1.9831 1.9098 1.7263 -0.1676 0.1983  -0.2443 72  PHE L CE2 
11969 C CZ  . PHE H 72  ? 1.9488 1.8774 1.6471 -0.1834 0.1740  -0.2483 72  PHE L CZ  
11970 N N   . THR H 73  ? 1.6999 1.7244 1.5922 -0.1730 0.0269  -0.1961 73  THR L N   
11971 C CA  . THR H 73  ? 1.6926 1.6894 1.5314 -0.1777 -0.0099 -0.1974 73  THR L CA  
11972 C C   . THR H 73  ? 1.7020 1.6616 1.4515 -0.1762 -0.0008 -0.2191 73  THR L C   
11973 O O   . THR H 73  ? 1.6747 1.6290 1.3939 -0.1806 0.0156  -0.2277 73  THR L O   
11974 C CB  . THR H 73  ? 1.8319 1.8235 1.6678 -0.2025 -0.0523 -0.1822 73  THR L CB  
11975 O OG1 . THR H 73  ? 1.8398 1.8759 1.7667 -0.2082 -0.0608 -0.1573 73  THR L OG1 
11976 C CG2 . THR H 73  ? 1.8560 1.8106 1.6481 -0.2159 -0.0921 -0.1764 73  THR L CG2 
11977 N N   . LEU H 74  ? 1.6672 1.6013 1.3798 -0.1716 -0.0146 -0.2243 74  LEU L N   
11978 C CA  . LEU H 74  ? 1.6705 1.5693 1.3086 -0.1702 -0.0099 -0.2404 74  LEU L CA  
11979 C C   . LEU H 74  ? 1.7472 1.6032 1.3455 -0.1852 -0.0428 -0.2392 74  LEU L C   
11980 O O   . LEU H 74  ? 1.7531 1.5984 1.3551 -0.1871 -0.0654 -0.2345 74  LEU L O   
11981 C CB  . LEU H 74  ? 1.6637 1.5607 1.2846 -0.1555 0.0094  -0.2500 74  LEU L CB  
11982 C CG  . LEU H 74  ? 1.7170 1.5903 1.2722 -0.1540 0.0204  -0.2630 74  LEU L CG  
11983 C CD1 . LEU H 74  ? 1.7404 1.5727 1.2512 -0.1575 -0.0006 -0.2705 74  LEU L CD1 
11984 C CD2 . LEU H 74  ? 1.7275 1.6095 1.2717 -0.1600 0.0357  -0.2602 74  LEU L CD2 
11985 N N   . THR H 75  ? 1.7275 1.5506 1.2829 -0.1989 -0.0430 -0.2418 75  THR L N   
11986 C CA  . THR H 75  ? 1.7818 1.5412 1.2782 -0.2222 -0.0648 -0.2419 75  THR L CA  
11987 C C   . THR H 75  ? 1.8631 1.5697 1.2943 -0.2187 -0.0418 -0.2577 75  THR L C   
11988 O O   . THR H 75  ? 1.8508 1.5673 1.2844 -0.2065 -0.0129 -0.2597 75  THR L O   
11989 C CB  . THR H 75  ? 1.9102 1.6555 1.4017 -0.2484 -0.0790 -0.2287 75  THR L CB  
11990 O OG1 . THR H 75  ? 1.8832 1.6917 1.4536 -0.2466 -0.0917 -0.2125 75  THR L OG1 
11991 C CG2 . THR H 75  ? 1.9637 1.6342 1.3869 -0.2860 -0.1089 -0.2228 75  THR L CG2 
11992 N N   . ILE H 76  ? 1.4548 1.8738 0.9491 -0.5120 -0.1718 -0.1036 76  ILE L N   
11993 C CA  . ILE H 76  ? 1.4798 1.8511 0.9471 -0.4962 -0.1446 -0.0981 76  ILE L CA  
11994 C C   . ILE H 76  ? 1.6419 1.9366 1.0208 -0.5332 -0.1285 -0.1025 76  ILE L C   
11995 O O   . ILE H 76  ? 1.6524 1.9607 1.0150 -0.5667 -0.1581 -0.1046 76  ILE L O   
11996 C CB  . ILE H 76  ? 1.4600 1.8716 0.9787 -0.4730 -0.1634 -0.0903 76  ILE L CB  
11997 C CG1 . ILE H 76  ? 1.3826 1.8626 0.9727 -0.4511 -0.1827 -0.0896 76  ILE L CG1 
11998 C CG2 . ILE H 76  ? 1.4910 1.8609 0.9930 -0.4515 -0.1324 -0.0784 76  ILE L CG2 
11999 C CD1 . ILE H 76  ? 1.3580 1.8766 0.9872 -0.4463 -0.2074 -0.0875 76  ILE L CD1 
12000 N N   . SER H 77  ? 1.6781 1.8909 0.9963 -0.5291 -0.0785 -0.1000 77  SER L N   
12001 C CA  . SER H 77  ? 1.7880 1.9029 1.0013 -0.5682 -0.0519 -0.1059 77  SER L CA  
12002 C C   . SER H 77  ? 1.8371 1.9305 1.0358 -0.5672 -0.0586 -0.0993 77  SER L C   
12003 O O   . SER H 77  ? 1.8649 1.9520 1.0239 -0.6082 -0.0856 -0.1060 77  SER L O   
12004 C CB  . SER H 77  ? 1.9287 1.9490 1.0760 -0.5603 0.0166  -0.1021 77  SER L CB  
12005 O OG  . SER H 77  ? 2.0497 2.0801 1.2466 -0.5045 0.0479  -0.0784 77  SER L OG  
12006 N N   . ARG H 78  ? 1.7499 1.8409 0.9856 -0.5211 -0.0364 -0.0826 78  ARG L N   
12007 C CA  . ARG H 78  ? 1.7416 1.8129 0.9735 -0.5113 -0.0382 -0.0742 78  ARG L CA  
12008 C C   . ARG H 78  ? 1.6524 1.8241 0.9882 -0.4786 -0.0772 -0.0676 78  ARG L C   
12009 O O   . ARG H 78  ? 1.5850 1.8001 0.9807 -0.4444 -0.0698 -0.0554 78  ARG L O   
12010 C CB  . ARG H 78  ? 1.8068 1.7859 0.9931 -0.4858 0.0264  -0.0541 78  ARG L CB  
12011 C CG  . ARG H 78  ? 2.0673 1.9140 1.1258 -0.5219 0.0775  -0.0608 78  ARG L CG  
12012 C CD  . ARG H 78  ? 2.2760 2.0306 1.2989 -0.4864 0.1510  -0.0323 78  ARG L CD  
12013 N NE  . ARG H 78  ? 2.5904 2.1975 1.4775 -0.5203 0.2145  -0.0384 78  ARG L NE  
12014 C CZ  . ARG H 78  ? 2.8508 2.3452 1.6792 -0.4954 0.2951  -0.0119 78  ARG L CZ  
12015 N NH1 . ARG H 78  ? 2.6291 2.1557 1.5335 -0.4351 0.3170  0.0274  78  ARG L NH1 
12016 N NH2 . ARG H 78  ? 2.7933 2.1393 1.4835 -0.5327 0.3581  -0.0211 78  ARG L NH2 
12017 N N   . LEU H 79  ? 1.5711 1.7799 0.9243 -0.4923 -0.1165 -0.0739 79  LEU L N   
12018 C CA  . LEU H 79  ? 1.4773 1.7651 0.9155 -0.4652 -0.1453 -0.0696 79  LEU L CA  
12019 C C   . LEU H 79  ? 1.5338 1.7941 0.9784 -0.4387 -0.1266 -0.0568 79  LEU L C   
12020 O O   . LEU H 79  ? 1.5741 1.7934 0.9807 -0.4487 -0.1258 -0.0572 79  LEU L O   
12021 C CB  . LEU H 79  ? 1.4486 1.7904 0.9090 -0.4849 -0.1867 -0.0751 79  LEU L CB  
12022 C CG  . LEU H 79  ? 1.4698 1.8722 0.9661 -0.4952 -0.2095 -0.0786 79  LEU L CG  
12023 C CD1 . LEU H 79  ? 1.4869 1.9194 0.9727 -0.5280 -0.2384 -0.0736 79  LEU L CD1 
12024 C CD2 . LEU H 79  ? 1.4190 1.8831 0.9928 -0.4644 -0.2192 -0.0769 79  LEU L CD2 
12025 N N   . GLU H 80  ? 1.4555 1.7391 0.9462 -0.4069 -0.1107 -0.0418 80  GLU L N   
12026 C CA  . GLU H 80  ? 1.4558 1.7263 0.9651 -0.3801 -0.0928 -0.0221 80  GLU L CA  
12027 C C   . GLU H 80  ? 1.4374 1.7697 1.0045 -0.3737 -0.1272 -0.0286 80  GLU L C   
12028 O O   . GLU H 80  ? 1.4012 1.7886 1.0002 -0.3832 -0.1559 -0.0429 80  GLU L O   
12029 C CB  . GLU H 80  ? 1.4669 1.7532 1.0073 -0.3530 -0.0635 0.0060  80  GLU L CB  
12030 C CG  . GLU H 80  ? 1.6839 1.8988 1.1661 -0.3516 -0.0148 0.0186  80  GLU L CG  
12031 C CD  . GLU H 80  ? 2.0015 2.1077 1.4104 -0.3490 0.0324  0.0314  80  GLU L CD  
12032 O OE1 . GLU H 80  ? 1.8688 1.9665 1.2999 -0.3230 0.0497  0.0573  80  GLU L OE1 
12033 O OE2 . GLU H 80  ? 1.9578 1.9818 1.2820 -0.3751 0.0558  0.0169  80  GLU L OE2 
12034 N N   . PRO H 81  ? 1.3780 1.6974 0.9574 -0.3570 -0.1202 -0.0177 81  PRO L N   
12035 C CA  . PRO H 81  ? 1.3280 1.6987 0.9562 -0.3526 -0.1467 -0.0261 81  PRO L CA  
12036 C C   . PRO H 81  ? 1.3451 1.7875 1.0289 -0.3515 -0.1638 -0.0284 81  PRO L C   
12037 O O   . PRO H 81  ? 1.3206 1.7967 1.0294 -0.3568 -0.1828 -0.0424 81  PRO L O   
12038 C CB  . PRO H 81  ? 1.3622 1.7032 0.9953 -0.3319 -0.1279 -0.0086 81  PRO L CB  
12039 C CG  . PRO H 81  ? 1.4867 1.7433 1.0553 -0.3310 -0.0948 0.0024  81  PRO L CG  
12040 C CD  . PRO H 81  ? 1.4463 1.6969 0.9934 -0.3403 -0.0823 0.0043  81  PRO L CD  
12041 N N   . GLU H 82  ? 1.2998 1.7609 0.9973 -0.3458 -0.1524 -0.0120 82  GLU L N   
12042 C CA  . GLU H 82  ? 1.2607 1.7855 0.9988 -0.3507 -0.1666 -0.0102 82  GLU L CA  
12043 C C   . GLU H 82  ? 1.2867 1.8290 1.0204 -0.3664 -0.1841 -0.0337 82  GLU L C   
12044 O O   . GLU H 82  ? 1.2680 1.8492 1.0254 -0.3753 -0.1984 -0.0421 82  GLU L O   
12045 C CB  . GLU H 82  ? 1.2904 1.8329 1.0410 -0.3392 -0.1467 0.0221  82  GLU L CB  
12046 C CG  . GLU H 82  ? 1.5425 2.0607 1.2968 -0.3174 -0.1180 0.0574  82  GLU L CG  
12047 C CD  . GLU H 82  ? 1.9792 2.4173 1.6823 -0.3042 -0.0787 0.0687  82  GLU L CD  
12048 O OE1 . GLU H 82  ? 2.0041 2.3829 1.6788 -0.2970 -0.0634 0.0699  82  GLU L OE1 
12049 O OE2 . GLU H 82  ? 1.9564 2.3847 1.6425 -0.3018 -0.0587 0.0773  82  GLU L OE2 
12050 N N   . ASP H 83  ? 1.2467 1.7558 0.9453 -0.3728 -0.1800 -0.0422 83  ASP L N   
12051 C CA  . ASP H 83  ? 1.2262 1.7504 0.9215 -0.3865 -0.1936 -0.0579 83  ASP L CA  
12052 C C   . ASP H 83  ? 1.2542 1.7987 0.9656 -0.3935 -0.2125 -0.0704 83  ASP L C   
12053 O O   . ASP H 83  ? 1.2314 1.7980 0.9540 -0.4001 -0.2212 -0.0771 83  ASP L O   
12054 C CB  . ASP H 83  ? 1.2863 1.7675 0.9344 -0.3971 -0.1820 -0.0597 83  ASP L CB  
12055 C CG  . ASP H 83  ? 1.4655 1.9180 1.0926 -0.3873 -0.1512 -0.0448 83  ASP L CG  
12056 O OD1 . ASP H 83  ? 1.4726 1.9265 1.1154 -0.3687 -0.1343 -0.0239 83  ASP L OD1 
12057 O OD2 . ASP H 83  ? 1.6100 2.0367 1.2039 -0.3979 -0.1400 -0.0501 83  ASP L OD2 
12058 N N   . PHE H 84  ? 1.2210 1.7570 0.9356 -0.3887 -0.2138 -0.0695 84  PHE L N   
12059 C CA  . PHE H 84  ? 1.2153 1.7709 0.9478 -0.3898 -0.2230 -0.0735 84  PHE L CA  
12060 C C   . PHE H 84  ? 1.2725 1.8515 1.0343 -0.3862 -0.2200 -0.0793 84  PHE L C   
12061 O O   . PHE H 84  ? 1.2725 1.8488 1.0438 -0.3813 -0.2136 -0.0807 84  PHE L O   
12062 C CB  . PHE H 84  ? 1.2505 1.7875 0.9731 -0.3849 -0.2220 -0.0688 84  PHE L CB  
12063 C CG  . PHE H 84  ? 1.3069 1.8146 0.9852 -0.3997 -0.2259 -0.0647 84  PHE L CG  
12064 C CD1 . PHE H 84  ? 1.3516 1.8816 1.0234 -0.4173 -0.2410 -0.0594 84  PHE L CD1 
12065 C CD2 . PHE H 84  ? 1.3681 1.8236 1.0065 -0.3996 -0.2110 -0.0625 84  PHE L CD2 
12066 C CE1 . PHE H 84  ? 1.4095 1.9103 1.0275 -0.4432 -0.2466 -0.0567 84  PHE L CE1 
12067 C CE2 . PHE H 84  ? 1.4565 1.8675 1.0352 -0.4213 -0.2086 -0.0618 84  PHE L CE2 
12068 C CZ  . PHE H 84  ? 1.4438 1.8778 1.0088 -0.4472 -0.2291 -0.0613 84  PHE L CZ  
12069 N N   . ALA H 85  ? 1.2365 1.8315 1.0057 -0.3919 -0.2217 -0.0829 85  ALA L N   
12070 C CA  . ALA H 85  ? 1.2389 1.8398 1.0187 -0.3946 -0.2132 -0.0900 85  ALA L CA  
12071 C C   . ALA H 85  ? 1.2929 1.9009 1.0807 -0.3944 -0.2089 -0.0875 85  ALA L C   
12072 O O   . ALA H 85  ? 1.2837 1.9043 1.0773 -0.3927 -0.2165 -0.0770 85  ALA L O   
12073 C CB  . ALA H 85  ? 1.2471 1.8548 1.0207 -0.4044 -0.2157 -0.0936 85  ALA L CB  
12074 N N   . VAL H 86  ? 1.2583 1.8556 1.0425 -0.3992 -0.1947 -0.0945 86  VAL L N   
12075 C CA  . VAL H 86  ? 1.2665 1.8601 1.0569 -0.3953 -0.1819 -0.0888 86  VAL L CA  
12076 C C   . VAL H 86  ? 1.3167 1.9165 1.0991 -0.4031 -0.1927 -0.0950 86  VAL L C   
12077 O O   . VAL H 86  ? 1.3185 1.9157 1.0840 -0.4152 -0.1973 -0.1058 86  VAL L O   
12078 C CB  . VAL H 86  ? 1.3511 1.9096 1.1290 -0.3960 -0.1495 -0.0921 86  VAL L CB  
12079 C CG1 . VAL H 86  ? 1.3652 1.9155 1.1556 -0.3830 -0.1267 -0.0751 86  VAL L CG1 
12080 C CG2 . VAL H 86  ? 1.3567 1.9050 1.1379 -0.3889 -0.1352 -0.0896 86  VAL L CG2 
12081 N N   . TYR H 87  ? 1.2704 1.8845 1.0672 -0.3972 -0.1971 -0.0843 87  TYR L N   
12082 C CA  . TYR H 87  ? 1.2690 1.8880 1.0606 -0.4014 -0.2046 -0.0893 87  TYR L CA  
12083 C C   . TYR H 87  ? 1.3431 1.9496 1.1401 -0.3963 -0.1881 -0.0847 87  TYR L C   
12084 O O   . TYR H 87  ? 1.3543 1.9680 1.1744 -0.3856 -0.1778 -0.0648 87  TYR L O   
12085 C CB  . TYR H 87  ? 1.2747 1.9117 1.0686 -0.4042 -0.2212 -0.0834 87  TYR L CB  
12086 C CG  . TYR H 87  ? 1.3096 1.9403 1.0846 -0.4084 -0.2280 -0.0897 87  TYR L CG  
12087 C CD1 . TYR H 87  ? 1.3428 1.9691 1.1152 -0.4076 -0.2302 -0.0861 87  TYR L CD1 
12088 C CD2 . TYR H 87  ? 1.3219 1.9495 1.0834 -0.4095 -0.2267 -0.0948 87  TYR L CD2 
12089 C CE1 . TYR H 87  ? 1.3568 1.9698 1.1120 -0.4078 -0.2300 -0.0875 87  TYR L CE1 
12090 C CE2 . TYR H 87  ? 1.3384 1.9577 1.0860 -0.4080 -0.2236 -0.0915 87  TYR L CE2 
12091 C CZ  . TYR H 87  ? 1.4155 2.0244 1.1591 -0.4072 -0.2248 -0.0879 87  TYR L CZ  
12092 O OH  . TYR H 87  ? 1.4106 2.0046 1.1406 -0.4024 -0.2162 -0.0802 87  TYR L OH  
12093 N N   . TYR H 88  ? 1.2953 1.8848 1.0713 -0.4036 -0.1838 -0.0983 88  TYR L N   
12094 C CA  . TYR H 88  ? 1.3076 1.8704 1.0768 -0.4002 -0.1639 -0.0970 88  TYR L CA  
12095 C C   . TYR H 88  ? 1.3276 1.9015 1.0982 -0.3991 -0.1738 -0.1009 88  TYR L C   
12096 O O   . TYR H 88  ? 1.2982 1.8898 1.0600 -0.4060 -0.1895 -0.1101 88  TYR L O   
12097 C CB  . TYR H 88  ? 1.3624 1.8821 1.0896 -0.4168 -0.1455 -0.1117 88  TYR L CB  
12098 C CG  . TYR H 88  ? 1.4085 1.8967 1.1262 -0.4165 -0.1199 -0.1080 88  TYR L CG  
12099 C CD1 . TYR H 88  ? 1.4715 1.9201 1.1897 -0.4016 -0.0813 -0.0925 88  TYR L CD1 
12100 C CD2 . TYR H 88  ? 1.4141 1.9081 1.1217 -0.4289 -0.1280 -0.1167 88  TYR L CD2 
12101 C CE1 . TYR H 88  ? 1.5197 1.9331 1.2266 -0.3979 -0.0478 -0.0862 88  TYR L CE1 
12102 C CE2 . TYR H 88  ? 1.4584 1.9188 1.1546 -0.4280 -0.0998 -0.1148 88  TYR L CE2 
12103 C CZ  . TYR H 88  ? 1.5980 2.0167 1.2924 -0.4119 -0.0579 -0.0999 88  TYR L CZ  
12104 O OH  . TYR H 88  ? 1.6586 2.0389 1.3402 -0.4072 -0.0207 -0.0947 88  TYR L OH  
12105 N N   . CYS H 89  ? 1.2899 1.8522 1.0733 -0.3876 -0.1597 -0.0901 89  CYS L N   
12106 C CA  . CYS H 89  ? 1.2797 1.8448 1.0630 -0.3846 -0.1637 -0.0948 89  CYS L CA  
12107 C C   . CYS H 89  ? 1.3679 1.8847 1.1204 -0.3868 -0.1400 -0.1021 89  CYS L C   
12108 O O   . CYS H 89  ? 1.3947 1.8710 1.1303 -0.3876 -0.1144 -0.0979 89  CYS L O   
12109 C CB  . CYS H 89  ? 1.2644 1.8546 1.0844 -0.3735 -0.1676 -0.0757 89  CYS L CB  
12110 S SG  . CYS H 89  ? 1.3373 1.9188 1.1900 -0.3557 -0.1402 -0.0409 89  CYS L SG  
12111 N N   . GLN H 90  ? 1.3366 1.8508 1.0745 -0.3892 -0.1440 -0.1127 90  GLN L N   
12112 C CA  . GLN H 90  ? 1.3948 1.8575 1.0924 -0.3963 -0.1226 -0.1209 90  GLN L CA  
12113 C C   . GLN H 90  ? 1.4669 1.9318 1.1712 -0.3846 -0.1228 -0.1220 90  GLN L C   
12114 O O   . GLN H 90  ? 1.4280 1.9365 1.1498 -0.3813 -0.1430 -0.1252 90  GLN L O   
12115 C CB  . GLN H 90  ? 1.4405 1.8958 1.0896 -0.4272 -0.1303 -0.1373 90  GLN L CB  
12116 C CG  . GLN H 90  ? 1.5876 1.9794 1.1747 -0.4478 -0.1080 -0.1481 90  GLN L CG  
12117 C CD  . GLN H 90  ? 1.6612 2.0798 1.2131 -0.4785 -0.1304 -0.1582 90  GLN L CD  
12118 O OE1 . GLN H 90  ? 1.4923 1.9787 1.0761 -0.4729 -0.1571 -0.1522 90  GLN L OE1 
12119 N NE2 . GLN H 90  ? 1.6256 1.9895 1.1069 -0.5135 -0.1159 -0.1695 90  GLN L NE2 
12120 N N   . GLN H 91  ? 1.4822 1.8930 1.1697 -0.3765 -0.0943 -0.1180 91  GLN L N   
12121 C CA  . GLN H 91  ? 1.4883 1.8904 1.1776 -0.3641 -0.0896 -0.1197 91  GLN L CA  
12122 C C   . GLN H 91  ? 1.6324 1.9882 1.2560 -0.3858 -0.0800 -0.1368 91  GLN L C   
12123 O O   . GLN H 91  ? 1.6914 1.9914 1.2640 -0.4065 -0.0602 -0.1422 91  GLN L O   
12124 C CB  . GLN H 91  ? 1.5064 1.8861 1.2312 -0.3366 -0.0646 -0.0962 91  GLN L CB  
12125 C CG  . GLN H 91  ? 1.6423 1.9474 1.3417 -0.3310 -0.0203 -0.0816 91  GLN L CG  
12126 C CD  . GLN H 91  ? 1.8412 2.0660 1.4835 -0.3337 0.0106  -0.0914 91  GLN L CD  
12127 O OE1 . GLN H 91  ? 1.7158 1.9473 1.3527 -0.3316 -0.0007 -0.1030 91  GLN L OE1 
12128 N NE2 . GLN H 91  ? 1.8691 2.0083 1.4612 -0.3390 0.0552  -0.0863 91  GLN L NE2 
12129 N N   . CYS H 92  ? 1.6023 1.9804 1.2212 -0.3850 -0.0926 -0.1444 92  CYS L N   
12130 C CA  . CYS H 92  ? 1.6648 2.0125 1.2202 -0.4107 -0.0896 -0.1569 92  CYS L CA  
12131 C C   . CYS H 92  ? 1.7542 2.0633 1.2998 -0.3928 -0.0707 -0.1577 92  CYS L C   
12132 O O   . CYS H 92  ? 1.7886 2.0809 1.2832 -0.4129 -0.0716 -0.1666 92  CYS L O   
12133 C CB  . CYS H 92  ? 1.6435 2.0630 1.1956 -0.4321 -0.1224 -0.1588 92  CYS L CB  
12134 S SG  . CYS H 92  ? 1.6713 2.1343 1.2385 -0.4496 -0.1426 -0.1552 92  CYS L SG  
12135 N N   . GLY H 93  ? 1.6986 1.9960 1.2921 -0.3579 -0.0542 -0.1452 93  GLY L N   
12136 C CA  . GLY H 93  ? 1.7128 1.9727 1.3110 -0.3335 -0.0326 -0.1411 93  GLY L CA  
12137 C C   . GLY H 93  ? 1.8582 2.0133 1.3953 -0.3391 0.0090  -0.1402 93  GLY L C   
12138 O O   . GLY H 93  ? 1.9179 2.0316 1.3814 -0.3680 0.0125  -0.1566 93  GLY L O   
12139 N N   . ASN H 94  ? 1.8274 1.9362 1.3881 -0.3147 0.0440  -0.1176 94  ASN L N   
12140 C CA  . ASN H 94  ? 1.9192 1.9101 1.4121 -0.3173 0.0964  -0.1136 94  ASN L CA  
12141 C C   . ASN H 94  ? 1.9999 1.9353 1.4209 -0.3540 0.1130  -0.1240 94  ASN L C   
12142 O O   . ASN H 94  ? 1.9527 1.9209 1.4067 -0.3526 0.1086  -0.1135 94  ASN L O   
12143 C CB  . ASN H 94  ? 1.9633 1.9176 1.5061 -0.2731 0.1388  -0.0765 94  ASN L CB  
12144 C CG  . ASN H 94  ? 2.4112 2.2313 1.8828 -0.2674 0.2022  -0.0689 94  ASN L CG  
12145 O OD1 . ASN H 94  ? 2.3391 2.1193 1.7923 -0.2555 0.2147  -0.0731 94  ASN L OD1 
12146 N ND2 . ASN H 94  ? 2.4148 2.1546 1.8425 -0.2731 0.2502  -0.0555 94  ASN L ND2 
12147 N N   . SER H 95  ? 1.3763 2.4037 1.3542 -0.3853 0.0997  -0.2242 95  SER L N   
12148 C CA  . SER H 95  ? 1.4199 2.3547 1.3533 -0.3634 0.1369  -0.2361 95  SER L CA  
12149 C C   . SER H 95  ? 1.5051 2.4577 1.4188 -0.3012 0.1859  -0.2681 95  SER L C   
12150 O O   . SER H 95  ? 1.5221 2.5507 1.4370 -0.3084 0.2002  -0.2831 95  SER L O   
12151 C CB  . SER H 95  ? 1.4961 2.3835 1.3854 -0.4393 0.1359  -0.2310 95  SER L CB  
12152 O OG  . SER H 95  ? 1.6202 2.4026 1.4668 -0.4229 0.1557  -0.2277 95  SER L OG  
12153 N N   . PRO H 96  ? 1.4608 2.3540 1.3659 -0.2398 0.2075  -0.2777 96  PRO L N   
12154 C CA  . PRO H 96  ? 1.4398 2.2495 1.3415 -0.2241 0.1937  -0.2597 96  PRO L CA  
12155 C C   . PRO H 96  ? 1.3934 2.2179 1.3466 -0.2019 0.1642  -0.2399 96  PRO L C   
12156 O O   . PRO H 96  ? 1.3576 2.2408 1.3438 -0.1739 0.1606  -0.2431 96  PRO L O   
12157 C CB  . PRO H 96  ? 1.5054 2.2710 1.3800 -0.1664 0.2251  -0.2826 96  PRO L CB  
12158 C CG  . PRO H 96  ? 1.5669 2.4054 1.4665 -0.1306 0.2486  -0.3089 96  PRO L CG  
12159 C CD  . PRO H 96  ? 1.5121 2.4223 1.4123 -0.1828 0.2473  -0.3090 96  PRO L CD  
12160 N N   . TRP H 97  ? 1.3125 2.0791 1.2704 -0.2155 0.1432  -0.2170 97  TRP L N   
12161 C CA  . TRP H 97  ? 1.2582 2.0250 1.2582 -0.1936 0.1189  -0.2008 97  TRP L CA  
12162 C C   . TRP H 97  ? 1.3045 2.0494 1.3014 -0.1268 0.1391  -0.2131 97  TRP L C   
12163 O O   . TRP H 97  ? 1.3302 2.0248 1.2952 -0.1083 0.1565  -0.2197 97  TRP L O   
12164 C CB  . TRP H 97  ? 1.2309 1.9410 1.2400 -0.2284 0.0963  -0.1741 97  TRP L CB  
12165 C CG  . TRP H 97  ? 1.2301 1.9562 1.2553 -0.3038 0.0666  -0.1584 97  TRP L CG  
12166 C CD1 . TRP H 97  ? 1.2679 2.0558 1.2916 -0.3468 0.0574  -0.1664 97  TRP L CD1 
12167 C CD2 . TRP H 97  ? 1.2092 1.8902 1.2603 -0.3505 0.0383  -0.1301 97  TRP L CD2 
12168 N NE1 . TRP H 97  ? 1.2455 2.0291 1.2911 -0.4222 0.0207  -0.1458 97  TRP L NE1 
12169 C CE2 . TRP H 97  ? 1.2499 1.9650 1.3163 -0.4259 0.0086  -0.1230 97  TRP L CE2 
12170 C CE3 . TRP H 97  ? 1.2130 1.8311 1.2812 -0.3383 0.0337  -0.1084 97  TRP L CE3 
12171 C CZ2 . TRP H 97  ? 1.2179 1.8996 1.3210 -0.4920 -0.0280 -0.0951 97  TRP L CZ2 
12172 C CZ3 . TRP H 97  ? 1.2109 1.7971 1.3158 -0.3980 0.0029  -0.0798 97  TRP L CZ3 
12173 C CH2 . TRP H 97  ? 1.2054 1.8207 1.3304 -0.4750 -0.0290 -0.0736 97  TRP L CH2 
12174 N N   . THR H 98  ? 1.2280 2.0095 1.2555 -0.0946 0.1324  -0.2144 98  THR L N   
12175 C CA  . THR H 98  ? 1.2290 1.9907 1.2589 -0.0412 0.1466  -0.2248 98  THR L CA  
12176 C C   . THR H 98  ? 1.2570 1.9930 1.3058 -0.0242 0.1289  -0.2097 98  THR L C   
12177 O O   . THR H 98  ? 1.2184 1.9717 1.2882 -0.0414 0.1055  -0.1949 98  THR L O   
12178 C CB  . THR H 98  ? 1.3201 2.1322 1.3651 -0.0169 0.1603  -0.2390 98  THR L CB  
12179 O OG1 . THR H 98  ? 1.2739 2.1426 1.3411 -0.0361 0.1395  -0.2239 98  THR L OG1 
12180 C CG2 . THR H 98  ? 1.3270 2.1512 1.3503 -0.0178 0.1894  -0.2633 98  THR L CG2 
12181 N N   . PHE H 99  ? 1.2384 1.9335 1.2785 0.0071  0.1372  -0.2143 99  PHE L N   
12182 C CA  . PHE H 99  ? 1.2256 1.8959 1.2776 0.0245  0.1261  -0.2039 99  PHE L CA  
12183 C C   . PHE H 99  ? 1.3009 1.9813 1.3654 0.0545  0.1282  -0.2115 99  PHE L C   
12184 O O   . PHE H 99  ? 1.3040 1.9943 1.3695 0.0691  0.1405  -0.2263 99  PHE L O   
12185 C CB  . PHE H 99  ? 1.2591 1.8797 1.2922 0.0315  0.1283  -0.1982 99  PHE L CB  
12186 C CG  . PHE H 99  ? 1.2797 1.8755 1.3064 -0.0008 0.1218  -0.1789 99  PHE L CG  
12187 C CD1 . PHE H 99  ? 1.2954 1.8798 1.3448 -0.0098 0.1101  -0.1618 99  PHE L CD1 
12188 C CD2 . PHE H 99  ? 1.3362 1.9144 1.3355 -0.0244 0.1272  -0.1764 99  PHE L CD2 
12189 C CE1 . PHE H 99  ? 1.3071 1.8650 1.3624 -0.0438 0.1019  -0.1397 99  PHE L CE1 
12190 C CE2 . PHE H 99  ? 1.3751 1.9200 1.3706 -0.0623 0.1177  -0.1515 99  PHE L CE2 
12191 C CZ  . PHE H 99  ? 1.3242 1.8602 1.3530 -0.0726 0.1042  -0.1319 99  PHE L CZ  
12192 N N   . GLY H 100 ? 1.2794 1.9519 1.3546 0.0613  0.1152  -0.2006 100 GLY L N   
12193 C CA  . GLY H 100 ? 1.2950 1.9619 1.3786 0.0816  0.1124  -0.1998 100 GLY L CA  
12194 C C   . GLY H 100 ? 1.3912 2.0267 1.4709 0.0983  0.1185  -0.2106 100 GLY L C   
12195 O O   . GLY H 100 ? 1.3961 2.0155 1.4624 0.0987  0.1226  -0.2171 100 GLY L O   
12196 N N   . GLN H 101 ? 1.3643 1.9882 1.4557 0.1080  0.1131  -0.2082 101 GLN L N   
12197 C CA  . GLN H 101 ? 1.3719 1.9694 1.4683 0.1157  0.1094  -0.2174 101 GLN L CA  
12198 C C   . GLN H 101 ? 1.4054 1.9739 1.4819 0.1127  0.1028  -0.2145 101 GLN L C   
12199 O O   . GLN H 101 ? 1.4020 1.9617 1.4727 0.1154  0.0978  -0.2222 101 GLN L O   
12200 C CB  . GLN H 101 ? 1.3945 1.9814 1.5142 0.1166  0.1016  -0.2097 101 GLN L CB  
12201 C CG  . GLN H 101 ? 1.6786 2.3003 1.8216 0.1206  0.1088  -0.2048 101 GLN L CG  
12202 C CD  . GLN H 101 ? 1.9722 2.5852 2.1535 0.1238  0.1048  -0.2020 101 GLN L CD  
12203 O OE1 . GLN H 101 ? 1.9124 2.5528 2.1224 0.1332  0.1165  -0.2167 101 GLN L OE1 
12204 N NE2 . GLN H 101 ? 1.8844 2.4562 2.0691 0.1136  0.0883  -0.1816 101 GLN L NE2 
12205 N N   . GLY H 102 ? 1.3445 1.9013 1.4102 0.1081  0.1009  -0.2026 102 GLY L N   
12206 C CA  . GLY H 102 ? 1.3378 1.8730 1.3874 0.1063  0.1001  -0.2003 102 GLY L CA  
12207 C C   . GLY H 102 ? 1.3827 1.8873 1.4236 0.1012  0.0925  -0.1980 102 GLY L C   
12208 O O   . GLY H 102 ? 1.3765 1.8712 1.4262 0.0955  0.0825  -0.2025 102 GLY L O   
12209 N N   . THR H 103 ? 1.3378 1.8241 1.3621 0.0997  0.0950  -0.1915 103 THR L N   
12210 C CA  . THR H 103 ? 1.3505 1.7978 1.3538 0.0903  0.0904  -0.1883 103 THR L CA  
12211 C C   . THR H 103 ? 1.3963 1.8393 1.3840 0.0892  0.0995  -0.1954 103 THR L C   
12212 O O   . THR H 103 ? 1.3928 1.8471 1.3820 0.0989  0.1107  -0.1957 103 THR L O   
12213 C CB  . THR H 103 ? 1.4604 1.8845 1.4484 0.0915  0.0848  -0.1749 103 THR L CB  
12214 O OG1 . THR H 103 ? 1.4804 1.9226 1.4861 0.0942  0.0753  -0.1633 103 THR L OG1 
12215 C CG2 . THR H 103 ? 1.4580 1.8269 1.4146 0.0772  0.0784  -0.1673 103 THR L CG2 
12216 N N   . LYS H 104 ? 1.3457 1.7758 1.3238 0.0743  0.0921  -0.1995 104 LYS L N   
12217 C CA  . LYS H 104 ? 1.3444 1.7778 1.3062 0.0704  0.0994  -0.2039 104 LYS L CA  
12218 C C   . LYS H 104 ? 1.4040 1.7996 1.3341 0.0611  0.1084  -0.2058 104 LYS L C   
12219 O O   . LYS H 104 ? 1.4172 1.7744 1.3315 0.0417  0.0971  -0.2016 104 LYS L O   
12220 C CB  . LYS H 104 ? 1.3660 1.8122 1.3314 0.0538  0.0791  -0.2061 104 LYS L CB  
12221 C CG  . LYS H 104 ? 1.5256 1.9966 1.4816 0.0557  0.0829  -0.2036 104 LYS L CG  
12222 C CD  . LYS H 104 ? 1.6549 2.1140 1.5841 0.0329  0.0840  -0.2082 104 LYS L CD  
12223 C CE  . LYS H 104 ? 1.7738 2.2682 1.6983 0.0377  0.0888  -0.2016 104 LYS L CE  
12224 N NZ  . LYS H 104 ? 1.8952 2.3863 1.7912 0.0133  0.0931  -0.2081 104 LYS L NZ  
12225 N N   . VAL H 105 ? 1.3590 1.7599 1.2803 0.0735  0.1284  -0.2105 105 VAL L N   
12226 C CA  . VAL H 105 ? 1.3955 1.7587 1.2816 0.0685  0.1407  -0.2168 105 VAL L CA  
12227 C C   . VAL H 105 ? 1.4717 1.8431 1.3391 0.0509  0.1477  -0.2244 105 VAL L C   
12228 O O   . VAL H 105 ? 1.4599 1.8701 1.3429 0.0625  0.1599  -0.2255 105 VAL L O   
12229 C CB  . VAL H 105 ? 1.4488 1.8127 1.3426 0.0934  0.1559  -0.2205 105 VAL L CB  
12230 C CG1 . VAL H 105 ? 1.5017 1.8188 1.3531 0.0916  0.1671  -0.2297 105 VAL L CG1 
12231 C CG2 . VAL H 105 ? 1.4193 1.7882 1.3347 0.1033  0.1396  -0.2102 105 VAL L CG2 
12232 N N   . GLU H 106 ? 1.4533 1.7894 1.2904 0.0177  0.1351  -0.2251 106 GLU L N   
12233 C CA  . GLU H 106 ? 1.4671 1.8120 1.2828 -0.0114 0.1337  -0.2316 106 GLU L CA  
12234 C C   . GLU H 106 ? 1.5739 1.8744 1.3377 -0.0256 0.1552  -0.2426 106 GLU L C   
12235 O O   . GLU H 106 ? 1.6033 1.8449 1.3387 -0.0254 0.1579  -0.2401 106 GLU L O   
12236 C CB  . GLU H 106 ? 1.4638 1.8070 1.2896 -0.0503 0.0957  -0.2250 106 GLU L CB  
12237 C CG  . GLU H 106 ? 1.6068 1.8838 1.4172 -0.0818 0.0780  -0.2165 106 GLU L CG  
12238 C CD  . GLU H 106 ? 1.8211 2.0927 1.6523 -0.1279 0.0373  -0.2105 106 GLU L CD  
12239 O OE1 . GLU H 106 ? 1.7363 2.0560 1.6102 -0.1211 0.0151  -0.2112 106 GLU L OE1 
12240 O OE2 . GLU H 106 ? 1.7761 1.9881 1.5823 -0.1731 0.0238  -0.2032 106 GLU L OE2 
12241 N N   . ILE H 107 ? 1.5475 1.8759 1.2953 -0.0385 0.1687  -0.2526 107 ILE L N   
12242 C CA  . ILE H 107 ? 1.6132 1.9057 1.3074 -0.0547 0.1941  -0.2677 107 ILE L CA  
12243 C C   . ILE H 107 ? 1.7009 1.9306 1.3529 -0.1109 0.1694  -0.2624 107 ILE L C   
12244 O O   . ILE H 107 ? 1.6720 1.9221 1.3371 -0.1508 0.1376  -0.2555 107 ILE L O   
12245 C CB  . ILE H 107 ? 1.6623 2.0156 1.3574 -0.0541 0.2160  -0.2778 107 ILE L CB  
12246 C CG1 . ILE H 107 ? 1.6355 2.0469 1.3834 -0.0042 0.2337  -0.2727 107 ILE L CG1 
12247 C CG2 . ILE H 107 ? 1.7508 2.0686 1.3881 -0.0677 0.2500  -0.2989 107 ILE L CG2 
12248 C CD1 . ILE H 107 ? 1.7197 2.2052 1.4921 -0.0088 0.2241  -0.2595 107 ILE L CD1 
12249 N N   . LYS H 108 ? 1.7219 1.8706 1.3259 -0.1165 0.1774  -0.2615 108 LYS L N   
12250 C CA  . LYS H 108 ? 1.7646 1.8350 1.3237 -0.1748 0.1535  -0.2489 108 LYS L CA  
12251 C C   . LYS H 108 ? 1.8775 1.9460 1.3907 -0.2232 0.1632  -0.2641 108 LYS L C   
12252 O O   . LYS H 108 ? 1.9141 2.0005 1.3993 -0.2034 0.2021  -0.2861 108 LYS L O   
12253 C CB  . LYS H 108 ? 1.8513 1.8263 1.3613 -0.1666 0.1561  -0.2360 108 LYS L CB  
12254 C CG  . LYS H 108 ? 1.9486 1.8669 1.4693 -0.1905 0.1171  -0.2018 108 LYS L CG  
12255 C CD  . LYS H 108 ? 2.0566 1.8889 1.5311 -0.2652 0.0931  -0.1836 108 LYS L CD  
12256 C CE  . LYS H 108 ? 2.0622 1.8351 1.5565 -0.2841 0.0561  -0.1434 108 LYS L CE  
12257 N NZ  . LYS H 108 ? 2.0171 1.8553 1.5970 -0.2907 0.0296  -0.1396 108 LYS L NZ  
12258 N N   . ARG H 109 ? 2.0603 1.3144 1.1429 0.2143  -0.5146 0.1036  109 ARG L N   
12259 C CA  . ARG H 109 ? 2.0397 1.3266 1.1564 0.2491  -0.4813 0.0872  109 ARG L CA  
12260 C C   . ARG H 109 ? 2.0837 1.3920 1.1927 0.2430  -0.4428 0.1017  109 ARG L C   
12261 O O   . ARG H 109 ? 2.0800 1.3833 1.1609 0.2133  -0.4388 0.1223  109 ARG L O   
12262 C CB  . ARG H 109 ? 1.9997 1.3305 1.1680 0.2634  -0.4533 0.0693  109 ARG L CB  
12263 C CG  . ARG H 109 ? 2.0209 1.3859 1.2067 0.2396  -0.4133 0.0800  109 ARG L CG  
12264 C CD  . ARG H 109 ? 2.0436 1.4574 1.2784 0.2572  -0.3760 0.0668  109 ARG L CD  
12265 N NE  . ARG H 109 ? 2.1014 1.5422 1.3456 0.2681  -0.3428 0.0698  109 ARG L NE  
12266 C CZ  . ARG H 109 ? 2.2697 1.7518 1.5491 0.2885  -0.3200 0.0579  109 ARG L CZ  
12267 N NH1 . ARG H 109 ? 2.1149 1.6194 1.4243 0.3026  -0.3258 0.0409  109 ARG L NH1 
12268 N NH2 . ARG H 109 ? 2.0896 1.5942 1.3738 0.2934  -0.2923 0.0636  109 ARG L NH2 
12269 N N   . THR H 110 ? 2.0301 1.3663 1.1642 0.2704  -0.4159 0.0904  110 THR L N   
12270 C CA  . THR H 110 ? 2.0066 1.3634 1.1382 0.2675  -0.3795 0.1024  110 THR L CA  
12271 C C   . THR H 110 ? 2.0294 1.4198 1.1797 0.2464  -0.3402 0.1119  110 THR L C   
12272 O O   . THR H 110 ? 2.0046 1.4160 1.1849 0.2452  -0.3304 0.1033  110 THR L O   
12273 C CB  . THR H 110 ? 2.1169 1.5021 1.2748 0.3000  -0.3616 0.0866  110 THR L CB  
12274 O OG1 . THR H 110 ? 2.1120 1.5356 1.3137 0.3150  -0.3493 0.0679  110 THR L OG1 
12275 C CG2 . THR H 110 ? 2.1420 1.4938 1.2754 0.3230  -0.3985 0.0772  110 THR L CG2 
12276 N N   . VAL H 111 ? 1.9879 1.3821 1.1199 0.2310  -0.3203 0.1286  111 VAL L N   
12277 C CA  . VAL H 111 ? 1.9562 1.3798 1.1028 0.2140  -0.2865 0.1355  111 VAL L CA  
12278 C C   . VAL H 111 ? 1.9862 1.4453 1.1799 0.2296  -0.2549 0.1248  111 VAL L C   
12279 O O   . VAL H 111 ? 1.9749 1.4460 1.1800 0.2468  -0.2419 0.1221  111 VAL L O   
12280 C CB  . VAL H 111 ? 1.9947 1.4189 1.1145 0.2000  -0.2726 0.1521  111 VAL L CB  
12281 C CG1 . VAL H 111 ? 1.9725 1.4190 1.0939 0.1781  -0.2571 0.1564  111 VAL L CG1 
12282 C CG2 . VAL H 111 ? 2.0281 1.4165 1.0994 0.1916  -0.3057 0.1646  111 VAL L CG2 
12283 N N   . ALA H 112 ? 1.9346 1.4112 1.1541 0.2221  -0.2458 0.1192  112 ALA L N   
12284 C CA  . ALA H 112 ? 1.9112 1.4208 1.1734 0.2313  -0.2204 0.1122  112 ALA L CA  
12285 C C   . ALA H 112 ? 1.9442 1.4684 1.2186 0.2165  -0.1963 0.1186  112 ALA L C   
12286 O O   . ALA H 112 ? 1.9426 1.4625 1.2108 0.2018  -0.2018 0.1183  112 ALA L O   
12287 C CB  . ALA H 112 ? 1.9262 1.4433 1.2115 0.2380  -0.2335 0.0989  112 ALA L CB  
12288 N N   . ALA H 113 ? 1.8891 1.4308 1.1799 0.2204  -0.1724 0.1236  113 ALA L N   
12289 C CA  . ALA H 113 ? 1.8771 1.4287 1.1821 0.2097  -0.1538 0.1280  113 ALA L CA  
12290 C C   . ALA H 113 ? 1.9325 1.4994 1.2713 0.2069  -0.1509 0.1215  113 ALA L C   
12291 O O   . ALA H 113 ? 1.9279 1.5108 1.2867 0.2151  -0.1522 0.1172  113 ALA L O   
12292 C CB  . ALA H 113 ? 1.8777 1.4386 1.1891 0.2134  -0.1346 0.1368  113 ALA L CB  
12293 N N   . PRO H 114 ? 1.9037 1.4689 1.2493 0.1961  -0.1488 0.1193  114 PRO L N   
12294 C CA  . PRO H 114 ? 1.9094 1.4849 1.2850 0.1926  -0.1492 0.1142  114 PRO L CA  
12295 C C   . PRO H 114 ? 1.9814 1.5740 1.3863 0.1921  -0.1361 0.1210  114 PRO L C   
12296 O O   . PRO H 114 ? 1.9631 1.5563 1.3669 0.1915  -0.1255 0.1293  114 PRO L O   
12297 C CB  . PRO H 114 ? 1.9339 1.5015 1.3041 0.1829  -0.1533 0.1081  114 PRO L CB  
12298 C CG  . PRO H 114 ? 1.9875 1.5508 1.3369 0.1823  -0.1468 0.1115  114 PRO L CG  
12299 C CD  . PRO H 114 ? 1.9290 1.4869 1.2555 0.1878  -0.1479 0.1191  114 PRO L CD  
12300 N N   . SER H 115 ? 1.9768 1.5847 1.4070 0.1898  -0.1388 0.1190  115 SER L N   
12301 C CA  . SER H 115 ? 1.9887 1.6177 1.4469 0.1829  -0.1311 0.1278  115 SER L CA  
12302 C C   . SER H 115 ? 2.0816 1.6928 1.5497 0.1719  -0.1365 0.1274  115 SER L C   
12303 O O   . SER H 115 ? 2.0819 1.6919 1.5607 0.1680  -0.1452 0.1214  115 SER L O   
12304 C CB  . SER H 115 ? 2.0322 1.6928 1.5103 0.1858  -0.1336 0.1250  115 SER L CB  
12305 O OG  . SER H 115 ? 2.1233 1.7901 1.5887 0.2015  -0.1387 0.1155  115 SER L OG  
12306 N N   . VAL H 116 ? 2.0601 1.6552 1.5225 0.1690  -0.1336 0.1313  116 VAL L N   
12307 C CA  . VAL H 116 ? 2.0735 1.6485 1.5426 0.1637  -0.1426 0.1262  116 VAL L CA  
12308 C C   . VAL H 116 ? 2.1707 1.7468 1.6658 0.1511  -0.1485 0.1378  116 VAL L C   
12309 O O   . VAL H 116 ? 2.1673 1.7529 1.6691 0.1443  -0.1434 0.1526  116 VAL L O   
12310 C CB  . VAL H 116 ? 2.1128 1.6715 1.5635 0.1693  -0.1411 0.1206  116 VAL L CB  
12311 C CG1 . VAL H 116 ? 2.1215 1.6633 1.5802 0.1690  -0.1541 0.1088  116 VAL L CG1 
12312 C CG2 . VAL H 116 ? 2.0998 1.6614 1.5218 0.1762  -0.1380 0.1130  116 VAL L CG2 
12313 N N   . PHE H 117 ? 2.1686 1.7353 1.6768 0.1457  -0.1615 0.1322  117 PHE L N   
12314 C CA  . PHE H 117 ? 2.1976 1.7596 1.7279 0.1307  -0.1739 0.1440  117 PHE L CA  
12315 C C   . PHE H 117 ? 2.2962 1.8264 1.8302 0.1317  -0.1928 0.1314  117 PHE L C   
12316 O O   . PHE H 117 ? 2.2908 1.8171 1.8167 0.1408  -0.1945 0.1135  117 PHE L O   
12317 C CB  . PHE H 117 ? 2.2169 1.8086 1.7632 0.1213  -0.1728 0.1523  117 PHE L CB  
12318 C CG  . PHE H 117 ? 2.2199 1.8501 1.7643 0.1256  -0.1569 0.1571  117 PHE L CG  
12319 C CD1 . PHE H 117 ? 2.2456 1.8887 1.7836 0.1380  -0.1527 0.1446  117 PHE L CD1 
12320 C CD2 . PHE H 117 ? 2.2495 1.9035 1.7986 0.1176  -0.1490 0.1729  117 PHE L CD2 
12321 C CE1 . PHE H 117 ? 2.2469 1.9240 1.7839 0.1462  -0.1428 0.1448  117 PHE L CE1 
12322 C CE2 . PHE H 117 ? 2.2719 1.9663 1.8199 0.1249  -0.1356 0.1731  117 PHE L CE2 
12323 C CZ  . PHE H 117 ? 2.2362 1.9408 1.7785 0.1411  -0.1335 0.1575  117 PHE L CZ  
12324 N N   . ILE H 118 ? 2.2909 1.7991 1.8366 0.1216  -0.2099 0.1404  118 ILE L N   
12325 C CA  . ILE H 118 ? 2.3183 1.7928 1.8693 0.1246  -0.2337 0.1268  118 ILE L CA  
12326 C C   . ILE H 118 ? 2.4067 1.8739 1.9763 0.1053  -0.2525 0.1419  118 ILE L C   
12327 O O   . ILE H 118 ? 2.4058 1.8824 1.9843 0.0858  -0.2556 0.1666  118 ILE L O   
12328 C CB  . ILE H 118 ? 2.3730 1.8185 1.9186 0.1344  -0.2462 0.1176  118 ILE L CB  
12329 C CG1 . ILE H 118 ? 2.4048 1.8193 1.9552 0.1448  -0.2731 0.0946  118 ILE L CG1 
12330 C CG2 . ILE H 118 ? 2.3925 1.8279 1.9446 0.1189  -0.2532 0.1421  118 ILE L CG2 
12331 C CD1 . ILE H 118 ? 2.4869 1.8895 2.0274 0.1666  -0.2796 0.0692  118 ILE L CD1 
12332 N N   . PHE H 119 ? 2.3941 1.8498 1.9681 0.1085  -0.2645 0.1281  119 PHE L N   
12333 C CA  . PHE H 119 ? 2.4251 1.8721 2.0147 0.0902  -0.2839 0.1416  119 PHE L CA  
12334 C C   . PHE H 119 ? 2.5257 1.9247 2.1196 0.0919  -0.3184 0.1321  119 PHE L C   
12335 O O   . PHE H 119 ? 2.5253 1.9099 2.1143 0.1108  -0.3247 0.1042  119 PHE L O   
12336 C CB  . PHE H 119 ? 2.4345 1.9051 2.0278 0.0896  -0.2738 0.1368  119 PHE L CB  
12337 C CG  . PHE H 119 ? 2.4290 1.9454 2.0229 0.0858  -0.2490 0.1483  119 PHE L CG  
12338 C CD1 . PHE H 119 ? 2.4736 2.0187 2.0812 0.0654  -0.2492 0.1718  119 PHE L CD1 
12339 C CD2 . PHE H 119 ? 2.4342 1.9676 2.0141 0.1023  -0.2285 0.1346  119 PHE L CD2 
12340 C CE1 . PHE H 119 ? 2.4631 2.0565 2.0729 0.0663  -0.2281 0.1769  119 PHE L CE1 
12341 C CE2 . PHE H 119 ? 2.4511 2.0228 2.0317 0.1025  -0.2109 0.1415  119 PHE L CE2 
12342 C CZ  . PHE H 119 ? 2.4294 2.0325 2.0261 0.0868  -0.2102 0.1603  119 PHE L CZ  
12343 N N   . PRO H 120 ? 2.5233 1.8990 2.1262 0.0710  -0.3442 0.1547  120 PRO L N   
12344 C CA  . PRO H 120 ? 2.5694 1.8916 2.1760 0.0733  -0.3847 0.1452  120 PRO L CA  
12345 C C   . PRO H 120 ? 2.6292 1.9415 2.2424 0.0709  -0.3990 0.1379  120 PRO L C   
12346 O O   . PRO H 120 ? 2.6004 1.9463 2.2183 0.0575  -0.3820 0.1516  120 PRO L O   
12347 C CB  . PRO H 120 ? 2.6262 1.9290 2.2378 0.0453  -0.4092 0.1779  120 PRO L CB  
12348 C CG  . PRO H 120 ? 2.6539 2.0104 2.2693 0.0215  -0.3832 0.2070  120 PRO L CG  
12349 C CD  . PRO H 120 ? 2.5456 1.9448 2.1544 0.0429  -0.3410 0.1898  120 PRO L CD  
12350 N N   . PRO H 121 ? 2.6260 1.8950 2.2399 0.0855  -0.4307 0.1143  121 PRO L N   
12351 C CA  . PRO H 121 ? 2.6398 1.8989 2.2594 0.0829  -0.4445 0.1075  121 PRO L CA  
12352 C C   . PRO H 121 ? 2.7228 1.9692 2.3510 0.0489  -0.4671 0.1432  121 PRO L C   
12353 O O   . PRO H 121 ? 2.7488 1.9720 2.3781 0.0296  -0.4911 0.1671  121 PRO L O   
12354 C CB  . PRO H 121 ? 2.6968 1.9127 2.3149 0.1083  -0.4771 0.0723  121 PRO L CB  
12355 C CG  . PRO H 121 ? 2.7484 1.9616 2.3599 0.1280  -0.4738 0.0563  121 PRO L CG  
12356 C CD  . PRO H 121 ? 2.6767 1.9056 2.2872 0.1066  -0.4573 0.0908  121 PRO L CD  
12357 N N   . SER H 122 ? 2.6699 1.9336 2.3034 0.0392  -0.4608 0.1482  122 SER L N   
12358 C CA  . SER H 122 ? 2.6901 1.9499 2.3311 0.0053  -0.4813 0.1820  122 SER L CA  
12359 C C   . SER H 122 ? 2.7994 1.9915 2.4401 -0.0004 -0.5356 0.1826  122 SER L C   
12360 O O   . SER H 122 ? 2.8125 1.9684 2.4506 0.0272  -0.5531 0.1483  122 SER L O   
12361 C CB  . SER H 122 ? 2.7042 1.9968 2.3507 0.0011  -0.4624 0.1819  122 SER L CB  
12362 O OG  . SER H 122 ? 2.8185 2.1144 2.4719 -0.0328 -0.4813 0.2151  122 SER L OG  
12363 N N   . ASP H 123 ? 2.7889 1.9666 2.4316 -0.0369 -0.5648 0.2208  123 ASP L N   
12364 C CA  . ASP H 123 ? 2.8537 1.9607 2.4940 -0.0482 -0.6243 0.2277  123 ASP L CA  
12365 C C   . ASP H 123 ? 2.9239 2.0075 2.5666 -0.0457 -0.6434 0.2172  123 ASP L C   
12366 O O   . ASP H 123 ? 2.9693 1.9873 2.6091 -0.0428 -0.6940 0.2096  123 ASP L O   
12367 C CB  . ASP H 123 ? 2.9101 2.0118 2.5486 -0.0938 -0.6520 0.2761  123 ASP L CB  
12368 C CG  . ASP H 123 ? 2.9880 2.0999 2.6231 -0.0948 -0.6419 0.2835  123 ASP L CG  
12369 O OD1 . ASP H 123 ? 3.0210 2.0766 2.6517 -0.0777 -0.6730 0.2668  123 ASP L OD1 
12370 O OD2 . ASP H 123 ? 3.0069 2.1842 2.6442 -0.1107 -0.6037 0.3039  123 ASP L OD2 
12371 N N   . GLU H 124 ? 2.8444 1.9795 2.4923 -0.0447 -0.6048 0.2145  124 GLU L N   
12372 C CA  . GLU H 124 ? 2.8521 1.9755 2.5028 -0.0408 -0.6131 0.2028  124 GLU L CA  
12373 C C   . GLU H 124 ? 2.8883 1.9914 2.5363 0.0027  -0.6105 0.1518  124 GLU L C   
12374 O O   . GLU H 124 ? 2.9140 1.9783 2.5618 0.0124  -0.6396 0.1337  124 GLU L O   
12375 C CB  . GLU H 124 ? 2.8208 2.0108 2.4783 -0.0536 -0.5711 0.2165  124 GLU L CB  
12376 C CG  . GLU H 124 ? 2.9618 2.1737 2.6235 -0.0977 -0.5829 0.2624  124 GLU L CG  
12377 C CD  . GLU H 124 ? 3.1475 2.4069 2.8104 -0.1225 -0.5678 0.2940  124 GLU L CD  
12378 O OE1 . GLU H 124 ? 3.1253 2.3693 2.7852 -0.1580 -0.6023 0.3291  124 GLU L OE1 
12379 O OE2 . GLU H 124 ? 2.9507 2.2646 2.6168 -0.1088 -0.5237 0.2851  124 GLU L OE2 
12380 N N   . GLN H 125 ? 2.7978 1.9317 2.4429 0.0275  -0.5763 0.1291  125 GLN L N   
12381 C CA  . GLN H 125 ? 2.7805 1.9135 2.4215 0.0663  -0.5681 0.0818  125 GLN L CA  
12382 C C   . GLN H 125 ? 2.8849 1.9599 2.5234 0.0863  -0.6140 0.0585  125 GLN L C   
12383 O O   . GLN H 125 ? 2.8892 1.9531 2.5264 0.1163  -0.6254 0.0174  125 GLN L O   
12384 C CB  . GLN H 125 ? 2.7394 1.9256 2.3761 0.0794  -0.5202 0.0729  125 GLN L CB  
12385 C CG  . GLN H 125 ? 2.8651 2.0699 2.4956 0.1125  -0.5044 0.0286  125 GLN L CG  
12386 C CD  . GLN H 125 ? 3.0572 2.3120 2.6804 0.1199  -0.4608 0.0255  125 GLN L CD  
12387 O OE1 . GLN H 125 ? 3.0036 2.2659 2.6250 0.1138  -0.4500 0.0433  125 GLN L OE1 
12388 N NE2 . GLN H 125 ? 2.9196 2.2085 2.5369 0.1322  -0.4378 0.0027  125 GLN L NE2 
12389 N N   . LEU H 126 ? 2.8844 1.9248 2.5222 0.0693  -0.6428 0.0839  126 LEU L N   
12390 C CA  . LEU H 126 ? 2.9464 1.9235 2.5823 0.0852  -0.6945 0.0664  126 LEU L CA  
12391 C C   . LEU H 126 ? 3.0503 1.9708 2.6872 0.0886  -0.7456 0.0543  126 LEU L C   
12392 O O   . LEU H 126 ? 3.0845 1.9635 2.7209 0.1199  -0.7826 0.0163  126 LEU L O   
12393 C CB  . LEU H 126 ? 2.9775 1.9299 2.6114 0.0557  -0.7162 0.1062  126 LEU L CB  
12394 C CG  . LEU H 126 ? 3.0252 1.9855 2.6565 0.0720  -0.7038 0.0958  126 LEU L CG  
12395 C CD1 . LEU H 126 ? 2.9553 1.9882 2.5859 0.0637  -0.6412 0.1113  126 LEU L CD1 
12396 C CD2 . LEU H 126 ? 3.1206 2.0263 2.7495 0.0489  -0.7522 0.1241  126 LEU L CD2 
12397 N N   . LYS H 127 ? 3.0063 1.9286 2.6449 0.0580  -0.7480 0.0845  127 LYS L N   
12398 C CA  . LYS H 127 ? 3.0519 1.9230 2.6903 0.0550  -0.7941 0.0802  127 LYS L CA  
12399 C C   . LYS H 127 ? 3.0935 1.9740 2.7337 0.0938  -0.7864 0.0283  127 LYS L C   
12400 O O   . LYS H 127 ? 3.1322 1.9735 2.7762 0.1057  -0.8231 0.0088  127 LYS L O   
12401 C CB  . LYS H 127 ? 3.0708 1.9554 2.7103 0.0100  -0.7903 0.1283  127 LYS L CB  
12402 C CG  . LYS H 127 ? 3.1752 2.0979 2.8473 -0.0033 -0.7661 0.1405  127 LYS L CG  
12403 C CD  . LYS H 127 ? 3.2037 2.1885 2.9031 -0.0204 -0.7215 0.1666  127 LYS L CD  
12404 C CE  . LYS H 127 ? 3.2195 2.2407 2.9449 -0.0237 -0.6937 0.1687  127 LYS L CE  
12405 N NZ  . LYS H 127 ? 3.2398 2.3049 2.9814 -0.0353 -0.6620 0.1880  127 LYS L NZ  
12406 N N   . SER H 128 ? 2.9816 1.9289 2.6231 0.1112  -0.7303 0.0072  128 SER L N   
12407 C CA  . SER H 128 ? 2.9638 1.9346 2.6055 0.1434  -0.7182 -0.0403 128 SER L CA  
12408 C C   . SER H 128 ? 3.0369 1.9932 2.6773 0.1864  -0.7420 -0.0920 128 SER L C   
12409 O O   . SER H 128 ? 3.0691 2.0088 2.7106 0.2111  -0.7690 -0.1303 128 SER L O   
12410 C CB  . SER H 128 ? 2.9393 1.9851 2.5804 0.1407  -0.6556 -0.0400 128 SER L CB  
12411 O OG  . SER H 128 ? 2.9920 2.0753 2.6294 0.1527  -0.6239 -0.0475 128 SER L OG  
12412 N N   . GLY H 129 ? 2.9684 1.9346 2.6070 0.1956  -0.7323 -0.0939 129 GLY L N   
12413 C CA  . GLY H 129 ? 2.9822 1.9424 2.6205 0.2364  -0.7524 -0.1418 129 GLY L CA  
12414 C C   . GLY H 129 ? 2.9576 1.9904 2.5920 0.2553  -0.7021 -0.1650 129 GLY L C   
12415 O O   . GLY H 129 ? 2.9616 2.0034 2.5957 0.2897  -0.7136 -0.2067 129 GLY L O   
12416 N N   . THR H 130 ? 2.8369 1.9227 2.4677 0.2332  -0.6487 -0.1391 130 THR L N   
12417 C CA  . THR H 130 ? 2.7677 1.9216 2.3915 0.2425  -0.5998 -0.1514 130 THR L CA  
12418 C C   . THR H 130 ? 2.7574 1.9288 2.3789 0.2104  -0.5634 -0.1026 130 THR L C   
12419 O O   . THR H 130 ? 2.7332 1.9133 2.3567 0.1859  -0.5480 -0.0756 130 THR L O   
12420 C CB  . THR H 130 ? 2.8210 2.0273 2.4409 0.2552  -0.5790 -0.1843 130 THR L CB  
12421 O OG1 . THR H 130 ? 2.8452 2.0391 2.4683 0.2874  -0.6158 -0.2324 130 THR L OG1 
12422 C CG2 . THR H 130 ? 2.7386 2.0153 2.3478 0.2593  -0.5327 -0.1933 130 THR L CG2 
12423 N N   . ALA H 131 ? 2.6875 1.8643 2.3056 0.2119  -0.5522 -0.0930 131 ALA L N   
12424 C CA  . ALA H 131 ? 2.6397 1.8353 2.2557 0.1855  -0.5203 -0.0510 131 ALA L CA  
12425 C C   . ALA H 131 ? 2.6168 1.8659 2.2225 0.1957  -0.4782 -0.0600 131 ALA L C   
12426 O O   . ALA H 131 ? 2.6135 1.8714 2.2143 0.2203  -0.4816 -0.0895 131 ALA L O   
12427 C CB  . ALA H 131 ? 2.6835 1.8330 2.3038 0.1700  -0.5483 -0.0222 131 ALA L CB  
12428 N N   . SER H 132 ? 2.5156 1.8006 2.1176 0.1770  -0.4411 -0.0349 132 SER L N   
12429 C CA  . SER H 132 ? 2.4634 1.7954 2.0531 0.1827  -0.4037 -0.0389 132 SER L CA  
12430 C C   . SER H 132 ? 2.4821 1.8203 2.0704 0.1673  -0.3842 -0.0055 132 SER L C   
12431 O O   . SER H 132 ? 2.4776 1.8054 2.0743 0.1450  -0.3864 0.0259  132 SER L O   
12432 C CB  . SER H 132 ? 2.4710 1.8420 2.0544 0.1783  -0.3796 -0.0449 132 SER L CB  
12433 O OG  . SER H 132 ? 2.5740 1.9450 2.1586 0.1904  -0.3965 -0.0755 132 SER L OG  
12434 N N   . VAL H 133 ? 2.4124 1.7727 1.9893 0.1786  -0.3651 -0.0128 133 VAL L N   
12435 C CA  . VAL H 133 ? 2.3856 1.7564 1.9588 0.1676  -0.3445 0.0144  133 VAL L CA  
12436 C C   . VAL H 133 ? 2.3797 1.7951 1.9389 0.1677  -0.3095 0.0144  133 VAL L C   
12437 O O   . VAL H 133 ? 2.3679 1.8052 1.9151 0.1811  -0.3030 -0.0107 133 VAL L O   
12438 C CB  . VAL H 133 ? 2.4494 1.8014 2.0202 0.1789  -0.3556 0.0093  133 VAL L CB  
12439 C CG1 . VAL H 133 ? 2.4261 1.7893 1.9933 0.1655  -0.3348 0.0388  133 VAL L CG1 
12440 C CG2 . VAL H 133 ? 2.4967 1.7973 2.0798 0.1796  -0.3983 0.0070  133 VAL L CG2 
12441 N N   . VAL H 134 ? 2.2933 1.7242 1.8535 0.1522  -0.2904 0.0418  134 VAL L N   
12442 C CA  . VAL H 134 ? 2.2455 1.7107 1.7924 0.1519  -0.2637 0.0437  134 VAL L CA  
12443 C C   . VAL H 134 ? 2.2655 1.7427 1.8032 0.1524  -0.2456 0.0578  134 VAL L C   
12444 O O   . VAL H 134 ? 2.2646 1.7340 1.8117 0.1431  -0.2472 0.0783  134 VAL L O   
12445 C CB  . VAL H 134 ? 2.2794 1.7572 1.8341 0.1390  -0.2582 0.0559  134 VAL L CB  
12446 C CG1 . VAL H 134 ? 2.2504 1.7553 1.7892 0.1416  -0.2400 0.0511  134 VAL L CG1 
12447 C CG2 . VAL H 134 ? 2.2960 1.7574 1.8615 0.1359  -0.2777 0.0462  134 VAL L CG2 
12448 N N   . CYS H 135 ? 2.1969 1.6948 1.7147 0.1608  -0.2301 0.0479  135 CYS L N   
12449 C CA  . CYS H 135 ? 2.1743 1.6839 1.6789 0.1629  -0.2130 0.0588  135 CYS L CA  
12450 C C   . CYS H 135 ? 2.1792 1.7101 1.6732 0.1589  -0.1989 0.0657  135 CYS L C   
12451 O O   . CYS H 135 ? 2.1811 1.7242 1.6554 0.1621  -0.1953 0.0550  135 CYS L O   
12452 C CB  . CYS H 135 ? 2.1825 1.6959 1.6706 0.1756  -0.2120 0.0417  135 CYS L CB  
12453 S SG  . CYS H 135 ? 2.2165 1.7409 1.6858 0.1779  -0.1925 0.0551  135 CYS L SG  
12454 N N   . LEU H 136 ? 2.0868 1.6242 1.5937 0.1510  -0.1945 0.0830  136 LEU L N   
12455 C CA  . LEU H 136 ? 2.0454 1.6010 1.5465 0.1505  -0.1862 0.0874  136 LEU L CA  
12456 C C   . LEU H 136 ? 2.0300 1.5943 1.5127 0.1570  -0.1741 0.0925  136 LEU L C   
12457 O O   . LEU H 136 ? 2.0253 1.5911 1.5112 0.1575  -0.1670 0.1031  136 LEU L O   
12458 C CB  . LEU H 136 ? 2.0462 1.6143 1.5701 0.1421  -0.1873 0.1003  136 LEU L CB  
12459 C CG  . LEU H 136 ? 2.0938 1.6870 1.6175 0.1455  -0.1788 0.1057  136 LEU L CG  
12460 C CD1 . LEU H 136 ? 2.0883 1.6808 1.6022 0.1495  -0.1846 0.0941  136 LEU L CD1 
12461 C CD2 . LEU H 136 ? 2.1398 1.7575 1.6877 0.1366  -0.1779 0.1192  136 LEU L CD2 
12462 N N   . LEU H 137 ? 1.9412 1.5098 1.4039 0.1603  -0.1743 0.0863  137 LEU L N   
12463 C CA  . LEU H 137 ? 1.9185 1.4907 1.3595 0.1661  -0.1678 0.0906  137 LEU L CA  
12464 C C   . LEU H 137 ? 1.9417 1.5219 1.3830 0.1692  -0.1719 0.0922  137 LEU L C   
12465 O O   . LEU H 137 ? 1.9413 1.5155 1.3650 0.1681  -0.1825 0.0862  137 LEU L O   
12466 C CB  . LEU H 137 ? 1.9201 1.4884 1.3327 0.1649  -0.1718 0.0817  137 LEU L CB  
12467 C CG  . LEU H 137 ? 1.9777 1.5450 1.3815 0.1680  -0.1655 0.0795  137 LEU L CG  
12468 C CD1 . LEU H 137 ? 1.9875 1.5503 1.4100 0.1685  -0.1703 0.0693  137 LEU L CD1 
12469 C CD2 . LEU H 137 ? 2.0031 1.5784 1.3750 0.1650  -0.1685 0.0739  137 LEU L CD2 
12470 N N   . ASN H 138 ? 1.8767 1.4736 1.3381 0.1724  -0.1660 0.0994  138 ASN L N   
12471 C CA  . ASN H 138 ? 1.8710 1.4822 1.3376 0.1795  -0.1716 0.0964  138 ASN L CA  
12472 C C   . ASN H 138 ? 1.9162 1.5256 1.3613 0.1917  -0.1741 0.0947  138 ASN L C   
12473 O O   . ASN H 138 ? 1.9075 1.5202 1.3453 0.1957  -0.1639 0.1010  138 ASN L O   
12474 C CB  . ASN H 138 ? 1.8761 1.5182 1.3731 0.1780  -0.1656 0.1022  138 ASN L CB  
12475 C CG  . ASN H 138 ? 2.1456 1.8026 1.6572 0.1806  -0.1754 0.0947  138 ASN L CG  
12476 O OD1 . ASN H 138 ? 2.0309 1.7151 1.5503 0.1919  -0.1765 0.0901  138 ASN L OD1 
12477 N ND2 . ASN H 138 ? 2.0546 1.6970 1.5715 0.1715  -0.1837 0.0915  138 ASN L ND2 
12478 N N   . ASN H 139 ? 1.8783 1.4792 1.3130 0.1969  -0.1910 0.0862  139 ASN L N   
12479 C CA  . ASN H 139 ? 1.8843 1.4759 1.2982 0.2095  -0.2045 0.0816  139 ASN L CA  
12480 C C   . ASN H 139 ? 1.9318 1.5070 1.3158 0.2101  -0.2015 0.0885  139 ASN L C   
12481 O O   . ASN H 139 ? 1.9061 1.4943 1.2935 0.2175  -0.1876 0.0934  139 ASN L O   
12482 C CB  . ASN H 139 ? 1.8999 1.5218 1.3351 0.2267  -0.2043 0.0747  139 ASN L CB  
12483 C CG  . ASN H 139 ? 2.1903 1.8299 1.6508 0.2278  -0.2121 0.0661  139 ASN L CG  
12484 O OD1 . ASN H 139 ? 2.0894 1.7677 1.5786 0.2291  -0.2004 0.0666  139 ASN L OD1 
12485 N ND2 . ASN H 139 ? 2.1028 1.7173 1.5529 0.2254  -0.2334 0.0593  139 ASN L ND2 
12486 N N   . PHE H 140 ? 1.9217 1.4714 1.2753 0.2001  -0.2161 0.0899  140 PHE L N   
12487 C CA  . PHE H 140 ? 1.9376 1.4720 1.2579 0.1965  -0.2175 0.0977  140 PHE L CA  
12488 C C   . PHE H 140 ? 2.0282 1.5368 1.3132 0.1875  -0.2465 0.0988  140 PHE L C   
12489 O O   . PHE H 140 ? 2.0378 1.5396 1.3244 0.1803  -0.2639 0.0937  140 PHE L O   
12490 C CB  . PHE H 140 ? 1.9514 1.4931 1.2704 0.1853  -0.1994 0.1026  140 PHE L CB  
12491 C CG  . PHE H 140 ? 1.9763 1.5198 1.2938 0.1703  -0.2045 0.0976  140 PHE L CG  
12492 C CD1 . PHE H 140 ? 2.0327 1.5714 1.3175 0.1558  -0.2176 0.0994  140 PHE L CD1 
12493 C CD2 . PHE H 140 ? 1.9980 1.5521 1.3457 0.1689  -0.1970 0.0917  140 PHE L CD2 
12494 C CE1 . PHE H 140 ? 2.0488 1.5987 1.3326 0.1416  -0.2218 0.0926  140 PHE L CE1 
12495 C CE2 . PHE H 140 ? 2.0397 1.5973 1.3861 0.1569  -0.2025 0.0846  140 PHE L CE2 
12496 C CZ  . PHE H 140 ? 2.0282 1.5865 1.3433 0.1440  -0.2138 0.0839  140 PHE L CZ  
12497 N N   . TYR H 141 ? 2.0041 1.4978 1.2557 0.1847  -0.2535 0.1076  141 TYR L N   
12498 C CA  . TYR H 141 ? 2.0344 1.5018 1.2463 0.1714  -0.2851 0.1137  141 TYR L CA  
12499 C C   . TYR H 141 ? 2.1016 1.5674 1.2798 0.1592  -0.2811 0.1270  141 TYR L C   
12500 O O   . TYR H 141 ? 2.0770 1.5450 1.2563 0.1716  -0.2652 0.1306  141 TYR L O   
12501 C CB  . TYR H 141 ? 2.0704 1.5122 1.2759 0.1880  -0.3135 0.1084  141 TYR L CB  
12502 C CG  . TYR H 141 ? 2.1191 1.5254 1.2842 0.1722  -0.3554 0.1156  141 TYR L CG  
12503 C CD1 . TYR H 141 ? 2.1575 1.5523 1.3222 0.1599  -0.3805 0.1120  141 TYR L CD1 
12504 C CD2 . TYR H 141 ? 2.1483 1.5302 1.2747 0.1678  -0.3733 0.1276  141 TYR L CD2 
12505 C CE1 . TYR H 141 ? 2.1999 1.5597 1.3259 0.1413  -0.4242 0.1211  141 TYR L CE1 
12506 C CE2 . TYR H 141 ? 2.1971 1.5434 1.2834 0.1491  -0.4176 0.1374  141 TYR L CE2 
12507 C CZ  . TYR H 141 ? 2.2841 1.6190 1.3703 0.1351  -0.4440 0.1345  141 TYR L CZ  
12508 O OH  . TYR H 141 ? 2.3254 1.6227 1.3704 0.1129  -0.4923 0.1466  141 TYR L OH  
12509 N N   . PRO H 142 ? 2.1047 1.5714 1.2522 0.1337  -0.2954 0.1348  142 PRO L N   
12510 C CA  . PRO H 142 ? 2.1390 1.6068 1.2796 0.1132  -0.3160 0.1330  142 PRO L CA  
12511 C C   . PRO H 142 ? 2.2072 1.7075 1.3760 0.1086  -0.2934 0.1225  142 PRO L C   
12512 O O   . PRO H 142 ? 2.1947 1.7139 1.3854 0.1200  -0.2644 0.1177  142 PRO L O   
12513 C CB  . PRO H 142 ? 2.1855 1.6484 1.2766 0.0858  -0.3399 0.1490  142 PRO L CB  
12514 C CG  . PRO H 142 ? 2.2118 1.6928 1.2943 0.0892  -0.3151 0.1550  142 PRO L CG  
12515 C CD  . PRO H 142 ? 2.1258 1.5991 1.2404 0.1207  -0.2918 0.1477  142 PRO L CD  
12516 N N   . ARG H 143 ? 2.1791 1.6834 1.3467 0.0916  -0.3096 0.1189  143 ARG L N   
12517 C CA  . ARG H 143 ? 2.1681 1.7007 1.3596 0.0862  -0.2943 0.1074  143 ARG L CA  
12518 C C   . ARG H 143 ? 2.2260 1.7945 1.4106 0.0795  -0.2745 0.1045  143 ARG L C   
12519 O O   . ARG H 143 ? 2.2065 1.7956 1.4175 0.0864  -0.2560 0.0917  143 ARG L O   
12520 C CB  . ARG H 143 ? 2.1939 1.7251 1.3738 0.0635  -0.3204 0.1072  143 ARG L CB  
12521 C CG  . ARG H 143 ? 2.2772 1.8286 1.4875 0.0627  -0.3087 0.0933  143 ARG L CG  
12522 C CD  . ARG H 143 ? 2.3289 1.8786 1.5267 0.0387  -0.3351 0.0944  143 ARG L CD  
12523 N NE  . ARG H 143 ? 2.3206 1.8755 1.5527 0.0443  -0.3270 0.0818  143 ARG L NE  
12524 C CZ  . ARG H 143 ? 2.4496 1.9993 1.6806 0.0280  -0.3471 0.0809  143 ARG L CZ  
12525 N NH1 . ARG H 143 ? 2.3326 1.8705 1.5294 0.0032  -0.3790 0.0925  143 ARG L NH1 
12526 N NH2 . ARG H 143 ? 2.2195 1.7735 1.4823 0.0343  -0.3379 0.0701  143 ARG L NH2 
12527 N N   . GLU H 144 ? 2.2051 1.7798 1.3534 0.0667  -0.2816 0.1160  144 GLU L N   
12528 C CA  . GLU H 144 ? 2.1960 1.8089 1.3294 0.0588  -0.2681 0.1146  144 GLU L CA  
12529 C C   . GLU H 144 ? 2.2149 1.8314 1.3757 0.0842  -0.2384 0.1068  144 GLU L C   
12530 O O   . GLU H 144 ? 2.2044 1.8027 1.3592 0.0949  -0.2322 0.1165  144 GLU L O   
12531 C CB  . GLU H 144 ? 2.2348 1.8473 1.3199 0.0373  -0.2878 0.1335  144 GLU L CB  
12532 C CG  . GLU H 144 ? 2.3925 1.9988 1.4464 0.0066  -0.3235 0.1446  144 GLU L CG  
12533 C CD  . GLU H 144 ? 2.6249 2.1748 1.6723 0.0102  -0.3521 0.1543  144 GLU L CD  
12534 O OE1 . GLU H 144 ? 2.4339 1.9644 1.5128 0.0259  -0.3515 0.1436  144 GLU L OE1 
12535 O OE2 . GLU H 144 ? 2.5762 2.1026 1.5858 -0.0034 -0.3784 0.1721  144 GLU L OE2 
12536 N N   . ALA H 145 ? 2.1540 1.7911 1.3449 0.0932  -0.2233 0.0894  145 ALA L N   
12537 C CA  . ALA H 145 ? 2.1341 1.7723 1.3534 0.1145  -0.2012 0.0808  145 ALA L CA  
12538 C C   . ALA H 145 ? 2.1817 1.8531 1.4165 0.1169  -0.1954 0.0594  145 ALA L C   
12539 O O   . ALA H 145 ? 2.1897 1.8823 1.4204 0.1042  -0.2058 0.0503  145 ALA L O   
12540 C CB  . ALA H 145 ? 2.1360 1.7428 1.3878 0.1303  -0.1952 0.0831  145 ALA L CB  
12541 N N   . LYS H 146 ? 2.1275 1.8026 1.3804 0.1338  -0.1816 0.0503  146 LYS L N   
12542 C CA  . LYS H 146 ? 2.1268 1.8290 1.3964 0.1421  -0.1802 0.0259  146 LYS L CA  
12543 C C   . LYS H 146 ? 2.1698 1.8469 1.4735 0.1626  -0.1731 0.0195  146 LYS L C   
12544 O O   . LYS H 146 ? 2.1610 1.8203 1.4667 0.1704  -0.1643 0.0304  146 LYS L O   
12545 C CB  . LYS H 146 ? 2.1631 1.9150 1.4076 0.1371  -0.1799 0.0151  146 LYS L CB  
12546 C CG  . LYS H 146 ? 2.3547 2.1450 1.6145 0.1484  -0.1822 -0.0166 146 LYS L CG  
12547 C CD  . LYS H 146 ? 2.4699 2.2792 1.7350 0.1385  -0.1930 -0.0302 146 LYS L CD  
12548 C CE  . LYS H 146 ? 2.6060 2.4406 1.8941 0.1566  -0.1970 -0.0639 146 LYS L CE  
12549 N NZ  . LYS H 146 ? 2.7180 2.5675 2.0123 0.1474  -0.2071 -0.0762 146 LYS L NZ  
12550 N N   . VAL H 147 ? 2.1295 1.8047 1.4583 0.1691  -0.1797 0.0025  147 VAL L N   
12551 C CA  . VAL H 147 ? 2.1323 1.7807 1.4927 0.1846  -0.1811 -0.0037 147 VAL L CA  
12552 C C   . VAL H 147 ? 2.2106 1.8827 1.5778 0.1987  -0.1894 -0.0337 147 VAL L C   
12553 O O   . VAL H 147 ? 2.2125 1.9187 1.5737 0.1961  -0.1963 -0.0534 147 VAL L O   
12554 C CB  . VAL H 147 ? 2.1783 1.7991 1.5628 0.1813  -0.1867 0.0024  147 VAL L CB  
12555 C CG1 . VAL H 147 ? 2.1821 1.7718 1.5951 0.1911  -0.1909 0.0044  147 VAL L CG1 
12556 C CG2 . VAL H 147 ? 2.1656 1.7745 1.5427 0.1701  -0.1814 0.0250  147 VAL L CG2 
12557 N N   . GLN H 148 ? 2.1823 1.8381 1.5623 0.2139  -0.1907 -0.0383 148 GLN L N   
12558 C CA  . GLN H 148 ? 2.1983 1.8711 1.5876 0.2329  -0.2029 -0.0698 148 GLN L CA  
12559 C C   . GLN H 148 ? 2.2782 1.9028 1.6980 0.2449  -0.2184 -0.0722 148 GLN L C   
12560 O O   . GLN H 148 ? 2.2786 1.8716 1.7050 0.2458  -0.2162 -0.0546 148 GLN L O   
12561 C CB  . GLN H 148 ? 2.2092 1.9100 1.5809 0.2403  -0.1954 -0.0751 148 GLN L CB  
12562 C CG  . GLN H 148 ? 2.3670 2.1219 1.7055 0.2261  -0.1854 -0.0740 148 GLN L CG  
12563 C CD  . GLN H 148 ? 2.6036 2.3701 1.9225 0.2263  -0.1743 -0.0631 148 GLN L CD  
12564 O OE1 . GLN H 148 ? 2.5242 2.2711 1.8276 0.2131  -0.1635 -0.0337 148 GLN L OE1 
12565 N NE2 . GLN H 148 ? 2.5229 2.3224 1.8425 0.2430  -0.1783 -0.0881 148 GLN L NE2 
12566 N N   . TRP H 149 ? 2.2210 2.0110 2.2699 0.3413  -0.2653 0.2327  149 TRP L N   
12567 C CA  . TRP H 149 ? 2.2202 2.0153 2.2743 0.3400  -0.2667 0.2315  149 TRP L CA  
12568 C C   . TRP H 149 ? 2.2615 2.0560 2.3076 0.3374  -0.2666 0.2303  149 TRP L C   
12569 O O   . TRP H 149 ? 2.2570 2.0511 2.2991 0.3369  -0.2687 0.2306  149 TRP L O   
12570 C CB  . TRP H 149 ? 2.2110 2.0106 2.2694 0.3412  -0.2725 0.2332  149 TRP L CB  
12571 C CG  . TRP H 149 ? 2.2292 2.0332 2.3022 0.3445  -0.2747 0.2335  149 TRP L CG  
12572 C CD1 . TRP H 149 ? 2.2749 2.0770 2.3521 0.3482  -0.2807 0.2376  149 TRP L CD1 
12573 C CD2 . TRP H 149 ? 2.2271 2.0366 2.3135 0.3442  -0.2713 0.2286  149 TRP L CD2 
12574 N NE1 . TRP H 149 ? 2.2686 2.0780 2.3659 0.3518  -0.2827 0.2366  149 TRP L NE1 
12575 C CE2 . TRP H 149 ? 2.2803 2.0946 2.3844 0.3488  -0.2758 0.2298  149 TRP L CE2 
12576 C CE3 . TRP H 149 ? 2.2408 2.0487 2.3245 0.3398  -0.2648 0.2219  149 TRP L CE3 
12577 C CZ2 . TRP H 149 ? 2.2705 2.0915 2.3950 0.3491  -0.2729 0.2232  149 TRP L CZ2 
12578 C CZ3 . TRP H 149 ? 2.2600 2.0706 2.3580 0.3384  -0.2607 0.2144  149 TRP L CZ3 
12579 C CH2 . TRP H 149 ? 2.2687 2.0873 2.3893 0.3430  -0.2642 0.2144  149 TRP L CH2 
12580 N N   . LYS H 150 ? 2.2123 2.0041 2.2562 0.3346  -0.2642 0.2284  150 LYS L N   
12581 C CA  . LYS H 150 ? 2.2059 1.9950 2.2424 0.3330  -0.2663 0.2283  150 LYS L CA  
12582 C C   . LYS H 150 ? 2.2504 2.0364 2.2824 0.3322  -0.2660 0.2263  150 LYS L C   
12583 O O   . LYS H 150 ? 2.2426 2.0214 2.2704 0.3283  -0.2627 0.2224  150 LYS L O   
12584 C CB  . LYS H 150 ? 2.2370 2.0203 2.2672 0.3284  -0.2650 0.2284  150 LYS L CB  
12585 C CG  . LYS H 150 ? 2.3245 2.1117 2.3547 0.3285  -0.2635 0.2292  150 LYS L CG  
12586 C CD  . LYS H 150 ? 2.3835 2.1661 2.4057 0.3213  -0.2609 0.2298  150 LYS L CD  
12587 C CE  . LYS H 150 ? 2.4176 2.2052 2.4371 0.3205  -0.2571 0.2290  150 LYS L CE  
12588 N NZ  . LYS H 150 ? 2.4860 2.2705 2.4957 0.3112  -0.2540 0.2303  150 LYS L NZ  
12589 N N   . VAL H 151 ? 2.2079 1.9971 2.2393 0.3342  -0.2673 0.2277  151 VAL L N   
12590 C CA  . VAL H 151 ? 2.2098 1.9955 2.2331 0.3333  -0.2645 0.2257  151 VAL L CA  
12591 C C   . VAL H 151 ? 2.2675 2.0463 2.2845 0.3345  -0.2677 0.2275  151 VAL L C   
12592 O O   . VAL H 151 ? 2.2564 2.0393 2.2804 0.3366  -0.2686 0.2302  151 VAL L O   
12593 C CB  . VAL H 151 ? 2.2536 2.0470 2.2798 0.3328  -0.2614 0.2269  151 VAL L CB  
12594 C CG1 . VAL H 151 ? 2.2540 2.0438 2.2686 0.3310  -0.2552 0.2247  151 VAL L CG1 
12595 C CG2 . VAL H 151 ? 2.2487 2.0488 2.2824 0.3324  -0.2620 0.2260  151 VAL L CG2 
12596 N N   . ASP H 152 ? 2.2423 2.0085 2.2470 0.3319  -0.2697 0.2256  152 ASP L N   
12597 C CA  . ASP H 152 ? 2.2568 2.0128 2.2530 0.3327  -0.2761 0.2282  152 ASP L CA  
12598 C C   . ASP H 152 ? 2.3212 2.0869 2.3322 0.3360  -0.2831 0.2325  152 ASP L C   
12599 O O   . ASP H 152 ? 2.3140 2.0845 2.3352 0.3406  -0.2853 0.2345  152 ASP L O   
12600 C CB  . ASP H 152 ? 2.2843 2.0340 2.2714 0.3355  -0.2732 0.2280  152 ASP L CB  
12601 C CG  . ASP H 152 ? 2.4011 2.1413 2.3703 0.3314  -0.2643 0.2211  152 ASP L CG  
12602 O OD1 . ASP H 152 ? 2.3936 2.1443 2.3698 0.3297  -0.2580 0.2178  152 ASP L OD1 
12603 O OD2 . ASP H 152 ? 2.4910 2.2125 2.4384 0.3297  -0.2637 0.2183  152 ASP L OD2 
12604 N N   . ASN H 153 ? 2.2923 2.0609 2.3056 0.3325  -0.2842 0.2325  153 ASN L N   
12605 C CA  . ASN H 153 ? 2.2928 2.0711 2.3168 0.3335  -0.2880 0.2337  153 ASN L CA  
12606 C C   . ASN H 153 ? 2.3305 2.1206 2.3691 0.3371  -0.2838 0.2315  153 ASN L C   
12607 O O   . ASN H 153 ? 2.3217 2.1174 2.3639 0.3358  -0.2821 0.2293  153 ASN L O   
12608 C CB  . ASN H 153 ? 2.3343 2.1105 2.3595 0.3350  -0.2986 0.2367  153 ASN L CB  
12609 C CG  . ASN H 153 ? 2.6712 2.4585 2.7063 0.3342  -0.3022 0.2360  153 ASN L CG  
12610 O OD1 . ASN H 153 ? 2.5954 2.3942 2.6477 0.3385  -0.3013 0.2325  153 ASN L OD1 
12611 N ND2 . ASN H 153 ? 2.5788 2.3616 2.6019 0.3266  -0.3043 0.2379  153 ASN L ND2 
12612 N N   . ALA H 154 ? 2.2782 2.0690 2.3214 0.3393  -0.2808 0.2313  154 ALA L N   
12613 C CA  . ALA H 154 ? 2.2623 2.0578 2.3149 0.3386  -0.2760 0.2288  154 ALA L CA  
12614 C C   . ALA H 154 ? 2.2854 2.0809 2.3324 0.3362  -0.2723 0.2282  154 ALA L C   
12615 O O   . ALA H 154 ? 2.2704 2.0648 2.3126 0.3357  -0.2704 0.2298  154 ALA L O   
12616 C CB  . ALA H 154 ? 2.2722 2.0657 2.3279 0.3382  -0.2717 0.2299  154 ALA L CB  
12617 N N   . LEU H 155 ? 2.2360 2.0322 2.2836 0.3350  -0.2714 0.2251  155 LEU L N   
12618 C CA  . LEU H 155 ? 2.2318 2.0251 2.2733 0.3339  -0.2690 0.2248  155 LEU L CA  
12619 C C   . LEU H 155 ? 2.2663 2.0551 2.3066 0.3306  -0.2679 0.2250  155 LEU L C   
12620 O O   . LEU H 155 ? 2.2627 2.0470 2.3048 0.3261  -0.2656 0.2212  155 LEU L O   
12621 C CB  . LEU H 155 ? 2.2363 2.0280 2.2733 0.3328  -0.2664 0.2203  155 LEU L CB  
12622 C CG  . LEU H 155 ? 2.2982 2.0934 2.3321 0.3328  -0.2655 0.2214  155 LEU L CG  
12623 C CD1 . LEU H 155 ? 2.2988 2.0996 2.3378 0.3321  -0.2687 0.2190  155 LEU L CD1 
12624 C CD2 . LEU H 155 ? 2.3382 2.1297 2.3626 0.3314  -0.2589 0.2194  155 LEU L CD2 
12625 N N   . GLN H 156 ? 2.2087 1.9981 2.2469 0.3311  -0.2693 0.2288  156 GLN L N   
12626 C CA  . GLN H 156 ? 2.2009 1.9865 2.2357 0.3261  -0.2698 0.2308  156 GLN L CA  
12627 C C   . GLN H 156 ? 2.2410 2.0177 2.2681 0.3245  -0.2732 0.2312  156 GLN L C   
12628 O O   . GLN H 156 ? 2.2362 2.0142 2.2644 0.3300  -0.2752 0.2324  156 GLN L O   
12629 C CB  . GLN H 156 ? 2.2135 2.0066 2.2507 0.3269  -0.2701 0.2340  156 GLN L CB  
12630 C CG  . GLN H 156 ? 2.3979 2.1942 2.4357 0.3272  -0.2656 0.2333  156 GLN L CG  
12631 C CD  . GLN H 156 ? 2.6404 2.4325 2.6783 0.3214  -0.2605 0.2331  156 GLN L CD  
12632 O OE1 . GLN H 156 ? 2.5780 2.3653 2.6121 0.3130  -0.2578 0.2343  156 GLN L OE1 
12633 N NE2 . GLN H 156 ? 2.5342 2.3263 2.5766 0.3245  -0.2589 0.2319  156 GLN L NE2 
12634 N N   . SER H 157 ? 2.1926 1.9570 2.2104 0.3155  -0.2729 0.2301  157 SER L N   
12635 C CA  . SER H 157 ? 2.1989 1.9474 2.2025 0.3114  -0.2772 0.2301  157 SER L CA  
12636 C C   . SER H 157 ? 2.2516 1.9910 2.2465 0.3003  -0.2804 0.2342  157 SER L C   
12637 O O   . SER H 157 ? 2.2367 1.9759 2.2330 0.2916  -0.2741 0.2334  157 SER L O   
12638 C CB  . SER H 157 ? 2.2466 1.9799 2.2390 0.3069  -0.2720 0.2210  157 SER L CB  
12639 O OG  . SER H 157 ? 2.3842 2.0979 2.3572 0.3040  -0.2757 0.2200  157 SER L OG  
12640 N N   . GLY H 158 ? 2.2270 1.9582 2.2131 0.2998  -0.2898 0.2391  158 GLY L N   
12641 C CA  . GLY H 158 ? 2.2421 1.9631 2.2166 0.2875  -0.2956 0.2445  158 GLY L CA  
12642 C C   . GLY H 158 ? 2.2898 2.0305 2.2774 0.2926  -0.3029 0.2523  158 GLY L C   
12643 O O   . GLY H 158 ? 2.3014 2.0372 2.2841 0.2911  -0.3150 0.2585  158 GLY L O   
12644 N N   . ASN H 159 ? 2.5340 2.1517 1.8728 0.4497  -0.1322 0.1746  159 ASN L N   
12645 C CA  . ASN H 159 ? 2.5772 2.1108 1.9049 0.4079  -0.1160 0.1624  159 ASN L CA  
12646 C C   . ASN H 159 ? 2.5322 2.1363 1.9520 0.3634  -0.1408 0.1519  159 ASN L C   
12647 O O   . ASN H 159 ? 2.5357 2.1065 1.9729 0.3125  -0.1434 0.1370  159 ASN L O   
12648 C CB  . ASN H 159 ? 2.6818 2.1310 1.9277 0.4479  -0.0710 0.1776  159 ASN L CB  
12649 C CG  . ASN H 159 ? 3.0043 2.5269 2.2480 0.5106  -0.0629 0.1997  159 ASN L CG  
12650 O OD1 . ASN H 159 ? 2.8497 2.4859 2.1712 0.5064  -0.0900 0.1990  159 ASN L OD1 
12651 N ND2 . ASN H 159 ? 3.0086 2.4697 2.1566 0.5717  -0.0221 0.2198  159 ASN L ND2 
12652 N N   . SER H 160 ? 2.3987 2.1035 1.8723 0.3824  -0.1577 0.1597  160 SER L N   
12653 C CA  . SER H 160 ? 2.3060 2.0791 1.8586 0.3496  -0.1791 0.1536  160 SER L CA  
12654 C C   . SER H 160 ? 2.2726 2.0960 1.8836 0.3102  -0.2084 0.1401  160 SER L C   
12655 O O   . SER H 160 ? 2.2471 2.1011 1.8603 0.3216  -0.2196 0.1387  160 SER L O   
12656 C CB  . SER H 160 ? 2.3031 2.1596 1.8802 0.3835  -0.1820 0.1645  160 SER L CB  
12657 O OG  . SER H 160 ? 2.3861 2.3107 1.9670 0.4070  -0.1934 0.1673  160 SER L OG  
12658 N N   . GLN H 161 ? 2.1847 2.0198 1.8401 0.2686  -0.2185 0.1325  161 GLN L N   
12659 C CA  . GLN H 161 ? 2.1161 2.0024 1.8243 0.2358  -0.2403 0.1226  161 GLN L CA  
12660 C C   . GLN H 161 ? 2.0972 2.0357 1.8551 0.2224  -0.2490 0.1270  161 GLN L C   
12661 O O   . GLN H 161 ? 2.1083 2.0229 1.8629 0.2149  -0.2409 0.1320  161 GLN L O   
12662 C CB  . GLN H 161 ? 2.1635 2.0084 1.8599 0.1985  -0.2391 0.1096  161 GLN L CB  
12663 C CG  . GLN H 161 ? 2.3393 2.1398 1.9914 0.2077  -0.2344 0.1026  161 GLN L CG  
12664 C CD  . GLN H 161 ? 2.5380 2.2842 2.1626 0.1678  -0.2262 0.0868  161 GLN L CD  
12665 O OE1 . GLN H 161 ? 2.4213 2.2083 2.0830 0.1302  -0.2367 0.0767  161 GLN L OE1 
12666 N NE2 . GLN H 161 ? 2.5058 2.1608 2.0581 0.1758  -0.2042 0.0842  161 GLN L NE2 
12667 N N   . GLU H 162 ? 1.9829 1.9863 1.7808 0.2212  -0.2623 0.1260  162 GLU L N   
12668 C CA  . GLU H 162 ? 1.9292 1.9741 1.7639 0.2106  -0.2671 0.1305  162 GLU L CA  
12669 C C   . GLU H 162 ? 1.9349 2.0026 1.7984 0.1830  -0.2739 0.1282  162 GLU L C   
12670 O O   . GLU H 162 ? 1.9308 2.0085 1.7986 0.1770  -0.2778 0.1212  162 GLU L O   
12671 C CB  . GLU H 162 ? 1.9162 2.0131 1.7635 0.2287  -0.2692 0.1312  162 GLU L CB  
12672 C CG  . GLU H 162 ? 2.0610 2.1617 1.8887 0.2572  -0.2604 0.1378  162 GLU L CG  
12673 C CD  . GLU H 162 ? 2.2733 2.4431 2.1123 0.2700  -0.2623 0.1352  162 GLU L CD  
12674 O OE1 . GLU H 162 ? 2.1503 2.3545 2.0178 0.2506  -0.2662 0.1312  162 GLU L OE1 
12675 O OE2 . GLU H 162 ? 2.1900 2.3809 2.0034 0.2994  -0.2575 0.1374  162 GLU L OE2 
12676 N N   . SER H 163 ? 1.8491 1.9286 1.7290 0.1718  -0.2737 0.1365  163 SER L N   
12677 C CA  . SER H 163 ? 1.8063 1.9131 1.7049 0.1540  -0.2754 0.1407  163 SER L CA  
12678 C C   . SER H 163 ? 1.8079 1.9323 1.7182 0.1568  -0.2731 0.1520  163 SER L C   
12679 O O   . SER H 163 ? 1.8127 1.9249 1.7204 0.1650  -0.2725 0.1574  163 SER L O   
12680 C CB  . SER H 163 ? 1.8651 1.9599 1.7565 0.1324  -0.2755 0.1413  163 SER L CB  
12681 O OG  . SER H 163 ? 1.9369 2.0744 1.8419 0.1219  -0.2755 0.1466  163 SER L OG  
12682 N N   . VAL H 164 ? 1.7196 1.8691 1.6375 0.1532  -0.2685 0.1563  164 VAL L N   
12683 C CA  . VAL H 164 ? 1.6964 1.8523 1.6143 0.1555  -0.2619 0.1673  164 VAL L CA  
12684 C C   . VAL H 164 ? 1.7400 1.9105 1.6516 0.1527  -0.2536 0.1817  164 VAL L C   
12685 O O   . VAL H 164 ? 1.7380 1.9268 1.6486 0.1529  -0.2483 0.1793  164 VAL L O   
12686 C CB  . VAL H 164 ? 1.7318 1.8947 1.6490 0.1591  -0.2551 0.1581  164 VAL L CB  
12687 C CG1 . VAL H 164 ? 1.7297 1.8950 1.6493 0.1664  -0.2605 0.1526  164 VAL L CG1 
12688 C CG2 . VAL H 164 ? 1.7267 1.9009 1.6459 0.1592  -0.2516 0.1458  164 VAL L CG2 
12689 N N   . THR H 165 ? 1.6836 1.8501 1.5877 0.1553  -0.2507 0.1984  165 THR L N   
12690 C CA  . THR H 165 ? 1.6748 1.8568 1.5621 0.1607  -0.2392 0.2182  165 THR L CA  
12691 C C   . THR H 165 ? 1.7220 1.8868 1.5880 0.1691  -0.2195 0.2207  165 THR L C   
12692 O O   . THR H 165 ? 1.7250 1.8699 1.5924 0.1650  -0.2191 0.2098  165 THR L O   
12693 C CB  . THR H 165 ? 1.7363 1.9213 1.6202 0.1615  -0.2456 0.2387  165 THR L CB  
12694 O OG1 . THR H 165 ? 1.6871 1.8457 1.5755 0.1654  -0.2503 0.2380  165 THR L OG1 
12695 C CG2 . THR H 165 ? 1.7347 1.9381 1.6303 0.1469  -0.2580 0.2376  165 THR L CG2 
12696 N N   . GLU H 166 ? 1.6690 1.8431 1.5099 0.1810  -0.1995 0.2347  166 GLU L N   
12697 C CA  . GLU H 166 ? 1.6790 1.8223 1.4842 0.1901  -0.1710 0.2395  166 GLU L CA  
12698 C C   . GLU H 166 ? 1.7201 1.8314 1.5003 0.1927  -0.1653 0.2542  166 GLU L C   
12699 O O   . GLU H 166 ? 1.6884 1.8103 1.4826 0.1927  -0.1844 0.2647  166 GLU L O   
12700 C CB  . GLU H 166 ? 1.7073 1.8687 1.4835 0.2116  -0.1458 0.2557  166 GLU L CB  
12701 C CG  . GLU H 166 ? 1.8084 1.9890 1.6007 0.2131  -0.1413 0.2386  166 GLU L CG  
12702 C CD  . GLU H 166 ? 2.1693 2.3108 1.9535 0.2065  -0.1238 0.2202  166 GLU L CD  
12703 O OE1 . GLU H 166 ? 2.1811 2.2758 1.9304 0.2032  -0.1020 0.2230  166 GLU L OE1 
12704 O OE2 . GLU H 166 ? 2.1261 2.2838 1.9360 0.2028  -0.1311 0.2025  166 GLU L OE2 
12705 N N   . GLN H 167 ? 1.7056 1.7731 1.4455 0.1938  -0.1368 0.2539  167 GLN L N   
12706 C CA  . GLN H 167 ? 1.7280 1.7557 1.4341 0.1951  -0.1262 0.2655  167 GLN L CA  
12707 C C   . GLN H 167 ? 1.7872 1.8261 1.4719 0.2196  -0.1273 0.3012  167 GLN L C   
12708 O O   . GLN H 167 ? 1.7932 1.8528 1.4548 0.2405  -0.1125 0.3211  167 GLN L O   
12709 C CB  . GLN H 167 ? 1.7955 1.7653 1.4469 0.1904  -0.0861 0.2594  167 GLN L CB  
12710 C CG  . GLN H 167 ? 1.8974 1.8275 1.5285 0.1720  -0.0808 0.2495  167 GLN L CG  
12711 C CD  . GLN H 167 ? 2.0759 1.9404 1.6465 0.1572  -0.0374 0.2381  167 GLN L CD  
12712 O OE1 . GLN H 167 ? 2.0314 1.8594 1.5528 0.1738  -0.0010 0.2508  167 GLN L OE1 
12713 N NE2 . GLN H 167 ? 1.9440 1.7923 1.5114 0.1259  -0.0365 0.2137  167 GLN L NE2 
12714 N N   . ASP H 168 ? 1.7340 1.7702 1.4289 0.2193  -0.1456 0.3101  168 ASP L N   
12715 C CA  . ASP H 168 ? 1.7284 1.7802 1.4066 0.2414  -0.1506 0.3453  168 ASP L CA  
12716 C C   . ASP H 168 ? 1.8301 1.8420 1.4328 0.2677  -0.1148 0.3745  168 ASP L C   
12717 O O   . ASP H 168 ? 1.8696 1.8197 1.4319 0.2626  -0.0898 0.3658  168 ASP L O   
12718 C CB  . ASP H 168 ? 1.7266 1.7801 1.4350 0.2370  -0.1771 0.3467  168 ASP L CB  
12719 C CG  . ASP H 168 ? 1.8096 1.9007 1.5251 0.2520  -0.1932 0.3770  168 ASP L CG  
12720 O OD1 . ASP H 168 ? 1.7827 1.9132 1.5411 0.2398  -0.2146 0.3691  168 ASP L OD1 
12721 O OD2 . ASP H 168 ? 1.8917 1.9710 1.5650 0.2752  -0.1825 0.4091  168 ASP L OD2 
12722 N N   . SER H 169 ? 1.7828 1.8318 1.3602 0.2954  -0.1090 0.4089  169 SER L N   
12723 C CA  . SER H 169 ? 1.8276 1.8462 1.3227 0.3319  -0.0717 0.4450  169 SER L CA  
12724 C C   . SER H 169 ? 1.8867 1.8547 1.3459 0.3425  -0.0703 0.4649  169 SER L C   
12725 O O   . SER H 169 ? 1.9485 1.8481 1.3298 0.3619  -0.0325 0.4808  169 SER L O   
12726 C CB  . SER H 169 ? 1.8551 1.9520 1.3378 0.3608  -0.0700 0.4775  169 SER L CB  
12727 O OG  . SER H 169 ? 1.9135 2.0677 1.4359 0.3555  -0.1060 0.4911  169 SER L OG  
12728 N N   . LYS H 170 ? 1.7814 1.7775 1.2931 0.3312  -0.1085 0.4639  170 LYS L N   
12729 C CA  . LYS H 170 ? 1.7890 1.7494 1.2770 0.3443  -0.1130 0.4839  170 LYS L CA  
12730 C C   . LYS H 170 ? 1.8530 1.7576 1.3520 0.3186  -0.1143 0.4511  170 LYS L C   
12731 O O   . LYS H 170 ? 1.9005 1.7404 1.3385 0.3281  -0.0907 0.4610  170 LYS L O   
12732 C CB  . LYS H 170 ? 1.7696 1.7912 1.3024 0.3516  -0.1492 0.5049  170 LYS L CB  
12733 C CG  . LYS H 170 ? 1.9014 2.0000 1.4306 0.3677  -0.1520 0.5328  170 LYS L CG  
12734 C CD  . LYS H 170 ? 1.9634 2.1188 1.5460 0.3601  -0.1886 0.5427  170 LYS L CD  
12735 C CE  . LYS H 170 ? 1.9557 2.1979 1.5677 0.3469  -0.2002 0.5433  170 LYS L CE  
12736 N NZ  . LYS H 170 ? 1.9282 2.2152 1.5847 0.3338  -0.2307 0.5515  170 LYS L NZ  
12737 N N   . ASP H 171 ? 1.7751 1.7070 1.3448 0.2872  -0.1390 0.4128  171 ASP L N   
12738 C CA  . ASP H 171 ? 1.7829 1.6875 1.3679 0.2640  -0.1426 0.3814  171 ASP L CA  
12739 C C   . ASP H 171 ? 1.8549 1.7532 1.4530 0.2306  -0.1316 0.3390  171 ASP L C   
12740 O O   . ASP H 171 ? 1.8455 1.7449 1.4641 0.2086  -0.1378 0.3103  171 ASP L O   
12741 C CB  . ASP H 171 ? 1.7501 1.6971 1.3996 0.2648  -0.1796 0.3777  171 ASP L CB  
12742 C CG  . ASP H 171 ? 1.7540 1.7555 1.4682 0.2548  -0.2043 0.3633  171 ASP L CG  
12743 O OD1 . ASP H 171 ? 1.7267 1.7510 1.4409 0.2579  -0.2039 0.3748  171 ASP L OD1 
12744 O OD2 . ASP H 171 ? 1.7977 1.8203 1.5578 0.2471  -0.2224 0.3428  171 ASP L OD2 
12745 N N   . SER H 172 ? 1.8318 1.7299 1.4157 0.2289  -0.1138 0.3362  172 SER L N   
12746 C CA  . SER H 172 ? 1.8431 1.7352 1.4346 0.2010  -0.1007 0.3008  172 SER L CA  
12747 C C   . SER H 172 ? 1.8488 1.7910 1.5105 0.1776  -0.1316 0.2678  172 SER L C   
12748 O O   . SER H 172 ? 1.8627 1.8009 1.5261 0.1506  -0.1235 0.2368  172 SER L O   
12749 C CB  . SER H 172 ? 1.9641 1.7832 1.4874 0.1856  -0.0601 0.2898  172 SER L CB  
12750 O OG  . SER H 172 ? 2.1497 1.9140 1.5956 0.2145  -0.0247 0.3234  172 SER L OG  
12751 N N   . THR H 173 ? 1.7499 1.7400 1.4631 0.1887  -0.1636 0.2753  173 THR L N   
12752 C CA  . THR H 173 ? 1.7059 1.7383 1.4750 0.1771  -0.1885 0.2507  173 THR L CA  
12753 C C   . THR H 173 ? 1.7244 1.7884 1.5270 0.1783  -0.2029 0.2473  173 THR L C   
12754 O O   . THR H 173 ? 1.7022 1.7752 1.5052 0.1903  -0.2080 0.2684  173 THR L O   
12755 C CB  . THR H 173 ? 1.7749 1.8228 1.5679 0.1891  -0.2083 0.2582  173 THR L CB  
12756 O OG1 . THR H 173 ? 1.7493 1.7997 1.5448 0.2095  -0.2187 0.2894  173 THR L OG1 
12757 C CG2 . THR H 173 ? 1.7816 1.8064 1.5469 0.1847  -0.1968 0.2542  173 THR L CG2 
12758 N N   . TYR H 174 ? 1.6854 1.7712 1.5137 0.1651  -0.2092 0.2204  174 TYR L N   
12759 C CA  . TYR H 174 ? 1.6740 1.7829 1.5292 0.1648  -0.2214 0.2126  174 TYR L CA  
12760 C C   . TYR H 174 ? 1.7190 1.8452 1.6046 0.1740  -0.2425 0.2139  174 TYR L C   
12761 O O   . TYR H 174 ? 1.7134 1.8439 1.6058 0.1816  -0.2475 0.2150  174 TYR L O   
12762 C CB  . TYR H 174 ? 1.6947 1.8151 1.5541 0.1504  -0.2151 0.1863  174 TYR L CB  
12763 C CG  . TYR H 174 ? 1.7486 1.8431 1.5739 0.1393  -0.1884 0.1823  174 TYR L CG  
12764 C CD1 . TYR H 174 ? 1.7850 1.8715 1.5989 0.1449  -0.1762 0.1887  174 TYR L CD1 
12765 C CD2 . TYR H 174 ? 1.7845 1.8615 1.5850 0.1229  -0.1715 0.1707  174 TYR L CD2 
12766 C CE1 . TYR H 174 ? 1.8359 1.8907 1.6122 0.1398  -0.1449 0.1864  174 TYR L CE1 
12767 C CE2 . TYR H 174 ? 1.8378 1.8760 1.5966 0.1103  -0.1397 0.1661  174 TYR L CE2 
12768 C CZ  . TYR H 174 ? 1.9447 1.9683 1.6902 0.1214  -0.1250 0.1754  174 TYR L CZ  
12769 O OH  . TYR H 174 ? 2.0015 1.9794 1.6999 0.1142  -0.0873 0.1727  174 TYR L OH  
12770 N N   . SER H 175 ? 1.6707 1.8034 1.5699 0.1741  -0.2514 0.2134  175 SER L N   
12771 C CA  . SER H 175 ? 1.6615 1.7946 1.5777 0.1812  -0.2637 0.2139  175 SER L CA  
12772 C C   . SER H 175 ? 1.7249 1.8592 1.6461 0.1771  -0.2667 0.1977  175 SER L C   
12773 O O   . SER H 175 ? 1.7242 1.8623 1.6415 0.1674  -0.2642 0.1940  175 SER L O   
12774 C CB  . SER H 175 ? 1.6911 1.8177 1.6064 0.1822  -0.2686 0.2359  175 SER L CB  
12775 O OG  . SER H 175 ? 1.7504 1.8744 1.6558 0.1909  -0.2660 0.2547  175 SER L OG  
12776 N N   . LEU H 176 ? 1.6918 1.8230 1.6167 0.1892  -0.2693 0.1898  176 LEU L N   
12777 C CA  . LEU H 176 ? 1.7059 1.8295 1.6247 0.1913  -0.2695 0.1772  176 LEU L CA  
12778 C C   . LEU H 176 ? 1.7894 1.8774 1.6979 0.1955  -0.2679 0.1820  176 LEU L C   
12779 O O   . LEU H 176 ? 1.7927 1.8692 1.7020 0.2070  -0.2655 0.1921  176 LEU L O   
12780 C CB  . LEU H 176 ? 1.7039 1.8543 1.6207 0.2064  -0.2670 0.1645  176 LEU L CB  
12781 C CG  . LEU H 176 ? 1.7707 1.9230 1.6767 0.2110  -0.2669 0.1530  176 LEU L CG  
12782 C CD1 . LEU H 176 ? 1.7559 1.9550 1.6655 0.2120  -0.2659 0.1411  176 LEU L CD1 
12783 C CD2 . LEU H 176 ? 1.8362 1.9626 1.7206 0.2342  -0.2615 0.1553  176 LEU L CD2 
12784 N N   . SER H 177 ? 1.7702 1.8370 1.6656 0.1861  -0.2668 0.1736  177 SER L N   
12785 C CA  . SER H 177 ? 1.8159 1.8353 1.6893 0.1832  -0.2594 0.1732  177 SER L CA  
12786 C C   . SER H 177 ? 1.9111 1.9065 1.7584 0.1931  -0.2534 0.1609  177 SER L C   
12787 O O   . SER H 177 ? 1.9065 1.9081 1.7537 0.1784  -0.2584 0.1517  177 SER L O   
12788 C CB  . SER H 177 ? 1.8645 1.8797 1.7402 0.1511  -0.2624 0.1760  177 SER L CB  
12789 O OG  . SER H 177 ? 2.0356 2.0009 1.8837 0.1371  -0.2524 0.1693  177 SER L OG  
12790 N N   . SER H 178 ? 1.9043 1.8761 1.7265 0.2236  -0.2409 0.1630  178 SER L N   
12791 C CA  . SER H 178 ? 1.9435 1.8878 1.7285 0.2425  -0.2313 0.1567  178 SER L CA  
12792 C C   . SER H 178 ? 2.0631 1.9246 1.8019 0.2393  -0.2113 0.1567  178 SER L C   
12793 O O   . SER H 178 ? 2.0819 1.9128 1.8077 0.2514  -0.1967 0.1656  178 SER L O   
12794 C CB  . SER H 178 ? 1.9746 1.9565 1.7517 0.2839  -0.2259 0.1609  178 SER L CB  
12795 O OG  . SER H 178 ? 2.0855 2.0610 1.8302 0.3034  -0.2211 0.1573  178 SER L OG  
12796 N N   . THR H 179 ? 2.0542 1.8767 1.7662 0.2208  -0.2086 0.1459  179 THR L N   
12797 C CA  . THR H 179 ? 2.1365 1.8698 1.7950 0.2073  -0.1860 0.1410  179 THR L CA  
12798 C C   . THR H 179 ? 2.2643 1.9400 1.8581 0.2437  -0.1647 0.1420  179 THR L C   
12799 O O   . THR H 179 ? 2.2456 1.9391 1.8352 0.2504  -0.1746 0.1368  179 THR L O   
12800 C CB  . THR H 179 ? 2.2123 1.9437 1.8816 0.1532  -0.1954 0.1265  179 THR L CB  
12801 O OG1 . THR H 179 ? 2.1107 1.9102 1.8358 0.1316  -0.2145 0.1312  179 THR L OG1 
12802 C CG2 . THR H 179 ? 2.2869 1.9295 1.9030 0.1240  -0.1705 0.1177  179 THR L CG2 
12803 N N   . LEU H 180 ? 2.4716 1.9786 1.8056 0.2411  -0.4345 0.1888  180 LEU L N   
12804 C CA  . LEU H 180 ? 2.5117 1.9777 1.8204 0.2506  -0.4305 0.1682  180 LEU L CA  
12805 C C   . LEU H 180 ? 2.6467 2.0651 1.9516 0.2392  -0.4668 0.1512  180 LEU L C   
12806 O O   . LEU H 180 ? 2.6238 2.0474 1.9890 0.2294  -0.4740 0.1586  180 LEU L O   
12807 C CB  . LEU H 180 ? 2.4645 1.9576 1.8181 0.2518  -0.4058 0.1849  180 LEU L CB  
12808 C CG  . LEU H 180 ? 2.5429 2.0065 1.8873 0.2608  -0.3895 0.1761  180 LEU L CG  
12809 C CD1 . LEU H 180 ? 2.5471 1.9985 1.8545 0.2796  -0.3621 0.1694  180 LEU L CD1 
12810 C CD2 . LEU H 180 ? 2.5264 2.0212 1.9281 0.2582  -0.3787 0.1976  180 LEU L CD2 
12811 N N   . THR H 181 ? 2.7022 2.0701 1.9337 0.2431  -0.4870 0.1269  181 THR L N   
12812 C CA  . THR H 181 ? 2.7920 2.1029 1.9991 0.2295  -0.5255 0.1036  181 THR L CA  
12813 C C   . THR H 181 ? 2.8970 2.1592 2.0898 0.2310  -0.4984 0.0898  181 THR L C   
12814 O O   . THR H 181 ? 2.9213 2.1378 2.0514 0.2479  -0.4643 0.0829  181 THR L O   
12815 C CB  . THR H 181 ? 2.9806 2.2452 2.0960 0.2340  -0.5576 0.0835  181 THR L CB  
12816 O OG1 . THR H 181 ? 3.0050 2.2352 2.0402 0.2635  -0.5176 0.0749  181 THR L OG1 
12817 C CG2 . THR H 181 ? 2.9386 2.2563 2.0922 0.2239  -0.5911 0.1040  181 THR L CG2 
12818 N N   . LEU H 182 ? 2.8604 2.1316 2.1238 0.2155  -0.5055 0.0905  182 LEU L N   
12819 C CA  . LEU H 182 ? 2.8815 2.1199 2.1543 0.2129  -0.4713 0.0839  182 LEU L CA  
12820 C C   . LEU H 182 ? 2.9824 2.1996 2.2972 0.1935  -0.4938 0.0646  182 LEU L C   
12821 O O   . LEU H 182 ? 2.9589 2.2094 2.3425 0.1855  -0.5319 0.0671  182 LEU L O   
12822 C CB  . LEU H 182 ? 2.7916 2.0904 2.1388 0.2231  -0.4285 0.1148  182 LEU L CB  
12823 C CG  . LEU H 182 ? 2.8476 2.1244 2.1658 0.2350  -0.3796 0.1259  182 LEU L CG  
12824 C CD1 . LEU H 182 ? 2.9264 2.1178 2.1972 0.2272  -0.3540 0.1104  182 LEU L CD1 
12825 C CD2 . LEU H 182 ? 2.8705 2.1479 2.1379 0.2522  -0.3748 0.1299  182 LEU L CD2 
12826 N N   . SER H 183 ? 2.9989 2.1574 2.2831 0.1858  -0.4638 0.0484  183 SER L N   
12827 C CA  . SER H 183 ? 3.0388 2.1750 2.3657 0.1664  -0.4726 0.0256  183 SER L CA  
12828 C C   . SER H 183 ? 3.0021 2.2139 2.4694 0.1730  -0.4388 0.0480  183 SER L C   
12829 O O   . SER H 183 ? 2.9237 2.1834 2.4246 0.1896  -0.3986 0.0798  183 SER L O   
12830 C CB  . SER H 183 ? 3.1786 2.2174 2.4167 0.1544  -0.4374 0.0043  183 SER L CB  
12831 O OG  . SER H 183 ? 3.2321 2.2734 2.4848 0.1644  -0.3654 0.0328  183 SER L OG  
12832 N N   . LYS H 184 ? 2.9745 2.1942 2.5255 0.1632  -0.4545 0.0310  184 LYS L N   
12833 C CA  . LYS H 184 ? 2.8922 2.1764 2.5854 0.1777  -0.4160 0.0497  184 LYS L CA  
12834 C C   . LYS H 184 ? 2.9440 2.2332 2.6540 0.1803  -0.3374 0.0610  184 LYS L C   
12835 O O   . LYS H 184 ? 2.8508 2.2044 2.6498 0.2019  -0.2936 0.0921  184 LYS L O   
12836 C CB  . LYS H 184 ? 2.9353 2.2181 2.7252 0.1701  -0.4494 0.0255  184 LYS L CB  
12837 C CG  . LYS H 184 ? 2.9670 2.3150 2.9144 0.1987  -0.4221 0.0522  184 LYS L CG  
12838 C CD  . LYS H 184 ? 3.0768 2.4186 3.1440 0.1960  -0.4385 0.0266  184 LYS L CD  
12839 C CE  . LYS H 184 ? 3.0942 2.4887 3.3222 0.2351  -0.3962 0.0559  184 LYS L CE  
12840 N NZ  . LYS H 184 ? 3.1941 2.5961 3.5464 0.2368  -0.3820 0.0334  184 LYS L NZ  
12841 N N   . ALA H 185 ? 3.0081 2.2222 2.6288 0.1588  -0.3167 0.0402  185 ALA L N   
12842 C CA  . ALA H 185 ? 3.0121 2.2129 2.6420 0.1539  -0.2350 0.0564  185 ALA L CA  
12843 C C   . ALA H 185 ? 3.0236 2.2616 2.6497 0.1723  -0.1990 0.1027  185 ALA L C   
12844 O O   . ALA H 185 ? 2.9503 2.2418 2.6607 0.1816  -0.1394 0.1349  185 ALA L O   
12845 C CB  . ALA H 185 ? 3.1457 2.2301 2.6568 0.1261  -0.2235 0.0278  185 ALA L CB  
12846 N N   . ASP H 186 ? 3.0215 2.2359 2.5580 0.1788  -0.2357 0.1063  186 ASP L N   
12847 C CA  . ASP H 186 ? 2.9782 2.2231 2.5096 0.1952  -0.2141 0.1442  186 ASP L CA  
12848 C C   . ASP H 186 ? 2.9570 2.2996 2.5667 0.2157  -0.2324 0.1672  186 ASP L C   
12849 O O   . ASP H 186 ? 2.9043 2.2884 2.5372 0.2281  -0.2094 0.2012  186 ASP L O   
12850 C CB  . ASP H 186 ? 3.0605 2.2394 2.4752 0.1985  -0.2395 0.1346  186 ASP L CB  
12851 C CG  . ASP H 186 ? 3.3077 2.3660 2.6270 0.1863  -0.2094 0.1204  186 ASP L CG  
12852 O OD1 . ASP H 186 ? 3.3293 2.3400 2.6115 0.1961  -0.1731 0.1432  186 ASP L OD1 
12853 O OD2 . ASP H 186 ? 3.4655 2.4674 2.7460 0.1677  -0.2221 0.0868  186 ASP L OD2 
12854 N N   . TYR H 187 ? 2.9141 2.2831 2.5637 0.2189  -0.2735 0.1511  187 TYR L N   
12855 C CA  . TYR H 187 ? 2.8472 2.2832 2.5629 0.2393  -0.2862 0.1736  187 TYR L CA  
12856 C C   . TYR H 187 ? 2.8565 2.3475 2.6769 0.2583  -0.2355 0.1995  187 TYR L C   
12857 O O   . TYR H 187 ? 2.8067 2.3433 2.6525 0.2790  -0.2279 0.2293  187 TYR L O   
12858 C CB  . TYR H 187 ? 2.8696 2.2983 2.6055 0.2368  -0.3384 0.1558  187 TYR L CB  
12859 C CG  . TYR H 187 ? 2.8325 2.3006 2.6032 0.2546  -0.3510 0.1833  187 TYR L CG  
12860 C CD1 . TYR H 187 ? 2.8577 2.3256 2.5589 0.2510  -0.3760 0.1910  187 TYR L CD1 
12861 C CD2 . TYR H 187 ? 2.7943 2.2909 2.6674 0.2771  -0.3302 0.2025  187 TYR L CD2 
12862 C CE1 . TYR H 187 ? 2.8289 2.3209 2.5544 0.2626  -0.3792 0.2179  187 TYR L CE1 
12863 C CE2 . TYR H 187 ? 2.7729 2.2823 2.6651 0.2940  -0.3342 0.2312  187 TYR L CE2 
12864 C CZ  . TYR H 187 ? 2.8803 2.3856 2.6947 0.2832  -0.3585 0.2392  187 TYR L CZ  
12865 O OH  . TYR H 187 ? 2.8794 2.3867 2.7056 0.2955  -0.3538 0.2693  187 TYR L OH  
12866 N N   . GLU H 188 ? 2.8277 2.3126 2.7059 0.2527  -0.1981 0.1876  188 GLU L N   
12867 C CA  . GLU H 188 ? 2.7659 2.3080 2.7549 0.2748  -0.1383 0.2117  188 GLU L CA  
12868 C C   . GLU H 188 ? 2.7861 2.3579 2.7727 0.2770  -0.0868 0.2504  188 GLU L C   
12869 O O   . GLU H 188 ? 2.7229 2.3561 2.7891 0.3024  -0.0449 0.2820  188 GLU L O   
12870 C CB  . GLU H 188 ? 2.7964 2.3276 2.8627 0.2678  -0.1097 0.1839  188 GLU L CB  
12871 C CG  . GLU H 188 ? 2.9112 2.4729 3.0933 0.2972  -0.1142 0.1791  188 GLU L CG  
12872 C CD  . GLU H 188 ? 3.2390 2.7698 3.4034 0.2963  -0.1886 0.1636  188 GLU L CD  
12873 O OE1 . GLU H 188 ? 3.2793 2.7587 3.3826 0.2655  -0.2391 0.1296  188 GLU L OE1 
12874 O OE2 . GLU H 188 ? 3.1059 2.6580 3.3192 0.3270  -0.1926 0.1888  188 GLU L OE2 
12875 N N   . LYS H 189 ? 2.7869 2.3109 2.6871 0.2538  -0.0891 0.2515  189 LYS L N   
12876 C CA  . LYS H 189 ? 2.7676 2.3056 2.6704 0.2514  -0.0457 0.2931  189 LYS L CA  
12877 C C   . LYS H 189 ? 2.7725 2.3654 2.6737 0.2721  -0.0707 0.3249  189 LYS L C   
12878 O O   . LYS H 189 ? 2.7326 2.3751 2.6863 0.2817  -0.0349 0.3669  189 LYS L O   
12879 C CB  . LYS H 189 ? 2.8662 2.3155 2.6795 0.2264  -0.0419 0.2855  189 LYS L CB  
12880 C CG  . LYS H 189 ? 3.0563 2.4401 2.8663 0.2022  0.0075  0.2695  189 LYS L CG  
12881 C CD  . LYS H 189 ? 3.2155 2.4948 2.9345 0.1845  0.0264  0.2753  189 LYS L CD  
12882 C CE  . LYS H 189 ? 3.3689 2.5638 3.0691 0.1576  0.0854  0.2640  189 LYS L CE  
12883 N NZ  . LYS H 189 ? 3.5329 2.6040 3.1395 0.1460  0.1137  0.2766  189 LYS L NZ  
12884 N N   . HIS H 190 ? 2.7301 2.3126 2.5702 0.2767  -0.1307 0.3063  190 HIS L N   
12885 C CA  . HIS H 190 ? 2.6967 2.3163 2.5155 0.2912  -0.1596 0.3273  190 HIS L CA  
12886 C C   . HIS H 190 ? 2.6819 2.3334 2.5343 0.3152  -0.1728 0.3290  190 HIS L C   
12887 O O   . HIS H 190 ? 2.6693 2.3123 2.5691 0.3212  -0.1651 0.3115  190 HIS L O   
12888 C CB  . HIS H 190 ? 2.7430 2.3225 2.4730 0.2793  -0.2019 0.3089  190 HIS L CB  
12889 C CG  . HIS H 190 ? 2.8255 2.3502 2.5207 0.2640  -0.1832 0.3070  190 HIS L CG  
12890 N ND1 . HIS H 190 ? 2.8385 2.3703 2.5535 0.2637  -0.1597 0.3419  190 HIS L ND1 
12891 C CD2 . HIS H 190 ? 2.9027 2.3547 2.5454 0.2508  -0.1828 0.2777  190 HIS L CD2 
12892 C CE1 . HIS H 190 ? 2.8760 2.3322 2.5556 0.2527  -0.1386 0.3353  190 HIS L CE1 
12893 N NE2 . HIS H 190 ? 2.9254 2.3283 2.5507 0.2455  -0.1511 0.2953  190 HIS L NE2 
12894 N N   . LYS H 191 ? 2.6036 2.2820 2.4338 0.3300  -0.1898 0.3511  191 LYS L N   
12895 C CA  . LYS H 191 ? 2.5810 2.2674 2.4323 0.3567  -0.1923 0.3598  191 LYS L CA  
12896 C C   . LYS H 191 ? 2.6198 2.2886 2.3975 0.3551  -0.2301 0.3611  191 LYS L C   
12897 O O   . LYS H 191 ? 2.6149 2.2562 2.3968 0.3647  -0.2371 0.3579  191 LYS L O   
12898 C CB  . LYS H 191 ? 2.5927 2.3246 2.5056 0.3880  -0.1503 0.3947  191 LYS L CB  
12899 C CG  . LYS H 191 ? 2.7752 2.5255 2.7895 0.4016  -0.0981 0.3927  191 LYS L CG  
12900 C CD  . LYS H 191 ? 2.8940 2.6741 2.9411 0.3839  -0.0596 0.4072  191 LYS L CD  
12901 C CE  . LYS H 191 ? 3.0056 2.7946 3.1454 0.3869  -0.0046 0.3959  191 LYS L CE  
12902 N NZ  . LYS H 191 ? 3.0963 2.9004 3.2633 0.3635  0.0428  0.4149  191 LYS L NZ  
12903 N N   . VAL H 192 ? 2.5698 2.2506 2.2900 0.3429  -0.2494 0.3686  192 VAL L N   
12904 C CA  . VAL H 192 ? 2.5763 2.2433 2.2270 0.3382  -0.2776 0.3683  192 VAL L CA  
12905 C C   . VAL H 192 ? 2.6124 2.2632 2.2157 0.3128  -0.3013 0.3419  192 VAL L C   
12906 O O   . VAL H 192 ? 2.6079 2.2653 2.2070 0.3030  -0.3026 0.3376  192 VAL L O   
12907 C CB  . VAL H 192 ? 2.6385 2.3302 2.2601 0.3488  -0.2828 0.3956  192 VAL L CB  
12908 C CG1 . VAL H 192 ? 2.6620 2.3325 2.2054 0.3389  -0.3075 0.3910  192 VAL L CG1 
12909 C CG2 . VAL H 192 ? 2.6369 2.3377 2.2967 0.3827  -0.2544 0.4230  192 VAL L CG2 
12910 N N   . TYR H 193 ? 2.5552 2.1810 2.1301 0.3057  -0.3136 0.3295  193 TYR L N   
12911 C CA  . TYR H 193 ? 2.5442 2.1591 2.0779 0.2878  -0.3291 0.3067  193 TYR L CA  
12912 C C   . TYR H 193 ? 2.5816 2.1992 2.0673 0.2812  -0.3337 0.3121  193 TYR L C   
12913 O O   . TYR H 193 ? 2.5876 2.1875 2.0686 0.2845  -0.3262 0.3287  193 TYR L O   
12914 C CB  . TYR H 193 ? 2.5566 2.1450 2.1063 0.2808  -0.3367 0.2893  193 TYR L CB  
12915 C CG  . TYR H 193 ? 2.5759 2.1538 2.1701 0.2837  -0.3303 0.2795  193 TYR L CG  
12916 C CD1 . TYR H 193 ? 2.5919 2.1674 2.2505 0.2960  -0.3192 0.2888  193 TYR L CD1 
12917 C CD2 . TYR H 193 ? 2.6002 2.1617 2.1745 0.2756  -0.3281 0.2613  193 TYR L CD2 
12918 C CE1 . TYR H 193 ? 2.6064 2.1760 2.3133 0.2967  -0.3070 0.2765  193 TYR L CE1 
12919 C CE2 . TYR H 193 ? 2.6245 2.1675 2.2320 0.2733  -0.3151 0.2517  193 TYR L CE2 
12920 C CZ  . TYR H 193 ? 2.6997 2.2530 2.3758 0.2820  -0.3053 0.2573  193 TYR L CZ  
12921 O OH  . TYR H 193 ? 2.7184 2.2572 2.4338 0.2779  -0.2866 0.2446  193 TYR L OH  
12922 N N   . ALA H 194 ? 2.5164 2.1483 1.9713 0.2733  -0.3391 0.2991  194 ALA L N   
12923 C CA  . ALA H 194 ? 2.5050 2.1452 1.9187 0.2643  -0.3373 0.2991  194 ALA L CA  
12924 C C   . ALA H 194 ? 2.5134 2.1613 1.9138 0.2580  -0.3319 0.2758  194 ALA L C   
12925 O O   . ALA H 194 ? 2.5065 2.1455 1.9188 0.2642  -0.3332 0.2602  194 ALA L O   
12926 C CB  . ALA H 194 ? 2.5293 2.1888 1.9294 0.2669  -0.3469 0.3095  194 ALA L CB  
12927 N N   . CYS H 195 ? 2.4432 2.1019 1.8164 0.2478  -0.3188 0.2746  195 CYS L N   
12928 C CA  . CYS H 195 ? 2.4075 2.0838 1.7762 0.2469  -0.3019 0.2545  195 CYS L CA  
12929 C C   . CYS H 195 ? 2.4270 2.1272 1.7793 0.2396  -0.2894 0.2498  195 CYS L C   
12930 O O   . CYS H 195 ? 2.4305 2.1238 1.7532 0.2240  -0.2784 0.2642  195 CYS L O   
12931 C CB  . CYS H 195 ? 2.3976 2.0682 1.7664 0.2395  -0.2875 0.2571  195 CYS L CB  
12932 S SG  . CYS H 195 ? 2.4499 2.1026 1.8098 0.2183  -0.2675 0.2909  195 CYS L SG  
12933 N N   . GLU H 196 ? 2.3617 2.0799 1.7355 0.2517  -0.2897 0.2308  196 GLU L N   
12934 C CA  . GLU H 196 ? 2.3500 2.0937 1.7239 0.2461  -0.2818 0.2201  196 GLU L CA  
12935 C C   . GLU H 196 ? 2.3473 2.1145 1.7245 0.2443  -0.2375 0.2051  196 GLU L C   
12936 O O   . GLU H 196 ? 2.3196 2.0923 1.7233 0.2649  -0.2181 0.1906  196 GLU L O   
12937 C CB  . GLU H 196 ? 2.3694 2.1191 1.7890 0.2626  -0.3003 0.2111  196 GLU L CB  
12938 C CG  . GLU H 196 ? 2.5345 2.3078 1.9600 0.2527  -0.3113 0.2034  196 GLU L CG  
12939 C CD  . GLU H 196 ? 2.8093 2.5882 2.3041 0.2697  -0.3267 0.1969  196 GLU L CD  
12940 O OE1 . GLU H 196 ? 2.6782 2.4610 2.1822 0.2611  -0.3670 0.2116  196 GLU L OE1 
12941 O OE2 . GLU H 196 ? 2.7468 2.5221 2.2905 0.2941  -0.2966 0.1802  196 GLU L OE2 
12942 N N   . VAL H 197 ? 2.2918 2.0672 1.6384 0.2208  -0.2152 0.2114  197 VAL L N   
12943 C CA  . VAL H 197 ? 2.2416 2.0458 1.5966 0.2134  -0.1605 0.2043  197 VAL L CA  
12944 C C   . VAL H 197 ? 2.2764 2.1127 1.6499 0.2117  -0.1426 0.1795  197 VAL L C   
12945 O O   . VAL H 197 ? 2.3253 2.1490 1.6651 0.1931  -0.1645 0.1804  197 VAL L O   
12946 C CB  . VAL H 197 ? 2.2978 2.0789 1.6158 0.1851  -0.1332 0.2357  197 VAL L CB  
12947 C CG1 . VAL H 197 ? 2.2520 2.0663 1.5828 0.1705  -0.0659 0.2361  197 VAL L CG1 
12948 C CG2 . VAL H 197 ? 2.2962 2.0527 1.6229 0.1908  -0.1501 0.2562  197 VAL L CG2 
12949 N N   . THR H 198 ? 2.1642 2.0384 1.5927 0.2345  -0.1034 0.1564  198 THR L N   
12950 C CA  . THR H 198 ? 2.1321 2.0424 1.6051 0.2406  -0.0779 0.1279  198 THR L CA  
12951 C C   . THR H 198 ? 2.1178 2.0722 1.6109 0.2353  0.0017  0.1226  198 THR L C   
12952 O O   . THR H 198 ? 2.0687 2.0443 1.5964 0.2626  0.0387  0.1211  198 THR L O   
12953 C CB  . THR H 198 ? 2.2291 2.1387 1.7725 0.2830  -0.0941 0.1075  198 THR L CB  
12954 O OG1 . THR H 198 ? 2.2083 2.1087 1.7658 0.3151  -0.0698 0.1089  198 THR L OG1 
12955 C CG2 . THR H 198 ? 2.2622 2.1356 1.8000 0.2815  -0.1640 0.1188  198 THR L CG2 
12956 N N   . HIS H 199 ? 2.0804 2.0446 1.5465 0.1996  0.0318  0.1227  199 HIS L N   
12957 C CA  . HIS H 199 ? 2.0254 2.0322 1.5120 0.1857  0.1200  0.1248  199 HIS L CA  
12958 C C   . HIS H 199 ? 2.0803 2.1078 1.5720 0.1614  0.1535  0.0999  199 HIS L C   
12959 O O   . HIS H 199 ? 2.1491 2.1443 1.6012 0.1453  0.0971  0.0883  199 HIS L O   
12960 C CB  . HIS H 199 ? 2.0508 2.0267 1.4826 0.1531  0.1422  0.1712  199 HIS L CB  
12961 C CG  . HIS H 199 ? 2.0345 2.0540 1.4982 0.1381  0.2378  0.1879  199 HIS L CG  
12962 N ND1 . HIS H 199 ? 2.0787 2.0788 1.5042 0.0919  0.2929  0.2083  199 HIS L ND1 
12963 C CD2 . HIS H 199 ? 1.9831 2.0604 1.5114 0.1642  0.2907  0.1906  199 HIS L CD2 
12964 C CE1 . HIS H 199 ? 2.0010 2.0546 1.4805 0.0882  0.3812  0.2259  199 HIS L CE1 
12965 N NE2 . HIS H 199 ? 1.9442 2.0505 1.4873 0.1325  0.3808  0.2158  199 HIS L NE2 
12966 N N   . GLN H 200 ? 1.9555 2.0390 1.4980 0.1588  0.2466  0.0919  200 GLN L N   
12967 C CA  . GLN H 200 ? 1.9409 2.0504 1.4975 0.1335  0.2967  0.0655  200 GLN L CA  
12968 C C   . GLN H 200 ? 2.0489 2.0941 1.4933 0.0724  0.3009  0.0909  200 GLN L C   
12969 O O   . GLN H 200 ? 2.0944 2.1215 1.5040 0.0464  0.2894  0.0657  200 GLN L O   
12970 C CB  . GLN H 200 ? 1.8518 2.0434 1.5023 0.1507  0.4097  0.0555  200 GLN L CB  
12971 C CG  . GLN H 200 ? 1.9549 2.1901 1.6617 0.1424  0.4607  0.0117  200 GLN L CG  
12972 C CD  . GLN H 200 ? 2.0338 2.3545 1.8346 0.1551  0.5897  0.0062  200 GLN L CD  
12973 O OE1 . GLN H 200 ? 1.9171 2.2726 1.7475 0.1750  0.6437  0.0365  200 GLN L OE1 
12974 N NE2 . GLN H 200 ? 1.8799 2.2399 1.7345 0.1440  0.6434  -0.0328 200 GLN L NE2 
12975 N N   . GLY H 201 ? 2.0096 2.0115 1.3992 0.0525  0.3163  0.1412  201 GLY L N   
12976 C CA  . GLY H 201 ? 2.0895 2.0065 1.3721 0.0021  0.3310  0.1768  201 GLY L CA  
12977 C C   . GLY H 201 ? 2.2454 2.0823 1.4316 -0.0045 0.2355  0.1741  201 GLY L C   
12978 O O   . GLY H 201 ? 2.3286 2.0861 1.4131 -0.0419 0.2451  0.1892  201 GLY L O   
12979 N N   . LEU H 202 ? 2.2041 2.0557 1.4189 0.0330  0.1484  0.1580  202 LEU L N   
12980 C CA  . LEU H 202 ? 2.2986 2.0927 1.4434 0.0349  0.0558  0.1581  202 LEU L CA  
12981 C C   . LEU H 202 ? 2.4167 2.2282 1.5634 0.0324  0.0088  0.1147  202 LEU L C   
12982 O O   . LEU H 202 ? 2.3362 2.2174 1.5834 0.0555  0.0127  0.0796  202 LEU L O   
12983 C CB  . LEU H 202 ? 2.2693 2.0718 1.4542 0.0727  -0.0046 0.1688  202 LEU L CB  
12984 C CG  . LEU H 202 ? 2.3361 2.0892 1.4890 0.0711  0.0016  0.2147  202 LEU L CG  
12985 C CD1 . LEU H 202 ? 2.2684 2.0621 1.4969 0.1046  -0.0118 0.2160  202 LEU L CD1 
12986 C CD2 . LEU H 202 ? 2.4630 2.1410 1.5336 0.0681  -0.0560 0.2350  202 LEU L CD2 
12987 N N   . SER H 203 ? 2.5201 2.2614 1.5574 0.0075  -0.0372 0.1194  203 SER L N   
12988 C CA  . SER H 203 ? 2.5953 2.3401 1.6163 -0.0010 -0.0999 0.0838  203 SER L CA  
12989 C C   . SER H 203 ? 2.6490 2.4256 1.7375 0.0354  -0.1889 0.0798  203 SER L C   
12990 O O   . SER H 203 ? 2.6250 2.4485 1.7942 0.0465  -0.2248 0.0479  203 SER L O   
12991 C CB  . SER H 203 ? 2.7891 2.4353 1.6519 -0.0365 -0.1219 0.0969  203 SER L CB  
12992 O OG  . SER H 203 ? 2.9573 2.5387 1.7492 -0.0228 -0.1598 0.1382  203 SER L OG  
12993 N N   . SER H 204 ? 2.6250 2.3723 1.6902 0.0536  -0.2174 0.1154  204 SER L N   
12994 C CA  . SER H 204 ? 2.6156 2.3836 1.7386 0.0849  -0.2870 0.1228  204 SER L CA  
12995 C C   . SER H 204 ? 2.6232 2.4009 1.7936 0.1115  -0.2606 0.1452  204 SER L C   
12996 O O   . SER H 204 ? 2.6263 2.3678 1.7445 0.1020  -0.2202 0.1699  204 SER L O   
12997 C CB  . SER H 204 ? 2.7573 2.4720 1.7869 0.0776  -0.3560 0.1446  204 SER L CB  
12998 O OG  . SER H 204 ? 2.8933 2.5358 1.8164 0.0672  -0.3258 0.1758  204 SER L OG  
12999 N N   . PRO H 205 ? 2.5354 2.3514 1.8034 0.1438  -0.2810 0.1392  205 PRO L N   
13000 C CA  . PRO H 205 ? 2.4820 2.2974 1.7799 0.1665  -0.2606 0.1568  205 PRO L CA  
13001 C C   . PRO H 205 ? 2.5905 2.3622 1.8330 0.1664  -0.2953 0.1907  205 PRO L C   
13002 O O   . PRO H 205 ? 2.5949 2.3675 1.8658 0.1823  -0.3408 0.2006  205 PRO L O   
13003 C CB  . PRO H 205 ? 2.4493 2.2962 1.8512 0.2001  -0.2718 0.1408  205 PRO L CB  
13004 C CG  . PRO H 205 ? 2.5122 2.3850 1.9601 0.1965  -0.2856 0.1138  205 PRO L CG  
13005 C CD  . PRO H 205 ? 2.5430 2.3920 1.8989 0.1610  -0.3215 0.1194  205 PRO L CD  
13006 N N   . VAL H 206 ? 2.5859 2.3162 1.7578 0.1495  -0.2660 0.2119  206 VAL L N   
13007 C CA  . VAL H 206 ? 2.6377 2.3186 1.7622 0.1541  -0.2857 0.2446  206 VAL L CA  
13008 C C   . VAL H 206 ? 2.6487 2.3395 1.8315 0.1763  -0.2857 0.2549  206 VAL L C   
13009 O O   . VAL H 206 ? 2.5781 2.2955 1.8081 0.1818  -0.2572 0.2436  206 VAL L O   
13010 C CB  . VAL H 206 ? 2.7476 2.3611 1.7833 0.1326  -0.2479 0.2680  206 VAL L CB  
13011 C CG1 . VAL H 206 ? 2.6940 2.2971 1.7558 0.1277  -0.1907 0.2859  206 VAL L CG1 
13012 C CG2 . VAL H 206 ? 2.8275 2.3797 1.7975 0.1426  -0.2781 0.2957  206 VAL L CG2 
13013 N N   . THR H 207 ? 2.6756 1.9522 1.8752 0.0017  -0.4317 0.3389  207 THR L N   
13014 C CA  . THR H 207 ? 2.6638 1.9681 1.9009 -0.0001 -0.4093 0.3184  207 THR L CA  
13015 C C   . THR H 207 ? 2.7065 2.0078 1.9791 0.0212  -0.3931 0.3048  207 THR L C   
13016 O O   . THR H 207 ? 2.6920 1.9843 1.9746 0.0339  -0.3851 0.3118  207 THR L O   
13017 C CB  . THR H 207 ? 2.7709 2.1091 2.0295 -0.0087 -0.3867 0.3213  207 THR L CB  
13018 O OG1 . THR H 207 ? 2.7906 2.1346 2.0144 -0.0276 -0.4015 0.3387  207 THR L OG1 
13019 C CG2 . THR H 207 ? 2.7486 2.1142 2.0322 -0.0137 -0.3716 0.3028  207 THR L CG2 
13020 N N   . LYS H 208 ? 2.6701 1.9775 1.9590 0.0228  -0.3894 0.2863  208 LYS L N   
13021 C CA  . LYS H 208 ? 2.6622 1.9727 1.9819 0.0393  -0.3755 0.2738  208 LYS L CA  
13022 C C   . LYS H 208 ? 2.7141 2.0460 2.0662 0.0377  -0.3536 0.2636  208 LYS L C   
13023 O O   . LYS H 208 ? 2.7076 2.0414 2.0581 0.0296  -0.3568 0.2555  208 LYS L O   
13024 C CB  . LYS H 208 ? 2.7104 2.0037 2.0168 0.0481  -0.3963 0.2621  208 LYS L CB  
13025 C CG  . LYS H 208 ? 2.9417 2.2103 2.2121 0.0553  -0.4231 0.2710  208 LYS L CG  
13026 C CD  . LYS H 208 ? 3.0482 2.3156 2.3277 0.0683  -0.4112 0.2829  208 LYS L CD  
13027 C CE  . LYS H 208 ? 3.1245 2.3624 2.3621 0.0750  -0.4397 0.2971  208 LYS L CE  
13028 N NZ  . LYS H 208 ? 3.1353 2.3653 2.3793 0.0827  -0.4265 0.3137  208 LYS L NZ  
13029 N N   . SER H 209 ? 2.6782 2.0208 2.0551 0.0445  -0.3345 0.2645  209 SER L N   
13030 C CA  . SER H 209 ? 2.6733 2.0320 2.0748 0.0450  -0.3184 0.2570  209 SER L CA  
13031 C C   . SER H 209 ? 2.7459 2.1062 2.1657 0.0528  -0.3115 0.2487  209 SER L C   
13032 O O   . SER H 209 ? 2.7412 2.0966 2.1610 0.0587  -0.3139 0.2478  209 SER L O   
13033 C CB  . SER H 209 ? 2.7085 2.0753 2.1180 0.0440  -0.3086 0.2622  209 SER L CB  
13034 O OG  . SER H 209 ? 2.8174 2.1703 2.2285 0.0484  -0.3066 0.2684  209 SER L OG  
13035 N N   . PHE H 210 ? 2.7232 2.0920 2.1560 0.0524  -0.3042 0.2432  210 PHE L N   
13036 C CA  . PHE H 210 ? 2.7295 2.1016 2.1750 0.0561  -0.2996 0.2382  210 PHE L CA  
13037 C C   . PHE H 210 ? 2.8095 2.1858 2.2614 0.0556  -0.2950 0.2377  210 PHE L C   
13038 O O   . PHE H 210 ? 2.8070 2.1866 2.2573 0.0556  -0.2952 0.2369  210 PHE L O   
13039 C CB  . PHE H 210 ? 2.7554 2.1244 2.2017 0.0576  -0.3046 0.2321  210 PHE L CB  
13040 C CG  . PHE H 210 ? 2.7731 2.1376 2.2213 0.0554  -0.3041 0.2310  210 PHE L CG  
13041 C CD1 . PHE H 210 ? 2.8165 2.1729 2.2548 0.0495  -0.3091 0.2304  210 PHE L CD1 
13042 C CD2 . PHE H 210 ? 2.7923 2.1583 2.2482 0.0575  -0.3009 0.2317  210 PHE L CD2 
13043 C CE1 . PHE H 210 ? 2.8263 2.1748 2.2655 0.0471  -0.3083 0.2297  210 PHE L CE1 
13044 C CE2 . PHE H 210 ? 2.8273 2.1829 2.2818 0.0572  -0.3019 0.2335  210 PHE L CE2 
13045 C CZ  . PHE H 210 ? 2.8071 2.1533 2.2549 0.0528  -0.3045 0.2320  210 PHE L CZ  
13046 N N   . ASN H 211 ? 2.7880 2.1638 2.2435 0.0542  -0.2940 0.2369  211 ASN L N   
13047 C CA  . ASN H 211 ? 2.7971 2.1701 2.2507 0.0529  -0.2976 0.2352  211 ASN L CA  
13048 C C   . ASN H 211 ? 2.8637 2.2370 2.3149 0.0533  -0.3017 0.2360  211 ASN L C   
13049 O O   . ASN H 211 ? 2.8596 2.2381 2.3135 0.0504  -0.3004 0.2367  211 ASN L O   
13050 C CB  . ASN H 211 ? 2.8160 2.1806 2.2669 0.0459  -0.3000 0.2340  211 ASN L CB  
13051 C CG  . ASN H 211 ? 3.1330 2.5022 2.5847 0.0388  -0.2977 0.2343  211 ASN L CG  
13052 O OD1 . ASN H 211 ? 3.0644 2.4425 2.5214 0.0425  -0.2926 0.2347  211 ASN L OD1 
13053 N ND2 . ASN H 211 ? 3.0351 2.3993 2.4788 0.0274  -0.3044 0.2324  211 ASN L ND2 
13054 N N   . ARG H 212 ? 2.8301 2.1987 2.2755 0.0580  -0.3076 0.2362  212 ARG L N   
13055 C CA  . ARG H 212 ? 2.8341 2.1956 2.2724 0.0598  -0.3142 0.2409  212 ARG L CA  
13056 C C   . ARG H 212 ? 2.9108 2.2696 2.3388 0.0513  -0.3229 0.2446  212 ARG L C   
13057 O O   . ARG H 212 ? 2.9142 2.2683 2.3323 0.0452  -0.3316 0.2417  212 ARG L O   
13058 C CB  . ARG H 212 ? 2.8221 2.1773 2.2517 0.0688  -0.3222 0.2399  212 ARG L CB  
13059 C CG  . ARG H 212 ? 2.8737 2.2241 2.3049 0.0736  -0.3185 0.2433  212 ARG L CG  
13060 C CD  . ARG H 212 ? 2.9358 2.2827 2.3568 0.0844  -0.3274 0.2415  212 ARG L CD  
13061 N NE  . ARG H 212 ? 2.9901 2.3178 2.3920 0.0889  -0.3442 0.2494  212 ARG L NE  
13062 C CZ  . ARG H 212 ? 3.1493 2.4703 2.5340 0.1000  -0.3616 0.2463  212 ARG L CZ  
13063 N NH1 . ARG H 212 ? 2.9675 2.3052 2.3572 0.1088  -0.3617 0.2327  212 ARG L NH1 
13064 N NH2 . ARG H 212 ? 2.9894 2.2878 2.3492 0.1025  -0.3820 0.2562  212 ARG L NH2 
13065 N N   . GLY H 213 ? 2.8808 2.2419 2.3094 0.0487  -0.3220 0.2504  213 GLY L N   
13066 C CA  . GLY H 213 ? 2.8926 2.2579 2.3093 0.0374  -0.3304 0.2559  213 GLY L CA  
13067 C C   . GLY H 213 ? 2.9526 2.3363 2.3736 0.0251  -0.3258 0.2503  213 GLY L C   
13068 O O   . GLY H 213 ? 2.9456 2.3497 2.3763 0.0214  -0.3187 0.2490  213 GLY L O   
13069 N N   . GLU H 214 ? 2.9170 2.2929 2.3302 0.0185  -0.3310 0.2456  214 GLU L N   
13070 C CA  . GLU H 214 ? 2.9150 2.3004 2.3287 0.0043  -0.3280 0.2405  214 GLU L CA  
13071 C C   . GLU H 214 ? 2.9572 2.3594 2.3928 0.0116  -0.3106 0.2355  214 GLU L C   
13072 O O   . GLU H 214 ? 2.9452 2.3418 2.3914 0.0255  -0.3041 0.2347  214 GLU L O   
13073 C CB  . GLU H 214 ? 2.9402 2.3015 2.3401 -0.0031 -0.3395 0.2359  214 GLU L CB  
13074 C CG  . GLU H 214 ? 3.0615 2.4030 2.4307 -0.0135 -0.3653 0.2380  214 GLU L CG  
13075 C CD  . GLU H 214 ? 3.2542 2.5655 2.6084 -0.0168 -0.3824 0.2292  214 GLU L CD  
13076 O OE1 . GLU H 214 ? 3.1121 2.4174 2.4795 0.0001  -0.3770 0.2239  214 GLU L OE1 
13077 O OE2 . GLU H 214 ? 3.1688 2.4622 2.4955 -0.0379 -0.4040 0.2265  214 GLU L OE2 
13078 N N   . CYS H 215 ? 2.9153 2.3394 2.3541 0.0014  -0.3059 0.2319  215 CYS L N   
13079 C CA  . CYS H 215 ? 3.3312 2.7727 2.7861 0.0101  -0.2942 0.2256  215 CYS L CA  
13080 C C   . CYS H 215 ? 3.5850 3.0078 3.0401 0.0119  -0.2908 0.2252  215 CYS L C   
13081 O O   . CYS H 215 ? 3.0700 2.4907 2.5326 0.0261  -0.2863 0.2245  215 CYS L O   
13082 C CB  . CYS H 215 ? 3.3380 2.8154 2.7960 0.0000  -0.2912 0.2198  215 CYS L CB  
13083 S SG  . CYS H 215 ? 3.3886 2.8901 2.8475 -0.0016 -0.2949 0.2221  215 CYS L SG  
# 
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   GLY 1   1   ?   ?   ?   A . n 
A 1 2   LEU 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   ILE 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   GLY 8   8   ?   ?   ?   A . n 
A 1 9   PHE 9   9   ?   ?   ?   A . n 
A 1 10  ILE 10  10  ?   ?   ?   A . n 
A 1 11  GLU 11  11  ?   ?   ?   A . n 
A 1 12  GLY 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  TRP 14  14  ?   ?   ?   A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  GLY 20  20  ?   ?   ?   A . n 
A 1 21  TRP 21  21  ?   ?   ?   A . n 
A 1 22  TYR 22  22  ?   ?   ?   A . n 
A 1 23  GLY 23  23  ?   ?   ?   A . n 
A 1 24  TYR 24  24  ?   ?   ?   A . n 
A 1 25  HIS 25  25  ?   ?   ?   A . n 
A 1 26  HIS 26  26  ?   ?   ?   A . n 
A 1 27  GLN 27  27  ?   ?   ?   A . n 
A 1 28  ASN 28  28  ?   ?   ?   A . n 
A 1 29  GLU 29  29  ?   ?   ?   A . n 
A 1 30  GLN 30  30  ?   ?   ?   A . n 
A 1 31  GLY 31  31  ?   ?   ?   A . n 
A 1 32  SER 32  32  ?   ?   ?   A . n 
A 1 33  GLY 33  33  ?   ?   ?   A . n 
A 1 34  TYR 34  34  ?   ?   ?   A . n 
A 1 35  ALA 35  35  ?   ?   ?   A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  MET 59  59  59  MET MET A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  ?   ?   ?   A . n 
A 1 71  ASN 71  71  ?   ?   ?   A . n 
A 1 72  HIS 72  72  ?   ?   ?   A . n 
A 1 73  LEU 73  73  ?   ?   ?   A . n 
A 1 74  GLU 74  74  ?   ?   ?   A . n 
A 1 75  LYS 75  75  ?   ?   ?   A . n 
A 1 76  ARG 76  76  ?   ?   ?   A . n 
A 1 77  ILE 77  77  ?   ?   ?   A . n 
A 1 78  GLU 78  78  ?   ?   ?   A . n 
A 1 79  ASN 79  79  ?   ?   ?   A . n 
A 1 80  LEU 80  80  ?   ?   ?   A . n 
A 1 81  ASN 81  81  ?   ?   ?   A . n 
A 1 82  LYS 82  82  ?   ?   ?   A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  TRP 92  92  92  TRP TRP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 TYR 110 110 110 TYR TYR A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LYS 127 127 ?   ?   ?   A . n 
A 1 128 ASN 128 128 ?   ?   ?   A . n 
A 1 129 ASN 129 129 ?   ?   ?   A . n 
A 1 130 ALA 130 130 ?   ?   ?   A . n 
A 1 131 LYS 131 131 ?   ?   ?   A . n 
A 1 132 GLU 132 132 ?   ?   ?   A . n 
A 1 133 ILE 133 133 ?   ?   ?   A . n 
A 1 134 GLY 134 134 ?   ?   ?   A . n 
A 1 135 ASN 135 135 ?   ?   ?   A . n 
A 1 136 GLY 136 136 ?   ?   ?   A . n 
A 1 137 CYS 137 137 ?   ?   ?   A . n 
A 1 138 PHE 138 138 ?   ?   ?   A . n 
A 1 139 GLU 139 139 ?   ?   ?   A . n 
A 1 140 PHE 140 140 ?   ?   ?   A . n 
A 1 141 TYR 141 141 ?   ?   ?   A . n 
A 1 142 HIS 142 142 ?   ?   ?   A . n 
A 1 143 LYS 143 143 ?   ?   ?   A . n 
A 1 144 CYS 144 144 ?   ?   ?   A . n 
A 1 145 ASP 145 145 ?   ?   ?   A . n 
A 1 146 ASN 146 146 ?   ?   ?   A . n 
A 1 147 THR 147 147 ?   ?   ?   A . n 
A 1 148 CYS 148 148 148 CYS CYS A . n 
A 1 149 MET 149 149 149 MET MET A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 GLY 155 155 ?   ?   ?   A . n 
A 1 156 THR 156 156 ?   ?   ?   A . n 
A 1 157 TYR 157 157 ?   ?   ?   A . n 
A 1 158 ASP 158 158 ?   ?   ?   A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 GLU 171 171 171 GLU GLU 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 ASP 174 174 174 ASP ASP A . n 
A 1 175 GLY 175 175 ?   ?   ?   A . n 
A 1 176 VAL 176 176 ?   ?   ?   A . n 
B 2 1   ALA 1   10  ?   ?   ?   B . n 
B 2 2   ASP 2   11  ?   ?   ?   B . n 
B 2 3   THR 3   12  ?   ?   ?   B . n 
B 2 4   LEU 4   13  ?   ?   ?   B . n 
B 2 5   CYS 5   14  ?   ?   ?   B . n 
B 2 6   ILE 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  ?   ?   ?   B . n 
B 2 8   TYR 8   17  ?   ?   ?   B . n 
B 2 9   HIS 9   18  ?   ?   ?   B . n 
B 2 10  ALA 10  19  ?   ?   ?   B . n 
B 2 11  ASN 11  20  20  ASN ASN B . n 
B 2 12  ASN 12  21  21  ASN ASN B . n 
B 2 13  SER 13  22  22  SER SER B . n 
B 2 14  THR 14  23  23  THR THR B . n 
B 2 15  ASP 15  24  24  ASP ASP B . n 
B 2 16  THR 16  25  25  THR THR B . n 
B 2 17  VAL 17  26  26  VAL VAL B . n 
B 2 18  ASP 18  27  27  ASP ASP B . n 
B 2 19  THR 19  28  28  THR THR B . n 
B 2 20  VAL 20  29  29  VAL VAL B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  GLU 22  31  31  GLU GLU B . n 
B 2 23  LYS 23  32  32  LYS LYS B . n 
B 2 24  ASN 24  33  33  ASN ASN B . n 
B 2 25  VAL 25  34  34  VAL VAL B . n 
B 2 26  THR 26  35  35  THR THR B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  THR 28  37  37  THR THR B . n 
B 2 29  HIS 29  38  38  HIS HIS B . n 
B 2 30  SER 30  39  39  SER SER B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  ASN 32  41  41  ASN ASN B . n 
B 2 33  LEU 33  42  42  LEU LEU B . n 
B 2 34  LEU 34  43  43  LEU LEU B . n 
B 2 35  GLU 35  44  44  GLU GLU B . n 
B 2 36  ASP 36  45  45  ASP ASP B . n 
B 2 37  LYS 37  46  46  LYS LYS B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  ASN 39  48  48  ASN ASN B . n 
B 2 40  GLY 40  49  49  GLY GLY B . n 
B 2 41  LYS 41  50  50  LYS LYS B . n 
B 2 42  LEU 42  51  51  LEU LEU B . n 
B 2 43  CYS 43  52  52  CYS CYS B . n 
B 2 44  LYS 44  53  53  LYS LYS B . n 
B 2 45  LEU 45  54  54  LEU LEU B . n 
B 2 46  ARG 46  55  55  ARG ARG B . n 
B 2 47  GLY 47  55  55  GLY GLY B A n 
B 2 48  VAL 48  56  56  VAL VAL B . n 
B 2 49  ALA 49  57  57  ALA ALA B . n 
B 2 50  PRO 50  58  58  PRO PRO B . n 
B 2 51  LEU 51  59  59  LEU LEU B . n 
B 2 52  HIS 52  60  60  HIS HIS B . n 
B 2 53  LEU 53  61  61  LEU LEU B . n 
B 2 54  GLY 54  62  62  GLY GLY B . n 
B 2 55  LYS 55  63  63  LYS LYS B . n 
B 2 56  CYS 56  64  64  CYS CYS B . n 
B 2 57  ASN 57  65  65  ASN ASN B . n 
B 2 58  ILE 58  66  66  ILE ILE B . n 
B 2 59  ALA 59  67  67  ALA ALA B . n 
B 2 60  GLY 60  68  68  GLY GLY B . n 
B 2 61  TRP 61  69  69  TRP TRP B . n 
B 2 62  ILE 62  70  70  ILE ILE B . n 
B 2 63  LEU 63  71  71  LEU LEU B . n 
B 2 64  GLY 64  72  72  GLY GLY B . n 
B 2 65  ASN 65  73  73  ASN ASN B . n 
B 2 66  PRO 66  74  74  PRO PRO B . n 
B 2 67  GLU 67  75  75  GLU GLU B . n 
B 2 68  CYS 68  76  76  CYS CYS B . n 
B 2 69  GLU 69  77  ?   ?   ?   B . n 
B 2 70  SER 70  78  ?   ?   ?   B . n 
B 2 71  LEU 71  79  ?   ?   ?   B . n 
B 2 72  SER 72  80  ?   ?   ?   B . n 
B 2 73  THR 73  81  ?   ?   ?   B . n 
B 2 74  ALA 74  82  82  ALA ALA B . n 
B 2 75  SER 75  83  83  SER SER B . n 
B 2 76  SER 76  83  83  SER SER B A n 
B 2 77  TRP 77  84  84  TRP TRP B . n 
B 2 78  SER 78  85  85  SER SER B . n 
B 2 79  TYR 79  86  86  TYR TYR B . n 
B 2 80  ILE 80  87  87  ILE ILE B . n 
B 2 81  VAL 81  88  88  VAL VAL B . n 
B 2 82  GLU 82  89  89  GLU GLU B . n 
B 2 83  THR 83  90  90  THR THR B . n 
B 2 84  PRO 84  90  90  PRO PRO B A n 
B 2 85  SER 85  91  91  SER SER B . n 
B 2 86  SER 86  92  92  SER SER B . n 
B 2 87  ASP 87  93  93  ASP ASP B . n 
B 2 88  ASN 88  94  94  ASN ASN B . n 
B 2 89  GLY 89  95  95  GLY GLY B . n 
B 2 90  THR 90  96  96  THR THR B . n 
B 2 91  CYS 91  97  97  CYS CYS B . n 
B 2 92  TYR 92  98  98  TYR TYR B . n 
B 2 93  PRO 93  99  99  PRO PRO B . n 
B 2 94  GLY 94  100 100 GLY GLY B . n 
B 2 95  ASP 95  101 101 ASP ASP B . n 
B 2 96  PHE 96  102 102 PHE PHE B . n 
B 2 97  ILE 97  103 103 ILE ILE B . n 
B 2 98  ASP 98  104 104 ASP ASP B . n 
B 2 99  TYR 99  105 105 TYR TYR B . n 
B 2 100 GLU 100 106 106 GLU GLU B . n 
B 2 101 GLU 101 107 107 GLU GLU B . n 
B 2 102 LEU 102 108 108 LEU LEU B . n 
B 2 103 ARG 103 109 109 ARG ARG B . n 
B 2 104 GLU 104 110 110 GLU GLU B . n 
B 2 105 GLN 105 111 111 GLN GLN B . n 
B 2 106 LEU 106 112 112 LEU LEU B . n 
B 2 107 SER 107 113 113 SER SER B . n 
B 2 108 SER 108 114 114 SER SER B . n 
B 2 109 VAL 109 115 115 VAL VAL B . n 
B 2 110 SER 110 116 116 SER SER B . n 
B 2 111 SER 111 116 116 SER SER B A n 
B 2 112 PHE 112 116 116 PHE PHE B B n 
B 2 113 GLU 113 116 116 GLU GLU B C n 
B 2 114 ARG 114 117 117 ARG ARG B . n 
B 2 115 PHE 115 118 118 PHE PHE B . n 
B 2 116 GLU 116 119 119 GLU GLU B . n 
B 2 117 ILE 117 120 120 ILE ILE B . n 
B 2 118 PHE 118 121 121 PHE PHE B . n 
B 2 119 PRO 119 122 122 PRO PRO B . n 
B 2 120 LYS 120 123 123 LYS LYS B . n 
B 2 121 THR 121 124 124 THR THR B . n 
B 2 122 SER 122 125 125 SER SER B . n 
B 2 123 SER 123 126 126 SER SER B . n 
B 2 124 TRP 124 127 127 TRP TRP B . n 
B 2 125 PRO 125 128 128 PRO PRO B . n 
B 2 126 ASN 126 129 129 ASN ASN B . n 
B 2 127 HIS 127 130 130 HIS HIS B . n 
B 2 128 ASP 128 131 131 ASP ASP B . n 
B 2 129 SER 129 132 132 SER SER B . n 
B 2 130 ASP 130 133 133 ASP ASP B . n 
B 2 131 LYS 131 133 133 LYS LYS B A n 
B 2 132 GLY 132 134 134 GLY GLY B . n 
B 2 133 VAL 133 135 135 VAL VAL B . n 
B 2 134 THR 134 136 136 THR THR B . n 
B 2 135 ALA 135 137 137 ALA ALA B . n 
B 2 136 ALA 136 138 138 ALA ALA B . n 
B 2 137 CYS 137 139 139 CYS CYS B . n 
B 2 138 PRO 138 140 140 PRO PRO B . n 
B 2 139 HIS 139 141 141 HIS HIS B . n 
B 2 140 ALA 140 142 142 ALA ALA B . n 
B 2 141 GLY 141 143 143 GLY GLY B . n 
B 2 142 ALA 142 144 144 ALA ALA B . n 
B 2 143 LYS 143 145 145 LYS LYS B . n 
B 2 144 SER 144 146 146 SER SER B . n 
B 2 145 PHE 145 147 147 PHE PHE B . n 
B 2 146 TYR 146 148 148 TYR TYR B . n 
B 2 147 LYS 147 149 149 LYS LYS B . n 
B 2 148 ASN 148 150 150 ASN ASN B . n 
B 2 149 LEU 149 151 151 LEU LEU B . n 
B 2 150 ILE 150 152 152 ILE ILE B . n 
B 2 151 TRP 151 153 153 TRP TRP B . n 
B 2 152 LEU 152 154 154 LEU LEU B . n 
B 2 153 VAL 153 155 155 VAL VAL B . n 
B 2 154 LYS 154 156 156 LYS LYS B . n 
B 2 155 LYS 155 157 157 LYS LYS B . n 
B 2 156 GLY 156 158 158 GLY GLY B . n 
B 2 157 ASN 157 159 159 ASN ASN B . n 
B 2 158 SER 158 160 160 SER SER B . n 
B 2 159 TYR 159 161 161 TYR TYR B . n 
B 2 160 PRO 160 162 162 PRO PRO B . n 
B 2 161 LYS 161 163 163 LYS LYS B . n 
B 2 162 LEU 162 164 164 LEU LEU B . n 
B 2 163 SER 163 165 165 SER SER B . n 
B 2 164 LYS 164 166 166 LYS LYS B . n 
B 2 165 SER 165 167 167 SER SER B . n 
B 2 166 TYR 166 168 168 TYR TYR B . n 
B 2 167 ILE 167 169 169 ILE ILE B . n 
B 2 168 ASN 168 170 170 ASN ASN B . n 
B 2 169 ASP 169 171 171 ASP ASP B . n 
B 2 170 LYS 170 172 172 LYS LYS B . n 
B 2 171 GLY 171 173 173 GLY GLY B . n 
B 2 172 LYS 172 174 174 LYS LYS B . n 
B 2 173 GLU 173 175 175 GLU GLU B . n 
B 2 174 VAL 174 176 176 VAL VAL B . n 
B 2 175 LEU 175 177 177 LEU LEU B . n 
B 2 176 VAL 176 178 178 VAL VAL B . n 
B 2 177 LEU 177 179 179 LEU LEU B . n 
B 2 178 TRP 178 180 180 TRP TRP B . n 
B 2 179 GLY 179 181 181 GLY GLY B . n 
B 2 180 ILE 180 182 182 ILE ILE B . n 
B 2 181 HIS 181 183 183 HIS HIS B . n 
B 2 182 HIS 182 184 184 HIS HIS B . n 
B 2 183 PRO 183 185 185 PRO PRO B . n 
B 2 184 SER 184 186 186 SER SER B . n 
B 2 185 THR 185 187 187 THR THR B . n 
B 2 186 SER 186 188 188 SER SER B . n 
B 2 187 ALA 187 189 189 ALA ALA B . n 
B 2 188 ASP 188 190 190 ASP ASP B . n 
B 2 189 GLN 189 191 191 GLN GLN B . n 
B 2 190 GLN 190 192 192 GLN GLN B . n 
B 2 191 SER 191 193 193 SER SER B . n 
B 2 192 LEU 192 194 194 LEU LEU B . n 
B 2 193 TYR 193 195 195 TYR TYR B . n 
B 2 194 GLN 194 196 196 GLN GLN B . n 
B 2 195 ASN 195 197 197 ASN ASN B . n 
B 2 196 ALA 196 198 198 ALA ALA B . n 
B 2 197 ASP 197 199 199 ASP ASP B . n 
B 2 198 ALA 198 200 200 ALA ALA B . n 
B 2 199 TYR 199 201 201 TYR TYR B . n 
B 2 200 VAL 200 202 202 VAL VAL B . n 
B 2 201 PHE 201 203 203 PHE PHE B . n 
B 2 202 VAL 202 204 204 VAL VAL B . n 
B 2 203 GLY 203 205 205 GLY GLY B . n 
B 2 204 SER 204 206 206 SER SER B . n 
B 2 205 SER 205 207 207 SER SER B . n 
B 2 206 ARG 206 208 208 ARG ARG B . n 
B 2 207 TYR 207 209 209 TYR TYR B . n 
B 2 208 SER 208 210 210 SER SER B . n 
B 2 209 LYS 209 211 211 LYS LYS B . n 
B 2 210 THR 210 212 212 THR THR B . n 
B 2 211 PHE 211 213 213 PHE PHE B . n 
B 2 212 LYS 212 214 214 LYS LYS B . n 
B 2 213 PRO 213 215 215 PRO PRO B . n 
B 2 214 GLU 214 216 216 GLU GLU B . n 
B 2 215 ILE 215 217 217 ILE ILE B . n 
B 2 216 ALA 216 218 218 ALA ALA B . n 
B 2 217 ILE 217 219 219 ILE ILE B . n 
B 2 218 ARG 218 220 220 ARG ARG B . n 
B 2 219 PRO 219 221 221 PRO PRO B . n 
B 2 220 LYS 220 222 222 LYS LYS B . n 
B 2 221 VAL 221 223 223 VAL VAL B . n 
B 2 222 ARG 222 224 224 ARG ARG B . n 
B 2 223 ASP 223 225 225 ASP ASP B . n 
B 2 224 ARG 224 226 226 ARG ARG B . n 
B 2 225 GLU 225 227 227 GLU GLU B . n 
B 2 226 GLY 226 228 228 GLY GLY B . n 
B 2 227 ARG 227 229 229 ARG ARG B . n 
B 2 228 MET 228 230 230 MET MET B . n 
B 2 229 ASN 229 231 231 ASN ASN B . n 
B 2 230 TYR 230 232 232 TYR TYR B . n 
B 2 231 TYR 231 233 233 TYR TYR B . n 
B 2 232 TRP 232 234 234 TRP TRP B . n 
B 2 233 THR 233 235 235 THR THR B . n 
B 2 234 LEU 234 236 236 LEU LEU B . n 
B 2 235 VAL 235 237 237 VAL VAL B . n 
B 2 236 GLU 236 238 238 GLU GLU B . n 
B 2 237 PRO 237 239 239 PRO PRO B . n 
B 2 238 GLY 238 240 240 GLY GLY B . n 
B 2 239 ASP 239 241 241 ASP ASP B . n 
B 2 240 LYS 240 242 242 LYS LYS B . n 
B 2 241 ILE 241 243 243 ILE ILE B . n 
B 2 242 THR 242 244 244 THR THR B . n 
B 2 243 PHE 243 245 245 PHE PHE B . n 
B 2 244 GLU 244 246 246 GLU GLU B . n 
B 2 245 ALA 245 247 247 ALA ALA B . n 
B 2 246 THR 246 248 248 THR THR B . n 
B 2 247 GLY 247 249 249 GLY GLY B . n 
B 2 248 ASN 248 250 250 ASN ASN B . n 
B 2 249 LEU 249 251 251 LEU LEU B . n 
B 2 250 VAL 250 252 252 VAL VAL B . n 
B 2 251 VAL 251 253 253 VAL VAL B . n 
B 2 252 PRO 252 254 254 PRO PRO B . n 
B 2 253 ARG 253 255 255 ARG ARG B . n 
B 2 254 TYR 254 256 256 TYR TYR B . n 
B 2 255 ALA 255 257 257 ALA ALA B . n 
B 2 256 PHE 256 258 258 PHE PHE B . n 
B 2 257 ALA 257 259 259 ALA ALA B . n 
B 2 258 MET 258 260 260 MET MET B . n 
B 2 259 GLU 259 261 261 GLU GLU B . n 
B 2 260 ARG 260 262 262 ARG ARG B . n 
B 2 261 ASN 261 263 263 ASN ASN B . n 
B 2 262 ALA 262 264 264 ALA ALA B . n 
B 2 263 GLY 263 265 265 GLY GLY B . n 
B 2 264 SER 264 266 266 SER SER B . n 
B 2 265 GLY 265 266 266 GLY GLY B A n 
B 2 266 ILE 266 267 267 ILE ILE B . n 
B 2 267 ILE 267 268 268 ILE ILE B . n 
B 2 268 ILE 268 269 269 ILE ILE B . n 
B 2 269 SER 269 270 270 SER SER B . n 
B 2 270 ASP 270 271 271 ASP ASP B . n 
B 2 271 THR 271 272 272 THR THR B . n 
B 2 272 PRO 272 273 273 PRO PRO B . n 
B 2 273 VAL 273 274 274 VAL VAL B . n 
B 2 274 HIS 274 275 275 HIS HIS B . n 
B 2 275 ASP 275 276 276 ASP ASP B . n 
B 2 276 CYS 276 277 277 CYS CYS B . n 
B 2 277 ASN 277 278 278 ASN ASN B . n 
B 2 278 THR 278 279 279 THR THR B . n 
B 2 279 THR 279 280 280 THR THR B . n 
B 2 280 CYS 280 281 281 CYS CYS B . n 
B 2 281 GLN 281 282 282 GLN GLN B . n 
B 2 282 THR 282 283 283 THR THR B . n 
B 2 283 PRO 283 284 284 PRO PRO B . n 
B 2 284 LYS 284 285 285 LYS LYS B . n 
B 2 285 GLY 285 286 286 GLY GLY B . n 
B 2 286 ALA 286 287 287 ALA ALA B . n 
B 2 287 ILE 287 288 288 ILE ILE B . n 
B 2 288 ASN 288 289 289 ASN ASN B . n 
B 2 289 THR 289 290 290 THR THR B . n 
B 2 290 SER 290 291 291 SER SER B . n 
B 2 291 LEU 291 292 292 LEU LEU B . n 
B 2 292 PRO 292 293 293 PRO PRO B . n 
B 2 293 PHE 293 294 294 PHE PHE B . n 
B 2 294 GLN 294 295 295 GLN GLN B . n 
B 2 295 ASN 295 296 296 ASN ASN B . n 
B 2 296 ILE 296 297 297 ILE ILE B . n 
B 2 297 HIS 297 298 298 HIS HIS B . n 
B 2 298 PRO 298 299 299 PRO PRO B . n 
B 2 299 ILE 299 300 300 ILE ILE B . n 
B 2 300 THR 300 301 301 THR THR B . n 
B 2 301 ILE 301 302 302 ILE ILE B . n 
B 2 302 GLY 302 303 303 GLY GLY B . n 
B 2 303 LYS 303 304 304 LYS LYS B . n 
B 2 304 CYS 304 305 305 CYS CYS B . n 
B 2 305 PRO 305 306 306 PRO PRO B . n 
B 2 306 LYS 306 307 307 LYS LYS B . n 
B 2 307 TYR 307 308 308 TYR TYR B . n 
B 2 308 VAL 308 309 309 VAL VAL B . n 
B 2 309 LYS 309 310 310 LYS LYS B . n 
B 2 310 SER 310 311 311 SER SER B . n 
B 2 311 THR 311 312 312 THR THR B . n 
B 2 312 LYS 312 313 313 LYS LYS B . n 
B 2 313 LEU 313 314 314 LEU LEU B . n 
B 2 314 ARG 314 315 ?   ?   ?   B . n 
B 2 315 LEU 315 316 ?   ?   ?   B . n 
B 2 316 ALA 316 317 ?   ?   ?   B . n 
B 2 317 THR 317 318 ?   ?   ?   B . n 
B 2 318 GLY 318 319 ?   ?   ?   B . n 
B 2 319 LEU 319 320 ?   ?   ?   B . n 
B 2 320 ARG 320 321 ?   ?   ?   B . n 
B 2 321 ASN 321 322 ?   ?   ?   B . n 
B 2 322 ILE 322 323 ?   ?   ?   B . n 
B 2 323 PRO 323 324 ?   ?   ?   B . n 
B 2 324 SER 324 325 ?   ?   ?   B . n 
B 2 325 ILE 325 326 ?   ?   ?   B . n 
B 2 326 GLN 326 327 ?   ?   ?   B . n 
B 2 327 SER 327 328 ?   ?   ?   B . n 
B 2 328 ARG 328 329 ?   ?   ?   B . n 
C 3 1   GLU 1   1   ?   ?   ?   C . n 
C 3 2   VAL 2   2   ?   ?   ?   C . n 
C 3 3   GLN 3   3   3   GLN GLN C . n 
C 3 4   LEU 4   4   4   LEU LEU C . n 
C 3 5   VAL 5   5   5   VAL VAL C . n 
C 3 6   GLN 6   6   6   GLN GLN C . n 
C 3 7   SER 7   7   7   SER SER C . n 
C 3 8   GLY 8   8   8   GLY GLY C . n 
C 3 9   ALA 9   9   9   ALA ALA C . n 
C 3 10  GLU 10  10  10  GLU GLU C . n 
C 3 11  VAL 11  11  11  VAL VAL C . n 
C 3 12  LYS 12  12  12  LYS LYS C . n 
C 3 13  LYS 13  13  13  LYS LYS C . n 
C 3 14  PRO 14  14  14  PRO PRO C . n 
C 3 15  GLY 15  15  15  GLY GLY C . n 
C 3 16  GLU 16  16  16  GLU GLU C . n 
C 3 17  SER 17  17  17  SER SER C . n 
C 3 18  LEU 18  18  18  LEU LEU C . n 
C 3 19  THR 19  19  19  THR THR C . n 
C 3 20  ILE 20  20  20  ILE ILE C . n 
C 3 21  SER 21  21  21  SER SER C . n 
C 3 22  CYS 22  22  22  CYS CYS C . n 
C 3 23  LYS 23  23  23  LYS LYS C . n 
C 3 24  GLY 24  24  24  GLY GLY C . n 
C 3 25  SER 25  25  25  SER SER C . n 
C 3 26  GLY 26  26  26  GLY GLY C . n 
C 3 27  TYR 27  27  27  TYR TYR C . n 
C 3 28  SER 28  28  28  SER SER C . n 
C 3 29  PHE 29  29  29  PHE PHE C . n 
C 3 30  SER 30  30  30  SER SER C . n 
C 3 31  SER 31  31  31  SER SER C . n 
C 3 32  TYR 32  32  32  TYR TYR C . n 
C 3 33  TRP 33  33  33  TRP TRP C . n 
C 3 34  ILE 34  34  34  ILE ILE C . n 
C 3 35  GLY 35  35  35  GLY GLY C . n 
C 3 36  TRP 36  36  36  TRP TRP C . n 
C 3 37  VAL 37  37  37  VAL VAL C . n 
C 3 38  ARG 38  38  38  ARG ARG C . n 
C 3 39  ARG 39  39  39  ARG ARG C . n 
C 3 40  MET 40  40  40  MET MET C . n 
C 3 41  PRO 41  41  41  PRO PRO C . n 
C 3 42  GLY 42  42  42  GLY GLY C . n 
C 3 43  LYS 43  43  43  LYS LYS C . n 
C 3 44  GLY 44  44  44  GLY GLY C . n 
C 3 45  LEU 45  45  45  LEU LEU C . n 
C 3 46  GLU 46  46  46  GLU GLU C . n 
C 3 47  TRP 47  47  47  TRP TRP C . n 
C 3 48  MET 48  48  48  MET MET C . n 
C 3 49  GLY 49  49  49  GLY GLY C . n 
C 3 50  ILE 50  50  50  ILE ILE C . n 
C 3 51  ILE 51  51  51  ILE ILE C . n 
C 3 52  ASN 52  52  52  ASN ASN C . n 
C 3 53  PRO 53  53  53  PRO PRO C . n 
C 3 54  ARG 54  54  54  ARG ARG C . n 
C 3 55  ASP 55  55  55  ASP ASP C . n 
C 3 56  SER 56  56  56  SER SER C . n 
C 3 57  ASP 57  57  57  ASP ASP C . n 
C 3 58  THR 58  58  58  THR THR C . n 
C 3 59  ARG 59  59  59  ARG ARG C . n 
C 3 60  TYR 60  60  60  TYR TYR C . n 
C 3 61  SER 61  61  61  SER SER C . n 
C 3 62  PRO 62  62  62  PRO PRO C . n 
C 3 63  SER 63  63  63  SER SER C . n 
C 3 64  PHE 64  64  64  PHE PHE C . n 
C 3 65  GLN 65  65  65  GLN GLN C . n 
C 3 66  GLY 66  66  66  GLY GLY C . n 
C 3 67  GLN 67  67  67  GLN GLN C . n 
C 3 68  VAL 68  68  68  VAL VAL C . n 
C 3 69  THR 69  69  69  THR THR C . n 
C 3 70  ILE 70  70  70  ILE ILE C . n 
C 3 71  SER 71  71  71  SER SER C . n 
C 3 72  ALA 72  72  72  ALA ALA C . n 
C 3 73  ASP 73  73  73  ASP ASP C . n 
C 3 74  LYS 74  74  74  LYS LYS C . n 
C 3 75  SER 75  75  75  SER SER C . n 
C 3 76  ILE 76  76  76  ILE ILE C . n 
C 3 77  SER 77  77  77  SER SER C . n 
C 3 78  THR 78  78  78  THR THR C . n 
C 3 79  ALA 79  79  79  ALA ALA C . n 
C 3 80  TYR 80  80  80  TYR TYR C . n 
C 3 81  LEU 81  81  81  LEU LEU C . n 
C 3 82  GLN 82  82  82  GLN GLN C . n 
C 3 83  TRP 83  83  83  TRP TRP C . n 
C 3 84  SER 84  84  84  SER SER C . n 
C 3 85  SER 85  85  85  SER SER C . n 
C 3 86  LEU 86  86  86  LEU LEU C . n 
C 3 87  LYS 87  87  87  LYS LYS C . n 
C 3 88  ALA 88  88  88  ALA ALA C . n 
C 3 89  SER 89  89  89  SER SER C . n 
C 3 90  ASP 90  90  90  ASP ASP C . n 
C 3 91  THR 91  91  91  THR THR C . n 
C 3 92  ALA 92  92  92  ALA ALA C . n 
C 3 93  MET 93  93  93  MET MET C . n 
C 3 94  TYR 94  94  94  TYR TYR C . n 
C 3 95  TYR 95  95  95  TYR TYR C . n 
C 3 96  CYS 96  96  96  CYS CYS C . n 
C 3 97  ALA 97  97  97  ALA ALA C . n 
C 3 98  ARG 98  98  98  ARG ARG C . n 
C 3 99  VAL 99  99  99  VAL VAL C . n 
C 3 100 VAL 100 100 100 VAL VAL C . n 
C 3 101 ALA 101 101 101 ALA ALA C . n 
C 3 102 ASP 102 102 102 ASP ASP C . n 
C 3 103 ARG 103 103 103 ARG ARG C . n 
C 3 104 GLU 104 104 104 GLU GLU C . n 
C 3 105 GLY 105 105 105 GLY GLY C . n 
C 3 106 PHE 106 106 106 PHE PHE C . n 
C 3 107 GLY 107 107 107 GLY GLY C . n 
C 3 108 TYR 108 108 108 TYR TYR C . n 
C 3 109 TYR 109 109 109 TYR TYR C . n 
C 3 110 TYR 110 110 110 TYR TYR C . n 
C 3 111 GLY 111 111 111 GLY GLY C . n 
C 3 112 MET 112 112 112 MET MET C . n 
C 3 113 ASP 113 113 113 ASP ASP C . n 
C 3 114 VAL 114 114 114 VAL VAL C . n 
C 3 115 TRP 115 115 115 TRP TRP C . n 
C 3 116 GLY 116 116 116 GLY GLY C . n 
C 3 117 GLN 117 117 117 GLN GLN C . n 
C 3 118 GLY 118 118 118 GLY GLY C . n 
C 3 119 THR 119 119 119 THR THR C . n 
C 3 120 THR 120 120 120 THR THR C . n 
C 3 121 VAL 121 121 121 VAL VAL C . n 
C 3 122 THR 122 122 122 THR THR C . n 
C 3 123 VAL 123 123 123 VAL VAL C . n 
C 3 124 SER 124 124 124 SER SER C . n 
C 3 125 SER 125 125 125 SER SER C . n 
C 3 126 ALA 126 126 126 ALA ALA C . n 
C 3 127 SER 127 127 127 SER SER C . n 
C 3 128 THR 128 128 128 THR THR C . n 
C 3 129 LYS 129 129 129 LYS LYS C . n 
C 3 130 GLY 130 130 130 GLY GLY C . n 
C 3 131 PRO 131 131 131 PRO PRO C . n 
C 3 132 SER 132 132 132 SER SER C . n 
C 3 133 VAL 133 133 133 VAL VAL C . n 
C 3 134 PHE 134 134 134 PHE PHE C . n 
C 3 135 PRO 135 135 135 PRO PRO C . n 
C 3 136 LEU 136 136 136 LEU LEU C . n 
C 3 137 ALA 137 137 137 ALA ALA C . n 
C 3 138 PRO 138 138 138 PRO PRO C . n 
C 3 139 SER 139 139 139 SER SER C . n 
C 3 140 SER 140 140 ?   ?   ?   C . n 
C 3 141 LYS 141 141 ?   ?   ?   C . n 
C 3 142 SER 142 142 ?   ?   ?   C . n 
C 3 143 THR 143 143 ?   ?   ?   C . n 
C 3 144 SER 144 144 ?   ?   ?   C . n 
C 3 145 GLY 145 145 ?   ?   ?   C . n 
C 3 146 GLY 146 146 ?   ?   ?   C . n 
C 3 147 THR 147 147 147 THR THR C . n 
C 3 148 ALA 148 148 148 ALA ALA C . n 
C 3 149 ALA 149 149 149 ALA ALA C . n 
C 3 150 LEU 150 150 150 LEU LEU C . n 
C 3 151 GLY 151 151 151 GLY GLY C . n 
C 3 152 CYS 152 152 152 CYS CYS C . n 
C 3 153 LEU 153 153 153 LEU LEU C . n 
C 3 154 VAL 154 154 154 VAL VAL C . n 
C 3 155 LYS 155 155 155 LYS LYS C . n 
C 3 156 ASP 156 156 156 ASP ASP C . n 
C 3 157 TYR 157 157 157 TYR TYR C . n 
C 3 158 PHE 158 158 158 PHE PHE C . n 
C 3 159 PRO 159 159 159 PRO PRO C . n 
C 3 160 GLU 160 160 160 GLU GLU C . n 
C 3 161 PRO 161 161 161 PRO PRO C . n 
C 3 162 VAL 162 162 162 VAL VAL C . n 
C 3 163 THR 163 163 163 THR THR C . n 
C 3 164 VAL 164 164 164 VAL VAL C . n 
C 3 165 SER 165 165 165 SER SER C . n 
C 3 166 TRP 166 166 166 TRP TRP C . n 
C 3 167 ASN 167 167 167 ASN ASN C . n 
C 3 168 SER 168 168 168 SER SER C . n 
C 3 169 GLY 169 169 169 GLY GLY C . n 
C 3 170 ALA 170 170 170 ALA ALA C . n 
C 3 171 LEU 171 171 171 LEU LEU C . n 
C 3 172 THR 172 172 172 THR THR C . n 
C 3 173 SER 173 173 173 SER SER C . n 
C 3 174 GLY 174 174 174 GLY GLY C . n 
C 3 175 VAL 175 175 175 VAL VAL C . n 
C 3 176 HIS 176 176 176 HIS HIS C . n 
C 3 177 THR 177 177 177 THR THR C . n 
C 3 178 PHE 178 178 178 PHE PHE C . n 
C 3 179 PRO 179 179 179 PRO PRO C . n 
C 3 180 ALA 180 180 180 ALA ALA C . n 
C 3 181 VAL 181 181 181 VAL VAL C . n 
C 3 182 LEU 182 182 182 LEU LEU C . n 
C 3 183 GLN 183 183 183 GLN GLN C . n 
C 3 184 SER 184 184 184 SER SER C . n 
C 3 185 SER 185 185 185 SER SER C . n 
C 3 186 GLY 186 186 186 GLY GLY C . n 
C 3 187 LEU 187 187 187 LEU LEU C . n 
C 3 188 TYR 188 188 188 TYR TYR C . n 
C 3 189 SER 189 189 189 SER SER C . n 
C 3 190 LEU 190 190 190 LEU LEU C . n 
C 3 191 SER 191 191 191 SER SER C . n 
C 3 192 SER 192 192 192 SER SER C . n 
C 3 193 VAL 193 193 193 VAL VAL C . n 
C 3 194 VAL 194 194 194 VAL VAL C . n 
C 3 195 THR 195 195 195 THR THR C . n 
C 3 196 VAL 196 196 196 VAL VAL C . n 
C 3 197 PRO 197 197 197 PRO PRO C . n 
C 3 198 SER 198 198 198 SER SER C . n 
C 3 199 SER 199 199 199 SER SER C . n 
C 3 200 SER 200 200 200 SER SER C . n 
C 3 201 LEU 201 201 201 LEU LEU C . n 
C 3 202 GLY 202 202 202 GLY GLY C . n 
C 3 203 THR 203 203 203 THR THR C . n 
C 3 204 GLN 204 204 204 GLN GLN C . n 
C 3 205 THR 205 205 205 THR THR C . n 
C 3 206 TYR 206 206 206 TYR TYR C . n 
C 3 207 ILE 207 207 207 ILE ILE C . n 
C 3 208 CYS 208 208 208 CYS CYS C . n 
C 3 209 ASN 209 209 209 ASN ASN C . n 
C 3 210 VAL 210 210 210 VAL VAL C . n 
C 3 211 ASN 211 211 211 ASN ASN C . n 
C 3 212 HIS 212 212 212 HIS HIS C . n 
C 3 213 LYS 213 213 213 LYS LYS C . n 
C 3 214 PRO 214 214 214 PRO PRO C . n 
C 3 215 SER 215 215 215 SER SER C . n 
C 3 216 ASN 216 216 216 ASN ASN C . n 
C 3 217 THR 217 217 217 THR THR C . n 
C 3 218 LYS 218 218 218 LYS LYS C . n 
C 3 219 VAL 219 219 219 VAL VAL C . n 
C 3 220 ASP 220 220 220 ASP ASP C . n 
C 3 221 LYS 221 221 221 LYS LYS C . n 
C 3 222 ARG 222 222 222 ARG ARG C . n 
C 3 223 VAL 223 223 223 VAL VAL C . n 
C 3 224 GLU 224 224 224 GLU GLU C . n 
C 3 225 PRO 225 225 225 PRO PRO C . n 
C 3 226 LYS 226 226 ?   ?   ?   C . n 
C 3 227 SER 227 227 ?   ?   ?   C . n 
C 3 228 CYS 228 228 ?   ?   ?   C . n 
C 3 229 ASP 229 229 ?   ?   ?   C . n 
C 3 230 LYS 230 230 ?   ?   ?   C . n 
D 4 1   GLU 1   1   1   GLU GLU D . n 
D 4 2   ILE 2   2   2   ILE ILE D . n 
D 4 3   VAL 3   3   3   VAL VAL D . n 
D 4 4   LEU 4   4   4   LEU LEU D . n 
D 4 5   THR 5   5   5   THR THR D . n 
D 4 6   GLN 6   6   6   GLN GLN D . n 
D 4 7   SER 7   7   7   SER SER D . n 
D 4 8   PRO 8   8   8   PRO PRO D . n 
D 4 9   GLY 9   9   9   GLY GLY D . n 
D 4 10  THR 10  10  10  THR THR D . n 
D 4 11  LEU 11  11  11  LEU LEU D . n 
D 4 12  SER 12  12  12  SER SER D . n 
D 4 13  LEU 13  13  13  LEU LEU D . n 
D 4 14  SER 14  14  14  SER SER D . n 
D 4 15  PRO 15  15  15  PRO PRO D . n 
D 4 16  GLY 16  16  16  GLY GLY D . n 
D 4 17  GLU 17  17  17  GLU GLU D . n 
D 4 18  GLY 18  18  18  GLY GLY D . n 
D 4 19  ALA 19  19  19  ALA ALA D . n 
D 4 20  THR 20  20  20  THR THR D . n 
D 4 21  LEU 21  21  21  LEU LEU D . n 
D 4 22  SER 22  22  22  SER SER D . n 
D 4 23  CYS 23  23  23  CYS CYS D . n 
D 4 24  ARG 24  24  24  ARG ARG D . n 
D 4 25  ALA 25  25  25  ALA ALA D . n 
D 4 26  SER 26  26  26  SER SER D . n 
D 4 27  GLN 27  27  27  GLN GLN D . n 
D 4 28  SER 28  28  28  SER SER D . n 
D 4 29  VAL 29  29  29  VAL VAL D . n 
D 4 30  ASP 30  30  30  ASP ASP D . n 
D 4 31  SER 31  31  31  SER SER D . n 
D 4 32  SER 32  32  32  SER SER D . n 
D 4 33  SER 33  33  33  SER SER D . n 
D 4 34  LEU 34  34  34  LEU LEU D . n 
D 4 35  ALA 35  35  35  ALA ALA D . n 
D 4 36  TRP 36  36  36  TRP TRP D . n 
D 4 37  TYR 37  37  37  TYR TYR D . n 
D 4 38  GLN 38  38  38  GLN GLN D . n 
D 4 39  GLN 39  39  39  GLN GLN D . n 
D 4 40  LYS 40  40  40  LYS LYS D . n 
D 4 41  PRO 41  41  41  PRO PRO D . n 
D 4 42  GLY 42  42  42  GLY GLY D . n 
D 4 43  GLN 43  43  43  GLN GLN D . n 
D 4 44  ALA 44  44  44  ALA ALA D . n 
D 4 45  PRO 45  45  45  PRO PRO D . n 
D 4 46  ARG 46  46  46  ARG ARG D . n 
D 4 47  LEU 47  47  47  LEU LEU D . n 
D 4 48  LEU 48  48  48  LEU LEU D . n 
D 4 49  ILE 49  49  49  ILE ILE D . n 
D 4 50  PHE 50  50  50  PHE PHE D . n 
D 4 51  ALA 51  51  51  ALA ALA D . n 
D 4 52  GLY 52  52  52  GLY GLY D . n 
D 4 53  SER 53  53  53  SER SER D . n 
D 4 54  SER 54  54  54  SER SER D . n 
D 4 55  ARG 55  55  55  ARG ARG D . n 
D 4 56  ALA 56  56  56  ALA ALA D . n 
D 4 57  THR 57  57  57  THR THR D . n 
D 4 58  GLY 58  58  58  GLY GLY D . n 
D 4 59  ILE 59  59  59  ILE ILE D . n 
D 4 60  PRO 60  60  60  PRO PRO D . n 
D 4 61  ASP 61  61  61  ASP ASP D . n 
D 4 62  ARG 62  62  62  ARG ARG D . n 
D 4 63  PHE 63  63  63  PHE PHE D . n 
D 4 64  SER 64  64  64  SER SER D . n 
D 4 65  GLY 65  65  65  GLY GLY D . n 
D 4 66  LYS 66  66  66  LYS LYS D . n 
D 4 67  THR 67  67  67  THR THR D . n 
D 4 68  SER 68  68  68  SER SER D . n 
D 4 69  GLY 69  69  69  GLY GLY D . n 
D 4 70  THR 70  70  70  THR THR D . n 
D 4 71  ASP 71  71  71  ASP ASP D . n 
D 4 72  PHE 72  72  72  PHE PHE D . n 
D 4 73  THR 73  73  73  THR THR D . n 
D 4 74  LEU 74  74  74  LEU LEU D . n 
D 4 75  THR 75  75  75  THR THR D . n 
D 4 76  ILE 76  76  76  ILE ILE D . n 
D 4 77  SER 77  77  77  SER SER D . n 
D 4 78  ARG 78  78  78  ARG ARG D . n 
D 4 79  LEU 79  79  79  LEU LEU D . n 
D 4 80  GLU 80  80  80  GLU GLU D . n 
D 4 81  PRO 81  81  81  PRO PRO D . n 
D 4 82  GLU 82  82  82  GLU GLU D . n 
D 4 83  ASP 83  83  83  ASP ASP D . n 
D 4 84  PHE 84  84  84  PHE PHE D . n 
D 4 85  ALA 85  85  85  ALA ALA D . n 
D 4 86  VAL 86  86  86  VAL VAL D . n 
D 4 87  TYR 87  87  87  TYR TYR D . n 
D 4 88  TYR 88  88  88  TYR TYR D . n 
D 4 89  CYS 89  89  89  CYS CYS D . n 
D 4 90  GLN 90  90  90  GLN GLN D . n 
D 4 91  GLN 91  91  91  GLN GLN D . n 
D 4 92  CYS 92  92  92  CYS CYS D . n 
D 4 93  GLY 93  93  93  GLY GLY D . n 
D 4 94  ASN 94  94  94  ASN ASN D . n 
D 4 95  SER 95  95  95  SER SER D . n 
D 4 96  PRO 96  96  96  PRO PRO D . n 
D 4 97  TRP 97  97  97  TRP TRP D . n 
D 4 98  THR 98  98  98  THR THR D . n 
D 4 99  PHE 99  99  99  PHE PHE D . n 
D 4 100 GLY 100 100 100 GLY GLY D . n 
D 4 101 GLN 101 101 101 GLN GLN D . n 
D 4 102 GLY 102 102 102 GLY GLY D . n 
D 4 103 THR 103 103 103 THR THR D . n 
D 4 104 LYS 104 104 104 LYS LYS D . n 
D 4 105 VAL 105 105 105 VAL VAL D . n 
D 4 106 GLU 106 106 106 GLU GLU D . n 
D 4 107 ILE 107 107 107 ILE ILE D . n 
D 4 108 LYS 108 108 108 LYS LYS D . n 
D 4 109 ARG 109 109 109 ARG ARG D . n 
D 4 110 THR 110 110 110 THR THR D . n 
D 4 111 VAL 111 111 111 VAL VAL D . n 
D 4 112 ALA 112 112 112 ALA ALA D . n 
D 4 113 ALA 113 113 113 ALA ALA D . n 
D 4 114 PRO 114 114 114 PRO PRO D . n 
D 4 115 SER 115 115 115 SER SER D . n 
D 4 116 VAL 116 116 116 VAL VAL D . n 
D 4 117 PHE 117 117 117 PHE PHE D . n 
D 4 118 ILE 118 118 118 ILE ILE D . n 
D 4 119 PHE 119 119 119 PHE PHE D . n 
D 4 120 PRO 120 120 120 PRO PRO D . n 
D 4 121 PRO 121 121 121 PRO PRO D . n 
D 4 122 SER 122 122 122 SER SER D . n 
D 4 123 ASP 123 123 123 ASP ASP D . n 
D 4 124 GLU 124 124 124 GLU GLU D . n 
D 4 125 GLN 125 125 125 GLN GLN D . n 
D 4 126 LEU 126 126 126 LEU LEU D . n 
D 4 127 LYS 127 127 127 LYS LYS D . n 
D 4 128 SER 128 128 128 SER SER D . n 
D 4 129 GLY 129 129 129 GLY GLY D . n 
D 4 130 THR 130 130 130 THR THR D . n 
D 4 131 ALA 131 131 131 ALA ALA D . n 
D 4 132 SER 132 132 132 SER SER D . n 
D 4 133 VAL 133 133 133 VAL VAL D . n 
D 4 134 VAL 134 134 134 VAL VAL D . n 
D 4 135 CYS 135 135 135 CYS CYS D . n 
D 4 136 LEU 136 136 136 LEU LEU D . n 
D 4 137 LEU 137 137 137 LEU LEU D . n 
D 4 138 ASN 138 138 138 ASN ASN D . n 
D 4 139 ASN 139 139 139 ASN ASN D . n 
D 4 140 PHE 140 140 140 PHE PHE D . n 
D 4 141 TYR 141 141 141 TYR TYR D . n 
D 4 142 PRO 142 142 142 PRO PRO D . n 
D 4 143 ARG 143 143 143 ARG ARG D . n 
D 4 144 GLU 144 144 144 GLU GLU D . n 
D 4 145 ALA 145 145 145 ALA ALA D . n 
D 4 146 LYS 146 146 146 LYS LYS D . n 
D 4 147 VAL 147 147 147 VAL VAL D . n 
D 4 148 GLN 148 148 148 GLN GLN D . n 
D 4 149 TRP 149 149 149 TRP TRP D . n 
D 4 150 LYS 150 150 150 LYS LYS D . n 
D 4 151 VAL 151 151 151 VAL VAL D . n 
D 4 152 ASP 152 152 152 ASP ASP D . n 
D 4 153 ASN 153 153 153 ASN ASN D . n 
D 4 154 ALA 154 154 154 ALA ALA D . n 
D 4 155 LEU 155 155 155 LEU LEU D . n 
D 4 156 GLN 156 156 156 GLN GLN D . n 
D 4 157 SER 157 157 157 SER SER D . n 
D 4 158 GLY 158 158 158 GLY GLY D . n 
D 4 159 ASN 159 159 159 ASN ASN D . n 
D 4 160 SER 160 160 160 SER SER D . n 
D 4 161 GLN 161 161 161 GLN GLN D . n 
D 4 162 GLU 162 162 162 GLU GLU D . n 
D 4 163 SER 163 163 163 SER SER D . n 
D 4 164 VAL 164 164 164 VAL VAL D . n 
D 4 165 THR 165 165 165 THR THR D . n 
D 4 166 GLU 166 166 166 GLU GLU D . n 
D 4 167 GLN 167 167 167 GLN GLN D . n 
D 4 168 ASP 168 168 168 ASP ASP D . n 
D 4 169 SER 169 169 169 SER SER D . n 
D 4 170 LYS 170 170 170 LYS LYS D . n 
D 4 171 ASP 171 171 171 ASP ASP D . n 
D 4 172 SER 172 172 172 SER SER D . n 
D 4 173 THR 173 173 173 THR THR D . n 
D 4 174 TYR 174 174 174 TYR TYR D . n 
D 4 175 SER 175 175 175 SER SER D . n 
D 4 176 LEU 176 176 176 LEU LEU D . n 
D 4 177 SER 177 177 177 SER SER D . n 
D 4 178 SER 178 178 178 SER SER D . n 
D 4 179 THR 179 179 179 THR THR D . n 
D 4 180 LEU 180 180 180 LEU LEU D . n 
D 4 181 THR 181 181 181 THR THR D . n 
D 4 182 LEU 182 182 182 LEU LEU D . n 
D 4 183 SER 183 183 183 SER SER D . n 
D 4 184 LYS 184 184 184 LYS LYS D . n 
D 4 185 ALA 185 185 185 ALA ALA D . n 
D 4 186 ASP 186 186 186 ASP ASP D . n 
D 4 187 TYR 187 187 187 TYR TYR D . n 
D 4 188 GLU 188 188 188 GLU GLU D . n 
D 4 189 LYS 189 189 189 LYS LYS D . n 
D 4 190 HIS 190 190 190 HIS HIS D . n 
D 4 191 LYS 191 191 191 LYS LYS D . n 
D 4 192 VAL 192 192 192 VAL VAL D . n 
D 4 193 TYR 193 193 193 TYR TYR D . n 
D 4 194 ALA 194 194 194 ALA ALA D . n 
D 4 195 CYS 195 195 195 CYS CYS D . n 
D 4 196 GLU 196 196 196 GLU GLU D . n 
D 4 197 VAL 197 197 197 VAL VAL D . n 
D 4 198 THR 198 198 198 THR THR D . n 
D 4 199 HIS 199 199 199 HIS HIS D . n 
D 4 200 GLN 200 200 200 GLN GLN D . n 
D 4 201 GLY 201 201 201 GLY GLY D . n 
D 4 202 LEU 202 202 202 LEU LEU D . n 
D 4 203 SER 203 203 203 SER SER D . n 
D 4 204 SER 204 204 204 SER SER D . n 
D 4 205 PRO 205 205 205 PRO PRO D . n 
D 4 206 VAL 206 206 206 VAL VAL D . n 
D 4 207 THR 207 207 207 THR THR D . n 
D 4 208 LYS 208 208 208 LYS LYS D . n 
D 4 209 SER 209 209 209 SER SER D . n 
D 4 210 PHE 210 210 210 PHE PHE D . n 
D 4 211 ASN 211 211 211 ASN ASN D . n 
D 4 212 ARG 212 212 212 ARG ARG D . n 
D 4 213 GLY 213 213 213 GLY GLY D . n 
D 4 214 GLU 214 214 214 GLU GLU D . n 
D 4 215 CYS 215 215 215 CYS CYS D . n 
E 1 1   GLY 1   1   ?   ?   ?   E . n 
E 1 2   LEU 2   2   ?   ?   ?   E . n 
E 1 3   PHE 3   3   ?   ?   ?   E . n 
E 1 4   GLY 4   4   ?   ?   ?   E . n 
E 1 5   ALA 5   5   ?   ?   ?   E . n 
E 1 6   ILE 6   6   ?   ?   ?   E . n 
E 1 7   ALA 7   7   ?   ?   ?   E . n 
E 1 8   GLY 8   8   ?   ?   ?   E . n 
E 1 9   PHE 9   9   ?   ?   ?   E . n 
E 1 10  ILE 10  10  10  ILE ILE E . n 
E 1 11  GLU 11  11  11  GLU GLU E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  GLY 13  13  13  GLY GLY E . n 
E 1 14  TRP 14  14  14  TRP TRP E . n 
E 1 15  THR 15  15  15  THR THR E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  MET 17  17  17  MET MET E . n 
E 1 18  VAL 18  18  18  VAL VAL E . n 
E 1 19  ASP 19  19  19  ASP ASP E . n 
E 1 20  GLY 20  20  20  GLY GLY E . n 
E 1 21  TRP 21  21  21  TRP TRP E . n 
E 1 22  TYR 22  22  22  TYR TYR E . n 
E 1 23  GLY 23  23  23  GLY GLY E . n 
E 1 24  TYR 24  24  ?   ?   ?   E . n 
E 1 25  HIS 25  25  ?   ?   ?   E . n 
E 1 26  HIS 26  26  ?   ?   ?   E . n 
E 1 27  GLN 27  27  ?   ?   ?   E . n 
E 1 28  ASN 28  28  ?   ?   ?   E . n 
E 1 29  GLU 29  29  ?   ?   ?   E . n 
E 1 30  GLN 30  30  ?   ?   ?   E . n 
E 1 31  GLY 31  31  ?   ?   ?   E . n 
E 1 32  SER 32  32  ?   ?   ?   E . n 
E 1 33  GLY 33  33  ?   ?   ?   E . n 
E 1 34  TYR 34  34  ?   ?   ?   E . n 
E 1 35  ALA 35  35  ?   ?   ?   E . n 
E 1 36  ALA 36  36  36  ALA ALA E . n 
E 1 37  ASP 37  37  37  ASP ASP E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  LYS 39  39  39  LYS LYS E . n 
E 1 40  SER 40  40  40  SER SER E . n 
E 1 41  THR 41  41  41  THR THR E . n 
E 1 42  GLN 42  42  42  GLN GLN E . n 
E 1 43  ASN 43  43  43  ASN ASN E . n 
E 1 44  ALA 44  44  44  ALA ALA E . n 
E 1 45  ILE 45  45  45  ILE ILE E . n 
E 1 46  ASP 46  46  46  ASP ASP E . n 
E 1 47  GLU 47  47  47  GLU GLU E . n 
E 1 48  ILE 48  48  48  ILE ILE E . n 
E 1 49  THR 49  49  49  THR THR E . n 
E 1 50  ASN 50  50  50  ASN ASN E . n 
E 1 51  LYS 51  51  51  LYS LYS E . n 
E 1 52  VAL 52  52  52  VAL VAL E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  SER 54  54  54  SER SER E . n 
E 1 55  VAL 55  55  55  VAL VAL E . n 
E 1 56  ILE 56  56  56  ILE ILE E . n 
E 1 57  GLU 57  57  57  GLU GLU E . n 
E 1 58  LYS 58  58  58  LYS LYS E . n 
E 1 59  MET 59  59  59  MET MET E . n 
E 1 60  ASN 60  60  60  ASN ASN E . n 
E 1 61  THR 61  61  61  THR THR E . n 
E 1 62  GLN 62  62  62  GLN GLN E . n 
E 1 63  PHE 63  63  63  PHE PHE E . n 
E 1 64  THR 64  64  64  THR THR E . n 
E 1 65  ALA 65  65  65  ALA ALA E . n 
E 1 66  VAL 66  66  66  VAL VAL E . n 
E 1 67  GLY 67  67  67  GLY GLY E . n 
E 1 68  LYS 68  68  68  LYS LYS E . n 
E 1 69  GLU 69  69  69  GLU GLU E . n 
E 1 70  PHE 70  70  ?   ?   ?   E . n 
E 1 71  ASN 71  71  ?   ?   ?   E . n 
E 1 72  HIS 72  72  ?   ?   ?   E . n 
E 1 73  LEU 73  73  ?   ?   ?   E . n 
E 1 74  GLU 74  74  ?   ?   ?   E . n 
E 1 75  LYS 75  75  ?   ?   ?   E . n 
E 1 76  ARG 76  76  ?   ?   ?   E . n 
E 1 77  ILE 77  77  ?   ?   ?   E . n 
E 1 78  GLU 78  78  ?   ?   ?   E . n 
E 1 79  ASN 79  79  ?   ?   ?   E . n 
E 1 80  LEU 80  80  ?   ?   ?   E . n 
E 1 81  ASN 81  81  ?   ?   ?   E . n 
E 1 82  LYS 82  82  ?   ?   ?   E . n 
E 1 83  LYS 83  83  83  LYS LYS E . n 
E 1 84  VAL 84  84  84  VAL VAL E . n 
E 1 85  ASP 85  85  85  ASP ASP E . n 
E 1 86  ASP 86  86  86  ASP ASP E . n 
E 1 87  GLY 87  87  87  GLY GLY E . n 
E 1 88  PHE 88  88  88  PHE PHE E . n 
E 1 89  LEU 89  89  89  LEU LEU E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  ILE 91  91  91  ILE ILE E . n 
E 1 92  TRP 92  92  92  TRP TRP E . n 
E 1 93  THR 93  93  93  THR THR E . n 
E 1 94  TYR 94  94  94  TYR TYR E . n 
E 1 95  ASN 95  95  95  ASN ASN E . n 
E 1 96  ALA 96  96  96  ALA ALA E . n 
E 1 97  GLU 97  97  97  GLU GLU E . n 
E 1 98  LEU 98  98  98  LEU LEU E . n 
E 1 99  LEU 99  99  99  LEU LEU E . n 
E 1 100 VAL 100 100 100 VAL VAL E . n 
E 1 101 LEU 101 101 101 LEU LEU E . n 
E 1 102 LEU 102 102 102 LEU LEU E . n 
E 1 103 GLU 103 103 103 GLU GLU E . n 
E 1 104 ASN 104 104 104 ASN ASN E . n 
E 1 105 GLU 105 105 105 GLU GLU E . n 
E 1 106 ARG 106 106 106 ARG ARG E . n 
E 1 107 THR 107 107 107 THR THR E . n 
E 1 108 LEU 108 108 108 LEU LEU E . n 
E 1 109 ASP 109 109 109 ASP ASP E . n 
E 1 110 TYR 110 110 110 TYR TYR E . n 
E 1 111 HIS 111 111 111 HIS HIS E . n 
E 1 112 ASP 112 112 112 ASP ASP E . n 
E 1 113 SER 113 113 113 SER SER E . n 
E 1 114 ASN 114 114 114 ASN ASN E . n 
E 1 115 VAL 115 115 115 VAL VAL E . n 
E 1 116 LYS 116 116 116 LYS LYS E . n 
E 1 117 ASN 117 117 117 ASN ASN E . n 
E 1 118 LEU 118 118 118 LEU LEU E . n 
E 1 119 TYR 119 119 119 TYR TYR E . n 
E 1 120 GLU 120 120 120 GLU GLU E . n 
E 1 121 LYS 121 121 121 LYS LYS E . n 
E 1 122 VAL 122 122 122 VAL VAL E . n 
E 1 123 ARG 123 123 123 ARG ARG E . n 
E 1 124 SER 124 124 124 SER SER E . n 
E 1 125 GLN 125 125 125 GLN GLN E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 LYS 127 127 ?   ?   ?   E . n 
E 1 128 ASN 128 128 ?   ?   ?   E . n 
E 1 129 ASN 129 129 ?   ?   ?   E . n 
E 1 130 ALA 130 130 ?   ?   ?   E . n 
E 1 131 LYS 131 131 ?   ?   ?   E . n 
E 1 132 GLU 132 132 ?   ?   ?   E . n 
E 1 133 ILE 133 133 ?   ?   ?   E . n 
E 1 134 GLY 134 134 ?   ?   ?   E . n 
E 1 135 ASN 135 135 ?   ?   ?   E . n 
E 1 136 GLY 136 136 ?   ?   ?   E . n 
E 1 137 CYS 137 137 ?   ?   ?   E . n 
E 1 138 PHE 138 138 ?   ?   ?   E . n 
E 1 139 GLU 139 139 ?   ?   ?   E . n 
E 1 140 PHE 140 140 ?   ?   ?   E . n 
E 1 141 TYR 141 141 ?   ?   ?   E . n 
E 1 142 HIS 142 142 ?   ?   ?   E . n 
E 1 143 LYS 143 143 ?   ?   ?   E . n 
E 1 144 CYS 144 144 ?   ?   ?   E . n 
E 1 145 ASP 145 145 ?   ?   ?   E . n 
E 1 146 ASN 146 146 ?   ?   ?   E . n 
E 1 147 THR 147 147 ?   ?   ?   E . n 
E 1 148 CYS 148 148 148 CYS CYS E . n 
E 1 149 MET 149 149 149 MET MET E . n 
E 1 150 GLU 150 150 150 GLU GLU E . n 
E 1 151 SER 151 151 151 SER SER E . n 
E 1 152 VAL 152 152 152 VAL VAL E . n 
E 1 153 LYS 153 153 153 LYS LYS E . n 
E 1 154 ASN 154 154 154 ASN ASN E . n 
E 1 155 GLY 155 155 ?   ?   ?   E . n 
E 1 156 THR 156 156 ?   ?   ?   E . n 
E 1 157 TYR 157 157 ?   ?   ?   E . n 
E 1 158 ASP 158 158 ?   ?   ?   E . n 
E 1 159 TYR 159 159 159 TYR TYR E . n 
E 1 160 PRO 160 160 160 PRO PRO E . n 
E 1 161 LYS 161 161 161 LYS LYS E . n 
E 1 162 TYR 162 162 162 TYR TYR E . n 
E 1 163 SER 163 163 163 SER SER E . n 
E 1 164 GLU 164 164 164 GLU GLU E . n 
E 1 165 GLU 165 165 165 GLU GLU E . n 
E 1 166 ALA 166 166 166 ALA ALA E . n 
E 1 167 LYS 167 167 167 LYS LYS E . n 
E 1 168 LEU 168 168 168 LEU LEU E . n 
E 1 169 ASN 169 169 169 ASN ASN E . n 
E 1 170 ARG 170 170 170 ARG ARG E . n 
E 1 171 GLU 171 171 171 GLU GLU E . n 
E 1 172 GLU 172 172 172 GLU GLU E . n 
E 1 173 ILE 173 173 173 ILE ILE E . n 
E 1 174 ASP 174 174 174 ASP ASP E . n 
E 1 175 GLY 175 175 ?   ?   ?   E . n 
E 1 176 VAL 176 176 ?   ?   ?   E . n 
F 2 1   ALA 1   10  ?   ?   ?   F . n 
F 2 2   ASP 2   11  ?   ?   ?   F . n 
F 2 3   THR 3   12  ?   ?   ?   F . n 
F 2 4   LEU 4   13  ?   ?   ?   F . n 
F 2 5   CYS 5   14  ?   ?   ?   F . n 
F 2 6   ILE 6   15  ?   ?   ?   F . n 
F 2 7   GLY 7   16  ?   ?   ?   F . n 
F 2 8   TYR 8   17  ?   ?   ?   F . n 
F 2 9   HIS 9   18  ?   ?   ?   F . n 
F 2 10  ALA 10  19  ?   ?   ?   F . n 
F 2 11  ASN 11  20  20  ASN ASN F . n 
F 2 12  ASN 12  21  21  ASN ASN F . n 
F 2 13  SER 13  22  22  SER SER F . n 
F 2 14  THR 14  23  23  THR THR F . n 
F 2 15  ASP 15  24  24  ASP ASP F . n 
F 2 16  THR 16  25  25  THR THR F . n 
F 2 17  VAL 17  26  26  VAL VAL F . n 
F 2 18  ASP 18  27  27  ASP ASP F . n 
F 2 19  THR 19  28  28  THR THR F . n 
F 2 20  VAL 20  29  29  VAL VAL F . n 
F 2 21  LEU 21  30  30  LEU LEU F . n 
F 2 22  GLU 22  31  31  GLU GLU F . n 
F 2 23  LYS 23  32  32  LYS LYS F . n 
F 2 24  ASN 24  33  33  ASN ASN F . n 
F 2 25  VAL 25  34  34  VAL VAL F . n 
F 2 26  THR 26  35  35  THR THR F . n 
F 2 27  VAL 27  36  36  VAL VAL F . n 
F 2 28  THR 28  37  37  THR THR F . n 
F 2 29  HIS 29  38  38  HIS HIS F . n 
F 2 30  SER 30  39  39  SER SER F . n 
F 2 31  VAL 31  40  40  VAL VAL F . n 
F 2 32  ASN 32  41  41  ASN ASN F . n 
F 2 33  LEU 33  42  42  LEU LEU F . n 
F 2 34  LEU 34  43  43  LEU LEU F . n 
F 2 35  GLU 35  44  44  GLU GLU F . n 
F 2 36  ASP 36  45  45  ASP ASP F . n 
F 2 37  LYS 37  46  46  LYS LYS F . n 
F 2 38  HIS 38  47  47  HIS HIS F . n 
F 2 39  ASN 39  48  48  ASN ASN F . n 
F 2 40  GLY 40  49  49  GLY GLY F . n 
F 2 41  LYS 41  50  50  LYS LYS F . n 
F 2 42  LEU 42  51  51  LEU LEU F . n 
F 2 43  CYS 43  52  52  CYS CYS F . n 
F 2 44  LYS 44  53  53  LYS LYS F . n 
F 2 45  LEU 45  54  54  LEU LEU F . n 
F 2 46  ARG 46  55  55  ARG ARG F . n 
F 2 47  GLY 47  55  55  GLY GLY F A n 
F 2 48  VAL 48  56  56  VAL VAL F . n 
F 2 49  ALA 49  57  57  ALA ALA F . n 
F 2 50  PRO 50  58  58  PRO PRO F . n 
F 2 51  LEU 51  59  59  LEU LEU F . n 
F 2 52  HIS 52  60  60  HIS HIS F . n 
F 2 53  LEU 53  61  61  LEU LEU F . n 
F 2 54  GLY 54  62  62  GLY GLY F . n 
F 2 55  LYS 55  63  63  LYS LYS F . n 
F 2 56  CYS 56  64  64  CYS CYS F . n 
F 2 57  ASN 57  65  65  ASN ASN F . n 
F 2 58  ILE 58  66  66  ILE ILE F . n 
F 2 59  ALA 59  67  67  ALA ALA F . n 
F 2 60  GLY 60  68  68  GLY GLY F . n 
F 2 61  TRP 61  69  69  TRP TRP F . n 
F 2 62  ILE 62  70  70  ILE ILE F . n 
F 2 63  LEU 63  71  71  LEU LEU F . n 
F 2 64  GLY 64  72  72  GLY GLY F . n 
F 2 65  ASN 65  73  73  ASN ASN F . n 
F 2 66  PRO 66  74  74  PRO PRO F . n 
F 2 67  GLU 67  75  75  GLU GLU F . n 
F 2 68  CYS 68  76  76  CYS CYS F . n 
F 2 69  GLU 69  77  ?   ?   ?   F . n 
F 2 70  SER 70  78  ?   ?   ?   F . n 
F 2 71  LEU 71  79  ?   ?   ?   F . n 
F 2 72  SER 72  80  ?   ?   ?   F . n 
F 2 73  THR 73  81  ?   ?   ?   F . n 
F 2 74  ALA 74  82  82  ALA ALA F . n 
F 2 75  SER 75  83  83  SER SER F . n 
F 2 76  SER 76  83  83  SER SER F A n 
F 2 77  TRP 77  84  84  TRP TRP F . n 
F 2 78  SER 78  85  85  SER SER F . n 
F 2 79  TYR 79  86  86  TYR TYR F . n 
F 2 80  ILE 80  87  87  ILE ILE F . n 
F 2 81  VAL 81  88  88  VAL VAL F . n 
F 2 82  GLU 82  89  89  GLU GLU F . n 
F 2 83  THR 83  90  90  THR THR F . n 
F 2 84  PRO 84  90  90  PRO PRO F A n 
F 2 85  SER 85  91  91  SER SER F . n 
F 2 86  SER 86  92  92  SER SER F . n 
F 2 87  ASP 87  93  93  ASP ASP F . n 
F 2 88  ASN 88  94  94  ASN ASN F . n 
F 2 89  GLY 89  95  95  GLY GLY F . n 
F 2 90  THR 90  96  96  THR THR F . n 
F 2 91  CYS 91  97  97  CYS CYS F . n 
F 2 92  TYR 92  98  98  TYR TYR F . n 
F 2 93  PRO 93  99  99  PRO PRO F . n 
F 2 94  GLY 94  100 100 GLY GLY F . n 
F 2 95  ASP 95  101 101 ASP ASP F . n 
F 2 96  PHE 96  102 102 PHE PHE F . n 
F 2 97  ILE 97  103 103 ILE ILE F . n 
F 2 98  ASP 98  104 104 ASP ASP F . n 
F 2 99  TYR 99  105 105 TYR TYR F . n 
F 2 100 GLU 100 106 106 GLU GLU F . n 
F 2 101 GLU 101 107 107 GLU GLU F . n 
F 2 102 LEU 102 108 108 LEU LEU F . n 
F 2 103 ARG 103 109 109 ARG ARG F . n 
F 2 104 GLU 104 110 110 GLU GLU F . n 
F 2 105 GLN 105 111 111 GLN GLN F . n 
F 2 106 LEU 106 112 112 LEU LEU F . n 
F 2 107 SER 107 113 113 SER SER F . n 
F 2 108 SER 108 114 114 SER SER F . n 
F 2 109 VAL 109 115 115 VAL VAL F . n 
F 2 110 SER 110 116 116 SER SER F . n 
F 2 111 SER 111 116 116 SER SER F A n 
F 2 112 PHE 112 116 116 PHE PHE F B n 
F 2 113 GLU 113 116 116 GLU GLU F C n 
F 2 114 ARG 114 117 117 ARG ARG F . n 
F 2 115 PHE 115 118 118 PHE PHE F . n 
F 2 116 GLU 116 119 119 GLU GLU F . n 
F 2 117 ILE 117 120 120 ILE ILE F . n 
F 2 118 PHE 118 121 121 PHE PHE F . n 
F 2 119 PRO 119 122 122 PRO PRO F . n 
F 2 120 LYS 120 123 123 LYS LYS F . n 
F 2 121 THR 121 124 124 THR THR F . n 
F 2 122 SER 122 125 125 SER SER F . n 
F 2 123 SER 123 126 126 SER SER F . n 
F 2 124 TRP 124 127 127 TRP TRP F . n 
F 2 125 PRO 125 128 128 PRO PRO F . n 
F 2 126 ASN 126 129 129 ASN ASN F . n 
F 2 127 HIS 127 130 130 HIS HIS F . n 
F 2 128 ASP 128 131 131 ASP ASP F . n 
F 2 129 SER 129 132 132 SER SER F . n 
F 2 130 ASP 130 133 133 ASP ASP F . n 
F 2 131 LYS 131 133 133 LYS LYS F A n 
F 2 132 GLY 132 134 134 GLY GLY F . n 
F 2 133 VAL 133 135 135 VAL VAL F . n 
F 2 134 THR 134 136 136 THR THR F . n 
F 2 135 ALA 135 137 137 ALA ALA F . n 
F 2 136 ALA 136 138 138 ALA ALA F . n 
F 2 137 CYS 137 139 139 CYS CYS F . n 
F 2 138 PRO 138 140 140 PRO PRO F . n 
F 2 139 HIS 139 141 141 HIS HIS F . n 
F 2 140 ALA 140 142 142 ALA ALA F . n 
F 2 141 GLY 141 143 143 GLY GLY F . n 
F 2 142 ALA 142 144 144 ALA ALA F . n 
F 2 143 LYS 143 145 145 LYS LYS F . n 
F 2 144 SER 144 146 146 SER SER F . n 
F 2 145 PHE 145 147 147 PHE PHE F . n 
F 2 146 TYR 146 148 148 TYR TYR F . n 
F 2 147 LYS 147 149 149 LYS LYS F . n 
F 2 148 ASN 148 150 150 ASN ASN F . n 
F 2 149 LEU 149 151 151 LEU LEU F . n 
F 2 150 ILE 150 152 152 ILE ILE F . n 
F 2 151 TRP 151 153 153 TRP TRP F . n 
F 2 152 LEU 152 154 154 LEU LEU F . n 
F 2 153 VAL 153 155 155 VAL VAL F . n 
F 2 154 LYS 154 156 156 LYS LYS F . n 
F 2 155 LYS 155 157 157 LYS LYS F . n 
F 2 156 GLY 156 158 158 GLY GLY F . n 
F 2 157 ASN 157 159 159 ASN ASN F . n 
F 2 158 SER 158 160 160 SER SER F . n 
F 2 159 TYR 159 161 161 TYR TYR F . n 
F 2 160 PRO 160 162 162 PRO PRO F . n 
F 2 161 LYS 161 163 163 LYS LYS F . n 
F 2 162 LEU 162 164 164 LEU LEU F . n 
F 2 163 SER 163 165 165 SER SER F . n 
F 2 164 LYS 164 166 166 LYS LYS F . n 
F 2 165 SER 165 167 167 SER SER F . n 
F 2 166 TYR 166 168 168 TYR TYR F . n 
F 2 167 ILE 167 169 169 ILE ILE F . n 
F 2 168 ASN 168 170 170 ASN ASN F . n 
F 2 169 ASP 169 171 171 ASP ASP F . n 
F 2 170 LYS 170 172 172 LYS LYS F . n 
F 2 171 GLY 171 173 173 GLY GLY F . n 
F 2 172 LYS 172 174 174 LYS LYS F . n 
F 2 173 GLU 173 175 175 GLU GLU F . n 
F 2 174 VAL 174 176 176 VAL VAL F . n 
F 2 175 LEU 175 177 177 LEU LEU F . n 
F 2 176 VAL 176 178 178 VAL VAL F . n 
F 2 177 LEU 177 179 179 LEU LEU F . n 
F 2 178 TRP 178 180 180 TRP TRP F . n 
F 2 179 GLY 179 181 181 GLY GLY F . n 
F 2 180 ILE 180 182 182 ILE ILE F . n 
F 2 181 HIS 181 183 183 HIS HIS F . n 
F 2 182 HIS 182 184 184 HIS HIS F . n 
F 2 183 PRO 183 185 185 PRO PRO F . n 
F 2 184 SER 184 186 186 SER SER F . n 
F 2 185 THR 185 187 187 THR THR F . n 
F 2 186 SER 186 188 188 SER SER F . n 
F 2 187 ALA 187 189 189 ALA ALA F . n 
F 2 188 ASP 188 190 190 ASP ASP F . n 
F 2 189 GLN 189 191 191 GLN GLN F . n 
F 2 190 GLN 190 192 192 GLN GLN F . n 
F 2 191 SER 191 193 193 SER SER F . n 
F 2 192 LEU 192 194 194 LEU LEU F . n 
F 2 193 TYR 193 195 195 TYR TYR F . n 
F 2 194 GLN 194 196 196 GLN GLN F . n 
F 2 195 ASN 195 197 197 ASN ASN F . n 
F 2 196 ALA 196 198 198 ALA ALA F . n 
F 2 197 ASP 197 199 199 ASP ASP F . n 
F 2 198 ALA 198 200 200 ALA ALA F . n 
F 2 199 TYR 199 201 201 TYR TYR F . n 
F 2 200 VAL 200 202 202 VAL VAL F . n 
F 2 201 PHE 201 203 203 PHE PHE F . n 
F 2 202 VAL 202 204 204 VAL VAL F . n 
F 2 203 GLY 203 205 205 GLY GLY F . n 
F 2 204 SER 204 206 206 SER SER F . n 
F 2 205 SER 205 207 207 SER SER F . n 
F 2 206 ARG 206 208 208 ARG ARG F . n 
F 2 207 TYR 207 209 209 TYR TYR F . n 
F 2 208 SER 208 210 210 SER SER F . n 
F 2 209 LYS 209 211 211 LYS LYS F . n 
F 2 210 THR 210 212 212 THR THR F . n 
F 2 211 PHE 211 213 213 PHE PHE F . n 
F 2 212 LYS 212 214 214 LYS LYS F . n 
F 2 213 PRO 213 215 215 PRO PRO F . n 
F 2 214 GLU 214 216 216 GLU GLU F . n 
F 2 215 ILE 215 217 217 ILE ILE F . n 
F 2 216 ALA 216 218 218 ALA ALA F . n 
F 2 217 ILE 217 219 219 ILE ILE F . n 
F 2 218 ARG 218 220 220 ARG ARG F . n 
F 2 219 PRO 219 221 221 PRO PRO F . n 
F 2 220 LYS 220 222 222 LYS LYS F . n 
F 2 221 VAL 221 223 223 VAL VAL F . n 
F 2 222 ARG 222 224 224 ARG ARG F . n 
F 2 223 ASP 223 225 225 ASP ASP F . n 
F 2 224 ARG 224 226 226 ARG ARG F . n 
F 2 225 GLU 225 227 227 GLU GLU F . n 
F 2 226 GLY 226 228 228 GLY GLY F . n 
F 2 227 ARG 227 229 229 ARG ARG F . n 
F 2 228 MET 228 230 230 MET MET F . n 
F 2 229 ASN 229 231 231 ASN ASN F . n 
F 2 230 TYR 230 232 232 TYR TYR F . n 
F 2 231 TYR 231 233 233 TYR TYR F . n 
F 2 232 TRP 232 234 234 TRP TRP F . n 
F 2 233 THR 233 235 235 THR THR F . n 
F 2 234 LEU 234 236 236 LEU LEU F . n 
F 2 235 VAL 235 237 237 VAL VAL F . n 
F 2 236 GLU 236 238 238 GLU GLU F . n 
F 2 237 PRO 237 239 239 PRO PRO F . n 
F 2 238 GLY 238 240 240 GLY GLY F . n 
F 2 239 ASP 239 241 241 ASP ASP F . n 
F 2 240 LYS 240 242 242 LYS LYS F . n 
F 2 241 ILE 241 243 243 ILE ILE F . n 
F 2 242 THR 242 244 244 THR THR F . n 
F 2 243 PHE 243 245 245 PHE PHE F . n 
F 2 244 GLU 244 246 246 GLU GLU F . n 
F 2 245 ALA 245 247 247 ALA ALA F . n 
F 2 246 THR 246 248 248 THR THR F . n 
F 2 247 GLY 247 249 249 GLY GLY F . n 
F 2 248 ASN 248 250 250 ASN ASN F . n 
F 2 249 LEU 249 251 251 LEU LEU F . n 
F 2 250 VAL 250 252 252 VAL VAL F . n 
F 2 251 VAL 251 253 253 VAL VAL F . n 
F 2 252 PRO 252 254 254 PRO PRO F . n 
F 2 253 ARG 253 255 255 ARG ARG F . n 
F 2 254 TYR 254 256 256 TYR TYR F . n 
F 2 255 ALA 255 257 257 ALA ALA F . n 
F 2 256 PHE 256 258 258 PHE PHE F . n 
F 2 257 ALA 257 259 259 ALA ALA F . n 
F 2 258 MET 258 260 260 MET MET F . n 
F 2 259 GLU 259 261 261 GLU GLU F . n 
F 2 260 ARG 260 262 262 ARG ARG F . n 
F 2 261 ASN 261 263 263 ASN ASN F . n 
F 2 262 ALA 262 264 264 ALA ALA F . n 
F 2 263 GLY 263 265 265 GLY GLY F . n 
F 2 264 SER 264 266 266 SER SER F . n 
F 2 265 GLY 265 266 266 GLY GLY F A n 
F 2 266 ILE 266 267 267 ILE ILE F . n 
F 2 267 ILE 267 268 268 ILE ILE F . n 
F 2 268 ILE 268 269 269 ILE ILE F . n 
F 2 269 SER 269 270 270 SER SER F . n 
F 2 270 ASP 270 271 271 ASP ASP F . n 
F 2 271 THR 271 272 272 THR THR F . n 
F 2 272 PRO 272 273 273 PRO PRO F . n 
F 2 273 VAL 273 274 274 VAL VAL F . n 
F 2 274 HIS 274 275 275 HIS HIS F . n 
F 2 275 ASP 275 276 276 ASP ASP F . n 
F 2 276 CYS 276 277 277 CYS CYS F . n 
F 2 277 ASN 277 278 278 ASN ASN F . n 
F 2 278 THR 278 279 279 THR THR F . n 
F 2 279 THR 279 280 280 THR THR F . n 
F 2 280 CYS 280 281 281 CYS CYS F . n 
F 2 281 GLN 281 282 282 GLN GLN F . n 
F 2 282 THR 282 283 283 THR THR F . n 
F 2 283 PRO 283 284 284 PRO PRO F . n 
F 2 284 LYS 284 285 285 LYS LYS F . n 
F 2 285 GLY 285 286 286 GLY GLY F . n 
F 2 286 ALA 286 287 287 ALA ALA F . n 
F 2 287 ILE 287 288 288 ILE ILE F . n 
F 2 288 ASN 288 289 289 ASN ASN F . n 
F 2 289 THR 289 290 290 THR THR F . n 
F 2 290 SER 290 291 291 SER SER F . n 
F 2 291 LEU 291 292 292 LEU LEU F . n 
F 2 292 PRO 292 293 293 PRO PRO F . n 
F 2 293 PHE 293 294 294 PHE PHE F . n 
F 2 294 GLN 294 295 295 GLN GLN F . n 
F 2 295 ASN 295 296 296 ASN ASN F . n 
F 2 296 ILE 296 297 297 ILE ILE F . n 
F 2 297 HIS 297 298 298 HIS HIS F . n 
F 2 298 PRO 298 299 299 PRO PRO F . n 
F 2 299 ILE 299 300 300 ILE ILE F . n 
F 2 300 THR 300 301 301 THR THR F . n 
F 2 301 ILE 301 302 302 ILE ILE F . n 
F 2 302 GLY 302 303 303 GLY GLY F . n 
F 2 303 LYS 303 304 304 LYS LYS F . n 
F 2 304 CYS 304 305 305 CYS CYS F . n 
F 2 305 PRO 305 306 306 PRO PRO F . n 
F 2 306 LYS 306 307 307 LYS LYS F . n 
F 2 307 TYR 307 308 308 TYR TYR F . n 
F 2 308 VAL 308 309 309 VAL VAL F . n 
F 2 309 LYS 309 310 310 LYS LYS F . n 
F 2 310 SER 310 311 311 SER SER F . n 
F 2 311 THR 311 312 312 THR THR F . n 
F 2 312 LYS 312 313 313 LYS LYS F . n 
F 2 313 LEU 313 314 314 LEU LEU F . n 
F 2 314 ARG 314 315 315 ARG ARG F . n 
F 2 315 LEU 315 316 316 LEU LEU F . n 
F 2 316 ALA 316 317 317 ALA ALA F . n 
F 2 317 THR 317 318 318 THR THR F . n 
F 2 318 GLY 318 319 319 GLY GLY F . n 
F 2 319 LEU 319 320 320 LEU LEU F . n 
F 2 320 ARG 320 321 321 ARG ARG F . n 
F 2 321 ASN 321 322 322 ASN ASN F . n 
F 2 322 ILE 322 323 ?   ?   ?   F . n 
F 2 323 PRO 323 324 ?   ?   ?   F . n 
F 2 324 SER 324 325 ?   ?   ?   F . n 
F 2 325 ILE 325 326 ?   ?   ?   F . n 
F 2 326 GLN 326 327 ?   ?   ?   F . n 
F 2 327 SER 327 328 ?   ?   ?   F . n 
F 2 328 ARG 328 329 ?   ?   ?   F . n 
G 3 1   GLU 1   1   1   GLU GLU H . n 
G 3 2   VAL 2   2   2   VAL VAL H . n 
G 3 3   GLN 3   3   3   GLN GLN H . n 
G 3 4   LEU 4   4   4   LEU LEU H . n 
G 3 5   VAL 5   5   5   VAL VAL H . n 
G 3 6   GLN 6   6   6   GLN GLN H . n 
G 3 7   SER 7   7   7   SER SER H . n 
G 3 8   GLY 8   8   8   GLY GLY H . n 
G 3 9   ALA 9   9   9   ALA ALA H . n 
G 3 10  GLU 10  10  10  GLU GLU H . n 
G 3 11  VAL 11  11  11  VAL VAL H . n 
G 3 12  LYS 12  12  12  LYS LYS H . n 
G 3 13  LYS 13  13  13  LYS LYS H . n 
G 3 14  PRO 14  14  14  PRO PRO H . n 
G 3 15  GLY 15  15  15  GLY GLY H . n 
G 3 16  GLU 16  16  16  GLU GLU H . n 
G 3 17  SER 17  17  17  SER SER H . n 
G 3 18  LEU 18  18  18  LEU LEU H . n 
G 3 19  THR 19  19  19  THR THR H . n 
G 3 20  ILE 20  20  20  ILE ILE H . n 
G 3 21  SER 21  21  21  SER SER H . n 
G 3 22  CYS 22  22  22  CYS CYS H . n 
G 3 23  LYS 23  23  23  LYS LYS H . n 
G 3 24  GLY 24  24  24  GLY GLY H . n 
G 3 25  SER 25  25  25  SER SER H . n 
G 3 26  GLY 26  26  26  GLY GLY H . n 
G 3 27  TYR 27  27  27  TYR TYR H . n 
G 3 28  SER 28  28  28  SER SER H . n 
G 3 29  PHE 29  29  29  PHE PHE H . n 
G 3 30  SER 30  30  30  SER SER H . n 
G 3 31  SER 31  31  31  SER SER H . n 
G 3 32  TYR 32  32  32  TYR TYR H . n 
G 3 33  TRP 33  33  33  TRP TRP H . n 
G 3 34  ILE 34  34  34  ILE ILE H . n 
G 3 35  GLY 35  35  35  GLY GLY H . n 
G 3 36  TRP 36  36  36  TRP TRP H . n 
G 3 37  VAL 37  37  37  VAL VAL H . n 
G 3 38  ARG 38  38  38  ARG ARG H . n 
G 3 39  ARG 39  39  39  ARG ARG H . n 
G 3 40  MET 40  40  40  MET MET H . n 
G 3 41  PRO 41  41  41  PRO PRO H . n 
G 3 42  GLY 42  42  42  GLY GLY H . n 
G 3 43  LYS 43  43  43  LYS LYS H . n 
G 3 44  GLY 44  44  44  GLY GLY H . n 
G 3 45  LEU 45  45  45  LEU LEU H . n 
G 3 46  GLU 46  46  46  GLU GLU H . n 
G 3 47  TRP 47  47  47  TRP TRP H . n 
G 3 48  MET 48  48  48  MET MET H . n 
G 3 49  GLY 49  49  49  GLY GLY H . n 
G 3 50  ILE 50  50  50  ILE ILE H . n 
G 3 51  ILE 51  51  51  ILE ILE H . n 
G 3 52  ASN 52  52  52  ASN ASN H . n 
G 3 53  PRO 53  53  53  PRO PRO H . n 
G 3 54  ARG 54  54  54  ARG ARG H . n 
G 3 55  ASP 55  55  55  ASP ASP H . n 
G 3 56  SER 56  56  56  SER SER H . n 
G 3 57  ASP 57  57  57  ASP ASP H . n 
G 3 58  THR 58  58  58  THR THR H . n 
G 3 59  ARG 59  59  59  ARG ARG H . n 
G 3 60  TYR 60  60  60  TYR TYR H . n 
G 3 61  SER 61  61  61  SER SER H . n 
G 3 62  PRO 62  62  62  PRO PRO H . n 
G 3 63  SER 63  63  63  SER SER H . n 
G 3 64  PHE 64  64  64  PHE PHE H . n 
G 3 65  GLN 65  65  65  GLN GLN H . n 
G 3 66  GLY 66  66  66  GLY GLY H . n 
G 3 67  GLN 67  67  67  GLN GLN H . n 
G 3 68  VAL 68  68  68  VAL VAL H . n 
G 3 69  THR 69  69  69  THR THR H . n 
G 3 70  ILE 70  70  70  ILE ILE H . n 
G 3 71  SER 71  71  71  SER SER H . n 
G 3 72  ALA 72  72  72  ALA ALA H . n 
G 3 73  ASP 73  73  73  ASP ASP H . n 
G 3 74  LYS 74  74  74  LYS LYS H . n 
G 3 75  SER 75  75  75  SER SER H . n 
G 3 76  ILE 76  76  76  ILE ILE H . n 
G 3 77  SER 77  77  77  SER SER H . n 
G 3 78  THR 78  78  78  THR THR H . n 
G 3 79  ALA 79  79  79  ALA ALA H . n 
G 3 80  TYR 80  80  80  TYR TYR H . n 
G 3 81  LEU 81  81  81  LEU LEU H . n 
G 3 82  GLN 82  82  82  GLN GLN H . n 
G 3 83  TRP 83  83  83  TRP TRP H . n 
G 3 84  SER 84  84  84  SER SER H . n 
G 3 85  SER 85  85  85  SER SER H . n 
G 3 86  LEU 86  86  86  LEU LEU H . n 
G 3 87  LYS 87  87  87  LYS LYS H . n 
G 3 88  ALA 88  88  88  ALA ALA H . n 
G 3 89  SER 89  89  89  SER SER H . n 
G 3 90  ASP 90  90  90  ASP ASP H . n 
G 3 91  THR 91  91  91  THR THR H . n 
G 3 92  ALA 92  92  92  ALA ALA H . n 
G 3 93  MET 93  93  93  MET MET H . n 
G 3 94  TYR 94  94  94  TYR TYR H . n 
G 3 95  TYR 95  95  95  TYR TYR H . n 
G 3 96  CYS 96  96  96  CYS CYS H . n 
G 3 97  ALA 97  97  97  ALA ALA H . n 
G 3 98  ARG 98  98  98  ARG ARG H . n 
G 3 99  VAL 99  99  99  VAL VAL H . n 
G 3 100 VAL 100 100 100 VAL VAL H . n 
G 3 101 ALA 101 101 101 ALA ALA H . n 
G 3 102 ASP 102 102 102 ASP ASP H . n 
G 3 103 ARG 103 103 103 ARG ARG H . n 
G 3 104 GLU 104 104 104 GLU GLU H . n 
G 3 105 GLY 105 105 105 GLY GLY H . n 
G 3 106 PHE 106 106 106 PHE PHE H . n 
G 3 107 GLY 107 107 107 GLY GLY H . n 
G 3 108 TYR 108 108 108 TYR TYR H . n 
G 3 109 TYR 109 109 109 TYR TYR H . n 
G 3 110 TYR 110 110 110 TYR TYR H . n 
G 3 111 GLY 111 111 111 GLY GLY H . n 
G 3 112 MET 112 112 112 MET MET H . n 
G 3 113 ASP 113 113 113 ASP ASP H . n 
G 3 114 VAL 114 114 114 VAL VAL H . n 
G 3 115 TRP 115 115 115 TRP TRP H . n 
G 3 116 GLY 116 116 116 GLY GLY H . n 
G 3 117 GLN 117 117 117 GLN GLN H . n 
G 3 118 GLY 118 118 118 GLY GLY H . n 
G 3 119 THR 119 119 119 THR THR H . n 
G 3 120 THR 120 120 120 THR THR H . n 
G 3 121 VAL 121 121 121 VAL VAL H . n 
G 3 122 THR 122 122 122 THR THR H . n 
G 3 123 VAL 123 123 123 VAL VAL H . n 
G 3 124 SER 124 124 124 SER SER H . n 
G 3 125 SER 125 125 125 SER SER H . n 
G 3 126 ALA 126 126 126 ALA ALA H . n 
G 3 127 SER 127 127 127 SER SER H . n 
G 3 128 THR 128 128 128 THR THR H . n 
G 3 129 LYS 129 129 129 LYS LYS H . n 
G 3 130 GLY 130 130 130 GLY GLY H . n 
G 3 131 PRO 131 131 131 PRO PRO H . n 
G 3 132 SER 132 132 132 SER SER H . n 
G 3 133 VAL 133 133 133 VAL VAL H . n 
G 3 134 PHE 134 134 134 PHE PHE H . n 
G 3 135 PRO 135 135 135 PRO PRO H . n 
G 3 136 LEU 136 136 136 LEU LEU H . n 
G 3 137 ALA 137 137 137 ALA ALA H . n 
G 3 138 PRO 138 138 138 PRO PRO H . n 
G 3 139 SER 139 139 ?   ?   ?   H . n 
G 3 140 SER 140 140 ?   ?   ?   H . n 
G 3 141 LYS 141 141 ?   ?   ?   H . n 
G 3 142 SER 142 142 ?   ?   ?   H . n 
G 3 143 THR 143 143 ?   ?   ?   H . n 
G 3 144 SER 144 144 ?   ?   ?   H . n 
G 3 145 GLY 145 145 ?   ?   ?   H . n 
G 3 146 GLY 146 146 ?   ?   ?   H . n 
G 3 147 THR 147 147 ?   ?   ?   H . n 
G 3 148 ALA 148 148 148 ALA ALA H . n 
G 3 149 ALA 149 149 149 ALA ALA H . n 
G 3 150 LEU 150 150 150 LEU LEU H . n 
G 3 151 GLY 151 151 151 GLY GLY H . n 
G 3 152 CYS 152 152 152 CYS CYS H . n 
G 3 153 LEU 153 153 153 LEU LEU H . n 
G 3 154 VAL 154 154 154 VAL VAL H . n 
G 3 155 LYS 155 155 155 LYS LYS H . n 
G 3 156 ASP 156 156 156 ASP ASP H . n 
G 3 157 TYR 157 157 157 TYR TYR H . n 
G 3 158 PHE 158 158 158 PHE PHE H . n 
G 3 159 PRO 159 159 159 PRO PRO H . n 
G 3 160 GLU 160 160 160 GLU GLU H . n 
G 3 161 PRO 161 161 161 PRO PRO H . n 
G 3 162 VAL 162 162 162 VAL VAL H . n 
G 3 163 THR 163 163 163 THR THR H . n 
G 3 164 VAL 164 164 164 VAL VAL H . n 
G 3 165 SER 165 165 165 SER SER H . n 
G 3 166 TRP 166 166 166 TRP TRP H . n 
G 3 167 ASN 167 167 167 ASN ASN H . n 
G 3 168 SER 168 168 168 SER SER H . n 
G 3 169 GLY 169 169 169 GLY GLY H . n 
G 3 170 ALA 170 170 170 ALA ALA H . n 
G 3 171 LEU 171 171 171 LEU LEU H . n 
G 3 172 THR 172 172 172 THR THR H . n 
G 3 173 SER 173 173 173 SER SER H . n 
G 3 174 GLY 174 174 174 GLY GLY H . n 
G 3 175 VAL 175 175 175 VAL VAL H . n 
G 3 176 HIS 176 176 176 HIS HIS H . n 
G 3 177 THR 177 177 177 THR THR H . n 
G 3 178 PHE 178 178 178 PHE PHE H . n 
G 3 179 PRO 179 179 179 PRO PRO H . n 
G 3 180 ALA 180 180 180 ALA ALA H . n 
G 3 181 VAL 181 181 181 VAL VAL H . n 
G 3 182 LEU 182 182 182 LEU LEU H . n 
G 3 183 GLN 183 183 183 GLN GLN H . n 
G 3 184 SER 184 184 184 SER SER H . n 
G 3 185 SER 185 185 185 SER SER H . n 
G 3 186 GLY 186 186 186 GLY GLY H . n 
G 3 187 LEU 187 187 187 LEU LEU H . n 
G 3 188 TYR 188 188 188 TYR TYR H . n 
G 3 189 SER 189 189 189 SER SER H . n 
G 3 190 LEU 190 190 190 LEU LEU H . n 
G 3 191 SER 191 191 191 SER SER H . n 
G 3 192 SER 192 192 192 SER SER H . n 
G 3 193 VAL 193 193 193 VAL VAL H . n 
G 3 194 VAL 194 194 194 VAL VAL H . n 
G 3 195 THR 195 195 195 THR THR H . n 
G 3 196 VAL 196 196 196 VAL VAL H . n 
G 3 197 PRO 197 197 197 PRO PRO H . n 
G 3 198 SER 198 198 198 SER SER H . n 
G 3 199 SER 199 199 199 SER SER H . n 
G 3 200 SER 200 200 200 SER SER H . n 
G 3 201 LEU 201 201 201 LEU LEU H . n 
G 3 202 GLY 202 202 202 GLY GLY H . n 
G 3 203 THR 203 203 203 THR THR H . n 
G 3 204 GLN 204 204 204 GLN GLN H . n 
G 3 205 THR 205 205 205 THR THR H . n 
G 3 206 TYR 206 206 206 TYR TYR H . n 
G 3 207 ILE 207 207 207 ILE ILE H . n 
G 3 208 CYS 208 208 208 CYS CYS H . n 
G 3 209 ASN 209 209 209 ASN ASN H . n 
G 3 210 VAL 210 210 210 VAL VAL H . n 
G 3 211 ASN 211 211 211 ASN ASN H . n 
G 3 212 HIS 212 212 212 HIS HIS H . n 
G 3 213 LYS 213 213 213 LYS LYS H . n 
G 3 214 PRO 214 214 214 PRO PRO H . n 
G 3 215 SER 215 215 215 SER SER H . n 
G 3 216 ASN 216 216 216 ASN ASN H . n 
G 3 217 THR 217 217 217 THR THR H . n 
G 3 218 LYS 218 218 218 LYS LYS H . n 
G 3 219 VAL 219 219 219 VAL VAL H . n 
G 3 220 ASP 220 220 220 ASP ASP H . n 
G 3 221 LYS 221 221 221 LYS LYS H . n 
G 3 222 ARG 222 222 222 ARG ARG H . n 
G 3 223 VAL 223 223 223 VAL VAL H . n 
G 3 224 GLU 224 224 224 GLU GLU H . n 
G 3 225 PRO 225 225 225 PRO PRO H . n 
G 3 226 LYS 226 226 ?   ?   ?   H . n 
G 3 227 SER 227 227 ?   ?   ?   H . n 
G 3 228 CYS 228 228 ?   ?   ?   H . n 
G 3 229 ASP 229 229 ?   ?   ?   H . n 
G 3 230 LYS 230 230 ?   ?   ?   H . n 
H 4 1   GLU 1   1   1   GLU GLU L . n 
H 4 2   ILE 2   2   2   ILE ILE L . n 
H 4 3   VAL 3   3   3   VAL VAL L . n 
H 4 4   LEU 4   4   4   LEU LEU L . n 
H 4 5   THR 5   5   5   THR THR L . n 
H 4 6   GLN 6   6   6   GLN GLN L . n 
H 4 7   SER 7   7   7   SER SER L . n 
H 4 8   PRO 8   8   8   PRO PRO L . n 
H 4 9   GLY 9   9   9   GLY GLY L . n 
H 4 10  THR 10  10  10  THR THR L . n 
H 4 11  LEU 11  11  11  LEU LEU L . n 
H 4 12  SER 12  12  12  SER SER L . n 
H 4 13  LEU 13  13  13  LEU LEU L . n 
H 4 14  SER 14  14  14  SER SER L . n 
H 4 15  PRO 15  15  15  PRO PRO L . n 
H 4 16  GLY 16  16  16  GLY GLY L . n 
H 4 17  GLU 17  17  17  GLU GLU L . n 
H 4 18  GLY 18  18  18  GLY GLY L . n 
H 4 19  ALA 19  19  19  ALA ALA L . n 
H 4 20  THR 20  20  20  THR THR L . n 
H 4 21  LEU 21  21  21  LEU LEU L . n 
H 4 22  SER 22  22  22  SER SER L . n 
H 4 23  CYS 23  23  23  CYS CYS L . n 
H 4 24  ARG 24  24  24  ARG ARG L . n 
H 4 25  ALA 25  25  25  ALA ALA L . n 
H 4 26  SER 26  26  26  SER SER L . n 
H 4 27  GLN 27  27  27  GLN GLN L . n 
H 4 28  SER 28  28  28  SER SER L . n 
H 4 29  VAL 29  29  29  VAL VAL L . n 
H 4 30  ASP 30  30  30  ASP ASP L . n 
H 4 31  SER 31  31  31  SER SER L . n 
H 4 32  SER 32  32  32  SER SER L . n 
H 4 33  SER 33  33  33  SER SER L . n 
H 4 34  LEU 34  34  34  LEU LEU L . n 
H 4 35  ALA 35  35  35  ALA ALA L . n 
H 4 36  TRP 36  36  36  TRP TRP L . n 
H 4 37  TYR 37  37  37  TYR TYR L . n 
H 4 38  GLN 38  38  38  GLN GLN L . n 
H 4 39  GLN 39  39  39  GLN GLN L . n 
H 4 40  LYS 40  40  40  LYS LYS L . n 
H 4 41  PRO 41  41  41  PRO PRO L . n 
H 4 42  GLY 42  42  42  GLY GLY L . n 
H 4 43  GLN 43  43  43  GLN GLN L . n 
H 4 44  ALA 44  44  44  ALA ALA L . n 
H 4 45  PRO 45  45  45  PRO PRO L . n 
H 4 46  ARG 46  46  46  ARG ARG L . n 
H 4 47  LEU 47  47  47  LEU LEU L . n 
H 4 48  LEU 48  48  48  LEU LEU L . n 
H 4 49  ILE 49  49  49  ILE ILE L . n 
H 4 50  PHE 50  50  50  PHE PHE L . n 
H 4 51  ALA 51  51  51  ALA ALA L . n 
H 4 52  GLY 52  52  52  GLY GLY L . n 
H 4 53  SER 53  53  53  SER SER L . n 
H 4 54  SER 54  54  54  SER SER L . n 
H 4 55  ARG 55  55  55  ARG ARG L . n 
H 4 56  ALA 56  56  56  ALA ALA L . n 
H 4 57  THR 57  57  57  THR THR L . n 
H 4 58  GLY 58  58  58  GLY GLY L . n 
H 4 59  ILE 59  59  59  ILE ILE L . n 
H 4 60  PRO 60  60  60  PRO PRO L . n 
H 4 61  ASP 61  61  61  ASP ASP L . n 
H 4 62  ARG 62  62  62  ARG ARG L . n 
H 4 63  PHE 63  63  63  PHE PHE L . n 
H 4 64  SER 64  64  64  SER SER L . n 
H 4 65  GLY 65  65  65  GLY GLY L . n 
H 4 66  LYS 66  66  66  LYS LYS L . n 
H 4 67  THR 67  67  67  THR THR L . n 
H 4 68  SER 68  68  68  SER SER L . n 
H 4 69  GLY 69  69  69  GLY GLY L . n 
H 4 70  THR 70  70  70  THR THR L . n 
H 4 71  ASP 71  71  71  ASP ASP L . n 
H 4 72  PHE 72  72  72  PHE PHE L . n 
H 4 73  THR 73  73  73  THR THR L . n 
H 4 74  LEU 74  74  74  LEU LEU L . n 
H 4 75  THR 75  75  75  THR THR L . n 
H 4 76  ILE 76  76  76  ILE ILE L . n 
H 4 77  SER 77  77  77  SER SER L . n 
H 4 78  ARG 78  78  78  ARG ARG L . n 
H 4 79  LEU 79  79  79  LEU LEU L . n 
H 4 80  GLU 80  80  80  GLU GLU L . n 
H 4 81  PRO 81  81  81  PRO PRO L . n 
H 4 82  GLU 82  82  82  GLU GLU L . n 
H 4 83  ASP 83  83  83  ASP ASP L . n 
H 4 84  PHE 84  84  84  PHE PHE L . n 
H 4 85  ALA 85  85  85  ALA ALA L . n 
H 4 86  VAL 86  86  86  VAL VAL L . n 
H 4 87  TYR 87  87  87  TYR TYR L . n 
H 4 88  TYR 88  88  88  TYR TYR L . n 
H 4 89  CYS 89  89  89  CYS CYS L . n 
H 4 90  GLN 90  90  90  GLN GLN L . n 
H 4 91  GLN 91  91  91  GLN GLN L . n 
H 4 92  CYS 92  92  92  CYS CYS L . n 
H 4 93  GLY 93  93  93  GLY GLY L . n 
H 4 94  ASN 94  94  94  ASN ASN L . n 
H 4 95  SER 95  95  95  SER SER L . n 
H 4 96  PRO 96  96  96  PRO PRO L . n 
H 4 97  TRP 97  97  97  TRP TRP L . n 
H 4 98  THR 98  98  98  THR THR L . n 
H 4 99  PHE 99  99  99  PHE PHE L . n 
H 4 100 GLY 100 100 100 GLY GLY L . n 
H 4 101 GLN 101 101 101 GLN GLN L . n 
H 4 102 GLY 102 102 102 GLY GLY L . n 
H 4 103 THR 103 103 103 THR THR L . n 
H 4 104 LYS 104 104 104 LYS LYS L . n 
H 4 105 VAL 105 105 105 VAL VAL L . n 
H 4 106 GLU 106 106 106 GLU GLU L . n 
H 4 107 ILE 107 107 107 ILE ILE L . n 
H 4 108 LYS 108 108 108 LYS LYS L . n 
H 4 109 ARG 109 109 109 ARG ARG L . n 
H 4 110 THR 110 110 110 THR THR L . n 
H 4 111 VAL 111 111 111 VAL VAL L . n 
H 4 112 ALA 112 112 112 ALA ALA L . n 
H 4 113 ALA 113 113 113 ALA ALA L . n 
H 4 114 PRO 114 114 114 PRO PRO L . n 
H 4 115 SER 115 115 115 SER SER L . n 
H 4 116 VAL 116 116 116 VAL VAL L . n 
H 4 117 PHE 117 117 117 PHE PHE L . n 
H 4 118 ILE 118 118 118 ILE ILE L . n 
H 4 119 PHE 119 119 119 PHE PHE L . n 
H 4 120 PRO 120 120 120 PRO PRO L . n 
H 4 121 PRO 121 121 121 PRO PRO L . n 
H 4 122 SER 122 122 122 SER SER L . n 
H 4 123 ASP 123 123 123 ASP ASP L . n 
H 4 124 GLU 124 124 124 GLU GLU L . n 
H 4 125 GLN 125 125 125 GLN GLN L . n 
H 4 126 LEU 126 126 126 LEU LEU L . n 
H 4 127 LYS 127 127 127 LYS LYS L . n 
H 4 128 SER 128 128 128 SER SER L . n 
H 4 129 GLY 129 129 129 GLY GLY L . n 
H 4 130 THR 130 130 130 THR THR L . n 
H 4 131 ALA 131 131 131 ALA ALA L . n 
H 4 132 SER 132 132 132 SER SER L . n 
H 4 133 VAL 133 133 133 VAL VAL L . n 
H 4 134 VAL 134 134 134 VAL VAL L . n 
H 4 135 CYS 135 135 135 CYS CYS L . n 
H 4 136 LEU 136 136 136 LEU LEU L . n 
H 4 137 LEU 137 137 137 LEU LEU L . n 
H 4 138 ASN 138 138 138 ASN ASN L . n 
H 4 139 ASN 139 139 139 ASN ASN L . n 
H 4 140 PHE 140 140 140 PHE PHE L . n 
H 4 141 TYR 141 141 141 TYR TYR L . n 
H 4 142 PRO 142 142 142 PRO PRO L . n 
H 4 143 ARG 143 143 143 ARG ARG L . n 
H 4 144 GLU 144 144 144 GLU GLU L . n 
H 4 145 ALA 145 145 145 ALA ALA L . n 
H 4 146 LYS 146 146 146 LYS LYS L . n 
H 4 147 VAL 147 147 147 VAL VAL L . n 
H 4 148 GLN 148 148 148 GLN GLN L . n 
H 4 149 TRP 149 149 149 TRP TRP L . n 
H 4 150 LYS 150 150 150 LYS LYS L . n 
H 4 151 VAL 151 151 151 VAL VAL L . n 
H 4 152 ASP 152 152 152 ASP ASP L . n 
H 4 153 ASN 153 153 153 ASN ASN L . n 
H 4 154 ALA 154 154 154 ALA ALA L . n 
H 4 155 LEU 155 155 155 LEU LEU L . n 
H 4 156 GLN 156 156 156 GLN GLN L . n 
H 4 157 SER 157 157 157 SER SER L . n 
H 4 158 GLY 158 158 158 GLY GLY L . n 
H 4 159 ASN 159 159 159 ASN ASN L . n 
H 4 160 SER 160 160 160 SER SER L . n 
H 4 161 GLN 161 161 161 GLN GLN L . n 
H 4 162 GLU 162 162 162 GLU GLU L . n 
H 4 163 SER 163 163 163 SER SER L . n 
H 4 164 VAL 164 164 164 VAL VAL L . n 
H 4 165 THR 165 165 165 THR THR L . n 
H 4 166 GLU 166 166 166 GLU GLU L . n 
H 4 167 GLN 167 167 167 GLN GLN L . n 
H 4 168 ASP 168 168 168 ASP ASP L . n 
H 4 169 SER 169 169 169 SER SER L . n 
H 4 170 LYS 170 170 170 LYS LYS L . n 
H 4 171 ASP 171 171 171 ASP ASP L . n 
H 4 172 SER 172 172 172 SER SER L . n 
H 4 173 THR 173 173 173 THR THR L . n 
H 4 174 TYR 174 174 174 TYR TYR L . n 
H 4 175 SER 175 175 175 SER SER L . n 
H 4 176 LEU 176 176 176 LEU LEU L . n 
H 4 177 SER 177 177 177 SER SER L . n 
H 4 178 SER 178 178 178 SER SER L . n 
H 4 179 THR 179 179 179 THR THR L . n 
H 4 180 LEU 180 180 180 LEU LEU L . n 
H 4 181 THR 181 181 181 THR THR L . n 
H 4 182 LEU 182 182 182 LEU LEU L . n 
H 4 183 SER 183 183 183 SER SER L . n 
H 4 184 LYS 184 184 184 LYS LYS L . n 
H 4 185 ALA 185 185 185 ALA ALA L . n 
H 4 186 ASP 186 186 186 ASP ASP L . n 
H 4 187 TYR 187 187 187 TYR TYR L . n 
H 4 188 GLU 188 188 188 GLU GLU L . n 
H 4 189 LYS 189 189 189 LYS LYS L . n 
H 4 190 HIS 190 190 190 HIS HIS L . n 
H 4 191 LYS 191 191 191 LYS LYS L . n 
H 4 192 VAL 192 192 192 VAL VAL L . n 
H 4 193 TYR 193 193 193 TYR TYR L . n 
H 4 194 ALA 194 194 194 ALA ALA L . n 
H 4 195 CYS 195 195 195 CYS CYS L . n 
H 4 196 GLU 196 196 196 GLU GLU L . n 
H 4 197 VAL 197 197 197 VAL VAL L . n 
H 4 198 THR 198 198 198 THR THR L . n 
H 4 199 HIS 199 199 199 HIS HIS L . n 
H 4 200 GLN 200 200 200 GLN GLN L . n 
H 4 201 GLY 201 201 201 GLY GLY L . n 
H 4 202 LEU 202 202 202 LEU LEU L . n 
H 4 203 SER 203 203 203 SER SER L . n 
H 4 204 SER 204 204 204 SER SER L . n 
H 4 205 PRO 205 205 205 PRO PRO L . n 
H 4 206 VAL 206 206 206 VAL VAL L . n 
H 4 207 THR 207 207 207 THR THR L . n 
H 4 208 LYS 208 208 208 LYS LYS L . n 
H 4 209 SER 209 209 209 SER SER L . n 
H 4 210 PHE 210 210 210 PHE PHE L . n 
H 4 211 ASN 211 211 211 ASN ASN L . n 
H 4 212 ARG 212 212 212 ARG ARG L . n 
H 4 213 GLY 213 213 213 GLY GLY L . n 
H 4 214 GLU 214 214 214 GLU GLU L . n 
H 4 215 CYS 215 215 215 CYS CYS L . n 
# 
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 
I 5 NAG 1 401 4 NAG NAG B . 
J 5 NAG 1 402 7 NAG NAG B . 
K 5 NAG 1 401 1 NAG NAG F . 
L 5 NAG 1 402 2 NAG NAG F . 
M 5 NAG 1 403 3 NAG NAG F . 
N 5 NAG 1 404 5 NAG NAG F . 
O 5 NAG 1 405 6 NAG NAG F . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? tetrameric 4 
2 author_defined_assembly ? tetrameric 4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,G,I,J           
2 1 C,D,E,F,H,K,L,M,N,O 
# 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-11-09 
2 'Structure model' 1 1 2016-11-23 
3 'Structure model' 1 2 2016-12-14 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined -41.6216 -27.0422  -39.6118 -0.0838 0.1014  0.0000  0.1165  -0.0816 -0.0685 0.2726  0.2359  
-0.4420 -0.1636 -0.4820 -0.7443 0.0072  0.0199  -0.0001 -0.0413 0.0106  -0.0447 0.0008  0.0445  -0.0178 
'X-RAY DIFFRACTION' 2  ? refined -29.8398 -30.2459  -17.8292 0.1530  -0.2413 0.1014  0.3915  -0.1384 0.0328  0.7615  1.2361  
-1.9864 1.7796  -4.5833 -2.0861 0.0029  0.0287  -0.1114 -0.3164 -0.0777 -0.0548 -0.1250 0.1363  0.0747  
'X-RAY DIFFRACTION' 3  ? refined -30.8688 -53.3897  1.3523   -0.0466 0.1969  0.1387  0.2498  0.1274  0.0820  0.3666  0.6067  
-0.7675 -0.1327 -1.0970 -1.1491 0.0018  0.0282  0.0304  -0.0136 -0.0189 0.0049  -0.0014 0.0015  0.0171  
'X-RAY DIFFRACTION' 4  ? refined -36.2516 -41.5497  -7.9388  -0.1678 -0.3444 -0.0118 0.2612  0.0015  -0.2376 -0.9067 1.6062  
-0.6578 2.3026  1.0271  -1.5692 0.0544  -0.0949 -0.1391 -0.0551 -0.0065 0.1791  -0.0599 -0.1507 -0.0479 
'X-RAY DIFFRACTION' 5  ? refined -41.6996 -26.6476  -19.3325 0.1743  0.0476  0.1381  0.3971  -0.2858 0.1748  0.1413  1.4047  
0.2372  0.4076  1.7619  -0.1999 0.0046  0.0292  -0.0053 -0.0051 0.0263  0.1130  -0.0103 0.0711  -0.0309 
'X-RAY DIFFRACTION' 6  ? refined -45.3615 -11.5923  -28.2806 0.0811  0.0591  -0.0700 0.4032  -0.1666 -0.1296 -0.2047 0.4881  
1.5603  -0.2413 1.2532  -1.2761 -0.0214 0.1332  -0.0971 0.0407  -0.0432 -0.0368 -0.1339 -0.0402 0.0646  
'X-RAY DIFFRACTION' 7  ? refined -39.5460 -8.4021   -39.6547 0.0220  -0.0989 0.1683  0.0435  -0.0708 0.2692  0.1164  1.5084  
-0.4578 1.2287  0.5022  -1.5424 0.0080  -0.0310 0.0228  -0.0409 0.0147  0.0407  -0.0253 -0.0046 -0.0226 
'X-RAY DIFFRACTION' 8  ? refined -54.5454 2.4502    -40.3108 0.2086  -0.0971 -0.0060 0.1668  -0.1159 0.0027  -0.0251 1.5329  
-0.9225 -1.0178 1.5633  -2.5811 -0.0100 -0.0232 0.0389  0.0084  0.0670  -0.1066 0.0694  0.1026  -0.0571 
'X-RAY DIFFRACTION' 9  ? refined -41.8242 -39.3084  -23.3685 0.0503  0.1717  -0.0150 0.4063  -0.1533 0.1640  3.8786  3.6440  
0.3791  -2.3229 6.8710  -3.5986 -0.0752 0.2010  0.1611  0.1573  0.1887  0.1850  -0.0499 0.0037  -0.1135 
'X-RAY DIFFRACTION' 10 ? refined -16.3123 -63.2828  -16.4073 0.0679  -0.0558 -0.3247 0.1348  0.1080  -0.0358 4.8935  -0.3879 
5.3251  -0.7121 0.4944  -0.5039 0.1082  0.3980  -0.1862 -0.4215 0.0239  -0.1379 0.0797  -0.2138 -0.1321 
'X-RAY DIFFRACTION' 11 ? refined -7.8321  -68.5789  -8.0733  0.1365  0.2082  -0.1665 -0.0358 0.1128  -0.0627 5.1945  -0.8351 
1.8416  -4.1309 5.0210  -1.1157 0.0518  0.3565  0.1312  -0.2136 0.0442  -0.2029 0.0110  0.0718  -0.0960 
'X-RAY DIFFRACTION' 12 ? refined -5.3360  -68.6726  0.5238   -0.1943 -0.1879 -0.1687 -0.0879 0.0854  -0.1902 6.2284  7.0236  
6.5846  -2.3262 -0.7038 -1.4073 -0.0808 0.3087  0.5057  -0.1066 -0.3324 -0.0083 0.0206  -0.8986 0.4132  
'X-RAY DIFFRACTION' 13 ? refined 0.3118   -82.3225  4.9784   -0.0368 0.0743  -0.0061 -0.1937 0.0751  -0.0090 0.2663  5.9355  
5.3107  -0.7762 -1.0975 0.7583  -0.0974 0.0413  0.1496  -0.2585 0.2590  -0.4972 0.1849  0.1584  -0.1616 
'X-RAY DIFFRACTION' 14 ? refined 1.8234   -69.0903  9.7912   -0.0751 -0.1910 0.1658  -0.0414 0.1230  -0.0101 2.7000  0.1687  
7.9554  2.0985  0.1372  0.3645  0.0035  -0.5120 0.6463  0.1364  -0.2840 -0.2558 -0.2729 -0.1365 0.2805  
'X-RAY DIFFRACTION' 15 ? refined -0.4088  -70.6031  18.2004  -0.1648 -0.0307 0.1951  -0.2892 -0.1823 -0.1310 1.6063  2.6259  
4.4785  -0.4466 -4.7847 3.9341  -0.0555 -0.2604 0.5542  0.4679  -0.1105 -0.2574 0.1389  -0.2560 0.1660  
'X-RAY DIFFRACTION' 16 ? refined -13.4620 -82.7212  13.7619  -0.0853 0.1805  -0.0725 -0.2032 -0.0398 -0.0451 0.8573  -2.2031 
3.6253  1.4569  -0.9381 5.7536  0.0406  -0.0958 -0.0748 -0.0036 0.0221  0.3214  -0.0083 -0.0160 -0.0627 
'X-RAY DIFFRACTION' 17 ? refined -0.8448  -67.2761  7.8513   -0.0465 -0.2298 -0.0379 -0.1442 -0.0199 -0.1601 5.8105  7.2394  
3.8870  -0.3302 -1.2581 -1.6904 0.0280  -0.2238 0.9298  0.1309  0.0191  -0.1953 -0.3165 -0.5622 -0.0471 
'X-RAY DIFFRACTION' 18 ? refined -22.5447 -54.4577  -15.7171 0.3742  0.2499  -0.1108 0.2284  -0.0219 0.0032  2.8948  1.0565  
-0.6251 0.5660  -0.3656 -0.9749 -0.0987 0.4568  0.2464  -0.5607 0.3323  0.0351  0.0636  -0.4142 -0.2336 
'X-RAY DIFFRACTION' 19 ? refined -91.7342 15.9189   -32.4914 -0.0481 0.4722  -0.1541 -0.0323 -0.0716 0.1151  3.8029  3.8728  
2.1195  3.2793  -3.2409 -1.5519 0.0413  -0.0712 -0.1260 0.1247  0.1353  0.2403  -0.1468 -0.3271 -0.1765 
'X-RAY DIFFRACTION' 20 ? refined -82.8777 20.1241   -25.4828 -0.2352 0.5301  -0.4289 -0.1798 0.1956  0.1809  4.0933  6.0491  
7.5494  4.3075  -1.1407 2.3422  -0.0145 -0.4394 -0.4489 0.1330  0.1345  -0.0516 0.2209  0.0355  -0.1200 
'X-RAY DIFFRACTION' 21 ? refined -89.5025 19.0374   -22.4502 -0.1010 0.2280  -0.1459 -0.0526 0.3183  0.1942  4.6237  1.8422  
-1.7821 0.5827  0.2244  -3.9480 0.0815  -0.4753 -0.1085 0.1761  0.0686  0.2053  -0.1627 -0.2789 -0.1501 
'X-RAY DIFFRACTION' 22 ? refined -87.4504 23.2201   -29.3328 -0.1466 0.3117  -0.2958 -0.1229 0.0455  0.2842  1.1363  4.2490  
2.8320  -0.6853 5.5238  0.1764  0.0146  0.0199  -0.0589 0.0738  -0.1004 0.0301  -0.4750 -0.5491 0.0858  
'X-RAY DIFFRACTION' 23 ? refined -68.6682 14.3674   -17.0509 -0.3583 0.5396  -0.1311 -0.3540 -0.0793 0.0188  2.1596  1.5858  
-0.3133 4.2734  0.4804  -0.2478 -0.0056 0.1256  -0.0089 0.0203  0.0308  0.0075  -0.1973 -0.0737 -0.0252 
'X-RAY DIFFRACTION' 24 ? refined -88.6250 22.7230   -36.0751 -0.1610 0.0304  -0.4527 0.0062  0.0524  0.1045  3.8261  0.7205  
3.0335  3.6155  3.2904  1.4827  -0.0037 0.0034  -0.2509 -0.4854 -0.2092 0.4639  0.1764  -0.0624 0.2129  
'X-RAY DIFFRACTION' 25 ? refined -95.3749 34.4342   -58.6552 -0.0981 0.3600  -0.1263 -0.3693 -0.2818 -0.0701 6.5037  -3.0001 
2.7412  -4.3460 3.6166  3.8281  0.0084  0.1973  -0.2984 -0.2511 0.0390  0.0469  0.1475  0.0179  -0.0474 
'X-RAY DIFFRACTION' 26 ? refined -90.2298 30.5750   -56.5258 -0.2059 0.2808  -0.3508 -0.3114 -0.0170 0.0246  3.9268  0.7983  
2.3236  -0.2389 -0.0501 -2.6064 -0.1227 0.1853  0.2061  -0.3390 -0.0358 -0.0158 0.1193  0.0164  0.1585  
'X-RAY DIFFRACTION' 27 ? refined -92.6861 27.7983   -65.9037 0.2459  0.4079  -0.2183 0.2068  -0.1964 -0.2476 2.6541  6.1162  
2.0459  0.2045  2.7484  0.0984  0.0746  0.0576  -0.0342 -0.3761 -0.1105 -0.0024 -0.0022 -0.0542 0.0359  
'X-RAY DIFFRACTION' 28 ? refined -98.1863 30.0618   -66.8900 -0.0191 0.1005  -0.0201 -0.1903 -0.2773 0.0655  0.7857  1.3369  
0.6762  -0.5979 4.1219  -0.1338 -0.0306 0.0120  0.0869  -0.0221 0.0163  0.0282  -0.0150 0.0367  0.0143  
'X-RAY DIFFRACTION' 29 ? refined -65.6838 33.6028   -36.9292 0.2859  0.2924  -0.2004 -0.2438 0.1872  -0.0411 3.4220  -1.3309 
2.2048  -2.6546 -1.1000 1.2816  -0.1720 0.0586  0.3318  0.2265  0.0776  -0.3152 -0.2555 -0.0576 0.0944  
'X-RAY DIFFRACTION' 30 ? refined -68.4437 26.6914   -27.5829 0.1287  0.1526  -0.2680 -0.2180 0.1730  0.0722  -1.6528 0.4196  
1.7297  -0.5259 6.7084  0.9342  0.0554  -0.1517 0.0345  0.2148  -0.0201 -0.2183 -0.2580 0.0593  -0.0354 
'X-RAY DIFFRACTION' 31 ? refined -69.8271 19.7824   -36.3157 0.0998  0.1654  -0.0635 -0.2002 0.2642  0.0827  -0.1643 5.9060  
-0.7304 1.6541  -1.3550 -0.8046 0.0054  0.0450  -0.0065 -0.4872 0.0308  0.3144  -0.0838 0.1474  -0.0362 
'X-RAY DIFFRACTION' 32 ? refined -63.8110 24.2409   -37.7975 -0.1471 0.0574  -0.3058 -0.2841 0.2013  0.0755  9.3449  1.2520  
5.6118  -0.4874 0.4490  -1.0993 -0.1389 0.5599  0.0819  -0.1102 0.0120  -0.4531 -0.0252 0.3869  0.1269  
'X-RAY DIFFRACTION' 33 ? refined -71.7823 30.6247   -35.5320 0.0988  0.1232  -0.5514 -0.2529 -0.1100 -0.0169 6.5417  2.9448  
-1.1587 -1.6910 3.9387  -3.8563 0.0114  -0.3021 0.0615  0.1976  -0.1918 0.0213  -0.0872 -0.1369 0.1804  
'X-RAY DIFFRACTION' 34 ? refined -86.1015 42.4195   -59.0985 -0.1052 -0.0077 -0.3954 -0.2803 -0.2060 0.3632  3.7658  4.5711  
1.6105  -0.6574 2.6216  -0.2733 -0.1100 0.2391  0.3587  -0.3989 0.0831  0.3754  0.0545  -0.1008 0.0269  
'X-RAY DIFFRACTION' 35 ? refined -89.6436 55.8855   -55.8060 0.1706  -0.1060 0.2817  -0.1729 -0.1446 0.1285  -0.5562 0.9433  
-0.2825 1.7094  0.6593  -0.6286 0.0130  -0.0466 0.0357  0.0115  0.0513  0.0363  0.0496  0.0130  -0.0643 
'X-RAY DIFFRACTION' 36 ? refined -82.2717 38.1354   -53.6538 0.0947  0.3063  -0.6230 -0.3842 -0.1889 0.0885  -0.2556 2.4952  
5.0736  2.2064  -1.8174 2.0766  0.0132  -0.0798 0.4574  -0.0528 0.0044  0.2086  -0.3354 -0.4931 -0.0176 
'X-RAY DIFFRACTION' 37 ? refined -88.7527 52.0711   -58.9865 0.3281  0.2326  0.3409  -0.1191 -0.4014 0.2315  1.3445  2.1735  
0.4979  -5.2075 0.8065  -2.0527 -0.0013 0.2205  0.2339  -0.0687 0.1230  0.3721  -0.1806 -0.2376 -0.1217 
'X-RAY DIFFRACTION' 38 ? refined -92.0340 51.9360   -67.7985 0.1473  0.0602  -0.0504 0.0932  -0.1854 0.1182  -0.0646 1.5358  
0.4444  0.1263  0.4582  -3.4639 -0.0118 0.0524  -0.0233 0.1019  -0.0732 -0.0247 0.0379  -0.0289 0.0850  
'X-RAY DIFFRACTION' 39 ? refined -35.1113 -56.0420  29.3294  0.2759  -0.2120 -0.0136 0.3506  0.2393  0.4012  -0.2337 3.3937  
1.6131  -0.2525 1.6145  -5.5316 -0.1182 0.1298  -0.0433 0.1862  -0.0679 -0.0144 0.1266  -0.0690 0.1860  
'X-RAY DIFFRACTION' 40 ? refined -25.9793 -47.4770  30.3423  -0.2709 0.0315  0.4485  0.2473  -0.0652 0.2195  2.5912  0.9719  
-1.8756 -1.6945 -0.7319 -3.7760 -0.0346 0.0500  -0.0150 0.0021  0.0002  0.0084  -0.0163 0.1401  0.0345  
'X-RAY DIFFRACTION' 41 ? refined -31.8217 -33.4783  11.7834  -0.0807 -0.2299 0.1705  -0.1608 -0.0257 -0.1264 4.1187  5.6292  
-1.6164 -3.9348 -2.3324 -2.1941 0.2094  0.0319  0.0941  -0.0902 -0.1969 -0.7166 -0.3501 0.0207  -0.0125 
'X-RAY DIFFRACTION' 42 ? refined -45.8888 -25.3505  -4.8106  0.3749  0.2307  0.0354  -0.1202 0.0300  -0.2445 0.5357  -0.2154 
0.2609  -0.3391 0.6082  0.2678  -0.0067 0.0566  0.0249  -0.0187 0.0712  0.0916  -0.0005 0.0178  -0.0645 
'X-RAY DIFFRACTION' 43 ? refined -36.4429 -41.8733  8.4384   -0.0057 -0.4751 0.1656  0.0852  0.1321  -0.0915 3.9372  0.6877  
1.5050  0.2918  -4.9315 2.9210  0.0952  0.0854  -0.5796 -0.1849 -0.2486 -0.0373 0.1487  -0.1460 0.1534  
'X-RAY DIFFRACTION' 44 ? refined -21.6690 -60.9889  25.7940  0.1081  -0.4381 0.4735  0.2994  0.3384  0.2558  0.9750  4.0226  
-0.2500 1.3634  -3.6052 0.1973  0.0468  -0.1623 -0.0642 0.0472  -0.0473 -0.0115 0.1272  -0.0019 0.0005  
'X-RAY DIFFRACTION' 45 ? refined -20.1864 -59.5517  38.8434  -0.0132 -0.0616 0.1168  0.3597  -0.3095 0.2786  0.4199  0.1980  
-0.2128 -0.3113 0.4488  -0.6488 -0.0053 -0.0040 0.0494  0.0216  0.0307  -0.0389 0.0206  0.0324  -0.0254 
'X-RAY DIFFRACTION' 46 ? refined -15.3582 -77.4974  36.7052  0.1761  -0.1103 0.0002  0.3992  0.0667  0.3402  -0.3870 1.1971  
1.0316  -1.5237 3.4129  -2.4208 0.0191  0.1478  -0.0042 0.0072  0.0437  -0.0019 -0.1756 0.1869  -0.0628 
'X-RAY DIFFRACTION' 47 ? refined -43.9525 -48.8771  18.5928  -0.3176 -0.0885 0.3278  0.0501  0.3344  0.0902  2.2620  1.0900  
-1.9193 -0.2970 -5.8010 -1.6755 0.0204  -0.2695 -0.0902 0.1052  0.0404  0.0113  0.0464  -0.1125 -0.0608 
'X-RAY DIFFRACTION' 48 ? refined -42.9866 -44.9921  16.4799  0.1645  -0.4739 0.4279  0.0582  0.0175  -0.0430 1.1786  3.9926  
7.4454  1.1662  -7.0032 2.1338  -0.0207 -0.0798 -0.3896 0.2505  -0.0352 -0.1722 -0.0623 -0.2181 0.0558  
'X-RAY DIFFRACTION' 49 ? refined -57.3664 -8.2746   7.8339   -0.2837 -0.0110 0.0376  -0.1737 0.0912  -0.1117 0.3437  8.8740  
2.1504  0.0177  -0.9571 -5.0007 0.1637  -0.0527 -0.1119 -0.5171 0.2206  0.3341  0.2751  0.1369  -0.3843 
'X-RAY DIFFRACTION' 50 ? refined -49.9339 4.2562    1.6774   -0.4515 -0.0021 0.0127  -0.2380 0.0202  -0.1242 3.8522  4.6011  
6.2152  -0.8640 0.6451  -3.9710 -0.1266 0.2626  -0.1040 0.1154  -0.3854 -0.4898 0.1977  0.5319  0.5121  
'X-RAY DIFFRACTION' 51 ? refined -62.2989 13.9755   -6.0959  -0.1653 0.0974  0.1052  -0.0039 0.1632  -0.0410 8.3440  7.7553  
-1.1997 -3.0422 0.8297  -2.1908 0.1285  -0.1439 0.2830  -0.2640 -0.3028 -0.0805 -0.5210 -0.4676 0.1743  
'X-RAY DIFFRACTION' 52 ? refined -48.0614 11.5829   -5.1336  -0.2642 0.1009  0.0063  -0.1552 0.1942  0.0224  1.6618  2.6994  
0.6134  -0.1337 -3.2906 -0.0205 0.1044  0.1360  0.2047  -0.1393 -0.0101 -1.0739 -0.3429 0.1945  -0.0944 
'X-RAY DIFFRACTION' 53 ? refined -49.3584 13.0618   -14.9224 -0.0601 0.2400  -0.2022 -0.2409 0.2364  -0.0801 1.8141  3.9458  
4.4167  1.2604  -3.0910 0.6303  -0.0189 0.4152  0.1421  -0.3787 0.1593  -0.3627 -0.2102 -0.0819 -0.1404 
'X-RAY DIFFRACTION' 54 ? refined -51.4290 6.6121    -8.4674  -0.2307 0.0774  -0.0698 -0.0913 0.2187  -0.0248 5.8972  3.0234  
4.0634  1.3801  -0.3104 -0.8962 -0.1315 0.5506  0.0689  -0.4317 0.0991  -0.2907 0.2090  -0.0600 0.0324  
'X-RAY DIFFRACTION' 55 ? refined -53.1411 -15.7248  13.2756  -0.4079 0.3580  0.0878  -0.1130 0.0175  -0.0316 0.3783  10.1738 
2.5249  -2.5971 0.3072  1.1397  -0.0674 -0.4164 0.4775  0.2124  0.2504  0.2082  -0.0162 -0.0619 -0.1829 
'X-RAY DIFFRACTION' 56 ? refined -44.9340 -31.7714  13.5352  0.0916  -0.1245 0.0632  -0.2435 -0.1736 -0.0862 10.3367 5.6623  
-0.9031 -7.4403 -2.9081 -0.6101 -0.0514 -0.1456 -0.2439 -0.0485 0.0646  -0.1871 0.6792  0.0396  -0.0132 
'X-RAY DIFFRACTION' 57 ? refined -15.8046 -115.6016 19.1883  -0.3527 0.1993  0.0501  -0.0918 -0.0672 -0.0310 5.5047  4.4849  
8.2501  5.2149  5.7607  -6.5208 0.1919  0.2741  -0.4132 0.2086  0.2721  -0.1540 0.2694  0.0251  -0.4640 
'X-RAY DIFFRACTION' 58 ? refined -6.7989  -109.0374 20.6802  -0.0620 0.1017  -0.2673 -0.0933 -0.0117 -0.1844 6.6554  3.6221  
2.1297  4.9080  -0.4201 -0.5204 0.0957  -0.3951 0.2194  0.2682  -0.0288 -0.2389 -0.2635 0.1716  -0.0670 
'X-RAY DIFFRACTION' 59 ? refined -7.1652  -109.7687 11.1797  -0.3768 0.3129  -0.2336 -0.2826 0.0954  -0.2883 2.8264  7.2562  
-1.8004 0.4104  -0.5998 -2.7574 -0.0101 0.2290  -0.2033 -0.1273 0.2926  -0.5975 0.0165  0.3933  -0.2826 
'X-RAY DIFFRACTION' 60 ? refined -6.8062  -114.5758 19.1017  -0.2094 0.1314  0.0354  -0.1116 -0.0179 -0.1518 3.5886  0.7528  
4.2285  -1.1527 4.2895  -2.4994 0.2864  0.2600  -0.3663 -0.2743 -0.0895 -0.3320 0.3581  0.9435  -0.1970 
'X-RAY DIFFRACTION' 61 ? refined -3.6612  -89.8155  12.9915  -0.0454 0.3565  0.2561  -0.2819 0.0017  -0.1551 1.6524  0.8340  
0.6165  1.5516  2.5078  -0.3071 -0.0158 0.0271  0.0209  -0.0210 -0.0529 -0.0688 0.0014  -0.0129 0.0688  
'X-RAY DIFFRACTION' 62 ? refined -9.7092  -115.2906 24.0515  -0.1951 -0.1265 -0.3057 -0.2155 0.2068  -0.1554 0.8093  3.7715  
3.5950  1.5834  2.5101  -1.0816 0.1898  0.1224  -0.3434 0.0860  0.2157  -0.0571 0.2116  0.1098  -0.4055 
'X-RAY DIFFRACTION' 63 ? refined -13.9929 -132.5184 43.4869  0.2288  -0.2427 0.0351  0.0403  -0.4071 0.3591  1.7517  1.1099  
-2.0007 1.9543  -5.3394 -1.8481 0.0157  -0.0694 -0.2806 0.0089  0.0700  0.2962  0.2716  -0.2043 -0.0857 
'X-RAY DIFFRACTION' 64 ? refined -11.9489 -127.5199 43.7251  -0.0053 -0.2795 0.0534  -0.0100 -0.2138 0.2314  0.1328  9.7844  
2.9230  4.1563  5.5558  -1.0478 -0.0396 -0.0568 0.0262  0.4012  0.0682  -0.0427 -0.0485 -0.1833 -0.0286 
'X-RAY DIFFRACTION' 65 ? refined -20.2295 -130.5168 50.5658  0.1002  0.2975  0.1779  -0.1143 0.0517  -0.0768 0.4892  -0.8922 
2.8721  -4.2581 2.4271  2.7547  -0.0236 -0.4442 -0.1596 0.0810  0.1532  0.2853  0.0894  -0.0088 -0.1296 
'X-RAY DIFFRACTION' 66 ? refined -20.4827 -136.6216 49.4463  0.1643  -0.1240 0.0647  -0.2766 -0.2969 0.1792  0.4713  2.6332  
-0.8068 5.4543  1.2295  -1.4344 -0.0251 0.0008  0.0328  0.2470  0.0284  -0.0464 0.0278  -0.0210 -0.0033 
'X-RAY DIFFRACTION' 67 ? refined 4.9630   -101.8693 38.2596  0.0639  0.1778  -0.1264 -0.0483 -0.0059 -0.2594 8.1191  0.3364  
8.4031  3.3792  3.9416  1.1916  -0.2067 0.4430  0.2278  0.6954  0.1486  -0.6088 -0.1512 0.2881  0.0581  
'X-RAY DIFFRACTION' 68 ? refined -1.7026  -101.5832 29.4001  -0.1630 0.0935  -0.1720 -0.1748 -0.0372 -0.1596 2.9432  0.6905  
6.6191  -2.8531 6.1262  3.2363  -0.1001 0.0532  -0.3148 0.5194  0.2245  -0.1162 -0.2344 0.5900  -0.1244 
'X-RAY DIFFRACTION' 69 ? refined -2.3210  -92.9787  32.8274  0.2461  0.1577  -0.1877 -0.1810 0.0564  -0.2388 0.2156  8.6636  
3.9472  4.9237  -2.4497 -3.6259 -0.1720 0.2745  0.2149  0.1203  0.1948  -0.5956 -0.0589 0.1746  -0.0228 
'X-RAY DIFFRACTION' 70 ? refined -3.5030  -100.3823 36.8892  -0.1995 0.4256  -0.4462 -0.4094 -0.2249 -0.0947 1.9441  4.3330  
5.8648  1.8454  -4.9399 -4.9304 0.0800  0.0458  -0.1758 0.1735  -0.0173 -0.1252 -0.1336 0.0280  -0.0627 
'X-RAY DIFFRACTION' 71 ? refined 1.3327   -106.1393 33.9146  -0.2988 0.2546  -0.2471 0.1010  0.1062  -0.1918 0.8439  3.1365  
-0.0195 4.0030  4.8443  -3.2949 -0.1265 0.3125  0.0156  0.1891  0.1171  -0.0986 0.0730  0.1814  0.0094  
'X-RAY DIFFRACTION' 72 ? refined -2.9388  -128.6068 51.7054  0.1769  -0.2817 -0.3283 0.1542  -0.1951 0.0713  2.8035  0.1866  
3.6926  1.0187  3.5208  0.4174  0.1424  0.0707  -0.6651 -0.0892 0.1363  0.3575  0.3239  -0.0582 -0.2787 
'X-RAY DIFFRACTION' 73 ? refined 8.8709   -136.8685 49.9354  0.1930  -0.0117 0.2334  0.3356  -0.2692 0.2302  -0.3734 2.3339  
1.0321  1.9679  -1.2095 1.0649  -0.0138 -0.0092 0.0322  0.0320  0.0196  0.0108  -0.0119 -0.0260 -0.0058 
'X-RAY DIFFRACTION' 74 ? refined -4.2399  -120.7322 47.6208  -0.1291 0.0140  -0.2157 0.1634  -0.2600 0.1938  1.4960  -1.0371 
8.1486  -1.8640 -3.8338 -0.7369 0.0489  0.1709  -0.3158 -0.0248 0.3370  -0.0856 0.1194  0.0353  -0.3859 
'X-RAY DIFFRACTION' 75 ? refined 4.2998   -135.7841 52.5271  0.4705  0.0884  -0.1035 0.2652  -0.3383 0.2578  1.9813  9.4278  
-3.1698 -1.7865 -5.6778 -3.5816 0.1225  -0.2573 -0.8600 -0.1335 0.0284  0.0238  0.3037  0.1828  -0.1509 
'X-RAY DIFFRACTION' 76 ? refined -0.2118  -140.7459 59.4293  0.4823  -0.1412 -0.0628 0.0554  -0.2944 0.2368  -1.4263 0.7710  
2.8663  1.2251  3.7784  0.6043  0.0079  0.0357  -0.0401 -0.0257 -0.0599 0.0753  -0.0264 -0.0589 0.0520  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  ? ? ? ? ? ? ? ? ? '{A|15 - 19}'   
'X-RAY DIFFRACTION' 2  2  ? ? ? ? ? ? ? ? ? '{A|36 - 68}'   
'X-RAY DIFFRACTION' 3  3  ? ? ? ? ? ? ? ? ? '{A|69 - 87}'   
'X-RAY DIFFRACTION' 4  4  ? ? ? ? ? ? ? ? ? '{A|88 - 103}'  
'X-RAY DIFFRACTION' 5  5  ? ? ? ? ? ? ? ? ? '{A|104 - 113}' 
'X-RAY DIFFRACTION' 6  6  ? ? ? ? ? ? ? ? ? '{A|114 - 126}' 
'X-RAY DIFFRACTION' 7  7  ? ? ? ? ? ? ? ? ? '{A|148 - 154}' 
'X-RAY DIFFRACTION' 8  8  ? ? ? ? ? ? ? ? ? '{A|159 - 174}' 
'X-RAY DIFFRACTION' 9  9  ? ? ? ? ? ? ? ? ? '{B|20 - 45}'   
'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? '{B|46 - 67}'   
'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? '{B|68 - 86}'   
'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? '{B|87 - 131}'  
'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? '{B|132 - 160}' 
'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? '{B|161 - 190}' 
'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? '{B|191 - 214}' 
'X-RAY DIFFRACTION' 16 16 ? ? ? ? ? ? ? ? ? '{B|215 - 226}' 
'X-RAY DIFFRACTION' 17 17 ? ? ? ? ? ? ? ? ? '{B|227 - 260}' 
'X-RAY DIFFRACTION' 18 18 ? ? ? ? ? ? ? ? ? '{B|261 - 313}' 
'X-RAY DIFFRACTION' 19 19 ? ? ? ? ? ? ? ? ? '{C|3 - 29}'    
'X-RAY DIFFRACTION' 20 20 ? ? ? ? ? ? ? ? ? '{C|30 - 58}'   
'X-RAY DIFFRACTION' 21 21 ? ? ? ? ? ? ? ? ? '{C|59 - 82}'   
'X-RAY DIFFRACTION' 22 22 ? ? ? ? ? ? ? ? ? '{C|83 - 102}'  
'X-RAY DIFFRACTION' 23 23 ? ? ? ? ? ? ? ? ? '{C|103 - 109}' 
'X-RAY DIFFRACTION' 24 24 ? ? ? ? ? ? ? ? ? '{C|110 - 129}' 
'X-RAY DIFFRACTION' 25 25 ? ? ? ? ? ? ? ? ? '{C|130 - 160}' 
'X-RAY DIFFRACTION' 26 26 ? ? ? ? ? ? ? ? ? '{C|161 - 194}' 
'X-RAY DIFFRACTION' 27 27 ? ? ? ? ? ? ? ? ? '{C|195 - 217}' 
'X-RAY DIFFRACTION' 28 28 ? ? ? ? ? ? ? ? ? '{C|218 - 225}' 
'X-RAY DIFFRACTION' 29 29 ? ? ? ? ? ? ? ? ? '{D|1 - 25}'    
'X-RAY DIFFRACTION' 30 30 ? ? ? ? ? ? ? ? ? '{D|26 - 39}'   
'X-RAY DIFFRACTION' 31 31 ? ? ? ? ? ? ? ? ? '{D|40 - 55}'   
'X-RAY DIFFRACTION' 32 32 ? ? ? ? ? ? ? ? ? '{D|56 - 91}'   
'X-RAY DIFFRACTION' 33 33 ? ? ? ? ? ? ? ? ? '{D|92 - 109}'  
'X-RAY DIFFRACTION' 34 34 ? ? ? ? ? ? ? ? ? '{D|110 - 148}' 
'X-RAY DIFFRACTION' 35 35 ? ? ? ? ? ? ? ? ? '{D|149 - 156}' 
'X-RAY DIFFRACTION' 36 36 ? ? ? ? ? ? ? ? ? '{D|157 - 181}' 
'X-RAY DIFFRACTION' 37 37 ? ? ? ? ? ? ? ? ? '{D|182 - 206}' 
'X-RAY DIFFRACTION' 38 38 ? ? ? ? ? ? ? ? ? '{D|207 - 215}' 
'X-RAY DIFFRACTION' 39 39 ? ? ? ? ? ? ? ? ? '{E|10 - 23}'   
'X-RAY DIFFRACTION' 40 40 ? ? ? ? ? ? ? ? ? '{E|36 - 45}'   
'X-RAY DIFFRACTION' 41 41 ? ? ? ? ? ? ? ? ? '{E|46 - 68}'   
'X-RAY DIFFRACTION' 42 42 ? ? ? ? ? ? ? ? ? '{E|69 - 87}'   
'X-RAY DIFFRACTION' 43 43 ? ? ? ? ? ? ? ? ? '{E|88 - 113}'  
'X-RAY DIFFRACTION' 44 44 ? ? ? ? ? ? ? ? ? '{E|114 - 126}' 
'X-RAY DIFFRACTION' 45 45 ? ? ? ? ? ? ? ? ? '{E|148 - 154}' 
'X-RAY DIFFRACTION' 46 46 ? ? ? ? ? ? ? ? ? '{E|159 - 174}' 
'X-RAY DIFFRACTION' 47 47 ? ? ? ? ? ? ? ? ? '{F|20 - 29}'   
'X-RAY DIFFRACTION' 48 48 ? ? ? ? ? ? ? ? ? '{F|30 - 44}'   
'X-RAY DIFFRACTION' 49 49 ? ? ? ? ? ? ? ? ? '{F|45 - 99}'   
'X-RAY DIFFRACTION' 50 50 ? ? ? ? ? ? ? ? ? '{F|100 - 128}' 
'X-RAY DIFFRACTION' 51 51 ? ? ? ? ? ? ? ? ? '{F|129 - 160}' 
'X-RAY DIFFRACTION' 52 52 ? ? ? ? ? ? ? ? ? '{F|161 - 188}' 
'X-RAY DIFFRACTION' 53 53 ? ? ? ? ? ? ? ? ? '{F|189 - 210}' 
'X-RAY DIFFRACTION' 54 54 ? ? ? ? ? ? ? ? ? '{F|211 - 261}' 
'X-RAY DIFFRACTION' 55 55 ? ? ? ? ? ? ? ? ? '{F|262 - 287}' 
'X-RAY DIFFRACTION' 56 56 ? ? ? ? ? ? ? ? ? '{F|288 - 321}' 
'X-RAY DIFFRACTION' 57 57 ? ? ? ? ? ? ? ? ? '{H|1 - 27}'    
'X-RAY DIFFRACTION' 58 58 ? ? ? ? ? ? ? ? ? '{H|28 - 46}'   
'X-RAY DIFFRACTION' 59 59 ? ? ? ? ? ? ? ? ? '{H|47 - 81}'   
'X-RAY DIFFRACTION' 60 60 ? ? ? ? ? ? ? ? ? '{H|82 - 102}'  
'X-RAY DIFFRACTION' 61 61 ? ? ? ? ? ? ? ? ? '{H|103 - 108}' 
'X-RAY DIFFRACTION' 62 62 ? ? ? ? ? ? ? ? ? '{H|109 - 129}' 
'X-RAY DIFFRACTION' 63 63 ? ? ? ? ? ? ? ? ? '{H|130 - 166}' 
'X-RAY DIFFRACTION' 64 64 ? ? ? ? ? ? ? ? ? '{H|167 - 193}' 
'X-RAY DIFFRACTION' 65 65 ? ? ? ? ? ? ? ? ? '{H|194 - 217}' 
'X-RAY DIFFRACTION' 66 66 ? ? ? ? ? ? ? ? ? '{H|218 - 225}' 
'X-RAY DIFFRACTION' 67 67 ? ? ? ? ? ? ? ? ? '{L|1 - 25}'    
'X-RAY DIFFRACTION' 68 68 ? ? ? ? ? ? ? ? ? '{L|26 - 46}'   
'X-RAY DIFFRACTION' 69 69 ? ? ? ? ? ? ? ? ? '{L|47 - 75}'   
'X-RAY DIFFRACTION' 70 70 ? ? ? ? ? ? ? ? ? '{L|76 - 94}'   
'X-RAY DIFFRACTION' 71 71 ? ? ? ? ? ? ? ? ? '{L|95 - 108}'  
'X-RAY DIFFRACTION' 72 72 ? ? ? ? ? ? ? ? ? '{L|109 - 148}' 
'X-RAY DIFFRACTION' 73 73 ? ? ? ? ? ? ? ? ? '{L|149 - 158}' 
'X-RAY DIFFRACTION' 74 74 ? ? ? ? ? ? ? ? ? '{L|159 - 179}' 
'X-RAY DIFFRACTION' 75 75 ? ? ? ? ? ? ? ? ? '{L|180 - 206}' 
'X-RAY DIFFRACTION' 76 76 ? ? ? ? ? ? ? ? ? '{L|207 - 215}' 
# 
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        ? ? ? ? ? ? ? ? ? ? ? BUSTER      ? ? ? 2.10.2 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .      2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .      3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20   4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .      5 
# 
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 ASN B 33  ? ? 55.91   77.40   
2  1 THR B 37  ? ? -68.68  -74.21  
3  1 ARG B 55  ? ? 37.47   44.58   
4  1 SER B 116 ? ? -88.78  -86.80  
5  1 PHE B 116 B ? -167.30 119.30  
6  1 THR B 124 ? ? -58.29  -75.48  
7  1 SER B 125 ? ? -76.44  -74.04  
8  1 SER B 126 ? ? -20.01  -46.01  
9  1 CYS B 139 ? ? -119.54 77.11   
10 1 HIS B 141 ? ? -162.51 109.36  
11 1 SER B 146 ? ? -114.70 -160.52 
12 1 SER B 160 ? ? -166.17 97.16   
13 1 SER B 165 ? ? -151.15 64.37   
14 1 GLN B 196 ? ? 62.69   -36.32  
15 1 ASP B 199 ? ? -103.40 75.03   
16 1 SER B 210 ? ? -160.15 107.55  
17 1 LYS B 222 ? ? -68.44  84.52   
18 1 ASN B 250 ? ? 67.98   -10.73  
19 1 ALA B 264 ? ? -109.62 -67.01  
20 1 LYS B 304 ? ? -63.90  99.00   
21 1 CYS C 22  ? ? -161.48 104.15  
22 1 ARG C 59  ? ? -162.42 83.92   
23 1 THR C 91  ? ? -67.66  96.14   
24 1 CYS C 152 ? ? -160.49 100.64  
25 1 ASP C 156 ? ? 52.80   95.76   
26 1 PRO C 161 ? ? -109.37 -168.19 
27 1 SER C 200 ? ? -102.32 -70.70  
28 1 LEU C 201 ? ? 60.64   -131.62 
29 1 PRO D 15  ? ? -58.50  100.32  
30 1 SER D 53  ? ? -131.48 -37.69  
31 1 THR D 57  ? ? -65.01  98.90   
32 1 ASP D 71  ? ? 164.37  -30.43  
33 1 ASN D 94  ? ? 62.17   145.43  
34 1 LEU D 137 ? ? -119.68 77.82   
35 1 ASN D 139 ? ? 35.16   103.38  
36 1 GLU D 144 ? ? -64.25  95.60   
37 1 ASN D 153 ? ? 68.90   -35.07  
38 1 LYS D 191 ? ? -135.06 -39.76  
39 1 PRO D 205 ? ? -69.62  88.20   
40 1 THR E 15  ? ? -138.22 -43.15  
41 1 VAL E 84  ? ? 24.89   27.36   
42 1 ASP E 85  ? ? -45.44  -85.59  
43 1 ASP E 86  ? ? -36.08  -36.38  
44 1 ILE E 91  ? ? -64.92  -73.54  
45 1 ASP F 24  ? ? -29.41  123.67  
46 1 LEU F 30  ? ? -83.93  -89.60  
47 1 LYS F 63  ? ? -98.83  44.28   
48 1 THR F 96  ? ? 60.14   62.47   
49 1 THR F 124 ? ? -56.58  -74.30  
50 1 SER F 125 ? ? -76.81  -72.93  
51 1 SER F 126 ? ? -19.81  -45.74  
52 1 CYS F 139 ? ? -117.07 76.86   
53 1 HIS F 141 ? ? -161.63 107.81  
54 1 SER F 146 ? ? -113.79 -161.10 
55 1 SER F 160 ? ? -165.80 96.76   
56 1 SER F 165 ? ? -150.83 68.09   
57 1 GLN F 196 ? ? 56.29   -24.93  
58 1 ASP F 199 ? ? -103.92 74.60   
59 1 SER F 210 ? ? -160.14 106.88  
60 1 LYS F 222 ? ? -68.78  84.54   
61 1 ASN F 250 ? ? 68.24   -11.06  
62 1 ALA F 264 ? ? -44.47  97.84   
63 1 SER F 266 ? ? -92.36  -98.51  
64 1 ILE F 269 ? ? -103.20 74.96   
65 1 LYS F 304 ? ? -63.11  99.30   
66 1 LEU F 320 ? ? -76.21  -164.63 
67 1 ARG F 321 ? ? -87.24  -139.76 
68 1 CYS H 22  ? ? -161.74 104.01  
69 1 SER H 56  ? ? 49.89   26.24   
70 1 THR H 91  ? ? -67.28  95.92   
71 1 SER H 127 ? ? 76.34   154.58  
72 1 CYS H 152 ? ? -160.41 100.98  
73 1 ASP H 156 ? ? 52.43   95.76   
74 1 PRO H 159 ? ? -80.02  -111.39 
75 1 PRO L 15  ? ? -58.54  99.89   
76 1 THR L 57  ? ? -64.63  98.47   
77 1 SER L 68  ? ? -161.78 110.05  
78 1 PHE L 72  ? ? 56.29   109.49  
79 1 LEU L 137 ? ? -119.16 79.92   
80 1 ASN L 139 ? ? 41.24   97.92   
81 1 GLU L 144 ? ? -63.76  95.93   
82 1 ASN L 153 ? ? 67.77   -33.82  
83 1 LYS L 191 ? ? -135.11 -39.82  
84 1 PRO L 205 ? ? -69.41  88.28   
# 
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 GLY 1   ? A GLY 1   
2   1 Y 1 A LEU 2   ? A LEU 2   
3   1 Y 1 A PHE 3   ? A PHE 3   
4   1 Y 1 A GLY 4   ? A GLY 4   
5   1 Y 1 A ALA 5   ? A ALA 5   
6   1 Y 1 A ILE 6   ? A ILE 6   
7   1 Y 1 A ALA 7   ? A ALA 7   
8   1 Y 1 A GLY 8   ? A GLY 8   
9   1 Y 1 A PHE 9   ? A PHE 9   
10  1 Y 1 A ILE 10  ? A ILE 10  
11  1 Y 1 A GLU 11  ? A GLU 11  
12  1 Y 1 A GLY 12  ? A GLY 12  
13  1 Y 1 A GLY 13  ? A GLY 13  
14  1 Y 1 A TRP 14  ? A TRP 14  
15  1 Y 1 A GLY 20  ? A GLY 20  
16  1 Y 1 A TRP 21  ? A TRP 21  
17  1 Y 1 A TYR 22  ? A TYR 22  
18  1 Y 1 A GLY 23  ? A GLY 23  
19  1 Y 1 A TYR 24  ? A TYR 24  
20  1 Y 1 A HIS 25  ? A HIS 25  
21  1 Y 1 A HIS 26  ? A HIS 26  
22  1 Y 1 A GLN 27  ? A GLN 27  
23  1 Y 1 A ASN 28  ? A ASN 28  
24  1 Y 1 A GLU 29  ? A GLU 29  
25  1 Y 1 A GLN 30  ? A GLN 30  
26  1 Y 1 A GLY 31  ? A GLY 31  
27  1 Y 1 A SER 32  ? A SER 32  
28  1 Y 1 A GLY 33  ? A GLY 33  
29  1 Y 1 A TYR 34  ? A TYR 34  
30  1 Y 1 A ALA 35  ? A ALA 35  
31  1 Y 1 A PHE 70  ? A PHE 70  
32  1 Y 1 A ASN 71  ? A ASN 71  
33  1 Y 1 A HIS 72  ? A HIS 72  
34  1 Y 1 A LEU 73  ? A LEU 73  
35  1 Y 1 A GLU 74  ? A GLU 74  
36  1 Y 1 A LYS 75  ? A LYS 75  
37  1 Y 1 A ARG 76  ? A ARG 76  
38  1 Y 1 A ILE 77  ? A ILE 77  
39  1 Y 1 A GLU 78  ? A GLU 78  
40  1 Y 1 A ASN 79  ? A ASN 79  
41  1 Y 1 A LEU 80  ? A LEU 80  
42  1 Y 1 A ASN 81  ? A ASN 81  
43  1 Y 1 A LYS 82  ? A LYS 82  
44  1 Y 1 A LYS 127 ? A LYS 127 
45  1 Y 1 A ASN 128 ? A ASN 128 
46  1 Y 1 A ASN 129 ? A ASN 129 
47  1 Y 1 A ALA 130 ? A ALA 130 
48  1 Y 1 A LYS 131 ? A LYS 131 
49  1 Y 1 A GLU 132 ? A GLU 132 
50  1 Y 1 A ILE 133 ? A ILE 133 
51  1 Y 1 A GLY 134 ? A GLY 134 
52  1 Y 1 A ASN 135 ? A ASN 135 
53  1 Y 1 A GLY 136 ? A GLY 136 
54  1 Y 1 A CYS 137 ? A CYS 137 
55  1 Y 1 A PHE 138 ? A PHE 138 
56  1 Y 1 A GLU 139 ? A GLU 139 
57  1 Y 1 A PHE 140 ? A PHE 140 
58  1 Y 1 A TYR 141 ? A TYR 141 
59  1 Y 1 A HIS 142 ? A HIS 142 
60  1 Y 1 A LYS 143 ? A LYS 143 
61  1 Y 1 A CYS 144 ? A CYS 144 
62  1 Y 1 A ASP 145 ? A ASP 145 
63  1 Y 1 A ASN 146 ? A ASN 146 
64  1 Y 1 A THR 147 ? A THR 147 
65  1 Y 1 A GLY 155 ? A GLY 155 
66  1 Y 1 A THR 156 ? A THR 156 
67  1 Y 1 A TYR 157 ? A TYR 157 
68  1 Y 1 A ASP 158 ? A ASP 158 
69  1 Y 1 A GLY 175 ? A GLY 175 
70  1 Y 1 A VAL 176 ? A VAL 176 
71  1 Y 1 B ALA 10  ? B ALA 1   
72  1 Y 1 B ASP 11  ? B ASP 2   
73  1 Y 1 B THR 12  ? B THR 3   
74  1 Y 1 B LEU 13  ? B LEU 4   
75  1 Y 1 B CYS 14  ? B CYS 5   
76  1 Y 1 B ILE 15  ? B ILE 6   
77  1 Y 1 B GLY 16  ? B GLY 7   
78  1 Y 1 B TYR 17  ? B TYR 8   
79  1 Y 1 B HIS 18  ? B HIS 9   
80  1 Y 1 B ALA 19  ? B ALA 10  
81  1 Y 1 B GLU 77  ? B GLU 69  
82  1 Y 1 B SER 78  ? B SER 70  
83  1 Y 1 B LEU 79  ? B LEU 71  
84  1 Y 1 B SER 80  ? B SER 72  
85  1 Y 1 B THR 81  ? B THR 73  
86  1 Y 1 B ARG 315 ? B ARG 314 
87  1 Y 1 B LEU 316 ? B LEU 315 
88  1 Y 1 B ALA 317 ? B ALA 316 
89  1 Y 1 B THR 318 ? B THR 317 
90  1 Y 1 B GLY 319 ? B GLY 318 
91  1 Y 1 B LEU 320 ? B LEU 319 
92  1 Y 1 B ARG 321 ? B ARG 320 
93  1 Y 1 B ASN 322 ? B ASN 321 
94  1 Y 1 B ILE 323 ? B ILE 322 
95  1 Y 1 B PRO 324 ? B PRO 323 
96  1 Y 1 B SER 325 ? B SER 324 
97  1 Y 1 B ILE 326 ? B ILE 325 
98  1 Y 1 B GLN 327 ? B GLN 326 
99  1 Y 1 B SER 328 ? B SER 327 
100 1 Y 1 B ARG 329 ? B ARG 328 
101 1 Y 1 C GLU 1   ? C GLU 1   
102 1 Y 1 C VAL 2   ? C VAL 2   
103 1 Y 1 C SER 140 ? C SER 140 
104 1 Y 1 C LYS 141 ? C LYS 141 
105 1 Y 1 C SER 142 ? C SER 142 
106 1 Y 1 C THR 143 ? C THR 143 
107 1 Y 1 C SER 144 ? C SER 144 
108 1 Y 1 C GLY 145 ? C GLY 145 
109 1 Y 1 C GLY 146 ? C GLY 146 
110 1 Y 1 C LYS 226 ? C LYS 226 
111 1 Y 1 C SER 227 ? C SER 227 
112 1 Y 1 C CYS 228 ? C CYS 228 
113 1 Y 1 C ASP 229 ? C ASP 229 
114 1 Y 1 C LYS 230 ? C LYS 230 
115 1 Y 1 E GLY 1   ? E GLY 1   
116 1 Y 1 E LEU 2   ? E LEU 2   
117 1 Y 1 E PHE 3   ? E PHE 3   
118 1 Y 1 E GLY 4   ? E GLY 4   
119 1 Y 1 E ALA 5   ? E ALA 5   
120 1 Y 1 E ILE 6   ? E ILE 6   
121 1 Y 1 E ALA 7   ? E ALA 7   
122 1 Y 1 E GLY 8   ? E GLY 8   
123 1 Y 1 E PHE 9   ? E PHE 9   
124 1 Y 1 E TYR 24  ? E TYR 24  
125 1 Y 1 E HIS 25  ? E HIS 25  
126 1 Y 1 E HIS 26  ? E HIS 26  
127 1 Y 1 E GLN 27  ? E GLN 27  
128 1 Y 1 E ASN 28  ? E ASN 28  
129 1 Y 1 E GLU 29  ? E GLU 29  
130 1 Y 1 E GLN 30  ? E GLN 30  
131 1 Y 1 E GLY 31  ? E GLY 31  
132 1 Y 1 E SER 32  ? E SER 32  
133 1 Y 1 E GLY 33  ? E GLY 33  
134 1 Y 1 E TYR 34  ? E TYR 34  
135 1 Y 1 E ALA 35  ? E ALA 35  
136 1 Y 1 E PHE 70  ? E PHE 70  
137 1 Y 1 E ASN 71  ? E ASN 71  
138 1 Y 1 E HIS 72  ? E HIS 72  
139 1 Y 1 E LEU 73  ? E LEU 73  
140 1 Y 1 E GLU 74  ? E GLU 74  
141 1 Y 1 E LYS 75  ? E LYS 75  
142 1 Y 1 E ARG 76  ? E ARG 76  
143 1 Y 1 E ILE 77  ? E ILE 77  
144 1 Y 1 E GLU 78  ? E GLU 78  
145 1 Y 1 E ASN 79  ? E ASN 79  
146 1 Y 1 E LEU 80  ? E LEU 80  
147 1 Y 1 E ASN 81  ? E ASN 81  
148 1 Y 1 E LYS 82  ? E LYS 82  
149 1 Y 1 E LYS 127 ? E LYS 127 
150 1 Y 1 E ASN 128 ? E ASN 128 
151 1 Y 1 E ASN 129 ? E ASN 129 
152 1 Y 1 E ALA 130 ? E ALA 130 
153 1 Y 1 E LYS 131 ? E LYS 131 
154 1 Y 1 E GLU 132 ? E GLU 132 
155 1 Y 1 E ILE 133 ? E ILE 133 
156 1 Y 1 E GLY 134 ? E GLY 134 
157 1 Y 1 E ASN 135 ? E ASN 135 
158 1 Y 1 E GLY 136 ? E GLY 136 
159 1 Y 1 E CYS 137 ? E CYS 137 
160 1 Y 1 E PHE 138 ? E PHE 138 
161 1 Y 1 E GLU 139 ? E GLU 139 
162 1 Y 1 E PHE 140 ? E PHE 140 
163 1 Y 1 E TYR 141 ? E TYR 141 
164 1 Y 1 E HIS 142 ? E HIS 142 
165 1 Y 1 E LYS 143 ? E LYS 143 
166 1 Y 1 E CYS 144 ? E CYS 144 
167 1 Y 1 E ASP 145 ? E ASP 145 
168 1 Y 1 E ASN 146 ? E ASN 146 
169 1 Y 1 E THR 147 ? E THR 147 
170 1 Y 1 E GLY 155 ? E GLY 155 
171 1 Y 1 E THR 156 ? E THR 156 
172 1 Y 1 E TYR 157 ? E TYR 157 
173 1 Y 1 E ASP 158 ? E ASP 158 
174 1 Y 1 E GLY 175 ? E GLY 175 
175 1 Y 1 E VAL 176 ? E VAL 176 
176 1 Y 1 F ALA 10  ? F ALA 1   
177 1 Y 1 F ASP 11  ? F ASP 2   
178 1 Y 1 F THR 12  ? F THR 3   
179 1 Y 1 F LEU 13  ? F LEU 4   
180 1 Y 1 F CYS 14  ? F CYS 5   
181 1 Y 1 F ILE 15  ? F ILE 6   
182 1 Y 1 F GLY 16  ? F GLY 7   
183 1 Y 1 F TYR 17  ? F TYR 8   
184 1 Y 1 F HIS 18  ? F HIS 9   
185 1 Y 1 F ALA 19  ? F ALA 10  
186 1 Y 1 F GLU 77  ? F GLU 69  
187 1 Y 1 F SER 78  ? F SER 70  
188 1 Y 1 F LEU 79  ? F LEU 71  
189 1 Y 1 F SER 80  ? F SER 72  
190 1 Y 1 F THR 81  ? F THR 73  
191 1 Y 1 F ILE 323 ? F ILE 322 
192 1 Y 1 F PRO 324 ? F PRO 323 
193 1 Y 1 F SER 325 ? F SER 324 
194 1 Y 1 F ILE 326 ? F ILE 325 
195 1 Y 1 F GLN 327 ? F GLN 326 
196 1 Y 1 F SER 328 ? F SER 327 
197 1 Y 1 F ARG 329 ? F ARG 328 
198 1 Y 1 H SER 139 ? G SER 139 
199 1 Y 1 H SER 140 ? G SER 140 
200 1 Y 1 H LYS 141 ? G LYS 141 
201 1 Y 1 H SER 142 ? G SER 142 
202 1 Y 1 H THR 143 ? G THR 143 
203 1 Y 1 H SER 144 ? G SER 144 
204 1 Y 1 H GLY 145 ? G GLY 145 
205 1 Y 1 H GLY 146 ? G GLY 146 
206 1 Y 1 H THR 147 ? G THR 147 
207 1 Y 1 H LYS 226 ? G LYS 226 
208 1 Y 1 H SER 227 ? G SER 227 
209 1 Y 1 H CYS 228 ? G CYS 228 
210 1 Y 1 H ASP 229 ? G ASP 229 
211 1 Y 1 H LYS 230 ? G LYS 230 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        N-ACETYL-D-GLUCOSAMINE 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
