data_3ZNL
# 
_entry.id   3ZNL 
# 
_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   3ZNL         
PDBE  EBI-55835    
WWPDB D_1290055835 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 3ZNK unspecified 
;H5 HAEMAGGLUTININ IN COMPLEX WITH 6-O-SULFO-2,3- SIALYLLACTOSAMINE (SULFATED 3'SLN)
;
PDB 3ZNM unspecified 'H5 HAEMAGGLUTININ IN COMPLEX WITH SIALYL-LEWIS X'                                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3ZNL 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2013-02-15 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Xiong, X.'     1 
'Tuzikov, A.'   2 
'Coombs, P.'    3 
'Martin, S.R.'  4 
'Walker, P.A.'  5 
'Gamblin, S.J.' 6 
'Bovin, N.'     7 
'Skehel, J.J.'  8 
# 
_citation.id                        primary 
_citation.title                     
'Recognition of Sulphated and Fucosylated Receptor Sialosides by A/Vietnam/1194/2004 (H5N1) Influenza Virus.' 
_citation.journal_abbrev            'Virus Res.' 
_citation.journal_volume            178 
_citation.page_first                12 
_citation.page_last                 ? 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   NE 
_citation.journal_id_ISSN           0168-1702 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24036174 
_citation.pdbx_database_id_DOI      10.1016/J.VIRUSRES.2013.08.007 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Xiong, X.'     1 
primary 'Tuzikov, A.'   2 
primary 'Coombs, P.'    3 
primary 'Martin, S.'    4 
primary 'Walker, P.A.'  5 
primary 'Gamblin, S.J.' 6 
primary 'Bovin, N.'     7 
primary 'Skehel, J.J.'  8 
# 
_cell.entry_id           3ZNL 
_cell.length_a           175.980 
_cell.length_b           101.600 
_cell.length_c           161.370 
_cell.angle_alpha        90.00 
_cell.angle_beta         111.32 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         3ZNL 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
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     nat HAEMAGGLUTININ                                           36950.766 3   ? ? 
'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-340'  ? 
2 polymer     nat HAEMAGGLUTININ                                           19097.990 3   ? ? 
'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                                   221.208   9   ? ? ? ? 
4 non-polymer man 'O-SIALIC ACID'                                          309.270   3   ? ? ? ? 
5 non-polymer man 'ALPHA D-GALACTOSE'                                      180.156   3   ? ? ? ? 
6 non-polymer man '2-(acetylamino)-2-deoxy-6-O-sulfo-beta-D-glucopyranose' 301.271   3   ? ? ? ? 
7 non-polymer man ALPHA-L-FUCOSE                                           164.156   3   ? ? ? ? 
8 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'    238.305   3   ? ? ? ? 
9 water       nat water                                                    18.015    265 ? ? ? ? 
# 
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 
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV
EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI
KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN
FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS
PQRETR
;
;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV
EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI
KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN
FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS
PQRETR
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEA
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEA
;
B,D,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   GLN n 
1 3   ILE n 
1 4   CYS n 
1 5   ILE n 
1 6   GLY n 
1 7   TYR n 
1 8   HIS n 
1 9   ALA n 
1 10  ASN n 
1 11  ASN n 
1 12  SER n 
1 13  THR n 
1 14  GLU n 
1 15  GLN n 
1 16  VAL n 
1 17  ASP n 
1 18  THR n 
1 19  ILE n 
1 20  MET n 
1 21  GLU n 
1 22  LYS n 
1 23  ASN n 
1 24  VAL n 
1 25  THR n 
1 26  VAL n 
1 27  THR n 
1 28  HIS n 
1 29  ALA n 
1 30  GLN n 
1 31  ASP n 
1 32  ILE n 
1 33  LEU n 
1 34  GLU n 
1 35  LYS n 
1 36  THR n 
1 37  HIS n 
1 38  ASN n 
1 39  GLY n 
1 40  LYS n 
1 41  LEU n 
1 42  CYS n 
1 43  ASP n 
1 44  LEU n 
1 45  ASP n 
1 46  GLY n 
1 47  VAL n 
1 48  LYS n 
1 49  PRO n 
1 50  LEU n 
1 51  ILE n 
1 52  LEU n 
1 53  ARG n 
1 54  ASP n 
1 55  CYS n 
1 56  SER n 
1 57  VAL n 
1 58  ALA n 
1 59  GLY n 
1 60  TRP n 
1 61  LEU n 
1 62  LEU n 
1 63  GLY n 
1 64  ASN n 
1 65  PRO n 
1 66  MET n 
1 67  CYS n 
1 68  ASP n 
1 69  GLU n 
1 70  PHE n 
1 71  ILE n 
1 72  ASN n 
1 73  VAL n 
1 74  PRO n 
1 75  GLU n 
1 76  TRP n 
1 77  SER n 
1 78  TYR n 
1 79  ILE n 
1 80  VAL n 
1 81  GLU n 
1 82  LYS n 
1 83  ALA n 
1 84  ASN n 
1 85  PRO n 
1 86  VAL n 
1 87  ASN n 
1 88  ASP n 
1 89  LEU n 
1 90  CYS n 
1 91  TYR n 
1 92  PRO n 
1 93  GLY n 
1 94  ASP n 
1 95  PHE n 
1 96  ASN n 
1 97  ASP n 
1 98  TYR n 
1 99  GLU n 
1 100 GLU n 
1 101 LEU n 
1 102 LYS n 
1 103 HIS n 
1 104 LEU n 
1 105 LEU n 
1 106 SER n 
1 107 ARG n 
1 108 ILE n 
1 109 ASN n 
1 110 HIS n 
1 111 PHE n 
1 112 GLU n 
1 113 LYS n 
1 114 ILE n 
1 115 GLN n 
1 116 ILE n 
1 117 ILE n 
1 118 PRO n 
1 119 LYS n 
1 120 SER n 
1 121 SER n 
1 122 TRP n 
1 123 SER n 
1 124 SER n 
1 125 HIS n 
1 126 GLU n 
1 127 ALA n 
1 128 SER n 
1 129 LEU n 
1 130 GLY n 
1 131 VAL n 
1 132 SER n 
1 133 SER n 
1 134 ALA n 
1 135 CYS n 
1 136 PRO n 
1 137 TYR n 
1 138 GLN n 
1 139 GLY n 
1 140 LYS n 
1 141 SER n 
1 142 SER n 
1 143 PHE n 
1 144 PHE n 
1 145 ARG n 
1 146 ASN n 
1 147 VAL n 
1 148 VAL n 
1 149 TRP n 
1 150 LEU n 
1 151 ILE n 
1 152 LYS n 
1 153 LYS n 
1 154 ASN n 
1 155 SER n 
1 156 THR n 
1 157 TYR n 
1 158 PRO n 
1 159 THR n 
1 160 ILE n 
1 161 LYS n 
1 162 ARG n 
1 163 SER n 
1 164 TYR n 
1 165 ASN n 
1 166 ASN n 
1 167 THR n 
1 168 ASN n 
1 169 GLN n 
1 170 GLU n 
1 171 ASP n 
1 172 LEU n 
1 173 LEU n 
1 174 VAL n 
1 175 LEU n 
1 176 TRP n 
1 177 GLY n 
1 178 ILE n 
1 179 HIS n 
1 180 HIS n 
1 181 PRO n 
1 182 ASN n 
1 183 ASP n 
1 184 ALA n 
1 185 ALA n 
1 186 GLU n 
1 187 GLN n 
1 188 THR n 
1 189 LYS n 
1 190 LEU n 
1 191 TYR n 
1 192 GLN n 
1 193 ASN n 
1 194 PRO n 
1 195 THR n 
1 196 THR n 
1 197 TYR n 
1 198 ILE n 
1 199 SER n 
1 200 VAL n 
1 201 GLY n 
1 202 THR n 
1 203 SER n 
1 204 THR n 
1 205 LEU n 
1 206 ASN n 
1 207 GLN n 
1 208 ARG n 
1 209 LEU n 
1 210 VAL n 
1 211 PRO n 
1 212 ARG n 
1 213 ILE n 
1 214 ALA n 
1 215 THR n 
1 216 ARG n 
1 217 SER n 
1 218 LYS n 
1 219 VAL n 
1 220 ASN n 
1 221 GLY n 
1 222 GLN n 
1 223 SER n 
1 224 GLY n 
1 225 ARG n 
1 226 MET n 
1 227 GLU n 
1 228 PHE n 
1 229 PHE n 
1 230 TRP n 
1 231 THR n 
1 232 ILE n 
1 233 LEU n 
1 234 LYS n 
1 235 PRO n 
1 236 ASN n 
1 237 ASP n 
1 238 ALA n 
1 239 ILE n 
1 240 ASN n 
1 241 PHE n 
1 242 GLU n 
1 243 SER n 
1 244 ASN n 
1 245 GLY n 
1 246 ASN n 
1 247 PHE n 
1 248 ILE n 
1 249 ALA n 
1 250 PRO n 
1 251 GLU n 
1 252 TYR n 
1 253 ALA n 
1 254 TYR n 
1 255 LYS n 
1 256 ILE n 
1 257 VAL n 
1 258 LYS n 
1 259 LYS n 
1 260 GLY n 
1 261 ASP n 
1 262 SER n 
1 263 THR n 
1 264 ILE n 
1 265 MET n 
1 266 LYS n 
1 267 SER n 
1 268 GLU n 
1 269 LEU n 
1 270 GLU n 
1 271 TYR n 
1 272 GLY n 
1 273 ASN n 
1 274 CYS n 
1 275 ASN n 
1 276 THR n 
1 277 LYS n 
1 278 CYS n 
1 279 GLN n 
1 280 THR n 
1 281 PRO n 
1 282 MET n 
1 283 GLY n 
1 284 ALA n 
1 285 ILE n 
1 286 ASN n 
1 287 SER n 
1 288 SER n 
1 289 MET n 
1 290 PRO n 
1 291 PHE n 
1 292 HIS n 
1 293 ASN n 
1 294 ILE n 
1 295 HIS n 
1 296 PRO n 
1 297 LEU n 
1 298 THR n 
1 299 ILE n 
1 300 GLY n 
1 301 GLU n 
1 302 CYS n 
1 303 PRO n 
1 304 LYS n 
1 305 TYR n 
1 306 VAL n 
1 307 LYS n 
1 308 SER n 
1 309 ASN n 
1 310 ARG n 
1 311 LEU n 
1 312 VAL n 
1 313 LEU n 
1 314 ALA n 
1 315 THR n 
1 316 GLY n 
1 317 LEU n 
1 318 ARG n 
1 319 ASN n 
1 320 SER n 
1 321 PRO n 
1 322 GLN n 
1 323 ARG n 
1 324 GLU n 
1 325 THR n 
1 326 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  GLN n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  SER n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  LYS n 
2 39  GLU n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  LYS n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLY n 
2 48  VAL n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  ILE n 
2 56  ILE n 
2 57  ASP n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  GLU n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  ARG n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  ASN n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  ILE n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  MET n 
2 85  GLU n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  VAL n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 LYS n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 ASP n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 LEU n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 ASP n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 LEU n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASP n 
2 146 ASN n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 ARG n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 GLN n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 ALA n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample ? ? ? 'INFLUENZA A VIRUS' 644788 ? ? 'A/VIETNAM/1194/2004 (H5N1)' ? ? ? ? 'A/VN/1194/04/NIBRG14 VACCINE STRAIN' ? ? ? ? 
? ? ? ? 'THE NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL (NIBSC)' 
2 1 sample ? ? ? 'INFLUENZA A VIRUS' 644788 ? ? 'A/VIETNAM/1194/2004 (H5N1)' ? ? ? ? 'A/VN/1194/04/NIBRG14 VACCINE STRAIN' ? ? ? ? 
? ? ? ? 'THE NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL (NIBSC)' 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 
2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? 
# 
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 3ZNL A 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
2 2 3ZNL B 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 
3 1 3ZNL C 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
4 2 3ZNL D 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 
5 1 3ZNL E 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
6 2 3ZNL F 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3ZNL THR A 325 ? UNP Q6DQ34 ARG 341 conflict 325 1 
3 3ZNL THR C 325 ? UNP Q6DQ34 ARG 341 conflict 325 2 
5 3ZNL THR E 325 ? UNP Q6DQ34 ARG 341 conflict 325 3 
# 
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 
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'    HEPES                            
'C8 H18 N2 O4 S' 238.305 
FUC saccharide          . ALPHA-L-FUCOSE                                           ?                                'C6 H12 O5' 
164.156 
GLA D-saccharide        . 'ALPHA D-GALACTOSE'                                      ?                                'C6 H12 O6' 
180.156 
GLN 'L-peptide linking' y GLUTAMINE                                                ?                                'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                          ?                                'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                  ?                                'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                ?                                
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                    ?                                'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                               ?                                'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                  ?                                'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                   ?                                
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                               ?                                
'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                                   ?                                'C8 H15 N O6' 
221.208 
NGS D-saccharide        . '2-(acetylamino)-2-deoxy-6-O-sulfo-beta-D-glucopyranose' N-ACETYL-D-GLUCOSAMINE-6-SULFATE 
'C8 H15 N O9 S'  301.271 
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 
SIA non-polymer         . 'O-SIALIC ACID'                                          ?                                'C11 H19 N O9' 
309.270 
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.entry_id          3ZNL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.04 
_exptl_crystal.density_percent_sol   70 
_exptl_crystal.description           
'DATA CORRECTED FOR ANISOTROPY USING UCLA MBI - DIFFRACTION ANISOTROPY SERVER RETAINING 3 SIGMA DATA.' 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES PH 7.0, 0.05 M MGCL2, 28 - 30 % PEG 550 MME' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 2M' 
_diffrn_detector.pdbx_collection_date   2012-04-23 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9173 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             0.9173 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     3ZNL 
_reflns.observed_criterion_sigma_I   3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             150.76 
_reflns.d_resolution_high            2.50 
_reflns.number_obs                   64504 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         70.4 
_reflns.pdbx_Rmerge_I_obs            0.11 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.30 
_reflns.B_iso_Wilson_estimate        52.4 
_reflns.pdbx_redundancy              3.3 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3ZNL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     61277 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             35.70 
_refine.ls_d_res_high                            2.50 
_refine.ls_percent_reflns_obs                    70.39 
_refine.ls_R_factor_obs                          0.23789 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23694 
_refine.ls_R_factor_R_free                       0.25582 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  3227 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.892 
_refine.correlation_coeff_Fo_to_Fc_free          0.869 
_refine.B_iso_mean                               45.063 
_refine.aniso_B[1][1]                            -0.20 
_refine.aniso_B[2][2]                            -1.01 
_refine.aniso_B[3][3]                            0.83 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.31 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. COMPLETENESS VS. RESOLUTION TABLE 999.99 5.39 9323 8903 5.39 4.28 9221 9089 4.28 3.74 9137 9040 3.74 3.40 9119 8419 3.40 3.15 9195 8800 3.15 2.97 9103 8814 2.97 2.82 9055 6258 2.82 2.70 9172 3148 2.70 2.59 9067 1560 2.59 2.50 9156 473
;
_refine.pdbx_starting_model                      'PDB ENTRY 2IBX' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.672 
_refine.pdbx_overall_ESU_R_Free                  0.327 
_refine.overall_SU_ML                            0.230 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             20.107 
_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          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11595 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         351 
_refine_hist.number_atoms_solvent             265 
_refine_hist.number_atoms_total               12211 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        35.70 
# 
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 
r_bond_refined_d             0.005  0.019  ? 12249 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 11232 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.008  1.971  ? 16635 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.710  3.003  ? 25851 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.270  5.000  ? 1446  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.161 25.174 ? 603   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.998 15.000 ? 2034  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.806 15.000 ? 51    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.056  0.200  ? 1812  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.003  0.020  ? 13824 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 2829  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.131  0.648  ? 5802  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.131  0.648  ? 5801  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.244  0.971  ? 7242  'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.488  0.883  ? 6447  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.502 
_refine_ls_shell.d_res_low                        2.567 
_refine_ls_shell.number_reflns_R_work             245 
_refine_ls_shell.R_factor_R_work                  0.461 
_refine_ls_shell.percent_reflns_obs               3.95 
_refine_ls_shell.R_factor_R_free                  0.373 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  3ZNL 
_struct.title                     'H5 Haemagglutinin in Complex with 6-O-Sulfo-Sialyl-Lewis X (Sulfated Lewis X)' 
_struct.pdbx_descriptor           HAEMAGGLUTININ 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3ZNL 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;VIRAL PROTEIN, SIALIC ACID, GLYCOPROTEIN, VIRUS RECEPTOR, SULFATED SIALOSIDE, FUCOSYLATED SIALOSIDE, SULFATION, FUCOSYLATION, AVIAN FLU, SIALYLLACTOSAMINE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 5 ? 
K  N N 6 ? 
L  N N 7 ? 
M  N N 3 ? 
N  N N 8 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 6 ? 
T  N N 7 ? 
U  N N 3 ? 
V  N N 8 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA N N 6 ? 
BA N N 7 ? 
CA N N 3 ? 
DA N N 8 ? 
EA N N 9 ? 
FA N N 9 ? 
GA N N 9 ? 
HA N N 9 ? 
IA N N 9 ? 
JA N N 9 ? 
# 
_struct_biol.id   1 
# 
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  1  SER A 56  ? GLY A 63  ? SER A 56  GLY A 63  1 ? 8  
HELX_P HELX_P2  2  ASN A 64  ? ILE A 71  ? ASN A 64  ILE A 71  5 ? 8  
HELX_P HELX_P3  3  ASP A 97  ? LEU A 105 ? ASP A 97  LEU A 105 1 ? 9  
HELX_P HELX_P4  4  SER A 106 ? ILE A 108 ? SER A 106 ILE A 108 5 ? 3  
HELX_P HELX_P5  5  ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 
HELX_P HELX_P6  6  ASP B 37  ? THR B 61  ? ASP B 37  THR B 61  1 ? 25 
HELX_P HELX_P7  7  GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P8  8  ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 
HELX_P HELX_P9  9  ASP B 158 ? SER B 163 ? ASP B 158 SER B 163 1 ? 6  
HELX_P HELX_P10 10 SER C 56  ? GLY C 63  ? SER C 56  GLY C 63  1 ? 8  
HELX_P HELX_P11 11 ASN C 64  ? ILE C 71  ? ASN C 64  ILE C 71  5 ? 8  
HELX_P HELX_P12 12 ASP C 97  ? LEU C 105 ? ASP C 97  LEU C 105 1 ? 9  
HELX_P HELX_P13 13 SER C 106 ? ILE C 108 ? SER C 106 ILE C 108 5 ? 3  
HELX_P HELX_P14 14 ASP C 183 ? GLN C 192 ? ASP C 183 GLN C 192 1 ? 10 
HELX_P HELX_P15 15 ASP D 37  ? THR D 61  ? ASP D 37  THR D 61  1 ? 25 
HELX_P HELX_P16 16 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P17 17 ASP D 145 ? GLY D 155 ? ASP D 145 GLY D 155 1 ? 11 
HELX_P HELX_P18 18 ASP D 158 ? SER D 163 ? ASP D 158 SER D 163 1 ? 6  
HELX_P HELX_P19 19 SER E 56  ? GLY E 63  ? SER E 56  GLY E 63  1 ? 8  
HELX_P HELX_P20 20 ASN E 64  ? ILE E 71  ? ASN E 64  ILE E 71  5 ? 8  
HELX_P HELX_P21 21 ASP E 97  ? LEU E 105 ? ASP E 97  LEU E 105 1 ? 9  
HELX_P HELX_P22 22 SER E 106 ? ILE E 108 ? SER E 106 ILE E 108 5 ? 3  
HELX_P HELX_P23 23 ASP E 183 ? GLN E 192 ? ASP E 183 GLN E 192 1 ? 10 
HELX_P HELX_P24 24 ASP F 37  ? THR F 61  ? ASP F 37  THR F 61  1 ? 25 
HELX_P HELX_P25 25 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P26 26 ASP F 145 ? GLY F 155 ? ASP F 145 GLY F 155 1 ? 11 
HELX_P HELX_P27 27 ASP F 158 ? SER F 163 ? ASP F 158 SER F 163 1 ? 6  
# 
_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 ? ? A  CYS 4   SG  ? ? ? 1_555 B  CYS 137 SG ? ? A CYS 4    B CYS 137  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf2  disulf ? ? A  CYS 42  SG  ? ? ? 1_555 A  CYS 274 SG ? ? A CYS 42   A CYS 274  1_555 ? ? ? ? ? ? ? 2.016 ? 
disulf3  disulf ? ? A  CYS 55  SG  ? ? ? 1_555 A  CYS 67  SG ? ? A CYS 55   A CYS 67   1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf4  disulf ? ? A  CYS 90  SG  ? ? ? 1_555 A  CYS 135 SG ? ? A CYS 90   A CYS 135  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf5  disulf ? ? A  CYS 278 SG  ? ? ? 1_555 A  CYS 302 SG ? ? A CYS 278  A CYS 302  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf6  disulf ? ? B  CYS 144 SG  ? ? ? 1_555 B  CYS 148 SG ? ? B CYS 144  B CYS 148  1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf7  disulf ? ? C  CYS 4   SG  ? ? ? 1_555 D  CYS 137 SG ? ? C CYS 4    D CYS 137  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf8  disulf ? ? C  CYS 42  SG  ? ? ? 1_555 C  CYS 274 SG ? ? C CYS 42   C CYS 274  1_555 ? ? ? ? ? ? ? 2.013 ? 
disulf9  disulf ? ? C  CYS 55  SG  ? ? ? 1_555 C  CYS 67  SG ? ? C CYS 55   C CYS 67   1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf10 disulf ? ? C  CYS 90  SG  ? ? ? 1_555 C  CYS 135 SG ? ? C CYS 90   C CYS 135  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf11 disulf ? ? C  CYS 278 SG  ? ? ? 1_555 C  CYS 302 SG ? ? C CYS 278  C CYS 302  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf12 disulf ? ? D  CYS 144 SG  ? ? ? 1_555 D  CYS 148 SG ? ? D CYS 144  D CYS 148  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf13 disulf ? ? E  CYS 4   SG  ? ? ? 1_555 F  CYS 137 SG ? ? E CYS 4    F CYS 137  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf14 disulf ? ? E  CYS 42  SG  ? ? ? 1_555 E  CYS 274 SG ? ? E CYS 42   E CYS 274  1_555 ? ? ? ? ? ? ? 2.013 ? 
disulf15 disulf ? ? E  CYS 55  SG  ? ? ? 1_555 E  CYS 67  SG ? ? E CYS 55   E CYS 67   1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf16 disulf ? ? E  CYS 90  SG  ? ? ? 1_555 E  CYS 135 SG ? ? E CYS 90   E CYS 135  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf17 disulf ? ? E  CYS 278 SG  ? ? ? 1_555 E  CYS 302 SG ? ? E CYS 278  E CYS 302  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf18 disulf ? ? F  CYS 144 SG  ? ? ? 1_555 F  CYS 148 SG ? ? F CYS 144  F CYS 148  1_555 ? ? ? ? ? ? ? 2.031 ? 
covale1  covale ? ? A  ASN 23  ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 23   A NAG 1023 1_555 ? ? ? ? ? ? ? 1.459 ? 
covale2  covale ? ? A  ASN 165 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? A ASN 165  A NAG 1165 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale3  covale ? ? J  GLA .   C1  ? ? ? 1_555 K  NGS .   O4 ? ? A GLA 1323 A NGS 1324 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale4  covale ? ? J  GLA .   O3  ? ? ? 1_555 I  SIA .   C2 ? ? A GLA 1323 A SIA 1322 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale5  covale ? ? L  FUC .   C1  ? ? ? 1_555 K  NGS .   O3 ? ? A FUC 1325 A NGS 1324 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale6  covale ? ? B  ASN 154 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? B ASN 154  B NAG 1154 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale7  covale ? ? C  ASN 23  ND2 ? ? ? 1_555 O  NAG .   C1 ? ? C ASN 23   C NAG 1023 1_555 ? ? ? ? ? ? ? 1.457 ? 
covale8  covale ? ? C  ASN 165 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? C ASN 165  C NAG 1165 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale9  covale ? ? R  GLA .   O3  ? ? ? 1_555 Q  SIA .   C2 ? ? C GLA 1323 C SIA 1322 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale10 covale ? ? R  GLA .   C1  ? ? ? 1_555 S  NGS .   O4 ? ? C GLA 1323 C NGS 1324 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale11 covale ? ? T  FUC .   C1  ? ? ? 1_555 S  NGS .   O3 ? ? C FUC 1325 C NGS 1324 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale12 covale ? ? D  ASN 154 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? D ASN 154  D NAG 1154 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale13 covale ? ? E  ASN 23  ND2 ? ? ? 1_555 W  NAG .   C1 ? ? E ASN 23   E NAG 1023 1_555 ? ? ? ? ? ? ? 1.460 ? 
covale14 covale ? ? E  ASN 165 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? E ASN 165  E NAG 1165 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale15 covale ? ? Z  GLA .   O3  ? ? ? 1_555 Y  SIA .   C2 ? ? E GLA 1323 E SIA 1322 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale16 covale ? ? Z  GLA .   C1  ? ? ? 1_555 AA NGS .   O4 ? ? E GLA 1323 E NGS 1324 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale17 covale ? ? BA FUC .   C1  ? ? ? 1_555 AA NGS .   O3 ? ? E FUC 1325 E NGS 1324 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale18 covale ? ? F  ASN 154 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? F ASN 154  F NAG 1154 1_555 ? ? ? ? ? ? ? 1.449 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
BA ? 5 ? 
AA ? 2 ? 
AB ? 2 ? 
AC ? 3 ? 
AD ? 2 ? 
AE ? 3 ? 
AF ? 5 ? 
AG ? 5 ? 
AH ? 2 ? 
AI ? 4 ? 
AJ ? 2 ? 
DA ? 5 ? 
CA ? 2 ? 
CB ? 2 ? 
CC ? 3 ? 
CD ? 2 ? 
CE ? 3 ? 
CF ? 5 ? 
CG ? 5 ? 
CH ? 2 ? 
CI ? 4 ? 
CJ ? 2 ? 
FA ? 5 ? 
EA ? 2 ? 
EB ? 2 ? 
EC ? 3 ? 
ED ? 2 ? 
EE ? 3 ? 
EF ? 5 ? 
EG ? 5 ? 
EH ? 2 ? 
EI ? 4 ? 
EJ ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
AA 1 2 ? anti-parallel 
AB 1 2 ? anti-parallel 
AC 1 2 ? parallel      
AC 2 3 ? parallel      
AD 1 2 ? parallel      
AE 1 2 ? parallel      
AE 2 3 ? parallel      
AF 1 2 ? parallel      
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AF 4 5 ? anti-parallel 
AG 1 2 ? parallel      
AG 2 3 ? anti-parallel 
AG 3 4 ? anti-parallel 
AG 4 5 ? anti-parallel 
AH 1 2 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
AI 3 4 ? anti-parallel 
AJ 1 2 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 4 5 ? anti-parallel 
CA 1 2 ? anti-parallel 
CB 1 2 ? anti-parallel 
CC 1 2 ? parallel      
CC 2 3 ? parallel      
CD 1 2 ? parallel      
CE 1 2 ? parallel      
CE 2 3 ? parallel      
CF 1 2 ? parallel      
CF 2 3 ? anti-parallel 
CF 3 4 ? anti-parallel 
CF 4 5 ? anti-parallel 
CG 1 2 ? parallel      
CG 2 3 ? anti-parallel 
CG 3 4 ? anti-parallel 
CG 4 5 ? anti-parallel 
CH 1 2 ? anti-parallel 
CI 1 2 ? anti-parallel 
CI 2 3 ? anti-parallel 
CI 3 4 ? anti-parallel 
CJ 1 2 ? anti-parallel 
FA 1 2 ? anti-parallel 
FA 2 3 ? anti-parallel 
FA 3 4 ? anti-parallel 
FA 4 5 ? anti-parallel 
EA 1 2 ? anti-parallel 
EB 1 2 ? anti-parallel 
EC 1 2 ? parallel      
EC 2 3 ? parallel      
ED 1 2 ? parallel      
EE 1 2 ? parallel      
EE 2 3 ? parallel      
EF 1 2 ? parallel      
EF 2 3 ? anti-parallel 
EF 3 4 ? anti-parallel 
EF 4 5 ? anti-parallel 
EG 1 2 ? parallel      
EG 2 3 ? anti-parallel 
EG 3 4 ? anti-parallel 
EG 4 5 ? anti-parallel 
EH 1 2 ? anti-parallel 
EI 1 2 ? anti-parallel 
EI 2 3 ? anti-parallel 
EI 3 4 ? anti-parallel 
EJ 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
BA 1 SER B 32  ? ALA B 36  ? SER B 32  ALA B 36  
BA 2 TYR B 22  ? SER B 27  ? TYR B 22  SER B 27  
BA 3 GLN A 2   ? TYR A 7   ? GLN A 2   TYR A 7   
BA 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 
AA 1 GLN A 15  ? VAL A 16  ? GLN A 15  VAL A 16  
AA 2 VAL A 24  ? THR A 25  ? VAL A 24  THR A 25  
AB 1 ALA A 29  ? ASP A 31  ? ALA A 29  ASP A 31  
AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 
AC 1 LEU A 33  ? GLU A 34  ? LEU A 33  GLU A 34  
AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 
AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 
AD 1 ASP A 43  ? LEU A 44  ? ASP A 43  LEU A 44  
AD 2 ASN A 275 ? THR A 276 ? ASN A 275 THR A 276 
AE 1 LEU A 50  ? ILE A 51  ? LEU A 50  ILE A 51  
AE 2 ILE A 79  ? GLU A 81  ? ILE A 79  GLU A 81  
AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 
AF 1 GLY A 93  ? PHE A 95  ? GLY A 93  PHE A 95  
AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 
AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 
AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 
AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 
AG 1 GLY A 93  ? PHE A 95  ? GLY A 93  PHE A 95  
AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 
AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 
AG 4 TYR A 252 ? LYS A 258 ? TYR A 252 LYS A 258 
AG 5 HIS A 110 ? GLN A 115 ? HIS A 110 GLN A 115 
AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 
AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 
AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 
AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 
AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 
AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 
AJ 1 CYS A 278 ? GLN A 279 ? CYS A 278 GLN A 279 
AJ 2 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 300 
DA 1 SER D 32  ? ALA D 36  ? SER D 32  ALA D 36  
DA 2 TYR D 22  ? SER D 27  ? TYR D 22  SER D 27  
DA 3 GLN C 2   ? TYR C 7   ? GLN C 2   TYR C 7   
DA 4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
DA 5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
CA 1 GLN C 15  ? VAL C 16  ? GLN C 15  VAL C 16  
CA 2 VAL C 24  ? THR C 25  ? VAL C 24  THR C 25  
CB 1 ALA C 29  ? ASP C 31  ? ALA C 29  ASP C 31  
CB 2 VAL C 312 ? ALA C 314 ? VAL C 312 ALA C 314 
CC 1 LEU C 33  ? GLU C 34  ? LEU C 33  GLU C 34  
CC 2 PHE C 291 ? HIS C 292 ? PHE C 291 HIS C 292 
CC 3 LYS C 304 ? TYR C 305 ? LYS C 304 TYR C 305 
CD 1 ASP C 43  ? LEU C 44  ? ASP C 43  LEU C 44  
CD 2 ASN C 275 ? THR C 276 ? ASN C 275 THR C 276 
CE 1 LEU C 50  ? ILE C 51  ? LEU C 50  ILE C 51  
CE 2 ILE C 79  ? GLU C 81  ? ILE C 79  GLU C 81  
CE 3 ILE C 264 ? LYS C 266 ? ILE C 264 LYS C 266 
CF 1 GLY C 93  ? PHE C 95  ? GLY C 93  PHE C 95  
CF 2 ARG C 225 ? LEU C 233 ? ARG C 225 LEU C 233 
CF 3 LEU C 172 ? HIS C 180 ? LEU C 172 HIS C 180 
CF 4 PHE C 247 ? PRO C 250 ? PHE C 247 PRO C 250 
CF 5 VAL C 147 ? TRP C 149 ? VAL C 147 TRP C 149 
CG 1 GLY C 93  ? PHE C 95  ? GLY C 93  PHE C 95  
CG 2 ARG C 225 ? LEU C 233 ? ARG C 225 LEU C 233 
CG 3 LEU C 172 ? HIS C 180 ? LEU C 172 HIS C 180 
CG 4 TYR C 252 ? LYS C 258 ? TYR C 252 LYS C 258 
CG 5 HIS C 110 ? GLN C 115 ? HIS C 110 GLN C 115 
CH 1 SER C 132 ? TYR C 137 ? SER C 132 TYR C 137 
CH 2 LYS C 140 ? SER C 142 ? LYS C 140 SER C 142 
CI 1 ILE C 160 ? ASN C 165 ? ILE C 160 ASN C 165 
CI 2 ALA C 238 ? SER C 243 ? ALA C 238 SER C 243 
CI 3 ILE C 198 ? GLY C 201 ? ILE C 198 GLY C 201 
CI 4 ASN C 206 ? LEU C 209 ? ASN C 206 LEU C 209 
CJ 1 CYS C 278 ? GLN C 279 ? CYS C 278 GLN C 279 
CJ 2 ILE C 299 ? GLY C 300 ? ILE C 299 GLY C 300 
FA 1 SER F 32  ? ALA F 36  ? SER F 32  ALA F 36  
FA 2 TYR F 22  ? SER F 27  ? TYR F 22  SER F 27  
FA 3 GLN E 2   ? TYR E 7   ? GLN E 2   TYR E 7   
FA 4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
FA 5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
EA 1 GLN E 15  ? VAL E 16  ? GLN E 15  VAL E 16  
EA 2 VAL E 24  ? THR E 25  ? VAL E 24  THR E 25  
EB 1 ALA E 29  ? ASP E 31  ? ALA E 29  ASP E 31  
EB 2 VAL E 312 ? ALA E 314 ? VAL E 312 ALA E 314 
EC 1 LEU E 33  ? GLU E 34  ? LEU E 33  GLU E 34  
EC 2 PHE E 291 ? HIS E 292 ? PHE E 291 HIS E 292 
EC 3 LYS E 304 ? TYR E 305 ? LYS E 304 TYR E 305 
ED 1 ASP E 43  ? LEU E 44  ? ASP E 43  LEU E 44  
ED 2 ASN E 275 ? THR E 276 ? ASN E 275 THR E 276 
EE 1 LEU E 50  ? ILE E 51  ? LEU E 50  ILE E 51  
EE 2 ILE E 79  ? GLU E 81  ? ILE E 79  GLU E 81  
EE 3 ILE E 264 ? LYS E 266 ? ILE E 264 LYS E 266 
EF 1 GLY E 93  ? PHE E 95  ? GLY E 93  PHE E 95  
EF 2 ARG E 225 ? LEU E 233 ? ARG E 225 LEU E 233 
EF 3 LEU E 172 ? HIS E 180 ? LEU E 172 HIS E 180 
EF 4 PHE E 247 ? PRO E 250 ? PHE E 247 PRO E 250 
EF 5 VAL E 147 ? TRP E 149 ? VAL E 147 TRP E 149 
EG 1 GLY E 93  ? PHE E 95  ? GLY E 93  PHE E 95  
EG 2 ARG E 225 ? LEU E 233 ? ARG E 225 LEU E 233 
EG 3 LEU E 172 ? HIS E 180 ? LEU E 172 HIS E 180 
EG 4 TYR E 252 ? LYS E 258 ? TYR E 252 LYS E 258 
EG 5 HIS E 110 ? GLN E 115 ? HIS E 110 GLN E 115 
EH 1 SER E 132 ? TYR E 137 ? SER E 132 TYR E 137 
EH 2 LYS E 140 ? SER E 142 ? LYS E 140 SER E 142 
EI 1 ILE E 160 ? ASN E 165 ? ILE E 160 ASN E 165 
EI 2 ALA E 238 ? SER E 243 ? ALA E 238 SER E 243 
EI 3 ILE E 198 ? GLY E 201 ? ILE E 198 GLY E 201 
EI 4 ASN E 206 ? LEU E 209 ? ASN E 206 LEU E 209 
EJ 1 CYS E 278 ? GLN E 279 ? CYS E 278 GLN E 279 
EJ 2 ILE E 299 ? GLY E 300 ? ILE E 299 GLY E 300 
# 
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 
BA 1 2 N ALA B 35  ? N ALA B 35  O TYR B 24  ? O TYR B 24  
BA 2 3 N SER B 27  ? N SER B 27  O GLN A 2   ? O GLN A 2   
BA 3 4 N ILE A 3   ? N ILE A 3   O PHE B 138 ? O PHE B 138 
BA 4 5 N GLU B 139 ? N GLU B 139 O LYS B 131 ? O LYS B 131 
AA 1 2 N VAL A 16  ? N VAL A 16  O VAL A 24  ? O VAL A 24  
AB 1 2 N GLN A 30  ? N GLN A 30  O LEU A 313 ? O LEU A 313 
AC 1 2 N GLU A 34  ? N GLU A 34  O PHE A 291 ? O PHE A 291 
AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 
AD 1 2 O ASP A 43  ? O ASP A 43  N THR A 276 ? N THR A 276 
AE 1 2 O LEU A 50  ? O LEU A 50  N VAL A 80  ? N VAL A 80  
AE 2 3 N GLU A 81  ? N GLU A 81  O MET A 265 ? O MET A 265 
AF 1 2 N ASP A 94  ? N ASP A 94  O MET A 226 ? O MET A 226 
AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 
AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 
AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 
AG 1 2 N ASP A 94  ? N ASP A 94  O MET A 226 ? O MET A 226 
AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 
AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 
AG 4 5 N LYS A 258 ? N LYS A 258 O HIS A 110 ? O HIS A 110 
AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 
AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 
AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 
AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 
AJ 1 2 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 299 
DA 1 2 N ALA D 35  ? N ALA D 35  O TYR D 24  ? O TYR D 24  
DA 2 3 N SER D 27  ? N SER D 27  O GLN C 2   ? O GLN C 2   
DA 3 4 N ILE C 3   ? N ILE C 3   O PHE D 138 ? O PHE D 138 
DA 4 5 N GLU D 139 ? N GLU D 139 O LYS D 131 ? O LYS D 131 
CA 1 2 N VAL C 16  ? N VAL C 16  O VAL C 24  ? O VAL C 24  
CB 1 2 N GLN C 30  ? N GLN C 30  O LEU C 313 ? O LEU C 313 
CC 1 2 N GLU C 34  ? N GLU C 34  O PHE C 291 ? O PHE C 291 
CC 2 3 N HIS C 292 ? N HIS C 292 O LYS C 304 ? O LYS C 304 
CD 1 2 O ASP C 43  ? O ASP C 43  N THR C 276 ? N THR C 276 
CE 1 2 O LEU C 50  ? O LEU C 50  N VAL C 80  ? N VAL C 80  
CE 2 3 N GLU C 81  ? N GLU C 81  O MET C 265 ? O MET C 265 
CF 1 2 N ASP C 94  ? N ASP C 94  O MET C 226 ? O MET C 226 
CF 2 3 N LEU C 233 ? N LEU C 233 O LEU C 172 ? O LEU C 172 
CF 3 4 N GLY C 177 ? N GLY C 177 O ILE C 248 ? O ILE C 248 
CF 4 5 N ALA C 249 ? N ALA C 249 O VAL C 148 ? O VAL C 148 
CG 1 2 N ASP C 94  ? N ASP C 94  O MET C 226 ? O MET C 226 
CG 2 3 N LEU C 233 ? N LEU C 233 O LEU C 172 ? O LEU C 172 
CG 3 4 N LEU C 173 ? N LEU C 173 O TYR C 254 ? O TYR C 254 
CG 4 5 N LYS C 258 ? N LYS C 258 O HIS C 110 ? O HIS C 110 
CH 1 2 N TYR C 137 ? N TYR C 137 O LYS C 140 ? O LYS C 140 
CI 1 2 N TYR C 164 ? N TYR C 164 O ILE C 239 ? O ILE C 239 
CI 2 3 N GLU C 242 ? N GLU C 242 O SER C 199 ? O SER C 199 
CI 3 4 N VAL C 200 ? N VAL C 200 O GLN C 207 ? O GLN C 207 
CJ 1 2 N GLN C 279 ? N GLN C 279 O ILE C 299 ? O ILE C 299 
FA 1 2 N ALA F 35  ? N ALA F 35  O TYR F 24  ? O TYR F 24  
FA 2 3 N SER F 27  ? N SER F 27  O GLN E 2   ? O GLN E 2   
FA 3 4 N ILE E 3   ? N ILE E 3   O PHE F 138 ? O PHE F 138 
FA 4 5 N GLU F 139 ? N GLU F 139 O LYS F 131 ? O LYS F 131 
EA 1 2 N VAL E 16  ? N VAL E 16  O VAL E 24  ? O VAL E 24  
EB 1 2 N GLN E 30  ? N GLN E 30  O LEU E 313 ? O LEU E 313 
EC 1 2 N GLU E 34  ? N GLU E 34  O PHE E 291 ? O PHE E 291 
EC 2 3 N HIS E 292 ? N HIS E 292 O LYS E 304 ? O LYS E 304 
ED 1 2 O ASP E 43  ? O ASP E 43  N THR E 276 ? N THR E 276 
EE 1 2 O LEU E 50  ? O LEU E 50  N VAL E 80  ? N VAL E 80  
EE 2 3 N GLU E 81  ? N GLU E 81  O MET E 265 ? O MET E 265 
EF 1 2 N ASP E 94  ? N ASP E 94  O MET E 226 ? O MET E 226 
EF 2 3 N LEU E 233 ? N LEU E 233 O LEU E 172 ? O LEU E 172 
EF 3 4 N GLY E 177 ? N GLY E 177 O ILE E 248 ? O ILE E 248 
EF 4 5 N ALA E 249 ? N ALA E 249 O VAL E 148 ? O VAL E 148 
EG 1 2 N ASP E 94  ? N ASP E 94  O MET E 226 ? O MET E 226 
EG 2 3 N LEU E 233 ? N LEU E 233 O LEU E 172 ? O LEU E 172 
EG 3 4 N LEU E 173 ? N LEU E 173 O TYR E 254 ? O TYR E 254 
EG 4 5 N LYS E 258 ? N LYS E 258 O HIS E 110 ? O HIS E 110 
EH 1 2 N TYR E 137 ? N TYR E 137 O LYS E 140 ? O LYS E 140 
EI 1 2 N TYR E 164 ? N TYR E 164 O ILE E 239 ? O ILE E 239 
EI 2 3 N GLU E 242 ? N GLU E 242 O SER E 199 ? O SER E 199 
EI 3 4 N VAL E 200 ? N VAL E 200 O GLN E 207 ? O GLN E 207 
EJ 1 2 N GLN E 279 ? N GLN E 279 O ILE E 299 ? O ILE E 299 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE EPE F 1164'                           
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE EPE B 1164'                           
AC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE EPE D 1164'                           
AC4 Software ? ? ? ? 13 'BINDING SITE FOR LINKED RESIDUES A 1322 A 1323 A 1324 A 1325'  
AC5 Software ? ? ? ? 13 'BINDING SITE FOR LINKED RESIDUES C 1322 C 1323 C 1324 C 1325'  
AC6 Software ? ? ? ? 13 'BINDING SITE FOR LINKED RESIDUES E 1322 E 1323 E 1324 E 1325'  
AC7 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1023 bound to ASN A 23'  
AC8 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1165 bound to ASN A 165' 
AC9 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG B1154 bound to ASN B 154' 
BC1 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1023 bound to ASN C 23'  
BC2 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1165 bound to ASN C 165' 
BC3 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG D1154 bound to ASN D 154' 
BC4 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG E1023 bound to ASN E 23'  
BC5 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG E1165 bound to ASN E 165' 
BC6 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG F1154 bound to ASN F 154' 
# 
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  TRP F  14  ? TRP F 14   . ? 1_555 ? 
2  AC1 4  HIS F  25  ? HIS F 25   . ? 1_555 ? 
3  AC1 4  TYR F  34  ? TYR F 34   . ? 1_555 ? 
4  AC1 4  ASN F  135 ? ASN F 135  . ? 1_555 ? 
5  AC2 4  TRP B  14  ? TRP B 14   . ? 1_555 ? 
6  AC2 4  HIS B  25  ? HIS B 25   . ? 1_555 ? 
7  AC2 4  TYR B  34  ? TYR B 34   . ? 1_555 ? 
8  AC2 4  ASN B  135 ? ASN B 135  . ? 1_555 ? 
9  AC3 3  TRP D  14  ? TRP D 14   . ? 1_555 ? 
10 AC3 3  HIS D  25  ? HIS D 25   . ? 1_555 ? 
11 AC3 3  ASN D  135 ? ASN D 135  . ? 1_555 ? 
12 AC4 13 TYR A  91  ? TYR A 91   . ? 1_555 ? 
13 AC4 13 LEU A  129 ? LEU A 129  . ? 1_555 ? 
14 AC4 13 VAL A  131 ? VAL A 131  . ? 1_555 ? 
15 AC4 13 SER A  132 ? SER A 132  . ? 1_555 ? 
16 AC4 13 SER A  133 ? SER A 133  . ? 1_555 ? 
17 AC4 13 HIS A  179 ? HIS A 179  . ? 1_555 ? 
18 AC4 13 ASN A  182 ? ASN A 182  . ? 1_555 ? 
19 AC4 13 GLU A  186 ? GLU A 186  . ? 1_555 ? 
20 AC4 13 LYS A  189 ? LYS A 189  . ? 1_555 ? 
21 AC4 13 LEU A  190 ? LEU A 190  . ? 1_555 ? 
22 AC4 13 LYS A  218 ? LYS A 218  . ? 1_555 ? 
23 AC4 13 GLN A  222 ? GLN A 222  . ? 1_555 ? 
24 AC4 13 HOH EA .   ? HOH A 2032 . ? 1_555 ? 
25 AC5 13 TYR C  91  ? TYR C 91   . ? 1_555 ? 
26 AC5 13 LEU C  129 ? LEU C 129  . ? 1_555 ? 
27 AC5 13 VAL C  131 ? VAL C 131  . ? 1_555 ? 
28 AC5 13 SER C  132 ? SER C 132  . ? 1_555 ? 
29 AC5 13 SER C  133 ? SER C 133  . ? 1_555 ? 
30 AC5 13 HIS C  179 ? HIS C 179  . ? 1_555 ? 
31 AC5 13 ASN C  182 ? ASN C 182  . ? 1_555 ? 
32 AC5 13 GLU C  186 ? GLU C 186  . ? 1_555 ? 
33 AC5 13 LYS C  189 ? LYS C 189  . ? 1_555 ? 
34 AC5 13 LEU C  190 ? LEU C 190  . ? 1_555 ? 
35 AC5 13 LYS C  218 ? LYS C 218  . ? 1_555 ? 
36 AC5 13 GLN C  222 ? GLN C 222  . ? 1_555 ? 
37 AC5 13 HOH GA .   ? HOH C 2024 . ? 1_555 ? 
38 AC6 13 TYR E  91  ? TYR E 91   . ? 1_555 ? 
39 AC6 13 LEU E  129 ? LEU E 129  . ? 1_555 ? 
40 AC6 13 VAL E  131 ? VAL E 131  . ? 1_555 ? 
41 AC6 13 SER E  132 ? SER E 132  . ? 1_555 ? 
42 AC6 13 SER E  133 ? SER E 133  . ? 1_555 ? 
43 AC6 13 HIS E  179 ? HIS E 179  . ? 1_555 ? 
44 AC6 13 ASN E  182 ? ASN E 182  . ? 1_555 ? 
45 AC6 13 GLU E  186 ? GLU E 186  . ? 1_555 ? 
46 AC6 13 LYS E  189 ? LYS E 189  . ? 1_555 ? 
47 AC6 13 LEU E  190 ? LEU E 190  . ? 1_555 ? 
48 AC6 13 LYS E  218 ? LYS E 218  . ? 1_555 ? 
49 AC6 13 GLN E  222 ? GLN E 222  . ? 1_555 ? 
50 AC6 13 HOH IA .   ? HOH E 2028 . ? 1_555 ? 
51 AC7 2  LYS A  22  ? LYS A 22   . ? 1_555 ? 
52 AC7 2  ASN A  23  ? ASN A 23   . ? 1_555 ? 
53 AC8 2  ASN A  165 ? ASN A 165  . ? 1_555 ? 
54 AC8 2  ASN A  236 ? ASN A 236  . ? 1_555 ? 
55 AC9 3  GLU B  147 ? GLU B 147  . ? 1_555 ? 
56 AC9 3  GLU B  150 ? GLU B 150  . ? 1_555 ? 
57 AC9 3  ASN B  154 ? ASN B 154  . ? 1_555 ? 
58 BC1 2  LYS C  22  ? LYS C 22   . ? 1_555 ? 
59 BC1 2  ASN C  23  ? ASN C 23   . ? 1_555 ? 
60 BC2 2  ASN C  165 ? ASN C 165  . ? 1_555 ? 
61 BC2 2  ASN C  236 ? ASN C 236  . ? 1_555 ? 
62 BC3 3  GLU D  147 ? GLU D 147  . ? 1_555 ? 
63 BC3 3  GLU D  150 ? GLU D 150  . ? 1_555 ? 
64 BC3 3  ASN D  154 ? ASN D 154  . ? 1_555 ? 
65 BC4 2  LYS E  22  ? LYS E 22   . ? 1_555 ? 
66 BC4 2  ASN E  23  ? ASN E 23   . ? 1_555 ? 
67 BC5 2  ASN E  165 ? ASN E 165  . ? 1_555 ? 
68 BC5 2  ASN E  236 ? ASN E 236  . ? 1_555 ? 
69 BC6 3  GLU F  147 ? GLU F 147  . ? 1_555 ? 
70 BC6 3  GLU F  150 ? GLU F 150  . ? 1_555 ? 
71 BC6 3  ASN F  154 ? ASN F 154  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3ZNL 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3ZNL 
_atom_sites.fract_transf_matrix[1][1]   0.005682 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002218 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009843 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006652 
_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   . ASP A  1 1   ? 10.526  56.185 -8.582  1.00 34.47  ? 1    ASP A N   1 
ATOM   2     C CA  . ASP A  1 1   ? 10.107  55.387 -7.396  1.00 34.90  ? 1    ASP A CA  1 
ATOM   3     C C   . ASP A  1 1   ? 11.247  55.279 -6.389  1.00 31.79  ? 1    ASP A C   1 
ATOM   4     O O   . ASP A  1 1   ? 12.413  55.214 -6.775  1.00 29.61  ? 1    ASP A O   1 
ATOM   5     C CB  . ASP A  1 1   ? 9.645   53.989 -7.821  1.00 36.91  ? 1    ASP A CB  1 
ATOM   6     C CG  . ASP A  1 1   ? 8.478   54.027 -8.794  1.00 40.48  ? 1    ASP A CG  1 
ATOM   7     O OD1 . ASP A  1 1   ? 7.987   55.131 -9.115  1.00 41.44  ? 1    ASP A OD1 1 
ATOM   8     O OD2 . ASP A  1 1   ? 8.050   52.945 -9.242  1.00 42.64  ? 1    ASP A OD2 1 
ATOM   9     N N   . GLN A  1 2   ? 10.906  55.270 -5.102  1.00 31.79  ? 2    GLN A N   1 
ATOM   10    C CA  . GLN A  1 2   ? 11.912  55.177 -4.044  1.00 29.15  ? 2    GLN A CA  1 
ATOM   11    C C   . GLN A  1 2   ? 11.385  54.560 -2.752  1.00 29.74  ? 2    GLN A C   1 
ATOM   12    O O   . GLN A  1 2   ? 10.203  54.665 -2.434  1.00 31.98  ? 2    GLN A O   1 
ATOM   13    C CB  . GLN A  1 2   ? 12.507  56.558 -3.738  1.00 27.52  ? 2    GLN A CB  1 
ATOM   14    C CG  . GLN A  1 2   ? 11.569  57.525 -3.032  1.00 28.94  ? 2    GLN A CG  1 
ATOM   15    C CD  . GLN A  1 2   ? 12.280  58.761 -2.510  1.00 27.43  ? 2    GLN A CD  1 
ATOM   16    O OE1 . GLN A  1 2   ? 11.945  59.260 -1.443  1.00 27.77  ? 2    GLN A OE1 1 
ATOM   17    N NE2 . GLN A  1 2   ? 13.249  59.268 -3.264  1.00 26.11  ? 2    GLN A NE2 1 
ATOM   18    N N   . ILE A  1 3   ? 12.289  53.917 -2.019  1.00 27.89  ? 3    ILE A N   1 
ATOM   19    C CA  . ILE A  1 3   ? 11.998  53.402 -0.686  1.00 28.07  ? 3    ILE A CA  1 
ATOM   20    C C   . ILE A  1 3   ? 12.985  54.013 0.303   1.00 25.46  ? 3    ILE A C   1 
ATOM   21    O O   . ILE A  1 3   ? 14.172  54.116 0.013   1.00 23.55  ? 3    ILE A O   1 
ATOM   22    C CB  . ILE A  1 3   ? 12.054  51.856 -0.639  1.00 29.06  ? 3    ILE A CB  1 
ATOM   23    C CG1 . ILE A  1 3   ? 11.436  51.341 0.666   1.00 30.06  ? 3    ILE A CG1 1 
ATOM   24    C CG2 . ILE A  1 3   ? 13.482  51.345 -0.795  1.00 27.02  ? 3    ILE A CG2 1 
ATOM   25    C CD1 . ILE A  1 3   ? 11.090  49.869 0.640   1.00 32.25  ? 3    ILE A CD1 1 
ATOM   26    N N   . CYS A  1 4   ? 12.484  54.423 1.464   1.00 25.66  ? 4    CYS A N   1 
ATOM   27    C CA  . CYS A  1 4   ? 13.310  55.067 2.479   1.00 23.60  ? 4    CYS A CA  1 
ATOM   28    C C   . CYS A  1 4   ? 13.283  54.278 3.767   1.00 23.37  ? 4    CYS A C   1 
ATOM   29    O O   . CYS A  1 4   ? 12.323  53.564 4.038   1.00 25.22  ? 4    CYS A O   1 
ATOM   30    C CB  . CYS A  1 4   ? 12.814  56.482 2.763   1.00 24.10  ? 4    CYS A CB  1 
ATOM   31    S SG  . CYS A  1 4   ? 12.636  57.515 1.299   1.00 25.04  ? 4    CYS A SG  1 
ATOM   32    N N   . ILE A  1 5   ? 14.345  54.419 4.554   1.00 21.31  ? 5    ILE A N   1 
ATOM   33    C CA  . ILE A  1 5   ? 14.395  53.864 5.897   1.00 20.98  ? 5    ILE A CA  1 
ATOM   34    C C   . ILE A  1 5   ? 14.345  55.021 6.883   1.00 20.23  ? 5    ILE A C   1 
ATOM   35    O O   . ILE A  1 5   ? 15.007  56.039 6.690   1.00 19.16  ? 5    ILE A O   1 
ATOM   36    C CB  . ILE A  1 5   ? 15.678  53.054 6.129   1.00 19.69  ? 5    ILE A CB  1 
ATOM   37    C CG1 . ILE A  1 5   ? 15.827  51.983 5.052   1.00 20.57  ? 5    ILE A CG1 1 
ATOM   38    C CG2 . ILE A  1 5   ? 15.680  52.422 7.515   1.00 19.73  ? 5    ILE A CG2 1 
ATOM   39    C CD1 . ILE A  1 5   ? 14.814  50.872 5.153   1.00 22.82  ? 5    ILE A CD1 1 
ATOM   40    N N   . GLY A  1 6   ? 13.555  54.855 7.938   1.00 21.02  ? 6    GLY A N   1 
ATOM   41    C CA  . GLY A  1 6   ? 13.356  55.915 8.913   1.00 20.70  ? 6    GLY A CA  1 
ATOM   42    C C   . GLY A  1 6   ? 12.838  55.400 10.230  1.00 21.18  ? 6    GLY A C   1 
ATOM   43    O O   . GLY A  1 6   ? 12.662  54.200 10.418  1.00 21.76  ? 6    GLY A O   1 
ATOM   44    N N   . TYR A  1 7   ? 12.574  56.326 11.137  1.00 21.16  ? 7    TYR A N   1 
ATOM   45    C CA  . TYR A  1 7   ? 12.268  55.981 12.513  1.00 21.33  ? 7    TYR A CA  1 
ATOM   46    C C   . TYR A  1 7   ? 11.117  56.812 13.064  1.00 23.01  ? 7    TYR A C   1 
ATOM   47    O O   . TYR A  1 7   ? 10.729  57.827 12.487  1.00 23.87  ? 7    TYR A O   1 
ATOM   48    C CB  . TYR A  1 7   ? 13.518  56.139 13.383  1.00 19.31  ? 7    TYR A CB  1 
ATOM   49    C CG  . TYR A  1 7   ? 14.178  57.504 13.312  1.00 18.44  ? 7    TYR A CG  1 
ATOM   50    C CD1 . TYR A  1 7   ? 15.115  57.803 12.330  1.00 17.48  ? 7    TYR A CD1 1 
ATOM   51    C CD2 . TYR A  1 7   ? 13.876  58.488 14.240  1.00 18.85  ? 7    TYR A CD2 1 
ATOM   52    C CE1 . TYR A  1 7   ? 15.718  59.047 12.269  1.00 17.11  ? 7    TYR A CE1 1 
ATOM   53    C CE2 . TYR A  1 7   ? 14.478  59.732 14.188  1.00 18.54  ? 7    TYR A CE2 1 
ATOM   54    C CZ  . TYR A  1 7   ? 15.395  60.005 13.202  1.00 17.72  ? 7    TYR A CZ  1 
ATOM   55    O OH  . TYR A  1 7   ? 15.979  61.247 13.157  1.00 17.84  ? 7    TYR A OH  1 
ATOM   56    N N   . HIS A  1 8   ? 10.586  56.359 14.192  1.00 23.71  ? 8    HIS A N   1 
ATOM   57    C CA  . HIS A  1 8   ? 9.384   56.923 14.793  1.00 25.75  ? 8    HIS A CA  1 
ATOM   58    C C   . HIS A  1 8   ? 9.632   58.301 15.399  1.00 25.36  ? 8    HIS A C   1 
ATOM   59    O O   . HIS A  1 8   ? 10.699  58.562 15.941  1.00 23.47  ? 8    HIS A O   1 
ATOM   60    C CB  . HIS A  1 8   ? 8.869   55.957 15.871  1.00 26.50  ? 8    HIS A CB  1 
ATOM   61    C CG  . HIS A  1 8   ? 7.586   56.380 16.518  1.00 28.86  ? 8    HIS A CG  1 
ATOM   62    N ND1 . HIS A  1 8   ? 6.396   56.465 15.829  1.00 31.64  ? 8    HIS A ND1 1 
ATOM   63    C CD2 . HIS A  1 8   ? 7.303   56.714 17.799  1.00 29.10  ? 8    HIS A CD2 1 
ATOM   64    C CE1 . HIS A  1 8   ? 5.438   56.850 16.653  1.00 33.60  ? 8    HIS A CE1 1 
ATOM   65    N NE2 . HIS A  1 8   ? 5.963   57.006 17.855  1.00 32.02  ? 8    HIS A NE2 1 
ATOM   66    N N   . ALA A  1 9   ? 8.644   59.183 15.276  1.00 27.58  ? 9    ALA A N   1 
ATOM   67    C CA  . ALA A  1 9   ? 8.601   60.430 16.036  1.00 28.10  ? 9    ALA A CA  1 
ATOM   68    C C   . ALA A  1 9   ? 7.187   60.598 16.562  1.00 31.03  ? 9    ALA A C   1 
ATOM   69    O O   . ALA A  1 9   ? 6.267   59.935 16.091  1.00 32.83  ? 9    ALA A O   1 
ATOM   70    C CB  . ALA A  1 9   ? 8.990   61.609 15.167  1.00 28.27  ? 9    ALA A CB  1 
ATOM   71    N N   . ASN A  1 10  ? 7.014   61.468 17.550  1.00 31.83  ? 10   ASN A N   1 
ATOM   72    C CA  . ASN A  1 10  ? 5.695   61.712 18.119  1.00 34.90  ? 10   ASN A CA  1 
ATOM   73    C C   . ASN A  1 10  ? 5.630   63.046 18.854  1.00 36.15  ? 10   ASN A C   1 
ATOM   74    O O   . ASN A  1 10  ? 6.599   63.802 18.853  1.00 34.76  ? 10   ASN A O   1 
ATOM   75    C CB  . ASN A  1 10  ? 5.277   60.548 19.033  1.00 34.84  ? 10   ASN A CB  1 
ATOM   76    C CG  . ASN A  1 10  ? 6.123   60.442 20.286  1.00 32.55  ? 10   ASN A CG  1 
ATOM   77    O OD1 . ASN A  1 10  ? 6.955   61.299 20.574  1.00 31.26  ? 10   ASN A OD1 1 
ATOM   78    N ND2 . ASN A  1 10  ? 5.909   59.378 21.042  1.00 32.32  ? 10   ASN A ND2 1 
ATOM   79    N N   . ASN A  1 11  ? 4.485   63.325 19.476  1.00 39.16  ? 11   ASN A N   1 
ATOM   80    C CA  . ASN A  1 11  ? 4.258   64.595 20.164  1.00 41.09  ? 11   ASN A CA  1 
ATOM   81    C C   . ASN A  1 11  ? 4.707   64.593 21.638  1.00 39.71  ? 11   ASN A C   1 
ATOM   82    O O   . ASN A  1 11  ? 4.274   65.441 22.420  1.00 41.67  ? 11   ASN A O   1 
ATOM   83    C CB  . ASN A  1 11  ? 2.778   65.002 20.033  1.00 45.47  ? 11   ASN A CB  1 
ATOM   84    C CG  . ASN A  1 11  ? 1.826   64.022 20.707  1.00 46.76  ? 11   ASN A CG  1 
ATOM   85    O OD1 . ASN A  1 11  ? 2.254   63.059 21.349  1.00 44.43  ? 11   ASN A OD1 1 
ATOM   86    N ND2 . ASN A  1 11  ? 0.520   64.267 20.565  1.00 50.85  ? 11   ASN A ND2 1 
ATOM   87    N N   . SER A  1 12  ? 5.582   63.653 22.002  1.00 36.58  ? 12   SER A N   1 
ATOM   88    C CA  . SER A  1 12  ? 6.100   63.535 23.368  1.00 35.14  ? 12   SER A CA  1 
ATOM   89    C C   . SER A  1 12  ? 7.089   64.652 23.675  1.00 34.43  ? 12   SER A C   1 
ATOM   90    O O   . SER A  1 12  ? 7.836   65.083 22.799  1.00 33.63  ? 12   SER A O   1 
ATOM   91    C CB  . SER A  1 12  ? 6.792   62.180 23.568  1.00 32.36  ? 12   SER A CB  1 
ATOM   92    O OG  . SER A  1 12  ? 7.328   62.043 24.874  1.00 31.03  ? 12   SER A OG  1 
ATOM   93    N N   . THR A  1 13  ? 7.072   65.117 24.925  1.00 35.03  ? 13   THR A N   1 
ATOM   94    C CA  . THR A  1 13  ? 8.026   66.112 25.426  1.00 34.63  ? 13   THR A CA  1 
ATOM   95    C C   . THR A  1 13  ? 8.851   65.576 26.599  1.00 32.48  ? 13   THR A C   1 
ATOM   96    O O   . THR A  1 13  ? 9.593   66.331 27.225  1.00 32.44  ? 13   THR A O   1 
ATOM   97    C CB  . THR A  1 13  ? 7.304   67.395 25.887  1.00 37.94  ? 13   THR A CB  1 
ATOM   98    O OG1 . THR A  1 13  ? 6.225   67.051 26.766  1.00 39.44  ? 13   THR A OG1 1 
ATOM   99    C CG2 . THR A  1 13  ? 6.766   68.170 24.693  1.00 40.36  ? 13   THR A CG2 1 
ATOM   100   N N   . GLU A  1 14  ? 8.725   64.283 26.895  1.00 31.04  ? 14   GLU A N   1 
ATOM   101   C CA  . GLU A  1 14  ? 9.503   63.665 27.967  1.00 29.14  ? 14   GLU A CA  1 
ATOM   102   C C   . GLU A  1 14  ? 10.993  63.716 27.655  1.00 27.00  ? 14   GLU A C   1 
ATOM   103   O O   . GLU A  1 14  ? 11.409  63.397 26.543  1.00 26.08  ? 14   GLU A O   1 
ATOM   104   C CB  . GLU A  1 14  ? 9.092   62.211 28.178  1.00 28.40  ? 14   GLU A CB  1 
ATOM   105   C CG  . GLU A  1 14  ? 7.710   62.033 28.781  1.00 30.65  ? 14   GLU A CG  1 
ATOM   106   C CD  . GLU A  1 14  ? 7.670   60.915 29.812  1.00 29.96  ? 14   GLU A CD  1 
ATOM   107   O OE1 . GLU A  1 14  ? 8.173   61.135 30.946  1.00 29.34  ? 14   GLU A OE1 1 
ATOM   108   O OE2 . GLU A  1 14  ? 7.153   59.816 29.485  1.00 30.26  ? 14   GLU A OE2 1 
ATOM   109   N N   . GLN A  1 15  ? 11.787  64.108 28.646  1.00 26.46  ? 15   GLN A N   1 
ATOM   110   C CA  . GLN A  1 15  ? 13.225  64.240 28.479  1.00 24.98  ? 15   GLN A CA  1 
ATOM   111   C C   . GLN A  1 15  ? 13.966  63.302 29.411  1.00 23.30  ? 15   GLN A C   1 
ATOM   112   O O   . GLN A  1 15  ? 13.452  62.930 30.462  1.00 23.49  ? 15   GLN A O   1 
ATOM   113   C CB  . GLN A  1 15  ? 13.655  65.671 28.773  1.00 26.53  ? 15   GLN A CB  1 
ATOM   114   C CG  . GLN A  1 15  ? 12.902  66.716 27.973  1.00 28.72  ? 15   GLN A CG  1 
ATOM   115   C CD  . GLN A  1 15  ? 13.393  68.115 28.250  1.00 30.61  ? 15   GLN A CD  1 
ATOM   116   O OE1 . GLN A  1 15  ? 13.567  68.910 27.332  1.00 31.77  ? 15   GLN A OE1 1 
ATOM   117   N NE2 . GLN A  1 15  ? 13.623  68.423 29.517  1.00 31.20  ? 15   GLN A NE2 1 
ATOM   118   N N   . VAL A  1 16  ? 15.177  62.923 29.014  1.00 21.82  ? 16   VAL A N   1 
ATOM   119   C CA  . VAL A  1 16  ? 16.053  62.116 29.854  1.00 20.64  ? 16   VAL A CA  1 
ATOM   120   C C   . VAL A  1 16  ? 17.452  62.696 29.801  1.00 20.55  ? 16   VAL A C   1 
ATOM   121   O O   . VAL A  1 16  ? 17.802  63.379 28.839  1.00 20.92  ? 16   VAL A O   1 
ATOM   122   C CB  . VAL A  1 16  ? 16.097  60.642 29.406  1.00 19.32  ? 16   VAL A CB  1 
ATOM   123   C CG1 . VAL A  1 16  ? 14.698  60.041 29.410  1.00 19.86  ? 16   VAL A CG1 1 
ATOM   124   C CG2 . VAL A  1 16  ? 16.733  60.504 28.032  1.00 18.61  ? 16   VAL A CG2 1 
ATOM   125   N N   . ASP A  1 17  ? 18.244  62.428 30.836  1.00 20.36  ? 17   ASP A N   1 
ATOM   126   C CA  . ASP A  1 17  ? 19.637  62.858 30.880  1.00 20.62  ? 17   ASP A CA  1 
ATOM   127   C C   . ASP A  1 17  ? 20.561  61.703 30.511  1.00 19.45  ? 17   ASP A C   1 
ATOM   128   O O   . ASP A  1 17  ? 20.247  60.533 30.740  1.00 18.56  ? 17   ASP A O   1 
ATOM   129   C CB  . ASP A  1 17  ? 20.003  63.385 32.271  1.00 21.71  ? 17   ASP A CB  1 
ATOM   130   C CG  . ASP A  1 17  ? 19.358  64.732 32.593  1.00 23.47  ? 17   ASP A CG  1 
ATOM   131   O OD1 . ASP A  1 17  ? 19.146  65.557 31.678  1.00 24.30  ? 17   ASP A OD1 1 
ATOM   132   O OD2 . ASP A  1 17  ? 19.078  64.974 33.789  1.00 24.26  ? 17   ASP A OD2 1 
ATOM   133   N N   . THR A  1 18  ? 21.700  62.060 29.928  1.00 19.82  ? 18   THR A N   1 
ATOM   134   C CA  . THR A  1 18  ? 22.787  61.134 29.631  1.00 19.32  ? 18   THR A CA  1 
ATOM   135   C C   . THR A  1 18  ? 24.081  61.788 30.104  1.00 20.80  ? 18   THR A C   1 
ATOM   136   O O   . THR A  1 18  ? 24.064  62.913 30.596  1.00 22.09  ? 18   THR A O   1 
ATOM   137   C CB  . THR A  1 18  ? 22.886  60.850 28.120  1.00 18.54  ? 18   THR A CB  1 
ATOM   138   O OG1 . THR A  1 18  ? 23.334  62.022 27.435  1.00 19.37  ? 18   THR A OG1 1 
ATOM   139   C CG2 . THR A  1 18  ? 21.544  60.432 27.561  1.00 17.68  ? 18   THR A CG2 1 
ATOM   140   N N   . ILE A  1 19  ? 25.202  61.095 29.949  1.00 21.07  ? 19   ILE A N   1 
ATOM   141   C CA  . ILE A  1 19  ? 26.494  61.634 30.375  1.00 22.93  ? 19   ILE A CA  1 
ATOM   142   C C   . ILE A  1 19  ? 26.848  62.902 29.585  1.00 24.24  ? 19   ILE A C   1 
ATOM   143   O O   . ILE A  1 19  ? 27.188  63.932 30.163  1.00 25.97  ? 19   ILE A O   1 
ATOM   144   C CB  . ILE A  1 19  ? 27.624  60.593 30.197  1.00 23.17  ? 19   ILE A CB  1 
ATOM   145   C CG1 . ILE A  1 19  ? 27.398  59.366 31.095  1.00 22.65  ? 19   ILE A CG1 1 
ATOM   146   C CG2 . ILE A  1 19  ? 28.986  61.209 30.490  1.00 25.40  ? 19   ILE A CG2 1 
ATOM   147   C CD1 . ILE A  1 19  ? 27.675  59.593 32.567  1.00 23.87  ? 19   ILE A CD1 1 
ATOM   148   N N   . MET A  1 20  ? 26.751  62.815 28.260  1.00 23.69  ? 20   MET A N   1 
ATOM   149   C CA  . MET A  1 20  ? 27.196  63.892 27.378  1.00 25.07  ? 20   MET A CA  1 
ATOM   150   C C   . MET A  1 20  ? 26.145  64.956 27.102  1.00 25.63  ? 20   MET A C   1 
ATOM   151   O O   . MET A  1 20  ? 26.484  66.050 26.648  1.00 27.24  ? 20   MET A O   1 
ATOM   152   C CB  . MET A  1 20  ? 27.639  63.318 26.040  1.00 24.21  ? 20   MET A CB  1 
ATOM   153   C CG  . MET A  1 20  ? 28.838  62.399 26.120  1.00 24.61  ? 20   MET A CG  1 
ATOM   154   S SD  . MET A  1 20  ? 29.499  62.111 24.480  1.00 24.39  ? 20   MET A SD  1 
ATOM   155   C CE  . MET A  1 20  ? 30.478  60.639 24.765  1.00 24.68  ? 20   MET A CE  1 
ATOM   156   N N   . GLU A  1 21  ? 24.876  64.638 27.342  1.00 24.78  ? 21   GLU A N   1 
ATOM   157   C CA  . GLU A  1 21  ? 23.798  65.560 27.020  1.00 25.63  ? 21   GLU A CA  1 
ATOM   158   C C   . GLU A  1 21  ? 22.653  65.441 28.015  1.00 25.82  ? 21   GLU A C   1 
ATOM   159   O O   . GLU A  1 21  ? 22.260  64.339 28.401  1.00 24.36  ? 21   GLU A O   1 
ATOM   160   C CB  . GLU A  1 21  ? 23.291  65.300 25.602  1.00 24.49  ? 21   GLU A CB  1 
ATOM   161   C CG  . GLU A  1 21  ? 22.560  66.483 24.981  1.00 25.75  ? 21   GLU A CG  1 
ATOM   162   C CD  . GLU A  1 21  ? 22.137  66.241 23.534  1.00 24.84  ? 21   GLU A CD  1 
ATOM   163   O OE1 . GLU A  1 21  ? 22.582  65.239 22.923  1.00 23.27  ? 21   GLU A OE1 1 
ATOM   164   O OE2 . GLU A  1 21  ? 21.352  67.062 23.007  1.00 25.86  ? 21   GLU A OE2 1 
ATOM   165   N N   . LYS A  1 22  ? 22.120  66.591 28.416  1.00 28.10  ? 22   LYS A N   1 
ATOM   166   C CA  . LYS A  1 22  ? 21.009  66.642 29.348  1.00 28.83  ? 22   LYS A CA  1 
ATOM   167   C C   . LYS A  1 22  ? 19.757  67.149 28.654  1.00 29.86  ? 22   LYS A C   1 
ATOM   168   O O   . LYS A  1 22  ? 19.843  67.820 27.632  1.00 30.71  ? 22   LYS A O   1 
ATOM   169   C CB  . LYS A  1 22  ? 21.373  67.527 30.538  1.00 30.92  ? 22   LYS A CB  1 
ATOM   170   C CG  . LYS A  1 22  ? 22.311  66.839 31.521  1.00 30.58  ? 22   LYS A CG  1 
ATOM   171   C CD  . LYS A  1 22  ? 23.101  67.834 32.354  1.00 33.19  ? 22   LYS A CD  1 
ATOM   172   C CE  . LYS A  1 22  ? 22.183  68.771 33.129  1.00 35.01  ? 22   LYS A CE  1 
ATOM   173   N NZ  . LYS A  1 22  ? 22.878  69.481 34.241  1.00 37.35  ? 22   LYS A NZ  1 
ATOM   174   N N   . ASN A  1 23  ? 18.599  66.813 29.215  1.00 30.36  ? 23   ASN A N   1 
ATOM   175   C CA  . ASN A  1 23  ? 17.311  67.250 28.683  1.00 31.86  ? 23   ASN A CA  1 
ATOM   176   C C   . ASN A  1 23  ? 17.103  66.832 27.220  1.00 29.97  ? 23   ASN A C   1 
ATOM   177   O O   . ASN A  1 23  ? 16.688  67.633 26.385  1.00 31.12  ? 23   ASN A O   1 
ATOM   178   C CB  . ASN A  1 23  ? 17.151  68.772 28.861  1.00 36.16  ? 23   ASN A CB  1 
ATOM   179   C CG  . ASN A  1 23  ? 17.073  69.191 30.322  1.00 39.48  ? 23   ASN A CG  1 
ATOM   180   O OD1 . ASN A  1 23  ? 16.785  68.375 31.202  1.00 38.47  ? 23   ASN A OD1 1 
ATOM   181   N ND2 . ASN A  1 23  ? 17.324  70.485 30.588  1.00 44.93  ? 23   ASN A ND2 1 
ATOM   182   N N   . VAL A  1 24  ? 17.397  65.566 26.929  1.00 27.02  ? 24   VAL A N   1 
ATOM   183   C CA  . VAL A  1 24  ? 17.176  64.983 25.598  1.00 25.44  ? 24   VAL A CA  1 
ATOM   184   C C   . VAL A  1 24  ? 15.728  64.508 25.458  1.00 25.18  ? 24   VAL A C   1 
ATOM   185   O O   . VAL A  1 24  ? 15.299  63.616 26.184  1.00 24.50  ? 24   VAL A O   1 
ATOM   186   C CB  . VAL A  1 24  ? 18.108  63.770 25.357  1.00 23.45  ? 24   VAL A CB  1 
ATOM   187   C CG1 . VAL A  1 24  ? 17.750  63.056 24.061  1.00 22.57  ? 24   VAL A CG1 1 
ATOM   188   C CG2 . VAL A  1 24  ? 19.565  64.206 25.340  1.00 23.54  ? 24   VAL A CG2 1 
ATOM   189   N N   . THR A  1 25  ? 14.984  65.093 24.523  1.00 25.84  ? 25   THR A N   1 
ATOM   190   C CA  . THR A  1 25  ? 13.578  64.735 24.329  1.00 26.31  ? 25   THR A CA  1 
ATOM   191   C C   . THR A  1 25  ? 13.464  63.381 23.643  1.00 24.56  ? 25   THR A C   1 
ATOM   192   O O   . THR A  1 25  ? 14.043  63.183 22.574  1.00 23.67  ? 25   THR A O   1 
ATOM   193   C CB  . THR A  1 25  ? 12.829  65.766 23.463  1.00 28.39  ? 25   THR A CB  1 
ATOM   194   O OG1 . THR A  1 25  ? 13.128  67.092 23.913  1.00 30.08  ? 25   THR A OG1 1 
ATOM   195   C CG2 . THR A  1 25  ? 11.332  65.535 23.540  1.00 29.94  ? 25   THR A CG2 1 
ATOM   196   N N   . VAL A  1 26  ? 12.706  62.467 24.249  1.00 24.21  ? 26   VAL A N   1 
ATOM   197   C CA  . VAL A  1 26  ? 12.541  61.112 23.715  1.00 23.05  ? 26   VAL A CA  1 
ATOM   198   C C   . VAL A  1 26  ? 11.080  60.793 23.450  1.00 24.57  ? 26   VAL A C   1 
ATOM   199   O O   . VAL A  1 26  ? 10.186  61.455 23.972  1.00 26.31  ? 26   VAL A O   1 
ATOM   200   C CB  . VAL A  1 26  ? 13.130  60.038 24.651  1.00 21.68  ? 26   VAL A CB  1 
ATOM   201   C CG1 . VAL A  1 26  ? 14.632  60.216 24.770  1.00 20.30  ? 26   VAL A CG1 1 
ATOM   202   C CG2 . VAL A  1 26  ? 12.471  60.071 26.023  1.00 22.50  ? 26   VAL A CG2 1 
ATOM   203   N N   . THR A  1 27  ? 10.852  59.768 22.638  1.00 24.17  ? 27   THR A N   1 
ATOM   204   C CA  . THR A  1 27  ? 9.503   59.381 22.256  1.00 26.03  ? 27   THR A CA  1 
ATOM   205   C C   . THR A  1 27  ? 8.806   58.622 23.375  1.00 26.74  ? 27   THR A C   1 
ATOM   206   O O   . THR A  1 27  ? 7.593   58.736 23.536  1.00 29.02  ? 27   THR A O   1 
ATOM   207   C CB  . THR A  1 27  ? 9.476   58.521 20.974  1.00 25.88  ? 27   THR A CB  1 
ATOM   208   O OG1 . THR A  1 27  ? 10.108  57.260 21.212  1.00 24.53  ? 27   THR A OG1 1 
ATOM   209   C CG2 . THR A  1 27  ? 10.172  59.233 19.826  1.00 25.10  ? 27   THR A CG2 1 
ATOM   210   N N   . HIS A  1 28  ? 9.564   57.835 24.132  1.00 25.10  ? 28   HIS A N   1 
ATOM   211   C CA  . HIS A  1 28  ? 9.014   57.085 25.262  1.00 25.73  ? 28   HIS A CA  1 
ATOM   212   C C   . HIS A  1 28  ? 10.003  57.047 26.405  1.00 24.13  ? 28   HIS A C   1 
ATOM   213   O O   . HIS A  1 28  ? 11.210  57.001 26.190  1.00 22.47  ? 28   HIS A O   1 
ATOM   214   C CB  . HIS A  1 28  ? 8.674   55.657 24.849  1.00 26.29  ? 28   HIS A CB  1 
ATOM   215   C CG  . HIS A  1 28  ? 7.749   55.575 23.678  1.00 28.07  ? 28   HIS A CG  1 
ATOM   216   N ND1 . HIS A  1 28  ? 8.187   55.685 22.377  1.00 27.39  ? 28   HIS A ND1 1 
ATOM   217   C CD2 . HIS A  1 28  ? 6.406   55.415 23.612  1.00 30.73  ? 28   HIS A CD2 1 
ATOM   218   C CE1 . HIS A  1 28  ? 7.155   55.588 21.560  1.00 29.53  ? 28   HIS A CE1 1 
ATOM   219   N NE2 . HIS A  1 28  ? 6.063   55.423 22.283  1.00 31.68  ? 28   HIS A NE2 1 
ATOM   220   N N   . ALA A  1 29  ? 9.486   57.045 27.623  1.00 24.92  ? 29   ALA A N   1 
ATOM   221   C CA  . ALA A  1 29  ? 10.327  57.017 28.808  1.00 23.74  ? 29   ALA A CA  1 
ATOM   222   C C   . ALA A  1 29  ? 9.616   56.259 29.917  1.00 24.77  ? 29   ALA A C   1 
ATOM   223   O O   . ALA A  1 29  ? 8.445   55.897 29.782  1.00 26.60  ? 29   ALA A O   1 
ATOM   224   C CB  . ALA A  1 29  ? 10.654  58.432 29.255  1.00 23.64  ? 29   ALA A CB  1 
ATOM   225   N N   . GLN A  1 30  ? 10.331  56.012 31.007  1.00 23.87  ? 30   GLN A N   1 
ATOM   226   C CA  . GLN A  1 30  ? 9.742   55.363 32.169  1.00 24.81  ? 30   GLN A CA  1 
ATOM   227   C C   . GLN A  1 30  ? 10.306  55.940 33.458  1.00 24.14  ? 30   GLN A C   1 
ATOM   228   O O   . GLN A  1 30  ? 11.467  55.714 33.794  1.00 22.78  ? 30   GLN A O   1 
ATOM   229   C CB  . GLN A  1 30  ? 9.970   53.852 32.124  1.00 24.83  ? 30   GLN A CB  1 
ATOM   230   C CG  . GLN A  1 30  ? 9.206   53.107 33.211  1.00 26.24  ? 30   GLN A CG  1 
ATOM   231   C CD  . GLN A  1 30  ? 9.186   51.607 33.010  1.00 27.07  ? 30   GLN A CD  1 
ATOM   232   O OE1 . GLN A  1 30  ? 9.297   51.115 31.891  1.00 27.26  ? 30   GLN A OE1 1 
ATOM   233   N NE2 . GLN A  1 30  ? 9.030   50.871 34.102  1.00 27.88  ? 30   GLN A NE2 1 
ATOM   234   N N   . ASP A  1 31  ? 9.471   56.696 34.167  1.00 25.38  ? 31   ASP A N   1 
ATOM   235   C CA  . ASP A  1 31  ? 9.811   57.188 35.496  1.00 25.18  ? 31   ASP A CA  1 
ATOM   236   C C   . ASP A  1 31  ? 9.849   55.990 36.445  1.00 25.10  ? 31   ASP A C   1 
ATOM   237   O O   . ASP A  1 31  ? 8.933   55.160 36.442  1.00 26.33  ? 31   ASP A O   1 
ATOM   238   C CB  . ASP A  1 31  ? 8.774   58.214 35.963  1.00 26.96  ? 31   ASP A CB  1 
ATOM   239   C CG  . ASP A  1 31  ? 9.240   59.026 37.156  1.00 26.87  ? 31   ASP A CG  1 
ATOM   240   O OD1 . ASP A  1 31  ? 10.158  58.585 37.877  1.00 25.67  ? 31   ASP A OD1 1 
ATOM   241   O OD2 . ASP A  1 31  ? 8.680   60.119 37.372  1.00 28.33  ? 31   ASP A OD2 1 
ATOM   242   N N   . ILE A  1 32  ? 10.920  55.901 37.233  1.00 23.95  ? 32   ILE A N   1 
ATOM   243   C CA  . ILE A  1 32  ? 11.101  54.806 38.193  1.00 24.01  ? 32   ILE A CA  1 
ATOM   244   C C   . ILE A  1 32  ? 11.208  55.285 39.649  1.00 24.21  ? 32   ILE A C   1 
ATOM   245   O O   . ILE A  1 32  ? 11.433  54.485 40.555  1.00 24.31  ? 32   ILE A O   1 
ATOM   246   C CB  . ILE A  1 32  ? 12.336  53.954 37.838  1.00 22.89  ? 32   ILE A CB  1 
ATOM   247   C CG1 . ILE A  1 32  ? 13.569  54.835 37.617  1.00 21.68  ? 32   ILE A CG1 1 
ATOM   248   C CG2 . ILE A  1 32  ? 12.053  53.127 36.599  1.00 23.17  ? 32   ILE A CG2 1 
ATOM   249   C CD1 . ILE A  1 32  ? 14.878  54.079 37.683  1.00 21.03  ? 32   ILE A CD1 1 
ATOM   250   N N   . LEU A  1 33  ? 11.025  56.584 39.865  1.00 24.55  ? 33   LEU A N   1 
ATOM   251   C CA  . LEU A  1 33  ? 11.116  57.184 41.187  1.00 24.96  ? 33   LEU A CA  1 
ATOM   252   C C   . LEU A  1 33  ? 9.732   57.595 41.674  1.00 26.75  ? 33   LEU A C   1 
ATOM   253   O O   . LEU A  1 33  ? 9.070   58.421 41.045  1.00 27.70  ? 33   LEU A O   1 
ATOM   254   C CB  . LEU A  1 33  ? 12.016  58.418 41.127  1.00 24.51  ? 33   LEU A CB  1 
ATOM   255   C CG  . LEU A  1 33  ? 12.321  59.116 42.447  1.00 25.00  ? 33   LEU A CG  1 
ATOM   256   C CD1 . LEU A  1 33  ? 13.195  58.225 43.313  1.00 24.29  ? 33   LEU A CD1 1 
ATOM   257   C CD2 . LEU A  1 33  ? 12.996  60.454 42.197  1.00 25.27  ? 33   LEU A CD2 1 
ATOM   258   N N   . GLU A  1 34  ? 9.300   57.023 42.795  1.00 27.52  ? 34   GLU A N   1 
ATOM   259   C CA  . GLU A  1 34  ? 8.040   57.420 43.422  1.00 29.45  ? 34   GLU A CA  1 
ATOM   260   C C   . GLU A  1 34  ? 8.255   58.678 44.255  1.00 29.92  ? 34   GLU A C   1 
ATOM   261   O O   . GLU A  1 34  ? 9.053   58.679 45.184  1.00 29.23  ? 34   GLU A O   1 
ATOM   262   C CB  . GLU A  1 34  ? 7.483   56.297 44.298  1.00 30.21  ? 34   GLU A CB  1 
ATOM   263   C CG  . GLU A  1 34  ? 6.158   56.634 44.961  1.00 32.40  ? 34   GLU A CG  1 
ATOM   264   C CD  . GLU A  1 34  ? 5.171   57.265 44.000  1.00 33.98  ? 34   GLU A CD  1 
ATOM   265   O OE1 . GLU A  1 34  ? 4.675   56.558 43.099  1.00 34.59  ? 34   GLU A OE1 1 
ATOM   266   O OE2 . GLU A  1 34  ? 4.913   58.480 44.135  1.00 34.92  ? 34   GLU A OE2 1 
ATOM   267   N N   . LYS A  1 35  ? 7.526   59.739 43.923  1.00 31.51  ? 35   LYS A N   1 
ATOM   268   C CA  . LYS A  1 35  ? 7.746   61.063 44.518  1.00 32.41  ? 35   LYS A CA  1 
ATOM   269   C C   . LYS A  1 35  ? 6.644   61.514 45.485  1.00 34.70  ? 35   LYS A C   1 
ATOM   270   O O   . LYS A  1 35  ? 6.820   62.521 46.171  1.00 35.64  ? 35   LYS A O   1 
ATOM   271   C CB  . LYS A  1 35  ? 7.920   62.115 43.407  1.00 32.82  ? 35   LYS A CB  1 
ATOM   272   C CG  . LYS A  1 35  ? 9.338   62.238 42.872  1.00 31.00  ? 35   LYS A CG  1 
ATOM   273   C CD  . LYS A  1 35  ? 9.417   63.175 41.673  1.00 31.56  ? 35   LYS A CD  1 
ATOM   274   C CE  . LYS A  1 35  ? 9.555   62.430 40.349  1.00 30.26  ? 35   LYS A CE  1 
ATOM   275   N NZ  . LYS A  1 35  ? 8.529   61.374 40.126  1.00 30.52  ? 35   LYS A NZ  1 
ATOM   276   N N   . THR A  1 36  ? 5.536   60.770 45.563  1.00 35.90  ? 36   THR A N   1 
ATOM   277   C CA  . THR A  1 36  ? 4.364   61.197 46.346  1.00 38.51  ? 36   THR A CA  1 
ATOM   278   C C   . THR A  1 36  ? 3.979   60.256 47.491  1.00 38.82  ? 36   THR A C   1 
ATOM   279   O O   . THR A  1 36  ? 4.328   59.077 47.493  1.00 37.47  ? 36   THR A O   1 
ATOM   280   C CB  . THR A  1 36  ? 3.122   61.364 45.447  1.00 40.77  ? 36   THR A CB  1 
ATOM   281   O OG1 . THR A  1 36  ? 2.735   60.093 44.909  1.00 40.42  ? 36   THR A OG1 1 
ATOM   282   C CG2 . THR A  1 36  ? 3.407   62.336 44.314  1.00 40.93  ? 36   THR A CG2 1 
ATOM   283   N N   . HIS A  1 37  ? 3.245   60.811 48.456  1.00 40.97  ? 37   HIS A N   1 
ATOM   284   C CA  . HIS A  1 37  ? 2.668   60.061 49.576  1.00 41.86  ? 37   HIS A CA  1 
ATOM   285   C C   . HIS A  1 37  ? 1.342   60.715 49.982  1.00 45.26  ? 37   HIS A C   1 
ATOM   286   O O   . HIS A  1 37  ? 1.072   61.855 49.598  1.00 46.79  ? 37   HIS A O   1 
ATOM   287   C CB  . HIS A  1 37  ? 3.637   60.039 50.762  1.00 40.34  ? 37   HIS A CB  1 
ATOM   288   C CG  . HIS A  1 37  ? 4.049   61.399 51.232  1.00 40.89  ? 37   HIS A CG  1 
ATOM   289   N ND1 . HIS A  1 37  ? 3.559   61.964 52.389  1.00 42.64  ? 37   HIS A ND1 1 
ATOM   290   C CD2 . HIS A  1 37  ? 4.901   62.309 50.702  1.00 40.22  ? 37   HIS A CD2 1 
ATOM   291   C CE1 . HIS A  1 37  ? 4.092   63.161 52.556  1.00 43.13  ? 37   HIS A CE1 1 
ATOM   292   N NE2 . HIS A  1 37  ? 4.911   63.395 51.545  1.00 41.75  ? 37   HIS A NE2 1 
ATOM   293   N N   . ASN A  1 38  ? 0.517   60.002 50.750  1.00 46.78  ? 38   ASN A N   1 
ATOM   294   C CA  . ASN A  1 38  ? -0.787  60.541 51.181  1.00 50.35  ? 38   ASN A CA  1 
ATOM   295   C C   . ASN A  1 38  ? -0.702  61.510 52.374  1.00 51.34  ? 38   ASN A C   1 
ATOM   296   O O   . ASN A  1 38  ? -1.675  62.203 52.686  1.00 54.46  ? 38   ASN A O   1 
ATOM   297   C CB  . ASN A  1 38  ? -1.801  59.412 51.460  1.00 52.05  ? 38   ASN A CB  1 
ATOM   298   C CG  . ASN A  1 38  ? -1.435  58.555 52.661  1.00 50.82  ? 38   ASN A CG  1 
ATOM   299   O OD1 . ASN A  1 38  ? -0.552  58.894 53.448  1.00 49.08  ? 38   ASN A OD1 1 
ATOM   300   N ND2 . ASN A  1 38  ? -2.126  57.433 52.806  1.00 52.05  ? 38   ASN A ND2 1 
ATOM   301   N N   . GLY A  1 39  ? 0.450   61.537 53.041  1.00 49.05  ? 39   GLY A N   1 
ATOM   302   C CA  . GLY A  1 39  ? 0.715   62.499 54.118  1.00 49.88  ? 39   GLY A CA  1 
ATOM   303   C C   . GLY A  1 39  ? 0.172   62.074 55.469  1.00 51.07  ? 39   GLY A C   1 
ATOM   304   O O   . GLY A  1 39  ? 0.038   62.901 56.376  1.00 52.54  ? 39   GLY A O   1 
ATOM   305   N N   . LYS A  1 40  ? -0.117  60.781 55.609  1.00 50.64  ? 40   LYS A N   1 
ATOM   306   C CA  . LYS A  1 40  ? -0.819  60.263 56.776  1.00 52.23  ? 40   LYS A CA  1 
ATOM   307   C C   . LYS A  1 40  ? -0.134  59.043 57.384  1.00 50.18  ? 40   LYS A C   1 
ATOM   308   O O   . LYS A  1 40  ? 0.512   58.261 56.685  1.00 48.21  ? 40   LYS A O   1 
ATOM   309   C CB  . LYS A  1 40  ? -2.255  59.901 56.389  1.00 55.25  ? 40   LYS A CB  1 
ATOM   310   C CG  . LYS A  1 40  ? -3.146  61.109 56.157  1.00 58.46  ? 40   LYS A CG  1 
ATOM   311   C CD  . LYS A  1 40  ? -4.340  60.783 55.278  1.00 61.23  ? 40   LYS A CD  1 
ATOM   312   C CE  . LYS A  1 40  ? -5.110  62.048 54.930  1.00 64.59  ? 40   LYS A CE  1 
ATOM   313   N NZ  . LYS A  1 40  ? -6.230  61.796 53.983  1.00 67.59  ? 40   LYS A NZ  1 
ATOM   314   N N   . LEU A  1 41  ? -0.306  58.888 58.695  1.00 51.02  ? 41   LEU A N   1 
ATOM   315   C CA  . LEU A  1 41  ? 0.116   57.690 59.419  1.00 49.87  ? 41   LEU A CA  1 
ATOM   316   C C   . LEU A  1 41  ? -1.045  56.694 59.365  1.00 52.01  ? 41   LEU A C   1 
ATOM   317   O O   . LEU A  1 41  ? -2.207  57.071 59.568  1.00 54.84  ? 41   LEU A O   1 
ATOM   318   C CB  . LEU A  1 41  ? 0.481   58.045 60.864  1.00 49.87  ? 41   LEU A CB  1 
ATOM   319   C CG  . LEU A  1 41  ? 1.748   58.895 61.116  1.00 48.14  ? 41   LEU A CG  1 
ATOM   320   C CD1 . LEU A  1 41  ? 2.880   58.058 61.706  1.00 46.04  ? 41   LEU A CD1 1 
ATOM   321   C CD2 . LEU A  1 41  ? 2.249   59.637 59.876  1.00 47.26  ? 41   LEU A CD2 1 
ATOM   322   N N   . CYS A  1 42  ? -0.734  55.431 59.078  1.00 51.05  ? 42   CYS A N   1 
ATOM   323   C CA  . CYS A  1 42  ? -1.750  54.492 58.610  1.00 53.23  ? 42   CYS A CA  1 
ATOM   324   C C   . CYS A  1 42  ? -1.545  53.049 59.037  1.00 52.99  ? 42   CYS A C   1 
ATOM   325   O O   . CYS A  1 42  ? -0.434  52.635 59.370  1.00 50.79  ? 42   CYS A O   1 
ATOM   326   C CB  . CYS A  1 42  ? -1.791  54.544 57.087  1.00 53.09  ? 42   CYS A CB  1 
ATOM   327   S SG  . CYS A  1 42  ? -2.500  56.070 56.442  1.00 54.91  ? 42   CYS A SG  1 
ATOM   328   N N   . ASP A  1 43  ? -2.633  52.284 58.991  1.00 55.68  ? 43   ASP A N   1 
ATOM   329   C CA  . ASP A  1 43  ? -2.599  50.858 59.289  1.00 56.28  ? 43   ASP A CA  1 
ATOM   330   C C   . ASP A  1 43  ? -1.731  50.145 58.265  1.00 54.39  ? 43   ASP A C   1 
ATOM   331   O O   . ASP A  1 43  ? -1.838  50.408 57.068  1.00 54.19  ? 43   ASP A O   1 
ATOM   332   C CB  . ASP A  1 43  ? -4.014  50.264 59.273  1.00 60.26  ? 43   ASP A CB  1 
ATOM   333   C CG  . ASP A  1 43  ? -4.904  50.818 60.382  1.00 62.49  ? 43   ASP A CG  1 
ATOM   334   O OD1 . ASP A  1 43  ? -4.453  51.701 61.140  1.00 60.94  ? 43   ASP A OD1 1 
ATOM   335   O OD2 . ASP A  1 43  ? -6.065  50.370 60.493  1.00 66.06  ? 43   ASP A OD2 1 
ATOM   336   N N   . LEU A  1 44  ? -0.865  49.256 58.742  1.00 53.20  ? 44   LEU A N   1 
ATOM   337   C CA  . LEU A  1 44  ? 0.017   48.489 57.868  1.00 51.79  ? 44   LEU A CA  1 
ATOM   338   C C   . LEU A  1 44  ? -0.541  47.083 57.686  1.00 54.46  ? 44   LEU A C   1 
ATOM   339   O O   . LEU A  1 44  ? -0.601  46.306 58.638  1.00 55.76  ? 44   LEU A O   1 
ATOM   340   C CB  . LEU A  1 44  ? 1.433   48.416 58.448  1.00 49.18  ? 44   LEU A CB  1 
ATOM   341   C CG  . LEU A  1 44  ? 2.515   47.879 57.502  1.00 47.48  ? 44   LEU A CG  1 
ATOM   342   C CD1 . LEU A  1 44  ? 2.966   48.963 56.530  1.00 45.37  ? 44   LEU A CD1 1 
ATOM   343   C CD2 . LEU A  1 44  ? 3.707   47.337 58.277  1.00 46.31  ? 44   LEU A CD2 1 
ATOM   344   N N   . ASP A  1 45  ? -0.944  46.766 56.458  1.00 55.52  ? 45   ASP A N   1 
ATOM   345   C CA  . ASP A  1 45  ? -1.489  45.450 56.127  1.00 58.47  ? 45   ASP A CA  1 
ATOM   346   C C   . ASP A  1 45  ? -2.742  45.160 56.958  1.00 61.99  ? 45   ASP A C   1 
ATOM   347   O O   . ASP A  1 45  ? -2.998  44.012 57.331  1.00 64.46  ? 45   ASP A O   1 
ATOM   348   C CB  . ASP A  1 45  ? -0.423  44.367 56.359  1.00 57.77  ? 45   ASP A CB  1 
ATOM   349   C CG  . ASP A  1 45  ? -0.478  43.263 55.325  1.00 59.60  ? 45   ASP A CG  1 
ATOM   350   O OD1 . ASP A  1 45  ? 0.119   43.449 54.241  1.00 57.85  ? 45   ASP A OD1 1 
ATOM   351   O OD2 . ASP A  1 45  ? -1.096  42.213 55.599  1.00 62.96  ? 45   ASP A OD2 1 
ATOM   352   N N   . GLY A  1 46  ? -3.506  46.213 57.253  1.00 62.46  ? 46   GLY A N   1 
ATOM   353   C CA  . GLY A  1 46  ? -4.687  46.117 58.117  1.00 65.78  ? 46   GLY A CA  1 
ATOM   354   C C   . GLY A  1 46  ? -4.411  46.348 59.597  1.00 64.84  ? 46   GLY A C   1 
ATOM   355   O O   . GLY A  1 46  ? -5.300  46.790 60.326  1.00 66.83  ? 46   GLY A O   1 
ATOM   356   N N   . VAL A  1 47  ? -3.184  46.063 60.038  1.00 62.00  ? 47   VAL A N   1 
ATOM   357   C CA  . VAL A  1 47  ? -2.824  46.088 61.463  1.00 61.28  ? 47   VAL A CA  1 
ATOM   358   C C   . VAL A  1 47  ? -2.448  47.506 61.910  1.00 58.76  ? 47   VAL A C   1 
ATOM   359   O O   . VAL A  1 47  ? -1.504  48.098 61.389  1.00 55.83  ? 47   VAL A O   1 
ATOM   360   C CB  . VAL A  1 47  ? -1.655  45.119 61.757  1.00 59.91  ? 47   VAL A CB  1 
ATOM   361   C CG1 . VAL A  1 47  ? -1.320  45.105 63.242  1.00 59.58  ? 47   VAL A CG1 1 
ATOM   362   C CG2 . VAL A  1 47  ? -1.991  43.711 61.281  1.00 62.74  ? 47   VAL A CG2 1 
ATOM   363   N N   . LYS A  1 48  ? -3.177  48.029 62.894  1.00 60.17  ? 48   LYS A N   1 
ATOM   364   C CA  . LYS A  1 48  ? -3.034  49.424 63.321  1.00 58.66  ? 48   LYS A CA  1 
ATOM   365   C C   . LYS A  1 48  ? -1.717  49.684 64.056  1.00 55.61  ? 48   LYS A C   1 
ATOM   366   O O   . LYS A  1 48  ? -1.248  48.829 64.810  1.00 55.50  ? 48   LYS A O   1 
ATOM   367   C CB  . LYS A  1 48  ? -4.204  49.826 64.233  1.00 61.52  ? 48   LYS A CB  1 
ATOM   368   C CG  . LYS A  1 48  ? -4.349  51.328 64.443  1.00 61.05  ? 48   LYS A CG  1 
ATOM   369   C CD  . LYS A  1 48  ? -5.241  51.674 65.622  1.00 63.55  ? 48   LYS A CD  1 
ATOM   370   C CE  . LYS A  1 48  ? -5.564  53.162 65.632  1.00 63.95  ? 48   LYS A CE  1 
ATOM   371   N NZ  . LYS A  1 48  ? -6.116  53.614 66.940  1.00 65.75  ? 48   LYS A NZ  1 
ATOM   372   N N   . PRO A  1 49  ? -1.117  50.870 63.841  1.00 53.44  ? 49   PRO A N   1 
ATOM   373   C CA  . PRO A  1 49  ? 0.051   51.242 64.640  1.00 51.13  ? 49   PRO A CA  1 
ATOM   374   C C   . PRO A  1 49  ? -0.321  51.641 66.056  1.00 52.15  ? 49   PRO A C   1 
ATOM   375   O O   . PRO A  1 49  ? -1.407  52.180 66.278  1.00 54.21  ? 49   PRO A O   1 
ATOM   376   C CB  . PRO A  1 49  ? 0.605   52.467 63.906  1.00 49.30  ? 49   PRO A CB  1 
ATOM   377   C CG  . PRO A  1 49  ? -0.577  53.053 63.211  1.00 51.21  ? 49   PRO A CG  1 
ATOM   378   C CD  . PRO A  1 49  ? -1.382  51.862 62.778  1.00 53.18  ? 49   PRO A CD  1 
ATOM   379   N N   . LEU A  1 50  ? 0.584   51.388 66.996  1.00 50.89  ? 50   LEU A N   1 
ATOM   380   C CA  . LEU A  1 50  ? 0.442   51.893 68.353  1.00 51.50  ? 50   LEU A CA  1 
ATOM   381   C C   . LEU A  1 50  ? 0.881   53.349 68.359  1.00 50.32  ? 50   LEU A C   1 
ATOM   382   O O   . LEU A  1 50  ? 2.076   53.638 68.338  1.00 48.35  ? 50   LEU A O   1 
ATOM   383   C CB  . LEU A  1 50  ? 1.288   51.071 69.332  1.00 50.88  ? 50   LEU A CB  1 
ATOM   384   C CG  . LEU A  1 50  ? 1.432   51.574 70.775  1.00 51.14  ? 50   LEU A CG  1 
ATOM   385   C CD1 . LEU A  1 50  ? 0.093   51.968 71.383  1.00 53.55  ? 50   LEU A CD1 1 
ATOM   386   C CD2 . LEU A  1 50  ? 2.109   50.513 71.631  1.00 51.08  ? 50   LEU A CD2 1 
ATOM   387   N N   . ILE A  1 51  ? -0.085  54.261 68.362  1.00 51.94  ? 51   ILE A N   1 
ATOM   388   C CA  . ILE A  1 51  ? 0.211   55.690 68.395  1.00 51.54  ? 51   ILE A CA  1 
ATOM   389   C C   . ILE A  1 51  ? 0.165   56.179 69.836  1.00 52.48  ? 51   ILE A C   1 
ATOM   390   O O   . ILE A  1 51  ? -0.913  56.323 70.418  1.00 54.81  ? 51   ILE A O   1 
ATOM   391   C CB  . ILE A  1 51  ? -0.767  56.496 67.512  1.00 53.17  ? 51   ILE A CB  1 
ATOM   392   C CG1 . ILE A  1 51  ? -0.663  55.999 66.065  1.00 52.22  ? 51   ILE A CG1 1 
ATOM   393   C CG2 . ILE A  1 51  ? -0.480  57.994 67.611  1.00 53.27  ? 51   ILE A CG2 1 
ATOM   394   C CD1 . ILE A  1 51  ? -1.294  56.904 65.030  1.00 53.35  ? 51   ILE A CD1 1 
ATOM   395   N N   . LEU A  1 52  ? 1.342   56.446 70.396  1.00 50.88  ? 52   LEU A N   1 
ATOM   396   C CA  . LEU A  1 52  ? 1.463   56.888 71.787  1.00 51.65  ? 52   LEU A CA  1 
ATOM   397   C C   . LEU A  1 52  ? 0.999   58.335 71.998  1.00 53.30  ? 52   LEU A C   1 
ATOM   398   O O   . LEU A  1 52  ? 0.850   58.779 73.138  1.00 54.51  ? 52   LEU A O   1 
ATOM   399   C CB  . LEU A  1 52  ? 2.907   56.732 72.272  1.00 49.77  ? 52   LEU A CB  1 
ATOM   400   C CG  . LEU A  1 52  ? 3.517   55.330 72.183  1.00 48.52  ? 52   LEU A CG  1 
ATOM   401   C CD1 . LEU A  1 52  ? 4.975   55.361 72.609  1.00 47.13  ? 52   LEU A CD1 1 
ATOM   402   C CD2 . LEU A  1 52  ? 2.744   54.327 73.026  1.00 49.96  ? 52   LEU A CD2 1 
ATOM   403   N N   . ARG A  1 53  ? 0.771   59.055 70.900  1.00 53.58  ? 53   ARG A N   1 
ATOM   404   C CA  . ARG A  1 53  ? 0.366   60.456 70.935  1.00 55.51  ? 53   ARG A CA  1 
ATOM   405   C C   . ARG A  1 53  ? 1.418   61.271 71.712  1.00 55.13  ? 53   ARG A C   1 
ATOM   406   O O   . ARG A  1 53  ? 2.564   61.354 71.261  1.00 53.31  ? 53   ARG A O   1 
ATOM   407   C CB  . ARG A  1 53  ? -1.070  60.608 71.470  1.00 58.59  ? 53   ARG A CB  1 
ATOM   408   C CG  . ARG A  1 53  ? -1.689  61.975 71.191  1.00 61.11  ? 53   ARG A CG  1 
ATOM   409   C CD  . ARG A  1 53  ? -3.058  62.161 71.838  1.00 64.54  ? 53   ARG A CD  1 
ATOM   410   N NE  . ARG A  1 53  ? -4.164  61.828 70.934  1.00 66.24  ? 53   ARG A NE  1 
ATOM   411   C CZ  . ARG A  1 53  ? -4.850  60.681 70.926  1.00 66.71  ? 53   ARG A CZ  1 
ATOM   412   N NH1 . ARG A  1 53  ? -4.573  59.698 71.779  1.00 65.56  ? 53   ARG A NH1 1 
ATOM   413   N NH2 . ARG A  1 53  ? -5.835  60.515 70.050  1.00 68.67  ? 53   ARG A NH2 1 
ATOM   414   N N   . ASP A  1 54  ? 1.062   61.844 72.863  1.00 57.07  ? 54   ASP A N   1 
ATOM   415   C CA  . ASP A  1 54  ? 2.000   62.656 73.648  1.00 57.20  ? 54   ASP A CA  1 
ATOM   416   C C   . ASP A  1 54  ? 2.723   61.868 74.743  1.00 56.02  ? 54   ASP A C   1 
ATOM   417   O O   . ASP A  1 54  ? 3.605   62.411 75.409  1.00 56.11  ? 54   ASP A O   1 
ATOM   418   C CB  . ASP A  1 54  ? 1.278   63.860 74.261  1.00 60.33  ? 54   ASP A CB  1 
ATOM   419   C CG  . ASP A  1 54  ? 0.931   64.916 73.230  1.00 61.83  ? 54   ASP A CG  1 
ATOM   420   O OD1 . ASP A  1 54  ? 1.854   65.401 72.539  1.00 60.77  ? 54   ASP A OD1 1 
ATOM   421   O OD2 . ASP A  1 54  ? -0.262  65.266 73.113  1.00 64.35  ? 54   ASP A OD2 1 
ATOM   422   N N   . CYS A  1 55  ? 2.351   60.604 74.938  1.00 55.31  ? 55   CYS A N   1 
ATOM   423   C CA  . CYS A  1 55  ? 3.073   59.727 75.864  1.00 54.24  ? 55   CYS A CA  1 
ATOM   424   C C   . CYS A  1 55  ? 4.334   59.166 75.200  1.00 51.80  ? 55   CYS A C   1 
ATOM   425   O O   . CYS A  1 55  ? 4.376   58.991 73.984  1.00 50.74  ? 55   CYS A O   1 
ATOM   426   C CB  . CYS A  1 55  ? 2.180   58.582 76.360  1.00 54.90  ? 55   CYS A CB  1 
ATOM   427   S SG  . CYS A  1 55  ? 1.001   59.066 77.643  1.00 57.86  ? 55   CYS A SG  1 
ATOM   428   N N   . SER A  1 56  ? 5.360   58.905 76.007  1.00 51.14  ? 56   SER A N   1 
ATOM   429   C CA  . SER A  1 56  ? 6.576   58.243 75.543  1.00 49.23  ? 56   SER A CA  1 
ATOM   430   C C   . SER A  1 56  ? 6.469   56.741 75.804  1.00 48.67  ? 56   SER A C   1 
ATOM   431   O O   . SER A  1 56  ? 5.462   56.261 76.331  1.00 49.69  ? 56   SER A O   1 
ATOM   432   C CB  . SER A  1 56  ? 7.806   58.810 76.260  1.00 49.41  ? 56   SER A CB  1 
ATOM   433   O OG  . SER A  1 56  ? 8.004   58.182 77.518  1.00 49.95  ? 56   SER A OG  1 
ATOM   434   N N   . VAL A  1 57  ? 7.516   56.007 75.439  1.00 47.34  ? 57   VAL A N   1 
ATOM   435   C CA  . VAL A  1 57  ? 7.563   54.562 75.660  1.00 47.15  ? 57   VAL A CA  1 
ATOM   436   C C   . VAL A  1 57  ? 7.677   54.281 77.156  1.00 48.27  ? 57   VAL A C   1 
ATOM   437   O O   . VAL A  1 57  ? 7.018   53.379 77.677  1.00 49.08  ? 57   VAL A O   1 
ATOM   438   C CB  . VAL A  1 57  ? 8.748   53.912 74.911  1.00 45.90  ? 57   VAL A CB  1 
ATOM   439   C CG1 . VAL A  1 57  ? 8.831   52.421 75.208  1.00 46.28  ? 57   VAL A CG1 1 
ATOM   440   C CG2 . VAL A  1 57  ? 8.619   54.140 73.410  1.00 44.77  ? 57   VAL A CG2 1 
ATOM   441   N N   . ALA A  1 58  ? 8.517   55.060 77.836  1.00 48.51  ? 58   ALA A N   1 
ATOM   442   C CA  . ALA A  1 58  ? 8.691   54.947 79.283  1.00 49.68  ? 58   ALA A CA  1 
ATOM   443   C C   . ALA A  1 58  ? 7.373   55.183 80.017  1.00 50.92  ? 58   ALA A C   1 
ATOM   444   O O   . ALA A  1 58  ? 6.975   54.382 80.866  1.00 51.74  ? 58   ALA A O   1 
ATOM   445   C CB  . ALA A  1 58  ? 9.746   55.931 79.767  1.00 50.07  ? 58   ALA A CB  1 
ATOM   446   N N   . GLY A  1 59  ? 6.699   56.279 79.678  1.00 51.29  ? 59   GLY A N   1 
ATOM   447   C CA  . GLY A  1 59  ? 5.418   56.613 80.291  1.00 52.83  ? 59   GLY A CA  1 
ATOM   448   C C   . GLY A  1 59  ? 4.383   55.519 80.103  1.00 53.13  ? 59   GLY A C   1 
ATOM   449   O O   . GLY A  1 59  ? 3.662   55.176 81.038  1.00 54.53  ? 59   GLY A O   1 
ATOM   450   N N   . TRP A  1 60  ? 4.303   54.976 78.893  1.00 52.06  ? 60   TRP A N   1 
ATOM   451   C CA  . TRP A  1 60  ? 3.390   53.871 78.609  1.00 52.66  ? 60   TRP A CA  1 
ATOM   452   C C   . TRP A  1 60  ? 3.732   52.649 79.465  1.00 53.02  ? 60   TRP A C   1 
ATOM   453   O O   . TRP A  1 60  ? 2.870   52.117 80.171  1.00 54.61  ? 60   TRP A O   1 
ATOM   454   C CB  . TRP A  1 60  ? 3.406   53.528 77.107  1.00 51.56  ? 60   TRP A CB  1 
ATOM   455   C CG  . TRP A  1 60  ? 2.969   52.127 76.761  1.00 52.06  ? 60   TRP A CG  1 
ATOM   456   C CD1 . TRP A  1 60  ? 1.914   51.439 77.284  1.00 53.99  ? 60   TRP A CD1 1 
ATOM   457   C CD2 . TRP A  1 60  ? 3.570   51.261 75.791  1.00 50.99  ? 60   TRP A CD2 1 
ATOM   458   N NE1 . TRP A  1 60  ? 1.831   50.192 76.715  1.00 54.33  ? 60   TRP A NE1 1 
ATOM   459   C CE2 . TRP A  1 60  ? 2.834   50.058 75.792  1.00 52.49  ? 60   TRP A CE2 1 
ATOM   460   C CE3 . TRP A  1 60  ? 4.664   51.384 74.924  1.00 49.16  ? 60   TRP A CE3 1 
ATOM   461   C CZ2 . TRP A  1 60  ? 3.157   48.982 74.959  1.00 52.30  ? 60   TRP A CZ2 1 
ATOM   462   C CZ3 . TRP A  1 60  ? 4.986   50.311 74.095  1.00 48.78  ? 60   TRP A CZ3 1 
ATOM   463   C CH2 . TRP A  1 60  ? 4.234   49.128 74.120  1.00 50.38  ? 60   TRP A CH2 1 
ATOM   464   N N   . LEU A  1 61  ? 4.993   52.226 79.417  1.00 51.84  ? 61   LEU A N   1 
ATOM   465   C CA  . LEU A  1 61  ? 5.420   50.997 80.091  1.00 52.40  ? 61   LEU A CA  1 
ATOM   466   C C   . LEU A  1 61  ? 5.413   51.091 81.619  1.00 53.61  ? 61   LEU A C   1 
ATOM   467   O O   . LEU A  1 61  ? 5.053   50.128 82.299  1.00 54.89  ? 61   LEU A O   1 
ATOM   468   C CB  . LEU A  1 61  ? 6.802   50.568 79.595  1.00 51.22  ? 61   LEU A CB  1 
ATOM   469   C CG  . LEU A  1 61  ? 6.876   50.097 78.141  1.00 50.23  ? 61   LEU A CG  1 
ATOM   470   C CD1 . LEU A  1 61  ? 8.291   49.635 77.829  1.00 49.51  ? 61   LEU A CD1 1 
ATOM   471   C CD2 . LEU A  1 61  ? 5.879   48.982 77.857  1.00 51.45  ? 61   LEU A CD2 1 
ATOM   472   N N   . LEU A  1 62  ? 5.807   52.239 82.164  1.00 53.41  ? 62   LEU A N   1 
ATOM   473   C CA  . LEU A  1 62  ? 5.732   52.454 83.617  1.00 54.65  ? 62   LEU A CA  1 
ATOM   474   C C   . LEU A  1 62  ? 4.297   52.691 84.088  1.00 56.12  ? 62   LEU A C   1 
ATOM   475   O O   . LEU A  1 62  ? 4.014   52.598 85.277  1.00 57.39  ? 62   LEU A O   1 
ATOM   476   C CB  . LEU A  1 62  ? 6.623   53.620 84.047  1.00 54.35  ? 62   LEU A CB  1 
ATOM   477   C CG  . LEU A  1 62  ? 8.121   53.352 83.909  1.00 53.58  ? 62   LEU A CG  1 
ATOM   478   C CD1 . LEU A  1 62  ? 8.908   54.650 83.992  1.00 53.52  ? 62   LEU A CD1 1 
ATOM   479   C CD2 . LEU A  1 62  ? 8.599   52.363 84.961  1.00 54.58  ? 62   LEU A CD2 1 
ATOM   480   N N   . GLY A  1 63  ? 3.396   52.987 83.154  1.00 56.19  ? 63   GLY A N   1 
ATOM   481   C CA  . GLY A  1 63  ? 1.996   53.212 83.480  1.00 58.00  ? 63   GLY A CA  1 
ATOM   482   C C   . GLY A  1 63  ? 1.774   54.595 84.059  1.00 58.81  ? 63   GLY A C   1 
ATOM   483   O O   . GLY A  1 63  ? 1.082   54.750 85.062  1.00 60.48  ? 63   GLY A O   1 
ATOM   484   N N   . ASN A  1 64  ? 2.376   55.600 83.428  1.00 57.86  ? 64   ASN A N   1 
ATOM   485   C CA  . ASN A  1 64  ? 2.120   56.996 83.766  1.00 59.02  ? 64   ASN A CA  1 
ATOM   486   C C   . ASN A  1 64  ? 0.608   57.260 83.672  1.00 61.06  ? 64   ASN A C   1 
ATOM   487   O O   . ASN A  1 64  ? -0.027  56.864 82.690  1.00 61.04  ? 64   ASN A O   1 
ATOM   488   C CB  . ASN A  1 64  ? 2.935   57.903 82.825  1.00 57.83  ? 64   ASN A CB  1 
ATOM   489   C CG  . ASN A  1 64  ? 2.557   59.377 82.918  1.00 59.38  ? 64   ASN A CG  1 
ATOM   490   O OD1 . ASN A  1 64  ? 1.384   59.733 82.938  1.00 61.12  ? 64   ASN A OD1 1 
ATOM   491   N ND2 . ASN A  1 64  ? 3.564   60.245 82.934  1.00 59.14  ? 64   ASN A ND2 1 
ATOM   492   N N   . PRO A  1 65  ? 0.024   57.917 84.695  1.00 63.15  ? 65   PRO A N   1 
ATOM   493   C CA  . PRO A  1 65  ? -1.436  58.104 84.757  1.00 65.59  ? 65   PRO A CA  1 
ATOM   494   C C   . PRO A  1 65  ? -2.046  58.876 83.579  1.00 66.37  ? 65   PRO A C   1 
ATOM   495   O O   . PRO A  1 65  ? -3.237  58.731 83.310  1.00 68.27  ? 65   PRO A O   1 
ATOM   496   C CB  . PRO A  1 65  ? -1.641  58.873 86.070  1.00 67.48  ? 65   PRO A CB  1 
ATOM   497   C CG  . PRO A  1 65  ? -0.325  59.503 86.367  1.00 66.23  ? 65   PRO A CG  1 
ATOM   498   C CD  . PRO A  1 65  ? 0.704   58.552 85.839  1.00 63.60  ? 65   PRO A CD  1 
ATOM   499   N N   . MET A  1 66  ? -1.244  59.689 82.896  1.00 65.26  ? 66   MET A N   1 
ATOM   500   C CA  . MET A  1 66  ? -1.682  60.380 81.677  1.00 65.83  ? 66   MET A CA  1 
ATOM   501   C C   . MET A  1 66  ? -1.742  59.431 80.474  1.00 64.31  ? 66   MET A C   1 
ATOM   502   O O   . MET A  1 66  ? -2.337  59.759 79.444  1.00 65.00  ? 66   MET A O   1 
ATOM   503   C CB  . MET A  1 66  ? -0.733  61.539 81.349  1.00 65.25  ? 66   MET A CB  1 
ATOM   504   C CG  . MET A  1 66  ? -0.606  62.594 82.438  1.00 67.18  ? 66   MET A CG  1 
ATOM   505   S SD  . MET A  1 66  ? -2.078  63.624 82.586  1.00 71.19  ? 66   MET A SD  1 
ATOM   506   C CE  . MET A  1 66  ? -1.482  64.895 83.700  1.00 73.01  ? 66   MET A CE  1 
ATOM   507   N N   . CYS A  1 67  ? -1.111  58.266 80.603  1.00 62.52  ? 67   CYS A N   1 
ATOM   508   C CA  . CYS A  1 67  ? -1.083  57.258 79.546  1.00 61.21  ? 67   CYS A CA  1 
ATOM   509   C C   . CYS A  1 67  ? -2.083  56.139 79.834  1.00 62.70  ? 67   CYS A C   1 
ATOM   510   O O   . CYS A  1 67  ? -1.810  54.963 79.578  1.00 61.76  ? 67   CYS A O   1 
ATOM   511   C CB  . CYS A  1 67  ? 0.335   56.701 79.428  1.00 58.64  ? 67   CYS A CB  1 
ATOM   512   S SG  . CYS A  1 67  ? 1.574   58.011 79.294  1.00 57.54  ? 67   CYS A SG  1 
ATOM   513   N N   . ASP A  1 68  ? -3.242  56.523 80.367  1.00 65.38  ? 68   ASP A N   1 
ATOM   514   C CA  . ASP A  1 68  ? -4.332  55.589 80.644  1.00 67.47  ? 68   ASP A CA  1 
ATOM   515   C C   . ASP A  1 68  ? -4.900  54.972 79.371  1.00 67.84  ? 68   ASP A C   1 
ATOM   516   O O   . ASP A  1 68  ? -5.461  53.885 79.416  1.00 69.06  ? 68   ASP A O   1 
ATOM   517   C CB  . ASP A  1 68  ? -5.464  56.287 81.410  1.00 70.62  ? 68   ASP A CB  1 
ATOM   518   C CG  . ASP A  1 68  ? -5.155  56.466 82.887  1.00 70.89  ? 68   ASP A CG  1 
ATOM   519   O OD1 . ASP A  1 68  ? -4.168  55.883 83.384  1.00 68.90  ? 68   ASP A OD1 1 
ATOM   520   O OD2 . ASP A  1 68  ? -5.913  57.193 83.563  1.00 73.35  ? 68   ASP A OD2 1 
ATOM   521   N N   . GLU A  1 69  ? -4.769  55.665 78.243  1.00 67.05  ? 69   GLU A N   1 
ATOM   522   C CA  . GLU A  1 69  ? -5.178  55.098 76.961  1.00 67.23  ? 69   GLU A CA  1 
ATOM   523   C C   . GLU A  1 69  ? -4.441  53.791 76.674  1.00 65.33  ? 69   GLU A C   1 
ATOM   524   O O   . GLU A  1 69  ? -5.011  52.866 76.096  1.00 66.52  ? 69   GLU A O   1 
ATOM   525   C CB  . GLU A  1 69  ? -4.920  56.088 75.821  1.00 66.25  ? 69   GLU A CB  1 
ATOM   526   C CG  . GLU A  1 69  ? -5.322  55.563 74.447  1.00 66.42  ? 69   GLU A CG  1 
ATOM   527   C CD  . GLU A  1 69  ? -5.099  56.566 73.333  1.00 65.65  ? 69   GLU A CD  1 
ATOM   528   O OE1 . GLU A  1 69  ? -4.910  57.767 73.629  1.00 65.86  ? 69   GLU A OE1 1 
ATOM   529   O OE2 . GLU A  1 69  ? -5.122  56.151 72.154  1.00 65.03  ? 69   GLU A OE2 1 
ATOM   530   N N   . PHE A  1 70  ? -3.182  53.719 77.101  1.00 62.85  ? 70   PHE A N   1 
ATOM   531   C CA  . PHE A  1 70  ? -2.294  52.623 76.726  1.00 61.00  ? 70   PHE A CA  1 
ATOM   532   C C   . PHE A  1 70  ? -2.144  51.544 77.807  1.00 61.71  ? 70   PHE A C   1 
ATOM   533   O O   . PHE A  1 70  ? -1.127  50.852 77.864  1.00 60.15  ? 70   PHE A O   1 
ATOM   534   C CB  . PHE A  1 70  ? -0.941  53.206 76.303  1.00 58.09  ? 70   PHE A CB  1 
ATOM   535   C CG  . PHE A  1 70  ? -1.070  54.368 75.354  1.00 57.66  ? 70   PHE A CG  1 
ATOM   536   C CD1 . PHE A  1 70  ? -1.539  54.170 74.066  1.00 57.77  ? 70   PHE A CD1 1 
ATOM   537   C CD2 . PHE A  1 70  ? -0.776  55.662 75.763  1.00 57.52  ? 70   PHE A CD2 1 
ATOM   538   C CE1 . PHE A  1 70  ? -1.681  55.233 73.193  1.00 57.65  ? 70   PHE A CE1 1 
ATOM   539   C CE2 . PHE A  1 70  ? -0.915  56.731 74.893  1.00 57.57  ? 70   PHE A CE2 1 
ATOM   540   C CZ  . PHE A  1 70  ? -1.371  56.515 73.606  1.00 57.58  ? 70   PHE A CZ  1 
ATOM   541   N N   . ILE A  1 71  ? -3.162  51.404 78.657  1.00 64.36  ? 71   ILE A N   1 
ATOM   542   C CA  . ILE A  1 71  ? -3.309  50.218 79.513  1.00 65.76  ? 71   ILE A CA  1 
ATOM   543   C C   . ILE A  1 71  ? -3.890  49.074 78.672  1.00 67.35  ? 71   ILE A C   1 
ATOM   544   O O   . ILE A  1 71  ? -4.884  49.263 77.965  1.00 69.15  ? 71   ILE A O   1 
ATOM   545   C CB  . ILE A  1 71  ? -4.196  50.480 80.763  1.00 68.18  ? 71   ILE A CB  1 
ATOM   546   C CG1 . ILE A  1 71  ? -4.397  49.194 81.577  1.00 69.84  ? 71   ILE A CG1 1 
ATOM   547   C CG2 . ILE A  1 71  ? -5.576  51.022 80.393  1.00 70.80  ? 71   ILE A CG2 1 
ATOM   548   C CD1 . ILE A  1 71  ? -4.868  49.437 82.996  1.00 71.49  ? 71   ILE A CD1 1 
ATOM   549   N N   . ASN A  1 72  ? -3.261  47.899 78.743  1.00 67.08  ? 72   ASN A N   1 
ATOM   550   C CA  . ASN A  1 72  ? -3.672  46.724 77.955  1.00 68.71  ? 72   ASN A CA  1 
ATOM   551   C C   . ASN A  1 72  ? -3.835  47.002 76.452  1.00 68.01  ? 72   ASN A C   1 
ATOM   552   O O   . ASN A  1 72  ? -4.887  46.736 75.873  1.00 70.47  ? 72   ASN A O   1 
ATOM   553   C CB  . ASN A  1 72  ? -4.960  46.111 78.535  1.00 72.56  ? 72   ASN A CB  1 
ATOM   554   C CG  . ASN A  1 72  ? -4.702  45.266 79.772  1.00 73.66  ? 72   ASN A CG  1 
ATOM   555   O OD1 . ASN A  1 72  ? -3.576  44.833 80.016  1.00 72.00  ? 72   ASN A OD1 1 
ATOM   556   N ND2 . ASN A  1 72  ? -5.749  45.016 80.553  1.00 76.78  ? 72   ASN A ND2 1 
ATOM   557   N N   . VAL A  1 73  ? -2.786  47.532 75.829  1.00 64.91  ? 73   VAL A N   1 
ATOM   558   C CA  . VAL A  1 73  ? -2.826  47.853 74.395  1.00 63.97  ? 73   VAL A CA  1 
ATOM   559   C C   . VAL A  1 73  ? -2.951  46.600 73.523  1.00 65.10  ? 73   VAL A C   1 
ATOM   560   O O   . VAL A  1 73  ? -2.362  45.564 73.839  1.00 65.33  ? 73   VAL A O   1 
ATOM   561   C CB  . VAL A  1 73  ? -1.580  48.648 73.927  1.00 60.52  ? 73   VAL A CB  1 
ATOM   562   C CG1 . VAL A  1 73  ? -1.561  50.032 74.554  1.00 59.79  ? 73   VAL A CG1 1 
ATOM   563   C CG2 . VAL A  1 73  ? -0.283  47.898 74.222  1.00 58.96  ? 73   VAL A CG2 1 
ATOM   564   N N   . PRO A  1 74  ? -3.710  46.694 72.413  1.00 66.08  ? 74   PRO A N   1 
ATOM   565   C CA  . PRO A  1 74  ? -3.768  45.581 71.469  1.00 67.13  ? 74   PRO A CA  1 
ATOM   566   C C   . PRO A  1 74  ? -2.480  45.510 70.653  1.00 63.98  ? 74   PRO A C   1 
ATOM   567   O O   . PRO A  1 74  ? -1.658  46.429 70.720  1.00 61.09  ? 74   PRO A O   1 
ATOM   568   C CB  . PRO A  1 74  ? -4.953  45.947 70.575  1.00 69.19  ? 74   PRO A CB  1 
ATOM   569   C CG  . PRO A  1 74  ? -4.958  47.436 70.569  1.00 67.52  ? 74   PRO A CG  1 
ATOM   570   C CD  . PRO A  1 74  ? -4.439  47.875 71.913  1.00 66.33  ? 74   PRO A CD  1 
ATOM   571   N N   . GLU A  1 75  ? -2.312  44.437 69.884  1.00 64.75  ? 75   GLU A N   1 
ATOM   572   C CA  . GLU A  1 75  ? -1.093  44.263 69.095  1.00 62.13  ? 75   GLU A CA  1 
ATOM   573   C C   . GLU A  1 75  ? -0.977  45.338 68.014  1.00 59.86  ? 75   GLU A C   1 
ATOM   574   O O   . GLU A  1 75  ? -1.984  45.841 67.510  1.00 61.05  ? 75   GLU A O   1 
ATOM   575   C CB  . GLU A  1 75  ? -1.009  42.859 68.486  1.00 64.01  ? 75   GLU A CB  1 
ATOM   576   C CG  . GLU A  1 75  ? -1.726  42.665 67.164  1.00 65.39  ? 75   GLU A CG  1 
ATOM   577   C CD  . GLU A  1 75  ? -1.377  41.335 66.532  1.00 66.97  ? 75   GLU A CD  1 
ATOM   578   O OE1 . GLU A  1 75  ? -1.840  40.291 67.039  1.00 70.28  ? 75   GLU A OE1 1 
ATOM   579   O OE2 . GLU A  1 75  ? -0.633  41.336 65.528  1.00 65.16  ? 75   GLU A OE2 1 
ATOM   580   N N   . TRP A  1 76  ? 0.264   45.672 67.669  1.00 56.82  ? 76   TRP A N   1 
ATOM   581   C CA  . TRP A  1 76  ? 0.555   46.774 66.759  1.00 54.51  ? 76   TRP A CA  1 
ATOM   582   C C   . TRP A  1 76  ? 1.447   46.311 65.614  1.00 53.00  ? 76   TRP A C   1 
ATOM   583   O O   . TRP A  1 76  ? 2.255   45.393 65.774  1.00 52.92  ? 76   TRP A O   1 
ATOM   584   C CB  . TRP A  1 76  ? 1.242   47.913 67.515  1.00 52.40  ? 76   TRP A CB  1 
ATOM   585   C CG  . TRP A  1 76  ? 2.525   47.491 68.185  1.00 51.11  ? 76   TRP A CG  1 
ATOM   586   C CD1 . TRP A  1 76  ? 3.781   47.491 67.636  1.00 49.07  ? 76   TRP A CD1 1 
ATOM   587   C CD2 . TRP A  1 76  ? 2.673   46.987 69.519  1.00 52.08  ? 76   TRP A CD2 1 
ATOM   588   N NE1 . TRP A  1 76  ? 4.698   47.023 68.550  1.00 48.89  ? 76   TRP A NE1 1 
ATOM   589   C CE2 . TRP A  1 76  ? 4.045   46.709 69.713  1.00 50.66  ? 76   TRP A CE2 1 
ATOM   590   C CE3 . TRP A  1 76  ? 1.780   46.748 70.571  1.00 54.21  ? 76   TRP A CE3 1 
ATOM   591   C CZ2 . TRP A  1 76  ? 4.544   46.206 70.919  1.00 51.32  ? 76   TRP A CZ2 1 
ATOM   592   C CZ3 . TRP A  1 76  ? 2.277   46.246 71.768  1.00 54.66  ? 76   TRP A CZ3 1 
ATOM   593   C CH2 . TRP A  1 76  ? 3.646   45.980 71.931  1.00 53.24  ? 76   TRP A CH2 1 
ATOM   594   N N   . SER A  1 77  ? 1.292   46.954 64.462  1.00 52.00  ? 77   SER A N   1 
ATOM   595   C CA  . SER A  1 77  ? 2.181   46.740 63.323  1.00 50.25  ? 77   SER A CA  1 
ATOM   596   C C   . SER A  1 77  ? 3.513   47.439 63.578  1.00 47.40  ? 77   SER A C   1 
ATOM   597   O O   . SER A  1 77  ? 4.581   46.845 63.428  1.00 46.49  ? 77   SER A O   1 
ATOM   598   C CB  . SER A  1 77  ? 1.541   47.296 62.052  1.00 50.28  ? 77   SER A CB  1 
ATOM   599   O OG  . SER A  1 77  ? 0.916   48.545 62.306  1.00 50.27  ? 77   SER A OG  1 
ATOM   600   N N   . TYR A  1 78  ? 3.429   48.708 63.963  1.00 46.38  ? 78   TYR A N   1 
ATOM   601   C CA  . TYR A  1 78  ? 4.594   49.501 64.338  1.00 44.22  ? 78   TYR A CA  1 
ATOM   602   C C   . TYR A  1 78  ? 4.187   50.523 65.403  1.00 44.56  ? 78   TYR A C   1 
ATOM   603   O O   . TYR A  1 78  ? 2.998   50.709 65.666  1.00 46.27  ? 78   TYR A O   1 
ATOM   604   C CB  . TYR A  1 78  ? 5.191   50.190 63.103  1.00 42.33  ? 78   TYR A CB  1 
ATOM   605   C CG  . TYR A  1 78  ? 4.251   51.150 62.396  1.00 42.63  ? 78   TYR A CG  1 
ATOM   606   C CD1 . TYR A  1 78  ? 3.242   50.683 61.548  1.00 44.00  ? 78   TYR A CD1 1 
ATOM   607   C CD2 . TYR A  1 78  ? 4.373   52.525 62.574  1.00 41.95  ? 78   TYR A CD2 1 
ATOM   608   C CE1 . TYR A  1 78  ? 2.380   51.561 60.902  1.00 44.66  ? 78   TYR A CE1 1 
ATOM   609   C CE2 . TYR A  1 78  ? 3.518   53.409 61.933  1.00 42.66  ? 78   TYR A CE2 1 
ATOM   610   C CZ  . TYR A  1 78  ? 2.521   52.923 61.098  1.00 44.00  ? 78   TYR A CZ  1 
ATOM   611   O OH  . TYR A  1 78  ? 1.676   53.810 60.469  1.00 45.02  ? 78   TYR A OH  1 
ATOM   612   N N   . ILE A  1 79  ? 5.171   51.172 66.020  1.00 43.27  ? 79   ILE A N   1 
ATOM   613   C CA  . ILE A  1 79  ? 4.912   52.155 67.076  1.00 43.73  ? 79   ILE A CA  1 
ATOM   614   C C   . ILE A  1 79  ? 5.249   53.558 66.583  1.00 42.72  ? 79   ILE A C   1 
ATOM   615   O O   . ILE A  1 79  ? 6.208   53.739 65.838  1.00 41.24  ? 79   ILE A O   1 
ATOM   616   C CB  . ILE A  1 79  ? 5.737   51.842 68.341  1.00 43.65  ? 79   ILE A CB  1 
ATOM   617   C CG1 . ILE A  1 79  ? 5.276   50.516 68.955  1.00 45.13  ? 79   ILE A CG1 1 
ATOM   618   C CG2 . ILE A  1 79  ? 5.607   52.962 69.366  1.00 44.07  ? 79   ILE A CG2 1 
ATOM   619   C CD1 . ILE A  1 79  ? 6.270   49.901 69.918  1.00 45.10  ? 79   ILE A CD1 1 
ATOM   620   N N   . VAL A  1 80  ? 4.457   54.543 67.005  1.00 43.86  ? 80   VAL A N   1 
ATOM   621   C CA  . VAL A  1 80  ? 4.692   55.940 66.638  1.00 43.56  ? 80   VAL A CA  1 
ATOM   622   C C   . VAL A  1 80  ? 4.873   56.808 67.886  1.00 44.37  ? 80   VAL A C   1 
ATOM   623   O O   . VAL A  1 80  ? 3.960   56.942 68.702  1.00 46.00  ? 80   VAL A O   1 
ATOM   624   C CB  . VAL A  1 80  ? 3.543   56.508 65.781  1.00 44.74  ? 80   VAL A CB  1 
ATOM   625   C CG1 . VAL A  1 80  ? 3.872   57.918 65.302  1.00 44.59  ? 80   VAL A CG1 1 
ATOM   626   C CG2 . VAL A  1 80  ? 3.274   55.600 64.591  1.00 44.31  ? 80   VAL A CG2 1 
ATOM   627   N N   . GLU A  1 81  ? 6.058   57.400 68.007  1.00 43.46  ? 81   GLU A N   1 
ATOM   628   C CA  . GLU A  1 81  ? 6.426   58.235 69.141  1.00 44.33  ? 81   GLU A CA  1 
ATOM   629   C C   . GLU A  1 81  ? 6.882   59.591 68.617  1.00 44.58  ? 81   GLU A C   1 
ATOM   630   O O   . GLU A  1 81  ? 7.623   59.661 67.642  1.00 43.40  ? 81   GLU A O   1 
ATOM   631   C CB  . GLU A  1 81  ? 7.566   57.569 69.924  1.00 43.57  ? 81   GLU A CB  1 
ATOM   632   C CG  . GLU A  1 81  ? 7.996   58.295 71.198  1.00 44.61  ? 81   GLU A CG  1 
ATOM   633   C CD  . GLU A  1 81  ? 9.233   57.692 71.854  1.00 44.10  ? 81   GLU A CD  1 
ATOM   634   O OE1 . GLU A  1 81  ? 10.196  57.350 71.129  1.00 42.96  ? 81   GLU A OE1 1 
ATOM   635   O OE2 . GLU A  1 81  ? 9.249   57.569 73.101  1.00 45.03  ? 81   GLU A OE2 1 
ATOM   636   N N   . LYS A  1 82  ? 6.445   60.665 69.264  1.00 46.45  ? 82   LYS A N   1 
ATOM   637   C CA  . LYS A  1 82  ? 6.904   62.010 68.916  1.00 47.30  ? 82   LYS A CA  1 
ATOM   638   C C   . LYS A  1 82  ? 8.374   62.218 69.292  1.00 46.84  ? 82   LYS A C   1 
ATOM   639   O O   . LYS A  1 82  ? 8.970   61.408 70.011  1.00 46.08  ? 82   LYS A O   1 
ATOM   640   C CB  . LYS A  1 82  ? 6.035   63.071 69.604  1.00 49.87  ? 82   LYS A CB  1 
ATOM   641   C CG  . LYS A  1 82  ? 4.668   63.260 68.967  1.00 51.12  ? 82   LYS A CG  1 
ATOM   642   C CD  . LYS A  1 82  ? 3.888   64.373 69.653  1.00 54.08  ? 82   LYS A CD  1 
ATOM   643   C CE  . LYS A  1 82  ? 2.731   64.865 68.797  1.00 55.83  ? 82   LYS A CE  1 
ATOM   644   N NZ  . LYS A  1 82  ? 1.601   63.897 68.764  1.00 56.08  ? 82   LYS A NZ  1 
ATOM   645   N N   . ALA A  1 83  ? 8.947   63.314 68.801  1.00 47.69  ? 83   ALA A N   1 
ATOM   646   C CA  . ALA A  1 83  ? 10.341  63.657 69.083  1.00 47.90  ? 83   ALA A CA  1 
ATOM   647   C C   . ALA A  1 83  ? 10.538  64.042 70.551  1.00 49.74  ? 83   ALA A C   1 
ATOM   648   O O   . ALA A  1 83  ? 11.452  63.538 71.208  1.00 49.46  ? 83   ALA A O   1 
ATOM   649   C CB  . ALA A  1 83  ? 10.813  64.779 68.165  1.00 48.64  ? 83   ALA A CB  1 
ATOM   650   N N   . ASN A  1 84  ? 9.674   64.919 71.065  1.00 51.97  ? 84   ASN A N   1 
ATOM   651   C CA  . ASN A  1 84  ? 9.751   65.369 72.462  1.00 53.99  ? 84   ASN A CA  1 
ATOM   652   C C   . ASN A  1 84  ? 8.405   65.233 73.193  1.00 55.02  ? 84   ASN A C   1 
ATOM   653   O O   . ASN A  1 84  ? 7.783   66.240 73.541  1.00 57.44  ? 84   ASN A O   1 
ATOM   654   C CB  . ASN A  1 84  ? 10.233  66.829 72.527  1.00 56.58  ? 84   ASN A CB  1 
ATOM   655   C CG  . ASN A  1 84  ? 11.470  67.086 71.674  1.00 56.15  ? 84   ASN A CG  1 
ATOM   656   O OD1 . ASN A  1 84  ? 12.429  66.308 71.694  1.00 54.75  ? 84   ASN A OD1 1 
ATOM   657   N ND2 . ASN A  1 84  ? 11.455  68.186 70.920  1.00 57.71  ? 84   ASN A ND2 1 
ATOM   658   N N   . PRO A  1 85  ? 7.948   63.987 73.436  1.00 53.56  ? 85   PRO A N   1 
ATOM   659   C CA  . PRO A  1 85  ? 6.654   63.787 74.102  1.00 54.69  ? 85   PRO A CA  1 
ATOM   660   C C   . PRO A  1 85  ? 6.630   64.375 75.513  1.00 56.79  ? 85   PRO A C   1 
ATOM   661   O O   . PRO A  1 85  ? 7.561   64.139 76.286  1.00 56.56  ? 85   PRO A O   1 
ATOM   662   C CB  . PRO A  1 85  ? 6.506   62.256 74.151  1.00 52.77  ? 85   PRO A CB  1 
ATOM   663   C CG  . PRO A  1 85  ? 7.480   61.725 73.158  1.00 50.66  ? 85   PRO A CG  1 
ATOM   664   C CD  . PRO A  1 85  ? 8.611   62.705 73.138  1.00 51.18  ? 85   PRO A CD  1 
ATOM   665   N N   . VAL A  1 86  ? 5.577   65.126 75.841  1.00 59.11  ? 86   VAL A N   1 
ATOM   666   C CA  . VAL A  1 86  ? 5.482   65.805 77.144  1.00 61.43  ? 86   VAL A CA  1 
ATOM   667   C C   . VAL A  1 86  ? 5.260   64.838 78.311  1.00 60.93  ? 86   VAL A C   1 
ATOM   668   O O   . VAL A  1 86  ? 5.847   65.014 79.380  1.00 61.76  ? 86   VAL A O   1 
ATOM   669   C CB  . VAL A  1 86  ? 4.386   66.907 77.171  1.00 64.50  ? 86   VAL A CB  1 
ATOM   670   C CG1 . VAL A  1 86  ? 4.639   67.945 76.085  1.00 65.43  ? 86   VAL A CG1 1 
ATOM   671   C CG2 . VAL A  1 86  ? 2.981   66.319 77.045  1.00 64.81  ? 86   VAL A CG2 1 
ATOM   672   N N   . ASN A  1 87  ? 4.416   63.826 78.103  1.00 59.86  ? 87   ASN A N   1 
ATOM   673   C CA  . ASN A  1 87  ? 4.114   62.834 79.138  1.00 59.53  ? 87   ASN A CA  1 
ATOM   674   C C   . ASN A  1 87  ? 5.154   61.724 79.160  1.00 57.15  ? 87   ASN A C   1 
ATOM   675   O O   . ASN A  1 87  ? 4.903   60.623 78.678  1.00 55.86  ? 87   ASN A O   1 
ATOM   676   C CB  . ASN A  1 87  ? 2.721   62.226 78.924  1.00 60.07  ? 87   ASN A CB  1 
ATOM   677   C CG  . ASN A  1 87  ? 1.599   63.190 79.258  1.00 63.03  ? 87   ASN A CG  1 
ATOM   678   O OD1 . ASN A  1 87  ? 1.729   64.036 80.146  1.00 64.83  ? 87   ASN A OD1 1 
ATOM   679   N ND2 . ASN A  1 87  ? 0.475   63.051 78.562  1.00 63.92  ? 87   ASN A ND2 1 
ATOM   680   N N   . ASP A  1 88  ? 6.326   62.023 79.713  1.00 56.97  ? 88   ASP A N   1 
ATOM   681   C CA  . ASP A  1 88  ? 7.394   61.037 79.848  1.00 55.22  ? 88   ASP A CA  1 
ATOM   682   C C   . ASP A  1 88  ? 7.456   60.594 81.320  1.00 56.00  ? 88   ASP A C   1 
ATOM   683   O O   . ASP A  1 88  ? 6.507   59.981 81.819  1.00 56.35  ? 88   ASP A O   1 
ATOM   684   C CB  . ASP A  1 88  ? 8.718   61.622 79.324  1.00 54.80  ? 88   ASP A CB  1 
ATOM   685   C CG  . ASP A  1 88  ? 9.829   60.581 79.214  1.00 53.28  ? 88   ASP A CG  1 
ATOM   686   O OD1 . ASP A  1 88  ? 9.556   59.370 79.355  1.00 52.34  ? 88   ASP A OD1 1 
ATOM   687   O OD2 . ASP A  1 88  ? 10.988  60.979 78.978  1.00 53.35  ? 88   ASP A OD2 1 
ATOM   688   N N   . LEU A  1 89  ? 8.549   60.906 82.014  1.00 56.49  ? 89   LEU A N   1 
ATOM   689   C CA  . LEU A  1 89  ? 8.686   60.587 83.430  1.00 57.45  ? 89   LEU A CA  1 
ATOM   690   C C   . LEU A  1 89  ? 8.063   61.715 84.249  1.00 59.63  ? 89   LEU A C   1 
ATOM   691   O O   . LEU A  1 89  ? 8.694   62.754 84.461  1.00 61.01  ? 89   LEU A O   1 
ATOM   692   C CB  . LEU A  1 89  ? 10.169  60.394 83.800  1.00 57.44  ? 89   LEU A CB  1 
ATOM   693   C CG  . LEU A  1 89  ? 10.757  58.974 83.795  1.00 56.15  ? 89   LEU A CG  1 
ATOM   694   C CD1 . LEU A  1 89  ? 10.139  58.075 82.735  1.00 54.37  ? 89   LEU A CD1 1 
ATOM   695   C CD2 . LEU A  1 89  ? 12.271  59.034 83.632  1.00 56.28  ? 89   LEU A CD2 1 
ATOM   696   N N   . CYS A  1 90  ? 6.822   61.510 84.692  1.00 60.21  ? 90   CYS A N   1 
ATOM   697   C CA  . CYS A  1 90  ? 6.120   62.511 85.497  1.00 62.57  ? 90   CYS A CA  1 
ATOM   698   C C   . CYS A  1 90  ? 6.926   62.844 86.753  1.00 63.90  ? 90   CYS A C   1 
ATOM   699   O O   . CYS A  1 90  ? 7.172   64.014 87.038  1.00 65.83  ? 90   CYS A O   1 
ATOM   700   C CB  . CYS A  1 90  ? 4.693   62.061 85.851  1.00 63.21  ? 90   CYS A CB  1 
ATOM   701   S SG  . CYS A  1 90  ? 4.522   60.388 86.517  1.00 62.05  ? 90   CYS A SG  1 
ATOM   702   N N   . TYR A  1 91  ? 7.357   61.813 87.477  1.00 58.35  ? 91   TYR A N   1 
ATOM   703   C CA  . TYR A  1 91  ? 8.317   61.989 88.563  1.00 59.26  ? 91   TYR A CA  1 
ATOM   704   C C   . TYR A  1 91  ? 9.736   61.939 87.982  1.00 56.90  ? 91   TYR A C   1 
ATOM   705   O O   . TYR A  1 91  ? 10.094  60.953 87.333  1.00 54.04  ? 91   TYR A O   1 
ATOM   706   C CB  . TYR A  1 91  ? 8.143   60.906 89.632  1.00 59.41  ? 91   TYR A CB  1 
ATOM   707   C CG  . TYR A  1 91  ? 8.794   61.257 90.957  1.00 61.65  ? 91   TYR A CG  1 
ATOM   708   C CD1 . TYR A  1 91  ? 10.153  61.035 91.171  1.00 60.51  ? 91   TYR A CD1 1 
ATOM   709   C CD2 . TYR A  1 91  ? 8.053   61.827 91.990  1.00 65.24  ? 91   TYR A CD2 1 
ATOM   710   C CE1 . TYR A  1 91  ? 10.753  61.362 92.378  1.00 62.93  ? 91   TYR A CE1 1 
ATOM   711   C CE2 . TYR A  1 91  ? 8.642   62.158 93.202  1.00 67.68  ? 91   TYR A CE2 1 
ATOM   712   C CZ  . TYR A  1 91  ? 9.993   61.924 93.392  1.00 66.55  ? 91   TYR A CZ  1 
ATOM   713   O OH  . TYR A  1 91  ? 10.579  62.251 94.595  1.00 69.36  ? 91   TYR A OH  1 
ATOM   714   N N   . PRO A  1 92  ? 10.553  62.989 88.221  1.00 58.38  ? 92   PRO A N   1 
ATOM   715   C CA  . PRO A  1 92  ? 11.899  63.079 87.629  1.00 56.56  ? 92   PRO A CA  1 
ATOM   716   C C   . PRO A  1 92  ? 12.763  61.850 87.878  1.00 54.24  ? 92   PRO A C   1 
ATOM   717   O O   . PRO A  1 92  ? 12.635  61.202 88.918  1.00 54.99  ? 92   PRO A O   1 
ATOM   718   C CB  . PRO A  1 92  ? 12.529  64.282 88.339  1.00 59.52  ? 92   PRO A CB  1 
ATOM   719   C CG  . PRO A  1 92  ? 11.397  65.067 88.871  1.00 62.84  ? 92   PRO A CG  1 
ATOM   720   C CD  . PRO A  1 92  ? 10.281  64.109 89.140  1.00 62.25  ? 92   PRO A CD  1 
ATOM   721   N N   . GLY A  1 93  ? 13.644  61.544 86.934  1.00 51.76  ? 93   GLY A N   1 
ATOM   722   C CA  . GLY A  1 93  ? 14.527  60.399 87.076  1.00 49.75  ? 93   GLY A CA  1 
ATOM   723   C C   . GLY A  1 93  ? 15.207  59.974 85.794  1.00 46.98  ? 93   GLY A C   1 
ATOM   724   O O   . GLY A  1 93  ? 15.261  60.729 84.822  1.00 46.70  ? 93   GLY A O   1 
ATOM   725   N N   . ASP A  1 94  ? 15.733  58.752 85.815  1.00 45.24  ? 94   ASP A N   1 
ATOM   726   C CA  . ASP A  1 94  ? 16.364  58.133 84.656  1.00 42.71  ? 94   ASP A CA  1 
ATOM   727   C C   . ASP A  1 94  ? 15.740  56.771 84.422  1.00 41.34  ? 94   ASP A C   1 
ATOM   728   O O   . ASP A  1 94  ? 15.241  56.131 85.356  1.00 42.19  ? 94   ASP A O   1 
ATOM   729   C CB  . ASP A  1 94  ? 17.861  57.943 84.889  1.00 42.28  ? 94   ASP A CB  1 
ATOM   730   C CG  . ASP A  1 94  ? 18.574  59.241 85.190  1.00 44.03  ? 94   ASP A CG  1 
ATOM   731   O OD1 . ASP A  1 94  ? 18.738  60.060 84.258  1.00 43.83  ? 94   ASP A OD1 1 
ATOM   732   O OD2 . ASP A  1 94  ? 18.980  59.437 86.358  1.00 45.93  ? 94   ASP A OD2 1 
ATOM   733   N N   . PHE A  1 95  ? 15.771  56.338 83.168  1.00 39.48  ? 95   PHE A N   1 
ATOM   734   C CA  . PHE A  1 95  ? 15.375  54.991 82.807  1.00 38.26  ? 95   PHE A CA  1 
ATOM   735   C C   . PHE A  1 95  ? 16.653  54.265 82.399  1.00 36.74  ? 95   PHE A C   1 
ATOM   736   O O   . PHE A  1 95  ? 17.305  54.636 81.418  1.00 35.74  ? 95   PHE A O   1 
ATOM   737   C CB  . PHE A  1 95  ? 14.356  55.027 81.667  1.00 37.83  ? 95   PHE A CB  1 
ATOM   738   C CG  . PHE A  1 95  ? 13.435  53.840 81.632  1.00 37.78  ? 95   PHE A CG  1 
ATOM   739   C CD1 . PHE A  1 95  ? 13.927  52.562 81.402  1.00 36.74  ? 95   PHE A CD1 1 
ATOM   740   C CD2 . PHE A  1 95  ? 12.069  54.002 81.826  1.00 39.09  ? 95   PHE A CD2 1 
ATOM   741   C CE1 . PHE A  1 95  ? 13.075  51.470 81.368  1.00 37.10  ? 95   PHE A CE1 1 
ATOM   742   C CE2 . PHE A  1 95  ? 11.212  52.914 81.790  1.00 39.34  ? 95   PHE A CE2 1 
ATOM   743   C CZ  . PHE A  1 95  ? 11.716  51.646 81.563  1.00 38.38  ? 95   PHE A CZ  1 
ATOM   744   N N   . ASN A  1 96  ? 17.016  53.245 83.168  1.00 36.80  ? 96   ASN A N   1 
ATOM   745   C CA  . ASN A  1 96  ? 18.250  52.507 82.931  1.00 35.80  ? 96   ASN A CA  1 
ATOM   746   C C   . ASN A  1 96  ? 18.173  51.653 81.661  1.00 34.32  ? 96   ASN A C   1 
ATOM   747   O O   . ASN A  1 96  ? 17.220  50.894 81.473  1.00 34.41  ? 96   ASN A O   1 
ATOM   748   C CB  . ASN A  1 96  ? 18.572  51.626 84.140  1.00 36.84  ? 96   ASN A CB  1 
ATOM   749   C CG  . ASN A  1 96  ? 20.010  51.138 84.137  1.00 36.49  ? 96   ASN A CG  1 
ATOM   750   O OD1 . ASN A  1 96  ? 20.949  51.940 84.132  1.00 36.55  ? 96   ASN A OD1 1 
ATOM   751   N ND2 . ASN A  1 96  ? 20.193  49.819 84.153  1.00 36.42  ? 96   ASN A ND2 1 
ATOM   752   N N   . ASP A  1 97  ? 19.188  51.781 80.803  1.00 33.20  ? 97   ASP A N   1 
ATOM   753   C CA  . ASP A  1 97  ? 19.242  51.095 79.503  1.00 32.02  ? 97   ASP A CA  1 
ATOM   754   C C   . ASP A  1 97  ? 17.928  51.250 78.733  1.00 31.87  ? 97   ASP A C   1 
ATOM   755   O O   . ASP A  1 97  ? 17.333  50.268 78.278  1.00 31.90  ? 97   ASP A O   1 
ATOM   756   C CB  . ASP A  1 97  ? 19.610  49.611 79.678  1.00 32.15  ? 97   ASP A CB  1 
ATOM   757   C CG  . ASP A  1 97  ? 21.057  49.406 80.117  1.00 32.25  ? 97   ASP A CG  1 
ATOM   758   O OD1 . ASP A  1 97  ? 21.874  50.341 79.984  1.00 32.02  ? 97   ASP A OD1 1 
ATOM   759   O OD2 . ASP A  1 97  ? 21.380  48.297 80.594  1.00 32.87  ? 97   ASP A OD2 1 
ATOM   760   N N   . TYR A  1 98  ? 17.485  52.497 78.605  1.00 32.01  ? 98   TYR A N   1 
ATOM   761   C CA  . TYR A  1 98  ? 16.227  52.832 77.936  1.00 32.27  ? 98   TYR A CA  1 
ATOM   762   C C   . TYR A  1 98  ? 16.296  52.541 76.436  1.00 31.48  ? 98   TYR A C   1 
ATOM   763   O O   . TYR A  1 98  ? 15.339  52.039 75.839  1.00 31.82  ? 98   TYR A O   1 
ATOM   764   C CB  . TYR A  1 98  ? 15.930  54.316 78.167  1.00 33.08  ? 98   TYR A CB  1 
ATOM   765   C CG  . TYR A  1 98  ? 14.579  54.820 77.692  1.00 33.96  ? 98   TYR A CG  1 
ATOM   766   C CD1 . TYR A  1 98  ? 13.418  54.068 77.866  1.00 34.56  ? 98   TYR A CD1 1 
ATOM   767   C CD2 . TYR A  1 98  ? 14.459  56.081 77.110  1.00 34.55  ? 98   TYR A CD2 1 
ATOM   768   C CE1 . TYR A  1 98  ? 12.185  54.548 77.444  1.00 35.66  ? 98   TYR A CE1 1 
ATOM   769   C CE2 . TYR A  1 98  ? 13.234  56.566 76.686  1.00 35.71  ? 98   TYR A CE2 1 
ATOM   770   C CZ  . TYR A  1 98  ? 12.100  55.799 76.857  1.00 36.25  ? 98   TYR A CZ  1 
ATOM   771   O OH  . TYR A  1 98  ? 10.885  56.286 76.440  1.00 37.67  ? 98   TYR A OH  1 
ATOM   772   N N   . GLU A  1 99  ? 17.445  52.850 75.843  1.00 30.63  ? 99   GLU A N   1 
ATOM   773   C CA  . GLU A  1 99  ? 17.646  52.691 74.412  1.00 30.13  ? 99   GLU A CA  1 
ATOM   774   C C   . GLU A  1 99  ? 17.720  51.214 74.046  1.00 29.87  ? 99   GLU A C   1 
ATOM   775   O O   . GLU A  1 99  ? 17.162  50.788 73.037  1.00 30.13  ? 99   GLU A O   1 
ATOM   776   C CB  . GLU A  1 99  ? 18.920  53.414 73.960  1.00 29.61  ? 99   GLU A CB  1 
ATOM   777   C CG  . GLU A  1 99  ? 18.830  54.936 73.991  1.00 30.23  ? 99   GLU A CG  1 
ATOM   778   C CD  . GLU A  1 99  ? 18.869  55.520 75.393  1.00 30.86  ? 99   GLU A CD  1 
ATOM   779   O OE1 . GLU A  1 99  ? 19.656  55.027 76.236  1.00 30.58  ? 99   GLU A OE1 1 
ATOM   780   O OE2 . GLU A  1 99  ? 18.111  56.479 75.645  1.00 31.89  ? 99   GLU A OE2 1 
ATOM   781   N N   . GLU A  1 100 ? 18.406  50.436 74.877  1.00 29.68  ? 100  GLU A N   1 
ATOM   782   C CA  . GLU A  1 100 ? 18.475  48.989 74.685  1.00 29.91  ? 100  GLU A CA  1 
ATOM   783   C C   . GLU A  1 100 ? 17.092  48.346 74.802  1.00 30.85  ? 100  GLU A C   1 
ATOM   784   O O   . GLU A  1 100 ? 16.785  47.401 74.083  1.00 31.43  ? 100  GLU A O   1 
ATOM   785   C CB  . GLU A  1 100 ? 19.446  48.358 75.685  1.00 29.90  ? 100  GLU A CB  1 
ATOM   786   C CG  . GLU A  1 100 ? 20.910  48.587 75.350  1.00 29.29  ? 100  GLU A CG  1 
ATOM   787   C CD  . GLU A  1 100 ? 21.360  47.801 74.136  1.00 29.27  ? 100  GLU A CD  1 
ATOM   788   O OE1 . GLU A  1 100 ? 21.077  46.589 74.073  1.00 30.02  ? 100  GLU A OE1 1 
ATOM   789   O OE2 . GLU A  1 100 ? 22.000  48.392 73.240  1.00 28.81  ? 100  GLU A OE2 1 
ATOM   790   N N   . LEU A  1 101 ? 16.259  48.863 75.701  1.00 31.31  ? 101  LEU A N   1 
ATOM   791   C CA  . LEU A  1 101 ? 14.894  48.360 75.839  1.00 32.42  ? 101  LEU A CA  1 
ATOM   792   C C   . LEU A  1 101 ? 14.068  48.748 74.625  1.00 32.77  ? 101  LEU A C   1 
ATOM   793   O O   . LEU A  1 101 ? 13.341  47.923 74.079  1.00 33.70  ? 101  LEU A O   1 
ATOM   794   C CB  . LEU A  1 101 ? 14.224  48.886 77.116  1.00 33.06  ? 101  LEU A CB  1 
ATOM   795   C CG  . LEU A  1 101 ? 12.809  48.359 77.400  1.00 34.42  ? 101  LEU A CG  1 
ATOM   796   C CD1 . LEU A  1 101 ? 12.757  46.836 77.373  1.00 35.11  ? 101  LEU A CD1 1 
ATOM   797   C CD2 . LEU A  1 101 ? 12.320  48.882 78.740  1.00 35.19  ? 101  LEU A CD2 1 
ATOM   798   N N   . LYS A  1 102 ? 14.178  50.006 74.215  1.00 32.38  ? 102  LYS A N   1 
ATOM   799   C CA  . LYS A  1 102 ? 13.525  50.478 72.992  1.00 32.96  ? 102  LYS A CA  1 
ATOM   800   C C   . LYS A  1 102 ? 13.901  49.639 71.773  1.00 32.97  ? 102  LYS A C   1 
ATOM   801   O O   . LYS A  1 102 ? 13.073  49.389 70.902  1.00 34.04  ? 102  LYS A O   1 
ATOM   802   C CB  . LYS A  1 102 ? 13.884  51.938 72.724  1.00 32.68  ? 102  LYS A CB  1 
ATOM   803   C CG  . LYS A  1 102 ? 12.960  52.943 73.392  1.00 33.65  ? 102  LYS A CG  1 
ATOM   804   C CD  . LYS A  1 102 ? 13.512  54.350 73.227  1.00 33.62  ? 102  LYS A CD  1 
ATOM   805   C CE  . LYS A  1 102 ? 12.436  55.346 72.829  1.00 35.15  ? 102  LYS A CE  1 
ATOM   806   N NZ  . LYS A  1 102 ? 13.045  56.682 72.584  1.00 35.43  ? 102  LYS A NZ  1 
ATOM   807   N N   . HIS A  1 103 ? 15.157  49.217 71.711  1.00 32.08  ? 103  HIS A N   1 
ATOM   808   C CA  . HIS A  1 103 ? 15.611  48.358 70.627  1.00 32.40  ? 103  HIS A CA  1 
ATOM   809   C C   . HIS A  1 103 ? 14.922  46.995 70.698  1.00 33.73  ? 103  HIS A C   1 
ATOM   810   O O   . HIS A  1 103 ? 14.604  46.406 69.671  1.00 34.87  ? 103  HIS A O   1 
ATOM   811   C CB  . HIS A  1 103 ? 17.133  48.193 70.670  1.00 31.35  ? 103  HIS A CB  1 
ATOM   812   C CG  . HIS A  1 103 ? 17.672  47.312 69.587  1.00 31.85  ? 103  HIS A CG  1 
ATOM   813   N ND1 . HIS A  1 103 ? 17.953  47.775 68.319  1.00 32.01  ? 103  HIS A ND1 1 
ATOM   814   C CD2 . HIS A  1 103 ? 17.974  45.993 69.581  1.00 32.57  ? 103  HIS A CD2 1 
ATOM   815   C CE1 . HIS A  1 103 ? 18.409  46.780 67.581  1.00 32.77  ? 103  HIS A CE1 1 
ATOM   816   N NE2 . HIS A  1 103 ? 18.432  45.688 68.323  1.00 33.17  ? 103  HIS A NE2 1 
ATOM   817   N N   . LEU A  1 104 ? 14.693  46.507 71.912  1.00 33.95  ? 104  LEU A N   1 
ATOM   818   C CA  . LEU A  1 104 ? 14.004  45.234 72.125  1.00 35.53  ? 104  LEU A CA  1 
ATOM   819   C C   . LEU A  1 104 ? 12.571  45.275 71.573  1.00 37.08  ? 104  LEU A C   1 
ATOM   820   O O   . LEU A  1 104 ? 12.061  44.266 71.089  1.00 38.68  ? 104  LEU A O   1 
ATOM   821   C CB  . LEU A  1 104 ? 13.981  44.887 73.622  1.00 35.59  ? 104  LEU A CB  1 
ATOM   822   C CG  . LEU A  1 104 ? 14.546  43.530 74.040  1.00 36.40  ? 104  LEU A CG  1 
ATOM   823   C CD1 . LEU A  1 104 ? 16.044  43.462 73.782  1.00 35.45  ? 104  LEU A CD1 1 
ATOM   824   C CD2 . LEU A  1 104 ? 14.265  43.300 75.513  1.00 36.82  ? 104  LEU A CD2 1 
ATOM   825   N N   . LEU A  1 105 ? 11.942  46.448 71.647  1.00 36.92  ? 105  LEU A N   1 
ATOM   826   C CA  . LEU A  1 105 ? 10.589  46.667 71.115  1.00 38.55  ? 105  LEU A CA  1 
ATOM   827   C C   . LEU A  1 105 ? 10.484  46.592 69.593  1.00 39.58  ? 105  LEU A C   1 
ATOM   828   O O   . LEU A  1 105 ? 9.386   46.413 69.059  1.00 41.41  ? 105  LEU A O   1 
ATOM   829   C CB  . LEU A  1 105 ? 10.051  48.028 71.561  1.00 38.26  ? 105  LEU A CB  1 
ATOM   830   C CG  . LEU A  1 105 ? 9.414   48.091 72.942  1.00 38.60  ? 105  LEU A CG  1 
ATOM   831   C CD1 . LEU A  1 105 ? 9.099   49.535 73.299  1.00 38.45  ? 105  LEU A CD1 1 
ATOM   832   C CD2 . LEU A  1 105 ? 8.156   47.236 72.978  1.00 40.61  ? 105  LEU A CD2 1 
ATOM   833   N N   . SER A  1 106 ? 11.606  46.756 68.898  1.00 38.69  ? 106  SER A N   1 
ATOM   834   C CA  . SER A  1 106 ? 11.630  46.589 67.448  1.00 39.91  ? 106  SER A CA  1 
ATOM   835   C C   . SER A  1 106 ? 11.396  45.129 67.046  1.00 41.75  ? 106  SER A C   1 
ATOM   836   O O   . SER A  1 106 ? 11.014  44.857 65.909  1.00 43.55  ? 106  SER A O   1 
ATOM   837   C CB  . SER A  1 106 ? 12.950  47.105 66.856  1.00 38.60  ? 106  SER A CB  1 
ATOM   838   O OG  . SER A  1 106 ? 14.049  46.282 67.206  1.00 37.81  ? 106  SER A OG  1 
ATOM   839   N N   . ARG A  1 107 ? 11.634  44.199 67.973  1.00 41.69  ? 107  ARG A N   1 
ATOM   840   C CA  . ARG A  1 107 ? 11.352  42.770 67.757  1.00 43.85  ? 107  ARG A CA  1 
ATOM   841   C C   . ARG A  1 107 ? 10.019  42.316 68.377  1.00 45.45  ? 107  ARG A C   1 
ATOM   842   O O   . ARG A  1 107 ? 9.737   41.115 68.414  1.00 47.39  ? 107  ARG A O   1 
ATOM   843   C CB  . ARG A  1 107 ? 12.486  41.901 68.330  1.00 43.37  ? 107  ARG A CB  1 
ATOM   844   C CG  . ARG A  1 107 ? 13.702  41.726 67.426  1.00 43.19  ? 107  ARG A CG  1 
ATOM   845   C CD  . ARG A  1 107 ? 14.489  40.476 67.823  1.00 44.06  ? 107  ARG A CD  1 
ATOM   846   N NE  . ARG A  1 107 ? 15.916  40.550 67.471  1.00 43.08  ? 107  ARG A NE  1 
ATOM   847   C CZ  . ARG A  1 107 ? 16.551  39.780 66.577  1.00 44.62  ? 107  ARG A CZ  1 
ATOM   848   N NH1 . ARG A  1 107 ? 15.917  38.828 65.887  1.00 47.42  ? 107  ARG A NH1 1 
ATOM   849   N NH2 . ARG A  1 107 ? 17.855  39.966 66.371  1.00 43.59  ? 107  ARG A NH2 1 
ATOM   850   N N   . ILE A  1 108 ? 9.205   43.260 68.853  1.00 44.87  ? 108  ILE A N   1 
ATOM   851   C CA  . ILE A  1 108 ? 7.983   42.931 69.590  1.00 46.30  ? 108  ILE A CA  1 
ATOM   852   C C   . ILE A  1 108 ? 6.740   43.550 68.947  1.00 47.80  ? 108  ILE A C   1 
ATOM   853   O O   . ILE A  1 108 ? 6.701   44.753 68.674  1.00 46.82  ? 108  ILE A O   1 
ATOM   854   C CB  . ILE A  1 108 ? 8.078   43.380 71.070  1.00 44.73  ? 108  ILE A CB  1 
ATOM   855   C CG1 . ILE A  1 108 ? 9.214   42.633 71.779  1.00 43.73  ? 108  ILE A CG1 1 
ATOM   856   C CG2 . ILE A  1 108 ? 6.763   43.122 71.801  1.00 46.46  ? 108  ILE A CG2 1 
ATOM   857   C CD1 . ILE A  1 108 ? 9.621   43.236 73.109  1.00 42.06  ? 108  ILE A CD1 1 
ATOM   858   N N   . ASN A  1 109 ? 5.724   42.714 68.734  1.00 50.46  ? 109  ASN A N   1 
ATOM   859   C CA  . ASN A  1 109 ? 4.441   43.145 68.174  1.00 52.52  ? 109  ASN A CA  1 
ATOM   860   C C   . ASN A  1 109 ? 3.301   43.218 69.194  1.00 53.51  ? 109  ASN A C   1 
ATOM   861   O O   . ASN A  1 109 ? 2.331   43.947 68.973  1.00 54.64  ? 109  ASN A O   1 
ATOM   862   C CB  . ASN A  1 109 ? 4.025   42.228 67.017  1.00 55.51  ? 109  ASN A CB  1 
ATOM   863   C CG  . ASN A  1 109 ? 4.450   42.765 65.667  1.00 55.57  ? 109  ASN A CG  1 
ATOM   864   O OD1 . ASN A  1 109 ? 3.613   43.054 64.812  1.00 57.81  ? 109  ASN A OD1 1 
ATOM   865   N ND2 . ASN A  1 109 ? 5.751   42.916 65.471  1.00 53.36  ? 109  ASN A ND2 1 
ATOM   866   N N   . HIS A  1 110 ? 3.398   42.463 70.291  1.00 53.33  ? 110  HIS A N   1 
ATOM   867   C CA  . HIS A  1 110 ? 2.354   42.500 71.317  1.00 54.42  ? 110  HIS A CA  1 
ATOM   868   C C   . HIS A  1 110 ? 2.814   42.145 72.729  1.00 53.22  ? 110  HIS A C   1 
ATOM   869   O O   . HIS A  1 110 ? 3.485   41.134 72.954  1.00 53.21  ? 110  HIS A O   1 
ATOM   870   C CB  . HIS A  1 110 ? 1.188   41.586 70.933  1.00 57.99  ? 110  HIS A CB  1 
ATOM   871   C CG  . HIS A  1 110 ? -0.072  41.864 71.697  1.00 59.55  ? 110  HIS A CG  1 
ATOM   872   N ND1 . HIS A  1 110 ? -0.979  40.880 72.025  1.00 62.47  ? 110  HIS A ND1 1 
ATOM   873   C CD2 . HIS A  1 110 ? -0.566  43.017 72.211  1.00 58.85  ? 110  HIS A CD2 1 
ATOM   874   C CE1 . HIS A  1 110 ? -1.984  41.416 72.695  1.00 63.42  ? 110  HIS A CE1 1 
ATOM   875   N NE2 . HIS A  1 110 ? -1.757  42.711 72.821  1.00 61.29  ? 110  HIS A NE2 1 
ATOM   876   N N   . PHE A  1 111 ? 2.415   42.996 73.671  1.00 52.54  ? 111  PHE A N   1 
ATOM   877   C CA  . PHE A  1 111 ? 2.556   42.734 75.095  1.00 52.14  ? 111  PHE A CA  1 
ATOM   878   C C   . PHE A  1 111 ? 1.193   42.362 75.657  1.00 54.86  ? 111  PHE A C   1 
ATOM   879   O O   . PHE A  1 111 ? 0.176   42.896 75.211  1.00 56.28  ? 111  PHE A O   1 
ATOM   880   C CB  . PHE A  1 111 ? 3.049   43.983 75.840  1.00 49.88  ? 111  PHE A CB  1 
ATOM   881   C CG  . PHE A  1 111 ? 4.541   44.185 75.807  1.00 47.27  ? 111  PHE A CG  1 
ATOM   882   C CD1 . PHE A  1 111 ? 5.418   43.139 76.077  1.00 46.93  ? 111  PHE A CD1 1 
ATOM   883   C CD2 . PHE A  1 111 ? 5.070   45.443 75.556  1.00 45.43  ? 111  PHE A CD2 1 
ATOM   884   C CE1 . PHE A  1 111 ? 6.788   43.341 76.061  1.00 44.77  ? 111  PHE A CE1 1 
ATOM   885   C CE2 . PHE A  1 111 ? 6.436   45.647 75.544  1.00 43.28  ? 111  PHE A CE2 1 
ATOM   886   C CZ  . PHE A  1 111 ? 7.297   44.596 75.798  1.00 42.92  ? 111  PHE A CZ  1 
ATOM   887   N N   . GLU A  1 112 ? 1.177   41.452 76.631  1.00 55.84  ? 112  GLU A N   1 
ATOM   888   C CA  . GLU A  1 112 ? -0.010  41.214 77.461  1.00 58.26  ? 112  GLU A CA  1 
ATOM   889   C C   . GLU A  1 112 ? 0.361   41.471 78.917  1.00 57.24  ? 112  GLU A C   1 
ATOM   890   O O   . GLU A  1 112 ? 1.300   40.875 79.436  1.00 56.37  ? 112  GLU A O   1 
ATOM   891   C CB  . GLU A  1 112 ? -0.545  39.786 77.305  1.00 61.25  ? 112  GLU A CB  1 
ATOM   892   C CG  . GLU A  1 112 ? -1.992  39.634 77.767  1.00 64.29  ? 112  GLU A CG  1 
ATOM   893   C CD  . GLU A  1 112 ? -2.275  38.298 78.437  1.00 66.91  ? 112  GLU A CD  1 
ATOM   894   O OE1 . GLU A  1 112 ? -1.831  37.255 77.907  1.00 67.89  ? 112  GLU A OE1 1 
ATOM   895   O OE2 . GLU A  1 112 ? -2.950  38.287 79.494  1.00 68.25  ? 112  GLU A OE2 1 
ATOM   896   N N   . LYS A  1 113 ? -0.379  42.354 79.573  1.00 57.67  ? 113  LYS A N   1 
ATOM   897   C CA  . LYS A  1 113 ? -0.069  42.738 80.946  1.00 57.01  ? 113  LYS A CA  1 
ATOM   898   C C   . LYS A  1 113 ? -0.585  41.692 81.937  1.00 59.38  ? 113  LYS A C   1 
ATOM   899   O O   . LYS A  1 113 ? -1.677  41.150 81.758  1.00 61.99  ? 113  LYS A O   1 
ATOM   900   C CB  . LYS A  1 113 ? -0.688  44.101 81.240  1.00 57.02  ? 113  LYS A CB  1 
ATOM   901   C CG  . LYS A  1 113 ? -0.184  44.769 82.506  1.00 56.13  ? 113  LYS A CG  1 
ATOM   902   C CD  . LYS A  1 113 ? 0.077   46.252 82.285  1.00 54.68  ? 113  LYS A CD  1 
ATOM   903   C CE  . LYS A  1 113 ? -1.163  47.036 81.875  1.00 56.42  ? 113  LYS A CE  1 
ATOM   904   N NZ  . LYS A  1 113 ? -0.793  48.443 81.550  1.00 55.15  ? 113  LYS A NZ  1 
ATOM   905   N N   . ILE A  1 114 ? 0.210   41.399 82.966  1.00 58.73  ? 114  ILE A N   1 
ATOM   906   C CA  . ILE A  1 114 ? -0.227  40.518 84.058  1.00 61.15  ? 114  ILE A CA  1 
ATOM   907   C C   . ILE A  1 114 ? 0.273   41.007 85.414  1.00 60.59  ? 114  ILE A C   1 
ATOM   908   O O   . ILE A  1 114 ? 1.306   41.673 85.502  1.00 58.26  ? 114  ILE A O   1 
ATOM   909   C CB  . ILE A  1 114 ? 0.237   39.055 83.869  1.00 62.22  ? 114  ILE A CB  1 
ATOM   910   C CG1 . ILE A  1 114 ? 1.758   38.980 83.668  1.00 59.70  ? 114  ILE A CG1 1 
ATOM   911   C CG2 . ILE A  1 114 ? -0.504  38.402 82.708  1.00 63.95  ? 114  ILE A CG2 1 
ATOM   912   C CD1 . ILE A  1 114 ? 2.350   37.644 84.064  1.00 61.08  ? 114  ILE A CD1 1 
ATOM   913   N N   . GLN A  1 115 ? -0.466  40.660 86.463  1.00 63.06  ? 115  GLN A N   1 
ATOM   914   C CA  . GLN A  1 115 ? -0.101  41.018 87.831  1.00 63.24  ? 115  GLN A CA  1 
ATOM   915   C C   . GLN A  1 115 ? 0.742   39.903 88.444  1.00 63.82  ? 115  GLN A C   1 
ATOM   916   O O   . GLN A  1 115 ? 0.323   38.745 88.463  1.00 66.06  ? 115  GLN A O   1 
ATOM   917   C CB  . GLN A  1 115 ? -1.363  41.277 88.667  1.00 65.92  ? 115  GLN A CB  1 
ATOM   918   C CG  . GLN A  1 115 ? -1.212  41.032 90.162  1.00 67.59  ? 115  GLN A CG  1 
ATOM   919   C CD  . GLN A  1 115 ? -2.387  41.565 90.962  1.00 70.04  ? 115  GLN A CD  1 
ATOM   920   O OE1 . GLN A  1 115 ? -2.763  42.730 90.830  1.00 69.48  ? 115  GLN A OE1 1 
ATOM   921   N NE2 . GLN A  1 115 ? -2.968  40.719 91.804  1.00 73.05  ? 115  GLN A NE2 1 
ATOM   922   N N   . ILE A  1 116 ? 1.925   40.259 88.943  1.00 62.12  ? 116  ILE A N   1 
ATOM   923   C CA  . ILE A  1 116 ? 2.805   39.293 89.614  1.00 62.88  ? 116  ILE A CA  1 
ATOM   924   C C   . ILE A  1 116 ? 2.834   39.512 91.133  1.00 64.52  ? 116  ILE A C   1 
ATOM   925   O O   . ILE A  1 116 ? 2.811   38.546 91.901  1.00 66.92  ? 116  ILE A O   1 
ATOM   926   C CB  . ILE A  1 116 ? 4.240   39.282 89.023  1.00 60.27  ? 116  ILE A CB  1 
ATOM   927   C CG1 . ILE A  1 116 ? 4.773   40.701 88.800  1.00 57.54  ? 116  ILE A CG1 1 
ATOM   928   C CG2 . ILE A  1 116 ? 4.261   38.514 87.708  1.00 59.91  ? 116  ILE A CG2 1 
ATOM   929   C CD1 . ILE A  1 116 ? 6.270   40.760 88.597  1.00 55.44  ? 116  ILE A CD1 1 
ATOM   930   N N   . ILE A  1 117 ? 2.876   40.775 91.558  1.00 63.57  ? 117  ILE A N   1 
ATOM   931   C CA  . ILE A  1 117 ? 2.752   41.139 92.972  1.00 65.48  ? 117  ILE A CA  1 
ATOM   932   C C   . ILE A  1 117 ? 1.464   41.946 93.149  1.00 66.76  ? 117  ILE A C   1 
ATOM   933   O O   . ILE A  1 117 ? 1.357   43.052 92.616  1.00 65.18  ? 117  ILE A O   1 
ATOM   934   C CB  . ILE A  1 117 ? 3.961   41.977 93.455  1.00 63.89  ? 117  ILE A CB  1 
ATOM   935   C CG1 . ILE A  1 117 ? 5.175   41.081 93.734  1.00 63.80  ? 117  ILE A CG1 1 
ATOM   936   C CG2 . ILE A  1 117 ? 3.624   42.774 94.716  1.00 65.79  ? 117  ILE A CG2 1 
ATOM   937   C CD1 . ILE A  1 117 ? 5.820   40.488 92.502  1.00 61.72  ? 117  ILE A CD1 1 
ATOM   938   N N   . PRO A  1 118 ? 0.477   41.394 93.881  1.00 69.91  ? 118  PRO A N   1 
ATOM   939   C CA  . PRO A  1 118 ? -0.720  42.190 94.179  1.00 71.52  ? 118  PRO A CA  1 
ATOM   940   C C   . PRO A  1 118 ? -0.416  43.368 95.111  1.00 71.74  ? 118  PRO A C   1 
ATOM   941   O O   . PRO A  1 118 ? 0.423   43.252 96.008  1.00 72.21  ? 118  PRO A O   1 
ATOM   942   C CB  . PRO A  1 118 ? -1.668  41.184 94.855  1.00 75.08  ? 118  PRO A CB  1 
ATOM   943   C CG  . PRO A  1 118 ? -1.138  39.833 94.507  1.00 75.10  ? 118  PRO A CG  1 
ATOM   944   C CD  . PRO A  1 118 ? 0.340   39.997 94.331  1.00 72.34  ? 118  PRO A CD  1 
ATOM   945   N N   . LYS A  1 119 ? -1.093  44.491 94.886  1.00 71.75  ? 119  LYS A N   1 
ATOM   946   C CA  . LYS A  1 119 ? -0.904  45.690 95.705  1.00 72.39  ? 119  LYS A CA  1 
ATOM   947   C C   . LYS A  1 119 ? -1.413  45.467 97.132  1.00 76.03  ? 119  LYS A C   1 
ATOM   948   O O   . LYS A  1 119 ? -0.835  45.975 98.098  1.00 76.97  ? 119  LYS A O   1 
ATOM   949   C CB  . LYS A  1 119 ? -1.623  46.879 95.066  1.00 72.04  ? 119  LYS A CB  1 
ATOM   950   C CG  . LYS A  1 119 ? -1.214  48.232 95.618  1.00 72.22  ? 119  LYS A CG  1 
ATOM   951   C CD  . LYS A  1 119 ? -1.846  49.351 94.807  1.00 71.83  ? 119  LYS A CD  1 
ATOM   952   C CE  . LYS A  1 119 ? -1.772  50.685 95.532  1.00 73.31  ? 119  LYS A CE  1 
ATOM   953   N NZ  . LYS A  1 119 ? -2.607  51.718 94.859  1.00 73.87  ? 119  LYS A NZ  1 
ATOM   954   N N   . SER A  1 120 ? -2.501  44.708 97.250  1.00 78.37  ? 120  SER A N   1 
ATOM   955   C CA  . SER A  1 120 ? -3.051  44.312 98.546  1.00 82.08  ? 120  SER A CA  1 
ATOM   956   C C   . SER A  1 120 ? -2.069  43.454 99.333  1.00 82.62  ? 120  SER A C   1 
ATOM   957   O O   . SER A  1 120 ? -1.973  43.566 100.550 1.00 85.10  ? 120  SER A O   1 
ATOM   958   C CB  . SER A  1 120 ? -4.342  43.518 98.342  1.00 84.35  ? 120  SER A CB  1 
ATOM   959   O OG  . SER A  1 120 ? -4.096  42.343 97.581  1.00 83.23  ? 120  SER A OG  1 
ATOM   960   N N   . SER A  1 121 ? -1.333  42.607 98.621  1.00 80.56  ? 121  SER A N   1 
ATOM   961   C CA  . SER A  1 121 ? -0.439  41.627 99.230  1.00 81.33  ? 121  SER A CA  1 
ATOM   962   C C   . SER A  1 121 ? 0.645   42.191 100.163 1.00 81.43  ? 121  SER A C   1 
ATOM   963   O O   . SER A  1 121 ? 1.243   41.437 100.928 1.00 83.01  ? 121  SER A O   1 
ATOM   964   C CB  . SER A  1 121 ? 0.181   40.765 98.128  1.00 78.93  ? 121  SER A CB  1 
ATOM   965   O OG  . SER A  1 121 ? 1.484   40.344 98.447  1.00 78.26  ? 121  SER A OG  1 
ATOM   966   N N   . TRP A  1 122 ? 0.892   43.498 100.105 1.00 80.11  ? 122  TRP A N   1 
ATOM   967   C CA  . TRP A  1 122 ? 1.824   44.149 101.026 1.00 80.76  ? 122  TRP A CA  1 
ATOM   968   C C   . TRP A  1 122 ? 1.146   44.397 102.369 1.00 84.88  ? 122  TRP A C   1 
ATOM   969   O O   . TRP A  1 122 ? 0.765   45.524 102.688 1.00 85.79  ? 122  TRP A O   1 
ATOM   970   C CB  . TRP A  1 122 ? 2.339   45.456 100.426 1.00 78.12  ? 122  TRP A CB  1 
ATOM   971   C CG  . TRP A  1 122 ? 3.108   45.230 99.172  1.00 74.35  ? 122  TRP A CG  1 
ATOM   972   C CD1 . TRP A  1 122 ? 2.672   45.427 97.897  1.00 71.99  ? 122  TRP A CD1 1 
ATOM   973   C CD2 . TRP A  1 122 ? 4.446   44.730 99.068  1.00 72.82  ? 122  TRP A CD2 1 
ATOM   974   N NE1 . TRP A  1 122 ? 3.661   45.096 97.002  1.00 69.05  ? 122  TRP A NE1 1 
ATOM   975   C CE2 . TRP A  1 122 ? 4.761   44.664 97.694  1.00 69.47  ? 122  TRP A CE2 1 
ATOM   976   C CE3 . TRP A  1 122 ? 5.414   44.340 100.004 1.00 74.21  ? 122  TRP A CE3 1 
ATOM   977   C CZ2 . TRP A  1 122 ? 6.004   44.222 97.230  1.00 67.43  ? 122  TRP A CZ2 1 
ATOM   978   C CZ3 . TRP A  1 122 ? 6.649   43.899 99.542  1.00 72.21  ? 122  TRP A CZ3 1 
ATOM   979   C CH2 . TRP A  1 122 ? 6.933   43.846 98.165  1.00 68.82  ? 122  TRP A CH2 1 
ATOM   980   N N   . SER A  1 123 ? 1.003   43.326 103.148 1.00 82.72  ? 123  SER A N   1 
ATOM   981   C CA  . SER A  1 123 ? 0.292   43.369 104.427 1.00 86.53  ? 123  SER A CA  1 
ATOM   982   C C   . SER A  1 123 ? 1.145   43.957 105.551 1.00 87.17  ? 123  SER A C   1 
ATOM   983   O O   . SER A  1 123 ? 0.606   44.496 106.517 1.00 90.03  ? 123  SER A O   1 
ATOM   984   C CB  . SER A  1 123 ? -0.177  41.964 104.819 1.00 88.73  ? 123  SER A CB  1 
ATOM   985   O OG  . SER A  1 123 ? 0.919   41.071 104.934 1.00 87.36  ? 123  SER A OG  1 
ATOM   986   N N   . SER A  1 124 ? 2.467   43.842 105.418 1.00 84.77  ? 124  SER A N   1 
ATOM   987   C CA  . SER A  1 124 ? 3.419   44.352 106.409 1.00 85.25  ? 124  SER A CA  1 
ATOM   988   C C   . SER A  1 124 ? 3.964   45.754 106.067 1.00 83.49  ? 124  SER A C   1 
ATOM   989   O O   . SER A  1 124 ? 4.757   46.315 106.825 1.00 83.88  ? 124  SER A O   1 
ATOM   990   C CB  . SER A  1 124 ? 4.578   43.360 106.553 1.00 84.06  ? 124  SER A CB  1 
ATOM   991   O OG  . SER A  1 124 ? 5.531   43.807 107.499 1.00 84.65  ? 124  SER A OG  1 
ATOM   992   N N   . HIS A  1 125 ? 3.536   46.312 104.934 1.00 81.80  ? 125  HIS A N   1 
ATOM   993   C CA  . HIS A  1 125 ? 3.982   47.639 104.488 1.00 80.20  ? 125  HIS A CA  1 
ATOM   994   C C   . HIS A  1 125 ? 2.803   48.474 103.998 1.00 81.06  ? 125  HIS A C   1 
ATOM   995   O O   . HIS A  1 125 ? 1.772   47.928 103.599 1.00 82.02  ? 125  HIS A O   1 
ATOM   996   C CB  . HIS A  1 125 ? 5.004   47.506 103.355 1.00 76.50  ? 125  HIS A CB  1 
ATOM   997   C CG  . HIS A  1 125 ? 6.298   46.880 103.774 1.00 75.65  ? 125  HIS A CG  1 
ATOM   998   N ND1 . HIS A  1 125 ? 6.537   45.526 103.673 1.00 75.32  ? 125  HIS A ND1 1 
ATOM   999   C CD2 . HIS A  1 125 ? 7.426   47.424 104.287 1.00 75.26  ? 125  HIS A CD2 1 
ATOM   1000  C CE1 . HIS A  1 125 ? 7.756   45.263 104.112 1.00 74.76  ? 125  HIS A CE1 1 
ATOM   1001  N NE2 . HIS A  1 125 ? 8.317   46.398 104.488 1.00 74.72  ? 125  HIS A NE2 1 
ATOM   1002  N N   . GLU A  1 126 ? 2.953   49.796 104.041 1.00 81.02  ? 126  GLU A N   1 
ATOM   1003  C CA  . GLU A  1 126 ? 1.935   50.701 103.510 1.00 81.70  ? 126  GLU A CA  1 
ATOM   1004  C C   . GLU A  1 126 ? 2.177   50.891 102.015 1.00 78.47  ? 126  GLU A C   1 
ATOM   1005  O O   . GLU A  1 126 ? 3.293   51.216 101.605 1.00 76.16  ? 126  GLU A O   1 
ATOM   1006  C CB  . GLU A  1 126 ? 1.978   52.046 104.235 1.00 83.34  ? 126  GLU A CB  1 
ATOM   1007  C CG  . GLU A  1 126 ? 0.915   53.040 103.788 1.00 84.44  ? 126  GLU A CG  1 
ATOM   1008  C CD  . GLU A  1 126 ? -0.501  52.528 104.000 1.00 87.24  ? 126  GLU A CD  1 
ATOM   1009  O OE1 . GLU A  1 126 ? -0.901  52.328 105.172 1.00 90.37  ? 126  GLU A OE1 1 
ATOM   1010  O OE2 . GLU A  1 126 ? -1.215  52.336 102.988 1.00 86.47  ? 126  GLU A OE2 1 
ATOM   1011  N N   . ALA A  1 127 ? 1.135   50.686 101.209 1.00 78.61  ? 127  ALA A N   1 
ATOM   1012  C CA  . ALA A  1 127 ? 1.267   50.668 99.742  1.00 75.73  ? 127  ALA A CA  1 
ATOM   1013  C C   . ALA A  1 127 ? 0.409   51.698 98.995  1.00 76.01  ? 127  ALA A C   1 
ATOM   1014  O O   . ALA A  1 127 ? 0.638   51.935 97.805  1.00 73.73  ? 127  ALA A O   1 
ATOM   1015  C CB  . ALA A  1 127 ? 0.959   49.270 99.221  1.00 75.28  ? 127  ALA A CB  1 
ATOM   1016  N N   . SER A  1 128 ? -0.560  52.309 99.678  1.00 78.89  ? 128  SER A N   1 
ATOM   1017  C CA  . SER A  1 128 ? -1.551  53.171 99.018  1.00 79.69  ? 128  SER A CA  1 
ATOM   1018  C C   . SER A  1 128 ? -1.302  54.673 99.197  1.00 79.90  ? 128  SER A C   1 
ATOM   1019  O O   . SER A  1 128 ? -2.084  55.492 98.712  1.00 80.78  ? 128  SER A O   1 
ATOM   1020  C CB  . SER A  1 128 ? -2.962  52.805 99.497  1.00 83.16  ? 128  SER A CB  1 
ATOM   1021  O OG  . SER A  1 128 ? -3.416  51.627 98.852  1.00 82.77  ? 128  SER A OG  1 
ATOM   1022  N N   . LEU A  1 129 ? -0.219  55.032 99.883  1.00 79.26  ? 129  LEU A N   1 
ATOM   1023  C CA  . LEU A  1 129 ? 0.163   56.435 100.042 1.00 79.46  ? 129  LEU A CA  1 
ATOM   1024  C C   . LEU A  1 129 ? 1.490   56.729 99.336  1.00 76.18  ? 129  LEU A C   1 
ATOM   1025  O O   . LEU A  1 129 ? 2.202   57.665 99.696  1.00 76.28  ? 129  LEU A O   1 
ATOM   1026  C CB  . LEU A  1 129 ? 0.244   56.807 101.529 1.00 82.27  ? 129  LEU A CB  1 
ATOM   1027  C CG  . LEU A  1 129 ? -1.087  56.857 102.291 1.00 86.10  ? 129  LEU A CG  1 
ATOM   1028  C CD1 . LEU A  1 129 ? -1.496  55.484 102.799 1.00 87.24  ? 129  LEU A CD1 1 
ATOM   1029  C CD2 . LEU A  1 129 ? -0.990  57.826 103.458 1.00 88.81  ? 129  LEU A CD2 1 
ATOM   1030  N N   . GLY A  1 130 ? 1.808   55.932 98.319  1.00 73.57  ? 130  GLY A N   1 
ATOM   1031  C CA  . GLY A  1 130 ? 3.016   56.129 97.523  1.00 70.55  ? 130  GLY A CA  1 
ATOM   1032  C C   . GLY A  1 130 ? 2.754   56.957 96.277  1.00 69.38  ? 130  GLY A C   1 
ATOM   1033  O O   . GLY A  1 130 ? 2.889   56.464 95.150  1.00 67.27  ? 130  GLY A O   1 
ATOM   1034  N N   . VAL A  1 131 ? 2.388   58.223 96.485  1.00 70.89  ? 131  VAL A N   1 
ATOM   1035  C CA  . VAL A  1 131 ? 2.024   59.132 95.392  1.00 70.30  ? 131  VAL A CA  1 
ATOM   1036  C C   . VAL A  1 131 ? 2.817   60.441 95.447  1.00 70.12  ? 131  VAL A C   1 
ATOM   1037  O O   . VAL A  1 131 ? 3.511   60.722 96.424  1.00 70.96  ? 131  VAL A O   1 
ATOM   1038  C CB  . VAL A  1 131 ? 0.507   59.455 95.399  1.00 72.82  ? 131  VAL A CB  1 
ATOM   1039  C CG1 . VAL A  1 131 ? -0.315  58.173 95.371  1.00 73.38  ? 131  VAL A CG1 1 
ATOM   1040  C CG2 . VAL A  1 131 ? 0.126   60.314 96.602  1.00 75.84  ? 131  VAL A CG2 1 
ATOM   1041  N N   . SER A  1 132 ? 2.702   61.231 94.382  1.00 69.30  ? 132  SER A N   1 
ATOM   1042  C CA  . SER A  1 132 ? 3.343   62.545 94.295  1.00 69.32  ? 132  SER A CA  1 
ATOM   1043  C C   . SER A  1 132 ? 2.495   63.499 93.460  1.00 70.09  ? 132  SER A C   1 
ATOM   1044  O O   . SER A  1 132 ? 1.672   63.068 92.649  1.00 69.80  ? 132  SER A O   1 
ATOM   1045  C CB  . SER A  1 132 ? 4.738   62.422 93.674  1.00 66.61  ? 132  SER A CB  1 
ATOM   1046  O OG  . SER A  1 132 ? 5.258   63.691 93.300  1.00 66.65  ? 132  SER A OG  1 
ATOM   1047  N N   . SER A  1 133 ? 2.713   64.796 93.660  1.00 71.20  ? 133  SER A N   1 
ATOM   1048  C CA  . SER A  1 133 ? 2.032   65.829 92.882  1.00 72.03  ? 133  SER A CA  1 
ATOM   1049  C C   . SER A  1 133 ? 2.548   65.899 91.439  1.00 69.45  ? 133  SER A C   1 
ATOM   1050  O O   . SER A  1 133 ? 1.875   66.448 90.566  1.00 69.86  ? 133  SER A O   1 
ATOM   1051  C CB  . SER A  1 133 ? 2.203   67.191 93.555  1.00 74.16  ? 133  SER A CB  1 
ATOM   1052  O OG  . SER A  1 133 ? 3.575   67.530 93.659  1.00 72.87  ? 133  SER A OG  1 
ATOM   1053  N N   . ALA A  1 134 ? 3.739   65.348 91.198  1.00 66.98  ? 134  ALA A N   1 
ATOM   1054  C CA  . ALA A  1 134 ? 4.339   65.335 89.861  1.00 64.63  ? 134  ALA A CA  1 
ATOM   1055  C C   . ALA A  1 134 ? 3.571   64.453 88.870  1.00 63.61  ? 134  ALA A C   1 
ATOM   1056  O O   . ALA A  1 134 ? 3.556   64.745 87.675  1.00 62.71  ? 134  ALA A O   1 
ATOM   1057  C CB  . ALA A  1 134 ? 5.796   64.902 89.939  1.00 62.66  ? 134  ALA A CB  1 
ATOM   1058  N N   . CYS A  1 135 ? 2.945   63.382 89.364  1.00 63.94  ? 135  CYS A N   1 
ATOM   1059  C CA  . CYS A  1 135 ? 2.043   62.549 88.556  1.00 63.62  ? 135  CYS A CA  1 
ATOM   1060  C C   . CYS A  1 135 ? 0.591   62.719 89.030  1.00 66.26  ? 135  CYS A C   1 
ATOM   1061  O O   . CYS A  1 135 ? 0.127   61.953 89.874  1.00 67.28  ? 135  CYS A O   1 
ATOM   1062  C CB  . CYS A  1 135 ? 2.434   61.063 88.641  1.00 62.14  ? 135  CYS A CB  1 
ATOM   1063  S SG  . CYS A  1 135 ? 4.198   60.687 88.514  1.00 59.55  ? 135  CYS A SG  1 
ATOM   1064  N N   . PRO A  1 136 ? -0.126  63.734 88.504  1.00 67.55  ? 136  PRO A N   1 
ATOM   1065  C CA  . PRO A  1 136 ? -1.528  63.943 88.877  1.00 70.37  ? 136  PRO A CA  1 
ATOM   1066  C C   . PRO A  1 136 ? -2.539  63.238 87.964  1.00 70.56  ? 136  PRO A C   1 
ATOM   1067  O O   . PRO A  1 136 ? -2.354  63.208 86.745  1.00 69.05  ? 136  PRO A O   1 
ATOM   1068  C CB  . PRO A  1 136 ? -1.683  65.456 88.749  1.00 71.85  ? 136  PRO A CB  1 
ATOM   1069  C CG  . PRO A  1 136 ? -0.768  65.813 87.628  1.00 69.52  ? 136  PRO A CG  1 
ATOM   1070  C CD  . PRO A  1 136 ? 0.403   64.877 87.735  1.00 66.94  ? 136  PRO A CD  1 
ATOM   1071  N N   . TYR A  1 137 ? -3.600  62.692 88.563  1.00 72.64  ? 137  TYR A N   1 
ATOM   1072  C CA  . TYR A  1 137 ? -4.712  62.074 87.827  1.00 73.55  ? 137  TYR A CA  1 
ATOM   1073  C C   . TYR A  1 137 ? -6.053  62.576 88.370  1.00 77.15  ? 137  TYR A C   1 
ATOM   1074  O O   . TYR A  1 137 ? -6.352  62.405 89.554  1.00 78.97  ? 137  TYR A O   1 
ATOM   1075  C CB  . TYR A  1 137 ? -4.641  60.547 87.940  1.00 72.55  ? 137  TYR A CB  1 
ATOM   1076  C CG  . TYR A  1 137 ? -5.843  59.806 87.373  1.00 74.05  ? 137  TYR A CG  1 
ATOM   1077  C CD1 . TYR A  1 137 ? -6.117  59.818 86.004  1.00 73.39  ? 137  TYR A CD1 1 
ATOM   1078  C CD2 . TYR A  1 137 ? -6.694  59.073 88.207  1.00 76.31  ? 137  TYR A CD2 1 
ATOM   1079  C CE1 . TYR A  1 137 ? -7.208  59.134 85.485  1.00 74.98  ? 137  TYR A CE1 1 
ATOM   1080  C CE2 . TYR A  1 137 ? -7.783  58.382 87.695  1.00 77.93  ? 137  TYR A CE2 1 
ATOM   1081  C CZ  . TYR A  1 137 ? -8.036  58.415 86.335  1.00 77.25  ? 137  TYR A CZ  1 
ATOM   1082  O OH  . TYR A  1 137 ? -9.118  57.733 85.828  1.00 79.08  ? 137  TYR A OH  1 
ATOM   1083  N N   . GLN A  1 138 ? -6.849  63.192 87.496  1.00 78.33  ? 138  GLN A N   1 
ATOM   1084  C CA  . GLN A  1 138 ? -8.152  63.763 87.863  1.00 81.98  ? 138  GLN A CA  1 
ATOM   1085  C C   . GLN A  1 138 ? -8.072  64.713 89.062  1.00 83.84  ? 138  GLN A C   1 
ATOM   1086  O O   . GLN A  1 138 ? -8.961  64.723 89.916  1.00 86.90  ? 138  GLN A O   1 
ATOM   1087  C CB  . GLN A  1 138 ? -9.175  62.653 88.135  1.00 83.82  ? 138  GLN A CB  1 
ATOM   1088  C CG  . GLN A  1 138 ? -9.267  61.622 87.022  1.00 82.23  ? 138  GLN A CG  1 
ATOM   1089  C CD  . GLN A  1 138 ? -10.570 60.838 87.040  1.00 84.96  ? 138  GLN A CD  1 
ATOM   1090  O OE1 . GLN A  1 138 ? -11.159 60.610 88.097  1.00 87.37  ? 138  GLN A OE1 1 
ATOM   1091  N NE2 . GLN A  1 138 ? -11.024 60.418 85.863  1.00 84.78  ? 138  GLN A NE2 1 
ATOM   1092  N N   . GLY A  1 139 ? -6.998  65.500 89.120  1.00 82.18  ? 139  GLY A N   1 
ATOM   1093  C CA  . GLY A  1 139 ? -6.817  66.508 90.168  1.00 83.94  ? 139  GLY A CA  1 
ATOM   1094  C C   . GLY A  1 139 ? -6.057  66.037 91.395  1.00 83.38  ? 139  GLY A C   1 
ATOM   1095  O O   . GLY A  1 139 ? -5.454  66.850 92.097  1.00 83.85  ? 139  GLY A O   1 
ATOM   1096  N N   . LYS A  1 140 ? -6.088  64.732 91.660  1.00 82.56  ? 140  LYS A N   1 
ATOM   1097  C CA  . LYS A  1 140 ? -5.424  64.165 92.831  1.00 82.24  ? 140  LYS A CA  1 
ATOM   1098  C C   . LYS A  1 140 ? -4.036  63.647 92.475  1.00 78.52  ? 140  LYS A C   1 
ATOM   1099  O O   . LYS A  1 140 ? -3.758  63.326 91.320  1.00 76.21  ? 140  LYS A O   1 
ATOM   1100  C CB  . LYS A  1 140 ? -6.261  63.034 93.445  1.00 83.93  ? 140  LYS A CB  1 
ATOM   1101  C CG  . LYS A  1 140 ? -7.568  63.492 94.079  1.00 88.11  ? 140  LYS A CG  1 
ATOM   1102  C CD  . LYS A  1 140 ? -8.761  63.288 93.153  1.00 89.36  ? 140  LYS A CD  1 
ATOM   1103  C CE  . LYS A  1 140 ? -9.950  64.154 93.547  1.00 93.50  ? 140  LYS A CE  1 
ATOM   1104  N NZ  . LYS A  1 140 ? -10.498 63.834 94.895  1.00 96.66  ? 140  LYS A NZ  1 
ATOM   1105  N N   . SER A  1 141 ? -3.172  63.576 93.484  1.00 78.22  ? 141  SER A N   1 
ATOM   1106  C CA  . SER A  1 141 ? -1.819  63.048 93.326  1.00 75.09  ? 141  SER A CA  1 
ATOM   1107  C C   . SER A  1 141 ? -1.862  61.539 93.085  1.00 73.68  ? 141  SER A C   1 
ATOM   1108  O O   . SER A  1 141 ? -2.552  60.810 93.799  1.00 75.43  ? 141  SER A O   1 
ATOM   1109  C CB  . SER A  1 141 ? -0.978  63.361 94.570  1.00 75.67  ? 141  SER A CB  1 
ATOM   1110  O OG  . SER A  1 141 ? -0.748  64.756 94.691  1.00 76.72  ? 141  SER A OG  1 
ATOM   1111  N N   . SER A  1 142 ? -1.123  61.084 92.075  1.00 70.72  ? 142  SER A N   1 
ATOM   1112  C CA  . SER A  1 142 ? -1.130  59.685 91.648  1.00 69.29  ? 142  SER A CA  1 
ATOM   1113  C C   . SER A  1 142 ? 0.307   59.219 91.393  1.00 66.32  ? 142  SER A C   1 
ATOM   1114  O O   . SER A  1 142 ? 1.259   59.881 91.817  1.00 65.75  ? 142  SER A O   1 
ATOM   1115  C CB  . SER A  1 142 ? -1.987  59.539 90.386  1.00 69.21  ? 142  SER A CB  1 
ATOM   1116  O OG  . SER A  1 142 ? -2.077  58.190 89.965  1.00 68.20  ? 142  SER A OG  1 
ATOM   1117  N N   . PHE A  1 143 ? 0.465   58.081 90.718  1.00 64.66  ? 143  PHE A N   1 
ATOM   1118  C CA  . PHE A  1 143 ? 1.794   57.544 90.412  1.00 62.03  ? 143  PHE A CA  1 
ATOM   1119  C C   . PHE A  1 143 ? 1.755   56.569 89.228  1.00 60.43  ? 143  PHE A C   1 
ATOM   1120  O O   . PHE A  1 143 ? 0.679   56.187 88.761  1.00 61.48  ? 143  PHE A O   1 
ATOM   1121  C CB  . PHE A  1 143 ? 2.376   56.852 91.656  1.00 62.28  ? 143  PHE A CB  1 
ATOM   1122  C CG  . PHE A  1 143 ? 3.879   56.734 91.647  1.00 60.16  ? 143  PHE A CG  1 
ATOM   1123  C CD1 . PHE A  1 143 ? 4.681   57.871 91.704  1.00 59.76  ? 143  PHE A CD1 1 
ATOM   1124  C CD2 . PHE A  1 143 ? 4.495   55.486 91.593  1.00 58.81  ? 143  PHE A CD2 1 
ATOM   1125  C CE1 . PHE A  1 143 ? 6.066   57.767 91.700  1.00 58.08  ? 143  PHE A CE1 1 
ATOM   1126  C CE2 . PHE A  1 143 ? 5.879   55.377 91.592  1.00 57.12  ? 143  PHE A CE2 1 
ATOM   1127  C CZ  . PHE A  1 143 ? 6.665   56.519 91.647  1.00 56.77  ? 143  PHE A CZ  1 
ATOM   1128  N N   . PHE A  1 144 ? 2.936   56.194 88.738  1.00 58.11  ? 144  PHE A N   1 
ATOM   1129  C CA  . PHE A  1 144 ? 3.079   55.128 87.745  1.00 56.64  ? 144  PHE A CA  1 
ATOM   1130  C C   . PHE A  1 144 ? 2.266   53.899 88.169  1.00 57.83  ? 144  PHE A C   1 
ATOM   1131  O O   . PHE A  1 144 ? 2.591   53.252 89.160  1.00 58.17  ? 144  PHE A O   1 
ATOM   1132  C CB  . PHE A  1 144 ? 4.552   54.721 87.600  1.00 54.50  ? 144  PHE A CB  1 
ATOM   1133  C CG  . PHE A  1 144 ? 5.472   55.843 87.191  1.00 53.43  ? 144  PHE A CG  1 
ATOM   1134  C CD1 . PHE A  1 144 ? 5.414   56.385 85.912  1.00 52.71  ? 144  PHE A CD1 1 
ATOM   1135  C CD2 . PHE A  1 144 ? 6.413   56.347 88.086  1.00 53.33  ? 144  PHE A CD2 1 
ATOM   1136  C CE1 . PHE A  1 144 ? 6.273   57.411 85.539  1.00 51.93  ? 144  PHE A CE1 1 
ATOM   1137  C CE2 . PHE A  1 144 ? 7.271   57.372 87.717  1.00 52.58  ? 144  PHE A CE2 1 
ATOM   1138  C CZ  . PHE A  1 144 ? 7.202   57.905 86.443  1.00 51.87  ? 144  PHE A CZ  1 
ATOM   1139  N N   . ARG A  1 145 ? 1.224   53.576 87.410  1.00 58.65  ? 145  ARG A N   1 
ATOM   1140  C CA  . ARG A  1 145 ? 0.256   52.545 87.802  1.00 60.35  ? 145  ARG A CA  1 
ATOM   1141  C C   . ARG A  1 145 ? 0.796   51.118 87.879  1.00 59.50  ? 145  ARG A C   1 
ATOM   1142  O O   . ARG A  1 145 ? 0.195   50.271 88.537  1.00 61.06  ? 145  ARG A O   1 
ATOM   1143  C CB  . ARG A  1 145 ? -0.930  52.542 86.841  1.00 61.52  ? 145  ARG A CB  1 
ATOM   1144  C CG  . ARG A  1 145 ? -1.675  53.857 86.761  1.00 62.91  ? 145  ARG A CG  1 
ATOM   1145  C CD  . ARG A  1 145 ? -3.122  53.614 86.380  1.00 65.24  ? 145  ARG A CD  1 
ATOM   1146  N NE  . ARG A  1 145 ? -3.785  54.854 85.992  1.00 66.43  ? 145  ARG A NE  1 
ATOM   1147  C CZ  . ARG A  1 145 ? -4.472  55.648 86.811  1.00 68.66  ? 145  ARG A CZ  1 
ATOM   1148  N NH1 . ARG A  1 145 ? -4.614  55.361 88.104  1.00 70.04  ? 145  ARG A NH1 1 
ATOM   1149  N NH2 . ARG A  1 145 ? -5.028  56.748 86.327  1.00 69.71  ? 145  ARG A NH2 1 
ATOM   1150  N N   . ASN A  1 146 ? 1.903   50.842 87.198  1.00 57.28  ? 146  ASN A N   1 
ATOM   1151  C CA  . ASN A  1 146 ? 2.434   49.479 87.120  1.00 56.53  ? 146  ASN A CA  1 
ATOM   1152  C C   . ASN A  1 146 ? 3.367   49.108 88.267  1.00 56.19  ? 146  ASN A C   1 
ATOM   1153  O O   . ASN A  1 146 ? 3.673   47.931 88.460  1.00 56.08  ? 146  ASN A O   1 
ATOM   1154  C CB  . ASN A  1 146 ? 3.135   49.259 85.774  1.00 54.61  ? 146  ASN A CB  1 
ATOM   1155  C CG  . ASN A  1 146 ? 2.158   49.200 84.613  1.00 55.27  ? 146  ASN A CG  1 
ATOM   1156  O OD1 . ASN A  1 146 ? 1.078   48.619 84.732  1.00 57.08  ? 146  ASN A OD1 1 
ATOM   1157  N ND2 . ASN A  1 146 ? 2.528   49.802 83.487  1.00 54.06  ? 146  ASN A ND2 1 
ATOM   1158  N N   . VAL A  1 147 ? 3.809   50.105 89.030  1.00 56.24  ? 147  VAL A N   1 
ATOM   1159  C CA  . VAL A  1 147 ? 4.709   49.870 90.160  1.00 56.18  ? 147  VAL A CA  1 
ATOM   1160  C C   . VAL A  1 147 ? 4.191   50.507 91.453  1.00 58.21  ? 147  VAL A C   1 
ATOM   1161  O O   . VAL A  1 147 ? 3.507   51.531 91.422  1.00 59.17  ? 147  VAL A O   1 
ATOM   1162  C CB  . VAL A  1 147 ? 6.138   50.377 89.863  1.00 54.18  ? 147  VAL A CB  1 
ATOM   1163  C CG1 . VAL A  1 147 ? 6.818   49.483 88.837  1.00 52.50  ? 147  VAL A CG1 1 
ATOM   1164  C CG2 . VAL A  1 147 ? 6.128   51.831 89.396  1.00 53.85  ? 147  VAL A CG2 1 
ATOM   1165  N N   . VAL A  1 148 ? 4.536   49.894 92.585  1.00 59.06  ? 148  VAL A N   1 
ATOM   1166  C CA  . VAL A  1 148 ? 4.066   50.333 93.905  1.00 61.33  ? 148  VAL A CA  1 
ATOM   1167  C C   . VAL A  1 148 ? 5.179   51.055 94.673  1.00 60.96  ? 148  VAL A C   1 
ATOM   1168  O O   . VAL A  1 148 ? 6.232   50.470 94.945  1.00 59.99  ? 148  VAL A O   1 
ATOM   1169  C CB  . VAL A  1 148 ? 3.580   49.129 94.749  1.00 63.08  ? 148  VAL A CB  1 
ATOM   1170  C CG1 . VAL A  1 148 ? 2.919   49.598 96.040  1.00 65.82  ? 148  VAL A CG1 1 
ATOM   1171  C CG2 . VAL A  1 148 ? 2.616   48.261 93.952  1.00 63.51  ? 148  VAL A CG2 1 
ATOM   1172  N N   . TRP A  1 149 ? 4.944   52.319 95.022  1.00 61.95  ? 149  TRP A N   1 
ATOM   1173  C CA  . TRP A  1 149 ? 5.871   53.068 95.872  1.00 62.22  ? 149  TRP A CA  1 
ATOM   1174  C C   . TRP A  1 149 ? 5.582   52.725 97.346  1.00 64.69  ? 149  TRP A C   1 
ATOM   1175  O O   . TRP A  1 149 ? 4.620   53.222 97.935  1.00 66.93  ? 149  TRP A O   1 
ATOM   1176  C CB  . TRP A  1 149 ? 5.746   54.576 95.614  1.00 62.48  ? 149  TRP A CB  1 
ATOM   1177  C CG  . TRP A  1 149 ? 6.816   55.433 96.273  1.00 62.56  ? 149  TRP A CG  1 
ATOM   1178  C CD1 . TRP A  1 149 ? 7.791   55.021 97.144  1.00 62.68  ? 149  TRP A CD1 1 
ATOM   1179  C CD2 . TRP A  1 149 ? 6.988   56.851 96.130  1.00 62.84  ? 149  TRP A CD2 1 
ATOM   1180  N NE1 . TRP A  1 149 ? 8.563   56.088 97.532  1.00 62.99  ? 149  TRP A NE1 1 
ATOM   1181  C CE2 . TRP A  1 149 ? 8.092   57.223 96.929  1.00 63.11  ? 149  TRP A CE2 1 
ATOM   1182  C CE3 . TRP A  1 149 ? 6.322   57.842 95.399  1.00 63.06  ? 149  TRP A CE3 1 
ATOM   1183  C CZ2 . TRP A  1 149 ? 8.545   58.543 97.017  1.00 63.62  ? 149  TRP A CZ2 1 
ATOM   1184  C CZ3 . TRP A  1 149 ? 6.774   59.156 95.487  1.00 63.56  ? 149  TRP A CZ3 1 
ATOM   1185  C CH2 . TRP A  1 149 ? 7.875   59.492 96.293  1.00 63.82  ? 149  TRP A CH2 1 
ATOM   1186  N N   . LEU A  1 150 ? 6.428   51.876 97.929  1.00 64.44  ? 150  LEU A N   1 
ATOM   1187  C CA  . LEU A  1 150 ? 6.217   51.365 99.285  1.00 66.80  ? 150  LEU A CA  1 
ATOM   1188  C C   . LEU A  1 150 ? 6.798   52.298 100.343 1.00 68.17  ? 150  LEU A C   1 
ATOM   1189  O O   . LEU A  1 150 ? 7.897   52.834 100.172 1.00 66.83  ? 150  LEU A O   1 
ATOM   1190  C CB  . LEU A  1 150 ? 6.842   49.971 99.442  1.00 66.12  ? 150  LEU A CB  1 
ATOM   1191  C CG  . LEU A  1 150 ? 6.210   48.821 98.648  1.00 65.52  ? 150  LEU A CG  1 
ATOM   1192  C CD1 . LEU A  1 150 ? 7.014   47.546 98.850  1.00 64.93  ? 150  LEU A CD1 1 
ATOM   1193  C CD2 . LEU A  1 150 ? 4.754   48.597 99.035  1.00 67.99  ? 150  LEU A CD2 1 
ATOM   1194  N N   . ILE A  1 151 ? 6.050   52.474 101.435 1.00 71.11  ? 151  ILE A N   1 
ATOM   1195  C CA  . ILE A  1 151 ? 6.500   53.248 102.600 1.00 73.02  ? 151  ILE A CA  1 
ATOM   1196  C C   . ILE A  1 151 ? 6.265   52.472 103.905 1.00 75.63  ? 151  ILE A C   1 
ATOM   1197  O O   . ILE A  1 151 ? 5.583   51.442 103.923 1.00 76.23  ? 151  ILE A O   1 
ATOM   1198  C CB  . ILE A  1 151 ? 5.812   54.635 102.673 1.00 74.53  ? 151  ILE A CB  1 
ATOM   1199  C CG1 . ILE A  1 151 ? 4.323   54.493 103.022 1.00 77.12  ? 151  ILE A CG1 1 
ATOM   1200  C CG2 . ILE A  1 151 ? 6.008   55.392 101.363 1.00 72.14  ? 151  ILE A CG2 1 
ATOM   1201  C CD1 . ILE A  1 151 ? 3.527   55.780 102.945 1.00 78.64  ? 151  ILE A CD1 1 
ATOM   1202  N N   . LYS A  1 152 ? 6.841   52.985 104.988 1.00 77.36  ? 152  LYS A N   1 
ATOM   1203  C CA  . LYS A  1 152 ? 6.745   52.362 106.316 1.00 80.14  ? 152  LYS A CA  1 
ATOM   1204  C C   . LYS A  1 152 ? 5.320   52.361 106.886 1.00 83.23  ? 152  LYS A C   1 
ATOM   1205  O O   . LYS A  1 152 ? 4.541   53.279 106.620 1.00 84.00  ? 152  LYS A O   1 
ATOM   1206  C CB  . LYS A  1 152 ? 7.690   53.070 107.298 1.00 81.45  ? 152  LYS A CB  1 
ATOM   1207  C CG  . LYS A  1 152 ? 7.373   54.543 107.527 1.00 82.95  ? 152  LYS A CG  1 
ATOM   1208  C CD  . LYS A  1 152 ? 8.432   55.232 108.370 1.00 84.09  ? 152  LYS A CD  1 
ATOM   1209  C CE  . LYS A  1 152 ? 7.960   56.622 108.786 1.00 86.36  ? 152  LYS A CE  1 
ATOM   1210  N NZ  . LYS A  1 152 ? 8.931   57.400 109.597 1.00 87.82  ? 152  LYS A NZ  1 
ATOM   1211  N N   . LYS A  1 153 ? 4.995   51.326 107.666 1.00 85.20  ? 153  LYS A N   1 
ATOM   1212  C CA  . LYS A  1 153 ? 3.715   51.239 108.384 1.00 88.70  ? 153  LYS A CA  1 
ATOM   1213  C C   . LYS A  1 153 ? 3.962   51.383 109.890 1.00 92.00  ? 153  LYS A C   1 
ATOM   1214  O O   . LYS A  1 153 ? 4.715   50.604 110.477 1.00 92.16  ? 153  LYS A O   1 
ATOM   1215  C CB  . LYS A  1 153 ? 3.002   49.907 108.091 1.00 88.86  ? 153  LYS A CB  1 
ATOM   1216  C CG  . LYS A  1 153 ? 1.484   49.958 108.315 1.00 91.86  ? 153  LYS A CG  1 
ATOM   1217  C CD  . LYS A  1 153 ? 0.838   48.612 108.641 1.00 93.62  ? 153  LYS A CD  1 
ATOM   1218  C CE  . LYS A  1 153 ? 0.079   48.014 107.472 1.00 92.28  ? 153  LYS A CE  1 
ATOM   1219  N NZ  . LYS A  1 153 ? 0.915   47.582 106.323 1.00 88.25  ? 153  LYS A NZ  1 
ATOM   1220  N N   . ASN A  1 154 ? 3.321   52.380 110.499 1.00 94.80  ? 154  ASN A N   1 
ATOM   1221  C CA  . ASN A  1 154 ? 3.499   52.711 111.921 1.00 98.33  ? 154  ASN A CA  1 
ATOM   1222  C C   . ASN A  1 154 ? 4.973   52.845 112.332 1.00 97.29  ? 154  ASN A C   1 
ATOM   1223  O O   . ASN A  1 154 ? 5.425   52.227 113.300 1.00 99.00  ? 154  ASN A O   1 
ATOM   1224  C CB  . ASN A  1 154 ? 2.763   51.706 112.820 1.00 101.57 ? 154  ASN A CB  1 
ATOM   1225  C CG  . ASN A  1 154 ? 2.432   52.280 114.192 1.00 106.11 ? 154  ASN A CG  1 
ATOM   1226  O OD1 . ASN A  1 154 ? 2.144   53.470 114.325 1.00 107.40 ? 154  ASN A OD1 1 
ATOM   1227  N ND2 . ASN A  1 154 ? 2.462   51.434 115.219 1.00 108.73 ? 154  ASN A ND2 1 
ATOM   1228  N N   . SER A  1 155 ? 5.706   53.659 111.573 1.00 94.65  ? 155  SER A N   1 
ATOM   1229  C CA  . SER A  1 155 ? 7.100   54.012 111.872 1.00 93.83  ? 155  SER A CA  1 
ATOM   1230  C C   . SER A  1 155 ? 8.067   52.819 111.894 1.00 92.25  ? 155  SER A C   1 
ATOM   1231  O O   . SER A  1 155 ? 8.999   52.787 112.694 1.00 93.34  ? 155  SER A O   1 
ATOM   1232  C CB  . SER A  1 155 ? 7.180   54.809 113.188 1.00 97.60  ? 155  SER A CB  1 
ATOM   1233  O OG  . SER A  1 155 ? 6.685   56.124 113.012 1.00 98.46  ? 155  SER A OG  1 
ATOM   1234  N N   . THR A  1 156 ? 7.845   51.842 111.017 1.00 89.93  ? 156  THR A N   1 
ATOM   1235  C CA  . THR A  1 156 ? 8.776   50.720 110.853 1.00 88.17  ? 156  THR A CA  1 
ATOM   1236  C C   . THR A  1 156 ? 8.749   50.252 109.406 1.00 84.61  ? 156  THR A C   1 
ATOM   1237  O O   . THR A  1 156 ? 7.676   49.978 108.868 1.00 84.51  ? 156  THR A O   1 
ATOM   1238  C CB  . THR A  1 156 ? 8.421   49.499 111.737 1.00 90.49  ? 156  THR A CB  1 
ATOM   1239  O OG1 . THR A  1 156 ? 7.361   48.749 111.128 1.00 90.07  ? 156  THR A OG1 1 
ATOM   1240  C CG2 . THR A  1 156 ? 8.009   49.906 113.154 1.00 94.70  ? 156  THR A CG2 1 
ATOM   1241  N N   . TYR A  1 157 ? 9.920   50.166 108.778 1.00 81.97  ? 157  TYR A N   1 
ATOM   1242  C CA  . TYR A  1 157 ? 10.033  49.600 107.434 1.00 78.73  ? 157  TYR A CA  1 
ATOM   1243  C C   . TYR A  1 157 ? 10.801  48.278 107.510 1.00 78.07  ? 157  TYR A C   1 
ATOM   1244  O O   . TYR A  1 157 ? 12.031  48.259 107.393 1.00 76.78  ? 157  TYR A O   1 
ATOM   1245  C CB  . TYR A  1 157 ? 10.715  50.579 106.476 1.00 76.21  ? 157  TYR A CB  1 
ATOM   1246  C CG  . TYR A  1 157 ? 10.523  50.224 105.011 1.00 73.24  ? 157  TYR A CG  1 
ATOM   1247  C CD1 . TYR A  1 157 ? 9.347   50.550 104.341 1.00 73.03  ? 157  TYR A CD1 1 
ATOM   1248  C CD2 . TYR A  1 157 ? 11.515  49.561 104.302 1.00 70.89  ? 157  TYR A CD2 1 
ATOM   1249  C CE1 . TYR A  1 157 ? 9.168   50.226 103.006 1.00 70.56  ? 157  TYR A CE1 1 
ATOM   1250  C CE2 . TYR A  1 157 ? 11.348  49.232 102.962 1.00 68.43  ? 157  TYR A CE2 1 
ATOM   1251  C CZ  . TYR A  1 157 ? 10.173  49.567 102.316 1.00 68.26  ? 157  TYR A CZ  1 
ATOM   1252  O OH  . TYR A  1 157 ? 9.998   49.244 100.986 1.00 66.01  ? 157  TYR A OH  1 
ATOM   1253  N N   . PRO A  1 158 ? 10.075  47.165 107.724 1.00 79.22  ? 158  PRO A N   1 
ATOM   1254  C CA  . PRO A  1 158 ? 10.733  45.864 107.822 1.00 78.90  ? 158  PRO A CA  1 
ATOM   1255  C C   . PRO A  1 158 ? 11.266  45.385 106.478 1.00 75.65  ? 158  PRO A C   1 
ATOM   1256  O O   . PRO A  1 158 ? 10.807  45.837 105.428 1.00 73.84  ? 158  PRO A O   1 
ATOM   1257  C CB  . PRO A  1 158 ? 9.618   44.939 108.328 1.00 81.18  ? 158  PRO A CB  1 
ATOM   1258  C CG  . PRO A  1 158 ? 8.356   45.585 107.878 1.00 81.44  ? 158  PRO A CG  1 
ATOM   1259  C CD  . PRO A  1 158 ? 8.615   47.062 107.915 1.00 81.14  ? 158  PRO A CD  1 
ATOM   1260  N N   . THR A  1 159 ? 12.235  44.477 106.525 1.00 75.18  ? 159  THR A N   1 
ATOM   1261  C CA  . THR A  1 159 ? 12.871  43.965 105.319 1.00 72.44  ? 159  THR A CA  1 
ATOM   1262  C C   . THR A  1 159 ? 11.855  43.231 104.446 1.00 71.80  ? 159  THR A C   1 
ATOM   1263  O O   . THR A  1 159 ? 11.002  42.493 104.949 1.00 73.68  ? 159  THR A O   1 
ATOM   1264  C CB  . THR A  1 159 ? 14.046  43.019 105.652 1.00 72.52  ? 159  THR A CB  1 
ATOM   1265  O OG1 . THR A  1 159 ? 14.959  43.677 106.538 1.00 73.62  ? 159  THR A OG1 1 
ATOM   1266  C CG2 . THR A  1 159 ? 14.794  42.603 104.388 1.00 69.74  ? 159  THR A CG2 1 
ATOM   1267  N N   . ILE A  1 160 ? 11.957  43.464 103.138 1.00 69.37  ? 160  ILE A N   1 
ATOM   1268  C CA  . ILE A  1 160 ? 11.108  42.826 102.137 1.00 68.58  ? 160  ILE A CA  1 
ATOM   1269  C C   . ILE A  1 160 ? 11.877  41.672 101.508 1.00 67.45  ? 160  ILE A C   1 
ATOM   1270  O O   . ILE A  1 160 ? 13.021  41.850 101.095 1.00 65.86  ? 160  ILE A O   1 
ATOM   1271  C CB  . ILE A  1 160 ? 10.725  43.825 101.023 1.00 66.67  ? 160  ILE A CB  1 
ATOM   1272  C CG1 . ILE A  1 160 ? 9.837   44.935 101.592 1.00 68.17  ? 160  ILE A CG1 1 
ATOM   1273  C CG2 . ILE A  1 160 ? 10.023  43.110 99.875  1.00 65.63  ? 160  ILE A CG2 1 
ATOM   1274  C CD1 . ILE A  1 160 ? 9.728   46.163 100.714 1.00 66.56  ? 160  ILE A CD1 1 
ATOM   1275  N N   . LYS A  1 161 ? 11.255  40.495 101.443 1.00 68.55  ? 161  LYS A N   1 
ATOM   1276  C CA  . LYS A  1 161 ? 11.838  39.334 100.757 1.00 67.66  ? 161  LYS A CA  1 
ATOM   1277  C C   . LYS A  1 161 ? 10.783  38.680 99.870  1.00 67.72  ? 161  LYS A C   1 
ATOM   1278  O O   . LYS A  1 161 ? 10.054  37.793 100.309 1.00 69.63  ? 161  LYS A O   1 
ATOM   1279  C CB  . LYS A  1 161 ? 12.395  38.319 101.763 1.00 69.44  ? 161  LYS A CB  1 
ATOM   1280  C CG  . LYS A  1 161 ? 13.694  38.745 102.430 1.00 69.37  ? 161  LYS A CG  1 
ATOM   1281  C CD  . LYS A  1 161 ? 14.080  37.796 103.554 1.00 71.63  ? 161  LYS A CD  1 
ATOM   1282  C CE  . LYS A  1 161 ? 15.377  38.223 104.228 1.00 71.83  ? 161  LYS A CE  1 
ATOM   1283  N NZ  . LYS A  1 161 ? 15.614  37.508 105.514 1.00 74.51  ? 161  LYS A NZ  1 
ATOM   1284  N N   . ARG A  1 162 ? 10.717  39.126 98.618  1.00 65.90  ? 162  ARG A N   1 
ATOM   1285  C CA  . ARG A  1 162 ? 9.681   38.696 97.685  1.00 66.02  ? 162  ARG A CA  1 
ATOM   1286  C C   . ARG A  1 162 ? 10.297  38.009 96.461  1.00 64.55  ? 162  ARG A C   1 
ATOM   1287  O O   . ARG A  1 162 ? 11.299  38.472 95.914  1.00 62.68  ? 162  ARG A O   1 
ATOM   1288  C CB  . ARG A  1 162 ? 8.813   39.902 97.278  1.00 65.56  ? 162  ARG A CB  1 
ATOM   1289  C CG  . ARG A  1 162 ? 7.779   40.304 98.314  1.00 67.91  ? 162  ARG A CG  1 
ATOM   1290  C CD  . ARG A  1 162 ? 6.775   39.192 98.624  1.00 70.18  ? 162  ARG A CD  1 
ATOM   1291  N NE  . ARG A  1 162 ? 5.406   39.563 98.257  1.00 71.17  ? 162  ARG A NE  1 
ATOM   1292  C CZ  . ARG A  1 162 ? 4.679   40.455 98.922  1.00 72.61  ? 162  ARG A CZ  1 
ATOM   1293  N NH1 . ARG A  1 162 ? 5.178   41.084 99.982  1.00 73.25  ? 162  ARG A NH1 1 
ATOM   1294  N NH2 . ARG A  1 162 ? 3.449   40.733 98.517  1.00 73.64  ? 162  ARG A NH2 1 
ATOM   1295  N N   . SER A  1 163 ? 9.700   36.889 96.059  1.00 65.79  ? 163  SER A N   1 
ATOM   1296  C CA  . SER A  1 163 ? 10.161  36.112 94.912  1.00 64.89  ? 163  SER A CA  1 
ATOM   1297  C C   . SER A  1 163 ? 8.992   35.808 93.978  1.00 65.68  ? 163  SER A C   1 
ATOM   1298  O O   . SER A  1 163 ? 7.890   35.521 94.443  1.00 67.62  ? 163  SER A O   1 
ATOM   1299  C CB  . SER A  1 163 ? 10.794  34.801 95.387  1.00 65.96  ? 163  SER A CB  1 
ATOM   1300  O OG  . SER A  1 163 ? 11.201  33.992 94.294  1.00 65.14  ? 163  SER A OG  1 
ATOM   1301  N N   . TYR A  1 164 ? 9.231   35.883 92.666  1.00 64.61  ? 164  TYR A N   1 
ATOM   1302  C CA  . TYR A  1 164 ? 8.235   35.467 91.674  1.00 65.56  ? 164  TYR A CA  1 
ATOM   1303  C C   . TYR A  1 164 ? 8.800   34.461 90.670  1.00 65.75  ? 164  TYR A C   1 
ATOM   1304  O O   . TYR A  1 164 ? 9.810   34.727 90.015  1.00 63.97  ? 164  TYR A O   1 
ATOM   1305  C CB  . TYR A  1 164 ? 7.663   36.657 90.907  1.00 64.30  ? 164  TYR A CB  1 
ATOM   1306  C CG  . TYR A  1 164 ? 6.875   36.204 89.700  1.00 64.49  ? 164  TYR A CG  1 
ATOM   1307  C CD1 . TYR A  1 164 ? 5.619   35.616 89.846  1.00 66.65  ? 164  TYR A CD1 1 
ATOM   1308  C CD2 . TYR A  1 164 ? 7.406   36.311 88.415  1.00 62.79  ? 164  TYR A CD2 1 
ATOM   1309  C CE1 . TYR A  1 164 ? 4.902   35.176 88.744  1.00 67.13  ? 164  TYR A CE1 1 
ATOM   1310  C CE2 . TYR A  1 164 ? 6.697   35.873 87.307  1.00 63.20  ? 164  TYR A CE2 1 
ATOM   1311  C CZ  . TYR A  1 164 ? 5.447   35.308 87.474  1.00 65.37  ? 164  TYR A CZ  1 
ATOM   1312  O OH  . TYR A  1 164 ? 4.747   34.875 86.372  1.00 66.04  ? 164  TYR A OH  1 
ATOM   1313  N N   . ASN A  1 165 ? 8.110   33.330 90.533  1.00 68.49  ? 165  ASN A N   1 
ATOM   1314  C CA  . ASN A  1 165 ? 8.475   32.285 89.581  1.00 69.43  ? 165  ASN A CA  1 
ATOM   1315  C C   . ASN A  1 165 ? 7.718   32.451 88.266  1.00 68.42  ? 165  ASN A C   1 
ATOM   1316  O O   . ASN A  1 165 ? 6.488   32.486 88.260  1.00 69.78  ? 165  ASN A O   1 
ATOM   1317  C CB  . ASN A  1 165 ? 8.149   30.917 90.179  1.00 73.43  ? 165  ASN A CB  1 
ATOM   1318  C CG  . ASN A  1 165 ? 8.814   29.776 89.439  1.00 75.66  ? 165  ASN A CG  1 
ATOM   1319  O OD1 . ASN A  1 165 ? 9.300   29.932 88.319  1.00 74.16  ? 165  ASN A OD1 1 
ATOM   1320  N ND2 . ASN A  1 165 ? 8.836   28.611 90.070  1.00 80.33  ? 165  ASN A ND2 1 
ATOM   1321  N N   . ASN A  1 166 ? 8.449   32.536 87.155  1.00 66.09  ? 166  ASN A N   1 
ATOM   1322  C CA  . ASN A  1 166 ? 7.825   32.672 85.838  1.00 65.26  ? 166  ASN A CA  1 
ATOM   1323  C C   . ASN A  1 166 ? 7.294   31.333 85.323  1.00 66.71  ? 166  ASN A C   1 
ATOM   1324  O O   . ASN A  1 166 ? 8.004   30.589 84.640  1.00 66.50  ? 166  ASN A O   1 
ATOM   1325  C CB  . ASN A  1 166 ? 8.804   33.278 84.827  1.00 63.04  ? 166  ASN A CB  1 
ATOM   1326  C CG  . ASN A  1 166 ? 8.122   33.699 83.537  1.00 62.76  ? 166  ASN A CG  1 
ATOM   1327  O OD1 . ASN A  1 166 ? 6.893   33.768 83.464  1.00 63.99  ? 166  ASN A OD1 1 
ATOM   1328  N ND2 . ASN A  1 166 ? 8.916   33.991 82.513  1.00 61.33  ? 166  ASN A ND2 1 
ATOM   1329  N N   . THR A  1 167 ? 6.039   31.042 85.657  1.00 68.16  ? 167  THR A N   1 
ATOM   1330  C CA  . THR A  1 167 ? 5.389   29.792 85.253  1.00 70.05  ? 167  THR A CA  1 
ATOM   1331  C C   . THR A  1 167 ? 4.803   29.832 83.836  1.00 69.85  ? 167  THR A C   1 
ATOM   1332  O O   . THR A  1 167 ? 4.488   28.781 83.274  1.00 71.60  ? 167  THR A O   1 
ATOM   1333  C CB  . THR A  1 167 ? 4.265   29.399 86.234  1.00 72.54  ? 167  THR A CB  1 
ATOM   1334  O OG1 . THR A  1 167 ? 3.374   30.508 86.415  1.00 72.43  ? 167  THR A OG1 1 
ATOM   1335  C CG2 . THR A  1 167 ? 4.851   28.986 87.577  1.00 73.01  ? 167  THR A CG2 1 
ATOM   1336  N N   . ASN A  1 168 ? 4.651   31.029 83.264  1.00 67.81  ? 168  ASN A N   1 
ATOM   1337  C CA  . ASN A  1 168 ? 4.203   31.157 81.869  1.00 67.54  ? 168  ASN A CA  1 
ATOM   1338  C C   . ASN A  1 168 ? 5.312   30.662 80.962  1.00 66.23  ? 168  ASN A C   1 
ATOM   1339  O O   . ASN A  1 168 ? 6.487   30.783 81.308  1.00 64.63  ? 168  ASN A O   1 
ATOM   1340  C CB  . ASN A  1 168 ? 3.869   32.605 81.462  1.00 66.07  ? 168  ASN A CB  1 
ATOM   1341  C CG  . ASN A  1 168 ? 3.424   33.472 82.622  1.00 65.96  ? 168  ASN A CG  1 
ATOM   1342  O OD1 . ASN A  1 168 ? 2.228   33.669 82.838  1.00 67.62  ? 168  ASN A OD1 1 
ATOM   1343  N ND2 . ASN A  1 168 ? 4.388   34.020 83.361  1.00 64.21  ? 168  ASN A ND2 1 
ATOM   1344  N N   . GLN A  1 169 ? 4.953   30.114 79.804  1.00 66.98  ? 169  GLN A N   1 
ATOM   1345  C CA  . GLN A  1 169 ? 5.964   29.708 78.829  1.00 66.02  ? 169  GLN A CA  1 
ATOM   1346  C C   . GLN A  1 169 ? 6.284   30.873 77.868  1.00 63.88  ? 169  GLN A C   1 
ATOM   1347  O O   . GLN A  1 169 ? 6.202   30.743 76.645  1.00 64.30  ? 169  GLN A O   1 
ATOM   1348  C CB  . GLN A  1 169 ? 5.566   28.415 78.101  1.00 68.42  ? 169  GLN A CB  1 
ATOM   1349  C CG  . GLN A  1 169 ? 4.276   28.456 77.293  1.00 70.16  ? 169  GLN A CG  1 
ATOM   1350  C CD  . GLN A  1 169 ? 4.315   27.515 76.091  1.00 71.83  ? 169  GLN A CD  1 
ATOM   1351  O OE1 . GLN A  1 169 ? 3.295   26.948 75.699  1.00 74.31  ? 169  GLN A OE1 1 
ATOM   1352  N NE2 . GLN A  1 169 ? 5.498   27.348 75.500  1.00 70.70  ? 169  GLN A NE2 1 
ATOM   1353  N N   . GLU A  1 170 ? 6.654   32.008 78.460  1.00 61.66  ? 170  GLU A N   1 
ATOM   1354  C CA  . GLU A  1 170 ? 7.019   33.224 77.734  1.00 59.61  ? 170  GLU A CA  1 
ATOM   1355  C C   . GLU A  1 170 ? 8.151   33.939 78.468  1.00 57.38  ? 170  GLU A C   1 
ATOM   1356  O O   . GLU A  1 170 ? 8.359   33.723 79.665  1.00 57.41  ? 170  GLU A O   1 
ATOM   1357  C CB  . GLU A  1 170 ? 5.828   34.191 77.629  1.00 59.80  ? 170  GLU A CB  1 
ATOM   1358  C CG  . GLU A  1 170 ? 4.784   33.836 76.578  1.00 61.63  ? 170  GLU A CG  1 
ATOM   1359  C CD  . GLU A  1 170 ? 3.528   33.198 77.150  1.00 63.99  ? 170  GLU A CD  1 
ATOM   1360  O OE1 . GLU A  1 170 ? 3.597   32.561 78.225  1.00 64.62  ? 170  GLU A OE1 1 
ATOM   1361  O OE2 . GLU A  1 170 ? 2.459   33.332 76.517  1.00 65.40  ? 170  GLU A OE2 1 
ATOM   1362  N N   . ASP A  1 171 ? 8.882   34.783 77.745  1.00 55.63  ? 171  ASP A N   1 
ATOM   1363  C CA  . ASP A  1 171 ? 9.759   35.762 78.374  1.00 53.65  ? 171  ASP A CA  1 
ATOM   1364  C C   . ASP A  1 171 ? 8.860   36.799 79.039  1.00 53.29  ? 171  ASP A C   1 
ATOM   1365  O O   . ASP A  1 171 ? 7.717   37.011 78.613  1.00 54.16  ? 171  ASP A O   1 
ATOM   1366  C CB  . ASP A  1 171 ? 10.674  36.449 77.349  1.00 52.36  ? 171  ASP A CB  1 
ATOM   1367  C CG  . ASP A  1 171 ? 11.723  35.514 76.758  1.00 52.64  ? 171  ASP A CG  1 
ATOM   1368  O OD1 . ASP A  1 171 ? 12.245  34.629 77.472  1.00 53.10  ? 171  ASP A OD1 1 
ATOM   1369  O OD2 . ASP A  1 171 ? 12.043  35.688 75.565  1.00 52.54  ? 171  ASP A OD2 1 
ATOM   1370  N N   . LEU A  1 172 ? 9.374   37.434 80.088  1.00 52.17  ? 172  LEU A N   1 
ATOM   1371  C CA  . LEU A  1 172 ? 8.600   38.400 80.853  1.00 52.03  ? 172  LEU A CA  1 
ATOM   1372  C C   . LEU A  1 172 ? 9.414   39.658 81.116  1.00 50.25  ? 172  LEU A C   1 
ATOM   1373  O O   . LEU A  1 172 ? 10.493  39.591 81.702  1.00 49.52  ? 172  LEU A O   1 
ATOM   1374  C CB  . LEU A  1 172 ? 8.161   37.777 82.176  1.00 53.27  ? 172  LEU A CB  1 
ATOM   1375  C CG  . LEU A  1 172 ? 7.199   38.603 83.038  1.00 53.86  ? 172  LEU A CG  1 
ATOM   1376  C CD1 . LEU A  1 172 ? 5.812   38.663 82.413  1.00 55.19  ? 172  LEU A CD1 1 
ATOM   1377  C CD2 . LEU A  1 172 ? 7.124   38.018 84.440  1.00 54.97  ? 172  LEU A CD2 1 
ATOM   1378  N N   . LEU A  1 173 ? 8.889   40.799 80.674  1.00 49.72  ? 173  LEU A N   1 
ATOM   1379  C CA  . LEU A  1 173 ? 9.507   42.091 80.944  1.00 48.34  ? 173  LEU A CA  1 
ATOM   1380  C C   . LEU A  1 173 ? 9.083   42.584 82.320  1.00 48.72  ? 173  LEU A C   1 
ATOM   1381  O O   . LEU A  1 173 ? 7.934   42.984 82.514  1.00 49.63  ? 173  LEU A O   1 
ATOM   1382  C CB  . LEU A  1 173 ? 9.107   43.124 79.891  1.00 47.92  ? 173  LEU A CB  1 
ATOM   1383  C CG  . LEU A  1 173 ? 9.576   44.563 80.150  1.00 46.88  ? 173  LEU A CG  1 
ATOM   1384  C CD1 . LEU A  1 173 ? 11.093  44.676 80.093  1.00 45.71  ? 173  LEU A CD1 1 
ATOM   1385  C CD2 . LEU A  1 173 ? 8.933   45.517 79.158  1.00 46.90  ? 173  LEU A CD2 1 
ATOM   1386  N N   . VAL A  1 174 ? 10.023  42.568 83.261  1.00 48.20  ? 174  VAL A N   1 
ATOM   1387  C CA  . VAL A  1 174 ? 9.789   43.058 84.614  1.00 48.65  ? 174  VAL A CA  1 
ATOM   1388  C C   . VAL A  1 174 ? 10.396  44.452 84.768  1.00 47.64  ? 174  VAL A C   1 
ATOM   1389  O O   . VAL A  1 174 ? 11.501  44.713 84.289  1.00 46.50  ? 174  VAL A O   1 
ATOM   1390  C CB  . VAL A  1 174 ? 10.417  42.123 85.667  1.00 49.11  ? 174  VAL A CB  1 
ATOM   1391  C CG1 . VAL A  1 174 ? 10.013  42.555 87.071  1.00 50.05  ? 174  VAL A CG1 1 
ATOM   1392  C CG2 . VAL A  1 174 ? 10.011  40.678 85.414  1.00 50.12  ? 174  VAL A CG2 1 
ATOM   1393  N N   . LEU A  1 175 ? 9.663   45.334 85.446  1.00 48.28  ? 175  LEU A N   1 
ATOM   1394  C CA  . LEU A  1 175 ? 10.119  46.692 85.739  1.00 47.72  ? 175  LEU A CA  1 
ATOM   1395  C C   . LEU A  1 175 ? 10.060  46.947 87.239  1.00 48.69  ? 175  LEU A C   1 
ATOM   1396  O O   . LEU A  1 175 ? 9.096   46.562 87.897  1.00 50.06  ? 175  LEU A O   1 
ATOM   1397  C CB  . LEU A  1 175 ? 9.222   47.715 85.046  1.00 47.84  ? 175  LEU A CB  1 
ATOM   1398  C CG  . LEU A  1 175 ? 9.076   47.622 83.529  1.00 47.23  ? 175  LEU A CG  1 
ATOM   1399  C CD1 . LEU A  1 175 ? 7.873   48.434 83.066  1.00 47.97  ? 175  LEU A CD1 1 
ATOM   1400  C CD2 . LEU A  1 175 ? 10.351  48.090 82.844  1.00 45.85  ? 175  LEU A CD2 1 
ATOM   1401  N N   . TRP A  1 176 ? 11.086  47.607 87.770  1.00 48.22  ? 176  TRP A N   1 
ATOM   1402  C CA  . TRP A  1 176 ? 11.076  48.081 89.152  1.00 49.27  ? 176  TRP A CA  1 
ATOM   1403  C C   . TRP A  1 176 ? 11.879  49.374 89.256  1.00 48.81  ? 176  TRP A C   1 
ATOM   1404  O O   . TRP A  1 176 ? 12.416  49.857 88.257  1.00 47.68  ? 176  TRP A O   1 
ATOM   1405  C CB  . TRP A  1 176 ? 11.626  47.008 90.103  1.00 49.83  ? 176  TRP A CB  1 
ATOM   1406  C CG  . TRP A  1 176 ? 13.079  46.701 89.912  1.00 48.78  ? 176  TRP A CG  1 
ATOM   1407  C CD1 . TRP A  1 176 ? 14.126  47.199 90.634  1.00 48.80  ? 176  TRP A CD1 1 
ATOM   1408  C CD2 . TRP A  1 176 ? 13.645  45.820 88.939  1.00 47.83  ? 176  TRP A CD2 1 
ATOM   1409  N NE1 . TRP A  1 176 ? 15.309  46.681 90.171  1.00 47.97  ? 176  TRP A NE1 1 
ATOM   1410  C CE2 . TRP A  1 176 ? 15.043  45.832 89.128  1.00 47.36  ? 176  TRP A CE2 1 
ATOM   1411  C CE3 . TRP A  1 176 ? 13.107  45.020 87.924  1.00 47.55  ? 176  TRP A CE3 1 
ATOM   1412  C CZ2 . TRP A  1 176 ? 15.911  45.076 88.336  1.00 46.64  ? 176  TRP A CZ2 1 
ATOM   1413  C CZ3 . TRP A  1 176 ? 13.970  44.269 87.140  1.00 46.82  ? 176  TRP A CZ3 1 
ATOM   1414  C CH2 . TRP A  1 176 ? 15.356  44.303 87.350  1.00 46.38  ? 176  TRP A CH2 1 
ATOM   1415  N N   . GLY A  1 177 ? 11.958  49.933 90.461  1.00 49.94  ? 177  GLY A N   1 
ATOM   1416  C CA  . GLY A  1 177 ? 12.664  51.194 90.665  1.00 49.89  ? 177  GLY A CA  1 
ATOM   1417  C C   . GLY A  1 177 ? 13.202  51.416 92.065  1.00 51.12  ? 177  GLY A C   1 
ATOM   1418  O O   . GLY A  1 177 ? 12.852  50.706 93.010  1.00 52.24  ? 177  GLY A O   1 
ATOM   1419  N N   . ILE A  1 178 ? 14.066  52.421 92.177  1.00 51.11  ? 178  ILE A N   1 
ATOM   1420  C CA  . ILE A  1 178 ? 14.612  52.867 93.454  1.00 52.51  ? 178  ILE A CA  1 
ATOM   1421  C C   . ILE A  1 178 ? 14.314  54.361 93.586  1.00 53.36  ? 178  ILE A C   1 
ATOM   1422  O O   . ILE A  1 178 ? 14.340  55.091 92.592  1.00 52.49  ? 178  ILE A O   1 
ATOM   1423  C CB  . ILE A  1 178 ? 16.141  52.603 93.550  1.00 52.03  ? 178  ILE A CB  1 
ATOM   1424  C CG1 . ILE A  1 178 ? 16.659  52.885 94.976  1.00 53.71  ? 178  ILE A CG1 1 
ATOM   1425  C CG2 . ILE A  1 178 ? 16.902  53.403 92.497  1.00 50.91  ? 178  ILE A CG2 1 
ATOM   1426  C CD1 . ILE A  1 178 ? 18.149  53.145 95.088  1.00 53.70  ? 178  ILE A CD1 1 
ATOM   1427  N N   . HIS A  1 179 ? 14.016  54.807 94.804  1.00 55.30  ? 179  HIS A N   1 
ATOM   1428  C CA  . HIS A  1 179 ? 13.819  56.232 95.066  1.00 56.50  ? 179  HIS A CA  1 
ATOM   1429  C C   . HIS A  1 179 ? 15.055  56.860 95.706  1.00 57.19  ? 179  HIS A C   1 
ATOM   1430  O O   . HIS A  1 179 ? 15.628  56.314 96.655  1.00 58.02  ? 179  HIS A O   1 
ATOM   1431  C CB  . HIS A  1 179 ? 12.604  56.467 95.961  1.00 58.58  ? 179  HIS A CB  1 
ATOM   1432  C CG  . HIS A  1 179 ? 12.413  57.903 96.341  1.00 60.19  ? 179  HIS A CG  1 
ATOM   1433  N ND1 . HIS A  1 179 ? 12.310  58.321 97.650  1.00 62.56  ? 179  HIS A ND1 1 
ATOM   1434  C CD2 . HIS A  1 179 ? 12.335  59.021 95.582  1.00 59.97  ? 179  HIS A CD2 1 
ATOM   1435  C CE1 . HIS A  1 179 ? 12.158  59.633 97.681  1.00 63.70  ? 179  HIS A CE1 1 
ATOM   1436  N NE2 . HIS A  1 179 ? 12.172  60.082 96.439  1.00 62.18  ? 179  HIS A NE2 1 
ATOM   1437  N N   . HIS A  1 180 ? 15.450  58.014 95.175  1.00 57.01  ? 180  HIS A N   1 
ATOM   1438  C CA  . HIS A  1 180 ? 16.569  58.784 95.696  1.00 57.94  ? 180  HIS A CA  1 
ATOM   1439  C C   . HIS A  1 180 ? 16.006  60.022 96.400  1.00 59.95  ? 180  HIS A C   1 
ATOM   1440  O O   . HIS A  1 180 ? 15.508  60.935 95.735  1.00 59.88  ? 180  HIS A O   1 
ATOM   1441  C CB  . HIS A  1 180 ? 17.493  59.213 94.555  1.00 56.60  ? 180  HIS A CB  1 
ATOM   1442  C CG  . HIS A  1 180 ? 18.085  58.072 93.783  1.00 54.82  ? 180  HIS A CG  1 
ATOM   1443  N ND1 . HIS A  1 180 ? 19.429  57.774 93.817  1.00 54.68  ? 180  HIS A ND1 1 
ATOM   1444  C CD2 . HIS A  1 180 ? 17.524  57.173 92.939  1.00 53.33  ? 180  HIS A CD2 1 
ATOM   1445  C CE1 . HIS A  1 180 ? 19.671  56.737 93.036  1.00 53.16  ? 180  HIS A CE1 1 
ATOM   1446  N NE2 . HIS A  1 180 ? 18.532  56.353 92.492  1.00 52.30  ? 180  HIS A NE2 1 
ATOM   1447  N N   . PRO A  1 181 ? 16.068  60.054 97.745  1.00 61.91  ? 181  PRO A N   1 
ATOM   1448  C CA  . PRO A  1 181 ? 15.503  61.172 98.501  1.00 64.15  ? 181  PRO A CA  1 
ATOM   1449  C C   . PRO A  1 181 ? 16.428  62.389 98.534  1.00 65.04  ? 181  PRO A C   1 
ATOM   1450  O O   . PRO A  1 181 ? 17.602  62.286 98.175  1.00 64.18  ? 181  PRO A O   1 
ATOM   1451  C CB  . PRO A  1 181 ? 15.334  60.585 99.902  1.00 66.04  ? 181  PRO A CB  1 
ATOM   1452  C CG  . PRO A  1 181 ? 16.442  59.594 100.019 1.00 65.12  ? 181  PRO A CG  1 
ATOM   1453  C CD  . PRO A  1 181 ? 16.690  59.053 98.633  1.00 62.38  ? 181  PRO A CD  1 
ATOM   1454  N N   . ASN A  1 182 ? 15.897  63.525 98.977  1.00 66.96  ? 182  ASN A N   1 
ATOM   1455  C CA  . ASN A  1 182 ? 16.630  64.794 98.950  1.00 68.09  ? 182  ASN A CA  1 
ATOM   1456  C C   . ASN A  1 182 ? 17.718  64.902 100.018 1.00 69.87  ? 182  ASN A C   1 
ATOM   1457  O O   . ASN A  1 182 ? 18.837  65.328 99.723  1.00 69.81  ? 182  ASN A O   1 
ATOM   1458  C CB  . ASN A  1 182 ? 15.660  65.970 99.084  1.00 69.87  ? 182  ASN A CB  1 
ATOM   1459  C CG  . ASN A  1 182 ? 14.778  66.132 97.865  1.00 68.28  ? 182  ASN A CG  1 
ATOM   1460  O OD1 . ASN A  1 182 ? 15.061  66.951 97.001  1.00 67.80  ? 182  ASN A OD1 1 
ATOM   1461  N ND2 . ASN A  1 182 ? 13.716  65.337 97.780  1.00 67.60  ? 182  ASN A ND2 1 
ATOM   1462  N N   . ASP A  1 183 ? 17.376  64.526 101.251 1.00 71.67  ? 183  ASP A N   1 
ATOM   1463  C CA  . ASP A  1 183 ? 18.312  64.573 102.384 1.00 73.74  ? 183  ASP A CA  1 
ATOM   1464  C C   . ASP A  1 183 ? 18.080  63.410 103.357 1.00 74.34  ? 183  ASP A C   1 
ATOM   1465  O O   . ASP A  1 183 ? 17.108  62.660 103.223 1.00 73.41  ? 183  ASP A O   1 
ATOM   1466  C CB  . ASP A  1 183 ? 18.210  65.923 103.117 1.00 76.77  ? 183  ASP A CB  1 
ATOM   1467  C CG  . ASP A  1 183 ? 16.775  66.308 103.464 1.00 78.11  ? 183  ASP A CG  1 
ATOM   1468  O OD1 . ASP A  1 183 ? 15.971  65.421 103.822 1.00 77.93  ? 183  ASP A OD1 1 
ATOM   1469  O OD2 . ASP A  1 183 ? 16.454  67.511 103.383 1.00 79.57  ? 183  ASP A OD2 1 
ATOM   1470  N N   . ALA A  1 184 ? 18.977  63.271 104.333 1.00 76.10  ? 184  ALA A N   1 
ATOM   1471  C CA  . ALA A  1 184 ? 18.885  62.208 105.344 1.00 77.05  ? 184  ALA A CA  1 
ATOM   1472  C C   . ALA A  1 184 ? 17.601  62.290 106.180 1.00 79.07  ? 184  ALA A C   1 
ATOM   1473  O O   . ALA A  1 184 ? 17.119  61.272 106.679 1.00 79.20  ? 184  ALA A O   1 
ATOM   1474  C CB  . ALA A  1 184 ? 20.107  62.235 106.253 1.00 79.00  ? 184  ALA A CB  1 
ATOM   1475  N N   . ALA A  1 185 ? 17.060  63.500 106.326 1.00 80.82  ? 185  ALA A N   1 
ATOM   1476  C CA  . ALA A  1 185 ? 15.801  63.719 107.044 1.00 83.02  ? 185  ALA A CA  1 
ATOM   1477  C C   . ALA A  1 185 ? 14.596  63.120 106.309 1.00 81.21  ? 185  ALA A C   1 
ATOM   1478  O O   . ALA A  1 185 ? 13.691  62.570 106.940 1.00 82.45  ? 185  ALA A O   1 
ATOM   1479  C CB  . ALA A  1 185 ? 15.586  65.207 107.285 1.00 85.38  ? 185  ALA A CB  1 
ATOM   1480  N N   . GLU A  1 186 ? 14.586  63.229 104.983 1.00 78.53  ? 186  GLU A N   1 
ATOM   1481  C CA  . GLU A  1 186 ? 13.514  62.643 104.175 1.00 76.79  ? 186  GLU A CA  1 
ATOM   1482  C C   . GLU A  1 186 ? 13.642  61.119 104.081 1.00 75.09  ? 186  GLU A C   1 
ATOM   1483  O O   . GLU A  1 186 ? 12.634  60.409 104.057 1.00 74.95  ? 186  GLU A O   1 
ATOM   1484  C CB  . GLU A  1 186 ? 13.487  63.256 102.773 1.00 74.65  ? 186  GLU A CB  1 
ATOM   1485  C CG  . GLU A  1 186 ? 12.226  62.918 101.990 1.00 73.52  ? 186  GLU A CG  1 
ATOM   1486  C CD  . GLU A  1 186 ? 12.107  63.696 100.694 1.00 72.01  ? 186  GLU A CD  1 
ATOM   1487  O OE1 . GLU A  1 186 ? 12.999  63.557 99.828  1.00 69.80  ? 186  GLU A OE1 1 
ATOM   1488  O OE2 . GLU A  1 186 ? 11.115  64.441 100.539 1.00 73.13  ? 186  GLU A OE2 1 
ATOM   1489  N N   . GLN A  1 187 ? 14.880  60.627 104.018 1.00 74.02  ? 187  GLN A N   1 
ATOM   1490  C CA  . GLN A  1 187 ? 15.158  59.186 104.039 1.00 72.79  ? 187  GLN A CA  1 
ATOM   1491  C C   . GLN A  1 187 ? 14.506  58.536 105.259 1.00 75.12  ? 187  GLN A C   1 
ATOM   1492  O O   . GLN A  1 187 ? 13.761  57.559 105.135 1.00 74.50  ? 187  GLN A O   1 
ATOM   1493  C CB  . GLN A  1 187 ? 16.676  58.929 104.043 1.00 72.10  ? 187  GLN A CB  1 
ATOM   1494  C CG  . GLN A  1 187 ? 17.104  57.491 104.338 1.00 71.51  ? 187  GLN A CG  1 
ATOM   1495  C CD  . GLN A  1 187 ? 16.615  56.492 103.297 1.00 68.93  ? 187  GLN A CD  1 
ATOM   1496  O OE1 . GLN A  1 187 ? 16.713  56.736 102.095 1.00 66.79  ? 187  GLN A OE1 1 
ATOM   1497  N NE2 . GLN A  1 187 ? 16.098  55.355 103.757 1.00 69.30  ? 187  GLN A NE2 1 
ATOM   1498  N N   . THR A  1 188 ? 14.790  59.091 106.435 1.00 78.02  ? 188  THR A N   1 
ATOM   1499  C CA  . THR A  1 188 ? 14.222  58.587 107.681 1.00 80.71  ? 188  THR A CA  1 
ATOM   1500  C C   . THR A  1 188 ? 12.704  58.797 107.729 1.00 81.87  ? 188  THR A C   1 
ATOM   1501  O O   . THR A  1 188 ? 11.968  57.926 108.193 1.00 82.76  ? 188  THR A O   1 
ATOM   1502  C CB  . THR A  1 188 ? 14.869  59.254 108.913 1.00 83.83  ? 188  THR A CB  1 
ATOM   1503  O OG1 . THR A  1 188 ? 14.750  60.678 108.805 1.00 84.94  ? 188  THR A OG1 1 
ATOM   1504  C CG2 . THR A  1 188 ? 16.347  58.872 109.029 1.00 83.21  ? 188  THR A CG2 1 
ATOM   1505  N N   . LYS A  1 189 ? 12.237  59.943 107.240 1.00 82.05  ? 189  LYS A N   1 
ATOM   1506  C CA  . LYS A  1 189 ? 10.801  60.229 107.202 1.00 83.31  ? 189  LYS A CA  1 
ATOM   1507  C C   . LYS A  1 189 ? 10.019  59.196 106.387 1.00 81.29  ? 189  LYS A C   1 
ATOM   1508  O O   . LYS A  1 189 ? 8.907   58.820 106.757 1.00 82.83  ? 189  LYS A O   1 
ATOM   1509  C CB  . LYS A  1 189 ? 10.537  61.625 106.632 1.00 83.54  ? 189  LYS A CB  1 
ATOM   1510  C CG  . LYS A  1 189 ? 9.059   61.910 106.411 1.00 84.66  ? 189  LYS A CG  1 
ATOM   1511  C CD  . LYS A  1 189 ? 8.793   63.320 105.923 1.00 85.28  ? 189  LYS A CD  1 
ATOM   1512  C CE  . LYS A  1 189 ? 7.297   63.572 105.824 1.00 86.87  ? 189  LYS A CE  1 
ATOM   1513  N NZ  . LYS A  1 189 ? 6.964   64.484 104.700 1.00 85.82  ? 189  LYS A NZ  1 
ATOM   1514  N N   . LEU A  1 190 ? 10.597  58.757 105.273 1.00 78.08  ? 190  LEU A N   1 
ATOM   1515  C CA  . LEU A  1 190 ? 9.922   57.832 104.365 1.00 76.12  ? 190  LEU A CA  1 
ATOM   1516  C C   . LEU A  1 190 ? 10.112  56.370 104.752 1.00 75.77  ? 190  LEU A C   1 
ATOM   1517  O O   . LEU A  1 190 ? 9.152   55.600 104.775 1.00 76.24  ? 190  LEU A O   1 
ATOM   1518  C CB  . LEU A  1 190 ? 10.423  58.038 102.934 1.00 73.07  ? 190  LEU A CB  1 
ATOM   1519  C CG  . LEU A  1 190 ? 9.784   59.203 102.182 1.00 73.08  ? 190  LEU A CG  1 
ATOM   1520  C CD1 . LEU A  1 190 ? 10.595  59.563 100.944 1.00 70.43  ? 190  LEU A CD1 1 
ATOM   1521  C CD2 . LEU A  1 190 ? 8.356   58.850 101.803 1.00 73.48  ? 190  LEU A CD2 1 
ATOM   1522  N N   . TYR A  1 191 ? 11.358  55.996 105.032 1.00 75.05  ? 191  TYR A N   1 
ATOM   1523  C CA  . TYR A  1 191 ? 11.728  54.592 105.235 1.00 74.39  ? 191  TYR A CA  1 
ATOM   1524  C C   . TYR A  1 191 ? 12.383  54.305 106.592 1.00 76.60  ? 191  TYR A C   1 
ATOM   1525  O O   . TYR A  1 191 ? 12.653  53.147 106.911 1.00 76.57  ? 191  TYR A O   1 
ATOM   1526  C CB  . TYR A  1 191 ? 12.668  54.154 104.107 1.00 71.27  ? 191  TYR A CB  1 
ATOM   1527  C CG  . TYR A  1 191 ? 12.271  54.692 102.746 1.00 69.15  ? 191  TYR A CG  1 
ATOM   1528  C CD1 . TYR A  1 191 ? 11.249  54.093 102.009 1.00 68.24  ? 191  TYR A CD1 1 
ATOM   1529  C CD2 . TYR A  1 191 ? 12.900  55.813 102.205 1.00 68.30  ? 191  TYR A CD2 1 
ATOM   1530  C CE1 . TYR A  1 191 ? 10.877  54.583 100.765 1.00 66.49  ? 191  TYR A CE1 1 
ATOM   1531  C CE2 . TYR A  1 191 ? 12.533  56.310 100.964 1.00 66.55  ? 191  TYR A CE2 1 
ATOM   1532  C CZ  . TYR A  1 191 ? 11.519  55.691 100.250 1.00 65.64  ? 191  TYR A CZ  1 
ATOM   1533  O OH  . TYR A  1 191 ? 11.144  56.177 99.023  1.00 64.09  ? 191  TYR A OH  1 
ATOM   1534  N N   . GLN A  1 192 ? 12.629  55.353 107.378 1.00 78.62  ? 192  GLN A N   1 
ATOM   1535  C CA  . GLN A  1 192 ? 13.312  55.261 108.678 1.00 81.02  ? 192  GLN A CA  1 
ATOM   1536  C C   . GLN A  1 192 ? 14.757  54.768 108.634 1.00 79.81  ? 192  GLN A C   1 
ATOM   1537  O O   . GLN A  1 192 ? 15.663  55.489 109.056 1.00 80.79  ? 192  GLN A O   1 
ATOM   1538  C CB  . GLN A  1 192 ? 12.496  54.455 109.695 1.00 83.50  ? 192  GLN A CB  1 
ATOM   1539  C CG  . GLN A  1 192 ? 11.737  55.362 110.653 1.00 86.89  ? 192  GLN A CG  1 
ATOM   1540  C CD  . GLN A  1 192 ? 11.181  54.665 111.877 1.00 90.01  ? 192  GLN A CD  1 
ATOM   1541  O OE1 . GLN A  1 192 ? 10.351  55.234 112.581 1.00 92.89  ? 192  GLN A OE1 1 
ATOM   1542  N NE2 . GLN A  1 192 ? 11.638  53.446 112.149 1.00 89.70  ? 192  GLN A NE2 1 
ATOM   1543  N N   . ASN A  1 193 ? 14.969  53.549 108.148 1.00 77.94  ? 193  ASN A N   1 
ATOM   1544  C CA  . ASN A  1 193 ? 16.315  52.976 108.061 1.00 76.88  ? 193  ASN A CA  1 
ATOM   1545  C C   . ASN A  1 193 ? 17.250  53.946 107.328 1.00 75.37  ? 193  ASN A C   1 
ATOM   1546  O O   . ASN A  1 193 ? 16.964  54.333 106.195 1.00 73.19  ? 193  ASN A O   1 
ATOM   1547  C CB  . ASN A  1 193 ? 16.291  51.618 107.346 1.00 74.79  ? 193  ASN A CB  1 
ATOM   1548  C CG  . ASN A  1 193 ? 15.233  50.673 107.905 1.00 76.17  ? 193  ASN A CG  1 
ATOM   1549  O OD1 . ASN A  1 193 ? 14.196  51.112 108.395 1.00 77.96  ? 193  ASN A OD1 1 
ATOM   1550  N ND2 . ASN A  1 193 ? 15.488  49.372 107.824 1.00 75.55  ? 193  ASN A ND2 1 
ATOM   1551  N N   . PRO A  1 194 ? 18.352  54.365 107.983 1.00 76.75  ? 194  PRO A N   1 
ATOM   1552  C CA  . PRO A  1 194 ? 19.220  55.391 107.394 1.00 75.89  ? 194  PRO A CA  1 
ATOM   1553  C C   . PRO A  1 194 ? 19.978  54.888 106.166 1.00 72.90  ? 194  PRO A C   1 
ATOM   1554  O O   . PRO A  1 194 ? 20.051  55.590 105.157 1.00 71.23  ? 194  PRO A O   1 
ATOM   1555  C CB  . PRO A  1 194 ? 20.189  55.736 108.532 1.00 78.60  ? 194  PRO A CB  1 
ATOM   1556  C CG  . PRO A  1 194 ? 20.225  54.523 109.396 1.00 79.84  ? 194  PRO A CG  1 
ATOM   1557  C CD  . PRO A  1 194 ? 18.889  53.845 109.257 1.00 79.26  ? 194  PRO A CD  1 
ATOM   1558  N N   . THR A  1 195 ? 20.525  53.679 106.266 1.00 72.41  ? 195  THR A N   1 
ATOM   1559  C CA  . THR A  1 195 ? 21.229  53.036 105.167 1.00 69.88  ? 195  THR A CA  1 
ATOM   1560  C C   . THR A  1 195 ? 20.325  51.936 104.618 1.00 68.29  ? 195  THR A C   1 
ATOM   1561  O O   . THR A  1 195 ? 19.877  51.070 105.372 1.00 69.47  ? 195  THR A O   1 
ATOM   1562  C CB  . THR A  1 195 ? 22.560  52.424 105.647 1.00 70.74  ? 195  THR A CB  1 
ATOM   1563  O OG1 . THR A  1 195 ? 23.246  53.362 106.484 1.00 73.02  ? 195  THR A OG1 1 
ATOM   1564  C CG2 . THR A  1 195 ? 23.449  52.059 104.468 1.00 68.50  ? 195  THR A CG2 1 
ATOM   1565  N N   . THR A  1 196 ? 20.041  51.986 103.317 1.00 65.84  ? 196  THR A N   1 
ATOM   1566  C CA  . THR A  1 196 ? 19.111  51.040 102.695 1.00 64.46  ? 196  THR A CA  1 
ATOM   1567  C C   . THR A  1 196 ? 19.652  50.477 101.385 1.00 62.00  ? 196  THR A C   1 
ATOM   1568  O O   . THR A  1 196 ? 20.625  50.989 100.830 1.00 61.24  ? 196  THR A O   1 
ATOM   1569  C CB  . THR A  1 196 ? 17.732  51.683 102.442 1.00 64.38  ? 196  THR A CB  1 
ATOM   1570  O OG1 . THR A  1 196 ? 17.881  52.837 101.608 1.00 63.27  ? 196  THR A OG1 1 
ATOM   1571  C CG2 . THR A  1 196 ? 17.083  52.091 103.759 1.00 67.10  ? 196  THR A CG2 1 
ATOM   1572  N N   . TYR A  1 197 ? 19.014  49.412 100.904 1.00 61.03  ? 197  TYR A N   1 
ATOM   1573  C CA  . TYR A  1 197 ? 19.442  48.737 99.686  1.00 58.94  ? 197  TYR A CA  1 
ATOM   1574  C C   . TYR A  1 197 ? 18.286  47.999 99.016  1.00 58.02  ? 197  TYR A C   1 
ATOM   1575  O O   . TYR A  1 197 ? 17.234  47.790 99.621  1.00 59.13  ? 197  TYR A O   1 
ATOM   1576  C CB  . TYR A  1 197 ? 20.550  47.729 100.003 1.00 59.32  ? 197  TYR A CB  1 
ATOM   1577  C CG  . TYR A  1 197 ? 20.054  46.511 100.751 1.00 60.46  ? 197  TYR A CG  1 
ATOM   1578  C CD1 . TYR A  1 197 ? 20.011  46.497 102.142 1.00 62.77  ? 197  TYR A CD1 1 
ATOM   1579  C CD2 . TYR A  1 197 ? 19.618  45.376 100.067 1.00 59.46  ? 197  TYR A CD2 1 
ATOM   1580  C CE1 . TYR A  1 197 ? 19.551  45.389 102.834 1.00 64.04  ? 197  TYR A CE1 1 
ATOM   1581  C CE2 . TYR A  1 197 ? 19.158  44.263 100.748 1.00 60.73  ? 197  TYR A CE2 1 
ATOM   1582  C CZ  . TYR A  1 197 ? 19.127  44.274 102.134 1.00 63.01  ? 197  TYR A CZ  1 
ATOM   1583  O OH  . TYR A  1 197 ? 18.669  43.174 102.820 1.00 64.46  ? 197  TYR A OH  1 
ATOM   1584  N N   . ILE A  1 198 ? 18.505  47.611 97.760  1.00 56.19  ? 198  ILE A N   1 
ATOM   1585  C CA  . ILE A  1 198 ? 17.591  46.734 97.028  1.00 55.37  ? 198  ILE A CA  1 
ATOM   1586  C C   . ILE A  1 198 ? 18.417  45.714 96.254  1.00 54.31  ? 198  ILE A C   1 
ATOM   1587  O O   . ILE A  1 198 ? 19.155  46.081 95.338  1.00 53.07  ? 198  ILE A O   1 
ATOM   1588  C CB  . ILE A  1 198 ? 16.713  47.497 96.012  1.00 54.21  ? 198  ILE A CB  1 
ATOM   1589  C CG1 . ILE A  1 198 ? 16.204  48.818 96.597  1.00 55.16  ? 198  ILE A CG1 1 
ATOM   1590  C CG2 . ILE A  1 198 ? 15.552  46.618 95.562  1.00 54.07  ? 198  ILE A CG2 1 
ATOM   1591  C CD1 . ILE A  1 198 ? 15.438  49.665 95.606  1.00 54.19  ? 198  ILE A CD1 1 
ATOM   1592  N N   . SER A  1 199 ? 18.291  44.441 96.617  1.00 55.01  ? 199  SER A N   1 
ATOM   1593  C CA  . SER A  1 199 ? 18.989  43.374 95.907  1.00 54.27  ? 199  SER A CA  1 
ATOM   1594  C C   . SER A  1 199 ? 18.011  42.593 95.039  1.00 53.60  ? 199  SER A C   1 
ATOM   1595  O O   . SER A  1 199 ? 16.992  42.104 95.527  1.00 54.59  ? 199  SER A O   1 
ATOM   1596  C CB  . SER A  1 199 ? 19.703  42.441 96.887  1.00 55.72  ? 199  SER A CB  1 
ATOM   1597  O OG  . SER A  1 199 ? 18.820  41.977 97.886  1.00 57.29  ? 199  SER A OG  1 
ATOM   1598  N N   . VAL A  1 200 ? 18.331  42.496 93.749  1.00 52.15  ? 200  VAL A N   1 
ATOM   1599  C CA  . VAL A  1 200 ? 17.508  41.777 92.778  1.00 51.57  ? 200  VAL A CA  1 
ATOM   1600  C C   . VAL A  1 200 ? 18.338  40.668 92.143  1.00 51.31  ? 200  VAL A C   1 
ATOM   1601  O O   . VAL A  1 200 ? 19.445  40.910 91.659  1.00 50.65  ? 200  VAL A O   1 
ATOM   1602  C CB  . VAL A  1 200 ? 16.989  42.708 91.664  1.00 50.25  ? 200  VAL A CB  1 
ATOM   1603  C CG1 . VAL A  1 200 ? 15.873  42.028 90.881  1.00 50.16  ? 200  VAL A CG1 1 
ATOM   1604  C CG2 . VAL A  1 200 ? 16.500  44.027 92.246  1.00 50.49  ? 200  VAL A CG2 1 
ATOM   1605  N N   . GLY A  1 201 ? 17.796  39.454 92.144  1.00 52.05  ? 201  GLY A N   1 
ATOM   1606  C CA  . GLY A  1 201 ? 18.500  38.296 91.605  1.00 52.13  ? 201  GLY A CA  1 
ATOM   1607  C C   . GLY A  1 201 ? 17.631  37.485 90.668  1.00 52.07  ? 201  GLY A C   1 
ATOM   1608  O O   . GLY A  1 201 ? 16.418  37.398 90.852  1.00 52.65  ? 201  GLY A O   1 
ATOM   1609  N N   . THR A  1 202 ? 18.259  36.922 89.640  1.00 51.58  ? 202  THR A N   1 
ATOM   1610  C CA  . THR A  1 202 ? 17.638  35.921 88.768  1.00 51.88  ? 202  THR A CA  1 
ATOM   1611  C C   . THR A  1 202 ? 18.711  34.870 88.505  1.00 52.45  ? 202  THR A C   1 
ATOM   1612  O O   . THR A  1 202 ? 19.689  34.790 89.252  1.00 52.95  ? 202  THR A O   1 
ATOM   1613  C CB  . THR A  1 202 ? 17.130  36.527 87.435  1.00 50.68  ? 202  THR A CB  1 
ATOM   1614  O OG1 . THR A  1 202 ? 18.240  36.907 86.609  1.00 49.68  ? 202  THR A OG1 1 
ATOM   1615  C CG2 . THR A  1 202 ? 16.235  37.736 87.689  1.00 50.13  ? 202  THR A CG2 1 
ATOM   1616  N N   . SER A  1 203 ? 18.539  34.058 87.466  1.00 52.62  ? 203  SER A N   1 
ATOM   1617  C CA  . SER A  1 203 ? 19.601  33.145 87.058  1.00 53.19  ? 203  SER A CA  1 
ATOM   1618  C C   . SER A  1 203 ? 20.804  33.935 86.550  1.00 52.15  ? 203  SER A C   1 
ATOM   1619  O O   . SER A  1 203 ? 21.945  33.530 86.755  1.00 52.79  ? 203  SER A O   1 
ATOM   1620  C CB  . SER A  1 203 ? 19.110  32.178 85.984  1.00 53.77  ? 203  SER A CB  1 
ATOM   1621  O OG  . SER A  1 203 ? 18.652  32.882 84.848  1.00 52.66  ? 203  SER A OG  1 
ATOM   1622  N N   . THR A  1 204 ? 20.544  35.069 85.905  1.00 50.77  ? 204  THR A N   1 
ATOM   1623  C CA  . THR A  1 204 ? 21.606  35.898 85.347  1.00 49.92  ? 204  THR A CA  1 
ATOM   1624  C C   . THR A  1 204 ? 21.834  37.164 86.170  1.00 49.31  ? 204  THR A C   1 
ATOM   1625  O O   . THR A  1 204 ? 22.978  37.529 86.438  1.00 49.42  ? 204  THR A O   1 
ATOM   1626  C CB  . THR A  1 204 ? 21.305  36.291 83.887  1.00 49.06  ? 204  THR A CB  1 
ATOM   1627  O OG1 . THR A  1 204 ? 20.126  37.104 83.832  1.00 48.25  ? 204  THR A OG1 1 
ATOM   1628  C CG2 . THR A  1 204 ? 21.108  35.052 83.026  1.00 49.91  ? 204  THR A CG2 1 
ATOM   1629  N N   . LEU A  1 205 ? 20.752  37.826 86.572  1.00 48.83  ? 205  LEU A N   1 
ATOM   1630  C CA  . LEU A  1 205 ? 20.856  39.119 87.245  1.00 48.32  ? 205  LEU A CA  1 
ATOM   1631  C C   . LEU A  1 205 ? 21.426  39.000 88.666  1.00 49.33  ? 205  LEU A C   1 
ATOM   1632  O O   . LEU A  1 205 ? 20.969  38.175 89.458  1.00 50.35  ? 205  LEU A O   1 
ATOM   1633  C CB  . LEU A  1 205 ? 19.486  39.809 87.285  1.00 47.86  ? 205  LEU A CB  1 
ATOM   1634  C CG  . LEU A  1 205 ? 19.444  41.272 87.750  1.00 47.34  ? 205  LEU A CG  1 
ATOM   1635  C CD1 . LEU A  1 205 ? 20.355  42.151 86.901  1.00 46.48  ? 205  LEU A CD1 1 
ATOM   1636  C CD2 . LEU A  1 205 ? 18.017  41.801 87.723  1.00 47.17  ? 205  LEU A CD2 1 
ATOM   1637  N N   . ASN A  1 206 ? 22.434  39.820 88.965  1.00 49.20  ? 206  ASN A N   1 
ATOM   1638  C CA  . ASN A  1 206 ? 22.996  39.929 90.314  1.00 50.22  ? 206  ASN A CA  1 
ATOM   1639  C C   . ASN A  1 206 ? 23.210  41.398 90.673  1.00 49.85  ? 206  ASN A C   1 
ATOM   1640  O O   . ASN A  1 206 ? 24.320  41.923 90.585  1.00 49.93  ? 206  ASN A O   1 
ATOM   1641  C CB  . ASN A  1 206 ? 24.313  39.156 90.426  1.00 51.16  ? 206  ASN A CB  1 
ATOM   1642  C CG  . ASN A  1 206 ? 24.911  39.215 91.827  1.00 52.48  ? 206  ASN A CG  1 
ATOM   1643  O OD1 . ASN A  1 206 ? 24.189  39.313 92.821  1.00 53.02  ? 206  ASN A OD1 1 
ATOM   1644  N ND2 . ASN A  1 206 ? 26.234  39.149 91.910  1.00 53.22  ? 206  ASN A ND2 1 
ATOM   1645  N N   . GLN A  1 207 ? 22.131  42.043 91.096  1.00 49.67  ? 207  GLN A N   1 
ATOM   1646  C CA  . GLN A  1 207 ? 22.111  43.485 91.293  1.00 49.36  ? 207  GLN A CA  1 
ATOM   1647  C C   . GLN A  1 207 ? 21.916  43.844 92.766  1.00 50.58  ? 207  GLN A C   1 
ATOM   1648  O O   . GLN A  1 207 ? 21.256  43.120 93.509  1.00 51.44  ? 207  GLN A O   1 
ATOM   1649  C CB  . GLN A  1 207 ? 20.999  44.086 90.423  1.00 48.28  ? 207  GLN A CB  1 
ATOM   1650  C CG  . GLN A  1 207 ? 20.506  45.469 90.824  1.00 48.27  ? 207  GLN A CG  1 
ATOM   1651  C CD  . GLN A  1 207 ? 19.359  45.948 89.952  1.00 47.43  ? 207  GLN A CD  1 
ATOM   1652  O OE1 . GLN A  1 207 ? 18.276  46.257 90.450  1.00 47.87  ? 207  GLN A OE1 1 
ATOM   1653  N NE2 . GLN A  1 207 ? 19.587  45.999 88.640  1.00 46.43  ? 207  GLN A NE2 1 
ATOM   1654  N N   . ARG A  1 208 ? 22.512  44.962 93.174  1.00 50.86  ? 208  ARG A N   1 
ATOM   1655  C CA  . ARG A  1 208 ? 22.269  45.547 94.488  1.00 52.12  ? 208  ARG A CA  1 
ATOM   1656  C C   . ARG A  1 208 ? 22.335  47.071 94.389  1.00 51.90  ? 208  ARG A C   1 
ATOM   1657  O O   . ARG A  1 208 ? 23.412  47.642 94.217  1.00 52.00  ? 208  ARG A O   1 
ATOM   1658  C CB  . ARG A  1 208 ? 23.282  45.041 95.516  1.00 53.63  ? 208  ARG A CB  1 
ATOM   1659  C CG  . ARG A  1 208 ? 22.890  45.354 96.952  1.00 55.27  ? 208  ARG A CG  1 
ATOM   1660  C CD  . ARG A  1 208 ? 24.062  45.203 97.908  1.00 56.90  ? 208  ARG A CD  1 
ATOM   1661  N NE  . ARG A  1 208 ? 23.624  45.133 99.302  1.00 58.72  ? 208  ARG A NE  1 
ATOM   1662  C CZ  . ARG A  1 208 ? 23.081  44.060 99.878  1.00 59.59  ? 208  ARG A CZ  1 
ATOM   1663  N NH1 . ARG A  1 208 ? 22.885  42.940 99.187  1.00 58.77  ? 208  ARG A NH1 1 
ATOM   1664  N NH2 . ARG A  1 208 ? 22.722  44.107 101.159 1.00 61.49  ? 208  ARG A NH2 1 
ATOM   1665  N N   . LEU A  1 209 ? 21.179  47.720 94.497  1.00 51.82  ? 209  LEU A N   1 
ATOM   1666  C CA  . LEU A  1 209 ? 21.086  49.173 94.376  1.00 51.76  ? 209  LEU A CA  1 
ATOM   1667  C C   . LEU A  1 209 ? 21.111  49.828 95.749  1.00 53.51  ? 209  LEU A C   1 
ATOM   1668  O O   . LEU A  1 209 ? 20.582  49.278 96.711  1.00 54.61  ? 209  LEU A O   1 
ATOM   1669  C CB  . LEU A  1 209 ? 19.794  49.563 93.656  1.00 50.88  ? 209  LEU A CB  1 
ATOM   1670  C CG  . LEU A  1 209 ? 19.571  48.951 92.270  1.00 49.36  ? 209  LEU A CG  1 
ATOM   1671  C CD1 . LEU A  1 209 ? 18.163  49.252 91.776  1.00 48.95  ? 209  LEU A CD1 1 
ATOM   1672  C CD2 . LEU A  1 209 ? 20.614  49.449 91.278  1.00 48.51  ? 209  LEU A CD2 1 
ATOM   1673  N N   . VAL A  1 210 ? 21.733  51.002 95.825  1.00 53.97  ? 210  VAL A N   1 
ATOM   1674  C CA  . VAL A  1 210 ? 21.722  51.828 97.034  1.00 55.82  ? 210  VAL A CA  1 
ATOM   1675  C C   . VAL A  1 210 ? 21.288  53.253 96.660  1.00 55.76  ? 210  VAL A C   1 
ATOM   1676  O O   . VAL A  1 210 ? 21.665  53.753 95.595  1.00 54.62  ? 210  VAL A O   1 
ATOM   1677  C CB  . VAL A  1 210 ? 23.098  51.846 97.754  1.00 57.15  ? 210  VAL A CB  1 
ATOM   1678  C CG1 . VAL A  1 210 ? 23.502  50.436 98.159  1.00 57.46  ? 210  VAL A CG1 1 
ATOM   1679  C CG2 . VAL A  1 210 ? 24.184  52.486 96.894  1.00 56.57  ? 210  VAL A CG2 1 
ATOM   1680  N N   . PRO A  1 211 ? 20.483  53.907 97.519  1.00 57.16  ? 211  PRO A N   1 
ATOM   1681  C CA  . PRO A  1 211 ? 20.068  55.275 97.188  1.00 57.33  ? 211  PRO A CA  1 
ATOM   1682  C C   . PRO A  1 211 ? 21.199  56.294 97.331  1.00 58.26  ? 211  PRO A C   1 
ATOM   1683  O O   . PRO A  1 211 ? 21.923  56.290 98.328  1.00 59.87  ? 211  PRO A O   1 
ATOM   1684  C CB  . PRO A  1 211 ? 18.952  55.572 98.201  1.00 58.95  ? 211  PRO A CB  1 
ATOM   1685  C CG  . PRO A  1 211 ? 18.563  54.253 98.771  1.00 59.19  ? 211  PRO A CG  1 
ATOM   1686  C CD  . PRO A  1 211 ? 19.795  53.405 98.720  1.00 58.69  ? 211  PRO A CD  1 
ATOM   1687  N N   . ARG A  1 212 ? 21.334  57.150 96.323  1.00 57.41  ? 212  ARG A N   1 
ATOM   1688  C CA  . ARG A  1 212 ? 22.321  58.225 96.315  1.00 58.40  ? 212  ARG A CA  1 
ATOM   1689  C C   . ARG A  1 212 ? 21.638  59.550 96.652  1.00 59.70  ? 212  ARG A C   1 
ATOM   1690  O O   . ARG A  1 212 ? 20.725  59.983 95.947  1.00 58.88  ? 212  ARG A O   1 
ATOM   1691  C CB  . ARG A  1 212 ? 22.997  58.319 94.943  1.00 56.88  ? 212  ARG A CB  1 
ATOM   1692  C CG  . ARG A  1 212 ? 23.590  57.004 94.447  1.00 55.63  ? 212  ARG A CG  1 
ATOM   1693  C CD  . ARG A  1 212 ? 24.401  57.185 93.169  1.00 54.63  ? 212  ARG A CD  1 
ATOM   1694  N NE  . ARG A  1 212 ? 23.686  57.956 92.149  1.00 53.70  ? 212  ARG A NE  1 
ATOM   1695  C CZ  . ARG A  1 212 ? 22.808  57.460 91.275  1.00 52.14  ? 212  ARG A CZ  1 
ATOM   1696  N NH1 . ARG A  1 212 ? 22.498  56.165 91.261  1.00 51.28  ? 212  ARG A NH1 1 
ATOM   1697  N NH2 . ARG A  1 212 ? 22.226  58.272 90.398  1.00 51.61  ? 212  ARG A NH2 1 
ATOM   1698  N N   . ILE A  1 213 ? 22.083  60.188 97.732  1.00 61.91  ? 213  ILE A N   1 
ATOM   1699  C CA  . ILE A  1 213 ? 21.500  61.452 98.183  1.00 63.58  ? 213  ILE A CA  1 
ATOM   1700  C C   . ILE A  1 213 ? 22.270  62.631 97.589  1.00 64.05  ? 213  ILE A C   1 
ATOM   1701  O O   . ILE A  1 213 ? 23.502  62.619 97.544  1.00 64.42  ? 213  ILE A O   1 
ATOM   1702  C CB  . ILE A  1 213 ? 21.480  61.545 99.724  1.00 66.12  ? 213  ILE A CB  1 
ATOM   1703  C CG1 . ILE A  1 213 ? 20.563  60.461 100.295 1.00 65.92  ? 213  ILE A CG1 1 
ATOM   1704  C CG2 . ILE A  1 213 ? 20.959  62.891 100.202 1.00 68.15  ? 213  ILE A CG2 1 
ATOM   1705  C CD1 . ILE A  1 213 ? 20.916  60.063 101.707 1.00 68.09  ? 213  ILE A CD1 1 
ATOM   1706  N N   . ALA A  1 214 ? 21.531  63.637 97.130  1.00 64.20  ? 214  ALA A N   1 
ATOM   1707  C CA  . ALA A  1 214 ? 22.123  64.859 96.592  1.00 64.95  ? 214  ALA A CA  1 
ATOM   1708  C C   . ALA A  1 214 ? 21.092  65.981 96.533  1.00 65.89  ? 214  ALA A C   1 
ATOM   1709  O O   . ALA A  1 214 ? 19.889  65.731 96.415  1.00 65.17  ? 214  ALA A O   1 
ATOM   1710  C CB  . ALA A  1 214 ? 22.699  64.603 95.205  1.00 62.95  ? 214  ALA A CB  1 
ATOM   1711  N N   . THR A  1 215 ? 21.575  67.217 96.620  1.00 67.70  ? 215  THR A N   1 
ATOM   1712  C CA  . THR A  1 215 ? 20.726  68.390 96.452  1.00 68.79  ? 215  THR A CA  1 
ATOM   1713  C C   . THR A  1 215 ? 20.538  68.611 94.958  1.00 66.92  ? 215  THR A C   1 
ATOM   1714  O O   . THR A  1 215 ? 21.502  68.867 94.240  1.00 66.56  ? 215  THR A O   1 
ATOM   1715  C CB  . THR A  1 215 ? 21.354  69.645 97.090  1.00 71.69  ? 215  THR A CB  1 
ATOM   1716  O OG1 . THR A  1 215 ? 21.722  69.365 98.446  1.00 73.53  ? 215  THR A OG1 1 
ATOM   1717  C CG2 . THR A  1 215 ? 20.375  70.822 97.061  1.00 73.15  ? 215  THR A CG2 1 
ATOM   1718  N N   . ARG A  1 216 ? 19.298  68.501 94.493  1.00 65.94  ? 216  ARG A N   1 
ATOM   1719  C CA  . ARG A  1 216 ? 19.006  68.560 93.064  1.00 64.16  ? 216  ARG A CA  1 
ATOM   1720  C C   . ARG A  1 216 ? 18.004  69.664 92.761  1.00 65.26  ? 216  ARG A C   1 
ATOM   1721  O O   . ARG A  1 216 ? 17.246  70.087 93.637  1.00 66.96  ? 216  ARG A O   1 
ATOM   1722  C CB  . ARG A  1 216 ? 18.460  67.214 92.587  1.00 61.78  ? 216  ARG A CB  1 
ATOM   1723  C CG  . ARG A  1 216 ? 19.405  66.045 92.823  1.00 60.73  ? 216  ARG A CG  1 
ATOM   1724  C CD  . ARG A  1 216 ? 18.717  64.714 92.574  1.00 58.86  ? 216  ARG A CD  1 
ATOM   1725  N NE  . ARG A  1 216 ? 17.912  64.276 93.718  1.00 59.79  ? 216  ARG A NE  1 
ATOM   1726  C CZ  . ARG A  1 216 ? 18.311  63.430 94.673  1.00 60.16  ? 216  ARG A CZ  1 
ATOM   1727  N NH1 . ARG A  1 216 ? 19.526  62.885 94.665  1.00 59.67  ? 216  ARG A NH1 1 
ATOM   1728  N NH2 . ARG A  1 216 ? 17.479  63.117 95.658  1.00 61.23  ? 216  ARG A NH2 1 
ATOM   1729  N N   . SER A  1 217 ? 18.013  70.129 91.514  1.00 64.48  ? 217  SER A N   1 
ATOM   1730  C CA  . SER A  1 217 ? 17.070  71.144 91.059  1.00 65.45  ? 217  SER A CA  1 
ATOM   1731  C C   . SER A  1 217 ? 15.674  70.541 90.954  1.00 64.66  ? 217  SER A C   1 
ATOM   1732  O O   . SER A  1 217 ? 15.524  69.342 90.716  1.00 62.76  ? 217  SER A O   1 
ATOM   1733  C CB  . SER A  1 217 ? 17.501  71.704 89.703  1.00 64.79  ? 217  SER A CB  1 
ATOM   1734  O OG  . SER A  1 217 ? 18.870  72.069 89.718  1.00 65.48  ? 217  SER A OG  1 
ATOM   1735  N N   . LYS A  1 218 ? 14.657  71.373 91.146  1.00 66.38  ? 218  LYS A N   1 
ATOM   1736  C CA  . LYS A  1 218 ? 13.278  70.917 91.034  1.00 66.10  ? 218  LYS A CA  1 
ATOM   1737  C C   . LYS A  1 218 ? 12.929  70.672 89.576  1.00 64.23  ? 218  LYS A C   1 
ATOM   1738  O O   . LYS A  1 218 ? 13.040  71.568 88.742  1.00 64.62  ? 218  LYS A O   1 
ATOM   1739  C CB  . LYS A  1 218 ? 12.298  71.926 91.637  1.00 68.82  ? 218  LYS A CB  1 
ATOM   1740  C CG  . LYS A  1 218 ? 12.073  71.755 93.130  1.00 70.73  ? 218  LYS A CG  1 
ATOM   1741  C CD  . LYS A  1 218 ? 10.973  72.684 93.618  1.00 73.55  ? 218  LYS A CD  1 
ATOM   1742  C CE  . LYS A  1 218 ? 10.802  72.624 95.128  1.00 75.91  ? 218  LYS A CE  1 
ATOM   1743  N NZ  . LYS A  1 218 ? 11.877  73.356 95.853  1.00 77.64  ? 218  LYS A NZ  1 
ATOM   1744  N N   . VAL A  1 219 ? 12.536  69.440 89.278  1.00 62.36  ? 219  VAL A N   1 
ATOM   1745  C CA  . VAL A  1 219 ? 11.988  69.084 87.984  1.00 60.82  ? 219  VAL A CA  1 
ATOM   1746  C C   . VAL A  1 219 ? 10.566  68.597 88.248  1.00 61.21  ? 219  VAL A C   1 
ATOM   1747  O O   . VAL A  1 219 ? 10.350  67.759 89.120  1.00 61.17  ? 219  VAL A O   1 
ATOM   1748  C CB  . VAL A  1 219 ? 12.840  67.989 87.318  1.00 58.52  ? 219  VAL A CB  1 
ATOM   1749  C CG1 . VAL A  1 219 ? 12.190  67.495 86.032  1.00 57.14  ? 219  VAL A CG1 1 
ATOM   1750  C CG2 . VAL A  1 219 ? 14.245  68.514 87.046  1.00 58.46  ? 219  VAL A CG2 1 
ATOM   1751  N N   . ASN A  1 220 ? 9.595   69.148 87.521  1.00 61.81  ? 220  ASN A N   1 
ATOM   1752  C CA  . ASN A  1 220 ? 8.173   68.890 87.794  1.00 62.79  ? 220  ASN A CA  1 
ATOM   1753  C C   . ASN A  1 220 ? 7.792   69.133 89.263  1.00 64.85  ? 220  ASN A C   1 
ATOM   1754  O O   . ASN A  1 220 ? 6.978   68.403 89.836  1.00 65.29  ? 220  ASN A O   1 
ATOM   1755  C CB  . ASN A  1 220 ? 7.785   67.466 87.361  1.00 61.07  ? 220  ASN A CB  1 
ATOM   1756  C CG  . ASN A  1 220 ? 7.457   67.370 85.882  1.00 60.01  ? 220  ASN A CG  1 
ATOM   1757  O OD1 . ASN A  1 220 ? 7.912   68.182 85.071  1.00 59.94  ? 220  ASN A OD1 1 
ATOM   1758  N ND2 . ASN A  1 220 ? 6.662   66.368 85.521  1.00 59.39  ? 220  ASN A ND2 1 
ATOM   1759  N N   . GLY A  1 221 ? 8.389   70.164 89.860  1.00 66.30  ? 221  GLY A N   1 
ATOM   1760  C CA  . GLY A  1 221 ? 8.096   70.548 91.240  1.00 68.65  ? 221  GLY A CA  1 
ATOM   1761  C C   . GLY A  1 221 ? 8.692   69.654 92.314  1.00 68.31  ? 221  GLY A C   1 
ATOM   1762  O O   . GLY A  1 221 ? 8.323   69.767 93.482  1.00 70.29  ? 221  GLY A O   1 
ATOM   1763  N N   . GLN A  1 222 ? 9.612   68.769 91.932  1.00 66.03  ? 222  GLN A N   1 
ATOM   1764  C CA  . GLN A  1 222 ? 10.240  67.843 92.876  1.00 65.66  ? 222  GLN A CA  1 
ATOM   1765  C C   . GLN A  1 222 ? 11.737  67.725 92.617  1.00 64.19  ? 222  GLN A C   1 
ATOM   1766  O O   . GLN A  1 222 ? 12.174  67.675 91.468  1.00 62.47  ? 222  GLN A O   1 
ATOM   1767  C CB  . GLN A  1 222 ? 9.591   66.456 92.786  1.00 64.47  ? 222  GLN A CB  1 
ATOM   1768  C CG  . GLN A  1 222 ? 8.108   66.421 93.146  1.00 66.18  ? 222  GLN A CG  1 
ATOM   1769  C CD  . GLN A  1 222 ? 7.821   66.909 94.560  1.00 69.06  ? 222  GLN A CD  1 
ATOM   1770  O OE1 . GLN A  1 222 ? 8.626   66.722 95.470  1.00 69.54  ? 222  GLN A OE1 1 
ATOM   1771  N NE2 . GLN A  1 222 ? 6.664   67.533 94.747  1.00 71.22  ? 222  GLN A NE2 1 
ATOM   1772  N N   . SER A  1 223 ? 12.512  67.681 93.699  1.00 65.07  ? 223  SER A N   1 
ATOM   1773  C CA  . SER A  1 223 ? 13.966  67.528 93.621  1.00 64.10  ? 223  SER A CA  1 
ATOM   1774  C C   . SER A  1 223 ? 14.418  66.093 93.932  1.00 62.59  ? 223  SER A C   1 
ATOM   1775  O O   . SER A  1 223 ? 15.608  65.788 93.866  1.00 61.81  ? 223  SER A O   1 
ATOM   1776  C CB  . SER A  1 223 ? 14.646  68.531 94.557  1.00 66.43  ? 223  SER A CB  1 
ATOM   1777  O OG  . SER A  1 223 ? 14.585  69.839 94.018  1.00 67.47  ? 223  SER A OG  1 
ATOM   1778  N N   . GLY A  1 224 ? 13.467  65.221 94.266  1.00 62.36  ? 224  GLY A N   1 
ATOM   1779  C CA  . GLY A  1 224 ? 13.732  63.790 94.412  1.00 60.92  ? 224  GLY A CA  1 
ATOM   1780  C C   . GLY A  1 224 ? 13.802  63.110 93.056  1.00 58.45  ? 224  GLY A C   1 
ATOM   1781  O O   . GLY A  1 224 ? 13.287  63.637 92.062  1.00 57.95  ? 224  GLY A O   1 
ATOM   1782  N N   . ARG A  1 225 ? 14.433  61.936 93.012  1.00 57.06  ? 225  ARG A N   1 
ATOM   1783  C CA  . ARG A  1 225 ? 14.616  61.198 91.757  1.00 54.89  ? 225  ARG A CA  1 
ATOM   1784  C C   . ARG A  1 225 ? 14.201  59.731 91.869  1.00 54.01  ? 225  ARG A C   1 
ATOM   1785  O O   . ARG A  1 225 ? 14.287  59.127 92.937  1.00 54.80  ? 225  ARG A O   1 
ATOM   1786  C CB  . ARG A  1 225 ? 16.076  61.272 91.299  1.00 54.07  ? 225  ARG A CB  1 
ATOM   1787  C CG  . ARG A  1 225 ? 16.574  62.675 90.988  1.00 54.88  ? 225  ARG A CG  1 
ATOM   1788  C CD  . ARG A  1 225 ? 15.992  63.215 89.692  1.00 54.14  ? 225  ARG A CD  1 
ATOM   1789  N NE  . ARG A  1 225 ? 16.537  64.535 89.360  1.00 55.04  ? 225  ARG A NE  1 
ATOM   1790  C CZ  . ARG A  1 225 ? 16.001  65.708 89.710  1.00 56.69  ? 225  ARG A CZ  1 
ATOM   1791  N NH1 . ARG A  1 225 ? 14.873  65.775 90.418  1.00 57.73  ? 225  ARG A NH1 1 
ATOM   1792  N NH2 . ARG A  1 225 ? 16.603  66.835 89.344  1.00 57.52  ? 225  ARG A NH2 1 
ATOM   1793  N N   . MET A  1 226 ? 13.751  59.174 90.747  1.00 52.55  ? 226  MET A N   1 
ATOM   1794  C CA  . MET A  1 226 ? 13.417  57.759 90.643  1.00 51.68  ? 226  MET A CA  1 
ATOM   1795  C C   . MET A  1 226 ? 14.244  57.149 89.524  1.00 49.84  ? 226  MET A C   1 
ATOM   1796  O O   . MET A  1 226 ? 14.263  57.675 88.416  1.00 49.15  ? 226  MET A O   1 
ATOM   1797  C CB  . MET A  1 226 ? 11.933  57.584 90.325  1.00 52.06  ? 226  MET A CB  1 
ATOM   1798  C CG  . MET A  1 226 ? 11.006  57.934 91.476  1.00 54.07  ? 226  MET A CG  1 
ATOM   1799  S SD  . MET A  1 226 ? 10.852  56.615 92.697  1.00 54.92  ? 226  MET A SD  1 
ATOM   1800  C CE  . MET A  1 226 ? 9.628   57.331 93.787  1.00 57.53  ? 226  MET A CE  1 
ATOM   1801  N N   . GLU A  1 227 ? 14.925  56.046 89.811  1.00 49.23  ? 227  GLU A N   1 
ATOM   1802  C CA  . GLU A  1 227 ? 15.758  55.382 88.812  1.00 47.74  ? 227  GLU A CA  1 
ATOM   1803  C C   . GLU A  1 227 ? 15.180  54.007 88.511  1.00 47.06  ? 227  GLU A C   1 
ATOM   1804  O O   . GLU A  1 227 ? 15.154  53.134 89.378  1.00 47.53  ? 227  GLU A O   1 
ATOM   1805  C CB  . GLU A  1 227 ? 17.200  55.278 89.308  1.00 47.86  ? 227  GLU A CB  1 
ATOM   1806  C CG  . GLU A  1 227 ? 18.219  55.086 88.200  1.00 46.79  ? 227  GLU A CG  1 
ATOM   1807  C CD  . GLU A  1 227 ? 19.650  55.214 88.685  1.00 47.29  ? 227  GLU A CD  1 
ATOM   1808  O OE1 . GLU A  1 227 ? 19.865  55.582 89.861  1.00 48.47  ? 227  GLU A OE1 1 
ATOM   1809  O OE2 . GLU A  1 227 ? 20.567  54.948 87.881  1.00 46.70  ? 227  GLU A OE2 1 
ATOM   1810  N N   . PHE A  1 228 ? 14.706  53.825 87.282  1.00 46.12  ? 228  PHE A N   1 
ATOM   1811  C CA  . PHE A  1 228 ? 13.975  52.616 86.917  1.00 45.77  ? 228  PHE A CA  1 
ATOM   1812  C C   . PHE A  1 228 ? 14.855  51.621 86.174  1.00 44.73  ? 228  PHE A C   1 
ATOM   1813  O O   . PHE A  1 228 ? 15.626  51.993 85.290  1.00 44.03  ? 228  PHE A O   1 
ATOM   1814  C CB  . PHE A  1 228 ? 12.736  52.975 86.099  1.00 45.84  ? 228  PHE A CB  1 
ATOM   1815  C CG  . PHE A  1 228 ? 11.712  53.744 86.882  1.00 47.11  ? 228  PHE A CG  1 
ATOM   1816  C CD1 . PHE A  1 228 ? 10.799  53.081 87.689  1.00 48.14  ? 228  PHE A CD1 1 
ATOM   1817  C CD2 . PHE A  1 228 ? 11.683  55.131 86.841  1.00 47.51  ? 228  PHE A CD2 1 
ATOM   1818  C CE1 . PHE A  1 228 ? 9.861   53.785 88.426  1.00 49.59  ? 228  PHE A CE1 1 
ATOM   1819  C CE2 . PHE A  1 228 ? 10.748  55.843 87.575  1.00 48.92  ? 228  PHE A CE2 1 
ATOM   1820  C CZ  . PHE A  1 228 ? 9.836   55.168 88.369  1.00 49.98  ? 228  PHE A CZ  1 
ATOM   1821  N N   . PHE A  1 229 ? 14.730  50.356 86.563  1.00 44.85  ? 229  PHE A N   1 
ATOM   1822  C CA  . PHE A  1 229 ? 15.516  49.268 86.001  1.00 44.19  ? 229  PHE A CA  1 
ATOM   1823  C C   . PHE A  1 229 ? 14.587  48.187 85.463  1.00 44.22  ? 229  PHE A C   1 
ATOM   1824  O O   . PHE A  1 229 ? 13.410  48.124 85.827  1.00 44.88  ? 229  PHE A O   1 
ATOM   1825  C CB  . PHE A  1 229 ? 16.439  48.680 87.067  1.00 44.62  ? 229  PHE A CB  1 
ATOM   1826  C CG  . PHE A  1 229 ? 17.508  49.628 87.528  1.00 44.76  ? 229  PHE A CG  1 
ATOM   1827  C CD1 . PHE A  1 229 ? 17.215  50.637 88.437  1.00 45.53  ? 229  PHE A CD1 1 
ATOM   1828  C CD2 . PHE A  1 229 ? 18.810  49.514 87.054  1.00 44.37  ? 229  PHE A CD2 1 
ATOM   1829  C CE1 . PHE A  1 229 ? 18.198  51.517 88.863  1.00 45.89  ? 229  PHE A CE1 1 
ATOM   1830  C CE2 . PHE A  1 229 ? 19.800  50.387 87.478  1.00 44.75  ? 229  PHE A CE2 1 
ATOM   1831  C CZ  . PHE A  1 229 ? 19.493  51.390 88.385  1.00 45.51  ? 229  PHE A CZ  1 
ATOM   1832  N N   . TRP A  1 230 ? 15.128  47.339 84.595  1.00 43.69  ? 230  TRP A N   1 
ATOM   1833  C CA  . TRP A  1 230 ? 14.339  46.298 83.958  1.00 43.87  ? 230  TRP A CA  1 
ATOM   1834  C C   . TRP A  1 230 ? 15.155  45.051 83.672  1.00 43.78  ? 230  TRP A C   1 
ATOM   1835  O O   . TRP A  1 230 ? 16.384  45.086 83.654  1.00 43.41  ? 230  TRP A O   1 
ATOM   1836  C CB  . TRP A  1 230 ? 13.735  46.827 82.659  1.00 43.52  ? 230  TRP A CB  1 
ATOM   1837  C CG  . TRP A  1 230 ? 14.743  47.233 81.620  1.00 42.76  ? 230  TRP A CG  1 
ATOM   1838  C CD1 . TRP A  1 230 ? 15.296  48.471 81.453  1.00 42.36  ? 230  TRP A CD1 1 
ATOM   1839  C CD2 . TRP A  1 230 ? 15.303  46.403 80.595  1.00 42.55  ? 230  TRP A CD2 1 
ATOM   1840  N NE1 . TRP A  1 230 ? 16.169  48.463 80.394  1.00 41.93  ? 230  TRP A NE1 1 
ATOM   1841  C CE2 . TRP A  1 230 ? 16.195  47.206 79.850  1.00 42.07  ? 230  TRP A CE2 1 
ATOM   1842  C CE3 . TRP A  1 230 ? 15.144  45.057 80.237  1.00 42.95  ? 230  TRP A CE3 1 
ATOM   1843  C CZ2 . TRP A  1 230 ? 16.922  46.708 78.762  1.00 42.00  ? 230  TRP A CZ2 1 
ATOM   1844  C CZ3 . TRP A  1 230 ? 15.868  44.563 79.156  1.00 42.85  ? 230  TRP A CZ3 1 
ATOM   1845  C CH2 . TRP A  1 230 ? 16.744  45.387 78.432  1.00 42.39  ? 230  TRP A CH2 1 
ATOM   1846  N N   . THR A  1 231 ? 14.450  43.949 83.453  1.00 44.36  ? 231  THR A N   1 
ATOM   1847  C CA  . THR A  1 231 ? 15.065  42.709 83.007  1.00 44.53  ? 231  THR A CA  1 
ATOM   1848  C C   . THR A  1 231 ? 14.054  41.883 82.219  1.00 45.18  ? 231  THR A C   1 
ATOM   1849  O O   . THR A  1 231 ? 12.849  42.132 82.290  1.00 45.65  ? 231  THR A O   1 
ATOM   1850  C CB  . THR A  1 231 ? 15.589  41.882 84.197  1.00 45.15  ? 231  THR A CB  1 
ATOM   1851  O OG1 . THR A  1 231 ? 16.440  40.835 83.721  1.00 45.29  ? 231  THR A OG1 1 
ATOM   1852  C CG2 . THR A  1 231 ? 14.440  41.276 85.001  1.00 46.23  ? 231  THR A CG2 1 
ATOM   1853  N N   . ILE A  1 232 ? 14.552  40.918 81.455  1.00 45.43  ? 232  ILE A N   1 
ATOM   1854  C CA  . ILE A  1 232 ? 13.698  39.909 80.839  1.00 46.43  ? 232  ILE A CA  1 
ATOM   1855  C C   . ILE A  1 232 ? 13.844  38.640 81.664  1.00 47.48  ? 232  ILE A C   1 
ATOM   1856  O O   . ILE A  1 232 ? 14.935  38.080 81.770  1.00 47.47  ? 232  ILE A O   1 
ATOM   1857  C CB  . ILE A  1 232 ? 14.039  39.670 79.347  1.00 46.30  ? 232  ILE A CB  1 
ATOM   1858  C CG1 . ILE A  1 232 ? 13.196  40.585 78.453  1.00 46.06  ? 232  ILE A CG1 1 
ATOM   1859  C CG2 . ILE A  1 232 ? 13.752  38.233 78.927  1.00 47.51  ? 232  ILE A CG2 1 
ATOM   1860  C CD1 . ILE A  1 232 ? 13.272  42.053 78.805  1.00 45.11  ? 232  ILE A CD1 1 
ATOM   1861  N N   . LEU A  1 233 ? 12.739  38.209 82.262  1.00 48.64  ? 233  LEU A N   1 
ATOM   1862  C CA  . LEU A  1 233 ? 12.718  37.003 83.071  1.00 49.94  ? 233  LEU A CA  1 
ATOM   1863  C C   . LEU A  1 233 ? 12.297  35.836 82.186  1.00 51.13  ? 233  LEU A C   1 
ATOM   1864  O O   . LEU A  1 233 ? 11.177  35.806 81.675  1.00 51.81  ? 233  LEU A O   1 
ATOM   1865  C CB  . LEU A  1 233 ? 11.748  37.174 84.245  1.00 50.82  ? 233  LEU A CB  1 
ATOM   1866  C CG  . LEU A  1 233 ? 11.703  36.072 85.311  1.00 52.25  ? 233  LEU A CG  1 
ATOM   1867  C CD1 . LEU A  1 233 ? 13.038  35.940 86.032  1.00 51.81  ? 233  LEU A CD1 1 
ATOM   1868  C CD2 . LEU A  1 233 ? 10.583  36.356 86.302  1.00 53.34  ? 233  LEU A CD2 1 
ATOM   1869  N N   . LYS A  1 234 ? 13.203  34.882 82.001  1.00 51.59  ? 234  LYS A N   1 
ATOM   1870  C CA  . LYS A  1 234 ? 12.946  33.743 81.125  1.00 52.92  ? 234  LYS A CA  1 
ATOM   1871  C C   . LYS A  1 234 ? 12.002  32.750 81.800  1.00 54.84  ? 234  LYS A C   1 
ATOM   1872  O O   . LYS A  1 234 ? 11.868  32.766 83.027  1.00 55.19  ? 234  LYS A O   1 
ATOM   1873  C CB  . LYS A  1 234 ? 14.266  33.071 80.736  1.00 52.94  ? 234  LYS A CB  1 
ATOM   1874  C CG  . LYS A  1 234 ? 15.195  34.004 79.973  1.00 51.49  ? 234  LYS A CG  1 
ATOM   1875  C CD  . LYS A  1 234 ? 16.353  33.270 79.319  1.00 51.93  ? 234  LYS A CD  1 
ATOM   1876  C CE  . LYS A  1 234 ? 17.104  34.189 78.368  1.00 50.85  ? 234  LYS A CE  1 
ATOM   1877  N NZ  . LYS A  1 234 ? 18.147  33.471 77.586  1.00 51.59  ? 234  LYS A NZ  1 
ATOM   1878  N N   . PRO A  1 235 ? 11.331  31.890 81.006  1.00 56.38  ? 235  PRO A N   1 
ATOM   1879  C CA  . PRO A  1 235 ? 10.374  30.963 81.617  1.00 58.44  ? 235  PRO A CA  1 
ATOM   1880  C C   . PRO A  1 235 ? 11.043  30.002 82.593  1.00 59.40  ? 235  PRO A C   1 
ATOM   1881  O O   . PRO A  1 235 ? 12.196  29.615 82.386  1.00 59.03  ? 235  PRO A O   1 
ATOM   1882  C CB  . PRO A  1 235 ? 9.791   30.189 80.423  1.00 59.84  ? 235  PRO A CB  1 
ATOM   1883  C CG  . PRO A  1 235 ? 10.247  30.889 79.194  1.00 58.49  ? 235  PRO A CG  1 
ATOM   1884  C CD  . PRO A  1 235 ? 11.467  31.674 79.554  1.00 56.51  ? 235  PRO A CD  1 
ATOM   1885  N N   . ASN A  1 236 ? 10.322  29.640 83.653  1.00 60.82  ? 236  ASN A N   1 
ATOM   1886  C CA  . ASN A  1 236 ? 10.806  28.679 84.639  1.00 62.12  ? 236  ASN A CA  1 
ATOM   1887  C C   . ASN A  1 236 ? 11.943  29.244 85.501  1.00 60.75  ? 236  ASN A C   1 
ATOM   1888  O O   . ASN A  1 236 ? 12.628  28.491 86.194  1.00 61.64  ? 236  ASN A O   1 
ATOM   1889  C CB  . ASN A  1 236 ? 11.254  27.381 83.935  1.00 63.49  ? 236  ASN A CB  1 
ATOM   1890  C CG  . ASN A  1 236 ? 10.722  26.124 84.601  1.00 66.15  ? 236  ASN A CG  1 
ATOM   1891  O OD1 . ASN A  1 236 ? 10.137  26.166 85.681  1.00 67.19  ? 236  ASN A OD1 1 
ATOM   1892  N ND2 . ASN A  1 236 ? 10.912  24.988 83.938  1.00 67.65  ? 236  ASN A ND2 1 
ATOM   1893  N N   . ASP A  1 237 ? 12.133  30.564 85.459  1.00 58.83  ? 237  ASP A N   1 
ATOM   1894  C CA  . ASP A  1 237 ? 13.147  31.240 86.265  1.00 57.62  ? 237  ASP A CA  1 
ATOM   1895  C C   . ASP A  1 237 ? 12.451  32.169 87.254  1.00 57.47  ? 237  ASP A C   1 
ATOM   1896  O O   . ASP A  1 237 ? 11.397  32.737 86.954  1.00 57.43  ? 237  ASP A O   1 
ATOM   1897  C CB  . ASP A  1 237 ? 14.107  32.040 85.372  1.00 55.74  ? 237  ASP A CB  1 
ATOM   1898  C CG  . ASP A  1 237 ? 15.302  32.615 86.139  1.00 54.82  ? 237  ASP A CG  1 
ATOM   1899  O OD1 . ASP A  1 237 ? 15.692  32.047 87.185  1.00 55.76  ? 237  ASP A OD1 1 
ATOM   1900  O OD2 . ASP A  1 237 ? 15.858  33.640 85.685  1.00 53.28  ? 237  ASP A OD2 1 
ATOM   1901  N N   . ALA A  1 238 ? 13.047  32.314 88.433  1.00 57.58  ? 238  ALA A N   1 
ATOM   1902  C CA  . ALA A  1 238 ? 12.485  33.144 89.486  1.00 57.76  ? 238  ALA A CA  1 
ATOM   1903  C C   . ALA A  1 238 ? 13.292  34.429 89.655  1.00 56.03  ? 238  ALA A C   1 
ATOM   1904  O O   . ALA A  1 238 ? 14.522  34.418 89.542  1.00 55.27  ? 238  ALA A O   1 
ATOM   1905  C CB  . ALA A  1 238 ? 12.442  32.368 90.795  1.00 59.61  ? 238  ALA A CB  1 
ATOM   1906  N N   . ILE A  1 239 ? 12.591  35.531 89.915  1.00 55.61  ? 239  ILE A N   1 
ATOM   1907  C CA  . ILE A  1 239 ? 13.232  36.789 90.306  1.00 54.40  ? 239  ILE A CA  1 
ATOM   1908  C C   . ILE A  1 239 ? 13.044  36.999 91.817  1.00 55.66  ? 239  ILE A C   1 
ATOM   1909  O O   . ILE A  1 239 ? 11.959  36.761 92.347  1.00 57.09  ? 239  ILE A O   1 
ATOM   1910  C CB  . ILE A  1 239 ? 12.698  37.998 89.499  1.00 53.15  ? 239  ILE A CB  1 
ATOM   1911  C CG1 . ILE A  1 239 ? 13.524  39.252 89.808  1.00 52.02  ? 239  ILE A CG1 1 
ATOM   1912  C CG2 . ILE A  1 239 ? 11.217  38.255 89.769  1.00 54.22  ? 239  ILE A CG2 1 
ATOM   1913  C CD1 . ILE A  1 239 ? 13.362  40.359 88.788  1.00 50.66  ? 239  ILE A CD1 1 
ATOM   1914  N N   . ASN A  1 240 ? 14.106  37.426 92.500  1.00 55.35  ? 240  ASN A N   1 
ATOM   1915  C CA  . ASN A  1 240 ? 14.079  37.611 93.954  1.00 56.70  ? 240  ASN A CA  1 
ATOM   1916  C C   . ASN A  1 240 ? 14.431  39.040 94.353  1.00 55.98  ? 240  ASN A C   1 
ATOM   1917  O O   . ASN A  1 240 ? 15.474  39.559 93.958  1.00 54.74  ? 240  ASN A O   1 
ATOM   1918  C CB  . ASN A  1 240 ? 15.064  36.663 94.632  1.00 57.63  ? 240  ASN A CB  1 
ATOM   1919  C CG  . ASN A  1 240 ? 14.855  35.214 94.236  1.00 58.49  ? 240  ASN A CG  1 
ATOM   1920  O OD1 . ASN A  1 240 ? 13.798  34.639 94.489  1.00 59.89  ? 240  ASN A OD1 1 
ATOM   1921  N ND2 . ASN A  1 240 ? 15.870  34.612 93.620  1.00 57.91  ? 240  ASN A ND2 1 
ATOM   1922  N N   . PHE A  1 241 ? 13.560  39.655 95.150  1.00 57.01  ? 241  PHE A N   1 
ATOM   1923  C CA  . PHE A  1 241 ? 13.775  41.001 95.677  1.00 56.81  ? 241  PHE A CA  1 
ATOM   1924  C C   . PHE A  1 241 ? 14.043  40.952 97.177  1.00 58.60  ? 241  PHE A C   1 
ATOM   1925  O O   . PHE A  1 241 ? 13.375  40.221 97.902  1.00 60.36  ? 241  PHE A O   1 
ATOM   1926  C CB  . PHE A  1 241 ? 12.545  41.871 95.419  1.00 56.86  ? 241  PHE A CB  1 
ATOM   1927  C CG  . PHE A  1 241 ? 12.341  42.215 93.975  1.00 55.16  ? 241  PHE A CG  1 
ATOM   1928  C CD1 . PHE A  1 241 ? 12.974  43.316 93.419  1.00 53.72  ? 241  PHE A CD1 1 
ATOM   1929  C CD2 . PHE A  1 241 ? 11.521  41.439 93.170  1.00 55.21  ? 241  PHE A CD2 1 
ATOM   1930  C CE1 . PHE A  1 241 ? 12.795  43.640 92.084  1.00 52.32  ? 241  PHE A CE1 1 
ATOM   1931  C CE2 . PHE A  1 241 ? 11.332  41.757 91.835  1.00 53.86  ? 241  PHE A CE2 1 
ATOM   1932  C CZ  . PHE A  1 241 ? 11.972  42.860 91.290  1.00 52.39  ? 241  PHE A CZ  1 
ATOM   1933  N N   . GLU A  1 242 ? 15.028  41.722 97.632  1.00 58.37  ? 242  GLU A N   1 
ATOM   1934  C CA  . GLU A  1 242 ? 15.235  41.960 99.059  1.00 60.22  ? 242  GLU A CA  1 
ATOM   1935  C C   . GLU A  1 242 ? 15.565  43.437 99.273  1.00 59.91  ? 242  GLU A C   1 
ATOM   1936  O O   . GLU A  1 242 ? 16.483  43.965 98.638  1.00 58.52  ? 242  GLU A O   1 
ATOM   1937  C CB  . GLU A  1 242 ? 16.349  41.066 99.621  1.00 60.95  ? 242  GLU A CB  1 
ATOM   1938  C CG  . GLU A  1 242 ? 16.496  41.127 101.139 1.00 63.25  ? 242  GLU A CG  1 
ATOM   1939  C CD  . GLU A  1 242 ? 17.655  40.288 101.659 1.00 64.06  ? 242  GLU A CD  1 
ATOM   1940  O OE1 . GLU A  1 242 ? 17.651  39.056 101.448 1.00 64.31  ? 242  GLU A OE1 1 
ATOM   1941  O OE2 . GLU A  1 242 ? 18.567  40.855 102.295 1.00 64.66  ? 242  GLU A OE2 1 
ATOM   1942  N N   . SER A  1 243 ? 14.815  44.101 100.152 1.00 61.41  ? 243  SER A N   1 
ATOM   1943  C CA  . SER A  1 243 ? 15.029  45.527 100.411 1.00 61.44  ? 243  SER A CA  1 
ATOM   1944  C C   . SER A  1 243 ? 14.567  45.976 101.798 1.00 63.93  ? 243  SER A C   1 
ATOM   1945  O O   . SER A  1 243 ? 13.516  45.549 102.283 1.00 65.43  ? 243  SER A O   1 
ATOM   1946  C CB  . SER A  1 243 ? 14.315  46.369 99.354  1.00 60.02  ? 243  SER A CB  1 
ATOM   1947  O OG  . SER A  1 243 ? 14.585  47.747 99.541  1.00 60.10  ? 243  SER A OG  1 
ATOM   1948  N N   . ASN A  1 244 ? 15.363  46.853 102.411 1.00 64.54  ? 244  ASN A N   1 
ATOM   1949  C CA  . ASN A  1 244 ? 15.023  47.490 103.688 1.00 67.01  ? 244  ASN A CA  1 
ATOM   1950  C C   . ASN A  1 244 ? 14.740  48.990 103.530 1.00 66.95  ? 244  ASN A C   1 
ATOM   1951  O O   . ASN A  1 244 ? 14.735  49.729 104.517 1.00 68.94  ? 244  ASN A O   1 
ATOM   1952  C CB  . ASN A  1 244 ? 16.156  47.285 104.702 1.00 68.42  ? 244  ASN A CB  1 
ATOM   1953  C CG  . ASN A  1 244 ? 17.449  47.967 104.281 1.00 67.22  ? 244  ASN A CG  1 
ATOM   1954  O OD1 . ASN A  1 244 ? 17.746  48.069 103.089 1.00 64.95  ? 244  ASN A OD1 1 
ATOM   1955  N ND2 . ASN A  1 244 ? 18.224  48.432 105.254 1.00 68.95  ? 244  ASN A ND2 1 
ATOM   1956  N N   . GLY A  1 245 ? 14.508  49.433 102.293 1.00 64.84  ? 245  GLY A N   1 
ATOM   1957  C CA  . GLY A  1 245 ? 14.193  50.835 102.025 1.00 64.76  ? 245  GLY A CA  1 
ATOM   1958  C C   . GLY A  1 245 ? 14.283  51.261 100.569 1.00 62.29  ? 245  GLY A C   1 
ATOM   1959  O O   . GLY A  1 245 ? 15.033  50.680 99.782  1.00 60.51  ? 245  GLY A O   1 
ATOM   1960  N N   . ASN A  1 246 ? 13.500  52.286 100.231 1.00 62.41  ? 246  ASN A N   1 
ATOM   1961  C CA  . ASN A  1 246 ? 13.587  53.010 98.951  1.00 60.50  ? 246  ASN A CA  1 
ATOM   1962  C C   . ASN A  1 246 ? 13.212  52.198 97.705  1.00 58.54  ? 246  ASN A C   1 
ATOM   1963  O O   . ASN A  1 246 ? 13.671  52.499 96.605  1.00 56.77  ? 246  ASN A O   1 
ATOM   1964  C CB  . ASN A  1 246 ? 14.981  53.642 98.786  1.00 59.82  ? 246  ASN A CB  1 
ATOM   1965  C CG  . ASN A  1 246 ? 15.356  54.545 99.952  1.00 61.93  ? 246  ASN A CG  1 
ATOM   1966  O OD1 . ASN A  1 246 ? 15.616  54.071 101.059 1.00 63.49  ? 246  ASN A OD1 1 
ATOM   1967  N ND2 . ASN A  1 246 ? 15.390  55.852 99.708  1.00 62.16  ? 246  ASN A ND2 1 
ATOM   1968  N N   . PHE A  1 247 ? 12.338  51.207 97.881  1.00 59.09  ? 247  PHE A N   1 
ATOM   1969  C CA  . PHE A  1 247 ? 12.021  50.231 96.832  1.00 57.57  ? 247  PHE A CA  1 
ATOM   1970  C C   . PHE A  1 247 ? 10.705  50.534 96.122  1.00 57.53  ? 247  PHE A C   1 
ATOM   1971  O O   . PHE A  1 247 ? 9.680   50.761 96.760  1.00 59.30  ? 247  PHE A O   1 
ATOM   1972  C CB  . PHE A  1 247 ? 11.970  48.830 97.453  1.00 58.40  ? 247  PHE A CB  1 
ATOM   1973  C CG  . PHE A  1 247 ? 11.604  47.732 96.488  1.00 57.31  ? 247  PHE A CG  1 
ATOM   1974  C CD1 . PHE A  1 247 ? 12.320  47.543 95.315  1.00 55.28  ? 247  PHE A CD1 1 
ATOM   1975  C CD2 . PHE A  1 247 ? 10.563  46.858 96.776  1.00 58.58  ? 247  PHE A CD2 1 
ATOM   1976  C CE1 . PHE A  1 247 ? 11.992  46.524 94.436  1.00 54.51  ? 247  PHE A CE1 1 
ATOM   1977  C CE2 . PHE A  1 247 ? 10.232  45.834 95.905  1.00 57.82  ? 247  PHE A CE2 1 
ATOM   1978  C CZ  . PHE A  1 247 ? 10.948  45.667 94.733  1.00 55.79  ? 247  PHE A CZ  1 
ATOM   1979  N N   . ILE A  1 248 ? 10.747  50.532 94.794  1.00 55.73  ? 248  ILE A N   1 
ATOM   1980  C CA  . ILE A  1 248 ? 9.547   50.672 93.982  1.00 55.68  ? 248  ILE A CA  1 
ATOM   1981  C C   . ILE A  1 248 ? 9.214   49.287 93.430  1.00 55.23  ? 248  ILE A C   1 
ATOM   1982  O O   . ILE A  1 248 ? 9.850   48.810 92.490  1.00 53.61  ? 248  ILE A O   1 
ATOM   1983  C CB  . ILE A  1 248 ? 9.740   51.682 92.831  1.00 54.28  ? 248  ILE A CB  1 
ATOM   1984  C CG1 . ILE A  1 248 ? 10.435  52.962 93.315  1.00 54.56  ? 248  ILE A CG1 1 
ATOM   1985  C CG2 . ILE A  1 248 ? 8.399   52.018 92.197  1.00 54.80  ? 248  ILE A CG2 1 
ATOM   1986  C CD1 . ILE A  1 248 ? 9.598   53.824 94.238  1.00 56.62  ? 248  ILE A CD1 1 
ATOM   1987  N N   . ALA A  1 249 ? 8.223   48.639 94.033  1.00 56.91  ? 249  ALA A N   1 
ATOM   1988  C CA  . ALA A  1 249 ? 7.906   47.249 93.715  1.00 56.97  ? 249  ALA A CA  1 
ATOM   1989  C C   . ALA A  1 249 ? 7.120   47.121 92.410  1.00 56.34  ? 249  ALA A C   1 
ATOM   1990  O O   . ALA A  1 249 ? 6.361   48.021 92.054  1.00 56.65  ? 249  ALA A O   1 
ATOM   1991  C CB  . ALA A  1 249 ? 7.125   46.616 94.859  1.00 59.32  ? 249  ALA A CB  1 
ATOM   1992  N N   . PRO A  1 250 ? 7.306   46.000 91.691  1.00 55.61  ? 250  PRO A N   1 
ATOM   1993  C CA  . PRO A  1 250 ? 6.477   45.710 90.523  1.00 55.46  ? 250  PRO A CA  1 
ATOM   1994  C C   . PRO A  1 250 ? 5.098   45.168 90.895  1.00 57.70  ? 250  PRO A C   1 
ATOM   1995  O O   . PRO A  1 250 ? 5.009   44.141 91.556  1.00 58.86  ? 250  PRO A O   1 
ATOM   1996  C CB  . PRO A  1 250 ? 7.276   44.633 89.782  1.00 54.20  ? 250  PRO A CB  1 
ATOM   1997  C CG  . PRO A  1 250 ? 8.120   43.986 90.815  1.00 54.48  ? 250  PRO A CG  1 
ATOM   1998  C CD  . PRO A  1 250 ? 8.410   45.034 91.846  1.00 54.87  ? 250  PRO A CD  1 
ATOM   1999  N N   . GLU A  1 251 ? 4.040   45.860 90.476  1.00 58.52  ? 251  GLU A N   1 
ATOM   2000  C CA  . GLU A  1 251 ? 2.680   45.316 90.545  1.00 60.71  ? 251  GLU A CA  1 
ATOM   2001  C C   . GLU A  1 251 ? 2.431   44.456 89.307  1.00 60.23  ? 251  GLU A C   1 
ATOM   2002  O O   . GLU A  1 251 ? 2.069   43.279 89.416  1.00 61.35  ? 251  GLU A O   1 
ATOM   2003  C CB  . GLU A  1 251 ? 1.636   46.443 90.635  1.00 62.08  ? 251  GLU A CB  1 
ATOM   2004  C CG  . GLU A  1 251 ? 0.788   46.439 91.900  1.00 64.82  ? 251  GLU A CG  1 
ATOM   2005  C CD  . GLU A  1 251 ? -0.639  45.977 91.657  1.00 67.15  ? 251  GLU A CD  1 
ATOM   2006  O OE1 . GLU A  1 251 ? -1.356  46.649 90.888  1.00 67.44  ? 251  GLU A OE1 1 
ATOM   2007  O OE2 . GLU A  1 251 ? -1.052  44.954 92.243  1.00 68.91  ? 251  GLU A OE2 1 
ATOM   2008  N N   . TYR A  1 252 ? 2.648   45.061 88.137  1.00 58.71  ? 252  TYR A N   1 
ATOM   2009  C CA  . TYR A  1 252 ? 2.454   44.402 86.846  1.00 58.30  ? 252  TYR A CA  1 
ATOM   2010  C C   . TYR A  1 252 ? 3.761   44.255 86.061  1.00 55.98  ? 252  TYR A C   1 
ATOM   2011  O O   . TYR A  1 252 ? 4.667   45.093 86.156  1.00 54.51  ? 252  TYR A O   1 
ATOM   2012  C CB  . TYR A  1 252 ? 1.455   45.187 85.991  1.00 58.92  ? 252  TYR A CB  1 
ATOM   2013  C CG  . TYR A  1 252 ? 0.084   45.320 86.607  1.00 61.52  ? 252  TYR A CG  1 
ATOM   2014  C CD1 . TYR A  1 252 ? -0.883  44.335 86.424  1.00 63.48  ? 252  TYR A CD1 1 
ATOM   2015  C CD2 . TYR A  1 252 ? -0.249  46.433 87.371  1.00 62.29  ? 252  TYR A CD2 1 
ATOM   2016  C CE1 . TYR A  1 252 ? -2.145  44.454 86.991  1.00 66.16  ? 252  TYR A CE1 1 
ATOM   2017  C CE2 . TYR A  1 252 ? -1.506  46.561 87.942  1.00 64.94  ? 252  TYR A CE2 1 
ATOM   2018  C CZ  . TYR A  1 252 ? -2.452  45.569 87.751  1.00 66.88  ? 252  TYR A CZ  1 
ATOM   2019  O OH  . TYR A  1 252 ? -3.700  45.698 88.314  1.00 69.72  ? 252  TYR A OH  1 
ATOM   2020  N N   . ALA A  1 253 ? 3.838   43.179 85.284  1.00 55.90  ? 253  ALA A N   1 
ATOM   2021  C CA  . ALA A  1 253 ? 4.948   42.939 84.370  1.00 54.10  ? 253  ALA A CA  1 
ATOM   2022  C C   . ALA A  1 253 ? 4.379   42.528 83.014  1.00 54.44  ? 253  ALA A C   1 
ATOM   2023  O O   . ALA A  1 253 ? 3.479   41.687 82.945  1.00 56.14  ? 253  ALA A O   1 
ATOM   2024  C CB  . ALA A  1 253 ? 5.857   41.850 84.919  1.00 53.86  ? 253  ALA A CB  1 
ATOM   2025  N N   . TYR A  1 254 ? 4.898   43.130 81.946  1.00 53.04  ? 254  TYR A N   1 
ATOM   2026  C CA  . TYR A  1 254 ? 4.401   42.874 80.596  1.00 53.40  ? 254  TYR A CA  1 
ATOM   2027  C C   . TYR A  1 254 ? 4.888   41.528 80.070  1.00 53.51  ? 254  TYR A C   1 
ATOM   2028  O O   . TYR A  1 254 ? 6.061   41.182 80.204  1.00 52.37  ? 254  TYR A O   1 
ATOM   2029  C CB  . TYR A  1 254 ? 4.834   43.985 79.639  1.00 52.08  ? 254  TYR A CB  1 
ATOM   2030  C CG  . TYR A  1 254 ? 4.123   45.301 79.856  1.00 52.39  ? 254  TYR A CG  1 
ATOM   2031  C CD1 . TYR A  1 254 ? 2.895   45.561 79.253  1.00 53.79  ? 254  TYR A CD1 1 
ATOM   2032  C CD2 . TYR A  1 254 ? 4.683   46.292 80.654  1.00 51.50  ? 254  TYR A CD2 1 
ATOM   2033  C CE1 . TYR A  1 254 ? 2.242   46.771 79.440  1.00 54.29  ? 254  TYR A CE1 1 
ATOM   2034  C CE2 . TYR A  1 254 ? 4.036   47.502 80.850  1.00 52.00  ? 254  TYR A CE2 1 
ATOM   2035  C CZ  . TYR A  1 254 ? 2.814   47.740 80.243  1.00 53.39  ? 254  TYR A CZ  1 
ATOM   2036  O OH  . TYR A  1 254 ? 2.167   48.943 80.441  1.00 54.07  ? 254  TYR A OH  1 
ATOM   2037  N N   . LYS A  1 255 ? 3.971   40.789 79.457  1.00 55.10  ? 255  LYS A N   1 
ATOM   2038  C CA  . LYS A  1 255 ? 4.245   39.458 78.929  1.00 55.70  ? 255  LYS A CA  1 
ATOM   2039  C C   . LYS A  1 255 ? 4.377   39.561 77.414  1.00 55.41  ? 255  LYS A C   1 
ATOM   2040  O O   . LYS A  1 255 ? 3.531   40.171 76.759  1.00 56.06  ? 255  LYS A O   1 
ATOM   2041  C CB  . LYS A  1 255 ? 3.097   38.514 79.310  1.00 58.08  ? 255  LYS A CB  1 
ATOM   2042  C CG  . LYS A  1 255 ? 3.504   37.069 79.540  1.00 58.86  ? 255  LYS A CG  1 
ATOM   2043  C CD  . LYS A  1 255 ? 2.505   36.337 80.431  1.00 61.12  ? 255  LYS A CD  1 
ATOM   2044  C CE  . LYS A  1 255 ? 1.267   35.882 79.675  1.00 63.39  ? 255  LYS A CE  1 
ATOM   2045  N NZ  . LYS A  1 255 ? 0.515   34.850 80.444  1.00 65.84  ? 255  LYS A NZ  1 
ATOM   2046  N N   . ILE A  1 256 ? 5.428   38.959 76.861  1.00 54.65  ? 256  ILE A N   1 
ATOM   2047  C CA  . ILE A  1 256 ? 5.749   39.116 75.437  1.00 54.35  ? 256  ILE A CA  1 
ATOM   2048  C C   . ILE A  1 256 ? 5.152   37.957 74.639  1.00 56.25  ? 256  ILE A C   1 
ATOM   2049  O O   . ILE A  1 256 ? 5.797   36.927 74.438  1.00 56.52  ? 256  ILE A O   1 
ATOM   2050  C CB  . ILE A  1 256 ? 7.276   39.194 75.176  1.00 52.72  ? 256  ILE A CB  1 
ATOM   2051  C CG1 . ILE A  1 256 ? 8.020   39.793 76.377  1.00 51.29  ? 256  ILE A CG1 1 
ATOM   2052  C CG2 . ILE A  1 256 ? 7.542   39.988 73.903  1.00 52.18  ? 256  ILE A CG2 1 
ATOM   2053  C CD1 . ILE A  1 256 ? 9.469   40.141 76.108  1.00 49.81  ? 256  ILE A CD1 1 
ATOM   2054  N N   . VAL A  1 257 ? 3.916   38.131 74.183  1.00 57.75  ? 257  VAL A N   1 
ATOM   2055  C CA  . VAL A  1 257 ? 3.206   37.049 73.494  1.00 59.97  ? 257  VAL A CA  1 
ATOM   2056  C C   . VAL A  1 257 ? 3.671   36.869 72.042  1.00 60.12  ? 257  VAL A C   1 
ATOM   2057  O O   . VAL A  1 257 ? 3.896   35.737 71.600  1.00 61.26  ? 257  VAL A O   1 
ATOM   2058  C CB  . VAL A  1 257 ? 1.662   37.197 73.577  1.00 62.00  ? 257  VAL A CB  1 
ATOM   2059  C CG1 . VAL A  1 257 ? 1.204   37.090 75.024  1.00 62.41  ? 257  VAL A CG1 1 
ATOM   2060  C CG2 . VAL A  1 257 ? 1.166   38.499 72.957  1.00 61.68  ? 257  VAL A CG2 1 
ATOM   2061  N N   . LYS A  1 258 ? 3.828   37.977 71.314  1.00 59.14  ? 258  LYS A N   1 
ATOM   2062  C CA  . LYS A  1 258 ? 4.247   37.932 69.907  1.00 59.43  ? 258  LYS A CA  1 
ATOM   2063  C C   . LYS A  1 258 ? 5.542   38.692 69.649  1.00 57.31  ? 258  LYS A C   1 
ATOM   2064  O O   . LYS A  1 258 ? 5.694   39.837 70.077  1.00 55.87  ? 258  LYS A O   1 
ATOM   2065  C CB  . LYS A  1 258 ? 3.149   38.485 68.988  1.00 60.89  ? 258  LYS A CB  1 
ATOM   2066  C CG  . LYS A  1 258 ? 2.384   37.416 68.219  1.00 63.55  ? 258  LYS A CG  1 
ATOM   2067  C CD  . LYS A  1 258 ? 2.221   37.778 66.747  1.00 64.56  ? 258  LYS A CD  1 
ATOM   2068  C CE  . LYS A  1 258 ? 1.306   38.975 66.538  1.00 64.84  ? 258  LYS A CE  1 
ATOM   2069  N NZ  . LYS A  1 258 ? 0.761   38.980 65.151  1.00 66.86  ? 258  LYS A NZ  1 
ATOM   2070  N N   . LYS A  1 259 ? 6.461   38.041 68.936  1.00 57.40  ? 259  LYS A N   1 
ATOM   2071  C CA  . LYS A  1 259 ? 7.694   38.667 68.464  1.00 55.92  ? 259  LYS A CA  1 
ATOM   2072  C C   . LYS A  1 259 ? 7.682   38.719 66.940  1.00 57.07  ? 259  LYS A C   1 
ATOM   2073  O O   . LYS A  1 259 ? 7.667   37.679 66.283  1.00 58.67  ? 259  LYS A O   1 
ATOM   2074  C CB  . LYS A  1 259 ? 8.918   37.872 68.923  1.00 55.27  ? 259  LYS A CB  1 
ATOM   2075  C CG  . LYS A  1 259 ? 9.066   37.758 70.427  1.00 54.26  ? 259  LYS A CG  1 
ATOM   2076  C CD  . LYS A  1 259 ? 10.337  37.013 70.803  1.00 53.79  ? 259  LYS A CD  1 
ATOM   2077  C CE  . LYS A  1 259 ? 10.448  36.861 72.312  1.00 53.03  ? 259  LYS A CE  1 
ATOM   2078  N NZ  . LYS A  1 259 ? 11.616  36.036 72.724  1.00 52.88  ? 259  LYS A NZ  1 
ATOM   2079  N N   . GLY A  1 260 ? 7.688   39.926 66.382  1.00 66.74  ? 260  GLY A N   1 
ATOM   2080  C CA  . GLY A  1 260 ? 7.699   40.102 64.931  1.00 65.22  ? 260  GLY A CA  1 
ATOM   2081  C C   . GLY A  1 260 ? 8.471   41.331 64.497  1.00 60.25  ? 260  GLY A C   1 
ATOM   2082  O O   . GLY A  1 260 ? 9.097   42.004 65.316  1.00 58.27  ? 260  GLY A O   1 
ATOM   2083  N N   . ASP A  1 261 ? 8.431   41.617 63.200  1.00 58.57  ? 261  ASP A N   1 
ATOM   2084  C CA  . ASP A  1 261 ? 9.049   42.823 62.670  1.00 54.23  ? 261  ASP A CA  1 
ATOM   2085  C C   . ASP A  1 261 ? 8.230   44.034 63.087  1.00 51.74  ? 261  ASP A C   1 
ATOM   2086  O O   . ASP A  1 261 ? 7.042   44.126 62.784  1.00 52.43  ? 261  ASP A O   1 
ATOM   2087  C CB  . ASP A  1 261 ? 9.163   42.765 61.140  1.00 53.46  ? 261  ASP A CB  1 
ATOM   2088  C CG  . ASP A  1 261 ? 10.246  41.811 60.670  1.00 55.49  ? 261  ASP A CG  1 
ATOM   2089  O OD1 . ASP A  1 261 ? 11.113  41.438 61.490  1.00 56.89  ? 261  ASP A OD1 1 
ATOM   2090  O OD2 . ASP A  1 261 ? 10.235  41.436 59.475  1.00 56.01  ? 261  ASP A OD2 1 
ATOM   2091  N N   . SER A  1 262 ? 8.874   44.949 63.799  1.00 49.41  ? 262  SER A N   1 
ATOM   2092  C CA  . SER A  1 262 ? 8.243   46.183 64.244  1.00 47.38  ? 262  SER A CA  1 
ATOM   2093  C C   . SER A  1 262 ? 9.284   47.296 64.186  1.00 44.46  ? 262  SER A C   1 
ATOM   2094  O O   . SER A  1 262 ? 10.443  47.052 63.839  1.00 44.22  ? 262  SER A O   1 
ATOM   2095  C CB  . SER A  1 262 ? 7.697   46.016 65.670  1.00 49.03  ? 262  SER A CB  1 
ATOM   2096  O OG  . SER A  1 262 ? 7.185   47.234 66.192  1.00 47.37  ? 262  SER A OG  1 
ATOM   2097  N N   . THR A  1 263 ? 8.871   48.515 64.514  1.00 42.80  ? 263  THR A N   1 
ATOM   2098  C CA  . THR A  1 263 ? 9.787   49.649 64.526  1.00 40.63  ? 263  THR A CA  1 
ATOM   2099  C C   . THR A  1 263 ? 9.178   50.803 65.315  1.00 40.06  ? 263  THR A C   1 
ATOM   2100  O O   . THR A  1 263 ? 7.956   50.987 65.312  1.00 40.73  ? 263  THR A O   1 
ATOM   2101  C CB  . THR A  1 263 ? 10.142  50.103 63.088  1.00 38.97  ? 263  THR A CB  1 
ATOM   2102  O OG1 . THR A  1 263 ? 11.386  50.807 63.099  1.00 37.81  ? 263  THR A OG1 1 
ATOM   2103  C CG2 . THR A  1 263 ? 9.063   50.999 62.485  1.00 38.15  ? 263  THR A CG2 1 
ATOM   2104  N N   . ILE A  1 264 ? 10.027  51.562 66.002  1.00 39.35  ? 264  ILE A N   1 
ATOM   2105  C CA  . ILE A  1 264 ? 9.586   52.780 66.669  1.00 39.05  ? 264  ILE A CA  1 
ATOM   2106  C C   . ILE A  1 264 ? 9.827   53.959 65.734  1.00 37.71  ? 264  ILE A C   1 
ATOM   2107  O O   . ILE A  1 264 ? 10.950  54.443 65.587  1.00 37.08  ? 264  ILE A O   1 
ATOM   2108  C CB  . ILE A  1 264 ? 10.288  52.994 68.021  1.00 39.61  ? 264  ILE A CB  1 
ATOM   2109  C CG1 . ILE A  1 264 ? 9.944   51.842 68.966  1.00 41.27  ? 264  ILE A CG1 1 
ATOM   2110  C CG2 . ILE A  1 264 ? 9.853   54.316 68.642  1.00 39.56  ? 264  ILE A CG2 1 
ATOM   2111  C CD1 . ILE A  1 264 ? 10.907  51.684 70.119  1.00 42.10  ? 264  ILE A CD1 1 
ATOM   2112  N N   . MET A  1 265 ? 8.746   54.396 65.100  1.00 37.77  ? 265  MET A N   1 
ATOM   2113  C CA  . MET A  1 265 ? 8.762   55.503 64.160  1.00 37.03  ? 265  MET A CA  1 
ATOM   2114  C C   . MET A  1 265 ? 8.700   56.830 64.910  1.00 37.70  ? 265  MET A C   1 
ATOM   2115  O O   . MET A  1 265 ? 7.961   56.967 65.884  1.00 38.87  ? 265  MET A O   1 
ATOM   2116  C CB  . MET A  1 265 ? 7.556   55.377 63.236  1.00 37.50  ? 265  MET A CB  1 
ATOM   2117  C CG  . MET A  1 265 ? 7.646   56.161 61.945  1.00 36.72  ? 265  MET A CG  1 
ATOM   2118  S SD  . MET A  1 265 ? 6.314   55.660 60.840  1.00 37.66  ? 265  MET A SD  1 
ATOM   2119  C CE  . MET A  1 265 ? 6.902   54.058 60.285  1.00 36.92  ? 265  MET A CE  1 
ATOM   2120  N N   . LYS A  1 266 ? 9.486   57.796 64.448  1.00 37.33  ? 266  LYS A N   1 
ATOM   2121  C CA  . LYS A  1 266 ? 9.534   59.119 65.050  1.00 38.56  ? 266  LYS A CA  1 
ATOM   2122  C C   . LYS A  1 266 ? 8.762   60.089 64.172  1.00 39.42  ? 266  LYS A C   1 
ATOM   2123  O O   . LYS A  1 266 ? 9.183   60.393 63.057  1.00 38.78  ? 266  LYS A O   1 
ATOM   2124  C CB  . LYS A  1 266 ? 10.984  59.578 65.207  1.00 38.51  ? 266  LYS A CB  1 
ATOM   2125  C CG  . LYS A  1 266 ? 11.684  58.987 66.423  1.00 38.81  ? 266  LYS A CG  1 
ATOM   2126  C CD  . LYS A  1 266 ? 11.253  59.673 67.714  1.00 40.32  ? 266  LYS A CD  1 
ATOM   2127  C CE  . LYS A  1 266 ? 12.154  59.297 68.888  1.00 40.91  ? 266  LYS A CE  1 
ATOM   2128  N NZ  . LYS A  1 266 ? 11.586  59.787 70.185  1.00 42.30  ? 266  LYS A NZ  1 
ATOM   2129  N N   . SER A  1 267 ? 7.630   60.571 64.675  1.00 41.27  ? 267  SER A N   1 
ATOM   2130  C CA  . SER A  1 267 ? 6.748   61.429 63.888  1.00 42.84  ? 267  SER A CA  1 
ATOM   2131  C C   . SER A  1 267 ? 5.810   62.268 64.758  1.00 45.72  ? 267  SER A C   1 
ATOM   2132  O O   . SER A  1 267 ? 5.270   61.786 65.757  1.00 46.35  ? 267  SER A O   1 
ATOM   2133  C CB  . SER A  1 267 ? 5.923   60.572 62.928  1.00 42.37  ? 267  SER A CB  1 
ATOM   2134  O OG  . SER A  1 267 ? 5.008   61.365 62.191  1.00 44.31  ? 267  SER A OG  1 
ATOM   2135  N N   . GLU A  1 268 ? 5.620   63.524 64.357  1.00 47.86  ? 268  GLU A N   1 
ATOM   2136  C CA  . GLU A  1 268 ? 4.683   64.429 65.022  1.00 51.33  ? 268  GLU A CA  1 
ATOM   2137  C C   . GLU A  1 268 ? 3.259   64.197 64.526  1.00 53.18  ? 268  GLU A C   1 
ATOM   2138  O O   . GLU A  1 268 ? 2.304   64.628 65.169  1.00 56.32  ? 268  GLU A O   1 
ATOM   2139  C CB  . GLU A  1 268 ? 5.069   65.895 64.781  1.00 53.70  ? 268  GLU A CB  1 
ATOM   2140  C CG  . GLU A  1 268 ? 6.503   66.252 65.145  1.00 52.79  ? 268  GLU A CG  1 
ATOM   2141  C CD  . GLU A  1 268 ? 6.837   65.947 66.592  1.00 52.57  ? 268  GLU A CD  1 
ATOM   2142  O OE1 . GLU A  1 268 ? 6.112   66.433 67.492  1.00 55.07  ? 268  GLU A OE1 1 
ATOM   2143  O OE2 . GLU A  1 268 ? 7.831   65.223 66.822  1.00 50.14  ? 268  GLU A OE2 1 
ATOM   2144  N N   . LEU A  1 269 ? 3.123   63.518 63.388  1.00 51.72  ? 269  LEU A N   1 
ATOM   2145  C CA  . LEU A  1 269 ? 1.817   63.299 62.757  1.00 53.86  ? 269  LEU A CA  1 
ATOM   2146  C C   . LEU A  1 269 ? 0.935   62.365 63.572  1.00 54.84  ? 269  LEU A C   1 
ATOM   2147  O O   . LEU A  1 269 ? 1.430   61.569 64.371  1.00 52.86  ? 269  LEU A O   1 
ATOM   2148  C CB  . LEU A  1 269 ? 1.983   62.749 61.333  1.00 51.96  ? 269  LEU A CB  1 
ATOM   2149  C CG  . LEU A  1 269 ? 2.279   63.798 60.255  1.00 52.63  ? 269  LEU A CG  1 
ATOM   2150  C CD1 . LEU A  1 269 ? 2.909   63.164 59.025  1.00 49.69  ? 269  LEU A CD1 1 
ATOM   2151  C CD2 . LEU A  1 269 ? 1.010   64.549 59.879  1.00 56.92  ? 269  LEU A CD2 1 
ATOM   2152  N N   . GLU A  1 270 ? -0.373  62.466 63.344  1.00 58.39  ? 270  GLU A N   1 
ATOM   2153  C CA  . GLU A  1 270 ? -1.366  61.725 64.131  1.00 60.53  ? 270  GLU A CA  1 
ATOM   2154  C C   . GLU A  1 270 ? -1.847  60.465 63.383  1.00 60.22  ? 270  GLU A C   1 
ATOM   2155  O O   . GLU A  1 270 ? -1.044  59.559 63.159  1.00 56.95  ? 270  GLU A O   1 
ATOM   2156  C CB  . GLU A  1 270 ? -2.515  62.647 64.613  1.00 65.56  ? 270  GLU A CB  1 
ATOM   2157  C CG  . GLU A  1 270 ? -3.007  63.704 63.621  1.00 68.58  ? 270  GLU A CG  1 
ATOM   2158  C CD  . GLU A  1 270 ? -4.149  64.551 64.170  1.00 74.27  ? 270  GLU A CD  1 
ATOM   2159  O OE1 . GLU A  1 270 ? -4.686  64.225 65.250  1.00 75.90  ? 270  GLU A OE1 1 
ATOM   2160  O OE2 . GLU A  1 270 ? -4.514  65.554 63.519  1.00 77.49  ? 270  GLU A OE2 1 
ATOM   2161  N N   . TYR A  1 271 ? -3.119  60.397 62.990  1.00 64.14  ? 271  TYR A N   1 
ATOM   2162  C CA  . TYR A  1 271 ? -3.688  59.173 62.418  1.00 64.77  ? 271  TYR A CA  1 
ATOM   2163  C C   . TYR A  1 271 ? -4.683  59.504 61.305  1.00 68.35  ? 271  TYR A C   1 
ATOM   2164  O O   . TYR A  1 271 ? -5.685  60.185 61.543  1.00 72.85  ? 271  TYR A O   1 
ATOM   2165  C CB  . TYR A  1 271 ? -4.377  58.367 63.525  1.00 66.96  ? 271  TYR A CB  1 
ATOM   2166  C CG  . TYR A  1 271 ? -4.909  57.016 63.091  1.00 68.10  ? 271  TYR A CG  1 
ATOM   2167  C CD1 . TYR A  1 271 ? -4.043  55.980 62.752  1.00 64.64  ? 271  TYR A CD1 1 
ATOM   2168  C CD2 . TYR A  1 271 ? -6.282  56.769 63.035  1.00 73.26  ? 271  TYR A CD2 1 
ATOM   2169  C CE1 . TYR A  1 271 ? -4.525  54.742 62.361  1.00 66.27  ? 271  TYR A CE1 1 
ATOM   2170  C CE2 . TYR A  1 271 ? -6.772  55.534 62.646  1.00 74.95  ? 271  TYR A CE2 1 
ATOM   2171  C CZ  . TYR A  1 271 ? -5.890  54.524 62.309  1.00 71.42  ? 271  TYR A CZ  1 
ATOM   2172  O OH  . TYR A  1 271 ? -6.376  53.297 61.923  1.00 73.66  ? 271  TYR A OH  1 
ATOM   2173  N N   . GLY A  1 272 ? -4.406  59.020 60.095  1.00 66.70  ? 272  GLY A N   1 
ATOM   2174  C CA  . GLY A  1 272 ? -5.269  59.280 58.938  1.00 69.95  ? 272  GLY A CA  1 
ATOM   2175  C C   . GLY A  1 272 ? -6.460  58.340 58.785  1.00 74.03  ? 272  GLY A C   1 
ATOM   2176  O O   . GLY A  1 272 ? -7.360  58.606 57.981  1.00 77.86  ? 272  GLY A O   1 
ATOM   2177  N N   . ASN A  1 273 ? -6.465  57.248 59.554  1.00 73.69  ? 273  ASN A N   1 
ATOM   2178  C CA  . ASN A  1 273 ? -7.462  56.176 59.417  1.00 77.58  ? 273  ASN A CA  1 
ATOM   2179  C C   . ASN A  1 273 ? -7.450  55.576 58.010  1.00 77.27  ? 273  ASN A C   1 
ATOM   2180  O O   . ASN A  1 273 ? -8.494  55.280 57.425  1.00 81.82  ? 273  ASN A O   1 
ATOM   2181  C CB  . ASN A  1 273 ? -8.862  56.668 59.811  1.00 84.00  ? 273  ASN A CB  1 
ATOM   2182  C CG  . ASN A  1 273 ? -9.770  55.540 60.273  1.00 88.16  ? 273  ASN A CG  1 
ATOM   2183  O OD1 . ASN A  1 273 ? -10.332 55.594 61.366  1.00 91.02  ? 273  ASN A OD1 1 
ATOM   2184  N ND2 . ASN A  1 273 ? -9.909  54.506 59.447  1.00 88.81  ? 273  ASN A ND2 1 
ATOM   2185  N N   . CYS A  1 274 ? -6.242  55.395 57.486  1.00 72.17  ? 274  CYS A N   1 
ATOM   2186  C CA  . CYS A  1 274 ? -6.042  54.846 56.160  1.00 71.22  ? 274  CYS A CA  1 
ATOM   2187  C C   . CYS A  1 274 ? -5.278  53.529 56.295  1.00 68.44  ? 274  CYS A C   1 
ATOM   2188  O O   . CYS A  1 274 ? -4.734  53.228 57.361  1.00 66.69  ? 274  CYS A O   1 
ATOM   2189  C CB  . CYS A  1 274 ? -5.286  55.861 55.293  1.00 68.16  ? 274  CYS A CB  1 
ATOM   2190  S SG  . CYS A  1 274 ? -3.584  55.428 54.868  1.00 61.95  ? 274  CYS A SG  1 
ATOM   2191  N N   . ASN A  1 275 ? -5.260  52.744 55.221  1.00 68.46  ? 275  ASN A N   1 
ATOM   2192  C CA  . ASN A  1 275 ? -4.523  51.482 55.181  1.00 66.46  ? 275  ASN A CA  1 
ATOM   2193  C C   . ASN A  1 275 ? -3.438  51.536 54.108  1.00 62.19  ? 275  ASN A C   1 
ATOM   2194  O O   . ASN A  1 275 ? -3.623  52.159 53.062  1.00 62.18  ? 275  ASN A O   1 
ATOM   2195  C CB  . ASN A  1 275 ? -5.480  50.319 54.902  1.00 71.27  ? 275  ASN A CB  1 
ATOM   2196  C CG  . ASN A  1 275 ? -4.822  48.961 55.090  1.00 70.47  ? 275  ASN A CG  1 
ATOM   2197  O OD1 . ASN A  1 275 ? -4.365  48.631 56.180  1.00 69.45  ? 275  ASN A OD1 1 
ATOM   2198  N ND2 . ASN A  1 275 ? -4.774  48.168 54.028  1.00 71.33  ? 275  ASN A ND2 1 
ATOM   2199  N N   . THR A  1 276 ? -2.308  50.884 54.365  1.00 58.90  ? 276  THR A N   1 
ATOM   2200  C CA  . THR A  1 276 ? -1.197  50.870 53.414  1.00 55.10  ? 276  THR A CA  1 
ATOM   2201  C C   . THR A  1 276 ? -0.404  49.572 53.520  1.00 54.24  ? 276  THR A C   1 
ATOM   2202  O O   . THR A  1 276 ? -0.692  48.727 54.367  1.00 56.49  ? 276  THR A O   1 
ATOM   2203  C CB  . THR A  1 276 ? -0.264  52.084 53.631  1.00 51.27  ? 276  THR A CB  1 
ATOM   2204  O OG1 . THR A  1 276 ? 0.742   52.122 52.610  1.00 48.23  ? 276  THR A OG1 1 
ATOM   2205  C CG2 . THR A  1 276 ? 0.405   52.039 55.011  1.00 49.80  ? 276  THR A CG2 1 
ATOM   2206  N N   . LYS A  1 277 ? 0.577   49.411 52.637  1.00 51.47  ? 277  LYS A N   1 
ATOM   2207  C CA  . LYS A  1 277 ? 1.508   48.287 52.710  1.00 50.71  ? 277  LYS A CA  1 
ATOM   2208  C C   . LYS A  1 277 ? 2.968   48.761 52.770  1.00 46.47  ? 277  LYS A C   1 
ATOM   2209  O O   . LYS A  1 277 ? 3.896   47.950 52.761  1.00 45.81  ? 277  LYS A O   1 
ATOM   2210  C CB  . LYS A  1 277 ? 1.280   47.348 51.526  1.00 52.69  ? 277  LYS A CB  1 
ATOM   2211  C CG  . LYS A  1 277 ? 1.156   45.883 51.940  1.00 56.08  ? 277  LYS A CG  1 
ATOM   2212  C CD  . LYS A  1 277 ? 0.914   44.979 50.733  1.00 58.53  ? 277  LYS A CD  1 
ATOM   2213  C CE  . LYS A  1 277 ? 2.231   44.585 50.039  1.00 56.04  ? 277  LYS A CE  1 
ATOM   2214  N NZ  . LYS A  1 277 ? 2.381   43.113 49.827  1.00 59.50  ? 277  LYS A NZ  1 
ATOM   2215  N N   . CYS A  1 278 ? 3.152   50.077 52.844  1.00 44.20  ? 278  CYS A N   1 
ATOM   2216  C CA  . CYS A  1 278 ? 4.463   50.697 52.966  1.00 40.85  ? 278  CYS A CA  1 
ATOM   2217  C C   . CYS A  1 278 ? 4.273   52.028 53.673  1.00 40.16  ? 278  CYS A C   1 
ATOM   2218  O O   . CYS A  1 278 ? 3.592   52.914 53.151  1.00 40.73  ? 278  CYS A O   1 
ATOM   2219  C CB  . CYS A  1 278 ? 5.077   50.938 51.589  1.00 39.03  ? 278  CYS A CB  1 
ATOM   2220  S SG  . CYS A  1 278 ? 6.645   51.848 51.623  1.00 35.71  ? 278  CYS A SG  1 
ATOM   2221  N N   . GLN A  1 279 ? 4.866   52.173 54.855  1.00 39.36  ? 279  GLN A N   1 
ATOM   2222  C CA  . GLN A  1 279 ? 4.652   53.367 55.667  1.00 39.24  ? 279  GLN A CA  1 
ATOM   2223  C C   . GLN A  1 279 ? 5.953   54.113 55.934  1.00 36.89  ? 279  GLN A C   1 
ATOM   2224  O O   . GLN A  1 279 ? 6.998   53.500 56.152  1.00 35.76  ? 279  GLN A O   1 
ATOM   2225  C CB  . GLN A  1 279 ? 3.988   52.985 56.989  1.00 41.16  ? 279  GLN A CB  1 
ATOM   2226  C CG  . GLN A  1 279 ? 3.655   54.165 57.893  1.00 41.62  ? 279  GLN A CG  1 
ATOM   2227  C CD  . GLN A  1 279 ? 2.489   54.994 57.385  1.00 43.68  ? 279  GLN A CD  1 
ATOM   2228  O OE1 . GLN A  1 279 ? 1.395   54.473 57.167  1.00 46.29  ? 279  GLN A OE1 1 
ATOM   2229  N NE2 . GLN A  1 279 ? 2.711   56.293 57.209  1.00 43.14  ? 279  GLN A NE2 1 
ATOM   2230  N N   . THR A  1 280 ? 5.864   55.442 55.906  1.00 36.76  ? 280  THR A N   1 
ATOM   2231  C CA  . THR A  1 280 ? 6.957   56.326 56.301  1.00 35.48  ? 280  THR A CA  1 
ATOM   2232  C C   . THR A  1 280 ? 6.474   57.272 57.406  1.00 36.89  ? 280  THR A C   1 
ATOM   2233  O O   . THR A  1 280 ? 5.266   57.442 57.594  1.00 38.76  ? 280  THR A O   1 
ATOM   2234  C CB  . THR A  1 280 ? 7.473   57.178 55.116  1.00 34.52  ? 280  THR A CB  1 
ATOM   2235  O OG1 . THR A  1 280 ? 6.636   58.330 54.933  1.00 36.00  ? 280  THR A OG1 1 
ATOM   2236  C CG2 . THR A  1 280 ? 7.511   56.364 53.830  1.00 33.74  ? 280  THR A CG2 1 
ATOM   2237  N N   . PRO A  1 281 ? 7.419   57.896 58.138  1.00 36.42  ? 281  PRO A N   1 
ATOM   2238  C CA  . PRO A  1 281 ? 7.071   58.947 59.113  1.00 37.99  ? 281  PRO A CA  1 
ATOM   2239  C C   . PRO A  1 281 ? 6.395   60.187 58.498  1.00 39.72  ? 281  PRO A C   1 
ATOM   2240  O O   . PRO A  1 281 ? 5.707   60.928 59.212  1.00 41.82  ? 281  PRO A O   1 
ATOM   2241  C CB  . PRO A  1 281 ? 8.421   59.332 59.744  1.00 37.18  ? 281  PRO A CB  1 
ATOM   2242  C CG  . PRO A  1 281 ? 9.474   58.541 59.047  1.00 35.40  ? 281  PRO A CG  1 
ATOM   2243  C CD  . PRO A  1 281 ? 8.824   57.463 58.246  1.00 34.89  ? 281  PRO A CD  1 
ATOM   2244  N N   . MET A  1 282 ? 6.602   60.402 57.197  1.00 39.17  ? 282  MET A N   1 
ATOM   2245  C CA  . MET A  1 282 ? 6.016   61.527 56.459  1.00 41.08  ? 282  MET A CA  1 
ATOM   2246  C C   . MET A  1 282 ? 4.614   61.196 55.945  1.00 42.70  ? 282  MET A C   1 
ATOM   2247  O O   . MET A  1 282 ? 3.789   62.088 55.746  1.00 45.35  ? 282  MET A O   1 
ATOM   2248  C CB  . MET A  1 282 ? 6.904   61.877 55.262  1.00 39.95  ? 282  MET A CB  1 
ATOM   2249  C CG  . MET A  1 282 ? 8.369   62.118 55.605  1.00 38.85  ? 282  MET A CG  1 
ATOM   2250  S SD  . MET A  1 282 ? 8.791   63.866 55.713  1.00 41.53  ? 282  MET A SD  1 
ATOM   2251  C CE  . MET A  1 282 ? 8.815   64.277 53.965  1.00 41.46  ? 282  MET A CE  1 
ATOM   2252  N N   . GLY A  1 283 ? 4.365   59.911 55.708  1.00 41.62  ? 283  GLY A N   1 
ATOM   2253  C CA  . GLY A  1 283 ? 3.092   59.443 55.166  1.00 43.51  ? 283  GLY A CA  1 
ATOM   2254  C C   . GLY A  1 283 ? 3.212   58.031 54.620  1.00 42.09  ? 283  GLY A C   1 
ATOM   2255  O O   . GLY A  1 283 ? 4.237   57.375 54.804  1.00 39.84  ? 283  GLY A O   1 
ATOM   2256  N N   . ALA A  1 284 ? 2.171   57.563 53.939  1.00 43.94  ? 284  ALA A N   1 
ATOM   2257  C CA  . ALA A  1 284 ? 2.160   56.210 53.382  1.00 43.41  ? 284  ALA A CA  1 
ATOM   2258  C C   . ALA A  1 284 ? 2.452   56.218 51.881  1.00 42.32  ? 284  ALA A C   1 
ATOM   2259  O O   . ALA A  1 284 ? 2.259   57.232 51.201  1.00 42.86  ? 284  ALA A O   1 
ATOM   2260  C CB  . ALA A  1 284 ? 0.825   55.543 53.656  1.00 46.79  ? 284  ALA A CB  1 
ATOM   2261  N N   . ILE A  1 285 ? 2.910   55.072 51.377  1.00 41.12  ? 285  ILE A N   1 
ATOM   2262  C CA  . ILE A  1 285 ? 3.278   54.913 49.969  1.00 39.94  ? 285  ILE A CA  1 
ATOM   2263  C C   . ILE A  1 285 ? 2.462   53.804 49.303  1.00 41.95  ? 285  ILE A C   1 
ATOM   2264  O O   . ILE A  1 285 ? 2.318   52.706 49.844  1.00 42.98  ? 285  ILE A O   1 
ATOM   2265  C CB  . ILE A  1 285 ? 4.794   54.633 49.819  1.00 36.83  ? 285  ILE A CB  1 
ATOM   2266  C CG1 . ILE A  1 285 ? 5.564   55.951 49.701  1.00 35.31  ? 285  ILE A CG1 1 
ATOM   2267  C CG2 . ILE A  1 285 ? 5.092   53.769 48.600  1.00 36.23  ? 285  ILE A CG2 1 
ATOM   2268  C CD1 . ILE A  1 285 ? 7.028   55.837 50.069  1.00 33.16  ? 285  ILE A CD1 1 
ATOM   2269  N N   . ASN A  1 286 ? 1.945   54.112 48.116  1.00 42.87  ? 286  ASN A N   1 
ATOM   2270  C CA  . ASN A  1 286 ? 1.235   53.152 47.284  1.00 44.98  ? 286  ASN A CA  1 
ATOM   2271  C C   . ASN A  1 286 ? 1.689   53.319 45.838  1.00 43.47  ? 286  ASN A C   1 
ATOM   2272  O O   . ASN A  1 286 ? 1.127   54.119 45.086  1.00 44.56  ? 286  ASN A O   1 
ATOM   2273  C CB  . ASN A  1 286 ? -0.278  53.363 47.395  1.00 49.20  ? 286  ASN A CB  1 
ATOM   2274  C CG  . ASN A  1 286 ? -1.067  52.434 46.488  1.00 52.12  ? 286  ASN A CG  1 
ATOM   2275  O OD1 . ASN A  1 286 ? -0.681  51.285 46.271  1.00 51.83  ? 286  ASN A OD1 1 
ATOM   2276  N ND2 . ASN A  1 286 ? -2.183  52.928 45.956  1.00 55.50  ? 286  ASN A ND2 1 
ATOM   2277  N N   . SER A  1 287 ? 2.721   52.571 45.458  1.00 41.23  ? 287  SER A N   1 
ATOM   2278  C CA  . SER A  1 287 ? 3.212   52.603 44.087  1.00 39.83  ? 287  SER A CA  1 
ATOM   2279  C C   . SER A  1 287 ? 3.888   51.296 43.694  1.00 39.27  ? 287  SER A C   1 
ATOM   2280  O O   . SER A  1 287 ? 4.192   50.457 44.540  1.00 39.61  ? 287  SER A O   1 
ATOM   2281  C CB  . SER A  1 287 ? 4.178   53.778 43.891  1.00 37.02  ? 287  SER A CB  1 
ATOM   2282  O OG  . SER A  1 287 ? 5.476   53.482 44.374  1.00 34.67  ? 287  SER A OG  1 
ATOM   2283  N N   . SER A  1 288 ? 4.107   51.141 42.394  1.00 38.72  ? 288  SER A N   1 
ATOM   2284  C CA  . SER A  1 288 ? 4.826   49.996 41.849  1.00 38.40  ? 288  SER A CA  1 
ATOM   2285  C C   . SER A  1 288 ? 6.246   50.384 41.412  1.00 35.14  ? 288  SER A C   1 
ATOM   2286  O O   . SER A  1 288 ? 6.997   49.544 40.912  1.00 34.86  ? 288  SER A O   1 
ATOM   2287  C CB  . SER A  1 288 ? 4.036   49.402 40.679  1.00 40.75  ? 288  SER A CB  1 
ATOM   2288  O OG  . SER A  1 288 ? 3.430   50.426 39.903  1.00 40.83  ? 288  SER A OG  1 
ATOM   2289  N N   . MET A  1 289 ? 6.615   51.648 41.621  1.00 33.17  ? 289  MET A N   1 
ATOM   2290  C CA  . MET A  1 289 ? 7.952   52.141 41.275  1.00 30.64  ? 289  MET A CA  1 
ATOM   2291  C C   . MET A  1 289 ? 9.007   51.342 42.030  1.00 30.16  ? 289  MET A C   1 
ATOM   2292  O O   . MET A  1 289 ? 8.768   50.926 43.158  1.00 31.13  ? 289  MET A O   1 
ATOM   2293  C CB  . MET A  1 289 ? 8.115   53.610 41.675  1.00 29.58  ? 289  MET A CB  1 
ATOM   2294  C CG  . MET A  1 289 ? 7.152   54.591 41.032  1.00 30.47  ? 289  MET A CG  1 
ATOM   2295  S SD  . MET A  1 289 ? 7.452   54.796 39.275  1.00 29.72  ? 289  MET A SD  1 
ATOM   2296  C CE  . MET A  1 289 ? 6.889   56.489 39.067  1.00 30.54  ? 289  MET A CE  1 
ATOM   2297  N N   . PRO A  1 290 ? 10.182  51.128 41.419  1.00 28.99  ? 290  PRO A N   1 
ATOM   2298  C CA  . PRO A  1 290 ? 11.275  50.468 42.142  1.00 29.05  ? 290  PRO A CA  1 
ATOM   2299  C C   . PRO A  1 290 ? 11.972  51.364 43.171  1.00 27.98  ? 290  PRO A C   1 
ATOM   2300  O O   . PRO A  1 290 ? 12.709  50.854 44.013  1.00 28.53  ? 290  PRO A O   1 
ATOM   2301  C CB  . PRO A  1 290 ? 12.250  50.096 41.027  1.00 28.69  ? 290  PRO A CB  1 
ATOM   2302  C CG  . PRO A  1 290 ? 12.004  51.114 39.975  1.00 27.37  ? 290  PRO A CG  1 
ATOM   2303  C CD  . PRO A  1 290 ? 10.527  51.364 40.007  1.00 28.12  ? 290  PRO A CD  1 
ATOM   2304  N N   . PHE A  1 291 ? 11.746  52.677 43.091  1.00 26.93  ? 291  PHE A N   1 
ATOM   2305  C CA  . PHE A  1 291 ? 12.387  53.652 43.980  1.00 26.33  ? 291  PHE A CA  1 
ATOM   2306  C C   . PHE A  1 291 ? 11.410  54.678 44.520  1.00 26.42  ? 291  PHE A C   1 
ATOM   2307  O O   . PHE A  1 291 ? 10.347  54.899 43.944  1.00 26.88  ? 291  PHE A O   1 
ATOM   2308  C CB  . PHE A  1 291 ? 13.454  54.446 43.232  1.00 25.60  ? 291  PHE A CB  1 
ATOM   2309  C CG  . PHE A  1 291 ? 14.657  53.652 42.855  1.00 25.86  ? 291  PHE A CG  1 
ATOM   2310  C CD1 . PHE A  1 291 ? 15.634  53.375 43.795  1.00 26.65  ? 291  PHE A CD1 1 
ATOM   2311  C CD2 . PHE A  1 291 ? 14.828  53.203 41.554  1.00 25.72  ? 291  PHE A CD2 1 
ATOM   2312  C CE1 . PHE A  1 291 ? 16.761  52.653 43.450  1.00 27.55  ? 291  PHE A CE1 1 
ATOM   2313  C CE2 . PHE A  1 291 ? 15.952  52.480 41.201  1.00 26.42  ? 291  PHE A CE2 1 
ATOM   2314  C CZ  . PHE A  1 291 ? 16.918  52.207 42.153  1.00 27.49  ? 291  PHE A CZ  1 
ATOM   2315  N N   . HIS A  1 292 ? 11.810  55.323 45.614  1.00 26.33  ? 292  HIS A N   1 
ATOM   2316  C CA  . HIS A  1 292 ? 11.128  56.507 46.127  1.00 26.77  ? 292  HIS A CA  1 
ATOM   2317  C C   . HIS A  1 292 ? 12.144  57.446 46.769  1.00 26.70  ? 292  HIS A C   1 
ATOM   2318  O O   . HIS A  1 292 ? 13.296  57.065 46.986  1.00 26.41  ? 292  HIS A O   1 
ATOM   2319  C CB  . HIS A  1 292 ? 10.061  56.110 47.144  1.00 27.77  ? 292  HIS A CB  1 
ATOM   2320  C CG  . HIS A  1 292 ? 10.621  55.635 48.446  1.00 27.80  ? 292  HIS A CG  1 
ATOM   2321  N ND1 . HIS A  1 292 ? 10.512  56.360 49.611  1.00 28.35  ? 292  HIS A ND1 1 
ATOM   2322  C CD2 . HIS A  1 292 ? 11.310  54.515 48.763  1.00 27.70  ? 292  HIS A CD2 1 
ATOM   2323  C CE1 . HIS A  1 292 ? 11.100  55.703 50.593  1.00 28.38  ? 292  HIS A CE1 1 
ATOM   2324  N NE2 . HIS A  1 292 ? 11.594  54.580 50.106  1.00 28.10  ? 292  HIS A NE2 1 
ATOM   2325  N N   . ASN A  1 293 ? 11.720  58.669 47.070  1.00 27.52  ? 293  ASN A N   1 
ATOM   2326  C CA  . ASN A  1 293 ? 12.599  59.650 47.706  1.00 28.19  ? 293  ASN A CA  1 
ATOM   2327  C C   . ASN A  1 293 ? 11.937  60.372 48.883  1.00 29.55  ? 293  ASN A C   1 
ATOM   2328  O O   . ASN A  1 293 ? 12.287  61.511 49.203  1.00 30.87  ? 293  ASN A O   1 
ATOM   2329  C CB  . ASN A  1 293 ? 13.080  60.664 46.668  1.00 28.65  ? 293  ASN A CB  1 
ATOM   2330  C CG  . ASN A  1 293 ? 11.964  61.556 46.159  1.00 29.83  ? 293  ASN A CG  1 
ATOM   2331  O OD1 . ASN A  1 293 ? 10.789  61.200 46.222  1.00 30.04  ? 293  ASN A OD1 1 
ATOM   2332  N ND2 . ASN A  1 293 ? 12.328  62.728 45.660  1.00 31.18  ? 293  ASN A ND2 1 
ATOM   2333  N N   . ILE A  1 294 ? 11.006  59.688 49.543  1.00 29.60  ? 294  ILE A N   1 
ATOM   2334  C CA  . ILE A  1 294 ? 10.202  60.294 50.605  1.00 31.12  ? 294  ILE A CA  1 
ATOM   2335  C C   . ILE A  1 294 ? 10.988  60.386 51.915  1.00 31.32  ? 294  ILE A C   1 
ATOM   2336  O O   . ILE A  1 294 ? 11.197  61.480 52.440  1.00 32.76  ? 294  ILE A O   1 
ATOM   2337  C CB  . ILE A  1 294 ? 8.879   59.520 50.851  1.00 31.60  ? 294  ILE A CB  1 
ATOM   2338  C CG1 . ILE A  1 294 ? 8.093   59.314 49.547  1.00 31.80  ? 294  ILE A CG1 1 
ATOM   2339  C CG2 . ILE A  1 294 ? 8.008   60.255 51.860  1.00 33.60  ? 294  ILE A CG2 1 
ATOM   2340  C CD1 . ILE A  1 294 ? 7.854   60.572 48.737  1.00 33.02  ? 294  ILE A CD1 1 
ATOM   2341  N N   . HIS A  1 295 ? 11.418  59.238 52.435  1.00 30.33  ? 295  HIS A N   1 
ATOM   2342  C CA  . HIS A  1 295 ? 12.089  59.176 53.735  1.00 30.70  ? 295  HIS A CA  1 
ATOM   2343  C C   . HIS A  1 295 ? 12.798  57.821 53.901  1.00 29.86  ? 295  HIS A C   1 
ATOM   2344  O O   . HIS A  1 295 ? 12.207  56.782 53.599  1.00 29.41  ? 295  HIS A O   1 
ATOM   2345  C CB  . HIS A  1 295 ? 11.050  59.367 54.844  1.00 31.76  ? 295  HIS A CB  1 
ATOM   2346  C CG  . HIS A  1 295 ? 11.634  59.726 56.174  1.00 32.55  ? 295  HIS A CG  1 
ATOM   2347  N ND1 . HIS A  1 295 ? 12.275  58.807 56.973  1.00 32.16  ? 295  HIS A ND1 1 
ATOM   2348  C CD2 . HIS A  1 295 ? 11.650  60.894 56.858  1.00 34.10  ? 295  HIS A CD2 1 
ATOM   2349  C CE1 . HIS A  1 295 ? 12.675  59.394 58.086  1.00 33.21  ? 295  HIS A CE1 1 
ATOM   2350  N NE2 . HIS A  1 295 ? 12.307  60.661 58.042  1.00 34.40  ? 295  HIS A NE2 1 
ATOM   2351  N N   . PRO A  1 296 ? 14.059  57.823 54.387  1.00 30.22  ? 296  PRO A N   1 
ATOM   2352  C CA  . PRO A  1 296 ? 14.850  56.583 54.486  1.00 30.12  ? 296  PRO A CA  1 
ATOM   2353  C C   . PRO A  1 296 ? 14.245  55.497 55.378  1.00 30.34  ? 296  PRO A C   1 
ATOM   2354  O O   . PRO A  1 296 ? 14.240  54.325 55.007  1.00 30.34  ? 296  PRO A O   1 
ATOM   2355  C CB  . PRO A  1 296 ? 16.188  57.060 55.075  1.00 31.32  ? 296  PRO A CB  1 
ATOM   2356  C CG  . PRO A  1 296 ? 15.896  58.373 55.708  1.00 32.07  ? 296  PRO A CG  1 
ATOM   2357  C CD  . PRO A  1 296 ? 14.824  58.991 54.864  1.00 31.41  ? 296  PRO A CD  1 
ATOM   2358  N N   . LEU A  1 297 ? 13.762  55.888 56.549  1.00 30.91  ? 297  LEU A N   1 
ATOM   2359  C CA  . LEU A  1 297 ? 13.175  54.948 57.507  1.00 31.47  ? 297  LEU A CA  1 
ATOM   2360  C C   . LEU A  1 297 ? 11.740  54.565 57.140  1.00 31.40  ? 297  LEU A C   1 
ATOM   2361  O O   . LEU A  1 297 ? 10.801  55.319 57.400  1.00 31.72  ? 297  LEU A O   1 
ATOM   2362  C CB  . LEU A  1 297 ? 13.213  55.543 58.920  1.00 32.27  ? 297  LEU A CB  1 
ATOM   2363  C CG  . LEU A  1 297 ? 14.594  55.974 59.426  1.00 33.04  ? 297  LEU A CG  1 
ATOM   2364  C CD1 . LEU A  1 297 ? 14.472  56.786 60.708  1.00 33.93  ? 297  LEU A CD1 1 
ATOM   2365  C CD2 . LEU A  1 297 ? 15.494  54.763 59.636  1.00 33.82  ? 297  LEU A CD2 1 
ATOM   2366  N N   . THR A  1 298 ? 11.580  53.390 56.538  1.00 31.55  ? 298  THR A N   1 
ATOM   2367  C CA  . THR A  1 298 ? 10.260  52.877 56.186  1.00 32.17  ? 298  THR A CA  1 
ATOM   2368  C C   . THR A  1 298 ? 10.035  51.511 56.813  1.00 33.70  ? 298  THR A C   1 
ATOM   2369  O O   . THR A  1 298 ? 10.971  50.868 57.290  1.00 34.12  ? 298  THR A O   1 
ATOM   2370  C CB  . THR A  1 298 ? 10.065  52.756 54.657  1.00 31.61  ? 298  THR A CB  1 
ATOM   2371  O OG1 . THR A  1 298 ? 10.750  51.597 54.159  1.00 31.90  ? 298  THR A OG1 1 
ATOM   2372  C CG2 . THR A  1 298 ? 10.572  53.999 53.945  1.00 30.33  ? 298  THR A CG2 1 
ATOM   2373  N N   . ILE A  1 299 ? 8.777   51.086 56.801  1.00 35.05  ? 299  ILE A N   1 
ATOM   2374  C CA  . ILE A  1 299 ? 8.380   49.781 57.313  1.00 37.24  ? 299  ILE A CA  1 
ATOM   2375  C C   . ILE A  1 299 ? 7.438   49.157 56.287  1.00 38.65  ? 299  ILE A C   1 
ATOM   2376  O O   . ILE A  1 299 ? 6.582   49.846 55.725  1.00 38.51  ? 299  ILE A O   1 
ATOM   2377  C CB  . ILE A  1 299 ? 7.731   49.893 58.726  1.00 38.41  ? 299  ILE A CB  1 
ATOM   2378  C CG1 . ILE A  1 299 ? 7.171   48.545 59.221  1.00 41.18  ? 299  ILE A CG1 1 
ATOM   2379  C CG2 . ILE A  1 299 ? 6.630   50.945 58.751  1.00 38.46  ? 299  ILE A CG2 1 
ATOM   2380  C CD1 . ILE A  1 299 ? 8.225   47.556 59.677  1.00 42.03  ? 299  ILE A CD1 1 
ATOM   2381  N N   . GLY A  1 300 ? 7.623   47.862 56.032  1.00 40.48  ? 300  GLY A N   1 
ATOM   2382  C CA  . GLY A  1 300 ? 6.760   47.106 55.130  1.00 42.60  ? 300  GLY A CA  1 
ATOM   2383  C C   . GLY A  1 300 ? 7.391   46.832 53.779  1.00 41.90  ? 300  GLY A C   1 
ATOM   2384  O O   . GLY A  1 300 ? 8.607   46.952 53.613  1.00 40.33  ? 300  GLY A O   1 
ATOM   2385  N N   . GLU A  1 301 ? 6.548   46.462 52.817  1.00 43.51  ? 301  GLU A N   1 
ATOM   2386  C CA  . GLU A  1 301 ? 6.974   46.169 51.445  1.00 43.15  ? 301  GLU A CA  1 
ATOM   2387  C C   . GLU A  1 301 ? 7.130   47.475 50.676  1.00 40.13  ? 301  GLU A C   1 
ATOM   2388  O O   . GLU A  1 301 ? 6.154   48.012 50.145  1.00 40.39  ? 301  GLU A O   1 
ATOM   2389  C CB  . GLU A  1 301 ? 5.942   45.273 50.749  1.00 46.46  ? 301  GLU A CB  1 
ATOM   2390  C CG  . GLU A  1 301 ? 6.311   44.842 49.333  1.00 46.55  ? 301  GLU A CG  1 
ATOM   2391  C CD  . GLU A  1 301 ? 7.359   43.737 49.290  1.00 47.93  ? 301  GLU A CD  1 
ATOM   2392  O OE1 . GLU A  1 301 ? 7.846   43.311 50.368  1.00 48.86  ? 301  GLU A OE1 1 
ATOM   2393  O OE2 . GLU A  1 301 ? 7.690   43.290 48.165  1.00 48.42  ? 301  GLU A OE2 1 
ATOM   2394  N N   . CYS A  1 302 ? 8.362   47.976 50.615  1.00 37.80  ? 302  CYS A N   1 
ATOM   2395  C CA  . CYS A  1 302 ? 8.627   49.300 50.065  1.00 35.28  ? 302  CYS A CA  1 
ATOM   2396  C C   . CYS A  1 302 ? 9.631   49.291 48.915  1.00 33.88  ? 302  CYS A C   1 
ATOM   2397  O O   . CYS A  1 302 ? 10.492  48.411 48.838  1.00 34.55  ? 302  CYS A O   1 
ATOM   2398  C CB  . CYS A  1 302 ? 9.156   50.216 51.166  1.00 34.07  ? 302  CYS A CB  1 
ATOM   2399  S SG  . CYS A  1 302 ? 7.963   50.543 52.479  1.00 35.50  ? 302  CYS A SG  1 
ATOM   2400  N N   . PRO A  1 303 ? 9.528   50.287 48.019  1.00 32.27  ? 303  PRO A N   1 
ATOM   2401  C CA  . PRO A  1 303 ? 10.607  50.520 47.065  1.00 30.80  ? 303  PRO A CA  1 
ATOM   2402  C C   . PRO A  1 303 ? 11.844  51.048 47.790  1.00 29.80  ? 303  PRO A C   1 
ATOM   2403  O O   . PRO A  1 303 ? 11.750  51.429 48.958  1.00 29.96  ? 303  PRO A O   1 
ATOM   2404  C CB  . PRO A  1 303 ? 10.028  51.577 46.118  1.00 29.83  ? 303  PRO A CB  1 
ATOM   2405  C CG  . PRO A  1 303 ? 8.935   52.240 46.880  1.00 30.52  ? 303  PRO A CG  1 
ATOM   2406  C CD  . PRO A  1 303 ? 8.395   51.212 47.825  1.00 32.31  ? 303  PRO A CD  1 
ATOM   2407  N N   . LYS A  1 304 ? 12.986  51.076 47.111  1.00 29.11  ? 304  LYS A N   1 
ATOM   2408  C CA  . LYS A  1 304 ? 14.229  51.503 47.749  1.00 28.89  ? 304  LYS A CA  1 
ATOM   2409  C C   . LYS A  1 304 ? 14.309  53.017 47.805  1.00 27.54  ? 304  LYS A C   1 
ATOM   2410  O O   . LYS A  1 304 ? 13.905  53.711 46.870  1.00 26.69  ? 304  LYS A O   1 
ATOM   2411  C CB  . LYS A  1 304 ? 15.454  50.954 47.013  1.00 29.57  ? 304  LYS A CB  1 
ATOM   2412  C CG  . LYS A  1 304 ? 15.431  49.447 46.798  1.00 31.45  ? 304  LYS A CG  1 
ATOM   2413  C CD  . LYS A  1 304 ? 15.541  48.671 48.107  1.00 33.35  ? 304  LYS A CD  1 
ATOM   2414  C CE  . LYS A  1 304 ? 14.516  47.547 48.187  1.00 35.02  ? 304  LYS A CE  1 
ATOM   2415  N NZ  . LYS A  1 304 ? 14.878  46.543 49.230  1.00 37.60  ? 304  LYS A NZ  1 
ATOM   2416  N N   . TYR A  1 305 ? 14.834  53.525 48.912  1.00 27.67  ? 305  TYR A N   1 
ATOM   2417  C CA  . TYR A  1 305 ? 14.983  54.954 49.085  1.00 27.15  ? 305  TYR A CA  1 
ATOM   2418  C C   . TYR A  1 305 ? 16.241  55.449 48.390  1.00 27.23  ? 305  TYR A C   1 
ATOM   2419  O O   . TYR A  1 305 ? 17.311  54.848 48.509  1.00 28.11  ? 305  TYR A O   1 
ATOM   2420  C CB  . TYR A  1 305 ? 15.050  55.321 50.562  1.00 27.80  ? 305  TYR A CB  1 
ATOM   2421  C CG  . TYR A  1 305 ? 15.262  56.795 50.776  1.00 28.04  ? 305  TYR A CG  1 
ATOM   2422  C CD1 . TYR A  1 305 ? 14.220  57.695 50.602  1.00 27.92  ? 305  TYR A CD1 1 
ATOM   2423  C CD2 . TYR A  1 305 ? 16.509  57.293 51.129  1.00 29.04  ? 305  TYR A CD2 1 
ATOM   2424  C CE1 . TYR A  1 305 ? 14.412  59.053 50.788  1.00 28.83  ? 305  TYR A CE1 1 
ATOM   2425  C CE2 . TYR A  1 305 ? 16.712  58.650 51.318  1.00 29.94  ? 305  TYR A CE2 1 
ATOM   2426  C CZ  . TYR A  1 305 ? 15.658  59.524 51.147  1.00 29.83  ? 305  TYR A CZ  1 
ATOM   2427  O OH  . TYR A  1 305 ? 15.840  60.872 51.333  1.00 31.33  ? 305  TYR A OH  1 
ATOM   2428  N N   . VAL A  1 306 ? 16.097  56.547 47.656  1.00 26.74  ? 306  VAL A N   1 
ATOM   2429  C CA  . VAL A  1 306 ? 17.240  57.282 47.130  1.00 27.33  ? 306  VAL A CA  1 
ATOM   2430  C C   . VAL A  1 306 ? 17.004  58.767 47.354  1.00 27.94  ? 306  VAL A C   1 
ATOM   2431  O O   . VAL A  1 306 ? 15.863  59.198 47.523  1.00 27.65  ? 306  VAL A O   1 
ATOM   2432  C CB  . VAL A  1 306 ? 17.489  56.996 45.631  1.00 26.71  ? 306  VAL A CB  1 
ATOM   2433  C CG1 . VAL A  1 306 ? 17.960  55.564 45.435  1.00 26.87  ? 306  VAL A CG1 1 
ATOM   2434  C CG2 . VAL A  1 306 ? 16.245  57.274 44.795  1.00 25.62  ? 306  VAL A CG2 1 
ATOM   2435  N N   . LYS A  1 307 ? 18.085  59.539 47.355  1.00 29.36  ? 307  LYS A N   1 
ATOM   2436  C CA  . LYS A  1 307 ? 18.009  60.987 47.539  1.00 30.79  ? 307  LYS A CA  1 
ATOM   2437  C C   . LYS A  1 307 ? 17.675  61.762 46.256  1.00 30.76  ? 307  LYS A C   1 
ATOM   2438  O O   . LYS A  1 307 ? 17.577  62.986 46.284  1.00 32.50  ? 307  LYS A O   1 
ATOM   2439  C CB  . LYS A  1 307 ? 19.334  61.517 48.093  1.00 33.18  ? 307  LYS A CB  1 
ATOM   2440  C CG  . LYS A  1 307 ? 19.599  61.172 49.543  1.00 33.95  ? 307  LYS A CG  1 
ATOM   2441  C CD  . LYS A  1 307 ? 20.766  61.997 50.059  1.00 37.03  ? 307  LYS A CD  1 
ATOM   2442  C CE  . LYS A  1 307 ? 21.339  61.436 51.349  1.00 38.10  ? 307  LYS A CE  1 
ATOM   2443  N NZ  . LYS A  1 307 ? 22.535  62.212 51.789  1.00 41.67  ? 307  LYS A NZ  1 
ATOM   2444  N N   . SER A  1 308 ? 17.504  61.065 45.137  1.00 29.17  ? 308  SER A N   1 
ATOM   2445  C CA  . SER A  1 308 ? 17.286  61.722 43.854  1.00 29.18  ? 308  SER A CA  1 
ATOM   2446  C C   . SER A  1 308 ? 15.973  62.501 43.819  1.00 29.50  ? 308  SER A C   1 
ATOM   2447  O O   . SER A  1 308 ? 14.999  62.132 44.479  1.00 28.93  ? 308  SER A O   1 
ATOM   2448  C CB  . SER A  1 308 ? 17.287  60.693 42.721  1.00 27.45  ? 308  SER A CB  1 
ATOM   2449  O OG  . SER A  1 308 ? 18.333  59.757 42.884  1.00 27.40  ? 308  SER A OG  1 
ATOM   2450  N N   . ASN A  1 309 ? 15.974  63.588 43.052  1.00 30.91  ? 309  ASN A N   1 
ATOM   2451  C CA  . ASN A  1 309 ? 14.753  64.294 42.686  1.00 31.71  ? 309  ASN A CA  1 
ATOM   2452  C C   . ASN A  1 309 ? 14.135  63.688 41.436  1.00 30.12  ? 309  ASN A C   1 
ATOM   2453  O O   . ASN A  1 309 ? 12.933  63.832 41.204  1.00 30.53  ? 309  ASN A O   1 
ATOM   2454  C CB  . ASN A  1 309 ? 15.044  65.770 42.425  1.00 34.70  ? 309  ASN A CB  1 
ATOM   2455  C CG  . ASN A  1 309 ? 15.446  66.517 43.683  1.00 37.02  ? 309  ASN A CG  1 
ATOM   2456  O OD1 . ASN A  1 309 ? 14.786  66.408 44.723  1.00 37.04  ? 309  ASN A OD1 1 
ATOM   2457  N ND2 . ASN A  1 309 ? 16.526  67.293 43.596  1.00 39.32  ? 309  ASN A ND2 1 
ATOM   2458  N N   . ARG A  1 310 ? 14.957  63.005 40.638  1.00 28.67  ? 310  ARG A N   1 
ATOM   2459  C CA  . ARG A  1 310 ? 14.537  62.543 39.320  1.00 27.46  ? 310  ARG A CA  1 
ATOM   2460  C C   . ARG A  1 310 ? 15.295  61.295 38.842  1.00 25.58  ? 310  ARG A C   1 
ATOM   2461  O O   . ARG A  1 310 ? 16.527  61.286 38.807  1.00 25.87  ? 310  ARG A O   1 
ATOM   2462  C CB  . ARG A  1 310 ? 14.744  63.679 38.319  1.00 29.06  ? 310  ARG A CB  1 
ATOM   2463  C CG  . ARG A  1 310 ? 13.877  63.586 37.079  1.00 28.68  ? 310  ARG A CG  1 
ATOM   2464  C CD  . ARG A  1 310 ? 14.248  64.662 36.071  1.00 30.40  ? 310  ARG A CD  1 
ATOM   2465  N NE  . ARG A  1 310 ? 14.164  64.148 34.707  1.00 29.16  ? 310  ARG A NE  1 
ATOM   2466  C CZ  . ARG A  1 310 ? 13.040  64.019 34.006  1.00 29.16  ? 310  ARG A CZ  1 
ATOM   2467  N NH1 . ARG A  1 310 ? 11.861  64.370 34.518  1.00 30.59  ? 310  ARG A NH1 1 
ATOM   2468  N NH2 . ARG A  1 310 ? 13.098  63.534 32.772  1.00 28.09  ? 310  ARG A NH2 1 
ATOM   2469  N N   . LEU A  1 311 ? 14.546  60.249 38.486  1.00 24.16  ? 311  LEU A N   1 
ATOM   2470  C CA  . LEU A  1 311 ? 15.097  59.063 37.816  1.00 22.90  ? 311  LEU A CA  1 
ATOM   2471  C C   . LEU A  1 311 ? 14.163  58.606 36.696  1.00 22.24  ? 311  LEU A C   1 
ATOM   2472  O O   . LEU A  1 311 ? 13.118  58.003 36.956  1.00 22.23  ? 311  LEU A O   1 
ATOM   2473  C CB  . LEU A  1 311 ? 15.307  57.911 38.799  1.00 22.52  ? 311  LEU A CB  1 
ATOM   2474  C CG  . LEU A  1 311 ? 16.372  58.075 39.880  1.00 23.27  ? 311  LEU A CG  1 
ATOM   2475  C CD1 . LEU A  1 311 ? 16.347  56.861 40.791  1.00 23.15  ? 311  LEU A CD1 1 
ATOM   2476  C CD2 . LEU A  1 311 ? 17.759  58.259 39.289  1.00 23.95  ? 311  LEU A CD2 1 
ATOM   2477  N N   . VAL A  1 312 ? 14.549  58.899 35.457  1.00 22.00  ? 312  VAL A N   1 
ATOM   2478  C CA  . VAL A  1 312 ? 13.748  58.569 34.284  1.00 21.60  ? 312  VAL A CA  1 
ATOM   2479  C C   . VAL A  1 312 ? 14.600  57.819 33.270  1.00 20.76  ? 312  VAL A C   1 
ATOM   2480  O O   . VAL A  1 312 ? 15.645  58.306 32.854  1.00 20.90  ? 312  VAL A O   1 
ATOM   2481  C CB  . VAL A  1 312 ? 13.196  59.841 33.614  1.00 22.65  ? 312  VAL A CB  1 
ATOM   2482  C CG1 . VAL A  1 312 ? 12.285  59.487 32.444  1.00 22.63  ? 312  VAL A CG1 1 
ATOM   2483  C CG2 . VAL A  1 312 ? 12.451  60.693 34.632  1.00 24.04  ? 312  VAL A CG2 1 
ATOM   2484  N N   . LEU A  1 313 ? 14.142  56.634 32.881  1.00 20.31  ? 313  LEU A N   1 
ATOM   2485  C CA  . LEU A  1 313 ? 14.821  55.821 31.880  1.00 19.92  ? 313  LEU A CA  1 
ATOM   2486  C C   . LEU A  1 313 ? 14.237  56.054 30.498  1.00 19.77  ? 313  LEU A C   1 
ATOM   2487  O O   . LEU A  1 313 ? 13.021  56.025 30.325  1.00 20.18  ? 313  LEU A O   1 
ATOM   2488  C CB  . LEU A  1 313 ? 14.688  54.337 32.213  1.00 20.20  ? 313  LEU A CB  1 
ATOM   2489  C CG  . LEU A  1 313 ? 15.606  53.809 33.307  1.00 20.64  ? 313  LEU A CG  1 
ATOM   2490  C CD1 . LEU A  1 313 ? 15.170  52.411 33.714  1.00 21.53  ? 313  LEU A CD1 1 
ATOM   2491  C CD2 . LEU A  1 313 ? 17.054  53.810 32.844  1.00 20.94  ? 313  LEU A CD2 1 
ATOM   2492  N N   . ALA A  1 314 ? 15.106  56.276 29.515  1.00 19.50  ? 314  ALA A N   1 
ATOM   2493  C CA  . ALA A  1 314 ? 14.689  56.287 28.121  1.00 19.37  ? 314  ALA A CA  1 
ATOM   2494  C C   . ALA A  1 314 ? 14.307  54.875 27.740  1.00 19.49  ? 314  ALA A C   1 
ATOM   2495  O O   . ALA A  1 314 ? 15.064  53.935 27.992  1.00 19.65  ? 314  ALA A O   1 
ATOM   2496  C CB  . ALA A  1 314 ? 15.806  56.780 27.221  1.00 19.25  ? 314  ALA A CB  1 
ATOM   2497  N N   . THR A  1 315 ? 13.117  54.731 27.170  1.00 20.00  ? 315  THR A N   1 
ATOM   2498  C CA  . THR A  1 315 ? 12.698  53.486 26.545  1.00 20.72  ? 315  THR A CA  1 
ATOM   2499  C C   . THR A  1 315 ? 12.658  53.663 25.029  1.00 20.66  ? 315  THR A C   1 
ATOM   2500  O O   . THR A  1 315 ? 13.111  52.801 24.287  1.00 20.84  ? 315  THR A O   1 
ATOM   2501  C CB  . THR A  1 315 ? 11.326  53.020 27.064  1.00 22.07  ? 315  THR A CB  1 
ATOM   2502  O OG1 . THR A  1 315 ? 10.426  54.132 27.131  1.00 22.48  ? 315  THR A OG1 1 
ATOM   2503  C CG2 . THR A  1 315 ? 11.467  52.410 28.451  1.00 22.41  ? 315  THR A CG2 1 
ATOM   2504  N N   . GLY A  1 316 ? 12.129  54.791 24.577  1.00 20.71  ? 316  GLY A N   1 
ATOM   2505  C CA  . GLY A  1 316 ? 12.086  55.101 23.161  1.00 20.77  ? 316  GLY A CA  1 
ATOM   2506  C C   . GLY A  1 316 ? 13.370  55.742 22.683  1.00 19.86  ? 316  GLY A C   1 
ATOM   2507  O O   . GLY A  1 316 ? 14.410  55.634 23.327  1.00 19.36  ? 316  GLY A O   1 
ATOM   2508  N N   . LEU A  1 317 ? 13.281  56.431 21.554  1.00 20.08  ? 317  LEU A N   1 
ATOM   2509  C CA  . LEU A  1 317 ? 14.450  56.985 20.885  1.00 19.71  ? 317  LEU A CA  1 
ATOM   2510  C C   . LEU A  1 317 ? 14.362  58.503 20.847  1.00 20.53  ? 317  LEU A C   1 
ATOM   2511  O O   . LEU A  1 317 ? 13.346  59.083 21.225  1.00 21.43  ? 317  LEU A O   1 
ATOM   2512  C CB  . LEU A  1 317 ? 14.595  56.392 19.472  1.00 19.55  ? 317  LEU A CB  1 
ATOM   2513  C CG  . LEU A  1 317 ? 13.377  56.350 18.540  1.00 20.24  ? 317  LEU A CG  1 
ATOM   2514  C CD1 . LEU A  1 317 ? 13.236  57.661 17.790  1.00 20.77  ? 317  LEU A CD1 1 
ATOM   2515  C CD2 . LEU A  1 317 ? 13.453  55.189 17.558  1.00 20.27  ? 317  LEU A CD2 1 
ATOM   2516  N N   . ARG A  1 318 ? 15.440  59.140 20.404  1.00 20.79  ? 318  ARG A N   1 
ATOM   2517  C CA  . ARG A  1 318 ? 15.505  60.587 20.353  1.00 22.24  ? 318  ARG A CA  1 
ATOM   2518  C C   . ARG A  1 318 ? 14.377  61.125 19.484  1.00 23.45  ? 318  ARG A C   1 
ATOM   2519  O O   . ARG A  1 318 ? 14.264  60.780 18.310  1.00 23.18  ? 318  ARG A O   1 
ATOM   2520  C CB  . ARG A  1 318 ? 16.860  61.035 19.813  1.00 22.65  ? 318  ARG A CB  1 
ATOM   2521  C CG  . ARG A  1 318 ? 17.045  62.541 19.753  1.00 24.66  ? 318  ARG A CG  1 
ATOM   2522  C CD  . ARG A  1 318 ? 18.402  62.890 19.172  1.00 25.54  ? 318  ARG A CD  1 
ATOM   2523  N NE  . ARG A  1 318 ? 19.479  62.630 20.123  1.00 25.75  ? 318  ARG A NE  1 
ATOM   2524  C CZ  . ARG A  1 318 ? 20.043  63.544 20.907  1.00 27.69  ? 318  ARG A CZ  1 
ATOM   2525  N NH1 . ARG A  1 318 ? 19.648  64.815 20.875  1.00 29.72  ? 318  ARG A NH1 1 
ATOM   2526  N NH2 . ARG A  1 318 ? 21.015  63.182 21.736  1.00 28.08  ? 318  ARG A NH2 1 
ATOM   2527  N N   . ASN A  1 319 ? 13.542  61.971 20.076  1.00 25.26  ? 319  ASN A N   1 
ATOM   2528  C CA  . ASN A  1 319 ? 12.381  62.513 19.396  1.00 27.22  ? 319  ASN A CA  1 
ATOM   2529  C C   . ASN A  1 319 ? 12.735  63.794 18.652  1.00 29.41  ? 319  ASN A C   1 
ATOM   2530  O O   . ASN A  1 319 ? 13.550  64.591 19.117  1.00 30.34  ? 319  ASN A O   1 
ATOM   2531  C CB  . ASN A  1 319 ? 11.266  62.768 20.401  1.00 28.60  ? 319  ASN A CB  1 
ATOM   2532  C CG  . ASN A  1 319 ? 9.932   63.011 19.742  1.00 30.73  ? 319  ASN A CG  1 
ATOM   2533  O OD1 . ASN A  1 319 ? 9.790   62.883 18.531  1.00 30.89  ? 319  ASN A OD1 1 
ATOM   2534  N ND2 . ASN A  1 319 ? 8.940   63.367 20.541  1.00 32.72  ? 319  ASN A ND2 1 
ATOM   2535  N N   . SER A  1 320 ? 12.093  63.994 17.506  1.00 30.89  ? 320  SER A N   1 
ATOM   2536  C CA  . SER A  1 320 ? 12.482  65.035 16.555  1.00 32.99  ? 320  SER A CA  1 
ATOM   2537  C C   . SER A  1 320 ? 11.745  66.368 16.774  1.00 36.93  ? 320  SER A C   1 
ATOM   2538  O O   . SER A  1 320 ? 10.579  66.373 17.173  1.00 38.33  ? 320  SER A O   1 
ATOM   2539  C CB  . SER A  1 320 ? 12.230  64.536 15.128  1.00 32.48  ? 320  SER A CB  1 
ATOM   2540  O OG  . SER A  1 320 ? 12.806  63.250 14.944  1.00 29.66  ? 320  SER A OG  1 
ATOM   2541  N N   . PRO A  1 321 ? 12.430  67.504 16.516  1.00 39.36  ? 321  PRO A N   1 
ATOM   2542  C CA  . PRO A  1 321 ? 11.802  68.829 16.571  1.00 43.75  ? 321  PRO A CA  1 
ATOM   2543  C C   . PRO A  1 321 ? 11.095  69.195 15.270  1.00 45.96  ? 321  PRO A C   1 
ATOM   2544  O O   . PRO A  1 321 ? 10.097  68.571 14.916  1.00 45.78  ? 321  PRO A O   1 
ATOM   2545  C CB  . PRO A  1 321 ? 12.993  69.764 16.799  1.00 45.40  ? 321  PRO A CB  1 
ATOM   2546  C CG  . PRO A  1 321 ? 14.129  69.080 16.113  1.00 42.58  ? 321  PRO A CG  1 
ATOM   2547  C CD  . PRO A  1 321 ? 13.889  67.603 16.292  1.00 38.57  ? 321  PRO A CD  1 
ATOM   2548  N N   . GLY B  2 1   ? 24.397  60.927 17.229  1.00 17.24  ? 1    GLY B N   1 
ATOM   2549  C CA  . GLY B  2 1   ? 24.522  59.567 17.824  1.00 15.52  ? 1    GLY B CA  1 
ATOM   2550  C C   . GLY B  2 1   ? 25.679  58.791 17.237  1.00 15.88  ? 1    GLY B C   1 
ATOM   2551  O O   . GLY B  2 1   ? 26.146  59.096 16.144  1.00 17.08  ? 1    GLY B O   1 
ATOM   2552  N N   . LEU B  2 2   ? 26.122  57.770 17.960  1.00 15.19  ? 2    LEU B N   1 
ATOM   2553  C CA  . LEU B  2 2   ? 27.321  57.021 17.598  1.00 16.13  ? 2    LEU B CA  1 
ATOM   2554  C C   . LEU B  2 2   ? 27.280  56.400 16.209  1.00 16.39  ? 2    LEU B C   1 
ATOM   2555  O O   . LEU B  2 2   ? 28.312  56.291 15.552  1.00 18.03  ? 2    LEU B O   1 
ATOM   2556  C CB  . LEU B  2 2   ? 27.592  55.922 18.629  1.00 15.52  ? 2    LEU B CB  1 
ATOM   2557  C CG  . LEU B  2 2   ? 28.246  56.359 19.936  1.00 15.95  ? 2    LEU B CG  1 
ATOM   2558  C CD1 . LEU B  2 2   ? 28.340  55.176 20.879  1.00 15.37  ? 2    LEU B CD1 1 
ATOM   2559  C CD2 . LEU B  2 2   ? 29.620  56.958 19.692  1.00 18.20  ? 2    LEU B CD2 1 
ATOM   2560  N N   . PHE B  2 3   ? 26.095  55.995 15.767  1.00 15.07  ? 3    PHE B N   1 
ATOM   2561  C CA  . PHE B  2 3   ? 25.965  55.214 14.538  1.00 15.22  ? 3    PHE B CA  1 
ATOM   2562  C C   . PHE B  2 3   ? 25.538  56.044 13.333  1.00 15.62  ? 3    PHE B C   1 
ATOM   2563  O O   . PHE B  2 3   ? 25.459  55.531 12.225  1.00 15.86  ? 3    PHE B O   1 
ATOM   2564  C CB  . PHE B  2 3   ? 25.062  54.005 14.798  1.00 14.01  ? 3    PHE B CB  1 
ATOM   2565  C CG  . PHE B  2 3   ? 25.643  53.074 15.818  1.00 14.22  ? 3    PHE B CG  1 
ATOM   2566  C CD1 . PHE B  2 3   ? 26.567  52.106 15.446  1.00 15.59  ? 3    PHE B CD1 1 
ATOM   2567  C CD2 . PHE B  2 3   ? 25.347  53.226 17.163  1.00 13.44  ? 3    PHE B CD2 1 
ATOM   2568  C CE1 . PHE B  2 3   ? 27.144  51.279 16.389  1.00 16.24  ? 3    PHE B CE1 1 
ATOM   2569  C CE2 . PHE B  2 3   ? 25.925  52.403 18.112  1.00 13.84  ? 3    PHE B CE2 1 
ATOM   2570  C CZ  . PHE B  2 3   ? 26.825  51.430 17.725  1.00 15.29  ? 3    PHE B CZ  1 
ATOM   2571  N N   . GLY B  2 4   ? 25.290  57.331 13.562  1.00 16.01  ? 4    GLY B N   1 
ATOM   2572  C CA  . GLY B  2 4   ? 25.171  58.314 12.492  1.00 17.19  ? 4    GLY B CA  1 
ATOM   2573  C C   . GLY B  2 4   ? 23.867  58.338 11.722  1.00 16.43  ? 4    GLY B C   1 
ATOM   2574  O O   . GLY B  2 4   ? 23.735  59.115 10.782  1.00 17.52  ? 4    GLY B O   1 
ATOM   2575  N N   . ALA B  2 5   ? 22.903  57.506 12.114  1.00 14.95  ? 5    ALA B N   1 
ATOM   2576  C CA  . ALA B  2 5   ? 21.645  57.382 11.387  1.00 14.48  ? 5    ALA B CA  1 
ATOM   2577  C C   . ALA B  2 5   ? 20.606  58.352 11.931  1.00 14.75  ? 5    ALA B C   1 
ATOM   2578  O O   . ALA B  2 5   ? 20.164  59.251 11.224  1.00 15.76  ? 5    ALA B O   1 
ATOM   2579  C CB  . ALA B  2 5   ? 21.135  55.954 11.456  1.00 13.41  ? 5    ALA B CB  1 
ATOM   2580  N N   . ILE B  2 6   ? 20.235  58.173 13.194  1.00 14.20  ? 6    ILE B N   1 
ATOM   2581  C CA  . ILE B  2 6   ? 19.243  59.027 13.841  1.00 14.86  ? 6    ILE B CA  1 
ATOM   2582  C C   . ILE B  2 6   ? 19.792  60.437 14.004  1.00 16.48  ? 6    ILE B C   1 
ATOM   2583  O O   . ILE B  2 6   ? 20.872  60.623 14.551  1.00 16.69  ? 6    ILE B O   1 
ATOM   2584  C CB  . ILE B  2 6   ? 18.822  58.461 15.213  1.00 14.09  ? 6    ILE B CB  1 
ATOM   2585  C CG1 . ILE B  2 6   ? 18.022  57.172 15.012  1.00 13.32  ? 6    ILE B CG1 1 
ATOM   2586  C CG2 . ILE B  2 6   ? 17.998  59.477 15.991  1.00 15.21  ? 6    ILE B CG2 1 
ATOM   2587  C CD1 . ILE B  2 6   ? 17.611  56.472 16.289  1.00 12.93  ? 6    ILE B CD1 1 
ATOM   2588  N N   . ALA B  2 7   ? 19.041  61.423 13.522  1.00 18.05  ? 7    ALA B N   1 
ATOM   2589  C CA  . ALA B  2 7   ? 19.475  62.814 13.538  1.00 20.31  ? 7    ALA B CA  1 
ATOM   2590  C C   . ALA B  2 7   ? 20.825  62.976 12.853  1.00 21.01  ? 7    ALA B C   1 
ATOM   2591  O O   . ALA B  2 7   ? 21.611  63.840 13.221  1.00 22.67  ? 7    ALA B O   1 
ATOM   2592  C CB  . ALA B  2 7   ? 19.540  63.333 14.968  1.00 20.84  ? 7    ALA B CB  1 
ATOM   2593  N N   . GLY B  2 8   ? 21.081  62.143 11.851  1.00 20.16  ? 8    GLY B N   1 
ATOM   2594  C CA  . GLY B  2 8   ? 22.370  62.111 11.179  1.00 21.04  ? 8    GLY B CA  1 
ATOM   2595  C C   . GLY B  2 8   ? 22.173  62.220 9.688   1.00 21.89  ? 8    GLY B C   1 
ATOM   2596  O O   . GLY B  2 8   ? 21.861  63.294 9.189   1.00 23.85  ? 8    GLY B O   1 
ATOM   2597  N N   . PHE B  2 9   ? 22.352  61.115 8.974   1.00 20.77  ? 9    PHE B N   1 
ATOM   2598  C CA  . PHE B  2 9   ? 22.073  61.102 7.549   1.00 21.39  ? 9    PHE B CA  1 
ATOM   2599  C C   . PHE B  2 9   ? 20.571  60.932 7.320   1.00 20.54  ? 9    PHE B C   1 
ATOM   2600  O O   . PHE B  2 9   ? 20.072  61.274 6.255   1.00 21.40  ? 9    PHE B O   1 
ATOM   2601  C CB  . PHE B  2 9   ? 22.923  60.058 6.798   1.00 21.03  ? 9    PHE B CB  1 
ATOM   2602  C CG  . PHE B  2 9   ? 22.466  58.637 6.969   1.00 18.96  ? 9    PHE B CG  1 
ATOM   2603  C CD1 . PHE B  2 9   ? 21.510  58.098 6.126   1.00 18.23  ? 9    PHE B CD1 1 
ATOM   2604  C CD2 . PHE B  2 9   ? 23.023  57.827 7.941   1.00 18.16  ? 9    PHE B CD2 1 
ATOM   2605  C CE1 . PHE B  2 9   ? 21.099  56.786 6.270   1.00 16.89  ? 9    PHE B CE1 1 
ATOM   2606  C CE2 . PHE B  2 9   ? 22.614  56.514 8.092   1.00 16.84  ? 9    PHE B CE2 1 
ATOM   2607  C CZ  . PHE B  2 9   ? 21.650  55.993 7.256   1.00 16.28  ? 9    PHE B CZ  1 
ATOM   2608  N N   . ILE B  2 10  ? 19.861  60.405 8.319   1.00 19.24  ? 10   ILE B N   1 
ATOM   2609  C CA  . ILE B  2 10  ? 18.399  60.479 8.362   1.00 19.20  ? 10   ILE B CA  1 
ATOM   2610  C C   . ILE B  2 10  ? 18.032  61.623 9.296   1.00 20.65  ? 10   ILE B C   1 
ATOM   2611  O O   . ILE B  2 10  ? 18.037  61.469 10.517  1.00 20.03  ? 10   ILE B O   1 
ATOM   2612  C CB  . ILE B  2 10  ? 17.761  59.175 8.865   1.00 17.48  ? 10   ILE B CB  1 
ATOM   2613  C CG1 . ILE B  2 10  ? 18.199  58.000 7.991   1.00 16.57  ? 10   ILE B CG1 1 
ATOM   2614  C CG2 . ILE B  2 10  ? 16.243  59.295 8.854   1.00 17.98  ? 10   ILE B CG2 1 
ATOM   2615  C CD1 . ILE B  2 10  ? 17.814  56.642 8.538   1.00 15.39  ? 10   ILE B CD1 1 
ATOM   2616  N N   . GLU B  2 11  ? 17.710  62.772 8.715   1.00 22.92  ? 11   GLU B N   1 
ATOM   2617  C CA  . GLU B  2 11  ? 17.638  64.018 9.481   1.00 25.12  ? 11   GLU B CA  1 
ATOM   2618  C C   . GLU B  2 11  ? 16.593  64.045 10.587  1.00 25.13  ? 11   GLU B C   1 
ATOM   2619  O O   . GLU B  2 11  ? 16.794  64.714 11.600  1.00 26.19  ? 11   GLU B O   1 
ATOM   2620  C CB  . GLU B  2 11  ? 17.392  65.199 8.550   1.00 28.09  ? 11   GLU B CB  1 
ATOM   2621  C CG  . GLU B  2 11  ? 18.534  65.480 7.590   1.00 29.09  ? 11   GLU B CG  1 
ATOM   2622  C CD  . GLU B  2 11  ? 18.530  66.921 7.112   1.00 32.84  ? 11   GLU B CD  1 
ATOM   2623  O OE1 . GLU B  2 11  ? 17.605  67.288 6.345   1.00 34.20  ? 11   GLU B OE1 1 
ATOM   2624  O OE2 . GLU B  2 11  ? 19.443  67.682 7.515   1.00 34.75  ? 11   GLU B OE2 1 
ATOM   2625  N N   . GLY B  2 12  ? 15.485  63.333 10.394  1.00 24.31  ? 12   GLY B N   1 
ATOM   2626  C CA  . GLY B  2 12  ? 14.382  63.341 11.362  1.00 24.90  ? 12   GLY B CA  1 
ATOM   2627  C C   . GLY B  2 12  ? 13.472  62.125 11.304  1.00 23.54  ? 12   GLY B C   1 
ATOM   2628  O O   . GLY B  2 12  ? 13.476  61.374 10.324  1.00 22.43  ? 12   GLY B O   1 
ATOM   2629  N N   . GLY B  2 13  ? 12.683  61.944 12.361  1.00 23.96  ? 13   GLY B N   1 
ATOM   2630  C CA  . GLY B  2 13  ? 11.755  60.822 12.466  1.00 23.38  ? 13   GLY B CA  1 
ATOM   2631  C C   . GLY B  2 13  ? 10.454  61.045 11.713  1.00 25.46  ? 13   GLY B C   1 
ATOM   2632  O O   . GLY B  2 13  ? 10.250  62.097 11.103  1.00 27.39  ? 13   GLY B O   1 
ATOM   2633  N N   . TRP B  2 14  ? 9.570   60.052 11.771  1.00 25.45  ? 14   TRP B N   1 
ATOM   2634  C CA  . TRP B  2 14  ? 8.298   60.082 11.058  1.00 27.58  ? 14   TRP B CA  1 
ATOM   2635  C C   . TRP B  2 14  ? 7.111   60.033 12.006  1.00 29.98  ? 14   TRP B C   1 
ATOM   2636  O O   . TRP B  2 14  ? 6.817   58.990 12.592  1.00 29.46  ? 14   TRP B O   1 
ATOM   2637  C CB  . TRP B  2 14  ? 8.204   58.896 10.106  1.00 26.20  ? 14   TRP B CB  1 
ATOM   2638  C CG  . TRP B  2 14  ? 9.175   58.938 8.982   1.00 24.50  ? 14   TRP B CG  1 
ATOM   2639  C CD1 . TRP B  2 14  ? 9.754   60.042 8.439   1.00 24.95  ? 14   TRP B CD1 1 
ATOM   2640  C CD2 . TRP B  2 14  ? 9.653   57.819 8.227   1.00 22.61  ? 14   TRP B CD2 1 
ATOM   2641  N NE1 . TRP B  2 14  ? 10.576  59.681 7.402   1.00 23.39  ? 14   TRP B NE1 1 
ATOM   2642  C CE2 . TRP B  2 14  ? 10.532  58.322 7.250   1.00 21.90  ? 14   TRP B CE2 1 
ATOM   2643  C CE3 . TRP B  2 14  ? 9.427   56.442 8.287   1.00 21.87  ? 14   TRP B CE3 1 
ATOM   2644  C CZ2 . TRP B  2 14  ? 11.186  57.497 6.336   1.00 20.40  ? 14   TRP B CZ2 1 
ATOM   2645  C CZ3 . TRP B  2 14  ? 10.081  55.623 7.382   1.00 20.45  ? 14   TRP B CZ3 1 
ATOM   2646  C CH2 . TRP B  2 14  ? 10.951  56.154 6.420   1.00 19.68  ? 14   TRP B CH2 1 
ATOM   2647  N N   . GLN B  2 15  ? 6.421   61.164 12.135  1.00 33.07  ? 15   GLN B N   1 
ATOM   2648  C CA  . GLN B  2 15  ? 5.153   61.223 12.860  1.00 36.30  ? 15   GLN B CA  1 
ATOM   2649  C C   . GLN B  2 15  ? 4.149   60.230 12.261  1.00 37.20  ? 15   GLN B C   1 
ATOM   2650  O O   . GLN B  2 15  ? 3.335   59.656 12.981  1.00 38.88  ? 15   GLN B O   1 
ATOM   2651  C CB  . GLN B  2 15  ? 4.564   62.635 12.797  1.00 40.10  ? 15   GLN B CB  1 
ATOM   2652  C CG  . GLN B  2 15  ? 5.394   63.720 13.474  1.00 40.29  ? 15   GLN B CG  1 
ATOM   2653  C CD  . GLN B  2 15  ? 5.021   63.955 14.927  1.00 42.15  ? 15   GLN B CD  1 
ATOM   2654  O OE1 . GLN B  2 15  ? 5.895   64.089 15.787  1.00 40.57  ? 15   GLN B OE1 1 
ATOM   2655  N NE2 . GLN B  2 15  ? 3.723   64.024 15.210  1.00 45.87  ? 15   GLN B NE2 1 
ATOM   2656  N N   . GLY B  2 16  ? 4.223   60.033 10.944  1.00 36.33  ? 16   GLY B N   1 
ATOM   2657  C CA  . GLY B  2 16  ? 3.307   59.157 10.219  1.00 37.37  ? 16   GLY B CA  1 
ATOM   2658  C C   . GLY B  2 16  ? 3.491   57.656 10.386  1.00 35.40  ? 16   GLY B C   1 
ATOM   2659  O O   . GLY B  2 16  ? 2.657   56.882 9.926   1.00 36.81  ? 16   GLY B O   1 
ATOM   2660  N N   . MET B  2 17  ? 4.578   57.231 11.024  1.00 32.52  ? 17   MET B N   1 
ATOM   2661  C CA  . MET B  2 17  ? 4.778   55.811 11.319  1.00 31.20  ? 17   MET B CA  1 
ATOM   2662  C C   . MET B  2 17  ? 4.480   55.520 12.788  1.00 32.31  ? 17   MET B C   1 
ATOM   2663  O O   . MET B  2 17  ? 5.301   55.797 13.658  1.00 30.75  ? 17   MET B O   1 
ATOM   2664  C CB  . MET B  2 17  ? 6.203   55.387 10.991  1.00 27.66  ? 17   MET B CB  1 
ATOM   2665  C CG  . MET B  2 17  ? 6.390   53.880 11.033  1.00 26.81  ? 17   MET B CG  1 
ATOM   2666  S SD  . MET B  2 17  ? 8.000   53.397 10.419  1.00 23.45  ? 17   MET B SD  1 
ATOM   2667  C CE  . MET B  2 17  ? 9.031   54.211 11.632  1.00 22.01  ? 17   MET B CE  1 
ATOM   2668  N N   . VAL B  2 18  ? 3.310   54.944 13.049  1.00 35.25  ? 18   VAL B N   1 
ATOM   2669  C CA  . VAL B  2 18  ? 2.808   54.765 14.418  1.00 37.23  ? 18   VAL B CA  1 
ATOM   2670  C C   . VAL B  2 18  ? 2.854   53.320 14.929  1.00 37.10  ? 18   VAL B C   1 
ATOM   2671  O O   . VAL B  2 18  ? 2.793   53.088 16.133  1.00 37.91  ? 18   VAL B O   1 
ATOM   2672  C CB  . VAL B  2 18  ? 1.360   55.295 14.547  1.00 41.80  ? 18   VAL B CB  1 
ATOM   2673  C CG1 . VAL B  2 18  ? 1.257   56.705 13.984  1.00 42.60  ? 18   VAL B CG1 1 
ATOM   2674  C CG2 . VAL B  2 18  ? 0.364   54.369 13.860  1.00 44.27  ? 18   VAL B CG2 1 
ATOM   2675  N N   . ASP B  2 19  ? 2.966   52.356 14.020  1.00 36.38  ? 19   ASP B N   1 
ATOM   2676  C CA  . ASP B  2 19  ? 2.883   50.936 14.379  1.00 37.18  ? 19   ASP B CA  1 
ATOM   2677  C C   . ASP B  2 19  ? 4.257   50.281 14.600  1.00 33.87  ? 19   ASP B C   1 
ATOM   2678  O O   . ASP B  2 19  ? 4.359   49.058 14.685  1.00 34.43  ? 19   ASP B O   1 
ATOM   2679  C CB  . ASP B  2 19  ? 2.068   50.165 13.323  1.00 39.32  ? 19   ASP B CB  1 
ATOM   2680  C CG  . ASP B  2 19  ? 2.581   50.374 11.900  1.00 37.06  ? 19   ASP B CG  1 
ATOM   2681  O OD1 . ASP B  2 19  ? 3.528   51.167 11.703  1.00 34.11  ? 19   ASP B OD1 1 
ATOM   2682  O OD2 . ASP B  2 19  ? 2.024   49.745 10.973  1.00 38.51  ? 19   ASP B OD2 1 
ATOM   2683  N N   . GLY B  2 20  ? 5.307   51.091 14.707  1.00 30.92  ? 20   GLY B N   1 
ATOM   2684  C CA  . GLY B  2 20  ? 6.635   50.569 15.002  1.00 28.20  ? 20   GLY B CA  1 
ATOM   2685  C C   . GLY B  2 20  ? 7.675   51.646 15.235  1.00 25.66  ? 20   GLY B C   1 
ATOM   2686  O O   . GLY B  2 20  ? 7.422   52.828 14.997  1.00 25.86  ? 20   GLY B O   1 
ATOM   2687  N N   . TRP B  2 21  ? 8.853   51.223 15.692  1.00 23.68  ? 21   TRP B N   1 
ATOM   2688  C CA  . TRP B  2 21  ? 9.966   52.136 15.962  1.00 21.50  ? 21   TRP B CA  1 
ATOM   2689  C C   . TRP B  2 21  ? 10.792  52.423 14.711  1.00 19.80  ? 21   TRP B C   1 
ATOM   2690  O O   . TRP B  2 21  ? 11.216  53.560 14.490  1.00 19.05  ? 21   TRP B O   1 
ATOM   2691  C CB  . TRP B  2 21  ? 10.880  51.577 17.061  1.00 20.50  ? 21   TRP B CB  1 
ATOM   2692  C CG  . TRP B  2 21  ? 10.585  52.085 18.439  1.00 21.26  ? 21   TRP B CG  1 
ATOM   2693  C CD1 . TRP B  2 21  ? 10.106  53.324 18.785  1.00 22.02  ? 21   TRP B CD1 1 
ATOM   2694  C CD2 . TRP B  2 21  ? 10.797  51.388 19.661  1.00 21.57  ? 21   TRP B CD2 1 
ATOM   2695  N NE1 . TRP B  2 21  ? 9.981   53.423 20.147  1.00 22.73  ? 21   TRP B NE1 1 
ATOM   2696  C CE2 . TRP B  2 21  ? 10.405  52.251 20.711  1.00 22.36  ? 21   TRP B CE2 1 
ATOM   2697  C CE3 . TRP B  2 21  ? 11.275  50.113 19.976  1.00 21.60  ? 21   TRP B CE3 1 
ATOM   2698  C CZ2 . TRP B  2 21  ? 10.475  51.878 22.050  1.00 22.88  ? 21   TRP B CZ2 1 
ATOM   2699  C CZ3 . TRP B  2 21  ? 11.345  49.740 21.307  1.00 22.25  ? 21   TRP B CZ3 1 
ATOM   2700  C CH2 . TRP B  2 21  ? 10.948  50.620 22.330  1.00 22.76  ? 21   TRP B CH2 1 
ATOM   2701  N N   . TYR B  2 22  ? 11.032  51.386 13.913  1.00 19.55  ? 22   TYR B N   1 
ATOM   2702  C CA  . TYR B  2 22  ? 11.794  51.513 12.674  1.00 18.30  ? 22   TYR B CA  1 
ATOM   2703  C C   . TYR B  2 22  ? 10.970  50.940 11.532  1.00 19.48  ? 22   TYR B C   1 
ATOM   2704  O O   . TYR B  2 22  ? 10.204  49.998 11.726  1.00 21.05  ? 22   TYR B O   1 
ATOM   2705  C CB  . TYR B  2 22  ? 13.129  50.759 12.771  1.00 17.07  ? 22   TYR B CB  1 
ATOM   2706  C CG  . TYR B  2 22  ? 13.712  50.673 14.167  1.00 16.61  ? 22   TYR B CG  1 
ATOM   2707  C CD1 . TYR B  2 22  ? 14.257  51.789 14.786  1.00 15.66  ? 22   TYR B CD1 1 
ATOM   2708  C CD2 . TYR B  2 22  ? 13.715  49.473 14.868  1.00 17.41  ? 22   TYR B CD2 1 
ATOM   2709  C CE1 . TYR B  2 22  ? 14.788  51.711 16.062  1.00 15.29  ? 22   TYR B CE1 1 
ATOM   2710  C CE2 . TYR B  2 22  ? 14.242  49.390 16.142  1.00 17.10  ? 22   TYR B CE2 1 
ATOM   2711  C CZ  . TYR B  2 22  ? 14.778  50.508 16.729  1.00 15.91  ? 22   TYR B CZ  1 
ATOM   2712  O OH  . TYR B  2 22  ? 15.304  50.423 17.991  1.00 15.66  ? 22   TYR B OH  1 
ATOM   2713  N N   . GLY B  2 23  ? 11.134  51.499 10.340  1.00 19.02  ? 23   GLY B N   1 
ATOM   2714  C CA  . GLY B  2 23  ? 10.443  50.973 9.180   1.00 20.08  ? 23   GLY B CA  1 
ATOM   2715  C C   . GLY B  2 23  ? 10.767  51.681 7.889   1.00 19.46  ? 23   GLY B C   1 
ATOM   2716  O O   . GLY B  2 23  ? 11.764  52.402 7.795   1.00 18.18  ? 23   GLY B O   1 
ATOM   2717  N N   . TYR B  2 24  ? 9.895   51.478 6.904   1.00 20.72  ? 24   TYR B N   1 
ATOM   2718  C CA  . TYR B  2 24  ? 10.099  51.968 5.544   1.00 20.44  ? 24   TYR B CA  1 
ATOM   2719  C C   . TYR B  2 24  ? 8.994   52.927 5.118   1.00 21.88  ? 24   TYR B C   1 
ATOM   2720  O O   . TYR B  2 24  ? 7.857   52.815 5.567   1.00 23.58  ? 24   TYR B O   1 
ATOM   2721  C CB  . TYR B  2 24  ? 10.118  50.802 4.551   1.00 20.79  ? 24   TYR B CB  1 
ATOM   2722  C CG  . TYR B  2 24  ? 10.822  49.560 5.041   1.00 20.66  ? 24   TYR B CG  1 
ATOM   2723  C CD1 . TYR B  2 24  ? 10.189  48.677 5.907   1.00 22.06  ? 24   TYR B CD1 1 
ATOM   2724  C CD2 . TYR B  2 24  ? 12.114  49.254 4.622   1.00 19.65  ? 24   TYR B CD2 1 
ATOM   2725  C CE1 . TYR B  2 24  ? 10.823  47.532 6.354   1.00 22.36  ? 24   TYR B CE1 1 
ATOM   2726  C CE2 . TYR B  2 24  ? 12.762  48.111 5.068   1.00 20.01  ? 24   TYR B CE2 1 
ATOM   2727  C CZ  . TYR B  2 24  ? 12.110  47.251 5.932   1.00 21.35  ? 24   TYR B CZ  1 
ATOM   2728  O OH  . TYR B  2 24  ? 12.726  46.105 6.377   1.00 22.17  ? 24   TYR B OH  1 
ATOM   2729  N N   . HIS B  2 25  ? 9.347   53.866 4.245   1.00 21.61  ? 25   HIS B N   1 
ATOM   2730  C CA  . HIS B  2 25  ? 8.366   54.662 3.526   1.00 23.34  ? 25   HIS B CA  1 
ATOM   2731  C C   . HIS B  2 25  ? 8.634   54.567 2.035   1.00 23.04  ? 25   HIS B C   1 
ATOM   2732  O O   . HIS B  2 25  ? 9.731   54.874 1.576   1.00 21.81  ? 25   HIS B O   1 
ATOM   2733  C CB  . HIS B  2 25  ? 8.401   56.122 3.951   1.00 24.05  ? 25   HIS B CB  1 
ATOM   2734  C CG  . HIS B  2 25  ? 7.375   56.963 3.262   1.00 26.36  ? 25   HIS B CG  1 
ATOM   2735  N ND1 . HIS B  2 25  ? 7.638   57.654 2.099   1.00 26.56  ? 25   HIS B ND1 1 
ATOM   2736  C CD2 . HIS B  2 25  ? 6.075   57.205 3.557   1.00 28.84  ? 25   HIS B CD2 1 
ATOM   2737  C CE1 . HIS B  2 25  ? 6.549   58.295 1.714   1.00 29.02  ? 25   HIS B CE1 1 
ATOM   2738  N NE2 . HIS B  2 25  ? 5.586   58.039 2.581   1.00 30.52  ? 25   HIS B NE2 1 
ATOM   2739  N N   . HIS B  2 26  ? 7.621   54.143 1.286   1.00 24.50  ? 26   HIS B N   1 
ATOM   2740  C CA  . HIS B  2 26  ? 7.737   53.960 -0.159  1.00 24.44  ? 26   HIS B CA  1 
ATOM   2741  C C   . HIS B  2 26  ? 6.926   55.015 -0.888  1.00 26.17  ? 26   HIS B C   1 
ATOM   2742  O O   . HIS B  2 26  ? 5.973   55.544 -0.334  1.00 27.99  ? 26   HIS B O   1 
ATOM   2743  C CB  . HIS B  2 26  ? 7.252   52.565 -0.551  1.00 24.96  ? 26   HIS B CB  1 
ATOM   2744  C CG  . HIS B  2 26  ? 5.769   52.389 -0.461  1.00 27.38  ? 26   HIS B CG  1 
ATOM   2745  N ND1 . HIS B  2 26  ? 5.143   51.912 0.670   1.00 28.60  ? 26   HIS B ND1 1 
ATOM   2746  C CD2 . HIS B  2 26  ? 4.788   52.618 -1.366  1.00 29.16  ? 26   HIS B CD2 1 
ATOM   2747  C CE1 . HIS B  2 26  ? 3.840   51.855 0.458   1.00 31.18  ? 26   HIS B CE1 1 
ATOM   2748  N NE2 . HIS B  2 26  ? 3.599   52.278 -0.769  1.00 31.55  ? 26   HIS B NE2 1 
ATOM   2749  N N   . SER B  2 27  ? 7.318   55.331 -2.119  1.00 25.96  ? 27   SER B N   1 
ATOM   2750  C CA  . SER B  2 27  ? 6.527   56.212 -2.985  1.00 27.88  ? 27   SER B CA  1 
ATOM   2751  C C   . SER B  2 27  ? 6.705   55.817 -4.451  1.00 27.62  ? 27   SER B C   1 
ATOM   2752  O O   . SER B  2 27  ? 7.822   55.789 -4.964  1.00 26.20  ? 27   SER B O   1 
ATOM   2753  C CB  . SER B  2 27  ? 6.899   57.682 -2.771  1.00 28.56  ? 27   SER B CB  1 
ATOM   2754  O OG  . SER B  2 27  ? 8.142   57.994 -3.366  1.00 27.31  ? 27   SER B OG  1 
ATOM   2755  N N   . ASN B  2 28  ? 5.593   55.492 -5.107  1.00 29.31  ? 28   ASN B N   1 
ATOM   2756  C CA  . ASN B  2 28  ? 5.593   55.060 -6.501  1.00 29.33  ? 28   ASN B CA  1 
ATOM   2757  C C   . ASN B  2 28  ? 4.317   55.545 -7.199  1.00 31.93  ? 28   ASN B C   1 
ATOM   2758  O O   . ASN B  2 28  ? 3.583   56.362 -6.638  1.00 33.79  ? 28   ASN B O   1 
ATOM   2759  C CB  . ASN B  2 28  ? 5.764   53.533 -6.581  1.00 28.42  ? 28   ASN B CB  1 
ATOM   2760  C CG  . ASN B  2 28  ? 4.635   52.769 -5.914  1.00 29.97  ? 28   ASN B CG  1 
ATOM   2761  O OD1 . ASN B  2 28  ? 3.586   53.323 -5.609  1.00 31.97  ? 28   ASN B OD1 1 
ATOM   2762  N ND2 . ASN B  2 28  ? 4.851   51.482 -5.684  1.00 29.55  ? 28   ASN B ND2 1 
ATOM   2763  N N   . GLU B  2 29  ? 4.058   55.064 -8.413  1.00 32.38  ? 29   GLU B N   1 
ATOM   2764  C CA  . GLU B  2 29  ? 2.876   55.486 -9.169  1.00 35.01  ? 29   GLU B CA  1 
ATOM   2765  C C   . GLU B  2 29  ? 1.561   55.201 -8.437  1.00 37.41  ? 29   GLU B C   1 
ATOM   2766  O O   . GLU B  2 29  ? 0.640   56.015 -8.474  1.00 40.04  ? 29   GLU B O   1 
ATOM   2767  C CB  . GLU B  2 29  ? 2.837   54.808 -10.538 1.00 34.98  ? 29   GLU B CB  1 
ATOM   2768  C CG  . GLU B  2 29  ? 3.919   55.274 -11.505 1.00 33.65  ? 29   GLU B CG  1 
ATOM   2769  C CD  . GLU B  2 29  ? 3.607   54.926 -12.957 1.00 34.39  ? 29   GLU B CD  1 
ATOM   2770  O OE1 . GLU B  2 29  ? 2.712   54.078 -13.209 1.00 35.54  ? 29   GLU B OE1 1 
ATOM   2771  O OE2 . GLU B  2 29  ? 4.266   55.497 -13.853 1.00 34.07  ? 29   GLU B OE2 1 
ATOM   2772  N N   . GLN B  2 30  ? 1.482   54.046 -7.780  1.00 36.93  ? 30   GLN B N   1 
ATOM   2773  C CA  . GLN B  2 30  ? 0.268   53.623 -7.070  1.00 39.55  ? 30   GLN B CA  1 
ATOM   2774  C C   . GLN B  2 30  ? -0.001  54.404 -5.779  1.00 40.51  ? 30   GLN B C   1 
ATOM   2775  O O   . GLN B  2 30  ? -1.145  54.529 -5.361  1.00 43.62  ? 30   GLN B O   1 
ATOM   2776  C CB  . GLN B  2 30  ? 0.344   52.131 -6.758  1.00 39.15  ? 30   GLN B CB  1 
ATOM   2777  C CG  . GLN B  2 30  ? 0.347   51.255 -8.001  1.00 39.17  ? 30   GLN B CG  1 
ATOM   2778  C CD  . GLN B  2 30  ? 1.465   50.229 -7.990  1.00 36.92  ? 30   GLN B CD  1 
ATOM   2779  O OE1 . GLN B  2 30  ? 2.582   50.499 -8.455  1.00 34.61  ? 30   GLN B OE1 1 
ATOM   2780  N NE2 . GLN B  2 30  ? 1.168   49.035 -7.471  1.00 38.10  ? 30   GLN B NE2 1 
ATOM   2781  N N   . GLY B  2 31  ? 1.047   54.918 -5.145  1.00 38.16  ? 31   GLY B N   1 
ATOM   2782  C CA  . GLY B  2 31  ? 0.884   55.719 -3.931  1.00 39.05  ? 31   GLY B CA  1 
ATOM   2783  C C   . GLY B  2 31  ? 2.109   55.719 -3.044  1.00 36.12  ? 31   GLY B C   1 
ATOM   2784  O O   . GLY B  2 31  ? 3.200   55.368 -3.479  1.00 33.53  ? 31   GLY B O   1 
ATOM   2785  N N   . SER B  2 32  ? 1.920   56.121 -1.793  1.00 36.82  ? 32   SER B N   1 
ATOM   2786  C CA  . SER B  2 32  ? 2.985   56.096 -0.798  1.00 34.34  ? 32   SER B CA  1 
ATOM   2787  C C   . SER B  2 32  ? 2.450   55.614 0.543   1.00 35.33  ? 32   SER B C   1 
ATOM   2788  O O   . SER B  2 32  ? 1.242   55.602 0.763   1.00 38.35  ? 32   SER B O   1 
ATOM   2789  C CB  . SER B  2 32  ? 3.597   57.484 -0.645  1.00 34.15  ? 32   SER B CB  1 
ATOM   2790  O OG  . SER B  2 32  ? 2.611   58.438 -0.327  1.00 37.37  ? 32   SER B OG  1 
ATOM   2791  N N   . GLY B  2 33  ? 3.346   55.212 1.439   1.00 33.11  ? 33   GLY B N   1 
ATOM   2792  C CA  . GLY B  2 33  ? 2.928   54.758 2.760   1.00 34.03  ? 33   GLY B CA  1 
ATOM   2793  C C   . GLY B  2 33  ? 4.039   54.316 3.691   1.00 31.45  ? 33   GLY B C   1 
ATOM   2794  O O   . GLY B  2 33  ? 5.152   54.033 3.259   1.00 28.96  ? 33   GLY B O   1 
ATOM   2795  N N   . TYR B  2 34  ? 3.716   54.258 4.980   1.00 32.38  ? 34   TYR B N   1 
ATOM   2796  C CA  . TYR B  2 34  ? 4.641   53.805 6.010   1.00 30.37  ? 34   TYR B CA  1 
ATOM   2797  C C   . TYR B  2 34  ? 4.368   52.350 6.357   1.00 30.98  ? 34   TYR B C   1 
ATOM   2798  O O   . TYR B  2 34  ? 3.219   51.947 6.484   1.00 33.76  ? 34   TYR B O   1 
ATOM   2799  C CB  . TYR B  2 34  ? 4.490   54.655 7.269   1.00 31.19  ? 34   TYR B CB  1 
ATOM   2800  C CG  . TYR B  2 34  ? 4.782   56.124 7.061   1.00 31.18  ? 34   TYR B CG  1 
ATOM   2801  C CD1 . TYR B  2 34  ? 6.089   56.602 7.059   1.00 28.70  ? 34   TYR B CD1 1 
ATOM   2802  C CD2 . TYR B  2 34  ? 3.750   57.039 6.873   1.00 34.18  ? 34   TYR B CD2 1 
ATOM   2803  C CE1 . TYR B  2 34  ? 6.357   57.948 6.871   1.00 29.25  ? 34   TYR B CE1 1 
ATOM   2804  C CE2 . TYR B  2 34  ? 4.012   58.387 6.685   1.00 34.75  ? 34   TYR B CE2 1 
ATOM   2805  C CZ  . TYR B  2 34  ? 5.316   58.835 6.688   1.00 32.29  ? 34   TYR B CZ  1 
ATOM   2806  O OH  . TYR B  2 34  ? 5.580   60.171 6.506   1.00 33.39  ? 34   TYR B OH  1 
ATOM   2807  N N   . ALA B  2 35  ? 5.430   51.568 6.503   1.00 28.89  ? 35   ALA B N   1 
ATOM   2808  C CA  . ALA B  2 35  ? 5.326   50.184 6.948   1.00 29.75  ? 35   ALA B CA  1 
ATOM   2809  C C   . ALA B  2 35  ? 6.404   49.915 7.996   1.00 28.03  ? 35   ALA B C   1 
ATOM   2810  O O   . ALA B  2 35  ? 7.590   50.027 7.715   1.00 25.73  ? 35   ALA B O   1 
ATOM   2811  C CB  . ALA B  2 35  ? 5.483   49.239 5.774   1.00 29.69  ? 35   ALA B CB  1 
ATOM   2812  N N   . ALA B  2 36  ? 5.984   49.570 9.205   1.00 29.47  ? 36   ALA B N   1 
ATOM   2813  C CA  . ALA B  2 36  ? 6.914   49.295 10.281  1.00 28.15  ? 36   ALA B CA  1 
ATOM   2814  C C   . ALA B  2 36  ? 7.600   47.951 10.073  1.00 28.00  ? 36   ALA B C   1 
ATOM   2815  O O   . ALA B  2 36  ? 6.955   46.966 9.731   1.00 30.16  ? 36   ALA B O   1 
ATOM   2816  C CB  . ALA B  2 36  ? 6.189   49.308 11.617  1.00 30.02  ? 36   ALA B CB  1 
ATOM   2817  N N   . ASP B  2 37  ? 8.911   47.921 10.290  1.00 26.00  ? 37   ASP B N   1 
ATOM   2818  C CA  . ASP B  2 37  ? 9.674   46.677 10.294  1.00 26.29  ? 37   ASP B CA  1 
ATOM   2819  C C   . ASP B  2 37  ? 9.491   45.989 11.655  1.00 27.90  ? 37   ASP B C   1 
ATOM   2820  O O   . ASP B  2 37  ? 9.984   46.472 12.682  1.00 26.70  ? 37   ASP B O   1 
ATOM   2821  C CB  . ASP B  2 37  ? 11.152  46.966 10.017  1.00 23.91  ? 37   ASP B CB  1 
ATOM   2822  C CG  . ASP B  2 37  ? 11.969  45.705 9.846   1.00 24.55  ? 37   ASP B CG  1 
ATOM   2823  O OD1 . ASP B  2 37  ? 12.432  45.147 10.869  1.00 24.98  ? 37   ASP B OD1 1 
ATOM   2824  O OD2 . ASP B  2 37  ? 12.139  45.267 8.689   1.00 24.87  ? 37   ASP B OD2 1 
ATOM   2825  N N   . LYS B  2 38  ? 8.773   44.866 11.652  1.00 30.90  ? 38   LYS B N   1 
ATOM   2826  C CA  . LYS B  2 38  ? 8.411   44.163 12.887  1.00 33.16  ? 38   LYS B CA  1 
ATOM   2827  C C   . LYS B  2 38  ? 9.608   43.534 13.590  1.00 32.50  ? 38   LYS B C   1 
ATOM   2828  O O   . LYS B  2 38  ? 9.767   43.690 14.801  1.00 32.34  ? 38   LYS B O   1 
ATOM   2829  C CB  . LYS B  2 38  ? 7.363   43.078 12.610  1.00 37.05  ? 38   LYS B CB  1 
ATOM   2830  C CG  . LYS B  2 38  ? 5.951   43.611 12.413  1.00 38.98  ? 38   LYS B CG  1 
ATOM   2831  C CD  . LYS B  2 38  ? 4.923   42.485 12.360  1.00 43.43  ? 38   LYS B CD  1 
ATOM   2832  C CE  . LYS B  2 38  ? 4.883   41.813 10.993  1.00 44.29  ? 38   LYS B CE  1 
ATOM   2833  N NZ  . LYS B  2 38  ? 4.025   40.589 11.000  1.00 49.03  ? 38   LYS B NZ  1 
ATOM   2834  N N   . GLU B  2 39  ? 10.437  42.820 12.829  1.00 32.43  ? 39   GLU B N   1 
ATOM   2835  C CA  . GLU B  2 39  ? 11.599  42.115 13.385  1.00 32.48  ? 39   GLU B CA  1 
ATOM   2836  C C   . GLU B  2 39  ? 12.518  43.034 14.197  1.00 29.58  ? 39   GLU B C   1 
ATOM   2837  O O   . GLU B  2 39  ? 12.762  42.778 15.375  1.00 30.05  ? 39   GLU B O   1 
ATOM   2838  C CB  . GLU B  2 39  ? 12.393  41.409 12.270  1.00 33.00  ? 39   GLU B CB  1 
ATOM   2839  C CG  . GLU B  2 39  ? 13.797  40.948 12.676  1.00 32.91  ? 39   GLU B CG  1 
ATOM   2840  C CD  . GLU B  2 39  ? 14.111  39.524 12.232  1.00 36.19  ? 39   GLU B CD  1 
ATOM   2841  O OE1 . GLU B  2 39  ? 13.875  39.190 11.050  1.00 37.14  ? 39   GLU B OE1 1 
ATOM   2842  O OE2 . GLU B  2 39  ? 14.579  38.728 13.082  1.00 38.18  ? 39   GLU B OE2 1 
ATOM   2843  N N   . SER B  2 40  ? 13.020  44.093 13.571  1.00 26.82  ? 40   SER B N   1 
ATOM   2844  C CA  . SER B  2 40  ? 13.927  45.017 14.254  1.00 24.44  ? 40   SER B CA  1 
ATOM   2845  C C   . SER B  2 40  ? 13.239  45.732 15.412  1.00 24.15  ? 40   SER B C   1 
ATOM   2846  O O   . SER B  2 40  ? 13.872  46.014 16.432  1.00 23.29  ? 40   SER B O   1 
ATOM   2847  C CB  . SER B  2 40  ? 14.511  46.045 13.282  1.00 22.32  ? 40   SER B CB  1 
ATOM   2848  O OG  . SER B  2 40  ? 13.498  46.832 12.689  1.00 22.10  ? 40   SER B OG  1 
ATOM   2849  N N   . THR B  2 41  ? 11.944  46.009 15.259  1.00 25.12  ? 41   THR B N   1 
ATOM   2850  C CA  . THR B  2 41  ? 11.174  46.680 16.304  1.00 25.46  ? 41   THR B CA  1 
ATOM   2851  C C   . THR B  2 41  ? 10.975  45.789 17.533  1.00 27.28  ? 41   THR B C   1 
ATOM   2852  O O   . THR B  2 41  ? 11.172  46.233 18.664  1.00 26.71  ? 41   THR B O   1 
ATOM   2853  C CB  . THR B  2 41  ? 9.804   47.149 15.779  1.00 26.85  ? 41   THR B CB  1 
ATOM   2854  O OG1 . THR B  2 41  ? 10.000  48.089 14.721  1.00 25.20  ? 41   THR B OG1 1 
ATOM   2855  C CG2 . THR B  2 41  ? 8.999   47.822 16.879  1.00 27.92  ? 41   THR B CG2 1 
ATOM   2856  N N   . GLN B  2 42  ? 10.578  44.539 17.309  1.00 29.71  ? 42   GLN B N   1 
ATOM   2857  C CA  . GLN B  2 42  ? 10.345  43.603 18.411  1.00 32.10  ? 42   GLN B CA  1 
ATOM   2858  C C   . GLN B  2 42  ? 11.642  43.294 19.141  1.00 30.90  ? 42   GLN B C   1 
ATOM   2859  O O   . GLN B  2 42  ? 11.644  43.099 20.351  1.00 31.72  ? 42   GLN B O   1 
ATOM   2860  C CB  . GLN B  2 42  ? 9.723   42.304 17.899  1.00 35.50  ? 42   GLN B CB  1 
ATOM   2861  C CG  . GLN B  2 42  ? 9.323   41.330 18.998  1.00 38.84  ? 42   GLN B CG  1 
ATOM   2862  C CD  . GLN B  2 42  ? 8.355   41.935 19.998  1.00 39.90  ? 42   GLN B CD  1 
ATOM   2863  O OE1 . GLN B  2 42  ? 8.638   42.001 21.194  1.00 39.80  ? 42   GLN B OE1 1 
ATOM   2864  N NE2 . GLN B  2 42  ? 7.210   42.396 19.508  1.00 41.13  ? 42   GLN B NE2 1 
ATOM   2865  N N   . LYS B  2 43  ? 12.739  43.254 18.392  1.00 29.20  ? 43   LYS B N   1 
ATOM   2866  C CA  . LYS B  2 43  ? 14.067  43.033 18.964  1.00 28.25  ? 43   LYS B CA  1 
ATOM   2867  C C   . LYS B  2 43  ? 14.474  44.186 19.879  1.00 25.73  ? 43   LYS B C   1 
ATOM   2868  O O   . LYS B  2 43  ? 15.100  43.966 20.917  1.00 25.76  ? 43   LYS B O   1 
ATOM   2869  C CB  . LYS B  2 43  ? 15.106  42.867 17.850  1.00 27.46  ? 43   LYS B CB  1 
ATOM   2870  C CG  . LYS B  2 43  ? 16.029  41.673 18.028  1.00 29.46  ? 43   LYS B CG  1 
ATOM   2871  C CD  . LYS B  2 43  ? 16.583  41.235 16.681  1.00 30.02  ? 43   LYS B CD  1 
ATOM   2872  C CE  . LYS B  2 43  ? 17.642  40.151 16.812  1.00 32.27  ? 43   LYS B CE  1 
ATOM   2873  N NZ  . LYS B  2 43  ? 18.509  40.136 15.597  1.00 32.07  ? 43   LYS B NZ  1 
ATOM   2874  N N   . ALA B  2 44  ? 14.115  45.407 19.484  1.00 23.80  ? 44   ALA B N   1 
ATOM   2875  C CA  . ALA B  2 44  ? 14.373  46.593 20.296  1.00 21.90  ? 44   ALA B CA  1 
ATOM   2876  C C   . ALA B  2 44  ? 13.500  46.600 21.541  1.00 23.19  ? 44   ALA B C   1 
ATOM   2877  O O   . ALA B  2 44  ? 13.962  46.943 22.624  1.00 22.50  ? 44   ALA B O   1 
ATOM   2878  C CB  . ALA B  2 44  ? 14.138  47.856 19.487  1.00 20.39  ? 44   ALA B CB  1 
ATOM   2879  N N   . ILE B  2 45  ? 12.234  46.226 21.383  1.00 25.30  ? 45   ILE B N   1 
ATOM   2880  C CA  . ILE B  2 45  ? 11.316  46.139 22.519  1.00 27.28  ? 45   ILE B CA  1 
ATOM   2881  C C   . ILE B  2 45  ? 11.825  45.148 23.567  1.00 28.36  ? 45   ILE B C   1 
ATOM   2882  O O   . ILE B  2 45  ? 11.752  45.421 24.765  1.00 28.63  ? 45   ILE B O   1 
ATOM   2883  C CB  . ILE B  2 45  ? 9.883   45.775 22.062  1.00 30.15  ? 45   ILE B CB  1 
ATOM   2884  C CG1 . ILE B  2 45  ? 9.217   47.001 21.427  1.00 29.47  ? 45   ILE B CG1 1 
ATOM   2885  C CG2 . ILE B  2 45  ? 9.039   45.276 23.228  1.00 33.21  ? 45   ILE B CG2 1 
ATOM   2886  C CD1 . ILE B  2 45  ? 7.972   46.687 20.624  1.00 32.06  ? 45   ILE B CD1 1 
ATOM   2887  N N   . ASP B  2 46  ? 12.345  44.011 23.113  1.00 29.22  ? 46   ASP B N   1 
ATOM   2888  C CA  . ASP B  2 46  ? 12.877  42.991 24.017  1.00 30.75  ? 46   ASP B CA  1 
ATOM   2889  C C   . ASP B  2 46  ? 14.128  43.470 24.743  1.00 28.34  ? 46   ASP B C   1 
ATOM   2890  O O   . ASP B  2 46  ? 14.261  43.280 25.946  1.00 29.06  ? 46   ASP B O   1 
ATOM   2891  C CB  . ASP B  2 46  ? 13.191  41.704 23.252  1.00 32.73  ? 46   ASP B CB  1 
ATOM   2892  C CG  . ASP B  2 46  ? 11.960  41.077 22.636  1.00 35.70  ? 46   ASP B CG  1 
ATOM   2893  O OD1 . ASP B  2 46  ? 10.847  41.580 22.886  1.00 36.48  ? 46   ASP B OD1 1 
ATOM   2894  O OD2 . ASP B  2 46  ? 12.106  40.083 21.894  1.00 37.58  ? 46   ASP B OD2 1 
ATOM   2895  N N   . GLY B  2 47  ? 15.041  44.088 24.009  1.00 25.76  ? 47   GLY B N   1 
ATOM   2896  C CA  . GLY B  2 47  ? 16.275  44.593 24.596  1.00 23.80  ? 47   GLY B CA  1 
ATOM   2897  C C   . GLY B  2 47  ? 16.052  45.644 25.671  1.00 22.61  ? 47   GLY B C   1 
ATOM   2898  O O   . GLY B  2 47  ? 16.711  45.627 26.712  1.00 22.34  ? 47   GLY B O   1 
ATOM   2899  N N   . VAL B  2 48  ? 15.113  46.555 25.423  1.00 22.17  ? 48   VAL B N   1 
ATOM   2900  C CA  . VAL B  2 48  ? 14.797  47.626 26.371  1.00 21.50  ? 48   VAL B CA  1 
ATOM   2901  C C   . VAL B  2 48  ? 14.029  47.102 27.588  1.00 23.71  ? 48   VAL B C   1 
ATOM   2902  O O   . VAL B  2 48  ? 14.269  47.540 28.707  1.00 23.32  ? 48   VAL B O   1 
ATOM   2903  C CB  . VAL B  2 48  ? 14.013  48.763 25.683  1.00 21.01  ? 48   VAL B CB  1 
ATOM   2904  C CG1 . VAL B  2 48  ? 13.428  49.729 26.707  1.00 21.41  ? 48   VAL B CG1 1 
ATOM   2905  C CG2 . VAL B  2 48  ? 14.919  49.502 24.706  1.00 18.83  ? 48   VAL B CG2 1 
ATOM   2906  N N   . THR B  2 49  ? 13.112  46.166 27.368  1.00 26.31  ? 49   THR B N   1 
ATOM   2907  C CA  . THR B  2 49  ? 12.359  45.575 28.463  1.00 29.08  ? 49   THR B CA  1 
ATOM   2908  C C   . THR B  2 49  ? 13.294  44.866 29.439  1.00 29.33  ? 49   THR B C   1 
ATOM   2909  O O   . THR B  2 49  ? 13.242  45.114 30.646  1.00 29.70  ? 49   THR B O   1 
ATOM   2910  C CB  . THR B  2 49  ? 11.303  44.590 27.943  1.00 32.33  ? 49   THR B CB  1 
ATOM   2911  O OG1 . THR B  2 49  ? 10.399  45.282 27.077  1.00 32.38  ? 49   THR B OG1 1 
ATOM   2912  C CG2 . THR B  2 49  ? 10.521  43.975 29.084  1.00 35.72  ? 49   THR B CG2 1 
ATOM   2913  N N   . ASN B  2 50  ? 14.151  43.994 28.912  1.00 29.42  ? 50   ASN B N   1 
ATOM   2914  C CA  . ASN B  2 50  ? 15.134  43.277 29.732  1.00 30.00  ? 50   ASN B CA  1 
ATOM   2915  C C   . ASN B  2 50  ? 16.023  44.233 30.513  1.00 27.48  ? 50   ASN B C   1 
ATOM   2916  O O   . ASN B  2 50  ? 16.304  44.019 31.687  1.00 28.15  ? 50   ASN B O   1 
ATOM   2917  C CB  . ASN B  2 50  ? 16.014  42.394 28.854  1.00 30.40  ? 50   ASN B CB  1 
ATOM   2918  C CG  . ASN B  2 50  ? 15.269  41.205 28.291  1.00 33.75  ? 50   ASN B CG  1 
ATOM   2919  O OD1 . ASN B  2 50  ? 14.620  40.469 29.026  1.00 36.81  ? 50   ASN B OD1 1 
ATOM   2920  N ND2 . ASN B  2 50  ? 15.366  41.003 26.986  1.00 33.51  ? 50   ASN B ND2 1 
ATOM   2921  N N   . LYS B  2 51  ? 16.469  45.281 29.834  1.00 24.89  ? 51   LYS B N   1 
ATOM   2922  C CA  . LYS B  2 51  ? 17.307  46.315 30.429  1.00 22.71  ? 51   LYS B CA  1 
ATOM   2923  C C   . LYS B  2 51  ? 16.652  46.981 31.631  1.00 23.08  ? 51   LYS B C   1 
ATOM   2924  O O   . LYS B  2 51  ? 17.297  47.205 32.653  1.00 22.55  ? 51   LYS B O   1 
ATOM   2925  C CB  . LYS B  2 51  ? 17.608  47.359 29.364  1.00 20.53  ? 51   LYS B CB  1 
ATOM   2926  C CG  . LYS B  2 51  ? 18.333  48.602 29.828  1.00 18.59  ? 51   LYS B CG  1 
ATOM   2927  C CD  . LYS B  2 51  ? 18.575  49.489 28.616  1.00 17.16  ? 51   LYS B CD  1 
ATOM   2928  C CE  . LYS B  2 51  ? 19.954  50.102 28.613  1.00 15.82  ? 51   LYS B CE  1 
ATOM   2929  N NZ  . LYS B  2 51  ? 20.566  50.100 27.260  1.00 15.34  ? 51   LYS B NZ  1 
ATOM   2930  N N   . VAL B  2 52  ? 15.375  47.311 31.496  1.00 24.29  ? 52   VAL B N   1 
ATOM   2931  C CA  . VAL B  2 52  ? 14.645  47.970 32.569  1.00 25.18  ? 52   VAL B CA  1 
ATOM   2932  C C   . VAL B  2 52  ? 14.507  47.023 33.760  1.00 27.46  ? 52   VAL B C   1 
ATOM   2933  O O   . VAL B  2 52  ? 14.716  47.431 34.902  1.00 27.31  ? 52   VAL B O   1 
ATOM   2934  C CB  . VAL B  2 52  ? 13.263  48.460 32.085  1.00 26.58  ? 52   VAL B CB  1 
ATOM   2935  C CG1 . VAL B  2 52  ? 12.400  48.919 33.253  1.00 28.42  ? 52   VAL B CG1 1 
ATOM   2936  C CG2 . VAL B  2 52  ? 13.430  49.593 31.081  1.00 24.59  ? 52   VAL B CG2 1 
ATOM   2937  N N   . ASN B  2 53  ? 14.176  45.763 33.485  1.00 29.90  ? 53   ASN B N   1 
ATOM   2938  C CA  . ASN B  2 53  ? 14.046  44.744 34.531  1.00 32.70  ? 53   ASN B CA  1 
ATOM   2939  C C   . ASN B  2 53  ? 15.391  44.408 35.169  1.00 31.78  ? 53   ASN B C   1 
ATOM   2940  O O   . ASN B  2 53  ? 15.478  44.198 36.378  1.00 32.83  ? 53   ASN B O   1 
ATOM   2941  C CB  . ASN B  2 53  ? 13.416  43.467 33.968  1.00 35.89  ? 53   ASN B CB  1 
ATOM   2942  C CG  . ASN B  2 53  ? 12.063  43.714 33.323  1.00 37.47  ? 53   ASN B CG  1 
ATOM   2943  O OD1 . ASN B  2 53  ? 11.357  44.656 33.683  1.00 37.42  ? 53   ASN B OD1 1 
ATOM   2944  N ND2 . ASN B  2 53  ? 11.698  42.873 32.358  1.00 39.23  ? 53   ASN B ND2 1 
ATOM   2945  N N   . SER B  2 54  ? 16.434  44.352 34.343  1.00 30.19  ? 54   SER B N   1 
ATOM   2946  C CA  . SER B  2 54  ? 17.797  44.126 34.823  1.00 29.50  ? 54   SER B CA  1 
ATOM   2947  C C   . SER B  2 54  ? 18.217  45.222 35.781  1.00 27.74  ? 54   SER B C   1 
ATOM   2948  O O   . SER B  2 54  ? 18.821  44.945 36.818  1.00 28.25  ? 54   SER B O   1 
ATOM   2949  C CB  . SER B  2 54  ? 18.790  44.064 33.657  1.00 28.07  ? 54   SER B CB  1 
ATOM   2950  O OG  . SER B  2 54  ? 18.727  42.812 33.004  1.00 30.40  ? 54   SER B OG  1 
ATOM   2951  N N   . ILE B  2 55  ? 17.901  46.464 35.418  1.00 26.10  ? 55   ILE B N   1 
ATOM   2952  C CA  . ILE B  2 55  ? 18.190  47.623 36.259  1.00 24.80  ? 55   ILE B CA  1 
ATOM   2953  C C   . ILE B  2 55  ? 17.404  47.557 37.564  1.00 26.76  ? 55   ILE B C   1 
ATOM   2954  O O   . ILE B  2 55  ? 17.976  47.698 38.644  1.00 26.58  ? 55   ILE B O   1 
ATOM   2955  C CB  . ILE B  2 55  ? 17.878  48.942 35.519  1.00 23.19  ? 55   ILE B CB  1 
ATOM   2956  C CG1 . ILE B  2 55  ? 18.947  49.198 34.450  1.00 21.41  ? 55   ILE B CG1 1 
ATOM   2957  C CG2 . ILE B  2 55  ? 17.830  50.116 36.492  1.00 22.62  ? 55   ILE B CG2 1 
ATOM   2958  C CD1 . ILE B  2 55  ? 18.647  50.355 33.520  1.00 20.25  ? 55   ILE B CD1 1 
ATOM   2959  N N   . ILE B  2 56  ? 16.095  47.346 37.462  1.00 29.04  ? 56   ILE B N   1 
ATOM   2960  C CA  . ILE B  2 56  ? 15.241  47.213 38.641  1.00 31.56  ? 56   ILE B CA  1 
ATOM   2961  C C   . ILE B  2 56  ? 15.795  46.162 39.611  1.00 33.21  ? 56   ILE B C   1 
ATOM   2962  O O   . ILE B  2 56  ? 15.936  46.433 40.807  1.00 33.45  ? 56   ILE B O   1 
ATOM   2963  C CB  . ILE B  2 56  ? 13.793  46.847 38.240  1.00 34.36  ? 56   ILE B CB  1 
ATOM   2964  C CG1 . ILE B  2 56  ? 13.092  48.063 37.623  1.00 33.59  ? 56   ILE B CG1 1 
ATOM   2965  C CG2 . ILE B  2 56  ? 12.998  46.334 39.439  1.00 37.66  ? 56   ILE B CG2 1 
ATOM   2966  C CD1 . ILE B  2 56  ? 11.782  47.737 36.930  1.00 36.16  ? 56   ILE B CD1 1 
ATOM   2967  N N   . ASP B  2 57  ? 16.122  44.977 39.089  1.00 34.70  ? 57   ASP B N   1 
ATOM   2968  C CA  . ASP B  2 57  ? 16.534  43.840 39.929  1.00 37.17  ? 57   ASP B CA  1 
ATOM   2969  C C   . ASP B  2 57  ? 17.885  44.020 40.617  1.00 35.66  ? 57   ASP B C   1 
ATOM   2970  O O   . ASP B  2 57  ? 18.064  43.591 41.753  1.00 37.16  ? 57   ASP B O   1 
ATOM   2971  C CB  . ASP B  2 57  ? 16.533  42.541 39.124  1.00 39.47  ? 57   ASP B CB  1 
ATOM   2972  C CG  . ASP B  2 57  ? 15.142  41.958 38.975  1.00 42.99  ? 57   ASP B CG  1 
ATOM   2973  O OD1 . ASP B  2 57  ? 14.464  41.780 40.017  1.00 45.53  ? 57   ASP B OD1 1 
ATOM   2974  O OD2 . ASP B  2 57  ? 14.723  41.682 37.825  1.00 43.52  ? 57   ASP B OD2 1 
ATOM   2975  N N   . LYS B  2 58  ? 18.830  44.656 39.940  1.00 33.11  ? 58   LYS B N   1 
ATOM   2976  C CA  . LYS B  2 58  ? 20.128  44.933 40.552  1.00 31.87  ? 58   LYS B CA  1 
ATOM   2977  C C   . LYS B  2 58  ? 20.016  45.891 41.734  1.00 31.26  ? 58   LYS B C   1 
ATOM   2978  O O   . LYS B  2 58  ? 20.785  45.792 42.689  1.00 31.41  ? 58   LYS B O   1 
ATOM   2979  C CB  . LYS B  2 58  ? 21.130  45.449 39.508  1.00 29.54  ? 58   LYS B CB  1 
ATOM   2980  C CG  . LYS B  2 58  ? 22.188  44.430 39.091  1.00 30.61  ? 58   LYS B CG  1 
ATOM   2981  C CD  . LYS B  2 58  ? 21.633  43.017 38.938  1.00 33.74  ? 58   LYS B CD  1 
ATOM   2982  C CE  . LYS B  2 58  ? 22.743  42.010 38.722  1.00 35.45  ? 58   LYS B CE  1 
ATOM   2983  N NZ  . LYS B  2 58  ? 22.238  40.611 38.810  1.00 39.24  ? 58   LYS B NZ  1 
ATOM   2984  N N   . MET B  2 59  ? 19.046  46.796 41.681  1.00 31.12  ? 59   MET B N   1 
ATOM   2985  C CA  . MET B  2 59  ? 18.819  47.751 42.768  1.00 30.94  ? 59   MET B CA  1 
ATOM   2986  C C   . MET B  2 59  ? 17.897  47.173 43.852  1.00 33.93  ? 59   MET B C   1 
ATOM   2987  O O   . MET B  2 59  ? 17.900  47.654 44.988  1.00 34.11  ? 59   MET B O   1 
ATOM   2988  C CB  . MET B  2 59  ? 18.230  49.044 42.204  1.00 29.72  ? 59   MET B CB  1 
ATOM   2989  C CG  . MET B  2 59  ? 19.061  49.660 41.083  1.00 27.42  ? 59   MET B CG  1 
ATOM   2990  S SD  . MET B  2 59  ? 20.708  50.172 41.599  1.00 25.82  ? 59   MET B SD  1 
ATOM   2991  C CE  . MET B  2 59  ? 20.375  51.427 42.841  1.00 25.77  ? 59   MET B CE  1 
ATOM   2992  N N   . ASN B  2 60  ? 17.128  46.141 43.496  1.00 36.64  ? 60   ASN B N   1 
ATOM   2993  C CA  . ASN B  2 60  ? 16.154  45.502 44.404  1.00 40.23  ? 60   ASN B CA  1 
ATOM   2994  C C   . ASN B  2 60  ? 16.697  45.126 45.800  1.00 41.28  ? 60   ASN B C   1 
ATOM   2995  O O   . ASN B  2 60  ? 15.994  45.308 46.798  1.00 42.99  ? 60   ASN B O   1 
ATOM   2996  C CB  . ASN B  2 60  ? 15.481  44.298 43.700  1.00 43.16  ? 60   ASN B CB  1 
ATOM   2997  C CG  . ASN B  2 60  ? 15.122  43.169 44.653  1.00 47.13  ? 60   ASN B CG  1 
ATOM   2998  O OD1 . ASN B  2 60  ? 15.999  42.447 45.124  1.00 47.73  ? 60   ASN B OD1 1 
ATOM   2999  N ND2 . ASN B  2 60  ? 13.829  42.990 44.917  1.00 50.41  ? 60   ASN B ND2 1 
ATOM   3000  N N   . THR B  2 61  ? 17.924  44.604 45.880  1.00 40.56  ? 61   THR B N   1 
ATOM   3001  C CA  . THR B  2 61  ? 18.582  44.420 47.188  1.00 41.13  ? 61   THR B CA  1 
ATOM   3002  C C   . THR B  2 61  ? 19.579  45.560 47.384  1.00 37.73  ? 61   THR B C   1 
ATOM   3003  O O   . THR B  2 61  ? 20.560  45.687 46.637  1.00 35.90  ? 61   THR B O   1 
ATOM   3004  C CB  . THR B  2 61  ? 19.308  43.058 47.350  1.00 43.30  ? 61   THR B CB  1 
ATOM   3005  O OG1 . THR B  2 61  ? 20.609  43.117 46.754  1.00 41.35  ? 61   THR B OG1 1 
ATOM   3006  C CG2 . THR B  2 61  ? 18.513  41.909 46.731  1.00 46.59  ? 61   THR B CG2 1 
ATOM   3007  N N   . GLN B  2 62  ? 19.308  46.400 48.375  1.00 37.33  ? 62   GLN B N   1 
ATOM   3008  C CA  . GLN B  2 62  ? 20.155  47.553 48.661  1.00 34.60  ? 62   GLN B CA  1 
ATOM   3009  C C   . GLN B  2 62  ? 19.933  47.993 50.108  1.00 35.28  ? 62   GLN B C   1 
ATOM   3010  O O   . GLN B  2 62  ? 18.990  47.536 50.762  1.00 37.86  ? 62   GLN B O   1 
ATOM   3011  C CB  . GLN B  2 62  ? 19.866  48.687 47.663  1.00 32.73  ? 62   GLN B CB  1 
ATOM   3012  C CG  . GLN B  2 62  ? 19.124  49.902 48.210  1.00 32.83  ? 62   GLN B CG  1 
ATOM   3013  C CD  . GLN B  2 62  ? 18.951  50.979 47.159  1.00 31.45  ? 62   GLN B CD  1 
ATOM   3014  O OE1 . GLN B  2 62  ? 19.036  50.708 45.956  1.00 30.81  ? 62   GLN B OE1 1 
ATOM   3015  N NE2 . GLN B  2 62  ? 18.705  52.212 47.604  1.00 31.34  ? 62   GLN B NE2 1 
ATOM   3016  N N   . PHE B  2 63  ? 20.796  48.882 50.597  1.00 33.23  ? 63   PHE B N   1 
ATOM   3017  C CA  . PHE B  2 63  ? 20.786  49.275 52.008  1.00 33.75  ? 63   PHE B CA  1 
ATOM   3018  C C   . PHE B  2 63  ? 19.413  49.782 52.471  1.00 35.36  ? 63   PHE B C   1 
ATOM   3019  O O   . PHE B  2 63  ? 18.720  50.487 51.733  1.00 35.27  ? 63   PHE B O   1 
ATOM   3020  C CB  . PHE B  2 63  ? 21.857  50.338 52.292  1.00 31.49  ? 63   PHE B CB  1 
ATOM   3021  C CG  . PHE B  2 63  ? 21.996  50.666 53.750  1.00 32.10  ? 63   PHE B CG  1 
ATOM   3022  C CD1 . PHE B  2 63  ? 22.565  49.747 54.629  1.00 33.10  ? 63   PHE B CD1 1 
ATOM   3023  C CD2 . PHE B  2 63  ? 21.526  51.878 54.255  1.00 32.03  ? 63   PHE B CD2 1 
ATOM   3024  C CE1 . PHE B  2 63  ? 22.676  50.036 55.978  1.00 33.72  ? 63   PHE B CE1 1 
ATOM   3025  C CE2 . PHE B  2 63  ? 21.636  52.173 55.604  1.00 32.75  ? 63   PHE B CE2 1 
ATOM   3026  C CZ  . PHE B  2 63  ? 22.210  51.251 56.465  1.00 33.45  ? 63   PHE B CZ  1 
ATOM   3027  N N   . GLU B  2 64  ? 19.030  49.392 53.685  1.00 37.21  ? 64   GLU B N   1 
ATOM   3028  C CA  . GLU B  2 64  ? 17.811  49.875 54.318  1.00 39.22  ? 64   GLU B CA  1 
ATOM   3029  C C   . GLU B  2 64  ? 18.166  50.503 55.655  1.00 39.01  ? 64   GLU B C   1 
ATOM   3030  O O   . GLU B  2 64  ? 18.862  49.887 56.467  1.00 39.24  ? 64   GLU B O   1 
ATOM   3031  C CB  . GLU B  2 64  ? 16.839  48.724 54.562  1.00 42.82  ? 64   GLU B CB  1 
ATOM   3032  C CG  . GLU B  2 64  ? 16.295  48.082 53.299  1.00 43.58  ? 64   GLU B CG  1 
ATOM   3033  C CD  . GLU B  2 64  ? 15.371  46.914 53.598  1.00 47.72  ? 64   GLU B CD  1 
ATOM   3034  O OE1 . GLU B  2 64  ? 14.881  46.804 54.747  1.00 50.25  ? 64   GLU B OE1 1 
ATOM   3035  O OE2 . GLU B  2 64  ? 15.139  46.101 52.677  1.00 48.72  ? 64   GLU B OE2 1 
ATOM   3036  N N   . ALA B  2 65  ? 17.679  51.718 55.891  1.00 38.78  ? 65   ALA B N   1 
ATOM   3037  C CA  . ALA B  2 65  ? 17.928  52.405 57.153  1.00 38.80  ? 65   ALA B CA  1 
ATOM   3038  C C   . ALA B  2 65  ? 17.072  51.803 58.266  1.00 41.94  ? 65   ALA B C   1 
ATOM   3039  O O   . ALA B  2 65  ? 15.962  51.322 58.013  1.00 44.51  ? 65   ALA B O   1 
ATOM   3040  C CB  . ALA B  2 65  ? 17.651  53.894 57.014  1.00 38.43  ? 65   ALA B CB  1 
ATOM   3041  N N   . VAL B  2 66  ? 17.604  51.814 59.489  1.00 41.84  ? 66   VAL B N   1 
ATOM   3042  C CA  . VAL B  2 66  ? 16.859  51.386 60.676  1.00 44.97  ? 66   VAL B CA  1 
ATOM   3043  C C   . VAL B  2 66  ? 17.053  52.416 61.788  1.00 44.81  ? 66   VAL B C   1 
ATOM   3044  O O   . VAL B  2 66  ? 18.129  53.015 61.922  1.00 42.20  ? 66   VAL B O   1 
ATOM   3045  C CB  . VAL B  2 66  ? 17.293  49.983 61.172  1.00 45.99  ? 66   VAL B CB  1 
ATOM   3046  C CG1 . VAL B  2 66  ? 16.393  49.502 62.306  1.00 50.01  ? 66   VAL B CG1 1 
ATOM   3047  C CG2 . VAL B  2 66  ? 17.282  48.980 60.022  1.00 45.94  ? 66   VAL B CG2 1 
ATOM   3048  N N   . GLY B  2 67  ? 15.998  52.617 62.575  1.00 47.86  ? 67   GLY B N   1 
ATOM   3049  C CA  . GLY B  2 67  ? 16.006  53.593 63.651  1.00 48.38  ? 67   GLY B CA  1 
ATOM   3050  C C   . GLY B  2 67  ? 16.701  53.052 64.885  1.00 48.22  ? 67   GLY B C   1 
ATOM   3051  O O   . GLY B  2 67  ? 16.351  51.977 65.381  1.00 50.52  ? 67   GLY B O   1 
ATOM   3052  N N   . ARG B  2 68  ? 17.684  53.804 65.376  1.00 45.71  ? 68   ARG B N   1 
ATOM   3053  C CA  . ARG B  2 68  ? 18.455  53.421 66.554  1.00 45.31  ? 68   ARG B CA  1 
ATOM   3054  C C   . ARG B  2 68  ? 18.673  54.648 67.430  1.00 45.12  ? 68   ARG B C   1 
ATOM   3055  O O   . ARG B  2 68  ? 19.043  55.713 66.936  1.00 43.42  ? 68   ARG B O   1 
ATOM   3056  C CB  . ARG B  2 68  ? 19.786  52.785 66.126  1.00 42.33  ? 68   ARG B CB  1 
ATOM   3057  C CG  . ARG B  2 68  ? 19.630  51.323 65.714  1.00 43.34  ? 68   ARG B CG  1 
ATOM   3058  C CD  . ARG B  2 68  ? 20.914  50.634 65.239  1.00 41.00  ? 68   ARG B CD  1 
ATOM   3059  N NE  . ARG B  2 68  ? 20.790  50.311 63.816  1.00 39.98  ? 68   ARG B NE  1 
ATOM   3060  C CZ  . ARG B  2 68  ? 21.364  50.962 62.810  1.00 37.25  ? 68   ARG B CZ  1 
ATOM   3061  N NH1 . ARG B  2 68  ? 22.141  52.010 63.011  1.00 35.34  ? 68   ARG B NH1 1 
ATOM   3062  N NH2 . ARG B  2 68  ? 21.148  50.559 61.571  1.00 36.74  ? 68   ARG B NH2 1 
ATOM   3063  N N   . GLU B  2 69  ? 18.430  54.489 68.727  1.00 47.11  ? 69   GLU B N   1 
ATOM   3064  C CA  . GLU B  2 69  ? 18.416  55.603 69.671  1.00 47.87  ? 69   GLU B CA  1 
ATOM   3065  C C   . GLU B  2 69  ? 19.643  55.564 70.567  1.00 45.90  ? 69   GLU B C   1 
ATOM   3066  O O   . GLU B  2 69  ? 20.086  54.490 70.966  1.00 45.74  ? 69   GLU B O   1 
ATOM   3067  C CB  . GLU B  2 69  ? 17.167  55.519 70.550  1.00 52.31  ? 69   GLU B CB  1 
ATOM   3068  C CG  . GLU B  2 69  ? 15.846  55.573 69.792  1.00 54.97  ? 69   GLU B CG  1 
ATOM   3069  C CD  . GLU B  2 69  ? 15.294  56.982 69.682  1.00 56.43  ? 69   GLU B CD  1 
ATOM   3070  O OE1 . GLU B  2 69  ? 16.027  57.873 69.199  1.00 53.93  ? 69   GLU B OE1 1 
ATOM   3071  O OE2 . GLU B  2 69  ? 14.130  57.193 70.087  1.00 60.59  ? 69   GLU B OE2 1 
ATOM   3072  N N   . PHE B  2 70  ? 20.174  56.739 70.894  1.00 44.74  ? 70   PHE B N   1 
ATOM   3073  C CA  . PHE B  2 70  ? 21.347  56.854 71.762  1.00 43.16  ? 70   PHE B CA  1 
ATOM   3074  C C   . PHE B  2 70  ? 21.163  57.987 72.770  1.00 44.76  ? 70   PHE B C   1 
ATOM   3075  O O   . PHE B  2 70  ? 20.593  59.027 72.446  1.00 45.85  ? 70   PHE B O   1 
ATOM   3076  C CB  . PHE B  2 70  ? 22.599  57.115 70.921  1.00 39.77  ? 70   PHE B CB  1 
ATOM   3077  C CG  . PHE B  2 70  ? 22.771  56.162 69.771  1.00 38.15  ? 70   PHE B CG  1 
ATOM   3078  C CD1 . PHE B  2 70  ? 22.212  56.440 68.529  1.00 37.65  ? 70   PHE B CD1 1 
ATOM   3079  C CD2 . PHE B  2 70  ? 23.492  54.988 69.929  1.00 37.39  ? 70   PHE B CD2 1 
ATOM   3080  C CE1 . PHE B  2 70  ? 22.370  55.564 67.471  1.00 36.31  ? 70   PHE B CE1 1 
ATOM   3081  C CE2 . PHE B  2 70  ? 23.654  54.108 68.872  1.00 36.32  ? 70   PHE B CE2 1 
ATOM   3082  C CZ  . PHE B  2 70  ? 23.092  54.397 67.644  1.00 35.70  ? 70   PHE B CZ  1 
ATOM   3083  N N   . ASN B  2 71  ? 21.654  57.791 73.989  1.00 45.09  ? 71   ASN B N   1 
ATOM   3084  C CA  . ASN B  2 71  ? 21.515  58.812 75.025  1.00 46.86  ? 71   ASN B CA  1 
ATOM   3085  C C   . ASN B  2 71  ? 22.564  59.925 74.874  1.00 44.97  ? 71   ASN B C   1 
ATOM   3086  O O   . ASN B  2 71  ? 23.296  59.967 73.882  1.00 42.41  ? 71   ASN B O   1 
ATOM   3087  C CB  . ASN B  2 71  ? 21.504  58.182 76.434  1.00 48.54  ? 71   ASN B CB  1 
ATOM   3088  C CG  . ASN B  2 71  ? 22.859  57.644 76.863  1.00 46.21  ? 71   ASN B CG  1 
ATOM   3089  O OD1 . ASN B  2 71  ? 23.862  58.356 76.838  1.00 44.41  ? 71   ASN B OD1 1 
ATOM   3090  N ND2 . ASN B  2 71  ? 22.889  56.384 77.286  1.00 46.72  ? 71   ASN B ND2 1 
ATOM   3091  N N   . ASN B  2 72  ? 22.623  60.820 75.858  1.00 46.54  ? 72   ASN B N   1 
ATOM   3092  C CA  . ASN B  2 72  ? 23.409  62.052 75.759  1.00 45.88  ? 72   ASN B CA  1 
ATOM   3093  C C   . ASN B  2 72  ? 24.926  61.857 75.880  1.00 43.17  ? 72   ASN B C   1 
ATOM   3094  O O   . ASN B  2 72  ? 25.699  62.719 75.462  1.00 42.34  ? 72   ASN B O   1 
ATOM   3095  C CB  . ASN B  2 72  ? 22.922  63.053 76.815  1.00 49.12  ? 72   ASN B CB  1 
ATOM   3096  C CG  . ASN B  2 72  ? 23.306  64.485 76.490  1.00 49.77  ? 72   ASN B CG  1 
ATOM   3097  O OD1 . ASN B  2 72  ? 23.198  64.923 75.342  1.00 49.26  ? 72   ASN B OD1 1 
ATOM   3098  N ND2 . ASN B  2 72  ? 23.748  65.226 77.502  1.00 51.21  ? 72   ASN B ND2 1 
ATOM   3099  N N   . LEU B  2 73  ? 25.346  60.736 76.460  1.00 42.27  ? 73   LEU B N   1 
ATOM   3100  C CA  . LEU B  2 73  ? 26.763  60.386 76.544  1.00 40.11  ? 73   LEU B CA  1 
ATOM   3101  C C   . LEU B  2 73  ? 27.075  59.172 75.664  1.00 38.17  ? 73   LEU B C   1 
ATOM   3102  O O   . LEU B  2 73  ? 27.913  58.336 76.003  1.00 37.35  ? 73   LEU B O   1 
ATOM   3103  C CB  . LEU B  2 73  ? 27.158  60.136 77.999  1.00 41.08  ? 73   LEU B CB  1 
ATOM   3104  C CG  . LEU B  2 73  ? 27.150  61.387 78.892  1.00 42.89  ? 73   LEU B CG  1 
ATOM   3105  C CD1 . LEU B  2 73  ? 27.133  61.003 80.365  1.00 44.33  ? 73   LEU B CD1 1 
ATOM   3106  C CD2 . LEU B  2 73  ? 28.338  62.290 78.580  1.00 41.83  ? 73   LEU B CD2 1 
ATOM   3107  N N   . GLU B  2 74  ? 26.380  59.096 74.531  1.00 37.76  ? 74   GLU B N   1 
ATOM   3108  C CA  . GLU B  2 74  ? 26.656  58.123 73.481  1.00 36.02  ? 74   GLU B CA  1 
ATOM   3109  C C   . GLU B  2 74  ? 26.689  58.838 72.132  1.00 34.85  ? 74   GLU B C   1 
ATOM   3110  O O   . GLU B  2 74  ? 26.202  58.321 71.131  1.00 34.23  ? 74   GLU B O   1 
ATOM   3111  C CB  . GLU B  2 74  ? 25.583  57.042 73.474  1.00 37.20  ? 74   GLU B CB  1 
ATOM   3112  C CG  . GLU B  2 74  ? 25.636  56.132 74.678  1.00 38.51  ? 74   GLU B CG  1 
ATOM   3113  C CD  . GLU B  2 74  ? 24.695  54.963 74.545  1.00 40.02  ? 74   GLU B CD  1 
ATOM   3114  O OE1 . GLU B  2 74  ? 23.490  55.197 74.334  1.00 41.62  ? 74   GLU B OE1 1 
ATOM   3115  O OE2 . GLU B  2 74  ? 25.166  53.815 74.647  1.00 39.99  ? 74   GLU B OE2 1 
ATOM   3116  N N   . ARG B  2 75  ? 27.267  60.036 72.122  1.00 34.84  ? 75   ARG B N   1 
ATOM   3117  C CA  . ARG B  2 75  ? 27.244  60.907 70.948  1.00 34.39  ? 75   ARG B CA  1 
ATOM   3118  C C   . ARG B  2 75  ? 28.153  60.410 69.837  1.00 32.24  ? 75   ARG B C   1 
ATOM   3119  O O   . ARG B  2 75  ? 27.853  60.598 68.654  1.00 31.59  ? 75   ARG B O   1 
ATOM   3120  C CB  . ARG B  2 75  ? 27.642  62.332 71.334  1.00 35.67  ? 75   ARG B CB  1 
ATOM   3121  C CG  . ARG B  2 75  ? 26.584  63.066 72.135  1.00 38.38  ? 75   ARG B CG  1 
ATOM   3122  C CD  . ARG B  2 75  ? 25.603  63.787 71.231  1.00 39.65  ? 75   ARG B CD  1 
ATOM   3123  N NE  . ARG B  2 75  ? 24.395  64.186 71.958  1.00 42.70  ? 75   ARG B NE  1 
ATOM   3124  C CZ  . ARG B  2 75  ? 23.281  63.455 72.067  1.00 43.74  ? 75   ARG B CZ  1 
ATOM   3125  N NH1 . ARG B  2 75  ? 23.187  62.254 71.493  1.00 41.95  ? 75   ARG B NH1 1 
ATOM   3126  N NH2 . ARG B  2 75  ? 22.245  63.932 72.762  1.00 47.02  ? 75   ARG B NH2 1 
ATOM   3127  N N   . ARG B  2 76  ? 29.269  59.792 70.214  1.00 31.42  ? 76   ARG B N   1 
ATOM   3128  C CA  . ARG B  2 76  ? 30.207  59.252 69.233  1.00 29.90  ? 76   ARG B CA  1 
ATOM   3129  C C   . ARG B  2 76  ? 29.566  58.161 68.384  1.00 29.17  ? 76   ARG B C   1 
ATOM   3130  O O   . ARG B  2 76  ? 29.630  58.218 67.160  1.00 28.19  ? 76   ARG B O   1 
ATOM   3131  C CB  . ARG B  2 76  ? 31.446  58.691 69.918  1.00 29.81  ? 76   ARG B CB  1 
ATOM   3132  C CG  . ARG B  2 76  ? 32.386  59.738 70.483  1.00 30.49  ? 76   ARG B CG  1 
ATOM   3133  C CD  . ARG B  2 76  ? 33.450  59.056 71.320  1.00 30.78  ? 76   ARG B CD  1 
ATOM   3134  N NE  . ARG B  2 76  ? 32.851  58.367 72.463  1.00 31.42  ? 76   ARG B NE  1 
ATOM   3135  C CZ  . ARG B  2 76  ? 33.421  57.385 73.160  1.00 31.79  ? 76   ARG B CZ  1 
ATOM   3136  N NH1 . ARG B  2 76  ? 34.632  56.934 72.850  1.00 31.70  ? 76   ARG B NH1 1 
ATOM   3137  N NH2 . ARG B  2 76  ? 32.766  56.845 74.180  1.00 32.67  ? 76   ARG B NH2 1 
ATOM   3138  N N   . ILE B  2 77  ? 28.958  57.171 69.037  1.00 29.92  ? 77   ILE B N   1 
ATOM   3139  C CA  . ILE B  2 77  ? 28.304  56.076 68.314  1.00 29.82  ? 77   ILE B CA  1 
ATOM   3140  C C   . ILE B  2 77  ? 27.029  56.521 67.596  1.00 30.16  ? 77   ILE B C   1 
ATOM   3141  O O   . ILE B  2 77  ? 26.679  55.966 66.557  1.00 29.61  ? 77   ILE B O   1 
ATOM   3142  C CB  . ILE B  2 77  ? 28.017  54.844 69.203  1.00 31.13  ? 77   ILE B CB  1 
ATOM   3143  C CG1 . ILE B  2 77  ? 27.065  55.178 70.350  1.00 32.93  ? 77   ILE B CG1 1 
ATOM   3144  C CG2 . ILE B  2 77  ? 29.323  54.276 69.738  1.00 31.03  ? 77   ILE B CG2 1 
ATOM   3145  C CD1 . ILE B  2 77  ? 26.522  53.951 71.054  1.00 34.74  ? 77   ILE B CD1 1 
ATOM   3146  N N   . GLU B  2 78  ? 26.345  57.521 68.141  1.00 31.38  ? 78   GLU B N   1 
ATOM   3147  C CA  . GLU B  2 78  ? 25.217  58.131 67.447  1.00 32.13  ? 78   GLU B CA  1 
ATOM   3148  C C   . GLU B  2 78  ? 25.687  58.745 66.137  1.00 30.62  ? 78   GLU B C   1 
ATOM   3149  O O   . GLU B  2 78  ? 25.026  58.622 65.113  1.00 30.37  ? 78   GLU B O   1 
ATOM   3150  C CB  . GLU B  2 78  ? 24.563  59.209 68.312  1.00 34.21  ? 78   GLU B CB  1 
ATOM   3151  C CG  . GLU B  2 78  ? 23.388  59.918 67.651  1.00 35.64  ? 78   GLU B CG  1 
ATOM   3152  C CD  . GLU B  2 78  ? 22.580  60.748 68.634  1.00 38.56  ? 78   GLU B CD  1 
ATOM   3153  O OE1 . GLU B  2 78  ? 23.177  61.615 69.317  1.00 39.03  ? 78   GLU B OE1 1 
ATOM   3154  O OE2 . GLU B  2 78  ? 21.347  60.536 68.723  1.00 40.74  ? 78   GLU B OE2 1 
ATOM   3155  N N   . ASN B  2 79  ? 26.835  59.407 66.184  1.00 29.89  ? 79   ASN B N   1 
ATOM   3156  C CA  . ASN B  2 79  ? 27.393  60.060 65.014  1.00 28.93  ? 79   ASN B CA  1 
ATOM   3157  C C   . ASN B  2 79  ? 27.954  59.053 64.010  1.00 27.26  ? 79   ASN B C   1 
ATOM   3158  O O   . ASN B  2 79  ? 27.819  59.232 62.800  1.00 26.56  ? 79   ASN B O   1 
ATOM   3159  C CB  . ASN B  2 79  ? 28.482  61.035 65.448  1.00 29.30  ? 79   ASN B CB  1 
ATOM   3160  C CG  . ASN B  2 79  ? 29.067  61.796 64.286  1.00 28.91  ? 79   ASN B CG  1 
ATOM   3161  O OD1 . ASN B  2 79  ? 28.458  62.731 63.771  1.00 29.88  ? 79   ASN B OD1 1 
ATOM   3162  N ND2 . ASN B  2 79  ? 30.244  61.387 63.854  1.00 27.90  ? 79   ASN B ND2 1 
ATOM   3163  N N   . LEU B  2 80  ? 28.593  58.005 64.522  1.00 26.95  ? 80   LEU B N   1 
ATOM   3164  C CA  . LEU B  2 80  ? 29.064  56.889 63.700  1.00 26.00  ? 80   LEU B CA  1 
ATOM   3165  C C   . LEU B  2 80  ? 27.877  56.289 62.973  1.00 26.05  ? 80   LEU B C   1 
ATOM   3166  O O   . LEU B  2 80  ? 27.924  56.065 61.767  1.00 25.18  ? 80   LEU B O   1 
ATOM   3167  C CB  . LEU B  2 80  ? 29.731  55.826 64.583  1.00 26.46  ? 80   LEU B CB  1 
ATOM   3168  C CG  . LEU B  2 80  ? 30.519  54.654 63.980  1.00 26.18  ? 80   LEU B CG  1 
ATOM   3169  C CD1 . LEU B  2 80  ? 31.242  53.906 65.092  1.00 27.22  ? 80   LEU B CD1 1 
ATOM   3170  C CD2 . LEU B  2 80  ? 29.639  53.688 63.204  1.00 26.26  ? 80   LEU B CD2 1 
ATOM   3171  N N   . ASN B  2 81  ? 26.811  56.038 63.720  1.00 27.40  ? 81   ASN B N   1 
ATOM   3172  C CA  . ASN B  2 81  ? 25.586  55.500 63.160  1.00 28.12  ? 81   ASN B CA  1 
ATOM   3173  C C   . ASN B  2 81  ? 25.010  56.366 62.040  1.00 27.78  ? 81   ASN B C   1 
ATOM   3174  O O   . ASN B  2 81  ? 24.612  55.844 61.006  1.00 27.34  ? 81   ASN B O   1 
ATOM   3175  C CB  . ASN B  2 81  ? 24.543  55.335 64.256  1.00 30.18  ? 81   ASN B CB  1 
ATOM   3176  C CG  . ASN B  2 81  ? 23.261  54.745 63.739  1.00 31.44  ? 81   ASN B CG  1 
ATOM   3177  O OD1 . ASN B  2 81  ? 23.276  53.686 63.128  1.00 31.29  ? 81   ASN B OD1 1 
ATOM   3178  N ND2 . ASN B  2 81  ? 22.147  55.419 63.972  1.00 33.11  ? 81   ASN B ND2 1 
ATOM   3179  N N   . LYS B  2 82  ? 24.971  57.680 62.250  1.00 28.32  ? 82   LYS B N   1 
ATOM   3180  C CA  . LYS B  2 82  ? 24.419  58.598 61.256  1.00 28.54  ? 82   LYS B CA  1 
ATOM   3181  C C   . LYS B  2 82  ? 25.231  58.549 59.977  1.00 26.84  ? 82   LYS B C   1 
ATOM   3182  O O   . LYS B  2 82  ? 24.674  58.386 58.892  1.00 26.48  ? 82   LYS B O   1 
ATOM   3183  C CB  . LYS B  2 82  ? 24.371  60.041 61.773  1.00 29.86  ? 82   LYS B CB  1 
ATOM   3184  C CG  . LYS B  2 82  ? 23.915  61.043 60.711  1.00 30.38  ? 82   LYS B CG  1 
ATOM   3185  C CD  . LYS B  2 82  ? 23.481  62.384 61.294  1.00 32.77  ? 82   LYS B CD  1 
ATOM   3186  C CE  . LYS B  2 82  ? 24.616  63.407 61.326  1.00 32.76  ? 82   LYS B CE  1 
ATOM   3187  N NZ  . LYS B  2 82  ? 24.263  64.620 62.125  1.00 35.50  ? 82   LYS B NZ  1 
ATOM   3188  N N   . LYS B  2 83  ? 26.546  58.691 60.117  1.00 26.15  ? 83   LYS B N   1 
ATOM   3189  C CA  . LYS B  2 83  ? 27.461  58.639 58.972  1.00 25.00  ? 83   LYS B CA  1 
ATOM   3190  C C   . LYS B  2 83  ? 27.390  57.322 58.215  1.00 24.17  ? 83   LYS B C   1 
ATOM   3191  O O   . LYS B  2 83  ? 27.478  57.304 56.988  1.00 23.43  ? 83   LYS B O   1 
ATOM   3192  C CB  . LYS B  2 83  ? 28.902  58.925 59.420  1.00 24.98  ? 83   LYS B CB  1 
ATOM   3193  C CG  . LYS B  2 83  ? 29.304  60.397 59.366  1.00 25.86  ? 83   LYS B CG  1 
ATOM   3194  C CD  . LYS B  2 83  ? 28.149  61.360 59.650  1.00 27.22  ? 83   LYS B CD  1 
ATOM   3195  C CE  . LYS B  2 83  ? 28.558  62.817 59.479  1.00 28.57  ? 83   LYS B CE  1 
ATOM   3196  N NZ  . LYS B  2 83  ? 29.023  63.413 60.763  1.00 29.91  ? 83   LYS B NZ  1 
ATOM   3197  N N   . MET B  2 84  ? 27.221  56.225 58.939  1.00 24.70  ? 84   MET B N   1 
ATOM   3198  C CA  . MET B  2 84  ? 27.070  54.926 58.304  1.00 24.61  ? 84   MET B CA  1 
ATOM   3199  C C   . MET B  2 84  ? 25.814  54.902 57.440  1.00 24.76  ? 84   MET B C   1 
ATOM   3200  O O   . MET B  2 84  ? 25.881  54.544 56.264  1.00 23.99  ? 84   MET B O   1 
ATOM   3201  C CB  . MET B  2 84  ? 27.005  53.813 59.348  1.00 25.80  ? 84   MET B CB  1 
ATOM   3202  C CG  . MET B  2 84  ? 27.267  52.432 58.773  1.00 26.15  ? 84   MET B CG  1 
ATOM   3203  S SD  . MET B  2 84  ? 26.148  51.195 59.438  1.00 28.42  ? 84   MET B SD  1 
ATOM   3204  C CE  . MET B  2 84  ? 24.646  51.646 58.584  1.00 28.53  ? 84   MET B CE  1 
ATOM   3205  N N   . GLU B  2 85  ? 24.679  55.299 58.020  1.00 26.01  ? 85   GLU B N   1 
ATOM   3206  C CA  . GLU B  2 85  ? 23.403  55.272 57.303  1.00 26.74  ? 85   GLU B CA  1 
ATOM   3207  C C   . GLU B  2 85  ? 23.421  56.244 56.123  1.00 25.74  ? 85   GLU B C   1 
ATOM   3208  O O   . GLU B  2 85  ? 23.058  55.876 55.012  1.00 25.27  ? 85   GLU B O   1 
ATOM   3209  C CB  . GLU B  2 85  ? 22.220  55.567 58.236  1.00 28.94  ? 85   GLU B CB  1 
ATOM   3210  C CG  . GLU B  2 85  ? 22.121  54.628 59.439  1.00 30.38  ? 85   GLU B CG  1 
ATOM   3211  C CD  . GLU B  2 85  ? 20.742  54.009 59.636  1.00 32.90  ? 85   GLU B CD  1 
ATOM   3212  O OE1 . GLU B  2 85  ? 19.874  54.651 60.269  1.00 34.84  ? 85   GLU B OE1 1 
ATOM   3213  O OE2 . GLU B  2 85  ? 20.536  52.861 59.183  1.00 33.41  ? 85   GLU B OE2 1 
ATOM   3214  N N   . ASP B  2 86  ? 23.864  57.473 56.367  1.00 25.66  ? 86   ASP B N   1 
ATOM   3215  C CA  . ASP B  2 86  ? 23.999  58.474 55.304  1.00 25.15  ? 86   ASP B CA  1 
ATOM   3216  C C   . ASP B  2 86  ? 24.971  58.065 54.210  1.00 23.45  ? 86   ASP B C   1 
ATOM   3217  O O   . ASP B  2 86  ? 24.726  58.322 53.031  1.00 23.03  ? 86   ASP B O   1 
ATOM   3218  C CB  . ASP B  2 86  ? 24.455  59.822 55.877  1.00 25.97  ? 86   ASP B CB  1 
ATOM   3219  C CG  . ASP B  2 86  ? 23.300  60.735 56.195  1.00 28.10  ? 86   ASP B CG  1 
ATOM   3220  O OD1 . ASP B  2 86  ? 22.388  60.842 55.341  1.00 28.77  ? 86   ASP B OD1 1 
ATOM   3221  O OD2 . ASP B  2 86  ? 23.306  61.353 57.283  1.00 29.47  ? 86   ASP B OD2 1 
ATOM   3222  N N   . GLY B  2 87  ? 26.083  57.459 54.611  1.00 22.78  ? 87   GLY B N   1 
ATOM   3223  C CA  . GLY B  2 87  ? 27.114  57.036 53.674  1.00 21.73  ? 87   GLY B CA  1 
ATOM   3224  C C   . GLY B  2 87  ? 26.611  56.039 52.646  1.00 21.25  ? 87   GLY B C   1 
ATOM   3225  O O   . GLY B  2 87  ? 26.941  56.142 51.460  1.00 20.57  ? 87   GLY B O   1 
ATOM   3226  N N   . PHE B  2 88  ? 25.811  55.076 53.104  1.00 21.87  ? 88   PHE B N   1 
ATOM   3227  C CA  . PHE B  2 88  ? 25.215  54.078 52.218  1.00 21.87  ? 88   PHE B CA  1 
ATOM   3228  C C   . PHE B  2 88  ? 24.158  54.683 51.289  1.00 21.85  ? 88   PHE B C   1 
ATOM   3229  O O   . PHE B  2 88  ? 24.030  54.256 50.139  1.00 21.35  ? 88   PHE B O   1 
ATOM   3230  C CB  . PHE B  2 88  ? 24.610  52.921 53.023  1.00 23.22  ? 88   PHE B CB  1 
ATOM   3231  C CG  . PHE B  2 88  ? 25.625  51.927 53.524  1.00 23.55  ? 88   PHE B CG  1 
ATOM   3232  C CD1 . PHE B  2 88  ? 26.434  51.232 52.637  1.00 23.23  ? 88   PHE B CD1 1 
ATOM   3233  C CD2 . PHE B  2 88  ? 25.763  51.674 54.879  1.00 24.55  ? 88   PHE B CD2 1 
ATOM   3234  C CE1 . PHE B  2 88  ? 27.366  50.312 53.090  1.00 24.11  ? 88   PHE B CE1 1 
ATOM   3235  C CE2 . PHE B  2 88  ? 26.692  50.753 55.340  1.00 25.24  ? 88   PHE B CE2 1 
ATOM   3236  C CZ  . PHE B  2 88  ? 27.495  50.072 54.443  1.00 25.14  ? 88   PHE B CZ  1 
ATOM   3237  N N   . LEU B  2 89  ? 23.406  55.669 51.776  1.00 22.63  ? 89   LEU B N   1 
ATOM   3238  C CA  . LEU B  2 89  ? 22.441  56.369 50.924  1.00 23.06  ? 89   LEU B CA  1 
ATOM   3239  C C   . LEU B  2 89  ? 23.115  57.107 49.775  1.00 21.84  ? 89   LEU B C   1 
ATOM   3240  O O   . LEU B  2 89  ? 22.582  57.146 48.674  1.00 21.65  ? 89   LEU B O   1 
ATOM   3241  C CB  . LEU B  2 89  ? 21.612  57.365 51.727  1.00 24.77  ? 89   LEU B CB  1 
ATOM   3242  C CG  . LEU B  2 89  ? 20.684  56.753 52.775  1.00 26.63  ? 89   LEU B CG  1 
ATOM   3243  C CD1 . LEU B  2 89  ? 19.996  57.862 53.566  1.00 28.57  ? 89   LEU B CD1 1 
ATOM   3244  C CD2 . LEU B  2 89  ? 19.675  55.801 52.135  1.00 27.49  ? 89   LEU B CD2 1 
ATOM   3245  N N   . ASP B  2 90  ? 24.276  57.697 50.034  1.00 21.29  ? 90   ASP B N   1 
ATOM   3246  C CA  . ASP B  2 90  ? 25.033  58.380 48.985  1.00 20.62  ? 90   ASP B CA  1 
ATOM   3247  C C   . ASP B  2 90  ? 25.568  57.396 47.962  1.00 19.48  ? 90   ASP B C   1 
ATOM   3248  O O   . ASP B  2 90  ? 25.571  57.685 46.763  1.00 19.10  ? 90   ASP B O   1 
ATOM   3249  C CB  . ASP B  2 90  ? 26.194  59.173 49.577  1.00 20.92  ? 90   ASP B CB  1 
ATOM   3250  C CG  . ASP B  2 90  ? 25.728  60.317 50.443  1.00 22.37  ? 90   ASP B CG  1 
ATOM   3251  O OD1 . ASP B  2 90  ? 24.531  60.674 50.364  1.00 23.27  ? 90   ASP B OD1 1 
ATOM   3252  O OD2 . ASP B  2 90  ? 26.563  60.853 51.205  1.00 22.93  ? 90   ASP B OD2 1 
ATOM   3253  N N   . VAL B  2 91  ? 26.028  56.242 48.438  1.00 19.19  ? 91   VAL B N   1 
ATOM   3254  C CA  . VAL B  2 91  ? 26.520  55.191 47.554  1.00 18.63  ? 91   VAL B CA  1 
ATOM   3255  C C   . VAL B  2 91  ? 25.399  54.672 46.657  1.00 18.49  ? 91   VAL B C   1 
ATOM   3256  O O   . VAL B  2 91  ? 25.580  54.555 45.444  1.00 17.98  ? 91   VAL B O   1 
ATOM   3257  C CB  . VAL B  2 91  ? 27.150  54.024 48.347  1.00 19.14  ? 91   VAL B CB  1 
ATOM   3258  C CG1 . VAL B  2 91  ? 27.365  52.805 47.458  1.00 19.30  ? 91   VAL B CG1 1 
ATOM   3259  C CG2 . VAL B  2 91  ? 28.470  54.463 48.967  1.00 19.32  ? 91   VAL B CG2 1 
ATOM   3260  N N   . TRP B  2 92  ? 24.248  54.362 47.246  1.00 19.17  ? 92   TRP B N   1 
ATOM   3261  C CA  . TRP B  2 92  ? 23.134  53.825 46.467  1.00 19.50  ? 92   TRP B CA  1 
ATOM   3262  C C   . TRP B  2 92  ? 22.450  54.882 45.603  1.00 19.24  ? 92   TRP B C   1 
ATOM   3263  O O   . TRP B  2 92  ? 21.967  54.570 44.517  1.00 19.07  ? 92   TRP B O   1 
ATOM   3264  C CB  . TRP B  2 92  ? 22.133  53.100 47.367  1.00 21.05  ? 92   TRP B CB  1 
ATOM   3265  C CG  . TRP B  2 92  ? 22.652  51.764 47.789  1.00 21.66  ? 92   TRP B CG  1 
ATOM   3266  C CD1 . TRP B  2 92  ? 23.044  51.388 49.042  1.00 22.43  ? 92   TRP B CD1 1 
ATOM   3267  C CD2 . TRP B  2 92  ? 22.875  50.633 46.944  1.00 21.91  ? 92   TRP B CD2 1 
ATOM   3268  N NE1 . TRP B  2 92  ? 23.479  50.085 49.032  1.00 23.29  ? 92   TRP B NE1 1 
ATOM   3269  C CE2 . TRP B  2 92  ? 23.386  49.599 47.754  1.00 23.09  ? 92   TRP B CE2 1 
ATOM   3270  C CE3 . TRP B  2 92  ? 22.677  50.388 45.581  1.00 21.50  ? 92   TRP B CE3 1 
ATOM   3271  C CZ2 . TRP B  2 92  ? 23.703  48.337 47.246  1.00 24.15  ? 92   TRP B CZ2 1 
ATOM   3272  C CZ3 . TRP B  2 92  ? 22.992  49.134 45.078  1.00 22.35  ? 92   TRP B CZ3 1 
ATOM   3273  C CH2 . TRP B  2 92  ? 23.499  48.125 45.909  1.00 23.78  ? 92   TRP B CH2 1 
ATOM   3274  N N   . THR B  2 93  ? 22.421  56.127 46.071  1.00 19.42  ? 93   THR B N   1 
ATOM   3275  C CA  . THR B  2 93  ? 21.928  57.229 45.249  1.00 19.58  ? 93   THR B CA  1 
ATOM   3276  C C   . THR B  2 93  ? 22.828  57.399 44.023  1.00 18.32  ? 93   THR B C   1 
ATOM   3277  O O   . THR B  2 93  ? 22.337  57.544 42.903  1.00 18.25  ? 93   THR B O   1 
ATOM   3278  C CB  . THR B  2 93  ? 21.872  58.555 46.031  1.00 20.61  ? 93   THR B CB  1 
ATOM   3279  O OG1 . THR B  2 93  ? 20.976  58.419 47.138  1.00 22.04  ? 93   THR B OG1 1 
ATOM   3280  C CG2 . THR B  2 93  ? 21.384  59.685 45.144  1.00 21.39  ? 93   THR B CG2 1 
ATOM   3281  N N   . TYR B  2 94  ? 24.137  57.382 44.247  1.00 17.59  ? 94   TYR B N   1 
ATOM   3282  C CA  . TYR B  2 94  ? 25.113  57.523 43.171  1.00 16.89  ? 94   TYR B CA  1 
ATOM   3283  C C   . TYR B  2 94  ? 24.982  56.406 42.135  1.00 16.21  ? 94   TYR B C   1 
ATOM   3284  O O   . TYR B  2 94  ? 24.999  56.662 40.935  1.00 15.87  ? 94   TYR B O   1 
ATOM   3285  C CB  . TYR B  2 94  ? 26.526  57.551 43.756  1.00 16.90  ? 94   TYR B CB  1 
ATOM   3286  C CG  . TYR B  2 94  ? 27.643  57.374 42.753  1.00 16.70  ? 94   TYR B CG  1 
ATOM   3287  C CD1 . TYR B  2 94  ? 28.114  56.105 42.423  1.00 16.43  ? 94   TYR B CD1 1 
ATOM   3288  C CD2 . TYR B  2 94  ? 28.244  58.472 42.150  1.00 17.26  ? 94   TYR B CD2 1 
ATOM   3289  C CE1 . TYR B  2 94  ? 29.141  55.938 41.513  1.00 16.68  ? 94   TYR B CE1 1 
ATOM   3290  C CE2 . TYR B  2 94  ? 29.271  58.310 41.235  1.00 17.51  ? 94   TYR B CE2 1 
ATOM   3291  C CZ  . TYR B  2 94  ? 29.714  57.043 40.923  1.00 17.17  ? 94   TYR B CZ  1 
ATOM   3292  O OH  . TYR B  2 94  ? 30.735  56.877 40.021  1.00 17.86  ? 94   TYR B OH  1 
ATOM   3293  N N   . ASN B  2 95  ? 24.844  55.175 42.613  1.00 16.29  ? 95   ASN B N   1 
ATOM   3294  C CA  . ASN B  2 95  ? 24.686  54.009 41.744  1.00 16.19  ? 95   ASN B CA  1 
ATOM   3295  C C   . ASN B  2 95  ? 23.486  54.117 40.824  1.00 16.19  ? 95   ASN B C   1 
ATOM   3296  O O   . ASN B  2 95  ? 23.588  53.853 39.620  1.00 15.80  ? 95   ASN B O   1 
ATOM   3297  C CB  . ASN B  2 95  ? 24.547  52.736 42.580  1.00 17.01  ? 95   ASN B CB  1 
ATOM   3298  C CG  . ASN B  2 95  ? 25.848  52.332 43.236  1.00 17.30  ? 95   ASN B CG  1 
ATOM   3299  O OD1 . ASN B  2 95  ? 26.901  52.900 42.945  1.00 16.97  ? 95   ASN B OD1 1 
ATOM   3300  N ND2 . ASN B  2 95  ? 25.786  51.346 44.127  1.00 18.29  ? 95   ASN B ND2 1 
ATOM   3301  N N   . ALA B  2 96  ? 22.353  54.493 41.408  1.00 16.86  ? 96   ALA B N   1 
ATOM   3302  C CA  . ALA B  2 96  ? 21.104  54.654 40.676  1.00 17.35  ? 96   ALA B CA  1 
ATOM   3303  C C   . ALA B  2 96  ? 21.213  55.740 39.613  1.00 16.76  ? 96   ALA B C   1 
ATOM   3304  O O   . ALA B  2 96  ? 20.869  55.514 38.461  1.00 16.54  ? 96   ALA B O   1 
ATOM   3305  C CB  . ALA B  2 96  ? 19.976  54.989 41.640  1.00 18.82  ? 96   ALA B CB  1 
ATOM   3306  N N   . GLU B  2 97  ? 21.690  56.915 40.003  1.00 16.78  ? 97   GLU B N   1 
ATOM   3307  C CA  . GLU B  2 97  ? 21.752  58.050 39.079  1.00 16.88  ? 97   GLU B CA  1 
ATOM   3308  C C   . GLU B  2 97  ? 22.762  57.825 37.957  1.00 15.81  ? 97   GLU B C   1 
ATOM   3309  O O   . GLU B  2 97  ? 22.517  58.212 36.816  1.00 15.86  ? 97   GLU B O   1 
ATOM   3310  C CB  . GLU B  2 97  ? 22.070  59.343 39.829  1.00 17.85  ? 97   GLU B CB  1 
ATOM   3311  C CG  . GLU B  2 97  ? 20.965  59.769 40.783  1.00 19.38  ? 97   GLU B CG  1 
ATOM   3312  C CD  . GLU B  2 97  ? 21.221  61.108 41.448  1.00 20.78  ? 97   GLU B CD  1 
ATOM   3313  O OE1 . GLU B  2 97  ? 22.265  61.738 41.172  1.00 20.67  ? 97   GLU B OE1 1 
ATOM   3314  O OE2 . GLU B  2 97  ? 20.364  61.538 42.247  1.00 22.43  ? 97   GLU B OE2 1 
ATOM   3315  N N   . LEU B  2 98  ? 23.887  57.191 38.281  1.00 15.14  ? 98   LEU B N   1 
ATOM   3316  C CA  . LEU B  2 98  ? 24.910  56.893 37.293  1.00 14.59  ? 98   LEU B CA  1 
ATOM   3317  C C   . LEU B  2 98  ? 24.432  55.833 36.316  1.00 14.07  ? 98   LEU B C   1 
ATOM   3318  O O   . LEU B  2 98  ? 24.606  55.977 35.115  1.00 13.86  ? 98   LEU B O   1 
ATOM   3319  C CB  . LEU B  2 98  ? 26.193  56.415 37.965  1.00 14.68  ? 98   LEU B CB  1 
ATOM   3320  C CG  . LEU B  2 98  ? 27.397  56.269 37.028  1.00 14.90  ? 98   LEU B CG  1 
ATOM   3321  C CD1 . LEU B  2 98  ? 27.867  57.628 36.536  1.00 15.57  ? 98   LEU B CD1 1 
ATOM   3322  C CD2 . LEU B  2 98  ? 28.529  55.542 37.729  1.00 15.44  ? 98   LEU B CD2 1 
ATOM   3323  N N   . LEU B  2 99  ? 23.832  54.770 36.834  1.00 14.11  ? 99   LEU B N   1 
ATOM   3324  C CA  . LEU B  2 99  ? 23.339  53.691 35.984  1.00 14.10  ? 99   LEU B CA  1 
ATOM   3325  C C   . LEU B  2 99  ? 22.313  54.205 34.982  1.00 13.96  ? 99   LEU B C   1 
ATOM   3326  O O   . LEU B  2 99  ? 22.359  53.857 33.807  1.00 13.69  ? 99   LEU B O   1 
ATOM   3327  C CB  . LEU B  2 99  ? 22.718  52.577 36.826  1.00 14.91  ? 99   LEU B CB  1 
ATOM   3328  C CG  . LEU B  2 99  ? 22.287  51.315 36.072  1.00 15.57  ? 99   LEU B CG  1 
ATOM   3329  C CD1 . LEU B  2 99  ? 23.464  50.686 35.342  1.00 15.54  ? 99   LEU B CD1 1 
ATOM   3330  C CD2 . LEU B  2 99  ? 21.658  50.311 37.022  1.00 16.95  ? 99   LEU B CD2 1 
ATOM   3331  N N   . VAL B  2 100 ? 21.387  55.035 35.451  1.00 14.38  ? 100  VAL B N   1 
ATOM   3332  C CA  . VAL B  2 100 ? 20.393  55.642 34.571  1.00 14.71  ? 100  VAL B CA  1 
ATOM   3333  C C   . VAL B  2 100 ? 21.080  56.472 33.473  1.00 14.15  ? 100  VAL B C   1 
ATOM   3334  O O   . VAL B  2 100 ? 20.801  56.282 32.297  1.00 13.95  ? 100  VAL B O   1 
ATOM   3335  C CB  . VAL B  2 100 ? 19.366  56.484 35.369  1.00 15.97  ? 100  VAL B CB  1 
ATOM   3336  C CG1 . VAL B  2 100 ? 18.546  57.386 34.452  1.00 16.78  ? 100  VAL B CG1 1 
ATOM   3337  C CG2 . VAL B  2 100 ? 18.447  55.568 36.162  1.00 16.95  ? 100  VAL B CG2 1 
ATOM   3338  N N   . LEU B  2 101 ? 21.980  57.368 33.868  1.00 14.13  ? 101  LEU B N   1 
ATOM   3339  C CA  . LEU B  2 101 ? 22.761  58.181 32.926  1.00 14.14  ? 101  LEU B CA  1 
ATOM   3340  C C   . LEU B  2 101 ? 23.509  57.363 31.865  1.00 13.42  ? 101  LEU B C   1 
ATOM   3341  O O   . LEU B  2 101 ? 23.452  57.673 30.671  1.00 13.49  ? 101  LEU B O   1 
ATOM   3342  C CB  . LEU B  2 101 ? 23.781  59.026 33.694  1.00 14.71  ? 101  LEU B CB  1 
ATOM   3343  C CG  . LEU B  2 101 ? 23.564  60.535 33.810  1.00 16.16  ? 101  LEU B CG  1 
ATOM   3344  C CD1 . LEU B  2 101 ? 22.108  60.925 34.017  1.00 17.01  ? 101  LEU B CD1 1 
ATOM   3345  C CD2 . LEU B  2 101 ? 24.429  61.065 34.941  1.00 16.80  ? 101  LEU B CD2 1 
ATOM   3346  N N   . MET B  2 102 ? 24.219  56.331 32.312  1.00 12.99  ? 102  MET B N   1 
ATOM   3347  C CA  . MET B  2 102 ? 25.030  55.511 31.427  1.00 12.85  ? 102  MET B CA  1 
ATOM   3348  C C   . MET B  2 102 ? 24.169  54.671 30.498  1.00 12.53  ? 102  MET B C   1 
ATOM   3349  O O   . MET B  2 102 ? 24.456  54.560 29.302  1.00 12.54  ? 102  MET B O   1 
ATOM   3350  C CB  . MET B  2 102 ? 25.954  54.602 32.238  1.00 13.15  ? 102  MET B CB  1 
ATOM   3351  C CG  . MET B  2 102 ? 27.066  55.344 32.966  1.00 13.71  ? 102  MET B CG  1 
ATOM   3352  S SD  . MET B  2 102 ? 28.353  54.262 33.629  1.00 14.57  ? 102  MET B SD  1 
ATOM   3353  C CE  . MET B  2 102 ? 27.374  53.158 34.655  1.00 14.24  ? 102  MET B CE  1 
ATOM   3354  N N   . GLU B  2 103 ? 23.115  54.076 31.048  1.00 12.51  ? 103  GLU B N   1 
ATOM   3355  C CA  . GLU B  2 103 ? 22.257  53.189 30.273  1.00 12.63  ? 103  GLU B CA  1 
ATOM   3356  C C   . GLU B  2 103 ? 21.268  53.941 29.384  1.00 12.56  ? 103  GLU B C   1 
ATOM   3357  O O   . GLU B  2 103 ? 20.883  53.434 28.337  1.00 12.60  ? 103  GLU B O   1 
ATOM   3358  C CB  . GLU B  2 103 ? 21.543  52.197 31.188  1.00 13.32  ? 103  GLU B CB  1 
ATOM   3359  C CG  . GLU B  2 103 ? 22.467  51.137 31.786  1.00 13.81  ? 103  GLU B CG  1 
ATOM   3360  C CD  . GLU B  2 103 ? 23.107  50.212 30.752  1.00 14.25  ? 103  GLU B CD  1 
ATOM   3361  O OE1 . GLU B  2 103 ? 22.648  50.171 29.597  1.00 14.14  ? 103  GLU B OE1 1 
ATOM   3362  O OE2 . GLU B  2 103 ? 24.087  49.515 31.090  1.00 14.98  ? 103  GLU B OE2 1 
ATOM   3363  N N   . ASN B  2 104 ? 20.870  55.147 29.784  1.00 12.72  ? 104  ASN B N   1 
ATOM   3364  C CA  . ASN B  2 104 ? 20.116  56.031 28.893  1.00 13.06  ? 104  ASN B CA  1 
ATOM   3365  C C   . ASN B  2 104 ? 20.900  56.345 27.627  1.00 12.69  ? 104  ASN B C   1 
ATOM   3366  O O   . ASN B  2 104 ? 20.348  56.346 26.531  1.00 12.73  ? 104  ASN B O   1 
ATOM   3367  C CB  . ASN B  2 104 ? 19.783  57.358 29.576  1.00 13.89  ? 104  ASN B CB  1 
ATOM   3368  C CG  . ASN B  2 104 ? 18.563  57.277 30.464  1.00 14.88  ? 104  ASN B CG  1 
ATOM   3369  O OD1 . ASN B  2 104 ? 17.816  56.305 30.430  1.00 15.09  ? 104  ASN B OD1 1 
ATOM   3370  N ND2 . ASN B  2 104 ? 18.353  58.313 31.263  1.00 15.91  ? 104  ASN B ND2 1 
ATOM   3371  N N   . GLU B  2 105 ? 22.187  56.634 27.792  1.00 18.68  ? 105  GLU B N   1 
ATOM   3372  C CA  . GLU B  2 105 ? 23.040  56.947 26.662  1.00 18.16  ? 105  GLU B CA  1 
ATOM   3373  C C   . GLU B  2 105 ? 23.190  55.745 25.751  1.00 16.45  ? 105  GLU B C   1 
ATOM   3374  O O   . GLU B  2 105 ? 23.213  55.883 24.530  1.00 15.17  ? 105  GLU B O   1 
ATOM   3375  C CB  . GLU B  2 105 ? 24.420  57.395 27.130  1.00 20.71  ? 105  GLU B CB  1 
ATOM   3376  C CG  . GLU B  2 105 ? 25.231  58.039 26.022  1.00 21.11  ? 105  GLU B CG  1 
ATOM   3377  C CD  . GLU B  2 105 ? 26.304  58.961 26.549  1.00 24.52  ? 105  GLU B CD  1 
ATOM   3378  O OE1 . GLU B  2 105 ? 27.084  58.520 27.412  1.00 26.48  ? 105  GLU B OE1 1 
ATOM   3379  O OE2 . GLU B  2 105 ? 26.360  60.128 26.103  1.00 25.78  ? 105  GLU B OE2 1 
ATOM   3380  N N   . ARG B  2 106 ? 23.304  54.568 26.352  1.00 16.90  ? 106  ARG B N   1 
ATOM   3381  C CA  . ARG B  2 106 ? 23.410  53.343 25.581  1.00 16.08  ? 106  ARG B CA  1 
ATOM   3382  C C   . ARG B  2 106 ? 22.098  53.019 24.873  1.00 14.04  ? 106  ARG B C   1 
ATOM   3383  O O   . ARG B  2 106 ? 22.113  52.494 23.763  1.00 13.08  ? 106  ARG B O   1 
ATOM   3384  C CB  . ARG B  2 106 ? 23.839  52.171 26.464  1.00 18.03  ? 106  ARG B CB  1 
ATOM   3385  C CG  . ARG B  2 106 ? 25.279  52.246 26.958  1.00 20.56  ? 106  ARG B CG  1 
ATOM   3386  C CD  . ARG B  2 106 ? 25.875  50.858 27.142  1.00 22.60  ? 106  ARG B CD  1 
ATOM   3387  N NE  . ARG B  2 106 ? 26.679  50.427 25.985  1.00 22.96  ? 106  ARG B NE  1 
ATOM   3388  C CZ  . ARG B  2 106 ? 26.829  49.161 25.575  1.00 24.14  ? 106  ARG B CZ  1 
ATOM   3389  N NH1 . ARG B  2 106 ? 26.214  48.150 26.190  1.00 25.10  ? 106  ARG B NH1 1 
ATOM   3390  N NH2 . ARG B  2 106 ? 27.600  48.894 24.522  1.00 24.90  ? 106  ARG B NH2 1 
ATOM   3391  N N   . THR B  2 107 ? 20.972  53.332 25.507  1.00 13.84  ? 107  THR B N   1 
ATOM   3392  C CA  . THR B  2 107 ? 19.661  53.076 24.907  1.00 12.60  ? 107  THR B CA  1 
ATOM   3393  C C   . THR B  2 107 ? 19.441  53.895 23.633  1.00 11.06  ? 107  THR B C   1 
ATOM   3394  O O   . THR B  2 107 ? 18.929  53.381 22.647  1.00 10.06  ? 107  THR B O   1 
ATOM   3395  C CB  . THR B  2 107 ? 18.507  53.340 25.898  1.00 13.54  ? 107  THR B CB  1 
ATOM   3396  O OG1 . THR B  2 107 ? 18.607  52.444 27.011  1.00 15.21  ? 107  THR B OG1 1 
ATOM   3397  C CG2 . THR B  2 107 ? 17.166  53.119 25.231  1.00 12.96  ? 107  THR B CG2 1 
ATOM   3398  N N   . LEU B  2 108 ? 19.835  55.161 23.649  1.00 11.30  ? 108  LEU B N   1 
ATOM   3399  C CA  . LEU B  2 108 ? 19.666  56.010 22.476  1.00 10.49  ? 108  LEU B CA  1 
ATOM   3400  C C   . LEU B  2 108 ? 20.583  55.579 21.333  1.00 9.75   ? 108  LEU B C   1 
ATOM   3401  O O   . LEU B  2 108 ? 20.191  55.596 20.169  1.00 8.80   ? 108  LEU B O   1 
ATOM   3402  C CB  . LEU B  2 108 ? 19.917  57.469 22.833  1.00 11.90  ? 108  LEU B CB  1 
ATOM   3403  C CG  . LEU B  2 108 ? 19.046  58.055 23.946  1.00 13.30  ? 108  LEU B CG  1 
ATOM   3404  C CD1 . LEU B  2 108 ? 19.383  59.525 24.121  1.00 15.33  ? 108  LEU B CD1 1 
ATOM   3405  C CD2 . LEU B  2 108 ? 17.561  57.871 23.676  1.00 12.85  ? 108  LEU B CD2 1 
ATOM   3406  N N   . ASP B  2 109 ? 21.803  55.185 21.670  1.00 10.61  ? 109  ASP B N   1 
ATOM   3407  C CA  . ASP B  2 109 ? 22.728  54.657 20.680  1.00 10.62  ? 109  ASP B CA  1 
ATOM   3408  C C   . ASP B  2 109 ? 22.294  53.285 20.152  1.00 9.89   ? 109  ASP B C   1 
ATOM   3409  O O   . ASP B  2 109 ? 22.585  52.943 19.017  1.00 9.70   ? 109  ASP B O   1 
ATOM   3410  C CB  . ASP B  2 109 ? 24.138  54.591 21.263  1.00 12.57  ? 109  ASP B CB  1 
ATOM   3411  C CG  . ASP B  2 109 ? 24.744  55.970 21.485  1.00 14.00  ? 109  ASP B CG  1 
ATOM   3412  O OD1 . ASP B  2 109 ? 24.431  56.900 20.705  1.00 13.65  ? 109  ASP B OD1 1 
ATOM   3413  O OD2 . ASP B  2 109 ? 25.550  56.116 22.436  1.00 15.98  ? 109  ASP B OD2 1 
ATOM   3414  N N   . PHE B  2 110 ? 21.603  52.505 20.980  1.00 10.01  ? 110  PHE B N   1 
ATOM   3415  C CA  . PHE B  2 110 ? 21.030  51.224 20.567  1.00 10.02  ? 110  PHE B CA  1 
ATOM   3416  C C   . PHE B  2 110 ? 20.005  51.438 19.451  1.00 8.73   ? 110  PHE B C   1 
ATOM   3417  O O   . PHE B  2 110 ? 20.033  50.763 18.426  1.00 8.77   ? 110  PHE B O   1 
ATOM   3418  C CB  . PHE B  2 110 ? 20.393  50.556 21.789  1.00 11.01  ? 110  PHE B CB  1 
ATOM   3419  C CG  . PHE B  2 110 ? 19.707  49.248 21.507  1.00 11.86  ? 110  PHE B CG  1 
ATOM   3420  C CD1 . PHE B  2 110 ? 20.402  48.172 20.978  1.00 13.19  ? 110  PHE B CD1 1 
ATOM   3421  C CD2 . PHE B  2 110 ? 18.366  49.078 21.825  1.00 12.07  ? 110  PHE B CD2 1 
ATOM   3422  C CE1 . PHE B  2 110 ? 19.761  46.964 20.740  1.00 14.71  ? 110  PHE B CE1 1 
ATOM   3423  C CE2 . PHE B  2 110 ? 17.723  47.872 21.596  1.00 13.58  ? 110  PHE B CE2 1 
ATOM   3424  C CZ  . PHE B  2 110 ? 18.418  46.813 21.051  1.00 14.92  ? 110  PHE B CZ  1 
ATOM   3425  N N   . HIS B  2 111 ? 19.109  52.398 19.653  1.00 8.07   ? 111  HIS B N   1 
ATOM   3426  C CA  . HIS B  2 111 ? 18.126  52.760 18.641  1.00 7.34   ? 111  HIS B CA  1 
ATOM   3427  C C   . HIS B  2 111 ? 18.790  53.247 17.361  1.00 6.84   ? 111  HIS B C   1 
ATOM   3428  O O   . HIS B  2 111 ? 18.349  52.922 16.261  1.00 6.60   ? 111  HIS B O   1 
ATOM   3429  C CB  . HIS B  2 111 ? 17.190  53.846 19.172  1.00 7.49   ? 111  HIS B CB  1 
ATOM   3430  C CG  . HIS B  2 111 ? 16.206  53.348 20.183  1.00 8.42   ? 111  HIS B CG  1 
ATOM   3431  N ND1 . HIS B  2 111 ? 15.250  52.402 19.885  1.00 8.99   ? 111  HIS B ND1 1 
ATOM   3432  C CD2 . HIS B  2 111 ? 16.025  53.668 21.486  1.00 9.38   ? 111  HIS B CD2 1 
ATOM   3433  C CE1 . HIS B  2 111 ? 14.527  52.157 20.962  1.00 10.32  ? 111  HIS B CE1 1 
ATOM   3434  N NE2 . HIS B  2 111 ? 14.978  52.912 21.947  1.00 10.48  ? 111  HIS B NE2 1 
ATOM   3435  N N   . ASP B  2 112 ? 19.845  54.037 17.514  1.00 7.13   ? 112  ASP B N   1 
ATOM   3436  C CA  . ASP B  2 112 ? 20.606  54.547 16.379  1.00 7.30   ? 112  ASP B CA  1 
ATOM   3437  C C   . ASP B  2 112 ? 21.236  53.386 15.603  1.00 7.66   ? 112  ASP B C   1 
ATOM   3438  O O   . ASP B  2 112 ? 21.205  53.356 14.376  1.00 7.65   ? 112  ASP B O   1 
ATOM   3439  C CB  . ASP B  2 112 ? 21.677  55.512 16.886  1.00 8.37   ? 112  ASP B CB  1 
ATOM   3440  C CG  . ASP B  2 112 ? 22.311  56.317 15.785  1.00 9.17   ? 112  ASP B CG  1 
ATOM   3441  O OD1 . ASP B  2 112 ? 21.798  56.311 14.651  1.00 8.68   ? 112  ASP B OD1 1 
ATOM   3442  O OD2 . ASP B  2 112 ? 23.335  56.969 16.066  1.00 10.72  ? 112  ASP B OD2 1 
ATOM   3443  N N   . SER B  2 113 ? 21.779  52.422 16.342  1.00 8.45   ? 113  SER B N   1 
ATOM   3444  C CA  . SER B  2 113 ? 22.351  51.209 15.770  1.00 9.60   ? 113  SER B CA  1 
ATOM   3445  C C   . SER B  2 113 ? 21.337  50.391 14.973  1.00 9.42   ? 113  SER B C   1 
ATOM   3446  O O   . SER B  2 113 ? 21.648  49.910 13.881  1.00 10.25  ? 113  SER B O   1 
ATOM   3447  C CB  . SER B  2 113 ? 22.944  50.342 16.879  1.00 11.00  ? 113  SER B CB  1 
ATOM   3448  O OG  . SER B  2 113 ? 23.261  49.052 16.407  1.00 12.66  ? 113  SER B OG  1 
ATOM   3449  N N   . ASN B  2 114 ? 20.136  50.222 15.523  1.00 8.89   ? 114  ASN B N   1 
ATOM   3450  C CA  . ASN B  2 114 ? 19.097  49.410 14.886  1.00 9.35   ? 114  ASN B CA  1 
ATOM   3451  C C   . ASN B  2 114 ? 18.606  49.988 13.569  1.00 8.77   ? 114  ASN B C   1 
ATOM   3452  O O   . ASN B  2 114 ? 18.299  49.244 12.639  1.00 9.70   ? 114  ASN B O   1 
ATOM   3453  C CB  . ASN B  2 114 ? 17.905  49.233 15.827  1.00 9.45   ? 114  ASN B CB  1 
ATOM   3454  C CG  . ASN B  2 114 ? 18.230  48.368 17.028  1.00 10.79  ? 114  ASN B CG  1 
ATOM   3455  O OD1 . ASN B  2 114 ? 19.084  47.488 16.968  1.00 12.24  ? 114  ASN B OD1 1 
ATOM   3456  N ND2 . ASN B  2 114 ? 17.538  48.612 18.125  1.00 10.82  ? 114  ASN B ND2 1 
ATOM   3457  N N   . VAL B  2 115 ? 18.528  51.314 13.502  1.00 7.73   ? 115  VAL B N   1 
ATOM   3458  C CA  . VAL B  2 115 ? 18.126  52.018 12.286  1.00 7.58   ? 115  VAL B CA  1 
ATOM   3459  C C   . VAL B  2 115 ? 19.189  51.841 11.208  1.00 8.35   ? 115  VAL B C   1 
ATOM   3460  O O   . VAL B  2 115 ? 18.879  51.591 10.038  1.00 8.98   ? 115  VAL B O   1 
ATOM   3461  C CB  . VAL B  2 115 ? 17.934  53.529 12.546  1.00 7.03   ? 115  VAL B CB  1 
ATOM   3462  C CG1 . VAL B  2 115 ? 17.745  54.291 11.244  1.00 7.43   ? 115  VAL B CG1 1 
ATOM   3463  C CG2 . VAL B  2 115 ? 16.749  53.776 13.461  1.00 6.93   ? 115  VAL B CG2 1 
ATOM   3464  N N   . LYS B  2 116 ? 20.447  51.968 11.619  1.00 8.80   ? 116  LYS B N   1 
ATOM   3465  C CA  . LYS B  2 116 ? 21.578  51.873 10.703  1.00 10.14  ? 116  LYS B CA  1 
ATOM   3466  C C   . LYS B  2 116 ? 21.729  50.475 10.135  1.00 11.59  ? 116  LYS B C   1 
ATOM   3467  O O   . LYS B  2 116 ? 22.022  50.305 8.956   1.00 12.76  ? 116  LYS B O   1 
ATOM   3468  C CB  . LYS B  2 116 ? 22.862  52.261 11.422  1.00 10.92  ? 116  LYS B CB  1 
ATOM   3469  C CG  . LYS B  2 116 ? 23.763  53.137 10.592  1.00 12.21  ? 116  LYS B CG  1 
ATOM   3470  C CD  . LYS B  2 116 ? 25.009  52.429 10.122  1.00 14.57  ? 116  LYS B CD  1 
ATOM   3471  C CE  . LYS B  2 116 ? 25.745  53.324 9.145   1.00 16.25  ? 116  LYS B CE  1 
ATOM   3472  N NZ  . LYS B  2 116 ? 27.207  53.073 9.232   1.00 19.12  ? 116  LYS B NZ  1 
ATOM   3473  N N   . ASN B  2 117 ? 21.532  49.474 10.982  1.00 12.02  ? 117  ASN B N   1 
ATOM   3474  C CA  . ASN B  2 117 ? 21.627  48.093 10.544  1.00 14.16  ? 117  ASN B CA  1 
ATOM   3475  C C   . ASN B  2 117 ? 20.494  47.728 9.588   1.00 14.45  ? 117  ASN B C   1 
ATOM   3476  O O   . ASN B  2 117 ? 20.690  46.949 8.647   1.00 16.53  ? 117  ASN B O   1 
ATOM   3477  C CB  . ASN B  2 117 ? 21.657  47.155 11.747  1.00 15.12  ? 117  ASN B CB  1 
ATOM   3478  C CG  . ASN B  2 117 ? 22.908  47.328 12.585  1.00 15.76  ? 117  ASN B CG  1 
ATOM   3479  O OD1 . ASN B  2 117 ? 23.927  47.824 12.105  1.00 16.39  ? 117  ASN B OD1 1 
ATOM   3480  N ND2 . ASN B  2 117 ? 22.842  46.908 13.844  1.00 16.10  ? 117  ASN B ND2 1 
ATOM   3481  N N   . LEU B  2 118 ? 19.321  48.306 9.825   1.00 12.90  ? 118  LEU B N   1 
ATOM   3482  C CA  . LEU B  2 118 ? 18.180  48.128 8.934   1.00 13.44  ? 118  LEU B CA  1 
ATOM   3483  C C   . LEU B  2 118 ? 18.419  48.833 7.599   1.00 13.54  ? 118  LEU B C   1 
ATOM   3484  O O   . LEU B  2 118 ? 18.058  48.317 6.540   1.00 15.10  ? 118  LEU B O   1 
ATOM   3485  C CB  . LEU B  2 118 ? 16.908  48.667 9.595   1.00 12.27  ? 118  LEU B CB  1 
ATOM   3486  C CG  . LEU B  2 118 ? 15.599  48.593 8.810   1.00 13.18  ? 118  LEU B CG  1 
ATOM   3487  C CD1 . LEU B  2 118 ? 15.316  47.183 8.326   1.00 15.79  ? 118  LEU B CD1 1 
ATOM   3488  C CD2 . LEU B  2 118 ? 14.460  49.093 9.678   1.00 12.63  ? 118  LEU B CD2 1 
ATOM   3489  N N   . TYR B  2 119 ? 19.028  50.012 7.652   1.00 12.37  ? 119  TYR B N   1 
ATOM   3490  C CA  . TYR B  2 119 ? 19.344  50.751 6.441   1.00 12.92  ? 119  TYR B CA  1 
ATOM   3491  C C   . TYR B  2 119 ? 20.375  50.005 5.610   1.00 15.04  ? 119  TYR B C   1 
ATOM   3492  O O   . TYR B  2 119 ? 20.246  49.917 4.394   1.00 16.44  ? 119  TYR B O   1 
ATOM   3493  C CB  . TYR B  2 119 ? 19.859  52.148 6.779   1.00 11.97  ? 119  TYR B CB  1 
ATOM   3494  C CG  . TYR B  2 119 ? 20.353  52.910 5.575   1.00 13.19  ? 119  TYR B CG  1 
ATOM   3495  C CD1 . TYR B  2 119 ? 19.463  53.558 4.728   1.00 13.48  ? 119  TYR B CD1 1 
ATOM   3496  C CD2 . TYR B  2 119 ? 21.710  52.976 5.273   1.00 14.62  ? 119  TYR B CD2 1 
ATOM   3497  C CE1 . TYR B  2 119 ? 19.908  54.256 3.620   1.00 15.04  ? 119  TYR B CE1 1 
ATOM   3498  C CE2 . TYR B  2 119 ? 22.161  53.670 4.159   1.00 16.27  ? 119  TYR B CE2 1 
ATOM   3499  C CZ  . TYR B  2 119 ? 21.254  54.310 3.338   1.00 16.41  ? 119  TYR B CZ  1 
ATOM   3500  O OH  . TYR B  2 119 ? 21.683  55.007 2.231   1.00 18.46  ? 119  TYR B OH  1 
ATOM   3501  N N   . ASP B  2 120 ? 21.401  49.476 6.267   1.00 15.78  ? 120  ASP B N   1 
ATOM   3502  C CA  . ASP B  2 120 ? 22.438  48.722 5.573   1.00 18.51  ? 120  ASP B CA  1 
ATOM   3503  C C   . ASP B  2 120 ? 21.881  47.423 4.990   1.00 20.54  ? 120  ASP B C   1 
ATOM   3504  O O   . ASP B  2 120 ? 22.257  47.020 3.896   1.00 22.95  ? 120  ASP B O   1 
ATOM   3505  C CB  . ASP B  2 120 ? 23.615  48.426 6.511   1.00 19.39  ? 120  ASP B CB  1 
ATOM   3506  C CG  . ASP B  2 120 ? 24.504  49.642 6.750   1.00 18.94  ? 120  ASP B CG  1 
ATOM   3507  O OD1 . ASP B  2 120 ? 24.663  50.480 5.831   1.00 19.32  ? 120  ASP B OD1 1 
ATOM   3508  O OD2 . ASP B  2 120 ? 25.065  49.748 7.862   1.00 18.71  ? 120  ASP B OD2 1 
ATOM   3509  N N   . LYS B  2 121 ? 20.975  46.785 5.722   1.00 20.08  ? 121  LYS B N   1 
ATOM   3510  C CA  . LYS B  2 121 ? 20.309  45.561 5.269   1.00 22.55  ? 121  LYS B CA  1 
ATOM   3511  C C   . LYS B  2 121 ? 19.660  45.763 3.906   1.00 23.35  ? 121  LYS B C   1 
ATOM   3512  O O   . LYS B  2 121 ? 19.818  44.943 3.003   1.00 26.43  ? 121  LYS B O   1 
ATOM   3513  C CB  . LYS B  2 121 ? 19.247  45.155 6.288   1.00 21.84  ? 121  LYS B CB  1 
ATOM   3514  C CG  . LYS B  2 121 ? 18.581  43.815 6.050   1.00 25.09  ? 121  LYS B CG  1 
ATOM   3515  C CD  . LYS B  2 121 ? 17.670  43.484 7.229   1.00 24.76  ? 121  LYS B CD  1 
ATOM   3516  C CE  . LYS B  2 121 ? 17.163  42.046 7.198   1.00 28.87  ? 121  LYS B CE  1 
ATOM   3517  N NZ  . LYS B  2 121 ? 15.887  41.909 6.436   1.00 30.20  ? 121  LYS B NZ  1 
ATOM   3518  N N   . VAL B  2 122 ? 18.934  46.867 3.772   1.00 21.06  ? 122  VAL B N   1 
ATOM   3519  C CA  . VAL B  2 122 ? 18.287  47.226 2.523   1.00 21.87  ? 122  VAL B CA  1 
ATOM   3520  C C   . VAL B  2 122 ? 19.331  47.584 1.467   1.00 23.24  ? 122  VAL B C   1 
ATOM   3521  O O   . VAL B  2 122 ? 19.232  47.154 0.317   1.00 25.70  ? 122  VAL B O   1 
ATOM   3522  C CB  . VAL B  2 122 ? 17.305  48.398 2.733   1.00 19.59  ? 122  VAL B CB  1 
ATOM   3523  C CG1 . VAL B  2 122 ? 16.747  48.901 1.406   1.00 20.77  ? 122  VAL B CG1 1 
ATOM   3524  C CG2 . VAL B  2 122 ? 16.177  47.963 3.651   1.00 19.14  ? 122  VAL B CG2 1 
ATOM   3525  N N   . ARG B  2 123 ? 20.331  48.363 1.865   1.00 22.14  ? 123  ARG B N   1 
ATOM   3526  C CA  . ARG B  2 123 ? 21.396  48.777 0.959   1.00 23.92  ? 123  ARG B CA  1 
ATOM   3527  C C   . ARG B  2 123 ? 22.067  47.568 0.317   1.00 27.52  ? 123  ARG B C   1 
ATOM   3528  O O   . ARG B  2 123 ? 22.314  47.556 -0.892  1.00 29.93  ? 123  ARG B O   1 
ATOM   3529  C CB  . ARG B  2 123 ? 22.437  49.593 1.720   1.00 22.87  ? 123  ARG B CB  1 
ATOM   3530  C CG  . ARG B  2 123 ? 23.459  50.290 0.839   1.00 24.87  ? 123  ARG B CG  1 
ATOM   3531  C CD  . ARG B  2 123 ? 24.508  51.015 1.675   1.00 24.53  ? 123  ARG B CD  1 
ATOM   3532  N NE  . ARG B  2 123 ? 25.115  50.159 2.699   1.00 24.77  ? 123  ARG B NE  1 
ATOM   3533  C CZ  . ARG B  2 123 ? 26.004  49.191 2.460   1.00 27.80  ? 123  ARG B CZ  1 
ATOM   3534  N NH1 . ARG B  2 123 ? 26.415  48.911 1.223   1.00 30.88  ? 123  ARG B NH1 1 
ATOM   3535  N NH2 . ARG B  2 123 ? 26.478  48.481 3.473   1.00 28.23  ? 123  ARG B NH2 1 
ATOM   3536  N N   . LEU B  2 124 ? 22.346  46.554 1.136   1.00 28.38  ? 124  LEU B N   1 
ATOM   3537  C CA  . LEU B  2 124 ? 23.027  45.337 0.683   1.00 32.51  ? 124  LEU B CA  1 
ATOM   3538  C C   . LEU B  2 124 ? 22.186  44.479 -0.268  1.00 35.16  ? 124  LEU B C   1 
ATOM   3539  O O   . LEU B  2 124 ? 22.738  43.728 -1.075  1.00 39.17  ? 124  LEU B O   1 
ATOM   3540  C CB  . LEU B  2 124 ? 23.480  44.501 1.887   1.00 33.11  ? 124  LEU B CB  1 
ATOM   3541  C CG  . LEU B  2 124 ? 24.610  45.136 2.709   1.00 32.13  ? 124  LEU B CG  1 
ATOM   3542  C CD1 . LEU B  2 124 ? 24.717  44.514 4.096   1.00 31.85  ? 124  LEU B CD1 1 
ATOM   3543  C CD2 . LEU B  2 124 ? 25.939  45.043 1.972   1.00 35.79  ? 124  LEU B CD2 1 
ATOM   3544  N N   . GLN B  2 125 ? 20.862  44.584 -0.164  1.00 33.53  ? 125  GLN B N   1 
ATOM   3545  C CA  . GLN B  2 125 ? 19.955  43.904 -1.084  1.00 36.23  ? 125  GLN B CA  1 
ATOM   3546  C C   . GLN B  2 125 ? 19.933  44.598 -2.426  1.00 37.04  ? 125  GLN B C   1 
ATOM   3547  O O   . GLN B  2 125 ? 20.125  43.969 -3.464  1.00 40.83  ? 125  GLN B O   1 
ATOM   3548  C CB  . GLN B  2 125 ? 18.531  43.881 -0.534  1.00 34.68  ? 125  GLN B CB  1 
ATOM   3549  C CG  . GLN B  2 125 ? 18.301  42.837 0.534   1.00 35.72  ? 125  GLN B CG  1 
ATOM   3550  C CD  . GLN B  2 125 ? 16.898  42.901 1.085   1.00 34.58  ? 125  GLN B CD  1 
ATOM   3551  O OE1 . GLN B  2 125 ? 15.945  42.496 0.420   1.00 36.99  ? 125  GLN B OE1 1 
ATOM   3552  N NE2 . GLN B  2 125 ? 16.758  43.412 2.304   1.00 31.44  ? 125  GLN B NE2 1 
ATOM   3553  N N   . LEU B  2 126 ? 19.683  45.901 -2.392  1.00 33.97  ? 126  LEU B N   1 
ATOM   3554  C CA  . LEU B  2 126 ? 19.510  46.678 -3.606  1.00 34.83  ? 126  LEU B CA  1 
ATOM   3555  C C   . LEU B  2 126 ? 20.791  46.745 -4.426  1.00 37.52  ? 126  LEU B C   1 
ATOM   3556  O O   . LEU B  2 126 ? 20.734  46.699 -5.645  1.00 40.30  ? 126  LEU B O   1 
ATOM   3557  C CB  . LEU B  2 126 ? 19.007  48.087 -3.282  1.00 31.49  ? 126  LEU B CB  1 
ATOM   3558  C CG  . LEU B  2 126 ? 17.666  48.194 -2.544  1.00 29.39  ? 126  LEU B CG  1 
ATOM   3559  C CD1 . LEU B  2 126 ? 17.198  49.639 -2.512  1.00 27.38  ? 126  LEU B CD1 1 
ATOM   3560  C CD2 . LEU B  2 126 ? 16.604  47.310 -3.174  1.00 31.93  ? 126  LEU B CD2 1 
ATOM   3561  N N   . ARG B  2 127 ? 21.941  46.840 -3.762  1.00 37.23  ? 127  ARG B N   1 
ATOM   3562  C CA  . ARG B  2 127 ? 23.233  46.896 -4.459  1.00 40.41  ? 127  ARG B CA  1 
ATOM   3563  C C   . ARG B  2 127 ? 23.222  48.045 -5.492  1.00 40.93  ? 127  ARG B C   1 
ATOM   3564  O O   . ARG B  2 127 ? 22.786  49.148 -5.160  1.00 38.06  ? 127  ARG B O   1 
ATOM   3565  C CB  . ARG B  2 127 ? 23.594  45.510 -5.048  1.00 45.02  ? 127  ARG B CB  1 
ATOM   3566  C CG  . ARG B  2 127 ? 24.251  44.586 -4.025  1.00 45.88  ? 127  ARG B CG  1 
ATOM   3567  C CD  . ARG B  2 127 ? 23.790  43.127 -4.073  1.00 49.00  ? 127  ARG B CD  1 
ATOM   3568  N NE  . ARG B  2 127 ? 24.019  42.325 -5.290  1.00 54.41  ? 127  ARG B NE  1 
ATOM   3569  C CZ  . ARG B  2 127 ? 25.078  42.356 -6.110  1.00 58.12  ? 127  ARG B CZ  1 
ATOM   3570  N NH1 . ARG B  2 127 ? 26.113  43.172 -5.924  1.00 57.39  ? 127  ARG B NH1 1 
ATOM   3571  N NH2 . ARG B  2 127 ? 25.105  41.530 -7.155  1.00 63.30  ? 127  ARG B NH2 1 
ATOM   3572  N N   . ASP B  2 128 ? 23.669  47.810 -6.724  1.00 45.02  ? 128  ASP B N   1 
ATOM   3573  C CA  . ASP B  2 128 ? 23.724  48.882 -7.721  1.00 46.20  ? 128  ASP B CA  1 
ATOM   3574  C C   . ASP B  2 128 ? 22.437  49.011 -8.557  1.00 46.42  ? 128  ASP B C   1 
ATOM   3575  O O   . ASP B  2 128 ? 22.445  49.671 -9.595  1.00 48.48  ? 128  ASP B O   1 
ATOM   3576  C CB  . ASP B  2 128 ? 24.947  48.701 -8.634  1.00 50.98  ? 128  ASP B CB  1 
ATOM   3577  C CG  . ASP B  2 128 ? 24.874  47.436 -9.473  1.00 55.11  ? 128  ASP B CG  1 
ATOM   3578  O OD1 . ASP B  2 128 ? 24.157  46.497 -9.066  1.00 54.46  ? 128  ASP B OD1 1 
ATOM   3579  O OD2 . ASP B  2 128 ? 25.532  47.381 -10.538 1.00 59.54  ? 128  ASP B OD2 1 
ATOM   3580  N N   . ASN B  2 129 ? 21.343  48.392 -8.106  1.00 44.84  ? 129  ASN B N   1 
ATOM   3581  C CA  . ASN B  2 129 ? 20.034  48.517 -8.767  1.00 45.22  ? 129  ASN B CA  1 
ATOM   3582  C C   . ASN B  2 129 ? 19.216  49.755 -8.343  1.00 41.95  ? 129  ASN B C   1 
ATOM   3583  O O   . ASN B  2 129 ? 18.110  49.964 -8.857  1.00 42.55  ? 129  ASN B O   1 
ATOM   3584  C CB  . ASN B  2 129 ? 19.192  47.247 -8.548  1.00 46.13  ? 129  ASN B CB  1 
ATOM   3585  C CG  . ASN B  2 129 ? 19.601  46.093 -9.457  1.00 51.11  ? 129  ASN B CG  1 
ATOM   3586  O OD1 . ASN B  2 129 ? 20.696  46.079 -10.031 1.00 53.73  ? 129  ASN B OD1 1 
ATOM   3587  N ND2 . ASN B  2 129 ? 18.708  45.115 -9.597  1.00 53.10  ? 129  ASN B ND2 1 
ATOM   3588  N N   . ALA B  2 130 ? 19.749  50.568 -7.426  1.00 39.08  ? 130  ALA B N   1 
ATOM   3589  C CA  . ALA B  2 130 ? 19.100  51.821 -7.010  1.00 36.66  ? 130  ALA B CA  1 
ATOM   3590  C C   . ALA B  2 130 ? 20.134  52.888 -6.666  1.00 36.02  ? 130  ALA B C   1 
ATOM   3591  O O   . ALA B  2 130 ? 21.285  52.561 -6.407  1.00 36.62  ? 130  ALA B O   1 
ATOM   3592  C CB  . ALA B  2 130 ? 18.202  51.570 -5.815  1.00 33.55  ? 130  ALA B CB  1 
ATOM   3593  N N   . LYS B  2 131 ? 19.725  54.156 -6.668  1.00 35.47  ? 131  LYS B N   1 
ATOM   3594  C CA  . LYS B  2 131 ? 20.606  55.269 -6.281  1.00 35.37  ? 131  LYS B CA  1 
ATOM   3595  C C   . LYS B  2 131 ? 20.562  55.506 -4.773  1.00 31.91  ? 131  LYS B C   1 
ATOM   3596  O O   . LYS B  2 131 ? 19.491  55.729 -4.213  1.00 29.94  ? 131  LYS B O   1 
ATOM   3597  C CB  . LYS B  2 131 ? 20.186  56.565 -6.977  1.00 37.31  ? 131  LYS B CB  1 
ATOM   3598  C CG  . LYS B  2 131 ? 20.292  56.558 -8.495  1.00 41.28  ? 131  LYS B CG  1 
ATOM   3599  C CD  . LYS B  2 131 ? 19.617  57.794 -9.087  1.00 43.31  ? 131  LYS B CD  1 
ATOM   3600  C CE  . LYS B  2 131 ? 20.175  58.199 -10.450 1.00 47.94  ? 131  LYS B CE  1 
ATOM   3601  N NZ  . LYS B  2 131 ? 21.556  58.772 -10.374 1.00 49.75  ? 131  LYS B NZ  1 
ATOM   3602  N N   . GLU B  2 132 ? 21.719  55.470 -4.116  1.00 31.55  ? 132  GLU B N   1 
ATOM   3603  C CA  . GLU B  2 132 ? 21.806  55.840 -2.705  1.00 28.83  ? 132  GLU B CA  1 
ATOM   3604  C C   . GLU B  2 132 ? 21.774  57.368 -2.597  1.00 29.55  ? 132  GLU B C   1 
ATOM   3605  O O   . GLU B  2 132 ? 22.778  58.034 -2.832  1.00 31.82  ? 132  GLU B O   1 
ATOM   3606  C CB  . GLU B  2 132 ? 23.080  55.273 -2.079  1.00 28.94  ? 132  GLU B CB  1 
ATOM   3607  C CG  . GLU B  2 132 ? 23.120  55.378 -0.562  1.00 26.19  ? 132  GLU B CG  1 
ATOM   3608  C CD  . GLU B  2 132 ? 24.266  54.602 0.072   1.00 26.57  ? 132  GLU B CD  1 
ATOM   3609  O OE1 . GLU B  2 132 ? 25.282  54.341 -0.602  1.00 29.47  ? 132  GLU B OE1 1 
ATOM   3610  O OE2 . GLU B  2 132 ? 24.150  54.253 1.261   1.00 24.42  ? 132  GLU B OE2 1 
ATOM   3611  N N   . LEU B  2 133 ? 20.607  57.914 -2.260  1.00 28.28  ? 133  LEU B N   1 
ATOM   3612  C CA  . LEU B  2 133 ? 20.399  59.372 -2.252  1.00 29.75  ? 133  LEU B CA  1 
ATOM   3613  C C   . LEU B  2 133 ? 21.169  60.122 -1.163  1.00 29.47  ? 133  LEU B C   1 
ATOM   3614  O O   . LEU B  2 133 ? 21.506  61.292 -1.346  1.00 32.06  ? 133  LEU B O   1 
ATOM   3615  C CB  . LEU B  2 133 ? 18.901  59.700 -2.147  1.00 29.05  ? 133  LEU B CB  1 
ATOM   3616  C CG  . LEU B  2 133 ? 18.136  59.904 -3.460  1.00 31.59  ? 133  LEU B CG  1 
ATOM   3617  C CD1 . LEU B  2 133 ? 18.578  58.949 -4.556  1.00 32.77  ? 133  LEU B CD1 1 
ATOM   3618  C CD2 . LEU B  2 133 ? 16.640  59.778 -3.217  1.00 30.70  ? 133  LEU B CD2 1 
ATOM   3619  N N   . GLY B  2 134 ? 21.432  59.459 -0.038  1.00 26.82  ? 134  GLY B N   1 
ATOM   3620  C CA  . GLY B  2 134 ? 22.188  60.060 1.060   1.00 26.74  ? 134  GLY B CA  1 
ATOM   3621  C C   . GLY B  2 134 ? 21.351  60.490 2.258   1.00 24.80  ? 134  GLY B C   1 
ATOM   3622  O O   . GLY B  2 134 ? 21.893  60.993 3.248   1.00 24.85  ? 134  GLY B O   1 
ATOM   3623  N N   . ASN B  2 135 ? 20.038  60.278 2.183   1.00 23.57  ? 135  ASN B N   1 
ATOM   3624  C CA  . ASN B  2 135 ? 19.106  60.764 3.208   1.00 22.49  ? 135  ASN B CA  1 
ATOM   3625  C C   . ASN B  2 135 ? 18.288  59.654 3.857   1.00 19.49  ? 135  ASN B C   1 
ATOM   3626  O O   . ASN B  2 135 ? 17.328  59.928 4.578   1.00 18.85  ? 135  ASN B O   1 
ATOM   3627  C CB  . ASN B  2 135 ? 18.161  61.798 2.594   1.00 25.05  ? 135  ASN B CB  1 
ATOM   3628  C CG  . ASN B  2 135 ? 17.432  61.268 1.381   1.00 25.86  ? 135  ASN B CG  1 
ATOM   3629  O OD1 . ASN B  2 135 ? 17.424  60.067 1.125   1.00 24.23  ? 135  ASN B OD1 1 
ATOM   3630  N ND2 . ASN B  2 135 ? 16.832  62.163 0.617   1.00 29.00  ? 135  ASN B ND2 1 
ATOM   3631  N N   . GLY B  2 136 ? 18.674  58.407 3.600   1.00 18.18  ? 136  GLY B N   1 
ATOM   3632  C CA  . GLY B  2 136 ? 17.919  57.247 4.057   1.00 16.20  ? 136  GLY B CA  1 
ATOM   3633  C C   . GLY B  2 136 ? 17.103  56.615 2.947   1.00 16.92  ? 136  GLY B C   1 
ATOM   3634  O O   . GLY B  2 136 ? 16.539  55.533 3.131   1.00 16.10  ? 136  GLY B O   1 
ATOM   3635  N N   . CYS B  2 137 ? 17.053  57.283 1.794   1.00 18.88  ? 137  CYS B N   1 
ATOM   3636  C CA  . CYS B  2 137 ? 16.229  56.838 0.680   1.00 20.20  ? 137  CYS B CA  1 
ATOM   3637  C C   . CYS B  2 137 ? 17.046  56.214 -0.439  1.00 21.57  ? 137  CYS B C   1 
ATOM   3638  O O   . CYS B  2 137 ? 18.189  56.603 -0.698  1.00 22.40  ? 137  CYS B O   1 
ATOM   3639  C CB  . CYS B  2 137 ? 15.401  57.993 0.121   1.00 22.21  ? 137  CYS B CB  1 
ATOM   3640  S SG  . CYS B  2 137 ? 14.268  58.742 1.316   1.00 21.76  ? 137  CYS B SG  1 
ATOM   3641  N N   . PHE B  2 138 ? 16.432  55.235 -1.093  1.00 22.29  ? 138  PHE B N   1 
ATOM   3642  C CA  . PHE B  2 138 ? 16.993  54.589 -2.261  1.00 24.27  ? 138  PHE B CA  1 
ATOM   3643  C C   . PHE B  2 138 ? 16.040  54.801 -3.414  1.00 26.64  ? 138  PHE B C   1 
ATOM   3644  O O   . PHE B  2 138 ? 14.868  54.468 -3.306  1.00 26.72  ? 138  PHE B O   1 
ATOM   3645  C CB  . PHE B  2 138 ? 17.161  53.097 -2.008  1.00 23.87  ? 138  PHE B CB  1 
ATOM   3646  C CG  . PHE B  2 138 ? 18.199  52.778 -0.973  1.00 22.27  ? 138  PHE B CG  1 
ATOM   3647  C CD1 . PHE B  2 138 ? 19.542  52.701 -1.322  1.00 23.47  ? 138  PHE B CD1 1 
ATOM   3648  C CD2 . PHE B  2 138 ? 17.835  52.563 0.354   1.00 20.01  ? 138  PHE B CD2 1 
ATOM   3649  C CE1 . PHE B  2 138 ? 20.501  52.407 -0.373  1.00 22.56  ? 138  PHE B CE1 1 
ATOM   3650  C CE2 . PHE B  2 138 ? 18.793  52.268 1.307   1.00 18.92  ? 138  PHE B CE2 1 
ATOM   3651  C CZ  . PHE B  2 138 ? 20.128  52.195 0.944   1.00 20.22  ? 138  PHE B CZ  1 
ATOM   3652  N N   . GLU B  2 139 ? 16.549  55.350 -4.512  1.00 29.05  ? 139  GLU B N   1 
ATOM   3653  C CA  . GLU B  2 139 ? 15.744  55.665 -5.678  1.00 31.85  ? 139  GLU B CA  1 
ATOM   3654  C C   . GLU B  2 139 ? 16.024  54.646 -6.780  1.00 34.15  ? 139  GLU B C   1 
ATOM   3655  O O   . GLU B  2 139 ? 17.156  54.523 -7.248  1.00 35.29  ? 139  GLU B O   1 
ATOM   3656  C CB  . GLU B  2 139 ? 16.084  57.073 -6.150  1.00 33.70  ? 139  GLU B CB  1 
ATOM   3657  C CG  . GLU B  2 139 ? 15.153  57.641 -7.204  1.00 36.83  ? 139  GLU B CG  1 
ATOM   3658  C CD  . GLU B  2 139 ? 15.739  58.879 -7.845  1.00 39.59  ? 139  GLU B CD  1 
ATOM   3659  O OE1 . GLU B  2 139 ? 15.724  59.952 -7.202  1.00 39.47  ? 139  GLU B OE1 1 
ATOM   3660  O OE2 . GLU B  2 139 ? 16.246  58.772 -8.980  1.00 42.35  ? 139  GLU B OE2 1 
ATOM   3661  N N   . PHE B  2 140 ? 14.985  53.932 -7.205  1.00 35.41  ? 140  PHE B N   1 
ATOM   3662  C CA  . PHE B  2 140 ? 15.137  52.782 -8.102  1.00 37.84  ? 140  PHE B CA  1 
ATOM   3663  C C   . PHE B  2 140 ? 15.372  53.178 -9.556  1.00 41.52  ? 140  PHE B C   1 
ATOM   3664  O O   . PHE B  2 140 ? 14.786  54.143 -10.044 1.00 42.89  ? 140  PHE B O   1 
ATOM   3665  C CB  . PHE B  2 140 ? 13.896  51.888 -8.024  1.00 38.53  ? 140  PHE B CB  1 
ATOM   3666  C CG  . PHE B  2 140 ? 13.699  51.250 -6.684  1.00 35.80  ? 140  PHE B CG  1 
ATOM   3667  C CD1 . PHE B  2 140 ? 12.995  51.904 -5.683  1.00 33.59  ? 140  PHE B CD1 1 
ATOM   3668  C CD2 . PHE B  2 140 ? 14.222  49.997 -6.420  1.00 35.98  ? 140  PHE B CD2 1 
ATOM   3669  C CE1 . PHE B  2 140 ? 12.818  51.318 -4.442  1.00 31.43  ? 140  PHE B CE1 1 
ATOM   3670  C CE2 . PHE B  2 140 ? 14.048  49.402 -5.183  1.00 33.96  ? 140  PHE B CE2 1 
ATOM   3671  C CZ  . PHE B  2 140 ? 13.346  50.064 -4.191  1.00 31.59  ? 140  PHE B CZ  1 
ATOM   3672  N N   . TYR B  2 141 ? 16.217  52.420 -10.248 1.00 43.68  ? 141  TYR B N   1 
ATOM   3673  C CA  . TYR B  2 141 ? 16.413  52.614 -11.689 1.00 47.82  ? 141  TYR B CA  1 
ATOM   3674  C C   . TYR B  2 141 ? 15.236  52.052 -12.473 1.00 50.57  ? 141  TYR B C   1 
ATOM   3675  O O   . TYR B  2 141 ? 14.859  52.587 -13.515 1.00 53.63  ? 141  TYR B O   1 
ATOM   3676  C CB  . TYR B  2 141 ? 17.711  51.958 -12.162 1.00 49.79  ? 141  TYR B CB  1 
ATOM   3677  C CG  . TYR B  2 141 ? 18.941  52.613 -11.589 1.00 48.37  ? 141  TYR B CG  1 
ATOM   3678  C CD1 . TYR B  2 141 ? 19.198  53.960 -11.810 1.00 48.92  ? 141  TYR B CD1 1 
ATOM   3679  C CD2 . TYR B  2 141 ? 19.834  51.896 -10.808 1.00 47.07  ? 141  TYR B CD2 1 
ATOM   3680  C CE1 . TYR B  2 141 ? 20.316  54.570 -11.282 1.00 48.26  ? 141  TYR B CE1 1 
ATOM   3681  C CE2 . TYR B  2 141 ? 20.957  52.498 -10.272 1.00 46.27  ? 141  TYR B CE2 1 
ATOM   3682  C CZ  . TYR B  2 141 ? 21.195  53.835 -10.512 1.00 46.89  ? 141  TYR B CZ  1 
ATOM   3683  O OH  . TYR B  2 141 ? 22.315  54.437 -9.978  1.00 46.71  ? 141  TYR B OH  1 
ATOM   3684  N N   . HIS B  2 142 ? 14.672  50.964 -11.961 1.00 50.03  ? 142  HIS B N   1 
ATOM   3685  C CA  . HIS B  2 142 ? 13.478  50.349 -12.528 1.00 52.86  ? 142  HIS B CA  1 
ATOM   3686  C C   . HIS B  2 142 ? 12.243  50.856 -11.803 1.00 51.22  ? 142  HIS B C   1 
ATOM   3687  O O   . HIS B  2 142 ? 12.332  51.368 -10.687 1.00 47.62  ? 142  HIS B O   1 
ATOM   3688  C CB  . HIS B  2 142 ? 13.554  48.821 -12.416 1.00 54.26  ? 142  HIS B CB  1 
ATOM   3689  C CG  . HIS B  2 142 ? 13.758  48.324 -11.019 1.00 50.83  ? 142  HIS B CG  1 
ATOM   3690  N ND1 . HIS B  2 142 ? 12.724  47.863 -10.233 1.00 50.05  ? 142  HIS B ND1 1 
ATOM   3691  C CD2 . HIS B  2 142 ? 14.878  48.230 -10.263 1.00 48.44  ? 142  HIS B CD2 1 
ATOM   3692  C CE1 . HIS B  2 142 ? 13.202  47.498 -9.056  1.00 47.19  ? 142  HIS B CE1 1 
ATOM   3693  N NE2 . HIS B  2 142 ? 14.505  47.712 -9.048  1.00 46.11  ? 142  HIS B NE2 1 
ATOM   3694  N N   . LYS B  2 143 ? 11.090  50.711 -12.444 1.00 54.41  ? 143  LYS B N   1 
ATOM   3695  C CA  . LYS B  2 143 ? 9.818   51.006 -11.801 1.00 53.94  ? 143  LYS B CA  1 
ATOM   3696  C C   . LYS B  2 143 ? 9.576   49.930 -10.748 1.00 52.37  ? 143  LYS B C   1 
ATOM   3697  O O   . LYS B  2 143 ? 9.747   48.742 -11.024 1.00 54.31  ? 143  LYS B O   1 
ATOM   3698  C CB  . LYS B  2 143 ? 8.697   51.013 -12.832 1.00 58.65  ? 143  LYS B CB  1 
ATOM   3699  C CG  . LYS B  2 143 ? 7.410   51.666 -12.367 1.00 59.14  ? 143  LYS B CG  1 
ATOM   3700  C CD  . LYS B  2 143 ? 6.335   51.555 -13.444 1.00 64.58  ? 143  LYS B CD  1 
ATOM   3701  C CE  . LYS B  2 143 ? 4.942   51.793 -12.882 1.00 65.98  ? 143  LYS B CE  1 
ATOM   3702  N NZ  . LYS B  2 143 ? 4.463   50.691 -11.995 1.00 65.44  ? 143  LYS B NZ  1 
ATOM   3703  N N   . CYS B  2 144 ? 9.201   50.350 -9.542  1.00 49.34  ? 144  CYS B N   1 
ATOM   3704  C CA  . CYS B  2 144 ? 9.051   49.436 -8.409  1.00 47.71  ? 144  CYS B CA  1 
ATOM   3705  C C   . CYS B  2 144 ? 7.641   49.526 -7.821  1.00 48.59  ? 144  CYS B C   1 
ATOM   3706  O O   . CYS B  2 144 ? 7.344   50.421 -7.031  1.00 46.40  ? 144  CYS B O   1 
ATOM   3707  C CB  . CYS B  2 144 ? 10.104  49.761 -7.346  1.00 43.28  ? 144  CYS B CB  1 
ATOM   3708  S SG  . CYS B  2 144 ? 10.202  48.603 -5.959  1.00 41.49  ? 144  CYS B SG  1 
ATOM   3709  N N   . ASP B  2 145 ? 6.776   48.592 -8.214  1.00 52.40  ? 145  ASP B N   1 
ATOM   3710  C CA  . ASP B  2 145 ? 5.385   48.561 -7.739  1.00 54.38  ? 145  ASP B CA  1 
ATOM   3711  C C   . ASP B  2 145 ? 5.299   48.093 -6.272  1.00 51.98  ? 145  ASP B C   1 
ATOM   3712  O O   . ASP B  2 145 ? 6.325   47.876 -5.625  1.00 48.54  ? 145  ASP B O   1 
ATOM   3713  C CB  . ASP B  2 145 ? 4.511   47.699 -8.673  1.00 60.01  ? 145  ASP B CB  1 
ATOM   3714  C CG  . ASP B  2 145 ? 4.935   46.238 -8.714  1.00 61.65  ? 145  ASP B CG  1 
ATOM   3715  O OD1 . ASP B  2 145 ? 5.830   45.832 -7.949  1.00 58.51  ? 145  ASP B OD1 1 
ATOM   3716  O OD2 . ASP B  2 145 ? 4.366   45.485 -9.524  1.00 66.65  ? 145  ASP B OD2 1 
ATOM   3717  N N   . ASN B  2 146 ? 4.082   47.943 -5.752  1.00 54.22  ? 146  ASN B N   1 
ATOM   3718  C CA  . ASN B  2 146 ? 3.887   47.579 -4.344  1.00 52.49  ? 146  ASN B CA  1 
ATOM   3719  C C   . ASN B  2 146 ? 4.369   46.174 -3.990  1.00 53.11  ? 146  ASN B C   1 
ATOM   3720  O O   . ASN B  2 146 ? 4.709   45.912 -2.840  1.00 50.64  ? 146  ASN B O   1 
ATOM   3721  C CB  . ASN B  2 146 ? 2.421   47.749 -3.942  1.00 55.68  ? 146  ASN B CB  1 
ATOM   3722  C CG  . ASN B  2 146 ? 1.957   49.192 -4.017  1.00 55.19  ? 146  ASN B CG  1 
ATOM   3723  O OD1 . ASN B  2 146 ? 2.757   50.124 -3.945  1.00 51.56  ? 146  ASN B OD1 1 
ATOM   3724  N ND2 . ASN B  2 146 ? 0.657   49.382 -4.165  1.00 59.52  ? 146  ASN B ND2 1 
ATOM   3725  N N   . GLU B  2 147 ? 4.407   45.277 -4.971  1.00 56.94  ? 147  GLU B N   1 
ATOM   3726  C CA  . GLU B  2 147 ? 4.988   43.947 -4.767  1.00 58.30  ? 147  GLU B CA  1 
ATOM   3727  C C   . GLU B  2 147 ? 6.512   44.051 -4.738  1.00 54.49  ? 147  GLU B C   1 
ATOM   3728  O O   . GLU B  2 147 ? 7.172   43.425 -3.907  1.00 53.08  ? 147  GLU B O   1 
ATOM   3729  C CB  . GLU B  2 147 ? 4.551   42.971 -5.861  1.00 64.30  ? 147  GLU B CB  1 
ATOM   3730  C CG  . GLU B  2 147 ? 3.045   42.747 -5.939  1.00 69.26  ? 147  GLU B CG  1 
ATOM   3731  C CD  . GLU B  2 147 ? 2.355   43.733 -6.865  1.00 70.65  ? 147  GLU B CD  1 
ATOM   3732  O OE1 . GLU B  2 147 ? 2.293   43.463 -8.085  1.00 74.35  ? 147  GLU B OE1 1 
ATOM   3733  O OE2 . GLU B  2 147 ? 1.880   44.780 -6.371  1.00 68.47  ? 147  GLU B OE2 1 
ATOM   3734  N N   . CYS B  2 148 ? 7.058   44.849 -5.654  1.00 53.41  ? 148  CYS B N   1 
ATOM   3735  C CA  . CYS B  2 148 ? 8.485   45.156 -5.674  1.00 50.12  ? 148  CYS B CA  1 
ATOM   3736  C C   . CYS B  2 148 ? 8.927   45.800 -4.356  1.00 45.44  ? 148  CYS B C   1 
ATOM   3737  O O   . CYS B  2 148 ? 9.966   45.440 -3.800  1.00 43.55  ? 148  CYS B O   1 
ATOM   3738  C CB  . CYS B  2 148 ? 8.805   46.080 -6.851  1.00 50.14  ? 148  CYS B CB  1 
ATOM   3739  S SG  . CYS B  2 148 ? 10.463  46.787 -6.826  1.00 46.20  ? 148  CYS B SG  1 
ATOM   3740  N N   . MET B  2 149 ? 8.134   46.746 -3.858  1.00 44.19  ? 149  MET B N   1 
ATOM   3741  C CA  . MET B  2 149 ? 8.412   47.379 -2.569  1.00 40.31  ? 149  MET B CA  1 
ATOM   3742  C C   . MET B  2 149 ? 8.340   46.350 -1.448  1.00 40.68  ? 149  MET B C   1 
ATOM   3743  O O   . MET B  2 149 ? 9.148   46.371 -0.525  1.00 37.79  ? 149  MET B O   1 
ATOM   3744  C CB  . MET B  2 149 ? 7.414   48.503 -2.291  1.00 39.87  ? 149  MET B CB  1 
ATOM   3745  C CG  . MET B  2 149 ? 7.502   49.685 -3.243  1.00 39.85  ? 149  MET B CG  1 
ATOM   3746  S SD  . MET B  2 149 ? 9.108   50.490 -3.221  1.00 36.00  ? 149  MET B SD  1 
ATOM   3747  C CE  . MET B  2 149 ? 8.769   51.981 -4.157  1.00 37.27  ? 149  MET B CE  1 
ATOM   3748  N N   . GLU B  2 150 ? 7.370   45.448 -1.539  1.00 44.99  ? 150  GLU B N   1 
ATOM   3749  C CA  . GLU B  2 150 ? 7.193   44.405 -0.533  1.00 46.51  ? 150  GLU B CA  1 
ATOM   3750  C C   . GLU B  2 150 ? 8.370   43.427 -0.500  1.00 46.99  ? 150  GLU B C   1 
ATOM   3751  O O   . GLU B  2 150 ? 8.730   42.943 0.569   1.00 46.13  ? 150  GLU B O   1 
ATOM   3752  C CB  . GLU B  2 150 ? 5.866   43.660 -0.765  1.00 51.77  ? 150  GLU B CB  1 
ATOM   3753  C CG  . GLU B  2 150 ? 5.581   42.490 0.173   1.00 54.30  ? 150  GLU B CG  1 
ATOM   3754  C CD  . GLU B  2 150 ? 5.587   42.871 1.643   1.00 51.21  ? 150  GLU B CD  1 
ATOM   3755  O OE1 . GLU B  2 150 ? 5.370   44.056 1.969   1.00 48.24  ? 150  GLU B OE1 1 
ATOM   3756  O OE2 . GLU B  2 150 ? 5.809   41.976 2.483   1.00 52.31  ? 150  GLU B OE2 1 
ATOM   3757  N N   . SER B  2 151 ? 8.964   43.142 -1.658  1.00 49.04  ? 151  SER B N   1 
ATOM   3758  C CA  . SER B  2 151 ? 10.110  42.229 -1.731  1.00 50.35  ? 151  SER B CA  1 
ATOM   3759  C C   . SER B  2 151 ? 11.330  42.798 -0.995  1.00 46.32  ? 151  SER B C   1 
ATOM   3760  O O   . SER B  2 151 ? 12.139  42.050 -0.438  1.00 46.76  ? 151  SER B O   1 
ATOM   3761  C CB  . SER B  2 151 ? 10.472  41.920 -3.184  1.00 53.38  ? 151  SER B CB  1 
ATOM   3762  O OG  . SER B  2 151 ? 11.058  43.036 -3.822  1.00 50.59  ? 151  SER B OG  1 
ATOM   3763  N N   . VAL B  2 152 ? 11.450  44.124 -0.997  1.00 43.14  ? 152  VAL B N   1 
ATOM   3764  C CA  . VAL B  2 152 ? 12.529  44.805 -0.291  1.00 39.57  ? 152  VAL B CA  1 
ATOM   3765  C C   . VAL B  2 152 ? 12.315  44.679 1.217   1.00 38.42  ? 152  VAL B C   1 
ATOM   3766  O O   . VAL B  2 152 ? 13.260  44.409 1.958   1.00 37.22  ? 152  VAL B O   1 
ATOM   3767  C CB  . VAL B  2 152 ? 12.623  46.294 -0.689  1.00 36.80  ? 152  VAL B CB  1 
ATOM   3768  C CG1 . VAL B  2 152 ? 13.752  46.985 0.065   1.00 33.34  ? 152  VAL B CG1 1 
ATOM   3769  C CG2 . VAL B  2 152 ? 12.831  46.434 -2.193  1.00 38.94  ? 152  VAL B CG2 1 
ATOM   3770  N N   . ARG B  2 153 ? 11.075  44.870 1.665   1.00 39.56  ? 153  ARG B N   1 
ATOM   3771  C CA  . ARG B  2 153 ? 10.737  44.693 3.080   1.00 39.33  ? 153  ARG B CA  1 
ATOM   3772  C C   . ARG B  2 153 ? 10.792  43.212 3.476   1.00 43.60  ? 153  ARG B C   1 
ATOM   3773  O O   . ARG B  2 153 ? 11.249  42.877 4.569   1.00 42.67  ? 153  ARG B O   1 
ATOM   3774  C CB  . ARG B  2 153 ? 9.349   45.264 3.392   1.00 39.56  ? 153  ARG B CB  1 
ATOM   3775  C CG  . ARG B  2 153 ? 9.176   46.740 3.071   1.00 36.98  ? 153  ARG B CG  1 
ATOM   3776  C CD  . ARG B  2 153 ? 7.817   47.259 3.526   1.00 37.94  ? 153  ARG B CD  1 
ATOM   3777  N NE  . ARG B  2 153 ? 7.190   48.084 2.488   1.00 39.05  ? 153  ARG B NE  1 
ATOM   3778  C CZ  . ARG B  2 153 ? 6.223   47.684 1.663   1.00 42.78  ? 153  ARG B CZ  1 
ATOM   3779  N NH1 . ARG B  2 153 ? 5.712   46.458 1.741   1.00 46.01  ? 153  ARG B NH1 1 
ATOM   3780  N NH2 . ARG B  2 153 ? 5.748   48.527 0.752   1.00 43.90  ? 153  ARG B NH2 1 
ATOM   3781  N N   . ASN B  2 154 ? 10.307  42.345 2.585   1.00 49.49  ? 154  ASN B N   1 
ATOM   3782  C CA  . ASN B  2 154 ? 10.453  40.884 2.709   1.00 54.96  ? 154  ASN B CA  1 
ATOM   3783  C C   . ASN B  2 154 ? 11.867  40.437 3.078   1.00 53.43  ? 154  ASN B C   1 
ATOM   3784  O O   . ASN B  2 154 ? 12.047  39.573 3.937   1.00 55.31  ? 154  ASN B O   1 
ATOM   3785  C CB  . ASN B  2 154 ? 10.103  40.196 1.377   1.00 61.56  ? 154  ASN B CB  1 
ATOM   3786  C CG  . ASN B  2 154 ? 8.674   39.689 1.313   1.00 68.75  ? 154  ASN B CG  1 
ATOM   3787  O OD1 . ASN B  2 154 ? 7.917   39.792 2.277   1.00 68.93  ? 154  ASN B OD1 1 
ATOM   3788  N ND2 . ASN B  2 154 ? 8.302   39.124 0.156   1.00 77.22  ? 154  ASN B ND2 1 
ATOM   3789  N N   . GLY B  2 155 ? 12.858  41.037 2.418   1.00 50.30  ? 155  GLY B N   1 
ATOM   3790  C CA  . GLY B  2 155 ? 14.223  40.517 2.386   1.00 50.24  ? 155  GLY B CA  1 
ATOM   3791  C C   . GLY B  2 155 ? 14.456  39.716 1.113   1.00 54.01  ? 155  GLY B C   1 
ATOM   3792  O O   . GLY B  2 155 ? 15.523  39.135 0.928   1.00 55.88  ? 155  GLY B O   1 
ATOM   3793  N N   . THR B  2 156 ? 13.459  39.713 0.228   1.00 55.43  ? 156  THR B N   1 
ATOM   3794  C CA  . THR B  2 156 ? 13.422  38.829 -0.937  1.00 60.19  ? 156  THR B CA  1 
ATOM   3795  C C   . THR B  2 156 ? 13.589  39.591 -2.253  1.00 59.24  ? 156  THR B C   1 
ATOM   3796  O O   . THR B  2 156 ? 13.217  39.093 -3.313  1.00 63.39  ? 156  THR B O   1 
ATOM   3797  C CB  . THR B  2 156 ? 12.077  38.069 -0.972  1.00 64.41  ? 156  THR B CB  1 
ATOM   3798  O OG1 . THR B  2 156 ? 11.824  37.485 0.311   1.00 64.99  ? 156  THR B OG1 1 
ATOM   3799  C CG2 . THR B  2 156 ? 12.071  36.959 -2.034  1.00 70.93  ? 156  THR B CG2 1 
ATOM   3800  N N   . TYR B  2 157 ? 14.153  40.794 -2.198  1.00 54.31  ? 157  TYR B N   1 
ATOM   3801  C CA  . TYR B  2 157 ? 14.326  41.599 -3.406  1.00 53.67  ? 157  TYR B CA  1 
ATOM   3802  C C   . TYR B  2 157 ? 15.186  40.851 -4.418  1.00 57.75  ? 157  TYR B C   1 
ATOM   3803  O O   . TYR B  2 157 ? 16.378  40.647 -4.195  1.00 57.69  ? 157  TYR B O   1 
ATOM   3804  C CB  . TYR B  2 157 ? 14.961  42.954 -3.085  1.00 48.60  ? 157  TYR B CB  1 
ATOM   3805  C CG  . TYR B  2 157 ? 15.231  43.792 -4.318  1.00 48.59  ? 157  TYR B CG  1 
ATOM   3806  C CD1 . TYR B  2 157 ? 14.191  44.428 -4.990  1.00 48.82  ? 157  TYR B CD1 1 
ATOM   3807  C CD2 . TYR B  2 157 ? 16.521  43.939 -4.818  1.00 48.98  ? 157  TYR B CD2 1 
ATOM   3808  C CE1 . TYR B  2 157 ? 14.429  45.192 -6.122  1.00 49.38  ? 157  TYR B CE1 1 
ATOM   3809  C CE2 . TYR B  2 157 ? 16.770  44.701 -5.948  1.00 49.60  ? 157  TYR B CE2 1 
ATOM   3810  C CZ  . TYR B  2 157 ? 15.723  45.325 -6.596  1.00 49.75  ? 157  TYR B CZ  1 
ATOM   3811  O OH  . TYR B  2 157 ? 15.969  46.080 -7.720  1.00 50.78  ? 157  TYR B OH  1 
ATOM   3812  N N   . ASP B  2 158 ? 14.575  40.450 -5.529  1.00 61.76  ? 158  ASP B N   1 
ATOM   3813  C CA  . ASP B  2 158 ? 15.263  39.641 -6.529  1.00 66.71  ? 158  ASP B CA  1 
ATOM   3814  C C   . ASP B  2 158 ? 16.159  40.507 -7.416  1.00 65.72  ? 158  ASP B C   1 
ATOM   3815  O O   . ASP B  2 158 ? 15.749  40.951 -8.497  1.00 67.14  ? 158  ASP B O   1 
ATOM   3816  C CB  . ASP B  2 158 ? 14.260  38.854 -7.379  1.00 72.03  ? 158  ASP B CB  1 
ATOM   3817  C CG  . ASP B  2 158 ? 14.904  37.691 -8.103  1.00 78.19  ? 158  ASP B CG  1 
ATOM   3818  O OD1 . ASP B  2 158 ? 15.483  36.817 -7.422  1.00 80.06  ? 158  ASP B OD1 1 
ATOM   3819  O OD2 . ASP B  2 158 ? 14.832  37.644 -9.348  1.00 81.67  ? 158  ASP B OD2 1 
ATOM   3820  N N   . TYR B  2 159 ? 17.386  40.731 -6.945  1.00 63.83  ? 159  TYR B N   1 
ATOM   3821  C CA  . TYR B  2 159 ? 18.369  41.556 -7.654  1.00 63.05  ? 159  TYR B CA  1 
ATOM   3822  C C   . TYR B  2 159 ? 18.556  41.135 -9.125  1.00 68.31  ? 159  TYR B C   1 
ATOM   3823  O O   . TYR B  2 159 ? 18.438  41.979 -10.015 1.00 68.05  ? 159  TYR B O   1 
ATOM   3824  C CB  . TYR B  2 159 ? 19.707  41.580 -6.886  1.00 61.70  ? 159  TYR B CB  1 
ATOM   3825  C CG  . TYR B  2 159 ? 20.859  42.203 -7.642  1.00 62.51  ? 159  TYR B CG  1 
ATOM   3826  C CD1 . TYR B  2 159 ? 21.650  41.441 -8.504  1.00 67.86  ? 159  TYR B CD1 1 
ATOM   3827  C CD2 . TYR B  2 159 ? 21.162  43.553 -7.492  1.00 58.54  ? 159  TYR B CD2 1 
ATOM   3828  C CE1 . TYR B  2 159 ? 22.703  42.010 -9.200  1.00 69.22  ? 159  TYR B CE1 1 
ATOM   3829  C CE2 . TYR B  2 159 ? 22.215  44.129 -8.180  1.00 59.96  ? 159  TYR B CE2 1 
ATOM   3830  C CZ  . TYR B  2 159 ? 22.982  43.353 -9.033  1.00 65.32  ? 159  TYR B CZ  1 
ATOM   3831  O OH  . TYR B  2 159 ? 24.033  43.909 -9.723  1.00 67.39  ? 159  TYR B OH  1 
ATOM   3832  N N   . PRO B  2 160 ? 18.825  39.834 -9.387  1.00 73.59  ? 160  PRO B N   1 
ATOM   3833  C CA  . PRO B  2 160 ? 19.010  39.370 -10.777 1.00 79.27  ? 160  PRO B CA  1 
ATOM   3834  C C   . PRO B  2 160 ? 17.863  39.659 -11.766 1.00 80.63  ? 160  PRO B C   1 
ATOM   3835  O O   . PRO B  2 160 ? 18.112  39.719 -12.974 1.00 84.26  ? 160  PRO B O   1 
ATOM   3836  C CB  . PRO B  2 160 ? 19.194  37.858 -10.617 1.00 84.76  ? 160  PRO B CB  1 
ATOM   3837  C CG  . PRO B  2 160 ? 19.786  37.701 -9.263  1.00 82.01  ? 160  PRO B CG  1 
ATOM   3838  C CD  . PRO B  2 160 ? 19.130  38.759 -8.420  1.00 75.13  ? 160  PRO B CD  1 
ATOM   3839  N N   . GLN B  2 161 ? 16.633  39.813 -11.273 1.00 78.43  ? 161  GLN B N   1 
ATOM   3840  C CA  . GLN B  2 161 ? 15.484  40.119 -12.142 1.00 79.98  ? 161  GLN B CA  1 
ATOM   3841  C C   . GLN B  2 161 ? 15.523  41.563 -12.638 1.00 76.66  ? 161  GLN B C   1 
ATOM   3842  O O   . GLN B  2 161 ? 15.287  41.828 -13.819 1.00 79.53  ? 161  GLN B O   1 
ATOM   3843  C CB  . GLN B  2 161 ? 14.159  39.861 -11.412 1.00 79.17  ? 161  GLN B CB  1 
ATOM   3844  C CG  . GLN B  2 161 ? 12.906  40.248 -12.195 1.00 80.78  ? 161  GLN B CG  1 
ATOM   3845  C CD  . GLN B  2 161 ? 11.633  40.097 -11.381 1.00 80.03  ? 161  GLN B CD  1 
ATOM   3846  O OE1 . GLN B  2 161 ? 11.639  40.245 -10.157 1.00 76.09  ? 161  GLN B OE1 1 
ATOM   3847  N NE2 . GLN B  2 161 ? 10.529  39.807 -12.061 1.00 84.25  ? 161  GLN B NE2 1 
ATOM   3848  N N   . TYR B  2 162 ? 15.814  42.488 -11.727 1.00 71.09  ? 162  TYR B N   1 
ATOM   3849  C CA  . TYR B  2 162 ? 15.832  43.912 -12.048 1.00 68.19  ? 162  TYR B CA  1 
ATOM   3850  C C   . TYR B  2 162 ? 17.212  44.408 -12.509 1.00 68.52  ? 162  TYR B C   1 
ATOM   3851  O O   . TYR B  2 162 ? 17.411  45.615 -12.676 1.00 66.46  ? 162  TYR B O   1 
ATOM   3852  C CB  . TYR B  2 162 ? 15.360  44.720 -10.833 1.00 62.73  ? 162  TYR B CB  1 
ATOM   3853  C CG  . TYR B  2 162 ? 13.972  44.348 -10.345 1.00 62.75  ? 162  TYR B CG  1 
ATOM   3854  C CD1 . TYR B  2 162 ? 12.832  44.768 -11.032 1.00 64.34  ? 162  TYR B CD1 1 
ATOM   3855  C CD2 . TYR B  2 162 ? 13.799  43.578 -9.194  1.00 61.74  ? 162  TYR B CD2 1 
ATOM   3856  C CE1 . TYR B  2 162 ? 11.560  44.430 -10.586 1.00 65.07  ? 162  TYR B CE1 1 
ATOM   3857  C CE2 . TYR B  2 162 ? 12.532  43.234 -8.741  1.00 62.36  ? 162  TYR B CE2 1 
ATOM   3858  C CZ  . TYR B  2 162 ? 11.416  43.662 -9.437  1.00 64.08  ? 162  TYR B CZ  1 
ATOM   3859  O OH  . TYR B  2 162 ? 10.157  43.323 -8.987  1.00 65.29  ? 162  TYR B OH  1 
ATOM   3860  N N   . SER B  2 163 ? 18.156  43.485 -12.708 1.00 71.84  ? 163  SER B N   1 
ATOM   3861  C CA  . SER B  2 163 ? 19.505  43.821 -13.179 1.00 73.21  ? 163  SER B CA  1 
ATOM   3862  C C   . SER B  2 163 ? 19.666  43.414 -14.645 1.00 79.05  ? 163  SER B C   1 
ATOM   3863  O O   . SER B  2 163 ? 20.780  43.339 -15.164 1.00 81.96  ? 163  SER B O   1 
ATOM   3864  C CB  . SER B  2 163 ? 20.567  43.125 -12.302 1.00 73.28  ? 163  SER B CB  1 
ATOM   3865  O OG  . SER B  2 163 ? 20.875  41.834 -12.794 1.00 78.93  ? 163  SER B OG  1 
ATOM   3866  N N   . ASP C  1 1   ? 34.655  32.887 -8.587  1.00 35.03  ? 1    ASP C N   1 
ATOM   3867  C CA  . ASP C  1 1   ? 35.560  32.915 -7.403  1.00 35.19  ? 1    ASP C CA  1 
ATOM   3868  C C   . ASP C  1 1   ? 35.090  33.957 -6.393  1.00 32.74  ? 1    ASP C C   1 
ATOM   3869  O O   . ASP C  1 1   ? 34.569  35.003 -6.776  1.00 31.12  ? 1    ASP C O   1 
ATOM   3870  C CB  . ASP C  1 1   ? 37.001  33.207 -7.833  1.00 36.59  ? 1    ASP C CB  1 
ATOM   3871  C CG  . ASP C  1 1   ? 37.544  32.177 -8.810  1.00 39.34  ? 1    ASP C CG  1 
ATOM   3872  O OD1 . ASP C  1 1   ? 36.827  31.204 -9.131  1.00 40.18  ? 1    ASP C OD1 1 
ATOM   3873  O OD2 . ASP C  1 1   ? 38.693  32.348 -9.264  1.00 40.91  ? 1    ASP C OD2 1 
ATOM   3874  N N   . GLN C  1 2   ? 35.270  33.663 -5.107  1.00 32.66  ? 2    GLN C N   1 
ATOM   3875  C CA  . GLN C  1 2   ? 34.847  34.579 -4.045  1.00 30.56  ? 2    GLN C CA  1 
ATOM   3876  C C   . GLN C  1 2   ? 35.648  34.436 -2.756  1.00 30.86  ? 2    GLN C C   1 
ATOM   3877  O O   . GLN C  1 2   ? 36.153  33.360 -2.440  1.00 32.61  ? 2    GLN C O   1 
ATOM   3878  C CB  . GLN C  1 2   ? 33.356  34.400 -3.739  1.00 29.42  ? 2    GLN C CB  1 
ATOM   3879  C CG  . GLN C  1 2   ? 32.993  33.102 -3.035  1.00 30.57  ? 2    GLN C CG  1 
ATOM   3880  C CD  . GLN C  1 2   ? 31.567  33.089 -2.519  1.00 29.50  ? 2    GLN C CD  1 
ATOM   3881  O OE1 . GLN C  1 2   ? 31.302  32.556 -1.447  1.00 29.68  ? 2    GLN C OE1 1 
ATOM   3882  N NE2 . GLN C  1 2   ? 30.643  33.671 -3.276  1.00 28.62  ? 2    GLN C NE2 1 
ATOM   3883  N N   . ILE C  1 3   ? 35.750  35.540 -2.023  1.00 29.31  ? 3    ILE C N   1 
ATOM   3884  C CA  . ILE C  1 3   ? 36.343  35.546 -0.693  1.00 29.31  ? 3    ILE C CA  1 
ATOM   3885  C C   . ILE C  1 3   ? 35.323  36.093 0.302   1.00 27.29  ? 3    ILE C C   1 
ATOM   3886  O O   . ILE C  1 3   ? 34.635  37.067 0.015   1.00 25.80  ? 3    ILE C O   1 
ATOM   3887  C CB  . ILE C  1 3   ? 37.651  36.367 -0.646  1.00 29.86  ? 3    ILE C CB  1 
ATOM   3888  C CG1 . ILE C  1 3   ? 38.409  36.087 0.658   1.00 30.48  ? 3    ILE C CG1 1 
ATOM   3889  C CG2 . ILE C  1 3   ? 37.378  37.858 -0.797  1.00 28.17  ? 3    ILE C CG2 1 
ATOM   3890  C CD1 . ILE C  1 3   ? 39.857  36.526 0.632   1.00 31.98  ? 3    ILE C CD1 1 
ATOM   3891  N N   . CYS C  1 4   ? 35.223  35.450 1.463   1.00 27.47  ? 4    CYS C N   1 
ATOM   3892  C CA  . CYS C  1 4   ? 34.255  35.835 2.481   1.00 25.87  ? 4    CYS C CA  1 
ATOM   3893  C C   . CYS C  1 4   ? 34.956  36.206 3.766   1.00 25.44  ? 4    CYS C C   1 
ATOM   3894  O O   . CYS C  1 4   ? 36.054  35.731 4.036   1.00 26.81  ? 4    CYS C O   1 
ATOM   3895  C CB  . CYS C  1 4   ? 33.281  34.693 2.765   1.00 26.50  ? 4    CYS C CB  1 
ATOM   3896  S SG  . CYS C  1 4   ? 32.473  34.025 1.300   1.00 27.56  ? 4    CYS C SG  1 
ATOM   3897  N N   . ILE C  1 5   ? 34.306  37.057 4.555   1.00 23.69  ? 5    ILE C N   1 
ATOM   3898  C CA  . ILE C  1 5   ? 34.764  37.376 5.896   1.00 23.20  ? 5    ILE C CA  1 
ATOM   3899  C C   . ILE C  1 5   ? 33.793  36.750 6.882   1.00 22.70  ? 5    ILE C C   1 
ATOM   3900  O O   . ILE C  1 5   ? 32.577  36.812 6.693   1.00 21.96  ? 5    ILE C O   1 
ATOM   3901  C CB  . ILE C  1 5   ? 34.823  38.892 6.129   1.00 21.91  ? 5    ILE C CB  1 
ATOM   3902  C CG1 . ILE C  1 5   ? 35.673  39.558 5.052   1.00 22.54  ? 5    ILE C CG1 1 
ATOM   3903  C CG2 . ILE C  1 5   ? 35.371  39.210 7.515   1.00 21.67  ? 5    ILE C CG2 1 
ATOM   3904  C CD1 . ILE C  1 5   ? 37.142  39.236 5.150   1.00 24.20  ? 5    ILE C CD1 1 
ATOM   3905  N N   . GLY C  1 6   ? 34.335  36.150 7.935   1.00 23.28  ? 6    GLY C N   1 
ATOM   3906  C CA  . GLY C  1 6   ? 33.518  35.446 8.911   1.00 23.15  ? 6    GLY C CA  1 
ATOM   3907  C C   . GLY C  1 6   ? 34.224  35.254 10.228  1.00 23.40  ? 6    GLY C C   1 
ATOM   3908  O O   . GLY C  1 6   ? 35.350  35.707 10.416  1.00 23.68  ? 6    GLY C O   1 
ATOM   3909  N N   . TYR C  1 7   ? 33.556  34.559 11.134  1.00 23.51  ? 7    TYR C N   1 
ATOM   3910  C CA  . TYR C  1 7   ? 34.009  34.471 12.510  1.00 23.55  ? 7    TYR C CA  1 
ATOM   3911  C C   . TYR C  1 7   ? 33.868  33.063 13.059  1.00 25.17  ? 7    TYR C C   1 
ATOM   3912  O O   . TYR C  1 7   ? 33.179  32.223 12.485  1.00 26.07  ? 7    TYR C O   1 
ATOM   3913  C CB  . TYR C  1 7   ? 33.242  35.477 13.383  1.00 21.72  ? 7    TYR C CB  1 
ATOM   3914  C CG  . TYR C  1 7   ? 31.728  35.368 13.313  1.00 21.12  ? 7    TYR C CG  1 
ATOM   3915  C CD1 . TYR C  1 7   ? 31.004  36.032 12.333  1.00 20.35  ? 7    TYR C CD1 1 
ATOM   3916  C CD2 . TYR C  1 7   ? 31.026  34.617 14.238  1.00 21.56  ? 7    TYR C CD2 1 
ATOM   3917  C CE1 . TYR C  1 7   ? 29.627  35.934 12.269  1.00 20.15  ? 7    TYR C CE1 1 
ATOM   3918  C CE2 . TYR C  1 7   ? 29.648  34.516 14.184  1.00 21.40  ? 7    TYR C CE2 1 
ATOM   3919  C CZ  . TYR C  1 7   ? 28.956  35.175 13.201  1.00 20.73  ? 7    TYR C CZ  1 
ATOM   3920  O OH  . TYR C  1 7   ? 27.587  35.067 13.154  1.00 20.90  ? 7    TYR C OH  1 
ATOM   3921  N N   . HIS C  1 8   ? 34.523  32.831 14.189  1.00 25.71  ? 8    HIS C N   1 
ATOM   3922  C CA  . HIS C  1 8   ? 34.629  31.510 14.795  1.00 27.60  ? 8    HIS C CA  1 
ATOM   3923  C C   . HIS C  1 8   ? 33.305  31.039 15.399  1.00 27.46  ? 8    HIS C C   1 
ATOM   3924  O O   . HIS C  1 8   ? 32.544  31.832 15.939  1.00 25.81  ? 8    HIS C O   1 
ATOM   3925  C CB  . HIS C  1 8   ? 35.716  31.550 15.879  1.00 28.09  ? 8    HIS C CB  1 
ATOM   3926  C CG  . HIS C  1 8   ? 35.988  30.228 16.529  1.00 30.24  ? 8    HIS C CG  1 
ATOM   3927  N ND1 . HIS C  1 8   ? 36.509  29.152 15.843  1.00 32.65  ? 8    HIS C ND1 1 
ATOM   3928  C CD2 . HIS C  1 8   ? 35.835  29.817 17.811  1.00 30.52  ? 8    HIS C CD2 1 
ATOM   3929  C CE1 . HIS C  1 8   ? 36.651  28.131 16.669  1.00 34.41  ? 8    HIS C CE1 1 
ATOM   3930  N NE2 . HIS C  1 8   ? 36.251  28.509 17.870  1.00 33.11  ? 8    HIS C NE2 1 
ATOM   3931  N N   . ALA C  1 9   ? 33.034  29.743 15.280  1.00 29.52  ? 9    ALA C N   1 
ATOM   3932  C CA  . ALA C  1 9   ? 31.971  29.086 16.038  1.00 30.10  ? 9    ALA C CA  1 
ATOM   3933  C C   . ALA C  1 9   ? 32.530  27.778 16.568  1.00 32.68  ? 9    ALA C C   1 
ATOM   3934  O O   . ALA C  1 9   ? 33.567  27.315 16.100  1.00 34.16  ? 9    ALA C O   1 
ATOM   3935  C CB  . ALA C  1 9   ? 30.758  28.831 15.165  1.00 30.35  ? 9    ALA C CB  1 
ATOM   3936  N N   . ASN C  1 10  ? 31.861  27.193 17.552  1.00 33.48  ? 10   ASN C N   1 
ATOM   3937  C CA  . ASN C  1 10  ? 32.308  25.929 18.120  1.00 36.19  ? 10   ASN C CA  1 
ATOM   3938  C C   . ASN C  1 10  ? 31.183  25.204 18.852  1.00 37.37  ? 10   ASN C C   1 
ATOM   3939  O O   . ASN C  1 10  ? 30.042  25.665 18.847  1.00 36.20  ? 10   ASN C O   1 
ATOM   3940  C CB  . ASN C  1 10  ? 33.522  26.149 19.036  1.00 36.11  ? 10   ASN C CB  1 
ATOM   3941  C CG  . ASN C  1 10  ? 33.188  26.937 20.287  1.00 34.19  ? 10   ASN C CG  1 
ATOM   3942  O OD1 . ASN C  1 10  ? 32.028  27.227 20.573  1.00 33.14  ? 10   ASN C OD1 1 
ATOM   3943  N ND2 . ASN C  1 10  ? 34.215  27.281 21.047  1.00 33.96  ? 10   ASN C ND2 1 
ATOM   3944  N N   . ASN C  1 11  ? 31.512  24.074 19.476  1.00 39.99  ? 11   ASN C N   1 
ATOM   3945  C CA  . ASN C  1 11  ? 30.521  23.243 20.161  1.00 41.72  ? 11   ASN C CA  1 
ATOM   3946  C C   . ASN C  1 11  ? 30.293  23.632 21.635  1.00 40.65  ? 11   ASN C C   1 
ATOM   3947  O O   . ASN C  1 11  ? 29.775  22.834 22.416  1.00 42.40  ? 11   ASN C O   1 
ATOM   3948  C CB  . ASN C  1 11  ? 30.908  21.757 20.031  1.00 45.45  ? 11   ASN C CB  1 
ATOM   3949  C CG  . ASN C  1 11  ? 32.233  21.424 20.707  1.00 46.58  ? 11   ASN C CG  1 
ATOM   3950  O OD1 . ASN C  1 11  ? 32.850  22.277 21.354  1.00 44.63  ? 11   ASN C OD1 1 
ATOM   3951  N ND2 . ASN C  1 11  ? 32.679  20.174 20.560  1.00 50.03  ? 11   ASN C ND2 1 
ATOM   3952  N N   . SER C  1 12  ? 30.667  24.861 21.999  1.00 37.96  ? 12   SER C N   1 
ATOM   3953  C CA  . SER C  1 12  ? 30.509  25.367 23.365  1.00 36.76  ? 12   SER C CA  1 
ATOM   3954  C C   . SER C  1 12  ? 29.048  25.664 23.669  1.00 36.11  ? 12   SER C C   1 
ATOM   3955  O O   . SER C  1 12  ? 28.304  26.097 22.791  1.00 35.36  ? 12   SER C O   1 
ATOM   3956  C CB  . SER C  1 12  ? 31.336  26.646 23.566  1.00 34.29  ? 12   SER C CB  1 
ATOM   3957  O OG  . SER C  1 12  ? 31.184  27.182 24.871  1.00 33.12  ? 12   SER C OG  1 
ATOM   3958  N N   . THR C  1 13  ? 28.652  25.419 24.919  1.00 36.65  ? 13   THR C N   1 
ATOM   3959  C CA  . THR C  1 13  ? 27.312  25.747 25.414  1.00 36.21  ? 13   THR C CA  1 
ATOM   3960  C C   . THR C  1 13  ? 27.359  26.732 26.583  1.00 34.23  ? 13   THR C C   1 
ATOM   3961  O O   . THR C  1 13  ? 26.330  26.998 27.205  1.00 34.07  ? 13   THR C O   1 
ATOM   3962  C CB  . THR C  1 13  ? 26.560  24.482 25.876  1.00 39.15  ? 13   THR C CB  1 
ATOM   3963  O OG1 . THR C  1 13  ? 27.396  23.722 26.759  1.00 40.58  ? 13   THR C OG1 1 
ATOM   3964  C CG2 . THR C  1 13  ? 26.163  23.626 24.684  1.00 41.23  ? 13   THR C CG2 1 
ATOM   3965  N N   . GLU C  1 14  ? 28.542  27.271 26.882  1.00 32.96  ? 14   GLU C N   1 
ATOM   3966  C CA  . GLU C  1 14  ? 28.688  28.253 27.953  1.00 31.15  ? 14   GLU C CA  1 
ATOM   3967  C C   . GLU C  1 14  ? 27.902  29.516 27.640  1.00 29.01  ? 14   GLU C C   1 
ATOM   3968  O O   . GLU C  1 14  ? 27.972  30.037 26.529  1.00 28.14  ? 14   GLU C O   1 
ATOM   3969  C CB  . GLU C  1 14  ? 30.154  28.624 28.168  1.00 30.51  ? 14   GLU C CB  1 
ATOM   3970  C CG  . GLU C  1 14  ? 30.999  27.516 28.775  1.00 32.69  ? 14   GLU C CG  1 
ATOM   3971  C CD  . GLU C  1 14  ? 31.984  28.041 29.810  1.00 32.00  ? 14   GLU C CD  1 
ATOM   3972  O OE1 . GLU C  1 14  ? 31.538  28.368 30.940  1.00 31.39  ? 14   GLU C OE1 1 
ATOM   3973  O OE2 . GLU C  1 14  ? 33.194  28.146 29.488  1.00 32.23  ? 14   GLU C OE2 1 
ATOM   3974  N N   . GLN C  1 15  ? 27.164  30.006 28.630  1.00 28.36  ? 15   GLN C N   1 
ATOM   3975  C CA  . GLN C  1 15  ? 26.330  31.185 28.466  1.00 26.76  ? 15   GLN C CA  1 
ATOM   3976  C C   . GLN C  1 15  ? 26.771  32.295 29.400  1.00 24.99  ? 15   GLN C C   1 
ATOM   3977  O O   . GLN C  1 15  ? 27.347  32.037 30.452  1.00 25.19  ? 15   GLN C O   1 
ATOM   3978  C CB  . GLN C  1 15  ? 24.876  30.840 28.759  1.00 28.02  ? 15   GLN C CB  1 
ATOM   3979  C CG  . GLN C  1 15  ? 24.350  29.667 27.956  1.00 30.15  ? 15   GLN C CG  1 
ATOM   3980  C CD  . GLN C  1 15  ? 22.894  29.388 28.232  1.00 31.67  ? 15   GLN C CD  1 
ATOM   3981  O OE1 . GLN C  1 15  ? 22.116  29.142 27.313  1.00 32.69  ? 15   GLN C OE1 1 
ATOM   3982  N NE2 . GLN C  1 15  ? 22.513  29.429 29.498  1.00 32.05  ? 15   GLN C NE2 1 
ATOM   3983  N N   . VAL C  1 16  ? 26.494  33.532 29.002  1.00 23.39  ? 16   VAL C N   1 
ATOM   3984  C CA  . VAL C  1 16  ? 26.753  34.694 29.844  1.00 21.97  ? 16   VAL C CA  1 
ATOM   3985  C C   . VAL C  1 16  ? 25.548  35.614 29.792  1.00 21.50  ? 16   VAL C C   1 
ATOM   3986  O O   . VAL C  1 16  ? 24.785  35.577 28.830  1.00 21.85  ? 16   VAL C O   1 
ATOM   3987  C CB  . VAL C  1 16  ? 28.009  35.471 29.397  1.00 20.70  ? 16   VAL C CB  1 
ATOM   3988  C CG1 . VAL C  1 16  ? 29.228  34.563 29.401  1.00 21.50  ? 16   VAL C CG1 1 
ATOM   3989  C CG2 . VAL C  1 16  ? 27.811  36.093 28.023  1.00 20.03  ? 16   VAL C CG2 1 
ATOM   3990  N N   . ASP C  1 17  ? 25.383  36.430 30.830  1.00 20.94  ? 17   ASP C N   1 
ATOM   3991  C CA  . ASP C  1 17  ? 24.318  37.422 30.876  1.00 20.71  ? 17   ASP C CA  1 
ATOM   3992  C C   . ASP C  1 17  ? 24.857  38.805 30.515  1.00 19.28  ? 17   ASP C C   1 
ATOM   3993  O O   . ASP C  1 17  ? 26.029  39.116 30.742  1.00 18.45  ? 17   ASP C O   1 
ATOM   3994  C CB  . ASP C  1 17  ? 23.676  37.472 32.265  1.00 21.37  ? 17   ASP C CB  1 
ATOM   3995  C CG  . ASP C  1 17  ? 22.833  36.238 32.583  1.00 23.22  ? 17   ASP C CG  1 
ATOM   3996  O OD1 . ASP C  1 17  ? 22.225  35.642 31.665  1.00 24.20  ? 17   ASP C OD1 1 
ATOM   3997  O OD2 . ASP C  1 17  ? 22.761  35.876 33.778  1.00 23.89  ? 17   ASP C OD2 1 
ATOM   3998  N N   . THR C  1 18  ? 23.979  39.615 29.933  1.00 19.26  ? 18   THR C N   1 
ATOM   3999  C CA  . THR C  1 18  ? 24.241  41.017 29.636  1.00 18.33  ? 18   THR C CA  1 
ATOM   4000  C C   . THR C  1 18  ? 23.030  41.814 30.111  1.00 19.05  ? 18   THR C C   1 
ATOM   4001  O O   . THR C  1 18  ? 22.057  41.237 30.597  1.00 20.23  ? 18   THR C O   1 
ATOM   4002  C CB  . THR C  1 18  ? 24.436  41.244 28.122  1.00 17.86  ? 18   THR C CB  1 
ATOM   4003  O OG1 . THR C  1 18  ? 23.198  41.047 27.435  1.00 18.66  ? 18   THR C OG1 1 
ATOM   4004  C CG2 . THR C  1 18  ? 25.469  40.292 27.562  1.00 17.68  ? 18   THR C CG2 1 
ATOM   4005  N N   . ILE C  1 19  ? 23.071  43.130 29.952  1.00 18.73  ? 19   ILE C N   1 
ATOM   4006  C CA  . ILE C  1 19  ? 21.956  43.980 30.368  1.00 19.70  ? 19   ILE C CA  1 
ATOM   4007  C C   . ILE C  1 19  ? 20.681  43.652 29.577  1.00 20.98  ? 19   ILE C C   1 
ATOM   4008  O O   . ILE C  1 19  ? 19.617  43.440 30.155  1.00 22.23  ? 19   ILE C O   1 
ATOM   4009  C CB  . ILE C  1 19  ? 22.295  45.480 30.188  1.00 19.26  ? 19   ILE C CB  1 
ATOM   4010  C CG1 . ILE C  1 19  ? 23.468  45.897 31.088  1.00 18.52  ? 19   ILE C CG1 1 
ATOM   4011  C CG2 . ILE C  1 19  ? 21.081  46.353 30.477  1.00 20.49  ? 19   ILE C CG2 1 
ATOM   4012  C CD1 . ILE C  1 19  ? 23.131  46.026 32.560  1.00 19.09  ? 19   ILE C CD1 1 
ATOM   4013  N N   . MET C  1 20  ? 20.804  43.612 28.252  1.00 20.86  ? 20   MET C N   1 
ATOM   4014  C CA  . MET C  1 20  ? 19.649  43.459 27.374  1.00 22.17  ? 20   MET C CA  1 
ATOM   4015  C C   . MET C  1 20  ? 19.251  42.014 27.103  1.00 23.32  ? 20   MET C C   1 
ATOM   4016  O O   . MET C  1 20  ? 18.133  41.758 26.653  1.00 24.69  ? 20   MET C O   1 
ATOM   4017  C CB  . MET C  1 20  ? 19.925  44.124 26.033  1.00 21.49  ? 20   MET C CB  1 
ATOM   4018  C CG  . MET C  1 20  ? 20.124  45.620 26.100  1.00 21.16  ? 20   MET C CG  1 
ATOM   4019  S SD  . MET C  1 20  ? 20.027  46.318 24.444  1.00 21.05  ? 20   MET C SD  1 
ATOM   4020  C CE  . MET C  1 20  ? 20.829  47.898 24.715  1.00 20.59  ? 20   MET C CE  1 
ATOM   4021  N N   . GLU C  1 21  ? 20.163  41.075 27.337  1.00 23.15  ? 21   GLU C N   1 
ATOM   4022  C CA  . GLU C  1 21  ? 19.905  39.678 27.010  1.00 24.51  ? 21   GLU C CA  1 
ATOM   4023  C C   . GLU C  1 21  ? 20.577  38.745 28.003  1.00 25.01  ? 21   GLU C C   1 
ATOM   4024  O O   . GLU C  1 21  ? 21.726  38.958 28.395  1.00 23.72  ? 21   GLU C O   1 
ATOM   4025  C CB  . GLU C  1 21  ? 20.386  39.374 25.592  1.00 23.95  ? 21   GLU C CB  1 
ATOM   4026  C CG  . GLU C  1 21  ? 19.729  38.153 24.965  1.00 25.44  ? 21   GLU C CG  1 
ATOM   4027  C CD  . GLU C  1 21  ? 20.153  37.916 23.516  1.00 25.04  ? 21   GLU C CD  1 
ATOM   4028  O OE1 . GLU C  1 21  ? 20.803  38.801 22.912  1.00 23.62  ? 21   GLU C OE1 1 
ATOM   4029  O OE2 . GLU C  1 21  ? 19.834  36.831 22.980  1.00 26.24  ? 21   GLU C OE2 1 
ATOM   4030  N N   . LYS C  1 22  ? 19.846  37.706 28.397  1.00 27.31  ? 22   LYS C N   1 
ATOM   4031  C CA  . LYS C  1 22  ? 20.355  36.717 29.333  1.00 28.37  ? 22   LYS C CA  1 
ATOM   4032  C C   . LYS C  1 22  ? 20.538  35.379 28.642  1.00 29.92  ? 22   LYS C C   1 
ATOM   4033  O O   . LYS C  1 22  ? 19.917  35.119 27.617  1.00 30.74  ? 22   LYS C O   1 
ATOM   4034  C CB  . LYS C  1 22  ? 19.406  36.590 30.523  1.00 29.88  ? 22   LYS C CB  1 
ATOM   4035  C CG  . LYS C  1 22  ? 19.534  37.744 31.507  1.00 29.07  ? 22   LYS C CG  1 
ATOM   4036  C CD  . LYS C  1 22  ? 18.276  37.930 32.337  1.00 30.91  ? 22   LYS C CD  1 
ATOM   4037  C CE  . LYS C  1 22  ? 17.921  36.663 33.104  1.00 32.82  ? 22   LYS C CE  1 
ATOM   4038  N NZ  . LYS C  1 22  ? 16.956  36.907 34.214  1.00 34.38  ? 22   LYS C NZ  1 
ATOM   4039  N N   . ASN C  1 23  ? 21.409  34.546 29.202  1.00 30.83  ? 23   ASN C N   1 
ATOM   4040  C CA  . ASN C  1 23  ? 21.675  33.215 28.669  1.00 32.77  ? 23   ASN C CA  1 
ATOM   4041  C C   . ASN C  1 23  ? 22.146  33.245 27.204  1.00 31.15  ? 23   ASN C C   1 
ATOM   4042  O O   . ASN C  1 23  ? 21.661  32.486 26.367  1.00 32.32  ? 23   ASN C O   1 
ATOM   4043  C CB  . ASN C  1 23  ? 20.435  32.315 28.848  1.00 36.85  ? 23   ASN C CB  1 
ATOM   4044  C CG  . ASN C  1 23  ? 20.123  32.013 30.308  1.00 40.05  ? 23   ASN C CG  1 
ATOM   4045  O OD1 . ASN C  1 23  ? 20.976  32.187 31.184  1.00 39.23  ? 23   ASN C OD1 1 
ATOM   4046  N ND2 . ASN C  1 23  ? 18.891  31.547 30.578  1.00 45.28  ? 23   ASN C ND2 1 
ATOM   4047  N N   . VAL C  1 24  ? 23.096  34.133 26.913  1.00 28.31  ? 24   VAL C N   1 
ATOM   4048  C CA  . VAL C  1 24  ? 23.715  34.236 25.585  1.00 26.97  ? 24   VAL C CA  1 
ATOM   4049  C C   . VAL C  1 24  ? 24.848  33.219 25.446  1.00 26.99  ? 24   VAL C C   1 
ATOM   4050  O O   . VAL C  1 24  ? 25.835  33.294 26.172  1.00 26.34  ? 24   VAL C O   1 
ATOM   4051  C CB  . VAL C  1 24  ? 24.300  35.648 25.346  1.00 24.96  ? 24   VAL C CB  1 
ATOM   4052  C CG1 . VAL C  1 24  ? 25.099  35.698 24.050  1.00 24.40  ? 24   VAL C CG1 1 
ATOM   4053  C CG2 . VAL C  1 24  ? 23.194  36.694 25.330  1.00 24.64  ? 24   VAL C CG2 1 
ATOM   4054  N N   . THR C  1 25  ? 24.717  32.284 24.508  1.00 27.72  ? 25   THR C N   1 
ATOM   4055  C CA  . THR C  1 25  ? 25.732  31.245 24.314  1.00 28.33  ? 25   THR C CA  1 
ATOM   4056  C C   . THR C  1 25  ? 26.962  31.821 23.629  1.00 26.74  ? 25   THR C C   1 
ATOM   4057  O O   . THR C  1 25  ? 26.847  32.424 22.562  1.00 25.88  ? 25   THR C O   1 
ATOM   4058  C CB  . THR C  1 25  ? 25.213  30.082 23.448  1.00 30.32  ? 25   THR C CB  1 
ATOM   4059  O OG1 . THR C  1 25  ? 23.915  29.680 23.898  1.00 31.68  ? 25   THR C OG1 1 
ATOM   4060  C CG2 . THR C  1 25  ? 26.162  28.899 23.525  1.00 31.89  ? 25   THR C CG2 1 
ATOM   4061  N N   . VAL C  1 26  ? 28.132  31.622 24.237  1.00 26.42  ? 26   VAL C N   1 
ATOM   4062  C CA  . VAL C  1 26  ? 29.387  32.159 23.705  1.00 25.32  ? 26   VAL C CA  1 
ATOM   4063  C C   . VAL C  1 26  ? 30.396  31.053 23.441  1.00 26.84  ? 26   VAL C C   1 
ATOM   4064  O O   . VAL C  1 26  ? 30.271  29.949 23.964  1.00 28.54  ? 26   VAL C O   1 
ATOM   4065  C CB  . VAL C  1 26  ? 30.022  33.208 24.642  1.00 23.85  ? 26   VAL C CB  1 
ATOM   4066  C CG1 . VAL C  1 26  ? 29.115  34.419 24.763  1.00 22.33  ? 26   VAL C CG1 1 
ATOM   4067  C CG2 . VAL C  1 26  ? 30.323  32.621 26.015  1.00 24.62  ? 26   VAL C CG2 1 
ATOM   4068  N N   . THR C  1 27  ? 31.400  31.368 22.631  1.00 26.42  ? 27   THR C N   1 
ATOM   4069  C CA  . THR C  1 27  ? 32.414  30.392 22.251  1.00 28.13  ? 27   THR C CA  1 
ATOM   4070  C C   . THR C  1 27  ? 33.417  30.170 23.375  1.00 28.70  ? 27   THR C C   1 
ATOM   4071  O O   . THR C  1 27  ? 33.923  29.063 23.539  1.00 30.83  ? 27   THR C O   1 
ATOM   4072  C CB  . THR C  1 27  ? 33.176  30.799 20.972  1.00 27.89  ? 27   THR C CB  1 
ATOM   4073  O OG1 . THR C  1 27  ? 33.950  31.977 21.213  1.00 26.46  ? 27   THR C OG1 1 
ATOM   4074  C CG2 . THR C  1 27  ? 32.213  31.045 19.822  1.00 27.27  ? 27   THR C CG2 1 
ATOM   4075  N N   . HIS C  1 28  ? 33.719  31.222 24.131  1.00 27.03  ? 28   HIS C N   1 
ATOM   4076  C CA  . HIS C  1 28  ? 34.638  31.124 25.264  1.00 27.51  ? 28   HIS C CA  1 
ATOM   4077  C C   . HIS C  1 28  ? 34.176  32.000 26.405  1.00 25.91  ? 28   HIS C C   1 
ATOM   4078  O O   . HIS C  1 28  ? 33.613  33.067 26.189  1.00 24.23  ? 28   HIS C O   1 
ATOM   4079  C CB  . HIS C  1 28  ? 36.047  31.542 24.854  1.00 27.80  ? 28   HIS C CB  1 
ATOM   4080  C CG  . HIS C  1 28  ? 36.583  30.777 23.687  1.00 29.45  ? 28   HIS C CG  1 
ATOM   4081  N ND1 . HIS C  1 28  ? 36.273  31.100 22.384  1.00 28.85  ? 28   HIS C ND1 1 
ATOM   4082  C CD2 . HIS C  1 28  ? 37.392  29.694 23.626  1.00 31.84  ? 28   HIS C CD2 1 
ATOM   4083  C CE1 . HIS C  1 28  ? 36.875  30.253 21.571  1.00 30.76  ? 28   HIS C CE1 1 
ATOM   4084  N NE2 . HIS C  1 28  ? 37.558  29.390 22.299  1.00 32.67  ? 28   HIS C NE2 1 
ATOM   4085  N N   . ALA C  1 29  ? 34.433  31.552 27.623  1.00 26.65  ? 29   ALA C N   1 
ATOM   4086  C CA  . ALA C  1 29  ? 34.036  32.290 28.807  1.00 25.44  ? 29   ALA C CA  1 
ATOM   4087  C C   . ALA C  1 29  ? 35.041  32.049 29.915  1.00 26.33  ? 29   ALA C C   1 
ATOM   4088  O O   . ALA C  1 29  ? 35.942  31.220 29.779  1.00 28.09  ? 29   ALA C O   1 
ATOM   4089  C CB  . ALA C  1 29  ? 32.646  31.867 29.251  1.00 25.49  ? 29   ALA C CB  1 
ATOM   4090  N N   . GLN C  1 30  ? 34.895  32.791 31.005  1.00 25.32  ? 30   GLN C N   1 
ATOM   4091  C CA  . GLN C  1 30  ? 35.749  32.605 32.169  1.00 26.13  ? 30   GLN C CA  1 
ATOM   4092  C C   . GLN C  1 30  ? 34.963  32.807 33.457  1.00 25.44  ? 30   GLN C C   1 
ATOM   4093  O O   . GLN C  1 30  ? 34.580  33.926 33.791  1.00 23.88  ? 30   GLN C O   1 
ATOM   4094  C CB  . GLN C  1 30  ? 36.947  33.556 32.124  1.00 25.80  ? 30   GLN C CB  1 
ATOM   4095  C CG  . GLN C  1 30  ? 37.969  33.262 33.212  1.00 27.04  ? 30   GLN C CG  1 
ATOM   4096  C CD  . GLN C  1 30  ? 39.285  33.985 33.013  1.00 27.42  ? 30   GLN C CD  1 
ATOM   4097  O OE1 . GLN C  1 30  ? 39.658  34.330 31.894  1.00 27.47  ? 30   GLN C OE1 1 
ATOM   4098  N NE2 . GLN C  1 30  ? 40.003  34.209 34.106  1.00 27.95  ? 30   GLN C NE2 1 
ATOM   4099  N N   . ASP C  1 31  ? 34.723  31.711 34.167  1.00 26.83  ? 31   ASP C N   1 
ATOM   4100  C CA  . ASP C  1 31  ? 34.127  31.761 35.493  1.00 26.59  ? 31   ASP C CA  1 
ATOM   4101  C C   . ASP C  1 31  ? 35.145  32.391 36.442  1.00 26.28  ? 31   ASP C C   1 
ATOM   4102  O O   . ASP C  1 31  ? 36.321  32.011 36.441  1.00 27.45  ? 31   ASP C O   1 
ATOM   4103  C CB  . ASP C  1 31  ? 33.753  30.349 35.960  1.00 28.58  ? 31   ASP C CB  1 
ATOM   4104  C CG  . ASP C  1 31  ? 32.815  30.347 37.154  1.00 28.46  ? 31   ASP C CG  1 
ATOM   4105  O OD1 . ASP C  1 31  ? 32.741  31.362 37.875  1.00 27.04  ? 31   ASP C OD1 1 
ATOM   4106  O OD2 . ASP C  1 31  ? 32.147  29.318 37.371  1.00 30.00  ? 31   ASP C OD2 1 
ATOM   4107  N N   . ILE C  1 32  ? 34.689  33.361 37.230  1.00 24.91  ? 32   ILE C N   1 
ATOM   4108  C CA  . ILE C  1 32  ? 35.547  34.066 38.189  1.00 24.63  ? 32   ILE C CA  1 
ATOM   4109  C C   . ILE C  1 32  ? 35.078  33.922 39.643  1.00 24.79  ? 32   ILE C C   1 
ATOM   4110  O O   . ILE C  1 32  ? 35.660  34.517 40.550  1.00 24.58  ? 32   ILE C O   1 
ATOM   4111  C CB  . ILE C  1 32  ? 35.668  35.563 37.833  1.00 23.05  ? 32   ILE C CB  1 
ATOM   4112  C CG1 . ILE C  1 32  ? 34.291  36.191 37.609  1.00 21.75  ? 32   ILE C CG1 1 
ATOM   4113  C CG2 . ILE C  1 32  ? 36.527  35.730 36.593  1.00 23.28  ? 32   ILE C CG2 1 
ATOM   4114  C CD1 . ILE C  1 32  ? 34.293  37.702 37.675  1.00 20.49  ? 32   ILE C CD1 1 
ATOM   4115  N N   . LEU C  1 33  ? 34.044  33.115 39.859  1.00 25.40  ? 33   LEU C N   1 
ATOM   4116  C CA  . LEU C  1 33  ? 33.481  32.893 41.182  1.00 25.78  ? 33   LEU C CA  1 
ATOM   4117  C C   . LEU C  1 33  ? 33.819  31.488 41.669  1.00 27.90  ? 33   LEU C C   1 
ATOM   4118  O O   . LEU C  1 33  ? 33.430  30.502 41.043  1.00 29.11  ? 33   LEU C O   1 
ATOM   4119  C CB  . LEU C  1 33  ? 31.963  33.057 41.124  1.00 25.25  ? 33   LEU C CB  1 
ATOM   4120  C CG  . LEU C  1 33  ? 31.208  32.974 42.445  1.00 25.60  ? 33   LEU C CG  1 
ATOM   4121  C CD1 . LEU C  1 33  ? 31.545  34.176 43.310  1.00 24.40  ? 33   LEU C CD1 1 
ATOM   4122  C CD2 . LEU C  1 33  ? 29.711  32.889 42.196  1.00 25.76  ? 33   LEU C CD2 1 
ATOM   4123  N N   . GLU C  1 34  ? 34.531  31.400 42.790  1.00 28.59  ? 34   GLU C N   1 
ATOM   4124  C CA  . GLU C  1 34  ? 34.815  30.110 43.418  1.00 30.79  ? 34   GLU C CA  1 
ATOM   4125  C C   . GLU C  1 34  ? 33.618  29.669 44.251  1.00 31.29  ? 34   GLU C C   1 
ATOM   4126  O O   . GLU C  1 34  ? 33.218  30.360 45.182  1.00 30.40  ? 34   GLU C O   1 
ATOM   4127  C CB  . GLU C  1 34  ? 36.065  30.190 44.296  1.00 31.44  ? 34   GLU C CB  1 
ATOM   4128  C CG  . GLU C  1 34  ? 36.435  28.874 44.960  1.00 33.90  ? 34   GLU C CG  1 
ATOM   4129  C CD  . GLU C  1 34  ? 36.384  27.702 44.001  1.00 35.70  ? 34   GLU C CD  1 
ATOM   4130  O OE1 . GLU C  1 34  ? 37.242  27.627 43.097  1.00 36.22  ? 34   GLU C OE1 1 
ATOM   4131  O OE2 . GLU C  1 34  ? 35.461  26.871 44.138  1.00 36.80  ? 34   GLU C OE2 1 
ATOM   4132  N N   . LYS C  1 35  ? 33.062  28.507 43.920  1.00 33.05  ? 35   LYS C N   1 
ATOM   4133  C CA  . LYS C  1 35  ? 31.807  28.040 44.518  1.00 33.89  ? 35   LYS C CA  1 
ATOM   4134  C C   . LYS C  1 35  ? 31.966  26.865 45.491  1.00 36.31  ? 35   LYS C C   1 
ATOM   4135  O O   . LYS C  1 35  ? 31.003  26.512 46.174  1.00 37.17  ? 35   LYS C O   1 
ATOM   4136  C CB  . LYS C  1 35  ? 30.807  27.662 43.409  1.00 34.29  ? 35   LYS C CB  1 
ATOM   4137  C CG  . LYS C  1 35  ? 29.990  28.830 42.872  1.00 32.21  ? 35   LYS C CG  1 
ATOM   4138  C CD  . LYS C  1 35  ? 29.138  28.430 41.674  1.00 32.75  ? 35   LYS C CD  1 
ATOM   4139  C CE  . LYS C  1 35  ? 29.713  28.921 40.351  1.00 31.52  ? 35   LYS C CE  1 
ATOM   4140  N NZ  . LYS C  1 35  ? 31.141  28.559 40.126  1.00 31.99  ? 35   LYS C NZ  1 
ATOM   4141  N N   . THR C  1 36  ? 33.164  26.276 45.570  1.00 37.65  ? 36   THR C N   1 
ATOM   4142  C CA  . THR C  1 36  ? 33.376  25.046 46.351  1.00 40.39  ? 36   THR C CA  1 
ATOM   4143  C C   . THR C  1 36  ? 34.384  25.181 47.497  1.00 40.73  ? 36   THR C C   1 
ATOM   4144  O O   . THR C  1 36  ? 35.230  26.073 47.497  1.00 39.26  ? 36   THR C O   1 
ATOM   4145  C CB  . THR C  1 36  ? 33.851  23.884 45.452  1.00 42.73  ? 36   THR C CB  1 
ATOM   4146  O OG1 . THR C  1 36  ? 35.145  24.182 44.913  1.00 42.36  ? 36   THR C OG1 1 
ATOM   4147  C CG2 . THR C  1 36  ? 32.866  23.642 44.321  1.00 42.81  ? 36   THR C CG2 1 
ATOM   4148  N N   . HIS C  1 37  ? 34.268  24.269 48.462  1.00 42.94  ? 37   HIS C N   1 
ATOM   4149  C CA  . HIS C  1 37  ? 35.204  24.147 49.584  1.00 43.87  ? 37   HIS C CA  1 
ATOM   4150  C C   . HIS C  1 37  ? 35.297  22.671 49.993  1.00 47.38  ? 37   HIS C C   1 
ATOM   4151  O O   . HIS C  1 37  ? 34.444  21.867 49.607  1.00 48.89  ? 37   HIS C O   1 
ATOM   4152  C CB  . HIS C  1 37  ? 34.741  25.002 50.769  1.00 42.25  ? 37   HIS C CB  1 
ATOM   4153  C CG  . HIS C  1 37  ? 33.356  24.683 51.243  1.00 42.75  ? 37   HIS C CG  1 
ATOM   4154  N ND1 . HIS C  1 37  ? 33.112  23.977 52.400  1.00 44.60  ? 37   HIS C ND1 1 
ATOM   4155  C CD2 . HIS C  1 37  ? 32.143  24.965 50.713  1.00 41.91  ? 37   HIS C CD2 1 
ATOM   4156  C CE1 . HIS C  1 37  ? 31.810  23.839 52.567  1.00 44.91  ? 37   HIS C CE1 1 
ATOM   4157  N NE2 . HIS C  1 37  ? 31.198  24.430 51.556  1.00 43.36  ? 37   HIS C NE2 1 
ATOM   4158  N N   . ASN C  1 38  ? 36.328  22.313 50.760  1.00 48.92  ? 38   ASN C N   1 
ATOM   4159  C CA  . ASN C  1 38  ? 36.515  20.916 51.187  1.00 52.53  ? 38   ASN C CA  1 
ATOM   4160  C C   . ASN C  1 38  ? 35.634  20.504 52.379  1.00 53.58  ? 38   ASN C C   1 
ATOM   4161  O O   . ASN C  1 38  ? 35.522  19.316 52.694  1.00 56.68  ? 38   ASN C O   1 
ATOM   4162  C CB  . ASN C  1 38  ? 38.000  20.605 51.463  1.00 54.21  ? 38   ASN C CB  1 
ATOM   4163  C CG  . ASN C  1 38  ? 38.562  21.353 52.661  1.00 53.04  ? 38   ASN C CG  1 
ATOM   4164  O OD1 . ASN C  1 38  ? 37.829  21.945 53.449  1.00 51.39  ? 38   ASN C OD1 1 
ATOM   4165  N ND2 . ASN C  1 38  ? 39.879  21.317 52.805  1.00 54.18  ? 38   ASN C ND2 1 
ATOM   4166  N N   . GLY C  1 39  ? 35.035  21.490 53.044  1.00 51.24  ? 39   GLY C N   1 
ATOM   4167  C CA  . GLY C  1 39  ? 34.071  21.240 54.123  1.00 52.03  ? 39   GLY C CA  1 
ATOM   4168  C C   . GLY C  1 39  ? 34.712  20.984 55.474  1.00 53.33  ? 39   GLY C C   1 
ATOM   4169  O O   . GLY C  1 39  ? 34.064  20.452 56.381  1.00 54.83  ? 39   GLY C O   1 
ATOM   4170  N N   . LYS C  1 40  ? 35.976  21.380 55.614  1.00 52.92  ? 40   LYS C N   1 
ATOM   4171  C CA  . LYS C  1 40  ? 36.778  21.029 56.780  1.00 54.60  ? 40   LYS C CA  1 
ATOM   4172  C C   . LYS C  1 40  ? 37.495  22.231 57.386  1.00 52.42  ? 40   LYS C C   1 
ATOM   4173  O O   . LYS C  1 40  ? 37.847  23.184 56.686  1.00 50.26  ? 40   LYS C O   1 
ATOM   4174  C CB  . LYS C  1 40  ? 37.809  19.967 56.391  1.00 57.66  ? 40   LYS C CB  1 
ATOM   4175  C CG  . LYS C  1 40  ? 37.209  18.590 56.161  1.00 60.87  ? 40   LYS C CG  1 
ATOM   4176  C CD  . LYS C  1 40  ? 38.089  17.717 55.281  1.00 63.49  ? 40   LYS C CD  1 
ATOM   4177  C CE  . LYS C  1 40  ? 37.380  16.418 54.935  1.00 66.69  ? 40   LYS C CE  1 
ATOM   4178  N NZ  . LYS C  1 40  ? 38.158  15.575 53.987  1.00 69.40  ? 40   LYS C NZ  1 
ATOM   4179  N N   . LEU C  1 41  ? 37.718  22.159 58.695  1.00 53.29  ? 41   LEU C N   1 
ATOM   4180  C CA  . LEU C  1 41  ? 38.543  23.126 59.416  1.00 51.97  ? 41   LEU C CA  1 
ATOM   4181  C C   . LEU C  1 41  ? 39.985  22.619 59.361  1.00 54.13  ? 41   LEU C C   1 
ATOM   4182  O O   . LEU C  1 41  ? 40.240  21.424 59.567  1.00 57.18  ? 41   LEU C O   1 
ATOM   4183  C CB  . LEU C  1 41  ? 38.052  23.265 60.861  1.00 51.99  ? 41   LEU C CB  1 
ATOM   4184  C CG  . LEU C  1 41  ? 36.683  23.937 61.114  1.00 50.03  ? 41   LEU C CG  1 
ATOM   4185  C CD1 . LEU C  1 41  ? 36.842  25.334 61.705  1.00 47.52  ? 41   LEU C CD1 1 
ATOM   4186  C CD2 . LEU C  1 41  ? 35.788  24.000 59.876  1.00 49.04  ? 41   LEU C CD2 1 
ATOM   4187  N N   . CYS C  1 42  ? 40.923  23.521 59.074  1.00 52.86  ? 42   CYS C N   1 
ATOM   4188  C CA  . CYS C  1 42  ? 42.244  23.112 58.605  1.00 54.92  ? 42   CYS C CA  1 
ATOM   4189  C C   . CYS C  1 42  ? 43.392  24.013 59.030  1.00 54.33  ? 42   CYS C C   1 
ATOM   4190  O O   . CYS C  1 42  ? 43.195  25.179 59.365  1.00 51.85  ? 42   CYS C O   1 
ATOM   4191  C CB  . CYS C  1 42  ? 42.219  23.050 57.082  1.00 54.65  ? 42   CYS C CB  1 
ATOM   4192  S SG  . CYS C  1 42  ? 41.251  21.672 56.440  1.00 56.72  ? 42   CYS C SG  1 
ATOM   4193  N N   . ASP C  1 43  ? 44.598  23.452 58.985  1.00 56.93  ? 43   ASP C N   1 
ATOM   4194  C CA  . ASP C  1 43  ? 45.817  24.195 59.284  1.00 57.08  ? 43   ASP C CA  1 
ATOM   4195  C C   . ASP C  1 43  ? 45.999  25.305 58.260  1.00 54.76  ? 43   ASP C C   1 
ATOM   4196  O O   . ASP C  1 43  ? 45.824  25.081 57.062  1.00 54.60  ? 43   ASP C O   1 
ATOM   4197  C CB  . ASP C  1 43  ? 47.039  23.268 59.266  1.00 60.92  ? 43   ASP C CB  1 
ATOM   4198  C CG  . ASP C  1 43  ? 47.006  22.218 60.374  1.00 63.54  ? 43   ASP C CG  1 
ATOM   4199  O OD1 . ASP C  1 43  ? 46.017  22.166 61.133  1.00 62.39  ? 43   ASP C OD1 1 
ATOM   4200  O OD2 . ASP C  1 43  ? 47.974  21.438 60.483  1.00 66.96  ? 43   ASP C OD2 1 
ATOM   4201  N N   . LEU C  1 44  ? 46.338  26.499 58.737  1.00 53.12  ? 44   LEU C N   1 
ATOM   4202  C CA  . LEU C  1 44  ? 46.562  27.647 57.862  1.00 51.17  ? 44   LEU C CA  1 
ATOM   4203  C C   . LEU C  1 44  ? 48.055  27.874 57.678  1.00 53.20  ? 44   LEU C C   1 
ATOM   4204  O O   . LEU C  1 44  ? 48.761  28.211 58.629  1.00 54.11  ? 44   LEU C O   1 
ATOM   4205  C CB  . LEU C  1 44  ? 45.915  28.907 58.442  1.00 48.29  ? 44   LEU C CB  1 
ATOM   4206  C CG  . LEU C  1 44  ? 45.839  30.113 57.495  1.00 46.05  ? 44   LEU C CG  1 
ATOM   4207  C CD1 . LEU C  1 44  ? 44.672  29.960 56.525  1.00 44.32  ? 44   LEU C CD1 1 
ATOM   4208  C CD2 . LEU C  1 44  ? 45.710  31.415 58.272  1.00 44.28  ? 44   LEU C CD2 1 
ATOM   4209  N N   . ASP C  1 45  ? 48.530  27.684 56.449  1.00 54.08  ? 45   ASP C N   1 
ATOM   4210  C CA  . ASP C  1 45  ? 49.943  27.865 56.118  1.00 56.37  ? 45   ASP C CA  1 
ATOM   4211  C C   . ASP C  1 45  ? 50.820  26.924 56.948  1.00 59.93  ? 45   ASP C C   1 
ATOM   4212  O O   . ASP C  1 45  ? 51.944  27.273 57.318  1.00 61.79  ? 45   ASP C O   1 
ATOM   4213  C CB  . ASP C  1 45  ? 50.355  29.328 56.345  1.00 54.91  ? 45   ASP C CB  1 
ATOM   4214  C CG  . ASP C  1 45  ? 51.338  29.827 55.305  1.00 55.98  ? 45   ASP C CG  1 
ATOM   4215  O OD1 . ASP C  1 45  ? 50.880  30.250 54.219  1.00 54.22  ? 45   ASP C OD1 1 
ATOM   4216  O OD2 . ASP C  1 45  ? 52.558  29.807 55.573  1.00 58.74  ? 45   ASP C OD2 1 
ATOM   4217  N N   . GLY C  1 46  ? 50.290  25.735 57.244  1.00 61.10  ? 46   GLY C N   1 
ATOM   4218  C CA  . GLY C  1 46  ? 50.966  24.759 58.107  1.00 64.54  ? 46   GLY C CA  1 
ATOM   4219  C C   . GLY C  1 46  ? 50.630  24.881 59.587  1.00 63.95  ? 46   GLY C C   1 
ATOM   4220  O O   . GLY C  1 46  ? 50.690  23.892 60.314  1.00 66.28  ? 46   GLY C O   1 
ATOM   4221  N N   . VAL C  1 47  ? 50.266  26.086 60.028  1.00 60.98  ? 47   VAL C N   1 
ATOM   4222  C CA  . VAL C  1 47  ? 50.064  26.385 61.453  1.00 60.43  ? 47   VAL C CA  1 
ATOM   4223  C C   . VAL C  1 47  ? 48.648  26.002 61.901  1.00 58.68  ? 47   VAL C C   1 
ATOM   4224  O O   . VAL C  1 47  ? 47.662  26.523 61.381  1.00 55.88  ? 47   VAL C O   1 
ATOM   4225  C CB  . VAL C  1 47  ? 50.318  27.882 61.747  1.00 58.35  ? 47   VAL C CB  1 
ATOM   4226  C CG1 . VAL C  1 47  ? 50.163  28.176 63.232  1.00 58.06  ? 47   VAL C CG1 1 
ATOM   4227  C CG2 . VAL C  1 47  ? 51.704  28.297 61.271  1.00 60.32  ? 47   VAL C CG2 1 
ATOM   4228  N N   . LYS C  1 48  ? 48.559  25.108 62.884  1.00 60.60  ? 48   LYS C N   1 
ATOM   4229  C CA  . LYS C  1 48  ? 47.280  24.534 63.312  1.00 59.79  ? 48   LYS C CA  1 
ATOM   4230  C C   . LYS C  1 48  ? 46.397  25.546 64.047  1.00 56.71  ? 48   LYS C C   1 
ATOM   4231  O O   . LYS C  1 48  ? 46.903  26.377 64.802  1.00 56.17  ? 48   LYS C O   1 
ATOM   4232  C CB  . LYS C  1 48  ? 47.519  23.321 64.225  1.00 63.05  ? 48   LYS C CB  1 
ATOM   4233  C CG  . LYS C  1 48  ? 46.291  22.443 64.437  1.00 63.20  ? 48   LYS C CG  1 
ATOM   4234  C CD  . LYS C  1 48  ? 46.441  21.497 65.616  1.00 66.04  ? 48   LYS C CD  1 
ATOM   4235  C CE  . LYS C  1 48  ? 45.315  20.473 65.628  1.00 66.93  ? 48   LYS C CE  1 
ATOM   4236  N NZ  . LYS C  1 48  ? 45.202  19.771 66.936  1.00 69.07  ? 48   LYS C NZ  1 
ATOM   4237  N N   . PRO C  1 49  ? 45.068  25.475 63.830  1.00 54.91  ? 49   PRO C N   1 
ATOM   4238  C CA  . PRO C  1 49  ? 44.161  26.294 64.633  1.00 52.52  ? 49   PRO C CA  1 
ATOM   4239  C C   . PRO C  1 49  ? 44.003  25.770 66.052  1.00 53.89  ? 49   PRO C C   1 
ATOM   4240  O O   . PRO C  1 49  ? 44.082  24.561 66.274  1.00 56.42  ? 49   PRO C O   1 
ATOM   4241  C CB  . PRO C  1 49  ? 42.823  26.161 63.901  1.00 50.93  ? 49   PRO C CB  1 
ATOM   4242  C CG  . PRO C  1 49  ? 42.907  24.846 63.207  1.00 53.29  ? 49   PRO C CG  1 
ATOM   4243  C CD  . PRO C  1 49  ? 44.341  24.745 62.772  1.00 55.01  ? 49   PRO C CD  1 
ATOM   4244  N N   . LEU C  1 50  ? 43.770  26.680 66.992  1.00 52.33  ? 50   LEU C N   1 
ATOM   4245  C CA  . LEU C  1 50  ? 43.404  26.303 68.348  1.00 53.22  ? 50   LEU C CA  1 
ATOM   4246  C C   . LEU C  1 50  ? 41.924  25.956 68.355  1.00 52.34  ? 50   LEU C C   1 
ATOM   4247  O O   . LEU C  1 50  ? 41.078  26.846 68.334  1.00 49.98  ? 50   LEU C O   1 
ATOM   4248  C CB  . LEU C  1 50  ? 43.694  27.447 69.325  1.00 52.02  ? 50   LEU C CB  1 
ATOM   4249  C CG  . LEU C  1 50  ? 43.188  27.319 70.769  1.00 52.44  ? 50   LEU C CG  1 
ATOM   4250  C CD1 . LEU C  1 50  ? 43.518  25.962 71.376  1.00 55.53  ? 50   LEU C CD1 1 
ATOM   4251  C CD2 . LEU C  1 50  ? 43.769  28.435 71.625  1.00 51.67  ? 50   LEU C CD2 1 
ATOM   4252  N N   . ILE C  1 51  ? 41.617  24.663 68.359  1.00 54.54  ? 51   ILE C N   1 
ATOM   4253  C CA  . ILE C  1 51  ? 40.232  24.204 68.391  1.00 54.35  ? 51   ILE C CA  1 
ATOM   4254  C C   . ILE C  1 51  ? 39.833  23.918 69.831  1.00 55.42  ? 51   ILE C C   1 
ATOM   4255  O O   . ILE C  1 51  ? 40.247  22.913 70.412  1.00 58.15  ? 51   ILE C O   1 
ATOM   4256  C CB  . ILE C  1 51  ? 40.023  22.954 67.509  1.00 56.41  ? 51   ILE C CB  1 
ATOM   4257  C CG1 . ILE C  1 51  ? 40.402  23.293 66.062  1.00 55.28  ? 51   ILE C CG1 1 
ATOM   4258  C CG2 . ILE C  1 51  ? 38.583  22.454 67.607  1.00 56.64  ? 51   ILE C CG2 1 
ATOM   4259  C CD1 . ILE C  1 51  ? 39.933  22.294 65.027  1.00 56.68  ? 51   ILE C CD1 1 
ATOM   4260  N N   . LEU C  1 52  ? 39.013  24.804 70.392  1.00 53.41  ? 52   LEU C N   1 
ATOM   4261  C CA  . LEU C  1 52  ? 38.572  24.686 71.783  1.00 54.18  ? 52   LEU C CA  1 
ATOM   4262  C C   . LEU C  1 52  ? 37.551  23.560 71.994  1.00 56.17  ? 52   LEU C C   1 
ATOM   4263  O O   . LEU C  1 52  ? 37.239  23.209 73.132  1.00 57.47  ? 52   LEU C O   1 
ATOM   4264  C CB  . LEU C  1 52  ? 37.985  26.015 72.269  1.00 51.60  ? 52   LEU C CB  1 
ATOM   4265  C CG  . LEU C  1 52  ? 38.894  27.245 72.180  1.00 49.80  ? 52   LEU C CG  1 
ATOM   4266  C CD1 . LEU C  1 52  ? 38.137  28.493 72.606  1.00 47.62  ? 52   LEU C CD1 1 
ATOM   4267  C CD2 . LEU C  1 52  ? 40.150  27.077 73.022  1.00 51.36  ? 52   LEU C CD2 1 
ATOM   4268  N N   . ARG C  1 53  ? 37.039  23.004 70.896  1.00 56.56  ? 53   ARG C N   1 
ATOM   4269  C CA  . ARG C  1 53  ? 36.028  21.954 70.931  1.00 58.66  ? 53   ARG C CA  1 
ATOM   4270  C C   . ARG C  1 53  ? 34.796  22.458 71.709  1.00 57.80  ? 53   ARG C C   1 
ATOM   4271  O O   . ARG C  1 53  ? 34.151  23.409 71.258  1.00 55.47  ? 53   ARG C O   1 
ATOM   4272  C CB  . ARG C  1 53  ? 36.613  20.635 71.463  1.00 62.25  ? 53   ARG C CB  1 
ATOM   4273  C CG  . ARG C  1 53  ? 35.737  19.418 71.181  1.00 64.93  ? 53   ARG C CG  1 
ATOM   4274  C CD  . ARG C  1 53  ? 36.260  18.138 71.825  1.00 68.80  ? 53   ARG C CD  1 
ATOM   4275  N NE  . ARG C  1 53  ? 37.102  17.358 70.912  1.00 70.68  ? 53   ARG C NE  1 
ATOM   4276  C CZ  . ARG C  1 53  ? 38.438  17.340 70.902  1.00 71.30  ? 53   ARG C CZ  1 
ATOM   4277  N NH1 . ARG C  1 53  ? 39.152  18.060 71.764  1.00 70.19  ? 53   ARG C NH1 1 
ATOM   4278  N NH2 . ARG C  1 53  ? 39.073  16.583 70.014  1.00 73.31  ? 53   ARG C NH2 1 
ATOM   4279  N N   . ASP C  1 54  ? 34.477  21.862 72.859  1.00 59.83  ? 54   ASP C N   1 
ATOM   4280  C CA  . ASP C  1 54  ? 33.305  22.269 73.643  1.00 59.45  ? 54   ASP C CA  1 
ATOM   4281  C C   . ASP C  1 54  ? 33.627  23.288 74.739  1.00 57.90  ? 54   ASP C C   1 
ATOM   4282  O O   . ASP C  1 54  ? 32.717  23.781 75.405  1.00 57.46  ? 54   ASP C O   1 
ATOM   4283  C CB  . ASP C  1 54  ? 32.623  21.042 74.256  1.00 62.80  ? 54   ASP C CB  1 
ATOM   4284  C CG  . ASP C  1 54  ? 31.881  20.214 73.225  1.00 64.31  ? 54   ASP C CG  1 
ATOM   4285  O OD1 . ASP C  1 54  ? 30.999  20.771 72.537  1.00 62.75  ? 54   ASP C OD1 1 
ATOM   4286  O OD2 . ASP C  1 54  ? 32.174  19.006 73.107  1.00 67.25  ? 54   ASP C OD2 1 
ATOM   4287  N N   . CYS C  1 55  ? 34.909  23.597 74.934  1.00 57.35  ? 55   CYS C N   1 
ATOM   4288  C CA  . CYS C  1 55  ? 35.308  24.661 75.860  1.00 55.82  ? 55   CYS C CA  1 
ATOM   4289  C C   . CYS C  1 55  ? 35.164  26.033 75.197  1.00 52.68  ? 55   CYS C C   1 
ATOM   4290  O O   . CYS C  1 55  ? 35.294  26.157 73.981  1.00 51.66  ? 55   CYS C O   1 
ATOM   4291  C CB  . CYS C  1 55  ? 36.747  24.462 76.353  1.00 56.84  ? 55   CYS C CB  1 
ATOM   4292  S SG  . CYS C  1 55  ? 36.918  23.198 77.634  1.00 60.43  ? 55   CYS C SG  1 
ATOM   4293  N N   . SER C  1 56  ? 34.879  27.051 76.005  1.00 51.32  ? 56   SER C N   1 
ATOM   4294  C CA  . SER C  1 56  ? 34.845  28.436 75.539  1.00 48.64  ? 56   SER C CA  1 
ATOM   4295  C C   . SER C  1 56  ? 36.198  29.096 75.802  1.00 47.93  ? 56   SER C C   1 
ATOM   4296  O O   . SER C  1 56  ? 37.118  28.464 76.326  1.00 49.50  ? 56   SER C O   1 
ATOM   4297  C CB  . SER C  1 56  ? 33.739  29.219 76.254  1.00 47.94  ? 56   SER C CB  1 
ATOM   4298  O OG  . SER C  1 56  ? 34.184  29.705 77.512  1.00 48.11  ? 56   SER C OG  1 
ATOM   4299  N N   . VAL C  1 57  ? 36.310  30.371 75.438  1.00 45.81  ? 57   VAL C N   1 
ATOM   4300  C CA  . VAL C  1 57  ? 37.539  31.136 75.656  1.00 45.23  ? 57   VAL C CA  1 
ATOM   4301  C C   . VAL C  1 57  ? 37.726  31.377 77.150  1.00 46.00  ? 57   VAL C C   1 
ATOM   4302  O O   . VAL C  1 57  ? 38.835  31.254 77.671  1.00 46.99  ? 57   VAL C O   1 
ATOM   4303  C CB  . VAL C  1 57  ? 37.509  32.487 74.907  1.00 43.04  ? 57   VAL C CB  1 
ATOM   4304  C CG1 . VAL C  1 57  ? 38.758  33.303 75.204  1.00 42.86  ? 57   VAL C CG1 1 
ATOM   4305  C CG2 . VAL C  1 57  ? 37.373  32.260 73.406  1.00 42.29  ? 57   VAL C CG2 1 
ATOM   4306  N N   . ALA C  1 58  ? 36.631  31.712 77.829  1.00 45.70  ? 58   ALA C N   1 
ATOM   4307  C CA  . ALA C  1 58  ? 36.642  31.916 79.278  1.00 46.49  ? 58   ALA C CA  1 
ATOM   4308  C C   . ALA C  1 58  ? 37.097  30.654 80.011  1.00 48.70  ? 58   ALA C C   1 
ATOM   4309  O O   . ALA C  1 58  ? 37.988  30.712 80.860  1.00 49.52  ? 58   ALA C O   1 
ATOM   4310  C CB  . ALA C  1 58  ? 35.261  32.338 79.763  1.00 46.14  ? 58   ALA C CB  1 
ATOM   4311  N N   . GLY C  1 59  ? 36.485  29.522 79.671  1.00 49.85  ? 59   GLY C N   1 
ATOM   4312  C CA  . GLY C  1 59  ? 36.833  28.245 80.280  1.00 52.30  ? 59   GLY C CA  1 
ATOM   4313  C C   . GLY C  1 59  ? 38.298  27.897 80.094  1.00 53.17  ? 59   GLY C C   1 
ATOM   4314  O O   . GLY C  1 59  ? 38.957  27.447 81.030  1.00 54.91  ? 59   GLY C O   1 
ATOM   4315  N N   . TRP C  1 60  ? 38.810  28.101 78.885  1.00 52.18  ? 60   TRP C N   1 
ATOM   4316  C CA  . TRP C  1 60  ? 40.225  27.865 78.602  1.00 53.13  ? 60   TRP C CA  1 
ATOM   4317  C C   . TRP C  1 60  ? 41.111  28.773 79.458  1.00 52.89  ? 60   TRP C C   1 
ATOM   4318  O O   . TRP C  1 60  ? 42.003  28.293 80.162  1.00 54.82  ? 60   TRP C O   1 
ATOM   4319  C CB  . TRP C  1 60  ? 40.512  28.053 77.101  1.00 52.01  ? 60   TRP C CB  1 
ATOM   4320  C CG  . TRP C  1 60  ? 41.944  28.375 76.754  1.00 52.35  ? 60   TRP C CG  1 
ATOM   4321  C CD1 . TRP C  1 60  ? 43.068  27.804 77.276  1.00 54.62  ? 60   TRP C CD1 1 
ATOM   4322  C CD2 . TRP C  1 60  ? 42.393  29.328 75.785  1.00 50.68  ? 60   TRP C CD2 1 
ATOM   4323  N NE1 . TRP C  1 60  ? 44.190  28.355 76.707  1.00 54.53  ? 60   TRP C NE1 1 
ATOM   4324  C CE2 . TRP C  1 60  ? 43.804  29.291 75.785  1.00 52.13  ? 60   TRP C CE2 1 
ATOM   4325  C CE3 . TRP C  1 60  ? 41.740  30.212 74.918  1.00 48.29  ? 60   TRP C CE3 1 
ATOM   4326  C CZ2 . TRP C  1 60  ? 44.576  30.108 74.952  1.00 51.33  ? 60   TRP C CZ2 1 
ATOM   4327  C CZ3 . TRP C  1 60  ? 42.508  31.026 74.090  1.00 47.38  ? 60   TRP C CZ3 1 
ATOM   4328  C CH2 . TRP C  1 60  ? 43.910  30.967 74.113  1.00 48.91  ? 60   TRP C CH2 1 
ATOM   4329  N N   . LEU C  1 61  ? 40.846  30.075 79.410  1.00 50.78  ? 61   LEU C N   1 
ATOM   4330  C CA  . LEU C  1 61  ? 41.698  31.059 80.084  1.00 50.56  ? 61   LEU C CA  1 
ATOM   4331  C C   . LEU C  1 61  ? 41.620  31.009 81.612  1.00 51.66  ? 61   LEU C C   1 
ATOM   4332  O O   . LEU C  1 61  ? 42.634  31.177 82.291  1.00 52.76  ? 61   LEU C O   1 
ATOM   4333  C CB  . LEU C  1 61  ? 41.377  32.472 79.590  1.00 48.26  ? 61   LEU C CB  1 
ATOM   4334  C CG  . LEU C  1 61  ? 41.748  32.772 78.136  1.00 47.21  ? 61   LEU C CG  1 
ATOM   4335  C CD1 . LEU C  1 61  ? 41.441  34.228 77.823  1.00 45.26  ? 61   LEU C CD1 1 
ATOM   4336  C CD2 . LEU C  1 61  ? 43.212  32.466 77.851  1.00 48.69  ? 61   LEU C CD2 1 
ATOM   4337  N N   . LEU C  1 62  ? 40.429  30.775 82.156  1.00 51.56  ? 62   LEU C N   1 
ATOM   4338  C CA  . LEU C  1 62  ? 40.281  30.601 83.609  1.00 52.80  ? 62   LEU C CA  1 
ATOM   4339  C C   . LEU C  1 62  ? 40.792  29.240 84.079  1.00 55.39  ? 62   LEU C C   1 
ATOM   4340  O O   . LEU C  1 62  ? 41.014  29.041 85.268  1.00 56.73  ? 62   LEU C O   1 
ATOM   4341  C CB  . LEU C  1 62  ? 38.824  30.789 84.039  1.00 52.12  ? 62   LEU C CB  1 
ATOM   4342  C CG  . LEU C  1 62  ? 38.307  32.220 83.901  1.00 50.03  ? 62   LEU C CG  1 
ATOM   4343  C CD1 . LEU C  1 62  ? 36.789  32.252 83.985  1.00 49.63  ? 62   LEU C CD1 1 
ATOM   4344  C CD2 . LEU C  1 62  ? 38.925  33.128 84.954  1.00 50.12  ? 62   LEU C CD2 1 
ATOM   4345  N N   . GLY C  1 63  ? 40.986  28.311 83.145  1.00 56.28  ? 63   GLY C N   1 
ATOM   4346  C CA  . GLY C  1 63  ? 41.492  26.986 83.471  1.00 59.08  ? 63   GLY C CA  1 
ATOM   4347  C C   . GLY C  1 63  ? 40.407  26.101 84.048  1.00 60.38  ? 63   GLY C C   1 
ATOM   4348  O O   . GLY C  1 63  ? 40.619  25.425 85.052  1.00 62.50  ? 63   GLY C O   1 
ATOM   4349  N N   . ASN C  1 64  ? 39.236  26.119 83.417  1.00 59.29  ? 64   ASN C N   1 
ATOM   4350  C CA  . ASN C  1 64  ? 38.156  25.201 83.756  1.00 60.84  ? 64   ASN C CA  1 
ATOM   4351  C C   . ASN C  1 64  ? 38.683  23.761 83.661  1.00 63.84  ? 64   ASN C C   1 
ATOM   4352  O O   . ASN C  1 64  ? 39.341  23.410 82.678  1.00 64.14  ? 64   ASN C O   1 
ATOM   4353  C CB  . ASN C  1 64  ? 36.962  25.453 82.816  1.00 59.31  ? 64   ASN C CB  1 
ATOM   4354  C CG  . ASN C  1 64  ? 35.875  24.390 82.911  1.00 61.26  ? 64   ASN C CG  1 
ATOM   4355  O OD1 . ASN C  1 64  ? 36.154  23.195 82.929  1.00 63.76  ? 64   ASN C OD1 1 
ATOM   4356  N ND2 . ASN C  1 64  ? 34.620  24.827 82.930  1.00 60.39  ? 64   ASN C ND2 1 
ATOM   4357  N N   . PRO C  1 65  ? 38.409  22.928 84.685  1.00 66.31  ? 65   PRO C N   1 
ATOM   4358  C CA  . PRO C  1 65  ? 38.977  21.571 84.745  1.00 69.60  ? 65   PRO C CA  1 
ATOM   4359  C C   . PRO C  1 65  ? 38.612  20.655 83.566  1.00 70.74  ? 65   PRO C C   1 
ATOM   4360  O O   . PRO C  1 65  ? 39.333  19.698 83.296  1.00 73.20  ? 65   PRO C O   1 
ATOM   4361  C CB  . PRO C  1 65  ? 38.414  21.006 86.057  1.00 71.69  ? 65   PRO C CB  1 
ATOM   4362  C CG  . PRO C  1 65  ? 37.211  21.830 86.355  1.00 69.70  ? 65   PRO C CG  1 
ATOM   4363  C CD  . PRO C  1 65  ? 37.519  23.197 85.828  1.00 66.38  ? 65   PRO C CD  1 
ATOM   4364  N N   . MET C  1 66  ? 37.505  20.943 82.884  1.00 69.23  ? 66   MET C N   1 
ATOM   4365  C CA  . MET C  1 66  ? 37.125  20.218 81.665  1.00 70.00  ? 66   MET C CA  1 
ATOM   4366  C C   . MET C  1 66  ? 37.975  20.642 80.462  1.00 68.40  ? 66   MET C C   1 
ATOM   4367  O O   . MET C  1 66  ? 37.990  19.962 79.433  1.00 69.32  ? 66   MET C O   1 
ATOM   4368  C CB  . MET C  1 66  ? 35.647  20.459 81.339  1.00 68.95  ? 66   MET C CB  1 
ATOM   4369  C CG  . MET C  1 66  ? 34.671  20.040 82.428  1.00 70.77  ? 66   MET C CG  1 
ATOM   4370  S SD  . MET C  1 66  ? 34.515  18.250 82.571  1.00 75.44  ? 66   MET C SD  1 
ATOM   4371  C CE  . MET C  1 66  ? 33.119  18.128 83.688  1.00 76.83  ? 66   MET C CE  1 
ATOM   4372  N N   . CYS C  1 67  ? 38.668  21.772 80.592  1.00 66.17  ? 67   CYS C N   1 
ATOM   4373  C CA  . CYS C  1 67  ? 39.527  22.300 79.536  1.00 64.69  ? 67   CYS C CA  1 
ATOM   4374  C C   . CYS C  1 67  ? 40.996  21.995 79.824  1.00 66.48  ? 67   CYS C C   1 
ATOM   4375  O O   . CYS C  1 67  ? 41.879  22.819 79.566  1.00 65.17  ? 67   CYS C O   1 
ATOM   4376  C CB  . CYS C  1 67  ? 39.301  23.805 79.417  1.00 61.29  ? 67   CYS C CB  1 
ATOM   4377  S SG  . CYS C  1 67  ? 37.546  24.223 79.283  1.00 59.64  ? 67   CYS C SG  1 
ATOM   4378  N N   . ASP C  1 68  ? 41.243  20.798 80.355  1.00 69.78  ? 68   ASP C N   1 
ATOM   4379  C CA  . ASP C  1 68  ? 42.597  20.321 80.629  1.00 72.16  ? 68   ASP C CA  1 
ATOM   4380  C C   . ASP C  1 68  ? 43.415  20.140 79.355  1.00 72.53  ? 68   ASP C C   1 
ATOM   4381  O O   . ASP C  1 68  ? 44.638  20.196 79.400  1.00 73.72  ? 68   ASP C O   1 
ATOM   4382  C CB  . ASP C  1 68  ? 42.562  18.992 81.394  1.00 75.93  ? 68   ASP C CB  1 
ATOM   4383  C CG  . ASP C  1 68  ? 42.255  19.170 82.869  1.00 76.23  ? 68   ASP C CG  1 
ATOM   4384  O OD1 . ASP C  1 68  ? 42.265  20.318 83.366  1.00 73.75  ? 68   ASP C OD1 1 
ATOM   4385  O OD2 . ASP C  1 68  ? 42.006  18.149 83.544  1.00 79.15  ? 68   ASP C OD2 1 
ATOM   4386  N N   . GLU C  1 69  ? 42.749  19.906 78.228  1.00 71.75  ? 69   GLU C N   1 
ATOM   4387  C CA  . GLU C  1 69  ? 43.444  19.832 76.946  1.00 71.82  ? 69   GLU C CA  1 
ATOM   4388  C C   . GLU C  1 69  ? 44.208  21.124 76.659  1.00 69.34  ? 69   GLU C C   1 
ATOM   4389  O O   . GLU C  1 69  ? 45.294  21.093 76.080  1.00 70.35  ? 69   GLU C O   1 
ATOM   4390  C CB  . GLU C  1 69  ? 42.458  19.557 75.808  1.00 70.88  ? 69   GLU C CB  1 
ATOM   4391  C CG  . GLU C  1 69  ? 43.114  19.470 74.434  1.00 70.95  ? 69   GLU C CG  1 
ATOM   4392  C CD  . GLU C  1 69  ? 42.132  19.160 73.320  1.00 70.20  ? 69   GLU C CD  1 
ATOM   4393  O OE1 . GLU C  1 69  ? 40.998  18.725 73.616  1.00 70.55  ? 69   GLU C OE1 1 
ATOM   4394  O OE2 . GLU C  1 69  ? 42.500  19.351 72.141  1.00 69.41  ? 69   GLU C OE2 1 
ATOM   4395  N N   . PHE C  1 70  ? 43.642  22.250 77.088  1.00 66.43  ? 70   PHE C N   1 
ATOM   4396  C CA  . PHE C  1 70  ? 44.146  23.567 76.714  1.00 63.90  ? 70   PHE C CA  1 
ATOM   4397  C C   . PHE C  1 70  ? 45.006  24.237 77.797  1.00 64.19  ? 70   PHE C C   1 
ATOM   4398  O O   . PHE C  1 70  ? 45.097  25.462 77.856  1.00 61.93  ? 70   PHE C O   1 
ATOM   4399  C CB  . PHE C  1 70  ? 42.963  24.448 76.291  1.00 60.61  ? 70   PHE C CB  1 
ATOM   4400  C CG  . PHE C  1 70  ? 42.020  23.754 75.342  1.00 60.54  ? 70   PHE C CG  1 
ATOM   4401  C CD1 . PHE C  1 70  ? 42.427  23.444 74.054  1.00 60.76  ? 70   PHE C CD1 1 
ATOM   4402  C CD2 . PHE C  1 70  ? 40.752  23.364 75.750  1.00 60.57  ? 70   PHE C CD2 1 
ATOM   4403  C CE1 . PHE C  1 70  ? 41.579  22.786 73.182  1.00 60.91  ? 70   PHE C CE1 1 
ATOM   4404  C CE2 . PHE C  1 70  ? 39.898  22.705 74.882  1.00 60.86  ? 70   PHE C CE2 1 
ATOM   4405  C CZ  . PHE C  1 70  ? 40.313  22.414 73.596  1.00 61.00  ? 70   PHE C CZ  1 
ATOM   4406  N N   . ILE C  1 71  ? 45.637  23.423 78.644  1.00 67.22  ? 71   ILE C N   1 
ATOM   4407  C CA  . ILE C  1 71  ? 46.739  23.888 79.501  1.00 68.26  ? 71   ILE C CA  1 
ATOM   4408  C C   . ILE C  1 71  ? 48.020  23.957 78.660  1.00 69.53  ? 71   ILE C C   1 
ATOM   4409  O O   . ILE C  1 71  ? 48.352  23.001 77.951  1.00 71.64  ? 71   ILE C O   1 
ATOM   4410  C CB  . ILE C  1 71  ? 46.955  22.988 80.750  1.00 71.18  ? 71   ILE C CB  1 
ATOM   4411  C CG1 . ILE C  1 71  ? 48.170  23.456 81.563  1.00 72.44  ? 71   ILE C CG1 1 
ATOM   4412  C CG2 . ILE C  1 71  ? 47.175  21.523 80.379  1.00 74.48  ? 71   ILE C CG2 1 
ATOM   4413  C CD1 . ILE C  1 71  ? 48.196  22.925 82.982  1.00 74.47  ? 71   ILE C CD1 1 
ATOM   4414  N N   . ASN C  1 72  ? 48.724  25.088 78.732  1.00 68.49  ? 72   ASN C N   1 
ATOM   4415  C CA  . ASN C  1 72  ? 49.946  25.320 77.944  1.00 69.67  ? 72   ASN C CA  1 
ATOM   4416  C C   . ASN C  1 72  ? 49.784  25.039 76.441  1.00 69.11  ? 72   ASN C C   1 
ATOM   4417  O O   . ASN C  1 72  ? 50.539  24.262 75.860  1.00 71.70  ? 72   ASN C O   1 
ATOM   4418  C CB  . ASN C  1 72  ? 51.122  24.510 78.522  1.00 73.68  ? 72   ASN C CB  1 
ATOM   4419  C CG  . ASN C  1 72  ? 51.727  25.155 79.758  1.00 74.32  ? 72   ASN C CG  1 
ATOM   4420  O OD1 . ASN C  1 72  ? 51.536  26.346 80.005  1.00 71.98  ? 72   ASN C OD1 1 
ATOM   4421  N ND2 . ASN C  1 72  ? 52.470  24.373 80.537  1.00 77.72  ? 72   ASN C ND2 1 
ATOM   4422  N N   . VAL C  1 73  ? 48.799  25.683 75.819  1.00 65.91  ? 73   VAL C N   1 
ATOM   4423  C CA  . VAL C  1 73  ? 48.541  25.490 74.385  1.00 65.10  ? 73   VAL C CA  1 
ATOM   4424  C C   . VAL C  1 73  ? 49.690  26.007 73.513  1.00 65.63  ? 73   VAL C C   1 
ATOM   4425  O O   . VAL C  1 73  ? 50.292  27.036 73.827  1.00 65.09  ? 73   VAL C O   1 
ATOM   4426  C CB  . VAL C  1 73  ? 47.230  26.171 73.916  1.00 61.56  ? 73   VAL C CB  1 
ATOM   4427  C CG1 . VAL C  1 73  ? 46.022  25.496 74.544  1.00 61.44  ? 73   VAL C CG1 1 
ATOM   4428  C CG2 . VAL C  1 73  ? 47.231  27.670 74.213  1.00 59.14  ? 73   VAL C CG2 1 
ATOM   4429  N N   . PRO C  1 74  ? 49.991  25.301 72.406  1.00 66.92  ? 74   PRO C N   1 
ATOM   4430  C CA  . PRO C  1 74  ? 50.981  25.809 71.461  1.00 67.33  ? 74   PRO C CA  1 
ATOM   4431  C C   . PRO C  1 74  ? 50.398  26.959 70.645  1.00 63.73  ? 74   PRO C C   1 
ATOM   4432  O O   . PRO C  1 74  ? 49.190  27.212 70.711  1.00 61.12  ? 74   PRO C O   1 
ATOM   4433  C CB  . PRO C  1 74  ? 51.258  24.600 70.566  1.00 69.80  ? 74   PRO C CB  1 
ATOM   4434  C CG  . PRO C  1 74  ? 49.972  23.849 70.560  1.00 68.92  ? 74   PRO C CG  1 
ATOM   4435  C CD  . PRO C  1 74  ? 49.333  24.079 71.906  1.00 67.95  ? 74   PRO C CD  1 
ATOM   4436  N N   . GLU C  1 75  ? 51.242  27.641 69.876  1.00 63.80  ? 75   GLU C N   1 
ATOM   4437  C CA  . GLU C  1 75  ? 50.780  28.783 69.086  1.00 60.68  ? 75   GLU C CA  1 
ATOM   4438  C C   . GLU C  1 75  ? 49.791  28.347 68.007  1.00 59.00  ? 75   GLU C C   1 
ATOM   4439  O O   . GLU C  1 75  ? 49.858  27.225 67.501  1.00 60.73  ? 75   GLU C O   1 
ATOM   4440  C CB  . GLU C  1 75  ? 51.953  29.559 68.476  1.00 61.61  ? 75   GLU C CB  1 
ATOM   4441  C CG  . GLU C  1 75  ? 52.481  29.034 67.154  1.00 63.00  ? 75   GLU C CG  1 
ATOM   4442  C CD  . GLU C  1 75  ? 53.460  30.000 66.522  1.00 63.52  ? 75   GLU C CD  1 
ATOM   4443  O OE1 . GLU C  1 75  ? 54.597  30.120 67.030  1.00 66.19  ? 75   GLU C OE1 1 
ATOM   4444  O OE2 . GLU C  1 75  ? 53.088  30.644 65.518  1.00 61.45  ? 75   GLU C OE2 1 
ATOM   4445  N N   . TRP C  1 76  ? 48.882  29.255 67.663  1.00 55.80  ? 76   TRP C N   1 
ATOM   4446  C CA  . TRP C  1 76  ? 47.781  28.960 66.753  1.00 54.02  ? 76   TRP C CA  1 
ATOM   4447  C C   . TRP C  1 76  ? 47.734  29.967 65.608  1.00 51.94  ? 76   TRP C C   1 
ATOM   4448  O O   . TRP C  1 76  ? 48.125  31.124 65.769  1.00 51.05  ? 76   TRP C O   1 
ATOM   4449  C CB  . TRP C  1 76  ? 46.451  28.986 67.509  1.00 52.27  ? 76   TRP C CB  1 
ATOM   4450  C CG  . TRP C  1 76  ? 46.175  30.307 68.179  1.00 50.27  ? 76   TRP C CG  1 
ATOM   4451  C CD1 . TRP C  1 76  ? 45.546  31.393 67.631  1.00 47.70  ? 76   TRP C CD1 1 
ATOM   4452  C CD2 . TRP C  1 76  ? 46.537  30.686 69.514  1.00 50.91  ? 76   TRP C CD2 1 
ATOM   4453  N NE1 . TRP C  1 76  ? 45.491  32.421 68.546  1.00 46.80  ? 76   TRP C NE1 1 
ATOM   4454  C CE2 . TRP C  1 76  ? 46.092  32.013 69.708  1.00 48.67  ? 76   TRP C CE2 1 
ATOM   4455  C CE3 . TRP C  1 76  ? 47.194  30.032 70.565  1.00 53.30  ? 76   TRP C CE3 1 
ATOM   4456  C CZ2 . TRP C  1 76  ? 46.280  32.696 70.914  1.00 48.74  ? 76   TRP C CZ2 1 
ATOM   4457  C CZ3 . TRP C  1 76  ? 47.382  30.712 71.762  1.00 53.24  ? 76   TRP C CZ3 1 
ATOM   4458  C CH2 . TRP C  1 76  ? 46.927  32.031 71.925  1.00 50.97  ? 76   TRP C CH2 1 
ATOM   4459  N N   . SER C  1 77  ? 47.256  29.512 64.455  1.00 51.35  ? 77   SER C N   1 
ATOM   4460  C CA  . SER C  1 77  ? 46.994  30.388 63.316  1.00 49.20  ? 77   SER C CA  1 
ATOM   4461  C C   . SER C  1 77  ? 45.723  31.191 63.569  1.00 46.27  ? 77   SER C C   1 
ATOM   4462  O O   . SER C  1 77  ? 45.703  32.413 63.420  1.00 44.65  ? 77   SER C O   1 
ATOM   4463  C CB  . SER C  1 77  ? 46.833  29.557 62.046  1.00 49.71  ? 77   SER C CB  1 
ATOM   4464  O OG  . SER C  1 77  ? 46.064  28.391 62.300  1.00 50.49  ? 77   SER C OG  1 
ATOM   4465  N N   . TYR C  1 78  ? 44.666  30.483 63.954  1.00 45.89  ? 78   TYR C N   1 
ATOM   4466  C CA  . TYR C  1 78  ? 43.398  31.096 64.335  1.00 43.62  ? 78   TYR C CA  1 
ATOM   4467  C C   . TYR C  1 78  ? 42.718  30.232 65.401  1.00 44.51  ? 78   TYR C C   1 
ATOM   4468  O O   . TYR C  1 78  ? 43.151  29.110 65.662  1.00 46.75  ? 78   TYR C O   1 
ATOM   4469  C CB  . TYR C  1 78  ? 42.500  31.269 63.100  1.00 41.83  ? 78   TYR C CB  1 
ATOM   4470  C CG  . TYR C  1 78  ? 42.138  29.973 62.393  1.00 42.92  ? 78   TYR C CG  1 
ATOM   4471  C CD1 . TYR C  1 78  ? 43.047  29.333 61.544  1.00 44.48  ? 78   TYR C CD1 1 
ATOM   4472  C CD2 . TYR C  1 78  ? 40.886  29.390 62.571  1.00 42.66  ? 78   TYR C CD2 1 
ATOM   4473  C CE1 . TYR C  1 78  ? 42.716  28.151 60.897  1.00 45.72  ? 78   TYR C CE1 1 
ATOM   4474  C CE2 . TYR C  1 78  ? 40.548  28.209 61.930  1.00 43.96  ? 78   TYR C CE2 1 
ATOM   4475  C CZ  . TYR C  1 78  ? 41.466  27.593 61.095  1.00 45.47  ? 78   TYR C CZ  1 
ATOM   4476  O OH  . TYR C  1 78  ? 41.120  26.417 60.467  1.00 46.98  ? 78   TYR C OH  1 
ATOM   4477  N N   . ILE C  1 79  ? 41.664  30.760 66.018  1.00 43.00  ? 79   ILE C N   1 
ATOM   4478  C CA  . ILE C  1 79  ? 40.942  30.043 67.072  1.00 43.90  ? 79   ILE C CA  1 
ATOM   4479  C C   . ILE C  1 79  ? 39.559  29.632 66.580  1.00 43.20  ? 79   ILE C C   1 
ATOM   4480  O O   . ILE C  1 79  ? 38.921  30.374 65.837  1.00 41.35  ? 79   ILE C O   1 
ATOM   4481  C CB  . ILE C  1 79  ? 40.801  30.914 68.338  1.00 43.22  ? 79   ILE C CB  1 
ATOM   4482  C CG1 . ILE C  1 79  ? 42.180  31.177 68.952  1.00 44.41  ? 79   ILE C CG1 1 
ATOM   4483  C CG2 . ILE C  1 79  ? 39.897  30.241 69.364  1.00 44.01  ? 79   ILE C CG2 1 
ATOM   4484  C CD1 . ILE C  1 79  ? 42.217  32.345 69.915  1.00 43.50  ? 79   ILE C CD1 1 
ATOM   4485  N N   . VAL C  1 80  ? 39.102  28.454 67.002  1.00 44.96  ? 80   VAL C N   1 
ATOM   4486  C CA  . VAL C  1 80  ? 37.774  27.959 66.636  1.00 44.88  ? 80   VAL C CA  1 
ATOM   4487  C C   . VAL C  1 80  ? 36.934  27.683 67.884  1.00 45.69  ? 80   VAL C C   1 
ATOM   4488  O O   . VAL C  1 80  ? 37.275  26.826 68.700  1.00 47.77  ? 80   VAL C O   1 
ATOM   4489  C CB  . VAL C  1 80  ? 37.857  26.679 65.781  1.00 46.70  ? 80   VAL C CB  1 
ATOM   4490  C CG1 . VAL C  1 80  ? 36.471  26.259 65.304  1.00 46.63  ? 80   VAL C CG1 1 
ATOM   4491  C CG2 . VAL C  1 80  ? 38.777  26.901 64.590  1.00 46.23  ? 80   VAL C CG2 1 
ATOM   4492  N N   . GLU C  1 81  ? 35.829  28.413 68.005  1.00 44.26  ? 81   GLU C N   1 
ATOM   4493  C CA  . GLU C  1 81  ? 34.923  28.314 69.141  1.00 44.96  ? 81   GLU C CA  1 
ATOM   4494  C C   . GLU C  1 81  ? 33.522  28.028 68.619  1.00 45.10  ? 81   GLU C C   1 
ATOM   4495  O O   . GLU C  1 81  ? 33.090  28.632 67.644  1.00 43.58  ? 81   GLU C O   1 
ATOM   4496  C CB  . GLU C  1 81  ? 34.928  29.634 69.924  1.00 43.38  ? 81   GLU C CB  1 
ATOM   4497  C CG  . GLU C  1 81  ? 34.088  29.638 71.197  1.00 44.11  ? 81   GLU C CG  1 
ATOM   4498  C CD  . GLU C  1 81  ? 33.990  31.011 71.852  1.00 42.62  ? 81   GLU C CD  1 
ATOM   4499  O OE1 . GLU C  1 81  ? 33.804  32.013 71.127  1.00 40.85  ? 81   GLU C OE1 1 
ATOM   4500  O OE2 . GLU C  1 81  ? 34.089  31.088 73.098  1.00 43.35  ? 81   GLU C OE2 1 
ATOM   4501  N N   . LYS C  1 82  ? 32.810  27.114 69.269  1.00 47.18  ? 82   LYS C N   1 
ATOM   4502  C CA  . LYS C  1 82  ? 31.414  26.838 68.921  1.00 47.78  ? 82   LYS C CA  1 
ATOM   4503  C C   . LYS C  1 82  ? 30.502  28.008 69.301  1.00 46.38  ? 82   LYS C C   1 
ATOM   4504  O O   . LYS C  1 82  ? 30.907  28.927 70.017  1.00 45.16  ? 82   LYS C O   1 
ATOM   4505  C CB  . LYS C  1 82  ? 30.928  25.556 69.607  1.00 50.71  ? 82   LYS C CB  1 
ATOM   4506  C CG  . LYS C  1 82  ? 31.446  24.279 68.967  1.00 52.68  ? 82   LYS C CG  1 
ATOM   4507  C CD  . LYS C  1 82  ? 30.872  23.046 69.653  1.00 55.86  ? 82   LYS C CD  1 
ATOM   4508  C CE  . LYS C  1 82  ? 31.022  21.798 68.797  1.00 58.08  ? 82   LYS C CE  1 
ATOM   4509  N NZ  . LYS C  1 82  ? 32.424  21.303 68.762  1.00 58.89  ? 82   LYS C NZ  1 
ATOM   4510  N N   . ALA C  1 83  ? 29.269  27.963 68.807  1.00 46.82  ? 83   ALA C N   1 
ATOM   4511  C CA  . ALA C  1 83  ? 28.282  29.008 69.087  1.00 45.99  ? 83   ALA C CA  1 
ATOM   4512  C C   . ALA C  1 83  ? 27.846  28.982 70.555  1.00 47.40  ? 83   ALA C C   1 
ATOM   4513  O O   . ALA C  1 83  ? 27.825  30.024 71.214  1.00 46.38  ? 83   ALA C O   1 
ATOM   4514  C CB  . ALA C  1 83  ? 27.078  28.861 68.166  1.00 46.41  ? 83   ALA C CB  1 
ATOM   4515  N N   . ASN C  1 84  ? 27.516  27.794 71.064  1.00 50.00  ? 84   ASN C N   1 
ATOM   4516  C CA  . ASN C  1 84  ? 27.085  27.630 72.459  1.00 51.66  ? 84   ASN C CA  1 
ATOM   4517  C C   . ASN C  1 84  ? 27.875  26.529 73.189  1.00 53.51  ? 84   ASN C C   1 
ATOM   4518  O O   . ASN C  1 84  ? 27.310  25.488 73.539  1.00 56.14  ? 84   ASN C O   1 
ATOM   4519  C CB  . ASN C  1 84  ? 25.577  27.318 72.518  1.00 53.63  ? 84   ASN C CB  1 
ATOM   4520  C CG  . ASN C  1 84  ? 24.739  28.265 71.664  1.00 52.33  ? 84   ASN C CG  1 
ATOM   4521  O OD1 . ASN C  1 84  ? 24.933  29.484 71.688  1.00 50.30  ? 84   ASN C OD1 1 
ATOM   4522  N ND2 . ASN C  1 84  ? 23.795  27.704 70.908  1.00 53.76  ? 84   ASN C ND2 1 
ATOM   4523  N N   . PRO C  1 85  ? 29.182  26.756 73.434  1.00 52.42  ? 85   PRO C N   1 
ATOM   4524  C CA  . PRO C  1 85  ? 30.001  25.735 74.101  1.00 54.31  ? 85   PRO C CA  1 
ATOM   4525  C C   . PRO C  1 85  ? 29.506  25.419 75.513  1.00 56.18  ? 85   PRO C C   1 
ATOM   4526  O O   . PRO C  1 85  ? 29.245  26.342 76.286  1.00 55.23  ? 85   PRO C O   1 
ATOM   4527  C CB  . PRO C  1 85  ? 31.401  26.371 74.149  1.00 52.60  ? 85   PRO C CB  1 
ATOM   4528  C CG  . PRO C  1 85  ? 31.374  27.480 73.158  1.00 49.97  ? 85   PRO C CG  1 
ATOM   4529  C CD  . PRO C  1 85  ? 29.961  27.971 73.140  1.00 49.71  ? 85   PRO C CD  1 
ATOM   4530  N N   . VAL C  1 86  ? 29.382  24.131 75.840  1.00 58.99  ? 86   VAL C N   1 
ATOM   4531  C CA  . VAL C  1 86  ? 28.840  23.709 77.145  1.00 61.13  ? 86   VAL C CA  1 
ATOM   4532  C C   . VAL C  1 86  ? 29.790  24.000 78.312  1.00 60.82  ? 86   VAL C C   1 
ATOM   4533  O O   . VAL C  1 86  ? 29.344  24.420 79.381  1.00 61.05  ? 86   VAL C O   1 
ATOM   4534  C CB  . VAL C  1 86  ? 28.435  22.208 77.174  1.00 64.67  ? 86   VAL C CB  1 
ATOM   4535  C CG1 . VAL C  1 86  ? 27.408  21.910 76.088  1.00 65.30  ? 86   VAL C CG1 1 
ATOM   4536  C CG2 . VAL C  1 86  ? 29.645  21.286 77.046  1.00 65.93  ? 86   VAL C CG2 1 
ATOM   4537  N N   . ASN C  1 87  ? 31.088  23.774 78.102  1.00 60.44  ? 87   ASN C N   1 
ATOM   4538  C CA  . ASN C  1 87  ? 32.100  24.009 79.133  1.00 60.30  ? 87   ASN C CA  1 
ATOM   4539  C C   . ASN C  1 87  ? 32.542  25.467 79.150  1.00 57.27  ? 87   ASN C C   1 
ATOM   4540  O O   . ASN C  1 87  ? 33.624  25.800 78.670  1.00 56.10  ? 87   ASN C O   1 
ATOM   4541  C CB  . ASN C  1 87  ? 33.321  23.106 78.917  1.00 61.77  ? 87   ASN C CB  1 
ATOM   4542  C CG  . ASN C  1 87  ? 33.049  21.652 79.253  1.00 65.31  ? 87   ASN C CG  1 
ATOM   4543  O OD1 . ASN C  1 87  ? 32.252  21.341 80.141  1.00 66.92  ? 87   ASN C OD1 1 
ATOM   4544  N ND2 . ASN C  1 87  ? 33.731  20.748 78.556  1.00 66.81  ? 87   ASN C ND2 1 
ATOM   4545  N N   . ASP C  1 88  ? 31.697  26.330 79.705  1.00 56.27  ? 88   ASP C N   1 
ATOM   4546  C CA  . ASP C  1 88  ? 32.016  27.748 79.842  1.00 53.77  ? 88   ASP C CA  1 
ATOM   4547  C C   . ASP C  1 88  ? 32.368  28.022 81.315  1.00 54.35  ? 88   ASP C C   1 
ATOM   4548  O O   . ASP C  1 88  ? 33.375  27.507 81.813  1.00 55.35  ? 88   ASP C O   1 
ATOM   4549  C CB  . ASP C  1 88  ? 30.847  28.602 79.320  1.00 52.40  ? 88   ASP C CB  1 
ATOM   4550  C CG  . ASP C  1 88  ? 31.193  30.085 79.208  1.00 49.97  ? 88   ASP C CG  1 
ATOM   4551  O OD1 . ASP C  1 88  ? 32.377  30.454 79.350  1.00 49.17  ? 88   ASP C OD1 1 
ATOM   4552  O OD2 . ASP C  1 88  ? 30.267  30.889 78.973  1.00 49.11  ? 88   ASP C OD2 1 
ATOM   4553  N N   . LEU C  1 89  ? 31.551  28.811 82.009  1.00 53.89  ? 89   LEU C N   1 
ATOM   4554  C CA  . LEU C  1 89  ? 31.759  29.089 83.425  1.00 54.55  ? 89   LEU C CA  1 
ATOM   4555  C C   . LEU C  1 89  ? 31.094  27.985 84.243  1.00 57.20  ? 89   LEU C C   1 
ATOM   4556  O O   . LEU C  1 89  ? 29.878  28.009 84.454  1.00 57.97  ? 89   LEU C O   1 
ATOM   4557  C CB  . LEU C  1 89  ? 31.184  30.469 83.795  1.00 53.12  ? 89   LEU C CB  1 
ATOM   4558  C CG  . LEU C  1 89  ? 32.120  31.689 83.789  1.00 51.17  ? 89   LEU C CG  1 
ATOM   4559  C CD1 . LEU C  1 89  ? 33.207  31.604 82.729  1.00 50.07  ? 89   LEU C CD1 1 
ATOM   4560  C CD2 . LEU C  1 89  ? 31.309  32.969 83.626  1.00 49.85  ? 89   LEU C CD2 1 
ATOM   4561  N N   . CYS C  1 90  ? 31.893  27.014 84.687  1.00 58.82  ? 90   CYS C N   1 
ATOM   4562  C CA  . CYS C  1 90  ? 31.378  25.904 85.490  1.00 61.65  ? 90   CYS C CA  1 
ATOM   4563  C C   . CYS C  1 90  ? 30.686  26.435 86.743  1.00 62.15  ? 90   CYS C C   1 
ATOM   4564  O O   . CYS C  1 90  ? 29.551  26.060 87.029  1.00 63.76  ? 90   CYS C O   1 
ATOM   4565  C CB  . CYS C  1 90  ? 32.483  24.895 85.844  1.00 63.40  ? 90   CYS C CB  1 
ATOM   4566  S SG  . CYS C  1 90  ? 34.017  25.584 86.511  1.00 62.29  ? 90   CYS C SG  1 
ATOM   4567  N N   . TYR C  1 91  ? 31.362  27.325 87.467  1.00 60.96  ? 91   TYR C N   1 
ATOM   4568  C CA  . TYR C  1 91  ? 30.730  28.065 88.555  1.00 61.12  ? 91   TYR C CA  1 
ATOM   4569  C C   . TYR C  1 91  ? 30.063  29.320 87.977  1.00 59.04  ? 91   TYR C C   1 
ATOM   4570  O O   . TYR C  1 91  ? 30.737  30.121 87.327  1.00 56.95  ? 91   TYR C O   1 
ATOM   4571  C CB  . TYR C  1 91  ? 31.754  28.455 89.624  1.00 61.06  ? 91   TYR C CB  1 
ATOM   4572  C CG  . TYR C  1 91  ? 31.124  28.841 90.948  1.00 62.09  ? 91   TYR C CG  1 
ATOM   4573  C CD1 . TYR C  1 91  ? 30.634  30.129 91.162  1.00 60.76  ? 91   TYR C CD1 1 
ATOM   4574  C CD2 . TYR C  1 91  ? 31.004  27.914 91.982  1.00 64.61  ? 91   TYR C CD2 1 
ATOM   4575  C CE1 . TYR C  1 91  ? 30.052  30.483 92.371  1.00 61.89  ? 91   TYR C CE1 1 
ATOM   4576  C CE2 . TYR C  1 91  ? 30.423  28.258 93.194  1.00 65.64  ? 91   TYR C CE2 1 
ATOM   4577  C CZ  . TYR C  1 91  ? 29.949  29.544 93.384  1.00 64.27  ? 91   TYR C CZ  1 
ATOM   4578  O OH  . TYR C  1 91  ? 29.373  29.886 94.588  1.00 65.55  ? 91   TYR C OH  1 
ATOM   4579  N N   . PRO C  1 92  ? 28.746  29.502 88.218  1.00 59.89  ? 92   PRO C N   1 
ATOM   4580  C CA  . PRO C  1 92  ? 27.991  30.619 87.623  1.00 58.36  ? 92   PRO C CA  1 
ATOM   4581  C C   . PRO C  1 92  ? 28.623  31.982 87.875  1.00 56.38  ? 92   PRO C C   1 
ATOM   4582  O O   . PRO C  1 92  ? 29.248  32.194 88.914  1.00 56.67  ? 92   PRO C O   1 
ATOM   4583  C CB  . PRO C  1 92  ? 26.635  30.560 88.331  1.00 60.38  ? 92   PRO C CB  1 
ATOM   4584  C CG  . PRO C  1 92  ? 26.524  29.186 88.866  1.00 62.95  ? 92   PRO C CG  1 
ATOM   4585  C CD  . PRO C  1 92  ? 27.913  28.702 89.135  1.00 62.63  ? 92   PRO C CD  1 
ATOM   4586  N N   . GLY C  1 93  ? 28.447  32.899 86.931  1.00 54.56  ? 93   GLY C N   1 
ATOM   4587  C CA  . GLY C  1 93  ? 28.995  34.237 87.074  1.00 52.90  ? 93   GLY C CA  1 
ATOM   4588  C C   . GLY C  1 93  ? 29.025  35.037 85.790  1.00 50.94  ? 93   GLY C C   1 
ATOM   4589  O O   . GLY C  1 93  ? 28.344  34.706 84.817  1.00 50.81  ? 93   GLY C O   1 
ATOM   4590  N N   . ASP C  1 94  ? 29.821  36.104 85.811  1.00 49.56  ? 94   ASP C N   1 
ATOM   4591  C CA  . ASP C  1 94  ? 30.042  36.958 84.652  1.00 47.72  ? 94   ASP C CA  1 
ATOM   4592  C C   . ASP C  1 94  ? 31.532  37.103 84.419  1.00 46.62  ? 94   ASP C C   1 
ATOM   4593  O O   . ASP C  1 94  ? 32.335  36.991 85.352  1.00 47.22  ? 94   ASP C O   1 
ATOM   4594  C CB  . ASP C  1 94  ? 29.455  38.351 84.883  1.00 47.51  ? 94   ASP C CB  1 
ATOM   4595  C CG  . ASP C  1 94  ? 27.973  38.320 85.178  1.00 48.90  ? 94   ASP C CG  1 
ATOM   4596  O OD1 . ASP C  1 94  ? 27.186  38.053 84.241  1.00 48.84  ? 94   ASP C OD1 1 
ATOM   4597  O OD2 . ASP C  1 94  ? 27.597  38.574 86.345  1.00 50.24  ? 94   ASP C OD2 1 
ATOM   4598  N N   . PHE C  1 95  ? 31.893  37.351 83.165  1.00 45.13  ? 95   PHE C N   1 
ATOM   4599  C CA  . PHE C  1 95  ? 33.258  37.681 82.804  1.00 44.18  ? 95   PHE C CA  1 
ATOM   4600  C C   . PHE C  1 95  ? 33.250  39.148 82.394  1.00 43.02  ? 95   PHE C C   1 
ATOM   4601  O O   . PHE C  1 95  ? 32.601  39.528 81.415  1.00 42.15  ? 95   PHE C O   1 
ATOM   4602  C CB  . PHE C  1 95  ? 33.739  36.779 81.664  1.00 43.72  ? 95   PHE C CB  1 
ATOM   4603  C CG  . PHE C  1 95  ? 35.229  36.576 81.631  1.00 43.77  ? 95   PHE C CG  1 
ATOM   4604  C CD1 . PHE C  1 95  ? 36.090  37.641 81.402  1.00 42.98  ? 95   PHE C CD1 1 
ATOM   4605  C CD2 . PHE C  1 95  ? 35.771  35.313 81.821  1.00 44.93  ? 95   PHE C CD2 1 
ATOM   4606  C CE1 . PHE C  1 95  ? 37.460  37.450 81.366  1.00 43.38  ? 95   PHE C CE1 1 
ATOM   4607  C CE2 . PHE C  1 95  ? 37.141  35.116 81.784  1.00 45.32  ? 95   PHE C CE2 1 
ATOM   4608  C CZ  . PHE C  1 95  ? 37.987  36.186 81.559  1.00 44.55  ? 95   PHE C CZ  1 
ATOM   4609  N N   . ASN C  1 96  ? 33.953  39.972 83.162  1.00 43.18  ? 96   ASN C N   1 
ATOM   4610  C CA  . ASN C  1 96  ? 33.974  41.410 82.928  1.00 42.54  ? 96   ASN C CA  1 
ATOM   4611  C C   . ASN C  1 96  ? 34.750  41.774 81.658  1.00 41.27  ? 96   ASN C C   1 
ATOM   4612  O O   . ASN C  1 96  ? 35.883  41.328 81.470  1.00 41.26  ? 96   ASN C O   1 
ATOM   4613  C CB  . ASN C  1 96  ? 34.575  42.127 84.139  1.00 43.47  ? 96   ASN C CB  1 
ATOM   4614  C CG  . ASN C  1 96  ? 34.276  43.613 84.143  1.00 43.46  ? 96   ASN C CG  1 
ATOM   4615  O OD1 . ASN C  1 96  ? 33.109  44.021 84.141  1.00 43.66  ? 96   ASN C OD1 1 
ATOM   4616  N ND2 . ASN C  1 96  ? 35.323  44.433 84.153  1.00 43.54  ? 96   ASN C ND2 1 
ATOM   4617  N N   . ASP C  1 97  ? 34.131  42.589 80.803  1.00 40.39  ? 97   ASP C N   1 
ATOM   4618  C CA  . ASP C  1 97  ? 34.697  42.980 79.502  1.00 39.20  ? 97   ASP C CA  1 
ATOM   4619  C C   . ASP C  1 97  ? 35.221  41.766 78.729  1.00 38.63  ? 97   ASP C C   1 
ATOM   4620  O O   . ASP C  1 97  ? 36.369  41.741 78.275  1.00 38.47  ? 97   ASP C O   1 
ATOM   4621  C CB  . ASP C  1 97  ? 35.796  44.041 79.677  1.00 39.47  ? 97   ASP C CB  1 
ATOM   4622  C CG  . ASP C  1 97  ? 35.250  45.393 80.120  1.00 39.99  ? 97   ASP C CG  1 
ATOM   4623  O OD1 . ASP C  1 97  ? 34.034  45.629 79.996  1.00 39.95  ? 97   ASP C OD1 1 
ATOM   4624  O OD2 . ASP C  1 97  ? 36.046  46.229 80.593  1.00 40.71  ? 97   ASP C OD2 1 
ATOM   4625  N N   . TYR C  1 98  ? 34.363  40.759 78.601  1.00 38.59  ? 98   TYR C N   1 
ATOM   4626  C CA  . TYR C  1 98  ? 34.703  39.502 77.933  1.00 38.41  ? 98   TYR C CA  1 
ATOM   4627  C C   . TYR C  1 98  ? 34.919  39.710 76.434  1.00 37.14  ? 98   TYR C C   1 
ATOM   4628  O O   . TYR C  1 98  ? 35.831  39.130 75.835  1.00 37.04  ? 98   TYR C O   1 
ATOM   4629  C CB  . TYR C  1 98  ? 33.567  38.501 78.165  1.00 39.07  ? 98   TYR C CB  1 
ATOM   4630  C CG  . TYR C  1 98  ? 33.806  37.080 77.691  1.00 39.50  ? 98   TYR C CG  1 
ATOM   4631  C CD1 . TYR C  1 98  ? 35.039  36.451 77.864  1.00 40.07  ? 98   TYR C CD1 1 
ATOM   4632  C CD2 . TYR C  1 98  ? 32.773  36.347 77.109  1.00 39.69  ? 98   TYR C CD2 1 
ATOM   4633  C CE1 . TYR C  1 98  ? 35.241  35.144 77.442  1.00 40.81  ? 98   TYR C CE1 1 
ATOM   4634  C CE2 . TYR C  1 98  ? 32.967  35.043 76.686  1.00 40.40  ? 98   TYR C CE2 1 
ATOM   4635  C CZ  . TYR C  1 98  ? 34.200  34.445 76.856  1.00 40.97  ? 98   TYR C CZ  1 
ATOM   4636  O OH  . TYR C  1 98  ? 34.384  33.149 76.436  1.00 41.99  ? 98   TYR C OH  1 
ATOM   4637  N N   . GLU C  1 99  ? 34.075  40.549 75.844  1.00 36.31  ? 99   GLU C N   1 
ATOM   4638  C CA  . GLU C  1 99  ? 34.108  40.803 74.412  1.00 35.14  ? 99   GLU C CA  1 
ATOM   4639  C C   . GLU C  1 99  ? 35.349  41.606 74.043  1.00 34.74  ? 99   GLU C C   1 
ATOM   4640  O O   . GLU C  1 99  ? 35.997  41.333 73.034  1.00 34.19  ? 99   GLU C O   1 
ATOM   4641  C CB  . GLU C  1 99  ? 32.844  41.542 73.964  1.00 34.71  ? 99   GLU C CB  1 
ATOM   4642  C CG  . GLU C  1 99  ? 31.571  40.703 74.000  1.00 35.21  ? 99   GLU C CG  1 
ATOM   4643  C CD  . GLU C  1 99  ? 31.050  40.448 75.403  1.00 36.51  ? 99   GLU C CD  1 
ATOM   4644  O OE1 . GLU C  1 99  ? 31.085  41.375 76.243  1.00 36.90  ? 99   GLU C OE1 1 
ATOM   4645  O OE2 . GLU C  1 99  ? 30.597  39.316 75.662  1.00 37.31  ? 99   GLU C OE2 1 
ATOM   4646  N N   . GLU C  1 100 ? 35.683  42.588 74.874  1.00 35.22  ? 100  GLU C N   1 
ATOM   4647  C CA  . GLU C  1 100 ? 36.903  43.366 74.683  1.00 35.33  ? 100  GLU C CA  1 
ATOM   4648  C C   . GLU C  1 100 ? 38.152  42.490 74.798  1.00 35.94  ? 100  GLU C C   1 
ATOM   4649  O O   . GLU C  1 100 ? 39.125  42.698 74.077  1.00 35.94  ? 100  GLU C O   1 
ATOM   4650  C CB  . GLU C  1 100 ? 36.968  44.524 75.682  1.00 36.11  ? 100  GLU C CB  1 
ATOM   4651  C CG  . GLU C  1 100 ? 36.041  45.678 75.344  1.00 35.81  ? 100  GLU C CG  1 
ATOM   4652  C CD  . GLU C  1 100 ? 36.496  46.454 74.124  1.00 35.24  ? 100  GLU C CD  1 
ATOM   4653  O OE1 . GLU C  1 100 ? 37.687  46.811 74.054  1.00 35.73  ? 100  GLU C OE1 1 
ATOM   4654  O OE2 . GLU C  1 100 ? 35.663  46.715 73.231  1.00 34.49  ? 100  GLU C OE2 1 
ATOM   4655  N N   . LEU C  1 101 ? 38.123  41.511 75.697  1.00 36.70  ? 101  LEU C N   1 
ATOM   4656  C CA  . LEU C  1 101 ? 39.242  40.583 75.835  1.00 37.59  ? 101  LEU C CA  1 
ATOM   4657  C C   . LEU C  1 101 ? 39.319  39.673 74.622  1.00 37.11  ? 101  LEU C C   1 
ATOM   4658  O O   . LEU C  1 101 ? 40.396  39.457 74.075  1.00 37.53  ? 101  LEU C O   1 
ATOM   4659  C CB  . LEU C  1 101 ? 39.122  39.739 77.111  1.00 38.70  ? 101  LEU C CB  1 
ATOM   4660  C CG  . LEU C  1 101 ? 40.286  38.779 77.394  1.00 40.01  ? 101  LEU C CG  1 
ATOM   4661  C CD1 . LEU C  1 101 ? 41.631  39.494 77.367  1.00 40.67  ? 101  LEU C CD1 1 
ATOM   4662  C CD2 . LEU C  1 101 ? 40.080  38.094 78.735  1.00 41.19  ? 101  LEU C CD2 1 
ATOM   4663  N N   . LYS C  1 102 ? 38.173  39.139 74.212  1.00 36.47  ? 102  LYS C N   1 
ATOM   4664  C CA  . LYS C  1 102 ? 38.090  38.336 72.991  1.00 36.04  ? 102  LYS C CA  1 
ATOM   4665  C C   . LYS C  1 102 ? 38.628  39.082 71.772  1.00 35.13  ? 102  LYS C C   1 
ATOM   4666  O O   . LYS C  1 102 ? 39.259  38.492 70.901  1.00 35.22  ? 102  LYS C O   1 
ATOM   4667  C CB  . LYS C  1 102 ? 36.647  37.917 72.724  1.00 35.57  ? 102  LYS C CB  1 
ATOM   4668  C CG  . LYS C  1 102 ? 36.237  36.617 73.390  1.00 36.80  ? 102  LYS C CG  1 
ATOM   4669  C CD  . LYS C  1 102 ? 34.742  36.391 73.222  1.00 36.63  ? 102  LYS C CD  1 
ATOM   4670  C CE  . LYS C  1 102 ? 34.419  34.962 72.826  1.00 37.55  ? 102  LYS C CE  1 
ATOM   4671  N NZ  . LYS C  1 102 ? 32.959  34.814 72.583  1.00 37.59  ? 102  LYS C NZ  1 
ATOM   4672  N N   . HIS C  1 103 ? 38.364  40.379 71.710  1.00 34.45  ? 103  HIS C N   1 
ATOM   4673  C CA  . HIS C  1 103 ? 38.881  41.200 70.626  1.00 33.84  ? 103  HIS C CA  1 
ATOM   4674  C C   . HIS C  1 103 ? 40.406  41.288 70.695  1.00 34.93  ? 103  HIS C C   1 
ATOM   4675  O O   . HIS C  1 103 ? 41.074  41.308 69.667  1.00 34.84  ? 103  HIS C O   1 
ATOM   4676  C CB  . HIS C  1 103 ? 38.258  42.599 70.667  1.00 33.26  ? 103  HIS C CB  1 
ATOM   4677  C CG  . HIS C  1 103 ? 38.749  43.508 69.585  1.00 32.77  ? 103  HIS C CG  1 
ATOM   4678  N ND1 . HIS C  1 103 ? 38.208  43.519 68.318  1.00 31.69  ? 103  HIS C ND1 1 
ATOM   4679  C CD2 . HIS C  1 103 ? 39.738  44.432 69.580  1.00 33.43  ? 103  HIS C CD2 1 
ATOM   4680  C CE1 . HIS C  1 103 ? 38.837  44.416 67.581  1.00 31.63  ? 103  HIS C CE1 1 
ATOM   4681  N NE2 . HIS C  1 103 ? 39.769  44.984 68.324  1.00 32.75  ? 103  HIS C NE2 1 
ATOM   4682  N N   . LEU C  1 104 ? 40.945  41.334 71.908  1.00 36.15  ? 104  LEU C N   1 
ATOM   4683  C CA  . LEU C  1 104 ? 42.393  41.375 72.120  1.00 37.63  ? 104  LEU C CA  1 
ATOM   4684  C C   . LEU C  1 104 ? 43.075  40.116 71.568  1.00 38.40  ? 104  LEU C C   1 
ATOM   4685  O O   . LEU C  1 104 ? 44.203  40.178 71.083  1.00 39.33  ? 104  LEU C O   1 
ATOM   4686  C CB  . LEU C  1 104 ? 42.705  41.528 73.615  1.00 38.86  ? 104  LEU C CB  1 
ATOM   4687  C CG  . LEU C  1 104 ? 43.599  42.696 74.032  1.00 39.90  ? 104  LEU C CG  1 
ATOM   4688  C CD1 . LEU C  1 104 ? 42.909  44.027 73.774  1.00 39.02  ? 104  LEU C CD1 1 
ATOM   4689  C CD2 . LEU C  1 104 ? 43.940  42.568 75.506  1.00 41.23  ? 104  LEU C CD2 1 
ATOM   4690  N N   . LEU C  1 105 ? 42.374  38.984 71.641  1.00 40.17  ? 105  LEU C N   1 
ATOM   4691  C CA  . LEU C  1 105 ? 42.862  37.703 71.111  1.00 40.80  ? 105  LEU C CA  1 
ATOM   4692  C C   . LEU C  1 105 ? 42.978  37.648 69.590  1.00 41.25  ? 105  LEU C C   1 
ATOM   4693  O O   . LEU C  1 105 ? 43.682  36.788 69.054  1.00 41.98  ? 105  LEU C O   1 
ATOM   4694  C CB  . LEU C  1 105 ? 41.952  36.556 71.558  1.00 40.59  ? 105  LEU C CB  1 
ATOM   4695  C CG  . LEU C  1 105 ? 42.217  35.973 72.938  1.00 40.85  ? 105  LEU C CG  1 
ATOM   4696  C CD1 . LEU C  1 105 ? 41.123  34.978 73.294  1.00 40.74  ? 105  LEU C CD1 1 
ATOM   4697  C CD2 . LEU C  1 105 ? 43.585  35.309 72.972  1.00 41.87  ? 105  LEU C CD2 1 
ATOM   4698  N N   . SER C  1 106 ? 42.273  38.537 68.896  1.00 41.01  ? 106  SER C N   1 
ATOM   4699  C CA  . SER C  1 106 ? 42.403  38.641 67.446  1.00 41.66  ? 106  SER C CA  1 
ATOM   4700  C C   . SER C  1 106 ? 43.786  39.171 67.042  1.00 42.63  ? 106  SER C C   1 
ATOM   4701  O O   . SER C  1 106 ? 44.212  38.973 65.905  1.00 43.45  ? 106  SER C O   1 
ATOM   4702  C CB  . SER C  1 106 ? 41.293  39.522 66.855  1.00 41.33  ? 106  SER C CB  1 
ATOM   4703  O OG  . SER C  1 106 ? 41.458  40.887 67.201  1.00 41.26  ? 106  SER C OG  1 
ATOM   4704  N N   . ARG C  1 107 ? 44.472  39.843 67.969  1.00 42.75  ? 107  ARG C N   1 
ATOM   4705  C CA  . ARG C  1 107 ? 45.852  40.311 67.753  1.00 43.86  ? 107  ARG C CA  1 
ATOM   4706  C C   . ARG C  1 107 ? 46.913  39.382 68.370  1.00 44.46  ? 107  ARG C C   1 
ATOM   4707  O O   . ARG C  1 107 ? 48.093  39.738 68.407  1.00 45.41  ? 107  ARG C O   1 
ATOM   4708  C CB  . ARG C  1 107 ? 46.038  41.728 68.326  1.00 43.90  ? 107  ARG C CB  1 
ATOM   4709  C CG  . ARG C  1 107 ? 45.580  42.867 67.421  1.00 44.18  ? 107  ARG C CG  1 
ATOM   4710  C CD  . ARG C  1 107 ? 46.272  44.175 67.809  1.00 44.83  ? 107  ARG C CD  1 
ATOM   4711  N NE  . ARG C  1 107 ? 45.493  45.376 67.466  1.00 44.83  ? 107  ARG C NE  1 
ATOM   4712  C CZ  . ARG C  1 107 ? 45.827  46.304 66.559  1.00 45.94  ? 107  ARG C CZ  1 
ATOM   4713  N NH1 . ARG C  1 107 ? 46.954  46.221 65.846  1.00 47.19  ? 107  ARG C NH1 1 
ATOM   4714  N NH2 . ARG C  1 107 ? 45.015  47.342 66.363  1.00 45.95  ? 107  ARG C NH2 1 
ATOM   4715  N N   . ILE C  1 108 ? 46.502  38.205 68.845  1.00 44.10  ? 108  ILE C N   1 
ATOM   4716  C CA  . ILE C  1 108 ? 47.399  37.311 69.583  1.00 44.80  ? 108  ILE C CA  1 
ATOM   4717  C C   . ILE C  1 108 ? 47.483  35.925 68.940  1.00 45.43  ? 108  ILE C C   1 
ATOM   4718  O O   . ILE C  1 108 ? 46.461  35.291 68.667  1.00 44.84  ? 108  ILE C O   1 
ATOM   4719  C CB  . ILE C  1 108 ? 46.963  37.169 71.062  1.00 44.16  ? 108  ILE C CB  1 
ATOM   4720  C CG1 . ILE C  1 108 ? 47.043  38.525 71.772  1.00 43.79  ? 108  ILE C CG1 1 
ATOM   4721  C CG2 . ILE C  1 108 ? 47.843  36.159 71.792  1.00 45.14  ? 108  ILE C CG2 1 
ATOM   4722  C CD1 . ILE C  1 108 ? 46.318  38.578 73.102  1.00 43.09  ? 108  ILE C CD1 1 
ATOM   4723  N N   . ASN C  1 109 ? 48.715  35.463 68.727  1.00 46.79  ? 109  ASN C N   1 
ATOM   4724  C CA  . ASN C  1 109 ? 48.984  34.135 68.167  1.00 47.74  ? 109  ASN C CA  1 
ATOM   4725  C C   . ASN C  1 109 ? 49.492  33.113 69.188  1.00 48.47  ? 109  ASN C C   1 
ATOM   4726  O O   . ASN C  1 109 ? 49.344  31.908 68.966  1.00 48.99  ? 109  ASN C O   1 
ATOM   4727  C CB  . ASN C  1 109 ? 49.986  34.233 67.009  1.00 49.10  ? 109  ASN C CB  1 
ATOM   4728  C CG  . ASN C  1 109 ? 49.306  34.333 65.659  1.00 48.92  ? 109  ASN C CG  1 
ATOM   4729  O OD1 . ASN C  1 109 ? 49.474  33.465 64.805  1.00 49.86  ? 109  ASN C OD1 1 
ATOM   4730  N ND2 . ASN C  1 109 ? 48.524  35.385 65.463  1.00 47.89  ? 109  ASN C ND2 1 
ATOM   4731  N N   . HIS C  1 110 ? 50.098  33.574 70.284  1.00 48.68  ? 110  HIS C N   1 
ATOM   4732  C CA  . HIS C  1 110 ? 50.588  32.651 71.310  1.00 49.61  ? 110  HIS C CA  1 
ATOM   4733  C C   . HIS C  1 110 ? 50.670  33.223 72.722  1.00 49.36  ? 110  HIS C C   1 
ATOM   4734  O O   . HIS C  1 110 ? 51.208  34.311 72.945  1.00 49.35  ? 110  HIS C O   1 
ATOM   4735  C CB  . HIS C  1 110 ? 51.962  32.096 70.925  1.00 51.55  ? 110  HIS C CB  1 
ATOM   4736  C CG  . HIS C  1 110 ? 52.350  30.866 71.689  1.00 52.79  ? 110  HIS C CG  1 
ATOM   4737  N ND1 . HIS C  1 110 ? 53.656  30.570 72.014  1.00 54.65  ? 110  HIS C ND1 1 
ATOM   4738  C CD2 . HIS C  1 110 ? 51.598  29.862 72.203  1.00 52.62  ? 110  HIS C CD2 1 
ATOM   4739  C CE1 . HIS C  1 110 ? 53.694  29.433 72.685  1.00 55.61  ? 110  HIS C CE1 1 
ATOM   4740  N NE2 . HIS C  1 110 ? 52.458  28.984 72.814  1.00 54.40  ? 110  HIS C NE2 1 
ATOM   4741  N N   . PHE C  1 111 ? 50.131  32.453 73.664  1.00 49.32  ? 111  PHE C N   1 
ATOM   4742  C CA  . PHE C  1 111 ? 50.289  32.707 75.087  1.00 49.55  ? 111  PHE C CA  1 
ATOM   4743  C C   . PHE C  1 111 ? 51.292  31.710 75.651  1.00 51.48  ? 111  PHE C C   1 
ATOM   4744  O O   . PHE C  1 111 ? 51.338  30.563 75.204  1.00 52.29  ? 111  PHE C O   1 
ATOM   4745  C CB  . PHE C  1 111 ? 48.959  32.511 75.831  1.00 48.45  ? 111  PHE C CB  1 
ATOM   4746  C CG  . PHE C  1 111 ? 48.038  33.703 75.795  1.00 46.82  ? 111  PHE C CG  1 
ATOM   4747  C CD1 . PHE C  1 111 ? 48.505  34.985 76.065  1.00 46.62  ? 111  PHE C CD1 1 
ATOM   4748  C CD2 . PHE C  1 111 ? 46.683  33.533 75.543  1.00 45.68  ? 111  PHE C CD2 1 
ATOM   4749  C CE1 . PHE C  1 111 ? 47.646  36.070 76.049  1.00 45.33  ? 111  PHE C CE1 1 
ATOM   4750  C CE2 . PHE C  1 111 ? 45.821  34.615 75.530  1.00 44.41  ? 111  PHE C CE2 1 
ATOM   4751  C CZ  . PHE C  1 111 ? 46.302  35.885 75.784  1.00 44.24  ? 111  PHE C CZ  1 
ATOM   4752  N N   . GLU C  1 112 ? 52.090  32.152 76.623  1.00 52.41  ? 112  GLU C N   1 
ATOM   4753  C CA  . GLU C  1 112 ? 52.890  31.243 77.454  1.00 54.37  ? 112  GLU C CA  1 
ATOM   4754  C C   . GLU C  1 112 ? 52.487  31.436 78.911  1.00 54.30  ? 112  GLU C C   1 
ATOM   4755  O O   . GLU C  1 112 ? 52.529  32.548 79.429  1.00 53.73  ? 112  GLU C O   1 
ATOM   4756  C CB  . GLU C  1 112 ? 54.392  31.494 77.297  1.00 56.10  ? 112  GLU C CB  1 
ATOM   4757  C CG  . GLU C  1 112 ? 55.248  30.316 77.758  1.00 58.43  ? 112  GLU C CG  1 
ATOM   4758  C CD  . GLU C  1 112 ? 56.546  30.740 78.428  1.00 60.28  ? 112  GLU C CD  1 
ATOM   4759  O OE1 . GLU C  1 112 ? 57.226  31.647 77.899  1.00 60.41  ? 112  GLU C OE1 1 
ATOM   4760  O OE2 . GLU C  1 112 ? 56.892  30.161 79.484  1.00 61.79  ? 112  GLU C OE2 1 
ATOM   4761  N N   . LYS C  1 113 ? 52.092  30.353 79.567  1.00 55.03  ? 113  LYS C N   1 
ATOM   4762  C CA  . LYS C  1 113 ? 51.603  30.429 80.940  1.00 55.16  ? 113  LYS C CA  1 
ATOM   4763  C C   . LYS C  1 113 ? 52.763  30.505 81.932  1.00 57.11  ? 113  LYS C C   1 
ATOM   4764  O O   . LYS C  1 113 ? 53.778  29.832 81.751  1.00 58.90  ? 113  LYS C O   1 
ATOM   4765  C CB  . LYS C  1 113 ? 50.730  29.212 81.233  1.00 55.48  ? 113  LYS C CB  1 
ATOM   4766  C CG  . LYS C  1 113 ? 49.899  29.315 82.499  1.00 55.36  ? 113  LYS C CG  1 
ATOM   4767  C CD  . LYS C  1 113 ? 48.483  28.800 82.278  1.00 54.30  ? 113  LYS C CD  1 
ATOM   4768  C CE  . LYS C  1 113 ? 48.423  27.335 81.865  1.00 55.46  ? 113  LYS C CE  1 
ATOM   4769  N NZ  . LYS C  1 113 ? 47.018  26.953 81.541  1.00 54.36  ? 113  LYS C NZ  1 
ATOM   4770  N N   . ILE C  1 114 ? 52.620  31.340 82.960  1.00 56.91  ? 114  ILE C N   1 
ATOM   4771  C CA  . ILE C  1 114 ? 53.601  31.405 84.050  1.00 58.93  ? 114  ILE C CA  1 
ATOM   4772  C C   . ILE C  1 114 ? 52.927  31.597 85.406  1.00 59.05  ? 114  ILE C C   1 
ATOM   4773  O O   . ILE C  1 114 ? 51.833  32.157 85.494  1.00 57.35  ? 114  ILE C O   1 
ATOM   4774  C CB  . ILE C  1 114 ? 54.634  32.538 83.860  1.00 59.20  ? 114  ILE C CB  1 
ATOM   4775  C CG1 . ILE C  1 114 ? 53.939  33.892 83.660  1.00 57.11  ? 114  ILE C CG1 1 
ATOM   4776  C CG2 . ILE C  1 114 ? 55.570  32.223 82.699  1.00 59.93  ? 114  ILE C CG2 1 
ATOM   4777  C CD1 . ILE C  1 114 ? 54.801  35.073 84.057  1.00 57.73  ? 114  ILE C CD1 1 
ATOM   4778  N N   . GLN C  1 115 ? 53.597  31.131 86.455  1.00 61.27  ? 115  GLN C N   1 
ATOM   4779  C CA  . GLN C  1 115 ? 53.105  31.269 87.823  1.00 61.86  ? 115  GLN C CA  1 
ATOM   4780  C C   . GLN C  1 115 ? 53.649  32.556 88.436  1.00 62.02  ? 115  GLN C C   1 
ATOM   4781  O O   . GLN C  1 115 ? 54.860  32.772 88.455  1.00 63.43  ? 115  GLN C O   1 
ATOM   4782  C CB  . GLN C  1 115 ? 53.510  30.046 88.659  1.00 64.46  ? 115  GLN C CB  1 
ATOM   4783  C CG  . GLN C  1 115 ? 53.647  30.299 90.154  1.00 66.09  ? 115  GLN C CG  1 
ATOM   4784  C CD  . GLN C  1 115 ? 53.771  29.015 90.953  1.00 68.64  ? 115  GLN C CD  1 
ATOM   4785  O OE1 . GLN C  1 115 ? 52.949  28.108 90.821  1.00 68.47  ? 115  GLN C OE1 1 
ATOM   4786  N NE2 . GLN C  1 115 ? 54.794  28.935 91.795  1.00 71.19  ? 115  GLN C NE2 1 
ATOM   4787  N N   . ILE C  1 116 ? 52.749  33.401 88.936  1.00 60.72  ? 116  ILE C N   1 
ATOM   4788  C CA  . ILE C  1 116 ? 53.145  34.645 89.607  1.00 60.96  ? 116  ILE C CA  1 
ATOM   4789  C C   . ILE C  1 116 ? 52.940  34.561 91.126  1.00 62.53  ? 116  ILE C C   1 
ATOM   4790  O O   . ILE C  1 116 ? 53.787  35.026 91.894  1.00 64.13  ? 116  ILE C O   1 
ATOM   4791  C CB  . ILE C  1 116 ? 52.436  35.894 89.016  1.00 58.57  ? 116  ILE C CB  1 
ATOM   4792  C CG1 . ILE C  1 116 ? 50.940  35.646 88.792  1.00 56.80  ? 116  ILE C CG1 1 
ATOM   4793  C CG2 . ILE C  1 116 ? 53.091  36.295 87.700  1.00 57.82  ? 116  ILE C CG2 1 
ATOM   4794  C CD1 . ILE C  1 116 ? 50.140  36.913 88.589  1.00 54.93  ? 116  ILE C CD1 1 
ATOM   4795  N N   . ILE C  1 117 ? 51.826  33.966 91.551  1.00 62.24  ? 117  ILE C N   1 
ATOM   4796  C CA  . ILE C  1 117 ? 51.571  33.680 92.966  1.00 64.02  ? 117  ILE C CA  1 
ATOM   4797  C C   . ILE C  1 117 ? 51.515  32.160 93.140  1.00 65.63  ? 117  ILE C C   1 
ATOM   4798  O O   . ILE C  1 117 ? 50.609  31.514 92.607  1.00 64.57  ? 117  ILE C O   1 
ATOM   4799  C CB  . ILE C  1 117 ? 50.240  34.307 93.448  1.00 62.67  ? 117  ILE C CB  1 
ATOM   4800  C CG1 . ILE C  1 117 ? 50.407  35.808 93.726  1.00 62.01  ? 117  ILE C CG1 1 
ATOM   4801  C CG2 . ILE C  1 117 ? 49.717  33.617 94.708  1.00 64.49  ? 117  ILE C CG2 1 
ATOM   4802  C CD1 . ILE C  1 117 ? 50.599  36.662 92.494  1.00 59.99  ? 117  ILE C CD1 1 
ATOM   4803  N N   . PRO C  1 118 ? 52.487  31.579 93.869  1.00 68.38  ? 118  PRO C N   1 
ATOM   4804  C CA  . PRO C  1 118 ? 52.396  30.147 94.168  1.00 70.25  ? 118  PRO C CA  1 
ATOM   4805  C C   . PRO C  1 118 ? 51.223  29.822 95.100  1.00 70.68  ? 118  PRO C C   1 
ATOM   4806  O O   . PRO C  1 118 ? 50.903  30.607 95.997  1.00 70.83  ? 118  PRO C O   1 
ATOM   4807  C CB  . PRO C  1 118 ? 53.741  29.829 94.842  1.00 73.30  ? 118  PRO C CB  1 
ATOM   4808  C CG  . PRO C  1 118 ? 54.648  30.963 94.493  1.00 72.70  ? 118  PRO C CG  1 
ATOM   4809  C CD  . PRO C  1 118 ? 53.766  32.160 94.319  1.00 70.03  ? 118  PRO C CD  1 
ATOM   4810  N N   . LYS C  1 119 ? 50.590  28.675 94.877  1.00 71.02  ? 119  LYS C N   1 
ATOM   4811  C CA  . LYS C  1 119 ? 49.459  28.240 95.698  1.00 71.67  ? 119  LYS C CA  1 
ATOM   4812  C C   . LYS C  1 119 ? 49.907  27.915 97.126  1.00 74.91  ? 119  LYS C C   1 
ATOM   4813  O O   . LYS C  1 119 ? 49.177  28.160 98.091  1.00 75.54  ? 119  LYS C O   1 
ATOM   4814  C CB  . LYS C  1 119 ? 48.789  27.021 95.060  1.00 71.55  ? 119  LYS C CB  1 
ATOM   4815  C CG  . LYS C  1 119 ? 47.412  26.700 95.611  1.00 71.58  ? 119  LYS C CG  1 
ATOM   4816  C CD  . LYS C  1 119 ? 46.759  25.594 94.799  1.00 71.24  ? 119  LYS C CD  1 
ATOM   4817  C CE  . LYS C  1 119 ? 45.566  24.991 95.522  1.00 72.30  ? 119  LYS C CE  1 
ATOM   4818  N NZ  . LYS C  1 119 ? 45.089  23.751 94.848  1.00 72.66  ? 119  LYS C NZ  1 
ATOM   4819  N N   . SER C  1 120 ? 51.111  27.356 97.245  1.00 77.17  ? 120  SER C N   1 
ATOM   4820  C CA  . SER C  1 120 ? 51.732  27.086 98.542  1.00 80.51  ? 120  SER C CA  1 
ATOM   4821  C C   . SER C  1 120 ? 51.978  28.373 99.326  1.00 80.49  ? 120  SER C C   1 
ATOM   4822  O O   . SER C  1 120 ? 51.833  28.393 100.544 1.00 82.56  ? 120  SER C O   1 
ATOM   4823  C CB  . SER C  1 120 ? 53.068  26.367 98.344  1.00 82.77  ? 120  SER C CB  1 
ATOM   4824  O OG  . SER C  1 120 ? 53.961  27.166 97.584  1.00 81.47  ? 120  SER C OG  1 
ATOM   4825  N N   . SER C  1 121 ? 52.341  29.440 98.613  1.00 78.32  ? 121  SER C N   1 
ATOM   4826  C CA  . SER C  1 121 ? 52.741  30.713 99.235  1.00 78.39  ? 121  SER C CA  1 
ATOM   4827  C C   . SER C  1 121 ? 51.706  31.344 100.177 1.00 78.12  ? 121  SER C C   1 
ATOM   4828  O O   . SER C  1 121 ? 52.051  32.236 100.953 1.00 78.94  ? 121  SER C O   1 
ATOM   4829  C CB  . SER C  1 121 ? 53.150  31.746 98.169  1.00 75.90  ? 121  SER C CB  1 
ATOM   4830  O OG  . SER C  1 121 ? 54.399  31.420 97.589  1.00 76.92  ? 121  SER C OG  1 
ATOM   4831  N N   . TRP C  1 122 ? 50.453  30.899 100.106 1.00 77.13  ? 122  TRP C N   1 
ATOM   4832  C CA  . TRP C  1 122 ? 49.420  31.373 101.024 1.00 77.24  ? 122  TRP C CA  1 
ATOM   4833  C C   . TRP C  1 122 ? 49.542  30.656 102.365 1.00 80.84  ? 122  TRP C C   1 
ATOM   4834  O O   . TRP C  1 122 ? 48.756  29.762 102.678 1.00 81.83  ? 122  TRP C O   1 
ATOM   4835  C CB  . TRP C  1 122 ? 48.034  31.165 100.419 1.00 75.04  ? 122  TRP C CB  1 
ATOM   4836  C CG  . TRP C  1 122 ? 47.846  31.945 99.164  1.00 71.76  ? 122  TRP C CG  1 
ATOM   4837  C CD1 . TRP C  1 122 ? 47.894  31.468 97.889  1.00 70.12  ? 122  TRP C CD1 1 
ATOM   4838  C CD2 . TRP C  1 122 ? 47.609  33.353 99.059  1.00 69.93  ? 122  TRP C CD2 1 
ATOM   4839  N NE1 . TRP C  1 122 ? 47.686  32.489 96.994  1.00 67.42  ? 122  TRP C NE1 1 
ATOM   4840  C CE2 . TRP C  1 122 ? 47.509  33.658 97.685  1.00 67.24  ? 122  TRP C CE2 1 
ATOM   4841  C CE3 . TRP C  1 122 ? 47.462  34.386 99.994  1.00 70.45  ? 122  TRP C CE3 1 
ATOM   4842  C CZ2 . TRP C  1 122 ? 47.270  34.955 97.220  1.00 65.13  ? 122  TRP C CZ2 1 
ATOM   4843  C CZ3 . TRP C  1 122 ? 47.226  35.675 99.532  1.00 68.31  ? 122  TRP C CZ3 1 
ATOM   4844  C CH2 . TRP C  1 122 ? 47.130  35.947 98.155  1.00 65.70  ? 122  TRP C CH2 1 
ATOM   4845  N N   . SER C  1 123 ? 50.540  31.062 103.149 1.00 82.98  ? 123  SER C N   1 
ATOM   4846  C CA  . SER C  1 123 ? 50.849  30.421 104.428 1.00 86.76  ? 123  SER C CA  1 
ATOM   4847  C C   . SER C  1 123 ? 49.907  30.867 105.546 1.00 87.63  ? 123  SER C C   1 
ATOM   4848  O O   . SER C  1 123 ? 49.697  30.128 106.510 1.00 90.53  ? 123  SER C O   1 
ATOM   4849  C CB  . SER C  1 123 ? 52.299  30.711 104.829 1.00 88.89  ? 123  SER C CB  1 
ATOM   4850  O OG  . SER C  1 123 ? 52.530  32.103 104.952 1.00 87.73  ? 123  SER C OG  1 
ATOM   4851  N N   . SER C  1 124 ? 49.356  32.074 105.413 1.00 85.35  ? 124  SER C N   1 
ATOM   4852  C CA  . SER C  1 124 ? 48.441  32.648 106.403 1.00 86.00  ? 124  SER C CA  1 
ATOM   4853  C C   . SER C  1 124 ? 46.957  32.421 106.060 1.00 84.26  ? 124  SER C C   1 
ATOM   4854  O O   . SER C  1 124 ? 46.074  32.832 106.815 1.00 84.76  ? 124  SER C O   1 
ATOM   4855  C CB  . SER C  1 124 ? 48.724  34.148 106.545 1.00 84.90  ? 124  SER C CB  1 
ATOM   4856  O OG  . SER C  1 124 ? 47.860  34.753 107.489 1.00 85.61  ? 124  SER C OG  1 
ATOM   4857  N N   . HIS C  1 125 ? 46.689  31.771 104.927 1.00 82.42  ? 125  HIS C N   1 
ATOM   4858  C CA  . HIS C  1 125 ? 45.319  31.494 104.479 1.00 80.81  ? 125  HIS C CA  1 
ATOM   4859  C C   . HIS C  1 125 ? 45.188  30.055 103.989 1.00 81.51  ? 125  HIS C C   1 
ATOM   4860  O O   . HIS C  1 125 ? 46.176  29.436 103.588 1.00 82.21  ? 125  HIS C O   1 
ATOM   4861  C CB  . HIS C  1 125 ? 44.924  32.447 103.346 1.00 77.08  ? 125  HIS C CB  1 
ATOM   4862  C CG  . HIS C  1 125 ? 44.820  33.880 103.766 1.00 76.33  ? 125  HIS C CG  1 
ATOM   4863  N ND1 . HIS C  1 125 ? 45.873  34.764 103.666 1.00 75.97  ? 125  HIS C ND1 1 
ATOM   4864  C CD2 . HIS C  1 125 ? 43.784  34.584 104.279 1.00 76.02  ? 125  HIS C CD2 1 
ATOM   4865  C CE1 . HIS C  1 125 ? 45.492  35.950 104.105 1.00 75.48  ? 125  HIS C CE1 1 
ATOM   4866  N NE2 . HIS C  1 125 ? 44.227  35.869 104.481 1.00 75.49  ? 125  HIS C NE2 1 
ATOM   4867  N N   . GLU C  1 126 ? 43.968  29.524 104.030 1.00 81.52  ? 126  GLU C N   1 
ATOM   4868  C CA  . GLU C  1 126 ? 43.696  28.191 103.497 1.00 82.04  ? 126  GLU C CA  1 
ATOM   4869  C C   . GLU C  1 126 ? 43.411  28.305 102.003 1.00 78.70  ? 126  GLU C C   1 
ATOM   4870  O O   . GLU C  1 126 ? 42.570  29.107 101.593 1.00 76.48  ? 126  GLU C O   1 
ATOM   4871  C CB  . GLU C  1 126 ? 42.511  27.555 104.223 1.00 83.79  ? 126  GLU C CB  1 
ATOM   4872  C CG  . GLU C  1 126 ? 42.186  26.137 103.776 1.00 84.71  ? 126  GLU C CG  1 
ATOM   4873  C CD  . GLU C  1 126 ? 43.340  25.169 103.988 1.00 87.29  ? 126  GLU C CD  1 
ATOM   4874  O OE1 . GLU C  1 126 ? 43.714  24.924 105.160 1.00 90.47  ? 126  GLU C OE1 1 
ATOM   4875  O OE2 . GLU C  1 126 ? 43.863  24.646 102.977 1.00 86.26  ? 126  GLU C OE2 1 
ATOM   4876  N N   . ALA C  1 127 ? 44.110  27.505 101.197 1.00 78.62  ? 127  ALA C N   1 
ATOM   4877  C CA  . ALA C  1 127 ? 44.060  27.628 99.732  1.00 75.59  ? 127  ALA C CA  1 
ATOM   4878  C C   . ALA C  1 127 ? 43.599  26.370 98.984  1.00 75.64  ? 127  ALA C C   1 
ATOM   4879  O O   . ALA C  1 127 ? 43.279  26.450 97.795  1.00 73.19  ? 127  ALA C O   1 
ATOM   4880  C CB  . ALA C  1 127 ? 45.425  28.061 99.211  1.00 74.98  ? 127  ALA C CB  1 
ATOM   4881  N N   . SER C  1 128 ? 43.556  25.225 99.666  1.00 78.50  ? 128  SER C N   1 
ATOM   4882  C CA  . SER C  1 128 ? 43.307  23.935 99.007  1.00 79.02  ? 128  SER C CA  1 
ATOM   4883  C C   . SER C  1 128 ? 41.881  23.399 99.187  1.00 79.37  ? 128  SER C C   1 
ATOM   4884  O O   . SER C  1 128 ? 41.563  22.312 98.700  1.00 80.01  ? 128  SER C O   1 
ATOM   4885  C CB  . SER C  1 128 ? 44.330  22.897 99.485  1.00 82.23  ? 128  SER C CB  1 
ATOM   4886  O OG  . SER C  1 128 ? 45.576  23.093 98.838  1.00 81.57  ? 128  SER C OG  1 
ATOM   4887  N N   . LEU C  1 129 ? 41.028  24.155 99.875  1.00 79.07  ? 129  LEU C N   1 
ATOM   4888  C CA  . LEU C  1 129 ? 39.622  23.782 100.034 1.00 79.38  ? 129  LEU C CA  1 
ATOM   4889  C C   . LEU C  1 129 ? 38.703  24.782 99.326  1.00 76.21  ? 129  LEU C C   1 
ATOM   4890  O O   . LEU C  1 129 ? 37.536  24.929 99.687  1.00 76.48  ? 129  LEU C O   1 
ATOM   4891  C CB  . LEU C  1 129 ? 39.261  23.667 101.521 1.00 82.42  ? 129  LEU C CB  1 
ATOM   4892  C CG  . LEU C  1 129 ? 39.885  22.491 102.282 1.00 86.12  ? 129  LEU C CG  1 
ATOM   4893  C CD1 . LEU C  1 129 ? 41.278  22.826 102.789 1.00 87.23  ? 129  LEU C CD1 1 
ATOM   4894  C CD2 . LEU C  1 129 ? 38.999  22.090 103.450 1.00 89.02  ? 129  LEU C CD2 1 
ATOM   4895  N N   . GLY C  1 130 ? 39.232  25.458 98.309  1.00 73.49  ? 130  GLY C N   1 
ATOM   4896  C CA  . GLY C  1 130 ? 38.456  26.405 97.515  1.00 70.50  ? 130  GLY C CA  1 
ATOM   4897  C C   . GLY C  1 130 ? 37.870  25.764 96.269  1.00 69.06  ? 130  GLY C C   1 
ATOM   4898  O O   . GLY C  1 130 ? 38.228  26.129 95.142  1.00 66.78  ? 130  GLY C O   1 
ATOM   4899  N N   . VAL C  1 131 ? 36.960  24.812 96.477  1.00 70.53  ? 131  VAL C N   1 
ATOM   4900  C CA  . VAL C  1 131 ? 36.356  24.042 95.383  1.00 69.67  ? 131  VAL C CA  1 
ATOM   4901  C C   . VAL C  1 131 ? 34.827  24.071 95.439  1.00 69.57  ? 131  VAL C C   1 
ATOM   4902  O O   . VAL C  1 131 ? 34.236  24.532 96.416  1.00 70.64  ? 131  VAL C O   1 
ATOM   4903  C CB  . VAL C  1 131 ? 36.836  22.568 95.388  1.00 71.93  ? 131  VAL C CB  1 
ATOM   4904  C CG1 . VAL C  1 131 ? 38.359  22.500 95.359  1.00 72.33  ? 131  VAL C CG1 1 
ATOM   4905  C CG2 . VAL C  1 131 ? 36.285  21.807 96.591  1.00 75.11  ? 131  VAL C CG2 1 
ATOM   4906  N N   . SER C  1 132 ? 34.201  23.575 94.374  1.00 68.49  ? 132  SER C N   1 
ATOM   4907  C CA  . SER C  1 132 ? 32.744  23.473 94.286  1.00 68.53  ? 132  SER C CA  1 
ATOM   4908  C C   . SER C  1 132 ? 32.342  22.263 93.451  1.00 69.01  ? 132  SER C C   1 
ATOM   4909  O O   . SER C  1 132 ? 33.128  21.768 92.638  1.00 68.42  ? 132  SER C O   1 
ATOM   4910  C CB  . SER C  1 132 ? 32.151  24.744 93.667  1.00 65.84  ? 132  SER C CB  1 
ATOM   4911  O OG  . SER C  1 132 ? 30.792  24.558 93.293  1.00 65.76  ? 132  SER C OG  1 
ATOM   4912  N N   . SER C  1 133 ? 31.110  21.801 93.650  1.00 70.18  ? 133  SER C N   1 
ATOM   4913  C CA  . SER C  1 133 ? 30.557  20.696 92.872  1.00 70.73  ? 133  SER C CA  1 
ATOM   4914  C C   . SER C  1 133 ? 30.236  21.110 91.430  1.00 67.95  ? 133  SER C C   1 
ATOM   4915  O O   . SER C  1 133 ? 30.097  20.253 90.555  1.00 68.05  ? 133  SER C O   1 
ATOM   4916  C CB  . SER C  1 133 ? 29.294  20.160 93.545  1.00 73.00  ? 133  SER C CB  1 
ATOM   4917  O OG  . SER C  1 133 ? 28.313  21.177 93.651  1.00 71.91  ? 133  SER C OG  1 
ATOM   4918  N N   . ALA C  1 134 ? 30.117  22.417 91.189  1.00 65.63  ? 134  ALA C N   1 
ATOM   4919  C CA  . ALA C  1 134 ? 29.827  22.944 89.851  1.00 63.07  ? 134  ALA C CA  1 
ATOM   4920  C C   . ALA C  1 134 ? 30.976  22.721 88.859  1.00 61.76  ? 134  ALA C C   1 
ATOM   4921  O O   . ALA C  1 134 ? 30.731  22.562 87.665  1.00 60.56  ? 134  ALA C O   1 
ATOM   4922  C CB  . ALA C  1 134 ? 29.474  24.422 89.930  1.00 61.30  ? 134  ALA C CB  1 
ATOM   4923  N N   . CYS C  1 135 ? 32.217  22.715 89.354  1.00 62.14  ? 135  CYS C N   1 
ATOM   4924  C CA  . CYS C  1 135 ? 33.390  22.353 88.547  1.00 61.49  ? 135  CYS C CA  1 
ATOM   4925  C C   . CYS C  1 135 ? 33.968  21.009 89.020  1.00 63.96  ? 135  CYS C C   1 
ATOM   4926  O O   . CYS C  1 135 ? 34.865  20.990 89.863  1.00 65.08  ? 135  CYS C O   1 
ATOM   4927  C CB  . CYS C  1 135 ? 34.480  23.435 88.634  1.00 60.12  ? 135  CYS C CB  1 
ATOM   4928  S SG  . CYS C  1 135 ? 33.922  25.151 88.508  1.00 57.81  ? 135  CYS C SG  1 
ATOM   4929  N N   . PRO C  1 136 ? 33.450  19.880 88.492  1.00 64.94  ? 136  PRO C N   1 
ATOM   4930  C CA  . PRO C  1 136 ? 33.970  18.563 88.863  1.00 67.50  ? 136  PRO C CA  1 
ATOM   4931  C C   . PRO C  1 136 ? 35.087  18.042 87.948  1.00 67.18  ? 136  PRO C C   1 
ATOM   4932  O O   . PRO C  1 136 ? 35.018  18.218 86.731  1.00 65.37  ? 136  PRO C O   1 
ATOM   4933  C CB  . PRO C  1 136 ? 32.737  17.670 88.735  1.00 68.88  ? 136  PRO C CB  1 
ATOM   4934  C CG  . PRO C  1 136 ? 31.971  18.284 87.615  1.00 66.48  ? 136  PRO C CG  1 
ATOM   4935  C CD  . PRO C  1 136 ? 32.195  19.766 87.723  1.00 64.22  ? 136  PRO C CD  1 
ATOM   4936  N N   . TYR C  1 137 ? 36.091  17.396 88.545  1.00 69.14  ? 137  TYR C N   1 
ATOM   4937  C CA  . TYR C  1 137 ? 37.180  16.744 87.806  1.00 69.49  ? 137  TYR C CA  1 
ATOM   4938  C C   . TYR C  1 137 ? 37.415  15.329 88.346  1.00 72.77  ? 137  TYR C C   1 
ATOM   4939  O O   . TYR C  1 137 ? 37.716  15.154 89.528  1.00 74.82  ? 137  TYR C O   1 
ATOM   4940  C CB  . TYR C  1 137 ? 38.468  17.570 87.917  1.00 68.55  ? 137  TYR C CB  1 
ATOM   4941  C CG  . TYR C  1 137 ? 39.709  16.901 87.347  1.00 69.46  ? 137  TYR C CG  1 
ATOM   4942  C CD1 . TYR C  1 137 ? 39.833  16.658 85.977  1.00 68.27  ? 137  TYR C CD1 1 
ATOM   4943  C CD2 . TYR C  1 137 ? 40.771  16.527 88.179  1.00 71.66  ? 137  TYR C CD2 1 
ATOM   4944  C CE1 . TYR C  1 137 ? 40.970  16.054 85.455  1.00 69.26  ? 137  TYR C CE1 1 
ATOM   4945  C CE2 . TYR C  1 137 ? 41.911  15.926 87.664  1.00 72.68  ? 137  TYR C CE2 1 
ATOM   4946  C CZ  . TYR C  1 137 ? 42.007  15.693 86.302  1.00 71.46  ? 137  TYR C CZ  1 
ATOM   4947  O OH  . TYR C  1 137 ? 43.137  15.096 85.794  1.00 72.65  ? 137  TYR C OH  1 
ATOM   4948  N N   . GLN C  1 138 ? 37.276  14.332 87.471  1.00 73.39  ? 138  GLN C N   1 
ATOM   4949  C CA  . GLN C  1 138 ? 37.435  12.918 87.833  1.00 76.65  ? 138  GLN C CA  1 
ATOM   4950  C C   . GLN C  1 138 ? 36.578  12.509 89.033  1.00 78.92  ? 138  GLN C C   1 
ATOM   4951  O O   . GLN C  1 138 ? 37.019  11.735 89.888  1.00 81.89  ? 138  GLN C O   1 
ATOM   4952  C CB  . GLN C  1 138 ? 38.908  12.587 88.100  1.00 78.15  ? 138  GLN C CB  1 
ATOM   4953  C CG  . GLN C  1 138 ? 39.845  13.024 86.986  1.00 76.16  ? 138  GLN C CG  1 
ATOM   4954  C CD  . GLN C  1 138 ? 41.173  12.284 86.997  1.00 78.31  ? 138  GLN C CD  1 
ATOM   4955  O OE1 . GLN C  1 138 ? 41.668  11.884 88.051  1.00 80.81  ? 138  GLN C OE1 1 
ATOM   4956  N NE2 . GLN C  1 138 ? 41.760  12.103 85.818  1.00 77.51  ? 138  GLN C NE2 1 
ATOM   4957  N N   . GLY C  1 139 ? 35.359  13.043 89.096  1.00 77.67  ? 139  GLY C N   1 
ATOM   4958  C CA  . GLY C  1 139 ? 34.402  12.692 90.148  1.00 79.80  ? 139  GLY C CA  1 
ATOM   4959  C C   . GLY C  1 139 ? 34.434  13.582 91.379  1.00 79.84  ? 139  GLY C C   1 
ATOM   4960  O O   . GLY C  1 139 ? 33.431  13.696 92.084  1.00 80.70  ? 139  GLY C O   1 
ATOM   4961  N N   . LYS C  1 140 ? 35.579  14.211 91.641  1.00 79.07  ? 140  LYS C N   1 
ATOM   4962  C CA  . LYS C  1 140 ? 35.740  15.074 92.811  1.00 79.25  ? 140  LYS C CA  1 
ATOM   4963  C C   . LYS C  1 140 ? 35.490  16.536 92.456  1.00 75.84  ? 140  LYS C C   1 
ATOM   4964  O O   . LYS C  1 140 ? 35.625  16.938 91.301  1.00 73.31  ? 140  LYS C O   1 
ATOM   4965  C CB  . LYS C  1 140 ? 37.140  14.916 93.421  1.00 80.82  ? 140  LYS C CB  1 
ATOM   4966  C CG  . LYS C  1 140 ? 37.400  13.554 94.052  1.00 84.72  ? 140  LYS C CG  1 
ATOM   4967  C CD  . LYS C  1 140 ? 38.172  12.625 93.122  1.00 85.29  ? 140  LYS C CD  1 
ATOM   4968  C CE  . LYS C  1 140 ? 38.019  11.161 93.516  1.00 89.09  ? 140  LYS C CE  1 
ATOM   4969  N NZ  . LYS C  1 140 ? 38.575  10.845 94.863  1.00 92.39  ? 140  LYS C NZ  1 
ATOM   4970  N N   . SER C  1 141 ? 35.119  17.319 93.466  1.00 75.99  ? 141  SER C N   1 
ATOM   4971  C CA  . SER C  1 141 ? 34.895  18.755 93.311  1.00 73.15  ? 141  SER C CA  1 
ATOM   4972  C C   . SER C  1 141 ? 36.223  19.474 93.070  1.00 71.68  ? 141  SER C C   1 
ATOM   4973  O O   . SER C  1 141 ? 37.200  19.243 93.783  1.00 73.41  ? 141  SER C O   1 
ATOM   4974  C CB  . SER C  1 141 ? 34.203  19.323 94.554  1.00 74.19  ? 141  SER C CB  1 
ATOM   4975  O OG  . SER C  1 141 ? 32.882  18.823 94.674  1.00 75.29  ? 141  SER C OG  1 
ATOM   4976  N N   . SER C  1 142 ? 36.244  20.344 92.062  1.00 68.68  ? 142  SER C N   1 
ATOM   4977  C CA  . SER C  1 142 ? 37.458  21.039 91.636  1.00 67.15  ? 142  SER C CA  1 
ATOM   4978  C C   . SER C  1 142 ? 37.142  22.516 91.384  1.00 64.46  ? 142  SER C C   1 
ATOM   4979  O O   . SER C  1 142 ? 36.092  23.007 91.807  1.00 64.17  ? 142  SER C O   1 
ATOM   4980  C CB  . SER C  1 142 ? 38.012  20.370 90.371  1.00 66.54  ? 142  SER C CB  1 
ATOM   4981  O OG  . SER C  1 142 ? 39.224  20.967 89.950  1.00 65.40  ? 142  SER C OG  1 
ATOM   4982  N N   . PHE C  1 143 ? 38.047  23.223 90.710  1.00 62.69  ? 143  PHE C N   1 
ATOM   4983  C CA  . PHE C  1 143 ? 37.845  24.643 90.405  1.00 60.27  ? 143  PHE C CA  1 
ATOM   4984  C C   . PHE C  1 143 ? 38.709  25.098 89.220  1.00 58.41  ? 143  PHE C C   1 
ATOM   4985  O O   . PHE C  1 143 ? 39.578  24.357 88.752  1.00 59.11  ? 143  PHE C O   1 
ATOM   4986  C CB  . PHE C  1 143 ? 38.153  25.492 91.649  1.00 60.91  ? 143  PHE C CB  1 
ATOM   4987  C CG  . PHE C  1 143 ? 37.502  26.852 91.643  1.00 59.03  ? 143  PHE C CG  1 
ATOM   4988  C CD1 . PHE C  1 143 ? 36.117  26.976 91.701  1.00 58.73  ? 143  PHE C CD1 1 
ATOM   4989  C CD2 . PHE C  1 143 ? 38.273  28.009 91.587  1.00 57.76  ? 143  PHE C CD2 1 
ATOM   4990  C CE1 . PHE C  1 143 ? 35.513  28.226 91.697  1.00 57.23  ? 143  PHE C CE1 1 
ATOM   4991  C CE2 . PHE C  1 143 ? 37.675  29.261 91.584  1.00 56.24  ? 143  PHE C CE2 1 
ATOM   4992  C CZ  . PHE C  1 143 ? 36.292  29.370 91.641  1.00 55.98  ? 143  PHE C CZ  1 
ATOM   4993  N N   . PHE C  1 144 ? 38.442  26.308 88.730  1.00 56.22  ? 144  PHE C N   1 
ATOM   4994  C CA  . PHE C  1 144 ? 39.292  26.965 87.735  1.00 54.56  ? 144  PHE C CA  1 
ATOM   4995  C C   . PHE C  1 144 ? 40.763  26.880 88.156  1.00 55.69  ? 144  PHE C C   1 
ATOM   4996  O O   . PHE C  1 144 ? 41.160  27.481 89.150  1.00 56.32  ? 144  PHE C O   1 
ATOM   4997  C CB  . PHE C  1 144 ? 38.908  28.444 87.590  1.00 52.66  ? 144  PHE C CB  1 
ATOM   4998  C CG  . PHE C  1 144 ? 37.475  28.679 87.182  1.00 51.62  ? 144  PHE C CG  1 
ATOM   4999  C CD1 . PHE C  1 144 ? 37.035  28.359 85.903  1.00 50.56  ? 144  PHE C CD1 1 
ATOM   5000  C CD2 . PHE C  1 144 ? 36.568  29.242 88.077  1.00 51.85  ? 144  PHE C CD2 1 
ATOM   5001  C CE1 . PHE C  1 144 ? 35.718  28.588 85.531  1.00 49.80  ? 144  PHE C CE1 1 
ATOM   5002  C CE2 . PHE C  1 144 ? 35.252  29.473 87.710  1.00 51.10  ? 144  PHE C CE2 1 
ATOM   5003  C CZ  . PHE C  1 144 ? 34.826  29.144 86.437  1.00 50.08  ? 144  PHE C CZ  1 
ATOM   5004  N N   . ARG C  1 145 ? 41.563  26.140 87.394  1.00 56.10  ? 145  ARG C N   1 
ATOM   5005  C CA  . ARG C  1 145 ? 42.940  25.815 87.785  1.00 57.69  ? 145  ARG C CA  1 
ATOM   5006  C C   . ARG C  1 145 ? 43.906  26.996 87.865  1.00 56.99  ? 145  ARG C C   1 
ATOM   5007  O O   . ARG C  1 145 ? 44.940  26.898 88.523  1.00 58.57  ? 145  ARG C O   1 
ATOM   5008  C CB  . ARG C  1 145 ? 43.537  24.788 86.826  1.00 58.28  ? 145  ARG C CB  1 
ATOM   5009  C CG  . ARG C  1 145 ? 42.772  23.483 86.747  1.00 59.46  ? 145  ARG C CG  1 
ATOM   5010  C CD  . ARG C  1 145 ? 43.707  22.353 86.365  1.00 61.21  ? 145  ARG C CD  1 
ATOM   5011  N NE  . ARG C  1 145 ? 42.966  21.158 85.975  1.00 62.08  ? 145  ARG C NE  1 
ATOM   5012  C CZ  . ARG C  1 145 ? 42.623  20.163 86.792  1.00 64.33  ? 145  ARG C CZ  1 
ATOM   5013  N NH1 . ARG C  1 145 ? 42.943  20.182 88.085  1.00 66.04  ? 145  ARG C NH1 1 
ATOM   5014  N NH2 . ARG C  1 145 ? 41.949  19.132 86.307  1.00 65.03  ? 145  ARG C NH2 1 
ATOM   5015  N N   . ASN C  1 146 ? 43.589  28.094 87.188  1.00 54.88  ? 146  ASN C N   1 
ATOM   5016  C CA  . ASN C  1 146 ? 44.505  29.233 87.110  1.00 54.24  ? 146  ASN C CA  1 
ATOM   5017  C C   . ASN C  1 146 ? 44.359  30.227 88.257  1.00 54.38  ? 146  ASN C C   1 
ATOM   5018  O O   . ASN C  1 146 ? 45.228  31.080 88.450  1.00 54.36  ? 146  ASN C O   1 
ATOM   5019  C CB  . ASN C  1 146 ? 44.345  29.949 85.764  1.00 52.13  ? 146  ASN C CB  1 
ATOM   5020  C CG  . ASN C  1 146 ? 44.886  29.132 84.604  1.00 52.27  ? 146  ASN C CG  1 
ATOM   5021  O OD1 . ASN C  1 146 ? 45.930  28.487 84.722  1.00 53.83  ? 146  ASN C OD1 1 
ATOM   5022  N ND2 . ASN C  1 146 ? 44.180  29.153 83.476  1.00 50.84  ? 146  ASN C ND2 1 
ATOM   5023  N N   . VAL C  1 147 ? 43.275  30.109 89.021  1.00 54.71  ? 147  VAL C N   1 
ATOM   5024  C CA  . VAL C  1 147 ? 43.028  31.006 90.152  1.00 55.06  ? 147  VAL C CA  1 
ATOM   5025  C C   . VAL C  1 147 ? 42.733  30.239 91.446  1.00 57.29  ? 147  VAL C C   1 
ATOM   5026  O O   . VAL C  1 147 ? 42.192  29.133 91.414  1.00 58.14  ? 147  VAL C O   1 
ATOM   5027  C CB  . VAL C  1 147 ? 41.875  31.988 89.856  1.00 53.21  ? 147  VAL C CB  1 
ATOM   5028  C CG1 . VAL C  1 147 ? 42.309  33.024 88.828  1.00 51.41  ? 147  VAL C CG1 1 
ATOM   5029  C CG2 . VAL C  1 147 ? 40.620  31.253 89.387  1.00 52.78  ? 147  VAL C CG2 1 
ATOM   5030  N N   . VAL C  1 148 ? 43.092  30.843 92.577  1.00 58.41  ? 148  VAL C N   1 
ATOM   5031  C CA  . VAL C  1 148 ? 42.949  30.216 93.898  1.00 60.86  ? 148  VAL C CA  1 
ATOM   5032  C C   . VAL C  1 148 ? 41.768  30.820 94.667  1.00 60.78  ? 148  VAL C C   1 
ATOM   5033  O O   . VAL C  1 148 ? 41.745  32.024 94.936  1.00 59.95  ? 148  VAL C O   1 
ATOM   5034  C CB  . VAL C  1 148 ? 44.236  30.399 94.740  1.00 62.68  ? 148  VAL C CB  1 
ATOM   5035  C CG1 . VAL C  1 148 ? 44.160  29.592 96.032  1.00 65.54  ? 148  VAL C CG1 1 
ATOM   5036  C CG2 . VAL C  1 148 ? 45.470  30.000 93.942  1.00 62.77  ? 148  VAL C CG2 1 
ATOM   5037  N N   . TRP C  1 149 ? 40.791  29.983 95.019  1.00 61.81  ? 149  TRP C N   1 
ATOM   5038  C CA  . TRP C  1 149 ? 39.677  30.411 95.867  1.00 62.32  ? 149  TRP C CA  1 
ATOM   5039  C C   . TRP C  1 149 ? 40.115  30.333 97.339  1.00 64.96  ? 149  TRP C C   1 
ATOM   5040  O O   . TRP C  1 149 ? 40.169  29.250 97.928  1.00 67.21  ? 149  TRP C O   1 
ATOM   5041  C CB  . TRP C  1 149 ? 38.434  29.545 95.609  1.00 62.53  ? 149  TRP C CB  1 
ATOM   5042  C CG  . TRP C  1 149 ? 37.158  30.041 96.268  1.00 62.82  ? 149  TRP C CG  1 
ATOM   5043  C CD1 . TRP C  1 149 ? 37.026  31.092 97.138  1.00 63.12  ? 149  TRP C CD1 1 
ATOM   5044  C CD2 . TRP C  1 149 ? 35.843  29.481 96.124  1.00 63.09  ? 149  TRP C CD2 1 
ATOM   5045  N NE1 . TRP C  1 149 ? 35.715  31.227 97.526  1.00 63.51  ? 149  TRP C NE1 1 
ATOM   5046  C CE2 . TRP C  1 149 ? 34.968  30.251 96.922  1.00 63.52  ? 149  TRP C CE2 1 
ATOM   5047  C CE3 . TRP C  1 149 ? 35.318  28.408 95.393  1.00 63.14  ? 149  TRP C CE3 1 
ATOM   5048  C CZ2 . TRP C  1 149 ? 33.598  29.984 97.008  1.00 64.02  ? 149  TRP C CZ2 1 
ATOM   5049  C CZ3 . TRP C  1 149 ? 33.955  28.142 95.481  1.00 63.65  ? 149  TRP C CZ3 1 
ATOM   5050  C CH2 . TRP C  1 149 ? 33.113  28.928 96.284  1.00 64.08  ? 149  TRP C CH2 1 
ATOM   5051  N N   . LEU C  1 150 ? 40.428  31.491 97.921  1.00 64.84  ? 150  LEU C N   1 
ATOM   5052  C CA  . LEU C  1 150 ? 40.978  31.565 99.276  1.00 67.34  ? 150  LEU C CA  1 
ATOM   5053  C C   . LEU C  1 150 ? 39.880  31.603 100.335 1.00 68.84  ? 150  LEU C C   1 
ATOM   5054  O O   . LEU C  1 150 ? 38.865  32.283 100.163 1.00 67.54  ? 150  LEU C O   1 
ATOM   5055  C CB  . LEU C  1 150 ? 41.873  32.803 99.431  1.00 66.72  ? 150  LEU C CB  1 
ATOM   5056  C CG  . LEU C  1 150 ? 43.185  32.831 98.637  1.00 65.98  ? 150  LEU C CG  1 
ATOM   5057  C CD1 . LEU C  1 150 ? 43.886  34.166 98.839  1.00 65.47  ? 150  LEU C CD1 1 
ATOM   5058  C CD2 . LEU C  1 150 ? 44.107  31.683 99.024  1.00 68.36  ? 150  LEU C CD2 1 
ATOM   5059  N N   . ILE C  1 151 ? 40.102  30.866 101.426 1.00 71.81  ? 151  ILE C N   1 
ATOM   5060  C CA  . ILE C  1 151 ? 39.206  30.867 102.590 1.00 73.82  ? 151  ILE C CA  1 
ATOM   5061  C C   . ILE C  1 151 ? 39.996  31.051 103.894 1.00 76.50  ? 151  ILE C C   1 
ATOM   5062  O O   . ILE C  1 151 ? 41.228  30.977 103.912 1.00 77.07  ? 151  ILE C O   1 
ATOM   5063  C CB  . ILE C  1 151 ? 38.350  29.575 102.664 1.00 75.30  ? 151  ILE C CB  1 
ATOM   5064  C CG1 . ILE C  1 151 ? 39.219  28.358 103.012 1.00 77.81  ? 151  ILE C CG1 1 
ATOM   5065  C CG2 . ILE C  1 151 ? 37.596  29.366 101.354 1.00 72.78  ? 151  ILE C CG2 1 
ATOM   5066  C CD1 . ILE C  1 151 ? 38.504  27.025 102.935 1.00 79.25  ? 151  ILE C CD1 1 
ATOM   5067  N N   . LYS C  1 152 ? 39.264  31.293 104.977 1.00 78.29  ? 152  LYS C N   1 
ATOM   5068  C CA  . LYS C  1 152 ? 39.851  31.523 106.306 1.00 81.12  ? 152  LYS C CA  1 
ATOM   5069  C C   . LYS C  1 152 ? 40.565  30.290 106.875 1.00 84.17  ? 152  LYS C C   1 
ATOM   5070  O O   . LYS C  1 152 ? 40.161  29.155 106.610 1.00 84.88  ? 152  LYS C O   1 
ATOM   5071  C CB  . LYS C  1 152 ? 38.765  31.986 107.288 1.00 82.49  ? 152  LYS C CB  1 
ATOM   5072  C CG  . LYS C  1 152 ? 37.648  30.974 107.516 1.00 83.98  ? 152  LYS C CG  1 
ATOM   5073  C CD  . LYS C  1 152 ? 36.521  31.546 108.359 1.00 85.13  ? 152  LYS C CD  1 
ATOM   5074  C CE  . LYS C  1 152 ? 35.554  30.441 108.775 1.00 87.42  ? 152  LYS C CE  1 
ATOM   5075  N NZ  . LYS C  1 152 ? 34.394  30.891 109.588 1.00 88.85  ? 152  LYS C NZ  1 
ATOM   5076  N N   . LYS C  1 153 ? 41.621  30.528 107.656 1.00 86.11  ? 153  LYS C N   1 
ATOM   5077  C CA  . LYS C  1 153 ? 42.335  29.463 108.373 1.00 89.53  ? 153  LYS C CA  1 
ATOM   5078  C C   . LYS C  1 153 ? 42.091  29.604 109.877 1.00 92.87  ? 153  LYS C C   1 
ATOM   5079  O O   . LYS C  1 153 ? 42.391  30.645 110.464 1.00 93.09  ? 153  LYS C O   1 
ATOM   5080  C CB  . LYS C  1 153 ? 43.839  29.516 108.079 1.00 89.60  ? 153  LYS C CB  1 
ATOM   5081  C CG  . LYS C  1 153 ? 44.565  28.190 108.300 1.00 92.44  ? 153  LYS C CG  1 
ATOM   5082  C CD  . LYS C  1 153 ? 46.030  28.414 108.656 1.00 94.03  ? 153  LYS C CD  1 
ATOM   5083  C CE  . LYS C  1 153 ? 46.857  28.992 107.506 1.00 91.14  ? 153  LYS C CE  1 
ATOM   5084  N NZ  . LYS C  1 153 ? 46.746  28.243 106.222 1.00 89.14  ? 153  LYS C NZ  1 
ATOM   5085  N N   . ASN C  1 154 ? 41.553  28.548 110.486 1.00 95.62  ? 154  ASN C N   1 
ATOM   5086  C CA  . ASN C  1 154 ? 41.178  28.537 111.907 1.00 99.16  ? 154  ASN C CA  1 
ATOM   5087  C C   . ASN C  1 154 ? 40.322  29.743 112.319 1.00 98.19  ? 154  ASN C C   1 
ATOM   5088  O O   . ASN C  1 154 ? 40.631  30.445 113.285 1.00 99.91  ? 154  ASN C O   1 
ATOM   5089  C CB  . ASN C  1 154 ? 42.421  28.404 112.806 1.00 102.32 ? 154  ASN C CB  1 
ATOM   5090  C CG  . ASN C  1 154 ? 42.094  27.827 114.177 1.00 106.81 ? 154  ASN C CG  1 
ATOM   5091  O OD1 . ASN C  1 154 ? 41.207  26.983 114.311 1.00 108.11 ? 154  ASN C OD1 1 
ATOM   5092  N ND2 . ASN C  1 154 ? 42.814  28.276 115.202 1.00 109.39 ? 154  ASN C ND2 1 
ATOM   5093  N N   . SER C  1 155 ? 39.249  29.970 111.560 1.00 95.55  ? 155  SER C N   1 
ATOM   5094  C CA  . SER C  1 155 ? 38.246  31.000 111.859 1.00 94.72  ? 155  SER C CA  1 
ATOM   5095  C C   . SER C  1 155 ? 38.793  32.436 111.880 1.00 93.12  ? 155  SER C C   1 
ATOM   5096  O O   . SER C  1 155 ? 38.355  33.257 112.682 1.00 94.16  ? 155  SER C O   1 
ATOM   5097  C CB  . SER C  1 155 ? 37.516  30.671 113.174 1.00 98.48  ? 155  SER C CB  1 
ATOM   5098  O OG  . SER C  1 155 ? 36.626  29.584 112.998 1.00 99.36  ? 155  SER C OG  1 
ATOM   5099  N N   . THR C  1 156 ? 39.749  32.735 111.003 1.00 90.80  ? 156  THR C N   1 
ATOM   5100  C CA  . THR C  1 156 ? 40.255  34.102 110.842 1.00 89.01  ? 156  THR C CA  1 
ATOM   5101  C C   . THR C  1 156 ? 40.674  34.314 109.395 1.00 85.43  ? 156  THR C C   1 
ATOM   5102  O O   . THR C  1 156 ? 41.448  33.523 108.856 1.00 85.33  ? 156  THR C O   1 
ATOM   5103  C CB  . THR C  1 156 ? 41.491  34.405 111.726 1.00 91.35  ? 156  THR C CB  1 
ATOM   5104  O OG1 . THR C  1 156 ? 42.671  33.864 111.117 1.00 90.96  ? 156  THR C OG1 1 
ATOM   5105  C CG2 . THR C  1 156 ? 41.345  33.844 113.142 1.00 95.58  ? 156  THR C CG2 1 
ATOM   5106  N N   . TYR C  1 157 ? 40.162  35.370 108.767 1.00 82.73  ? 157  TYR C N   1 
ATOM   5107  C CA  . TYR C  1 157 ? 40.596  35.753 107.424 1.00 79.46  ? 157  TYR C CA  1 
ATOM   5108  C C   . TYR C  1 157 ? 41.355  37.081 107.499 1.00 78.75  ? 157  TYR C C   1 
ATOM   5109  O O   . TYR C  1 157 ? 40.756  38.154 107.381 1.00 77.35  ? 157  TYR C O   1 
ATOM   5110  C CB  . TYR C  1 157 ? 39.407  35.852 106.466 1.00 76.88  ? 157  TYR C CB  1 
ATOM   5111  C CG  . TYR C  1 157 ? 39.811  35.863 105.002 1.00 73.87  ? 157  TYR C CG  1 
ATOM   5112  C CD1 . TYR C  1 157 ? 40.117  34.681 104.332 1.00 73.67  ? 157  TYR C CD1 1 
ATOM   5113  C CD2 . TYR C  1 157 ? 39.889  37.055 104.292 1.00 71.44  ? 157  TYR C CD2 1 
ATOM   5114  C CE1 . TYR C  1 157 ? 40.487  34.688 102.997 1.00 71.12  ? 157  TYR C CE1 1 
ATOM   5115  C CE2 . TYR C  1 157 ? 40.257  37.075 102.953 1.00 68.91  ? 157  TYR C CE2 1 
ATOM   5116  C CZ  . TYR C  1 157 ? 40.554  35.889 102.306 1.00 68.74  ? 157  TYR C CZ  1 
ATOM   5117  O OH  . TYR C  1 157 ? 40.921  35.898 100.975 1.00 66.39  ? 157  TYR C OH  1 
ATOM   5118  N N   . PRO C  1 158 ? 42.682  37.011 107.716 1.00 79.94  ? 158  PRO C N   1 
ATOM   5119  C CA  . PRO C  1 158 ? 43.481  38.231 107.812 1.00 79.58  ? 158  PRO C CA  1 
ATOM   5120  C C   . PRO C  1 158 ? 43.629  38.931 106.467 1.00 76.25  ? 158  PRO C C   1 
ATOM   5121  O O   . PRO C  1 158 ? 43.467  38.306 105.417 1.00 74.41  ? 158  PRO C O   1 
ATOM   5122  C CB  . PRO C  1 158 ? 44.838  37.729 108.319 1.00 81.92  ? 158  PRO C CB  1 
ATOM   5123  C CG  . PRO C  1 158 ? 44.911  36.314 107.870 1.00 82.21  ? 158  PRO C CG  1 
ATOM   5124  C CD  . PRO C  1 158 ? 43.502  35.799 107.906 1.00 81.92  ? 158  PRO C CD  1 
ATOM   5125  N N   . THR C  1 159 ? 43.931  40.224 106.514 1.00 75.69  ? 159  THR C N   1 
ATOM   5126  C CA  . THR C  1 159 ? 44.055  41.031 105.308 1.00 72.84  ? 159  THR C CA  1 
ATOM   5127  C C   . THR C  1 159 ? 45.198  40.518 104.436 1.00 72.22  ? 159  THR C C   1 
ATOM   5128  O O   . THR C  1 159 ? 46.264  40.147 104.940 1.00 74.16  ? 159  THR C O   1 
ATOM   5129  C CB  . THR C  1 159 ? 44.287  42.521 105.641 1.00 72.81  ? 159  THR C CB  1 
ATOM   5130  O OG1 . THR C  1 159 ? 43.260  42.983 106.527 1.00 73.83  ? 159  THR C OG1 1 
ATOM   5131  C CG2 . THR C  1 159 ? 44.274  43.374 104.377 1.00 69.93  ? 159  THR C CG2 1 
ATOM   5132  N N   . ILE C  1 160 ? 44.945  40.490 103.128 1.00 69.70  ? 160  ILE C N   1 
ATOM   5133  C CA  . ILE C  1 160 ? 45.921  40.072 102.126 1.00 68.86  ? 160  ILE C CA  1 
ATOM   5134  C C   . ILE C  1 160 ? 46.539  41.315 101.499 1.00 67.64  ? 160  ILE C C   1 
ATOM   5135  O O   . ILE C  1 160 ? 45.813  42.214 101.086 1.00 65.98  ? 160  ILE C O   1 
ATOM   5136  C CB  . ILE C  1 160 ? 45.248  39.240 101.014 1.00 66.89  ? 160  ILE C CB  1 
ATOM   5137  C CG1 . ILE C  1 160 ? 44.731  37.915 101.583 1.00 68.44  ? 160  ILE C CG1 1 
ATOM   5138  C CG2 . ILE C  1 160 ? 46.220  38.988 99.866  1.00 65.75  ? 160  ILE C CG2 1 
ATOM   5139  C CD1 . ILE C  1 160 ? 43.724  37.206 100.704 1.00 66.75  ? 160  ILE C CD1 1 
ATOM   5140  N N   . LYS C  1 161 ? 47.869  41.364 101.435 1.00 68.73  ? 161  LYS C N   1 
ATOM   5141  C CA  . LYS C  1 161 ? 48.583  42.448 100.749 1.00 67.78  ? 161  LYS C CA  1 
ATOM   5142  C C   . LYS C  1 161 ? 49.677  41.858 99.863  1.00 67.77  ? 161  LYS C C   1 
ATOM   5143  O O   . LYS C  1 161 ? 50.810  41.672 100.303 1.00 69.69  ? 161  LYS C O   1 
ATOM   5144  C CB  . LYS C  1 161 ? 49.184  43.439 101.752 1.00 69.59  ? 161  LYS C CB  1 
ATOM   5145  C CG  . LYS C  1 161 ? 48.165  44.352 102.416 1.00 69.51  ? 161  LYS C CG  1 
ATOM   5146  C CD  . LYS C  1 161 ? 48.794  45.163 103.540 1.00 71.78  ? 161  LYS C CD  1 
ATOM   5147  C CE  . LYS C  1 161 ? 47.775  46.073 104.212 1.00 71.89  ? 161  LYS C CE  1 
ATOM   5148  N NZ  . LYS C  1 161 ? 48.276  46.639 105.497 1.00 74.57  ? 161  LYS C NZ  1 
ATOM   5149  N N   . ARG C  1 162 ? 49.325  41.578 98.610  1.00 65.84  ? 162  ARG C N   1 
ATOM   5150  C CA  . ARG C  1 162 ? 50.215  40.896 97.676  1.00 65.80  ? 162  ARG C CA  1 
ATOM   5151  C C   . ARG C  1 162 ? 50.503  41.771 96.452  1.00 64.19  ? 162  ARG C C   1 
ATOM   5152  O O   . ARG C  1 162 ? 49.602  42.408 95.905  1.00 62.31  ? 162  ARG C O   1 
ATOM   5153  C CB  . ARG C  1 162 ? 49.606  39.542 97.269  1.00 65.27  ? 162  ARG C CB  1 
ATOM   5154  C CG  . ARG C  1 162 ? 49.775  38.447 98.305  1.00 67.69  ? 162  ARG C CG  1 
ATOM   5155  C CD  . ARG C  1 162 ? 51.241  38.132 98.615  1.00 69.89  ? 162  ARG C CD  1 
ATOM   5156  N NE  . ARG C  1 162 ? 51.606  36.761 98.251  1.00 70.69  ? 162  ARG C NE  1 
ATOM   5157  C CZ  . ARG C  1 162 ? 51.198  35.684 98.916  1.00 72.15  ? 162  ARG C CZ  1 
ATOM   5158  N NH1 . ARG C  1 162 ? 50.400  35.806 99.974  1.00 72.99  ? 162  ARG C NH1 1 
ATOM   5159  N NH2 . ARG C  1 162 ? 51.575  34.479 98.516  1.00 72.93  ? 162  ARG C NH2 1 
ATOM   5160  N N   . SER C  1 163 ? 51.773  41.816 96.051  1.00 65.32  ? 163  SER C N   1 
ATOM   5161  C CA  . SER C  1 163 ? 52.218  42.605 94.905  1.00 64.27  ? 163  SER C CA  1 
ATOM   5162  C C   . SER C  1 163 ? 53.066  41.745 93.971  1.00 64.81  ? 163  SER C C   1 
ATOM   5163  O O   . SER C  1 163 ? 53.865  40.935 94.437  1.00 66.70  ? 163  SER C O   1 
ATOM   5164  C CB  . SER C  1 163 ? 53.035  43.809 95.381  1.00 65.39  ? 163  SER C CB  1 
ATOM   5165  O OG  . SER C  1 163 ? 53.533  44.566 94.289  1.00 64.41  ? 163  SER C OG  1 
ATOM   5166  N N   . TYR C  1 164 ? 52.883  41.915 92.659  1.00 63.52  ? 164  TYR C N   1 
ATOM   5167  C CA  . TYR C  1 164 ? 53.743  41.262 91.667  1.00 64.18  ? 164  TYR C CA  1 
ATOM   5168  C C   . TYR C  1 164 ? 54.332  42.254 90.661  1.00 64.17  ? 164  TYR C C   1 
ATOM   5169  O O   . TYR C  1 164 ? 53.596  42.994 90.007  1.00 62.31  ? 164  TYR C O   1 
ATOM   5170  C CB  . TYR C  1 164 ? 52.999  40.170 90.901  1.00 62.79  ? 164  TYR C CB  1 
ATOM   5171  C CG  . TYR C  1 164 ? 53.786  39.716 89.692  1.00 62.65  ? 164  TYR C CG  1 
ATOM   5172  C CD1 . TYR C  1 164 ? 54.924  38.923 89.838  1.00 64.61  ? 164  TYR C CD1 1 
ATOM   5173  C CD2 . TYR C  1 164 ? 53.427  40.121 88.407  1.00 60.75  ? 164  TYR C CD2 1 
ATOM   5174  C CE1 . TYR C  1 164 ? 55.664  38.521 88.736  1.00 64.70  ? 164  TYR C CE1 1 
ATOM   5175  C CE2 . TYR C  1 164 ? 54.161  39.726 87.299  1.00 60.82  ? 164  TYR C CE2 1 
ATOM   5176  C CZ  . TYR C  1 164 ? 55.276  38.926 87.466  1.00 62.78  ? 164  TYR C CZ  1 
ATOM   5177  O OH  . TYR C  1 164 ? 56.002  38.534 86.366  1.00 63.02  ? 164  TYR C OH  1 
ATOM   5178  N N   . ASN C  1 165 ? 55.658  42.224 90.524  1.00 66.72  ? 165  ASN C N   1 
ATOM   5179  C CA  . ASN C  1 165 ? 56.382  43.063 89.573  1.00 67.44  ? 165  ASN C CA  1 
ATOM   5180  C C   . ASN C  1 165 ? 56.615  42.321 88.259  1.00 66.21  ? 165  ASN C C   1 
ATOM   5181  O O   . ASN C  1 165 ? 57.200  41.238 88.254  1.00 67.39  ? 165  ASN C O   1 
ATOM   5182  C CB  . ASN C  1 165 ? 57.731  43.467 90.170  1.00 71.24  ? 165  ASN C CB  1 
ATOM   5183  C CG  . ASN C  1 165 ? 58.384  44.619 89.430  1.00 73.10  ? 165  ASN C CG  1 
ATOM   5184  O OD1 . ASN C  1 165 ? 58.006  44.953 88.308  1.00 71.45  ? 165  ASN C OD1 1 
ATOM   5185  N ND2 . ASN C  1 165 ? 59.376  45.233 90.064  1.00 77.45  ? 165  ASN C ND2 1 
ATOM   5186  N N   . ASN C  1 166 ? 56.177  42.911 87.148  1.00 63.88  ? 166  ASN C N   1 
ATOM   5187  C CA  . ASN C  1 166 ? 56.371  42.301 85.832  1.00 62.81  ? 166  ASN C CA  1 
ATOM   5188  C C   . ASN C  1 166 ? 57.798  42.510 85.319  1.00 64.13  ? 166  ASN C C   1 
ATOM   5189  O O   . ASN C  1 166 ? 58.087  43.494 84.632  1.00 63.83  ? 166  ASN C O   1 
ATOM   5190  C CB  . ASN C  1 166 ? 55.356  42.845 84.820  1.00 60.49  ? 166  ASN C CB  1 
ATOM   5191  C CG  . ASN C  1 166 ? 55.333  42.042 83.530  1.00 59.79  ? 166  ASN C CG  1 
ATOM   5192  O OD1 . ASN C  1 166 ? 55.888  40.945 83.457  1.00 60.72  ? 166  ASN C OD1 1 
ATOM   5193  N ND2 . ASN C  1 166 ? 54.683  42.586 82.505  1.00 58.24  ? 166  ASN C ND2 1 
ATOM   5194  N N   . THR C  1 167 ? 58.678  41.568 85.656  1.00 65.53  ? 167  THR C N   1 
ATOM   5195  C CA  . THR C  1 167 ? 60.086  41.625 85.251  1.00 67.23  ? 167  THR C CA  1 
ATOM   5196  C C   . THR C  1 167 ? 60.344  41.095 83.832  1.00 66.61  ? 167  THR C C   1 
ATOM   5197  O O   . THR C  1 167 ? 61.412  41.346 83.270  1.00 68.09  ? 167  THR C O   1 
ATOM   5198  C CB  . THR C  1 167 ? 60.985  40.848 86.231  1.00 69.72  ? 167  THR C CB  1 
ATOM   5199  O OG1 . THR C  1 167 ? 60.469  39.523 86.412  1.00 69.50  ? 167  THR C OG1 1 
ATOM   5200  C CG2 . THR C  1 167 ? 61.050  41.564 87.573  1.00 70.65  ? 167  THR C CG2 1 
ATOM   5201  N N   . ASN C  1 168 ? 59.382  40.367 83.259  1.00 64.50  ? 168  ASN C N   1 
ATOM   5202  C CA  . ASN C  1 168 ? 59.493  39.916 81.863  1.00 63.78  ? 168  ASN C CA  1 
ATOM   5203  C C   . ASN C  1 168 ? 59.372  41.128 80.954  1.00 62.50  ? 168  ASN C C   1 
ATOM   5204  O O   . ASN C  1 168 ? 58.679  42.083 81.299  1.00 61.31  ? 168  ASN C O   1 
ATOM   5205  C CB  . ASN C  1 168 ? 58.404  38.905 81.455  1.00 62.20  ? 168  ASN C CB  1 
ATOM   5206  C CG  . ASN C  1 168 ? 57.875  38.087 82.614  1.00 62.34  ? 168  ASN C CG  1 
ATOM   5207  O OD1 . ASN C  1 168 ? 58.304  36.953 82.831  1.00 63.76  ? 168  ASN C OD1 1 
ATOM   5208  N ND2 . ASN C  1 168 ? 56.919  38.648 83.352  1.00 61.08  ? 168  ASN C ND2 1 
ATOM   5209  N N   . GLN C  1 169 ? 60.025  41.090 79.795  1.00 62.79  ? 169  GLN C N   1 
ATOM   5210  C CA  . GLN C  1 169 ? 59.872  42.165 78.816  1.00 61.77  ? 169  GLN C CA  1 
ATOM   5211  C C   . GLN C  1 169 ? 58.702  41.860 77.857  1.00 59.47  ? 169  GLN C C   1 
ATOM   5212  O O   . GLN C  1 169 ? 58.854  41.852 76.635  1.00 59.48  ? 169  GLN C O   1 
ATOM   5213  C CB  . GLN C  1 169 ? 61.194  42.459 78.083  1.00 63.78  ? 169  GLN C CB  1 
ATOM   5214  C CG  . GLN C  1 169 ? 61.800  41.310 77.287  1.00 64.89  ? 169  GLN C CG  1 
ATOM   5215  C CD  . GLN C  1 169 ? 62.616  41.783 76.088  1.00 66.16  ? 169  GLN C CD  1 
ATOM   5216  O OE1 . GLN C  1 169 ? 62.318  42.811 75.473  1.00 65.43  ? 169  GLN C OE1 1 
ATOM   5217  N NE2 . GLN C  1 169 ? 63.648  41.021 75.742  1.00 68.23  ? 169  GLN C NE2 1 
ATOM   5218  N N   . GLU C  1 170 ? 57.533  41.614 78.450  1.00 57.57  ? 170  GLU C N   1 
ATOM   5219  C CA  . GLU C  1 170 ? 56.295  41.324 77.726  1.00 55.41  ? 170  GLU C CA  1 
ATOM   5220  C C   . GLU C  1 170 ? 55.113  41.947 78.460  1.00 53.66  ? 170  GLU C C   1 
ATOM   5221  O O   . GLU C  1 170 ? 55.194  42.235 79.657  1.00 54.05  ? 170  GLU C O   1 
ATOM   5222  C CB  . GLU C  1 170 ? 56.051  39.810 77.622  1.00 55.33  ? 170  GLU C CB  1 
ATOM   5223  C CG  . GLU C  1 170 ? 56.881  39.083 76.568  1.00 56.53  ? 170  GLU C CG  1 
ATOM   5224  C CD  . GLU C  1 170 ? 58.062  38.315 77.140  1.00 58.69  ? 170  GLU C CD  1 
ATOM   5225  O OE1 . GLU C  1 170 ? 58.577  38.691 78.216  1.00 59.65  ? 170  GLU C OE1 1 
ATOM   5226  O OE2 . GLU C  1 170 ? 58.479  37.323 76.505  1.00 59.57  ? 170  GLU C OE2 1 
ATOM   5227  N N   . ASP C  1 171 ? 54.017  42.160 77.737  1.00 51.88  ? 171  ASP C N   1 
ATOM   5228  C CA  . ASP C  1 171 ? 52.728  42.430 78.366  1.00 50.26  ? 171  ASP C CA  1 
ATOM   5229  C C   . ASP C  1 171 ? 52.280  41.132 79.033  1.00 49.98  ? 171  ASP C C   1 
ATOM   5230  O O   . ASP C  1 171 ? 52.666  40.037 78.605  1.00 50.51  ? 171  ASP C O   1 
ATOM   5231  C CB  . ASP C  1 171 ? 51.676  42.879 77.340  1.00 48.80  ? 171  ASP C CB  1 
ATOM   5232  C CG  . ASP C  1 171 ? 51.962  44.255 76.749  1.00 49.02  ? 171  ASP C CG  1 
ATOM   5233  O OD1 . ASP C  1 171 ? 52.466  45.149 77.462  1.00 49.72  ? 171  ASP C OD1 1 
ATOM   5234  O OD2 . ASP C  1 171 ? 51.654  44.446 75.556  1.00 48.62  ? 171  ASP C OD2 1 
ATOM   5235  N N   . LEU C  1 172 ? 51.472  41.260 80.081  1.00 49.26  ? 172  LEU C N   1 
ATOM   5236  C CA  . LEU C  1 172 ? 51.021  40.109 80.846  1.00 49.24  ? 172  LEU C CA  1 
ATOM   5237  C C   . LEU C  1 172 ? 49.523  40.187 81.108  1.00 47.70  ? 172  LEU C C   1 
ATOM   5238  O O   . LEU C  1 172 ? 49.043  41.153 81.694  1.00 47.23  ? 172  LEU C O   1 
ATOM   5239  C CB  . LEU C  1 172 ? 51.780  40.040 82.169  1.00 50.74  ? 172  LEU C CB  1 
ATOM   5240  C CG  . LEU C  1 172 ? 51.546  38.795 83.031  1.00 51.41  ? 172  LEU C CG  1 
ATOM   5241  C CD1 . LEU C  1 172 ? 52.186  37.563 82.406  1.00 52.31  ? 172  LEU C CD1 1 
ATOM   5242  C CD2 . LEU C  1 172 ? 52.091  39.022 84.433  1.00 52.85  ? 172  LEU C CD2 1 
ATOM   5243  N N   . LEU C  1 173 ? 48.797  39.162 80.666  1.00 47.02  ? 173  LEU C N   1 
ATOM   5244  C CA  . LEU C  1 173 ? 47.369  39.051 80.936  1.00 45.86  ? 173  LEU C CA  1 
ATOM   5245  C C   . LEU C  1 173 ? 47.154  38.435 82.311  1.00 46.57  ? 173  LEU C C   1 
ATOM   5246  O O   . LEU C  1 173 ? 47.383  37.240 82.505  1.00 47.36  ? 173  LEU C O   1 
ATOM   5247  C CB  . LEU C  1 173 ? 46.675  38.187 79.884  1.00 45.11  ? 173  LEU C CB  1 
ATOM   5248  C CG  . LEU C  1 173 ? 45.192  37.875 80.143  1.00 44.23  ? 173  LEU C CG  1 
ATOM   5249  C CD1 . LEU C  1 173 ? 44.336  39.132 80.085  1.00 43.22  ? 173  LEU C CD1 1 
ATOM   5250  C CD2 . LEU C  1 173 ? 44.687  36.841 79.150  1.00 43.90  ? 173  LEU C CD2 1 
ATOM   5251  N N   . VAL C  1 174 ? 46.698  39.257 83.253  1.00 46.42  ? 174  VAL C N   1 
ATOM   5252  C CA  . VAL C  1 174 ? 46.390  38.810 84.607  1.00 47.19  ? 174  VAL C CA  1 
ATOM   5253  C C   . VAL C  1 174 ? 44.880  38.638 84.762  1.00 46.29  ? 174  VAL C C   1 
ATOM   5254  O O   . VAL C  1 174 ? 44.101  39.466 84.281  1.00 45.14  ? 174  VAL C O   1 
ATOM   5255  C CB  . VAL C  1 174 ? 46.886  39.822 85.659  1.00 47.94  ? 174  VAL C CB  1 
ATOM   5256  C CG1 . VAL C  1 174 ? 46.715  39.256 87.062  1.00 49.16  ? 174  VAL C CG1 1 
ATOM   5257  C CG2 . VAL C  1 174 ? 48.341  40.193 85.406  1.00 48.84  ? 174  VAL C CG2 1 
ATOM   5258  N N   . LEU C  1 175 ? 44.483  37.563 85.440  1.00 47.01  ? 175  LEU C N   1 
ATOM   5259  C CA  . LEU C  1 175 ? 43.078  37.280 85.732  1.00 46.54  ? 175  LEU C CA  1 
ATOM   5260  C C   . LEU C  1 175 ? 42.883  37.100 87.231  1.00 47.82  ? 175  LEU C C   1 
ATOM   5261  O O   . LEU C  1 175 ? 43.700  36.459 87.889  1.00 49.23  ? 175  LEU C O   1 
ATOM   5262  C CB  . LEU C  1 175 ? 42.639  35.992 85.039  1.00 46.43  ? 175  LEU C CB  1 
ATOM   5263  C CG  . LEU C  1 175 ? 42.793  35.913 83.521  1.00 45.46  ? 175  LEU C CG  1 
ATOM   5264  C CD1 . LEU C  1 175 ? 42.692  34.465 83.059  1.00 45.94  ? 175  LEU C CD1 1 
ATOM   5265  C CD2 . LEU C  1 175 ? 41.751  36.782 82.836  1.00 44.04  ? 175  LEU C CD2 1 
ATOM   5266  N N   . TRP C  1 176 ? 41.799  37.660 87.761  1.00 47.50  ? 176  TRP C N   1 
ATOM   5267  C CA  . TRP C  1 176 ? 41.393  37.415 89.143  1.00 48.80  ? 176  TRP C CA  1 
ATOM   5268  C C   . TRP C  1 176 ? 39.870  37.464 89.247  1.00 48.33  ? 176  TRP C C   1 
ATOM   5269  O O   . TRP C  1 176 ? 39.182  37.685 88.249  1.00 47.01  ? 176  TRP C O   1 
ATOM   5270  C CB  . TRP C  1 176 ? 42.049  38.426 90.095  1.00 49.56  ? 176  TRP C CB  1 
ATOM   5271  C CG  . TRP C  1 176 ? 41.590  39.836 89.905  1.00 48.52  ? 176  TRP C CG  1 
ATOM   5272  C CD1 . TRP C  1 176 ? 40.633  40.493 90.626  1.00 48.65  ? 176  TRP C CD1 1 
ATOM   5273  C CD2 . TRP C  1 176 ? 42.068  40.767 88.930  1.00 47.43  ? 176  TRP C CD2 1 
ATOM   5274  N NE1 . TRP C  1 176 ? 40.487  41.776 90.159  1.00 47.71  ? 176  TRP C NE1 1 
ATOM   5275  C CE2 . TRP C  1 176 ? 41.356  41.970 89.117  1.00 46.96  ? 176  TRP C CE2 1 
ATOM   5276  C CE3 . TRP C  1 176 ? 43.030  40.701 87.915  1.00 46.96  ? 176  TRP C CE3 1 
ATOM   5277  C CZ2 . TRP C  1 176 ? 41.577  43.100 88.324  1.00 46.08  ? 176  TRP C CZ2 1 
ATOM   5278  C CZ3 . TRP C  1 176 ? 43.249  41.824 87.129  1.00 46.09  ? 176  TRP C CZ3 1 
ATOM   5279  C CH2 . TRP C  1 176 ? 42.526  43.006 87.338  1.00 45.67  ? 176  TRP C CH2 1 
ATOM   5280  N N   . GLY C  1 177 ? 39.346  37.253 90.451  1.00 49.62  ? 177  GLY C N   1 
ATOM   5281  C CA  . GLY C  1 177 ? 37.899  37.231 90.655  1.00 49.55  ? 177  GLY C CA  1 
ATOM   5282  C C   . GLY C  1 177 ? 37.435  37.586 92.055  1.00 50.94  ? 177  GLY C C   1 
ATOM   5283  O O   . GLY C  1 177 ? 38.226  37.637 93.000  1.00 52.23  ? 177  GLY C O   1 
ATOM   5284  N N   . ILE C  1 178 ? 36.133  37.831 92.166  1.00 50.85  ? 178  ILE C N   1 
ATOM   5285  C CA  . ILE C  1 178 ? 35.472  38.081 93.444  1.00 52.34  ? 178  ILE C CA  1 
ATOM   5286  C C   . ILE C  1 178 ? 34.329  37.073 93.578  1.00 53.16  ? 178  ILE C C   1 
ATOM   5287  O O   . ILE C  1 178 ? 33.684  36.730 92.584  1.00 52.11  ? 178  ILE C O   1 
ATOM   5288  C CB  . ILE C  1 178 ? 34.936  39.535 93.542  1.00 51.75  ? 178  ILE C CB  1 
ATOM   5289  C CG1 . ILE C  1 178 ? 34.434  39.841 94.968  1.00 53.53  ? 178  ILE C CG1 1 
ATOM   5290  C CG2 . ILE C  1 178 ? 33.863  39.793 92.490  1.00 50.40  ? 178  ILE C CG2 1 
ATOM   5291  C CD1 . ILE C  1 178 ? 33.463  41.001 95.080  1.00 53.31  ? 178  ILE C CD1 1 
ATOM   5292  N N   . HIS C  1 179 ? 34.091  36.593 94.796  1.00 55.21  ? 179  HIS C N   1 
ATOM   5293  C CA  . HIS C  1 179 ? 32.957  35.708 95.058  1.00 56.38  ? 179  HIS C CA  1 
ATOM   5294  C C   . HIS C  1 179 ? 31.794  36.465 95.699  1.00 57.02  ? 179  HIS C C   1 
ATOM   5295  O O   . HIS C  1 179 ? 31.981  37.233 96.647  1.00 57.92  ? 179  HIS C O   1 
ATOM   5296  C CB  . HIS C  1 179 ? 33.362  34.538 95.954  1.00 58.58  ? 179  HIS C CB  1 
ATOM   5297  C CG  . HIS C  1 179 ? 32.215  33.653 96.334  1.00 60.14  ? 179  HIS C CG  1 
ATOM   5298  N ND1 . HIS C  1 179 ? 31.905  33.354 97.643  1.00 62.61  ? 179  HIS C ND1 1 
ATOM   5299  C CD2 . HIS C  1 179 ? 31.286  33.025 95.575  1.00 59.77  ? 179  HIS C CD2 1 
ATOM   5300  C CE1 . HIS C  1 179 ? 30.846  32.565 97.674  1.00 63.68  ? 179  HIS C CE1 1 
ATOM   5301  N NE2 . HIS C  1 179 ? 30.451  32.350 96.432  1.00 62.02  ? 179  HIS C NE2 1 
ATOM   5302  N N   . HIS C  1 180 ? 30.596  36.228 95.169  1.00 56.72  ? 180  HIS C N   1 
ATOM   5303  C CA  . HIS C  1 180 ? 29.368  36.811 95.691  1.00 57.54  ? 180  HIS C CA  1 
ATOM   5304  C C   . HIS C  1 180 ? 28.580  35.702 96.394  1.00 59.64  ? 180  HIS C C   1 
ATOM   5305  O O   . HIS C  1 180 ? 28.040  34.812 95.730  1.00 59.53  ? 180  HIS C O   1 
ATOM   5306  C CB  . HIS C  1 180 ? 28.535  37.394 94.549  1.00 55.95  ? 180  HIS C CB  1 
ATOM   5307  C CG  . HIS C  1 180 ? 29.226  38.476 93.775  1.00 54.07  ? 180  HIS C CG  1 
ATOM   5308  N ND1 . HIS C  1 180 ? 28.812  39.789 93.810  1.00 53.74  ? 180  HIS C ND1 1 
ATOM   5309  C CD2 . HIS C  1 180 ? 30.285  38.440 92.932  1.00 52.61  ? 180  HIS C CD2 1 
ATOM   5310  C CE1 . HIS C  1 180 ? 29.589  40.518 93.030  1.00 52.15  ? 180  HIS C CE1 1 
ATOM   5311  N NE2 . HIS C  1 180 ? 30.492  39.724 92.485  1.00 51.44  ? 180  HIS C NE2 1 
ATOM   5312  N N   . PRO C  1 181 ? 28.521  35.739 97.740  1.00 61.70  ? 181  PRO C N   1 
ATOM   5313  C CA  . PRO C  1 181 ? 27.838  34.691 98.496  1.00 64.03  ? 181  PRO C CA  1 
ATOM   5314  C C   . PRO C  1 181 ? 26.321  34.881 98.529  1.00 64.73  ? 181  PRO C C   1 
ATOM   5315  O O   . PRO C  1 181 ? 25.822  35.948 98.169  1.00 63.66  ? 181  PRO C O   1 
ATOM   5316  C CB  . PRO C  1 181 ? 28.430  34.840 99.896  1.00 66.07  ? 181  PRO C CB  1 
ATOM   5317  C CG  . PRO C  1 181 ? 28.734  36.295 100.012 1.00 65.03  ? 181  PRO C CG  1 
ATOM   5318  C CD  . PRO C  1 181 ? 29.077  36.779 98.627  1.00 62.18  ? 181  PRO C CD  1 
ATOM   5319  N N   . ASN C  1 182 ? 25.603  33.852 98.973  1.00 66.71  ? 182  ASN C N   1 
ATOM   5320  C CA  . ASN C  1 182 ? 24.137  33.851 98.945  1.00 67.64  ? 182  ASN C CA  1 
ATOM   5321  C C   . ASN C  1 182 ? 23.501  34.739 100.013 1.00 69.26  ? 182  ASN C C   1 
ATOM   5322  O O   . ASN C  1 182 ? 22.571  35.494 99.717  1.00 68.93  ? 182  ASN C O   1 
ATOM   5323  C CB  . ASN C  1 182 ? 23.605  32.423 99.081  1.00 69.53  ? 182  ASN C CB  1 
ATOM   5324  C CG  . ASN C  1 182 ? 23.908  31.576 97.864  1.00 67.97  ? 182  ASN C CG  1 
ATOM   5325  O OD1 . ASN C  1 182 ? 23.056  31.408 96.999  1.00 67.35  ? 182  ASN C OD1 1 
ATOM   5326  N ND2 . ASN C  1 182 ? 25.128  31.057 97.779  1.00 67.46  ? 182  ASN C ND2 1 
ATOM   5327  N N   . ASP C  1 183 ? 23.996  34.631 101.247 1.00 71.17  ? 183  ASP C N   1 
ATOM   5328  C CA  . ASP C  1 183 ? 23.487  35.418 102.380 1.00 73.04  ? 183  ASP C CA  1 
ATOM   5329  C C   . ASP C  1 183 ? 24.610  35.801 103.353 1.00 73.75  ? 183  ASP C C   1 
ATOM   5330  O O   . ASP C  1 183 ? 25.746  35.337 103.218 1.00 73.05  ? 183  ASP C O   1 
ATOM   5331  C CB  . ASP C  1 183 ? 22.370  34.656 103.113 1.00 76.03  ? 183  ASP C CB  1 
ATOM   5332  C CG  . ASP C  1 183 ? 22.755  33.223 103.461 1.00 77.67  ? 183  ASP C CG  1 
ATOM   5333  O OD1 . ASP C  1 183 ? 23.925  32.971 103.819 1.00 77.70  ? 183  ASP C OD1 1 
ATOM   5334  O OD2 . ASP C  1 183 ? 21.874  32.342 103.382 1.00 79.11  ? 183  ASP C OD2 1 
ATOM   5335  N N   . ALA C  1 184 ? 24.281  36.648 104.329 1.00 75.29  ? 184  ALA C N   1 
ATOM   5336  C CA  . ALA C  1 184 ? 25.248  37.103 105.338 1.00 76.30  ? 184  ALA C CA  1 
ATOM   5337  C C   . ALA C  1 184 ? 25.820  35.953 106.174 1.00 78.59  ? 184  ALA C C   1 
ATOM   5338  O O   . ALA C  1 184 ? 26.943  36.046 106.673 1.00 78.90  ? 184  ALA C O   1 
ATOM   5339  C CB  . ALA C  1 184 ? 24.612  38.148 106.245 1.00 77.91  ? 184  ALA C CB  1 
ATOM   5340  N N   . ALA C  1 185 ? 25.044  34.878 106.322 1.00 80.37  ? 185  ALA C N   1 
ATOM   5341  C CA  . ALA C  1 185 ? 25.486  33.681 107.041 1.00 82.80  ? 185  ALA C CA  1 
ATOM   5342  C C   . ALA C  1 185 ? 26.608  32.938 106.306 1.00 81.20  ? 185  ALA C C   1 
ATOM   5343  O O   . ALA C  1 185 ? 27.537  32.428 106.936 1.00 82.61  ? 185  ALA C O   1 
ATOM   5344  C CB  . ALA C  1 185 ? 24.305  32.749 107.283 1.00 85.12  ? 185  ALA C CB  1 
ATOM   5345  N N   . GLU C  1 186 ? 26.518  32.874 104.979 1.00 78.45  ? 186  GLU C N   1 
ATOM   5346  C CA  . GLU C  1 186 ? 27.561  32.237 104.171 1.00 76.84  ? 186  GLU C CA  1 
ATOM   5347  C C   . GLU C  1 186 ? 28.816  33.111 104.076 1.00 75.18  ? 186  GLU C C   1 
ATOM   5348  O O   . GLU C  1 186 ? 29.935  32.593 104.051 1.00 75.20  ? 186  GLU C O   1 
ATOM   5349  C CB  . GLU C  1 186 ? 27.043  31.905 102.769 1.00 74.58  ? 186  GLU C CB  1 
ATOM   5350  C CG  . GLU C  1 186 ? 27.966  30.982 101.985 1.00 73.52  ? 186  GLU C CG  1 
ATOM   5351  C CD  . GLU C  1 186 ? 27.350  30.489 100.691 1.00 71.85  ? 186  GLU C CD  1 
ATOM   5352  O OE1 . GLU C  1 186 ? 27.025  31.329 99.824  1.00 69.51  ? 186  GLU C OE1 1 
ATOM   5353  O OE2 . GLU C  1 186 ? 27.202  29.257 100.537 1.00 73.03  ? 186  GLU C OE2 1 
ATOM   5354  N N   . GLN C  1 187 ? 28.622  34.429 104.012 1.00 73.93  ? 187  GLN C N   1 
ATOM   5355  C CA  . GLN C  1 187 ? 29.731  35.392 104.033 1.00 72.71  ? 187  GLN C CA  1 
ATOM   5356  C C   . GLN C  1 187 ? 30.620  35.155 105.252 1.00 75.18  ? 187  GLN C C   1 
ATOM   5357  O O   . GLN C  1 187 ? 31.838  34.996 105.127 1.00 74.71  ? 187  GLN C O   1 
ATOM   5358  C CB  . GLN C  1 187 ? 29.192  36.834 104.034 1.00 71.77  ? 187  GLN C CB  1 
ATOM   5359  C CG  . GLN C  1 187 ? 30.223  37.924 104.329 1.00 71.16  ? 187  GLN C CG  1 
ATOM   5360  C CD  . GLN C  1 187 ? 31.333  37.999 103.289 1.00 68.70  ? 187  GLN C CD  1 
ATOM   5361  O OE1 . GLN C  1 187 ? 31.073  37.961 102.087 1.00 66.51  ? 187  GLN C OE1 1 
ATOM   5362  N NE2 . GLN C  1 187 ? 32.577  38.121 103.749 1.00 69.21  ? 187  GLN C NE2 1 
ATOM   5363  N N   . THR C  1 188 ? 29.998  35.122 106.428 1.00 78.01  ? 188  THR C N   1 
ATOM   5364  C CA  . THR C  1 188 ? 30.718  34.881 107.675 1.00 80.81  ? 188  THR C CA  1 
ATOM   5365  C C   . THR C  1 188 ? 31.296  33.461 107.723 1.00 82.19  ? 188  THR C C   1 
ATOM   5366  O O   . THR C  1 188 ? 32.418  33.260 108.185 1.00 83.20  ? 188  THR C O   1 
ATOM   5367  C CB  . THR C  1 188 ? 29.818  35.108 108.906 1.00 83.77  ? 188  THR C CB  1 
ATOM   5368  O OG1 . THR C  1 188 ? 28.645  34.293 108.799 1.00 84.83  ? 188  THR C OG1 1 
ATOM   5369  C CG2 . THR C  1 188 ? 29.408  36.578 109.021 1.00 82.87  ? 188  THR C CG2 1 
ATOM   5370  N N   . LYS C  1 189 ? 30.538  32.483 107.233 1.00 82.37  ? 189  LYS C N   1 
ATOM   5371  C CA  . LYS C  1 189 ? 31.009  31.098 107.196 1.00 83.76  ? 189  LYS C CA  1 
ATOM   5372  C C   . LYS C  1 189 ? 32.296  30.938 106.380 1.00 81.78  ? 189  LYS C C   1 
ATOM   5373  O O   . LYS C  1 189 ? 33.177  30.162 106.749 1.00 83.41  ? 189  LYS C O   1 
ATOM   5374  C CB  . LYS C  1 189 ? 29.932  30.170 106.626 1.00 83.96  ? 189  LYS C CB  1 
ATOM   5375  C CG  . LYS C  1 189 ? 30.427  28.748 106.404 1.00 85.16  ? 189  LYS C CG  1 
ATOM   5376  C CD  . LYS C  1 189 ? 29.340  27.811 105.913 1.00 85.73  ? 189  LYS C CD  1 
ATOM   5377  C CE  . LYS C  1 189 ? 29.874  26.391 105.808 1.00 87.35  ? 189  LYS C CE  1 
ATOM   5378  N NZ  . LYS C  1 189 ? 29.254  25.649 104.680 1.00 86.18  ? 189  LYS C NZ  1 
ATOM   5379  N N   . LEU C  1 190 ? 32.386  31.658 105.266 1.00 78.47  ? 190  LEU C N   1 
ATOM   5380  C CA  . LEU C  1 190 ? 33.524  31.536 104.357 1.00 76.50  ? 190  LEU C CA  1 
ATOM   5381  C C   . LEU C  1 190 ? 34.694  32.432 104.742 1.00 76.19  ? 190  LEU C C   1 
ATOM   5382  O O   . LEU C  1 190 ? 35.843  31.986 104.764 1.00 76.70  ? 190  LEU C O   1 
ATOM   5383  C CB  . LEU C  1 190 ? 33.094  31.864 102.925 1.00 73.31  ? 190  LEU C CB  1 
ATOM   5384  C CG  . LEU C  1 190 ? 32.405  30.729 102.172 1.00 73.23  ? 190  LEU C CG  1 
ATOM   5385  C CD1 . LEU C  1 190 ? 31.686  31.249 100.936 1.00 70.39  ? 190  LEU C CD1 1 
ATOM   5386  C CD2 . LEU C  1 190 ? 33.426  29.670 101.794 1.00 73.65  ? 190  LEU C CD2 1 
ATOM   5387  N N   . TYR C  1 191 ? 34.394  33.697 105.023 1.00 75.42  ? 191  TYR C N   1 
ATOM   5388  C CA  . TYR C  1 191 ? 35.424  34.720 105.225 1.00 74.80  ? 191  TYR C CA  1 
ATOM   5389  C C   . TYR C  1 191 ? 35.343  35.432 106.581 1.00 77.02  ? 191  TYR C C   1 
ATOM   5390  O O   . TYR C  1 191 ? 36.212  36.244 106.901 1.00 77.02  ? 191  TYR C O   1 
ATOM   5391  C CB  . TYR C  1 191 ? 35.332  35.754 104.098 1.00 71.54  ? 191  TYR C CB  1 
ATOM   5392  C CG  . TYR C  1 191 ? 35.066  35.140 102.736 1.00 69.36  ? 191  TYR C CG  1 
ATOM   5393  C CD1 . TYR C  1 191 ? 36.096  34.554 102.001 1.00 68.49  ? 191  TYR C CD1 1 
ATOM   5394  C CD2 . TYR C  1 191 ? 33.780  35.123 102.196 1.00 68.40  ? 191  TYR C CD2 1 
ATOM   5395  C CE1 . TYR C  1 191 ? 35.857  33.985 100.759 1.00 66.65  ? 191  TYR C CE1 1 
ATOM   5396  C CE2 . TYR C  1 191 ? 33.532  34.554 100.956 1.00 66.59  ? 191  TYR C CE2 1 
ATOM   5397  C CZ  . TYR C  1 191 ? 34.576  33.985 100.244 1.00 65.70  ? 191  TYR C CZ  1 
ATOM   5398  O OH  . TYR C  1 191 ? 34.343  33.417 99.015  1.00 64.04  ? 191  TYR C OH  1 
ATOM   5399  N N   . GLN C  1 192 ? 34.313  35.121 107.368 1.00 79.03  ? 192  GLN C N   1 
ATOM   5400  C CA  . GLN C  1 192 ? 34.052  35.759 108.668 1.00 81.37  ? 192  GLN C CA  1 
ATOM   5401  C C   . GLN C  1 192 ? 33.756  37.253 108.624 1.00 79.95  ? 192  GLN C C   1 
ATOM   5402  O O   . GLN C  1 192 ? 32.680  37.678 109.047 1.00 80.75  ? 192  GLN C O   1 
ATOM   5403  C CB  . GLN C  1 192 ? 35.159  35.454 109.684 1.00 83.99  ? 192  GLN C CB  1 
ATOM   5404  C CG  . GLN C  1 192 ? 34.755  34.342 110.644 1.00 87.45  ? 192  GLN C CG  1 
ATOM   5405  C CD  . GLN C  1 192 ? 35.637  34.208 111.866 1.00 90.64  ? 192  GLN C CD  1 
ATOM   5406  O OE1 . GLN C  1 192 ? 35.560  33.204 112.569 1.00 93.58  ? 192  GLN C OE1 1 
ATOM   5407  N NE2 . GLN C  1 192 ? 36.463  35.213 112.139 1.00 90.30  ? 192  GLN C NE2 1 
ATOM   5408  N N   . ASN C  1 193 ? 34.706  38.048 108.138 1.00 78.08  ? 193  ASN C N   1 
ATOM   5409  C CA  . ASN C  1 193 ? 34.528  39.499 108.054 1.00 76.80  ? 193  ASN C CA  1 
ATOM   5410  C C   . ASN C  1 193 ? 33.220  39.822 107.322 1.00 75.11  ? 193  ASN C C   1 
ATOM   5411  O O   . ASN C  1 193 ? 33.029  39.382 106.187 1.00 73.00  ? 193  ASN C O   1 
ATOM   5412  C CB  . ASN C  1 193 ? 35.715  40.159 107.338 1.00 74.75  ? 193  ASN C CB  1 
ATOM   5413  C CG  . ASN C  1 193 ? 37.062  39.718 107.895 1.00 76.33  ? 193  ASN C CG  1 
ATOM   5414  O OD1 . ASN C  1 193 ? 37.202  38.599 108.385 1.00 78.27  ? 193  ASN C OD1 1 
ATOM   5415  N ND2 . ASN C  1 193 ? 38.061  40.589 107.811 1.00 75.69  ? 193  ASN C ND2 1 
ATOM   5416  N N   . PRO C  1 194 ? 32.306  40.567 107.976 1.00 76.22  ? 194  PRO C N   1 
ATOM   5417  C CA  . PRO C  1 194 ? 30.984  40.806 107.387 1.00 75.12  ? 194  PRO C CA  1 
ATOM   5418  C C   . PRO C  1 194 ? 31.041  41.713 106.160 1.00 71.99  ? 194  PRO C C   1 
ATOM   5419  O O   . PRO C  1 194 ? 30.396  41.427 105.151 1.00 70.28  ? 194  PRO C O   1 
ATOM   5420  C CB  . PRO C  1 194 ? 30.200  41.473 108.526 1.00 77.53  ? 194  PRO C CB  1 
ATOM   5421  C CG  . PRO C  1 194 ? 31.233  42.110 109.390 1.00 78.77  ? 194  PRO C CG  1 
ATOM   5422  C CD  . PRO C  1 194 ? 32.488  41.293 109.250 1.00 78.57  ? 194  PRO C CD  1 
ATOM   5423  N N   . THR C  1 195 ? 31.815  42.792 106.259 1.00 71.41  ? 195  THR C N   1 
ATOM   5424  C CA  . THR C  1 195 ? 32.020  43.724 105.159 1.00 68.74  ? 195  THR C CA  1 
ATOM   5425  C C   . THR C  1 195 ? 33.422  43.492 104.609 1.00 67.45  ? 195  THR C C   1 
ATOM   5426  O O   . THR C  1 195 ? 34.397  43.537 105.360 1.00 68.75  ? 195  THR C O   1 
ATOM   5427  C CB  . THR C  1 195 ? 31.884  45.183 105.640 1.00 69.24  ? 195  THR C CB  1 
ATOM   5428  O OG1 . THR C  1 195 ? 30.730  45.308 106.479 1.00 71.23  ? 195  THR C OG1 1 
ATOM   5429  C CG2 . THR C  1 195 ? 31.754  46.135 104.461 1.00 66.77  ? 195  THR C CG2 1 
ATOM   5430  N N   . THR C  1 196 ? 33.521  43.221 103.308 1.00 65.08  ? 196  THR C N   1 
ATOM   5431  C CA  . THR C  1 196 ? 34.806  42.888 102.685 1.00 63.92  ? 196  THR C CA  1 
ATOM   5432  C C   . THR C  1 196 ? 35.022  43.639 101.376 1.00 61.35  ? 196  THR C C   1 
ATOM   5433  O O   . THR C  1 196 ? 34.091  44.224 100.821 1.00 60.33  ? 196  THR C O   1 
ATOM   5434  C CB  . THR C  1 196 ? 34.938  41.372 102.432 1.00 64.10  ? 196  THR C CB  1 
ATOM   5435  O OG1 . THR C  1 196 ? 33.864  40.924 101.599 1.00 62.91  ? 196  THR C OG1 1 
ATOM   5436  C CG2 . THR C  1 196 ? 34.910  40.607 103.749 1.00 66.96  ? 196  THR C CG2 1 
ATOM   5437  N N   . TYR C  1 197 ? 36.263  43.619 100.895 1.00 60.54  ? 197  TYR C N   1 
ATOM   5438  C CA  . TYR C  1 197 ? 36.635  44.326 99.676  1.00 58.34  ? 197  TYR C CA  1 
ATOM   5439  C C   . TYR C  1 197 ? 37.850  43.693 99.005  1.00 57.61  ? 197  TYR C C   1 
ATOM   5440  O O   . TYR C  1 197 ? 38.559  42.888 99.611  1.00 58.92  ? 197  TYR C O   1 
ATOM   5441  C CB  . TYR C  1 197 ? 36.953  45.789 99.993  1.00 58.53  ? 197  TYR C CB  1 
ATOM   5442  C CG  . TYR C  1 197 ? 38.256  45.969 100.742 1.00 59.83  ? 197  TYR C CG  1 
ATOM   5443  C CD1 . TYR C  1 197 ? 38.290  45.939 102.133 1.00 62.16  ? 197  TYR C CD1 1 
ATOM   5444  C CD2 . TYR C  1 197 ? 39.457  46.160 100.059 1.00 58.91  ? 197  TYR C CD2 1 
ATOM   5445  C CE1 . TYR C  1 197 ? 39.480  46.095 102.824 1.00 63.56  ? 197  TYR C CE1 1 
ATOM   5446  C CE2 . TYR C  1 197 ? 40.651  46.319 100.739 1.00 60.30  ? 197  TYR C CE2 1 
ATOM   5447  C CZ  . TYR C  1 197 ? 40.657  46.286 102.124 1.00 62.62  ? 197  TYR C CZ  1 
ATOM   5448  O OH  . TYR C  1 197 ? 41.839  46.441 102.808 1.00 64.17  ? 197  TYR C OH  1 
ATOM   5449  N N   . ILE C  1 198 ? 38.077  44.076 97.747  1.00 55.70  ? 198  ILE C N   1 
ATOM   5450  C CA  . ILE C  1 198 ? 39.294  43.725 97.016  1.00 54.99  ? 198  ILE C CA  1 
ATOM   5451  C C   . ILE C  1 198 ? 39.765  44.948 96.242  1.00 53.79  ? 198  ILE C C   1 
ATOM   5452  O O   . ILE C  1 198 ? 39.078  45.405 95.328  1.00 52.36  ? 198  ILE C O   1 
ATOM   5453  C CB  . ILE C  1 198 ? 39.073  42.584 96.000  1.00 53.84  ? 198  ILE C CB  1 
ATOM   5454  C CG1 . ILE C  1 198 ? 38.185  41.482 96.585  1.00 54.88  ? 198  ILE C CG1 1 
ATOM   5455  C CG2 . ILE C  1 198 ? 40.416  42.018 95.551  1.00 53.80  ? 198  ILE C CG2 1 
ATOM   5456  C CD1 . ILE C  1 198 ? 37.834  40.395 95.595  1.00 53.87  ? 198  ILE C CD1 1 
ATOM   5457  N N   . SER C  1 199 ? 40.931  45.476 96.605  1.00 54.59  ? 199  SER C N   1 
ATOM   5458  C CA  . SER C  1 199 ? 41.506  46.615 95.896  1.00 53.74  ? 199  SER C CA  1 
ATOM   5459  C C   . SER C  1 199 ? 42.672  46.159 95.028  1.00 53.17  ? 199  SER C C   1 
ATOM   5460  O O   . SER C  1 199 ? 43.605  45.523 95.517  1.00 54.32  ? 199  SER C O   1 
ATOM   5461  C CB  . SER C  1 199 ? 41.955  47.700 96.876  1.00 55.17  ? 199  SER C CB  1 
ATOM   5462  O OG  . SER C  1 199 ? 42.798  47.169 97.875  1.00 56.95  ? 199  SER C OG  1 
ATOM   5463  N N   . VAL C  1 200 ? 42.597  46.485 93.739  1.00 51.58  ? 200  VAL C N   1 
ATOM   5464  C CA  . VAL C  1 200 ? 43.632  46.134 92.768  1.00 51.02  ? 200  VAL C CA  1 
ATOM   5465  C C   . VAL C  1 200 ? 44.181  47.407 92.132  1.00 50.63  ? 200  VAL C C   1 
ATOM   5466  O O   . VAL C  1 200 ? 43.418  48.244 91.649  1.00 49.77  ? 200  VAL C O   1 
ATOM   5467  C CB  . VAL C  1 200 ? 43.086  45.219 91.653  1.00 49.61  ? 200  VAL C CB  1 
ATOM   5468  C CG1 . VAL C  1 200 ? 44.236  44.592 90.871  1.00 49.49  ? 200  VAL C CG1 1 
ATOM   5469  C CG2 . VAL C  1 200 ? 42.189  44.135 92.235  1.00 49.96  ? 200  VAL C CG2 1 
ATOM   5470  N N   . GLY C  1 201 ? 45.504  47.544 92.135  1.00 51.47  ? 201  GLY C N   1 
ATOM   5471  C CA  . GLY C  1 201 ? 46.157  48.730 91.598  1.00 51.46  ? 201  GLY C CA  1 
ATOM   5472  C C   . GLY C  1 201 ? 47.295  48.383 90.662  1.00 51.39  ? 201  GLY C C   1 
ATOM   5473  O O   . GLY C  1 201 ? 47.976  47.377 90.846  1.00 52.06  ? 201  GLY C O   1 
ATOM   5474  N N   . THR C  1 202 ? 47.470  49.207 89.633  1.00 50.73  ? 202  THR C N   1 
ATOM   5475  C CA  . THR C  1 202 ? 48.648  49.170 88.763  1.00 50.97  ? 202  THR C CA  1 
ATOM   5476  C C   . THR C  1 202 ? 49.029  50.626 88.502  1.00 51.42  ? 202  THR C C   1 
ATOM   5477  O O   . THR C  1 202 ? 48.605  51.514 89.248  1.00 51.94  ? 202  THR C O   1 
ATOM   5478  C CB  . THR C  1 202 ? 48.377  48.428 87.431  1.00 49.61  ? 202  THR C CB  1 
ATOM   5479  O OG1 . THR C  1 202 ? 47.494  49.201 86.604  1.00 48.42  ? 202  THR C OG1 1 
ATOM   5480  C CG2 . THR C  1 202 ? 47.776  47.052 87.685  1.00 49.16  ? 202  THR C CG2 1 
ATOM   5481  N N   . SER C  1 203 ? 49.820  50.885 87.465  1.00 51.44  ? 203  SER C N   1 
ATOM   5482  C CA  . SER C  1 203 ? 50.079  52.261 87.057  1.00 51.85  ? 203  SER C CA  1 
ATOM   5483  C C   . SER C  1 203 ? 48.794  52.908 86.546  1.00 50.62  ? 203  SER C C   1 
ATOM   5484  O O   . SER C  1 203 ? 48.574  54.100 86.750  1.00 51.13  ? 203  SER C O   1 
ATOM   5485  C CB  . SER C  1 203 ? 51.162  52.318 85.984  1.00 52.30  ? 203  SER C CB  1 
ATOM   5486  O OG  . SER C  1 203 ? 50.781  51.571 84.848  1.00 51.04  ? 203  SER C OG  1 
ATOM   5487  N N   . THR C  1 204 ? 47.941  52.116 85.902  1.00 49.19  ? 204  THR C N   1 
ATOM   5488  C CA  . THR C  1 204 ? 46.690  52.621 85.344  1.00 48.13  ? 204  THR C CA  1 
ATOM   5489  C C   . THR C  1 204 ? 45.480  52.186 86.166  1.00 47.59  ? 204  THR C C   1 
ATOM   5490  O O   . THR C  1 204 ? 44.593  52.995 86.435  1.00 47.60  ? 204  THR C O   1 
ATOM   5491  C CB  . THR C  1 204 ? 46.500  52.162 83.882  1.00 47.06  ? 204  THR C CB  1 
ATOM   5492  O OG1 . THR C  1 204 ? 46.383  50.735 83.828  1.00 46.36  ? 204  THR C OG1 1 
ATOM   5493  C CG2 . THR C  1 204 ? 47.674  52.610 83.022  1.00 47.78  ? 204  THR C CG2 1 
ATOM   5494  N N   . LEU C  1 205 ? 45.445  50.918 86.566  1.00 47.35  ? 205  LEU C N   1 
ATOM   5495  C CA  . LEU C  1 205 ? 44.271  50.362 87.240  1.00 46.93  ? 205  LEU C CA  1 
ATOM   5496  C C   . LEU C  1 205 ? 44.090  50.916 88.661  1.00 48.06  ? 205  LEU C C   1 
ATOM   5497  O O   . LEU C  1 205 ? 45.030  50.931 89.454  1.00 49.26  ? 205  LEU C O   1 
ATOM   5498  C CB  . LEU C  1 205 ? 44.356  48.830 87.278  1.00 46.63  ? 205  LEU C CB  1 
ATOM   5499  C CG  . LEU C  1 205 ? 43.108  48.064 87.741  1.00 46.18  ? 205  LEU C CG  1 
ATOM   5500  C CD1 . LEU C  1 205 ? 41.891  48.414 86.893  1.00 45.07  ? 205  LEU C CD1 1 
ATOM   5501  C CD2 . LEU C  1 205 ? 43.363  46.563 87.714  1.00 46.13  ? 205  LEU C CD2 1 
ATOM   5502  N N   . ASN C  1 206 ? 42.876  51.379 88.960  1.00 47.82  ? 206  ASN C N   1 
ATOM   5503  C CA  . ASN C  1 206 ? 42.496  51.811 90.308  1.00 48.89  ? 206  ASN C CA  1 
ATOM   5504  C C   . ASN C  1 206 ? 41.116  51.260 90.663  1.00 48.48  ? 206  ASN C C   1 
ATOM   5505  O O   . ASN C  1 206 ? 40.106  51.959 90.571  1.00 48.29  ? 206  ASN C O   1 
ATOM   5506  C CB  . ASN C  1 206 ? 42.508  53.338 90.419  1.00 49.59  ? 206  ASN C CB  1 
ATOM   5507  C CG  . ASN C  1 206 ? 42.152  53.828 91.817  1.00 50.90  ? 206  ASN C CG  1 
ATOM   5508  O OD1 . ASN C  1 206 ? 42.421  53.153 92.813  1.00 51.71  ? 206  ASN C OD1 1 
ATOM   5509  N ND2 . ASN C  1 206 ? 41.549  55.007 91.897  1.00 51.32  ? 206  ASN C ND2 1 
ATOM   5510  N N   . GLN C  1 207 ? 41.094  50.003 91.085  1.00 48.54  ? 207  GLN C N   1 
ATOM   5511  C CA  . GLN C  1 207 ? 39.855  49.264 91.283  1.00 48.24  ? 207  GLN C CA  1 
ATOM   5512  C C   . GLN C  1 207 ? 39.637  48.913 92.754  1.00 49.66  ? 207  GLN C C   1 
ATOM   5513  O O   . GLN C  1 207 ? 40.593  48.706 93.499  1.00 50.72  ? 207  GLN C O   1 
ATOM   5514  C CB  . GLN C  1 207 ? 39.891  48.001 90.413  1.00 47.25  ? 207  GLN C CB  1 
ATOM   5515  C CG  . GLN C  1 207 ? 38.939  46.884 90.812  1.00 47.34  ? 207  GLN C CG  1 
ATOM   5516  C CD  . GLN C  1 207 ? 39.098  45.652 89.939  1.00 46.54  ? 207  GLN C CD  1 
ATOM   5517  O OE1 . GLN C  1 207 ? 39.369  44.558 90.439  1.00 47.19  ? 207  GLN C OE1 1 
ATOM   5518  N NE2 . GLN C  1 207 ? 38.941  45.823 88.628  1.00 45.32  ? 207  GLN C NE2 1 
ATOM   5519  N N   . ARG C  1 208 ? 38.370  48.871 93.161  1.00 49.89  ? 208  ARG C N   1 
ATOM   5520  C CA  . ARG C  1 208 ? 37.982  48.369 94.477  1.00 51.33  ? 208  ARG C CA  1 
ATOM   5521  C C   . ARG C  1 208 ? 36.628  47.664 94.379  1.00 51.08  ? 208  ARG C C   1 
ATOM   5522  O O   . ARG C  1 208 ? 35.595  48.310 94.207  1.00 50.90  ? 208  ARG C O   1 
ATOM   5523  C CB  . ARG C  1 208 ? 37.912  49.500 95.505  1.00 52.69  ? 208  ARG C CB  1 
ATOM   5524  C CG  . ARG C  1 208 ? 37.836  49.003 96.941  1.00 54.50  ? 208  ARG C CG  1 
ATOM   5525  C CD  . ARG C  1 208 ? 37.381  50.094 97.897  1.00 55.89  ? 208  ARG C CD  1 
ATOM   5526  N NE  . ARG C  1 208 ? 37.660  49.750 99.292  1.00 57.88  ? 208  ARG C NE  1 
ATOM   5527  C CZ  . ARG C  1 208 ? 38.861  49.815 99.867  1.00 58.94  ? 208  ARG C CZ  1 
ATOM   5528  N NH1 . ARG C  1 208 ? 39.929  50.208 99.176  1.00 58.18  ? 208  ARG C NH1 1 
ATOM   5529  N NH2 . ARG C  1 208 ? 39.002  49.481 101.148 1.00 60.96  ? 208  ARG C NH2 1 
ATOM   5530  N N   . LEU C  1 209 ? 36.645  46.338 94.489  1.00 51.26  ? 209  LEU C N   1 
ATOM   5531  C CA  . LEU C  1 209 ? 35.433  45.531 94.367  1.00 51.17  ? 209  LEU C CA  1 
ATOM   5532  C C   . LEU C  1 209 ? 34.853  45.223 95.740  1.00 53.02  ? 209  LEU C C   1 
ATOM   5533  O O   . LEU C  1 209 ? 35.595  45.040 96.701  1.00 54.29  ? 209  LEU C O   1 
ATOM   5534  C CB  . LEU C  1 209 ? 35.743  44.217 93.645  1.00 50.45  ? 209  LEU C CB  1 
ATOM   5535  C CG  . LEU C  1 209 ? 36.384  44.332 92.259  1.00 48.84  ? 209  LEU C CG  1 
ATOM   5536  C CD1 . LEU C  1 209 ? 36.829  42.963 91.765  1.00 48.56  ? 209  LEU C CD1 1 
ATOM   5537  C CD2 . LEU C  1 209 ? 35.432  44.986 91.267  1.00 47.69  ? 209  LEU C CD2 1 
ATOM   5538  N N   . VAL C  1 210 ? 33.525  45.175 95.817  1.00 53.34  ? 210  VAL C N   1 
ATOM   5539  C CA  . VAL C  1 210 ? 32.814  44.752 97.025  1.00 55.26  ? 210  VAL C CA  1 
ATOM   5540  C C   . VAL C  1 210 ? 31.796  43.664 96.652  1.00 55.24  ? 210  VAL C C   1 
ATOM   5541  O O   . VAL C  1 210 ? 31.175  43.738 95.589  1.00 53.94  ? 210  VAL C O   1 
ATOM   5542  C CB  . VAL C  1 210 ? 32.111  45.934 97.745  1.00 56.30  ? 210  VAL C CB  1 
ATOM   5543  C CG1 . VAL C  1 210 ? 33.130  46.991 98.150  1.00 56.57  ? 210  VAL C CG1 1 
ATOM   5544  C CG2 . VAL C  1 210 ? 31.015  46.555 96.885  1.00 55.37  ? 210  VAL C CG2 1 
ATOM   5545  N N   . PRO C  1 211 ? 31.633  42.639 97.512  1.00 56.88  ? 211  PRO C N   1 
ATOM   5546  C CA  . PRO C  1 211 ? 30.658  41.595 97.180  1.00 57.08  ? 211  PRO C CA  1 
ATOM   5547  C C   . PRO C  1 211 ? 29.208  42.061 97.324  1.00 57.76  ? 211  PRO C C   1 
ATOM   5548  O O   . PRO C  1 211 ? 28.849  42.692 98.322  1.00 59.26  ? 211  PRO C O   1 
ATOM   5549  C CB  . PRO C  1 211 ? 30.959  40.479 98.193  1.00 58.96  ? 211  PRO C CB  1 
ATOM   5550  C CG  . PRO C  1 211 ? 32.296  40.804 98.764  1.00 59.35  ? 211  PRO C CG  1 
ATOM   5551  C CD  . PRO C  1 211 ? 32.413  42.295 98.713  1.00 58.64  ? 211  PRO C CD  1 
ATOM   5552  N N   . ARG C  1 212 ? 28.400  41.748 96.317  1.00 56.83  ? 212  ARG C N   1 
ATOM   5553  C CA  . ARG C  1 212 ? 26.974  42.066 96.309  1.00 57.54  ? 212  ARG C CA  1 
ATOM   5554  C C   . ARG C  1 212 ? 26.169  40.811 96.645  1.00 58.96  ? 212  ARG C C   1 
ATOM   5555  O O   . ARG C  1 212 ? 26.250  39.804 95.939  1.00 58.29  ? 212  ARG C O   1 
ATOM   5556  C CB  . ARG C  1 212 ? 26.556  42.606 94.936  1.00 55.78  ? 212  ARG C CB  1 
ATOM   5557  C CG  . ARG C  1 212 ? 27.398  43.778 94.442  1.00 54.43  ? 212  ARG C CG  1 
ATOM   5558  C CD  . ARG C  1 212 ? 26.839  44.391 93.163  1.00 53.13  ? 212  ARG C CD  1 
ATOM   5559  N NE  . ARG C  1 212 ? 26.530  43.389 92.139  1.00 52.27  ? 212  ARG C NE  1 
ATOM   5560  C CZ  . ARG C  1 212 ? 27.401  42.880 91.265  1.00 50.89  ? 212  ARG C CZ  1 
ATOM   5561  N NH1 . ARG C  1 212 ? 28.678  43.259 91.254  1.00 50.16  ? 212  ARG C NH1 1 
ATOM   5562  N NH2 . ARG C  1 212 ? 26.989  41.974 90.385  1.00 50.36  ? 212  ARG C NH2 1 
ATOM   5563  N N   . ILE C  1 213 ? 25.393  40.877 97.723  1.00 61.09  ? 213  ILE C N   1 
ATOM   5564  C CA  . ILE C  1 213 ? 24.590  39.740 98.176  1.00 62.87  ? 213  ILE C CA  1 
ATOM   5565  C C   . ILE C  1 213 ? 23.183  39.815 97.583  1.00 63.04  ? 213  ILE C C   1 
ATOM   5566  O O   . ILE C  1 213 ? 22.576  40.886 97.538  1.00 63.05  ? 213  ILE C O   1 
ATOM   5567  C CB  . ILE C  1 213 ? 24.521  39.679 99.717  1.00 65.46  ? 213  ILE C CB  1 
ATOM   5568  C CG1 . ILE C  1 213 ? 25.918  39.427 100.287 1.00 65.58  ? 213  ILE C CG1 1 
ATOM   5569  C CG2 . ILE C  1 213 ? 23.617  38.550 100.195 1.00 67.57  ? 213  ILE C CG2 1 
ATOM   5570  C CD1 . ILE C  1 213 ? 26.086  39.934 101.698 1.00 67.71  ? 213  ILE C CD1 1 
ATOM   5571  N N   . ALA C  1 214 ? 22.683  38.670 97.124  1.00 63.32  ? 214  ALA C N   1 
ATOM   5572  C CA  . ALA C  1 214 ? 21.328  38.569 96.585  1.00 63.80  ? 214  ALA C CA  1 
ATOM   5573  C C   . ALA C  1 214 ? 20.874  37.114 96.524  1.00 64.92  ? 214  ALA C C   1 
ATOM   5574  O O   . ALA C  1 214 ? 21.694  36.199 96.410  1.00 64.51  ? 214  ALA C O   1 
ATOM   5575  C CB  . ALA C  1 214 ? 21.260  39.195 95.200  1.00 61.58  ? 214  ALA C CB  1 
ATOM   5576  N N   . THR C  1 215 ? 19.563  36.911 96.612  1.00 66.55  ? 215  THR C N   1 
ATOM   5577  C CA  . THR C  1 215 ? 18.973  35.588 96.448  1.00 67.73  ? 215  THR C CA  1 
ATOM   5578  C C   . THR C  1 215 ? 18.873  35.313 94.956  1.00 65.76  ? 215  THR C C   1 
ATOM   5579  O O   . THR C  1 215 ? 18.167  36.020 94.239  1.00 65.09  ? 215  THR C O   1 
ATOM   5580  C CB  . THR C  1 215 ? 17.572  35.503 97.089  1.00 70.42  ? 215  THR C CB  1 
ATOM   5581  O OG1 . THR C  1 215 ? 17.632  35.963 98.445  1.00 72.23  ? 215  THR C OG1 1 
ATOM   5582  C CG2 . THR C  1 215 ? 17.043  34.066 97.061  1.00 72.04  ? 215  THR C CG2 1 
ATOM   5583  N N   . ARG C  1 216 ? 19.589  34.296 94.492  1.00 64.99  ? 216  ARG C N   1 
ATOM   5584  C CA  . ARG C  1 216 ? 19.685  34.013 93.063  1.00 63.08  ? 216  ARG C CA  1 
ATOM   5585  C C   . ARG C  1 216 ? 19.232  32.592 92.761  1.00 64.21  ? 216  ARG C C   1 
ATOM   5586  O O   . ARG C  1 216 ? 19.247  31.725 93.636  1.00 66.11  ? 216  ARG C O   1 
ATOM   5587  C CB  . ARG C  1 216 ? 21.124  34.216 92.587  1.00 60.85  ? 216  ARG C CB  1 
ATOM   5588  C CG  . ARG C  1 216 ? 21.661  35.619 92.823  1.00 59.74  ? 216  ARG C CG  1 
ATOM   5589  C CD  . ARG C  1 216 ? 23.158  35.692 92.573  1.00 58.08  ? 216  ARG C CD  1 
ATOM   5590  N NE  . ARG C  1 216 ? 23.940  35.215 93.718  1.00 59.31  ? 216  ARG C NE  1 
ATOM   5591  C CZ  . ARG C  1 216 ? 24.475  35.986 94.671  1.00 59.74  ? 216  ARG C CZ  1 
ATOM   5592  N NH1 . ARG C  1 216 ? 24.337  37.311 94.661  1.00 59.05  ? 216  ARG C NH1 1 
ATOM   5593  N NH2 . ARG C  1 216 ? 25.165  35.424 95.654  1.00 61.05  ? 216  ARG C NH2 1 
ATOM   5594  N N   . SER C  1 217 ? 18.825  32.368 91.515  1.00 63.19  ? 217  SER C N   1 
ATOM   5595  C CA  . SER C  1 217 ? 18.421  31.044 91.057  1.00 64.13  ? 217  SER C CA  1 
ATOM   5596  C C   . SER C  1 217 ? 19.643  30.139 90.950  1.00 63.51  ? 217  SER C C   1 
ATOM   5597  O O   . SER C  1 217 ? 20.756  30.610 90.713  1.00 61.67  ? 217  SER C O   1 
ATOM   5598  C CB  . SER C  1 217 ? 17.720  31.138 89.701  1.00 63.16  ? 217  SER C CB  1 
ATOM   5599  O OG  . SER C  1 217 ? 16.719  32.142 89.719  1.00 63.58  ? 217  SER C OG  1 
ATOM   5600  N N   . LYS C  1 218 ? 19.434  28.841 91.140  1.00 65.26  ? 218  LYS C N   1 
ATOM   5601  C CA  . LYS C  1 218 ? 20.520  27.878 91.029  1.00 65.06  ? 218  LYS C CA  1 
ATOM   5602  C C   . LYS C  1 218 ? 20.907  27.700 89.570  1.00 62.95  ? 218  LYS C C   1 
ATOM   5603  O O   . LYS C  1 218 ? 20.077  27.348 88.736  1.00 63.12  ? 218  LYS C O   1 
ATOM   5604  C CB  . LYS C  1 218 ? 20.137  26.524 91.630  1.00 67.87  ? 218  LYS C CB  1 
ATOM   5605  C CG  . LYS C  1 218 ? 20.398  26.412 93.123  1.00 70.02  ? 218  LYS C CG  1 
ATOM   5606  C CD  . LYS C  1 218 ? 20.145  24.993 93.610  1.00 72.88  ? 218  LYS C CD  1 
ATOM   5607  C CE  . LYS C  1 218 ? 20.282  24.872 95.121  1.00 75.42  ? 218  LYS C CE  1 
ATOM   5608  N NZ  . LYS C  1 218 ? 19.110  25.436 95.846  1.00 77.09  ? 218  LYS C NZ  1 
ATOM   5609  N N   . VAL C  1 219 ? 22.170  27.977 89.274  1.00 61.10  ? 219  VAL C N   1 
ATOM   5610  C CA  . VAL C  1 219 ? 22.753  27.682 87.979  1.00 59.33  ? 219  VAL C CA  1 
ATOM   5611  C C   . VAL C  1 219 ? 23.883  26.695 88.242  1.00 59.77  ? 219  VAL C C   1 
ATOM   5612  O O   . VAL C  1 219 ? 24.719  26.930 89.113  1.00 59.96  ? 219  VAL C O   1 
ATOM   5613  C CB  . VAL C  1 219 ? 23.273  28.969 87.314  1.00 56.93  ? 219  VAL C CB  1 
ATOM   5614  C CG1 . VAL C  1 219 ? 24.026  28.656 86.026  1.00 55.34  ? 219  VAL C CG1 1 
ATOM   5615  C CG2 . VAL C  1 219 ? 22.115  29.922 87.042  1.00 56.73  ? 219  VAL C CG2 1 
ATOM   5616  N N   . ASN C  1 220 ? 23.894  25.580 87.515  1.00 60.15  ? 220  ASN C N   1 
ATOM   5617  C CA  . ASN C  1 220 ? 24.832  24.480 87.786  1.00 61.11  ? 220  ASN C CA  1 
ATOM   5618  C C   . ASN C  1 220 ? 24.814  24.029 89.255  1.00 63.43  ? 220  ASN C C   1 
ATOM   5619  O O   . ASN C  1 220 ? 25.853  23.690 89.827  1.00 63.97  ? 220  ASN C O   1 
ATOM   5620  C CB  . ASN C  1 220 ? 26.260  24.858 87.353  1.00 59.32  ? 220  ASN C CB  1 
ATOM   5621  C CG  . ASN C  1 220 ? 26.507  24.626 85.873  1.00 57.86  ? 220  ASN C CG  1 
ATOM   5622  O OD1 . ASN C  1 220 ? 25.576  24.612 85.063  1.00 57.59  ? 220  ASN C OD1 1 
ATOM   5623  N ND2 . ASN C  1 220 ? 27.773  24.441 85.511  1.00 57.10  ? 220  ASN C ND2 1 
ATOM   5624  N N   . GLY C  1 221 ? 23.623  24.031 89.852  1.00 64.98  ? 221  GLY C N   1 
ATOM   5625  C CA  . GLY C  1 221 ? 23.437  23.581 91.230  1.00 67.56  ? 221  GLY C CA  1 
ATOM   5626  C C   . GLY C  1 221 ? 23.913  24.543 92.305  1.00 67.47  ? 221  GLY C C   1 
ATOM   5627  O O   . GLY C  1 221 ? 23.998  24.165 93.473  1.00 69.66  ? 221  GLY C O   1 
ATOM   5628  N N   . GLN C  1 222 ? 24.216  25.783 91.924  1.00 65.14  ? 222  GLN C N   1 
ATOM   5629  C CA  . GLN C  1 222 ? 24.702  26.789 92.870  1.00 64.97  ? 222  GLN C CA  1 
ATOM   5630  C C   . GLN C  1 222 ? 24.054  28.143 92.613  1.00 63.45  ? 222  GLN C C   1 
ATOM   5631  O O   . GLN C  1 222 ? 23.878  28.547 91.464  1.00 61.56  ? 222  GLN C O   1 
ATOM   5632  C CB  . GLN C  1 222 ? 26.227  26.924 92.780  1.00 63.81  ? 222  GLN C CB  1 
ATOM   5633  C CG  . GLN C  1 222 ? 27.001  25.658 93.139  1.00 65.53  ? 222  GLN C CG  1 
ATOM   5634  C CD  . GLN C  1 222 ? 26.721  25.164 94.552  1.00 68.58  ? 222  GLN C CD  1 
ATOM   5635  O OE1 . GLN C  1 222 ? 26.480  25.953 95.464  1.00 69.12  ? 222  GLN C OE1 1 
ATOM   5636  N NE2 . GLN C  1 222 ? 26.759  23.849 94.738  1.00 70.70  ? 222  GLN C NE2 1 
ATOM   5637  N N   . SER C  1 223 ? 23.704  28.835 93.695  1.00 64.46  ? 223  SER C N   1 
ATOM   5638  C CA  . SER C  1 223 ? 23.107  30.170 93.619  1.00 63.41  ? 223  SER C CA  1 
ATOM   5639  C C   . SER C  1 223 ? 24.122  31.280 93.931  1.00 61.99  ? 223  SER C C   1 
ATOM   5640  O O   . SER C  1 223 ? 23.789  32.464 93.865  1.00 61.10  ? 223  SER C O   1 
ATOM   5641  C CB  . SER C  1 223 ? 21.898  30.255 94.554  1.00 65.72  ? 223  SER C CB  1 
ATOM   5642  O OG  . SER C  1 223 ? 20.797  29.546 94.014  1.00 66.62  ? 223  SER C OG  1 
ATOM   5643  N N   . GLY C  1 224 ? 25.354  30.894 94.263  1.00 61.93  ? 224  GLY C N   1 
ATOM   5644  C CA  . GLY C  1 224 ? 26.459  31.842 94.408  1.00 60.56  ? 224  GLY C CA  1 
ATOM   5645  C C   . GLY C  1 224 ? 27.012  32.244 93.052  1.00 57.94  ? 224  GLY C C   1 
ATOM   5646  O O   . GLY C  1 224 ? 26.813  31.535 92.058  1.00 57.31  ? 224  GLY C O   1 
ATOM   5647  N N   . ARG C  1 225 ? 27.712  33.378 93.009  1.00 56.56  ? 225  ARG C N   1 
ATOM   5648  C CA  . ARG C  1 225 ? 28.259  33.907 91.753  1.00 54.23  ? 225  ARG C CA  1 
ATOM   5649  C C   . ARG C  1 225 ? 29.736  34.282 91.865  1.00 53.46  ? 225  ARG C C   1 
ATOM   5650  O O   . ARG C  1 225 ? 30.216  34.661 92.934  1.00 54.42  ? 225  ARG C O   1 
ATOM   5651  C CB  . ARG C  1 225 ? 27.462  35.134 91.296  1.00 53.21  ? 225  ARG C CB  1 
ATOM   5652  C CG  . ARG C  1 225 ? 25.998  34.862 90.986  1.00 53.85  ? 225  ARG C CG  1 
ATOM   5653  C CD  . ARG C  1 225 ? 25.822  34.088 89.691  1.00 52.96  ? 225  ARG C CD  1 
ATOM   5654  N NE  . ARG C  1 225 ? 24.407  33.897 89.361  1.00 53.67  ? 225  ARG C NE  1 
ATOM   5655  C CZ  . ARG C  1 225 ? 23.661  32.844 89.711  1.00 55.36  ? 225  ARG C CZ  1 
ATOM   5656  N NH1 . ARG C  1 225 ? 24.169  31.835 90.418  1.00 56.60  ? 225  ARG C NH1 1 
ATOM   5657  N NH2 . ARG C  1 225 ? 22.384  32.800 89.345  1.00 56.00  ? 225  ARG C NH2 1 
ATOM   5658  N N   . MET C  1 226 ? 30.443  34.173 90.743  1.00 51.88  ? 226  MET C N   1 
ATOM   5659  C CA  . MET C  1 226 ? 31.834  34.595 90.639  1.00 51.07  ? 226  MET C CA  1 
ATOM   5660  C C   . MET C  1 226 ? 31.945  35.618 89.521  1.00 49.07  ? 226  MET C C   1 
ATOM   5661  O O   . MET C  1 226 ? 31.485  35.371 88.410  1.00 48.18  ? 226  MET C O   1 
ATOM   5662  C CB  . MET C  1 226 ? 32.730  33.399 90.321  1.00 51.42  ? 226  MET C CB  1 
ATOM   5663  C CG  . MET C  1 226 ? 32.893  32.420 91.471  1.00 53.60  ? 226  MET C CG  1 
ATOM   5664  S SD  . MET C  1 226 ? 34.111  32.948 92.690  1.00 54.66  ? 226  MET C SD  1 
ATOM   5665  C CE  . MET C  1 226 ? 34.106  31.530 93.780  1.00 57.43  ? 226  MET C CE  1 
ATOM   5666  N N   . GLU C  1 227 ? 32.560  36.761 89.808  1.00 48.53  ? 227  GLU C N   1 
ATOM   5667  C CA  . GLU C  1 227 ? 32.722  37.812 88.808  1.00 46.86  ? 227  GLU C CA  1 
ATOM   5668  C C   . GLU C  1 227 ? 34.203  37.997 88.507  1.00 46.24  ? 227  GLU C C   1 
ATOM   5669  O O   . GLU C  1 227 ? 34.972  38.415 89.372  1.00 46.88  ? 227  GLU C O   1 
ATOM   5670  C CB  . GLU C  1 227 ? 32.092  39.113 89.303  1.00 46.93  ? 227  GLU C CB  1 
ATOM   5671  C CG  . GLU C  1 227 ? 31.748  40.091 88.194  1.00 45.59  ? 227  GLU C CG  1 
ATOM   5672  C CD  . GLU C  1 227 ? 30.922  41.267 88.678  1.00 45.96  ? 227  GLU C CD  1 
ATOM   5673  O OE1 . GLU C  1 227 ? 30.496  41.270 89.855  1.00 47.24  ? 227  GLU C OE1 1 
ATOM   5674  O OE2 . GLU C  1 227 ? 30.695  42.195 87.872  1.00 45.12  ? 227  GLU C OE2 1 
ATOM   5675  N N   . PHE C  1 228 ? 34.600  37.678 87.277  1.00 45.14  ? 228  PHE C N   1 
ATOM   5676  C CA  . PHE C  1 228 ? 36.013  37.651 86.911  1.00 44.79  ? 228  PHE C CA  1 
ATOM   5677  C C   . PHE C  1 228 ? 36.436  38.910 86.167  1.00 43.62  ? 228  PHE C C   1 
ATOM   5678  O O   . PHE C  1 228 ? 35.728  39.393 85.285  1.00 42.72  ? 228  PHE C O   1 
ATOM   5679  C CB  . PHE C  1 228 ? 36.323  36.400 86.093  1.00 44.70  ? 228  PHE C CB  1 
ATOM   5680  C CG  . PHE C  1 228 ? 36.169  35.131 86.876  1.00 46.10  ? 228  PHE C CG  1 
ATOM   5681  C CD1 . PHE C  1 228 ? 37.201  34.672 87.683  1.00 47.28  ? 228  PHE C CD1 1 
ATOM   5682  C CD2 . PHE C  1 228 ? 34.981  34.412 86.835  1.00 46.47  ? 228  PHE C CD2 1 
ATOM   5683  C CE1 . PHE C  1 228 ? 37.060  33.507 88.420  1.00 48.82  ? 228  PHE C CE1 1 
ATOM   5684  C CE2 . PHE C  1 228 ? 34.832  33.247 87.571  1.00 47.99  ? 228  PHE C CE2 1 
ATOM   5685  C CZ  . PHE C  1 228 ? 35.874  32.793 88.363  1.00 49.18  ? 228  PHE C CZ  1 
ATOM   5686  N N   . PHE C  1 229 ? 37.596  39.435 86.555  1.00 43.86  ? 229  PHE C N   1 
ATOM   5687  C CA  . PHE C  1 229 ? 38.145  40.662 85.994  1.00 43.10  ? 229  PHE C CA  1 
ATOM   5688  C C   . PHE C  1 229 ? 39.548  40.403 85.459  1.00 43.07  ? 229  PHE C C   1 
ATOM   5689  O O   . PHE C  1 229 ? 40.191  39.414 85.822  1.00 43.82  ? 229  PHE C O   1 
ATOM   5690  C CB  . PHE C  1 229 ? 38.189  41.756 87.058  1.00 43.69  ? 229  PHE C CB  1 
ATOM   5691  C CG  . PHE C  1 229 ? 36.831  42.207 87.516  1.00 43.81  ? 229  PHE C CG  1 
ATOM   5692  C CD1 . PHE C  1 229 ? 36.104  41.448 88.427  1.00 44.74  ? 229  PHE C CD1 1 
ATOM   5693  C CD2 . PHE C  1 229 ? 36.281  43.393 87.045  1.00 43.22  ? 229  PHE C CD2 1 
ATOM   5694  C CE1 . PHE C  1 229 ? 34.851  41.860 88.855  1.00 45.05  ? 229  PHE C CE1 1 
ATOM   5695  C CE2 . PHE C  1 229 ? 35.032  43.813 87.471  1.00 43.52  ? 229  PHE C CE2 1 
ATOM   5696  C CZ  . PHE C  1 229 ? 34.314  43.045 88.376  1.00 44.44  ? 229  PHE C CZ  1 
ATOM   5697  N N   . TRP C  1 230 ? 40.012  41.296 84.591  1.00 42.36  ? 230  TRP C N   1 
ATOM   5698  C CA  . TRP C  1 230 ? 41.308  41.133 83.952  1.00 42.42  ? 230  TRP C CA  1 
ATOM   5699  C C   . TRP C  1 230 ? 41.980  42.462 83.662  1.00 42.28  ? 230  TRP C C   1 
ATOM   5700  O O   . TRP C  1 230 ? 41.335  43.508 83.645  1.00 41.87  ? 230  TRP C O   1 
ATOM   5701  C CB  . TRP C  1 230 ? 41.151  40.345 82.654  1.00 41.78  ? 230  TRP C CB  1 
ATOM   5702  C CG  . TRP C  1 230 ? 40.295  41.017 81.615  1.00 40.79  ? 230  TRP C CG  1 
ATOM   5703  C CD1 . TRP C  1 230 ? 38.947  40.877 81.449  1.00 40.34  ? 230  TRP C CD1 1 
ATOM   5704  C CD2 . TRP C  1 230 ? 40.734  41.918 80.591  1.00 40.36  ? 230  TRP C CD2 1 
ATOM   5705  N NE1 . TRP C  1 230 ? 38.516  41.637 80.390  1.00 39.67  ? 230  TRP C NE1 1 
ATOM   5706  C CE2 . TRP C  1 230 ? 39.592  42.289 79.846  1.00 39.69  ? 230  TRP C CE2 1 
ATOM   5707  C CE3 . TRP C  1 230 ? 41.979  42.452 80.233  1.00 40.67  ? 230  TRP C CE3 1 
ATOM   5708  C CZ2 . TRP C  1 230 ? 39.659  43.167 78.758  1.00 39.36  ? 230  TRP C CZ2 1 
ATOM   5709  C CZ3 . TRP C  1 230 ? 42.044  43.327 79.152  1.00 40.33  ? 230  TRP C CZ3 1 
ATOM   5710  C CH2 . TRP C  1 230 ? 40.892  43.674 78.428  1.00 39.70  ? 230  TRP C CH2 1 
ATOM   5711  N N   . THR C  1 231 ? 43.288  42.400 83.442  1.00 42.79  ? 231  THR C N   1 
ATOM   5712  C CA  . THR C  1 231 ? 44.055  43.553 82.997  1.00 42.85  ? 231  THR C CA  1 
ATOM   5713  C C   . THR C  1 231 ? 45.274  43.089 82.208  1.00 43.27  ? 231  THR C C   1 
ATOM   5714  O O   . THR C  1 231 ? 45.662  41.922 82.282  1.00 43.70  ? 231  THR C O   1 
ATOM   5715  C CB  . THR C  1 231 ? 44.509  44.420 84.187  1.00 43.73  ? 231  THR C CB  1 
ATOM   5716  O OG1 . THR C  1 231 ? 44.990  45.681 83.711  1.00 43.76  ? 231  THR C OG1 1 
ATOM   5717  C CG2 . THR C  1 231 ? 45.608  43.729 84.991  1.00 44.98  ? 231  THR C CG2 1 
ATOM   5718  N N   . ILE C  1 232 ? 45.861  44.002 81.442  1.00 43.33  ? 232  ILE C N   1 
ATOM   5719  C CA  . ILE C  1 232 ? 47.164  43.768 80.829  1.00 44.10  ? 232  ILE C CA  1 
ATOM   5720  C C   . ILE C  1 232 ? 48.191  44.529 81.656  1.00 45.30  ? 232  ILE C C   1 
ATOM   5721  O O   . ILE C  1 232 ? 48.131  45.754 81.764  1.00 45.35  ? 232  ILE C O   1 
ATOM   5722  C CB  . ILE C  1 232 ? 47.202  44.182 79.337  1.00 43.62  ? 232  ILE C CB  1 
ATOM   5723  C CG1 . ILE C  1 232 ? 46.829  42.996 78.443  1.00 43.10  ? 232  ILE C CG1 1 
ATOM   5724  C CG2 . ILE C  1 232 ? 48.591  44.651 78.918  1.00 44.70  ? 232  ILE C CG2 1 
ATOM   5725  C CD1 . ILE C  1 232 ? 45.520  42.329 78.797  1.00 42.26  ? 232  ILE C CD1 1 
ATOM   5726  N N   . LEU C  1 233 ? 49.118  43.788 82.252  1.00 46.46  ? 233  LEU C N   1 
ATOM   5727  C CA  . LEU C  1 233 ? 50.174  44.372 83.062  1.00 47.87  ? 233  LEU C CA  1 
ATOM   5728  C C   . LEU C  1 233 ? 51.395  44.593 82.177  1.00 48.72  ? 233  LEU C C   1 
ATOM   5729  O O   . LEU C  1 233 ? 51.980  43.636 81.666  1.00 49.19  ? 233  LEU C O   1 
ATOM   5730  C CB  . LEU C  1 233 ? 50.509  43.447 84.238  1.00 48.94  ? 233  LEU C CB  1 
ATOM   5731  C CG  . LEU C  1 233 ? 51.484  43.958 85.303  1.00 50.58  ? 233  LEU C CG  1 
ATOM   5732  C CD1 . LEU C  1 233 ? 50.931  45.180 86.024  1.00 50.38  ? 233  LEU C CD1 1 
ATOM   5733  C CD2 . LEU C  1 233 ? 51.798  42.846 86.294  1.00 51.80  ? 233  LEU C CD2 1 
ATOM   5734  N N   . LYS C  1 234 ? 51.770  45.854 81.993  1.00 63.64  ? 234  LYS C N   1 
ATOM   5735  C CA  . LYS C  1 234 ? 52.884  46.200 81.118  1.00 65.15  ? 234  LYS C CA  1 
ATOM   5736  C C   . LYS C  1 234 ? 54.215  45.876 81.793  1.00 66.85  ? 234  LYS C C   1 
ATOM   5737  O O   . LYS C  1 234 ? 54.269  45.753 83.019  1.00 66.77  ? 234  LYS C O   1 
ATOM   5738  C CB  . LYS C  1 234 ? 52.807  47.677 80.728  1.00 65.35  ? 234  LYS C CB  1 
ATOM   5739  C CG  . LYS C  1 234 ? 51.534  48.015 79.966  1.00 64.01  ? 234  LYS C CG  1 
ATOM   5740  C CD  . LYS C  1 234 ? 51.589  49.383 79.312  1.00 64.75  ? 234  LYS C CD  1 
ATOM   5741  C CE  . LYS C  1 234 ? 50.416  49.571 78.360  1.00 63.69  ? 234  LYS C CE  1 
ATOM   5742  N NZ  . LYS C  1 234 ? 50.514  50.833 77.576  1.00 64.78  ? 234  LYS C NZ  1 
ATOM   5743  N N   . PRO C  1 235 ? 55.296  45.722 80.999  1.00 68.60  ? 235  PRO C N   1 
ATOM   5744  C CA  . PRO C  1 235 ? 56.577  45.357 81.609  1.00 70.43  ? 235  PRO C CA  1 
ATOM   5745  C C   . PRO C  1 235 ? 57.077  46.416 82.585  1.00 70.96  ? 235  PRO C C   1 
ATOM   5746  O O   . PRO C  1 235 ? 56.837  47.609 82.378  1.00 70.75  ? 235  PRO C O   1 
ATOM   5747  C CB  . PRO C  1 235 ? 57.540  45.240 80.414  1.00 72.31  ? 235  PRO C CB  1 
ATOM   5748  C CG  . PRO C  1 235 ? 56.705  45.285 79.186  1.00 71.38  ? 235  PRO C CG  1 
ATOM   5749  C CD  . PRO C  1 235 ? 55.414  45.950 79.547  1.00 69.20  ? 235  PRO C CD  1 
ATOM   5750  N N   . ASN C  1 236 ? 57.751  45.972 83.644  1.00 71.82  ? 236  ASN C N   1 
ATOM   5751  C CA  . ASN C  1 236 ? 58.343  46.870 84.630  1.00 72.53  ? 236  ASN C CA  1 
ATOM   5752  C C   . ASN C  1 236 ? 57.286  47.576 85.490  1.00 70.87  ? 236  ASN C C   1 
ATOM   5753  O O   . ASN C  1 236 ? 57.597  48.547 86.180  1.00 71.37  ? 236  ASN C O   1 
ATOM   5754  C CB  . ASN C  1 236 ? 59.247  47.902 83.926  1.00 74.21  ? 236  ASN C CB  1 
ATOM   5755  C CG  . ASN C  1 236 ? 60.604  48.061 84.591  1.00 76.28  ? 236  ASN C CG  1 
ATOM   5756  O OD1 . ASN C  1 236 ? 60.853  47.540 85.676  1.00 76.53  ? 236  ASN C OD1 1 
ATOM   5757  N ND2 . ASN C  1 236 ? 61.499  48.782 83.925  1.00 78.12  ? 236  ASN C ND2 1 
ATOM   5758  N N   . ASP C  1 237 ? 56.047  47.082 85.450  1.00 69.15  ? 237  ASP C N   1 
ATOM   5759  C CA  . ASP C  1 237 ? 54.952  47.623 86.257  1.00 67.75  ? 237  ASP C CA  1 
ATOM   5760  C C   . ASP C  1 237 ? 54.497  46.556 87.247  1.00 67.23  ? 237  ASP C C   1 
ATOM   5761  O O   . ASP C  1 237 ? 54.528  45.360 86.946  1.00 67.32  ? 237  ASP C O   1 
ATOM   5762  C CB  . ASP C  1 237 ? 53.780  48.054 85.364  1.00 66.43  ? 237  ASP C CB  1 
ATOM   5763  C CG  . ASP C  1 237 ? 52.685  48.799 86.133  1.00 65.44  ? 237  ASP C CG  1 
ATOM   5764  O OD1 . ASP C  1 237 ? 52.980  49.418 87.179  1.00 65.99  ? 237  ASP C OD1 1 
ATOM   5765  O OD2 . ASP C  1 237 ? 51.518  48.771 85.681  1.00 64.24  ? 237  ASP C OD2 1 
ATOM   5766  N N   . ALA C  1 238 ? 54.074  46.999 88.427  1.00 66.90  ? 238  ALA C N   1 
ATOM   5767  C CA  . ALA C  1 238 ? 53.633  46.098 89.482  1.00 66.72  ? 238  ALA C CA  1 
ATOM   5768  C C   . ALA C  1 238 ? 52.115  46.157 89.654  1.00 65.33  ? 238  ALA C C   1 
ATOM   5769  O O   . ALA C  1 238 ? 51.509  47.226 89.538  1.00 64.74  ? 238  ALA C O   1 
ATOM   5770  C CB  . ALA C  1 238 ? 54.326  46.447 90.788  1.00 67.71  ? 238  ALA C CB  1 
ATOM   5771  N N   . ILE C  1 239 ? 51.511  45.000 89.915  1.00 65.03  ? 239  ILE C N   1 
ATOM   5772  C CA  . ILE C  1 239 ? 50.099  44.925 90.302  1.00 64.09  ? 239  ILE C CA  1 
ATOM   5773  C C   . ILE C  1 239 ? 50.009  44.657 91.809  1.00 64.88  ? 239  ILE C C   1 
ATOM   5774  O O   . ILE C  1 239 ? 50.757  43.836 92.339  1.00 65.94  ? 239  ILE C O   1 
ATOM   5775  C CB  . ILE C  1 239 ? 49.318  43.858 89.493  1.00 63.36  ? 239  ILE C CB  1 
ATOM   5776  C CG1 . ILE C  1 239 ? 47.818  43.947 89.799  1.00 62.52  ? 239  ILE C CG1 1 
ATOM   5777  C CG2 . ILE C  1 239 ? 49.836  42.447 89.762  1.00 64.37  ? 239  ILE C CG2 1 
ATOM   5778  C CD1 . ILE C  1 239 ? 46.941  43.254 88.778  1.00 61.60  ? 239  ILE C CD1 1 
ATOM   5779  N N   . ASN C  1 240 ? 49.107  45.361 92.492  1.00 64.57  ? 240  ASN C N   1 
ATOM   5780  C CA  . ASN C  1 240 ? 48.957  45.245 93.944  1.00 65.49  ? 240  ASN C CA  1 
ATOM   5781  C C   . ASN C  1 240 ? 47.543  44.836 94.343  1.00 65.24  ? 240  ASN C C   1 
ATOM   5782  O O   . ASN C  1 240 ? 46.572  45.481 93.949  1.00 64.43  ? 240  ASN C O   1 
ATOM   5783  C CB  . ASN C  1 240 ? 49.288  46.572 94.623  1.00 65.94  ? 240  ASN C CB  1 
ATOM   5784  C CG  . ASN C  1 240 ? 50.646  47.114 94.223  1.00 66.31  ? 240  ASN C CG  1 
ATOM   5785  O OD1 . ASN C  1 240 ? 51.673  46.489 94.481  1.00 67.17  ? 240  ASN C OD1 1 
ATOM   5786  N ND2 . ASN C  1 240 ? 50.660  48.292 93.603  1.00 65.96  ? 240  ASN C ND2 1 
ATOM   5787  N N   . PHE C  1 241 ? 47.446  43.775 95.141  1.00 66.16  ? 241  PHE C N   1 
ATOM   5788  C CA  . PHE C  1 241 ? 46.172  43.290 95.667  1.00 66.43  ? 241  PHE C CA  1 
ATOM   5789  C C   . PHE C  1 241 ? 46.079  43.546 97.168  1.00 67.79  ? 241  PHE C C   1 
ATOM   5790  O O   . PHE C  1 241 ? 47.047  43.334 97.893  1.00 68.82  ? 241  PHE C O   1 
ATOM   5791  C CB  . PHE C  1 241 ? 46.035  41.790 95.408  1.00 66.85  ? 241  PHE C CB  1 
ATOM   5792  C CG  . PHE C  1 241 ? 45.839  41.442 93.964  1.00 65.58  ? 241  PHE C CG  1 
ATOM   5793  C CD1 . PHE C  1 241 ? 44.568  41.440 93.408  1.00 64.69  ? 241  PHE C CD1 1 
ATOM   5794  C CD2 . PHE C  1 241 ? 46.923  41.119 93.159  1.00 65.45  ? 241  PHE C CD2 1 
ATOM   5795  C CE1 . PHE C  1 241 ? 44.379  41.121 92.074  1.00 63.56  ? 241  PHE C CE1 1 
ATOM   5796  C CE2 . PHE C  1 241 ? 46.742  40.797 91.825  1.00 64.45  ? 241  PHE C CE2 1 
ATOM   5797  C CZ  . PHE C  1 241 ? 45.467  40.798 91.280  1.00 63.44  ? 241  PHE C CZ  1 
ATOM   5798  N N   . GLU C  1 242 ? 44.919  44.014 97.622  1.00 67.94  ? 242  GLU C N   1 
ATOM   5799  C CA  . GLU C  1 242 ? 44.609  44.076 99.050  1.00 69.55  ? 242  GLU C CA  1 
ATOM   5800  C C   . GLU C  1 242 ? 43.164  43.623 99.263  1.00 70.09  ? 242  GLU C C   1 
ATOM   5801  O O   . GLU C  1 242 ? 42.248  44.152 98.628  1.00 69.24  ? 242  GLU C O   1 
ATOM   5802  C CB  . GLU C  1 242 ? 44.825  45.487 99.612  1.00 69.77  ? 242  GLU C CB  1 
ATOM   5803  C CG  . GLU C  1 242 ? 44.699  45.585 101.130 1.00 71.64  ? 242  GLU C CG  1 
ATOM   5804  C CD  . GLU C  1 242 ? 44.845  47.007 101.650 1.00 71.98  ? 242  GLU C CD  1 
ATOM   5805  O OE1 . GLU C  1 242 ? 45.911  47.621 101.437 1.00 71.50  ? 242  GLU C OE1 1 
ATOM   5806  O OE2 . GLU C  1 242 ? 43.898  47.513 102.284 1.00 72.94  ? 242  GLU C OE2 1 
ATOM   5807  N N   . SER C  1 243 ? 42.964  42.641 100.142 1.00 71.70  ? 243  SER C N   1 
ATOM   5808  C CA  . SER C  1 243 ? 41.622  42.113 100.401 1.00 72.61  ? 243  SER C CA  1 
ATOM   5809  C C   . SER C  1 243 ? 41.465  41.490 101.788 1.00 75.11  ? 243  SER C C   1 
ATOM   5810  O O   . SER C  1 243 ? 42.360  40.794 102.273 1.00 76.09  ? 243  SER C O   1 
ATOM   5811  C CB  . SER C  1 243 ? 41.251  41.073 99.345  1.00 71.79  ? 243  SER C CB  1 
ATOM   5812  O OG  . SER C  1 243 ? 39.922  40.617 99.531  1.00 72.70  ? 243  SER C OG  1 
ATOM   5813  N N   . ASN C  1 244 ? 40.308  41.740 102.400 1.00 76.35  ? 244  ASN C N   1 
ATOM   5814  C CA  . ASN C  1 244 ? 39.926  41.129 103.676 1.00 79.07  ? 244  ASN C CA  1 
ATOM   5815  C C   . ASN C  1 244 ? 38.769  40.131 103.518 1.00 80.16  ? 244  ASN C C   1 
ATOM   5816  O O   . ASN C  1 244 ? 38.131  39.758 104.507 1.00 82.63  ? 244  ASN C O   1 
ATOM   5817  C CB  . ASN C  1 244 ? 39.537  42.212 104.690 1.00 80.33  ? 244  ASN C CB  1 
ATOM   5818  C CG  . ASN C  1 244 ? 38.300  42.991 104.269 1.00 79.93  ? 244  ASN C CG  1 
ATOM   5819  O OD1 . ASN C  1 244 ? 38.062  43.195 103.077 1.00 77.89  ? 244  ASN C OD1 1 
ATOM   5820  N ND2 . ASN C  1 244 ? 37.509  43.428 105.243 1.00 82.05  ? 244  ASN C ND2 1 
ATOM   5821  N N   . GLY C  1 245 ? 38.501  39.708 102.282 1.00 78.46  ? 245  GLY C N   1 
ATOM   5822  C CA  . GLY C  1 245 ? 37.443  38.734 102.015 1.00 79.37  ? 245  GLY C CA  1 
ATOM   5823  C C   . GLY C  1 245 ? 37.028  38.598 100.560 1.00 77.16  ? 245  GLY C C   1 
ATOM   5824  O O   . GLY C  1 245 ? 37.158  39.536 99.772  1.00 75.00  ? 245  GLY C O   1 
ATOM   5825  N N   . ASN C  1 246 ? 36.532  37.407 100.223 1.00 77.91  ? 246  ASN C N   1 
ATOM   5826  C CA  . ASN C  1 246 ? 35.863  37.120 98.944  1.00 76.32  ? 246  ASN C CA  1 
ATOM   5827  C C   . ASN C  1 246 ? 36.754  37.199 97.696  1.00 73.75  ? 246  ASN C C   1 
ATOM   5828  O O   . ASN C  1 246 ? 36.264  37.448 96.596  1.00 71.96  ? 246  ASN C O   1 
ATOM   5829  C CB  . ASN C  1 246 ? 34.618  38.010 98.778  1.00 75.94  ? 246  ASN C CB  1 
ATOM   5830  C CG  . ASN C  1 246 ? 33.649  37.882 99.945  1.00 78.80  ? 246  ASN C CG  1 
ATOM   5831  O OD1 . ASN C  1 246 ? 33.929  38.345 101.051 1.00 80.27  ? 246  ASN C OD1 1 
ATOM   5832  N ND2 . ASN C  1 246 ? 32.500  37.258 99.701  1.00 79.74  ? 246  ASN C ND2 1 
ATOM   5833  N N   . PHE C  1 247 ? 38.049  36.938 97.871  1.00 73.83  ? 247  PHE C N   1 
ATOM   5834  C CA  . PHE C  1 247 ? 39.054  37.154 96.822  1.00 71.74  ? 247  PHE C CA  1 
ATOM   5835  C C   . PHE C  1 247 ? 39.450  35.863 96.112  1.00 71.93  ? 247  PHE C C   1 
ATOM   5836  O O   . PHE C  1 247 ? 39.767  34.862 96.752  1.00 73.96  ? 247  PHE C O   1 
ATOM   5837  C CB  . PHE C  1 247 ? 40.293  37.812 97.442  1.00 71.82  ? 247  PHE C CB  1 
ATOM   5838  C CG  . PHE C  1 247 ? 41.428  38.044 96.477  1.00 70.16  ? 247  PHE C CG  1 
ATOM   5839  C CD1 . PHE C  1 247 ? 41.233  38.759 95.304  1.00 68.04  ? 247  PHE C CD1 1 
ATOM   5840  C CD2 . PHE C  1 247 ? 42.706  37.580 96.766  1.00 70.97  ? 247  PHE C CD2 1 
ATOM   5841  C CE1 . PHE C  1 247 ? 42.281  38.985 94.426  1.00 66.83  ? 247  PHE C CE1 1 
ATOM   5842  C CE2 . PHE C  1 247 ? 43.757  37.806 95.895  1.00 69.76  ? 247  PHE C CE2 1 
ATOM   5843  C CZ  . PHE C  1 247 ? 43.545  38.510 94.723  1.00 67.73  ? 247  PHE C CZ  1 
ATOM   5844  N N   . ILE C  1 248 ? 39.432  35.900 94.783  1.00 70.03  ? 248  ILE C N   1 
ATOM   5845  C CA  . ILE C  1 248 ? 39.913  34.792 93.970  1.00 70.12  ? 248  ILE C CA  1 
ATOM   5846  C C   . ILE C  1 248 ? 41.279  35.196 93.418  1.00 69.04  ? 248  ILE C C   1 
ATOM   5847  O O   . ILE C  1 248 ? 41.373  35.986 92.480  1.00 67.08  ? 248  ILE C O   1 
ATOM   5848  C CB  . ILE C  1 248 ? 38.941  34.454 92.819  1.00 68.97  ? 248  ILE C CB  1 
ATOM   5849  C CG1 . ILE C  1 248 ? 37.484  34.415 93.305  1.00 69.76  ? 248  ILE C CG1 1 
ATOM   5850  C CG2 . ILE C  1 248 ? 39.321  33.125 92.187  1.00 69.75  ? 248  ILE C CG2 1 
ATOM   5851  C CD1 . ILE C  1 248 ? 37.157  33.259 94.229  1.00 72.54  ? 248  ILE C CD1 1 
ATOM   5852  N N   . ALA C  1 249 ? 42.336  34.662 94.020  1.00 70.58  ? 249  ALA C N   1 
ATOM   5853  C CA  . ALA C  1 249 ? 43.699  35.083 93.704  1.00 70.04  ? 249  ALA C CA  1 
ATOM   5854  C C   . ALA C  1 249 ? 44.205  34.465 92.402  1.00 69.49  ? 249  ALA C C   1 
ATOM   5855  O O   . ALA C  1 249 ? 43.804  33.360 92.045  1.00 70.32  ? 249  ALA C O   1 
ATOM   5856  C CB  . ALA C  1 249 ? 44.637  34.725 94.850  1.00 72.09  ? 249  ALA C CB  1 
ATOM   5857  N N   . PRO C  1 250 ? 45.084  35.186 91.684  1.00 68.30  ? 250  PRO C N   1 
ATOM   5858  C CA  . PRO C  1 250 ? 45.749  34.616 90.513  1.00 68.23  ? 250  PRO C CA  1 
ATOM   5859  C C   . PRO C  1 250 ? 46.909  33.696 90.882  1.00 70.45  ? 250  PRO C C   1 
ATOM   5860  O O   . PRO C  1 250 ? 47.842  34.132 91.547  1.00 71.13  ? 250  PRO C O   1 
ATOM   5861  C CB  . PRO C  1 250 ? 46.280  35.847 89.772  1.00 66.52  ? 250  PRO C CB  1 
ATOM   5862  C CG  . PRO C  1 250 ? 46.418  36.901 90.807  1.00 66.39  ? 250  PRO C CG  1 
ATOM   5863  C CD  . PRO C  1 250 ? 45.366  36.626 91.838  1.00 67.05  ? 250  PRO C CD  1 
ATOM   5864  N N   . GLU C  1 251 ? 46.839  32.435 90.463  1.00 71.78  ? 251  GLU C N   1 
ATOM   5865  C CA  . GLU C  1 251 ? 47.989  31.529 90.534  1.00 74.04  ? 251  GLU C CA  1 
ATOM   5866  C C   . GLU C  1 251 ? 48.858  31.744 89.298  1.00 73.41  ? 251  GLU C C   1 
ATOM   5867  O O   . GLU C  1 251 ? 50.058  32.018 89.407  1.00 74.17  ? 251  GLU C O   1 
ATOM   5868  C CB  . GLU C  1 251 ? 47.536  30.061 90.627  1.00 76.14  ? 251  GLU C CB  1 
ATOM   5869  C CG  . GLU C  1 251 ? 47.964  29.328 91.891  1.00 78.97  ? 251  GLU C CG  1 
ATOM   5870  C CD  . GLU C  1 251 ? 49.077  28.324 91.647  1.00 81.50  ? 251  GLU C CD  1 
ATOM   5871  O OE1 . GLU C  1 251 ? 48.853  27.367 90.880  1.00 82.43  ? 251  GLU C OE1 1 
ATOM   5872  O OE2 . GLU C  1 251 ? 50.169  28.477 92.233  1.00 82.77  ? 251  GLU C OE2 1 
ATOM   5873  N N   . TYR C  1 252 ? 48.227  31.626 88.129  1.00 72.16  ? 252  TYR C N   1 
ATOM   5874  C CA  . TYR C  1 252 ? 48.897  31.787 86.838  1.00 71.69  ? 252  TYR C CA  1 
ATOM   5875  C C   . TYR C  1 252 ? 48.371  32.992 86.054  1.00 69.05  ? 252  TYR C C   1 
ATOM   5876  O O   . TYR C  1 252 ? 47.192  33.357 86.149  1.00 67.54  ? 252  TYR C O   1 
ATOM   5877  C CB  . TYR C  1 252 ? 48.716  30.529 85.983  1.00 72.84  ? 252  TYR C CB  1 
ATOM   5878  C CG  . TYR C  1 252 ? 49.285  29.276 86.598  1.00 75.88  ? 252  TYR C CG  1 
ATOM   5879  C CD1 . TYR C  1 252 ? 50.621  28.930 86.415  1.00 77.87  ? 252  TYR C CD1 1 
ATOM   5880  C CD2 . TYR C  1 252 ? 48.488  28.431 87.362  1.00 77.08  ? 252  TYR C CD2 1 
ATOM   5881  C CE1 . TYR C  1 252 ? 51.147  27.779 86.981  1.00 80.96  ? 252  TYR C CE1 1 
ATOM   5882  C CE2 . TYR C  1 252 ? 49.004  27.279 87.932  1.00 80.18  ? 252  TYR C CE2 1 
ATOM   5883  C CZ  . TYR C  1 252 ? 50.335  26.957 87.741  1.00 82.11  ? 252  TYR C CZ  1 
ATOM   5884  O OH  . TYR C  1 252 ? 50.848  25.813 88.305  1.00 85.44  ? 252  TYR C OH  1 
ATOM   5885  N N   . ALA C  1 253 ? 49.264  33.597 85.276  1.00 68.79  ? 253  ALA C N   1 
ATOM   5886  C CA  . ALA C  1 253 ? 48.917  34.677 84.362  1.00 66.75  ? 253  ALA C CA  1 
ATOM   5887  C C   . ALA C  1 253 ? 49.556  34.390 83.007  1.00 67.24  ? 253  ALA C C   1 
ATOM   5888  O O   . ALA C  1 253 ? 50.733  34.031 82.937  1.00 69.06  ? 253  ALA C O   1 
ATOM   5889  C CB  . ALA C  1 253 ? 49.404  36.009 84.911  1.00 66.12  ? 253  ALA C CB  1 
ATOM   5890  N N   . TYR C  1 254 ? 48.776  34.539 81.938  1.00 65.81  ? 254  TYR C N   1 
ATOM   5891  C CA  . TYR C  1 254 ? 49.246  34.235 80.589  1.00 66.30  ? 254  TYR C CA  1 
ATOM   5892  C C   . TYR C  1 254 ? 50.169  35.329 80.063  1.00 66.26  ? 254  TYR C C   1 
ATOM   5893  O O   . TYR C  1 254 ? 49.881  36.518 80.196  1.00 64.86  ? 254  TYR C O   1 
ATOM   5894  C CB  . TYR C  1 254 ? 48.066  34.055 79.631  1.00 64.82  ? 254  TYR C CB  1 
ATOM   5895  C CG  . TYR C  1 254 ? 47.281  32.782 79.848  1.00 65.37  ? 254  TYR C CG  1 
ATOM   5896  C CD1 . TYR C  1 254 ? 47.672  31.587 79.246  1.00 67.13  ? 254  TYR C CD1 1 
ATOM   5897  C CD2 . TYR C  1 254 ? 46.143  32.772 80.644  1.00 64.41  ? 254  TYR C CD2 1 
ATOM   5898  C CE1 . TYR C  1 254 ? 46.951  30.418 79.433  1.00 67.89  ? 254  TYR C CE1 1 
ATOM   5899  C CE2 . TYR C  1 254 ? 45.418  31.608 80.840  1.00 65.19  ? 254  TYR C CE2 1 
ATOM   5900  C CZ  . TYR C  1 254 ? 45.824  30.430 80.235  1.00 66.91  ? 254  TYR C CZ  1 
ATOM   5901  O OH  . TYR C  1 254 ? 45.105  29.269 80.433  1.00 67.92  ? 254  TYR C OH  1 
ATOM   5902  N N   . LYS C  1 255 ? 51.267  34.905 79.448  1.00 68.09  ? 255  LYS C N   1 
ATOM   5903  C CA  . LYS C  1 255 ? 52.282  35.807 78.920  1.00 68.67  ? 255  LYS C CA  1 
ATOM   5904  C C   . LYS C  1 255 ? 52.125  35.869 77.404  1.00 68.42  ? 255  LYS C C   1 
ATOM   5905  O O   . LYS C  1 255 ? 52.021  34.832 76.750  1.00 69.27  ? 255  LYS C O   1 
ATOM   5906  C CB  . LYS C  1 255 ? 53.672  35.285 79.302  1.00 71.32  ? 255  LYS C CB  1 
ATOM   5907  C CG  . LYS C  1 255 ? 54.720  36.359 79.532  1.00 71.97  ? 255  LYS C CG  1 
ATOM   5908  C CD  . LYS C  1 255 ? 55.855  35.861 80.423  1.00 74.24  ? 255  LYS C CD  1 
ATOM   5909  C CE  . LYS C  1 255 ? 56.868  35.015 79.667  1.00 76.98  ? 255  LYS C CE  1 
ATOM   5910  N NZ  . LYS C  1 255 ? 58.138  34.880 80.435  1.00 79.33  ? 255  LYS C NZ  1 
ATOM   5911  N N   . ILE C  1 256 ? 52.121  37.080 76.850  1.00 67.46  ? 256  ILE C N   1 
ATOM   5912  C CA  . ILE C  1 256 ? 51.825  37.279 75.427  1.00 67.06  ? 256  ILE C CA  1 
ATOM   5913  C C   . ILE C  1 256 ? 53.125  37.342 74.628  1.00 69.36  ? 256  ILE C C   1 
ATOM   5914  O O   . ILE C  1 256 ? 53.696  38.414 74.428  1.00 69.72  ? 256  ILE C O   1 
ATOM   5915  C CB  . ILE C  1 256 ? 50.995  38.563 75.166  1.00 65.04  ? 256  ILE C CB  1 
ATOM   5916  C CG1 . ILE C  1 256 ? 50.104  38.908 76.369  1.00 63.35  ? 256  ILE C CG1 1 
ATOM   5917  C CG2 . ILE C  1 256 ? 50.174  38.398 73.893  1.00 64.16  ? 256  ILE C CG2 1 
ATOM   5918  C CD1 . ILE C  1 256 ? 49.078  39.990 76.100  1.00 61.49  ? 256  ILE C CD1 1 
ATOM   5919  N N   . VAL C  1 257 ? 53.594  36.185 74.172  1.00 71.17  ? 257  VAL C N   1 
ATOM   5920  C CA  . VAL C  1 257 ? 54.887  36.110 73.483  1.00 73.87  ? 257  VAL C CA  1 
ATOM   5921  C C   . VAL C  1 257 ? 54.810  36.602 72.030  1.00 74.00  ? 257  VAL C C   1 
ATOM   5922  O O   . VAL C  1 257 ? 55.679  37.362 71.588  1.00 75.44  ? 257  VAL C O   1 
ATOM   5923  C CB  . VAL C  1 257 ? 55.531  34.699 73.567  1.00 76.35  ? 257  VAL C CB  1 
ATOM   5924  C CG1 . VAL C  1 257 ? 55.853  34.357 75.015  1.00 76.78  ? 257  VAL C CG1 1 
ATOM   5925  C CG2 . VAL C  1 257 ? 54.650  33.620 72.947  1.00 75.96  ? 257  VAL C CG2 1 
ATOM   5926  N N   . LYS C  1 258 ? 53.771  36.185 71.304  1.00 72.63  ? 258  LYS C N   1 
ATOM   5927  C CA  . LYS C  1 258 ? 53.600  36.570 69.897  1.00 72.73  ? 258  LYS C CA  1 
ATOM   5928  C C   . LYS C  1 258 ? 52.293  37.312 69.639  1.00 69.88  ? 258  LYS C C   1 
ATOM   5929  O O   . LYS C  1 258 ? 51.226  36.872 70.067  1.00 67.96  ? 258  LYS C O   1 
ATOM   5930  C CB  . LYS C  1 258 ? 53.669  35.342 68.979  1.00 74.30  ? 258  LYS C CB  1 
ATOM   5931  C CG  . LYS C  1 258 ? 54.978  35.213 68.209  1.00 77.64  ? 258  LYS C CG  1 
ATOM   5932  C CD  . LYS C  1 258 ? 54.744  34.892 66.738  1.00 78.44  ? 258  LYS C CD  1 
ATOM   5933  C CE  . LYS C  1 258 ? 54.164  33.503 66.529  1.00 78.51  ? 258  LYS C CE  1 
ATOM   5934  N NZ  . LYS C  1 258 ? 54.429  33.029 65.142  1.00 80.57  ? 258  LYS C NZ  1 
ATOM   5935  N N   . LYS C  1 259 ? 52.397  38.434 68.926  1.00 69.88  ? 259  LYS C N   1 
ATOM   5936  C CA  . LYS C  1 259 ? 51.238  39.190 68.455  1.00 67.69  ? 259  LYS C CA  1 
ATOM   5937  C C   . LYS C  1 259 ? 51.198  39.153 66.931  1.00 68.58  ? 259  LYS C C   1 
ATOM   5938  O O   . LYS C  1 259 ? 52.107  39.658 66.274  1.00 70.68  ? 259  LYS C O   1 
ATOM   5939  C CB  . LYS C  1 259 ? 51.316  40.647 68.913  1.00 67.16  ? 259  LYS C CB  1 
ATOM   5940  C CG  . LYS C  1 259 ? 51.341  40.833 70.417  1.00 66.32  ? 259  LYS C CG  1 
ATOM   5941  C CD  . LYS C  1 259 ? 51.353  42.305 70.794  1.00 65.92  ? 259  LYS C CD  1 
ATOM   5942  C CE  . LYS C  1 259 ? 51.431  42.476 72.303  1.00 65.28  ? 259  LYS C CE  1 
ATOM   5943  N NZ  . LYS C  1 259 ? 51.565  43.901 72.715  1.00 65.27  ? 259  LYS C NZ  1 
ATOM   5944  N N   . GLY C  1 260 ? 50.149  38.556 66.373  1.00 67.16  ? 260  GLY C N   1 
ATOM   5945  C CA  . GLY C  1 260 ? 49.991  38.477 64.922  1.00 67.87  ? 260  GLY C CA  1 
ATOM   5946  C C   . GLY C  1 260 ? 48.540  38.535 64.490  1.00 65.44  ? 260  GLY C C   1 
ATOM   5947  O O   . GLY C  1 260 ? 47.644  38.740 65.310  1.00 63.27  ? 260  GLY C O   1 
ATOM   5948  N N   . ASP C  1 261 ? 48.312  38.358 63.194  1.00 65.97  ? 261  ASP C N   1 
ATOM   5949  C CA  . ASP C  1 261 ? 46.956  38.289 62.664  1.00 63.90  ? 261  ASP C CA  1 
ATOM   5950  C C   . ASP C  1 261 ? 46.315  36.974 63.081  1.00 62.87  ? 261  ASP C C   1 
ATOM   5951  O O   . ASP C  1 261 ? 46.830  35.900 62.778  1.00 64.44  ? 261  ASP C O   1 
ATOM   5952  C CB  . ASP C  1 261 ? 46.950  38.417 61.135  1.00 65.00  ? 261  ASP C CB  1 
ATOM   5953  C CG  . ASP C  1 261 ? 47.232  39.833 60.664  1.00 65.77  ? 261  ASP C CG  1 
ATOM   5954  O OD1 . ASP C  1 261 ? 47.122  40.769 61.486  1.00 64.89  ? 261  ASP C OD1 1 
ATOM   5955  O OD2 . ASP C  1 261 ? 47.559  40.011 59.469  1.00 67.46  ? 261  ASP C OD2 1 
ATOM   5956  N N   . SER C  1 262 ? 45.201  37.074 63.794  1.00 60.52  ? 262  SER C N   1 
ATOM   5957  C CA  . SER C  1 262 ? 44.448  35.911 64.240  1.00 59.57  ? 262  SER C CA  1 
ATOM   5958  C C   . SER C  1 262 ? 42.964  36.257 64.184  1.00 57.19  ? 262  SER C C   1 
ATOM   5959  O O   . SER C  1 262 ? 42.597  37.383 63.836  1.00 56.42  ? 262  SER C O   1 
ATOM   5960  C CB  . SER C  1 262 ? 44.867  35.521 65.664  1.00 59.83  ? 262  SER C CB  1 
ATOM   5961  O OG  . SER C  1 262 ? 44.069  34.470 66.187  1.00 59.05  ? 262  SER C OG  1 
ATOM   5962  N N   . THR C  1 263 ? 42.114  35.290 64.511  1.00 56.27  ? 263  THR C N   1 
ATOM   5963  C CA  . THR C  1 263 ? 40.673  35.515 64.524  1.00 54.17  ? 263  THR C CA  1 
ATOM   5964  C C   . THR C  1 263 ? 39.977  34.412 65.312  1.00 53.69  ? 263  THR C C   1 
ATOM   5965  O O   . THR C  1 263 ? 40.429  33.263 65.311  1.00 55.01  ? 263  THR C O   1 
ATOM   5966  C CB  . THR C  1 263 ? 40.101  35.597 63.087  1.00 53.77  ? 263  THR C CB  1 
ATOM   5967  O OG1 . THR C  1 263 ? 38.871  36.325 63.099  1.00 51.91  ? 263  THR C OG1 1 
ATOM   5968  C CG2 . THR C  1 263 ? 39.863  34.217 62.486  1.00 54.28  ? 263  THR C CG2 1 
ATOM   5969  N N   . ILE C  1 264 ? 38.895  34.768 65.998  1.00 52.12  ? 264  ILE C N   1 
ATOM   5970  C CA  . ILE C  1 264 ? 38.061  33.780 66.667  1.00 51.76  ? 264  ILE C CA  1 
ATOM   5971  C C   . ILE C  1 264 ? 36.918  33.402 65.732  1.00 50.86  ? 264  ILE C C   1 
ATOM   5972  O O   . ILE C  1 264 ? 35.933  34.129 65.592  1.00 49.41  ? 264  ILE C O   1 
ATOM   5973  C CB  . ILE C  1 264 ? 37.528  34.281 68.019  1.00 50.93  ? 264  ILE C CB  1 
ATOM   5974  C CG1 . ILE C  1 264 ? 38.700  34.559 68.963  1.00 51.98  ? 264  ILE C CG1 1 
ATOM   5975  C CG2 . ILE C  1 264 ? 36.601  33.242 68.641  1.00 50.81  ? 264  ILE C CG2 1 
ATOM   5976  C CD1 . ILE C  1 264 ? 38.356  35.472 70.116  1.00 51.25  ? 264  ILE C CD1 1 
ATOM   5977  N N   . MET C  1 265 ? 37.082  32.249 65.094  1.00 42.29  ? 265  MET C N   1 
ATOM   5978  C CA  . MET C  1 265 ? 36.113  31.707 64.160  1.00 40.51  ? 265  MET C CA  1 
ATOM   5979  C C   . MET C  1 265 ? 34.997  30.987 64.916  1.00 40.94  ? 265  MET C C   1 
ATOM   5980  O O   . MET C  1 265 ? 35.250  30.274 65.886  1.00 42.32  ? 265  MET C O   1 
ATOM   5981  C CB  . MET C  1 265 ? 36.825  30.725 63.236  1.00 40.23  ? 265  MET C CB  1 
ATOM   5982  C CG  . MET C  1 265 ? 36.101  30.410 61.946  1.00 38.48  ? 265  MET C CG  1 
ATOM   5983  S SD  . MET C  1 265 ? 37.199  29.506 60.841  1.00 38.78  ? 265  MET C SD  1 
ATOM   5984  C CE  . MET C  1 265 ? 38.291  30.817 60.283  1.00 38.68  ? 265  MET C CE  1 
ATOM   5985  N N   . LYS C  1 266 ? 33.765  31.185 64.460  1.00 40.15  ? 266  LYS C N   1 
ATOM   5986  C CA  . LYS C  1 266 ? 32.594  30.561 65.061  1.00 41.09  ? 266  LYS C CA  1 
ATOM   5987  C C   . LYS C  1 266 ? 32.140  29.410 64.180  1.00 40.84  ? 266  LYS C C   1 
ATOM   5988  O O   . LYS C  1 266 ? 31.667  29.626 63.064  1.00 39.70  ? 266  LYS C O   1 
ATOM   5989  C CB  . LYS C  1 266 ? 31.470  31.587 65.224  1.00 41.39  ? 266  LYS C CB  1 
ATOM   5990  C CG  . LYS C  1 266 ? 31.625  32.476 66.445  1.00 42.85  ? 266  LYS C CG  1 
ATOM   5991  C CD  . LYS C  1 266 ? 31.135  31.765 67.694  1.00 44.58  ? 266  LYS C CD  1 
ATOM   5992  C CE  . LYS C  1 266 ? 31.386  32.602 68.937  1.00 46.23  ? 266  LYS C CE  1 
ATOM   5993  N NZ  . LYS C  1 266 ? 31.052  31.842 70.181  1.00 47.94  ? 266  LYS C NZ  1 
ATOM   5994  N N   . SER C  1 267 ? 32.289  28.187 64.679  1.00 42.36  ? 267  SER C N   1 
ATOM   5995  C CA  . SER C  1 267 ? 31.989  26.997 63.889  1.00 42.98  ? 267  SER C CA  1 
ATOM   5996  C C   . SER C  1 267 ? 31.733  25.764 64.757  1.00 45.60  ? 267  SER C C   1 
ATOM   5997  O O   . SER C  1 267 ? 32.422  25.536 65.756  1.00 46.71  ? 267  SER C O   1 
ATOM   5998  C CB  . SER C  1 267 ? 33.146  26.713 62.929  1.00 42.22  ? 267  SER C CB  1 
ATOM   5999  O OG  . SER C  1 267 ? 32.917  25.526 62.190  1.00 43.31  ? 267  SER C OG  1 
ATOM   6000  N N   . GLU C  1 268 ? 30.739  24.973 64.356  1.00 47.02  ? 268  GLU C N   1 
ATOM   6001  C CA  . GLU C  1 268 ? 30.423  23.710 65.021  1.00 50.14  ? 268  GLU C CA  1 
ATOM   6002  C C   . GLU C  1 268 ? 31.335  22.591 64.526  1.00 51.51  ? 268  GLU C C   1 
ATOM   6003  O O   . GLU C  1 268 ? 31.439  21.548 65.169  1.00 54.42  ? 268  GLU C O   1 
ATOM   6004  C CB  . GLU C  1 268 ? 28.959  23.312 64.783  1.00 51.98  ? 268  GLU C CB  1 
ATOM   6005  C CG  . GLU C  1 268 ? 27.934  24.377 65.148  1.00 51.48  ? 268  GLU C CG  1 
ATOM   6006  C CD  . GLU C  1 268 ? 28.035  24.820 66.595  1.00 52.03  ? 268  GLU C CD  1 
ATOM   6007  O OE1 . GLU C  1 268 ? 27.976  23.950 67.496  1.00 54.49  ? 268  GLU C OE1 1 
ATOM   6008  O OE2 . GLU C  1 268 ? 28.170  26.043 66.823  1.00 50.30  ? 268  GLU C OE2 1 
ATOM   6009  N N   . LEU C  1 269 ? 31.992  22.814 63.388  1.00 49.85  ? 269  LEU C N   1 
ATOM   6010  C CA  . LEU C  1 269 ? 32.834  21.793 62.758  1.00 51.54  ? 269  LEU C CA  1 
ATOM   6011  C C   . LEU C  1 269 ? 34.084  21.495 63.571  1.00 52.93  ? 269  LEU C C   1 
ATOM   6012  O O   . LEU C  1 269 ? 34.528  22.321 64.370  1.00 51.70  ? 269  LEU C O   1 
ATOM   6013  C CB  . LEU C  1 269 ? 33.227  22.213 61.334  1.00 49.41  ? 269  LEU C CB  1 
ATOM   6014  C CG  . LEU C  1 269 ? 32.169  21.945 60.258  1.00 49.48  ? 269  LEU C CG  1 
ATOM   6015  C CD1 . LEU C  1 269 ? 32.402  22.808 59.027  1.00 46.52  ? 269  LEU C CD1 1 
ATOM   6016  C CD2 . LEU C  1 269 ? 32.152  20.471 59.882  1.00 53.13  ? 269  LEU C CD2 1 
ATOM   6017  N N   . GLU C  1 270 ? 34.651  20.311 63.340  1.00 56.03  ? 270  GLU C N   1 
ATOM   6018  C CA  . GLU C  1 270 ? 35.790  19.821 64.127  1.00 58.48  ? 270  GLU C CA  1 
ATOM   6019  C C   . GLU C  1 270 ? 37.124  20.036 63.380  1.00 58.28  ? 270  GLU C C   1 
ATOM   6020  O O   . GLU C  1 270 ? 37.507  21.185 63.156  1.00 55.47  ? 270  GLU C O   1 
ATOM   6021  C CB  . GLU C  1 270 ? 35.566  18.364 64.608  1.00 63.04  ? 270  GLU C CB  1 
ATOM   6022  C CG  . GLU C  1 270 ? 34.898  17.411 63.614  1.00 65.22  ? 270  GLU C CG  1 
ATOM   6023  C CD  . GLU C  1 270 ? 34.734  15.997 64.159  1.00 70.51  ? 270  GLU C CD  1 
ATOM   6024  O OE1 . GLU C  1 270 ? 35.283  15.692 65.240  1.00 72.48  ? 270  GLU C OE1 1 
ATOM   6025  O OE2 . GLU C  1 270 ? 34.047  15.183 63.504  1.00 73.09  ? 270  GLU C OE2 1 
ATOM   6026  N N   . TYR C  1 271 ? 37.820  18.968 62.990  1.00 61.76  ? 271  TYR C N   1 
ATOM   6027  C CA  . TYR C  1 271 ? 39.165  19.086 62.418  1.00 62.55  ? 271  TYR C CA  1 
ATOM   6028  C C   . TYR C  1 271 ? 39.376  18.059 61.303  1.00 65.37  ? 271  TYR C C   1 
ATOM   6029  O O   . TYR C  1 271 ? 39.288  16.851 61.540  1.00 69.48  ? 271  TYR C O   1 
ATOM   6030  C CB  . TYR C  1 271 ? 40.208  18.892 63.523  1.00 65.31  ? 271  TYR C CB  1 
ATOM   6031  C CG  . TYR C  1 271 ? 41.644  19.108 63.089  1.00 66.77  ? 271  TYR C CG  1 
ATOM   6032  C CD1 . TYR C  1 271 ? 42.108  20.377 62.750  1.00 63.85  ? 271  TYR C CD1 1 
ATOM   6033  C CD2 . TYR C  1 271 ? 42.544  18.045 63.032  1.00 71.72  ? 271  TYR C CD2 1 
ATOM   6034  C CE1 . TYR C  1 271 ? 43.421  20.580 62.359  1.00 65.79  ? 271  TYR C CE1 1 
ATOM   6035  C CE2 . TYR C  1 271 ? 43.859  18.238 62.643  1.00 73.72  ? 271  TYR C CE2 1 
ATOM   6036  C CZ  . TYR C  1 271 ? 44.293  19.507 62.307  1.00 70.73  ? 271  TYR C CZ  1 
ATOM   6037  O OH  . TYR C  1 271 ? 45.600  19.700 61.920  1.00 73.31  ? 271  TYR C OH  1 
ATOM   6038  N N   . GLY C  1 272 ? 39.653  18.545 60.092  1.00 63.53  ? 272  GLY C N   1 
ATOM   6039  C CA  . GLY C  1 272 ? 39.860  17.669 58.935  1.00 66.14  ? 272  GLY C CA  1 
ATOM   6040  C C   . GLY C  1 272 ? 41.270  17.111 58.779  1.00 70.26  ? 272  GLY C C   1 
ATOM   6041  O O   . GLY C  1 272 ? 41.489  16.198 57.975  1.00 73.62  ? 272  GLY C O   1 
ATOM   6042  N N   . ASN C  1 273 ? 42.219  17.651 59.548  1.00 70.53  ? 273  ASN C N   1 
ATOM   6043  C CA  . ASN C  1 273 ? 43.646  17.323 59.412  1.00 74.60  ? 273  ASN C CA  1 
ATOM   6044  C C   . ASN C  1 273 ? 44.158  17.634 58.006  1.00 74.07  ? 273  ASN C C   1 
ATOM   6045  O O   . ASN C  1 273 ? 44.937  16.879 57.420  1.00 78.38  ? 273  ASN C O   1 
ATOM   6046  C CB  . ASN C  1 273 ? 43.919  15.863 59.804  1.00 80.68  ? 273  ASN C CB  1 
ATOM   6047  C CG  . ASN C  1 273 ? 45.350  15.640 60.265  1.00 85.30  ? 273  ASN C CG  1 
ATOM   6048  O OD1 . ASN C  1 273 ? 45.583  15.124 61.356  1.00 88.42  ? 273  ASN C OD1 1 
ATOM   6049  N ND2 . ASN C  1 273 ? 46.314  16.038 59.439  1.00 86.10  ? 273  ASN C ND2 1 
ATOM   6050  N N   . CYS C  1 274 ? 43.708  18.770 57.482  1.00 69.04  ? 274  CYS C N   1 
ATOM   6051  C CA  . CYS C  1 274 ? 44.084  19.217 56.156  1.00 67.91  ? 274  CYS C CA  1 
ATOM   6052  C C   . CYS C  1 274 ? 44.842  20.539 56.291  1.00 65.85  ? 274  CYS C C   1 
ATOM   6053  O O   . CYS C  1 274 ? 44.831  21.161 57.356  1.00 64.67  ? 274  CYS C O   1 
ATOM   6054  C CB  . CYS C  1 274 ? 42.826  19.364 55.291  1.00 64.31  ? 274  CYS C CB  1 
ATOM   6055  S SG  . CYS C  1 274 ? 42.347  21.055 54.868  1.00 58.32  ? 274  CYS C SG  1 
ATOM   6056  N N   . ASN C  1 275 ? 45.511  20.948 55.217  1.00 65.92  ? 275  ASN C N   1 
ATOM   6057  C CA  . ASN C  1 275 ? 46.233  22.219 55.177  1.00 64.59  ? 275  ASN C CA  1 
ATOM   6058  C C   . ASN C  1 275 ? 45.641  23.131 54.105  1.00 60.21  ? 275  ASN C C   1 
ATOM   6059  O O   . ASN C  1 275 ? 45.195  22.659 53.060  1.00 59.65  ? 275  ASN C O   1 
ATOM   6060  C CB  . ASN C  1 275 ? 47.719  21.975 54.895  1.00 69.60  ? 275  ASN C CB  1 
ATOM   6061  C CG  . ASN C  1 275 ? 48.566  23.225 55.081  1.00 69.55  ? 275  ASN C CG  1 
ATOM   6062  O OD1 . ASN C  1 275 ? 48.625  23.785 56.170  1.00 69.16  ? 275  ASN C OD1 1 
ATOM   6063  N ND2 . ASN C  1 275 ? 49.228  23.661 54.020  1.00 70.39  ? 275  ASN C ND2 1 
ATOM   6064  N N   . THR C  1 276 ? 45.642  24.436 54.362  1.00 57.55  ? 276  THR C N   1 
ATOM   6065  C CA  . THR C  1 276 ? 45.100  25.404 53.410  1.00 53.70  ? 276  THR C CA  1 
ATOM   6066  C C   . THR C  1 276 ? 45.829  26.740 53.514  1.00 53.63  ? 276  THR C C   1 
ATOM   6067  O O   . THR C  1 276 ? 46.703  26.915 54.361  1.00 56.48  ? 276  THR C O   1 
ATOM   6068  C CB  . THR C  1 276 ? 43.581  25.603 53.628  1.00 49.64  ? 276  THR C CB  1 
ATOM   6069  O OG1 . THR C  1 276 ? 43.044  26.453 52.607  1.00 46.40  ? 276  THR C OG1 1 
ATOM   6070  C CG2 . THR C  1 276 ? 43.286  26.205 55.007  1.00 48.78  ? 276  THR C CG2 1 
ATOM   6071  N N   . LYS C  1 277 ? 45.477  27.669 52.628  1.00 50.89  ? 277  LYS C N   1 
ATOM   6072  C CA  . LYS C  1 277 ? 45.984  29.044 52.690  1.00 50.86  ? 277  LYS C CA  1 
ATOM   6073  C C   . LYS C  1 277 ? 44.842  30.061 52.766  1.00 46.81  ? 277  LYS C C   1 
ATOM   6074  O O   . LYS C  1 277 ? 45.080  31.268 52.755  1.00 46.72  ? 277  LYS C O   1 
ATOM   6075  C CB  . LYS C  1 277 ? 46.879  29.327 51.471  1.00 52.60  ? 277  LYS C CB  1 
ATOM   6076  C CG  . LYS C  1 277 ? 48.156  30.112 51.767  1.00 56.38  ? 277  LYS C CG  1 
ATOM   6077  C CD  . LYS C  1 277 ? 49.180  30.022 50.643  1.00 59.42  ? 277  LYS C CD  1 
ATOM   6078  C CE  . LYS C  1 277 ? 49.340  31.332 49.921  1.00 58.75  ? 277  LYS C CE  1 
ATOM   6079  N NZ  . LYS C  1 277 ? 50.062  32.351 50.726  1.00 61.65  ? 277  LYS C NZ  1 
ATOM   6080  N N   . CYS C  1 278 ? 43.610  29.561 52.844  1.00 44.13  ? 278  CYS C N   1 
ATOM   6081  C CA  . CYS C  1 278 ? 42.418  30.387 52.964  1.00 40.89  ? 278  CYS C CA  1 
ATOM   6082  C C   . CYS C  1 278 ? 41.359  29.558 53.669  1.00 39.93  ? 278  CYS C C   1 
ATOM   6083  O O   . CYS C  1 278 ? 40.934  28.523 53.147  1.00 39.84  ? 278  CYS C O   1 
ATOM   6084  C CB  . CYS C  1 278 ? 41.905  30.797 51.586  1.00 38.62  ? 278  CYS C CB  1 
ATOM   6085  S SG  . CYS C  1 278 ? 40.333  31.699 51.617  1.00 35.30  ? 278  CYS C SG  1 
ATOM   6086  N N   . GLN C  1 279 ? 40.939  30.000 54.851  1.00 39.69  ? 279  GLN C N   1 
ATOM   6087  C CA  . GLN C  1 279 ? 40.014  29.217 55.665  1.00 39.40  ? 279  GLN C CA  1 
ATOM   6088  C C   . GLN C  1 279 ? 38.716  29.969 55.931  1.00 37.21  ? 279  GLN C C   1 
ATOM   6089  O O   . GLN C  1 279 ? 38.725  31.180 56.152  1.00 36.68  ? 279  GLN C O   1 
ATOM   6090  C CB  . GLN C  1 279 ? 40.678  28.831 56.987  1.00 41.83  ? 279  GLN C CB  1 
ATOM   6091  C CG  . GLN C  1 279 ? 39.824  27.952 57.892  1.00 42.06  ? 279  GLN C CG  1 
ATOM   6092  C CD  . GLN C  1 279 ? 39.688  26.528 57.384  1.00 43.27  ? 279  GLN C CD  1 
ATOM   6093  O OE1 . GLN C  1 279 ? 40.685  25.843 57.165  1.00 45.74  ? 279  GLN C OE1 1 
ATOM   6094  N NE2 . GLN C  1 279 ? 38.452  26.071 57.208  1.00 42.19  ? 279  GLN C NE2 1 
ATOM   6095  N N   . THR C  1 280 ? 37.610  29.227 55.902  1.00 36.59  ? 280  THR C N   1 
ATOM   6096  C CA  . THR C  1 280 ? 36.299  29.731 56.299  1.00 35.45  ? 280  THR C CA  1 
ATOM   6097  C C   . THR C  1 280 ? 35.720  28.839 57.403  1.00 36.84  ? 280  THR C C   1 
ATOM   6098  O O   . THR C  1 280 ? 36.179  27.709 57.593  1.00 38.43  ? 280  THR C O   1 
ATOM   6099  C CB  . THR C  1 280 ? 35.303  29.751 55.115  1.00 33.91  ? 280  THR C CB  1 
ATOM   6100  O OG1 . THR C  1 280 ? 34.723  28.451 54.933  1.00 34.76  ? 280  THR C OG1 1 
ATOM   6101  C CG2 . THR C  1 280 ? 35.991  30.190 53.828  1.00 32.99  ? 280  THR C CG2 1 
ATOM   6102  N N   . PRO C  1 281 ? 34.708  29.345 58.136  1.00 36.70  ? 281  PRO C N   1 
ATOM   6103  C CA  . PRO C  1 281 ? 33.974  28.520 59.114  1.00 38.20  ? 281  PRO C CA  1 
ATOM   6104  C C   . PRO C  1 281 ? 33.235  27.316 58.501  1.00 39.15  ? 281  PRO C C   1 
ATOM   6105  O O   . PRO C  1 281 ? 32.941  26.349 59.214  1.00 41.05  ? 281  PRO C O   1 
ATOM   6106  C CB  . PRO C  1 281 ? 32.967  29.497 59.748  1.00 37.83  ? 281  PRO C CB  1 
ATOM   6107  C CG  . PRO C  1 281 ? 33.126  30.804 59.050  1.00 36.36  ? 281  PRO C CG  1 
ATOM   6108  C CD  . PRO C  1 281 ? 34.383  30.779 58.247  1.00 35.76  ? 281  PRO C CD  1 
ATOM   6109  N N   . MET C  1 282 ? 32.944  27.389 57.200  1.00 38.25  ? 282  MET C N   1 
ATOM   6110  C CA  . MET C  1 282 ? 32.262  26.318 56.461  1.00 39.50  ? 282  MET C CA  1 
ATOM   6111  C C   . MET C  1 282 ? 33.250  25.271 55.943  1.00 40.73  ? 282  MET C C   1 
ATOM   6112  O O   . MET C  1 282 ? 32.890  24.108 55.749  1.00 42.88  ? 282  MET C O   1 
ATOM   6113  C CB  . MET C  1 282 ? 31.515  26.911 55.265  1.00 38.23  ? 282  MET C CB  1 
ATOM   6114  C CG  . MET C  1 282 ? 30.576  28.060 55.609  1.00 37.58  ? 282  MET C CG  1 
ATOM   6115  S SD  . MET C  1 282 ? 28.849  27.554 55.718  1.00 40.04  ? 282  MET C SD  1 
ATOM   6116  C CE  . MET C  1 282 ? 28.482  27.370 53.968  1.00 39.41  ? 282  MET C CE  1 
ATOM   6117  N N   . GLY C  1 283 ? 34.489  25.698 55.704  1.00 39.89  ? 283  GLY C N   1 
ATOM   6118  C CA  . GLY C  1 283 ? 35.531  24.828 55.165  1.00 41.48  ? 283  GLY C CA  1 
ATOM   6119  C C   . GLY C  1 283 ? 36.692  25.637 54.616  1.00 40.34  ? 283  GLY C C   1 
ATOM   6120  O O   . GLY C  1 283 ? 36.750  26.851 54.802  1.00 38.58  ? 283  GLY C O   1 
ATOM   6121  N N   . ALA C  1 284 ? 37.618  24.970 53.935  1.00 41.92  ? 284  ALA C N   1 
ATOM   6122  C CA  . ALA C  1 284 ? 38.797  25.635 53.380  1.00 41.64  ? 284  ALA C CA  1 
ATOM   6123  C C   . ALA C  1 284 ? 38.646  25.881 51.880  1.00 40.18  ? 284  ALA C C   1 
ATOM   6124  O O   . ALA C  1 284 ? 37.864  25.207 51.201  1.00 40.17  ? 284  ALA C O   1 
ATOM   6125  C CB  . ALA C  1 284 ? 40.042  24.812 53.655  1.00 45.06  ? 284  ALA C CB  1 
ATOM   6126  N N   . ILE C  1 285 ? 39.409  26.850 51.376  1.00 39.28  ? 285  ILE C N   1 
ATOM   6127  C CA  . ILE C  1 285 ? 39.363  27.249 49.964  1.00 37.84  ? 285  ILE C CA  1 
ATOM   6128  C C   . ILE C  1 285 ? 40.733  27.102 49.296  1.00 39.89  ? 285  ILE C C   1 
ATOM   6129  O O   . ILE C  1 285 ? 41.755  27.525 49.839  1.00 41.40  ? 285  ILE C O   1 
ATOM   6130  C CB  . ILE C  1 285 ? 38.846  28.701 49.814  1.00 35.04  ? 285  ILE C CB  1 
ATOM   6131  C CG1 . ILE C  1 285 ? 37.321  28.708 49.698  1.00 33.23  ? 285  ILE C CG1 1 
ATOM   6132  C CG2 . ILE C  1 285 ? 39.447  29.391 48.595  1.00 34.43  ? 285  ILE C CG2 1 
ATOM   6133  C CD1 . ILE C  1 285 ? 36.689  30.032 50.068  1.00 31.47  ? 285  ILE C CD1 1 
ATOM   6134  N N   . ASN C  1 286 ? 40.725  26.498 48.110  1.00 40.35  ? 286  ASN C N   1 
ATOM   6135  C CA  . ASN C  1 286 ? 41.913  26.359 47.281  1.00 42.45  ? 286  ASN C CA  1 
ATOM   6136  C C   . ASN C  1 286 ? 41.550  26.663 45.834  1.00 40.66  ? 286  ASN C C   1 
ATOM   6137  O O   . ASN C  1 286 ? 41.141  25.775 45.084  1.00 41.34  ? 286  ASN C O   1 
ATOM   6138  C CB  . ASN C  1 286 ? 42.485  24.941 47.401  1.00 46.44  ? 286  ASN C CB  1 
ATOM   6139  C CG  . ASN C  1 286 ? 43.691  24.717 46.505  1.00 49.36  ? 286  ASN C CG  1 
ATOM   6140  O OD1 . ASN C  1 286 ? 44.495  25.626 46.290  1.00 49.41  ? 286  ASN C OD1 1 
ATOM   6141  N ND2 . ASN C  1 286 ? 43.824  23.502 45.976  1.00 52.39  ? 286  ASN C ND2 1 
ATOM   6142  N N   . SER C  1 287 ? 41.678  27.930 45.454  1.00 38.67  ? 287  SER C N   1 
ATOM   6143  C CA  . SER C  1 287 ? 41.400  28.339 44.082  1.00 37.05  ? 287  SER C CA  1 
ATOM   6144  C C   . SER C  1 287 ? 42.190  29.578 43.686  1.00 36.85  ? 287  SER C C   1 
ATOM   6145  O O   . SER C  1 287 ? 42.766  30.264 44.531  1.00 37.67  ? 287  SER C O   1 
ATOM   6146  C CB  . SER C  1 287 ? 39.899  28.587 43.887  1.00 34.04  ? 287  SER C CB  1 
ATOM   6147  O OG  . SER C  1 287 ? 39.506  29.860 44.368  1.00 32.01  ? 287  SER C OG  1 
ATOM   6148  N N   . SER C  1 288 ? 42.214  29.842 42.386  1.00 36.16  ? 288  SER C N   1 
ATOM   6149  C CA  . SER C  1 288 ? 42.847  31.037 41.838  1.00 36.15  ? 288  SER C CA  1 
ATOM   6150  C C   . SER C  1 288 ? 41.801  32.072 41.398  1.00 32.89  ? 288  SER C C   1 
ATOM   6151  O O   . SER C  1 288 ? 42.154  33.142 40.899  1.00 32.79  ? 288  SER C O   1 
ATOM   6152  C CB  . SER C  1 288 ? 43.758  30.648 40.668  1.00 38.34  ? 288  SER C CB  1 
ATOM   6153  O OG  . SER C  1 288 ? 43.175  29.612 39.892  1.00 38.00  ? 288  SER C OG  1 
ATOM   6154  N N   . MET C  1 289 ? 40.522  31.758 41.607  1.00 30.73  ? 289  MET C N   1 
ATOM   6155  C CA  . MET C  1 289 ? 39.429  32.670 41.266  1.00 28.23  ? 289  MET C CA  1 
ATOM   6156  C C   . MET C  1 289 ? 39.599  33.984 42.020  1.00 28.21  ? 289  MET C C   1 
ATOM   6157  O O   . MET C  1 289 ? 40.076  33.984 43.149  1.00 29.52  ? 289  MET C O   1 
ATOM   6158  C CB  . MET C  1 289 ? 38.075  32.080 41.670  1.00 26.98  ? 289  MET C CB  1 
ATOM   6159  C CG  . MET C  1 289 ? 37.704  30.754 41.028  1.00 27.51  ? 289  MET C CG  1 
ATOM   6160  S SD  . MET C  1 289 ? 37.369  30.913 39.271  1.00 26.57  ? 289  MET C SD  1 
ATOM   6161  C CE  . MET C  1 289 ? 36.191  29.575 39.064  1.00 27.08  ? 289  MET C CE  1 
ATOM   6162  N N   . PRO C  1 290 ? 39.200  35.110 41.408  1.00 27.11  ? 290  PRO C N   1 
ATOM   6163  C CA  . PRO C  1 290 ? 39.222  36.386 42.134  1.00 27.64  ? 290  PRO C CA  1 
ATOM   6164  C C   . PRO C  1 290 ? 38.099  36.541 43.165  1.00 26.68  ? 290  PRO C C   1 
ATOM   6165  O O   . PRO C  1 290 ? 38.174  37.436 44.007  1.00 27.72  ? 290  PRO C O   1 
ATOM   6166  C CB  . PRO C  1 290 ? 39.054  37.418 41.020  1.00 27.25  ? 290  PRO C CB  1 
ATOM   6167  C CG  . PRO C  1 290 ? 38.294  36.694 39.968  1.00 25.41  ? 290  PRO C CG  1 
ATOM   6168  C CD  . PRO C  1 290 ? 38.815  35.291 39.998  1.00 25.91  ? 290  PRO C CD  1 
ATOM   6169  N N   . PHE C  1 291 ? 37.073  35.689 43.086  1.00 25.19  ? 291  PHE C N   1 
ATOM   6170  C CA  . PHE C  1 291 ? 35.911  35.759 43.976  1.00 24.65  ? 291  PHE C CA  1 
ATOM   6171  C C   . PHE C  1 291 ? 35.513  34.402 44.518  1.00 24.44  ? 291  PHE C C   1 
ATOM   6172  O O   . PHE C  1 291 ? 35.847  33.369 43.939  1.00 24.57  ? 291  PHE C O   1 
ATOM   6173  C CB  . PHE C  1 291 ? 34.689  36.286 43.227  1.00 23.75  ? 291  PHE C CB  1 
ATOM   6174  C CG  . PHE C  1 291 ? 34.775  37.726 42.849  1.00 24.32  ? 291  PHE C CG  1 
ATOM   6175  C CD1 . PHE C  1 291 ? 34.532  38.711 43.790  1.00 25.61  ? 291  PHE C CD1 1 
ATOM   6176  C CD2 . PHE C  1 291 ? 35.075  38.098 41.548  1.00 24.01  ? 291  PHE C CD2 1 
ATOM   6177  C CE1 . PHE C  1 291 ? 34.596  40.048 43.445  1.00 26.81  ? 291  PHE C CE1 1 
ATOM   6178  C CE2 . PHE C  1 291 ? 35.141  39.432 41.195  1.00 24.97  ? 291  PHE C CE2 1 
ATOM   6179  C CZ  . PHE C  1 291 ? 34.901  40.406 42.147  1.00 26.53  ? 291  PHE C CZ  1 
ATOM   6180  N N   . HIS C  1 292 ? 34.755  34.427 45.612  1.00 24.47  ? 292  HIS C N   1 
ATOM   6181  C CA  . HIS C  1 292 ? 34.067  33.246 46.123  1.00 24.58  ? 292  HIS C CA  1 
ATOM   6182  C C   . HIS C  1 292 ? 32.744  33.658 46.763  1.00 24.62  ? 292  HIS C C   1 
ATOM   6183  O O   . HIS C  1 292 ? 32.500  34.847 46.982  1.00 24.67  ? 292  HIS C O   1 
ATOM   6184  C CB  . HIS C  1 292 ? 34.939  32.519 47.142  1.00 25.71  ? 292  HIS C CB  1 
ATOM   6185  C CG  . HIS C  1 292 ? 35.072  33.242 48.443  1.00 26.29  ? 292  HIS C CG  1 
ATOM   6186  N ND1 . HIS C  1 292 ? 34.497  32.787 49.607  1.00 26.92  ? 292  HIS C ND1 1 
ATOM   6187  C CD2 . HIS C  1 292 ? 35.698  34.398 48.759  1.00 26.74  ? 292  HIS C CD2 1 
ATOM   6188  C CE1 . HIS C  1 292 ? 34.773  33.626 50.589  1.00 27.57  ? 292  HIS C CE1 1 
ATOM   6189  N NE2 . HIS C  1 292 ? 35.502  34.612 50.101  1.00 27.59  ? 292  HIS C NE2 1 
ATOM   6190  N N   . ASN C  1 293 ? 31.895  32.680 47.064  1.00 25.13  ? 293  ASN C N   1 
ATOM   6191  C CA  . ASN C  1 293 ? 30.606  32.952 47.703  1.00 25.87  ? 293  ASN C CA  1 
ATOM   6192  C C   . ASN C  1 293 ? 30.313  32.022 48.881  1.00 27.18  ? 293  ASN C C   1 
ATOM   6193  O O   . ASN C  1 293 ? 29.151  31.758 49.202  1.00 28.42  ? 293  ASN C O   1 
ATOM   6194  C CB  . ASN C  1 293 ? 29.488  32.860 46.667  1.00 26.00  ? 293  ASN C CB  1 
ATOM   6195  C CG  . ASN C  1 293 ? 29.272  31.447 46.163  1.00 26.72  ? 293  ASN C CG  1 
ATOM   6196  O OD1 . ASN C  1 293 ? 30.168  30.609 46.221  1.00 26.77  ? 293  ASN C OD1 1 
ATOM   6197  N ND2 . ASN C  1 293 ? 28.074  31.175 45.667  1.00 27.89  ? 293  ASN C ND2 1 
ATOM   6198  N N   . ILE C  1 294 ? 31.368  31.557 49.542  1.00 27.34  ? 294  ILE C N   1 
ATOM   6199  C CA  . ILE C  1 294 ? 31.241  30.556 50.605  1.00 28.81  ? 294  ILE C CA  1 
ATOM   6200  C C   . ILE C  1 294 ? 30.769  31.193 51.914  1.00 29.47  ? 294  ILE C C   1 
ATOM   6201  O O   . ILE C  1 294 ? 29.719  30.827 52.441  1.00 30.82  ? 294  ILE C O   1 
ATOM   6202  C CB  . ILE C  1 294 ? 32.572  29.794 50.851  1.00 29.26  ? 294  ILE C CB  1 
ATOM   6203  C CG1 . ILE C  1 294 ? 33.143  29.215 49.547  1.00 29.05  ? 294  ILE C CG1 1 
ATOM   6204  C CG2 . ILE C  1 294 ? 32.370  28.675 51.862  1.00 31.13  ? 294  ILE C CG2 1 
ATOM   6205  C CD1 . ILE C  1 294 ? 32.172  28.380 48.739  1.00 29.77  ? 294  ILE C CD1 1 
ATOM   6206  N N   . HIS C  1 295 ? 31.548  32.141 52.432  1.00 29.03  ? 295  HIS C N   1 
ATOM   6207  C CA  . HIS C  1 295 ? 31.270  32.750 53.733  1.00 30.00  ? 295  HIS C CA  1 
ATOM   6208  C C   . HIS C  1 295 ? 32.089  34.042 53.899  1.00 29.82  ? 295  HIS C C   1 
ATOM   6209  O O   . HIS C  1 295 ? 33.283  34.049 53.595  1.00 29.48  ? 295  HIS C O   1 
ATOM   6210  C CB  . HIS C  1 295 ? 31.623  31.753 54.844  1.00 31.12  ? 295  HIS C CB  1 
ATOM   6211  C CG  . HIS C  1 295 ? 31.024  32.080 56.176  1.00 32.41  ? 295  HIS C CG  1 
ATOM   6212  N ND1 . HIS C  1 295 ? 31.501  33.095 56.974  1.00 32.79  ? 295  HIS C ND1 1 
ATOM   6213  C CD2 . HIS C  1 295 ? 30.004  31.512 56.861  1.00 33.82  ? 295  HIS C CD2 1 
ATOM   6214  C CE1 . HIS C  1 295 ? 30.792  33.150 58.087  1.00 34.18  ? 295  HIS C CE1 1 
ATOM   6215  N NE2 . HIS C  1 295 ? 29.877  32.200 58.045  1.00 34.79  ? 295  HIS C NE2 1 
ATOM   6216  N N   . PRO C  1 296 ? 31.459  35.132 54.390  1.00 30.66  ? 296  PRO C N   1 
ATOM   6217  C CA  . PRO C  1 296 ? 32.139  36.439 54.483  1.00 31.21  ? 296  PRO C CA  1 
ATOM   6218  C C   . PRO C  1 296 ? 33.384  36.456 55.372  1.00 32.02  ? 296  PRO C C   1 
ATOM   6219  O O   . PRO C  1 296 ? 34.399  37.038 55.002  1.00 32.30  ? 296  PRO C O   1 
ATOM   6220  C CB  . PRO C  1 296 ? 31.059  37.360 55.075  1.00 32.85  ? 296  PRO C CB  1 
ATOM   6221  C CG  . PRO C  1 296 ? 30.066  36.451 55.711  1.00 33.31  ? 296  PRO C CG  1 
ATOM   6222  C CD  . PRO C  1 296 ? 30.065  35.213 54.867  1.00 31.84  ? 296  PRO C CD  1 
ATOM   6223  N N   . LEU C  1 297 ? 33.287  35.842 56.544  1.00 32.78  ? 297  LEU C N   1 
ATOM   6224  C CA  . LEU C  1 297 ? 34.391  35.804 57.502  1.00 33.97  ? 297  LEU C CA  1 
ATOM   6225  C C   . LEU C  1 297 ? 35.436  34.751 57.135  1.00 33.48  ? 297  LEU C C   1 
ATOM   6226  O O   . LEU C  1 297 ? 35.252  33.562 57.397  1.00 33.33  ? 297  LEU C O   1 
ATOM   6227  C CB  . LEU C  1 297 ? 33.859  35.540 58.917  1.00 35.18  ? 297  LEU C CB  1 
ATOM   6228  C CG  . LEU C  1 297 ? 32.798  36.523 59.424  1.00 36.41  ? 297  LEU C CG  1 
ATOM   6229  C CD1 . LEU C  1 297 ? 32.157  36.011 60.707  1.00 37.53  ? 297  LEU C CD1 1 
ATOM   6230  C CD2 . LEU C  1 297 ? 33.397  37.907 59.634  1.00 38.10  ? 297  LEU C CD2 1 
ATOM   6231  N N   . THR C  1 298 ? 36.534  35.201 56.532  1.00 33.79  ? 298  THR C N   1 
ATOM   6232  C CA  . THR C  1 298 ? 37.639  34.314 56.183  1.00 34.11  ? 298  THR C CA  1 
ATOM   6233  C C   . THR C  1 298 ? 38.929  34.799 56.818  1.00 36.44  ? 298  THR C C   1 
ATOM   6234  O O   . THR C  1 298 ? 39.016  35.931 57.296  1.00 37.64  ? 298  THR C O   1 
ATOM   6235  C CB  . THR C  1 298 ? 37.843  34.206 54.655  1.00 32.88  ? 298  THR C CB  1 
ATOM   6236  O OG1 . THR C  1 298 ? 38.503  35.378 54.158  1.00 33.59  ? 298  THR C OG1 1 
ATOM   6237  C CG2 . THR C  1 298 ? 36.512  34.024 53.942  1.00 30.96  ? 298  THR C CG2 1 
ATOM   6238  N N   . ILE C  1 299 ? 39.926  33.924 56.806  1.00 37.65  ? 299  ILE C N   1 
ATOM   6239  C CA  . ILE C  1 299 ? 41.255  34.235 57.317  1.00 40.57  ? 299  ILE C CA  1 
ATOM   6240  C C   . ILE C  1 299 ? 42.267  33.729 56.290  1.00 41.54  ? 299  ILE C C   1 
ATOM   6241  O O   . ILE C  1 299 ? 42.098  32.646 55.724  1.00 40.60  ? 299  ILE C O   1 
ATOM   6242  C CB  . ILE C  1 299 ? 41.485  33.617 58.728  1.00 42.23  ? 299  ILE C CB  1 
ATOM   6243  C CG1 . ILE C  1 299 ? 42.932  33.807 59.221  1.00 45.80  ? 299  ILE C CG1 1 
ATOM   6244  C CG2 . ILE C  1 299 ? 41.124  32.139 58.752  1.00 41.48  ? 299  ILE C CG2 1 
ATOM   6245  C CD1 . ILE C  1 299 ? 43.261  35.214 59.675  1.00 47.71  ? 299  ILE C CD1 1 
ATOM   6246  N N   . GLY C  1 300 ? 43.295  34.538 56.035  1.00 43.91  ? 300  GLY C N   1 
ATOM   6247  C CA  . GLY C  1 300 ? 44.379  34.171 55.131  1.00 45.73  ? 300  GLY C CA  1 
ATOM   6248  C C   . GLY C  1 300 ? 44.298  34.855 53.780  1.00 44.65  ? 300  GLY C C   1 
ATOM   6249  O O   . GLY C  1 300 ? 43.589  35.850 53.613  1.00 43.22  ? 300  GLY C O   1 
ATOM   6250  N N   . GLU C  1 301 ? 45.041  34.307 52.821  1.00 45.77  ? 301  GLU C N   1 
ATOM   6251  C CA  . GLU C  1 301 ? 45.088  34.822 51.452  1.00 45.03  ? 301  GLU C CA  1 
ATOM   6252  C C   . GLU C  1 301 ? 43.883  34.301 50.681  1.00 41.17  ? 301  GLU C C   1 
ATOM   6253  O O   . GLU C  1 301 ? 43.911  33.193 50.146  1.00 40.83  ? 301  GLU C O   1 
ATOM   6254  C CB  . GLU C  1 301 ? 46.388  34.377 50.773  1.00 48.24  ? 301  GLU C CB  1 
ATOM   6255  C CG  . GLU C  1 301 ? 46.595  34.910 49.360  1.00 48.04  ? 301  GLU C CG  1 
ATOM   6256  C CD  . GLU C  1 301 ? 47.032  36.369 49.319  1.00 50.09  ? 301  GLU C CD  1 
ATOM   6257  O OE1 . GLU C  1 301 ? 47.146  37.008 50.396  1.00 51.74  ? 301  GLU C OE1 1 
ATOM   6258  O OE2 . GLU C  1 301 ? 47.269  36.875 48.195  1.00 50.37  ? 301  GLU C OE2 1 
ATOM   6259  N N   . CYS C  1 302 ? 42.834  35.117 50.616  1.00 38.87  ? 302  CYS C N   1 
ATOM   6260  C CA  . CYS C  1 302 ? 41.556  34.686 50.061  1.00 35.68  ? 302  CYS C CA  1 
ATOM   6261  C C   . CYS C  1 302 ? 41.063  35.556 48.908  1.00 34.04  ? 302  CYS C C   1 
ATOM   6262  O O   . CYS C  1 302 ? 41.395  36.742 48.829  1.00 35.15  ? 302  CYS C O   1 
ATOM   6263  C CB  . CYS C  1 302 ? 40.495  34.687 51.161  1.00 34.66  ? 302  CYS C CB  1 
ATOM   6264  S SG  . CYS C  1 302 ? 40.808  33.492 52.475  1.00 36.24  ? 302  CYS C SG  1 
ATOM   6265  N N   . PRO C  1 303 ? 40.252  34.967 48.013  1.00 31.76  ? 303  PRO C N   1 
ATOM   6266  C CA  . PRO C  1 303 ? 39.513  35.783 47.057  1.00 30.14  ? 303  PRO C CA  1 
ATOM   6267  C C   . PRO C  1 303 ? 38.438  36.592 47.781  1.00 29.47  ? 303  PRO C C   1 
ATOM   6268  O O   . PRO C  1 303 ? 38.153  36.319 48.950  1.00 29.89  ? 303  PRO C O   1 
ATOM   6269  C CB  . PRO C  1 303 ? 38.886  34.752 46.111  1.00 28.42  ? 303  PRO C CB  1 
ATOM   6270  C CG  . PRO C  1 303 ? 38.856  33.476 46.875  1.00 28.92  ? 303  PRO C CG  1 
ATOM   6271  C CD  . PRO C  1 303 ? 40.015  33.524 47.820  1.00 31.21  ? 303  PRO C CD  1 
ATOM   6272  N N   . LYS C  1 304 ? 37.846  37.569 47.104  1.00 28.80  ? 304  LYS C N   1 
ATOM   6273  C CA  . LYS C  1 304 ? 36.856  38.434 47.744  1.00 28.95  ? 304  LYS C CA  1 
ATOM   6274  C C   . LYS C  1 304 ? 35.502  37.749 47.799  1.00 27.19  ? 304  LYS C C   1 
ATOM   6275  O O   . LYS C  1 304 ? 35.103  37.050 46.864  1.00 25.75  ? 304  LYS C O   1 
ATOM   6276  C CB  . LYS C  1 304 ? 36.723  39.766 47.009  1.00 29.81  ? 304  LYS C CB  1 
ATOM   6277  C CG  . LYS C  1 304 ? 38.041  40.496 46.794  1.00 32.10  ? 304  LYS C CG  1 
ATOM   6278  C CD  . LYS C  1 304 ? 38.659  40.979 48.102  1.00 34.80  ? 304  LYS C CD  1 
ATOM   6279  C CE  . LYS C  1 304 ? 40.145  40.653 48.182  1.00 36.70  ? 304  LYS C CE  1 
ATOM   6280  N NZ  . LYS C  1 304 ? 40.836  41.464 49.229  1.00 40.19  ? 304  LYS C NZ  1 
ATOM   6281  N N   . TYR C  1 305 ? 34.800  37.951 48.906  1.00 27.68  ? 305  TYR C N   1 
ATOM   6282  C CA  . TYR C  1 305 ? 33.488  37.366 49.079  1.00 26.82  ? 305  TYR C CA  1 
ATOM   6283  C C   . TYR C  1 305 ? 32.433  38.209 48.380  1.00 26.86  ? 305  TYR C C   1 
ATOM   6284  O O   . TYR C  1 305 ? 32.419  39.436 48.501  1.00 28.19  ? 305  TYR C O   1 
ATOM   6285  C CB  . TYR C  1 305 ? 33.136  37.243 50.556  1.00 27.85  ? 305  TYR C CB  1 
ATOM   6286  C CG  . TYR C  1 305 ? 31.754  36.690 50.771  1.00 27.74  ? 305  TYR C CG  1 
ATOM   6287  C CD1 . TYR C  1 305 ? 31.493  35.337 50.598  1.00 27.06  ? 305  TYR C CD1 1 
ATOM   6288  C CD2 . TYR C  1 305 ? 30.702  37.519 51.127  1.00 29.00  ? 305  TYR C CD2 1 
ATOM   6289  C CE1 . TYR C  1 305 ? 30.222  34.825 50.786  1.00 27.68  ? 305  TYR C CE1 1 
ATOM   6290  C CE2 . TYR C  1 305 ? 29.427  37.017 51.318  1.00 29.62  ? 305  TYR C CE2 1 
ATOM   6291  C CZ  . TYR C  1 305 ? 29.194  35.668 51.147  1.00 28.95  ? 305  TYR C CZ  1 
ATOM   6292  O OH  . TYR C  1 305 ? 27.934  35.155 51.334  1.00 30.19  ? 305  TYR C OH  1 
ATOM   6293  N N   . VAL C  1 306 ? 31.554  37.534 47.647  1.00 25.87  ? 306  VAL C N   1 
ATOM   6294  C CA  . VAL C  1 306 ? 30.346  38.154 47.123  1.00 26.43  ? 306  VAL C CA  1 
ATOM   6295  C C   . VAL C  1 306 ? 29.178  37.206 47.347  1.00 26.74  ? 306  VAL C C   1 
ATOM   6296  O O   . VAL C  1 306 ? 29.371  36.004 47.518  1.00 26.15  ? 306  VAL C O   1 
ATOM   6297  C CB  . VAL C  1 306 ? 30.468  38.513 45.622  1.00 25.53  ? 306  VAL C CB  1 
ATOM   6298  C CG1 . VAL C  1 306 ? 31.475  39.637 45.424  1.00 26.05  ? 306  VAL C CG1 1 
ATOM   6299  C CG2 . VAL C  1 306 ? 30.848  37.296 44.787  1.00 23.91  ? 306  VAL C CG2 1 
ATOM   6300  N N   . LYS C  1 307 ? 27.970  37.759 47.347  1.00 28.31  ? 307  LYS C N   1 
ATOM   6301  C CA  . LYS C  1 307 ? 26.750  36.974 47.536  1.00 29.52  ? 307  LYS C CA  1 
ATOM   6302  C C   . LYS C  1 307 ? 26.246  36.297 46.256  1.00 29.03  ? 307  LYS C C   1 
ATOM   6303  O O   . LYS C  1 307 ? 25.229  35.607 46.284  1.00 30.61  ? 307  LYS C O   1 
ATOM   6304  C CB  . LYS C  1 307 ? 25.633  37.863 48.091  1.00 32.25  ? 307  LYS C CB  1 
ATOM   6305  C CG  . LYS C  1 307 ? 25.803  38.267 49.540  1.00 33.54  ? 307  LYS C CG  1 
ATOM   6306  C CD  . LYS C  1 307 ? 24.513  38.876 50.060  1.00 36.89  ? 307  LYS C CD  1 
ATOM   6307  C CE  . LYS C  1 307 ? 24.723  39.656 51.348  1.00 38.64  ? 307  LYS C CE  1 
ATOM   6308  N NZ  . LYS C  1 307 ? 23.460  40.317 51.791  1.00 42.49  ? 307  LYS C NZ  1 
ATOM   6309  N N   . SER C  1 308 ? 26.938  36.491 45.139  1.00 27.31  ? 308  SER C N   1 
ATOM   6310  C CA  . SER C  1 308 ? 26.473  35.972 43.857  1.00 26.98  ? 308  SER C CA  1 
ATOM   6311  C C   . SER C  1 308 ? 26.448  34.445 43.827  1.00 26.99  ? 308  SER C C   1 
ATOM   6312  O O   . SER C  1 308 ? 27.257  33.787 44.483  1.00 26.35  ? 308  SER C O   1 
ATOM   6313  C CB  . SER C  1 308 ? 27.363  36.483 42.722  1.00 25.18  ? 308  SER C CB  1 
ATOM   6314  O OG  . SER C  1 308 ? 27.651  37.857 42.884  1.00 25.50  ? 308  SER C OG  1 
ATOM   6315  N N   . ASN C  1 309 ? 25.505  33.902 43.061  1.00 28.22  ? 309  ASN C N   1 
ATOM   6316  C CA  . ASN C  1 309 ? 25.506  32.492 42.689  1.00 28.74  ? 309  ASN C CA  1 
ATOM   6317  C C   . ASN C  1 309 ? 26.339  32.261 41.437  1.00 26.98  ? 309  ASN C C   1 
ATOM   6318  O O   . ASN C  1 309 ? 26.815  31.148 41.205  1.00 27.22  ? 309  ASN C O   1 
ATOM   6319  C CB  . ASN C  1 309 ? 24.082  32.004 42.430  1.00 31.67  ? 309  ASN C CB  1 
ATOM   6320  C CG  . ASN C  1 309 ? 23.240  31.969 43.691  1.00 34.11  ? 309  ASN C CG  1 
ATOM   6321  O OD1 . ASN C  1 309 ? 23.666  31.442 44.722  1.00 34.11  ? 309  ASN C OD1 1 
ATOM   6322  N ND2 . ASN C  1 309 ? 22.030  32.522 43.616  1.00 36.58  ? 309  ASN C ND2 1 
ATOM   6323  N N   . ARG C  1 310 ? 26.518  33.312 40.637  1.00 25.63  ? 310  ARG C N   1 
ATOM   6324  C CA  . ARG C  1 310 ? 27.129  33.176 39.316  1.00 24.28  ? 310  ARG C CA  1 
ATOM   6325  C C   . ARG C  1 310 ? 27.833  34.456 38.838  1.00 22.52  ? 310  ARG C C   1 
ATOM   6326  O O   . ARG C  1 310 ? 27.225  35.528 38.803  1.00 22.98  ? 310  ARG C O   1 
ATOM   6327  C CB  . ARG C  1 310 ? 26.043  32.786 38.314  1.00 25.83  ? 310  ARG C CB  1 
ATOM   6328  C CG  . ARG C  1 310 ? 26.558  32.082 37.075  1.00 25.35  ? 310  ARG C CG  1 
ATOM   6329  C CD  . ARG C  1 310 ? 25.443  31.861 36.066  1.00 27.14  ? 310  ARG C CD  1 
ATOM   6330  N NE  . ARG C  1 310 ? 25.931  32.044 34.699  1.00 25.95  ? 310  ARG C NE  1 
ATOM   6331  C CZ  . ARG C  1 310 ? 26.607  31.136 33.997  1.00 25.87  ? 310  ARG C CZ  1 
ATOM   6332  N NH1 . ARG C  1 310 ? 26.894  29.941 34.511  1.00 27.18  ? 310  ARG C NH1 1 
ATOM   6333  N NH2 . ARG C  1 310 ? 27.001  31.429 32.764  1.00 24.86  ? 310  ARG C NH2 1 
ATOM   6334  N N   . LEU C  1 311 ? 29.112  34.331 38.484  1.00 21.02  ? 311  LEU C N   1 
ATOM   6335  C CA  . LEU C  1 311 ? 29.866  35.403 37.812  1.00 19.84  ? 311  LEU C CA  1 
ATOM   6336  C C   . LEU C  1 311 ? 30.730  34.824 36.690  1.00 18.99  ? 311  LEU C C   1 
ATOM   6337  O O   . LEU C  1 311 ? 31.772  34.219 36.951  1.00 18.92  ? 311  LEU C O   1 
ATOM   6338  C CB  . LEU C  1 311 ? 30.759  36.160 38.794  1.00 19.69  ? 311  LEU C CB  1 
ATOM   6339  C CG  . LEU C  1 311 ? 30.083  37.001 39.876  1.00 20.72  ? 311  LEU C CG  1 
ATOM   6340  C CD1 . LEU C  1 311 ? 31.148  37.586 40.787  1.00 20.90  ? 311  LEU C CD1 1 
ATOM   6341  C CD2 . LEU C  1 311 ? 29.229  38.110 39.287  1.00 21.52  ? 311  LEU C CD2 1 
ATOM   6342  N N   . VAL C  1 312 ? 30.285  35.012 35.450  1.00 18.68  ? 312  VAL C N   1 
ATOM   6343  C CA  . VAL C  1 312 ? 30.970  34.483 34.278  1.00 18.15  ? 312  VAL C CA  1 
ATOM   6344  C C   . VAL C  1 312 ? 31.197  35.597 33.265  1.00 17.38  ? 312  VAL C C   1 
ATOM   6345  O O   . VAL C  1 312 ? 30.253  36.256 32.844  1.00 17.60  ? 312  VAL C O   1 
ATOM   6346  C CB  . VAL C  1 312 ? 30.144  33.367 33.608  1.00 19.12  ? 312  VAL C CB  1 
ATOM   6347  C CG1 . VAL C  1 312 ? 30.907  32.754 32.438  1.00 19.06  ? 312  VAL C CG1 1 
ATOM   6348  C CG2 . VAL C  1 312 ? 29.778  32.296 34.625  1.00 20.44  ? 312  VAL C CG2 1 
ATOM   6349  N N   . LEU C  1 313 ? 32.453  35.791 32.876  1.00 16.88  ? 313  LEU C N   1 
ATOM   6350  C CA  . LEU C  1 313 ? 32.818  36.785 31.875  1.00 16.52  ? 313  LEU C CA  1 
ATOM   6351  C C   . LEU C  1 313 ? 32.909  36.162 30.492  1.00 16.28  ? 313  LEU C C   1 
ATOM   6352  O O   . LEU C  1 313 ? 33.543  35.123 30.321  1.00 16.62  ? 313  LEU C O   1 
ATOM   6353  C CB  . LEU C  1 313 ? 34.170  37.407 32.210  1.00 16.88  ? 313  LEU C CB  1 
ATOM   6354  C CG  . LEU C  1 313 ? 34.169  38.466 33.303  1.00 17.52  ? 313  LEU C CG  1 
ATOM   6355  C CD1 . LEU C  1 313 ? 35.599  38.788 33.711  1.00 18.53  ? 313  LEU C CD1 1 
ATOM   6356  C CD2 . LEU C  1 313 ? 33.446  39.720 32.838  1.00 17.93  ? 313  LEU C CD2 1 
ATOM   6357  N N   . ALA C  1 314 ? 32.283  36.802 29.509  1.00 16.05  ? 314  ALA C N   1 
ATOM   6358  C CA  . ALA C  1 314 ? 32.485  36.436 28.113  1.00 15.90  ? 314  ALA C CA  1 
ATOM   6359  C C   . ALA C  1 314 ? 33.902  36.815 27.730  1.00 15.97  ? 314  ALA C C   1 
ATOM   6360  O O   . ALA C  1 314 ? 34.339  37.938 27.983  1.00 16.16  ? 314  ALA C O   1 
ATOM   6361  C CB  . ALA C  1 314 ? 31.499  37.155 27.215  1.00 15.90  ? 314  ALA C CB  1 
ATOM   6362  N N   . THR C  1 315 ? 34.625  35.857 27.163  1.00 16.41  ? 315  THR C N   1 
ATOM   6363  C CA  . THR C  1 315 ? 35.918  36.116 26.541  1.00 17.10  ? 315  THR C CA  1 
ATOM   6364  C C   . THR C  1 315 ? 35.789  35.989 25.027  1.00 17.10  ? 315  THR C C   1 
ATOM   6365  O O   . THR C  1 315 ? 36.309  36.807 24.285  1.00 17.31  ? 315  THR C O   1 
ATOM   6366  C CB  . THR C  1 315 ? 37.004  35.158 27.066  1.00 18.38  ? 315  THR C CB  1 
ATOM   6367  O OG1 . THR C  1 315 ? 36.489  33.821 27.134  1.00 18.77  ? 315  THR C OG1 1 
ATOM   6368  C CG2 . THR C  1 315 ? 37.457  35.585 28.456  1.00 18.69  ? 315  THR C CG2 1 
ATOM   6369  N N   . GLY C  1 316 ? 35.076  34.968 24.576  1.00 17.23  ? 316  GLY C N   1 
ATOM   6370  C CA  . GLY C  1 316 ? 34.830  34.771 23.161  1.00 17.46  ? 316  GLY C CA  1 
ATOM   6371  C C   . GLY C  1 316 ? 33.633  35.562 22.681  1.00 16.66  ? 316  GLY C C   1 
ATOM   6372  O O   . GLY C  1 316 ? 33.203  36.514 23.326  1.00 16.09  ? 316  GLY C O   1 
ATOM   6373  N N   . LEU C  1 317 ? 33.085  35.141 21.549  1.00 17.11  ? 317  LEU C N   1 
ATOM   6374  C CA  . LEU C  1 317 ? 32.022  35.875 20.878  1.00 16.91  ? 317  LEU C CA  1 
ATOM   6375  C C   . LEU C  1 317 ? 30.750  35.040 20.838  1.00 17.93  ? 317  LEU C C   1 
ATOM   6376  O O   . LEU C  1 317 ? 30.753  33.871 21.219  1.00 18.85  ? 317  LEU C O   1 
ATOM   6377  C CB  . LEU C  1 317 ? 32.466  36.298 19.467  1.00 16.94  ? 317  LEU C CB  1 
ATOM   6378  C CG  . LEU C  1 317 ? 33.113  35.261 18.539  1.00 17.85  ? 317  LEU C CG  1 
ATOM   6379  C CD1 . LEU C  1 317 ? 32.051  34.480 17.788  1.00 18.81  ? 317  LEU C CD1 1 
ATOM   6380  C CD2 . LEU C  1 317 ? 34.085  35.905 17.560  1.00 17.91  ? 317  LEU C CD2 1 
ATOM   6381  N N   . ARG C  1 318 ? 29.662  35.655 20.395  1.00 18.34  ? 318  ARG C N   1 
ATOM   6382  C CA  . ARG C  1 318 ? 28.375  34.989 20.346  1.00 20.04  ? 318  ARG C CA  1 
ATOM   6383  C C   . ARG C  1 318 ? 28.474  33.743 19.477  1.00 21.53  ? 318  ARG C C   1 
ATOM   6384  O O   . ARG C  1 318 ? 28.830  33.821 18.302  1.00 21.50  ? 318  ARG C O   1 
ATOM   6385  C CB  . ARG C  1 318 ? 27.309  35.939 19.807  1.00 20.68  ? 318  ARG C CB  1 
ATOM   6386  C CG  . ARG C  1 318 ? 25.911  35.350 19.746  1.00 23.04  ? 318  ARG C CG  1 
ATOM   6387  C CD  . ARG C  1 318 ? 24.935  36.354 19.164  1.00 24.15  ? 318  ARG C CD  1 
ATOM   6388  N NE  . ARG C  1 318 ? 24.623  37.416 20.118  1.00 24.09  ? 318  ARG C NE  1 
ATOM   6389  C CZ  . ARG C  1 318 ? 23.544  37.450 20.896  1.00 26.08  ? 318  ARG C CZ  1 
ATOM   6390  N NH1 . ARG C  1 318 ? 22.636  36.476 20.856  1.00 28.42  ? 318  ARG C NH1 1 
ATOM   6391  N NH2 . ARG C  1 318 ? 23.372  38.471 21.727  1.00 26.25  ? 318  ARG C NH2 1 
ATOM   6392  N N   . ASN C  1 319 ? 28.157  32.596 20.068  1.00 23.28  ? 319  ASN C N   1 
ATOM   6393  C CA  . ASN C  1 319 ? 28.269  31.322 19.389  1.00 25.51  ? 319  ASN C CA  1 
ATOM   6394  C C   . ASN C  1 319 ? 26.982  30.988 18.645  1.00 28.15  ? 319  ASN C C   1 
ATOM   6395  O O   . ASN C  1 319 ? 25.884  31.301 19.105  1.00 29.06  ? 319  ASN C O   1 
ATOM   6396  C CB  . ASN C  1 319 ? 28.602  30.228 20.394  1.00 26.71  ? 319  ASN C CB  1 
ATOM   6397  C CG  . ASN C  1 319 ? 29.056  28.949 19.735  1.00 29.14  ? 319  ASN C CG  1 
ATOM   6398  O OD1 . ASN C  1 319 ? 29.243  28.891 18.524  1.00 29.66  ? 319  ASN C OD1 1 
ATOM   6399  N ND2 . ASN C  1 319 ? 29.238  27.913 20.534  1.00 31.01  ? 319  ASN C ND2 1 
ATOM   6400  N N   . SER C  1 320 ? 27.133  30.332 17.498  1.00 29.99  ? 320  SER C N   1 
ATOM   6401  C CA  . SER C  1 320 ? 26.041  30.162 16.538  1.00 32.59  ? 320  SER C CA  1 
ATOM   6402  C C   . SER C  1 320 ? 25.244  28.870 16.760  1.00 36.82  ? 320  SER C C   1 
ATOM   6403  O O   . SER C  1 320 ? 25.813  27.853 17.166  1.00 38.16  ? 320  SER C O   1 
ATOM   6404  C CB  . SER C  1 320 ? 26.604  30.183 15.113  1.00 32.48  ? 320  SER C CB  1 
ATOM   6405  O OG  . SER C  1 320 ? 27.437  31.316 14.923  1.00 29.27  ? 320  SER C OG  1 
ATOM   6406  N N   . PRO C  1 321 ? 23.920  28.909 16.493  1.00 39.58  ? 321  PRO C N   1 
ATOM   6407  C CA  . PRO C  1 321 ? 23.081  27.709 16.528  1.00 44.41  ? 321  PRO C CA  1 
ATOM   6408  C C   . PRO C  1 321 ? 23.133  26.936 15.215  1.00 47.28  ? 321  PRO C C   1 
ATOM   6409  O O   . PRO C  1 321 ? 24.176  26.386 14.868  1.00 46.97  ? 321  PRO C O   1 
ATOM   6410  C CB  . PRO C  1 321 ? 21.677  28.277 16.747  1.00 46.22  ? 321  PRO C CB  1 
ATOM   6411  C CG  . PRO C  1 321 ? 21.714  29.607 16.068  1.00 43.36  ? 321  PRO C CG  1 
ATOM   6412  C CD  . PRO C  1 321 ? 23.116  30.128 16.259  1.00 38.77  ? 321  PRO C CD  1 
ATOM   6413  N N   . GLY D  2 1   ? 23.625  42.530 17.223  1.00 17.54  ? 1    GLY D N   1 
ATOM   6414  C CA  . GLY D  2 1   ? 24.741  43.316 17.817  1.00 15.80  ? 1    GLY D CA  1 
ATOM   6415  C C   . GLY D  2 1   ? 24.833  44.705 17.229  1.00 16.04  ? 1    GLY D C   1 
ATOM   6416  O O   . GLY D  2 1   ? 24.342  44.956 16.134  1.00 17.16  ? 1    GLY D O   1 
ATOM   6417  N N   . LEU D  2 2   ? 25.499  45.597 17.952  1.00 15.29  ? 2    LEU D N   1 
ATOM   6418  C CA  . LEU D  2 2   ? 25.552  47.008 17.588  1.00 16.10  ? 2    LEU D CA  1 
ATOM   6419  C C   . LEU D  2 2   ? 26.114  47.283 16.198  1.00 16.30  ? 2    LEU D C   1 
ATOM   6420  O O   . LEU D  2 2   ? 25.691  48.230 15.539  1.00 17.84  ? 2    LEU D O   1 
ATOM   6421  C CB  . LEU D  2 2   ? 26.368  47.791 18.620  1.00 15.46  ? 2    LEU D CB  1 
ATOM   6422  C CG  . LEU D  2 2   ? 25.663  48.138 19.925  1.00 15.89  ? 2    LEU D CG  1 
ATOM   6423  C CD1 . LEU D  2 2   ? 26.639  48.818 20.863  1.00 15.30  ? 2    LEU D CD1 1 
ATOM   6424  C CD2 . LEU D  2 2   ? 24.451  49.023 19.680  1.00 18.07  ? 2    LEU D CD2 1 
ATOM   6425  N N   . PHE D  2 3   ? 27.059  46.460 15.756  1.00 15.03  ? 3    PHE D N   1 
ATOM   6426  C CA  . PHE D  2 3   ? 27.794  46.734 14.526  1.00 15.12  ? 3    PHE D CA  1 
ATOM   6427  C C   . PHE D  2 3   ? 27.290  45.954 13.322  1.00 15.57  ? 3    PHE D C   1 
ATOM   6428  O O   . PHE D  2 3   ? 27.781  46.135 12.213  1.00 15.75  ? 3    PHE D O   1 
ATOM   6429  C CB  . PHE D  2 3   ? 29.291  46.558 14.785  1.00 13.94  ? 3    PHE D CB  1 
ATOM   6430  C CG  . PHE D  2 3   ? 29.805  47.531 15.806  1.00 14.09  ? 3    PHE D CG  1 
ATOM   6431  C CD1 . PHE D  2 3   ? 30.179  48.816 15.431  1.00 15.33  ? 3    PHE D CD1 1 
ATOM   6432  C CD2 . PHE D  2 3   ? 29.823  47.197 17.152  1.00 13.37  ? 3    PHE D CD2 1 
ATOM   6433  C CE1 . PHE D  2 3   ? 30.606  49.728 16.371  1.00 15.92  ? 3    PHE D CE1 1 
ATOM   6434  C CE2 . PHE D  2 3   ? 30.246  48.109 18.099  1.00 13.72  ? 3    PHE D CE2 1 
ATOM   6435  C CZ  . PHE D  2 3   ? 30.637  49.376 17.708  1.00 15.04  ? 3    PHE D CZ  1 
ATOM   6436  N N   . GLY D  2 4   ? 26.296  45.097 13.551  1.00 16.05  ? 4    GLY D N   1 
ATOM   6437  C CA  . GLY D  2 4   ? 25.508  44.498 12.482  1.00 17.23  ? 4    GLY D CA  1 
ATOM   6438  C C   . GLY D  2 4   ? 26.142  43.354 11.717  1.00 16.56  ? 4    GLY D C   1 
ATOM   6439  O O   . GLY D  2 4   ? 25.537  42.847 10.777  1.00 17.70  ? 4    GLY D O   1 
ATOM   6440  N N   . ALA D  2 5   ? 27.344  42.935 12.110  1.00 15.13  ? 5    ALA D N   1 
ATOM   6441  C CA  . ALA D  2 5   ? 28.079  41.905 11.382  1.00 14.73  ? 5    ALA D CA  1 
ATOM   6442  C C   . ALA D  2 5   ? 27.760  40.522 11.926  1.00 15.11  ? 5    ALA D C   1 
ATOM   6443  O O   . ALA D  2 5   ? 27.204  39.689 11.222  1.00 16.16  ? 5    ALA D O   1 
ATOM   6444  C CB  . ALA D  2 5   ? 29.572  42.178 11.449  1.00 13.66  ? 5    ALA D CB  1 
ATOM   6445  N N   . ILE D  2 6   ? 28.099  40.291 13.189  1.00 14.61  ? 6    ILE D N   1 
ATOM   6446  C CA  . ILE D  2 6   ? 27.859  39.005 13.840  1.00 15.34  ? 6    ILE D CA  1 
ATOM   6447  C C   . ILE D  2 6   ? 26.366  38.776 14.005  1.00 16.94  ? 6    ILE D C   1 
ATOM   6448  O O   . ILE D  2 6   ? 25.664  39.621 14.551  1.00 17.10  ? 6    ILE D O   1 
ATOM   6449  C CB  . ILE D  2 6   ? 28.559  38.927 15.213  1.00 14.60  ? 6    ILE D CB  1 
ATOM   6450  C CG1 . ILE D  2 6   ? 30.075  38.879 15.008  1.00 13.85  ? 6    ILE D CG1 1 
ATOM   6451  C CG2 . ILE D  2 6   ? 28.092  37.706 15.994  1.00 15.79  ? 6    ILE D CG2 1 
ATOM   6452  C CD1 . ILE D  2 6   ? 30.887  38.873 16.284  1.00 13.48  ? 6    ILE D CD1 1 
ATOM   6453  N N   . ALA D  2 7   ? 25.888  37.631 13.526  1.00 18.57  ? 7    ALA D N   1 
ATOM   6454  C CA  . ALA D  2 7   ? 24.464  37.309 13.544  1.00 20.81  ? 7    ALA D CA  1 
ATOM   6455  C C   . ALA D  2 7   ? 23.649  38.394 12.855  1.00 21.43  ? 7    ALA D C   1 
ATOM   6456  O O   . ALA D  2 7   ? 22.509  38.646 13.227  1.00 23.05  ? 7    ALA D O   1 
ATOM   6457  C CB  . ALA D  2 7   ? 23.982  37.112 14.975  1.00 21.34  ? 7    ALA D CB  1 
ATOM   6458  N N   . GLY D  2 8   ? 24.243  39.031 11.852  1.00 20.50  ? 8    GLY D N   1 
ATOM   6459  C CA  . GLY D  2 8   ? 23.626  40.166 11.183  1.00 21.26  ? 8    GLY D CA  1 
ATOM   6460  C C   . GLY D  2 8   ? 23.626  39.939 9.692   1.00 22.08  ? 8    GLY D C   1 
ATOM   6461  O O   . GLY D  2 8   ? 22.852  39.130 9.197   1.00 24.03  ? 8    GLY D O   1 
ATOM   6462  N N   . PHE D  2 9   ? 24.491  40.648 8.974   1.00 20.90  ? 9    PHE D N   1 
ATOM   6463  C CA  . PHE D  2 9   ? 24.640  40.409 7.548   1.00 21.51  ? 9    PHE D CA  1 
ATOM   6464  C C   . PHE D  2 9   ? 25.539  39.192 7.320   1.00 20.78  ? 9    PHE D C   1 
ATOM   6465  O O   . PHE D  2 9   ? 25.490  38.586 6.256   1.00 21.64  ? 9    PHE D O   1 
ATOM   6466  C CB  . PHE D  2 9   ? 25.121  41.665 6.794   1.00 21.04  ? 9    PHE D CB  1 
ATOM   6467  C CG  . PHE D  2 9   ? 26.583  41.979 6.963   1.00 18.99  ? 9    PHE D CG  1 
ATOM   6468  C CD1 . PHE D  2 9   ? 27.526  41.422 6.118   1.00 18.30  ? 9    PHE D CD1 1 
ATOM   6469  C CD2 . PHE D  2 9   ? 27.007  42.868 7.935   1.00 18.14  ? 9    PHE D CD2 1 
ATOM   6470  C CE1 . PHE D  2 9   ? 28.867  41.724 6.262   1.00 16.97  ? 9    PHE D CE1 1 
ATOM   6471  C CE2 . PHE D  2 9   ? 28.350  43.172 8.087   1.00 16.82  ? 9    PHE D CE2 1 
ATOM   6472  C CZ  . PHE D  2 9   ? 29.281  42.597 7.251   1.00 16.31  ? 9    PHE D CZ  1 
ATOM   6473  N N   . ILE D  2 10  ? 26.352  38.845 8.319   1.00 19.54  ? 10   ILE D N   1 
ATOM   6474  C CA  . ILE D  2 10  ? 27.019  37.541 8.365   1.00 19.62  ? 10   ILE D CA  1 
ATOM   6475  C C   . ILE D  2 10  ? 26.208  36.658 9.301   1.00 21.13  ? 10   ILE D C   1 
ATOM   6476  O O   . ILE D  2 10  ? 26.343  36.739 10.520  1.00 20.52  ? 10   ILE D O   1 
ATOM   6477  C CB  . ILE D  2 10  ? 28.467  37.641 8.868   1.00 17.93  ? 10   ILE D CB  1 
ATOM   6478  C CG1 . ILE D  2 10  ? 29.266  38.607 7.992   1.00 16.95  ? 10   ILE D CG1 1 
ATOM   6479  C CG2 . ILE D  2 10  ? 29.123  36.268 8.857   1.00 18.55  ? 10   ILE D CG2 1 
ATOM   6480  C CD1 . ILE D  2 10  ? 30.635  38.953 8.539   1.00 15.77  ? 10   ILE D CD1 1 
ATOM   6481  N N   . GLU D  2 11  ? 25.371  35.804 8.726   1.00 23.42  ? 11   GLU D N   1 
ATOM   6482  C CA  . GLU D  2 11  ? 24.332  35.117 9.494   1.00 25.65  ? 11   GLU D CA  1 
ATOM   6483  C C   . GLU D  2 11  ? 24.837  34.200 10.597  1.00 25.72  ? 11   GLU D C   1 
ATOM   6484  O O   . GLU D  2 11  ? 24.158  34.038 11.612  1.00 26.79  ? 11   GLU D O   1 
ATOM   6485  C CB  . GLU D  2 11  ? 23.431  34.311 8.566   1.00 28.65  ? 11   GLU D CB  1 
ATOM   6486  C CG  . GLU D  2 11  ? 22.611  35.156 7.608   1.00 29.59  ? 11   GLU D CG  1 
ATOM   6487  C CD  . GLU D  2 11  ? 21.373  34.423 7.130   1.00 33.33  ? 11   GLU D CD  1 
ATOM   6488  O OE1 . GLU D  2 11  ? 21.525  33.444 6.357   1.00 34.73  ? 11   GLU D OE1 1 
ATOM   6489  O OE2 . GLU D  2 11  ? 20.255  34.822 7.535   1.00 35.22  ? 11   GLU D OE2 1 
ATOM   6490  N N   . GLY D  2 12  ? 26.005  33.595 10.398  1.00 24.95  ? 12   GLY D N   1 
ATOM   6491  C CA  . GLY D  2 12  ? 26.545  32.629 11.356  1.00 25.62  ? 12   GLY D CA  1 
ATOM   6492  C C   . GLY D  2 12  ? 28.050  32.442 11.296  1.00 24.33  ? 12   GLY D C   1 
ATOM   6493  O O   . GLY D  2 12  ? 28.701  32.828 10.324  1.00 23.19  ? 12   GLY D O   1 
ATOM   6494  N N   . GLY D  2 13  ? 28.596  31.840 12.350  1.00 24.83  ? 13   GLY D N   1 
ATOM   6495  C CA  . GLY D  2 13  ? 30.033  31.599 12.461  1.00 24.28  ? 13   GLY D CA  1 
ATOM   6496  C C   . GLY D  2 13  ? 30.491  30.365 11.703  1.00 26.43  ? 13   GLY D C   1 
ATOM   6497  O O   . GLY D  2 13  ? 29.684  29.668 11.085  1.00 28.37  ? 13   GLY D O   1 
ATOM   6498  N N   . TRP D  2 14  ? 31.794  30.099 11.764  1.00 26.45  ? 14   TRP D N   1 
ATOM   6499  C CA  . TRP D  2 14  ? 32.407  28.984 11.053  1.00 28.64  ? 14   TRP D CA  1 
ATOM   6500  C C   . TRP D  2 14  ? 33.044  27.988 12.009  1.00 31.07  ? 14   TRP D C   1 
ATOM   6501  O O   . TRP D  2 14  ? 34.096  28.255 12.589  1.00 30.54  ? 14   TRP D O   1 
ATOM   6502  C CB  . TRP D  2 14  ? 33.481  29.495 10.100  1.00 27.25  ? 14   TRP D CB  1 
ATOM   6503  C CG  . TRP D  2 14  ? 32.959  30.318 8.970   1.00 25.50  ? 14   TRP D CG  1 
ATOM   6504  C CD1 . TRP D  2 14  ? 31.711  30.270 8.427   1.00 25.91  ? 14   TRP D CD1 1 
ATOM   6505  C CD2 . TRP D  2 14  ? 33.689  31.289 8.214   1.00 23.56  ? 14   TRP D CD2 1 
ATOM   6506  N NE1 . TRP D  2 14  ? 31.613  31.161 7.387   1.00 24.30  ? 14   TRP D NE1 1 
ATOM   6507  C CE2 . TRP D  2 14  ? 32.814  31.799 7.234   1.00 22.80  ? 14   TRP D CE2 1 
ATOM   6508  C CE3 . TRP D  2 14  ? 34.996  31.783 8.275   1.00 22.81  ? 14   TRP D CE3 1 
ATOM   6509  C CZ2 . TRP D  2 14  ? 33.202  32.782 6.323   1.00 21.23  ? 14   TRP D CZ2 1 
ATOM   6510  C CZ3 . TRP D  2 14  ? 35.378  32.758 7.372   1.00 21.33  ? 14   TRP D CZ3 1 
ATOM   6511  C CH2 . TRP D  2 14  ? 34.483  33.248 6.408   1.00 20.50  ? 14   TRP D CH2 1 
ATOM   6512  N N   . GLN D  2 15  ? 32.409  26.830 12.151  1.00 34.19  ? 15   GLN D N   1 
ATOM   6513  C CA  . GLN D  2 15  ? 32.997  25.705 12.878  1.00 37.45  ? 15   GLN D CA  1 
ATOM   6514  C C   . GLN D  2 15  ? 34.351  25.321 12.268  1.00 38.45  ? 15   GLN D C   1 
ATOM   6515  O O   . GLN D  2 15  ? 35.257  24.901 12.982  1.00 40.14  ? 15   GLN D O   1 
ATOM   6516  C CB  . GLN D  2 15  ? 32.062  24.495 12.832  1.00 41.25  ? 15   GLN D CB  1 
ATOM   6517  C CG  . GLN D  2 15  ? 30.717  24.684 13.525  1.00 41.32  ? 15   GLN D CG  1 
ATOM   6518  C CD  . GLN D  2 15  ? 30.716  24.252 14.981  1.00 43.13  ? 15   GLN D CD  1 
ATOM   6519  O OE1 . GLN D  2 15  ? 30.172  24.946 15.843  1.00 41.45  ? 15   GLN D OE1 1 
ATOM   6520  N NE2 . GLN D  2 15  ? 31.304  23.092 15.262  1.00 46.88  ? 15   GLN D NE2 1 
ATOM   6521  N N   . GLY D  2 16  ? 34.478  25.479 10.949  1.00 37.64  ? 16   GLY D N   1 
ATOM   6522  C CA  . GLY D  2 16  ? 35.697  25.123 10.217  1.00 38.73  ? 16   GLY D CA  1 
ATOM   6523  C C   . GLY D  2 16  ? 36.906  26.034 10.379  1.00 36.74  ? 16   GLY D C   1 
ATOM   6524  O O   . GLY D  2 16  ? 37.991  25.698 9.920   1.00 38.20  ? 16   GLY D O   1 
ATOM   6525  N N   . MET D  2 17  ? 36.734  27.189 11.018  1.00 33.79  ? 17   MET D N   1 
ATOM   6526  C CA  . MET D  2 17  ? 37.866  28.071 11.314  1.00 32.44  ? 17   MET D CA  1 
ATOM   6527  C C   . MET D  2 17  ? 38.267  27.959 12.782  1.00 33.50  ? 17   MET D C   1 
ATOM   6528  O O   . MET D  2 17  ? 37.617  28.529 13.651  1.00 31.87  ? 17   MET D O   1 
ATOM   6529  C CB  . MET D  2 17  ? 37.523  29.518 10.986  1.00 28.83  ? 17   MET D CB  1 
ATOM   6530  C CG  . MET D  2 17  ? 38.735  30.432 11.028  1.00 27.96  ? 17   MET D CG  1 
ATOM   6531  S SD  . MET D  2 17  ? 38.346  32.066 10.409  1.00 24.53  ? 17   MET D SD  1 
ATOM   6532  C CE  . MET D  2 17  ? 37.127  32.554 11.623  1.00 23.01  ? 17   MET D CE  1 
ATOM   6533  N N   . VAL D  2 18  ? 39.352  27.234 13.042  1.00 36.47  ? 18   VAL D N   1 
ATOM   6534  C CA  . VAL D  2 18  ? 39.757  26.885 14.410  1.00 38.43  ? 18   VAL D CA  1 
ATOM   6535  C C   . VAL D  2 18  ? 40.988  27.645 14.920  1.00 38.27  ? 18   VAL D C   1 
ATOM   6536  O O   . VAL D  2 18  ? 41.221  27.704 16.123  1.00 39.07  ? 18   VAL D O   1 
ATOM   6537  C CB  . VAL D  2 18  ? 40.023  25.366 14.536  1.00 43.07  ? 18   VAL D CB  1 
ATOM   6538  C CG1 . VAL D  2 18  ? 38.852  24.572 13.973  1.00 43.90  ? 18   VAL D CG1 1 
ATOM   6539  C CG2 . VAL D  2 18  ? 41.322  24.967 13.845  1.00 45.59  ? 18   VAL D CG2 1 
ATOM   6540  N N   . ASP D  2 19  ? 41.765  28.226 14.012  1.00 37.54  ? 19   ASP D N   1 
ATOM   6541  C CA  . ASP D  2 19  ? 43.035  28.864 14.373  1.00 38.30  ? 19   ASP D CA  1 
ATOM   6542  C C   . ASP D  2 19  ? 42.915  30.382 14.595  1.00 34.87  ? 19   ASP D C   1 
ATOM   6543  O O   . ASP D  2 19  ? 43.925  31.082 14.678  1.00 35.38  ? 19   ASP D O   1 
ATOM   6544  C CB  . ASP D  2 19  ? 44.111  28.545 13.316  1.00 40.52  ? 19   ASP D CB  1 
ATOM   6545  C CG  . ASP D  2 19  ? 43.674  28.885 11.894  1.00 38.28  ? 19   ASP D CG  1 
ATOM   6546  O OD1 . ASP D  2 19  ? 42.513  29.308 11.699  1.00 35.29  ? 19   ASP D OD1 1 
ATOM   6547  O OD2 . ASP D  2 19  ? 44.498  28.717 10.965  1.00 39.77  ? 19   ASP D OD2 1 
ATOM   6548  N N   . GLY D  2 20  ? 41.688  30.887 14.703  1.00 31.84  ? 20   GLY D N   1 
ATOM   6549  C CA  . GLY D  2 20  ? 41.477  32.301 14.994  1.00 29.00  ? 20   GLY D CA  1 
ATOM   6550  C C   . GLY D  2 20  ? 40.025  32.666 15.226  1.00 26.40  ? 20   GLY D C   1 
ATOM   6551  O O   . GLY D  2 20  ? 39.128  31.855 14.990  1.00 26.66  ? 20   GLY D O   1 
ATOM   6552  N N   . TRP D  2 21  ? 39.802  33.897 15.682  1.00 24.28  ? 21   TRP D N   1 
ATOM   6553  C CA  . TRP D  2 21  ? 38.455  34.402 15.952  1.00 22.04  ? 21   TRP D CA  1 
ATOM   6554  C C   . TRP D  2 21  ? 37.793  34.972 14.702  1.00 20.31  ? 21   TRP D C   1 
ATOM   6555  O O   . TRP D  2 21  ? 36.595  34.772 14.480  1.00 19.56  ? 21   TRP D O   1 
ATOM   6556  C CB  . TRP D  2 21  ? 38.480  35.474 17.052  1.00 20.94  ? 21   TRP D CB  1 
ATOM   6557  C CG  . TRP D  2 21  ? 38.190  34.962 18.434  1.00 21.70  ? 21   TRP D CG  1 
ATOM   6558  C CD1 . TRP D  2 21  ? 37.359  33.928 18.781  1.00 22.52  ? 21   TRP D CD1 1 
ATOM   6559  C CD2 . TRP D  2 21  ? 38.690  35.495 19.657  1.00 21.96  ? 21   TRP D CD2 1 
ATOM   6560  N NE1 . TRP D  2 21  ? 37.336  33.769 20.145  1.00 23.20  ? 21   TRP D NE1 1 
ATOM   6561  C CE2 . TRP D  2 21  ? 38.143  34.721 20.707  1.00 22.77  ? 21   TRP D CE2 1 
ATOM   6562  C CE3 . TRP D  2 21  ? 39.554  36.548 19.971  1.00 21.90  ? 21   TRP D CE3 1 
ATOM   6563  C CZ2 . TRP D  2 21  ? 38.434  34.967 22.042  1.00 23.26  ? 21   TRP D CZ2 1 
ATOM   6564  C CZ3 . TRP D  2 21  ? 39.844  36.794 21.299  1.00 22.51  ? 21   TRP D CZ3 1 
ATOM   6565  C CH2 . TRP D  2 21  ? 39.284  36.007 22.321  1.00 23.06  ? 21   TRP D CH2 1 
ATOM   6566  N N   . TYR D  2 22  ? 38.570  35.701 13.906  1.00 20.01  ? 22   TYR D N   1 
ATOM   6567  C CA  . TYR D  2 22  ? 38.079  36.300 12.667  1.00 18.71  ? 22   TYR D CA  1 
ATOM   6568  C C   . TYR D  2 22  ? 38.989  35.877 11.523  1.00 19.94  ? 22   TYR D C   1 
ATOM   6569  O O   . TYR D  2 22  ? 40.189  35.677 11.719  1.00 21.53  ? 22   TYR D O   1 
ATOM   6570  C CB  . TYR D  2 22  ? 38.063  37.832 12.765  1.00 17.35  ? 22   TYR D CB  1 
ATOM   6571  C CG  . TYR D  2 22  ? 37.846  38.382 14.162  1.00 16.82  ? 22   TYR D CG  1 
ATOM   6572  C CD1 . TYR D  2 22  ? 36.609  38.298 14.780  1.00 15.86  ? 22   TYR D CD1 1 
ATOM   6573  C CD2 . TYR D  2 22  ? 38.886  38.981 14.865  1.00 17.57  ? 22   TYR D CD2 1 
ATOM   6574  C CE1 . TYR D  2 22  ? 36.411  38.799 16.056  1.00 15.46  ? 22   TYR D CE1 1 
ATOM   6575  C CE2 . TYR D  2 22  ? 38.698  39.483 16.136  1.00 17.21  ? 22   TYR D CE2 1 
ATOM   6576  C CZ  . TYR D  2 22  ? 37.460  39.392 16.724  1.00 16.03  ? 22   TYR D CZ  1 
ATOM   6577  O OH  . TYR D  2 22  ? 37.273  39.890 17.986  1.00 15.72  ? 22   TYR D OH  1 
ATOM   6578  N N   . GLY D  2 23  ? 38.424  35.739 10.331  1.00 19.50  ? 23   GLY D N   1 
ATOM   6579  C CA  . GLY D  2 23  ? 39.228  35.396 9.172   1.00 20.62  ? 23   GLY D CA  1 
ATOM   6580  C C   . GLY D  2 23  ? 38.452  35.319 7.881   1.00 20.00  ? 23   GLY D C   1 
ATOM   6581  O O   . GLY D  2 23  ? 37.330  35.822 7.786   1.00 18.67  ? 23   GLY D O   1 
ATOM   6582  N N   . TYR D  2 24  ? 39.063  34.665 6.897   1.00 21.33  ? 24   TYR D N   1 
ATOM   6583  C CA  . TYR D  2 24  ? 38.537  34.600 5.539   1.00 21.06  ? 24   TYR D CA  1 
ATOM   6584  C C   . TYR D  2 24  ? 38.258  33.165 5.114   1.00 22.64  ? 24   TYR D C   1 
ATOM   6585  O O   . TYR D  2 24  ? 38.923  32.236 5.565   1.00 24.44  ? 24   TYR D O   1 
ATOM   6586  C CB  . TYR D  2 24  ? 39.539  35.199 4.544   1.00 21.35  ? 24   TYR D CB  1 
ATOM   6587  C CG  . TYR D  2 24  ? 40.263  36.429 5.031   1.00 21.08  ? 24   TYR D CG  1 
ATOM   6588  C CD1 . TYR D  2 24  ? 41.345  36.322 5.897   1.00 22.48  ? 24   TYR D CD1 1 
ATOM   6589  C CD2 . TYR D  2 24  ? 39.883  37.698 4.612   1.00 19.93  ? 24   TYR D CD2 1 
ATOM   6590  C CE1 . TYR D  2 24  ? 42.021  37.443 6.344   1.00 22.66  ? 24   TYR D CE1 1 
ATOM   6591  C CE2 . TYR D  2 24  ? 40.552  38.830 5.058   1.00 20.18  ? 24   TYR D CE2 1 
ATOM   6592  C CZ  . TYR D  2 24  ? 41.622  38.695 5.922   1.00 21.53  ? 24   TYR D CZ  1 
ATOM   6593  O OH  . TYR D  2 24  ? 42.304  39.801 6.368   1.00 22.23  ? 24   TYR D OH  1 
ATOM   6594  N N   . HIS D  2 25  ? 37.271  33.002 4.239   1.00 22.40  ? 25   HIS D N   1 
ATOM   6595  C CA  . HIS D  2 25  ? 37.072  31.753 3.520   1.00 24.25  ? 25   HIS D CA  1 
ATOM   6596  C C   . HIS D  2 25  ? 37.022  32.032 2.026   1.00 23.94  ? 25   HIS D C   1 
ATOM   6597  O O   . HIS D  2 25  ? 36.207  32.827 1.566   1.00 22.61  ? 25   HIS D O   1 
ATOM   6598  C CB  . HIS D  2 25  ? 35.788  31.055 3.946   1.00 24.98  ? 25   HIS D CB  1 
ATOM   6599  C CG  . HIS D  2 25  ? 35.572  29.745 3.258   1.00 27.40  ? 25   HIS D CG  1 
ATOM   6600  N ND1 . HIS D  2 25  ? 34.842  29.628 2.096   1.00 27.60  ? 25   HIS D ND1 1 
ATOM   6601  C CD2 . HIS D  2 25  ? 36.009  28.499 3.556   1.00 29.99  ? 25   HIS D CD2 1 
ATOM   6602  C CE1 . HIS D  2 25  ? 34.827  28.364 1.713   1.00 30.17  ? 25   HIS D CE1 1 
ATOM   6603  N NE2 . HIS D  2 25  ? 35.529  27.658 2.582   1.00 31.74  ? 25   HIS D NE2 1 
ATOM   6604  N N   . HIS D  2 26  ? 37.896  31.364 1.278   1.00 25.49  ? 26   HIS D N   1 
ATOM   6605  C CA  . HIS D  2 26  ? 37.997  31.555 -0.166  1.00 25.41  ? 26   HIS D CA  1 
ATOM   6606  C C   . HIS D  2 26  ? 37.484  30.323 -0.892  1.00 27.24  ? 26   HIS D C   1 
ATOM   6607  O O   . HIS D  2 26  ? 37.501  29.235 -0.337  1.00 29.16  ? 26   HIS D O   1 
ATOM   6608  C CB  . HIS D  2 26  ? 39.450  31.829 -0.557  1.00 25.97  ? 26   HIS D CB  1 
ATOM   6609  C CG  . HIS D  2 26  ? 40.344  30.631 -0.466  1.00 28.52  ? 26   HIS D CG  1 
ATOM   6610  N ND1 . HIS D  2 26  ? 41.070  30.328 0.665   1.00 29.78  ? 26   HIS D ND1 1 
ATOM   6611  C CD2 . HIS D  2 26  ? 40.632  29.663 -1.368  1.00 30.40  ? 26   HIS D CD2 1 
ATOM   6612  C CE1 . HIS D  2 26  ? 41.767  29.225 0.456   1.00 32.46  ? 26   HIS D CE1 1 
ATOM   6613  N NE2 . HIS D  2 26  ? 41.518  28.801 -0.769  1.00 32.88  ? 26   HIS D NE2 1 
ATOM   6614  N N   . SER D  2 27  ? 37.015  30.504 -2.124  1.00 27.00  ? 27   SER D N   1 
ATOM   6615  C CA  . SER D  2 27  ? 36.648  29.377 -2.987  1.00 29.01  ? 27   SER D CA  1 
ATOM   6616  C C   . SER D  2 27  ? 36.905  29.726 -4.457  1.00 28.73  ? 27   SER D C   1 
ATOM   6617  O O   . SER D  2 27  ? 36.368  30.707 -4.971  1.00 27.18  ? 27   SER D O   1 
ATOM   6618  C CB  . SER D  2 27  ? 35.189  28.964 -2.771  1.00 29.68  ? 27   SER D CB  1 
ATOM   6619  O OG  . SER D  2 27  ? 34.297  29.887 -3.359  1.00 28.32  ? 27   SER D OG  1 
ATOM   6620  N N   . ASN D  2 28  ? 37.743  28.925 -5.111  1.00 30.51  ? 28   ASN D N   1 
ATOM   6621  C CA  . ASN D  2 28  ? 38.117  29.137 -6.506  1.00 30.55  ? 28   ASN D CA  1 
ATOM   6622  C C   . ASN D  2 28  ? 38.334  27.790 -7.204  1.00 33.33  ? 28   ASN D C   1 
ATOM   6623  O O   . ASN D  2 28  ? 37.991  26.747 -6.642  1.00 35.28  ? 28   ASN D O   1 
ATOM   6624  C CB  . ASN D  2 28  ? 39.355  30.045 -6.589  1.00 29.58  ? 28   ASN D CB  1 
ATOM   6625  C CG  . ASN D  2 28  ? 40.580  29.450 -5.921  1.00 31.22  ? 28   ASN D CG  1 
ATOM   6626  O OD1 . ASN D  2 28  ? 40.622  28.266 -5.613  1.00 33.32  ? 28   ASN D OD1 1 
ATOM   6627  N ND2 . ASN D  2 28  ? 41.587  30.281 -5.692  1.00 30.74  ? 28   ASN D ND2 1 
ATOM   6628  N N   . GLU D  2 29  ? 38.882  27.804 -8.419  1.00 33.83  ? 29   GLU D N   1 
ATOM   6629  C CA  . GLU D  2 29  ? 39.109  26.565 -9.173  1.00 36.63  ? 29   GLU D CA  1 
ATOM   6630  C C   . GLU D  2 29  ? 40.007  25.571 -8.434  1.00 39.15  ? 29   GLU D C   1 
ATOM   6631  O O   . GLU D  2 29  ? 39.759  24.368 -8.468  1.00 41.90  ? 29   GLU D O   1 
ATOM   6632  C CB  . GLU D  2 29  ? 39.725  26.864 -10.542 1.00 36.65  ? 29   GLU D CB  1 
ATOM   6633  C CG  . GLU D  2 29  ? 38.786  27.559 -11.521 1.00 35.24  ? 29   GLU D CG  1 
ATOM   6634  C CD  . GLU D  2 29  ? 39.257  27.456 -12.968 1.00 36.02  ? 29   GLU D CD  1 
ATOM   6635  O OE1 . GLU D  2 29  ? 40.441  27.112 -13.206 1.00 37.26  ? 29   GLU D OE1 1 
ATOM   6636  O OE2 . GLU D  2 29  ? 38.442  27.733 -13.875 1.00 35.64  ? 29   GLU D OE2 1 
ATOM   6637  N N   . GLN D  2 30  ? 41.045  26.081 -7.776  1.00 38.66  ? 30   GLN D N   1 
ATOM   6638  C CA  . GLN D  2 30  ? 42.016  25.241 -7.067  1.00 41.38  ? 30   GLN D CA  1 
ATOM   6639  C C   . GLN D  2 30  ? 41.472  24.621 -5.775  1.00 42.31  ? 30   GLN D C   1 
ATOM   6640  O O   . GLN D  2 30  ? 41.936  23.568 -5.353  1.00 45.51  ? 30   GLN D O   1 
ATOM   6641  C CB  . GLN D  2 30  ? 43.274  26.053 -6.756  1.00 40.98  ? 30   GLN D CB  1 
ATOM   6642  C CG  . GLN D  2 30  ? 44.037  26.486 -8.001  1.00 41.04  ? 30   GLN D CG  1 
ATOM   6643  C CD  . GLN D  2 30  ? 44.371  27.968 -7.996  1.00 38.66  ? 30   GLN D CD  1 
ATOM   6644  O OE1 . GLN D  2 30  ? 43.575  28.802 -8.456  1.00 36.22  ? 30   GLN D OE1 1 
ATOM   6645  N NE2 . GLN D  2 30  ? 45.554  28.306 -7.479  1.00 39.84  ? 30   GLN D NE2 1 
ATOM   6646  N N   . GLY D  2 31  ? 40.505  25.275 -5.143  1.00 39.81  ? 31   GLY D N   1 
ATOM   6647  C CA  . GLY D  2 31  ? 39.891  24.736 -3.929  1.00 40.66  ? 31   GLY D CA  1 
ATOM   6648  C C   . GLY D  2 31  ? 39.281  25.799 -3.044  1.00 37.57  ? 31   GLY D C   1 
ATOM   6649  O O   . GLY D  2 31  ? 39.043  26.917 -3.481  1.00 34.84  ? 31   GLY D O   1 
ATOM   6650  N N   . SER D  2 32  ? 39.026  25.435 -1.793  1.00 38.27  ? 32   SER D N   1 
ATOM   6651  C CA  . SER D  2 32  ? 38.516  26.371 -0.797  1.00 35.70  ? 32   SER D CA  1 
ATOM   6652  C C   . SER D  2 32  ? 39.199  26.150 0.543   1.00 36.71  ? 32   SER D C   1 
ATOM   6653  O O   . SER D  2 32  ? 39.811  25.110 0.765   1.00 39.82  ? 32   SER D O   1 
ATOM   6654  C CB  . SER D  2 32  ? 37.007  26.209 -0.643  1.00 35.47  ? 32   SER D CB  1 
ATOM   6655  O OG  . SER D  2 32  ? 36.669  24.878 -0.328  1.00 38.77  ? 32   SER D OG  1 
ATOM   6656  N N   . GLY D  2 33  ? 39.099  27.127 1.436   1.00 34.40  ? 33   GLY D N   1 
ATOM   6657  C CA  . GLY D  2 33  ? 39.701  26.992 2.759   1.00 35.32  ? 33   GLY D CA  1 
ATOM   6658  C C   . GLY D  2 33  ? 39.527  28.178 3.688   1.00 32.62  ? 33   GLY D C   1 
ATOM   6659  O O   . GLY D  2 33  ? 39.221  29.284 3.255   1.00 30.03  ? 33   GLY D O   1 
ATOM   6660  N N   . TYR D  2 34  ? 39.740  27.927 4.976   1.00 33.57  ? 34   TYR D N   1 
ATOM   6661  C CA  . TYR D  2 34  ? 39.672  28.954 6.006   1.00 31.46  ? 34   TYR D CA  1 
ATOM   6662  C C   . TYR D  2 34  ? 41.070  29.443 6.352   1.00 32.07  ? 34   TYR D C   1 
ATOM   6663  O O   . TYR D  2 34  ? 41.992  28.650 6.480   1.00 34.92  ? 34   TYR D O   1 
ATOM   6664  C CB  . TYR D  2 34  ? 39.009  28.399 7.261   1.00 32.29  ? 34   TYR D CB  1 
ATOM   6665  C CG  . TYR D  2 34  ? 37.590  27.917 7.054   1.00 32.29  ? 34   TYR D CG  1 
ATOM   6666  C CD1 . TYR D  2 34  ? 36.525  28.809 7.051   1.00 29.74  ? 34   TYR D CD1 1 
ATOM   6667  C CD2 . TYR D  2 34  ? 37.310  26.567 6.871   1.00 35.37  ? 34   TYR D CD2 1 
ATOM   6668  C CE1 . TYR D  2 34  ? 35.224  28.368 6.866   1.00 30.30  ? 34   TYR D CE1 1 
ATOM   6669  C CE2 . TYR D  2 34  ? 36.011  26.121 6.687   1.00 35.94  ? 34   TYR D CE2 1 
ATOM   6670  C CZ  . TYR D  2 34  ? 34.974  27.024 6.687   1.00 33.42  ? 34   TYR D CZ  1 
ATOM   6671  O OH  . TYR D  2 34  ? 33.684  26.587 6.506   1.00 34.49  ? 34   TYR D OH  1 
ATOM   6672  N N   . ALA D  2 35  ? 41.220  30.754 6.496   1.00 29.90  ? 35   ALA D N   1 
ATOM   6673  C CA  . ALA D  2 35  ? 42.473  31.355 6.939   1.00 30.75  ? 35   ALA D CA  1 
ATOM   6674  C C   . ALA D  2 35  ? 42.173  32.424 7.986   1.00 28.95  ? 35   ALA D C   1 
ATOM   6675  O O   . ALA D  2 35  ? 41.477  33.396 7.709   1.00 26.59  ? 35   ALA D O   1 
ATOM   6676  C CB  . ALA D  2 35  ? 43.212  31.963 5.765   1.00 30.66  ? 35   ALA D CB  1 
ATOM   6677  N N   . ALA D  2 36  ? 42.684  32.232 9.196   1.00 30.41  ? 36   ALA D N   1 
ATOM   6678  C CA  . ALA D  2 36  ? 42.449  33.176 10.277  1.00 28.98  ? 36   ALA D CA  1 
ATOM   6679  C C   . ALA D  2 36  ? 43.271  34.443 10.072  1.00 28.73  ? 36   ALA D C   1 
ATOM   6680  O O   . ALA D  2 36  ? 44.448  34.375 9.731   1.00 30.91  ? 36   ALA D O   1 
ATOM   6681  C CB  . ALA D  2 36  ? 42.795  32.542 11.612  1.00 30.87  ? 36   ALA D CB  1 
ATOM   6682  N N   . ASP D  2 37  ? 42.639  35.595 10.283  1.00 26.58  ? 37   ASP D N   1 
ATOM   6683  C CA  . ASP D  2 37  ? 43.334  36.877 10.287  1.00 26.72  ? 37   ASP D CA  1 
ATOM   6684  C C   . ASP D  2 37  ? 44.023  37.064 11.647  1.00 28.25  ? 37   ASP D C   1 
ATOM   6685  O O   . ASP D  2 37  ? 43.356  37.246 12.674  1.00 27.03  ? 37   ASP D O   1 
ATOM   6686  C CB  . ASP D  2 37  ? 42.345  38.010 10.012  1.00 24.26  ? 37   ASP D CB  1 
ATOM   6687  C CG  . ASP D  2 37  ? 43.027  39.348 9.840   1.00 24.79  ? 37   ASP D CG  1 
ATOM   6688  O OD1 . ASP D  2 37  ? 43.276  40.028 10.864  1.00 25.14  ? 37   ASP D OD1 1 
ATOM   6689  O OD2 . ASP D  2 37  ? 43.321  39.714 8.681   1.00 25.08  ? 37   ASP D OD2 1 
ATOM   6690  N N   . LYS D  2 38  ? 45.355  37.004 11.644  1.00 31.14  ? 38   LYS D N   1 
ATOM   6691  C CA  . LYS D  2 38  ? 46.140  37.046 12.878  1.00 33.33  ? 38   LYS D CA  1 
ATOM   6692  C C   . LYS D  2 38  ? 46.079  38.398 13.578  1.00 32.50  ? 38   LYS D C   1 
ATOM   6693  O O   . LYS D  2 38  ? 45.869  38.457 14.790  1.00 32.34  ? 38   LYS D O   1 
ATOM   6694  C CB  . LYS D  2 38  ? 47.605  36.682 12.607  1.00 37.22  ? 38   LYS D CB  1 
ATOM   6695  C CG  . LYS D  2 38  ? 47.852  35.193 12.420  1.00 39.29  ? 38   LYS D CG  1 
ATOM   6696  C CD  . LYS D  2 38  ? 49.342  34.868 12.380  1.00 43.76  ? 38   LYS D CD  1 
ATOM   6697  C CE  . LYS D  2 38  ? 49.955  35.164 11.016  1.00 44.66  ? 38   LYS D CE  1 
ATOM   6698  N NZ  . LYS D  2 38  ? 51.444  35.037 11.037  1.00 49.40  ? 38   LYS D NZ  1 
ATOM   6699  N N   . GLU D  2 39  ? 46.283  39.473 12.817  1.00 32.31  ? 39   GLU D N   1 
ATOM   6700  C CA  . GLU D  2 39  ? 46.315  40.833 13.372  1.00 32.22  ? 39   GLU D CA  1 
ATOM   6701  C C   . GLU D  2 39  ? 45.062  41.168 14.185  1.00 29.30  ? 39   GLU D C   1 
ATOM   6702  O O   . GLU D  2 39  ? 45.162  41.506 15.364  1.00 29.74  ? 39   GLU D O   1 
ATOM   6703  C CB  . GLU D  2 39  ? 46.528  41.874 12.257  1.00 32.64  ? 39   GLU D CB  1 
ATOM   6704  C CG  . GLU D  2 39  ? 46.216  43.321 12.660  1.00 32.38  ? 39   GLU D CG  1 
ATOM   6705  C CD  . GLU D  2 39  ? 47.275  44.316 12.203  1.00 35.49  ? 39   GLU D CD  1 
ATOM   6706  O OE1 . GLU D  2 39  ? 47.675  44.276 11.015  1.00 36.40  ? 39   GLU D OE1 1 
ATOM   6707  O OE2 . GLU D  2 39  ? 47.722  45.131 13.047  1.00 37.38  ? 39   GLU D OE2 1 
ATOM   6708  N N   . SER D  2 40  ? 43.892  41.070 13.560  1.00 26.56  ? 40   SER D N   1 
ATOM   6709  C CA  . SER D  2 40  ? 42.638  41.388 14.246  1.00 24.15  ? 40   SER D CA  1 
ATOM   6710  C C   . SER D  2 40  ? 42.363  40.436 15.404  1.00 23.91  ? 40   SER D C   1 
ATOM   6711  O O   . SER D  2 40  ? 41.805  40.846 16.425  1.00 22.99  ? 40   SER D O   1 
ATOM   6712  C CB  . SER D  2 40  ? 41.457  41.378 13.274  1.00 22.06  ? 40   SER D CB  1 
ATOM   6713  O OG  . SER D  2 40  ? 41.284  40.106 12.682  1.00 21.99  ? 40   SER D OG  1 
ATOM   6714  N N   . THR D  2 41  ? 42.769  39.178 15.250  1.00 24.98  ? 41   THR D N   1 
ATOM   6715  C CA  . THR D  2 41  ? 42.577  38.175 16.296  1.00 25.42  ? 41   THR D CA  1 
ATOM   6716  C C   . THR D  2 41  ? 43.449  38.448 17.523  1.00 27.22  ? 41   THR D C   1 
ATOM   6717  O O   . THR D  2 41  ? 42.967  38.399 18.655  1.00 26.66  ? 41   THR D O   1 
ATOM   6718  C CB  . THR D  2 41  ? 42.854  36.754 15.772  1.00 26.91  ? 41   THR D CB  1 
ATOM   6719  O OG1 . THR D  2 41  ? 41.943  36.455 14.713  1.00 25.32  ? 41   THR D OG1 1 
ATOM   6720  C CG2 . THR D  2 41  ? 42.673  35.725 16.867  1.00 28.02  ? 41   THR D CG2 1 
ATOM   6721  N N   . GLN D  2 42  ? 44.731  38.729 17.298  1.00 29.65  ? 42   GLN D N   1 
ATOM   6722  C CA  . GLN D  2 42  ? 45.656  38.996 18.397  1.00 31.99  ? 42   GLN D CA  1 
ATOM   6723  C C   . GLN D  2 42  ? 45.276  40.273 19.128  1.00 30.68  ? 42   GLN D C   1 
ATOM   6724  O O   . GLN D  2 42  ? 45.448  40.372 20.339  1.00 31.51  ? 42   GLN D O   1 
ATOM   6725  C CB  . GLN D  2 42  ? 47.091  39.107 17.883  1.00 35.39  ? 42   GLN D CB  1 
ATOM   6726  C CG  . GLN D  2 42  ? 48.137  39.244 18.982  1.00 38.70  ? 42   GLN D CG  1 
ATOM   6727  C CD  . GLN D  2 42  ? 48.090  38.101 19.979  1.00 39.83  ? 42   GLN D CD  1 
ATOM   6728  O OE1 . GLN D  2 42  ? 47.897  38.311 21.177  1.00 39.72  ? 42   GLN D OE1 1 
ATOM   6729  N NE2 . GLN D  2 42  ? 48.260  36.880 19.486  1.00 41.14  ? 42   GLN D NE2 1 
ATOM   6730  N N   . LYS D  2 43  ? 44.763  41.245 18.381  1.00 28.91  ? 43   LYS D N   1 
ATOM   6731  C CA  . LYS D  2 43  ? 44.294  42.506 18.955  1.00 27.86  ? 43   LYS D CA  1 
ATOM   6732  C C   . LYS D  2 43  ? 43.095  42.277 19.871  1.00 25.41  ? 43   LYS D C   1 
ATOM   6733  O O   . LYS D  2 43  ? 42.971  42.930 20.909  1.00 25.44  ? 43   LYS D O   1 
ATOM   6734  C CB  . LYS D  2 43  ? 43.914  43.487 17.841  1.00 26.96  ? 43   LYS D CB  1 
ATOM   6735  C CG  . LYS D  2 43  ? 44.478  44.886 18.018  1.00 28.79  ? 43   LYS D CG  1 
ATOM   6736  C CD  . LYS D  2 43  ? 44.571  45.585 16.671  1.00 29.24  ? 43   LYS D CD  1 
ATOM   6737  C CE  . LYS D  2 43  ? 44.972  47.048 16.801  1.00 31.32  ? 43   LYS D CE  1 
ATOM   6738  N NZ  . LYS D  2 43  ? 44.543  47.804 15.587  1.00 31.01  ? 43   LYS D NZ  1 
ATOM   6739  N N   . ALA D  2 44  ? 42.216  41.355 19.479  1.00 23.57  ? 44   ALA D N   1 
ATOM   6740  C CA  . ALA D  2 44  ? 41.061  40.990 20.290  1.00 21.71  ? 44   ALA D CA  1 
ATOM   6741  C C   . ALA D  2 44  ? 41.493  40.232 21.535  1.00 23.06  ? 44   ALA D C   1 
ATOM   6742  O O   . ALA D  2 44  ? 40.961  40.457 22.617  1.00 22.37  ? 44   ALA D O   1 
ATOM   6743  C CB  . ALA D  2 44  ? 40.082  40.156 19.481  1.00 20.28  ? 44   ALA D CB  1 
ATOM   6744  N N   . ILE D  2 45  ? 42.448  39.323 21.377  1.00 25.23  ? 45   ILE D N   1 
ATOM   6745  C CA  . ILE D  2 45  ? 42.979  38.567 22.510  1.00 27.24  ? 45   ILE D CA  1 
ATOM   6746  C C   . ILE D  2 45  ? 43.586  39.499 23.560  1.00 28.26  ? 45   ILE D C   1 
ATOM   6747  O O   . ILE D  2 45  ? 43.385  39.300 24.758  1.00 28.50  ? 45   ILE D O   1 
ATOM   6748  C CB  . ILE D  2 45  ? 44.007  37.507 22.051  1.00 30.16  ? 45   ILE D CB  1 
ATOM   6749  C CG1 . ILE D  2 45  ? 43.279  36.319 21.416  1.00 29.57  ? 45   ILE D CG1 1 
ATOM   6750  C CG2 . ILE D  2 45  ? 44.862  37.024 23.216  1.00 33.21  ? 45   ILE D CG2 1 
ATOM   6751  C CD1 . ILE D  2 45  ? 44.173  35.397 20.612  1.00 32.23  ? 45   ILE D CD1 1 
ATOM   6752  N N   . ASP D  2 46  ? 44.309  40.520 23.107  1.00 29.07  ? 46   ASP D N   1 
ATOM   6753  C CA  . ASP D  2 46  ? 44.926  41.490 24.011  1.00 30.53  ? 46   ASP D CA  1 
ATOM   6754  C C   . ASP D  2 46  ? 43.885  42.335 24.735  1.00 28.12  ? 46   ASP D C   1 
ATOM   6755  O O   . ASP D  2 46  ? 43.980  42.546 25.937  1.00 28.81  ? 46   ASP D O   1 
ATOM   6756  C CB  . ASP D  2 46  ? 45.884  42.403 23.245  1.00 32.43  ? 46   ASP D CB  1 
ATOM   6757  C CG  . ASP D  2 46  ? 47.044  41.650 22.627  1.00 35.41  ? 46   ASP D CG  1 
ATOM   6758  O OD1 . ASP D  2 46  ? 47.163  40.435 22.874  1.00 36.26  ? 46   ASP D OD1 1 
ATOM   6759  O OD2 . ASP D  2 46  ? 47.832  42.272 21.886  1.00 37.23  ? 46   ASP D OD2 1 
ATOM   6760  N N   . GLY D  2 47  ? 42.894  42.816 23.999  1.00 25.57  ? 47   GLY D N   1 
ATOM   6761  C CA  . GLY D  2 47  ? 41.841  43.632 24.585  1.00 23.61  ? 47   GLY D CA  1 
ATOM   6762  C C   . GLY D  2 47  ? 41.044  42.912 25.658  1.00 22.51  ? 47   GLY D C   1 
ATOM   6763  O O   . GLY D  2 47  ? 40.722  43.494 26.697  1.00 22.25  ? 47   GLY D O   1 
ATOM   6764  N N   . VAL D  2 48  ? 40.725  41.644 25.410  1.00 22.17  ? 48   VAL D N   1 
ATOM   6765  C CA  . VAL D  2 48  ? 39.951  40.840 26.360  1.00 21.57  ? 48   VAL D CA  1 
ATOM   6766  C C   . VAL D  2 48  ? 40.786  40.436 27.578  1.00 23.78  ? 48   VAL D C   1 
ATOM   6767  O O   . VAL D  2 48  ? 40.285  40.427 28.697  1.00 23.40  ? 48   VAL D O   1 
ATOM   6768  C CB  . VAL D  2 48  ? 39.354  39.593 25.673  1.00 21.15  ? 48   VAL D CB  1 
ATOM   6769  C CG1 . VAL D  2 48  ? 38.808  38.603 26.697  1.00 21.60  ? 48   VAL D CG1 1 
ATOM   6770  C CG2 . VAL D  2 48  ? 38.260  40.009 24.698  1.00 18.97  ? 48   VAL D CG2 1 
ATOM   6771  N N   . THR D  2 49  ? 42.054  40.109 27.360  1.00 26.38  ? 49   THR D N   1 
ATOM   6772  C CA  . THR D  2 49  ? 42.943  39.754 28.457  1.00 29.14  ? 49   THR D CA  1 
ATOM   6773  C C   . THR D  2 49  ? 43.089  40.921 29.431  1.00 29.31  ? 49   THR D C   1 
ATOM   6774  O O   . THR D  2 49  ? 42.895  40.756 30.637  1.00 29.65  ? 49   THR D O   1 
ATOM   6775  C CB  . THR D  2 49  ? 44.327  39.332 27.938  1.00 32.39  ? 49   THR D CB  1 
ATOM   6776  O OG1 . THR D  2 49  ? 44.186  38.202 27.071  1.00 32.53  ? 49   THR D OG1 1 
ATOM   6777  C CG2 . THR D  2 49  ? 45.247  38.966 29.082  1.00 35.73  ? 49   THR D CG2 1 
ATOM   6778  N N   . ASN D  2 50  ? 43.416  42.097 28.903  1.00 29.35  ? 50   ASN D N   1 
ATOM   6779  C CA  . ASN D  2 50  ? 43.540  43.309 29.721  1.00 29.84  ? 50   ASN D CA  1 
ATOM   6780  C C   . ASN D  2 50  ? 42.266  43.606 30.499  1.00 27.35  ? 50   ASN D C   1 
ATOM   6781  O O   . ASN D  2 50  ? 42.309  43.957 31.673  1.00 27.98  ? 50   ASN D O   1 
ATOM   6782  C CB  . ASN D  2 50  ? 43.868  44.511 28.841  1.00 30.17  ? 50   ASN D CB  1 
ATOM   6783  C CG  . ASN D  2 50  ? 45.273  44.458 28.281  1.00 33.47  ? 50   ASN D CG  1 
ATOM   6784  O OD1 . ASN D  2 50  ? 46.231  44.265 29.018  1.00 36.48  ? 50   ASN D OD1 1 
ATOM   6785  N ND2 . ASN D  2 50  ? 45.403  44.639 26.977  1.00 33.24  ? 50   ASN D ND2 1 
ATOM   6786  N N   . LYS D  2 51  ? 41.137  43.466 29.820  1.00 24.83  ? 51   LYS D N   1 
ATOM   6787  C CA  . LYS D  2 51  ? 39.821  43.673 30.416  1.00 22.71  ? 51   LYS D CA  1 
ATOM   6788  C C   . LYS D  2 51  ? 39.566  42.773 31.615  1.00 23.14  ? 51   LYS D C   1 
ATOM   6789  O O   . LYS D  2 51  ? 39.055  43.220 32.641  1.00 22.65  ? 51   LYS D O   1 
ATOM   6790  C CB  . LYS D  2 51  ? 38.768  43.410 29.354  1.00 20.59  ? 51   LYS D CB  1 
ATOM   6791  C CG  . LYS D  2 51  ? 37.331  43.416 29.820  1.00 18.68  ? 51   LYS D CG  1 
ATOM   6792  C CD  . LYS D  2 51  ? 36.445  43.185 28.608  1.00 17.30  ? 51   LYS D CD  1 
ATOM   6793  C CE  . LYS D  2 51  ? 35.226  44.076 28.608  1.00 15.95  ? 51   LYS D CE  1 
ATOM   6794  N NZ  . LYS D  2 51  ? 34.925  44.610 27.255  1.00 15.46  ? 51   LYS D NZ  1 
ATOM   6795  N N   . VAL D  2 52  ? 39.918  41.501 31.481  1.00 24.43  ? 52   VAL D N   1 
ATOM   6796  C CA  . VAL D  2 52  ? 39.716  40.543 32.556  1.00 25.37  ? 52   VAL D CA  1 
ATOM   6797  C C   . VAL D  2 52  ? 40.606  40.901 33.747  1.00 27.60  ? 52   VAL D C   1 
ATOM   6798  O O   . VAL D  2 52  ? 40.148  40.878 34.891  1.00 27.47  ? 52   VAL D O   1 
ATOM   6799  C CB  . VAL D  2 52  ? 39.985  39.101 32.074  1.00 26.85  ? 52   VAL D CB  1 
ATOM   6800  C CG1 . VAL D  2 52  ? 40.020  38.124 33.245  1.00 28.70  ? 52   VAL D CG1 1 
ATOM   6801  C CG2 . VAL D  2 52  ? 38.922  38.676 31.070  1.00 24.91  ? 52   VAL D CG2 1 
ATOM   6802  N N   . ASN D  2 53  ? 41.865  41.243 33.473  1.00 29.99  ? 53   ASN D N   1 
ATOM   6803  C CA  . ASN D  2 53  ? 42.812  41.644 34.519  1.00 32.71  ? 53   ASN D CA  1 
ATOM   6804  C C   . ASN D  2 53  ? 42.430  42.979 35.157  1.00 31.71  ? 53   ASN D C   1 
ATOM   6805  O O   . ASN D  2 53  ? 42.566  43.160 36.365  1.00 32.69  ? 53   ASN D O   1 
ATOM   6806  C CB  . ASN D  2 53  ? 44.232  41.736 33.956  1.00 35.84  ? 53   ASN D CB  1 
ATOM   6807  C CG  . ASN D  2 53  ? 44.694  40.440 33.313  1.00 37.46  ? 53   ASN D CG  1 
ATOM   6808  O OD1 . ASN D  2 53  ? 44.233  39.359 33.674  1.00 37.49  ? 53   ASN D OD1 1 
ATOM   6809  N ND2 . ASN D  2 53  ? 45.606  40.544 32.353  1.00 39.21  ? 53   ASN D ND2 1 
ATOM   6810  N N   . SER D  2 54  ? 41.955  43.907 34.331  1.00 30.07  ? 54   SER D N   1 
ATOM   6811  C CA  . SER D  2 54  ? 41.467  45.199 34.810  1.00 29.32  ? 54   SER D CA  1 
ATOM   6812  C C   . SER D  2 54  ? 40.304  45.015 35.766  1.00 27.59  ? 54   SER D C   1 
ATOM   6813  O O   . SER D  2 54  ? 40.238  45.678 36.802  1.00 28.05  ? 54   SER D O   1 
ATOM   6814  C CB  . SER D  2 54  ? 41.026  46.088 33.641  1.00 27.88  ? 54   SER D CB  1 
ATOM   6815  O OG  . SER D  2 54  ? 42.142  46.659 32.985  1.00 30.14  ? 54   SER D OG  1 
ATOM   6816  N N   . ILE D  2 55  ? 39.390  44.117 35.405  1.00 26.04  ? 55   ILE D N   1 
ATOM   6817  C CA  . ILE D  2 55  ? 38.241  43.783 36.246  1.00 24.79  ? 55   ILE D CA  1 
ATOM   6818  C C   . ILE D  2 55  ? 38.690  43.138 37.554  1.00 26.78  ? 55   ILE D C   1 
ATOM   6819  O O   . ILE D  2 55  ? 38.279  43.563 38.633  1.00 26.58  ? 55   ILE D O   1 
ATOM   6820  C CB  . ILE D  2 55  ? 37.258  42.850 35.507  1.00 23.24  ? 55   ILE D CB  1 
ATOM   6821  C CG1 . ILE D  2 55  ? 36.504  43.645 34.438  1.00 21.44  ? 55   ILE D CG1 1 
ATOM   6822  C CG2 . ILE D  2 55  ? 36.265  42.218 36.479  1.00 22.70  ? 55   ILE D CG2 1 
ATOM   6823  C CD1 . ILE D  2 55  ? 35.654  42.805 33.508  1.00 20.34  ? 55   ILE D CD1 1 
ATOM   6824  N N   . ILE D  2 56  ? 39.531  42.113 37.451  1.00 29.09  ? 56   ILE D N   1 
ATOM   6825  C CA  . ILE D  2 56  ? 40.075  41.444 38.629  1.00 31.61  ? 56   ILE D CA  1 
ATOM   6826  C C   . ILE D  2 56  ? 40.701  42.454 39.598  1.00 33.16  ? 56   ILE D C   1 
ATOM   6827  O O   . ILE D  2 56  ? 40.400  42.438 40.795  1.00 33.37  ? 56   ILE D O   1 
ATOM   6828  C CB  . ILE D  2 56  ? 41.119  40.375 38.228  1.00 34.45  ? 56   ILE D CB  1 
ATOM   6829  C CG1 . ILE D  2 56  ? 40.418  39.157 37.613  1.00 33.76  ? 56   ILE D CG1 1 
ATOM   6830  C CG2 . ILE D  2 56  ? 41.960  39.944 39.428  1.00 37.72  ? 56   ILE D CG2 1 
ATOM   6831  C CD1 . ILE D  2 56  ? 41.355  38.188 36.922  1.00 36.36  ? 56   ILE D CD1 1 
ATOM   6832  N N   . ASP D  2 57  ? 41.559  43.333 39.075  1.00 34.61  ? 57   ASP D N   1 
ATOM   6833  C CA  . ASP D  2 57  ? 42.335  44.259 39.916  1.00 36.99  ? 57   ASP D CA  1 
ATOM   6834  C C   . ASP D  2 57  ? 41.497  45.332 40.605  1.00 35.41  ? 57   ASP D C   1 
ATOM   6835  O O   . ASP D  2 57  ? 41.778  45.706 41.739  1.00 36.87  ? 57   ASP D O   1 
ATOM   6836  C CB  . ASP D  2 57  ? 43.459  44.911 39.111  1.00 39.24  ? 57   ASP D CB  1 
ATOM   6837  C CG  . ASP D  2 57  ? 44.659  44.000 38.957  1.00 42.78  ? 57   ASP D CG  1 
ATOM   6838  O OD1 . ASP D  2 57  ? 45.155  43.501 39.998  1.00 45.36  ? 57   ASP D OD1 1 
ATOM   6839  O OD2 . ASP D  2 57  ? 45.115  43.785 37.806  1.00 43.37  ? 57   ASP D OD2 1 
ATOM   6840  N N   . LYS D  2 58  ? 40.474  45.830 39.926  1.00 32.88  ? 58   LYS D N   1 
ATOM   6841  C CA  . LYS D  2 58  ? 39.584  46.815 40.538  1.00 31.65  ? 58   LYS D CA  1 
ATOM   6842  C C   . LYS D  2 58  ? 38.806  46.238 41.717  1.00 31.15  ? 58   LYS D C   1 
ATOM   6843  O O   . LYS D  2 58  ? 38.509  46.951 42.673  1.00 31.33  ? 58   LYS D O   1 
ATOM   6844  C CB  . LYS D  2 58  ? 38.639  47.422 39.492  1.00 29.31  ? 58   LYS D CB  1 
ATOM   6845  C CG  . LYS D  2 58  ? 38.988  48.848 39.076  1.00 30.26  ? 58   LYS D CG  1 
ATOM   6846  C CD  . LYS D  2 58  ? 40.489  49.080 38.925  1.00 33.28  ? 58   LYS D CD  1 
ATOM   6847  C CE  . LYS D  2 58  ? 40.801  50.547 38.711  1.00 34.84  ? 58   LYS D CE  1 
ATOM   6848  N NZ  . LYS D  2 58  ? 42.260  50.813 38.801  1.00 38.51  ? 58   LYS D NZ  1 
ATOM   6849  N N   . MET D  2 59  ? 38.510  44.943 41.665  1.00 31.08  ? 59   MET D N   1 
ATOM   6850  C CA  . MET D  2 59  ? 37.808  44.267 42.754  1.00 30.94  ? 59   MET D CA  1 
ATOM   6851  C C   . MET D  2 59  ? 38.771  43.763 43.839  1.00 33.92  ? 59   MET D C   1 
ATOM   6852  O O   . MET D  2 59  ? 38.356  43.523 44.974  1.00 34.04  ? 59   MET D O   1 
ATOM   6853  C CB  . MET D  2 59  ? 36.990  43.105 42.191  1.00 29.79  ? 59   MET D CB  1 
ATOM   6854  C CG  . MET D  2 59  ? 36.038  43.513 41.073  1.00 27.52  ? 59   MET D CG  1 
ATOM   6855  S SD  . MET D  2 59  ? 34.760  44.672 41.597  1.00 25.81  ? 59   MET D SD  1 
ATOM   6856  C CE  . MET D  2 59  ? 33.849  43.755 42.835  1.00 25.76  ? 59   MET D CE  1 
ATOM   6857  N N   . ASN D  2 60  ? 40.050  43.618 43.483  1.00 36.66  ? 60   ASN D N   1 
ATOM   6858  C CA  . ASN D  2 60  ? 41.091  43.099 44.390  1.00 40.26  ? 60   ASN D CA  1 
ATOM   6859  C C   . ASN D  2 60  ? 41.138  43.759 45.785  1.00 41.32  ? 60   ASN D C   1 
ATOM   6860  O O   . ASN D  2 60  ? 41.337  43.062 46.784  1.00 43.03  ? 60   ASN D O   1 
ATOM   6861  C CB  . ASN D  2 60  ? 42.471  43.123 43.689  1.00 43.15  ? 60   ASN D CB  1 
ATOM   6862  C CG  . ASN D  2 60  ? 43.626  43.383 44.644  1.00 47.06  ? 60   ASN D CG  1 
ATOM   6863  O OD1 . ASN D  2 60  ? 43.809  44.504 45.112  1.00 47.56  ? 60   ASN D OD1 1 
ATOM   6864  N ND2 . ASN D  2 60  ? 44.432  42.356 44.909  1.00 50.36  ? 60   ASN D ND2 1 
ATOM   6865  N N   . THR D  2 61  ? 40.973  45.082 45.863  1.00 40.67  ? 61   THR D N   1 
ATOM   6866  C CA  . THR D  2 61  ? 40.805  45.747 47.171  1.00 41.31  ? 61   THR D CA  1 
ATOM   6867  C C   . THR D  2 61  ? 39.319  46.035 47.369  1.00 38.03  ? 61   THR D C   1 
ATOM   6868  O O   . THR D  2 61  ? 38.715  46.812 46.620  1.00 36.12  ? 61   THR D O   1 
ATOM   6869  C CB  . THR D  2 61  ? 41.618  47.062 47.329  1.00 43.41  ? 61   THR D CB  1 
ATOM   6870  O OG1 . THR D  2 61  ? 40.912  48.154 46.727  1.00 41.55  ? 61   THR D OG1 1 
ATOM   6871  C CG2 . THR D  2 61  ? 43.009  46.951 46.710  1.00 46.64  ? 61   THR D CG2 1 
ATOM   6872  N N   . GLN D  2 62  ? 38.732  45.378 48.364  1.00 37.68  ? 62   GLN D N   1 
ATOM   6873  C CA  . GLN D  2 62  ? 37.308  45.521 48.650  1.00 35.00  ? 62   GLN D CA  1 
ATOM   6874  C C   . GLN D  2 62  ? 37.039  45.101 50.097  1.00 35.56  ? 62   GLN D C   1 
ATOM   6875  O O   . GLN D  2 62  ? 37.911  44.514 50.751  1.00 38.19  ? 62   GLN D O   1 
ATOM   6876  C CB  . GLN D  2 62  ? 36.478  44.699 47.651  1.00 33.23  ? 62   GLN D CB  1 
ATOM   6877  C CG  . GLN D  2 62  ? 35.803  43.445 48.201  1.00 33.46  ? 62   GLN D CG  1 
ATOM   6878  C CD  . GLN D  2 62  ? 34.960  42.748 47.150  1.00 32.24  ? 62   GLN D CD  1 
ATOM   6879  O OE1 . GLN D  2 62  ? 35.147  42.962 45.946  1.00 31.66  ? 62   GLN D OE1 1 
ATOM   6880  N NE2 . GLN D  2 62  ? 34.015  41.916 47.597  1.00 32.18  ? 62   GLN D NE2 1 
ATOM   6881  N N   . PHE D  2 63  ? 35.839  45.403 50.588  1.00 33.38  ? 63   PHE D N   1 
ATOM   6882  C CA  . PHE D  2 63  ? 35.505  45.199 51.999  1.00 33.78  ? 63   PHE D CA  1 
ATOM   6883  C C   . PHE D  2 63  ? 35.755  43.758 52.464  1.00 35.33  ? 63   PHE D C   1 
ATOM   6884  O O   . PHE D  2 63  ? 35.495  42.803 51.728  1.00 35.26  ? 63   PHE D O   1 
ATOM   6885  C CB  . PHE D  2 63  ? 34.049  45.596 52.284  1.00 31.55  ? 63   PHE D CB  1 
ATOM   6886  C CG  . PHE D  2 63  ? 33.695  45.552 53.742  1.00 32.14  ? 63   PHE D CG  1 
ATOM   6887  C CD1 . PHE D  2 63  ? 34.204  46.504 54.620  1.00 33.09  ? 63   PHE D CD1 1 
ATOM   6888  C CD2 . PHE D  2 63  ? 32.883  44.539 54.247  1.00 32.06  ? 63   PHE D CD2 1 
ATOM   6889  C CE1 . PHE D  2 63  ? 33.901  46.455 55.970  1.00 33.69  ? 63   PHE D CE1 1 
ATOM   6890  C CE2 . PHE D  2 63  ? 32.574  44.486 55.596  1.00 32.79  ? 63   PHE D CE2 1 
ATOM   6891  C CZ  . PHE D  2 63  ? 33.083  45.444 56.458  1.00 33.46  ? 63   PHE D CZ  1 
ATOM   6892  N N   . GLU D  2 64  ? 36.283  43.623 53.679  1.00 37.08  ? 64   GLU D N   1 
ATOM   6893  C CA  . GLU D  2 64  ? 36.478  42.328 54.318  1.00 39.03  ? 64   GLU D CA  1 
ATOM   6894  C C   . GLU D  2 64  ? 35.758  42.320 55.659  1.00 38.80  ? 64   GLU D C   1 
ATOM   6895  O O   . GLU D  2 64  ? 35.941  43.233 56.470  1.00 39.01  ? 64   GLU D O   1 
ATOM   6896  C CB  . GLU D  2 64  ? 37.962  42.067 54.561  1.00 42.47  ? 64   GLU D CB  1 
ATOM   6897  C CG  . GLU D  2 64  ? 38.792  41.918 53.300  1.00 43.17  ? 64   GLU D CG  1 
ATOM   6898  C CD  . GLU D  2 64  ? 40.267  41.713 53.603  1.00 47.18  ? 64   GLU D CD  1 
ATOM   6899  O OE1 . GLU D  2 64  ? 40.608  41.357 54.756  1.00 49.62  ? 64   GLU D OE1 1 
ATOM   6900  O OE2 . GLU D  2 64  ? 41.087  41.910 52.681  1.00 48.11  ? 64   GLU D OE2 1 
ATOM   6901  N N   . ALA D  2 65  ? 34.952  41.289 55.897  1.00 38.58  ? 65   ALA D N   1 
ATOM   6902  C CA  . ALA D  2 65  ? 34.226  41.165 57.158  1.00 38.57  ? 65   ALA D CA  1 
ATOM   6903  C C   . ALA D  2 65  ? 35.172  40.728 58.276  1.00 41.60  ? 65   ALA D C   1 
ATOM   6904  O O   . ALA D  2 65  ? 36.149  40.013 58.027  1.00 44.09  ? 65   ALA D O   1 
ATOM   6905  C CB  . ALA D  2 65  ? 33.077  40.179 57.015  1.00 38.24  ? 65   ALA D CB  1 
ATOM   6906  N N   . VAL D  2 66  ? 34.887  41.180 59.498  1.00 41.47  ? 66   VAL D N   1 
ATOM   6907  C CA  . VAL D  2 66  ? 35.627  40.747 60.686  1.00 44.51  ? 66   VAL D CA  1 
ATOM   6908  C C   . VAL D  2 66  ? 34.635  40.385 61.794  1.00 44.40  ? 66   VAL D C   1 
ATOM   6909  O O   . VAL D  2 66  ? 33.568  41.001 61.920  1.00 41.92  ? 66   VAL D O   1 
ATOM   6910  C CB  . VAL D  2 66  ? 36.612  41.831 61.186  1.00 45.42  ? 66   VAL D CB  1 
ATOM   6911  C CG1 . VAL D  2 66  ? 37.479  41.301 62.324  1.00 49.31  ? 66   VAL D CG1 1 
ATOM   6912  C CG2 . VAL D  2 66  ? 37.488  42.337 60.043  1.00 45.36  ? 66   VAL D CG2 1 
ATOM   6913  N N   . GLY D  2 67  ? 34.995  39.380 62.586  1.00 47.38  ? 67   GLY D N   1 
ATOM   6914  C CA  . GLY D  2 67  ? 34.147  38.897 63.663  1.00 47.91  ? 67   GLY D CA  1 
ATOM   6915  C C   . GLY D  2 67  ? 34.260  39.776 64.893  1.00 47.74  ? 67   GLY D C   1 
ATOM   6916  O O   . GLY D  2 67  ? 35.363  40.021 65.387  1.00 49.97  ? 67   GLY D O   1 
ATOM   6917  N N   . ARG D  2 68  ? 33.115  40.244 65.384  1.00 45.34  ? 68   ARG D N   1 
ATOM   6918  C CA  . ARG D  2 68  ? 33.057  41.102 66.562  1.00 44.95  ? 68   ARG D CA  1 
ATOM   6919  C C   . ARG D  2 68  ? 31.885  40.683 67.436  1.00 44.81  ? 68   ARG D C   1 
ATOM   6920  O O   . ARG D  2 68  ? 30.775  40.477 66.941  1.00 43.18  ? 68   ARG D O   1 
ATOM   6921  C CB  . ARG D  2 68  ? 32.937  42.568 66.140  1.00 42.05  ? 68   ARG D CB  1 
ATOM   6922  C CG  . ARG D  2 68  ? 34.272  43.168 65.726  1.00 42.97  ? 68   ARG D CG  1 
ATOM   6923  C CD  . ARG D  2 68  ? 34.192  44.653 65.415  1.00 40.81  ? 68   ARG D CD  1 
ATOM   6924  N NE  . ARG D  2 68  ? 33.357  44.967 64.265  1.00 37.88  ? 68   ARG D NE  1 
ATOM   6925  C CZ  . ARG D  2 68  ? 33.730  44.893 62.989  1.00 37.20  ? 68   ARG D CZ  1 
ATOM   6926  N NH1 . ARG D  2 68  ? 34.946  44.506 62.628  1.00 39.20  ? 68   ARG D NH1 1 
ATOM   6927  N NH2 . ARG D  2 68  ? 32.861  45.206 62.046  1.00 34.72  ? 68   ARG D NH2 1 
ATOM   6928  N N   . GLU D  2 69  ? 32.145  40.560 68.735  1.00 46.75  ? 69   GLU D N   1 
ATOM   6929  C CA  . GLU D  2 69  ? 31.186  40.006 69.687  1.00 47.50  ? 69   GLU D CA  1 
ATOM   6930  C C   . GLU D  2 69  ? 30.614  41.100 70.575  1.00 45.60  ? 69   GLU D C   1 
ATOM   6931  O O   . GLU D  2 69  ? 31.326  42.019 70.969  1.00 45.42  ? 69   GLU D O   1 
ATOM   6932  C CB  . GLU D  2 69  ? 31.877  38.970 70.572  1.00 51.80  ? 69   GLU D CB  1 
ATOM   6933  C CG  . GLU D  2 69  ? 32.479  37.788 69.820  1.00 54.40  ? 69   GLU D CG  1 
ATOM   6934  C CD  . GLU D  2 69  ? 31.525  36.612 69.726  1.00 55.83  ? 69   GLU D CD  1 
ATOM   6935  O OE1 . GLU D  2 69  ? 30.386  36.805 69.246  1.00 53.46  ? 69   GLU D OE1 1 
ATOM   6936  O OE2 . GLU D  2 69  ? 31.918  35.497 70.137  1.00 59.86  ? 69   GLU D OE2 1 
ATOM   6937  N N   . PHE D  2 70  ? 29.329  40.982 70.898  1.00 44.48  ? 70   PHE D N   1 
ATOM   6938  C CA  . PHE D  2 70  ? 28.646  41.945 71.759  1.00 42.98  ? 70   PHE D CA  1 
ATOM   6939  C C   . PHE D  2 70  ? 27.758  41.221 72.768  1.00 44.56  ? 70   PHE D C   1 
ATOM   6940  O O   . PHE D  2 70  ? 27.144  40.205 72.447  1.00 45.64  ? 70   PHE D O   1 
ATOM   6941  C CB  . PHE D  2 70  ? 27.797  42.893 70.913  1.00 39.75  ? 70   PHE D CB  1 
ATOM   6942  C CG  . PHE D  2 70  ? 28.540  43.513 69.763  1.00 38.17  ? 70   PHE D CG  1 
ATOM   6943  C CD1 . PHE D  2 70  ? 28.579  42.886 68.522  1.00 37.68  ? 70   PHE D CD1 1 
ATOM   6944  C CD2 . PHE D  2 70  ? 29.195  44.726 69.916  1.00 37.42  ? 70   PHE D CD2 1 
ATOM   6945  C CE1 . PHE D  2 70  ? 29.256  43.458 67.460  1.00 36.34  ? 70   PHE D CE1 1 
ATOM   6946  C CE2 . PHE D  2 70  ? 29.874  45.304 68.854  1.00 36.36  ? 70   PHE D CE2 1 
ATOM   6947  C CZ  . PHE D  2 70  ? 29.905  44.669 67.627  1.00 35.74  ? 70   PHE D CZ  1 
ATOM   6948  N N   . ASN D  2 71  ? 27.682  41.747 73.986  1.00 44.89  ? 71   ASN D N   1 
ATOM   6949  C CA  . ASN D  2 71  ? 26.867  41.116 75.025  1.00 46.62  ? 71   ASN D CA  1 
ATOM   6950  C C   . ASN D  2 71  ? 25.377  41.465 74.870  1.00 44.85  ? 71   ASN D C   1 
ATOM   6951  O O   . ASN D  2 71  ? 24.975  42.076 73.875  1.00 42.39  ? 71   ASN D O   1 
ATOM   6952  C CB  . ASN D  2 71  ? 27.417  41.427 76.432  1.00 48.23  ? 71   ASN D CB  1 
ATOM   6953  C CG  . ASN D  2 71  ? 27.202  42.870 76.858  1.00 46.03  ? 71   ASN D CG  1 
ATOM   6954  O OD1 . ASN D  2 71  ? 26.083  43.382 76.830  1.00 44.36  ? 71   ASN D OD1 1 
ATOM   6955  N ND2 . ASN D  2 71  ? 28.277  43.528 77.280  1.00 46.51  ? 71   ASN D ND2 1 
ATOM   6956  N N   . ASN D  2 72  ? 24.571  41.070 75.855  1.00 46.39  ? 72   ASN D N   1 
ATOM   6957  C CA  . ASN D  2 72  ? 23.113  41.132 75.754  1.00 45.80  ? 72   ASN D CA  1 
ATOM   6958  C C   . ASN D  2 72  ? 22.522  42.543 75.870  1.00 43.24  ? 72   ASN D C   1 
ATOM   6959  O O   . ASN D  2 72  ? 21.388  42.779 75.449  1.00 42.53  ? 72   ASN D O   1 
ATOM   6960  C CB  . ASN D  2 72  ? 22.486  40.213 76.811  1.00 48.95  ? 72   ASN D CB  1 
ATOM   6961  C CG  . ASN D  2 72  ? 21.054  39.834 76.484  1.00 49.64  ? 72   ASN D CG  1 
ATOM   6962  O OD1 . ASN D  2 72  ? 20.733  39.512 75.338  1.00 49.18  ? 72   ASN D OD1 1 
ATOM   6963  N ND2 . ASN D  2 72  ? 20.187  39.859 77.491  1.00 51.07  ? 72   ASN D ND2 1 
ATOM   6964  N N   . LEU D  2 73  ? 23.280  43.469 76.450  1.00 42.30  ? 73   LEU D N   1 
ATOM   6965  C CA  . LEU D  2 73  ? 22.872  44.872 76.528  1.00 40.25  ? 73   LEU D CA  1 
ATOM   6966  C C   . LEU D  2 73  ? 23.767  45.749 75.645  1.00 38.29  ? 73   LEU D C   1 
ATOM   6967  O O   . LEU D  2 73  ? 24.070  46.895 75.980  1.00 37.48  ? 73   LEU D O   1 
ATOM   6968  C CB  . LEU D  2 73  ? 22.887  45.344 77.981  1.00 41.22  ? 73   LEU D CB  1 
ATOM   6969  C CG  . LEU D  2 73  ? 21.810  44.711 78.873  1.00 43.05  ? 73   LEU D CG  1 
ATOM   6970  C CD1 . LEU D  2 73  ? 22.149  44.894 80.346  1.00 44.44  ? 73   LEU D CD1 1 
ATOM   6971  C CD2 . LEU D  2 73  ? 20.432  45.281 78.559  1.00 42.18  ? 73   LEU D CD2 1 
ATOM   6972  N N   . GLU D  2 74  ? 24.179  45.182 74.512  1.00 37.79  ? 74   GLU D N   1 
ATOM   6973  C CA  . GLU D  2 74  ? 24.884  45.907 73.460  1.00 36.05  ? 74   GLU D CA  1 
ATOM   6974  C C   . GLU D  2 74  ? 24.251  45.569 72.112  1.00 34.89  ? 74   GLU D C   1 
ATOM   6975  O O   . GLU D  2 74  ? 24.945  45.403 71.112  1.00 34.22  ? 74   GLU D O   1 
ATOM   6976  C CB  . GLU D  2 74  ? 26.360  45.519 73.458  1.00 37.09  ? 74   GLU D CB  1 
ATOM   6977  C CG  . GLU D  2 74  ? 27.121  46.024 74.660  1.00 38.36  ? 74   GLU D CG  1 
ATOM   6978  C CD  . GLU D  2 74  ? 28.605  45.795 74.526  1.00 39.74  ? 74   GLU D CD  1 
ATOM   6979  O OE1 . GLU D  2 74  ? 29.007  44.634 74.320  1.00 41.24  ? 74   GLU D OE1 1 
ATOM   6980  O OE2 . GLU D  2 74  ? 29.366  46.776 74.625  1.00 39.72  ? 74   GLU D OE2 1 
ATOM   6981  N N   . ARG D  2 75  ? 22.924  45.466 72.101  1.00 34.94  ? 75   ARG D N   1 
ATOM   6982  C CA  . ARG D  2 75  ? 22.184  45.005 70.927  1.00 34.50  ? 75   ARG D CA  1 
ATOM   6983  C C   . ARG D  2 75  ? 22.156  46.037 69.808  1.00 32.40  ? 75   ARG D C   1 
ATOM   6984  O O   . ARG D  2 75  ? 22.149  45.679 68.629  1.00 31.73  ? 75   ARG D O   1 
ATOM   6985  C CB  . ARG D  2 75  ? 20.751  44.634 71.313  1.00 35.84  ? 75   ARG D CB  1 
ATOM   6986  C CG  . ARG D  2 75  ? 20.646  43.354 72.120  1.00 38.45  ? 75   ARG D CG  1 
ATOM   6987  C CD  . ARG D  2 75  ? 20.516  42.140 71.219  1.00 39.65  ? 75   ARG D CD  1 
ATOM   6988  N NE  . ARG D  2 75  ? 20.778  40.897 71.949  1.00 42.57  ? 75   ARG D NE  1 
ATOM   6989  C CZ  . ARG D  2 75  ? 21.969  40.301 72.061  1.00 43.47  ? 75   ARG D CZ  1 
ATOM   6990  N NH1 . ARG D  2 75  ? 23.055  40.822 71.488  1.00 41.67  ? 75   ARG D NH1 1 
ATOM   6991  N NH2 . ARG D  2 75  ? 22.076  39.168 72.761  1.00 46.63  ? 75   ARG D NH2 1 
ATOM   6992  N N   . ARG D  2 76  ? 22.129  47.312 70.179  1.00 31.63  ? 76   ARG D N   1 
ATOM   6993  C CA  . ARG D  2 76  ? 22.129  48.391 69.195  1.00 30.16  ? 76   ARG D CA  1 
ATOM   6994  C C   . ARG D  2 76  ? 23.396  48.385 68.351  1.00 29.34  ? 76   ARG D C   1 
ATOM   6995  O O   . ARG D  2 76  ? 23.318  48.411 67.126  1.00 28.37  ? 76   ARG D O   1 
ATOM   6996  C CB  . ARG D  2 76  ? 21.989  49.745 69.880  1.00 30.16  ? 76   ARG D CB  1 
ATOM   6997  C CG  . ARG D  2 76  ? 20.606  50.033 70.434  1.00 30.94  ? 76   ARG D CG  1 
ATOM   6998  C CD  . ARG D  2 76  ? 20.653  51.292 71.276  1.00 31.29  ? 76   ARG D CD  1 
ATOM   6999  N NE  . ARG D  2 76  ? 21.533  51.112 72.430  1.00 31.86  ? 76   ARG D NE  1 
ATOM   7000  C CZ  . ARG D  2 76  ? 22.085  52.091 73.142  1.00 32.25  ? 76   ARG D CZ  1 
ATOM   7001  N NH1 . ARG D  2 76  ? 21.869  53.367 72.840  1.00 32.25  ? 76   ARG D NH1 1 
ATOM   7002  N NH2 . ARG D  2 76  ? 22.868  51.788 74.170  1.00 33.04  ? 76   ARG D NH2 1 
ATOM   7003  N N   . ILE D  2 77  ? 24.557  48.356 69.006  1.00 29.99  ? 77   ILE D N   1 
ATOM   7004  C CA  . ILE D  2 77  ? 25.835  48.336 68.285  1.00 29.79  ? 77   ILE D CA  1 
ATOM   7005  C C   . ILE D  2 77  ? 26.092  47.009 67.571  1.00 30.05  ? 77   ILE D C   1 
ATOM   7006  O O   . ILE D  2 77  ? 26.752  46.981 66.534  1.00 29.45  ? 77   ILE D O   1 
ATOM   7007  C CB  . ILE D  2 77  ? 27.043  48.710 69.175  1.00 31.03  ? 77   ILE D CB  1 
ATOM   7008  C CG1 . ILE D  2 77  ? 27.232  47.722 70.326  1.00 32.75  ? 77   ILE D CG1 1 
ATOM   7009  C CG2 . ILE D  2 77  ? 26.877  50.127 69.705  1.00 30.99  ? 77   ILE D CG2 1 
ATOM   7010  C CD1 . ILE D  2 77  ? 28.566  47.871 71.030  1.00 34.44  ? 77   ILE D CD1 1 
ATOM   7011  N N   . GLU D  2 78  ? 25.567  45.919 68.118  1.00 31.25  ? 78   GLU D N   1 
ATOM   7012  C CA  . GLU D  2 78  ? 25.607  44.636 67.429  1.00 31.97  ? 78   GLU D CA  1 
ATOM   7013  C C   . GLU D  2 78  ? 24.844  44.732 66.117  1.00 30.55  ? 78   GLU D C   1 
ATOM   7014  O O   . GLU D  2 78  ? 25.284  44.220 65.096  1.00 30.27  ? 78   GLU D O   1 
ATOM   7015  C CB  . GLU D  2 78  ? 25.002  43.533 68.297  1.00 34.00  ? 78   GLU D CB  1 
ATOM   7016  C CG  . GLU D  2 78  ? 24.981  42.158 67.643  1.00 35.37  ? 78   GLU D CG  1 
ATOM   7017  C CD  . GLU D  2 78  ? 24.666  41.046 68.630  1.00 38.21  ? 78   GLU D CD  1 
ATOM   7018  O OE1 . GLU D  2 78  ? 23.616  41.127 69.310  1.00 38.72  ? 78   GLU D OE1 1 
ATOM   7019  O OE2 . GLU D  2 78  ? 25.466  40.086 68.722  1.00 40.30  ? 78   GLU D OE2 1 
ATOM   7020  N N   . ASN D  2 79  ? 23.695  45.390 66.161  1.00 29.96  ? 79   ASN D N   1 
ATOM   7021  C CA  . ASN D  2 79  ? 22.853  45.543 64.991  1.00 29.09  ? 79   ASN D CA  1 
ATOM   7022  C C   . ASN D  2 79  ? 23.446  46.533 63.984  1.00 27.46  ? 79   ASN D C   1 
ATOM   7023  O O   . ASN D  2 79  ? 23.361  46.323 62.775  1.00 26.75  ? 79   ASN D O   1 
ATOM   7024  C CB  . ASN D  2 79  ? 21.463  45.997 65.419  1.00 29.58  ? 79   ASN D CB  1 
ATOM   7025  C CG  . ASN D  2 79  ? 20.515  46.119 64.253  1.00 29.27  ? 79   ASN D CG  1 
ATOM   7026  O OD1 . ASN D  2 79  ? 20.007  45.124 63.746  1.00 30.24  ? 79   ASN D OD1 1 
ATOM   7027  N ND2 . ASN D  2 79  ? 20.283  47.343 63.813  1.00 28.34  ? 79   ASN D ND2 1 
ATOM   7028  N N   . LEU D  2 80  ? 24.033  47.613 64.494  1.00 27.17  ? 80   LEU D N   1 
ATOM   7029  C CA  . LEU D  2 80  ? 24.767  48.576 63.673  1.00 26.23  ? 80   LEU D CA  1 
ATOM   7030  C C   . LEU D  2 80  ? 25.884  47.852 62.950  1.00 26.19  ? 80   LEU D C   1 
ATOM   7031  O O   . LEU D  2 80  ? 26.053  47.997 61.743  1.00 25.33  ? 80   LEU D O   1 
ATOM   7032  C CB  . LEU D  2 80  ? 25.349  49.687 64.552  1.00 26.70  ? 80   LEU D CB  1 
ATOM   7033  C CG  . LEU D  2 80  ? 25.972  50.954 63.947  1.00 26.43  ? 80   LEU D CG  1 
ATOM   7034  C CD1 . LEU D  2 80  ? 26.257  51.959 65.056  1.00 27.48  ? 80   LEU D CD1 1 
ATOM   7035  C CD2 . LEU D  2 80  ? 27.251  50.673 63.175  1.00 26.41  ? 80   LEU D CD2 1 
ATOM   7036  N N   . ASN D  2 81  ? 26.636  47.057 63.700  1.00 27.45  ? 81   ASN D N   1 
ATOM   7037  C CA  . ASN D  2 81  ? 27.715  46.260 63.139  1.00 28.08  ? 81   ASN D CA  1 
ATOM   7038  C C   . ASN D  2 81  ? 27.251  45.327 62.023  1.00 27.77  ? 81   ASN D C   1 
ATOM   7039  O O   . ASN D  2 81  ? 27.902  45.238 60.991  1.00 27.32  ? 81   ASN D O   1 
ATOM   7040  C CB  . ASN D  2 81  ? 28.381  45.441 64.237  1.00 30.04  ? 81   ASN D CB  1 
ATOM   7041  C CG  . ASN D  2 81  ? 29.536  44.621 63.721  1.00 31.18  ? 81   ASN D CG  1 
ATOM   7042  O OD1 . ASN D  2 81  ? 30.451  45.156 63.113  1.00 30.99  ? 81   ASN D OD1 1 
ATOM   7043  N ND2 . ASN D  2 81  ? 29.501  43.319 63.959  1.00 32.79  ? 81   ASN D ND2 1 
ATOM   7044  N N   . LYS D  2 82  ? 26.130  44.636 62.233  1.00 28.37  ? 82   LYS D N   1 
ATOM   7045  C CA  . LYS D  2 82  ? 25.612  43.696 61.240  1.00 28.61  ? 82   LYS D CA  1 
ATOM   7046  C C   . LYS D  2 82  ? 25.249  44.421 59.959  1.00 27.02  ? 82   LYS D C   1 
ATOM   7047  O O   . LYS D  2 82  ? 25.666  44.017 58.876  1.00 26.64  ? 82   LYS D O   1 
ATOM   7048  C CB  . LYS D  2 82  ? 24.386  42.934 61.758  1.00 29.95  ? 82   LYS D CB  1 
ATOM   7049  C CG  . LYS D  2 82  ? 23.748  42.033 60.696  1.00 30.46  ? 82   LYS D CG  1 
ATOM   7050  C CD  . LYS D  2 82  ? 22.803  40.989 61.280  1.00 32.82  ? 82   LYS D CD  1 
ATOM   7051  C CE  . LYS D  2 82  ? 21.349  41.459 61.306  1.00 32.89  ? 82   LYS D CE  1 
ATOM   7052  N NZ  . LYS D  2 82  ? 20.474  40.544 62.101  1.00 35.61  ? 82   LYS D NZ  1 
ATOM   7053  N N   . LYS D  2 83  ? 24.470  45.489 60.095  1.00 26.46  ? 83   LYS D N   1 
ATOM   7054  C CA  . LYS D  2 83  ? 24.056  46.305 58.951  1.00 25.40  ? 83   LYS D CA  1 
ATOM   7055  C C   . LYS D  2 83  ? 25.233  46.899 58.195  1.00 24.55  ? 83   LYS D C   1 
ATOM   7056  O O   . LYS D  2 83  ? 25.204  46.984 56.968  1.00 23.81  ? 83   LYS D O   1 
ATOM   7057  C CB  . LYS D  2 83  ? 23.088  47.411 59.396  1.00 25.49  ? 83   LYS D CB  1 
ATOM   7058  C CG  . LYS D  2 83  ? 21.611  47.020 59.343  1.00 26.46  ? 83   LYS D CG  1 
ATOM   7059  C CD  . LYS D  2 83  ? 21.355  45.539 59.627  1.00 27.79  ? 83   LYS D CD  1 
ATOM   7060  C CE  . LYS D  2 83  ? 19.889  45.162 59.453  1.00 29.23  ? 83   LYS D CE  1 
ATOM   7061  N NZ  . LYS D  2 83  ? 19.135  45.268 60.738  1.00 30.62  ? 83   LYS D NZ  1 
ATOM   7062  N N   . MET D  2 84  ? 26.270  47.298 58.921  1.00 25.03  ? 84   MET D N   1 
ATOM   7063  C CA  . MET D  2 84  ? 27.470  47.820 58.286  1.00 24.84  ? 84   MET D CA  1 
ATOM   7064  C C   . MET D  2 84  ? 28.121  46.744 57.426  1.00 24.89  ? 84   MET D C   1 
ATOM   7065  O O   . MET D  2 84  ? 28.396  46.980 56.248  1.00 24.13  ? 84   MET D O   1 
ATOM   7066  C CB  . MET D  2 84  ? 28.464  48.323 59.327  1.00 26.01  ? 84   MET D CB  1 
ATOM   7067  C CG  . MET D  2 84  ? 29.528  49.240 58.752  1.00 26.33  ? 84   MET D CG  1 
ATOM   7068  S SD  . MET D  2 84  ? 31.157  48.888 59.421  1.00 28.55  ? 84   MET D SD  1 
ATOM   7069  C CE  . MET D  2 84  ? 31.519  47.360 58.568  1.00 28.63  ? 84   MET D CE  1 
ATOM   7070  N N   . GLU D  2 85  ? 28.341  45.563 58.006  1.00 26.02  ? 85   GLU D N   1 
ATOM   7071  C CA  . GLU D  2 85  ? 29.001  44.469 57.290  1.00 26.65  ? 85   GLU D CA  1 
ATOM   7072  C C   . GLU D  2 85  ? 28.151  44.000 56.108  1.00 25.67  ? 85   GLU D C   1 
ATOM   7073  O O   . GLU D  2 85  ? 28.654  43.866 54.998  1.00 25.16  ? 85   GLU D O   1 
ATOM   7074  C CB  . GLU D  2 85  ? 29.331  43.295 58.223  1.00 28.78  ? 85   GLU D CB  1 
ATOM   7075  C CG  . GLU D  2 85  ? 30.191  43.682 59.427  1.00 30.17  ? 85   GLU D CG  1 
ATOM   7076  C CD  . GLU D  2 85  ? 31.416  42.796 59.630  1.00 32.59  ? 85   GLU D CD  1 
ATOM   7077  O OE1 . GLU D  2 85  ? 31.291  41.722 60.261  1.00 34.44  ? 85   GLU D OE1 1 
ATOM   7078  O OE2 . GLU D  2 85  ? 32.516  43.193 59.180  1.00 33.09  ? 85   GLU D OE2 1 
ATOM   7079  N N   . ASP D  2 86  ? 26.863  43.772 56.350  1.00 25.59  ? 86   ASP D N   1 
ATOM   7080  C CA  . ASP D  2 86  ? 25.928  43.384 55.289  1.00 25.08  ? 86   ASP D CA  1 
ATOM   7081  C C   . ASP D  2 86  ? 25.795  44.428 54.197  1.00 23.39  ? 86   ASP D C   1 
ATOM   7082  O O   . ASP D  2 86  ? 25.697  44.086 53.017  1.00 22.98  ? 86   ASP D O   1 
ATOM   7083  C CB  . ASP D  2 86  ? 24.535  43.104 55.863  1.00 25.94  ? 86   ASP D CB  1 
ATOM   7084  C CG  . ASP D  2 86  ? 24.323  41.649 56.181  1.00 28.00  ? 86   ASP D CG  1 
ATOM   7085  O OD1 . ASP D  2 86  ? 24.680  40.806 55.326  1.00 28.59  ? 86   ASP D OD1 1 
ATOM   7086  O OD2 . ASP D  2 86  ? 23.790  41.343 57.270  1.00 29.38  ? 86   ASP D OD2 1 
ATOM   7087  N N   . GLY D  2 87  ? 25.769  45.694 54.597  1.00 22.70  ? 87   GLY D N   1 
ATOM   7088  C CA  . GLY D  2 87  ? 25.623  46.797 53.659  1.00 21.64  ? 87   GLY D CA  1 
ATOM   7089  C C   . GLY D  2 87  ? 26.737  46.860 52.633  1.00 21.06  ? 87   GLY D C   1 
ATOM   7090  O O   . GLY D  2 87  ? 26.484  47.093 51.448  1.00 20.39  ? 87   GLY D O   1 
ATOM   7091  N N   . PHE D  2 88  ? 27.970  46.650 53.092  1.00 21.58  ? 88   PHE D N   1 
ATOM   7092  C CA  . PHE D  2 88  ? 29.133  46.629 52.206  1.00 21.51  ? 88   PHE D CA  1 
ATOM   7093  C C   . PHE D  2 88  ? 29.142  45.407 51.279  1.00 21.49  ? 88   PHE D C   1 
ATOM   7094  O O   . PHE D  2 88  ? 29.574  45.508 50.128  1.00 20.97  ? 88   PHE D O   1 
ATOM   7095  C CB  . PHE D  2 88  ? 30.435  46.687 53.011  1.00 22.76  ? 88   PHE D CB  1 
ATOM   7096  C CG  . PHE D  2 88  ? 30.786  48.063 53.509  1.00 23.05  ? 88   PHE D CG  1 
ATOM   7097  C CD1 . PHE D  2 88  ? 30.980  49.110 52.621  1.00 22.68  ? 88   PHE D CD1 1 
ATOM   7098  C CD2 . PHE D  2 88  ? 30.941  48.310 54.863  1.00 24.02  ? 88   PHE D CD2 1 
ATOM   7099  C CE1 . PHE D  2 88  ? 31.312  50.376 53.071  1.00 23.52  ? 88   PHE D CE1 1 
ATOM   7100  C CE2 . PHE D  2 88  ? 31.277  49.573 55.321  1.00 24.67  ? 88   PHE D CE2 1 
ATOM   7101  C CZ  . PHE D  2 88  ? 31.461  50.607 54.422  1.00 24.54  ? 88   PHE D CZ  1 
ATOM   7102  N N   . LEU D  2 89  ? 28.663  44.264 51.766  1.00 22.30  ? 89   LEU D N   1 
ATOM   7103  C CA  . LEU D  2 89  ? 28.537  43.078 50.915  1.00 22.75  ? 89   LEU D CA  1 
ATOM   7104  C C   . LEU D  2 89  ? 27.563  43.296 49.763  1.00 21.61  ? 89   LEU D C   1 
ATOM   7105  O O   . LEU D  2 89  ? 27.797  42.811 48.664  1.00 21.41  ? 89   LEU D O   1 
ATOM   7106  C CB  . LEU D  2 89  ? 28.086  41.864 51.718  1.00 24.44  ? 89   LEU D CB  1 
ATOM   7107  C CG  . LEU D  2 89  ? 29.080  41.368 52.768  1.00 26.25  ? 89   LEU D CG  1 
ATOM   7108  C CD1 . LEU D  2 89  ? 28.465  40.219 53.562  1.00 28.17  ? 89   LEU D CD1 1 
ATOM   7109  C CD2 . LEU D  2 89  ? 30.411  40.969 52.130  1.00 27.05  ? 89   LEU D CD2 1 
ATOM   7110  N N   . ASP D  2 90  ? 26.470  44.009 50.021  1.00 21.12  ? 90   ASP D N   1 
ATOM   7111  C CA  . ASP D  2 90  ? 25.499  44.321 48.974  1.00 20.52  ? 90   ASP D CA  1 
ATOM   7112  C C   . ASP D  2 90  ? 26.083  45.275 47.951  1.00 19.38  ? 90   ASP D C   1 
ATOM   7113  O O   . ASP D  2 90  ? 25.833  45.131 46.752  1.00 19.00  ? 90   ASP D O   1 
ATOM   7114  C CB  . ASP D  2 90  ? 24.232  44.933 49.563  1.00 20.86  ? 90   ASP D CB  1 
ATOM   7115  C CG  . ASP D  2 90  ? 23.469  43.963 50.424  1.00 22.32  ? 90   ASP D CG  1 
ATOM   7116  O OD1 . ASP D  2 90  ? 23.758  42.745 50.346  1.00 23.21  ? 90   ASP D OD1 1 
ATOM   7117  O OD2 . ASP D  2 90  ? 22.587  44.424 51.184  1.00 22.88  ? 90   ASP D OD2 1 
ATOM   7118  N N   . VAL D  2 91  ? 26.855  46.247 48.428  1.00 19.10  ? 91   VAL D N   1 
ATOM   7119  C CA  . VAL D  2 91  ? 27.521  47.198 47.545  1.00 18.54  ? 91   VAL D CA  1 
ATOM   7120  C C   . VAL D  2 91  ? 28.533  46.488 46.649  1.00 18.39  ? 91   VAL D C   1 
ATOM   7121  O O   . VAL D  2 91  ? 28.542  46.701 45.436  1.00 17.88  ? 91   VAL D O   1 
ATOM   7122  C CB  . VAL D  2 91  ? 28.216  48.327 48.338  1.00 19.00  ? 91   VAL D CB  1 
ATOM   7123  C CG1 . VAL D  2 91  ? 29.166  49.121 47.451  1.00 19.09  ? 91   VAL D CG1 1 
ATOM   7124  C CG2 . VAL D  2 91  ? 27.174  49.252 48.954  1.00 19.22  ? 91   VAL D CG2 1 
ATOM   7125  N N   . TRP D  2 92  ? 29.376  45.646 47.238  1.00 19.08  ? 92   TRP D N   1 
ATOM   7126  C CA  . TRP D  2 92  ? 30.397  44.945 46.458  1.00 19.43  ? 92   TRP D CA  1 
ATOM   7127  C C   . TRP D  2 92  ? 29.821  43.826 45.593  1.00 19.22  ? 92   TRP D C   1 
ATOM   7128  O O   . TRP D  2 92  ? 30.334  43.565 44.507  1.00 19.07  ? 92   TRP D O   1 
ATOM   7129  C CB  . TRP D  2 92  ? 31.528  44.439 47.357  1.00 20.94  ? 92   TRP D CB  1 
ATOM   7130  C CG  . TRP D  2 92  ? 32.423  45.557 47.779  1.00 21.52  ? 92   TRP D CG  1 
ATOM   7131  C CD1 . TRP D  2 92  ? 32.548  46.087 49.032  1.00 22.28  ? 92   TRP D CD1 1 
ATOM   7132  C CD2 . TRP D  2 92  ? 33.286  46.320 46.934  1.00 21.73  ? 92   TRP D CD2 1 
ATOM   7133  N NE1 . TRP D  2 92  ? 33.454  47.121 49.021  1.00 23.08  ? 92   TRP D NE1 1 
ATOM   7134  C CE2 . TRP D  2 92  ? 33.923  47.284 47.744  1.00 22.86  ? 92   TRP D CE2 1 
ATOM   7135  C CE3 . TRP D  2 92  ? 33.598  46.272 45.572  1.00 21.32  ? 92   TRP D CE3 1 
ATOM   7136  C CZ2 . TRP D  2 92  ? 34.856  48.192 47.237  1.00 23.85  ? 92   TRP D CZ2 1 
ATOM   7137  C CZ3 . TRP D  2 92  ? 34.522  47.177 45.068  1.00 22.11  ? 92   TRP D CZ3 1 
ATOM   7138  C CH2 . TRP D  2 92  ? 35.141  48.125 45.901  1.00 23.47  ? 92   TRP D CH2 1 
ATOM   7139  N N   . THR D  2 93  ? 28.756  43.179 46.060  1.00 19.47  ? 93   THR D N   1 
ATOM   7140  C CA  . THR D  2 93  ? 28.048  42.201 45.239  1.00 19.69  ? 93   THR D CA  1 
ATOM   7141  C C   . THR D  2 93  ? 27.450  42.895 44.014  1.00 18.49  ? 93   THR D C   1 
ATOM   7142  O O   . THR D  2 93  ? 27.570  42.400 42.895  1.00 18.44  ? 93   THR D O   1 
ATOM   7143  C CB  . THR D  2 93  ? 26.927  41.492 46.023  1.00 20.76  ? 93   THR D CB  1 
ATOM   7144  O OG1 . THR D  2 93  ? 27.493  40.784 47.131  1.00 22.14  ? 93   THR D OG1 1 
ATOM   7145  C CG2 . THR D  2 93  ? 26.190  40.504 45.138  1.00 21.55  ? 93   THR D CG2 1 
ATOM   7146  N N   . TYR D  2 94  ? 26.811  44.038 44.238  1.00 17.82  ? 94   TYR D N   1 
ATOM   7147  C CA  . TYR D  2 94  ? 26.202  44.817 43.160  1.00 17.14  ? 94   TYR D CA  1 
ATOM   7148  C C   . TYR D  2 94  ? 27.235  45.263 42.125  1.00 16.46  ? 94   TYR D C   1 
ATOM   7149  O O   . TYR D  2 94  ? 27.006  45.149 40.923  1.00 16.12  ? 94   TYR D O   1 
ATOM   7150  C CB  . TYR D  2 94  ? 25.475  46.029 43.747  1.00 17.16  ? 94   TYR D CB  1 
ATOM   7151  C CG  . TYR D  2 94  ? 25.072  47.087 42.744  1.00 16.94  ? 94   TYR D CG  1 
ATOM   7152  C CD1 . TYR D  2 94  ? 25.939  48.126 42.413  1.00 16.61  ? 94   TYR D CD1 1 
ATOM   7153  C CD2 . TYR D  2 94  ? 23.820  47.061 42.140  1.00 17.53  ? 94   TYR D CD2 1 
ATOM   7154  C CE1 . TYR D  2 94  ? 25.572  49.103 41.504  1.00 16.84  ? 94   TYR D CE1 1 
ATOM   7155  C CE2 . TYR D  2 94  ? 23.449  48.032 41.225  1.00 17.75  ? 94   TYR D CE2 1 
ATOM   7156  C CZ  . TYR D  2 94  ? 24.328  49.051 40.914  1.00 17.36  ? 94   TYR D CZ  1 
ATOM   7157  O OH  . TYR D  2 94  ? 23.963  50.018 40.012  1.00 17.97  ? 94   TYR D OH  1 
ATOM   7158  N N   . ASN D  2 95  ? 28.371  45.758 42.604  1.00 16.52  ? 95   ASN D N   1 
ATOM   7159  C CA  . ASN D  2 95  ? 29.462  46.202 41.735  1.00 16.40  ? 95   ASN D CA  1 
ATOM   7160  C C   . ASN D  2 95  ? 29.970  45.106 40.813  1.00 16.36  ? 95   ASN D C   1 
ATOM   7161  O O   . ASN D  2 95  ? 30.148  45.327 39.611  1.00 15.95  ? 95   ASN D O   1 
ATOM   7162  C CB  . ASN D  2 95  ? 30.631  46.718 42.573  1.00 17.22  ? 95   ASN D CB  1 
ATOM   7163  C CG  . ASN D  2 95  ? 30.330  48.044 43.233  1.00 17.53  ? 95   ASN D CG  1 
ATOM   7164  O OD1 . ASN D  2 95  ? 29.314  48.678 42.942  1.00 17.28  ? 95   ASN D OD1 1 
ATOM   7165  N ND2 . ASN D  2 95  ? 31.216  48.477 44.121  1.00 18.51  ? 95   ASN D ND2 1 
ATOM   7166  N N   . ALA D  2 96  ? 30.207  43.936 41.396  1.00 17.02  ? 96   ALA D N   1 
ATOM   7167  C CA  . ALA D  2 96  ? 30.691  42.773 40.666  1.00 17.49  ? 96   ALA D CA  1 
ATOM   7168  C C   . ALA D  2 96  ? 29.699  42.324 39.603  1.00 16.95  ? 96   ALA D C   1 
ATOM   7169  O O   . ALA D  2 96  ? 30.066  42.142 38.449  1.00 16.74  ? 96   ALA D O   1 
ATOM   7170  C CB  . ALA D  2 96  ? 30.964  41.631 41.631  1.00 18.97  ? 96   ALA D CB  1 
ATOM   7171  N N   . GLU D  2 97  ? 28.441  42.153 39.992  1.00 17.00  ? 97   GLU D N   1 
ATOM   7172  C CA  . GLU D  2 97  ? 27.426  41.647 39.067  1.00 17.13  ? 97   GLU D CA  1 
ATOM   7173  C C   . GLU D  2 97  ? 27.122  42.634 37.942  1.00 16.04  ? 97   GLU D C   1 
ATOM   7174  O O   . GLU D  2 97  ? 26.904  42.229 36.803  1.00 16.11  ? 97   GLU D O   1 
ATOM   7175  C CB  . GLU D  2 97  ? 26.142  41.281 39.818  1.00 18.11  ? 97   GLU D CB  1 
ATOM   7176  C CG  . GLU D  2 97  ? 26.318  40.112 40.776  1.00 19.65  ? 97   GLU D CG  1 
ATOM   7177  C CD  . GLU D  2 97  ? 25.028  39.673 41.445  1.00 21.06  ? 97   GLU D CD  1 
ATOM   7178  O OE1 . GLU D  2 97  ? 23.963  40.268 41.173  1.00 20.96  ? 97   GLU D OE1 1 
ATOM   7179  O OE2 . GLU D  2 97  ? 25.077  38.713 42.239  1.00 22.70  ? 97   GLU D OE2 1 
ATOM   7180  N N   . LEU D  2 98  ? 27.113  43.924 38.265  1.00 15.35  ? 98   LEU D N   1 
ATOM   7181  C CA  . LEU D  2 98  ? 26.854  44.958 37.279  1.00 14.80  ? 98   LEU D CA  1 
ATOM   7182  C C   . LEU D  2 98  ? 28.009  45.071 36.304  1.00 14.26  ? 98   LEU D C   1 
ATOM   7183  O O   . LEU D  2 98  ? 27.798  45.157 35.104  1.00 14.05  ? 98   LEU D O   1 
ATOM   7184  C CB  . LEU D  2 98  ? 26.627  46.307 37.954  1.00 14.87  ? 98   LEU D CB  1 
ATOM   7185  C CG  . LEU D  2 98  ? 26.156  47.426 37.018  1.00 15.07  ? 98   LEU D CG  1 
ATOM   7186  C CD1 . LEU D  2 98  ? 24.742  47.156 36.526  1.00 15.76  ? 98   LEU D CD1 1 
ATOM   7187  C CD2 . LEU D  2 98  ? 26.224  48.772 37.723  1.00 15.56  ? 98   LEU D CD2 1 
ATOM   7188  N N   . LEU D  2 99  ? 29.231  45.079 36.822  1.00 14.28  ? 99   LEU D N   1 
ATOM   7189  C CA  . LEU D  2 99  ? 30.411  45.197 35.974  1.00 14.23  ? 99   LEU D CA  1 
ATOM   7190  C C   . LEU D  2 99  ? 30.477  44.055 34.969  1.00 14.13  ? 99   LEU D C   1 
ATOM   7191  O O   . LEU D  2 99  ? 30.762  44.273 33.796  1.00 13.85  ? 99   LEU D O   1 
ATOM   7192  C CB  . LEU D  2 99  ? 31.687  45.216 36.816  1.00 15.01  ? 99   LEU D CB  1 
ATOM   7193  C CG  . LEU D  2 99  ? 32.995  45.475 36.062  1.00 15.61  ? 99   LEU D CG  1 
ATOM   7194  C CD1 . LEU D  2 99  ? 32.955  46.811 35.337  1.00 15.53  ? 99   LEU D CD1 1 
ATOM   7195  C CD2 . LEU D  2 99  ? 34.176  45.430 37.015  1.00 16.97  ? 99   LEU D CD2 1 
ATOM   7196  N N   . VAL D  2 100 ? 30.218  42.839 35.436  1.00 14.60  ? 100  VAL D N   1 
ATOM   7197  C CA  . VAL D  2 100 ? 30.194  41.677 34.554  1.00 14.98  ? 100  VAL D CA  1 
ATOM   7198  C C   . VAL D  2 100 ? 29.134  41.858 33.458  1.00 14.44  ? 100  VAL D C   1 
ATOM   7199  O O   . VAL D  2 100 ? 29.440  41.715 32.281  1.00 14.23  ? 100  VAL D O   1 
ATOM   7200  C CB  . VAL D  2 100 ? 29.976  40.367 35.347  1.00 16.27  ? 100  VAL D CB  1 
ATOM   7201  C CG1 . VAL D  2 100 ? 29.604  39.209 34.425  1.00 17.11  ? 100  VAL D CG1 1 
ATOM   7202  C CG2 . VAL D  2 100 ? 31.230  40.026 36.140  1.00 17.22  ? 100  VAL D CG2 1 
ATOM   7203  N N   . LEU D  2 101 ? 27.908  42.192 33.853  1.00 14.43  ? 101  LEU D N   1 
ATOM   7204  C CA  . LEU D  2 101 ? 26.818  42.464 32.910  1.00 14.44  ? 101  LEU D CA  1 
ATOM   7205  C C   . LEU D  2 101 ? 27.158  43.520 31.851  1.00 13.67  ? 101  LEU D C   1 
ATOM   7206  O O   . LEU D  2 101 ? 26.915  43.323 30.655  1.00 13.72  ? 101  LEU D O   1 
ATOM   7207  C CB  . LEU D  2 101 ? 25.572  42.924 33.676  1.00 15.03  ? 101  LEU D CB  1 
ATOM   7208  C CG  . LEU D  2 101 ? 24.369  41.982 33.787  1.00 16.52  ? 101  LEU D CG  1 
ATOM   7209  C CD1 . LEU D  2 101 ? 24.756  40.526 33.991  1.00 17.39  ? 101  LEU D CD1 1 
ATOM   7210  C CD2 . LEU D  2 101 ? 23.480  42.465 34.918  1.00 17.16  ? 101  LEU D CD2 1 
ATOM   7211  N N   . MET D  2 102 ? 27.696  44.648 32.301  1.00 13.23  ? 102  MET D N   1 
ATOM   7212  C CA  . MET D  2 102 ? 28.000  45.767 31.417  1.00 13.04  ? 102  MET D CA  1 
ATOM   7213  C C   . MET D  2 102 ? 29.162  45.449 30.491  1.00 12.69  ? 102  MET D C   1 
ATOM   7214  O O   . MET D  2 102 ? 29.116  45.754 29.293  1.00 12.67  ? 102  MET D O   1 
ATOM   7215  C CB  . MET D  2 102 ? 28.324  47.019 32.231  1.00 13.30  ? 102  MET D CB  1 
ATOM   7216  C CG  . MET D  2 102 ? 27.123  47.605 32.959  1.00 13.88  ? 102  MET D CG  1 
ATOM   7217  S SD  . MET D  2 102 ? 27.421  49.258 33.622  1.00 14.68  ? 102  MET D SD  1 
ATOM   7218  C CE  . MET D  2 102 ? 28.865  48.961 34.650  1.00 14.35  ? 102  MET D CE  1 
ATOM   7219  N N   . GLU D  2 103 ? 30.200  44.831 31.043  1.00 12.67  ? 103  GLU D N   1 
ATOM   7220  C CA  . GLU D  2 103 ? 31.395  44.530 30.266  1.00 12.77  ? 103  GLU D CA  1 
ATOM   7221  C C   . GLU D  2 103 ? 31.235  43.301 29.371  1.00 12.72  ? 103  GLU D C   1 
ATOM   7222  O O   . GLU D  2 103 ? 31.875  43.221 28.326  1.00 12.75  ? 103  GLU D O   1 
ATOM   7223  C CB  . GLU D  2 103 ? 32.612  44.402 31.180  1.00 13.45  ? 103  GLU D CB  1 
ATOM   7224  C CG  . GLU D  2 103 ? 33.067  45.732 31.779  1.00 13.87  ? 103  GLU D CG  1 
ATOM   7225  C CD  . GLU D  2 103 ? 33.548  46.751 30.746  1.00 14.24  ? 103  GLU D CD  1 
ATOM   7226  O OE1 . GLU D  2 103 ? 33.819  46.377 29.593  1.00 14.14  ? 103  GLU D OE1 1 
ATOM   7227  O OE2 . GLU D  2 103 ? 33.663  47.947 31.087  1.00 14.92  ? 103  GLU D OE2 1 
ATOM   7228  N N   . ASN D  2 104 ? 30.388  42.354 29.768  1.00 12.91  ? 104  ASN D N   1 
ATOM   7229  C CA  . ASN D  2 104 ? 30.002  41.260 28.878  1.00 13.28  ? 104  ASN D CA  1 
ATOM   7230  C C   . ASN D  2 104 ? 29.342  41.786 27.613  1.00 12.88  ? 104  ASN D C   1 
ATOM   7231  O O   . ASN D  2 104 ? 29.619  41.308 26.518  1.00 12.95  ? 104  ASN D O   1 
ATOM   7232  C CB  . ASN D  2 104 ? 29.017  40.308 29.558  1.00 14.16  ? 104  ASN D CB  1 
ATOM   7233  C CG  . ASN D  2 104 ? 29.695  39.288 30.438  1.00 15.17  ? 104  ASN D CG  1 
ATOM   7234  O OD1 . ASN D  2 104 ? 30.911  39.126 30.401  1.00 15.37  ? 104  ASN D OD1 1 
ATOM   7235  N ND2 . ASN D  2 104 ? 28.902  38.583 31.233  1.00 16.22  ? 104  ASN D ND2 1 
ATOM   7236  N N   . GLU D  2 105 ? 28.450  42.756 27.776  1.00 18.37  ? 105  GLU D N   1 
ATOM   7237  C CA  . GLU D  2 105 ? 27.758  43.340 26.646  1.00 18.02  ? 105  GLU D CA  1 
ATOM   7238  C C   . GLU D  2 105 ? 28.727  44.066 25.738  1.00 16.18  ? 105  GLU D C   1 
ATOM   7239  O O   . GLU D  2 105 ? 28.597  44.022 24.519  1.00 15.05  ? 105  GLU D O   1 
ATOM   7240  C CB  . GLU D  2 105 ? 26.680  44.311 27.114  1.00 20.66  ? 105  GLU D CB  1 
ATOM   7241  C CG  . GLU D  2 105 ? 25.719  44.694 26.004  1.00 21.29  ? 105  GLU D CG  1 
ATOM   7242  C CD  . GLU D  2 105 ? 24.383  45.162 26.530  1.00 24.84  ? 105  GLU D CD  1 
ATOM   7243  O OE1 . GLU D  2 105 ? 24.374  46.056 27.401  1.00 26.71  ? 105  GLU D OE1 1 
ATOM   7244  O OE2 . GLU D  2 105 ? 23.344  44.630 26.075  1.00 26.30  ? 105  GLU D OE2 1 
ATOM   7245  N N   . ARG D  2 106 ? 29.689  44.752 26.340  1.00 16.36  ? 106  ARG D N   1 
ATOM   7246  C CA  . ARG D  2 106 ? 30.698  45.460 25.572  1.00 15.41  ? 106  ARG D CA  1 
ATOM   7247  C C   . ARG D  2 106 ? 31.640  44.491 24.866  1.00 13.35  ? 106  ARG D C   1 
ATOM   7248  O O   . ARG D  2 106 ? 32.086  44.765 23.756  1.00 12.43  ? 106  ARG D O   1 
ATOM   7249  C CB  . ARG D  2 106 ? 31.496  46.412 26.458  1.00 17.04  ? 106  ARG D CB  1 
ATOM   7250  C CG  . ARG D  2 106 ? 30.715  47.621 26.954  1.00 19.55  ? 106  ARG D CG  1 
ATOM   7251  C CD  . ARG D  2 106 ? 31.626  48.829 27.128  1.00 21.28  ? 106  ARG D CD  1 
ATOM   7252  N NE  . ARG D  2 106 ? 31.608  49.710 25.947  1.00 21.61  ? 106  ARG D NE  1 
ATOM   7253  C CZ  . ARG D  2 106 ? 32.638  50.449 25.519  1.00 22.51  ? 106  ARG D CZ  1 
ATOM   7254  N NH1 . ARG D  2 106 ? 33.817  50.430 26.143  1.00 23.22  ? 106  ARG D NH1 1 
ATOM   7255  N NH2 . ARG D  2 106 ? 32.495  51.222 24.443  1.00 23.23  ? 106  ARG D NH2 1 
ATOM   7256  N N   . THR D  2 107 ? 31.927  43.357 25.498  1.00 13.06  ? 107  THR D N   1 
ATOM   7257  C CA  . THR D  2 107 ? 32.800  42.349 24.899  1.00 11.78  ? 107  THR D CA  1 
ATOM   7258  C C   . THR D  2 107 ? 32.198  41.753 23.626  1.00 10.51  ? 107  THR D C   1 
ATOM   7259  O O   . THR D  2 107 ? 32.900  41.563 22.641  1.00 9.56   ? 107  THR D O   1 
ATOM   7260  C CB  . THR D  2 107 ? 33.143  41.214 25.889  1.00 12.58  ? 107  THR D CB  1 
ATOM   7261  O OG1 . THR D  2 107 ? 33.865  41.745 27.001  1.00 13.93  ? 107  THR D OG1 1 
ATOM   7262  C CG2 . THR D  2 107 ? 34.007  40.159 25.221  1.00 11.99  ? 107  THR D CG2 1 
ATOM   7263  N N   . LEU D  2 108 ? 30.907  41.460 23.642  1.00 10.92  ? 108  LEU D N   1 
ATOM   7264  C CA  . LEU D  2 108 ? 30.259  40.890 22.470  1.00 10.32  ? 108  LEU D CA  1 
ATOM   7265  C C   . LEU D  2 108 ? 30.177  41.899 21.323  1.00 9.65   ? 108  LEU D C   1 
ATOM   7266  O O   . LEU D  2 108 ? 30.352  41.549 20.161  1.00 8.79   ? 108  LEU D O   1 
ATOM   7267  C CB  . LEU D  2 108 ? 28.866  40.376 22.823  1.00 11.88  ? 108  LEU D CB  1 
ATOM   7268  C CG  . LEU D  2 108 ? 28.791  39.329 23.934  1.00 13.21  ? 108  LEU D CG  1 
ATOM   7269  C CD1 . LEU D  2 108 ? 27.350  38.886 24.109  1.00 15.41  ? 108  LEU D CD1 1 
ATOM   7270  C CD2 . LEU D  2 108 ? 29.692  38.135 23.660  1.00 12.67  ? 108  LEU D CD2 1 
ATOM   7271  N N   . ASP D  2 109 ? 29.908  43.154 21.661  1.00 10.45  ? 109  ASP D N   1 
ATOM   7272  C CA  . ASP D  2 109 ? 29.901  44.219 20.670  1.00 10.49  ? 109  ASP D CA  1 
ATOM   7273  C C   . ASP D  2 109 ? 31.309  44.526 20.140  1.00 9.61   ? 109  ASP D C   1 
ATOM   7274  O O   . ASP D  2 109 ? 31.458  44.949 19.006  1.00 9.45   ? 109  ASP D O   1 
ATOM   7275  C CB  . ASP D  2 109 ? 29.253  45.474 21.253  1.00 12.40  ? 109  ASP D CB  1 
ATOM   7276  C CG  . ASP D  2 109 ? 27.755  45.311 21.476  1.00 14.00  ? 109  ASP D CG  1 
ATOM   7277  O OD1 . ASP D  2 109 ? 27.102  44.574 20.700  1.00 13.83  ? 109  ASP D OD1 1 
ATOM   7278  O OD2 . ASP D  2 109 ? 27.230  45.941 22.427  1.00 15.93  ? 109  ASP D OD2 1 
ATOM   7279  N N   . PHE D  2 110 ? 32.329  44.313 20.967  1.00 9.53   ? 110  PHE D N   1 
ATOM   7280  C CA  . PHE D  2 110 ? 33.725  44.456 20.557  1.00 9.40   ? 110  PHE D CA  1 
ATOM   7281  C C   . PHE D  2 110 ? 34.048  43.460 19.441  1.00 8.25   ? 110  PHE D C   1 
ATOM   7282  O O   . PHE D  2 110 ? 34.616  43.822 18.414  1.00 8.33   ? 110  PHE D O   1 
ATOM   7283  C CB  . PHE D  2 110 ? 34.622  44.235 21.780  1.00 10.14  ? 110  PHE D CB  1 
ATOM   7284  C CG  . PHE D  2 110 ? 36.097  44.289 21.499  1.00 10.82  ? 110  PHE D CG  1 
ATOM   7285  C CD1 . PHE D  2 110 ? 36.685  45.425 20.970  1.00 12.07  ? 110  PHE D CD1 1 
ATOM   7286  C CD2 . PHE D  2 110 ? 36.911  43.212 21.817  1.00 10.95  ? 110  PHE D CD2 1 
ATOM   7287  C CE1 . PHE D  2 110 ? 38.051  45.471 20.730  1.00 13.43  ? 110  PHE D CE1 1 
ATOM   7288  C CE2 . PHE D  2 110 ? 38.277  43.253 21.587  1.00 12.29  ? 110  PHE D CE2 1 
ATOM   7289  C CZ  . PHE D  2 110 ? 38.848  44.384 21.042  1.00 13.56  ? 110  PHE D CZ  1 
ATOM   7290  N N   . HIS D  2 111 ? 33.669  42.204 19.646  1.00 7.66   ? 111  HIS D N   1 
ATOM   7291  C CA  . HIS D  2 111 ? 33.843  41.174 18.636  1.00 7.05   ? 111  HIS D CA  1 
ATOM   7292  C C   . HIS D  2 111 ? 33.089  41.508 17.356  1.00 6.71   ? 111  HIS D C   1 
ATOM   7293  O O   . HIS D  2 111 ? 33.591  41.285 16.254  1.00 6.54   ? 111  HIS D O   1 
ATOM   7294  C CB  . HIS D  2 111 ? 33.369  39.824 19.169  1.00 7.24   ? 111  HIS D CB  1 
ATOM   7295  C CG  . HIS D  2 111 ? 34.292  39.219 20.180  1.00 7.99   ? 111  HIS D CG  1 
ATOM   7296  N ND1 . HIS D  2 111 ? 35.587  38.853 19.881  1.00 8.47   ? 111  HIS D ND1 1 
ATOM   7297  C CD2 . HIS D  2 111 ? 34.103  38.898 21.482  1.00 8.83   ? 111  HIS D CD2 1 
ATOM   7298  C CE1 . HIS D  2 111 ? 36.158  38.342 20.956  1.00 9.60   ? 111  HIS D CE1 1 
ATOM   7299  N NE2 . HIS D  2 111 ? 35.279  38.359 21.941  1.00 9.74   ? 111  HIS D NE2 1 
ATOM   7300  N N   . ASP D  2 112 ? 31.876  42.028 17.507  1.00 7.04   ? 112  ASP D N   1 
ATOM   7301  C CA  . ASP D  2 112 ? 31.056  42.428 16.373  1.00 7.32   ? 112  ASP D CA  1 
ATOM   7302  C C   . ASP D  2 112 ? 31.745  43.552 15.594  1.00 7.60   ? 112  ASP D C   1 
ATOM   7303  O O   . ASP D  2 112 ? 31.786  43.541 14.368  1.00 7.67   ? 112  ASP D O   1 
ATOM   7304  C CB  . ASP D  2 112 ? 29.684  42.872 16.880  1.00 8.45   ? 112  ASP D CB  1 
ATOM   7305  C CG  . ASP D  2 112 ? 28.666  43.016 15.780  1.00 9.36   ? 112  ASP D CG  1 
ATOM   7306  O OD1 . ASP D  2 112 ? 28.929  42.577 14.645  1.00 8.92   ? 112  ASP D OD1 1 
ATOM   7307  O OD2 . ASP D  2 112 ? 27.592  43.579 16.060  1.00 10.94  ? 112  ASP D OD2 1 
ATOM   7308  N N   . SER D  2 113 ? 32.305  44.506 16.330  1.00 8.23   ? 113  SER D N   1 
ATOM   7309  C CA  . SER D  2 113 ? 33.075  45.607 15.757  1.00 9.26   ? 113  SER D CA  1 
ATOM   7310  C C   . SER D  2 113 ? 34.296  45.134 14.959  1.00 9.05   ? 113  SER D C   1 
ATOM   7311  O O   . SER D  2 113 ? 34.560  45.642 13.870  1.00 9.89   ? 113  SER D O   1 
ATOM   7312  C CB  . SER D  2 113 ? 33.533  46.557 16.867  1.00 10.46  ? 113  SER D CB  1 
ATOM   7313  O OG  . SER D  2 113 ? 34.500  47.469 16.394  1.00 11.97  ? 113  SER D OG  1 
ATOM   7314  N N   . ASN D  2 114 ? 35.038  44.177 15.509  1.00 8.45   ? 114  ASN D N   1 
ATOM   7315  C CA  . ASN D  2 114 ? 36.260  43.681 14.874  1.00 8.90   ? 114  ASN D CA  1 
ATOM   7316  C C   . ASN D  2 114 ? 36.004  42.968 13.557  1.00 8.50   ? 114  ASN D C   1 
ATOM   7317  O O   . ASN D  2 114 ? 36.805  43.067 12.630  1.00 9.46   ? 114  ASN D O   1 
ATOM   7318  C CB  . ASN D  2 114 ? 37.007  42.739 15.817  1.00 8.87   ? 114  ASN D CB  1 
ATOM   7319  C CG  . ASN D  2 114 ? 37.586  43.452 17.019  1.00 9.95   ? 114  ASN D CG  1 
ATOM   7320  O OD1 . ASN D  2 114 ? 37.926  44.629 16.958  1.00 11.27  ? 114  ASN D OD1 1 
ATOM   7321  N ND2 . ASN D  2 114 ? 37.718  42.730 18.118  1.00 9.85   ? 114  ASN D ND2 1 
ATOM   7322  N N   . VAL D  2 115 ? 34.893  42.241 13.491  1.00 7.58   ? 115  VAL D N   1 
ATOM   7323  C CA  . VAL D  2 115 ? 34.486  41.539 12.278  1.00 7.58   ? 115  VAL D CA  1 
ATOM   7324  C C   . VAL D  2 115 ? 34.111  42.550 11.199  1.00 8.40   ? 115  VAL D C   1 
ATOM   7325  O O   . VAL D  2 115 ? 34.479  42.402 10.028  1.00 9.07   ? 115  VAL D O   1 
ATOM   7326  C CB  . VAL D  2 115 ? 33.275  40.620 12.540  1.00 7.10   ? 115  VAL D CB  1 
ATOM   7327  C CG1 . VAL D  2 115 ? 32.709  40.074 11.238  1.00 7.59   ? 115  VAL D CG1 1 
ATOM   7328  C CG2 . VAL D  2 115 ? 33.652  39.471 13.455  1.00 6.95   ? 115  VAL D CG2 1 
ATOM   7329  N N   . LYS D  2 116 ? 33.372  43.575 11.608  1.00 8.82   ? 116  LYS D N   1 
ATOM   7330  C CA  . LYS D  2 116 ? 32.888  44.599 10.691  1.00 10.17  ? 116  LYS D CA  1 
ATOM   7331  C C   . LYS D  2 116 ? 34.022  45.426 10.124  1.00 11.56  ? 116  LYS D C   1 
ATOM   7332  O O   . LYS D  2 116 ? 34.024  45.764 8.941   1.00 12.77  ? 116  LYS D O   1 
ATOM   7333  C CB  . LYS D  2 116 ? 31.913  45.517 11.409  1.00 10.91  ? 116  LYS D CB  1 
ATOM   7334  C CG  . LYS D  2 116 ? 30.704  45.860 10.579  1.00 12.24  ? 116  LYS D CG  1 
ATOM   7335  C CD  . LYS D  2 116 ? 30.695  47.294 10.110  1.00 14.49  ? 116  LYS D CD  1 
ATOM   7336  C CE  . LYS D  2 116 ? 29.551  47.484 9.132   1.00 16.18  ? 116  LYS D CE  1 
ATOM   7337  N NZ  . LYS D  2 116 ? 29.041  48.874 9.218   1.00 18.91  ? 116  LYS D NZ  1 
ATOM   7338  N N   . ASN D  2 117 ? 34.990  45.755 10.970  1.00 11.89  ? 117  ASN D N   1 
ATOM   7339  C CA  . ASN D  2 117 ? 36.144  46.522 10.529  1.00 13.94  ? 117  ASN D CA  1 
ATOM   7340  C C   . ASN D  2 117 ? 37.022  45.723 9.572   1.00 14.34  ? 117  ASN D C   1 
ATOM   7341  O O   . ASN D  2 117 ? 37.597  46.281 8.632   1.00 16.40  ? 117  ASN D O   1 
ATOM   7342  C CB  . ASN D  2 117 ? 36.947  47.017 11.731  1.00 14.73  ? 117  ASN D CB  1 
ATOM   7343  C CG  . ASN D  2 117 ? 36.178  48.023 12.566  1.00 15.28  ? 117  ASN D CG  1 
ATOM   7344  O OD1 . ASN D  2 117 ? 35.237  48.654 12.087  1.00 15.92  ? 117  ASN D OD1 1 
ATOM   7345  N ND2 . ASN D  2 117 ? 36.576  48.177 13.823  1.00 15.48  ? 117  ASN D ND2 1 
ATOM   7346  N N   . LEU D  2 118 ? 37.107  44.418 9.810   1.00 12.88  ? 118  LEU D N   1 
ATOM   7347  C CA  . LEU D  2 118 ? 37.830  43.517 8.923   1.00 13.55  ? 118  LEU D CA  1 
ATOM   7348  C C   . LEU D  2 118 ? 37.099  43.371 7.588   1.00 13.78  ? 118  LEU D C   1 
ATOM   7349  O O   . LEU D  2 118 ? 37.726  43.316 6.527   1.00 15.39  ? 118  LEU D O   1 
ATOM   7350  C CB  . LEU D  2 118 ? 37.996  42.150 9.584   1.00 12.40  ? 118  LEU D CB  1 
ATOM   7351  C CG  . LEU D  2 118 ? 38.712  41.052 8.801   1.00 13.42  ? 118  LEU D CG  1 
ATOM   7352  C CD1 . LEU D  2 118 ? 40.076  41.509 8.317   1.00 16.02  ? 118  LEU D CD1 1 
ATOM   7353  C CD2 . LEU D  2 118 ? 38.848  39.815 9.668   1.00 12.84  ? 118  LEU D CD2 1 
ATOM   7354  N N   . TYR D  2 119 ? 35.774  43.313 7.642   1.00 12.66  ? 119  TYR D N   1 
ATOM   7355  C CA  . TYR D  2 119 ? 34.977  43.216 6.430   1.00 13.30  ? 119  TYR D CA  1 
ATOM   7356  C C   . TYR D  2 119 ? 35.114  44.480 5.597   1.00 15.42  ? 119  TYR D C   1 
ATOM   7357  O O   . TYR D  2 119 ? 35.251  44.409 4.379   1.00 16.84  ? 119  TYR D O   1 
ATOM   7358  C CB  . TYR D  2 119 ? 33.508  42.967 6.767   1.00 12.35  ? 119  TYR D CB  1 
ATOM   7359  C CG  . TYR D  2 119 ? 32.601  43.012 5.562   1.00 13.56  ? 119  TYR D CG  1 
ATOM   7360  C CD1 . TYR D  2 119 ? 32.485  41.915 4.718   1.00 13.91  ? 119  TYR D CD1 1 
ATOM   7361  C CD2 . TYR D  2 119 ? 31.868  44.151 5.258   1.00 14.90  ? 119  TYR D CD2 1 
ATOM   7362  C CE1 . TYR D  2 119 ? 31.656  41.946 3.612   1.00 15.43  ? 119  TYR D CE1 1 
ATOM   7363  C CE2 . TYR D  2 119 ? 31.041  44.192 4.147   1.00 16.52  ? 119  TYR D CE2 1 
ATOM   7364  C CZ  . TYR D  2 119 ? 30.935  43.085 3.329   1.00 16.71  ? 119  TYR D CZ  1 
ATOM   7365  O OH  . TYR D  2 119 ? 30.114  43.108 2.223   1.00 18.69  ? 119  TYR D OH  1 
ATOM   7366  N N   . ASP D  2 120 ? 35.058  45.635 6.251   1.00 16.09  ? 120  ASP D N   1 
ATOM   7367  C CA  . ASP D  2 120 ? 35.190  46.905 5.554   1.00 18.77  ? 120  ASP D CA  1 
ATOM   7368  C C   . ASP D  2 120 ? 36.591  47.066 4.970   1.00 20.82  ? 120  ASP D C   1 
ATOM   7369  O O   . ASP D  2 120 ? 36.753  47.597 3.876   1.00 23.23  ? 120  ASP D O   1 
ATOM   7370  C CB  . ASP D  2 120 ? 34.860  48.073 6.491   1.00 19.55  ? 120  ASP D CB  1 
ATOM   7371  C CG  . ASP D  2 120 ? 33.360  48.236 6.732   1.00 19.10  ? 120  ASP D CG  1 
ATOM   7372  O OD1 . ASP D  2 120 ? 32.555  47.955 5.813   1.00 19.54  ? 120  ASP D OD1 1 
ATOM   7373  O OD2 . ASP D  2 120 ? 32.989  48.674 7.844   1.00 18.82  ? 120  ASP D OD2 1 
ATOM   7374  N N   . LYS D  2 121 ? 37.597  46.598 5.701   1.00 20.39  ? 121  LYS D N   1 
ATOM   7375  C CA  . LYS D  2 121 ? 38.989  46.638 5.250   1.00 22.88  ? 121  LYS D CA  1 
ATOM   7376  C C   . LYS D  2 121 ? 39.143  45.973 3.890   1.00 23.83  ? 121  LYS D C   1 
ATOM   7377  O O   . LYS D  2 121 ? 39.771  46.520 2.985   1.00 26.89  ? 121  LYS D O   1 
ATOM   7378  C CB  . LYS D  2 121 ? 39.871  45.925 6.272   1.00 22.17  ? 121  LYS D CB  1 
ATOM   7379  C CG  . LYS D  2 121 ? 41.367  46.019 6.035   1.00 25.41  ? 121  LYS D CG  1 
ATOM   7380  C CD  . LYS D  2 121 ? 42.107  45.395 7.214   1.00 25.00  ? 121  LYS D CD  1 
ATOM   7381  C CE  . LYS D  2 121 ? 43.604  45.673 7.183   1.00 29.04  ? 121  LYS D CE  1 
ATOM   7382  N NZ  . LYS D  2 121 ? 44.360  44.637 6.420   1.00 30.54  ? 121  LYS D NZ  1 
ATOM   7383  N N   . VAL D  2 122 ? 38.551  44.793 3.757   1.00 21.66  ? 122  VAL D N   1 
ATOM   7384  C CA  . VAL D  2 122 ? 38.561  44.054 2.507   1.00 22.59  ? 122  VAL D CA  1 
ATOM   7385  C C   . VAL D  2 122 ? 37.728  44.779 1.449   1.00 23.94  ? 122  VAL D C   1 
ATOM   7386  O O   . VAL D  2 122 ? 38.149  44.906 0.299   1.00 26.44  ? 122  VAL D O   1 
ATOM   7387  C CB  . VAL D  2 122 ? 38.033  42.621 2.719   1.00 20.38  ? 122  VAL D CB  1 
ATOM   7388  C CG1 . VAL D  2 122 ? 37.875  41.885 1.392   1.00 21.63  ? 122  VAL D CG1 1 
ATOM   7389  C CG2 . VAL D  2 122 ? 38.972  41.862 3.640   1.00 19.95  ? 122  VAL D CG2 1 
ATOM   7390  N N   . ARG D  2 123 ? 36.552  45.257 1.846   1.00 22.78  ? 123  ARG D N   1 
ATOM   7391  C CA  . ARG D  2 123 ? 35.660  45.969 0.939   1.00 24.46  ? 123  ARG D CA  1 
ATOM   7392  C C   . ARG D  2 123 ? 36.372  47.150 0.298   1.00 27.98  ? 123  ARG D C   1 
ATOM   7393  O O   . ARG D  2 123 ? 36.258  47.370 -0.912  1.00 30.36  ? 123  ARG D O   1 
ATOM   7394  C CB  . ARG D  2 123 ? 34.435  46.463 1.699   1.00 23.32  ? 123  ARG D CB  1 
ATOM   7395  C CG  . ARG D  2 123 ? 33.319  46.998 0.821   1.00 25.20  ? 123  ARG D CG  1 
ATOM   7396  C CD  . ARG D  2 123 ? 32.169  47.545 1.658   1.00 24.77  ? 123  ARG D CD  1 
ATOM   7397  N NE  . ARG D  2 123 ? 32.612  48.498 2.680   1.00 24.95  ? 123  ARG D NE  1 
ATOM   7398  C CZ  . ARG D  2 123 ? 33.005  49.752 2.441   1.00 27.86  ? 123  ARG D CZ  1 
ATOM   7399  N NH1 . ARG D  2 123 ? 33.037  50.248 1.203   1.00 30.86  ? 123  ARG D NH1 1 
ATOM   7400  N NH2 . ARG D  2 123 ? 33.383  50.520 3.452   1.00 28.21  ? 123  ARG D NH2 1 
ATOM   7401  N N   . LEU D  2 124 ? 37.113  47.898 1.116   1.00 28.81  ? 124  LEU D N   1 
ATOM   7402  C CA  . LEU D  2 124 ? 37.826  49.099 0.661   1.00 32.86  ? 124  LEU D CA  1 
ATOM   7403  C C   . LEU D  2 124 ? 38.991  48.800 -0.291  1.00 35.63  ? 124  LEU D C   1 
ATOM   7404  O O   . LEU D  2 124 ? 39.362  49.652 -1.102  1.00 39.55  ? 124  LEU D O   1 
ATOM   7405  C CB  . LEU D  2 124 ? 38.325  49.912 1.861   1.00 33.36  ? 124  LEU D CB  1 
ATOM   7406  C CG  . LEU D  2 124 ? 37.210  50.575 2.682   1.00 32.26  ? 124  LEU D CG  1 
ATOM   7407  C CD1 . LEU D  2 124 ? 37.696  50.981 4.071   1.00 31.88  ? 124  LEU D CD1 1 
ATOM   7408  C CD2 . LEU D  2 124 ? 36.626  51.770 1.943   1.00 35.75  ? 124  LEU D CD2 1 
ATOM   7409  N N   . GLN D  2 125 ? 39.562  47.602 -0.185  1.00 34.17  ? 125  GLN D N   1 
ATOM   7410  C CA  . GLN D  2 125 ? 40.605  47.155 -1.107  1.00 36.99  ? 125  GLN D CA  1 
ATOM   7411  C C   . GLN D  2 125 ? 40.014  46.784 -2.449  1.00 37.86  ? 125  GLN D C   1 
ATOM   7412  O O   . GLN D  2 125 ? 40.459  47.266 -3.487  1.00 41.62  ? 125  GLN D O   1 
ATOM   7413  C CB  . GLN D  2 125 ? 41.336  45.935 -0.556  1.00 35.56  ? 125  GLN D CB  1 
ATOM   7414  C CG  . GLN D  2 125 ? 42.353  46.259 0.513   1.00 36.53  ? 125  GLN D CG  1 
ATOM   7415  C CD  . GLN D  2 125 ? 42.999  45.013 1.067   1.00 35.48  ? 125  GLN D CD  1 
ATOM   7416  O OE1 . GLN D  2 125 ? 43.823  44.386 0.403   1.00 37.99  ? 125  GLN D OE1 1 
ATOM   7417  N NE2 . GLN D  2 125 ? 42.626  44.640 2.287   1.00 32.29  ? 125  GLN D NE2 1 
ATOM   7418  N N   . LEU D  2 126 ? 39.012  45.914 -2.414  1.00 34.83  ? 126  LEU D N   1 
ATOM   7419  C CA  . LEU D  2 126 ? 38.421  45.376 -3.626  1.00 35.71  ? 126  LEU D CA  1 
ATOM   7420  C C   . LEU D  2 126 ? 37.719  46.448 -4.446  1.00 38.24  ? 126  LEU D C   1 
ATOM   7421  O O   . LEU D  2 126 ? 37.786  46.422 -5.666  1.00 41.01  ? 126  LEU D O   1 
ATOM   7422  C CB  . LEU D  2 126 ? 37.451  44.237 -3.297  1.00 32.38  ? 126  LEU D CB  1 
ATOM   7423  C CG  . LEU D  2 126 ? 38.030  43.025 -2.557  1.00 30.39  ? 126  LEU D CG  1 
ATOM   7424  C CD1 . LEU D  2 126 ? 37.012  41.896 -2.525  1.00 28.37  ? 126  LEU D CD1 1 
ATOM   7425  C CD2 . LEU D  2 126 ? 39.325  42.546 -3.189  1.00 33.07  ? 126  LEU D CD2 1 
ATOM   7426  N N   . ARG D  2 127 ? 37.062  47.397 -3.783  1.00 37.86  ? 127  ARG D N   1 
ATOM   7427  C CA  . ARG D  2 127 ? 36.366  48.488 -4.482  1.00 40.88  ? 127  ARG D CA  1 
ATOM   7428  C C   . ARG D  2 127 ? 35.377  47.902 -5.515  1.00 41.36  ? 127  ARG D C   1 
ATOM   7429  O O   . ARG D  2 127 ? 34.639  46.975 -5.180  1.00 38.52  ? 127  ARG D O   1 
ATOM   7430  C CB  . ARG D  2 127 ? 37.386  49.495 -5.072  1.00 45.44  ? 127  ARG D CB  1 
ATOM   7431  C CG  . ARG D  2 127 ? 37.858  50.527 -4.051  1.00 46.22  ? 127  ARG D CG  1 
ATOM   7432  C CD  . ARG D  2 127 ? 39.353  50.858 -4.101  1.00 49.41  ? 127  ARG D CD  1 
ATOM   7433  N NE  . ARG D  2 127 ? 39.933  51.457 -5.317  1.00 54.77  ? 127  ARG D NE  1 
ATOM   7434  C CZ  . ARG D  2 127 ? 39.376  52.357 -6.138  1.00 58.29  ? 127  ARG D CZ  1 
ATOM   7435  N NH1 . ARG D  2 127 ? 38.152  52.845 -5.951  1.00 57.39  ? 127  ARG D NH1 1 
ATOM   7436  N NH2 . ARG D  2 127 ? 40.078  52.791 -7.183  1.00 63.46  ? 127  ARG D NH2 1 
ATOM   7437  N N   . ASP D  2 128 ? 35.356  48.404 -6.749  1.00 45.33  ? 128  ASP D N   1 
ATOM   7438  C CA  . ASP D  2 128 ? 34.400  47.914 -7.746  1.00 46.38  ? 128  ASP D CA  1 
ATOM   7439  C C   . ASP D  2 128 ? 34.932  46.732 -8.580  1.00 46.71  ? 128  ASP D C   1 
ATOM   7440  O O   . ASP D  2 128 ? 34.357  46.406 -9.615  1.00 48.65  ? 128  ASP D O   1 
ATOM   7441  C CB  . ASP D  2 128 ? 33.947  49.060 -8.663  1.00 50.94  ? 128  ASP D CB  1 
ATOM   7442  C CG  . ASP D  2 128 ? 35.080  49.625 -9.502  1.00 55.08  ? 128  ASP D CG  1 
ATOM   7443  O OD1 . ASP D  2 128 ? 36.250  49.481 -9.091  1.00 54.62  ? 128  ASP D OD1 1 
ATOM   7444  O OD2 . ASP D  2 128 ? 34.800  50.216 -10.571 1.00 59.37  ? 128  ASP D OD2 1 
ATOM   7445  N N   . ASN D  2 129 ? 36.016  46.097 -8.128  1.00 45.34  ? 129  ASN D N   1 
ATOM   7446  C CA  . ASN D  2 129 ? 36.562  44.902 -8.787  1.00 45.84  ? 129  ASN D CA  1 
ATOM   7447  C C   . ASN D  2 129 ? 35.897  43.576 -8.362  1.00 42.61  ? 129  ASN D C   1 
ATOM   7448  O O   . ASN D  2 129 ? 36.269  42.512 -8.873  1.00 43.29  ? 129  ASN D O   1 
ATOM   7449  C CB  . ASN D  2 129 ? 38.083  44.810 -8.566  1.00 46.95  ? 129  ASN D CB  1 
ATOM   7450  C CG  . ASN D  2 129 ? 38.877  45.740 -9.475  1.00 51.90  ? 129  ASN D CG  1 
ATOM   7451  O OD1 . ASN D  2 129 ? 38.343  46.695 -10.050 1.00 54.33  ? 129  ASN D OD1 1 
ATOM   7452  N ND2 . ASN D  2 129 ? 40.171  45.456 -9.614  1.00 54.08  ? 129  ASN D ND2 1 
ATOM   7453  N N   . ALA D  2 130 ? 34.926  43.633 -7.446  1.00 39.68  ? 130  ALA D N   1 
ATOM   7454  C CA  . ALA D  2 130 ? 34.166  42.446 -7.025  1.00 37.26  ? 130  ALA D CA  1 
ATOM   7455  C C   . ALA D  2 130 ? 32.725  42.809 -6.680  1.00 36.42  ? 130  ALA D C   1 
ATOM   7456  O O   . ALA D  2 130 ? 32.435  43.967 -6.421  1.00 36.89  ? 130  ALA D O   1 
ATOM   7457  C CB  . ALA D  2 130 ? 34.835  41.794 -5.828  1.00 34.35  ? 130  ALA D CB  1 
ATOM   7458  N N   . LYS D  2 131 ? 31.832  41.819 -6.677  1.00 35.81  ? 131  LYS D N   1 
ATOM   7459  C CA  . LYS D  2 131 ? 30.430  42.023 -6.289  1.00 35.57  ? 131  LYS D CA  1 
ATOM   7460  C C   . LYS D  2 131 ? 30.249  41.871 -4.778  1.00 32.22  ? 131  LYS D C   1 
ATOM   7461  O O   . LYS D  2 131 ? 30.589  40.835 -4.218  1.00 30.42  ? 131  LYS D O   1 
ATOM   7462  C CB  . LYS D  2 131 ? 29.517  41.010 -6.983  1.00 37.37  ? 131  LYS D CB  1 
ATOM   7463  C CG  . LYS D  2 131 ? 29.468  41.101 -8.502  1.00 41.18  ? 131  LYS D CG  1 
ATOM   7464  C CD  . LYS D  2 131 ? 28.735  39.896 -9.092  1.00 43.08  ? 131  LYS D CD  1 
ATOM   7465  C CE  . LYS D  2 131 ? 28.107  40.171 -10.457 1.00 47.41  ? 131  LYS D CE  1 
ATOM   7466  N NZ  . LYS D  2 131 ? 26.919  41.078 -10.384 1.00 49.03  ? 131  LYS D NZ  1 
ATOM   7467  N N   . GLU D  2 132 ? 29.705  42.893 -4.122  1.00 31.78  ? 132  GLU D N   1 
ATOM   7468  C CA  . GLU D  2 132 ? 29.339  42.786 -2.714  1.00 29.16  ? 132  GLU D CA  1 
ATOM   7469  C C   . GLU D  2 132 ? 28.031  41.994 -2.607  1.00 29.78  ? 132  GLU D C   1 
ATOM   7470  O O   . GLU D  2 132 ? 26.949  42.533 -2.840  1.00 31.89  ? 132  GLU D O   1 
ATOM   7471  C CB  . GLU D  2 132 ? 29.190  44.175 -2.089  1.00 29.26  ? 132  GLU D CB  1 
ATOM   7472  C CG  . GLU D  2 132 ? 29.078  44.160 -0.571  1.00 26.62  ? 132  GLU D CG  1 
ATOM   7473  C CD  . GLU D  2 132 ? 29.176  45.541 0.062   1.00 26.97  ? 132  GLU D CD  1 
ATOM   7474  O OE1 . GLU D  2 132 ? 28.897  46.553 -0.613  1.00 29.73  ? 132  GLU D OE1 1 
ATOM   7475  O OE2 . GLU D  2 132 ? 29.539  45.616 1.250   1.00 24.92  ? 132  GLU D OE2 1 
ATOM   7476  N N   . LEU D  2 133 ? 28.140  40.712 -2.265  1.00 28.56  ? 133  LEU D N   1 
ATOM   7477  C CA  . LEU D  2 133 ? 26.981  39.804 -2.254  1.00 29.91  ? 133  LEU D CA  1 
ATOM   7478  C C   . LEU D  2 133 ? 25.946  40.099 -1.163  1.00 29.62  ? 133  LEU D C   1 
ATOM   7479  O O   . LEU D  2 133 ? 24.763  39.807 -1.347  1.00 32.09  ? 133  LEU D O   1 
ATOM   7480  C CB  . LEU D  2 133 ? 27.443  38.343 -2.148  1.00 29.27  ? 133  LEU D CB  1 
ATOM   7481  C CG  . LEU D  2 133 ? 27.647  37.576 -3.458  1.00 31.72  ? 133  LEU D CG  1 
ATOM   7482  C CD1 . LEU D  2 133 ? 28.255  38.433 -4.557  1.00 32.86  ? 133  LEU D CD1 1 
ATOM   7483  C CD2 . LEU D  2 133 ? 28.504  36.345 -3.212  1.00 30.94  ? 133  LEU D CD2 1 
ATOM   7484  N N   . GLY D  2 134 ? 26.388  40.660 -0.040  1.00 27.10  ? 134  GLY D N   1 
ATOM   7485  C CA  . GLY D  2 134 ? 25.486  41.015 1.059   1.00 27.02  ? 134  GLY D CA  1 
ATOM   7486  C C   . GLY D  2 134 ? 25.527  40.073 2.254   1.00 25.21  ? 134  GLY D C   1 
ATOM   7487  O O   . GLY D  2 134 ? 24.824  40.292 3.244   1.00 25.28  ? 134  GLY D O   1 
ATOM   7488  N N   . ASN D  2 135 ? 26.367  39.041 2.180   1.00 24.04  ? 135  ASN D N   1 
ATOM   7489  C CA  . ASN D  2 135 ? 26.416  37.996 3.210   1.00 23.01  ? 135  ASN D CA  1 
ATOM   7490  C C   . ASN D  2 135 ? 27.787  37.847 3.859   1.00 20.11  ? 135  ASN D C   1 
ATOM   7491  O O   . ASN D  2 135 ? 28.033  36.879 4.580   1.00 19.57  ? 135  ASN D O   1 
ATOM   7492  C CB  . ASN D  2 135 ? 25.999  36.660 2.600   1.00 25.50  ? 135  ASN D CB  1 
ATOM   7493  C CG  . ASN D  2 135 ? 26.824  36.290 1.389   1.00 26.17  ? 135  ASN D CG  1 
ATOM   7494  O OD1 . ASN D  2 135 ? 27.867  36.886 1.129   1.00 24.61  ? 135  ASN D OD1 1 
ATOM   7495  N ND2 . ASN D  2 135 ? 26.349  35.318 0.627   1.00 29.07  ? 135  ASN D ND2 1 
ATOM   7496  N N   . GLY D  2 136 ? 28.674  38.806 3.603   1.00 18.78  ? 136  GLY D N   1 
ATOM   7497  C CA  . GLY D  2 136 ? 30.058  38.732 4.056   1.00 16.84  ? 136  GLY D CA  1 
ATOM   7498  C C   . GLY D  2 136 ? 31.013  38.336 2.947   1.00 17.54  ? 136  GLY D C   1 
ATOM   7499  O O   . GLY D  2 136 ? 32.233  38.389 3.130   1.00 16.79  ? 136  GLY D O   1 
ATOM   7500  N N   . CYS D  2 137 ? 30.462  37.958 1.794   1.00 19.40  ? 137  CYS D N   1 
ATOM   7501  C CA  . CYS D  2 137 ? 31.260  37.469 0.680   1.00 20.70  ? 137  CYS D CA  1 
ATOM   7502  C C   . CYS D  2 137 ? 31.390  38.486 -0.440  1.00 22.02  ? 137  CYS D C   1 
ATOM   7503  O O   . CYS D  2 137 ? 30.482  39.278 -0.699  1.00 22.78  ? 137  CYS D O   1 
ATOM   7504  C CB  . CYS D  2 137 ? 30.676  36.174 0.122   1.00 22.61  ? 137  CYS D CB  1 
ATOM   7505  S SG  . CYS D  2 137 ? 30.595  34.822 1.316   1.00 22.11  ? 137  CYS D SG  1 
ATOM   7506  N N   . PHE D  2 138 ? 32.545  38.444 -1.096  1.00 22.80  ? 138  PHE D N   1 
ATOM   7507  C CA  . PHE D  2 138 ? 32.825  39.249 -2.265  1.00 24.73  ? 138  PHE D CA  1 
ATOM   7508  C C   . PHE D  2 138 ? 33.116  38.317 -3.418  1.00 27.09  ? 138  PHE D C   1 
ATOM   7509  O O   . PHE D  2 138 ? 33.995  37.468 -3.311  1.00 27.25  ? 138  PHE D O   1 
ATOM   7510  C CB  . PHE D  2 138 ? 34.034  40.139 -2.013  1.00 24.43  ? 138  PHE D CB  1 
ATOM   7511  C CG  . PHE D  2 138 ? 33.793  41.198 -0.980  1.00 22.82  ? 138  PHE D CG  1 
ATOM   7512  C CD1 . PHE D  2 138 ? 33.188  42.397 -1.330  1.00 23.92  ? 138  PHE D CD1 1 
ATOM   7513  C CD2 . PHE D  2 138 ? 34.160  40.991 0.347   1.00 20.64  ? 138  PHE D CD2 1 
ATOM   7514  C CE1 . PHE D  2 138 ? 32.960  43.376 -0.380  1.00 22.98  ? 138  PHE D CE1 1 
ATOM   7515  C CE2 . PHE D  2 138 ? 33.933  41.968 1.301   1.00 19.51  ? 138  PHE D CE2 1 
ATOM   7516  C CZ  . PHE D  2 138 ? 33.329  43.161 0.937   1.00 20.71  ? 138  PHE D CZ  1 
ATOM   7517  N N   . GLU D  2 139 ? 32.385  38.482 -4.516  1.00 29.37  ? 139  GLU D N   1 
ATOM   7518  C CA  . GLU D  2 139 ? 32.515  37.623 -5.681  1.00 32.12  ? 139  GLU D CA  1 
ATOM   7519  C C   . GLU D  2 139 ? 33.257  38.371 -6.790  1.00 34.45  ? 139  GLU D C   1 
ATOM   7520  O O   . GLU D  2 139 ? 32.800  39.409 -7.255  1.00 35.46  ? 139  GLU D O   1 
ATOM   7521  C CB  . GLU D  2 139 ? 31.127  37.209 -6.148  1.00 33.74  ? 139  GLU D CB  1 
ATOM   7522  C CG  . GLU D  2 139 ? 31.102  36.117 -7.198  1.00 36.76  ? 139  GLU D CG  1 
ATOM   7523  C CD  . GLU D  2 139 ? 29.738  36.003 -7.839  1.00 39.24  ? 139  GLU D CD  1 
ATOM   7524  O OE1 . GLU D  2 139 ? 28.819  35.452 -7.194  1.00 39.05  ? 139  GLU D OE1 1 
ATOM   7525  O OE2 . GLU D  2 139 ? 29.579  36.492 -8.976  1.00 41.84  ? 139  GLU D OE2 1 
ATOM   7526  N N   . PHE D  2 140 ? 34.394  37.824 -7.217  1.00 35.89  ? 140  PHE D N   1 
ATOM   7527  C CA  . PHE D  2 140 ? 35.316  38.528 -8.114  1.00 38.38  ? 140  PHE D CA  1 
ATOM   7528  C C   . PHE D  2 140 ? 34.857  38.528 -9.565  1.00 41.92  ? 140  PHE D C   1 
ATOM   7529  O O   . PHE D  2 140 ? 34.315  37.537 -10.049 1.00 43.18  ? 140  PHE D O   1 
ATOM   7530  C CB  . PHE D  2 140 ? 36.712  37.902 -8.034  1.00 39.24  ? 140  PHE D CB  1 
ATOM   7531  C CG  . PHE D  2 140 ? 37.363  38.053 -6.694  1.00 36.63  ? 140  PHE D CG  1 
ATOM   7532  C CD1 . PHE D  2 140 ? 37.150  37.120 -5.694  1.00 34.44  ? 140  PHE D CD1 1 
ATOM   7533  C CD2 . PHE D  2 140 ? 38.186  39.134 -6.431  1.00 36.88  ? 140  PHE D CD2 1 
ATOM   7534  C CE1 . PHE D  2 140 ? 37.748  37.262 -4.454  1.00 32.38  ? 140  PHE D CE1 1 
ATOM   7535  C CE2 . PHE D  2 140 ? 38.790  39.283 -5.196  1.00 34.94  ? 140  PHE D CE2 1 
ATOM   7536  C CZ  . PHE D  2 140 ? 38.570  38.346 -4.205  1.00 32.59  ? 140  PHE D CZ  1 
ATOM   7537  N N   . TYR D  2 141 ? 35.091  39.638 -10.260 1.00 44.06  ? 141  TYR D N   1 
ATOM   7538  C CA  . TYR D  2 141 ? 34.824  39.708 -11.699 1.00 48.04  ? 141  TYR D CA  1 
ATOM   7539  C C   . TYR D  2 141 ? 35.899  38.970 -12.482 1.00 50.93  ? 141  TYR D C   1 
ATOM   7540  O O   . TYR D  2 141 ? 35.625  38.375 -13.525 1.00 53.90  ? 141  TYR D O   1 
ATOM   7541  C CB  . TYR D  2 141 ? 34.741  41.159 -12.172 1.00 49.90  ? 141  TYR D CB  1 
ATOM   7542  C CG  . TYR D  2 141 ? 33.559  41.897 -11.599 1.00 48.31  ? 141  TYR D CG  1 
ATOM   7543  C CD1 . TYR D  2 141 ? 32.264  41.444 -11.819 1.00 48.64  ? 141  TYR D CD1 1 
ATOM   7544  C CD2 . TYR D  2 141 ? 33.732  43.032 -10.823 1.00 47.07  ? 141  TYR D CD2 1 
ATOM   7545  C CE1 . TYR D  2 141 ? 31.176  42.108 -11.290 1.00 47.84  ? 141  TYR D CE1 1 
ATOM   7546  C CE2 . TYR D  2 141 ? 32.649  43.705 -10.287 1.00 46.12  ? 141  TYR D CE2 1 
ATOM   7547  C CZ  . TYR D  2 141 ? 31.372  43.239 -10.524 1.00 46.54  ? 141  TYR D CZ  1 
ATOM   7548  O OH  . TYR D  2 141 ? 30.292  43.909 -9.993  1.00 46.21  ? 141  TYR D OH  1 
ATOM   7549  N N   . HIS D  2 142 ? 37.124  39.028 -11.970 1.00 50.62  ? 142  HIS D N   1 
ATOM   7550  C CA  . HIS D  2 142 ? 38.256  38.303 -12.541 1.00 53.60  ? 142  HIS D CA  1 
ATOM   7551  C C   . HIS D  2 142 ? 38.435  36.980 -11.815 1.00 52.02  ? 142  HIS D C   1 
ATOM   7552  O O   . HIS D  2 142 ? 37.947  36.802 -10.698 1.00 48.39  ? 142  HIS D O   1 
ATOM   7553  C CB  . HIS D  2 142 ? 39.541  39.135 -12.431 1.00 55.20  ? 142  HIS D CB  1 
ATOM   7554  C CG  . HIS D  2 142 ? 39.869  39.564 -11.034 1.00 51.89  ? 142  HIS D CG  1 
ATOM   7555  N ND1 . HIS D  2 142 ? 40.785  38.902 -10.247 1.00 51.29  ? 142  HIS D ND1 1 
ATOM   7556  C CD2 . HIS D  2 142 ? 39.389  40.581 -10.278 1.00 49.42  ? 142  HIS D CD2 1 
ATOM   7557  C CE1 . HIS D  2 142 ? 40.861  39.498 -9.069  1.00 48.45  ? 142  HIS D CE1 1 
ATOM   7558  N NE2 . HIS D  2 142 ? 40.022  40.518 -9.062  1.00 47.22  ? 142  HIS D NE2 1 
ATOM   7559  N N   . LYS D  2 143 ? 39.139  36.054 -12.456 1.00 55.24  ? 143  LYS D N   1 
ATOM   7560  C CA  . LYS D  2 143 ? 39.523  34.806 -11.812 1.00 54.83  ? 143  LYS D CA  1 
ATOM   7561  C C   . LYS D  2 143 ? 40.573  35.140 -10.757 1.00 53.45  ? 143  LYS D C   1 
ATOM   7562  O O   . LYS D  2 143 ? 41.516  35.882 -11.035 1.00 55.52  ? 143  LYS D O   1 
ATOM   7563  C CB  . LYS D  2 143 ? 40.083  33.831 -12.841 1.00 59.53  ? 143  LYS D CB  1 
ATOM   7564  C CG  . LYS D  2 143 ? 40.163  32.390 -12.375 1.00 59.99  ? 143  LYS D CG  1 
ATOM   7565  C CD  . LYS D  2 143 ? 40.797  31.515 -13.452 1.00 65.43  ? 143  LYS D CD  1 
ATOM   7566  C CE  . LYS D  2 143 ? 41.291  30.191 -12.889 1.00 66.85  ? 143  LYS D CE  1 
ATOM   7567  N NZ  . LYS D  2 143 ? 42.483  30.330 -12.001 1.00 66.55  ? 143  LYS D NZ  1 
ATOM   7568  N N   . CYS D  2 144 ? 40.397  34.607 -9.549  1.00 50.42  ? 144  CYS D N   1 
ATOM   7569  C CA  . CYS D  2 144 ? 41.263  34.938 -8.416  1.00 48.93  ? 144  CYS D CA  1 
ATOM   7570  C C   . CYS D  2 144 ? 41.890  33.672 -7.825  1.00 49.87  ? 144  CYS D C   1 
ATOM   7571  O O   . CYS D  2 144 ? 41.262  32.968 -7.038  1.00 47.61  ? 144  CYS D O   1 
ATOM   7572  C CB  . CYS D  2 144 ? 40.452  35.687 -7.357  1.00 44.45  ? 144  CYS D CB  1 
ATOM   7573  S SG  . CYS D  2 144 ? 41.405  36.353 -5.970  1.00 42.79  ? 144  CYS D SG  1 
ATOM   7574  N N   . ASP D  2 145 ? 43.131  33.389 -8.217  1.00 53.84  ? 145  ASP D N   1 
ATOM   7575  C CA  . ASP D  2 145 ? 43.853  32.199 -7.744  1.00 55.87  ? 145  ASP D CA  1 
ATOM   7576  C C   . ASP D  2 145 ? 44.301  32.361 -6.279  1.00 53.48  ? 145  ASP D C   1 
ATOM   7577  O O   . ASP D  2 145 ? 43.974  33.359 -5.632  1.00 50.01  ? 145  ASP D O   1 
ATOM   7578  C CB  . ASP D  2 145 ? 45.036  31.874 -8.676  1.00 61.66  ? 145  ASP D CB  1 
ATOM   7579  C CG  . ASP D  2 145 ? 46.090  32.972 -8.719  1.00 63.46  ? 145  ASP D CG  1 
ATOM   7580  O OD1 . ASP D  2 145 ? 45.993  33.950 -7.956  1.00 60.29  ? 145  ASP D OD1 1 
ATOM   7581  O OD2 . ASP D  2 145 ? 47.028  32.854 -9.531  1.00 68.63  ? 145  ASP D OD2 1 
ATOM   7582  N N   . ASN D  2 146 ? 45.039  31.383 -5.758  1.00 55.72  ? 146  ASN D N   1 
ATOM   7583  C CA  . ASN D  2 146 ? 45.448  31.399 -4.350  1.00 53.94  ? 146  ASN D CA  1 
ATOM   7584  C C   . ASN D  2 146 ? 46.426  32.517 -3.995  1.00 54.67  ? 146  ASN D C   1 
ATOM   7585  O O   . ASN D  2 146 ? 46.483  32.944 -2.845  1.00 52.13  ? 146  ASN D O   1 
ATOM   7586  C CB  . ASN D  2 146 ? 46.031  30.045 -3.945  1.00 57.07  ? 146  ASN D CB  1 
ATOM   7587  C CG  . ASN D  2 146 ? 45.011  28.922 -4.020  1.00 56.44  ? 146  ASN D CG  1 
ATOM   7588  O OD1 . ASN D  2 146 ? 43.805  29.147 -3.945  1.00 52.65  ? 146  ASN D OD1 1 
ATOM   7589  N ND2 . ASN D  2 146 ? 45.498  27.701 -4.166  1.00 60.76  ? 146  ASN D ND2 1 
ATOM   7590  N N   . GLU D  2 147 ? 47.183  32.999 -4.976  1.00 58.63  ? 147  GLU D N   1 
ATOM   7591  C CA  . GLU D  2 147 ? 48.044  34.166 -4.773  1.00 60.07  ? 147  GLU D CA  1 
ATOM   7592  C C   . GLU D  2 147 ? 47.192  35.433 -4.745  1.00 56.17  ? 147  GLU D C   1 
ATOM   7593  O O   . GLU D  2 147 ? 47.405  36.320 -3.916  1.00 54.70  ? 147  GLU D O   1 
ATOM   7594  C CB  . GLU D  2 147 ? 49.109  34.276 -5.868  1.00 66.26  ? 147  GLU D CB  1 
ATOM   7595  C CG  . GLU D  2 147 ? 50.054  33.084 -5.944  1.00 71.28  ? 147  GLU D CG  1 
ATOM   7596  C CD  . GLU D  2 147 ? 49.543  31.993 -6.867  1.00 72.65  ? 147  GLU D CD  1 
ATOM   7597  O OE1 . GLU D  2 147 ? 49.809  32.070 -8.087  1.00 76.48  ? 147  GLU D OE1 1 
ATOM   7598  O OE2 . GLU D  2 147 ? 48.876  31.058 -6.372  1.00 70.35  ? 147  GLU D OE2 1 
ATOM   7599  N N   . CYS D  2 148 ? 46.229  35.507 -5.661  1.00 55.06  ? 148  CYS D N   1 
ATOM   7600  C CA  . CYS D  2 148 ? 45.249  36.591 -5.684  1.00 51.67  ? 148  CYS D CA  1 
ATOM   7601  C C   . CYS D  2 148 ? 44.472  36.654 -4.367  1.00 46.81  ? 148  CYS D C   1 
ATOM   7602  O O   . CYS D  2 148 ? 44.264  37.733 -3.811  1.00 44.86  ? 148  CYS D O   1 
ATOM   7603  C CB  . CYS D  2 148 ? 44.289  36.405 -6.861  1.00 51.66  ? 148  CYS D CB  1 
ATOM   7604  S SG  . CYS D  2 148 ? 42.848  37.487 -6.838  1.00 47.59  ? 148  CYS D SG  1 
ATOM   7605  N N   . MET D  2 149 ? 44.048  35.495 -3.869  1.00 45.48  ? 149  MET D N   1 
ATOM   7606  C CA  . MET D  2 149 ? 43.362  35.422 -2.581  1.00 41.47  ? 149  MET D CA  1 
ATOM   7607  C C   . MET D  2 149 ? 44.287  35.875 -1.460  1.00 41.84  ? 149  MET D C   1 
ATOM   7608  O O   . MET D  2 149 ? 43.862  36.563 -0.536  1.00 38.86  ? 149  MET D O   1 
ATOM   7609  C CB  . MET D  2 149 ? 42.886  33.995 -2.300  1.00 40.95  ? 149  MET D CB  1 
ATOM   7610  C CG  . MET D  2 149 ? 41.816  33.480 -3.251  1.00 40.83  ? 149  MET D CG  1 
ATOM   7611  S SD  . MET D  2 149 ? 40.316  34.470 -3.232  1.00 36.79  ? 149  MET D SD  1 
ATOM   7612  C CE  . MET D  2 149 ? 39.197  33.427 -4.165  1.00 37.97  ? 149  MET D CE  1 
ATOM   7613  N N   . GLU D  2 150 ? 45.553  35.484 -1.548  1.00 46.24  ? 150  GLU D N   1 
ATOM   7614  C CA  . GLU D  2 150 ? 46.543  35.853 -0.542  1.00 47.73  ? 150  GLU D CA  1 
ATOM   7615  C C   . GLU D  2 150 ? 46.802  37.360 -0.510  1.00 48.21  ? 150  GLU D C   1 
ATOM   7616  O O   . GLU D  2 150 ? 47.040  37.916 0.558   1.00 47.25  ? 150  GLU D O   1 
ATOM   7617  C CB  . GLU D  2 150 ? 47.851  35.076 -0.772  1.00 53.07  ? 150  GLU D CB  1 
ATOM   7618  C CG  . GLU D  2 150 ? 49.007  35.415 0.167   1.00 55.54  ? 150  GLU D CG  1 
ATOM   7619  C CD  . GLU D  2 150 ? 48.673  35.233 1.636   1.00 52.25  ? 150  GLU D CD  1 
ATOM   7620  O OE1 . GLU D  2 150 ? 47.755  34.453 1.962   1.00 49.22  ? 150  GLU D OE1 1 
ATOM   7621  O OE2 . GLU D  2 150 ? 49.337  35.872 2.476   1.00 53.22  ? 150  GLU D OE2 1 
ATOM   7622  N N   . SER D  2 151 ? 46.752  38.016 -1.670  1.00 50.34  ? 151  SER D N   1 
ATOM   7623  C CA  . SER D  2 151 ? 46.970  39.465 -1.744  1.00 51.63  ? 151  SER D CA  1 
ATOM   7624  C C   . SER D  2 151 ? 45.868  40.239 -1.011  1.00 47.45  ? 151  SER D C   1 
ATOM   7625  O O   . SER D  2 151 ? 46.112  41.314 -0.453  1.00 47.76  ? 151  SER D O   1 
ATOM   7626  C CB  . SER D  2 151 ? 47.060  39.930 -3.198  1.00 54.78  ? 151  SER D CB  1 
ATOM   7627  O OG  . SER D  2 151 ? 45.799  39.879 -3.836  1.00 51.98  ? 151  SER D OG  1 
ATOM   7628  N N   . VAL D  2 152 ? 44.659  39.681 -1.014  1.00 44.31  ? 152  VAL D N   1 
ATOM   7629  C CA  . VAL D  2 152 ? 43.529  40.274 -0.306  1.00 40.63  ? 152  VAL D CA  1 
ATOM   7630  C C   . VAL D  2 152 ? 43.742  40.152 1.202   1.00 39.36  ? 152  VAL D C   1 
ATOM   7631  O O   . VAL D  2 152 ? 43.507  41.107 1.942   1.00 38.02  ? 152  VAL D O   1 
ATOM   7632  C CB  . VAL D  2 152 ? 42.193  39.610 -0.704  1.00 37.91  ? 152  VAL D CB  1 
ATOM   7633  C CG1 . VAL D  2 152 ? 41.030  40.242 0.049   1.00 34.38  ? 152  VAL D CG1 1 
ATOM   7634  C CG2 . VAL D  2 152 ? 41.968  39.719 -2.208  1.00 40.09  ? 152  VAL D CG2 1 
ATOM   7635  N N   . ARG D  2 153 ? 44.195  38.984 1.653   1.00 40.53  ? 153  ARG D N   1 
ATOM   7636  C CA  . ARG D  2 153 ? 44.518  38.782 3.068   1.00 40.22  ? 153  ARG D CA  1 
ATOM   7637  C C   . ARG D  2 153 ? 45.771  39.574 3.461   1.00 44.44  ? 153  ARG D C   1 
ATOM   7638  O O   . ARG D  2 153 ? 45.835  40.137 4.553   1.00 43.45  ? 153  ARG D O   1 
ATOM   7639  C CB  . ARG D  2 153 ? 44.719  37.296 3.382   1.00 40.50  ? 153  ARG D CB  1 
ATOM   7640  C CG  . ARG D  2 153 ? 43.527  36.408 3.062   1.00 37.98  ? 153  ARG D CG  1 
ATOM   7641  C CD  . ARG D  2 153 ? 43.756  34.971 3.518   1.00 38.94  ? 153  ARG D CD  1 
ATOM   7642  N NE  . ARG D  2 153 ? 43.355  34.015 2.482   1.00 40.16  ? 153  ARG D NE  1 
ATOM   7643  C CZ  . ARG D  2 153 ? 44.187  33.378 1.656   1.00 44.05  ? 153  ARG D CZ  1 
ATOM   7644  N NH1 . ARG D  2 153 ? 45.505  33.548 1.735   1.00 47.27  ? 153  ARG D NH1 1 
ATOM   7645  N NH2 . ARG D  2 153 ? 43.695  32.544 0.744   1.00 45.23  ? 153  ARG D NH2 1 
ATOM   7646  N N   . ASN D  2 154 ? 46.766  39.586 2.571   1.00 50.42  ? 154  ASN D N   1 
ATOM   7647  C CA  . ASN D  2 154 ? 47.959  40.442 2.697   1.00 55.83  ? 154  ASN D CA  1 
ATOM   7648  C C   . ASN D  2 154 ? 47.640  41.889 3.065   1.00 54.22  ? 154  ASN D C   1 
ATOM   7649  O O   . ASN D  2 154 ? 48.300  42.477 3.924   1.00 56.01  ? 154  ASN D O   1 
ATOM   7650  C CB  . ASN D  2 154 ? 48.734  40.482 1.367   1.00 62.48  ? 154  ASN D CB  1 
ATOM   7651  C CG  . ASN D  2 154 ? 49.885  39.496 1.305   1.00 69.61  ? 154  ASN D CG  1 
ATOM   7652  O OD1 . ASN D  2 154 ? 50.172  38.789 2.270   1.00 69.57  ? 154  ASN D OD1 1 
ATOM   7653  N ND2 . ASN D  2 154 ? 50.561  39.453 0.149   1.00 78.05  ? 154  ASN D ND2 1 
ATOM   7654  N N   . GLY D  2 155 ? 46.627  42.446 2.402   1.00 51.08  ? 155  GLY D N   1 
ATOM   7655  C CA  . GLY D  2 155 ? 46.397  43.888 2.369   1.00 50.83  ? 155  GLY D CA  1 
ATOM   7656  C C   . GLY D  2 155 ? 46.975  44.488 1.097   1.00 54.60  ? 155  GLY D C   1 
ATOM   7657  O O   . GLY D  2 155 ? 46.946  45.702 0.911   1.00 56.35  ? 155  GLY D O   1 
ATOM   7658  N N   . THR D  2 156 ? 47.476  43.625 0.212   1.00 56.11  ? 156  THR D N   1 
ATOM   7659  C CA  . THR D  2 156 ? 48.261  44.034 -0.954  1.00 60.91  ? 156  THR D CA  1 
ATOM   7660  C C   . THR D  2 156 ? 47.517  43.794 -2.270  1.00 60.02  ? 156  THR D C   1 
ATOM   7661  O O   . THR D  2 156 ? 48.136  43.720 -3.331  1.00 64.28  ? 156  THR D O   1 
ATOM   7662  C CB  . THR D  2 156 ? 49.592  43.249 -0.988  1.00 65.21  ? 156  THR D CB  1 
ATOM   7663  O OG1 . THR D  2 156 ? 50.224  43.324 0.295   1.00 65.66  ? 156  THR D OG1 1 
ATOM   7664  C CG2 . THR D  2 156 ? 50.555  43.797 -2.050  1.00 71.82  ? 156  THR D CG2 1 
ATOM   7665  N N   . TYR D  2 157 ? 46.192  43.681 -2.214  1.00 54.93  ? 157  TYR D N   1 
ATOM   7666  C CA  . TYR D  2 157 ? 45.409  43.426 -3.424  1.00 54.30  ? 157  TYR D CA  1 
ATOM   7667  C C   . TYR D  2 157 ? 45.625  44.544 -4.440  1.00 58.38  ? 157  TYR D C   1 
ATOM   7668  O O   . TYR D  2 157 ? 45.208  45.679 -4.217  1.00 58.18  ? 157  TYR D O   1 
ATOM   7669  C CB  . TYR D  2 157 ? 43.919  43.299 -3.104  1.00 49.09  ? 157  TYR D CB  1 
ATOM   7670  C CG  . TYR D  2 157 ? 43.060  43.111 -4.337  1.00 49.03  ? 157  TYR D CG  1 
ATOM   7671  C CD1 . TYR D  2 157 ? 43.028  41.892 -5.008  1.00 49.29  ? 157  TYR D CD1 1 
ATOM   7672  C CD2 . TYR D  2 157 ? 42.289  44.155 -4.839  1.00 49.29  ? 157  TYR D CD2 1 
ATOM   7673  C CE1 . TYR D  2 157 ? 42.248  41.716 -6.139  1.00 49.77  ? 157  TYR D CE1 1 
ATOM   7674  C CE2 . TYR D  2 157 ? 41.506  43.988 -5.971  1.00 49.85  ? 157  TYR D CE2 1 
ATOM   7675  C CZ  . TYR D  2 157 ? 41.488  42.767 -6.616  1.00 50.03  ? 157  TYR D CZ  1 
ATOM   7676  O OH  . TYR D  2 157 ? 40.708  42.603 -7.738  1.00 50.94  ? 157  TYR D OH  1 
ATOM   7677  N N   . ASP D  2 158 ? 46.277  44.214 -5.552  1.00 62.52  ? 158  ASP D N   1 
ATOM   7678  C CA  . ASP D  2 158 ? 46.636  45.215 -6.553  1.00 67.46  ? 158  ASP D CA  1 
ATOM   7679  C C   . ASP D  2 158 ? 45.440  45.557 -7.441  1.00 66.32  ? 158  ASP D C   1 
ATOM   7680  O O   . ASP D  2 158 ? 45.259  44.978 -8.519  1.00 67.73  ? 158  ASP D O   1 
ATOM   7681  C CB  . ASP D  2 158 ? 47.819  44.737 -7.401  1.00 73.02  ? 158  ASP D CB  1 
ATOM   7682  C CG  . ASP D  2 158 ? 48.507  45.875 -8.127  1.00 79.21  ? 158  ASP D CG  1 
ATOM   7683  O OD1 . ASP D  2 158 ? 48.976  46.813 -7.445  1.00 81.00  ? 158  ASP D OD1 1 
ATOM   7684  O OD2 . ASP D  2 158 ? 48.582  45.836 -9.373  1.00 82.73  ? 158  ASP D OD2 1 
ATOM   7685  N N   . TYR D  2 159 ? 44.634  46.510 -6.973  1.00 64.30  ? 159  TYR D N   1 
ATOM   7686  C CA  . TYR D  2 159 ? 43.427  46.946 -7.679  1.00 63.43  ? 159  TYR D CA  1 
ATOM   7687  C C   . TYR D  2 159 ? 43.698  47.315 -9.149  1.00 68.69  ? 159  TYR D C   1 
ATOM   7688  O O   . TYR D  2 159 ? 43.025  46.790 -10.038 1.00 68.43  ? 159  TYR D O   1 
ATOM   7689  C CB  . TYR D  2 159 ? 42.737  48.093 -6.912  1.00 61.96  ? 159  TYR D CB  1 
ATOM   7690  C CG  . TYR D  2 159 ? 41.619  48.778 -7.667  1.00 62.65  ? 159  TYR D CG  1 
ATOM   7691  C CD1 . TYR D  2 159 ? 41.883  49.844 -8.528  1.00 67.93  ? 159  TYR D CD1 1 
ATOM   7692  C CD2 . TYR D  2 159 ? 40.298  48.366 -7.516  1.00 58.65  ? 159  TYR D CD2 1 
ATOM   7693  C CE1 . TYR D  2 159 ? 40.863  50.471 -9.224  1.00 69.14  ? 159  TYR D CE1 1 
ATOM   7694  C CE2 . TYR D  2 159 ? 39.272  48.988 -8.204  1.00 59.90  ? 159  TYR D CE2 1 
ATOM   7695  C CZ  . TYR D  2 159 ? 39.560  50.042 -9.055  1.00 65.17  ? 159  TYR D CZ  1 
ATOM   7696  O OH  . TYR D  2 159 ? 38.552  50.671 -9.748  1.00 67.09  ? 159  TYR D OH  1 
ATOM   7697  N N   . PRO D  2 160 ? 44.690  48.198 -9.412  1.00 73.96  ? 160  PRO D N   1 
ATOM   7698  C CA  . PRO D  2 160 ? 44.998  48.589 -10.802 1.00 79.63  ? 160  PRO D CA  1 
ATOM   7699  C C   . PRO D  2 160 ? 45.326  47.453 -11.791 1.00 81.15  ? 160  PRO D C   1 
ATOM   7700  O O   . PRO D  2 160 ? 45.145  47.636 -12.999 1.00 84.67  ? 160  PRO D O   1 
ATOM   7701  C CB  . PRO D  2 160 ? 46.216  49.507 -10.644 1.00 85.15  ? 160  PRO D CB  1 
ATOM   7702  C CG  . PRO D  2 160 ? 46.055  50.099 -9.290  1.00 82.27  ? 160  PRO D CG  1 
ATOM   7703  C CD  . PRO D  2 160 ? 45.467  49.002 -8.446  1.00 75.46  ? 160  PRO D CD  1 
ATOM   7704  N N   . GLN D  2 161 ? 45.806  46.310 -11.297 1.00 79.08  ? 161  GLN D N   1 
ATOM   7705  C CA  . GLN D  2 161 ? 46.113  45.162 -12.166 1.00 80.76  ? 161  GLN D CA  1 
ATOM   7706  C C   . GLN D  2 161 ? 44.841  44.474 -12.660 1.00 77.33  ? 161  GLN D C   1 
ATOM   7707  O O   . GLN D  2 161 ? 44.728  44.136 -13.841 1.00 80.16  ? 161  GLN D O   1 
ATOM   7708  C CB  . GLN D  2 161 ? 46.999  44.143 -11.436 1.00 80.13  ? 161  GLN D CB  1 
ATOM   7709  C CG  . GLN D  2 161 ? 47.290  42.865 -12.219 1.00 81.88  ? 161  GLN D CG  1 
ATOM   7710  C CD  . GLN D  2 161 ? 48.058  41.839 -11.404 1.00 81.27  ? 161  GLN D CD  1 
ATOM   7711  O OE1 . GLN D  2 161 ? 47.926  41.770 -10.179 1.00 77.29  ? 161  GLN D OE1 1 
ATOM   7712  N NE2 . GLN D  2 161 ? 48.860  41.027 -12.083 1.00 85.65  ? 161  GLN D NE2 1 
ATOM   7713  N N   . TYR D  2 162 ? 43.895  44.264 -11.747 1.00 71.66  ? 162  TYR D N   1 
ATOM   7714  C CA  . TYR D  2 162 ? 42.651  43.566 -12.066 1.00 68.63  ? 162  TYR D CA  1 
ATOM   7715  C C   . TYR D  2 162 ? 41.530  44.513 -12.527 1.00 68.66  ? 162  TYR D C   1 
ATOM   7716  O O   . TYR D  2 162 ? 40.387  44.081 -12.695 1.00 66.40  ? 162  TYR D O   1 
ATOM   7717  C CB  . TYR D  2 162 ? 42.188  42.754 -10.852 1.00 63.22  ? 162  TYR D CB  1 
ATOM   7718  C CG  . TYR D  2 162 ? 43.205  41.739 -10.363 1.00 63.48  ? 162  TYR D CG  1 
ATOM   7719  C CD1 . TYR D  2 162 ? 43.413  40.541 -11.051 1.00 65.19  ? 162  TYR D CD1 1 
ATOM   7720  C CD2 . TYR D  2 162 ? 43.958  41.975 -9.211  1.00 62.51  ? 162  TYR D CD2 1 
ATOM   7721  C CE1 . TYR D  2 162 ? 44.341  39.609 -10.604 1.00 66.06  ? 162  TYR D CE1 1 
ATOM   7722  C CE2 . TYR D  2 162 ? 44.888  41.050 -8.757  1.00 63.28  ? 162  TYR D CE2 1 
ATOM   7723  C CZ  . TYR D  2 162 ? 45.076  39.869 -9.454  1.00 65.12  ? 162  TYR D CZ  1 
ATOM   7724  O OH  . TYR D  2 162 ? 45.999  38.950 -9.003  1.00 66.50  ? 162  TYR D OH  1 
ATOM   7725  N N   . SER D  2 163 ? 41.859  45.791 -12.728 1.00 71.88  ? 163  SER D N   1 
ATOM   7726  C CA  . SER D  2 163 ? 40.894  46.791 -13.201 1.00 73.00  ? 163  SER D CA  1 
ATOM   7727  C C   . SER D  2 163 ? 41.167  47.132 -14.666 1.00 78.77  ? 163  SER D C   1 
ATOM   7728  O O   . SER D  2 163 ? 40.675  48.134 -15.187 1.00 81.47  ? 163  SER D O   1 
ATOM   7729  C CB  . SER D  2 163 ? 40.965  48.058 -12.325 1.00 72.97  ? 163  SER D CB  1 
ATOM   7730  O OG  . SER D  2 163 ? 41.930  48.970 -12.818 1.00 78.63  ? 163  SER D OG  1 
ATOM   7731  N N   . ASP E  1 1   ? 42.823  65.424 -8.594  1.00 31.01  ? 1    ASP E N   1 
ATOM   7732  C CA  . ASP E  1 1   ? 42.331  66.188 -7.412  1.00 31.31  ? 1    ASP E CA  1 
ATOM   7733  C C   . ASP E  1 1   ? 41.670  65.253 -6.406  1.00 28.97  ? 1    ASP E C   1 
ATOM   7734  O O   . ASP E  1 1   ? 41.034  64.274 -6.792  1.00 27.44  ? 1    ASP E O   1 
ATOM   7735  C CB  . ASP E  1 1   ? 41.346  67.279 -7.844  1.00 32.90  ? 1    ASP E CB  1 
ATOM   7736  C CG  . ASP E  1 1   ? 41.958  68.269 -8.822  1.00 35.59  ? 1    ASP E CG  1 
ATOM   7737  O OD1 . ASP E  1 1   ? 43.162  68.150 -9.141  1.00 36.25  ? 1    ASP E OD1 1 
ATOM   7738  O OD2 . ASP E  1 1   ? 41.225  69.172 -9.277  1.00 37.36  ? 1    ASP E OD2 1 
ATOM   7739  N N   . GLN E  1 2   ? 41.827  65.559 -5.120  1.00 28.90  ? 2    GLN E N   1 
ATOM   7740  C CA  . GLN E  1 2   ? 41.245  64.738 -4.058  1.00 26.92  ? 2    GLN E CA  1 
ATOM   7741  C C   . GLN E  1 2   ? 40.972  65.508 -2.770  1.00 27.34  ? 2    GLN E C   1 
ATOM   7742  O O   . GLN E  1 2   ? 41.657  66.479 -2.453  1.00 29.00  ? 2    GLN E O   1 
ATOM   7743  C CB  . GLN E  1 2   ? 42.146  63.535 -3.752  1.00 25.65  ? 2    GLN E CB  1 
ATOM   7744  C CG  . GLN E  1 2   ? 43.456  63.868 -3.051  1.00 26.62  ? 2    GLN E CG  1 
ATOM   7745  C CD  . GLN E  1 2   ? 44.181  62.639 -2.539  1.00 25.50  ? 2    GLN E CD  1 
ATOM   7746  O OE1 . GLN E  1 2   ? 44.772  62.672 -1.467  1.00 25.65  ? 2    GLN E OE1 1 
ATOM   7747  N NE2 . GLN E  1 2   ? 44.143  61.550 -3.299  1.00 24.64  ? 2    GLN E NE2 1 
ATOM   7748  N N   . ILE E  1 3   ? 39.963  65.051 -2.036  1.00 26.00  ? 3    ILE E N   1 
ATOM   7749  C CA  . ILE E  1 3   ? 39.667  65.563 -0.704  1.00 26.12  ? 3    ILE E CA  1 
ATOM   7750  C C   . ILE E  1 3   ? 39.702  64.404 0.291   1.00 24.12  ? 3    ILE E C   1 
ATOM   7751  O O   . ILE E  1 3   ? 39.199  63.322 0.002   1.00 22.74  ? 3    ILE E O   1 
ATOM   7752  C CB  . ILE E  1 3   ? 38.305  66.289 -0.655  1.00 26.97  ? 3    ILE E CB  1 
ATOM   7753  C CG1 . ILE E  1 3   ? 38.173  67.083 0.650   1.00 27.69  ? 3    ILE E CG1 1 
ATOM   7754  C CG2 . ILE E  1 3   ? 37.147  65.311 -0.806  1.00 25.52  ? 3    ILE E CG2 1 
ATOM   7755  C CD1 . ILE E  1 3   ? 37.075  68.121 0.626   1.00 29.50  ? 3    ILE E CD1 1 
ATOM   7756  N N   . CYS E  1 4   ? 40.311  64.634 1.450   1.00 24.23  ? 4    CYS E N   1 
ATOM   7757  C CA  . CYS E  1 4   ? 40.460  63.595 2.465   1.00 22.65  ? 4    CYS E CA  1 
ATOM   7758  C C   . CYS E  1 4   ? 39.790  64.009 3.752   1.00 22.42  ? 4    CYS E C   1 
ATOM   7759  O O   . CYS E  1 4   ? 39.647  65.196 4.023   1.00 23.84  ? 4    CYS E O   1 
ATOM   7760  C CB  . CYS E  1 4   ? 41.937  63.318 2.748   1.00 23.02  ? 4    CYS E CB  1 
ATOM   7761  S SG  . CYS E  1 4   ? 42.912  62.943 1.278   1.00 23.82  ? 4    CYS E SG  1 
ATOM   7762  N N   . ILE E  1 5   ? 39.380  63.016 4.537   1.00 20.82  ? 5    ILE E N   1 
ATOM   7763  C CA  . ILE E  1 5   ? 38.866  63.245 5.876   1.00 20.49  ? 5    ILE E CA  1 
ATOM   7764  C C   . ILE E  1 5   ? 39.884  62.707 6.864   1.00 19.85  ? 5    ILE E C   1 
ATOM   7765  O O   . ILE E  1 5   ? 40.437  61.624 6.672   1.00 19.06  ? 5    ILE E O   1 
ATOM   7766  C CB  . ILE E  1 5   ? 37.520  62.538 6.099   1.00 19.52  ? 5    ILE E CB  1 
ATOM   7767  C CG1 . ILE E  1 5   ? 36.523  62.946 5.019   1.00 20.33  ? 5    ILE E CG1 1 
ATOM   7768  C CG2 . ILE E  1 5   ? 36.963  62.849 7.484   1.00 19.44  ? 5    ILE E CG2 1 
ATOM   7769  C CD1 . ILE E  1 5   ? 36.066  64.377 5.121   1.00 22.06  ? 5    ILE E CD1 1 
ATOM   7770  N N   . GLY E  1 6   ? 40.129  63.473 7.920   1.00 20.42  ? 6    GLY E N   1 
ATOM   7771  C CA  . GLY E  1 6   ? 41.139  63.114 8.900   1.00 20.17  ? 6    GLY E CA  1 
ATOM   7772  C C   . GLY E  1 6   ? 40.946  63.821 10.217  1.00 20.50  ? 6    GLY E C   1 
ATOM   7773  O O   . GLY E  1 6   ? 39.994  64.571 10.404  1.00 20.93  ? 6    GLY E O   1 
ATOM   7774  N N   . TYR E  1 7   ? 41.877  63.583 11.126  1.00 20.53  ? 7    TYR E N   1 
ATOM   7775  C CA  . TYR E  1 7   ? 41.725  64.015 12.503  1.00 20.64  ? 7    TYR E CA  1 
ATOM   7776  C C   . TYR E  1 7   ? 43.022  64.590 13.051  1.00 22.10  ? 7    TYR E C   1 
ATOM   7777  O O   . TYR E  1 7   ? 44.092  64.411 12.476  1.00 22.84  ? 7    TYR E O   1 
ATOM   7778  C CB  . TYR E  1 7   ? 41.232  62.851 13.373  1.00 18.95  ? 7    TYR E CB  1 
ATOM   7779  C CG  . TYR E  1 7   ? 42.080  61.597 13.299  1.00 18.29  ? 7    TYR E CG  1 
ATOM   7780  C CD1 . TYR E  1 7   ? 41.869  60.640 12.313  1.00 17.59  ? 7    TYR E CD1 1 
ATOM   7781  C CD2 . TYR E  1 7   ? 43.084  61.362 14.224  1.00 18.63  ? 7    TYR E CD2 1 
ATOM   7782  C CE1 . TYR E  1 7   ? 42.646  59.496 12.246  1.00 17.37  ? 7    TYR E CE1 1 
ATOM   7783  C CE2 . TYR E  1 7   ? 43.860  60.220 14.166  1.00 18.46  ? 7    TYR E CE2 1 
ATOM   7784  C CZ  . TYR E  1 7   ? 43.637  59.293 13.178  1.00 17.88  ? 7    TYR E CZ  1 
ATOM   7785  O OH  . TYR E  1 7   ? 44.419  58.166 13.129  1.00 18.09  ? 7    TYR E OH  1 
ATOM   7786  N N   . HIS E  1 8   ? 42.896  65.279 14.177  1.00 22.74  ? 8    HIS E N   1 
ATOM   7787  C CA  . HIS E  1 8   ? 43.985  66.036 14.776  1.00 24.55  ? 8    HIS E CA  1 
ATOM   7788  C C   . HIS E  1 8   ? 45.053  65.128 15.384  1.00 24.35  ? 8    HIS E C   1 
ATOM   7789  O O   . HIS E  1 8   ? 44.745  64.070 15.925  1.00 22.79  ? 8    HIS E O   1 
ATOM   7790  C CB  . HIS E  1 8   ? 43.406  66.959 15.854  1.00 25.17  ? 8    HIS E CB  1 
ATOM   7791  C CG  . HIS E  1 8   ? 44.414  67.854 16.503  1.00 27.25  ? 8    HIS E CG  1 
ATOM   7792  N ND1 . HIS E  1 8   ? 45.081  68.845 15.816  1.00 29.64  ? 8    HIS E ND1 1 
ATOM   7793  C CD2 . HIS E  1 8   ? 44.846  67.928 17.785  1.00 27.54  ? 8    HIS E CD2 1 
ATOM   7794  C CE1 . HIS E  1 8   ? 45.893  69.481 16.642  1.00 31.39  ? 8    HIS E CE1 1 
ATOM   7795  N NE2 . HIS E  1 8   ? 45.768  68.945 17.843  1.00 30.10  ? 8    HIS E NE2 1 
ATOM   7796  N N   . ALA E  1 9   ? 46.311  65.542 15.264  1.00 26.32  ? 9    ALA E N   1 
ATOM   7797  C CA  . ALA E  1 9   ? 47.411  64.949 16.022  1.00 26.88  ? 9    ALA E CA  1 
ATOM   7798  C C   . ALA E  1 9   ? 48.266  66.090 16.547  1.00 29.45  ? 9    ALA E C   1 
ATOM   7799  O O   . ALA E  1 9   ? 48.151  67.218 16.075  1.00 30.96  ? 9    ALA E O   1 
ATOM   7800  C CB  . ALA E  1 9   ? 48.235  64.022 15.150  1.00 27.07  ? 9    ALA E CB  1 
ATOM   7801  N N   . ASN E  1 10  ? 49.108  65.806 17.530  1.00 30.25  ? 10   ASN E N   1 
ATOM   7802  C CA  . ASN E  1 10  ? 49.978  66.827 18.095  1.00 32.97  ? 10   ASN E CA  1 
ATOM   7803  C C   . ASN E  1 10  ? 51.169  66.218 18.826  1.00 34.19  ? 10   ASN E C   1 
ATOM   7804  O O   . ASN E  1 10  ? 51.340  65.000 18.825  1.00 33.01  ? 10   ASN E O   1 
ATOM   7805  C CB  . ASN E  1 10  ? 49.179  67.771 19.010  1.00 32.95  ? 10   ASN E CB  1 
ATOM   7806  C CG  . ASN E  1 10  ? 48.668  67.093 20.266  1.00 31.05  ? 10   ASN E CG  1 
ATOM   7807  O OD1 . ASN E  1 10  ? 48.992  65.941 20.553  1.00 29.96  ? 10   ASN E OD1 1 
ATOM   7808  N ND2 . ASN E  1 10  ? 47.855  67.812 21.024  1.00 30.86  ? 10   ASN E ND2 1 
ATOM   7809  N N   . ASN E  1 11  ? 51.981  67.069 19.451  1.00 36.91  ? 11   ASN E N   1 
ATOM   7810  C CA  . ASN E  1 11  ? 53.197  66.631 20.138  1.00 38.71  ? 11   ASN E CA  1 
ATOM   7811  C C   . ASN E  1 11  ? 52.972  66.241 21.611  1.00 37.67  ? 11   ASN E C   1 
ATOM   7812  O O   . ASN E  1 11  ? 53.921  66.194 22.393  1.00 39.51  ? 11   ASN E O   1 
ATOM   7813  C CB  . ASN E  1 11  ? 54.287  67.712 20.008  1.00 42.58  ? 11   ASN E CB  1 
ATOM   7814  C CG  . ASN E  1 11  ? 53.910  69.027 20.683  1.00 43.77  ? 11   ASN E CG  1 
ATOM   7815  O OD1 . ASN E  1 11  ? 52.863  69.134 21.329  1.00 41.79  ? 11   ASN E OD1 1 
ATOM   7816  N ND2 . ASN E  1 11  ? 54.769  70.039 20.536  1.00 47.35  ? 11   ASN E ND2 1 
ATOM   7817  N N   . SER E  1 12  ? 51.722  65.951 21.975  1.00 34.95  ? 12   SER E N   1 
ATOM   7818  C CA  . SER E  1 12  ? 51.363  65.562 23.343  1.00 33.78  ? 12   SER E CA  1 
ATOM   7819  C C   . SER E  1 12  ? 51.840  64.148 23.648  1.00 33.19  ? 12   SER E C   1 
ATOM   7820  O O   . SER E  1 12  ? 51.834  63.286 22.772  1.00 32.43  ? 12   SER E O   1 
ATOM   7821  C CB  . SER E  1 12  ? 49.840  65.640 23.543  1.00 31.25  ? 12   SER E CB  1 
ATOM   7822  O OG  . SER E  1 12  ? 49.454  65.242 24.850  1.00 30.14  ? 12   SER E OG  1 
ATOM   7823  N N   . THR E  1 13  ? 52.254  63.931 24.896  1.00 33.82  ? 13   THR E N   1 
ATOM   7824  C CA  . THR E  1 13  ? 52.639  62.608 25.392  1.00 33.50  ? 13   THR E CA  1 
ATOM   7825  C C   . THR E  1 13  ? 51.763  62.158 26.564  1.00 31.61  ? 13   THR E C   1 
ATOM   7826  O O   . THR E  1 13  ? 52.044  61.133 27.183  1.00 31.54  ? 13   THR E O   1 
ATOM   7827  C CB  . THR E  1 13  ? 54.110  62.590 25.851  1.00 36.51  ? 13   THR E CB  1 
ATOM   7828  O OG1 . THR E  1 13  ? 54.351  63.695 26.732  1.00 37.94  ? 13   THR E OG1 1 
ATOM   7829  C CG2 . THR E  1 13  ? 55.046  62.670 24.657  1.00 38.59  ? 13   THR E CG2 1 
ATOM   7830  N N   . GLU E  1 14  ? 50.705  62.914 26.864  1.00 30.37  ? 14   GLU E N   1 
ATOM   7831  C CA  . GLU E  1 14  ? 49.782  62.548 27.936  1.00 28.68  ? 14   GLU E CA  1 
ATOM   7832  C C   . GLU E  1 14  ? 49.081  61.234 27.628  1.00 26.63  ? 14   GLU E C   1 
ATOM   7833  O O   . GLU E  1 14  ? 48.591  61.034 26.516  1.00 25.73  ? 14   GLU E O   1 
ATOM   7834  C CB  . GLU E  1 14  ? 48.724  63.631 28.151  1.00 28.05  ? 14   GLU E CB  1 
ATOM   7835  C CG  . GLU E  1 14  ? 49.261  64.916 28.756  1.00 30.24  ? 14   GLU E CG  1 
ATOM   7836  C CD  . GLU E  1 14  ? 48.314  65.504 29.792  1.00 29.65  ? 14   GLU E CD  1 
ATOM   7837  O OE1 . GLU E  1 14  ? 48.255  64.954 30.923  1.00 29.09  ? 14   GLU E OE1 1 
ATOM   7838  O OE2 . GLU E  1 14  ? 47.619  66.503 29.468  1.00 29.97  ? 14   GLU E OE2 1 
ATOM   7839  N N   . GLN E  1 15  ? 49.028  60.351 28.620  1.00 26.09  ? 15   GLN E N   1 
ATOM   7840  C CA  . GLN E  1 15  ? 48.425  59.038 28.455  1.00 24.66  ? 15   GLN E CA  1 
ATOM   7841  C C   . GLN E  1 15  ? 47.244  58.861 29.391  1.00 23.01  ? 15   GLN E C   1 
ATOM   7842  O O   . GLN E  1 15  ? 47.179  59.492 30.444  1.00 23.19  ? 15   GLN E O   1 
ATOM   7843  C CB  . GLN E  1 15  ? 49.450  57.953 28.744  1.00 26.05  ? 15   GLN E CB  1 
ATOM   7844  C CG  . GLN E  1 15  ? 50.728  58.085 27.939  1.00 28.12  ? 15   GLN E CG  1 
ATOM   7845  C CD  . GLN E  1 15  ? 51.701  56.964 28.211  1.00 29.84  ? 15   GLN E CD  1 
ATOM   7846  O OE1 . GLN E  1 15  ? 52.299  56.415 27.291  1.00 30.90  ? 15   GLN E OE1 1 
ATOM   7847  N NE2 . GLN E  1 15  ? 51.860  56.611 29.478  1.00 30.34  ? 15   GLN E NE2 1 
ATOM   7848  N N   . VAL E  1 16  ? 46.311  58.002 28.995  1.00 21.55  ? 16   VAL E N   1 
ATOM   7849  C CA  . VAL E  1 16  ? 45.176  57.645 29.836  1.00 20.28  ? 16   VAL E CA  1 
ATOM   7850  C C   . VAL E  1 16  ? 44.985  56.142 29.785  1.00 20.09  ? 16   VAL E C   1 
ATOM   7851  O O   . VAL E  1 16  ? 45.395  55.500 28.822  1.00 20.49  ? 16   VAL E O   1 
ATOM   7852  C CB  . VAL E  1 16  ? 43.873  58.343 29.391  1.00 19.02  ? 16   VAL E CB  1 
ATOM   7853  C CG1 . VAL E  1 16  ? 44.049  59.856 29.396  1.00 19.61  ? 16   VAL E CG1 1 
ATOM   7854  C CG2 . VAL E  1 16  ? 43.431  57.861 28.019  1.00 18.41  ? 16   VAL E CG2 1 
ATOM   7855  N N   . ASP E  1 17  ? 44.364  55.590 30.824  1.00 19.71  ? 17   ASP E N   1 
ATOM   7856  C CA  . ASP E  1 17  ? 44.041  54.173 30.867  1.00 19.81  ? 17   ASP E CA  1 
ATOM   7857  C C   . ASP E  1 17  ? 42.573  53.947 30.504  1.00 18.61  ? 17   ASP E C   1 
ATOM   7858  O O   . ASP E  1 17  ? 41.715  54.801 30.735  1.00 17.69  ? 17   ASP E O   1 
ATOM   7859  C CB  . ASP E  1 17  ? 44.321  53.593 32.257  1.00 20.62  ? 17   ASP E CB  1 
ATOM   7860  C CG  . ASP E  1 17  ? 45.810  53.480 32.572  1.00 22.36  ? 17   ASP E CG  1 
ATOM   7861  O OD1 . ASP E  1 17  ? 46.627  53.252 31.653  1.00 23.29  ? 17   ASP E OD1 1 
ATOM   7862  O OD2 . ASP E  1 17  ? 46.162  53.600 33.766  1.00 23.01  ? 17   ASP E OD2 1 
ATOM   7863  N N   . THR E  1 18  ? 42.312  52.781 29.922  1.00 18.93  ? 18   THR E N   1 
ATOM   7864  C CA  . THR E  1 18  ? 40.968  52.303 29.630  1.00 18.35  ? 18   THR E CA  1 
ATOM   7865  C C   . THR E  1 18  ? 40.887  50.858 30.106  1.00 19.52  ? 18   THR E C   1 
ATOM   7866  O O   . THR E  1 18  ? 41.874  50.310 30.595  1.00 20.72  ? 18   THR E O   1 
ATOM   7867  C CB  . THR E  1 18  ? 40.666  52.358 28.119  1.00 17.85  ? 18   THR E CB  1 
ATOM   7868  O OG1 . THR E  1 18  ? 41.455  51.383 27.433  1.00 18.76  ? 18   THR E OG1 1 
ATOM   7869  C CG2 . THR E  1 18  ? 40.970  53.728 27.556  1.00 17.25  ? 18   THR E CG2 1 
ATOM   7870  N N   . ILE E  1 19  ? 39.727  50.234 29.955  1.00 19.63  ? 19   ILE E N   1 
ATOM   7871  C CA  . ILE E  1 19  ? 39.553  48.846 30.380  1.00 21.13  ? 19   ILE E CA  1 
ATOM   7872  C C   . ILE E  1 19  ? 40.473  47.904 29.588  1.00 22.55  ? 19   ILE E C   1 
ATOM   7873  O O   . ILE E  1 19  ? 41.198  47.096 30.167  1.00 24.00  ? 19   ILE E O   1 
ATOM   7874  C CB  . ILE E  1 19  ? 38.087  48.385 30.209  1.00 21.14  ? 19   ILE E CB  1 
ATOM   7875  C CG1 . ILE E  1 19  ? 37.141  49.194 31.111  1.00 20.39  ? 19   ILE E CG1 1 
ATOM   7876  C CG2 . ILE E  1 19  ? 37.944  46.897 30.507  1.00 22.95  ? 19   ILE E CG2 1 
ATOM   7877  C CD1 . ILE E  1 19  ? 37.206  48.842 32.585  1.00 21.09  ? 19   ILE E CD1 1 
ATOM   7878  N N   . MET E  1 20  ? 40.441  48.028 28.264  1.00 22.38  ? 20   MET E N   1 
ATOM   7879  C CA  . MET E  1 20  ? 41.151  47.104 27.384  1.00 23.88  ? 20   MET E CA  1 
ATOM   7880  C C   . MET E  1 20  ? 42.599  47.483 27.103  1.00 24.61  ? 20   MET E C   1 
ATOM   7881  O O   . MET E  1 20  ? 43.377  46.643 26.650  1.00 26.16  ? 20   MET E O   1 
ATOM   7882  C CB  . MET E  1 20  ? 40.429  47.005 26.047  1.00 23.33  ? 20   MET E CB  1 
ATOM   7883  C CG  . MET E  1 20  ? 39.036  46.423 26.131  1.00 23.49  ? 20   MET E CG  1 
ATOM   7884  S SD  . MET E  1 20  ? 38.463  45.975 24.490  1.00 23.66  ? 20   MET E SD  1 
ATOM   7885  C CE  . MET E  1 20  ? 36.698  45.865 24.773  1.00 23.64  ? 20   MET E CE  1 
ATOM   7886  N N   . GLU E  1 21  ? 42.955  48.743 27.335  1.00 23.91  ? 21   GLU E N   1 
ATOM   7887  C CA  . GLU E  1 21  ? 44.291  49.219 27.006  1.00 24.86  ? 21   GLU E CA  1 
ATOM   7888  C C   . GLU E  1 21  ? 44.762  50.268 27.998  1.00 24.98  ? 21   GLU E C   1 
ATOM   7889  O O   . GLU E  1 21  ? 44.002  51.157 28.390  1.00 23.54  ? 21   GLU E O   1 
ATOM   7890  C CB  . GLU E  1 21  ? 44.310  49.788 25.589  1.00 24.04  ? 21   GLU E CB  1 
ATOM   7891  C CG  . GLU E  1 21  ? 45.696  49.832 24.961  1.00 25.33  ? 21   GLU E CG  1 
ATOM   7892  C CD  . GLU E  1 21  ? 45.689  50.323 23.515  1.00 24.69  ? 21   GLU E CD  1 
ATOM   7893  O OE1 . GLU E  1 21  ? 44.597  50.436 22.910  1.00 23.31  ? 21   GLU E OE1 1 
ATOM   7894  O OE2 . GLU E  1 21  ? 46.787  50.594 22.982  1.00 25.69  ? 21   GLU E OE2 1 
ATOM   7895  N N   . LYS E  1 22  ? 46.027  50.157 28.393  1.00 27.13  ? 22   LYS E N   1 
ATOM   7896  C CA  . LYS E  1 22  ? 46.630  51.095 29.324  1.00 27.82  ? 22   LYS E CA  1 
ATOM   7897  C C   . LYS E  1 22  ? 47.692  51.927 28.627  1.00 28.97  ? 22   LYS E C   1 
ATOM   7898  O O   . LYS E  1 22  ? 48.226  51.520 27.602  1.00 29.80  ? 22   LYS E O   1 
ATOM   7899  C CB  . LYS E  1 22  ? 47.221  50.338 30.511  1.00 29.55  ? 22   LYS E CB  1 
ATOM   7900  C CG  . LYS E  1 22  ? 46.162  49.869 31.500  1.00 28.96  ? 22   LYS E CG  1 
ATOM   7901  C CD  . LYS E  1 22  ? 46.638  48.690 32.328  1.00 31.13  ? 22   LYS E CD  1 
ATOM   7902  C CE  . LYS E  1 22  ? 47.917  49.020 33.089  1.00 32.89  ? 22   LYS E CE  1 
ATOM   7903  N NZ  . LYS E  1 22  ? 48.200  48.060 34.197  1.00 34.78  ? 22   LYS E NZ  1 
ATOM   7904  N N   . ASN E  1 23  ? 47.979  53.099 29.186  1.00 29.52  ? 23   ASN E N   1 
ATOM   7905  C CA  . ASN E  1 23  ? 48.996  53.997 28.649  1.00 31.13  ? 23   ASN E CA  1 
ATOM   7906  C C   . ASN E  1 23  ? 48.730  54.387 27.188  1.00 29.39  ? 23   ASN E C   1 
ATOM   7907  O O   . ASN E  1 23  ? 49.628  54.350 26.349  1.00 30.57  ? 23   ASN E O   1 
ATOM   7908  C CB  . ASN E  1 23  ? 50.396  53.379 28.818  1.00 35.24  ? 23   ASN E CB  1 
ATOM   7909  C CG  . ASN E  1 23  ? 50.813  53.243 30.276  1.00 38.42  ? 23   ASN E CG  1 
ATOM   7910  O OD1 . ASN E  1 23  ? 50.247  53.893 31.161  1.00 37.50  ? 23   ASN E OD1 1 
ATOM   7911  N ND2 . ASN E  1 23  ? 51.826  52.393 30.534  1.00 43.60  ? 23   ASN E ND2 1 
ATOM   7912  N N   . VAL E  1 24  ? 47.486  54.762 26.902  1.00 26.53  ? 24   VAL E N   1 
ATOM   7913  C CA  . VAL E  1 24  ? 47.083  55.244 25.575  1.00 25.06  ? 24   VAL E CA  1 
ATOM   7914  C C   . VAL E  1 24  ? 47.397  56.737 25.436  1.00 24.79  ? 24   VAL E C   1 
ATOM   7915  O O   . VAL E  1 24  ? 46.838  57.554 26.163  1.00 24.09  ? 24   VAL E O   1 
ATOM   7916  C CB  . VAL E  1 24  ? 45.568  55.043 25.341  1.00 23.17  ? 24   VAL E CB  1 
ATOM   7917  C CG1 . VAL E  1 24  ? 45.122  55.711 24.047  1.00 22.49  ? 24   VAL E CG1 1 
ATOM   7918  C CG2 . VAL E  1 24  ? 45.218  53.564 25.325  1.00 23.21  ? 24   VAL E CG2 1 
ATOM   7919  N N   . THR E  1 25  ? 48.271  57.091 24.497  1.00 25.37  ? 25   THR E N   1 
ATOM   7920  C CA  . THR E  1 25  ? 48.661  58.487 24.302  1.00 25.72  ? 25   THR E CA  1 
ATOM   7921  C C   . THR E  1 25  ? 47.542  59.259 23.622  1.00 24.04  ? 25   THR E C   1 
ATOM   7922  O O   . THR E  1 25  ? 47.080  58.860 22.553  1.00 23.22  ? 25   THR E O   1 
ATOM   7923  C CB  . THR E  1 25  ? 49.926  58.620 23.433  1.00 27.64  ? 25   THR E CB  1 
ATOM   7924  O OG1 . THR E  1 25  ? 50.922  57.696 23.879  1.00 29.18  ? 25   THR E OG1 1 
ATOM   7925  C CG2 . THR E  1 25  ? 50.479  60.031 23.509  1.00 29.04  ? 25   THR E CG2 1 
ATOM   7926  N N   . VAL E  1 26  ? 47.131  60.372 24.228  1.00 23.63  ? 26   VAL E N   1 
ATOM   7927  C CA  . VAL E  1 26  ? 46.041  61.194 23.697  1.00 22.52  ? 26   VAL E CA  1 
ATOM   7928  C C   . VAL E  1 26  ? 46.496  62.620 23.429  1.00 23.91  ? 26   VAL E C   1 
ATOM   7929  O O   . VAL E  1 26  ? 47.516  63.064 23.950  1.00 25.53  ? 26   VAL E O   1 
ATOM   7930  C CB  . VAL E  1 26  ? 44.816  61.221 24.635  1.00 21.16  ? 26   VAL E CB  1 
ATOM   7931  C CG1 . VAL E  1 26  ? 44.221  59.831 24.757  1.00 19.86  ? 26   VAL E CG1 1 
ATOM   7932  C CG2 . VAL E  1 26  ? 45.177  61.775 26.006  1.00 21.89  ? 26   VAL E CG2 1 
ATOM   7933  N N   . THR E  1 27  ? 45.722  63.331 22.617  1.00 23.49  ? 27   THR E N   1 
ATOM   7934  C CA  . THR E  1 27  ? 46.059  64.694 22.235  1.00 25.13  ? 27   THR E CA  1 
ATOM   7935  C C   . THR E  1 27  ? 45.748  65.677 23.355  1.00 25.78  ? 27   THR E C   1 
ATOM   7936  O O   . THR E  1 27  ? 46.456  66.671 23.518  1.00 27.91  ? 27   THR E O   1 
ATOM   7937  C CB  . THR E  1 27  ? 45.325  65.146 20.955  1.00 24.91  ? 27   THR E CB  1 
ATOM   7938  O OG1 . THR E  1 27  ? 43.918  65.228 21.198  1.00 23.64  ? 27   THR E OG1 1 
ATOM   7939  C CG2 . THR E  1 27  ? 45.594  64.188 19.808  1.00 24.24  ? 27   THR E CG2 1 
ATOM   7940  N N   . HIS E  1 28  ? 44.689  65.411 24.115  1.00 24.26  ? 28   HIS E N   1 
ATOM   7941  C CA  . HIS E  1 28  ? 44.316  66.256 25.249  1.00 24.80  ? 28   HIS E CA  1 
ATOM   7942  C C   . HIS E  1 28  ? 43.794  65.417 26.394  1.00 23.31  ? 28   HIS E C   1 
ATOM   7943  O O   . HIS E  1 28  ? 43.147  64.397 26.179  1.00 21.74  ? 28   HIS E O   1 
ATOM   7944  C CB  . HIS E  1 28  ? 43.248  67.264 24.839  1.00 25.20  ? 28   HIS E CB  1 
ATOM   7945  C CG  . HIS E  1 28  ? 43.639  68.109 23.670  1.00 26.79  ? 28   HIS E CG  1 
ATOM   7946  N ND1 . HIS E  1 28  ? 43.514  67.675 22.368  1.00 26.15  ? 28   HIS E ND1 1 
ATOM   7947  C CD2 . HIS E  1 28  ? 44.168  69.352 23.606  1.00 29.19  ? 28   HIS E CD2 1 
ATOM   7948  C CE1 . HIS E  1 28  ? 43.943  68.619 21.552  1.00 28.03  ? 28   HIS E CE1 1 
ATOM   7949  N NE2 . HIS E  1 28  ? 44.345  69.646 22.278  1.00 29.99  ? 28   HIS E NE2 1 
ATOM   7950  N N   . ALA E  1 29  ? 44.055  65.864 27.613  1.00 24.05  ? 29   ALA E N   1 
ATOM   7951  C CA  . ALA E  1 29  ? 43.612  65.150 28.800  1.00 22.90  ? 29   ALA E CA  1 
ATOM   7952  C C   . ALA E  1 29  ? 43.313  66.140 29.909  1.00 23.83  ? 29   ALA E C   1 
ATOM   7953  O O   . ALA E  1 29  ? 43.578  67.336 29.774  1.00 25.59  ? 29   ALA E O   1 
ATOM   7954  C CB  . ALA E  1 29  ? 44.673  64.161 29.244  1.00 22.87  ? 29   ALA E CB  1 
ATOM   7955  N N   . GLN E  1 30  ? 42.744  65.642 31.000  1.00 22.91  ? 30   GLN E N   1 
ATOM   7956  C CA  . GLN E  1 30  ? 42.476  66.475 32.164  1.00 23.77  ? 30   GLN E CA  1 
ATOM   7957  C C   . GLN E  1 30  ? 42.695  65.697 33.452  1.00 23.13  ? 30   GLN E C   1 
ATOM   7958  O O   . GLN E  1 30  ? 41.918  64.806 33.790  1.00 21.71  ? 30   GLN E O   1 
ATOM   7959  C CB  . GLN E  1 30  ? 41.052  67.034 32.120  1.00 23.60  ? 30   GLN E CB  1 
ATOM   7960  C CG  . GLN E  1 30  ? 40.785  68.064 33.207  1.00 24.89  ? 30   GLN E CG  1 
ATOM   7961  C CD  . GLN E  1 30  ? 39.490  68.825 33.005  1.00 25.48  ? 30   GLN E CD  1 
ATOM   7962  O OE1 . GLN E  1 30  ? 39.008  68.978 31.883  1.00 25.55  ? 30   GLN E OE1 1 
ATOM   7963  N NE2 . GLN E  1 30  ? 38.928  69.325 34.097  1.00 26.13  ? 30   GLN E NE2 1 
ATOM   7964  N N   . ASP E  1 31  ? 43.765  66.041 34.161  1.00 24.47  ? 31   ASP E N   1 
ATOM   7965  C CA  . ASP E  1 31  ? 44.021  65.502 35.491  1.00 24.28  ? 31   ASP E CA  1 
ATOM   7966  C C   . ASP E  1 31  ? 42.968  66.071 36.443  1.00 24.08  ? 31   ASP E C   1 
ATOM   7967  O O   . ASP E  1 31  ? 42.704  67.279 36.437  1.00 25.26  ? 31   ASP E O   1 
ATOM   7968  C CB  . ASP E  1 31  ? 45.430  65.886 35.956  1.00 26.19  ? 31   ASP E CB  1 
ATOM   7969  C CG  . ASP E  1 31  ? 45.902  65.077 37.148  1.00 26.11  ? 31   ASP E CG  1 
ATOM   7970  O OD1 . ASP E  1 31  ? 45.062  64.505 37.872  1.00 24.81  ? 31   ASP E OD1 1 
ATOM   7971  O OD2 . ASP E  1 31  ? 47.128  65.017 37.366  1.00 27.68  ? 31   ASP E OD2 1 
ATOM   7972  N N   . ILE E  1 32  ? 42.357  65.190 37.231  1.00 22.79  ? 32   ILE E N   1 
ATOM   7973  C CA  . ILE E  1 32  ? 41.315  65.579 38.190  1.00 22.63  ? 32   ILE E CA  1 
ATOM   7974  C C   . ILE E  1 32  ? 41.678  65.251 39.646  1.00 22.78  ? 32   ILE E C   1 
ATOM   7975  O O   . ILE E  1 32  ? 40.871  65.451 40.552  1.00 22.65  ? 32   ILE E O   1 
ATOM   7976  C CB  . ILE E  1 32  ? 39.959  64.931 37.833  1.00 21.25  ? 32   ILE E CB  1 
ATOM   7977  C CG1 . ILE E  1 32  ? 40.107  63.425 37.612  1.00 20.00  ? 32   ILE E CG1 1 
ATOM   7978  C CG2 . ILE E  1 32  ? 39.384  65.588 36.595  1.00 21.53  ? 32   ILE E CG2 1 
ATOM   7979  C CD1 . ILE E  1 32  ? 38.798  62.669 37.679  1.00 19.03  ? 32   ILE E CD1 1 
ATOM   7980  N N   . LEU E  1 33  ? 42.895  64.760 39.861  1.00 23.27  ? 33   LEU E N   1 
ATOM   7981  C CA  . LEU E  1 33  ? 43.369  64.377 41.184  1.00 23.63  ? 33   LEU E CA  1 
ATOM   7982  C C   . LEU E  1 33  ? 44.418  65.373 41.671  1.00 25.64  ? 33   LEU E C   1 
ATOM   7983  O O   . LEU E  1 33  ? 45.463  65.532 41.040  1.00 26.77  ? 33   LEU E O   1 
ATOM   7984  C CB  . LEU E  1 33  ? 43.988  62.981 41.123  1.00 23.12  ? 33   LEU E CB  1 
ATOM   7985  C CG  . LEU E  1 33  ? 44.441  62.368 42.444  1.00 23.48  ? 33   LEU E CG  1 
ATOM   7986  C CD1 . LEU E  1 33  ? 43.232  62.058 43.310  1.00 22.44  ? 33   LEU E CD1 1 
ATOM   7987  C CD2 . LEU E  1 33  ? 45.263  61.116 42.195  1.00 23.69  ? 33   LEU E CD2 1 
ATOM   7988  N N   . GLU E  1 34  ? 44.141  66.032 42.794  1.00 26.35  ? 34   GLU E N   1 
ATOM   7989  C CA  . GLU E  1 34  ? 45.112  66.927 43.419  1.00 28.46  ? 34   GLU E CA  1 
ATOM   7990  C C   . GLU E  1 34  ? 46.093  66.114 44.251  1.00 28.93  ? 34   GLU E C   1 
ATOM   7991  O O   . GLU E  1 34  ? 45.694  65.421 45.180  1.00 28.07  ? 34   GLU E O   1 
ATOM   7992  C CB  . GLU E  1 34  ? 44.414  67.970 44.297  1.00 29.18  ? 34   GLU E CB  1 
ATOM   7993  C CG  . GLU E  1 34  ? 45.366  68.950 44.961  1.00 31.59  ? 34   GLU E CG  1 
ATOM   7994  C CD  . GLU E  1 34  ? 46.406  69.493 44.002  1.00 33.36  ? 34   GLU E CD  1 
ATOM   7995  O OE1 . GLU E  1 34  ? 46.040  70.273 43.098  1.00 33.94  ? 34   GLU E OE1 1 
ATOM   7996  O OE2 . GLU E  1 34  ? 47.588  69.108 44.135  1.00 34.40  ? 34   GLU E OE2 1 
ATOM   7997  N N   . LYS E  1 35  ? 47.377  66.217 43.920  1.00 30.66  ? 35   LYS E N   1 
ATOM   7998  C CA  . LYS E  1 35  ? 48.412  65.365 44.516  1.00 31.50  ? 35   LYS E CA  1 
ATOM   7999  C C   . LYS E  1 35  ? 49.351  66.092 45.486  1.00 33.95  ? 35   LYS E C   1 
ATOM   8000  O O   . LYS E  1 35  ? 50.138  65.436 46.169  1.00 34.84  ? 35   LYS E O   1 
ATOM   8001  C CB  . LYS E  1 35  ? 49.236  64.688 43.406  1.00 31.88  ? 35   LYS E CB  1 
ATOM   8002  C CG  . LYS E  1 35  ? 48.634  63.396 42.869  1.00 29.84  ? 35   LYS E CG  1 
ATOM   8003  C CD  . LYS E  1 35  ? 49.405  62.858 41.669  1.00 30.40  ? 35   LYS E CD  1 
ATOM   8004  C CE  . LYS E  1 35  ? 48.694  63.110 40.344  1.00 29.13  ? 35   LYS E CE  1 
ATOM   8005  N NZ  . LYS E  1 35  ? 48.293  64.527 40.120  1.00 29.53  ? 35   LYS E NZ  1 
ATOM   8006  N N   . THR E  1 36  ? 49.259  67.423 45.565  1.00 35.31  ? 36   THR E N   1 
ATOM   8007  C CA  . THR E  1 36  ? 50.214  68.224 46.346  1.00 38.10  ? 36   THR E CA  1 
ATOM   8008  C C   . THR E  1 36  ? 49.592  69.030 47.491  1.00 38.49  ? 36   THR E C   1 
ATOM   8009  O O   . THR E  1 36  ? 48.395  69.316 47.492  1.00 37.03  ? 36   THR E O   1 
ATOM   8010  C CB  . THR E  1 36  ? 50.980  69.216 45.447  1.00 40.48  ? 36   THR E CB  1 
ATOM   8011  O OG1 . THR E  1 36  ? 50.074  70.187 44.908  1.00 40.16  ? 36   THR E OG1 1 
ATOM   8012  C CG2 . THR E  1 36  ? 51.682  68.485 44.314  1.00 40.54  ? 36   THR E CG2 1 
ATOM   8013  N N   . HIS E  1 37  ? 50.440  69.390 48.456  1.00 40.78  ? 37   HIS E N   1 
ATOM   8014  C CA  . HIS E  1 37  ? 50.077  70.263 49.576  1.00 41.77  ? 37   HIS E CA  1 
ATOM   8015  C C   . HIS E  1 37  ? 51.306  71.087 49.981  1.00 45.41  ? 37   HIS E C   1 
ATOM   8016  O O   . HIS E  1 37  ? 52.429  70.750 49.598  1.00 46.97  ? 37   HIS E O   1 
ATOM   8017  C CB  . HIS E  1 37  ? 49.573  69.434 50.762  1.00 40.11  ? 37   HIS E CB  1 
ATOM   8018  C CG  . HIS E  1 37  ? 50.545  68.397 51.234  1.00 40.60  ? 37   HIS E CG  1 
ATOM   8019  N ND1 . HIS E  1 37  ? 51.281  68.541 52.390  1.00 42.48  ? 37   HIS E ND1 1 
ATOM   8020  C CD2 . HIS E  1 37  ? 50.909  67.205 50.704  1.00 39.75  ? 37   HIS E CD2 1 
ATOM   8021  C CE1 . HIS E  1 37  ? 52.052  67.482 52.557  1.00 42.82  ? 37   HIS E CE1 1 
ATOM   8022  N NE2 . HIS E  1 37  ? 51.846  66.656 51.547  1.00 41.25  ? 37   HIS E NE2 1 
ATOM   8023  N N   . ASN E  1 38  ? 51.101  72.158 50.750  1.00 47.08  ? 38   ASN E N   1 
ATOM   8024  C CA  . ASN E  1 38  ? 52.218  73.017 51.182  1.00 50.83  ? 38   ASN E CA  1 
ATOM   8025  C C   . ASN E  1 38  ? 53.014  72.460 52.375  1.00 51.90  ? 38   ASN E C   1 
ATOM   8026  O O   . ASN E  1 38  ? 54.100  72.956 52.690  1.00 55.18  ? 38   ASN E O   1 
ATOM   8027  C CB  . ASN E  1 38  ? 51.745  74.458 51.461  1.00 52.65  ? 38   ASN E CB  1 
ATOM   8028  C CG  . ASN E  1 38  ? 50.821  74.569 52.665  1.00 51.47  ? 38   ASN E CG  1 
ATOM   8029  O OD1 . ASN E  1 38  ? 50.671  73.634 53.449  1.00 49.66  ? 38   ASN E OD1 1 
ATOM   8030  N ND2 . ASN E  1 38  ? 50.193  75.728 52.811  1.00 52.75  ? 38   ASN E ND2 1 
ATOM   8031  N N   . GLY E  1 39  ? 52.461  71.447 53.042  1.00 49.44  ? 39   GLY E N   1 
ATOM   8032  C CA  . GLY E  1 39  ? 53.162  70.737 54.120  1.00 50.23  ? 39   GLY E CA  1 
ATOM   8033  C C   . GLY E  1 39  ? 53.064  71.417 55.472  1.00 51.58  ? 39   GLY E C   1 
ATOM   8034  O O   . GLY E  1 39  ? 53.849  71.122 56.380  1.00 53.12  ? 39   GLY E O   1 
ATOM   8035  N N   . LYS E  1 40  ? 52.087  72.313 55.612  1.00 51.17  ? 40   LYS E N   1 
ATOM   8036  C CA  . LYS E  1 40  ? 51.989  73.182 56.780  1.00 52.92  ? 40   LYS E CA  1 
ATOM   8037  C C   . LYS E  1 40  ? 50.589  73.199 57.388  1.00 50.65  ? 40   LYS E C   1 
ATOM   8038  O O   . LYS E  1 40  ? 49.588  73.026 56.687  1.00 48.44  ? 40   LYS E O   1 
ATOM   8039  C CB  . LYS E  1 40  ? 52.392  74.606 56.392  1.00 56.18  ? 40   LYS E CB  1 
ATOM   8040  C CG  . LYS E  1 40  ? 53.884  74.776 56.162  1.00 59.54  ? 40   LYS E CG  1 
ATOM   8041  C CD  . LYS E  1 40  ? 54.200  75.973 55.283  1.00 62.38  ? 40   LYS E CD  1 
ATOM   8042  C CE  . LYS E  1 40  ? 55.680  76.009 54.937  1.00 65.76  ? 40   LYS E CE  1 
ATOM   8043  N NZ  . LYS E  1 40  ? 56.023  77.105 53.990  1.00 68.71  ? 40   LYS E NZ  1 
ATOM   8044  N N   . LEU E  1 41  ? 50.539  73.424 58.698  1.00 51.49  ? 41   LEU E N   1 
ATOM   8045  C CA  . LEU E  1 41  ? 49.289  73.653 59.421  1.00 50.12  ? 41   LEU E CA  1 
ATOM   8046  C C   . LEU E  1 41  ? 49.005  75.156 59.367  1.00 52.45  ? 41   LEU E C   1 
ATOM   8047  O O   . LEU E  1 41  ? 49.912  75.975 59.571  1.00 55.67  ? 41   LEU E O   1 
ATOM   8048  C CB  . LEU E  1 41  ? 49.415  73.160 60.866  1.00 50.08  ? 41   LEU E CB  1 
ATOM   8049  C CG  . LEU E  1 41  ? 49.519  71.638 61.119  1.00 47.99  ? 41   LEU E CG  1 
ATOM   8050  C CD1 . LEU E  1 41  ? 48.231  71.076 61.709  1.00 45.42  ? 41   LEU E CD1 1 
ATOM   8051  C CD2 . LEU E  1 41  ? 49.914  70.835 59.879  1.00 46.97  ? 41   LEU E CD2 1 
ATOM   8052  N N   . CYS E  1 42  ? 47.755  75.517 59.083  1.00 51.17  ? 42   CYS E N   1 
ATOM   8053  C CA  . CYS E  1 42  ? 47.449  76.865 58.614  1.00 53.42  ? 42   CYS E CA  1 
ATOM   8054  C C   . CYS E  1 42  ? 46.096  77.408 59.040  1.00 52.94  ? 42   CYS E C   1 
ATOM   8055  O O   . CYS E  1 42  ? 45.183  76.652 59.371  1.00 50.36  ? 42   CYS E O   1 
ATOM   8056  C CB  . CYS E  1 42  ? 47.515  76.875 57.088  1.00 53.15  ? 42   CYS E CB  1 
ATOM   8057  S SG  . CYS E  1 42  ? 49.193  76.728 56.443  1.00 55.19  ? 42   CYS E SG  1 
ATOM   8058  N N   . ASP E  1 43  ? 45.977  78.733 58.995  1.00 55.77  ? 43   ASP E N   1 
ATOM   8059  C CA  . ASP E  1 43  ? 44.723  79.414 59.292  1.00 56.11  ? 43   ASP E CA  1 
ATOM   8060  C C   . ASP E  1 43  ? 43.671  79.016 58.268  1.00 53.78  ? 43   ASP E C   1 
ATOM   8061  O O   . ASP E  1 43  ? 43.952  78.977 57.070  1.00 53.61  ? 43   ASP E O   1 
ATOM   8062  C CB  . ASP E  1 43  ? 44.913  80.937 59.276  1.00 60.28  ? 43   ASP E CB  1 
ATOM   8063  C CG  . ASP E  1 43  ? 45.840  81.433 60.384  1.00 62.95  ? 43   ASP E CG  1 
ATOM   8064  O OD1 . ASP E  1 43  ? 46.381  80.603 61.141  1.00 61.56  ? 43   ASP E OD1 1 
ATOM   8065  O OD2 . ASP E  1 43  ? 46.030  82.662 60.493  1.00 66.67  ? 43   ASP E OD2 1 
ATOM   8066  N N   . LEU E  1 44  ? 42.467  78.710 58.744  1.00 52.16  ? 44   LEU E N   1 
ATOM   8067  C CA  . LEU E  1 44  ? 41.362  78.328 57.870  1.00 50.26  ? 44   LEU E CA  1 
ATOM   8068  C C   . LEU E  1 44  ? 40.418  79.507 57.688  1.00 52.66  ? 44   LEU E C   1 
ATOM   8069  O O   . LEU E  1 44  ? 39.775  79.950 58.640  1.00 53.76  ? 44   LEU E O   1 
ATOM   8070  C CB  . LEU E  1 44  ? 40.594  77.138 58.451  1.00 47.23  ? 44   LEU E CB  1 
ATOM   8071  C CG  . LEU E  1 44  ? 39.589  76.467 57.504  1.00 45.03  ? 44   LEU E CG  1 
ATOM   8072  C CD1 . LEU E  1 44  ? 40.304  75.537 56.532  1.00 43.08  ? 44   LEU E CD1 1 
ATOM   8073  C CD2 . LEU E  1 44  ? 38.524  75.704 58.280  1.00 43.28  ? 44   LEU E CD2 1 
ATOM   8074  N N   . ASP E  1 45  ? 40.343  80.013 56.459  1.00 53.70  ? 45   ASP E N   1 
ATOM   8075  C CA  . ASP E  1 45  ? 39.476  81.142 56.129  1.00 56.38  ? 45   ASP E CA  1 
ATOM   8076  C C   . ASP E  1 45  ? 39.852  82.374 56.959  1.00 60.18  ? 45   ASP E C   1 
ATOM   8077  O O   . ASP E  1 45  ? 38.986  83.171 57.330  1.00 62.37  ? 45   ASP E O   1 
ATOM   8078  C CB  . ASP E  1 45  ? 38.005  80.760 56.360  1.00 55.05  ? 45   ASP E CB  1 
ATOM   8079  C CG  . ASP E  1 45  ? 37.075  81.358 55.327  1.00 56.47  ? 45   ASP E CG  1 
ATOM   8080  O OD1 . ASP E  1 45  ? 36.936  80.746 54.244  1.00 54.59  ? 45   ASP E OD1 1 
ATOM   8081  O OD2 . ASP E  1 45  ? 36.477  82.423 55.600  1.00 59.60  ? 45   ASP E OD2 1 
ATOM   8082  N N   . GLY E  1 46  ? 41.146  82.513 57.254  1.00 61.21  ? 46   GLY E N   1 
ATOM   8083  C CA  . GLY E  1 46  ? 41.653  83.587 58.116  1.00 64.87  ? 46   GLY E CA  1 
ATOM   8084  C C   . GLY E  1 46  ? 41.717  83.236 59.596  1.00 64.12  ? 46   GLY E C   1 
ATOM   8085  O O   . GLY E  1 46  ? 42.545  83.785 60.323  1.00 66.50  ? 46   GLY E O   1 
ATOM   8086  N N   . VAL E  1 47  ? 40.858  82.315 60.038  1.00 60.96  ? 47   VAL E N   1 
ATOM   8087  C CA  . VAL E  1 47  ? 40.700  81.991 61.462  1.00 60.28  ? 47   VAL E CA  1 
ATOM   8088  C C   . VAL E  1 47  ? 41.740  80.957 61.912  1.00 58.14  ? 47   VAL E C   1 
ATOM   8089  O O   . VAL E  1 47  ? 41.784  79.844 61.390  1.00 55.07  ? 47   VAL E O   1 
ATOM   8090  C CB  . VAL E  1 47  ? 39.277  81.463 61.756  1.00 58.24  ? 47   VAL E CB  1 
ATOM   8091  C CG1 . VAL E  1 47  ? 39.100  81.181 63.241  1.00 57.86  ? 47   VAL E CG1 1 
ATOM   8092  C CG2 . VAL E  1 47  ? 38.224  82.455 61.280  1.00 60.64  ? 47   VAL E CG2 1 
ATOM   8093  N N   . LYS E  1 48  ? 42.558  81.329 62.895  1.00 60.04  ? 48   LYS E N   1 
ATOM   8094  C CA  . LYS E  1 48  ? 43.698  80.509 63.322  1.00 58.94  ? 48   LYS E CA  1 
ATOM   8095  C C   . LYS E  1 48  ? 43.267  79.239 64.057  1.00 55.59  ? 48   LYS E C   1 
ATOM   8096  O O   . LYS E  1 48  ? 42.291  79.260 64.810  1.00 55.13  ? 48   LYS E O   1 
ATOM   8097  C CB  . LYS E  1 48  ? 44.629  81.324 64.234  1.00 62.33  ? 48   LYS E CB  1 
ATOM   8098  C CG  . LYS E  1 48  ? 46.003  80.699 64.446  1.00 62.27  ? 48   LYS E CG  1 
ATOM   8099  C CD  . LYS E  1 48  ? 46.747  81.302 65.625  1.00 65.21  ? 48   LYS E CD  1 
ATOM   8100  C CE  . LYS E  1 48  ? 48.197  80.838 65.636  1.00 65.99  ? 48   LYS E CE  1 
ATOM   8101  N NZ  . LYS E  1 48  ? 48.862  81.091 66.945  1.00 68.17  ? 48   LYS E NZ  1 
ATOM   8102  N N   . PRO E  1 49  ? 43.994  78.125 63.839  1.00 53.52  ? 49   PRO E N   1 
ATOM   8103  C CA  . PRO E  1 49  ? 43.735  76.929 64.639  1.00 50.90  ? 49   PRO E CA  1 
ATOM   8104  C C   . PRO E  1 49  ? 44.267  77.055 66.058  1.00 52.22  ? 49   PRO E C   1 
ATOM   8105  O O   . PRO E  1 49  ? 45.274  77.726 66.281  1.00 54.81  ? 49   PRO E O   1 
ATOM   8106  C CB  . PRO E  1 49  ? 44.520  75.838 63.906  1.00 49.10  ? 49   PRO E CB  1 
ATOM   8107  C CG  . PRO E  1 49  ? 45.616  76.569 63.212  1.00 51.53  ? 49   PRO E CG  1 
ATOM   8108  C CD  . PRO E  1 49  ? 44.986  77.860 62.778  1.00 53.51  ? 49   PRO E CD  1 
ATOM   8109  N N   . LEU E  1 50  ? 43.595  76.399 66.999  1.00 50.58  ? 50   LEU E N   1 
ATOM   8110  C CA  . LEU E  1 50  ? 44.103  76.269 68.354  1.00 51.38  ? 50   LEU E CA  1 
ATOM   8111  C C   . LEU E  1 50  ? 45.143  75.160 68.358  1.00 50.29  ? 50   LEU E C   1 
ATOM   8112  O O   . LEU E  1 50  ? 44.798  73.982 68.339  1.00 47.80  ? 50   LEU E O   1 
ATOM   8113  C CB  . LEU E  1 50  ? 42.968  75.946 69.332  1.00 50.19  ? 50   LEU E CB  1 
ATOM   8114  C CG  . LEU E  1 50  ? 43.330  75.572 70.776  1.00 50.49  ? 50   LEU E CG  1 
ATOM   8115  C CD1 . LEU E  1 50  ? 44.341  76.534 71.384  1.00 53.65  ? 50   LEU E CD1 1 
ATOM   8116  C CD2 . LEU E  1 50  ? 42.073  75.515 71.633  1.00 49.80  ? 50   LEU E CD2 1 
ATOM   8117  N N   . ILE E  1 51  ? 46.417  75.542 68.362  1.00 52.52  ? 51   ILE E N   1 
ATOM   8118  C CA  . ILE E  1 51  ? 47.508  74.572 68.396  1.00 52.19  ? 51   ILE E CA  1 
ATOM   8119  C C   . ILE E  1 51  ? 47.952  74.370 69.838  1.00 53.19  ? 51   ILE E C   1 
ATOM   8120  O O   . ILE E  1 51  ? 48.617  75.230 70.420  1.00 56.01  ? 51   ILE E O   1 
ATOM   8121  C CB  . ILE E  1 51  ? 48.695  75.017 67.514  1.00 54.32  ? 51   ILE E CB  1 
ATOM   8122  C CG1 . ILE E  1 51  ? 48.213  75.175 66.068  1.00 53.23  ? 51   ILE E CG1 1 
ATOM   8123  C CG2 . ILE E  1 51  ? 49.850  74.020 67.613  1.00 54.45  ? 51   ILE E CG2 1 
ATOM   8124  C CD1 . ILE E  1 51  ? 49.313  75.269 65.033  1.00 54.66  ? 51   ILE E CD1 1 
ATOM   8125  N N   . LEU E  1 52  ? 47.594  73.216 70.399  1.00 51.04  ? 52   LEU E N   1 
ATOM   8126  C CA  . LEU E  1 52  ? 47.918  72.891 71.790  1.00 51.76  ? 52   LEU E CA  1 
ATOM   8127  C C   . LEU E  1 52  ? 49.405  72.571 72.003  1.00 53.75  ? 52   LEU E C   1 
ATOM   8128  O O   . LEU E  1 52  ? 49.863  72.476 73.142  1.00 55.04  ? 52   LEU E O   1 
ATOM   8129  C CB  . LEU E  1 52  ? 47.062  71.716 72.274  1.00 49.08  ? 52   LEU E CB  1 
ATOM   8130  C CG  . LEU E  1 52  ? 45.542  71.889 72.184  1.00 47.31  ? 52   LEU E CG  1 
ATOM   8131  C CD1 . LEU E  1 52  ? 44.840  70.609 72.610  1.00 45.07  ? 52   LEU E CD1 1 
ATOM   8132  C CD2 . LEU E  1 52  ? 45.059  73.059 73.027  1.00 48.95  ? 52   LEU E CD2 1 
ATOM   8133  N N   . ARG E  1 53  ? 50.144  72.407 70.906  1.00 54.20  ? 53   ARG E N   1 
ATOM   8134  C CA  . ARG E  1 53  ? 51.560  72.057 70.943  1.00 56.35  ? 53   ARG E CA  1 
ATOM   8135  C C   . ARG E  1 53  ? 51.739  70.737 71.719  1.00 55.41  ? 53   ARG E C   1 
ATOM   8136  O O   . ARG E  1 53  ? 51.239  69.704 71.267  1.00 53.01  ? 53   ARG E O   1 
ATOM   8137  C CB  . ARG E  1 53  ? 52.407  73.224 71.479  1.00 60.10  ? 53   ARG E CB  1 
ATOM   8138  C CG  . ARG E  1 53  ? 53.899  73.075 71.199  1.00 62.93  ? 53   ARG E CG  1 
ATOM   8139  C CD  . ARG E  1 53  ? 54.743  74.168 71.845  1.00 66.99  ? 53   ARG E CD  1 
ATOM   8140  N NE  . ARG E  1 53  ? 55.000  75.289 70.934  1.00 69.09  ? 53   ARG E NE  1 
ATOM   8141  C CZ  . ARG E  1 53  ? 54.348  76.454 70.924  1.00 69.82  ? 53   ARG E CZ  1 
ATOM   8142  N NH1 . ARG E  1 53  ? 53.363  76.709 71.782  1.00 68.63  ? 53   ARG E NH1 1 
ATOM   8143  N NH2 . ARG E  1 53  ? 54.690  77.386 70.041  1.00 72.05  ? 53   ARG E NH2 1 
ATOM   8144  N N   . ASP E  1 54  ? 52.413  70.759 72.869  1.00 57.47  ? 54   ASP E N   1 
ATOM   8145  C CA  . ASP E  1 54  ? 52.646  69.539 73.654  1.00 57.05  ? 54   ASP E CA  1 
ATOM   8146  C C   . ASP E  1 54  ? 51.601  69.306 74.748  1.00 55.39  ? 54   ASP E C   1 
ATOM   8147  O O   . ASP E  1 54  ? 51.629  68.272 75.413  1.00 54.92  ? 54   ASP E O   1 
ATOM   8148  C CB  . ASP E  1 54  ? 54.050  69.563 74.270  1.00 60.53  ? 54   ASP E CB  1 
ATOM   8149  C CG  . ASP E  1 54  ? 55.140  69.336 73.240  1.00 62.18  ? 54   ASP E CG  1 
ATOM   8150  O OD1 . ASP E  1 54  ? 55.100  68.296 72.549  1.00 60.64  ? 54   ASP E OD1 1 
ATOM   8151  O OD2 . ASP E  1 54  ? 56.038  70.196 73.123  1.00 65.26  ? 54   ASP E OD2 1 
ATOM   8152  N N   . CYS E  1 55  ? 50.693  70.261 74.943  1.00 54.79  ? 55   CYS E N   1 
ATOM   8153  C CA  . CYS E  1 55  ? 49.571  70.073 75.869  1.00 53.17  ? 55   CYS E CA  1 
ATOM   8154  C C   . CYS E  1 55  ? 48.456  69.261 75.201  1.00 49.98  ? 55   CYS E C   1 
ATOM   8155  O O   . CYS E  1 55  ? 48.284  69.316 73.986  1.00 48.98  ? 55   CYS E O   1 
ATOM   8156  C CB  . CYS E  1 55  ? 49.024  71.420 76.363  1.00 54.21  ? 55   CYS E CB  1 
ATOM   8157  S SG  . CYS E  1 55  ? 50.032  72.199 77.646  1.00 57.85  ? 55   CYS E SG  1 
ATOM   8158  N N   . SER E  1 56  ? 47.716  68.503 76.008  1.00 48.58  ? 56   SER E N   1 
ATOM   8159  C CA  . SER E  1 56  ? 46.534  67.783 75.541  1.00 45.88  ? 56   SER E CA  1 
ATOM   8160  C C   . SER E  1 56  ? 45.287  68.627 75.802  1.00 45.19  ? 56   SER E C   1 
ATOM   8161  O O   . SER E  1 56  ? 45.373  69.739 76.330  1.00 46.74  ? 56   SER E O   1 
ATOM   8162  C CB  . SER E  1 56  ? 46.409  66.435 76.256  1.00 45.21  ? 56   SER E CB  1 
ATOM   8163  O OG  . SER E  1 56  ? 45.764  66.576 77.515  1.00 45.38  ? 56   SER E OG  1 
ATOM   8164  N N   . VAL E  1 57  ? 44.127  68.088 75.436  1.00 43.12  ? 57   VAL E N   1 
ATOM   8165  C CA  . VAL E  1 57  ? 42.851  68.768 75.658  1.00 42.63  ? 57   VAL E CA  1 
ATOM   8166  C C   . VAL E  1 57  ? 42.549  68.810 77.155  1.00 43.39  ? 57   VAL E C   1 
ATOM   8167  O O   . VAL E  1 57  ? 42.098  69.831 77.676  1.00 44.40  ? 57   VAL E O   1 
ATOM   8168  C CB  . VAL E  1 57  ? 41.697  68.067 74.909  1.00 40.57  ? 57   VAL E CB  1 
ATOM   8169  C CG1 . VAL E  1 57  ? 40.364  68.739 75.206  1.00 40.52  ? 57   VAL E CG1 1 
ATOM   8170  C CG2 . VAL E  1 57  ? 41.960  68.064 73.409  1.00 39.83  ? 57   VAL E CG2 1 
ATOM   8171  N N   . ALA E  1 58  ? 42.804  67.693 77.834  1.00 43.06  ? 58   ALA E N   1 
ATOM   8172  C CA  . ALA E  1 58  ? 42.618  67.599 79.281  1.00 43.83  ? 58   ALA E CA  1 
ATOM   8173  C C   . ALA E  1 58  ? 43.482  68.623 80.014  1.00 45.96  ? 58   ALA E C   1 
ATOM   8174  O O   . ALA E  1 58  ? 42.986  69.367 80.865  1.00 46.79  ? 58   ALA E O   1 
ATOM   8175  C CB  . ALA E  1 58  ? 42.943  66.193 79.766  1.00 43.51  ? 58   ALA E CB  1 
ATOM   8176  N N   . GLY E  1 59  ? 44.770  68.659 79.674  1.00 47.05  ? 59   GLY E N   1 
ATOM   8177  C CA  . GLY E  1 59  ? 45.704  69.599 80.286  1.00 49.43  ? 59   GLY E CA  1 
ATOM   8178  C C   . GLY E  1 59  ? 45.273  71.042 80.100  1.00 50.34  ? 59   GLY E C   1 
ATOM   8179  O O   . GLY E  1 59  ? 45.331  71.836 81.037  1.00 52.09  ? 59   GLY E O   1 
ATOM   8180  N N   . TRP E  1 60  ? 44.840  71.384 78.891  1.00 49.40  ? 60   TRP E N   1 
ATOM   8181  C CA  . TRP E  1 60  ? 44.336  72.727 78.608  1.00 50.44  ? 60   TRP E CA  1 
ATOM   8182  C C   . TRP E  1 60  ? 43.106  73.041 79.464  1.00 50.27  ? 60   TRP E C   1 
ATOM   8183  O O   . TRP E  1 60  ? 43.077  74.053 80.171  1.00 52.25  ? 60   TRP E O   1 
ATOM   8184  C CB  . TRP E  1 60  ? 44.032  72.885 77.107  1.00 49.39  ? 60   TRP E CB  1 
ATOM   8185  C CG  . TRP E  1 60  ? 43.038  73.962 76.759  1.00 49.89  ? 60   TRP E CG  1 
ATOM   8186  C CD1 . TRP E  1 60  ? 42.969  75.220 77.282  1.00 52.28  ? 60   TRP E CD1 1 
ATOM   8187  C CD2 . TRP E  1 60  ? 41.988  73.875 75.790  1.00 48.32  ? 60   TRP E CD2 1 
ATOM   8188  N NE1 . TRP E  1 60  ? 41.931  75.916 76.713  1.00 52.39  ? 60   TRP E NE1 1 
ATOM   8189  C CE2 . TRP E  1 60  ? 41.314  75.114 75.791  1.00 49.96  ? 60   TRP E CE2 1 
ATOM   8190  C CE3 . TRP E  1 60  ? 41.549  72.867 74.923  1.00 45.92  ? 60   TRP E CE3 1 
ATOM   8191  C CZ2 . TRP E  1 60  ? 40.221  75.374 74.957  1.00 49.33  ? 60   TRP E CZ2 1 
ATOM   8192  C CZ3 . TRP E  1 60  ? 40.460  73.125 74.094  1.00 45.16  ? 60   TRP E CZ3 1 
ATOM   8193  C CH2 . TRP E  1 60  ? 39.811  74.369 74.118  1.00 46.88  ? 60   TRP E CH2 1 
ATOM   8194  N N   . LEU E  1 61  ? 42.110  72.161 79.417  1.00 48.16  ? 61   LEU E N   1 
ATOM   8195  C CA  . LEU E  1 61  ? 40.832  72.405 80.091  1.00 48.05  ? 61   LEU E CA  1 
ATOM   8196  C C   . LEU E  1 61  ? 40.915  72.362 81.619  1.00 49.09  ? 61   LEU E C   1 
ATOM   8197  O O   . LEU E  1 61  ? 40.262  73.157 82.298  1.00 50.29  ? 61   LEU E O   1 
ATOM   8198  C CB  . LEU E  1 61  ? 39.769  71.421 79.595  1.00 45.82  ? 61   LEU E CB  1 
ATOM   8199  C CG  . LEU E  1 61  ? 39.325  71.595 78.140  1.00 44.88  ? 61   LEU E CG  1 
ATOM   8200  C CD1 . LEU E  1 61  ? 38.219  70.600 77.827  1.00 43.05  ? 61   LEU E CD1 1 
ATOM   8201  C CD2 . LEU E  1 61  ? 38.859  73.015 77.856  1.00 46.51  ? 61   LEU E CD2 1 
ATOM   8202  N N   . LEU E  1 62  ? 41.711  71.446 82.164  1.00 48.83  ? 62   LEU E N   1 
ATOM   8203  C CA  . LEU E  1 62  ? 41.935  71.405 83.617  1.00 49.98  ? 62   LEU E CA  1 
ATOM   8204  C C   . LEU E  1 62  ? 42.859  72.527 84.088  1.00 52.54  ? 62   LEU E C   1 
ATOM   8205  O O   . LEU E  1 62  ? 42.919  72.819 85.277  1.00 53.86  ? 62   LEU E O   1 
ATOM   8206  C CB  . LEU E  1 62  ? 42.500  70.050 84.046  1.00 49.20  ? 62   LEU E CB  1 
ATOM   8207  C CG  . LEU E  1 62  ? 41.518  68.888 83.906  1.00 47.20  ? 62   LEU E CG  1 
ATOM   8208  C CD1 . LEU E  1 62  ? 42.249  67.558 83.989  1.00 46.75  ? 62   LEU E CD1 1 
ATOM   8209  C CD2 . LEU E  1 62  ? 40.423  68.969 84.960  1.00 47.37  ? 62   LEU E CD2 1 
ATOM   8210  N N   . GLY E  1 63  ? 43.566  73.159 83.154  1.00 53.44  ? 63   GLY E N   1 
ATOM   8211  C CA  . GLY E  1 63  ? 44.462  74.260 83.481  1.00 56.27  ? 63   GLY E CA  1 
ATOM   8212  C C   . GLY E  1 63  ? 45.770  73.761 84.059  1.00 57.44  ? 63   GLY E C   1 
ATOM   8213  O O   . GLY E  1 63  ? 46.249  74.283 85.064  1.00 59.57  ? 63   GLY E O   1 
ATOM   8214  N N   . ASN E  1 64  ? 46.340  72.738 83.428  1.00 56.27  ? 64   ASN E N   1 
ATOM   8215  C CA  . ASN E  1 64  ? 47.675  72.262 83.767  1.00 57.78  ? 64   ASN E CA  1 
ATOM   8216  C C   . ASN E  1 64  ? 48.660  73.438 83.673  1.00 60.89  ? 64   ASN E C   1 
ATOM   8217  O O   . ASN E  1 64  ? 48.635  74.185 82.692  1.00 61.27  ? 64   ASN E O   1 
ATOM   8218  C CB  . ASN E  1 64  ? 48.053  71.103 82.827  1.00 56.21  ? 64   ASN E CB  1 
ATOM   8219  C CG  . ASN E  1 64  ? 49.517  70.692 82.923  1.00 58.18  ? 64   ASN E CG  1 
ATOM   8220  O OD1 . ASN E  1 64  ? 50.413  71.531 82.942  1.00 60.75  ? 64   ASN E OD1 1 
ATOM   8221  N ND2 . ASN E  1 64  ? 49.766  69.387 82.941  1.00 57.29  ? 64   ASN E ND2 1 
ATOM   8222  N N   . PRO E  1 65  ? 49.520  73.616 84.697  1.00 63.39  ? 65   PRO E N   1 
ATOM   8223  C CA  . PRO E  1 65  ? 50.412  74.786 84.761  1.00 66.84  ? 65   PRO E CA  1 
ATOM   8224  C C   . PRO E  1 65  ? 51.388  74.929 83.585  1.00 68.11  ? 65   PRO E C   1 
ATOM   8225  O O   . PRO E  1 65  ? 51.855  76.032 83.315  1.00 70.73  ? 65   PRO E O   1 
ATOM   8226  C CB  . PRO E  1 65  ? 51.179  74.579 86.074  1.00 68.91  ? 65   PRO E CB  1 
ATOM   8227  C CG  . PRO E  1 65  ? 51.066  73.125 86.371  1.00 66.78  ? 65   PRO E CG  1 
ATOM   8228  C CD  . PRO E  1 65  ? 49.729  72.709 85.842  1.00 63.36  ? 65   PRO E CD  1 
ATOM   8229  N N   . MET E  1 66  ? 51.690  73.827 82.900  1.00 66.56  ? 66   MET E N   1 
ATOM   8230  C CA  . MET E  1 66  ? 52.507  73.861 81.680  1.00 67.43  ? 66   MET E CA  1 
ATOM   8231  C C   . MET E  1 66  ? 51.716  74.385 80.477  1.00 65.88  ? 66   MET E C   1 
ATOM   8232  O O   . MET E  1 66  ? 52.298  74.741 79.449  1.00 66.94  ? 66   MET E O   1 
ATOM   8233  C CB  . MET E  1 66  ? 53.037  72.461 81.353  1.00 66.31  ? 66   MET E CB  1 
ATOM   8234  C CG  . MET E  1 66  ? 53.886  71.823 82.444  1.00 68.15  ? 66   MET E CG  1 
ATOM   8235  S SD  . MET E  1 66  ? 55.515  72.577 82.589  1.00 73.04  ? 66   MET E SD  1 
ATOM   8236  C CE  . MET E  1 66  ? 56.318  71.427 83.703  1.00 74.46  ? 66   MET E CE  1 
ATOM   8237  N N   . CYS E  1 67  ? 50.391  74.422 80.606  1.00 63.61  ? 67   CYS E N   1 
ATOM   8238  C CA  . CYS E  1 67  ? 49.504  74.904 79.549  1.00 62.20  ? 67   CYS E CA  1 
ATOM   8239  C C   . CYS E  1 67  ? 49.034  76.328 79.839  1.00 64.16  ? 67   CYS E C   1 
ATOM   8240  O O   . CYS E  1 67  ? 47.879  76.681 79.581  1.00 62.90  ? 67   CYS E O   1 
ATOM   8241  C CB  . CYS E  1 67  ? 48.315  73.957 79.429  1.00 58.69  ? 67   CYS E CB  1 
ATOM   8242  S SG  . CYS E  1 67  ? 48.831  72.230 79.295  1.00 56.95  ? 67   CYS E SG  1 
ATOM   8243  N N   . ASP E  1 68  ? 49.946  77.141 80.373  1.00 67.56  ? 68   ASP E N   1 
ATOM   8244  C CA  . ASP E  1 68  ? 49.681  78.550 80.648  1.00 70.14  ? 68   ASP E CA  1 
ATOM   8245  C C   . ASP E  1 68  ? 49.430  79.348 79.375  1.00 70.66  ? 68   ASP E C   1 
ATOM   8246  O O   . ASP E  1 68  ? 48.772  80.381 79.420  1.00 72.03  ? 68   ASP E O   1 
ATOM   8247  C CB  . ASP E  1 68  ? 50.851  79.183 81.414  1.00 74.07  ? 68   ASP E CB  1 
ATOM   8248  C CG  . ASP E  1 68  ? 50.851  78.829 82.889  1.00 74.27  ? 68   ASP E CG  1 
ATOM   8249  O OD1 . ASP E  1 68  ? 49.852  78.264 83.386  1.00 71.64  ? 68   ASP E OD1 1 
ATOM   8250  O OD2 . ASP E  1 68  ? 51.859  79.121 83.565  1.00 77.31  ? 68   ASP E OD2 1 
ATOM   8251  N N   . GLU E  1 69  ? 49.965  78.889 78.247  1.00 69.82  ? 69   GLU E N   1 
ATOM   8252  C CA  . GLU E  1 69  ? 49.683  79.531 76.965  1.00 70.03  ? 69   GLU E CA  1 
ATOM   8253  C C   . GLU E  1 69  ? 48.183  79.549 76.679  1.00 67.51  ? 69   GLU E C   1 
ATOM   8254  O O   . GLU E  1 69  ? 47.668  80.505 76.099  1.00 68.72  ? 69   GLU E O   1 
ATOM   8255  C CB  . GLU E  1 69  ? 50.414  78.816 75.826  1.00 69.01  ? 69   GLU E CB  1 
ATOM   8256  C CG  . GLU E  1 69  ? 50.163  79.430 74.454  1.00 69.23  ? 69   GLU E CG  1 
ATOM   8257  C CD  . GLU E  1 69  ? 50.922  78.738 73.340  1.00 68.42  ? 69   GLU E CD  1 
ATOM   8258  O OE1 . GLU E  1 69  ? 51.865  77.972 73.635  1.00 68.69  ? 69   GLU E OE1 1 
ATOM   8259  O OE2 . GLU E  1 69  ? 50.573  78.963 72.161  1.00 67.69  ? 69   GLU E OE2 1 
ATOM   8260  N N   . PHE E  1 70  ? 47.491  78.495 77.105  1.00 64.37  ? 70   PHE E N   1 
ATOM   8261  C CA  . PHE E  1 70  ? 46.098  78.273 76.727  1.00 61.82  ? 70   PHE E CA  1 
ATOM   8262  C C   . PHE E  1 70  ? 45.088  78.684 77.808  1.00 62.18  ? 70   PHE E C   1 
ATOM   8263  O O   . PHE E  1 70  ? 43.980  78.149 77.865  1.00 59.87  ? 70   PHE E O   1 
ATOM   8264  C CB  . PHE E  1 70  ? 45.926  76.810 76.303  1.00 58.29  ? 70   PHE E CB  1 
ATOM   8265  C CG  . PHE E  1 70  ? 46.996  76.342 75.355  1.00 58.15  ? 70   PHE E CG  1 
ATOM   8266  C CD1 . PHE E  1 70  ? 47.062  76.849 74.068  1.00 58.49  ? 70   PHE E CD1 1 
ATOM   8267  C CD2 . PHE E  1 70  ? 47.968  75.438 75.764  1.00 58.06  ? 70   PHE E CD2 1 
ATOM   8268  C CE1 . PHE E  1 70  ? 48.054  76.442 73.195  1.00 58.60  ? 70   PHE E CE1 1 
ATOM   8269  C CE2 . PHE E  1 70  ? 48.965  75.027 74.895  1.00 58.34  ? 70   PHE E CE2 1 
ATOM   8270  C CZ  . PHE E  1 70  ? 49.008  75.531 73.608  1.00 58.57  ? 70   PHE E CZ  1 
ATOM   8271  N N   . ILE E  1 71  ? 45.477  79.637 78.657  1.00 65.31  ? 71   ILE E N   1 
ATOM   8272  C CA  . ILE E  1 71  ? 44.523  80.356 79.513  1.00 66.49  ? 71   ILE E CA  1 
ATOM   8273  C C   . ILE E  1 71  ? 43.825  81.433 78.673  1.00 68.05  ? 71   ILE E C   1 
ATOM   8274  O O   . ILE E  1 71  ? 44.486  82.198 77.965  1.00 70.35  ? 71   ILE E O   1 
ATOM   8275  C CB  . ILE E  1 71  ? 45.193  80.992 80.765  1.00 69.48  ? 71   ILE E CB  1 
ATOM   8276  C CG1 . ILE E  1 71  ? 44.180  81.809 81.577  1.00 70.93  ? 71   ILE E CG1 1 
ATOM   8277  C CG2 . ILE E  1 71  ? 46.353  81.916 80.396  1.00 72.99  ? 71   ILE E CG2 1 
ATOM   8278  C CD1 . ILE E  1 71  ? 44.624  82.095 82.996  1.00 72.95  ? 71   ILE E CD1 1 
ATOM   8279  N N   . ASN E  1 72  ? 42.493  81.477 78.743  1.00 67.09  ? 72   ASN E N   1 
ATOM   8280  C CA  . ASN E  1 72  ? 41.682  82.421 77.953  1.00 68.58  ? 72   ASN E CA  1 
ATOM   8281  C C   . ASN E  1 72  ? 42.006  82.425 76.449  1.00 68.03  ? 72   ASN E C   1 
ATOM   8282  O O   . ASN E  1 72  ? 42.304  83.468 75.869  1.00 70.84  ? 72   ASN E O   1 
ATOM   8283  C CB  . ASN E  1 72  ? 41.794  83.842 78.534  1.00 72.92  ? 72   ASN E CB  1 
ATOM   8284  C CG  . ASN E  1 72  ? 40.932  84.040 79.770  1.00 73.62  ? 72   ASN E CG  1 
ATOM   8285  O OD1 . ASN E  1 72  ? 39.995  83.280 80.015  1.00 71.17  ? 72   ASN E OD1 1 
ATOM   8286  N ND2 . ASN E  1 72  ? 41.238  85.073 80.550  1.00 77.26  ? 72   ASN E ND2 1 
ATOM   8287  N N   . VAL E  1 73  ? 41.940  81.250 75.827  1.00 64.57  ? 73   VAL E N   1 
ATOM   8288  C CA  . VAL E  1 73  ? 42.238  81.122 74.394  1.00 63.77  ? 73   VAL E CA  1 
ATOM   8289  C C   . VAL E  1 73  ? 41.216  81.857 73.522  1.00 64.60  ? 73   VAL E C   1 
ATOM   8290  O O   . VAL E  1 73  ? 40.024  81.864 73.837  1.00 64.20  ? 73   VAL E O   1 
ATOM   8291  C CB  . VAL E  1 73  ? 42.303  79.645 73.926  1.00 59.92  ? 73   VAL E CB  1 
ATOM   8292  C CG1 . VAL E  1 73  ? 43.491  78.936 74.554  1.00 59.56  ? 73   VAL E CG1 1 
ATOM   8293  C CG2 . VAL E  1 73  ? 41.004  78.896 74.222  1.00 57.45  ? 73   VAL E CG2 1 
ATOM   8294  N N   . PRO E  1 74  ? 41.676  82.467 72.413  1.00 66.02  ? 74   PRO E N   1 
ATOM   8295  C CA  . PRO E  1 74  ? 40.741  83.073 71.468  1.00 66.74  ? 74   PRO E CA  1 
ATOM   8296  C C   . PRO E  1 74  ? 40.036  81.993 70.652  1.00 63.02  ? 74   PRO E C   1 
ATOM   8297  O O   . PRO E  1 74  ? 40.421  80.820 70.719  1.00 60.08  ? 74   PRO E O   1 
ATOM   8298  C CB  . PRO E  1 74  ? 41.650  83.916 70.573  1.00 69.37  ? 74   PRO E CB  1 
ATOM   8299  C CG  . PRO E  1 74  ? 42.944  83.176 70.568  1.00 68.15  ? 74   PRO E CG  1 
ATOM   8300  C CD  . PRO E  1 74  ? 43.064  82.508 71.913  1.00 66.93  ? 74   PRO E CD  1 
ATOM   8301  N N   . GLU E  1 75  ? 39.024  82.382 69.883  1.00 63.38  ? 75   GLU E N   1 
ATOM   8302  C CA  . GLU E  1 75  ? 38.265  81.413 69.094  1.00 60.19  ? 75   GLU E CA  1 
ATOM   8303  C C   . GLU E  1 75  ? 39.137  80.773 68.015  1.00 58.28  ? 75   GLU E C   1 
ATOM   8304  O O   . GLU E  1 75  ? 40.076  81.393 67.509  1.00 60.06  ? 75   GLU E O   1 
ATOM   8305  C CB  . GLU E  1 75  ? 37.007  82.041 68.483  1.00 61.51  ? 75   GLU E CB  1 
ATOM   8306  C CG  . GLU E  1 75  ? 37.198  82.759 67.159  1.00 63.10  ? 75   GLU E CG  1 
ATOM   8307  C CD  . GLU E  1 75  ? 35.872  83.123 66.526  1.00 63.97  ? 75   GLU E CD  1 
ATOM   8308  O OE1 . GLU E  1 75  ? 35.199  84.047 67.032  1.00 67.03  ? 75   GLU E OE1 1 
ATOM   8309  O OE2 . GLU E  1 75  ? 35.500  82.477 65.523  1.00 61.84  ? 75   GLU E OE2 1 
ATOM   8310  N N   . TRP E  1 76  ? 38.805  79.531 67.671  1.00 54.87  ? 76   TRP E N   1 
ATOM   8311  C CA  . TRP E  1 76  ? 39.613  78.726 66.761  1.00 52.84  ? 76   TRP E CA  1 
ATOM   8312  C C   . TRP E  1 76  ? 38.766  78.182 65.617  1.00 50.80  ? 76   TRP E C   1 
ATOM   8313  O O   . TRP E  1 76  ? 37.568  77.941 65.777  1.00 50.06  ? 76   TRP E O   1 
ATOM   8314  C CB  . TRP E  1 76  ? 40.256  77.562 67.517  1.00 50.78  ? 76   TRP E CB  1 
ATOM   8315  C CG  . TRP E  1 76  ? 39.250  76.663 68.186  1.00 48.76  ? 76   TRP E CG  1 
ATOM   8316  C CD1 . TRP E  1 76  ? 38.625  75.575 67.638  1.00 46.15  ? 76   TRP E CD1 1 
ATOM   8317  C CD2 . TRP E  1 76  ? 38.741  76.787 69.520  1.00 49.45  ? 76   TRP E CD2 1 
ATOM   8318  N NE1 . TRP E  1 76  ? 37.762  75.013 68.553  1.00 45.29  ? 76   TRP E NE1 1 
ATOM   8319  C CE2 . TRP E  1 76  ? 37.813  75.738 69.715  1.00 47.20  ? 76   TRP E CE2 1 
ATOM   8320  C CE3 . TRP E  1 76  ? 38.978  77.683 70.571  1.00 51.91  ? 76   TRP E CE3 1 
ATOM   8321  C CZ2 . TRP E  1 76  ? 37.127  75.559 70.919  1.00 47.32  ? 76   TRP E CZ2 1 
ATOM   8322  C CZ3 . TRP E  1 76  ? 38.294  77.505 71.768  1.00 51.87  ? 76   TRP E CZ3 1 
ATOM   8323  C CH2 . TRP E  1 76  ? 37.379  76.452 71.930  1.00 49.59  ? 76   TRP E CH2 1 
ATOM   8324  N N   . SER E  1 77  ? 39.401  77.996 64.464  1.00 50.08  ? 77   SER E N   1 
ATOM   8325  C CA  . SER E  1 77  ? 38.772  77.331 63.324  1.00 47.91  ? 77   SER E CA  1 
ATOM   8326  C C   . SER E  1 77  ? 38.711  75.828 63.579  1.00 44.72  ? 77   SER E C   1 
ATOM   8327  O O   . SER E  1 77  ? 37.665  75.201 63.428  1.00 43.17  ? 77   SER E O   1 
ATOM   8328  C CB  . SER E  1 77  ? 39.573  77.607 62.053  1.00 48.37  ? 77   SER E CB  1 
ATOM   8329  O OG  . SER E  1 77  ? 40.967  77.526 62.307  1.00 48.96  ? 77   SER E OG  1 
ATOM   8330  N N   . TYR E  1 78  ? 39.853  75.267 63.964  1.00 44.07  ? 78   TYR E N   1 
ATOM   8331  C CA  . TYR E  1 78  ? 39.959  73.864 64.341  1.00 41.58  ? 78   TYR E CA  1 
ATOM   8332  C C   . TYR E  1 78  ? 41.047  73.710 65.407  1.00 42.32  ? 78   TYR E C   1 
ATOM   8333  O O   . TYR E  1 78  ? 41.802  74.645 65.667  1.00 44.57  ? 78   TYR E O   1 
ATOM   8334  C CB  . TYR E  1 78  ? 40.260  73.002 63.105  1.00 39.68  ? 78   TYR E CB  1 
ATOM   8335  C CG  . TYR E  1 78  ? 41.560  73.336 62.397  1.00 40.66  ? 78   TYR E CG  1 
ATOM   8336  C CD1 . TYR E  1 78  ? 41.658  74.442 61.548  1.00 42.34  ? 78   TYR E CD1 1 
ATOM   8337  C CD2 . TYR E  1 78  ? 42.691  72.544 62.574  1.00 40.21  ? 78   TYR E CD2 1 
ATOM   8338  C CE1 . TYR E  1 78  ? 42.848  74.749 60.902  1.00 43.53  ? 78   TYR E CE1 1 
ATOM   8339  C CE2 . TYR E  1 78  ? 43.884  72.842 61.933  1.00 41.45  ? 78   TYR E CE2 1 
ATOM   8340  C CZ  . TYR E  1 78  ? 43.959  73.946 61.099  1.00 43.09  ? 78   TYR E CZ  1 
ATOM   8341  O OH  . TYR E  1 78  ? 45.150  74.238 60.470  1.00 44.58  ? 78   TYR E OH  1 
ATOM   8342  N N   . ILE E  1 79  ? 41.118  72.534 66.025  1.00 40.69  ? 79   ILE E N   1 
ATOM   8343  C CA  . ILE E  1 79  ? 42.099  72.266 67.077  1.00 41.42  ? 79   ILE E CA  1 
ATOM   8344  C C   . ILE E  1 79  ? 43.146  71.275 66.582  1.00 40.58  ? 79   ILE E C   1 
ATOM   8345  O O   . ILE E  1 79  ? 42.824  70.351 65.840  1.00 38.70  ? 79   ILE E O   1 
ATOM   8346  C CB  . ILE E  1 79  ? 41.415  71.707 68.341  1.00 40.75  ? 79   ILE E CB  1 
ATOM   8347  C CG1 . ILE E  1 79  ? 40.496  72.769 68.956  1.00 42.11  ? 79   ILE E CG1 1 
ATOM   8348  C CG2 . ILE E  1 79  ? 42.450  71.261 69.367  1.00 41.40  ? 79   ILE E CG2 1 
ATOM   8349  C CD1 . ILE E  1 79  ? 39.466  72.216 69.920  1.00 41.28  ? 79   ILE E CD1 1 
ATOM   8350  N N   . VAL E  1 80  ? 44.395  71.469 67.003  1.00 42.27  ? 80   VAL E N   1 
ATOM   8351  C CA  . VAL E  1 80  ? 45.488  70.566 66.638  1.00 42.09  ? 80   VAL E CA  1 
ATOM   8352  C C   . VAL E  1 80  ? 46.146  69.975 67.886  1.00 42.83  ? 80   VAL E C   1 
ATOM   8353  O O   . VAL E  1 80  ? 46.718  70.700 68.703  1.00 44.93  ? 80   VAL E O   1 
ATOM   8354  C CB  . VAL E  1 80  ? 46.555  71.279 65.783  1.00 43.92  ? 80   VAL E CB  1 
ATOM   8355  C CG1 . VAL E  1 80  ? 47.612  70.289 65.304  1.00 43.80  ? 80   VAL E CG1 1 
ATOM   8356  C CG2 . VAL E  1 80  ? 45.904  71.964 64.594  1.00 43.54  ? 80   VAL E CG2 1 
ATOM   8357  N N   . GLU E  1 81  ? 46.067  68.653 68.006  1.00 41.38  ? 81   GLU E N   1 
ATOM   8358  C CA  . GLU E  1 81  ? 46.607  67.917 69.143  1.00 42.05  ? 81   GLU E CA  1 
ATOM   8359  C C   . GLU E  1 81  ? 47.555  66.844 68.623  1.00 42.21  ? 81   GLU E C   1 
ATOM   8360  O O   . GLU E  1 81  ? 47.251  66.172 67.645  1.00 40.76  ? 81   GLU E O   1 
ATOM   8361  C CB  . GLU E  1 81  ? 45.461  67.261 69.924  1.00 40.50  ? 81   GLU E CB  1 
ATOM   8362  C CG  . GLU E  1 81  ? 45.876  66.531 71.197  1.00 41.23  ? 81   GLU E CG  1 
ATOM   8363  C CD  . GLU E  1 81  ? 44.737  65.760 71.852  1.00 39.82  ? 81   GLU E CD  1 
ATOM   8364  O OE1 . GLU E  1 81  ? 43.962  65.097 71.126  1.00 38.14  ? 81   GLU E OE1 1 
ATOM   8365  O OE2 . GLU E  1 81  ? 44.620  65.808 73.099  1.00 40.53  ? 81   GLU E OE2 1 
ATOM   8366  N N   . LYS E  1 82  ? 48.703  66.687 69.272  1.00 44.31  ? 82   LYS E N   1 
ATOM   8367  C CA  . LYS E  1 82  ? 49.642  65.620 68.923  1.00 44.98  ? 82   LYS E CA  1 
ATOM   8368  C C   . LYS E  1 82  ? 49.087  64.245 69.301  1.00 43.66  ? 82   LYS E C   1 
ATOM   8369  O O   . LYS E  1 82  ? 48.088  64.135 70.017  1.00 42.45  ? 82   LYS E O   1 
ATOM   8370  C CB  . LYS E  1 82  ? 50.994  65.841 69.611  1.00 47.97  ? 82   LYS E CB  1 
ATOM   8371  C CG  . LYS E  1 82  ? 51.842  66.930 68.974  1.00 49.97  ? 82   LYS E CG  1 
ATOM   8372  C CD  . LYS E  1 82  ? 53.195  67.049 69.661  1.00 53.25  ? 82   LYS E CD  1 
ATOM   8373  C CE  . LYS E  1 82  ? 54.199  67.806 68.806  1.00 55.58  ? 82   LYS E CE  1 
ATOM   8374  N NZ  . LYS E  1 82  ? 53.926  69.268 68.771  1.00 56.38  ? 82   LYS E NZ  1 
ATOM   8375  N N   . ALA E  1 83  ? 49.746  63.200 68.808  1.00 44.21  ? 83   ALA E N   1 
ATOM   8376  C CA  . ALA E  1 83  ? 49.334  61.824 69.088  1.00 43.52  ? 83   ALA E CA  1 
ATOM   8377  C C   . ALA E  1 83  ? 49.573  61.457 70.557  1.00 45.00  ? 83   ALA E C   1 
ATOM   8378  O O   . ALA E  1 83  ? 48.680  60.919 71.215  1.00 44.02  ? 83   ALA E O   1 
ATOM   8379  C CB  . ALA E  1 83  ? 50.064  60.855 68.168  1.00 44.09  ? 83   ALA E CB  1 
ATOM   8380  N N   . ASN E  1 84  ? 50.767  61.763 71.067  1.00 47.62  ? 84   ASN E N   1 
ATOM   8381  C CA  . ASN E  1 84  ? 51.121  61.472 72.462  1.00 49.34  ? 84   ASN E CA  1 
ATOM   8382  C C   . ASN E  1 84  ? 51.679  62.710 73.190  1.00 51.09  ? 84   ASN E C   1 
ATOM   8383  O O   . ASN E  1 84  ? 52.862  62.743 73.540  1.00 53.79  ? 84   ASN E O   1 
ATOM   8384  C CB  . ASN E  1 84  ? 52.145  60.324 72.526  1.00 51.53  ? 84   ASN E CB  1 
ATOM   8385  C CG  . ASN E  1 84  ? 51.743  59.123 71.677  1.00 50.40  ? 84   ASN E CG  1 
ATOM   8386  O OD1 . ASN E  1 84  ? 50.589  58.686 71.698  1.00 48.39  ? 84   ASN E OD1 1 
ATOM   8387  N ND2 . ASN E  1 84  ? 52.699  58.584 70.922  1.00 52.01  ? 84   ASN E ND2 1 
ATOM   8388  N N   . PRO E  1 85  ? 50.827  63.727 73.435  1.00 49.86  ? 85   PRO E N   1 
ATOM   8389  C CA  . PRO E  1 85  ? 51.299  64.945 74.105  1.00 51.68  ? 85   PRO E CA  1 
ATOM   8390  C C   . PRO E  1 85  ? 51.818  64.672 75.519  1.00 53.57  ? 85   PRO E C   1 
ATOM   8391  O O   . PRO E  1 85  ? 51.148  63.983 76.290  1.00 52.62  ? 85   PRO E O   1 
ATOM   8392  C CB  . PRO E  1 85  ? 50.046  65.838 74.155  1.00 49.88  ? 85   PRO E CB  1 
ATOM   8393  C CG  . PRO E  1 85  ? 49.101  65.261 73.161  1.00 47.27  ? 85   PRO E CG  1 
ATOM   8394  C CD  . PRO E  1 85  ? 49.385  63.792 73.141  1.00 47.11  ? 85   PRO E CD  1 
ATOM   8395  N N   . VAL E  1 86  ? 52.995  65.209 75.847  1.00 56.42  ? 86   VAL E N   1 
ATOM   8396  C CA  . VAL E  1 86  ? 53.629  64.950 77.149  1.00 58.60  ? 86   VAL E CA  1 
ATOM   8397  C C   . VAL E  1 86  ? 52.898  65.624 78.317  1.00 58.14  ? 86   VAL E C   1 
ATOM   8398  O O   . VAL E  1 86  ? 52.759  65.027 79.386  1.00 58.41  ? 86   VAL E O   1 
ATOM   8399  C CB  . VAL E  1 86  ? 55.132  65.350 77.179  1.00 62.29  ? 86   VAL E CB  1 
ATOM   8400  C CG1 . VAL E  1 86  ? 55.905  64.612 76.094  1.00 63.07  ? 86   VAL E CG1 1 
ATOM   8401  C CG2 . VAL E  1 86  ? 55.325  66.859 77.055  1.00 63.52  ? 86   VAL E CG2 1 
ATOM   8402  N N   . ASN E  1 87  ? 52.445  66.861 78.110  1.00 57.65  ? 87   ASN E N   1 
ATOM   8403  C CA  . ASN E  1 87  ? 51.736  67.618 79.142  1.00 57.43  ? 87   ASN E CA  1 
ATOM   8404  C C   . ASN E  1 87  ? 50.254  67.273 79.161  1.00 54.33  ? 87   ASN E C   1 
ATOM   8405  O O   . ASN E  1 87  ? 49.424  68.043 78.678  1.00 53.15  ? 87   ASN E O   1 
ATOM   8406  C CB  . ASN E  1 87  ? 51.907  69.128 78.928  1.00 58.89  ? 87   ASN E CB  1 
ATOM   8407  C CG  . ASN E  1 87  ? 53.303  69.619 79.268  1.00 62.54  ? 87   ASN E CG  1 
ATOM   8408  O OD1 . ASN E  1 87  ? 53.968  69.082 80.155  1.00 64.17  ? 87   ASN E OD1 1 
ATOM   8409  N ND2 . ASN E  1 87  ? 53.746  70.662 78.572  1.00 64.13  ? 87   ASN E ND2 1 
ATOM   8410  N N   . ASP E  1 88  ? 49.928  66.108 79.714  1.00 53.35  ? 88   ASP E N   1 
ATOM   8411  C CA  . ASP E  1 88  ? 48.540  65.675 79.849  1.00 50.82  ? 88   ASP E CA  1 
ATOM   8412  C C   . ASP E  1 88  ? 48.124  65.843 81.321  1.00 51.36  ? 88   ASP E C   1 
ATOM   8413  O O   . ASP E  1 88  ? 48.068  66.971 81.819  1.00 52.31  ? 88   ASP E O   1 
ATOM   8414  C CB  . ASP E  1 88  ? 48.385  64.236 79.325  1.00 49.53  ? 88   ASP E CB  1 
ATOM   8415  C CG  . ASP E  1 88  ? 46.928  63.793 79.214  1.00 47.13  ? 88   ASP E CG  1 
ATOM   8416  O OD1 . ASP E  1 88  ? 46.015  64.635 79.353  1.00 46.25  ? 88   ASP E OD1 1 
ATOM   8417  O OD2 . ASP E  1 88  ? 46.697  62.589 78.979  1.00 46.38  ? 88   ASP E OD2 1 
ATOM   8418  N N   . LEU E  1 89  ? 47.848  64.740 82.015  1.00 50.98  ? 89   LEU E N   1 
ATOM   8419  C CA  . LEU E  1 89  ? 47.502  64.781 83.431  1.00 51.60  ? 89   LEU E CA  1 
ATOM   8420  C C   . LEU E  1 89  ? 48.788  64.755 84.252  1.00 54.25  ? 89   LEU E C   1 
ATOM   8421  O O   . LEU E  1 89  ? 49.374  63.689 84.463  1.00 55.14  ? 89   LEU E O   1 
ATOM   8422  C CB  . LEU E  1 89  ? 46.594  63.593 83.799  1.00 50.28  ? 89   LEU E CB  1 
ATOM   8423  C CG  . LEU E  1 89  ? 45.069  63.795 83.792  1.00 48.36  ? 89   LEU E CG  1 
ATOM   8424  C CD1 . LEU E  1 89  ? 44.600  64.780 82.733  1.00 47.21  ? 89   LEU E CD1 1 
ATOM   8425  C CD2 . LEU E  1 89  ? 44.364  62.454 83.629  1.00 47.23  ? 89   LEU E CD2 1 
ATOM   8426  N N   . CYS E  1 90  ? 49.232  65.932 84.697  1.00 55.81  ? 90   CYS E N   1 
ATOM   8427  C CA  . CYS E  1 90  ? 50.451  66.039 85.501  1.00 58.65  ? 90   CYS E CA  1 
ATOM   8428  C C   . CYS E  1 90  ? 50.335  65.175 86.754  1.00 59.14  ? 90   CYS E C   1 
ATOM   8429  O O   . CYS E  1 90  ? 51.225  64.377 87.040  1.00 60.83  ? 90   CYS E O   1 
ATOM   8430  C CB  . CYS E  1 90  ? 50.773  67.499 85.854  1.00 60.37  ? 90   CYS E CB  1 
ATOM   8431  S SG  . CYS E  1 90  ? 49.409  68.484 86.520  1.00 59.20  ? 90   CYS E SG  1 
ATOM   8432  N N   . TYR E  1 91  ? 49.226  65.316 87.476  1.00 57.86  ? 91   TYR E N   1 
ATOM   8433  C CA  . TYR E  1 91  ? 48.897  64.398 88.563  1.00 58.03  ? 91   TYR E CA  1 
ATOM   8434  C C   . TYR E  1 91  ? 48.143  63.194 87.983  1.00 56.08  ? 91   TYR E C   1 
ATOM   8435  O O   . TYR E  1 91  ? 47.112  63.378 87.333  1.00 53.98  ? 91   TYR E O   1 
ATOM   8436  C CB  . TYR E  1 91  ? 48.046  65.089 89.632  1.00 57.86  ? 91   TYR E CB  1 
ATOM   8437  C CG  . TYR E  1 91  ? 48.024  64.349 90.955  1.00 58.90  ? 91   TYR E CG  1 
ATOM   8438  C CD1 . TYR E  1 91  ? 47.152  63.281 91.167  1.00 57.66  ? 91   TYR E CD1 1 
ATOM   8439  C CD2 . TYR E  1 91  ? 48.888  64.706 91.989  1.00 61.38  ? 91   TYR E CD2 1 
ATOM   8440  C CE1 . TYR E  1 91  ? 47.134  62.599 92.374  1.00 58.84  ? 91   TYR E CE1 1 
ATOM   8441  C CE2 . TYR E  1 91  ? 48.878  64.030 93.201  1.00 62.44  ? 91   TYR E CE2 1 
ATOM   8442  C CZ  . TYR E  1 91  ? 47.999  62.977 93.389  1.00 61.16  ? 91   TYR E CZ  1 
ATOM   8443  O OH  . TYR E  1 91  ? 47.990  62.307 94.594  1.00 62.49  ? 91   TYR E OH  1 
ATOM   8444  N N   . PRO E  1 92  ? 48.642  61.962 88.223  1.00 57.09  ? 92   PRO E N   1 
ATOM   8445  C CA  . PRO E  1 92  ? 48.050  60.752 87.627  1.00 55.74  ? 92   PRO E CA  1 
ATOM   8446  C C   . PRO E  1 92  ? 46.553  60.619 87.876  1.00 53.79  ? 92   PRO E C   1 
ATOM   8447  O O   . PRO E  1 92  ? 46.056  61.054 88.916  1.00 54.02  ? 92   PRO E O   1 
ATOM   8448  C CB  . PRO E  1 92  ? 48.777  59.605 88.335  1.00 57.95  ? 92   PRO E CB  1 
ATOM   8449  C CG  . PRO E  1 92  ? 50.023  60.194 88.871  1.00 60.45  ? 92   PRO E CG  1 
ATOM   8450  C CD  . PRO E  1 92  ? 49.750  61.638 89.142  1.00 59.89  ? 92   PRO E CD  1 
ATOM   8451  N N   . GLY E  1 93  ? 45.847  60.010 86.932  1.00 52.10  ? 93   GLY E N   1 
ATOM   8452  C CA  . GLY E  1 93  ? 44.413  59.818 87.073  1.00 50.54  ? 93   GLY E CA  1 
ATOM   8453  C C   . GLY E  1 93  ? 43.706  59.444 85.788  1.00 48.72  ? 93   GLY E C   1 
ATOM   8454  O O   . GLY E  1 93  ? 44.333  59.018 84.816  1.00 48.64  ? 93   GLY E O   1 
ATOM   8455  N N   . ASP E  1 94  ? 42.385  59.598 85.809  1.00 47.42  ? 94   ASP E N   1 
ATOM   8456  C CA  . ASP E  1 94  ? 41.534  59.363 84.651  1.00 45.74  ? 94   ASP E CA  1 
ATOM   8457  C C   . ASP E  1 94  ? 40.670  60.584 84.419  1.00 44.57  ? 94   ASP E C   1 
ATOM   8458  O O   . ASP E  1 94  ? 40.363  61.333 85.353  1.00 45.07  ? 94   ASP E O   1 
ATOM   8459  C CB  . ASP E  1 94  ? 40.619  58.159 84.881  1.00 45.84  ? 94   ASP E CB  1 
ATOM   8460  C CG  . ASP E  1 94  ? 41.384  56.889 85.171  1.00 47.40  ? 94   ASP E CG  1 
ATOM   8461  O OD1 . ASP E  1 94  ? 42.007  56.343 84.233  1.00 47.40  ? 94   ASP E OD1 1 
ATOM   8462  O OD2 . ASP E  1 94  ? 41.351  56.435 86.338  1.00 48.81  ? 94   ASP E OD2 1 
ATOM   8463  N N   . PHE E  1 95  ? 40.279  60.775 83.164  1.00 43.16  ? 95   PHE E N   1 
ATOM   8464  C CA  . PHE E  1 95  ? 39.311  61.792 82.803  1.00 42.22  ? 95   PHE E CA  1 
ATOM   8465  C C   . PHE E  1 95  ? 38.042  61.051 82.393  1.00 41.39  ? 95   PHE E C   1 
ATOM   8466  O O   . PHE E  1 95  ? 38.038  60.299 81.412  1.00 40.68  ? 95   PHE E O   1 
ATOM   8467  C CB  . PHE E  1 95  ? 39.852  62.655 81.663  1.00 41.61  ? 95   PHE E CB  1 
ATOM   8468  C CG  . PHE E  1 95  ? 39.286  64.047 81.628  1.00 41.59  ? 95   PHE E CG  1 
ATOM   8469  C CD1 . PHE E  1 95  ? 37.933  64.259 81.397  1.00 40.99  ? 95   PHE E CD1 1 
ATOM   8470  C CD2 . PHE E  1 95  ? 40.109  65.148 81.821  1.00 42.54  ? 95   PHE E CD2 1 
ATOM   8471  C CE1 . PHE E  1 95  ? 37.414  65.542 81.362  1.00 41.37  ? 95   PHE E CE1 1 
ATOM   8472  C CE2 . PHE E  1 95  ? 39.594  66.433 81.785  1.00 42.91  ? 95   PHE E CE2 1 
ATOM   8473  C CZ  . PHE E  1 95  ? 38.246  66.631 81.557  1.00 42.33  ? 95   PHE E CZ  1 
ATOM   8474  N N   . ASN E  1 96  ? 36.976  61.246 83.162  1.00 41.70  ? 96   ASN E N   1 
ATOM   8475  C CA  . ASN E  1 96  ? 35.721  60.543 82.928  1.00 41.41  ? 96   ASN E CA  1 
ATOM   8476  C C   . ASN E  1 96  ? 35.020  61.034 81.658  1.00 40.26  ? 96   ASN E C   1 
ATOM   8477  O O   . ASN E  1 96  ? 34.840  62.238 81.469  1.00 40.12  ? 96   ASN E O   1 
ATOM   8478  C CB  . ASN E  1 96  ? 34.798  60.705 84.139  1.00 42.45  ? 96   ASN E CB  1 
ATOM   8479  C CG  . ASN E  1 96  ? 33.658  59.703 84.142  1.00 42.86  ? 96   ASN E CG  1 
ATOM   8480  O OD1 . ASN E  1 96  ? 33.886  58.489 84.137  1.00 43.24  ? 96   ASN E OD1 1 
ATOM   8481  N ND2 . ASN E  1 96  ? 32.425  60.203 84.152  1.00 43.13  ? 96   ASN E ND2 1 
ATOM   8482  N N   . ASP E  1 97  ? 34.625  60.090 80.802  1.00 39.67  ? 97   ASP E N   1 
ATOM   8483  C CA  . ASP E  1 97  ? 34.011  60.388 79.499  1.00 38.64  ? 97   ASP E CA  1 
ATOM   8484  C C   . ASP E  1 97  ? 34.802  61.450 78.730  1.00 37.77  ? 97   ASP E C   1 
ATOM   8485  O O   . ASP E  1 97  ? 34.247  62.454 78.274  1.00 37.63  ? 97   ASP E O   1 
ATOM   8486  C CB  . ASP E  1 97  ? 32.540  60.800 79.666  1.00 39.19  ? 97   ASP E CB  1 
ATOM   8487  C CG  . ASP E  1 97  ? 31.645  59.639 80.080  1.00 40.11  ? 97   ASP E CG  1 
ATOM   8488  O OD1 . ASP E  1 97  ? 32.047  58.469 79.910  1.00 40.14  ? 97   ASP E OD1 1 
ATOM   8489  O OD2 . ASP E  1 97  ? 30.529  59.897 80.578  1.00 41.12  ? 97   ASP E OD2 1 
ATOM   8490  N N   . TYR E  1 98  ? 36.103  61.208 78.599  1.00 37.51  ? 98   TYR E N   1 
ATOM   8491  C CA  . TYR E  1 98  ? 37.021  62.130 77.928  1.00 37.06  ? 98   TYR E CA  1 
ATOM   8492  C C   . TYR E  1 98  ? 36.735  62.215 76.430  1.00 35.87  ? 98   TYR E C   1 
ATOM   8493  O O   . TYR E  1 98  ? 36.781  63.294 75.832  1.00 35.66  ? 98   TYR E O   1 
ATOM   8494  C CB  . TYR E  1 98  ? 38.454  61.646 78.160  1.00 37.55  ? 98   TYR E CB  1 
ATOM   8495  C CG  . TYR E  1 98  ? 39.564  62.564 77.686  1.00 37.72  ? 98   TYR E CG  1 
ATOM   8496  C CD1 . TYR E  1 98  ? 39.493  63.945 77.859  1.00 38.16  ? 98   TYR E CD1 1 
ATOM   8497  C CD2 . TYR E  1 98  ? 40.717  62.037 77.105  1.00 37.85  ? 98   TYR E CD2 1 
ATOM   8498  C CE1 . TYR E  1 98  ? 40.525  64.772 77.439  1.00 38.72  ? 98   TYR E CE1 1 
ATOM   8499  C CE2 . TYR E  1 98  ? 41.752  62.855 76.685  1.00 38.37  ? 98   TYR E CE2 1 
ATOM   8500  C CZ  . TYR E  1 98  ? 41.654  64.220 76.855  1.00 38.82  ? 98   TYR E CZ  1 
ATOM   8501  O OH  . TYR E  1 98  ? 42.685  65.028 76.437  1.00 39.69  ? 98   TYR E OH  1 
ATOM   8502  N N   . GLU E  1 99  ? 36.430  61.065 75.837  1.00 35.26  ? 99   GLU E N   1 
ATOM   8503  C CA  . GLU E  1 99  ? 36.195  60.969 74.407  1.00 34.18  ? 99   GLU E CA  1 
ATOM   8504  C C   . GLU E  1 99  ? 34.879  61.644 74.042  1.00 33.97  ? 99   GLU E C   1 
ATOM   8505  O O   . GLU E  1 99  ? 34.790  62.339 73.030  1.00 33.39  ? 99   GLU E O   1 
ATOM   8506  C CB  . GLU E  1 99  ? 36.186  59.506 73.956  1.00 34.00  ? 99   GLU E CB  1 
ATOM   8507  C CG  . GLU E  1 99  ? 37.549  58.822 73.991  1.00 34.37  ? 99   GLU E CG  1 
ATOM   8508  C CD  . GLU E  1 99  ? 38.031  58.495 75.393  1.00 35.63  ? 99   GLU E CD  1 
ATOM   8509  O OE1 . GLU E  1 99  ? 37.211  58.060 76.233  1.00 36.24  ? 99   GLU E OE1 1 
ATOM   8510  O OE2 . GLU E  1 99  ? 39.239  58.670 75.652  1.00 36.19  ? 99   GLU E OE2 1 
ATOM   8511  N N   . GLU E  1 100 ? 33.862  61.442 74.873  1.00 34.68  ? 100  GLU E N   1 
ATOM   8512  C CA  . GLU E  1 100 ? 32.574  62.105 74.680  1.00 35.01  ? 100  GLU E CA  1 
ATOM   8513  C C   . GLU E  1 100 ? 32.707  63.622 74.798  1.00 35.38  ? 100  GLU E C   1 
ATOM   8514  O O   . GLU E  1 100 ? 32.044  64.361 74.074  1.00 35.48  ? 100  GLU E O   1 
ATOM   8515  C CB  . GLU E  1 100 ? 31.540  61.581 75.679  1.00 36.12  ? 100  GLU E CB  1 
ATOM   8516  C CG  . GLU E  1 100 ? 31.005  60.201 75.340  1.00 36.20  ? 100  GLU E CG  1 
ATOM   8517  C CD  . GLU E  1 100 ? 30.102  60.207 74.123  1.00 35.94  ? 100  GLU E CD  1 
ATOM   8518  O OE1 . GLU E  1 100 ? 29.195  61.058 74.056  1.00 36.57  ? 100  GLU E OE1 1 
ATOM   8519  O OE2 . GLU E  1 100 ? 30.292  59.358 73.229  1.00 35.31  ? 100  GLU E OE2 1 
ATOM   8520  N N   . LEU E  1 101 ? 33.569  64.085 75.700  1.00 35.82  ? 101  LEU E N   1 
ATOM   8521  C CA  . LEU E  1 101 ? 33.817  65.519 75.836  1.00 36.52  ? 101  LEU E CA  1 
ATOM   8522  C C   . LEU E  1 101 ? 34.568  66.041 74.620  1.00 35.85  ? 101  LEU E C   1 
ATOM   8523  O O   . LEU E  1 101 ? 34.217  67.083 74.074  1.00 36.31  ? 101  LEU E O   1 
ATOM   8524  C CB  . LEU E  1 101 ? 34.607  65.838 77.111  1.00 37.39  ? 101  LEU E CB  1 
ATOM   8525  C CG  . LEU E  1 101 ? 34.856  67.326 77.394  1.00 38.56  ? 101  LEU E CG  1 
ATOM   8526  C CD1 . LEU E  1 101 ? 33.563  68.132 77.367  1.00 39.48  ? 101  LEU E CD1 1 
ATOM   8527  C CD2 . LEU E  1 101 ? 35.551  67.489 78.735  1.00 39.56  ? 101  LEU E CD2 1 
ATOM   8528  N N   . LYS E  1 102 ? 35.604  65.316 74.211  1.00 35.01  ? 102  LYS E N   1 
ATOM   8529  C CA  . LYS E  1 102 ? 36.340  65.645 72.990  1.00 34.43  ? 102  LYS E CA  1 
ATOM   8530  C C   . LYS E  1 102 ? 35.425  65.737 71.771  1.00 33.73  ? 102  LYS E C   1 
ATOM   8531  O O   . LYS E  1 102 ? 35.622  66.579 70.901  1.00 33.77  ? 102  LYS E O   1 
ATOM   8532  C CB  . LYS E  1 102 ? 37.427  64.604 72.723  1.00 33.83  ? 102  LYS E CB  1 
ATOM   8533  C CG  . LYS E  1 102 ? 38.757  64.900 73.388  1.00 34.77  ? 102  LYS E CG  1 
ATOM   8534  C CD  . LYS E  1 102 ? 39.700  63.720 73.222  1.00 34.56  ? 102  LYS E CD  1 
ATOM   8535  C CE  . LYS E  1 102 ? 41.102  64.154 72.826  1.00 35.26  ? 102  LYS E CE  1 
ATOM   8536  N NZ  . LYS E  1 102 ? 41.962  62.966 72.583  1.00 35.30  ? 102  LYS E NZ  1 
ATOM   8537  N N   . HIS E  1 103 ? 34.433  64.860 71.708  1.00 33.32  ? 103  HIS E N   1 
ATOM   8538  C CA  . HIS E  1 103 ? 33.464  64.897 70.625  1.00 32.97  ? 103  HIS E CA  1 
ATOM   8539  C C   . HIS E  1 103 ? 32.629  66.175 70.694  1.00 34.20  ? 103  HIS E C   1 
ATOM   8540  O O   . HIS E  1 103 ? 32.277  66.745 69.665  1.00 34.22  ? 103  HIS E O   1 
ATOM   8541  C CB  . HIS E  1 103 ? 32.561  63.661 70.663  1.00 32.72  ? 103  HIS E CB  1 
ATOM   8542  C CG  . HIS E  1 103 ? 31.527  63.635 69.579  1.00 32.55  ? 103  HIS E CG  1 
ATOM   8543  N ND1 . HIS E  1 103 ? 31.788  63.159 68.312  1.00 31.47  ? 103  HIS E ND1 1 
ATOM   8544  C CD2 . HIS E  1 103 ? 30.234  64.034 69.572  1.00 33.53  ? 103  HIS E CD2 1 
ATOM   8545  C CE1 . HIS E  1 103 ? 30.697  63.260 67.574  1.00 31.72  ? 103  HIS E CE1 1 
ATOM   8546  N NE2 . HIS E  1 103 ? 29.740  63.788 68.315  1.00 33.05  ? 103  HIS E NE2 1 
ATOM   8547  N N   . LEU E  1 104 ? 32.320  66.618 71.907  1.00 35.45  ? 104  LEU E N   1 
ATOM   8548  C CA  . LEU E  1 104 ? 31.559  67.851 72.119  1.00 37.08  ? 104  LEU E CA  1 
ATOM   8549  C C   . LEU E  1 104 ? 32.310  69.068 71.566  1.00 37.66  ? 104  LEU E C   1 
ATOM   8550  O O   . LEU E  1 104 ? 31.691  70.016 71.083  1.00 38.80  ? 104  LEU E O   1 
ATOM   8551  C CB  . LEU E  1 104 ? 31.269  68.045 73.614  1.00 38.34  ? 104  LEU E CB  1 
ATOM   8552  C CG  . LEU E  1 104 ? 29.811  68.235 74.031  1.00 39.79  ? 104  LEU E CG  1 
ATOM   8553  C CD1 . LEU E  1 104 ? 29.002  66.973 73.773  1.00 39.20  ? 104  LEU E CD1 1 
ATOM   8554  C CD2 . LEU E  1 104 ? 29.748  68.595 75.506  1.00 41.09  ? 104  LEU E CD2 1 
ATOM   8555  N N   . LEU E  1 105 ? 33.640  69.027 71.639  1.00 43.82  ? 105  LEU E N   1 
ATOM   8556  C CA  . LEU E  1 105 ? 34.505  70.092 71.112  1.00 44.54  ? 105  LEU E CA  1 
ATOM   8557  C C   . LEU E  1 105 ? 34.495  70.222 69.591  1.00 45.03  ? 105  LEU E C   1 
ATOM   8558  O O   . LEU E  1 105 ? 34.886  71.262 69.058  1.00 45.77  ? 105  LEU E O   1 
ATOM   8559  C CB  . LEU E  1 105 ? 35.952  69.878 71.559  1.00 44.52  ? 105  LEU E CB  1 
ATOM   8560  C CG  . LEU E  1 105 ? 36.323  70.399 72.940  1.00 44.72  ? 105  LEU E CG  1 
ATOM   8561  C CD1 . LEU E  1 105 ? 37.732  69.950 73.297  1.00 44.77  ? 105  LEU E CD1 1 
ATOM   8562  C CD2 . LEU E  1 105 ? 36.214  71.916 72.976  1.00 45.63  ? 105  LEU E CD2 1 
ATOM   8563  N N   . SER E  1 106 ? 34.081  69.166 68.895  1.00 44.81  ? 106  SER E N   1 
ATOM   8564  C CA  . SER E  1 106 ? 33.925  69.229 67.445  1.00 45.47  ? 106  SER E CA  1 
ATOM   8565  C C   . SER E  1 106 ? 32.773  70.162 67.041  1.00 46.17  ? 106  SER E C   1 
ATOM   8566  O O   . SER E  1 106 ? 32.730  70.629 65.906  1.00 47.00  ? 106  SER E O   1 
ATOM   8567  C CB  . SER E  1 106 ? 33.717  67.827 66.853  1.00 45.20  ? 106  SER E CB  1 
ATOM   8568  O OG  . SER E  1 106 ? 32.454  67.286 67.199  1.00 44.89  ? 106  SER E OG  1 
ATOM   8569  N N   . ARG E  1 107 ? 31.848  70.421 67.967  1.00 46.06  ? 107  ARG E N   1 
ATOM   8570  C CA  . ARG E  1 107 ? 30.752  71.382 67.752  1.00 46.86  ? 107  ARG E CA  1 
ATOM   8571  C C   . ARG E  1 107 ? 31.023  72.764 68.373  1.00 47.40  ? 107  ARG E C   1 
ATOM   8572  O O   . ARG E  1 107 ? 30.124  73.607 68.412  1.00 48.06  ? 107  ARG E O   1 
ATOM   8573  C CB  . ARG E  1 107 ? 29.432  70.831 68.324  1.00 46.63  ? 107  ARG E CB  1 
ATOM   8574  C CG  . ARG E  1 107 ? 28.678  69.865 67.417  1.00 46.78  ? 107  ARG E CG  1 
ATOM   8575  C CD  . ARG E  1 107 ? 27.201  69.799 67.808  1.00 47.05  ? 107  ARG E CD  1 
ATOM   8576  N NE  . ARG E  1 107 ? 26.565  68.521 67.449  1.00 46.93  ? 107  ARG E NE  1 
ATOM   8577  C CZ  . ARG E  1 107 ? 25.587  68.350 66.549  1.00 47.71  ? 107  ARG E CZ  1 
ATOM   8578  N NH1 . ARG E  1 107 ? 25.073  69.374 65.862  1.00 48.72  ? 107  ARG E NH1 1 
ATOM   8579  N NH2 . ARG E  1 107 ? 25.109  67.126 66.335  1.00 47.61  ? 107  ARG E NH2 1 
ATOM   8580  N N   . ILE E  1 108 ? 32.247  72.997 68.849  1.00 47.26  ? 108  ILE E N   1 
ATOM   8581  C CA  . ILE E  1 108 ? 32.572  74.220 69.589  1.00 47.89  ? 108  ILE E CA  1 
ATOM   8582  C C   . ILE E  1 108 ? 33.731  74.986 68.948  1.00 48.65  ? 108  ILE E C   1 
ATOM   8583  O O   . ILE E  1 108 ? 34.792  74.419 68.673  1.00 48.32  ? 108  ILE E O   1 
ATOM   8584  C CB  . ILE E  1 108 ? 32.914  73.913 71.068  1.00 47.31  ? 108  ILE E CB  1 
ATOM   8585  C CG1 . ILE E  1 108 ? 31.700  73.302 71.776  1.00 46.78  ? 108  ILE E CG1 1 
ATOM   8586  C CG2 . ILE E  1 108 ? 33.348  75.179 71.798  1.00 48.19  ? 108  ILE E CG2 1 
ATOM   8587  C CD1 . ILE E  1 108 ? 32.018  72.648 73.106  1.00 46.16  ? 108  ILE E CD1 1 
ATOM   8588  N N   . ASN E  1 109 ? 33.515  76.283 68.735  1.00 49.82  ? 109  ASN E N   1 
ATOM   8589  C CA  . ASN E  1 109 ? 34.530  77.178 68.175  1.00 50.85  ? 109  ASN E CA  1 
ATOM   8590  C C   . ASN E  1 109 ? 35.162  78.129 69.195  1.00 51.52  ? 109  ASN E C   1 
ATOM   8591  O O   . ASN E  1 109 ? 36.278  78.605 68.973  1.00 52.16  ? 109  ASN E O   1 
ATOM   8592  C CB  . ASN E  1 109 ? 33.944  77.997 67.016  1.00 52.04  ? 109  ASN E CB  1 
ATOM   8593  C CG  . ASN E  1 109 ? 34.198  77.359 65.666  1.00 52.03  ? 109  ASN E CG  1 
ATOM   8594  O OD1 . ASN E  1 109 ? 34.866  77.940 64.811  1.00 53.06  ? 109  ASN E OD1 1 
ATOM   8595  N ND2 . ASN E  1 109 ? 33.679  76.155 65.471  1.00 51.05  ? 109  ASN E ND2 1 
ATOM   8596  N N   . HIS E  1 110 ? 34.458  78.423 70.291  1.00 51.54  ? 110  HIS E N   1 
ATOM   8597  C CA  . HIS E  1 110 ? 35.012  79.309 71.317  1.00 52.39  ? 110  HIS E CA  1 
ATOM   8598  C C   . HIS E  1 110 ? 34.475  79.093 72.728  1.00 52.02  ? 110  HIS E C   1 
ATOM   8599  O O   . HIS E  1 110 ? 33.264  79.016 72.951  1.00 51.84  ? 110  HIS E O   1 
ATOM   8600  C CB  . HIS E  1 110 ? 34.804  80.777 70.931  1.00 54.09  ? 110  HIS E CB  1 
ATOM   8601  C CG  . HIS E  1 110 ? 35.675  81.729 71.695  1.00 55.26  ? 110  HIS E CG  1 
ATOM   8602  N ND1 . HIS E  1 110 ? 35.277  83.008 72.020  1.00 56.84  ? 110  HIS E ND1 1 
ATOM   8603  C CD2 . HIS E  1 110 ? 36.919  81.580 72.210  1.00 55.26  ? 110  HIS E CD2 1 
ATOM   8604  C CE1 . HIS E  1 110 ? 36.242  83.609 72.692  1.00 57.77  ? 110  HIS E CE1 1 
ATOM   8605  N NE2 . HIS E  1 110 ? 37.250  82.765 72.821  1.00 56.83  ? 110  HIS E NE2 1 
ATOM   8606  N N   . PHE E  1 111 ? 35.411  79.010 73.670  1.00 52.08  ? 111  PHE E N   1 
ATOM   8607  C CA  . PHE E  1 111 ? 35.113  79.019 75.095  1.00 52.21  ? 111  PHE E CA  1 
ATOM   8608  C C   . PHE E  1 111 ? 35.473  80.390 75.658  1.00 53.95  ? 111  PHE E C   1 
ATOM   8609  O O   . PHE E  1 111 ? 36.445  81.003 75.213  1.00 54.78  ? 111  PHE E O   1 
ATOM   8610  C CB  . PHE E  1 111 ? 35.947  77.968 75.839  1.00 51.31  ? 111  PHE E CB  1 
ATOM   8611  C CG  . PHE E  1 111 ? 35.375  76.574 75.805  1.00 49.81  ? 111  PHE E CG  1 
ATOM   8612  C CD1 . PHE E  1 111 ? 34.030  76.338 76.073  1.00 49.48  ? 111  PHE E CD1 1 
ATOM   8613  C CD2 . PHE E  1 111 ? 36.201  75.487 75.553  1.00 48.89  ? 111  PHE E CD2 1 
ATOM   8614  C CE1 . PHE E  1 111 ? 33.520  75.051 76.058  1.00 48.27  ? 111  PHE E CE1 1 
ATOM   8615  C CE2 . PHE E  1 111 ? 35.694  74.201 75.539  1.00 47.71  ? 111  PHE E CE2 1 
ATOM   8616  C CZ  . PHE E  1 111 ? 34.353  73.982 75.793  1.00 47.41  ? 111  PHE E CZ  1 
ATOM   8617  N N   . GLU E  1 112 ? 34.691  80.860 76.630  1.00 54.67  ? 112  GLU E N   1 
ATOM   8618  C CA  . GLU E  1 112 ? 35.079  82.005 77.461  1.00 56.41  ? 112  GLU E CA  1 
ATOM   8619  C C   . GLU E  1 112 ? 35.114  81.554 78.916  1.00 56.32  ? 112  GLU E C   1 
ATOM   8620  O O   . GLU E  1 112 ? 34.129  81.037 79.435  1.00 55.71  ? 112  GLU E O   1 
ATOM   8621  C CB  . GLU E  1 112 ? 34.110  83.180 77.303  1.00 57.86  ? 112  GLU E CB  1 
ATOM   8622  C CG  . GLU E  1 112 ? 34.702  84.509 77.765  1.00 59.98  ? 112  GLU E CG  1 
ATOM   8623  C CD  . GLU E  1 112 ? 33.686  85.421 78.436  1.00 61.52  ? 112  GLU E CD  1 
ATOM   8624  O OE1 . GLU E  1 112 ? 32.562  85.557 77.905  1.00 61.54  ? 112  GLU E OE1 1 
ATOM   8625  O OE2 . GLU E  1 112 ? 34.013  86.010 79.493  1.00 62.90  ? 112  GLU E OE2 1 
ATOM   8626  N N   . LYS E  1 113 ? 36.249  81.753 79.572  1.00 57.05  ? 113  LYS E N   1 
ATOM   8627  C CA  . LYS E  1 113 ? 36.425  81.292 80.945  1.00 57.18  ? 113  LYS E CA  1 
ATOM   8628  C C   . LYS E  1 113 ? 35.780  82.261 81.938  1.00 58.87  ? 113  LYS E C   1 
ATOM   8629  O O   . LYS E  1 113 ? 35.855  83.477 81.758  1.00 60.46  ? 113  LYS E O   1 
ATOM   8630  C CB  . LYS E  1 113 ? 37.915  81.146 81.239  1.00 57.55  ? 113  LYS E CB  1 
ATOM   8631  C CG  . LYS E  1 113 ? 38.241  80.375 82.506  1.00 57.44  ? 113  LYS E CG  1 
ATOM   8632  C CD  . LYS E  1 113 ? 39.395  79.406 82.285  1.00 56.55  ? 113  LYS E CD  1 
ATOM   8633  C CE  . LYS E  1 113 ? 40.694  80.087 81.873  1.00 57.63  ? 113  LYS E CE  1 
ATOM   8634  N NZ  . LYS E  1 113 ? 41.727  79.064 81.549  1.00 56.71  ? 113  LYS E NZ  1 
ATOM   8635  N N   . ILE E  1 114 ? 35.128  81.719 82.967  1.00 58.66  ? 114  ILE E N   1 
ATOM   8636  C CA  . ILE E  1 114 ? 34.581  82.535 84.057  1.00 60.44  ? 114  ILE E CA  1 
ATOM   8637  C C   . ILE E  1 114 ? 34.752  81.855 85.413  1.00 60.58  ? 114  ILE E C   1 
ATOM   8638  O O   . ILE E  1 114 ? 34.812  80.629 85.500  1.00 59.08  ? 114  ILE E O   1 
ATOM   8639  C CB  . ILE E  1 114 ? 33.083  82.864 83.867  1.00 60.58  ? 114  ILE E CB  1 
ATOM   8640  C CG1 . ILE E  1 114 ? 32.257  81.586 83.667  1.00 58.65  ? 114  ILE E CG1 1 
ATOM   8641  C CG2 . ILE E  1 114 ? 32.889  83.833 82.705  1.00 61.17  ? 114  ILE E CG2 1 
ATOM   8642  C CD1 . ILE E  1 114 ? 30.803  81.741 84.062  1.00 59.11  ? 114  ILE E CD1 1 
ATOM   8643  N N   . GLN E  1 115 ? 34.820  82.668 86.463  1.00 62.60  ? 115  GLN E N   1 
ATOM   8644  C CA  . GLN E  1 115 ? 34.946  82.174 87.830  1.00 63.19  ? 115  GLN E CA  1 
ATOM   8645  C C   . GLN E  1 115 ? 33.560  82.003 88.445  1.00 63.33  ? 115  GLN E C   1 
ATOM   8646  O O   . GLN E  1 115 ? 32.766  82.944 88.462  1.00 64.57  ? 115  GLN E O   1 
ATOM   8647  C CB  . GLN E  1 115 ? 35.803  83.136 88.665  1.00 65.55  ? 115  GLN E CB  1 
ATOM   8648  C CG  . GLN E  1 115 ? 35.515  83.131 90.160  1.00 67.06  ? 115  GLN E CG  1 
ATOM   8649  C CD  . GLN E  1 115 ? 36.566  83.883 90.958  1.00 69.35  ? 115  GLN E CD  1 
ATOM   8650  O OE1 . GLN E  1 115 ? 37.763  83.624 90.827  1.00 69.18  ? 115  GLN E OE1 1 
ATOM   8651  N NE2 . GLN E  1 115 ? 36.124  84.810 91.799  1.00 71.67  ? 115  GLN E NE2 1 
ATOM   8652  N N   . ILE E  1 116 ? 33.275  80.802 88.944  1.00 62.21  ? 116  ILE E N   1 
ATOM   8653  C CA  . ILE E  1 116 ? 31.997  80.524 89.614  1.00 62.44  ? 116  ILE E CA  1 
ATOM   8654  C C   . ILE E  1 116 ? 32.174  80.391 91.134  1.00 63.96  ? 116  ILE E C   1 
ATOM   8655  O O   . ILE E  1 116 ? 31.347  80.892 91.902  1.00 65.44  ? 116  ILE E O   1 
ATOM   8656  C CB  . ILE E  1 116 ? 31.270  79.288 89.022  1.00 60.25  ? 116  ILE E CB  1 
ATOM   8657  C CG1 . ILE E  1 116 ? 32.233  78.116 88.799  1.00 58.70  ? 116  ILE E CG1 1 
ATOM   8658  C CG2 . ILE E  1 116 ? 30.596  79.653 87.704  1.00 59.46  ? 116  ILE E CG2 1 
ATOM   8659  C CD1 . ILE E  1 116 ? 31.535  76.788 88.595  1.00 56.99  ? 116  ILE E CD1 1 
ATOM   8660  N N   . ILE E  1 117 ? 33.247  79.724 91.560  1.00 63.75  ? 117  ILE E N   1 
ATOM   8661  C CA  . ILE E  1 117 ? 33.623  79.648 92.974  1.00 65.45  ? 117  ILE E CA  1 
ATOM   8662  C C   . ILE E  1 117 ? 34.967  80.361 93.146  1.00 66.89  ? 117  ILE E C   1 
ATOM   8663  O O   . ILE E  1 117 ? 35.979  79.897 92.615  1.00 65.91  ? 117  ILE E O   1 
ATOM   8664  C CB  . ILE E  1 117 ? 33.744  78.181 93.456  1.00 64.27  ? 117  ILE E CB  1 
ATOM   8665  C CG1 . ILE E  1 117 ? 32.360  77.577 93.736  1.00 63.70  ? 117  ILE E CG1 1 
ATOM   8666  C CG2 . ILE E  1 117 ? 34.604  78.073 94.716  1.00 65.96  ? 117  ILE E CG2 1 
ATOM   8667  C CD1 . ILE E  1 117 ? 31.524  77.315 92.504  1.00 61.80  ? 117  ILE E CD1 1 
ATOM   8668  N N   . PRO E  1 118 ? 34.986  81.494 93.875  1.00 69.40  ? 118  PRO E N   1 
ATOM   8669  C CA  . PRO E  1 118 ? 36.274  82.129 94.176  1.00 71.07  ? 118  PRO E CA  1 
ATOM   8670  C C   . PRO E  1 118 ? 37.141  81.276 95.109  1.00 71.48  ? 118  PRO E C   1 
ATOM   8671  O O   . PRO E  1 118 ? 36.621  80.605 96.005  1.00 71.67  ? 118  PRO E O   1 
ATOM   8672  C CB  . PRO E  1 118 ? 35.877  83.453 94.849  1.00 73.83  ? 118  PRO E CB  1 
ATOM   8673  C CG  . PRO E  1 118 ? 34.442  83.672 94.501  1.00 73.31  ? 118  PRO E CG  1 
ATOM   8674  C CD  . PRO E  1 118 ? 33.845  82.311 94.327  1.00 70.92  ? 118  PRO E CD  1 
ATOM   8675  N N   . LYS E  1 119 ? 38.451  81.299 94.885  1.00 71.74  ? 119  LYS E N   1 
ATOM   8676  C CA  . LYS E  1 119 ? 39.394  80.534 95.704  1.00 72.32  ? 119  LYS E CA  1 
ATOM   8677  C C   . LYS E  1 119 ? 39.455  81.086 97.133  1.00 75.30  ? 119  LYS E C   1 
ATOM   8678  O O   . LYS E  1 119 ? 39.606  80.331 98.099  1.00 75.90  ? 119  LYS E O   1 
ATOM   8679  C CB  . LYS E  1 119 ? 40.784  80.560 95.065  1.00 72.12  ? 119  LYS E CB  1 
ATOM   8680  C CG  . LYS E  1 119 ? 41.751  79.528 95.616  1.00 72.11  ? 119  LYS E CG  1 
ATOM   8681  C CD  . LYS E  1 119 ? 43.036  79.514 94.804  1.00 71.70  ? 119  LYS E CD  1 
ATOM   8682  C CE  . LYS E  1 119 ? 44.153  78.781 95.528  1.00 72.57  ? 119  LYS E CE  1 
ATOM   8683  N NZ  . LYS E  1 119 ? 45.465  78.984 94.853  1.00 72.79  ? 119  LYS E NZ  1 
ATOM   8684  N N   . SER E  1 120 ? 39.338  82.407 97.251  1.00 77.33  ? 120  SER E N   1 
ATOM   8685  C CA  . SER E  1 120 ? 39.261  83.079 98.547  1.00 80.40  ? 120  SER E CA  1 
ATOM   8686  C C   . SER E  1 120 ? 38.024  82.650 99.332  1.00 80.52  ? 120  SER E C   1 
ATOM   8687  O O   . SER E  1 120 ? 38.079  82.515 100.551 1.00 82.46  ? 120  SER E O   1 
ATOM   8688  C CB  . SER E  1 120 ? 39.218  84.594 98.347  1.00 82.43  ? 120  SER E CB  1 
ATOM   8689  O OG  . SER E  1 120 ? 38.081  84.969 97.585  1.00 81.28  ? 120  SER E OG  1 
ATOM   8690  N N   . SER E  1 121 ? 36.918  82.432 98.620  1.00 78.60  ? 121  SER E N   1 
ATOM   8691  C CA  . SER E  1 121 ? 35.615  82.146 99.244  1.00 78.79  ? 121  SER E CA  1 
ATOM   8692  C C   . SER E  1 121 ? 35.584  80.934 100.187 1.00 78.63  ? 121  SER E C   1 
ATOM   8693  O O   . SER E  1 121 ? 34.638  80.788 100.964 1.00 79.49  ? 121  SER E O   1 
ATOM   8694  C CB  . SER E  1 121 ? 34.516  81.987 98.177  1.00 76.53  ? 121  SER E CB  1 
ATOM   8695  O OG  . SER E  1 121 ? 34.175  83.233 97.597  1.00 77.42  ? 121  SER E OG  1 
ATOM   8696  N N   . TRP E  1 122 ? 36.594  80.069 100.116 1.00 77.64  ? 122  TRP E N   1 
ATOM   8697  C CA  . TRP E  1 122 ? 36.699  78.937 101.035 1.00 77.78  ? 122  TRP E CA  1 
ATOM   8698  C C   . TRP E  1 122 ? 37.260  79.398 102.376 1.00 81.05  ? 122  TRP E C   1 
ATOM   8699  O O   . TRP E  1 122 ? 38.428  79.164 102.687 1.00 81.84  ? 122  TRP E O   1 
ATOM   8700  C CB  . TRP E  1 122 ? 37.572  77.840 100.429 1.00 75.70  ? 122  TRP E CB  1 
ATOM   8701  C CG  . TRP E  1 122 ? 36.990  77.288 99.172  1.00 72.71  ? 122  TRP E CG  1 
ATOM   8702  C CD1 . TRP E  1 122 ? 37.379  77.569 97.896  1.00 71.14  ? 122  TRP E CD1 1 
ATOM   8703  C CD2 . TRP E  1 122 ? 35.890  76.378 99.068  1.00 71.13  ? 122  TRP E CD2 1 
ATOM   8704  N NE1 . TRP E  1 122 ? 36.598  76.879 97.002  1.00 68.71  ? 122  TRP E NE1 1 
ATOM   8705  C CE2 . TRP E  1 122 ? 35.675  76.140 97.694  1.00 68.64  ? 122  TRP E CE2 1 
ATOM   8706  C CE3 . TRP E  1 122 ? 35.070  75.733 100.004 1.00 71.71  ? 122  TRP E CE3 1 
ATOM   8707  C CZ2 . TRP E  1 122 ? 34.670  75.283 97.229  1.00 66.75  ? 122  TRP E CZ2 1 
ATOM   8708  C CZ3 . TRP E  1 122 ? 34.071  74.883 99.543  1.00 69.80  ? 122  TRP E CZ3 1 
ATOM   8709  C CH2 . TRP E  1 122 ? 33.881  74.666 98.165  1.00 67.36  ? 122  TRP E CH2 1 
ATOM   8710  N N   . SER E  1 123 ? 36.412  80.059 103.161 1.00 83.09  ? 123  SER E N   1 
ATOM   8711  C CA  . SER E  1 123 ? 36.815  80.649 104.440 1.00 86.57  ? 123  SER E CA  1 
ATOM   8712  C C   . SER E  1 123 ? 36.899  79.611 105.559 1.00 87.43  ? 123  SER E C   1 
ATOM   8713  O O   . SER E  1 123 ? 37.644  79.797 106.522 1.00 90.04  ? 123  SER E O   1 
ATOM   8714  C CB  . SER E  1 123 ? 35.842  81.763 104.842 1.00 88.62  ? 123  SER E CB  1 
ATOM   8715  O OG  . SER E  1 123 ? 34.520  81.269 104.966 1.00 87.70  ? 123  SER E OG  1 
ATOM   8716  N N   . SER E  1 124 ? 36.128  78.532 105.427 1.00 85.42  ? 124  SER E N   1 
ATOM   8717  C CA  . SER E  1 124 ? 36.087  77.452 106.416 1.00 86.07  ? 124  SER E CA  1 
ATOM   8718  C C   . SER E  1 124 ? 37.024  76.279 106.071 1.00 84.33  ? 124  SER E C   1 
ATOM   8719  O O   . SER E  1 124 ? 37.108  75.309 106.826 1.00 84.81  ? 124  SER E O   1 
ATOM   8720  C CB  . SER E  1 124 ? 34.646  76.949 106.559 1.00 85.25  ? 124  SER E CB  1 
ATOM   8721  O OG  . SER E  1 124 ? 34.551  75.897 107.502 1.00 85.99  ? 124  SER E OG  1 
ATOM   8722  N N   . HIS E  1 125 ? 37.720  76.371 104.938 1.00 82.47  ? 125  HIS E N   1 
ATOM   8723  C CA  . HIS E  1 125 ? 38.643  75.322 104.488 1.00 80.84  ? 125  HIS E CA  1 
ATOM   8724  C C   . HIS E  1 125 ? 39.955  75.926 103.999 1.00 81.31  ? 125  HIS E C   1 
ATOM   8725  O O   . HIS E  1 125 ? 39.998  77.091 103.598 1.00 81.93  ? 125  HIS E O   1 
ATOM   8726  C CB  . HIS E  1 125 ? 38.015  74.505 103.355 1.00 77.42  ? 125  HIS E CB  1 
ATOM   8727  C CG  . HIS E  1 125 ? 36.826  73.699 103.774 1.00 76.83  ? 125  HIS E CG  1 
ATOM   8728  N ND1 . HIS E  1 125 ? 35.534  74.169 103.673 1.00 76.63  ? 125  HIS E ND1 1 
ATOM   8729  C CD2 . HIS E  1 125 ? 36.733  72.451 104.289 1.00 76.56  ? 125  HIS E CD2 1 
ATOM   8730  C CE1 . HIS E  1 125 ? 34.697  73.246 104.114 1.00 76.27  ? 125  HIS E CE1 1 
ATOM   8731  N NE2 . HIS E  1 125 ? 35.399  72.193 104.490 1.00 76.22  ? 125  HIS E NE2 1 
ATOM   8732  N N   . GLU E  1 126 ? 41.024  75.134 104.039 1.00 81.20  ? 126  GLU E N   1 
ATOM   8733  C CA  . GLU E  1 126 ? 42.315  75.563 103.507 1.00 81.51  ? 126  GLU E CA  1 
ATOM   8734  C C   . GLU E  1 126 ? 42.359  75.259 102.013 1.00 78.45  ? 126  GLU E C   1 
ATOM   8735  O O   . GLU E  1 126 ? 42.084  74.131 101.603 1.00 76.46  ? 126  GLU E O   1 
ATOM   8736  C CB  . GLU E  1 126 ? 43.457  74.853 104.234 1.00 82.95  ? 126  GLU E CB  1 
ATOM   8737  C CG  . GLU E  1 126 ? 44.850  75.278 103.787 1.00 83.58  ? 126  GLU E CG  1 
ATOM   8738  C CD  . GLU E  1 126 ? 45.112  76.761 103.998 1.00 85.90  ? 126  GLU E CD  1 
ATOM   8739  O OE1 . GLU E  1 126 ? 45.137  77.208 105.170 1.00 88.82  ? 126  GLU E OE1 1 
ATOM   8740  O OE2 . GLU E  1 126 ? 45.303  77.475 102.988 1.00 84.94  ? 126  GLU E OE2 1 
ATOM   8741  N N   . ALA E  1 127 ? 42.703  76.265 101.208 1.00 78.35  ? 127  ALA E N   1 
ATOM   8742  C CA  . ALA E  1 127 ? 42.620  76.159 99.742  1.00 75.60  ? 127  ALA E CA  1 
ATOM   8743  C C   . ALA E  1 127 ? 43.942  76.384 98.996  1.00 75.52  ? 127  ALA E C   1 
ATOM   8744  O O   . ALA E  1 127 ? 44.032  76.070 97.805  1.00 73.30  ? 127  ALA E O   1 
ATOM   8745  C CB  . ALA E  1 127 ? 41.565  77.128 99.219  1.00 75.16  ? 127  ALA E CB  1 
ATOM   8746  N N   . SER E  1 128 ? 44.956  76.919 99.678  1.00 78.01  ? 128  SER E N   1 
ATOM   8747  C CA  . SER E  1 128 ? 46.197  77.348 99.018  1.00 78.35  ? 128  SER E CA  1 
ATOM   8748  C C   . SER E  1 128 ? 47.374  76.381 99.201  1.00 78.52  ? 128  SER E C   1 
ATOM   8749  O O   . SER E  1 128 ? 48.475  76.648 98.714  1.00 78.96  ? 128  SER E O   1 
ATOM   8750  C CB  . SER E  1 128 ? 46.586  78.752 99.495  1.00 81.22  ? 128  SER E CB  1 
ATOM   8751  O OG  . SER E  1 128 ? 45.795  79.734 98.845  1.00 80.73  ? 128  SER E OG  1 
ATOM   8752  N N   . LEU E  1 129 ? 47.144  75.265 99.888  1.00 78.28  ? 129  LEU E N   1 
ATOM   8753  C CA  . LEU E  1 129 ? 48.168  74.234 100.048 1.00 78.41  ? 129  LEU E CA  1 
ATOM   8754  C C   . LEU E  1 129 ? 47.759  72.938 99.340  1.00 75.60  ? 129  LEU E C   1 
ATOM   8755  O O   . LEU E  1 129 ? 48.214  71.853 99.700  1.00 75.74  ? 129  LEU E O   1 
ATOM   8756  C CB  . LEU E  1 129 ? 48.448  73.978 101.535 1.00 81.07  ? 129  LEU E CB  1 
ATOM   8757  C CG  . LEU E  1 129 ? 49.156  75.106 102.296 1.00 84.32  ? 129  LEU E CG  1 
ATOM   8758  C CD1 . LEU E  1 129 ? 48.170  76.145 102.802 1.00 85.51  ? 129  LEU E CD1 1 
ATOM   8759  C CD2 . LEU E  1 129 ? 49.945  74.538 103.464 1.00 86.77  ? 129  LEU E CD2 1 
ATOM   8760  N N   . GLY E  1 130 ? 46.910  73.061 98.323  1.00 73.30  ? 130  GLY E N   1 
ATOM   8761  C CA  . GLY E  1 130 ? 46.477  71.916 97.527  1.00 70.67  ? 130  GLY E CA  1 
ATOM   8762  C C   . GLY E  1 130 ? 47.326  71.728 96.282  1.00 69.33  ? 130  GLY E C   1 
ATOM   8763  O O   . GLY E  1 130 ? 46.830  71.854 95.154  1.00 67.36  ? 130  GLY E O   1 
ATOM   8764  N N   . VAL E  1 131 ? 48.605  71.414 96.491  1.00 70.51  ? 131  VAL E N   1 
ATOM   8765  C CA  . VAL E  1 131 ? 49.573  71.274 95.398  1.00 69.69  ? 131  VAL E CA  1 
ATOM   8766  C C   . VAL E  1 131 ? 50.311  69.935 95.453  1.00 69.50  ? 131  VAL E C   1 
ATOM   8767  O O   . VAL E  1 131 ? 50.204  69.191 96.429  1.00 70.41  ? 131  VAL E O   1 
ATOM   8768  C CB  . VAL E  1 131 ? 50.610  72.425 95.404  1.00 71.61  ? 131  VAL E CB  1 
ATOM   8769  C CG1 . VAL E  1 131 ? 49.909  73.778 95.375  1.00 72.08  ? 131  VAL E CG1 1 
ATOM   8770  C CG2 . VAL E  1 131 ? 51.544  72.326 96.606  1.00 74.27  ? 131  VAL E CG2 1 
ATOM   8771  N N   . SER E  1 132 ? 51.054  69.641 94.388  1.00 68.52  ? 132  SER E N   1 
ATOM   8772  C CA  . SER E  1 132 ? 51.869  68.428 94.299  1.00 68.43  ? 132  SER E CA  1 
ATOM   8773  C C   . SER E  1 132 ? 53.118  68.685 93.463  1.00 68.73  ? 132  SER E C   1 
ATOM   8774  O O   . SER E  1 132 ? 53.156  69.613 92.653  1.00 68.29  ? 132  SER E O   1 
ATOM   8775  C CB  . SER E  1 132 ? 51.063  67.281 93.678  1.00 66.16  ? 132  SER E CB  1 
ATOM   8776  O OG  . SER E  1 132 ? 51.901  66.196 93.304  1.00 66.06  ? 132  SER E OG  1 
ATOM   8777  N N   . SER E  1 133 ? 54.131  67.847 93.662  1.00 69.57  ? 133  SER E N   1 
ATOM   8778  C CA  . SER E  1 133 ? 55.367  67.920 92.886  1.00 69.95  ? 133  SER E CA  1 
ATOM   8779  C C   . SER E  1 133 ? 55.168  67.439 91.444  1.00 67.57  ? 133  SER E C   1 
ATOM   8780  O O   . SER E  1 133 ? 55.981  67.747 90.570  1.00 67.67  ? 133  SER E O   1 
ATOM   8781  C CB  . SER E  1 133 ? 56.461  67.092 93.559  1.00 71.72  ? 133  SER E CB  1 
ATOM   8782  O OG  . SER E  1 133 ? 56.069  65.734 93.664  1.00 70.74  ? 133  SER E OG  1 
ATOM   8783  N N   . ALA E  1 134 ? 54.096  66.683 91.202  1.00 65.58  ? 134  ALA E N   1 
ATOM   8784  C CA  . ALA E  1 134 ? 53.786  66.169 89.864  1.00 63.41  ? 134  ALA E CA  1 
ATOM   8785  C C   . ALA E  1 134 ? 53.407  67.276 88.872  1.00 62.37  ? 134  ALA E C   1 
ATOM   8786  O O   . ALA E  1 134 ? 53.668  67.143 87.678  1.00 61.37  ? 134  ALA E O   1 
ATOM   8787  C CB  . ALA E  1 134 ? 52.681  65.126 89.943  1.00 61.89  ? 134  ALA E CB  1 
ATOM   8788  N N   . CYS E  1 135 ? 52.793  68.353 89.368  1.00 62.72  ? 135  CYS E N   1 
ATOM   8789  C CA  . CYS E  1 135 ? 52.522  69.550 88.560  1.00 62.24  ? 135  CYS E CA  1 
ATOM   8790  C C   . CYS E  1 135 ? 53.396  70.723 89.035  1.00 64.33  ? 135  CYS E C   1 
ATOM   8791  O O   . CYS E  1 135 ? 52.964  71.508 89.878  1.00 65.31  ? 135  CYS E O   1 
ATOM   8792  C CB  . CYS E  1 135 ? 51.040  69.955 88.645  1.00 61.13  ? 135  CYS E CB  1 
ATOM   8793  S SG  . CYS E  1 135 ? 49.832  68.616 88.518  1.00 59.12  ? 135  CYS E SG  1 
ATOM   8794  N N   . PRO E  1 136 ? 54.632  70.837 88.509  1.00 65.13  ? 136  PRO E N   1 
ATOM   8795  C CA  . PRO E  1 136 ? 55.515  71.946 88.881  1.00 67.31  ? 136  PRO E CA  1 
ATOM   8796  C C   . PRO E  1 136 ? 55.409  73.174 87.967  1.00 67.17  ? 136  PRO E C   1 
ATOM   8797  O O   . PRO E  1 136 ? 55.290  73.028 86.749  1.00 65.71  ? 136  PRO E O   1 
ATOM   8798  C CB  . PRO E  1 136 ? 56.903  71.324 88.752  1.00 68.39  ? 136  PRO E CB  1 
ATOM   8799  C CG  . PRO E  1 136 ? 56.754  70.354 87.632  1.00 66.38  ? 136  PRO E CG  1 
ATOM   8800  C CD  . PRO E  1 136 ? 55.357  69.808 87.739  1.00 64.48  ? 136  PRO E CD  1 
ATOM   8801  N N   . TYR E  1 137 ? 55.466  74.366 88.564  1.00 68.86  ? 137  TYR E N   1 
ATOM   8802  C CA  . TYR E  1 137 ? 55.486  75.636 87.826  1.00 69.28  ? 137  TYR E CA  1 
ATOM   8803  C C   . TYR E  1 137 ? 56.593  76.546 88.365  1.00 72.06  ? 137  TYR E C   1 
ATOM   8804  O O   . TYR E  1 137 ? 56.597  76.893 89.549  1.00 73.78  ? 137  TYR E O   1 
ATOM   8805  C CB  . TYR E  1 137 ? 54.128  76.339 87.939  1.00 68.57  ? 137  TYR E CB  1 
ATOM   8806  C CG  . TYR E  1 137 ? 54.088  77.749 87.370  1.00 69.46  ? 137  TYR E CG  1 
ATOM   8807  C CD1 . TYR E  1 137 ? 54.235  77.979 85.999  1.00 68.53  ? 137  TYR E CD1 1 
ATOM   8808  C CD2 . TYR E  1 137 ? 53.882  78.854 88.202  1.00 71.37  ? 137  TYR E CD2 1 
ATOM   8809  C CE1 . TYR E  1 137 ? 54.189  79.265 85.477  1.00 69.48  ? 137  TYR E CE1 1 
ATOM   8810  C CE2 . TYR E  1 137 ? 53.832  80.143 87.686  1.00 72.35  ? 137  TYR E CE2 1 
ATOM   8811  C CZ  . TYR E  1 137 ? 53.985  80.344 86.325  1.00 71.38  ? 137  TYR E CZ  1 
ATOM   8812  O OH  . TYR E  1 137 ? 53.938  81.621 85.817  1.00 72.49  ? 137  TYR E OH  1 
ATOM   8813  N N   . GLN E  1 138 ? 57.525  76.924 87.490  1.00 72.63  ? 138  GLN E N   1 
ATOM   8814  C CA  . GLN E  1 138 ? 58.673  77.767 87.852  1.00 75.38  ? 138  GLN E CA  1 
ATOM   8815  C C   . GLN E  1 138 ? 59.456  77.225 89.052  1.00 77.14  ? 138  GLN E C   1 
ATOM   8816  O O   . GLN E  1 138 ? 59.908  77.991 89.906  1.00 79.65  ? 138  GLN E O   1 
ATOM   8817  C CB  . GLN E  1 138 ? 58.225  79.208 88.121  1.00 76.76  ? 138  GLN E CB  1 
ATOM   8818  C CG  . GLN E  1 138 ? 57.378  79.801 87.007  1.00 75.21  ? 138  GLN E CG  1 
ATOM   8819  C CD  . GLN E  1 138 ? 57.354  81.321 87.018  1.00 77.13  ? 138  GLN E CD  1 
ATOM   8820  O OE1 . GLN E  1 138 ? 57.456  81.949 88.072  1.00 79.24  ? 138  GLN E OE1 1 
ATOM   8821  N NE2 . GLN E  1 138 ? 57.217  81.919 85.839  1.00 76.58  ? 138  GLN E NE2 1 
ATOM   8822  N N   . GLY E  1 139 ? 59.600  75.902 89.114  1.00 75.98  ? 139  GLY E N   1 
ATOM   8823  C CA  . GLY E  1 139 ? 60.383  75.244 90.163  1.00 77.61  ? 139  GLY E CA  1 
ATOM   8824  C C   . GLY E  1 139 ? 59.595  74.824 91.392  1.00 77.59  ? 139  GLY E C   1 
ATOM   8825  O O   . GLY E  1 139 ? 59.999  73.898 92.096  1.00 78.18  ? 139  GLY E O   1 
ATOM   8826  N N   . LYS E  1 140 ? 58.479  75.502 91.656  1.00 77.04  ? 140  LYS E N   1 
ATOM   8827  C CA  . LYS E  1 140 ? 57.655  75.212 92.829  1.00 77.18  ? 140  LYS E CA  1 
ATOM   8828  C C   . LYS E  1 140 ? 56.512  74.268 92.474  1.00 74.30  ? 140  LYS E C   1 
ATOM   8829  O O   . LYS E  1 140 ? 56.095  74.188 91.320  1.00 72.20  ? 140  LYS E O   1 
ATOM   8830  C CB  . LYS E  1 140 ? 57.096  76.504 93.443  1.00 78.65  ? 140  LYS E CB  1 
ATOM   8831  C CG  . LYS E  1 140 ? 58.147  77.408 94.074  1.00 81.93  ? 140  LYS E CG  1 
ATOM   8832  C CD  . LYS E  1 140 ? 58.566  78.542 93.145  1.00 82.49  ? 140  LYS E CD  1 
ATOM   8833  C CE  . LYS E  1 140 ? 59.912  79.139 93.536  1.00 85.64  ? 140  LYS E CE  1 
ATOM   8834  N NZ  . LYS E  1 140 ? 59.912  79.776 94.884  1.00 88.47  ? 140  LYS E NZ  1 
ATOM   8835  N N   . SER E  1 141 ? 56.018  73.556 93.484  1.00 74.38  ? 141  SER E N   1 
ATOM   8836  C CA  . SER E  1 141 ? 54.886  72.647 93.328  1.00 71.99  ? 141  SER E CA  1 
ATOM   8837  C C   . SER E  1 141 ? 53.600  73.439 93.087  1.00 70.87  ? 141  SER E C   1 
ATOM   8838  O O   . SER E  1 141 ? 53.313  74.401 93.802  1.00 72.43  ? 141  SER E O   1 
ATOM   8839  C CB  . SER E  1 141 ? 54.737  71.763 94.572  1.00 72.81  ? 141  SER E CB  1 
ATOM   8840  O OG  . SER E  1 141 ? 55.829  70.867 94.692  1.00 73.60  ? 141  SER E OG  1 
ATOM   8841  N N   . SER E  1 142 ? 52.836  73.024 92.079  1.00 68.33  ? 142  SER E N   1 
ATOM   8842  C CA  . SER E  1 142 ? 51.627  73.730 91.653  1.00 67.13  ? 142  SER E CA  1 
ATOM   8843  C C   . SER E  1 142 ? 50.504  72.719 91.400  1.00 64.83  ? 142  SER E C   1 
ATOM   8844  O O   . SER E  1 142 ? 50.602  71.563 91.821  1.00 64.50  ? 142  SER E O   1 
ATOM   8845  C CB  . SER E  1 142 ? 51.929  74.546 90.390  1.00 66.66  ? 142  SER E CB  1 
ATOM   8846  O OG  . SER E  1 142 ? 50.806  75.299 89.970  1.00 65.78  ? 142  SER E OG  1 
ATOM   8847  N N   . PHE E  1 143 ? 49.439  73.150 90.725  1.00 63.38  ? 143  PHE E N   1 
ATOM   8848  C CA  . PHE E  1 143 ? 48.310  72.267 90.417  1.00 61.30  ? 143  PHE E CA  1 
ATOM   8849  C C   . PHE E  1 143 ? 47.485  72.790 89.232  1.00 59.75  ? 143  PHE E C   1 
ATOM   8850  O O   . PHE E  1 143 ? 47.692  73.912 88.765  1.00 60.43  ? 143  PHE E O   1 
ATOM   8851  C CB  . PHE E  1 143 ? 47.420  72.109 91.661  1.00 61.88  ? 143  PHE E CB  1 
ATOM   8852  C CG  . PHE E  1 143 ? 46.566  70.866 91.652  1.00 60.23  ? 143  PHE E CG  1 
ATOM   8853  C CD1 . PHE E  1 143 ? 47.150  69.604 91.710  1.00 59.89  ? 143  PHE E CD1 1 
ATOM   8854  C CD2 . PHE E  1 143 ? 45.176  70.956 91.593  1.00 59.19  ? 143  PHE E CD2 1 
ATOM   8855  C CE1 . PHE E  1 143 ? 46.367  68.458 91.705  1.00 58.56  ? 143  PHE E CE1 1 
ATOM   8856  C CE2 . PHE E  1 143 ? 44.390  69.814 91.590  1.00 57.85  ? 143  PHE E CE2 1 
ATOM   8857  C CZ  . PHE E  1 143 ? 44.986  68.563 91.647  1.00 57.54  ? 143  PHE E CZ  1 
ATOM   8858  N N   . PHE E  1 144 ? 46.569  71.955 88.741  1.00 57.84  ? 144  PHE E N   1 
ATOM   8859  C CA  . PHE E  1 144 ? 45.575  72.364 87.747  1.00 56.44  ? 144  PHE E CA  1 
ATOM   8860  C C   . PHE E  1 144 ? 44.917  73.680 88.169  1.00 57.47  ? 144  PHE E C   1 
ATOM   8861  O O   . PHE E  1 144 ? 44.195  73.723 89.160  1.00 58.03  ? 144  PHE E O   1 
ATOM   8862  C CB  . PHE E  1 144 ? 44.486  71.292 87.600  1.00 54.76  ? 144  PHE E CB  1 
ATOM   8863  C CG  . PHE E  1 144 ? 44.999  69.934 87.192  1.00 53.81  ? 144  PHE E CG  1 
ATOM   8864  C CD1 . PHE E  1 144 ? 45.498  69.713 85.912  1.00 52.93  ? 144  PHE E CD1 1 
ATOM   8865  C CD2 . PHE E  1 144 ? 44.963  68.868 88.086  1.00 53.94  ? 144  PHE E CD2 1 
ATOM   8866  C CE1 . PHE E  1 144 ? 45.958  68.458 85.538  1.00 52.23  ? 144  PHE E CE1 1 
ATOM   8867  C CE2 . PHE E  1 144 ? 45.423  67.614 87.718  1.00 53.25  ? 144  PHE E CE2 1 
ATOM   8868  C CZ  . PHE E  1 144 ? 45.921  67.407 86.442  1.00 52.40  ? 144  PHE E CZ  1 
ATOM   8869  N N   . ARG E  1 145 ? 45.158  74.744 87.408  1.00 57.86  ? 145  ARG E N   1 
ATOM   8870  C CA  . ARG E  1 145 ? 44.750  76.098 87.800  1.00 59.28  ? 145  ARG E CA  1 
ATOM   8871  C C   . ARG E  1 145 ? 43.245  76.344 87.876  1.00 58.68  ? 145  ARG E C   1 
ATOM   8872  O O   . ARG E  1 145 ? 42.812  77.289 88.533  1.00 60.11  ? 145  ARG E O   1 
ATOM   8873  C CB  . ARG E  1 145 ? 45.342  77.129 86.841  1.00 59.84  ? 145  ARG E CB  1 
ATOM   8874  C CG  . ARG E  1 145 ? 46.855  77.118 86.763  1.00 60.85  ? 145  ARG E CG  1 
ATOM   8875  C CD  . ARG E  1 145 ? 47.367  78.493 86.383  1.00 62.43  ? 145  ARG E CD  1 
ATOM   8876  N NE  . ARG E  1 145 ? 48.773  78.448 85.995  1.00 63.18  ? 145  ARG E NE  1 
ATOM   8877  C CZ  . ARG E  1 145 ? 49.804  78.646 86.813  1.00 65.08  ? 145  ARG E CZ  1 
ATOM   8878  N NH1 . ARG E  1 145 ? 49.627  78.915 88.105  1.00 66.54  ? 145  ARG E NH1 1 
ATOM   8879  N NH2 . ARG E  1 145 ? 51.034  78.576 86.328  1.00 65.69  ? 145  ARG E NH2 1 
ATOM   8880  N N   . ASN E  1 146 ? 42.453  75.523 87.197  1.00 56.79  ? 146  ASN E N   1 
ATOM   8881  C CA  . ASN E  1 146 ? 41.008  75.747 87.119  1.00 56.22  ? 146  ASN E CA  1 
ATOM   8882  C C   . ASN E  1 146 ? 40.218  75.125 88.266  1.00 56.32  ? 146  ASN E C   1 
ATOM   8883  O O   . ASN E  1 146 ? 39.044  75.450 88.458  1.00 56.31  ? 146  ASN E O   1 
ATOM   8884  C CB  . ASN E  1 146 ? 40.469  75.252 85.774  1.00 54.35  ? 146  ASN E CB  1 
ATOM   8885  C CG  . ASN E  1 146 ? 40.911  76.128 84.615  1.00 54.52  ? 146  ASN E CG  1 
ATOM   8886  O OD1 . ASN E  1 146 ? 40.945  77.355 84.732  1.00 55.90  ? 146  ASN E OD1 1 
ATOM   8887  N ND2 . ASN E  1 146 ? 41.246  75.506 83.487  1.00 53.28  ? 146  ASN E ND2 1 
ATOM   8888  N N   . VAL E  1 147 ? 40.861  74.245 89.030  1.00 56.59  ? 147  VAL E N   1 
ATOM   8889  C CA  . VAL E  1 147 ? 40.207  73.582 90.160  1.00 56.89  ? 147  VAL E CA  1 
ATOM   8890  C C   . VAL E  1 147 ? 41.018  73.709 91.453  1.00 58.87  ? 147  VAL E C   1 
ATOM   8891  O O   . VAL E  1 147 ? 42.247  73.791 91.422  1.00 59.58  ? 147  VAL E O   1 
ATOM   8892  C CB  . VAL E  1 147 ? 39.931  72.092 89.862  1.00 55.20  ? 147  VAL E CB  1 
ATOM   8893  C CG1 . VAL E  1 147 ? 38.817  71.951 88.835  1.00 53.60  ? 147  VAL E CG1 1 
ATOM   8894  C CG2 . VAL E  1 147 ? 41.195  71.373 89.394  1.00 54.78  ? 147  VAL E CG2 1 
ATOM   8895  N N   . VAL E  1 148 ? 40.316  73.719 92.585  1.00 59.93  ? 148  VAL E N   1 
ATOM   8896  C CA  . VAL E  1 148 ? 40.932  73.909 93.907  1.00 62.12  ? 148  VAL E CA  1 
ATOM   8897  C C   . VAL E  1 148 ? 40.999  72.582 94.675  1.00 62.05  ? 148  VAL E C   1 
ATOM   8898  O O   . VAL E  1 148 ? 39.966  71.963 94.944  1.00 61.36  ? 148  VAL E O   1 
ATOM   8899  C CB  . VAL E  1 148 ? 40.131  74.930 94.748  1.00 63.82  ? 148  VAL E CB  1 
ATOM   8900  C CG1 . VAL E  1 148 ? 40.868  75.268 96.039  1.00 66.38  ? 148  VAL E CG1 1 
ATOM   8901  C CG2 . VAL E  1 148 ? 39.860  76.199 93.950  1.00 63.91  ? 148  VAL E CG2 1 
ATOM   8902  N N   . TRP E  1 149 ? 42.211  72.153 95.024  1.00 62.91  ? 149  TRP E N   1 
ATOM   8903  C CA  . TRP E  1 149 ? 42.395  70.974 95.873  1.00 63.36  ? 149  TRP E CA  1 
ATOM   8904  C C   . TRP E  1 149 ? 42.244  71.394 97.346  1.00 65.76  ? 149  TRP E C   1 
ATOM   8905  O O   . TRP E  1 149 ? 43.156  71.979 97.937  1.00 67.71  ? 149  TRP E O   1 
ATOM   8906  C CB  . TRP E  1 149 ? 43.764  70.329 95.617  1.00 63.46  ? 149  TRP E CB  1 
ATOM   8907  C CG  . TRP E  1 149 ? 43.970  68.973 96.277  1.00 63.70  ? 149  TRP E CG  1 
ATOM   8908  C CD1 . TRP E  1 149 ? 43.125  68.335 97.146  1.00 64.04  ? 149  TRP E CD1 1 
ATOM   8909  C CD2 . TRP E  1 149 ? 45.112  68.113 96.133  1.00 63.85  ? 149  TRP E CD2 1 
ATOM   8910  N NE1 . TRP E  1 149 ? 43.662  67.132 97.535  1.00 64.32  ? 149  TRP E NE1 1 
ATOM   8911  C CE2 . TRP E  1 149 ? 44.881  66.971 96.931  1.00 64.22  ? 149  TRP E CE2 1 
ATOM   8912  C CE3 . TRP E  1 149 ? 46.304  68.195 95.402  1.00 63.83  ? 149  TRP E CE3 1 
ATOM   8913  C CZ2 . TRP E  1 149 ? 45.798  65.918 97.018  1.00 64.58  ? 149  TRP E CZ2 1 
ATOM   8914  C CZ3 . TRP E  1 149 ? 47.215  67.146 95.491  1.00 64.20  ? 149  TRP E CZ3 1 
ATOM   8915  C CH2 . TRP E  1 149 ? 46.955  66.024 96.295  1.00 64.58  ? 149  TRP E CH2 1 
ATOM   8916  N N   . LEU E  1 150 ? 41.085  71.086 97.928  1.00 65.74  ? 150  LEU E N   1 
ATOM   8917  C CA  . LEU E  1 150 ? 40.751  71.525 99.283  1.00 68.07  ? 150  LEU E CA  1 
ATOM   8918  C C   . LEU E  1 150 ? 41.264  70.554 100.343 1.00 69.37  ? 150  LEU E C   1 
ATOM   8919  O O   . LEU E  1 150 ? 41.179  69.336 100.172 1.00 68.15  ? 150  LEU E O   1 
ATOM   8920  C CB  . LEU E  1 150 ? 39.233  71.686 99.436  1.00 67.66  ? 150  LEU E CB  1 
ATOM   8921  C CG  . LEU E  1 150 ? 38.551  72.808 98.643  1.00 67.03  ? 150  LEU E CG  1 
ATOM   8922  C CD1 . LEU E  1 150 ? 37.044  72.748 98.847  1.00 66.68  ? 150  LEU E CD1 1 
ATOM   8923  C CD2 . LEU E  1 150 ? 39.084  74.181 99.031  1.00 69.18  ? 150  LEU E CD2 1 
ATOM   8924  N N   . ILE E  1 151 ? 41.790  71.112 101.436 1.00 72.04  ? 151  ILE E N   1 
ATOM   8925  C CA  . ILE E  1 151 ? 42.236  70.334 102.601 1.00 73.81  ? 151  ILE E CA  1 
ATOM   8926  C C   . ILE E  1 151 ? 41.685  70.927 103.905 1.00 76.37  ? 151  ILE E C   1 
ATOM   8927  O O   . ILE E  1 151 ? 41.134  72.033 103.924 1.00 77.00  ? 151  ILE E O   1 
ATOM   8928  C CB  . ILE E  1 151 ? 43.782  70.236 102.674 1.00 74.94  ? 151  ILE E CB  1 
ATOM   8929  C CG1 . ILE E  1 151 ? 44.403  71.598 103.022 1.00 77.18  ? 151  ILE E CG1 1 
ATOM   8930  C CG2 . ILE E  1 151 ? 44.340  69.689 101.364 1.00 72.56  ? 151  ILE E CG2 1 
ATOM   8931  C CD1 . ILE E  1 151 ? 45.916  71.645 102.946 1.00 78.26  ? 151  ILE E CD1 1 
ATOM   8932  N N   . LYS E  1 152 ? 41.844  70.174 104.989 1.00 77.99  ? 152  LYS E N   1 
ATOM   8933  C CA  . LYS E  1 152 ? 41.354  70.570 106.319 1.00 80.68  ? 152  LYS E CA  1 
ATOM   8934  C C   . LYS E  1 152 ? 42.065  71.801 106.888 1.00 83.41  ? 152  LYS E C   1 
ATOM   8935  O O   . LYS E  1 152 ? 43.249  72.017 106.622 1.00 83.87  ? 152  LYS E O   1 
ATOM   8936  C CB  . LYS E  1 152 ? 41.489  69.397 107.298 1.00 81.88  ? 152  LYS E CB  1 
ATOM   8937  C CG  . LYS E  1 152 ? 42.921  68.930 107.528 1.00 82.97  ? 152  LYS E CG  1 
ATOM   8938  C CD  . LYS E  1 152 ? 42.965  67.663 108.358 1.00 83.92  ? 152  LYS E CD  1 
ATOM   8939  C CE  . LYS E  1 152 ? 44.385  67.221 108.642 1.00 85.31  ? 152  LYS E CE  1 
ATOM   8940  N NZ  . LYS E  1 152 ? 44.798  67.213 110.065 1.00 88.84  ? 152  LYS E NZ  1 
ATOM   8941  N N   . LYS E  1 153 ? 41.330  72.599 107.667 1.00 85.37  ? 153  LYS E N   1 
ATOM   8942  C CA  . LYS E  1 153 ? 41.894  73.749 108.385 1.00 88.46  ? 153  LYS E CA  1 
ATOM   8943  C C   . LYS E  1 153 ? 41.890  73.465 109.890 1.00 91.58  ? 153  LYS E C   1 
ATOM   8944  O O   . LYS E  1 153 ? 40.837  73.207 110.476 1.00 91.98  ? 153  LYS E O   1 
ATOM   8945  C CB  . LYS E  1 153 ? 41.096  75.025 108.090 1.00 88.67  ? 153  LYS E CB  1 
ATOM   8946  C CG  . LYS E  1 153 ? 41.883  76.315 108.311 1.00 91.16  ? 153  LYS E CG  1 
ATOM   8947  C CD  . LYS E  1 153 ? 40.958  77.473 108.667 1.00 92.79  ? 153  LYS E CD  1 
ATOM   8948  C CE  . LYS E  1 153 ? 40.044  77.901 107.517 1.00 90.23  ? 153  LYS E CE  1 
ATOM   8949  N NZ  . LYS E  1 153 ? 40.749  78.178 106.233 1.00 88.24  ? 153  LYS E NZ  1 
ATOM   8950  N N   . ASN E  1 154 ? 43.073  73.524 110.500 1.00 93.92  ? 154  ASN E N   1 
ATOM   8951  C CA  . ASN E  1 154 ? 43.269  73.206 111.922 1.00 97.19  ? 154  ASN E CA  1 
ATOM   8952  C C   . ASN E  1 154 ? 42.648  71.863 112.332 1.00 96.42  ? 154  ASN E C   1 
ATOM   8953  O O   . ASN E  1 154 ? 41.885  71.780 113.299 1.00 98.17  ? 154  ASN E O   1 
ATOM   8954  C CB  . ASN E  1 154 ? 42.764  74.348 112.821 1.00 100.27 ? 154  ASN E CB  1 
ATOM   8955  C CG  . ASN E  1 154 ? 43.427  74.353 114.193 1.00 104.33 ? 154  ASN E CG  1 
ATOM   8956  O OD1 . ASN E  1 154 ? 44.601  74.005 114.328 1.00 105.26 ? 154  ASN E OD1 1 
ATOM   8957  N ND2 . ASN E  1 154 ? 42.678  74.753 115.219 1.00 106.96 ? 154  ASN E ND2 1 
ATOM   8958  N N   . SER E  1 155 ? 42.985  70.820 111.572 1.00 93.88  ? 155  SER E N   1 
ATOM   8959  C CA  . SER E  1 155 ? 42.593  69.436 111.870 1.00 93.17  ? 155  SER E CA  1 
ATOM   8960  C C   . SER E  1 155 ? 41.076  69.194 111.892 1.00 92.02  ? 155  SER E C   1 
ATOM   8961  O O   . SER E  1 155 ? 40.582  68.404 112.695 1.00 93.09  ? 155  SER E O   1 
ATOM   8962  C CB  . SER E  1 155 ? 43.242  68.968 113.186 1.00 96.51  ? 155  SER E CB  1 
ATOM   8963  O OG  . SER E  1 155 ? 44.629  68.737 113.009 1.00 96.99  ? 155  SER E OG  1 
ATOM   8964  N N   . THR E  1 156 ? 40.342  69.874 111.014 1.00 90.01  ? 156  THR E N   1 
ATOM   8965  C CA  . THR E  1 156 ? 38.905  69.630 110.851 1.00 88.62  ? 156  THR E CA  1 
ATOM   8966  C C   . THR E  1 156 ? 38.515  69.887 109.403 1.00 85.36  ? 156  THR E C   1 
ATOM   8967  O O   . THR E  1 156 ? 38.815  70.954 108.867 1.00 85.24  ? 156  THR E O   1 
ATOM   8968  C CB  . THR E  1 156 ? 38.025  70.548 111.736 1.00 90.99  ? 156  THR E CB  1 
ATOM   8969  O OG1 . THR E  1 156 ? 37.907  71.841 111.127 1.00 90.65  ? 156  THR E OG1 1 
ATOM   8970  C CG2 . THR E  1 156 ? 38.583  70.701 113.153 1.00 94.86  ? 156  THR E CG2 1 
ATOM   8971  N N   . TYR E  1 157 ? 37.857  68.916 108.773 1.00 82.93  ? 157  TYR E N   1 
ATOM   8972  C CA  . TYR E  1 157 ? 37.309  69.102 107.430 1.00 79.96  ? 157  TYR E CA  1 
ATOM   8973  C C   . TYR E  1 157 ? 35.780  69.097 107.507 1.00 79.54  ? 157  TYR E C   1 
ATOM   8974  O O   . TYR E  1 157 ? 35.149  68.041 107.389 1.00 78.31  ? 157  TYR E O   1 
ATOM   8975  C CB  . TYR E  1 157 ? 37.816  68.021 106.468 1.00 77.44  ? 157  TYR E CB  1 
ATOM   8976  C CG  . TYR E  1 157 ? 37.609  68.370 105.004 1.00 74.65  ? 157  TYR E CG  1 
ATOM   8977  C CD1 . TYR E  1 157 ? 38.291  69.432 104.423 1.00 74.59  ? 157  TYR E CD1 1 
ATOM   8978  C CD2 . TYR E  1 157 ? 36.740  67.639 104.201 1.00 72.28  ? 157  TYR E CD2 1 
ATOM   8979  C CE1 . TYR E  1 157 ? 38.111  69.761 103.087 1.00 72.26  ? 157  TYR E CE1 1 
ATOM   8980  C CE2 . TYR E  1 157 ? 36.554  67.963 102.863 1.00 69.96  ? 157  TYR E CE2 1 
ATOM   8981  C CZ  . TYR E  1 157 ? 37.240  69.020 102.309 1.00 69.95  ? 157  TYR E CZ  1 
ATOM   8982  O OH  . TYR E  1 157 ? 37.042  69.321 100.978 1.00 67.76  ? 157  TYR E OH  1 
ATOM   8983  N N   . PRO E  1 158 ? 35.179  70.282 107.725 1.00 80.77  ? 158  PRO E N   1 
ATOM   8984  C CA  . PRO E  1 158 ? 33.723  70.364 107.823 1.00 80.64  ? 158  PRO E CA  1 
ATOM   8985  C C   . PRO E  1 158 ? 33.042  70.141 106.479 1.00 77.56  ? 158  PRO E C   1 
ATOM   8986  O O   . PRO E  1 158 ? 33.665  70.313 105.428 1.00 75.76  ? 158  PRO E O   1 
ATOM   8987  C CB  . PRO E  1 158 ? 33.480  71.791 108.329 1.00 82.87  ? 158  PRO E CB  1 
ATOM   8988  C CG  . PRO E  1 158 ? 34.669  72.561 107.878 1.00 82.97  ? 158  PRO E CG  1 
ATOM   8989  C CD  . PRO E  1 158 ? 35.820  71.598 107.915 1.00 82.55  ? 158  PRO E CD  1 
ATOM   8990  N N   . THR E  1 159 ? 31.771  69.756 106.526 1.00 77.19  ? 159  THR E N   1 
ATOM   8991  C CA  . THR E  1 159 ? 31.010  69.461 105.320 1.00 74.55  ? 159  THR E CA  1 
ATOM   8992  C C   . THR E  1 159 ? 30.885  70.708 104.447 1.00 73.96  ? 159  THR E C   1 
ATOM   8993  O O   . THR E  1 159 ? 30.675  71.816 104.951 1.00 75.81  ? 159  THR E O   1 
ATOM   8994  C CB  . THR E  1 159 ? 29.602  68.920 105.651 1.00 74.64  ? 159  THR E CB  1 
ATOM   8995  O OG1 . THR E  1 159 ? 29.714  67.799 106.536 1.00 75.62  ? 159  THR E OG1 1 
ATOM   8996  C CG2 . THR E  1 159 ? 28.869  68.481 104.385 1.00 71.90  ? 159  THR E CG2 1 
ATOM   8997  N N   . ILE E  1 160 ? 31.037  70.502 103.138 1.00 71.57  ? 160  ILE E N   1 
ATOM   8998  C CA  . ILE E  1 160 ? 30.912  71.555 102.136 1.00 70.76  ? 160  ILE E CA  1 
ATOM   8999  C C   . ILE E  1 160 ? 29.526  71.470 101.510 1.00 69.67  ? 160  ILE E C   1 
ATOM   9000  O O   . ILE E  1 160 ? 29.108  70.396 101.093 1.00 68.10  ? 160  ILE E O   1 
ATOM   9001  C CB  . ILE E  1 160 ? 31.969  71.387 101.024 1.00 68.80  ? 160  ILE E CB  1 
ATOM   9002  C CG1 . ILE E  1 160 ? 33.375  71.601 101.593 1.00 70.18  ? 160  ILE E CG1 1 
ATOM   9003  C CG2 . ILE E  1 160 ? 31.703  72.355 99.876  1.00 67.70  ? 160  ILE E CG2 1 
ATOM   9004  C CD1 . ILE E  1 160 ? 34.494  71.083 100.715 1.00 68.50  ? 160  ILE E CD1 1 
ATOM   9005  N N   . LYS E  1 161 ? 28.821  72.599 101.451 1.00 70.73  ? 161  LYS E N   1 
ATOM   9006  C CA  . LYS E  1 161 ? 27.524  72.681 100.769 1.00 69.84  ? 161  LYS E CA  1 
ATOM   9007  C C   . LYS E  1 161 ? 27.475  73.923 99.891  1.00 69.78  ? 161  LYS E C   1 
ATOM   9008  O O   . LYS E  1 161 ? 27.110  75.007 100.348 1.00 71.61  ? 161  LYS E O   1 
ATOM   9009  C CB  . LYS E  1 161 ? 26.369  72.707 101.774 1.00 71.64  ? 161  LYS E CB  1 
ATOM   9010  C CG  . LYS E  1 161 ? 26.083  71.368 102.433 1.00 71.61  ? 161  LYS E CG  1 
ATOM   9011  C CD  . LYS E  1 161 ? 25.066  71.507 103.556 1.00 73.84  ? 161  LYS E CD  1 
ATOM   9012  C CE  . LYS E  1 161 ? 24.784  70.168 104.222 1.00 74.00  ? 161  LYS E CE  1 
ATOM   9013  N NZ  . LYS E  1 161 ? 24.042  70.318 105.507 1.00 76.66  ? 161  LYS E NZ  1 
ATOM   9014  N N   . ARG E  1 162 ? 27.846  73.758 98.626  1.00 67.90  ? 162  ARG E N   1 
ATOM   9015  C CA  . ARG E  1 162 ? 27.882  74.874 97.698  1.00 67.84  ? 162  ARG E CA  1 
ATOM   9016  C C   . ARG E  1 162 ? 27.022  74.662 96.480  1.00 66.25  ? 162  ARG E C   1 
ATOM   9017  O O   . ARG E  1 162 ? 27.006  73.573 95.908  1.00 64.43  ? 162  ARG E O   1 
ATOM   9018  C CB  . ARG E  1 162 ? 29.285  75.045 97.172  1.00 67.16  ? 162  ARG E CB  1 
ATOM   9019  C CG  . ARG E  1 162 ? 29.785  76.466 97.095  1.00 68.52  ? 162  ARG E CG  1 
ATOM   9020  C CD  . ARG E  1 162 ? 29.856  77.240 98.383  1.00 71.30  ? 162  ARG E CD  1 
ATOM   9021  N NE  . ARG E  1 162 ? 30.926  78.207 98.208  1.00 72.21  ? 162  ARG E NE  1 
ATOM   9022  C CZ  . ARG E  1 162 ? 32.068  78.320 98.896  1.00 73.52  ? 162  ARG E CZ  1 
ATOM   9023  N NH1 . ARG E  1 162 ? 32.363  77.565 99.956  1.00 74.37  ? 162  ARG E NH1 1 
ATOM   9024  N NH2 . ARG E  1 162 ? 32.930  79.260 98.523  1.00 74.21  ? 162  ARG E NH2 1 
ATOM   9025  N N   . SER E  1 163 ? 26.403  75.751 96.037  1.00 67.19  ? 163  SER E N   1 
ATOM   9026  C CA  . SER E  1 163 ? 25.524  75.745 94.889  1.00 66.12  ? 163  SER E CA  1 
ATOM   9027  C C   . SER E  1 163 ? 25.857  76.911 93.958  1.00 66.57  ? 163  SER E C   1 
ATOM   9028  O O   . SER E  1 163 ? 26.156  78.012 94.422  1.00 68.34  ? 163  SER E O   1 
ATOM   9029  C CB  . SER E  1 163 ? 24.078  75.853 95.364  1.00 67.13  ? 163  SER E CB  1 
ATOM   9030  O OG  . SER E  1 163 ? 23.181  75.902 94.270  1.00 66.06  ? 163  SER E OG  1 
ATOM   9031  N N   . TYR E  1 164 ? 25.815  76.663 92.648  1.00 65.29  ? 164  TYR E N   1 
ATOM   9032  C CA  . TYR E  1 164 ? 25.959  77.733 91.658  1.00 65.82  ? 164  TYR E CA  1 
ATOM   9033  C C   . TYR E  1 164 ? 24.808  77.748 90.653  1.00 65.71  ? 164  TYR E C   1 
ATOM   9034  O O   . TYR E  1 164 ? 24.533  76.741 90.001  1.00 63.96  ? 164  TYR E O   1 
ATOM   9035  C CB  . TYR E  1 164 ? 27.280  77.633 90.898  1.00 64.52  ? 164  TYR E CB  1 
ATOM   9036  C CG  . TYR E  1 164 ? 27.284  78.542 89.691  1.00 64.25  ? 164  TYR E CG  1 
ATOM   9037  C CD1 . TYR E  1 164 ? 27.402  79.923 89.837  1.00 66.02  ? 164  TYR E CD1 1 
ATOM   9038  C CD2 . TYR E  1 164 ? 27.113  78.029 88.406  1.00 62.42  ? 164  TYR E CD2 1 
ATOM   9039  C CE1 . TYR E  1 164 ? 27.382  80.764 88.736  1.00 65.99  ? 164  TYR E CE1 1 
ATOM   9040  C CE2 . TYR E  1 164 ? 27.088  78.862 87.299  1.00 62.38  ? 164  TYR E CE2 1 
ATOM   9041  C CZ  . TYR E  1 164 ? 27.225  80.227 87.467  1.00 64.14  ? 164  TYR E CZ  1 
ATOM   9042  O OH  . TYR E  1 164 ? 27.202  81.052 86.366  1.00 64.27  ? 164  TYR E OH  1 
ATOM   9043  N N   . ASN E  1 165 ? 24.172  78.911 90.517  1.00 68.04  ? 165  ASN E N   1 
ATOM   9044  C CA  . ASN E  1 165 ? 23.084  79.118 89.567  1.00 68.60  ? 165  ASN E CA  1 
ATOM   9045  C C   . ASN E  1 165 ? 23.608  79.695 88.254  1.00 67.24  ? 165  ASN E C   1 
ATOM   9046  O O   . ASN E  1 165 ? 24.255  80.742 88.250  1.00 68.34  ? 165  ASN E O   1 
ATOM   9047  C CB  . ASN E  1 165 ? 22.057  80.081 90.166  1.00 72.25  ? 165  ASN E CB  1 
ATOM   9048  C CG  . ASN E  1 165 ? 20.731  80.059 89.432  1.00 74.03  ? 165  ASN E CG  1 
ATOM   9049  O OD1 . ASN E  1 165 ? 20.633  79.580 88.305  1.00 72.43  ? 165  ASN E OD1 1 
ATOM   9050  N ND2 . ASN E  1 165 ? 19.698  80.587 90.078  1.00 78.41  ? 165  ASN E ND2 1 
ATOM   9051  N N   . ASN E  1 166 ? 23.321  79.020 87.143  1.00 64.81  ? 166  ASN E N   1 
ATOM   9052  C CA  . ASN E  1 166 ? 23.755  79.491 85.828  1.00 63.63  ? 166  ASN E CA  1 
ATOM   9053  C C   . ASN E  1 166 ? 22.862  80.620 85.313  1.00 64.55  ? 166  ASN E C   1 
ATOM   9054  O O   . ASN E  1 166 ? 21.863  80.378 84.628  1.00 64.08  ? 166  ASN E O   1 
ATOM   9055  C CB  . ASN E  1 166 ? 23.790  78.340 84.816  1.00 61.46  ? 166  ASN E CB  1 
ATOM   9056  C CG  . ASN E  1 166 ? 24.496  78.722 83.526  1.00 60.79  ? 166  ASN E CG  1 
ATOM   9057  O OD1 . ASN E  1 166 ? 25.172  79.750 83.455  1.00 61.69  ? 166  ASN E OD1 1 
ATOM   9058  N ND2 . ASN E  1 166 ? 24.352  77.888 82.501  1.00 59.30  ? 166  ASN E ND2 1 
ATOM   9059  N N   . THR E  1 167 ? 23.237  81.852 85.650  1.00 65.77  ? 167  THR E N   1 
ATOM   9060  C CA  . THR E  1 167 ? 22.480  83.041 85.244  1.00 67.04  ? 167  THR E CA  1 
ATOM   9061  C C   . THR E  1 167 ? 22.809  83.526 83.825  1.00 66.30  ? 167  THR E C   1 
ATOM   9062  O O   . THR E  1 167 ? 22.056  84.325 83.262  1.00 67.44  ? 167  THR E O   1 
ATOM   9063  C CB  . THR E  1 167 ? 22.701  84.210 86.224  1.00 69.35  ? 167  THR E CB  1 
ATOM   9064  O OG1 . THR E  1 167 ? 24.107  84.427 86.405  1.00 69.31  ? 167  THR E OG1 1 
ATOM   9065  C CG2 . THR E  1 167 ? 22.048  83.908 87.565  1.00 70.27  ? 167  THR E CG2 1 
ATOM   9066  N N   . ASN E  1 168 ? 23.923  83.059 83.254  1.00 64.42  ? 168  ASN E N   1 
ATOM   9067  C CA  . ASN E  1 168 ? 24.262  83.385 81.860  1.00 63.64  ? 168  ASN E CA  1 
ATOM   9068  C C   . ASN E  1 168 ? 23.276  82.673 80.951  1.00 62.26  ? 168  ASN E C   1 
ATOM   9069  O O   . ASN E  1 168 ? 22.793  81.597 81.296  1.00 61.16  ? 168  ASN E O   1 
ATOM   9070  C CB  . ASN E  1 168 ? 25.682  82.948 81.455  1.00 62.38  ? 168  ASN E CB  1 
ATOM   9071  C CG  . ASN E  1 168 ? 26.655  82.898 82.616  1.00 62.69  ? 168  ASN E CG  1 
ATOM   9072  O OD1 . ASN E  1 168 ? 27.423  83.836 82.834  1.00 64.03  ? 168  ASN E OD1 1 
ATOM   9073  N ND2 . ASN E  1 168 ? 26.646  81.789 83.353  1.00 61.61  ? 168  ASN E ND2 1 
ATOM   9074  N N   . GLN E  1 169 ? 22.984  83.259 79.793  1.00 62.33  ? 169  GLN E N   1 
ATOM   9075  C CA  . GLN E  1 169 ? 22.127  82.591 78.814  1.00 61.22  ? 169  GLN E CA  1 
ATOM   9076  C C   . GLN E  1 169 ? 22.976  81.728 77.856  1.00 59.24  ? 169  GLN E C   1 
ATOM   9077  O O   . GLN E  1 169 ? 22.910  81.867 76.634  1.00 59.15  ? 169  GLN E O   1 
ATOM   9078  C CB  . GLN E  1 169 ? 21.214  83.590 78.080  1.00 62.78  ? 169  GLN E CB  1 
ATOM   9079  C CG  . GLN E  1 169 ? 21.907  84.691 77.285  1.00 63.79  ? 169  GLN E CG  1 
ATOM   9080  C CD  . GLN E  1 169 ? 21.091  85.162 76.085  1.00 64.66  ? 169  GLN E CD  1 
ATOM   9081  O OE1 . GLN E  1 169 ? 20.350  84.389 75.469  1.00 63.81  ? 169  GLN E OE1 1 
ATOM   9082  N NE2 . GLN E  1 169 ? 21.237  86.436 75.739  1.00 66.46  ? 169  GLN E NE2 1 
ATOM   9083  N N   . GLU E  1 170 ? 23.773  80.839 78.450  1.00 57.72  ? 170  GLU E N   1 
ATOM   9084  C CA  . GLU E  1 170 ? 24.647  79.915 77.726  1.00 55.90  ? 170  GLU E CA  1 
ATOM   9085  C C   . GLU E  1 170 ? 24.697  78.578 78.459  1.00 54.42  ? 170  GLU E C   1 
ATOM   9086  O O   . GLU E  1 170 ? 24.405  78.505 79.656  1.00 54.81  ? 170  GLU E O   1 
ATOM   9087  C CB  . GLU E  1 170 ? 26.080  80.462 77.624  1.00 56.01  ? 170  GLU E CB  1 
ATOM   9088  C CG  . GLU E  1 170 ? 26.297  81.544 76.573  1.00 57.05  ? 170  GLU E CG  1 
ATOM   9089  C CD  . GLU E  1 170 ? 26.373  82.950 77.145  1.00 58.98  ? 170  GLU E CD  1 
ATOM   9090  O OE1 . GLU E  1 170 ? 25.786  83.209 78.219  1.00 59.81  ? 170  GLU E OE1 1 
ATOM   9091  O OE2 . GLU E  1 170 ? 27.023  83.808 76.513  1.00 59.82  ? 170  GLU E OE2 1 
ATOM   9092  N N   . ASP E  1 171 ? 25.063  77.523 77.736  1.00 52.85  ? 171  ASP E N   1 
ATOM   9093  C CA  . ASP E  1 171 ? 25.472  76.273 78.364  1.00 51.51  ? 171  ASP E CA  1 
ATOM   9094  C C   . ASP E  1 171 ? 26.820  76.532 79.032  1.00 51.45  ? 171  ASP E C   1 
ATOM   9095  O O   . ASP E  1 171 ? 27.575  77.415 78.607  1.00 52.00  ? 171  ASP E O   1 
ATOM   9096  C CB  . ASP E  1 171 ? 25.608  75.139 77.338  1.00 50.21  ? 171  ASP E CB  1 
ATOM   9097  C CG  . ASP E  1 171 ? 24.274  74.701 76.747  1.00 50.21  ? 171  ASP E CG  1 
ATOM   9098  O OD1 . ASP E  1 171 ? 23.247  74.689 77.459  1.00 50.71  ? 171  ASP E OD1 1 
ATOM   9099  O OD2 . ASP E  1 171 ? 24.262  74.337 75.556  1.00 49.84  ? 171  ASP E OD2 1 
ATOM   9100  N N   . LEU E  1 172 ? 27.113  75.766 80.077  1.00 50.87  ? 172  LEU E N   1 
ATOM   9101  C CA  . LEU E  1 172 ? 28.334  75.953 80.845  1.00 51.02  ? 172  LEU E CA  1 
ATOM   9102  C C   . LEU E  1 172 ? 29.016  74.621 81.109  1.00 49.72  ? 172  LEU E C   1 
ATOM   9103  O O   . LEU E  1 172 ? 28.417  73.720 81.695  1.00 49.27  ? 172  LEU E O   1 
ATOM   9104  C CB  . LEU E  1 172 ? 28.012  76.645 82.170  1.00 52.38  ? 172  LEU E CB  1 
ATOM   9105  C CG  . LEU E  1 172 ? 29.206  77.063 83.032  1.00 53.14  ? 172  LEU E CG  1 
ATOM   9106  C CD1 . LEU E  1 172 ? 29.954  78.234 82.409  1.00 53.99  ? 172  LEU E CD1 1 
ATOM   9107  C CD2 . LEU E  1 172 ? 28.736  77.422 84.435  1.00 54.47  ? 172  LEU E CD2 1 
ATOM   9108  N N   . LEU E  1 173 ? 30.267  74.504 80.669  1.00 49.21  ? 173  LEU E N   1 
ATOM   9109  C CA  . LEU E  1 173 ? 31.077  73.321 80.940  1.00 48.22  ? 173  LEU E CA  1 
ATOM   9110  C C   . LEU E  1 173 ? 31.716  73.440 82.314  1.00 48.90  ? 173  LEU E C   1 
ATOM   9111  O O   . LEU E  1 173 ? 32.634  74.236 82.510  1.00 49.69  ? 173  LEU E O   1 
ATOM   9112  C CB  . LEU E  1 173 ? 32.172  73.151 79.886  1.00 47.64  ? 173  LEU E CB  1 
ATOM   9113  C CG  . LEU E  1 173 ? 33.183  72.023 80.146  1.00 46.93  ? 173  LEU E CG  1 
ATOM   9114  C CD1 . LEU E  1 173 ? 32.522  70.653 80.087  1.00 45.95  ? 173  LEU E CD1 1 
ATOM   9115  C CD2 . LEU E  1 173 ? 34.331  72.103 79.155  1.00 46.74  ? 173  LEU E CD2 1 
ATOM   9116  N N   . VAL E  1 174 ? 31.231  72.634 83.254  1.00 48.73  ? 174  VAL E N   1 
ATOM   9117  C CA  . VAL E  1 174 ? 31.769  72.593 84.610  1.00 49.48  ? 174  VAL E CA  1 
ATOM   9118  C C   . VAL E  1 174 ? 32.672  71.370 84.766  1.00 48.72  ? 174  VAL E C   1 
ATOM   9119  O O   . VAL E  1 174 ? 32.345  70.282 84.284  1.00 47.65  ? 174  VAL E O   1 
ATOM   9120  C CB  . VAL E  1 174 ? 30.643  72.518 85.663  1.00 50.11  ? 174  VAL E CB  1 
ATOM   9121  C CG1 . VAL E  1 174 ? 31.217  72.652 87.066  1.00 51.29  ? 174  VAL E CG1 1 
ATOM   9122  C CG2 . VAL E  1 174 ? 29.595  73.593 85.410  1.00 50.84  ? 174  VAL E CG2 1 
ATOM   9123  N N   . LEU E  1 175 ? 33.802  71.563 85.444  1.00 49.43  ? 175  LEU E N   1 
ATOM   9124  C CA  . LEU E  1 175 ? 34.748  70.490 85.737  1.00 49.04  ? 175  LEU E CA  1 
ATOM   9125  C C   . LEU E  1 175 ? 34.998  70.413 87.237  1.00 50.20  ? 175  LEU E C   1 
ATOM   9126  O O   . LEU E  1 175 ? 35.146  71.441 87.894  1.00 51.48  ? 175  LEU E O   1 
ATOM   9127  C CB  . LEU E  1 175 ? 36.084  70.755 85.043  1.00 48.99  ? 175  LEU E CB  1 
ATOM   9128  C CG  . LEU E  1 175 ? 36.077  70.927 83.525  1.00 48.11  ? 175  LEU E CG  1 
ATOM   9129  C CD1 . LEU E  1 175 ? 37.382  71.562 83.063  1.00 48.61  ? 175  LEU E CD1 1 
ATOM   9130  C CD2 . LEU E  1 175 ? 35.846  69.589 82.841  1.00 46.82  ? 175  LEU E CD2 1 
ATOM   9131  N N   . TRP E  1 176 ? 35.053  69.195 87.767  1.00 49.90  ? 176  TRP E N   1 
ATOM   9132  C CA  . TRP E  1 176 ? 35.467  68.966 89.150  1.00 51.10  ? 176  TRP E CA  1 
ATOM   9133  C C   . TRP E  1 176 ? 36.184  67.620 89.254  1.00 50.68  ? 176  TRP E C   1 
ATOM   9134  O O   . TRP E  1 176 ? 36.338  66.916 88.254  1.00 49.46  ? 176  TRP E O   1 
ATOM   9135  C CB  . TRP E  1 176 ? 34.263  69.030 90.101  1.00 51.78  ? 176  TRP E CB  1 
ATOM   9136  C CG  . TRP E  1 176 ? 33.270  67.927 89.911  1.00 50.79  ? 176  TRP E CG  1 
ATOM   9137  C CD1 . TRP E  1 176 ? 33.177  66.770 90.632  1.00 50.89  ? 176  TRP E CD1 1 
ATOM   9138  C CD2 . TRP E  1 176 ? 32.225  67.876 88.935  1.00 49.72  ? 176  TRP E CD2 1 
ATOM   9139  N NE1 . TRP E  1 176 ? 32.141  66.003 90.163  1.00 49.97  ? 176  TRP E NE1 1 
ATOM   9140  C CE2 . TRP E  1 176 ? 31.539  66.659 89.121  1.00 49.25  ? 176  TRP E CE2 1 
ATOM   9141  C CE3 . TRP E  1 176 ? 31.803  68.742 87.920  1.00 49.27  ? 176  TRP E CE3 1 
ATOM   9142  C CZ2 . TRP E  1 176 ? 30.452  66.285 88.329  1.00 48.38  ? 176  TRP E CZ2 1 
ATOM   9143  C CZ3 . TRP E  1 176 ? 30.724  68.371 87.134  1.00 48.40  ? 176  TRP E CZ3 1 
ATOM   9144  C CH2 . TRP E  1 176 ? 30.061  67.153 87.343  1.00 47.98  ? 176  TRP E CH2 1 
ATOM   9145  N N   . GLY E  1 177 ? 36.629  67.273 90.459  1.00 51.86  ? 177  GLY E N   1 
ATOM   9146  C CA  . GLY E  1 177 ? 37.371  66.033 90.662  1.00 51.80  ? 177  GLY E CA  1 
ATOM   9147  C C   . GLY E  1 177 ? 37.296  65.455 92.060  1.00 53.09  ? 177  GLY E C   1 
ATOM   9148  O O   . GLY E  1 177 ? 36.856  66.113 93.006  1.00 54.31  ? 177  GLY E O   1 
ATOM   9149  N N   . ILE E  1 178 ? 37.734  64.205 92.171  1.00 53.01  ? 178  ILE E N   1 
ATOM   9150  C CA  . ILE E  1 178 ? 37.846  63.506 93.448  1.00 54.39  ? 178  ILE E CA  1 
ATOM   9151  C C   . ILE E  1 178 ? 39.288  63.017 93.582  1.00 55.09  ? 178  ILE E C   1 
ATOM   9152  O O   . ILE E  1 178 ? 39.908  62.630 92.588  1.00 54.10  ? 178  ILE E O   1 
ATOM   9153  C CB  . ILE E  1 178 ? 36.852  62.316 93.545  1.00 53.84  ? 178  ILE E CB  1 
ATOM   9154  C CG1 . ILE E  1 178 ? 36.837  61.727 94.972  1.00 55.44  ? 178  ILE E CG1 1 
ATOM   9155  C CG2 . ILE E  1 178 ? 37.164  61.257 92.492  1.00 52.55  ? 178  ILE E CG2 1 
ATOM   9156  C CD1 . ILE E  1 178 ? 36.315  60.308 95.083  1.00 55.21  ? 178  ILE E CD1 1 
ATOM   9157  N N   . HIS E  1 179 ? 39.823  63.050 94.799  1.00 56.97  ? 179  HIS E N   1 
ATOM   9158  C CA  . HIS E  1 179 ? 41.155  62.509 95.062  1.00 57.97  ? 179  HIS E CA  1 
ATOM   9159  C C   . HIS E  1 179 ? 41.079  61.123 95.702  1.00 58.47  ? 179  HIS E C   1 
ATOM   9160  O O   . HIS E  1 179 ? 40.321  60.901 96.650  1.00 59.32  ? 179  HIS E O   1 
ATOM   9161  C CB  . HIS E  1 179 ? 41.967  63.443 95.959  1.00 59.99  ? 179  HIS E CB  1 
ATOM   9162  C CG  . HIS E  1 179 ? 43.305  62.890 96.339  1.00 61.33  ? 179  HIS E CG  1 
ATOM   9163  N ND1 . HIS E  1 179 ? 43.718  62.768 97.648  1.00 63.55  ? 179  HIS E ND1 1 
ATOM   9164  C CD2 . HIS E  1 179 ? 44.312  62.398 95.580  1.00 60.94  ? 179  HIS E CD2 1 
ATOM   9165  C CE1 . HIS E  1 179 ? 44.930  62.243 97.678  1.00 64.41  ? 179  HIS E CE1 1 
ATOM   9166  N NE2 . HIS E  1 179 ? 45.313  62.008 96.436  1.00 62.87  ? 179  HIS E NE2 1 
ATOM   9167  N N   . HIS E  1 180 ? 41.881  60.203 95.170  1.00 58.07  ? 180  HIS E N   1 
ATOM   9168  C CA  . HIS E  1 180 ? 41.988  58.847 95.691  1.00 58.70  ? 180  HIS E CA  1 
ATOM   9169  C C   . HIS E  1 180 ? 43.340  58.717 96.394  1.00 60.43  ? 180  HIS E C   1 
ATOM   9170  O O   . HIS E  1 180 ? 44.382  58.693 95.729  1.00 60.24  ? 180  HIS E O   1 
ATOM   9171  C CB  . HIS E  1 180 ? 41.900  57.835 94.548  1.00 57.23  ? 180  HIS E CB  1 
ATOM   9172  C CG  . HIS E  1 180 ? 40.617  57.894 93.774  1.00 55.63  ? 180  HIS E CG  1 
ATOM   9173  N ND1 . HIS E  1 180 ? 39.686  56.881 93.807  1.00 55.33  ? 180  HIS E ND1 1 
ATOM   9174  C CD2 . HIS E  1 180 ? 40.120  58.831 92.931  1.00 54.41  ? 180  HIS E CD2 1 
ATOM   9175  C CE1 . HIS E  1 180 ? 38.667  57.191 93.026  1.00 53.96  ? 180  HIS E CE1 1 
ATOM   9176  N NE2 . HIS E  1 180 ? 38.906  58.370 92.482  1.00 53.38  ? 180  HIS E NE2 1 
ATOM   9177  N N   . PRO E  1 181 ? 43.337  58.647 97.740  1.00 62.24  ? 181  PRO E N   1 
ATOM   9178  C CA  . PRO E  1 181 ? 44.587  58.575 98.497  1.00 64.17  ? 181  PRO E CA  1 
ATOM   9179  C C   . PRO E  1 181 ? 45.178  57.165 98.529  1.00 64.62  ? 181  PRO E C   1 
ATOM   9180  O O   . PRO E  1 181 ? 44.501  56.201 98.167  1.00 63.67  ? 181  PRO E O   1 
ATOM   9181  C CB  . PRO E  1 181 ? 44.163  59.014 99.898  1.00 66.07  ? 181  PRO E CB  1 
ATOM   9182  C CG  . PRO E  1 181 ? 42.750  58.553 100.012 1.00 65.28  ? 181  PRO E CG  1 
ATOM   9183  C CD  . PRO E  1 181 ? 42.159  58.610 98.628  1.00 62.79  ? 181  PRO E CD  1 
ATOM   9184  N N   . ASN E  1 182 ? 46.427  57.055 98.971  1.00 66.21  ? 182  ASN E N   1 
ATOM   9185  C CA  . ASN E  1 182 ? 47.158  55.784 98.944  1.00 66.86  ? 182  ASN E CA  1 
ATOM   9186  C C   . ASN E  1 182 ? 46.706  54.789 100.010 1.00 68.28  ? 182  ASN E C   1 
ATOM   9187  O O   . ASN E  1 182 ? 46.513  53.608 99.713  1.00 67.92  ? 182  ASN E O   1 
ATOM   9188  C CB  . ASN E  1 182 ? 48.661  56.034 99.079  1.00 68.35  ? 182  ASN E CB  1 
ATOM   9189  C CG  . ASN E  1 182 ? 49.243  56.719 97.861  1.00 66.96  ? 182  ASN E CG  1 
ATOM   9190  O OD1 . ASN E  1 182 ? 49.814  56.066 96.997  1.00 66.32  ? 182  ASN E OD1 1 
ATOM   9191  N ND2 . ASN E  1 182 ? 49.086  58.035 97.777  1.00 66.60  ? 182  ASN E ND2 1 
ATOM   9192  N N   . ASP E  1 183 ? 46.552  55.270 101.244 1.00 70.04  ? 183  ASP E N   1 
ATOM   9193  C CA  . ASP E  1 183 ? 46.120  54.436 102.376 1.00 71.72  ? 183  ASP E CA  1 
ATOM   9194  C C   . ASP E  1 183 ? 45.228  55.218 103.349 1.00 72.56  ? 183  ASP E C   1 
ATOM   9195  O O   . ASP E  1 183 ? 45.065  56.433 103.215 1.00 72.05  ? 183  ASP E O   1 
ATOM   9196  C CB  . ASP E  1 183 ? 47.338  53.846 103.108 1.00 74.16  ? 183  ASP E CB  1 
ATOM   9197  C CG  . ASP E  1 183 ? 48.390  54.895 103.455 1.00 75.53  ? 183  ASP E CG  1 
ATOM   9198  O OD1 . ASP E  1 183 ? 48.025  56.034 103.817 1.00 75.71  ? 183  ASP E OD1 1 
ATOM   9199  O OD2 . ASP E  1 183 ? 49.592  54.570 103.374 1.00 76.60  ? 183  ASP E OD2 1 
ATOM   9200  N N   . ALA E  1 184 ? 44.659  54.511 104.326 1.00 73.99  ? 184  ALA E N   1 
ATOM   9201  C CA  . ALA E  1 184 ? 43.785  55.123 105.339 1.00 75.10  ? 184  ALA E CA  1 
ATOM   9202  C C   . ALA E  1 184 ? 44.499  56.191 106.176 1.00 77.14  ? 184  ALA E C   1 
ATOM   9203  O O   . ALA E  1 184 ? 43.859  57.120 106.676 1.00 77.61  ? 184  ALA E O   1 
ATOM   9204  C CB  . ALA E  1 184 ? 43.195  54.051 106.245 1.00 76.58  ? 184  ALA E CB  1 
ATOM   9205  N N   . ALA E  1 185 ? 45.817  56.053 106.323 1.00 78.50  ? 185  ALA E N   1 
ATOM   9206  C CA  . ALA E  1 185 ? 46.636  57.032 107.042 1.00 80.61  ? 185  ALA E CA  1 
ATOM   9207  C C   . ALA E  1 185 ? 46.721  58.375 106.307 1.00 79.24  ? 185  ALA E C   1 
ATOM   9208  O O   . ALA E  1 185 ? 46.701  59.435 106.938 1.00 80.59  ? 185  ALA E O   1 
ATOM   9209  C CB  . ALA E  1 185 ? 48.032  56.472 107.281 1.00 82.38  ? 185  ALA E CB  1 
ATOM   9210  N N   . GLU E  1 186 ? 46.820  58.330 104.980 1.00 76.73  ? 186  GLU E N   1 
ATOM   9211  C CA  . GLU E  1 186 ? 46.852  59.552 104.173 1.00 75.36  ? 186  GLU E CA  1 
ATOM   9212  C C   . GLU E  1 186 ? 45.470  60.206 104.080 1.00 74.14  ? 186  GLU E C   1 
ATOM   9213  O O   . GLU E  1 186 ? 45.362  61.435 104.055 1.00 74.24  ? 186  GLU E O   1 
ATOM   9214  C CB  . GLU E  1 186 ? 47.396  59.269 102.771 1.00 73.24  ? 186  GLU E CB  1 
ATOM   9215  C CG  . GLU E  1 186 ? 47.738  60.529 101.988 1.00 72.32  ? 186  GLU E CG  1 
ATOM   9216  C CD  . GLU E  1 186 ? 48.475  60.241 100.695 1.00 70.73  ? 186  GLU E CD  1 
ATOM   9217  O OE1 . GLU E  1 186 ? 47.906  59.545 99.826  1.00 68.69  ? 186  GLU E OE1 1 
ATOM   9218  O OE2 . GLU E  1 186 ? 49.619  60.723 100.545 1.00 71.65  ? 186  GLU E OE2 1 
ATOM   9219  N N   . GLN E  1 187 ? 44.424  59.382 104.015 1.00 73.14  ? 187  GLN E N   1 
ATOM   9220  C CA  . GLN E  1 187 ? 43.039  59.865 104.036 1.00 72.30  ? 187  GLN E CA  1 
ATOM   9221  C C   . GLN E  1 187 ? 42.803  60.756 105.256 1.00 74.66  ? 187  GLN E C   1 
ATOM   9222  O O   . GLN E  1 187 ? 42.331  61.889 105.132 1.00 74.36  ? 187  GLN E O   1 
ATOM   9223  C CB  . GLN E  1 187 ? 42.056  58.680 104.037 1.00 71.51  ? 187  GLN E CB  1 
ATOM   9224  C CG  . GLN E  1 187 ? 40.597  59.030 104.332 1.00 71.19  ? 187  GLN E CG  1 
ATOM   9225  C CD  . GLN E  1 187 ? 39.978  59.955 103.292 1.00 69.05  ? 187  GLN E CD  1 
ATOM   9226  O OE1 . GLN E  1 187 ? 40.141  59.749 102.090 1.00 66.99  ? 187  GLN E OE1 1 
ATOM   9227  N NE2 . GLN E  1 187 ? 39.252  60.971 103.752 1.00 69.68  ? 187  GLN E NE2 1 
ATOM   9228  N N   . THR E  1 188 ? 43.142  60.233 106.431 1.00 77.19  ? 188  THR E N   1 
ATOM   9229  C CA  . THR E  1 188 ? 42.992  60.977 107.679 1.00 79.86  ? 188  THR E CA  1 
ATOM   9230  C C   . THR E  1 188 ? 43.936  62.185 107.727 1.00 81.04  ? 188  THR E C   1 
ATOM   9231  O O   . THR E  1 188 ? 43.551  63.260 108.188 1.00 82.10  ? 188  THR E O   1 
ATOM   9232  C CB  . THR E  1 188 ? 43.245  60.083 108.910 1.00 82.48  ? 188  THR E CB  1 
ATOM   9233  O OG1 . THR E  1 188 ? 44.536  59.470 108.802 1.00 83.15  ? 188  THR E OG1 1 
ATOM   9234  C CG2 . THR E  1 188 ? 42.174  58.996 109.025 1.00 81.79  ? 188  THR E CG2 1 
ATOM   9235  N N   . LYS E  1 189 ? 45.163  62.012 107.238 1.00 81.00  ? 189  LYS E N   1 
ATOM   9236  C CA  . LYS E  1 189 ? 46.130  63.109 107.198 1.00 82.16  ? 189  LYS E CA  1 
ATOM   9237  C C   . LYS E  1 189 ? 45.630  64.303 106.380 1.00 80.55  ? 189  LYS E C   1 
ATOM   9238  O O   . LYS E  1 189 ? 45.869  65.453 106.742 1.00 82.02  ? 189  LYS E O   1 
ATOM   9239  C CB  . LYS E  1 189 ? 47.469  62.634 106.628 1.00 82.06  ? 189  LYS E CB  1 
ATOM   9240  C CG  . LYS E  1 189 ? 48.459  63.769 106.406 1.00 83.04  ? 189  LYS E CG  1 
ATOM   9241  C CD  . LYS E  1 189 ? 49.812  63.288 105.918 1.00 83.27  ? 189  LYS E CD  1 
ATOM   9242  C CE  . LYS E  1 189 ? 50.783  64.455 105.817 1.00 84.62  ? 189  LYS E CE  1 
ATOM   9243  N NZ  . LYS E  1 189 ? 51.738  64.281 104.691 1.00 83.41  ? 189  LYS E NZ  1 
ATOM   9244  N N   . LEU E  1 190 ? 44.955  64.023 105.270 1.00 77.68  ? 190  LEU E N   1 
ATOM   9245  C CA  . LEU E  1 190 ? 44.491  65.073 104.367 1.00 76.05  ? 190  LEU E CA  1 
ATOM   9246  C C   . LEU E  1 190 ? 43.131  65.642 104.756 1.00 76.01  ? 190  LEU E C   1 
ATOM   9247  O O   . LEU E  1 190 ? 42.948  66.860 104.781 1.00 76.57  ? 190  LEU E O   1 
ATOM   9248  C CB  . LEU E  1 190 ? 44.419  64.539 102.934 1.00 73.17  ? 190  LEU E CB  1 
ATOM   9249  C CG  . LEU E  1 190 ? 45.746  64.507 102.181 1.00 72.93  ? 190  LEU E CG  1 
ATOM   9250  C CD1 . LEU E  1 190 ? 45.654  63.626 100.943 1.00 70.39  ? 190  LEU E CD1 1 
ATOM   9251  C CD2 . LEU E  1 190 ? 46.155  65.920 101.804 1.00 73.32  ? 190  LEU E CD2 1 
ATOM   9252  N N   . TYR E  1 191 ? 42.182  64.752 105.033 1.00 75.41  ? 191  TYR E N   1 
ATOM   9253  C CA  . TYR E  1 191 ? 40.781  65.136 105.232 1.00 75.06  ? 191  TYR E CA  1 
ATOM   9254  C C   . TYR E  1 191 ? 40.203  64.710 106.585 1.00 77.19  ? 191  TYR E C   1 
ATOM   9255  O O   . TYR E  1 191 ? 39.065  65.059 106.905 1.00 77.39  ? 191  TYR E O   1 
ATOM   9256  C CB  . TYR E  1 191 ? 39.931  64.541 104.104 1.00 72.15  ? 191  TYR E CB  1 
ATOM   9257  C CG  . TYR E  1 191 ? 40.596  64.617 102.743 1.00 70.03  ? 191  TYR E CG  1 
ATOM   9258  C CD1 . TYR E  1 191 ? 40.591  65.801 102.008 1.00 69.27  ? 191  TYR E CD1 1 
ATOM   9259  C CD2 . TYR E  1 191 ? 41.251  63.510 102.202 1.00 69.01  ? 191  TYR E CD2 1 
ATOM   9260  C CE1 . TYR E  1 191 ? 41.202  65.879 100.766 1.00 67.51  ? 191  TYR E CE1 1 
ATOM   9261  C CE2 . TYR E  1 191 ? 41.867  63.580 100.962 1.00 67.27  ? 191  TYR E CE2 1 
ATOM   9262  C CZ  . TYR E  1 191 ? 41.840  64.768 100.250 1.00 66.52  ? 191  TYR E CZ  1 
ATOM   9263  O OH  . TYR E  1 191 ? 42.448  64.850 99.022  1.00 64.95  ? 191  TYR E OH  1 
ATOM   9264  N N   . GLN E  1 192 ? 40.987  63.971 107.371 1.00 78.90  ? 192  GLN E N   1 
ATOM   9265  C CA  . GLN E  1 192 ? 40.567  63.428 108.674 1.00 81.13  ? 192  GLN E CA  1 
ATOM   9266  C C   . GLN E  1 192 ? 39.417  62.427 108.632 1.00 79.98  ? 192  GLN E C   1 
ATOM   9267  O O   . GLN E  1 192 ? 39.588  61.282 109.055 1.00 80.64  ? 192  GLN E O   1 
ATOM   9268  C CB  . GLN E  1 192 ? 40.280  64.540 109.689 1.00 83.67  ? 192  GLN E CB  1 
ATOM   9269  C CG  . GLN E  1 192 ? 41.446  64.750 110.645 1.00 86.67  ? 192  GLN E CG  1 
ATOM   9270  C CD  . GLN E  1 192 ? 41.119  65.576 111.871 1.00 89.74  ? 192  GLN E CD  1 
ATOM   9271  O OE1 . GLN E  1 192 ? 42.026  66.009 112.578 1.00 92.31  ? 192  GLN E OE1 1 
ATOM   9272  N NE2 . GLN E  1 192 ? 39.835  65.787 112.142 1.00 89.70  ? 192  GLN E NE2 1 
ATOM   9273  N N   . ASN E  1 193 ? 38.255  62.852 108.145 1.00 78.45  ? 193  ASN E N   1 
ATOM   9274  C CA  . ASN E  1 193 ? 37.087  61.972 108.059 1.00 77.40  ? 193  ASN E CA  1 
ATOM   9275  C C   . ASN E  1 193 ? 37.461  60.678 107.326 1.00 75.67  ? 193  ASN E C   1 
ATOM   9276  O O   . ASN E  1 193 ? 37.936  60.732 106.192 1.00 73.62  ? 193  ASN E O   1 
ATOM   9277  C CB  . ASN E  1 193 ? 35.922  62.670 107.344 1.00 75.69  ? 193  ASN E CB  1 
ATOM   9278  C CG  . ASN E  1 193 ? 35.631  64.057 107.903 1.00 77.28  ? 193  ASN E CG  1 
ATOM   9279  O OD1 . ASN E  1 193 ? 36.531  64.739 108.392 1.00 79.01  ? 193  ASN E OD1 1 
ATOM   9280  N ND2 . ASN E  1 193 ? 34.377  64.487 107.820 1.00 76.87  ? 193  ASN E ND2 1 
ATOM   9281  N N   . PRO E  1 194 ? 37.271  59.513 107.981 1.00 76.66  ? 194  PRO E N   1 
ATOM   9282  C CA  . PRO E  1 194 ? 37.724  58.248 107.390 1.00 75.47  ? 194  PRO E CA  1 
ATOM   9283  C C   . PRO E  1 194 ? 36.909  57.844 106.163 1.00 72.62  ? 194  PRO E C   1 
ATOM   9284  O O   . PRO E  1 194 ? 37.480  57.428 105.154 1.00 70.92  ? 194  PRO E O   1 
ATOM   9285  C CB  . PRO E  1 194 ? 37.538  57.236 108.528 1.00 77.68  ? 194  PRO E CB  1 
ATOM   9286  C CG  . PRO E  1 194 ? 36.470  57.813 109.392 1.00 79.06  ? 194  PRO E CG  1 
ATOM   9287  C CD  . PRO E  1 194 ? 36.551  59.308 109.253 1.00 78.97  ? 194  PRO E CD  1 
ATOM   9288  N N   . THR E  1 195 ? 35.588  57.974 106.263 1.00 72.24  ? 195  THR E N   1 
ATOM   9289  C CA  . THR E  1 195 ? 34.678  57.685 105.163 1.00 69.81  ? 195  THR E CA  1 
ATOM   9290  C C   . THR E  1 195 ? 34.181  59.019 104.615 1.00 68.70  ? 195  THR E C   1 
ATOM   9291  O O   . THR E  1 195 ? 33.653  59.840 105.367 1.00 70.05  ? 195  THR E O   1 
ATOM   9292  C CB  . THR E  1 195 ? 33.482  56.839 105.644 1.00 70.35  ? 195  THR E CB  1 
ATOM   9293  O OG1 . THR E  1 195 ? 33.952  55.776 106.481 1.00 72.11  ? 195  THR E OG1 1 
ATOM   9294  C CG2 . THR E  1 195 ? 32.722  56.253 104.465 1.00 68.06  ? 195  THR E CG2 1 
ATOM   9295  N N   . THR E  1 196 ? 34.364  59.240 103.313 1.00 66.42  ? 196  THR E N   1 
ATOM   9296  C CA  . THR E  1 196 ? 34.009  60.519 102.690 1.00 65.40  ? 196  THR E CA  1 
ATOM   9297  C C   . THR E  1 196 ? 33.248  60.333 101.380 1.00 62.98  ? 196  THR E C   1 
ATOM   9298  O O   . THR E  1 196 ? 33.205  59.235 100.824 1.00 61.97  ? 196  THR E O   1 
ATOM   9299  C CB  . THR E  1 196 ? 35.257  61.391 102.437 1.00 65.49  ? 196  THR E CB  1 
ATOM   9300  O OG1 . THR E  1 196 ? 36.181  60.686 101.602 1.00 64.25  ? 196  THR E OG1 1 
ATOM   9301  C CG2 . THR E  1 196 ? 35.935  61.748 103.754 1.00 68.11  ? 196  THR E CG2 1 
ATOM   9302  N N   . TYR E  1 197 ? 32.645  61.419 100.901 1.00 62.25  ? 197  TYR E N   1 
ATOM   9303  C CA  . TYR E  1 197 ? 31.847  61.390 99.680  1.00 60.19  ? 197  TYR E CA  1 
ATOM   9304  C C   . TYR E  1 197 ? 31.790  62.760 99.009  1.00 59.52  ? 197  TYR E C   1 
ATOM   9305  O O   . TYR E  1 197 ? 32.135  63.774 99.615  1.00 60.79  ? 197  TYR E O   1 
ATOM   9306  C CB  . TYR E  1 197 ? 30.421  60.935 99.996  1.00 60.42  ? 197  TYR E CB  1 
ATOM   9307  C CG  . TYR E  1 197 ? 29.616  61.974 100.745 1.00 61.74  ? 197  TYR E CG  1 
ATOM   9308  C CD1 . TYR E  1 197 ? 29.625  62.017 102.136 1.00 64.00  ? 197  TYR E CD1 1 
ATOM   9309  C CD2 . TYR E  1 197 ? 28.853  62.920 100.062 1.00 60.91  ? 197  TYR E CD2 1 
ATOM   9310  C CE1 . TYR E  1 197 ? 28.897  62.971 102.829 1.00 65.42  ? 197  TYR E CE1 1 
ATOM   9311  C CE2 . TYR E  1 197 ? 28.122  63.877 100.743 1.00 62.30  ? 197  TYR E CE2 1 
ATOM   9312  C CZ  . TYR E  1 197 ? 28.146  63.897 102.128 1.00 64.56  ? 197  TYR E CZ  1 
ATOM   9313  O OH  . TYR E  1 197 ? 27.422  64.845 102.812 1.00 66.11  ? 197  TYR E OH  1 
ATOM   9314  N N   . ILE E  1 198 ? 31.346  62.767 97.753  1.00 57.66  ? 198  ILE E N   1 
ATOM   9315  C CA  . ILE E  1 198 ? 31.044  63.998 97.021  1.00 57.00  ? 198  ILE E CA  1 
ATOM   9316  C C   . ILE E  1 198 ? 29.748  63.796 96.247  1.00 55.84  ? 198  ILE E C   1 
ATOM   9317  O O   . ILE E  1 198 ? 29.695  62.974 95.332  1.00 54.43  ? 198  ILE E O   1 
ATOM   9318  C CB  . ILE E  1 198 ? 32.144  64.377 96.005  1.00 55.89  ? 198  ILE E CB  1 
ATOM   9319  C CG1 . ILE E  1 198 ? 33.543  64.156 96.589  1.00 56.81  ? 198  ILE E CG1 1 
ATOM   9320  C CG2 . ILE E  1 198 ? 31.964  65.823 95.556  1.00 55.87  ? 198  ILE E CG2 1 
ATOM   9321  C CD1 . ILE E  1 198 ? 34.661  64.397 95.599  1.00 55.82  ? 198  ILE E CD1 1 
ATOM   9322  N N   . SER E  1 199 ? 28.710  64.544 96.610  1.00 56.59  ? 199  SER E N   1 
ATOM   9323  C CA  . SER E  1 199 ? 27.437  64.474 95.901  1.00 55.73  ? 199  SER E CA  1 
ATOM   9324  C C   . SER E  1 199 ? 27.251  65.712 95.033  1.00 55.15  ? 199  SER E C   1 
ATOM   9325  O O   . SER E  1 199 ? 27.335  66.838 95.522  1.00 56.26  ? 199  SER E O   1 
ATOM   9326  C CB  . SER E  1 199 ? 26.271  64.323 96.881  1.00 57.09  ? 199  SER E CB  1 
ATOM   9327  O OG  . SER E  1 199 ? 26.311  65.318 97.882  1.00 58.84  ? 199  SER E OG  1 
ATOM   9328  N N   . VAL E  1 200 ? 27.007  65.484 93.743  1.00 53.57  ? 200  VAL E N   1 
ATOM   9329  C CA  . VAL E  1 200 ? 26.793  66.554 92.771  1.00 52.98  ? 200  VAL E CA  1 
ATOM   9330  C C   . VAL E  1 200 ? 25.415  66.390 92.135  1.00 52.47  ? 200  VAL E C   1 
ATOM   9331  O O   . VAL E  1 200 ? 25.072  65.310 91.649  1.00 51.61  ? 200  VAL E O   1 
ATOM   9332  C CB  . VAL E  1 200 ? 27.859  66.537 91.657  1.00 51.65  ? 200  VAL E CB  1 
ATOM   9333  C CG1 . VAL E  1 200 ? 27.828  67.844 90.874  1.00 51.51  ? 200  VAL E CG1 1 
ATOM   9334  C CG2 . VAL E  1 200 ? 29.246  66.301 92.240  1.00 52.05  ? 200  VAL E CG2 1 
ATOM   9335  N N   . GLY E  1 201 ? 24.633  67.465 92.138  1.00 53.17  ? 201  GLY E N   1 
ATOM   9336  C CA  . GLY E  1 201 ? 23.280  67.435 91.595  1.00 52.98  ? 201  GLY E CA  1 
ATOM   9337  C C   . GLY E  1 201 ? 23.013  68.592 90.655  1.00 52.78  ? 201  GLY E C   1 
ATOM   9338  O O   . GLY E  1 201 ? 23.544  69.684 90.839  1.00 53.46  ? 201  GLY E O   1 
ATOM   9339  N N   . THR E  1 202 ? 22.213  68.330 89.626  1.00 51.98  ? 202  THR E N   1 
ATOM   9340  C CA  . THR E  1 202 ? 21.658  69.367 88.754  1.00 52.06  ? 202  THR E CA  1 
ATOM   9341  C C   . THR E  1 202 ? 20.207  68.967 88.489  1.00 52.28  ? 202  THR E C   1 
ATOM   9342  O O   . THR E  1 202 ? 19.648  68.156 89.234  1.00 52.73  ? 202  THR E O   1 
ATOM   9343  C CB  . THR E  1 202 ? 22.438  69.504 87.421  1.00 50.76  ? 202  THR E CB  1 
ATOM   9344  O OG1 . THR E  1 202 ? 22.213  68.353 86.594  1.00 49.58  ? 202  THR E OG1 1 
ATOM   9345  C CG2 . THR E  1 202 ? 23.931  69.674 87.676  1.00 50.51  ? 202  THR E CG2 1 
ATOM   9346  N N   . SER E  1 203 ? 19.590  69.523 87.450  1.00 52.11  ? 203  SER E N   1 
ATOM   9347  C CA  . SER E  1 203 ? 18.270  69.059 87.037  1.00 52.27  ? 203  SER E CA  1 
ATOM   9348  C C   . SER E  1 203 ? 18.352  67.622 86.527  1.00 51.09  ? 203  SER E C   1 
ATOM   9349  O O   . SER E  1 203 ? 17.430  66.836 86.732  1.00 51.44  ? 203  SER E O   1 
ATOM   9350  C CB  . SER E  1 203 ? 17.681  69.968 85.962  1.00 52.46  ? 203  SER E CB  1 
ATOM   9351  O OG  . SER E  1 203 ? 18.522  70.012 84.828  1.00 51.31  ? 203  SER E OG  1 
ATOM   9352  N N   . THR E  1 204 ? 19.465  67.280 85.885  1.00 49.87  ? 204  THR E N   1 
ATOM   9353  C CA  . THR E  1 204 ? 19.655  65.944 85.329  1.00 48.87  ? 204  THR E CA  1 
ATOM   9354  C C   . THR E  1 204 ? 20.637  65.116 86.156  1.00 48.58  ? 204  THR E C   1 
ATOM   9355  O O   . THR E  1 204 ? 20.381  63.943 86.424  1.00 48.56  ? 204  THR E O   1 
ATOM   9356  C CB  . THR E  1 204 ? 20.149  66.007 83.868  1.00 47.83  ? 204  THR E CB  1 
ATOM   9357  O OG1 . THR E  1 204 ? 21.444  66.620 83.815  1.00 47.39  ? 204  THR E OG1 1 
ATOM   9358  C CG2 . THR E  1 204 ? 19.176  66.799 83.007  1.00 48.27  ? 204  THR E CG2 1 
ATOM   9359  N N   . LEU E  1 205 ? 21.751  65.722 86.560  1.00 48.54  ? 205  LEU E N   1 
ATOM   9360  C CA  . LEU E  1 205 ? 22.819  64.985 87.236  1.00 48.33  ? 205  LEU E CA  1 
ATOM   9361  C C   . LEU E  1 205 ? 22.428  64.552 88.655  1.00 49.44  ? 205  LEU E C   1 
ATOM   9362  O O   . LEU E  1 205 ? 21.940  65.358 89.445  1.00 50.56  ? 205  LEU E O   1 
ATOM   9363  C CB  . LEU E  1 205 ? 24.101  65.824 87.276  1.00 48.19  ? 205  LEU E CB  1 
ATOM   9364  C CG  . LEU E  1 205 ? 25.388  65.128 87.742  1.00 47.91  ? 205  LEU E CG  1 
ATOM   9365  C CD1 . LEU E  1 205 ? 25.694  63.899 86.894  1.00 46.85  ? 205  LEU E CD1 1 
ATOM   9366  C CD2 . LEU E  1 205 ? 26.560  66.099 87.714  1.00 47.97  ? 205  LEU E CD2 1 
ATOM   9367  N N   . ASN E  1 206 ? 22.635  63.270 88.956  1.00 49.30  ? 206  ASN E N   1 
ATOM   9368  C CA  . ASN E  1 206 ? 22.448  62.729 90.305  1.00 50.42  ? 206  ASN E CA  1 
ATOM   9369  C C   . ASN E  1 206 ? 23.612  61.809 90.666  1.00 50.19  ? 206  ASN E C   1 
ATOM   9370  O O   . ASN E  1 206 ? 23.511  60.585 90.579  1.00 49.97  ? 206  ASN E O   1 
ATOM   9371  C CB  . ASN E  1 206 ? 21.118  61.977 90.418  1.00 50.93  ? 206  ASN E CB  1 
ATOM   9372  C CG  . ASN E  1 206 ? 20.869  61.434 91.819  1.00 52.24  ? 206  ASN E CG  1 
ATOM   9373  O OD1 . ASN E  1 206 ? 21.316  62.009 92.813  1.00 53.12  ? 206  ASN E OD1 1 
ATOM   9374  N ND2 . ASN E  1 206 ? 20.147  60.322 91.904  1.00 52.54  ? 206  ASN E ND2 1 
ATOM   9375  N N   . GLN E  1 207 ? 24.711  62.420 91.087  1.00 50.43  ? 207  GLN E N   1 
ATOM   9376  C CA  . GLN E  1 207 ? 25.968  61.716 91.287  1.00 50.26  ? 207  GLN E CA  1 
ATOM   9377  C C   . GLN E  1 207 ? 26.377  61.706 92.759  1.00 51.67  ? 207  GLN E C   1 
ATOM   9378  O O   . GLN E  1 207 ? 26.080  62.639 93.502  1.00 52.69  ? 207  GLN E O   1 
ATOM   9379  C CB  . GLN E  1 207 ? 27.045  62.377 90.417  1.00 49.40  ? 207  GLN E CB  1 
ATOM   9380  C CG  . GLN E  1 207 ? 28.489  62.110 90.818  1.00 49.57  ? 207  GLN E CG  1 
ATOM   9381  C CD  . GLN E  1 207 ? 29.478  62.863 89.945  1.00 48.87  ? 207  GLN E CD  1 
ATOM   9382  O OE1 . GLN E  1 207 ? 30.288  63.647 90.444  1.00 49.52  ? 207  GLN E OE1 1 
ATOM   9383  N NE2 . GLN E  1 207 ? 29.409  62.639 88.633  1.00 47.70  ? 207  GLN E NE2 1 
ATOM   9384  N N   . ARG E  1 208 ? 27.045  60.631 93.167  1.00 51.88  ? 208  ARG E N   1 
ATOM   9385  C CA  . ARG E  1 208 ? 27.674  60.547 94.481  1.00 53.28  ? 208  ARG E CA  1 
ATOM   9386  C C   . ARG E  1 208 ? 28.960  59.727 94.382  1.00 53.04  ? 208  ARG E C   1 
ATOM   9387  O O   . ARG E  1 208 ? 28.915  58.508 94.209  1.00 52.82  ? 208  ARG E O   1 
ATOM   9388  C CB  . ARG E  1 208 ? 26.728  59.922 95.508  1.00 54.56  ? 208  ARG E CB  1 
ATOM   9389  C CG  . ARG E  1 208 ? 27.195  60.105 96.945  1.00 56.32  ? 208  ARG E CG  1 
ATOM   9390  C CD  . ARG E  1 208 ? 26.475  59.165 97.901  1.00 57.61  ? 208  ARG E CD  1 
ATOM   9391  N NE  . ARG E  1 208 ? 26.633  59.578 99.295  1.00 59.57  ? 208  ARG E NE  1 
ATOM   9392  C CZ  . ARG E  1 208 ? 25.976  60.586 99.870  1.00 60.63  ? 208  ARG E CZ  1 
ATOM   9393  N NH1 . ARG E  1 208 ? 25.103  61.315 99.180  1.00 59.89  ? 208  ARG E NH1 1 
ATOM   9394  N NH2 . ARG E  1 208 ? 26.197  60.873 101.151 1.00 62.61  ? 208  ARG E NH2 1 
ATOM   9395  N N   . LEU E  1 209 ? 30.101  60.402 94.492  1.00 53.24  ? 209  LEU E N   1 
ATOM   9396  C CA  . LEU E  1 209 ? 31.408  59.756 94.369  1.00 53.11  ? 209  LEU E CA  1 
ATOM   9397  C C   . LEU E  1 209 ? 31.964  59.406 95.741  1.00 54.82  ? 209  LEU E C   1 
ATOM   9398  O O   . LEU E  1 209 ? 31.750  60.138 96.704  1.00 56.06  ? 209  LEU E O   1 
ATOM   9399  C CB  . LEU E  1 209 ? 32.392  60.679 93.649  1.00 52.47  ? 209  LEU E CB  1 
ATOM   9400  C CG  . LEU E  1 209 ? 31.974  61.177 92.264  1.00 50.98  ? 209  LEU E CG  1 
ATOM   9401  C CD1 . LEU E  1 209 ? 32.939  62.245 91.770  1.00 50.76  ? 209  LEU E CD1 1 
ATOM   9402  C CD2 . LEU E  1 209 ? 31.882  60.025 91.271  1.00 49.87  ? 209  LEU E CD2 1 
ATOM   9403  N N   . VAL E  1 210 ? 32.669  58.278 95.816  1.00 55.02  ? 210  VAL E N   1 
ATOM   9404  C CA  . VAL E  1 210 ? 33.389  57.872 97.025  1.00 56.75  ? 210  VAL E CA  1 
ATOM   9405  C C   . VAL E  1 210 ? 34.838  57.533 96.652  1.00 56.62  ? 210  VAL E C   1 
ATOM   9406  O O   . VAL E  1 210 ? 35.082  56.959 95.587  1.00 55.35  ? 210  VAL E O   1 
ATOM   9407  C CB  . VAL E  1 210 ? 32.714  56.672 97.744  1.00 57.68  ? 210  VAL E CB  1 
ATOM   9408  C CG1 . VAL E  1 210 ? 31.290  57.028 98.149  1.00 58.03  ? 210  VAL E CG1 1 
ATOM   9409  C CG2 . VAL E  1 210 ? 32.723  55.413 96.883  1.00 56.72  ? 210  VAL E CG2 1 
ATOM   9410  N N   . PRO E  1 211 ? 35.806  57.899 97.512  1.00 58.08  ? 211  PRO E N   1 
ATOM   9411  C CA  . PRO E  1 211 ? 37.199  57.576 97.181  1.00 58.14  ? 211  PRO E CA  1 
ATOM   9412  C C   . PRO E  1 211 ? 37.517  56.088 97.321  1.00 58.62  ? 211  PRO E C   1 
ATOM   9413  O O   . PRO E  1 211 ? 37.150  55.461 98.318  1.00 59.97  ? 211  PRO E O   1 
ATOM   9414  C CB  . PRO E  1 211 ? 38.015  58.393 98.194  1.00 59.85  ? 211  PRO E CB  1 
ATOM   9415  C CG  . PRO E  1 211 ? 37.066  59.390 98.765  1.00 60.35  ? 211  PRO E CG  1 
ATOM   9416  C CD  . PRO E  1 211 ? 35.716  58.747 98.713  1.00 59.77  ? 211  PRO E CD  1 
ATOM   9417  N N   . ARG E  1 212 ? 38.190  55.544 96.313  1.00 57.66  ? 212  ARG E N   1 
ATOM   9418  C CA  . ARG E  1 212 ? 38.624  54.151 96.301  1.00 58.16  ? 212  ARG E CA  1 
ATOM   9419  C C   . ARG E  1 212 ? 40.113  54.077 96.637  1.00 59.33  ? 212  ARG E C   1 
ATOM   9420  O O   . ARG E  1 212 ? 40.948  54.651 95.933  1.00 58.70  ? 212  ARG E O   1 
ATOM   9421  C CB  . ARG E  1 212 ? 38.365  53.521 94.929  1.00 56.52  ? 212  ARG E CB  1 
ATOM   9422  C CG  . ARG E  1 212 ? 36.931  53.667 94.435  1.00 55.36  ? 212  ARG E CG  1 
ATOM   9423  C CD  . ARG E  1 212 ? 36.681  52.877 93.156  1.00 54.12  ? 212  ARG E CD  1 
ATOM   9424  N NE  . ARG E  1 212 ? 37.708  53.109 92.137  1.00 53.33  ? 212  ARG E NE  1 
ATOM   9425  C CZ  . ARG E  1 212 ? 37.719  54.119 91.264  1.00 52.15  ? 212  ARG E CZ  1 
ATOM   9426  N NH1 . ARG E  1 212 ? 36.753  55.036 91.250  1.00 51.56  ? 212  ARG E NH1 1 
ATOM   9427  N NH2 . ARG E  1 212 ? 38.714  54.216 90.387  1.00 51.67  ? 212  ARG E NH2 1 
ATOM   9428  N N   . ILE E  1 213 ? 40.437  53.370 97.716  1.00 61.18  ? 213  ILE E N   1 
ATOM   9429  C CA  . ILE E  1 213 ? 41.812  53.241 98.180  1.00 62.65  ? 213  ILE E CA  1 
ATOM   9430  C C   . ILE E  1 213 ? 42.459  51.989 97.569  1.00 62.63  ? 213  ILE E C   1 
ATOM   9431  O O   . ILE E  1 213 ? 41.839  50.923 97.508  1.00 62.62  ? 213  ILE E O   1 
ATOM   9432  C CB  . ILE E  1 213 ? 41.873  53.164 99.735  1.00 65.01  ? 213  ILE E CB  1 
ATOM   9433  C CG1 . ILE E  1 213 ? 41.101  54.338 100.403 1.00 65.29  ? 213  ILE E CG1 1 
ATOM   9434  C CG2 . ILE E  1 213 ? 43.327  52.991 100.195 1.00 66.69  ? 213  ILE E CG2 1 
ATOM   9435  C CD1 . ILE E  1 213 ? 39.886  53.939 101.241 1.00 66.06  ? 213  ILE E CD1 1 
ATOM   9436  N N   . ALA E  1 214 ? 43.705  52.128 97.113  1.00 62.76  ? 214  ALA E N   1 
ATOM   9437  C CA  . ALA E  1 214 ? 44.471  51.003 96.572  1.00 63.02  ? 214  ALA E CA  1 
ATOM   9438  C C   . ALA E  1 214 ? 45.960  51.333 96.518  1.00 63.91  ? 214  ALA E C   1 
ATOM   9439  O O   . ALA E  1 214 ? 46.346  52.500 96.404  1.00 63.58  ? 214  ALA E O   1 
ATOM   9440  C CB  . ALA E  1 214 ? 43.968  50.631 95.184  1.00 61.07  ? 214  ALA E CB  1 
ATOM   9441  N N   . THR E  1 215 ? 46.791  50.297 96.605  1.00 65.20  ? 215  THR E N   1 
ATOM   9442  C CA  . THR E  1 215 ? 48.233  50.446 96.439  1.00 66.14  ? 215  THR E CA  1 
ATOM   9443  C C   . THR E  1 215 ? 48.522  50.500 94.946  1.00 64.46  ? 215  THR E C   1 
ATOM   9444  O O   . THR E  1 215 ? 48.263  49.538 94.226  1.00 63.87  ? 215  THR E O   1 
ATOM   9445  C CB  . THR E  1 215 ? 49.006  49.274 97.076  1.00 68.30  ? 215  THR E CB  1 
ATOM   9446  O OG1 . THR E  1 215 ? 48.576  49.091 98.430  1.00 69.90  ? 215  THR E OG1 1 
ATOM   9447  C CG2 . THR E  1 215 ? 50.513  49.535 97.050  1.00 69.56  ? 215  THR E CG2 1 
ATOM   9448  N N   . ARG E  1 216 ? 49.045  51.631 94.483  1.00 63.86  ? 216  ARG E N   1 
ATOM   9449  C CA  . ARG E  1 216 ? 49.241  51.856 93.054  1.00 62.28  ? 216  ARG E CA  1 
ATOM   9450  C C   . ARG E  1 216 ? 50.697  52.173 92.751  1.00 63.25  ? 216  ARG E C   1 
ATOM   9451  O O   . ARG E  1 216 ? 51.442  52.615 93.629  1.00 64.82  ? 216  ARG E O   1 
ATOM   9452  C CB  . ARG E  1 216 ? 48.348  53.003 92.578  1.00 60.45  ? 216  ARG E CB  1 
ATOM   9453  C CG  . ARG E  1 216 ? 46.864  52.768 92.813  1.00 59.54  ? 216  ARG E CG  1 
ATOM   9454  C CD  . ARG E  1 216 ? 46.054  54.029 92.566  1.00 58.19  ? 216  ARG E CD  1 
ATOM   9455  N NE  . ARG E  1 216 ? 46.077  54.942 93.712  1.00 59.27  ? 216  ARG E NE  1 
ATOM   9456  C CZ  . ARG E  1 216 ? 45.142  55.020 94.665  1.00 59.70  ? 216  ARG E CZ  1 
ATOM   9457  N NH1 . ARG E  1 216 ? 44.064  54.239 94.655  1.00 59.12  ? 216  ARG E NH1 1 
ATOM   9458  N NH2 . ARG E  1 216 ? 45.285  55.896 95.650  1.00 60.88  ? 216  ARG E NH2 1 
ATOM   9459  N N   . SER E  1 217 ? 51.094  51.934 91.504  1.00 62.46  ? 217  SER E N   1 
ATOM   9460  C CA  . SER E  1 217 ? 52.444  52.243 91.049  1.00 63.29  ? 217  SER E CA  1 
ATOM   9461  C C   . SER E  1 217 ? 52.621  53.753 90.948  1.00 62.89  ? 217  SER E C   1 
ATOM   9462  O O   . SER E  1 217 ? 51.659  54.484 90.711  1.00 61.42  ? 217  SER E O   1 
ATOM   9463  C CB  . SER E  1 217 ? 52.713  51.593 89.691  1.00 62.51  ? 217  SER E CB  1 
ATOM   9464  O OG  . SER E  1 217 ? 52.340  50.225 89.699  1.00 62.83  ? 217  SER E OG  1 
ATOM   9465  N N   . LYS E  1 218 ? 53.852  54.216 91.141  1.00 64.41  ? 218  LYS E N   1 
ATOM   9466  C CA  . LYS E  1 218 ? 54.146  55.638 91.032  1.00 64.36  ? 218  LYS E CA  1 
ATOM   9467  C C   . LYS E  1 218 ? 54.109  56.063 89.575  1.00 62.67  ? 218  LYS E C   1 
ATOM   9468  O O   . LYS E  1 218 ? 54.830  55.521 88.740  1.00 62.83  ? 218  LYS E O   1 
ATOM   9469  C CB  . LYS E  1 218 ? 55.511  55.980 91.635  1.00 66.69  ? 218  LYS E CB  1 
ATOM   9470  C CG  . LYS E  1 218 ? 55.476  56.260 93.127  1.00 68.52  ? 218  LYS E CG  1 
ATOM   9471  C CD  . LYS E  1 218 ? 56.831  56.747 93.614  1.00 70.91  ? 218  LYS E CD  1 
ATOM   9472  C CE  . LYS E  1 218 ? 56.866  56.923 95.124  1.00 73.10  ? 218  LYS E CE  1 
ATOM   9473  N NZ  . LYS E  1 218 ? 56.962  55.624 95.848  1.00 74.46  ? 218  LYS E NZ  1 
ATOM   9474  N N   . VAL E  1 219 ? 53.240  57.020 89.279  1.00 61.18  ? 219  VAL E N   1 
ATOM   9475  C CA  . VAL E  1 219 ? 53.207  57.675 87.986  1.00 59.78  ? 219  VAL E CA  1 
ATOM   9476  C C   . VAL E  1 219 ? 53.502  59.148 88.254  1.00 60.20  ? 219  VAL E C   1 
ATOM   9477  O O   . VAL E  1 219 ? 52.879  59.753 89.123  1.00 60.33  ? 219  VAL E O   1 
ATOM   9478  C CB  . VAL E  1 219 ? 51.833  57.487 87.317  1.00 57.82  ? 219  VAL E CB  1 
ATOM   9479  C CG1 . VAL E  1 219 ? 51.732  58.297 86.031  1.00 56.60  ? 219  VAL E CG1 1 
ATOM   9480  C CG2 . VAL E  1 219 ? 51.585  56.008 87.043  1.00 57.62  ? 219  VAL E CG2 1 
ATOM   9481  N N   . ASN E  1 220 ? 54.464  59.713 87.529  1.00 60.56  ? 220  ASN E N   1 
ATOM   9482  C CA  . ASN E  1 220 ? 54.949  61.075 87.801  1.00 61.41  ? 220  ASN E CA  1 
ATOM   9483  C C   . ASN E  1 220 ? 55.347  61.283 89.270  1.00 63.26  ? 220  ASN E C   1 
ATOM   9484  O O   . ASN E  1 220 ? 55.121  62.352 89.844  1.00 63.73  ? 220  ASN E O   1 
ATOM   9485  C CB  . ASN E  1 220 ? 53.910  62.123 87.366  1.00 60.01  ? 220  ASN E CB  1 
ATOM   9486  C CG  . ASN E  1 220 ? 53.994  62.455 85.888  1.00 58.93  ? 220  ASN E CG  1 
ATOM   9487  O OD1 . ASN E  1 220 ? 54.473  61.656 85.078  1.00 58.74  ? 220  ASN E OD1 1 
ATOM   9488  N ND2 . ASN E  1 220 ? 53.521  63.644 85.526  1.00 58.38  ? 220  ASN E ND2 1 
ATOM   9489  N N   . GLY E  1 221 ? 55.939  60.250 89.867  1.00 64.45  ? 221  GLY E N   1 
ATOM   9490  C CA  . GLY E  1 221 ? 56.419  60.310 91.246  1.00 66.52  ? 221  GLY E CA  1 
ATOM   9491  C C   . GLY E  1 221 ? 55.345  60.240 92.320  1.00 66.44  ? 221  GLY E C   1 
ATOM   9492  O O   . GLY E  1 221 ? 55.627  60.502 93.488  1.00 68.23  ? 221  GLY E O   1 
ATOM   9493  N N   . GLN E  1 222 ? 54.119  59.886 91.937  1.00 64.53  ? 222  GLN E N   1 
ATOM   9494  C CA  . GLN E  1 222 ? 53.002  59.805 92.881  1.00 64.40  ? 222  GLN E CA  1 
ATOM   9495  C C   . GLN E  1 222 ? 52.153  58.568 92.620  1.00 63.03  ? 222  GLN E C   1 
ATOM   9496  O O   . GLN E  1 222 ? 51.891  58.216 91.469  1.00 61.44  ? 222  GLN E O   1 
ATOM   9497  C CB  . GLN E  1 222 ? 52.126  61.059 92.790  1.00 63.58  ? 222  GLN E CB  1 
ATOM   9498  C CG  . GLN E  1 222 ? 52.836  62.361 93.149  1.00 65.11  ? 222  GLN E CG  1 
ATOM   9499  C CD  . GLN E  1 222 ? 53.399  62.367 94.563  1.00 67.69  ? 222  GLN E CD  1 
ATOM   9500  O OE1 . GLN E  1 222 ? 52.835  61.763 95.473  1.00 68.27  ? 222  GLN E OE1 1 
ATOM   9501  N NE2 . GLN E  1 222 ? 54.520  63.056 94.751  1.00 69.47  ? 222  GLN E NE2 1 
ATOM   9502  N N   . SER E  1 223 ? 51.727  57.918 93.701  1.00 63.79  ? 223  SER E N   1 
ATOM   9503  C CA  . SER E  1 223 ? 50.868  56.736 93.621  1.00 62.83  ? 223  SER E CA  1 
ATOM   9504  C C   . SER E  1 223 ? 49.398  57.061 93.932  1.00 61.67  ? 223  SER E C   1 
ATOM   9505  O O   . SER E  1 223 ? 48.538  56.183 93.862  1.00 60.91  ? 223  SER E O   1 
ATOM   9506  C CB  . SER E  1 223 ? 51.396  55.644 94.554  1.00 64.70  ? 223  SER E CB  1 
ATOM   9507  O OG  . SER E  1 223 ? 52.559  55.043 94.013  1.00 65.36  ? 223  SER E OG  1 
ATOM   9508  N N   . GLY E  1 224 ? 49.119  58.321 94.267  1.00 61.65  ? 224  GLY E N   1 
ATOM   9509  C CA  . GLY E  1 224 ? 47.746  58.806 94.410  1.00 60.54  ? 224  GLY E CA  1 
ATOM   9510  C C   . GLY E  1 224 ? 47.124  59.089 93.053  1.00 58.29  ? 224  GLY E C   1 
ATOM   9511  O O   . GLY E  1 224 ? 47.838  59.270 92.060  1.00 57.72  ? 224  GLY E O   1 
ATOM   9512  N N   . ARG E  1 225 ? 45.791  59.129 93.008  1.00 57.10  ? 225  ARG E N   1 
ATOM   9513  C CA  . ARG E  1 225 ? 45.060  59.339 91.751  1.00 55.08  ? 225  ARG E CA  1 
ATOM   9514  C C   . ARG E  1 225 ? 43.997  60.432 91.864  1.00 54.46  ? 225  ARG E C   1 
ATOM   9515  O O   . ARG E  1 225 ? 43.430  60.658 92.933  1.00 55.33  ? 225  ARG E O   1 
ATOM   9516  C CB  . ARG E  1 225 ? 44.394  58.037 91.294  1.00 54.16  ? 225  ARG E CB  1 
ATOM   9517  C CG  . ARG E  1 225 ? 45.360  56.906 90.983  1.00 54.63  ? 225  ARG E CG  1 
ATOM   9518  C CD  . ARG E  1 225 ? 46.120  57.142 89.688  1.00 53.86  ? 225  ARG E CD  1 
ATOM   9519  N NE  . ARG E  1 225 ? 46.991  56.012 89.356  1.00 54.41  ? 225  ARG E NE  1 
ATOM   9520  C CZ  . ARG E  1 225 ? 48.274  55.890 89.707  1.00 55.80  ? 225  ARG E CZ  1 
ATOM   9521  N NH1 . ARG E  1 225 ? 48.895  56.830 90.417  1.00 56.86  ? 225  ARG E NH1 1 
ATOM   9522  N NH2 . ARG E  1 225 ? 48.950  54.806 89.339  1.00 56.29  ? 225  ARG E NH2 1 
ATOM   9523  N N   . MET E  1 226 ? 43.740  61.100 90.743  1.00 53.06  ? 226  MET E N   1 
ATOM   9524  C CA  . MET E  1 226 ? 42.682  62.097 90.640  1.00 52.39  ? 226  MET E CA  1 
ATOM   9525  C C   . MET E  1 226 ? 41.741  61.685 89.522  1.00 50.61  ? 226  MET E C   1 
ATOM   9526  O O   . MET E  1 226 ? 42.187  61.407 88.412  1.00 49.82  ? 226  MET E O   1 
ATOM   9527  C CB  . MET E  1 226 ? 43.272  63.469 90.323  1.00 52.73  ? 226  MET E CB  1 
ATOM   9528  C CG  . MET E  1 226 ? 44.039  64.097 91.475  1.00 54.63  ? 226  MET E CG  1 
ATOM   9529  S SD  . MET E  1 226 ? 42.973  64.888 92.695  1.00 55.62  ? 226  MET E SD  1 
ATOM   9530  C CE  . MET E  1 226 ? 44.205  65.590 93.787  1.00 58.04  ? 226  MET E CE  1 
ATOM   9531  N N   . GLU E  1 227 ? 40.444  61.645 89.809  1.00 61.27  ? 227  GLU E N   1 
ATOM   9532  C CA  . GLU E  1 227 ? 39.454  61.259 88.810  1.00 58.91  ? 227  GLU E CA  1 
ATOM   9533  C C   . GLU E  1 227 ? 38.555  62.449 88.509  1.00 58.23  ? 227  GLU E C   1 
ATOM   9534  O O   . GLU E  1 227 ? 37.809  62.906 89.375  1.00 59.23  ? 227  GLU E O   1 
ATOM   9535  C CB  . GLU E  1 227 ? 38.641  60.064 89.303  1.00 59.05  ? 227  GLU E CB  1 
ATOM   9536  C CG  . GLU E  1 227 ? 37.965  59.278 88.192  1.00 57.06  ? 227  GLU E CG  1 
ATOM   9537  C CD  . GLU E  1 227 ? 37.357  57.976 88.676  1.00 57.62  ? 227  GLU E CD  1 
ATOM   9538  O OE1 . GLU E  1 227 ? 37.568  57.604 89.852  1.00 59.51  ? 227  GLU E OE1 1 
ATOM   9539  O OE2 . GLU E  1 227 ? 36.668  57.317 87.871  1.00 56.40  ? 227  GLU E OE2 1 
ATOM   9540  N N   . PHE E  1 228 ? 38.633  62.950 87.278  1.00 56.67  ? 228  PHE E N   1 
ATOM   9541  C CA  . PHE E  1 228 ? 37.952  64.188 86.914  1.00 56.34  ? 228  PHE E CA  1 
ATOM   9542  C C   . PHE E  1 228 ? 36.652  63.924 86.171  1.00 54.79  ? 228  PHE E C   1 
ATOM   9543  O O   . PHE E  1 228 ? 36.589  63.072 85.286  1.00 53.47  ? 228  PHE E O   1 
ATOM   9544  C CB  . PHE E  1 228 ? 38.883  65.082 86.097  1.00 56.22  ? 228  PHE E CB  1 
ATOM   9545  C CG  . PHE E  1 228 ? 40.060  65.583 86.882  1.00 58.18  ? 228  PHE E CG  1 
ATOM   9546  C CD1 . PHE E  1 228 ? 39.941  66.704 87.689  1.00 59.97  ? 228  PHE E CD1 1 
ATOM   9547  C CD2 . PHE E  1 228 ? 41.276  64.914 86.842  1.00 58.50  ? 228  PHE E CD2 1 
ATOM   9548  C CE1 . PHE E  1 228 ? 41.020  67.164 88.427  1.00 62.17  ? 228  PHE E CE1 1 
ATOM   9549  C CE2 . PHE E  1 228 ? 42.359  65.366 87.577  1.00 60.65  ? 228  PHE E CE2 1 
ATOM   9550  C CZ  . PHE E  1 228 ? 42.231  66.493 88.372  1.00 62.56  ? 228  PHE E CZ  1 
ATOM   9551  N N   . PHE E  1 229 ? 35.619  64.665 86.560  1.00 55.22  ? 229  PHE E N   1 
ATOM   9552  C CA  . PHE E  1 229 ? 34.283  64.529 85.996  1.00 54.24  ? 229  PHE E CA  1 
ATOM   9553  C C   . PHE E  1 229 ? 33.810  65.872 85.460  1.00 54.27  ? 229  PHE E C   1 
ATOM   9554  O O   . PHE E  1 229 ? 34.342  66.923 85.824  1.00 55.32  ? 229  PHE E O   1 
ATOM   9555  C CB  . PHE E  1 229 ? 33.310  64.022 87.061  1.00 55.01  ? 229  PHE E CB  1 
ATOM   9556  C CG  . PHE E  1 229 ? 33.595  62.622 87.522  1.00 55.16  ? 229  PHE E CG  1 
ATOM   9557  C CD1 . PHE E  1 229 ? 34.616  62.371 88.431  1.00 56.39  ? 229  PHE E CD1 1 
ATOM   9558  C CD2 . PHE E  1 229 ? 32.844  61.554 87.050  1.00 54.40  ? 229  PHE E CD2 1 
ATOM   9559  C CE1 . PHE E  1 229 ? 34.883  61.080 88.858  1.00 56.82  ? 229  PHE E CE1 1 
ATOM   9560  C CE2 . PHE E  1 229 ? 33.106  60.261 87.474  1.00 54.83  ? 229  PHE E CE2 1 
ATOM   9561  C CZ  . PHE E  1 229 ? 34.127  60.024 88.379  1.00 56.02  ? 229  PHE E CZ  1 
ATOM   9562  N N   . TRP E  1 230 ? 32.805  65.827 84.591  1.00 53.39  ? 230  TRP E N   1 
ATOM   9563  C CA  . TRP E  1 230 ? 32.298  67.031 83.952  1.00 53.56  ? 230  TRP E CA  1 
ATOM   9564  C C   . TRP E  1 230 ? 30.811  66.949 83.661  1.00 53.38  ? 230  TRP E C   1 
ATOM   9565  O O   . TRP E  1 230 ? 30.226  65.869 83.645  1.00 52.85  ? 230  TRP E O   1 
ATOM   9566  C CB  . TRP E  1 230 ? 33.061  67.289 82.654  1.00 52.83  ? 230  TRP E CB  1 
ATOM   9567  C CG  . TRP E  1 230 ? 32.907  66.214 81.615  1.00 51.50  ? 230  TRP E CG  1 
ATOM   9568  C CD1 . TRP E  1 230 ? 33.702  65.117 81.449  1.00 50.76  ? 230  TRP E CD1 1 
ATOM   9569  C CD2 . TRP E  1 230 ? 31.909  66.144 80.589  1.00 51.05  ? 230  TRP E CD2 1 
ATOM   9570  N NE1 . TRP E  1 230 ? 33.259  64.364 80.389  1.00 49.83  ? 230  TRP E NE1 1 
ATOM   9571  C CE2 . TRP E  1 230 ? 32.158  64.971 79.844  1.00 50.06  ? 230  TRP E CE2 1 
ATOM   9572  C CE3 . TRP E  1 230 ? 30.824  66.955 80.231  1.00 51.62  ? 230  TRP E CE3 1 
ATOM   9573  C CZ2 . TRP E  1 230 ? 31.366  64.591 78.757  1.00 49.73  ? 230  TRP E CZ2 1 
ATOM   9574  C CZ3 . TRP E  1 230 ? 30.036  66.576 79.151  1.00 51.30  ? 230  TRP E CZ3 1 
ATOM   9575  C CH2 . TRP E  1 230 ? 30.312  65.405 78.426  1.00 50.40  ? 230  TRP E CH2 1 
ATOM   9576  N N   . THR E  1 231 ? 30.210  68.113 83.442  1.00 54.08  ? 231  THR E N   1 
ATOM   9577  C CA  . THR E  1 231 ? 28.827  68.202 82.997  1.00 54.17  ? 231  THR E CA  1 
ATOM   9578  C C   . THR E  1 231 ? 28.619  69.491 82.211  1.00 54.83  ? 231  THR E C   1 
ATOM   9579  O O   . THR E  1 231 ? 29.438  70.408 82.283  1.00 55.44  ? 231  THR E O   1 
ATOM   9580  C CB  . THR E  1 231 ? 27.849  68.161 84.187  1.00 55.02  ? 231  THR E CB  1 
ATOM   9581  O OG1 . THR E  1 231 ? 26.518  67.946 83.708  1.00 55.06  ? 231  THR E OG1 1 
ATOM   9582  C CG2 . THR E  1 231 ? 27.898  69.458 84.992  1.00 56.36  ? 231  THR E CG2 1 
ATOM   9583  N N   . ILE E  1 232 ? 27.536  69.543 81.443  1.00 54.99  ? 232  ILE E N   1 
ATOM   9584  C CA  . ILE E  1 232 ? 27.090  70.788 80.828  1.00 56.08  ? 232  ILE E CA  1 
ATOM   9585  C C   . ILE E  1 232 ? 25.916  71.296 81.652  1.00 57.26  ? 232  ILE E C   1 
ATOM   9586  O O   . ILE E  1 232 ? 24.887  70.632 81.758  1.00 57.22  ? 232  ILE E O   1 
ATOM   9587  C CB  . ILE E  1 232 ? 26.713  70.612 79.337  1.00 55.84  ? 232  ILE E CB  1 
ATOM   9588  C CG1 . ILE E  1 232 ? 27.928  70.884 78.444  1.00 55.47  ? 232  ILE E CG1 1 
ATOM   9589  C CG2 . ILE E  1 232 ? 25.615  71.580 78.916  1.00 57.27  ? 232  ILE E CG2 1 
ATOM   9590  C CD1 . ILE E  1 232 ? 29.160  70.082 78.797  1.00 54.29  ? 232  ILE E CD1 1 
ATOM   9591  N N   . LEU E  1 233 ? 26.094  72.468 82.249  1.00 58.54  ? 233  LEU E N   1 
ATOM   9592  C CA  . LEU E  1 233 ? 25.059  73.090 83.058  1.00 59.86  ? 233  LEU E CA  1 
ATOM   9593  C C   . LEU E  1 233 ? 24.261  74.037 82.174  1.00 61.06  ? 233  LEU E C   1 
ATOM   9594  O O   . LEU E  1 233 ? 24.796  75.021 81.664  1.00 61.89  ? 233  LEU E O   1 
ATOM   9595  C CB  . LEU E  1 233 ? 25.692  73.843 84.234  1.00 60.89  ? 233  LEU E CB  1 
ATOM   9596  C CG  . LEU E  1 233 ? 24.760  74.432 85.300  1.00 62.27  ? 233  LEU E CG  1 
ATOM   9597  C CD1 . LEU E  1 233 ? 23.977  73.341 86.019  1.00 61.69  ? 233  LEU E CD1 1 
ATOM   9598  C CD2 . LEU E  1 233 ? 25.564  75.259 86.293  1.00 63.57  ? 233  LEU E CD2 1 
ATOM   9599  N N   . LYS E  1 234 ? 22.981  73.732 81.988  1.00 61.44  ? 234  LYS E N   1 
ATOM   9600  C CA  . LYS E  1 234 ? 22.125  74.524 81.111  1.00 62.86  ? 234  LYS E CA  1 
ATOM   9601  C C   . LYS E  1 234 ? 21.739  75.838 81.786  1.00 64.75  ? 234  LYS E C   1 
ATOM   9602  O O   . LYS E  1 234 ? 21.817  75.946 83.013  1.00 64.95  ? 234  LYS E O   1 
ATOM   9603  C CB  . LYS E  1 234 ? 20.884  73.718 80.719  1.00 62.87  ? 234  LYS E CB  1 
ATOM   9604  C CG  . LYS E  1 234 ? 21.228  72.446 79.957  1.00 61.45  ? 234  LYS E CG  1 
ATOM   9605  C CD  . LYS E  1 234 ? 20.014  71.810 79.302  1.00 62.04  ? 234  LYS E CD  1 
ATOM   9606  C CE  . LYS E  1 234 ? 20.435  70.700 78.352  1.00 61.00  ? 234  LYS E CE  1 
ATOM   9607  N NZ  . LYS E  1 234 ? 19.294  70.155 77.568  1.00 62.01  ? 234  LYS E NZ  1 
ATOM   9608  N N   . PRO E  1 235 ? 21.333  76.851 80.992  1.00 66.41  ? 235  PRO E N   1 
ATOM   9609  C CA  . PRO E  1 235 ? 21.006  78.142 81.602  1.00 68.41  ? 235  PRO E CA  1 
ATOM   9610  C C   . PRO E  1 235 ? 19.838  78.043 82.576  1.00 69.05  ? 235  PRO E C   1 
ATOM   9611  O O   . PRO E  1 235 ? 18.925  77.240 82.368  1.00 68.64  ? 235  PRO E O   1 
ATOM   9612  C CB  . PRO E  1 235 ? 20.627  79.034 80.408  1.00 70.06  ? 235  PRO E CB  1 
ATOM   9613  C CG  . PRO E  1 235 ? 21.008  78.290 79.181  1.00 68.94  ? 235  PRO E CG  1 
ATOM   9614  C CD  . PRO E  1 235 ? 21.078  76.840 79.540  1.00 66.78  ? 235  PRO E CD  1 
ATOM   9615  N N   . ASN E  1 236 ? 19.883  78.848 83.636  1.00 70.29  ? 236  ASN E N   1 
ATOM   9616  C CA  . ASN E  1 236 ? 18.808  78.910 84.622  1.00 71.18  ? 236  ASN E CA  1 
ATOM   9617  C C   . ASN E  1 236 ? 18.724  77.640 85.481  1.00 69.65  ? 236  ASN E C   1 
ATOM   9618  O O   . ASN E  1 236 ? 17.728  77.423 86.170  1.00 70.22  ? 236  ASN E O   1 
ATOM   9619  C CB  . ASN E  1 236 ? 17.462  79.176 83.917  1.00 72.50  ? 236  ASN E CB  1 
ATOM   9620  C CG  . ASN E  1 236 ? 16.642  80.268 84.585  1.00 74.75  ? 236  ASN E CG  1 
ATOM   9621  O OD1 . ASN E  1 236 ? 16.971  80.746 85.668  1.00 75.49  ? 236  ASN E OD1 1 
ATOM   9622  N ND2 . ASN E  1 236 ? 15.567  80.677 83.923  1.00 76.25  ? 236  ASN E ND2 1 
ATOM   9623  N N   . ASP E  1 237 ? 19.773  76.816 85.441  1.00 67.97  ? 237  ASP E N   1 
ATOM   9624  C CA  . ASP E  1 237 ? 19.851  75.597 86.246  1.00 66.71  ? 237  ASP E CA  1 
ATOM   9625  C C   . ASP E  1 237 ? 21.002  75.736 87.237  1.00 66.67  ? 237  ASP E C   1 
ATOM   9626  O O   . ASP E  1 237 ? 22.021  76.364 86.939  1.00 66.87  ? 237  ASP E O   1 
ATOM   9627  C CB  . ASP E  1 237 ? 20.065  74.368 85.354  1.00 65.02  ? 237  ASP E CB  1 
ATOM   9628  C CG  . ASP E  1 237 ? 19.966  73.046 86.121  1.00 64.08  ? 237  ASP E CG  1 
ATOM   9629  O OD1 . ASP E  1 237 ? 19.279  72.992 87.165  1.00 64.82  ? 237  ASP E OD1 1 
ATOM   9630  O OD2 . ASP E  1 237 ? 20.575  72.050 85.667  1.00 62.70  ? 237  ASP E OD2 1 
ATOM   9631  N N   . ALA E  1 238 ? 20.828  75.146 88.415  1.00 66.67  ? 238  ALA E N   1 
ATOM   9632  C CA  . ALA E  1 238 ? 21.827  75.218 89.470  1.00 67.03  ? 238  ALA E CA  1 
ATOM   9633  C C   . ALA E  1 238 ? 22.535  73.876 89.642  1.00 65.56  ? 238  ALA E C   1 
ATOM   9634  O O   . ALA E  1 238 ? 21.912  72.816 89.525  1.00 64.70  ? 238  ALA E O   1 
ATOM   9635  C CB  . ALA E  1 238 ? 21.174  75.643 90.776  1.00 68.60  ? 238  ALA E CB  1 
ATOM   9636  N N   . ILE E  1 239 ? 23.839  73.931 89.905  1.00 65.48  ? 239  ILE E N   1 
ATOM   9637  C CA  . ILE E  1 239 ? 24.607  72.747 90.296  1.00 64.55  ? 239  ILE E CA  1 
ATOM   9638  C C   . ILE E  1 239 ? 24.881  72.803 91.804  1.00 66.01  ? 239  ILE E C   1 
ATOM   9639  O O   . ILE E  1 239 ? 25.216  73.862 92.334  1.00 67.58  ? 239  ILE E O   1 
ATOM   9640  C CB  . ILE E  1 239 ? 25.923  72.605 89.489  1.00 63.56  ? 239  ILE E CB  1 
ATOM   9641  C CG1 . ILE E  1 239 ? 26.597  71.262 89.796  1.00 62.63  ? 239  ILE E CG1 1 
ATOM   9642  C CG2 . ILE E  1 239 ? 26.886  73.759 89.760  1.00 64.93  ? 239  ILE E CG2 1 
ATOM   9643  C CD1 . ILE E  1 239 ? 27.637  70.849 88.777  1.00 61.31  ? 239  ILE E CD1 1 
ATOM   9644  N N   . ASN E  1 240 ? 24.721  71.670 92.488  1.00 65.75  ? 240  ASN E N   1 
ATOM   9645  C CA  . ASN E  1 240 ? 24.891  71.601 93.941  1.00 67.36  ? 240  ASN E CA  1 
ATOM   9646  C C   . ASN E  1 240 ? 25.952  70.583 94.345  1.00 67.15  ? 240  ASN E C   1 
ATOM   9647  O O   . ASN E  1 240 ? 25.883  69.421 93.950  1.00 65.86  ? 240  ASN E O   1 
ATOM   9648  C CB  . ASN E  1 240 ? 23.574  71.224 94.616  1.00 67.96  ? 240  ASN E CB  1 
ATOM   9649  C CG  . ASN E  1 240 ? 22.424  72.128 94.215  1.00 68.25  ? 240  ASN E CG  1 
ATOM   9650  O OD1 . ASN E  1 240 ? 22.450  73.330 94.470  1.00 69.53  ? 240  ASN E OD1 1 
ATOM   9651  N ND2 . ASN E  1 240 ? 21.398  71.549 93.596  1.00 67.35  ? 240  ASN E ND2 1 
ATOM   9652  N N   . PHE E  1 241 ? 26.917  71.031 95.148  1.00 68.66  ? 241  PHE E N   1 
ATOM   9653  C CA  . PHE E  1 241 ? 27.979  70.175 95.674  1.00 69.02  ? 241  PHE E CA  1 
ATOM   9654  C C   . PHE E  1 241 ? 27.811  69.968 97.175  1.00 71.17  ? 241  PHE E C   1 
ATOM   9655  O O   . PHE E  1 241 ? 27.518  70.915 97.903  1.00 72.92  ? 241  PHE E O   1 
ATOM   9656  C CB  . PHE E  1 241 ? 29.347  70.808 95.413  1.00 69.52  ? 241  PHE E CB  1 
ATOM   9657  C CG  . PHE E  1 241 ? 29.747  70.810 93.968  1.00 67.50  ? 241  PHE E CG  1 
ATOM   9658  C CD1 . PHE E  1 241 ? 30.388  69.711 93.413  1.00 66.09  ? 241  PHE E CD1 1 
ATOM   9659  C CD2 . PHE E  1 241 ? 29.486  71.908 93.163  1.00 67.24  ? 241  PHE E CD2 1 
ATOM   9660  C CE1 . PHE E  1 241 ? 30.762  69.704 92.079  1.00 64.38  ? 241  PHE E CE1 1 
ATOM   9661  C CE2 . PHE E  1 241 ? 29.858  71.911 91.828  1.00 65.65  ? 241  PHE E CE2 1 
ATOM   9662  C CZ  . PHE E  1 241 ? 30.496  70.805 91.284  1.00 64.16  ? 241  PHE E CZ  1 
ATOM   9663  N N   . GLU E  1 242 ? 27.988  68.729 97.628  1.00 71.22  ? 242  GLU E N   1 
ATOM   9664  C CA  . GLU E  1 242 ? 28.093  68.429 99.055  1.00 73.58  ? 242  GLU E CA  1 
ATOM   9665  C C   . GLU E  1 242 ? 29.205  67.402 99.266  1.00 73.95  ? 242  GLU E C   1 
ATOM   9666  O O   . GLU E  1 242 ? 29.202  66.344 98.632  1.00 72.38  ? 242  GLU E O   1 
ATOM   9667  C CB  . GLU E  1 242 ? 26.762  67.912 99.618  1.00 73.92  ? 242  GLU E CB  1 
ATOM   9668  C CG  . GLU E  1 242 ? 26.740  67.751 101.136 1.00 76.70  ? 242  GLU E CG  1 
ATOM   9669  C CD  . GLU E  1 242 ? 25.434  67.167 101.655 1.00 77.11  ? 242  GLU E CD  1 
ATOM   9670  O OE1 . GLU E  1 242 ? 24.371  67.786 101.444 1.00 76.64  ? 242  GLU E OE1 1 
ATOM   9671  O OE2 . GLU E  1 242 ? 25.467  66.093 102.289 1.00 78.11  ? 242  GLU E OE2 1 
ATOM   9672  N N   . SER E  1 243 ? 30.157  67.716 100.146 1.00 76.25  ? 243  SER E N   1 
ATOM   9673  C CA  . SER E  1 243 ? 31.282  66.816 100.406 1.00 77.04  ? 243  SER E CA  1 
ATOM   9674  C C   . SER E  1 243 ? 31.901  66.989 101.794 1.00 80.51  ? 243  SER E C   1 
ATOM   9675  O O   . SER E  1 243 ? 32.060  68.110 102.281 1.00 82.25  ? 243  SER E O   1 
ATOM   9676  C CB  . SER E  1 243 ? 32.368  67.013 99.350  1.00 75.61  ? 243  SER E CB  1 
ATOM   9677  O OG  . SER E  1 243 ? 33.424  66.087 99.534  1.00 76.30  ? 243  SER E OG  1 
ATOM   9678  N N   . ASN E  1 244 ? 32.260  65.861 102.408 1.00 81.76  ? 244  ASN E N   1 
ATOM   9679  C CA  . ASN E  1 244 ? 32.980  65.833 103.684 1.00 85.34  ? 244  ASN E CA  1 
ATOM   9680  C C   . ASN E  1 244 ? 34.417  65.322 103.525 1.00 86.07  ? 244  ASN E C   1 
ATOM   9681  O O   . ASN E  1 244 ? 35.059  64.953 104.515 1.00 89.08  ? 244  ASN E O   1 
ATOM   9682  C CB  . ASN E  1 244 ? 32.234  64.955 104.697 1.00 87.00  ? 244  ASN E CB  1 
ATOM   9683  C CG  . ASN E  1 244 ? 32.176  63.495 104.276 1.00 85.71  ? 244  ASN E CG  1 
ATOM   9684  O OD1 . ASN E  1 244 ? 32.116  63.187 103.084 1.00 82.74  ? 244  ASN E OD1 1 
ATOM   9685  N ND2 . ASN E  1 244 ? 32.191  62.591 105.250 1.00 88.16  ? 244  ASN E ND2 1 
ATOM   9686  N N   . GLY E  1 245 ? 34.916  65.299 102.286 1.00 83.49  ? 245  GLY E N   1 
ATOM   9687  C CA  . GLY E  1 245 ? 36.291  64.873 102.019 1.00 83.99  ? 245  GLY E CA  1 
ATOM   9688  C C   . GLY E  1 245 ? 36.618  64.585 100.565 1.00 80.72  ? 245  GLY E C   1 
ATOM   9689  O O   . GLY E  1 245 ? 35.740  64.232 99.776  1.00 78.05  ? 245  GLY E O   1 
ATOM   9690  N N   . ASN E  1 246 ? 37.898  64.753 100.228 1.00 81.22  ? 246  ASN E N   1 
ATOM   9691  C CA  . ASN E  1 246 ? 38.482  64.319 98.948  1.00 78.68  ? 246  ASN E CA  1 
ATOM   9692  C C   . ASN E  1 246 ? 37.966  65.052 97.702  1.00 75.69  ? 246  ASN E C   1 
ATOM   9693  O O   . ASN E  1 246 ? 37.997  64.505 96.602  1.00 73.19  ? 246  ASN E O   1 
ATOM   9694  C CB  . ASN E  1 246 ? 38.332  62.798 98.782  1.00 77.72  ? 246  ASN E CB  1 
ATOM   9695  C CG  . ASN E  1 246 ? 38.926  62.022 99.949  1.00 80.89  ? 246  ASN E CG  1 
ATOM   9696  O OD1 . ASN E  1 246 ? 38.384  62.031 101.055 1.00 83.04  ? 246  ASN E OD1 1 
ATOM   9697  N ND2 . ASN E  1 246 ? 40.040  61.339 99.704  1.00 81.35  ? 246  ASN E ND2 1 
ATOM   9698  N N   . PHE E  1 247 ? 37.549  66.305 97.878  1.00 76.28  ? 247  PHE E N   1 
ATOM   9699  C CA  . PHE E  1 247 ? 36.863  67.069 96.829  1.00 73.91  ? 247  PHE E CA  1 
ATOM   9700  C C   . PHE E  1 247 ? 37.784  68.058 96.120  1.00 73.95  ? 247  PHE E C   1 
ATOM   9701  O O   . PHE E  1 247 ? 38.493  68.830 96.759  1.00 76.48  ? 247  PHE E O   1 
ATOM   9702  C CB  . PHE E  1 247 ? 35.675  67.814 97.448  1.00 74.62  ? 247  PHE E CB  1 
ATOM   9703  C CG  . PHE E  1 247 ? 34.909  68.682 96.483  1.00 72.72  ? 247  PHE E CG  1 
ATOM   9704  C CD1 . PHE E  1 247 ? 34.384  68.157 95.311  1.00 69.86  ? 247  PHE E CD1 1 
ATOM   9705  C CD2 . PHE E  1 247 ? 34.673  70.020 96.774  1.00 74.11  ? 247  PHE E CD2 1 
ATOM   9706  C CE1 . PHE E  1 247 ? 33.664  68.952 94.432  1.00 68.47  ? 247  PHE E CE1 1 
ATOM   9707  C CE2 . PHE E  1 247 ? 33.951  70.818 95.903  1.00 72.66  ? 247  PHE E CE2 1 
ATOM   9708  C CZ  . PHE E  1 247 ? 33.445  70.284 94.731  1.00 69.87  ? 247  PHE E CZ  1 
ATOM   9709  N N   . ILE E  1 248 ? 37.760  68.024 94.790  1.00 71.37  ? 248  ILE E N   1 
ATOM   9710  C CA  . ILE E  1 248 ? 38.481  68.993 93.977  1.00 71.27  ? 248  ILE E CA  1 
ATOM   9711  C C   . ILE E  1 248 ? 37.448  69.974 93.425  1.00 70.28  ? 248  ILE E C   1 
ATOM   9712  O O   . ILE E  1 248 ? 36.716  69.663 92.487  1.00 67.86  ? 248  ILE E O   1 
ATOM   9713  C CB  . ILE E  1 248 ? 39.259  68.320 92.827  1.00 69.35  ? 248  ILE E CB  1 
ATOM   9714  C CG1 . ILE E  1 248 ? 40.018  67.077 93.312  1.00 69.95  ? 248  ILE E CG1 1 
ATOM   9715  C CG2 . ILE E  1 248 ? 40.221  69.313 92.195  1.00 70.00  ? 248  ILE E CG2 1 
ATOM   9716  C CD1 . ILE E  1 248 ? 41.183  67.370 94.236  1.00 73.09  ? 248  ILE E CD1 1 
ATOM   9717  N N   . ALA E  1 249 ? 37.384  71.157 94.028  1.00 72.44  ? 249  ALA E N   1 
ATOM   9718  C CA  . ALA E  1 249 ? 36.338  72.130 93.712  1.00 72.06  ? 249  ALA E CA  1 
ATOM   9719  C C   . ALA E  1 249 ? 36.620  72.877 92.411  1.00 71.04  ? 249  ALA E C   1 
ATOM   9720  O O   . ALA E  1 249 ? 37.779  73.080 92.053  1.00 71.67  ? 249  ALA E O   1 
ATOM   9721  C CB  . ALA E  1 249 ? 36.181  73.120 94.858  1.00 75.01  ? 249  ALA E CB  1 
ATOM   9722  N N   . PRO E  1 250 ? 35.556  73.277 91.692  1.00 69.66  ? 250  PRO E N   1 
ATOM   9723  C CA  . PRO E  1 250 ? 35.719  74.135 90.521  1.00 69.23  ? 250  PRO E CA  1 
ATOM   9724  C C   . PRO E  1 250 ? 35.938  75.599 90.890  1.00 71.95  ? 250  PRO E C   1 
ATOM   9725  O O   . PRO E  1 250 ? 35.093  76.190 91.555  1.00 73.13  ? 250  PRO E O   1 
ATOM   9726  C CB  . PRO E  1 250 ? 34.387  73.981 89.781  1.00 67.23  ? 250  PRO E CB  1 
ATOM   9727  C CG  . PRO E  1 250 ? 33.404  73.574 90.814  1.00 67.49  ? 250  PRO E CG  1 
ATOM   9728  C CD  . PRO E  1 250 ? 34.168  72.801 91.845  1.00 68.42  ? 250  PRO E CD  1 
ATOM   9729  N N   . GLU E  1 251 ? 37.066  76.168 90.471  1.00 73.15  ? 251  GLU E N   1 
ATOM   9730  C CA  . GLU E  1 251 ? 37.276  77.617 90.543  1.00 75.75  ? 251  GLU E CA  1 
ATOM   9731  C C   . GLU E  1 251 ? 36.655  78.261 89.305  1.00 74.70  ? 251  GLU E C   1 
ATOM   9732  O O   . GLU E  1 251 ? 35.818  79.164 89.414  1.00 75.75  ? 251  GLU E O   1 
ATOM   9733  C CB  . GLU E  1 251 ? 38.774  77.958 90.635  1.00 77.88  ? 251  GLU E CB  1 
ATOM   9734  C CG  . GLU E  1 251 ? 39.196  78.694 91.899  1.00 81.53  ? 251  GLU E CG  1 
ATOM   9735  C CD  . GLU E  1 251 ? 39.511  80.160 91.656  1.00 84.27  ? 251  GLU E CD  1 
ATOM   9736  O OE1 . GLU E  1 251 ? 40.452  80.444 90.888  1.00 84.77  ? 251  GLU E OE1 1 
ATOM   9737  O OE2 . GLU E  1 251 ? 38.832  81.031 92.242  1.00 86.13  ? 251  GLU E OE2 1 
ATOM   9738  N N   . TYR E  1 252 ? 37.071  77.772 88.135  1.00 72.77  ? 252  TYR E N   1 
ATOM   9739  C CA  . TYR E  1 252 ? 36.600  78.271 86.844  1.00 71.88  ? 252  TYR E CA  1 
ATOM   9740  C C   . TYR E  1 252 ? 35.820  77.211 86.056  1.00 68.81  ? 252  TYR E C   1 
ATOM   9741  O O   . TYR E  1 252 ? 36.093  76.008 86.150  1.00 67.13  ? 252  TYR E O   1 
ATOM   9742  C CB  . TYR E  1 252 ? 37.780  78.744 85.990  1.00 72.71  ? 252  TYR E CB  1 
ATOM   9743  C CG  . TYR E  1 252 ? 38.581  79.864 86.605  1.00 76.11  ? 252  TYR E CG  1 
ATOM   9744  C CD1 . TYR E  1 252 ? 38.213  81.192 86.421  1.00 78.27  ? 252  TYR E CD1 1 
ATOM   9745  C CD2 . TYR E  1 252 ? 39.711  79.596 87.369  1.00 77.49  ? 252  TYR E CD2 1 
ATOM   9746  C CE1 . TYR E  1 252 ? 38.946  82.224 86.989  1.00 81.73  ? 252  TYR E CE1 1 
ATOM   9747  C CE2 . TYR E  1 252 ? 40.451  80.618 87.941  1.00 80.98  ? 252  TYR E CE2 1 
ATOM   9748  C CZ  . TYR E  1 252 ? 40.064  81.932 87.749  1.00 83.10  ? 252  TYR E CZ  1 
ATOM   9749  O OH  . TYR E  1 252 ? 40.800  82.948 88.313  1.00 86.84  ? 252  TYR E OH  1 
ATOM   9750  N N   . ALA E  1 253 ? 34.850  77.683 85.279  1.00 68.39  ? 253  ALA E N   1 
ATOM   9751  C CA  . ALA E  1 253 ? 34.087  76.843 84.366  1.00 65.98  ? 253  ALA E CA  1 
ATOM   9752  C C   . ALA E  1 253 ? 34.018  77.541 83.012  1.00 66.18  ? 253  ALA E C   1 
ATOM   9753  O O   . ALA E  1 253 ? 33.739  78.741 82.942  1.00 68.12  ? 253  ALA E O   1 
ATOM   9754  C CB  . ALA E  1 253 ? 32.689  76.601 84.915  1.00 65.54  ? 253  ALA E CB  1 
ATOM   9755  N N   . TYR E  1 254 ? 34.280  76.792 81.944  1.00 64.42  ? 254  TYR E N   1 
ATOM   9756  C CA  . TYR E  1 254 ? 34.308  77.351 80.595  1.00 64.69  ? 254  TYR E CA  1 
ATOM   9757  C C   . TYR E  1 254 ? 32.900  77.603 80.067  1.00 64.63  ? 254  TYR E C   1 
ATOM   9758  O O   . TYR E  1 254 ? 32.013  76.761 80.200  1.00 63.22  ? 254  TYR E O   1 
ATOM   9759  C CB  . TYR E  1 254 ? 35.054  76.421 79.638  1.00 62.96  ? 254  TYR E CB  1 
ATOM   9760  C CG  . TYR E  1 254 ? 36.549  76.378 79.857  1.00 63.44  ? 254  TYR E CG  1 
ATOM   9761  C CD1 . TYR E  1 254 ? 37.389  77.313 79.255  1.00 65.09  ? 254  TYR E CD1 1 
ATOM   9762  C CD2 . TYR E  1 254 ? 37.127  75.398 80.654  1.00 62.51  ? 254  TYR E CD2 1 
ATOM   9763  C CE1 . TYR E  1 254 ? 38.762  77.273 79.443  1.00 65.76  ? 254  TYR E CE1 1 
ATOM   9764  C CE2 . TYR E  1 254 ? 38.497  75.352 80.851  1.00 63.19  ? 254  TYR E CE2 1 
ATOM   9765  C CZ  . TYR E  1 254 ? 39.314  76.292 80.245  1.00 64.80  ? 254  TYR E CZ  1 
ATOM   9766  O OH  . TYR E  1 254 ? 40.679  76.250 80.442  1.00 65.69  ? 254  TYR E OH  1 
ATOM   9767  N N   . LYS E  1 255 ? 32.719  78.767 79.452  1.00 66.44  ? 255  LYS E N   1 
ATOM   9768  C CA  . LYS E  1 255 ? 31.430  79.196 78.923  1.00 66.99  ? 255  LYS E CA  1 
ATOM   9769  C C   . LYS E  1 255 ? 31.453  79.032 77.408  1.00 66.54  ? 255  LYS E C   1 
ATOM   9770  O O   . LYS E  1 255 ? 32.404  79.459 76.755  1.00 67.29  ? 255  LYS E O   1 
ATOM   9771  C CB  . LYS E  1 255 ? 31.187  80.661 79.305  1.00 69.79  ? 255  LYS E CB  1 
ATOM   9772  C CG  . LYS E  1 255 ? 29.732  81.032 79.535  1.00 70.50  ? 255  LYS E CG  1 
ATOM   9773  C CD  . LYS E  1 255 ? 29.596  82.262 80.427  1.00 73.04  ? 255  LYS E CD  1 
ATOM   9774  C CE  . LYS E  1 255 ? 29.822  83.563 79.672  1.00 75.68  ? 255  LYS E CE  1 
ATOM   9775  N NZ  . LYS E  1 255 ? 29.305  84.731 80.441  1.00 78.29  ? 255  LYS E NZ  1 
ATOM   9776  N N   . ILE E  1 256 ? 30.408  78.422 76.855  1.00 65.55  ? 256  ILE E N   1 
ATOM   9777  C CA  . ILE E  1 256 ? 30.383  78.065 75.432  1.00 65.10  ? 256  ILE E CA  1 
ATOM   9778  C C   . ILE E  1 256 ? 29.679  79.160 74.631  1.00 67.37  ? 256  ILE E C   1 
ATOM   9779  O O   . ILE E  1 256 ? 28.464  79.117 74.431  1.00 67.72  ? 256  ILE E O   1 
ATOM   9780  C CB  . ILE E  1 256 ? 29.687  76.704 75.170  1.00 63.10  ? 256  ILE E CB  1 
ATOM   9781  C CG1 . ILE E  1 256 ? 29.834  75.760 76.372  1.00 61.45  ? 256  ILE E CG1 1 
ATOM   9782  C CG2 . ILE E  1 256 ? 30.242  76.076 73.897  1.00 62.28  ? 256  ILE E CG2 1 
ATOM   9783  C CD1 . ILE E  1 256 ? 29.411  74.331 76.103  1.00 59.60  ? 256  ILE E CD1 1 
ATOM   9784  N N   . VAL E  1 257 ? 30.447  80.146 74.176  1.00 69.14  ? 257  VAL E N   1 
ATOM   9785  C CA  . VAL E  1 257 ? 29.864  81.301 73.488  1.00 71.79  ? 257  VAL E CA  1 
ATOM   9786  C C   . VAL E  1 257 ? 29.477  80.988 72.035  1.00 71.95  ? 257  VAL E C   1 
ATOM   9787  O O   . VAL E  1 257 ? 28.385  81.361 71.592  1.00 73.36  ? 257  VAL E O   1 
ATOM   9788  C CB  . VAL E  1 257 ? 30.765  82.564 73.572  1.00 74.22  ? 257  VAL E CB  1 
ATOM   9789  C CG1 . VAL E  1 257 ? 30.901  83.014 75.020  1.00 74.74  ? 257  VAL E CG1 1 
ATOM   9790  C CG2 . VAL E  1 257 ? 32.140  82.341 72.952  1.00 73.80  ? 257  VAL E CG2 1 
ATOM   9791  N N   . LYS E  1 258 ? 30.358  80.297 71.309  1.00 70.66  ? 258  LYS E N   1 
ATOM   9792  C CA  . LYS E  1 258 ? 30.111  79.956 69.902  1.00 70.94  ? 258  LYS E CA  1 
ATOM   9793  C C   . LYS E  1 258 ? 30.123  78.455 69.645  1.00 68.27  ? 258  LYS E C   1 
ATOM   9794  O O   . LYS E  1 258 ? 31.038  77.751 70.073  1.00 66.35  ? 258  LYS E O   1 
ATOM   9795  C CB  . LYS E  1 258 ? 31.140  80.631 68.985  1.00 72.53  ? 258  LYS E CB  1 
ATOM   9796  C CG  . LYS E  1 258 ? 30.597  81.828 68.215  1.00 75.85  ? 258  LYS E CG  1 
ATOM   9797  C CD  . LYS E  1 258 ? 30.993  81.786 66.744  1.00 76.90  ? 258  LYS E CD  1 
ATOM   9798  C CE  . LYS E  1 258 ? 32.487  81.979 66.535  1.00 76.94  ? 258  LYS E CE  1 
ATOM   9799  N NZ  . LYS E  1 258 ? 32.764  82.447 65.147  1.00 79.20  ? 258  LYS E NZ  1 
ATOM   9800  N N   . LYS E  1 259 ? 29.099  77.984 68.932  1.00 68.46  ? 259  LYS E N   1 
ATOM   9801  C CA  . LYS E  1 259 ? 29.026  76.604 68.460  1.00 66.54  ? 259  LYS E CA  1 
ATOM   9802  C C   . LYS E  1 259 ? 29.080  76.592 66.937  1.00 67.78  ? 259  LYS E C   1 
ATOM   9803  O O   . LYS E  1 259 ? 28.188  77.127 66.280  1.00 69.96  ? 259  LYS E O   1 
ATOM   9804  C CB  . LYS E  1 259 ? 27.726  75.941 68.917  1.00 66.00  ? 259  LYS E CB  1 
ATOM   9805  C CG  . LYS E  1 259 ? 27.552  75.868 70.420  1.00 64.89  ? 259  LYS E CG  1 
ATOM   9806  C CD  . LYS E  1 259 ? 26.272  75.140 70.795  1.00 64.49  ? 259  LYS E CD  1 
ATOM   9807  C CE  . LYS E  1 259 ? 26.083  75.123 72.305  1.00 63.64  ? 259  LYS E CE  1 
ATOM   9808  N NZ  . LYS E  1 259 ? 24.783  74.526 72.717  1.00 63.58  ? 259  LYS E NZ  1 
ATOM   9809  N N   . GLY E  1 260 ? 30.122  75.981 66.379  1.00 66.59  ? 260  GLY E N   1 
ATOM   9810  C CA  . GLY E  1 260 ? 30.269  75.883 64.927  1.00 67.76  ? 260  GLY E CA  1 
ATOM   9811  C C   . GLY E  1 260 ? 30.944  74.598 64.494  1.00 65.69  ? 260  GLY E C   1 
ATOM   9812  O O   . GLY E  1 260 ? 31.214  73.718 65.313  1.00 63.40  ? 260  GLY E O   1 
ATOM   9813  N N   . ASP E  1 261 ? 31.213  74.490 63.198  1.00 66.72  ? 261  ASP E N   1 
ATOM   9814  C CA  . ASP E  1 261 ? 31.950  73.351 62.668  1.00 65.07  ? 261  ASP E CA  1 
ATOM   9815  C C   . ASP E  1 261 ? 33.409  73.453 63.085  1.00 63.78  ? 261  ASP E C   1 
ATOM   9816  O O   . ASP E  1 261 ? 34.082  74.435 62.782  1.00 65.21  ? 261  ASP E O   1 
ATOM   9817  C CB  . ASP E  1 261 ? 31.840  73.282 61.140  1.00 66.88  ? 261  ASP E CB  1 
ATOM   9818  C CG  . ASP E  1 261 ? 30.471  72.821 60.672  1.00 68.05  ? 261  ASP E CG  1 
ATOM   9819  O OD1 . ASP E  1 261 ? 29.718  72.255 61.494  1.00 66.91  ? 261  ASP E OD1 1 
ATOM   9820  O OD2 . ASP E  1 261 ? 30.148  73.019 59.477  1.00 70.34  ? 261  ASP E OD2 1 
ATOM   9821  N N   . SER E  1 262 ? 33.880  72.436 63.795  1.00 61.33  ? 262  SER E N   1 
ATOM   9822  C CA  . SER E  1 262 ? 35.264  72.365 64.243  1.00 60.13  ? 262  SER E CA  1 
ATOM   9823  C C   . SER E  1 262 ? 35.709  70.908 64.187  1.00 58.02  ? 262  SER E C   1 
ATOM   9824  O O   . SER E  1 262 ? 34.918  70.027 63.839  1.00 57.66  ? 262  SER E O   1 
ATOM   9825  C CB  . SER E  1 262 ? 35.391  72.922 65.669  1.00 59.75  ? 262  SER E CB  1 
ATOM   9826  O OG  . SER E  1 262 ? 36.701  72.757 66.193  1.00 58.69  ? 262  SER E OG  1 
ATOM   9827  N N   . THR E  1 263 ? 36.971  70.656 64.516  1.00 56.92  ? 263  THR E N   1 
ATOM   9828  C CA  . THR E  1 263 ? 37.497  69.296 64.529  1.00 55.02  ? 263  THR E CA  1 
ATOM   9829  C C   . THR E  1 263 ? 38.800  69.246 65.317  1.00 54.08  ? 263  THR E C   1 
ATOM   9830  O O   . THR E  1 263 ? 39.569  70.210 65.314  1.00 55.13  ? 263  THR E O   1 
ATOM   9831  C CB  . THR E  1 263 ? 37.712  68.761 63.091  1.00 55.38  ? 263  THR E CB  1 
ATOM   9832  O OG1 . THR E  1 263 ? 37.699  67.330 63.103  1.00 53.81  ? 263  THR E OG1 1 
ATOM   9833  C CG2 . THR E  1 263 ? 39.028  69.244 62.488  1.00 55.92  ? 263  THR E CG2 1 
ATOM   9834  N N   . ILE E  1 264 ? 39.034  68.131 66.003  1.00 52.40  ? 264  ILE E N   1 
ATOM   9835  C CA  . ILE E  1 264 ? 40.307  67.903 66.670  1.00 51.64  ? 264  ILE E CA  1 
ATOM   9836  C C   . ILE E  1 264 ? 41.209  67.103 65.734  1.00 51.11  ? 264  ILE E C   1 
ATOM   9837  O O   . ILE E  1 264 ? 41.070  65.887 65.590  1.00 49.96  ? 264  ILE E O   1 
ATOM   9838  C CB  . ILE E  1 264 ? 40.139  67.189 68.021  1.00 50.43  ? 264  ILE E CB  1 
ATOM   9839  C CG1 . ILE E  1 264 ? 39.312  68.064 68.966  1.00 51.17  ? 264  ILE E CG1 1 
ATOM   9840  C CG2 . ILE E  1 264 ? 41.500  66.907 68.643  1.00 49.92  ? 264  ILE E CG2 1 
ATOM   9841  C CD1 . ILE E  1 264 ? 38.693  67.310 70.118  1.00 50.24  ? 264  ILE E CD1 1 
ATOM   9842  N N   . MET E  1 265 ? 42.127  67.821 65.098  1.00 44.74  ? 265  MET E N   1 
ATOM   9843  C CA  . MET E  1 265 ? 43.081  67.254 64.160  1.00 43.06  ? 265  MET E CA  1 
ATOM   9844  C C   . MET E  1 265 ? 44.261  66.648 64.911  1.00 43.75  ? 265  MET E C   1 
ATOM   9845  O O   . MET E  1 265 ? 44.749  67.222 65.886  1.00 45.37  ? 265  MET E O   1 
ATOM   9846  C CB  . MET E  1 265 ? 43.574  68.362 63.239  1.00 42.83  ? 265  MET E CB  1 
ATOM   9847  C CG  . MET E  1 265 ? 44.209  67.892 61.948  1.00 41.08  ? 265  MET E CG  1 
ATOM   9848  S SD  . MET E  1 265 ? 44.439  69.297 60.843  1.00 41.40  ? 265  MET E SD  1 
ATOM   9849  C CE  . MET E  1 265 ? 42.756  69.585 60.285  1.00 40.96  ? 265  MET E CE  1 
ATOM   9850  N N   . LYS E  1 266 ? 44.707  65.484 64.453  1.00 42.97  ? 266  LYS E N   1 
ATOM   9851  C CA  . LYS E  1 266 ? 45.831  64.781 65.056  1.00 44.15  ? 266  LYS E CA  1 
ATOM   9852  C C   . LYS E  1 266 ? 47.058  64.963 64.177  1.00 44.02  ? 266  LYS E C   1 
ATOM   9853  O O   . LYS E  1 266 ? 47.108  64.445 63.062  1.00 42.81  ? 266  LYS E O   1 
ATOM   9854  C CB  . LYS E  1 266 ? 45.506  63.295 65.221  1.00 44.34  ? 266  LYS E CB  1 
ATOM   9855  C CG  . LYS E  1 266 ? 44.658  62.984 66.443  1.00 45.77  ? 266  LYS E CG  1 
ATOM   9856  C CD  . LYS E  1 266 ? 45.517  62.915 67.694  1.00 47.75  ? 266  LYS E CD  1 
ATOM   9857  C CE  . LYS E  1 266 ? 44.665  62.713 68.936  1.00 49.38  ? 266  LYS E CE  1 
ATOM   9858  N NZ  . LYS E  1 266 ? 45.488  62.803 70.180  1.00 51.38  ? 266  LYS E NZ  1 
ATOM   9859  N N   . SER E  1 267 ? 48.041  65.704 64.678  1.00 45.75  ? 267  SER E N   1 
ATOM   9860  C CA  . SER E  1 267 ? 49.222  66.040 63.890  1.00 46.44  ? 267  SER E CA  1 
ATOM   9861  C C   . SER E  1 267 ? 50.416  66.435 64.760  1.00 49.31  ? 267  SER E C   1 
ATOM   9862  O O   . SER E  1 267 ? 50.267  67.146 65.759  1.00 50.54  ? 267  SER E O   1 
ATOM   9863  C CB  . SER E  1 267 ? 48.889  67.183 62.930  1.00 45.62  ? 267  SER E CB  1 
ATOM   9864  O OG  . SER E  1 267 ? 50.033  67.579 62.191  1.00 46.81  ? 267  SER E OG  1 
ATOM   9865  N N   . GLU E  1 268 ? 51.598  65.972 64.361  1.00 50.76  ? 268  GLU E N   1 
ATOM   9866  C CA  . GLU E  1 268 ? 52.850  66.333 65.029  1.00 54.08  ? 268  GLU E CA  1 
ATOM   9867  C C   . GLU E  1 268 ? 53.361  67.684 64.532  1.00 55.48  ? 268  GLU E C   1 
ATOM   9868  O O   . GLU E  1 268 ? 54.210  68.296 65.177  1.00 58.57  ? 268  GLU E O   1 
ATOM   9869  C CB  . GLU E  1 268 ? 53.929  65.266 64.792  1.00 55.92  ? 268  GLU E CB  1 
ATOM   9870  C CG  . GLU E  1 268 ? 53.521  63.845 65.156  1.00 55.33  ? 268  GLU E CG  1 
ATOM   9871  C CD  . GLU E  1 268 ? 53.084  63.708 66.600  1.00 56.01  ? 268  GLU E CD  1 
ATOM   9872  O OE1 . GLU E  1 268 ? 53.864  64.093 67.501  1.00 58.68  ? 268  GLU E OE1 1 
ATOM   9873  O OE2 . GLU E  1 268 ? 51.959  63.210 66.829  1.00 54.18  ? 268  GLU E OE2 1 
ATOM   9874  N N   . LEU E  1 269 ? 52.842  68.141 63.392  1.00 53.67  ? 269  LEU E N   1 
ATOM   9875  C CA  . LEU E  1 269 ? 53.304  69.381 62.761  1.00 55.36  ? 269  LEU E CA  1 
ATOM   9876  C C   . LEU E  1 269 ? 52.933  70.611 63.575  1.00 56.83  ? 269  LEU E C   1 
ATOM   9877  O O   . LEU E  1 269 ? 51.995  70.579 64.372  1.00 55.59  ? 269  LEU E O   1 
ATOM   9878  C CB  . LEU E  1 269 ? 52.744  69.512 61.337  1.00 53.07  ? 269  LEU E CB  1 
ATOM   9879  C CG  . LEU E  1 269 ? 53.506  68.733 60.261  1.00 53.06  ? 269  LEU E CG  1 
ATOM   9880  C CD1 . LEU E  1 269 ? 52.643  68.503 59.029  1.00 49.92  ? 269  LEU E CD1 1 
ATOM   9881  C CD2 . LEU E  1 269 ? 54.789  69.458 59.885  1.00 56.82  ? 269  LEU E CD2 1 
ATOM   9882  N N   . GLU E  1 270 ? 53.674  71.694 63.347  1.00 59.97  ? 270  GLU E N   1 
ATOM   9883  C CA  . GLU E  1 270 ? 53.527  72.925 64.135  1.00 62.48  ? 270  GLU E CA  1 
ATOM   9884  C C   . GLU E  1 270 ? 52.672  73.972 63.387  1.00 62.13  ? 270  GLU E C   1 
ATOM   9885  O O   . GLU E  1 270 ? 51.487  73.728 63.161  1.00 59.18  ? 270  GLU E O   1 
ATOM   9886  C CB  . GLU E  1 270 ? 54.898  73.461 64.619  1.00 67.19  ? 270  GLU E CB  1 
ATOM   9887  C CG  . GLU E  1 270 ? 56.061  73.359 63.629  1.00 69.36  ? 270  GLU E CG  1 
ATOM   9888  C CD  . GLU E  1 270 ? 57.365  73.925 64.181  1.00 74.77  ? 270  GLU E CD  1 
ATOM   9889  O OE1 . GLU E  1 270 ? 57.347  74.555 65.261  1.00 76.82  ? 270  GLU E OE1 1 
ATOM   9890  O OE2 . GLU E  1 270 ? 58.417  73.737 63.532  1.00 77.33  ? 270  GLU E OE2 1 
ATOM   9891  N N   . TYR E  1 271 ? 53.249  75.109 62.996  1.00 65.62  ? 271  TYR E N   1 
ATOM   9892  C CA  . TYR E  1 271 ? 52.474  76.211 62.422  1.00 66.28  ? 271  TYR E CA  1 
ATOM   9893  C C   . TYR E  1 271 ? 53.257  76.908 61.307  1.00 69.11  ? 271  TYR E C   1 
ATOM   9894  O O   . TYR E  1 271 ? 54.347  77.436 61.545  1.00 73.33  ? 271  TYR E O   1 
ATOM   9895  C CB  . TYR E  1 271 ? 52.119  77.211 63.528  1.00 69.08  ? 271  TYR E CB  1 
ATOM   9896  C CG  . TYR E  1 271 ? 51.213  78.347 63.095  1.00 70.39  ? 271  TYR E CG  1 
ATOM   9897  C CD1 . TYR E  1 271 ? 49.883  78.113 62.756  1.00 67.28  ? 271  TYR E CD1 1 
ATOM   9898  C CD2 . TYR E  1 271 ? 51.684  79.659 63.040  1.00 75.38  ? 271  TYR E CD2 1 
ATOM   9899  C CE1 . TYR E  1 271 ? 49.050  79.150 62.365  1.00 69.07  ? 271  TYR E CE1 1 
ATOM   9900  C CE2 . TYR E  1 271 ? 50.858  80.702 62.653  1.00 77.24  ? 271  TYR E CE2 1 
ATOM   9901  C CZ  . TYR E  1 271 ? 49.542  80.443 62.317  1.00 74.07  ? 271  TYR E CZ  1 
ATOM   9902  O OH  . TYR E  1 271 ? 48.721  81.477 61.930  1.00 76.47  ? 271  TYR E OH  1 
ATOM   9903  N N   . GLY E  1 272 ? 52.698  76.907 60.097  1.00 67.14  ? 272  GLY E N   1 
ATOM   9904  C CA  . GLY E  1 272 ? 53.352  77.527 58.939  1.00 69.76  ? 272  GLY E CA  1 
ATOM   9905  C C   . GLY E  1 272 ? 53.129  79.027 58.783  1.00 73.86  ? 272  GLY E C   1 
ATOM   9906  O O   . GLY E  1 272 ? 53.810  79.675 57.982  1.00 77.28  ? 272  GLY E O   1 
ATOM   9907  N N   . ASN E  1 273 ? 52.186  79.577 59.553  1.00 74.05  ? 273  ASN E N   1 
ATOM   9908  C CA  . ASN E  1 273 ? 51.755  80.975 59.418  1.00 78.06  ? 273  ASN E CA  1 
ATOM   9909  C C   . ASN E  1 273 ? 51.228  81.264 58.013  1.00 77.41  ? 273  ASN E C   1 
ATOM   9910  O O   . ASN E  1 273 ? 51.492  82.317 57.428  1.00 81.73  ? 273  ASN E O   1 
ATOM   9911  C CB  . ASN E  1 273 ? 52.880  81.944 59.810  1.00 84.27  ? 273  ASN E CB  1 
ATOM   9912  C CG  . ASN E  1 273 ? 52.355  83.293 60.272  1.00 88.80  ? 273  ASN E CG  1 
ATOM   9913  O OD1 . ASN E  1 273 ? 52.685  83.754 61.363  1.00 92.01  ? 273  ASN E OD1 1 
ATOM   9914  N ND2 . ASN E  1 273 ? 51.527  83.927 59.447  1.00 89.44  ? 273  ASN E ND2 1 
ATOM   9915  N N   . CYS E  1 274 ? 50.471  80.306 57.490  1.00 72.30  ? 274  CYS E N   1 
ATOM   9916  C CA  . CYS E  1 274 ? 49.896  80.408 56.163  1.00 71.08  ? 274  CYS E CA  1 
ATOM   9917  C C   . CYS E  1 274 ? 48.374  80.400 56.298  1.00 68.76  ? 274  CYS E C   1 
ATOM   9918  O O   . CYS E  1 274 ? 47.842  80.081 57.363  1.00 67.53  ? 274  CYS E O   1 
ATOM   9919  C CB  . CYS E  1 274 ? 50.399  79.247 55.297  1.00 67.55  ? 274  CYS E CB  1 
ATOM   9920  S SG  . CYS E  1 274 ? 49.176  77.987 54.872  1.00 61.44  ? 274  CYS E SG  1 
ATOM   9921  N N   . ASN E  1 275 ? 47.685  80.777 55.225  1.00 68.65  ? 275  ASN E N   1 
ATOM   9922  C CA  . ASN E  1 275 ? 46.224  80.766 55.185  1.00 67.04  ? 275  ASN E CA  1 
ATOM   9923  C C   . ASN E  1 275 ? 45.731  79.798 54.113  1.00 62.54  ? 275  ASN E C   1 
ATOM   9924  O O   . ASN E  1 275 ? 46.362  79.649 53.066  1.00 62.05  ? 275  ASN E O   1 
ATOM   9925  C CB  . ASN E  1 275 ? 45.690  82.174 54.905  1.00 71.95  ? 275  ASN E CB  1 
ATOM   9926  C CG  . ASN E  1 275 ? 44.185  82.280 55.093  1.00 71.61  ? 275  ASN E CG  1 
ATOM   9927  O OD1 . ASN E  1 275 ? 43.671  82.051 56.182  1.00 71.11  ? 275  ASN E OD1 1 
ATOM   9928  N ND2 . ASN E  1 275 ? 43.474  82.636 54.031  1.00 72.31  ? 275  ASN E ND2 1 
ATOM   9929  N N   . THR E  1 276 ? 44.602  79.144 54.370  1.00 59.65  ? 276  THR E N   1 
ATOM   9930  C CA  . THR E  1 276 ? 44.035  78.191 53.417  1.00 55.66  ? 276  THR E CA  1 
ATOM   9931  C C   . THR E  1 276 ? 42.514  78.152 53.522  1.00 55.27  ? 276  THR E C   1 
ATOM   9932  O O   . THR E  1 276 ? 41.924  78.822 54.370  1.00 58.00  ? 276  THR E O   1 
ATOM   9933  C CB  . THR E  1 276 ? 44.622  76.776 53.633  1.00 51.68  ? 276  THR E CB  1 
ATOM   9934  O OG1 . THR E  1 276 ? 44.153  75.888 52.610  1.00 48.34  ? 276  THR E OG1 1 
ATOM   9935  C CG2 . THR E  1 276 ? 44.247  76.219 55.011  1.00 50.77  ? 276  THR E CG2 1 
ATOM   9936  N N   . LYS E  1 277 ? 41.885  77.384 52.638  1.00 52.35  ? 277  LYS E N   1 
ATOM   9937  C CA  . LYS E  1 277 ? 40.446  77.138 52.713  1.00 52.00  ? 277  LYS E CA  1 
ATOM   9938  C C   . LYS E  1 277 ? 40.128  75.634 52.775  1.00 47.83  ? 277  LYS E C   1 
ATOM   9939  O O   . LYS E  1 277 ? 38.962  75.235 52.763  1.00 47.42  ? 277  LYS E O   1 
ATOM   9940  C CB  . LYS E  1 277 ? 39.744  77.805 51.529  1.00 53.73  ? 277  LYS E CB  1 
ATOM   9941  C CG  . LYS E  1 277 ? 38.536  78.642 51.944  1.00 57.60  ? 277  LYS E CG  1 
ATOM   9942  C CD  . LYS E  1 277 ? 37.872  79.303 50.737  1.00 59.76  ? 277  LYS E CD  1 
ATOM   9943  C CE  . LYS E  1 277 ? 36.876  78.359 50.040  1.00 57.15  ? 277  LYS E CE  1 
ATOM   9944  N NZ  . LYS E  1 277 ? 35.526  78.963 49.828  1.00 60.85  ? 277  LYS E NZ  1 
ATOM   9945  N N   . CYS E  1 278 ? 41.177  74.818 52.849  1.00 45.34  ? 278  CYS E N   1 
ATOM   9946  C CA  . CYS E  1 278 ? 41.061  73.373 52.969  1.00 42.04  ? 278  CYS E CA  1 
ATOM   9947  C C   . CYS E  1 278 ? 42.308  72.874 53.673  1.00 41.33  ? 278  CYS E C   1 
ATOM   9948  O O   . CYS E  1 278 ? 43.417  73.024 53.150  1.00 41.46  ? 278  CYS E O   1 
ATOM   9949  C CB  . CYS E  1 278 ? 40.964  72.724 51.590  1.00 39.70  ? 278  CYS E CB  1 
ATOM   9950  S SG  . CYS E  1 278 ? 40.971  70.913 51.622  1.00 36.31  ? 278  CYS E SG  1 
ATOM   9951  N N   . GLN E  1 279 ? 42.137  72.290 54.855  1.00 41.07  ? 279  GLN E N   1 
ATOM   9952  C CA  . GLN E  1 279 ? 43.278  71.880 55.665  1.00 41.00  ? 279  GLN E CA  1 
ATOM   9953  C C   . GLN E  1 279 ? 43.279  70.380 55.929  1.00 38.78  ? 279  GLN E C   1 
ATOM   9954  O O   . GLN E  1 279 ? 42.227  69.780 56.153  1.00 38.04  ? 279  GLN E O   1 
ATOM   9955  C CB  . GLN E  1 279 ? 43.279  72.646 56.989  1.00 43.50  ? 279  GLN E CB  1 
ATOM   9956  C CG  . GLN E  1 279 ? 44.470  72.347 57.893  1.00 43.97  ? 279  GLN E CG  1 
ATOM   9957  C CD  . GLN E  1 279 ? 45.770  72.943 57.385  1.00 45.39  ? 279  GLN E CD  1 
ATOM   9958  O OE1 . GLN E  1 279 ? 45.864  74.149 57.167  1.00 47.88  ? 279  GLN E OE1 1 
ATOM   9959  N NE2 . GLN E  1 279 ? 46.785  72.103 57.208  1.00 44.44  ? 279  GLN E NE2 1 
ATOM   9960  N N   . THR E  1 280 ? 44.475  69.794 55.899  1.00 38.37  ? 280  THR E N   1 
ATOM   9961  C CA  . THR E  1 280 ? 44.697  68.406 56.298  1.00 37.23  ? 280  THR E CA  1 
ATOM   9962  C C   . THR E  1 280 ? 45.758  68.353 57.404  1.00 38.88  ? 280  THR E C   1 
ATOM   9963  O O   . THR E  1 280 ? 46.507  69.317 57.593  1.00 40.68  ? 280  THR E O   1 
ATOM   9964  C CB  . THR E  1 280 ? 45.180  67.536 55.115  1.00 35.63  ? 280  THR E CB  1 
ATOM   9965  O OG1 . THR E  1 280 ? 46.595  67.687 54.932  1.00 36.68  ? 280  THR E OG1 1 
ATOM   9966  C CG2 . THR E  1 280 ? 44.455  67.910 53.830  1.00 34.55  ? 280  THR E CG2 1 
ATOM   9967  N N   . PRO E  1 281 ? 45.827  67.223 58.137  1.00 38.75  ? 281  PRO E N   1 
ATOM   9968  C CA  . PRO E  1 281 ? 46.910  67.002 59.114  1.00 40.46  ? 281  PRO E CA  1 
ATOM   9969  C C   . PRO E  1 281 ? 48.323  66.968 58.500  1.00 41.54  ? 281  PRO E C   1 
ATOM   9970  O O   . PRO E  1 281 ? 49.307  67.195 59.213  1.00 43.65  ? 281  PRO E O   1 
ATOM   9971  C CB  . PRO E  1 281 ? 46.571  65.640 59.746  1.00 40.02  ? 281  PRO E CB  1 
ATOM   9972  C CG  . PRO E  1 281 ? 45.361  65.121 59.049  1.00 38.29  ? 281  PRO E CG  1 
ATOM   9973  C CD  . PRO E  1 281 ? 44.752  66.222 58.246  1.00 37.61  ? 281  PRO E CD  1 
ATOM   9974  N N   . MET E  1 282 ? 48.406  66.682 57.198  1.00 40.51  ? 282  MET E N   1 
ATOM   9975  C CA  . MET E  1 282 ? 49.675  66.630 56.459  1.00 41.82  ? 282  MET E CA  1 
ATOM   9976  C C   . MET E  1 282 ? 50.087  68.009 55.943  1.00 43.16  ? 282  MET E C   1 
ATOM   9977  O O   . MET E  1 282 ? 51.274  68.279 55.749  1.00 45.44  ? 282  MET E O   1 
ATOM   9978  C CB  . MET E  1 282 ? 49.537  65.687 55.261  1.00 40.33  ? 282  MET E CB  1 
ATOM   9979  C CG  . MET E  1 282 ? 49.016  64.298 55.604  1.00 39.51  ? 282  MET E CG  1 
ATOM   9980  S SD  . MET E  1 282 ? 50.318  63.057 55.708  1.00 41.92  ? 282  MET E SD  1 
ATOM   9981  C CE  . MET E  1 282 ? 50.661  62.830 53.961  1.00 41.13  ? 282  MET E CE  1 
ATOM   9982  N N   . GLY E  1 283 ? 49.096  68.865 55.704  1.00 42.25  ? 283  GLY E N   1 
ATOM   9983  C CA  . GLY E  1 283 ? 49.326  70.202 55.164  1.00 43.91  ? 283  GLY E CA  1 
ATOM   9984  C C   . GLY E  1 283 ? 48.043  70.802 54.617  1.00 42.62  ? 283  GLY E C   1 
ATOM   9985  O O   . GLY E  1 283 ? 46.964  70.243 54.803  1.00 40.70  ? 283  GLY E O   1 
ATOM   9986  N N   . ALA E  1 284 ? 48.157  71.936 53.935  1.00 44.24  ? 284  ALA E N   1 
ATOM   9987  C CA  . ALA E  1 284 ? 46.991  72.621 53.380  1.00 43.83  ? 284  ALA E CA  1 
ATOM   9988  C C   . ALA E  1 284 ? 46.853  72.367 51.877  1.00 42.31  ? 284  ALA E C   1 
ATOM   9989  O O   . ALA E  1 284 ? 47.828  72.030 51.198  1.00 42.38  ? 284  ALA E O   1 
ATOM   9990  C CB  . ALA E  1 284 ? 47.079  74.111 53.655  1.00 47.34  ? 284  ALA E CB  1 
ATOM   9991  N N   . ILE E  1 285 ? 45.631  72.540 51.374  1.00 41.23  ? 285  ILE E N   1 
ATOM   9992  C CA  . ILE E  1 285 ? 45.309  72.300 49.965  1.00 39.72  ? 285  ILE E CA  1 
ATOM   9993  C C   . ILE E  1 285 ? 44.750  73.557 49.296  1.00 41.75  ? 285  ILE E C   1 
ATOM   9994  O O   . ILE E  1 285 ? 43.872  74.233 49.841  1.00 43.17  ? 285  ILE E O   1 
ATOM   9995  C CB  . ILE E  1 285 ? 44.310  71.126 49.816  1.00 36.70  ? 285  ILE E CB  1 
ATOM   9996  C CG1 . ILE E  1 285 ? 45.068  69.802 49.698  1.00 34.91  ? 285  ILE E CG1 1 
ATOM   9997  C CG2 . ILE E  1 285 ? 43.412  71.300 48.598  1.00 35.94  ? 285  ILE E CG2 1 
ATOM   9998  C CD1 . ILE E  1 285 ? 44.239  68.592 50.069  1.00 32.95  ? 285  ILE E CD1 1 
ATOM   9999  N N   . ASN E  1 286 ? 45.276  73.851 48.110  1.00 42.30  ? 286  ASN E N   1 
ATOM   10000 C CA  . ASN E  1 286 ? 44.804  74.950 47.280  1.00 44.41  ? 286  ASN E CA  1 
ATOM   10001 C C   . ASN E  1 286 ? 44.719  74.483 45.831  1.00 42.58  ? 286  ASN E C   1 
ATOM   10002 O O   . ASN E  1 286 ? 45.693  74.571 45.080  1.00 43.38  ? 286  ASN E O   1 
ATOM   10003 C CB  . ASN E  1 286 ? 45.746  76.153 47.399  1.00 48.62  ? 286  ASN E CB  1 
ATOM   10004 C CG  . ASN E  1 286 ? 45.340  77.307 46.501  1.00 51.56  ? 286  ASN E CG  1 
ATOM   10005 O OD1 . ASN E  1 286 ? 44.150  77.548 46.282  1.00 51.44  ? 286  ASN E OD1 1 
ATOM   10006 N ND2 . ASN E  1 286 ? 46.328  78.029 45.974  1.00 54.77  ? 286  ASN E ND2 1 
ATOM   10007 N N   . SER E  1 287 ? 43.558  73.960 45.452  1.00 40.38  ? 287  SER E N   1 
ATOM   10008 C CA  . SER E  1 287 ? 43.340  73.515 44.081  1.00 38.68  ? 287  SER E CA  1 
ATOM   10009 C C   . SER E  1 287 ? 41.871  73.580 43.692  1.00 38.22  ? 287  SER E C   1 
ATOM   10010 O O   . SER E  1 287 ? 40.992  73.733 44.538  1.00 38.83  ? 287  SER E O   1 
ATOM   10011 C CB  . SER E  1 287 ? 43.876  72.091 43.886  1.00 35.67  ? 287  SER E CB  1 
ATOM   10012 O OG  . SER E  1 287 ? 42.973  71.112 44.369  1.00 33.44  ? 287  SER E OG  1 
ATOM   10013 N N   . SER E  1 288 ? 41.626  73.465 42.392  1.00 37.48  ? 288  SER E N   1 
ATOM   10014 C CA  . SER E  1 288 ? 40.272  73.412 41.850  1.00 37.19  ? 288  SER E CA  1 
ATOM   10015 C C   . SER E  1 288 ? 39.905  71.989 41.407  1.00 33.74  ? 288  SER E C   1 
ATOM   10016 O O   . SER E  1 288 ? 38.802  71.756 40.909  1.00 33.48  ? 288  SER E O   1 
ATOM   10017 C CB  . SER E  1 288 ? 40.146  74.397 40.685  1.00 39.47  ? 288  SER E CB  1 
ATOM   10018 O OG  . SER E  1 288 ? 41.336  74.419 39.907  1.00 39.43  ? 288  SER E OG  1 
ATOM   10019 N N   . MET E  1 289 ? 40.819  71.041 41.610  1.00 31.63  ? 289  MET E N   1 
ATOM   10020 C CA  . MET E  1 289 ? 40.579  69.638 41.267  1.00 28.91  ? 289  MET E CA  1 
ATOM   10021 C C   . MET E  1 289 ? 39.359  69.123 42.022  1.00 28.57  ? 289  MET E C   1 
ATOM   10022 O O   . MET E  1 289 ? 39.120  69.536 43.153  1.00 29.87  ? 289  MET E O   1 
ATOM   10023 C CB  . MET E  1 289 ? 41.769  68.761 41.671  1.00 27.81  ? 289  MET E CB  1 
ATOM   10024 C CG  . MET E  1 289 ? 43.101  69.105 41.028  1.00 28.58  ? 289  MET E CG  1 
ATOM   10025 S SD  . MET E  1 289 ? 43.127  68.739 39.269  1.00 27.64  ? 289  MET E SD  1 
ATOM   10026 C CE  . MET E  1 289 ? 44.877  68.383 39.061  1.00 28.36  ? 289  MET E CE  1 
ATOM   10027 N N   . PRO E  1 290 ? 38.589  68.210 41.412  1.00 27.19  ? 290  PRO E N   1 
ATOM   10028 C CA  . PRO E  1 290 ? 37.473  67.591 42.139  1.00 27.42  ? 290  PRO E CA  1 
ATOM   10029 C C   . PRO E  1 290 ? 37.902  66.540 43.168  1.00 26.43  ? 290  PRO E C   1 
ATOM   10030 O O   . PRO E  1 290 ? 37.092  66.158 44.011  1.00 27.29  ? 290  PRO E O   1 
ATOM   10031 C CB  . PRO E  1 290 ? 36.662  66.929 41.024  1.00 26.80  ? 290  PRO E CB  1 
ATOM   10032 C CG  . PRO E  1 290 ? 37.667  66.637 39.971  1.00 25.15  ? 290  PRO E CG  1 
ATOM   10033 C CD  . PRO E  1 290 ? 38.621  67.792 40.001  1.00 25.96  ? 290  PRO E CD  1 
ATOM   10034 N N   . PHE E  1 291 ? 39.152  66.080 43.088  1.00 25.14  ? 291  PHE E N   1 
ATOM   10035 C CA  . PHE E  1 291 ? 39.673  65.039 43.976  1.00 24.58  ? 291  PHE E CA  1 
ATOM   10036 C C   . PHE E  1 291 ? 41.048  65.377 44.517  1.00 24.66  ? 291  PHE E C   1 
ATOM   10037 O O   . PHE E  1 291 ? 41.771  66.186 43.939  1.00 24.98  ? 291  PHE E O   1 
ATOM   10038 C CB  . PHE E  1 291 ? 39.829  63.720 43.228  1.00 23.54  ? 291  PHE E CB  1 
ATOM   10039 C CG  . PHE E  1 291 ? 38.540  63.076 42.850  1.00 23.77  ? 291  PHE E CG  1 
ATOM   10040 C CD1 . PHE E  1 291 ? 37.809  62.368 43.793  1.00 24.86  ? 291  PHE E CD1 1 
ATOM   10041 C CD2 . PHE E  1 291 ? 38.066  63.150 41.550  1.00 23.33  ? 291  PHE E CD2 1 
ATOM   10042 C CE1 . PHE E  1 291 ? 36.620  61.753 43.450  1.00 25.71  ? 291  PHE E CE1 1 
ATOM   10043 C CE2 . PHE E  1 291 ? 36.878  62.539 41.200  1.00 23.98  ? 291  PHE E CE2 1 
ATOM   10044 C CZ  . PHE E  1 291 ? 36.158  61.840 42.152  1.00 25.31  ? 291  PHE E CZ  1 
ATOM   10045 N N   . HIS E  1 292 ? 41.407  64.710 45.612  1.00 24.71  ? 292  HIS E N   1 
ATOM   10046 C CA  . HIS E  1 292 ? 42.775  64.709 46.124  1.00 25.05  ? 292  HIS E CA  1 
ATOM   10047 C C   . HIS E  1 292 ? 43.082  63.358 46.766  1.00 25.00  ? 292  HIS E C   1 
ATOM   10048 O O   . HIS E  1 292 ? 42.177  62.550 46.983  1.00 24.86  ? 292  HIS E O   1 
ATOM   10049 C CB  . HIS E  1 292 ? 42.966  65.830 47.142  1.00 26.37  ? 292  HIS E CB  1 
ATOM   10050 C CG  . HIS E  1 292 ? 42.275  65.584 48.445  1.00 26.86  ? 292  HIS E CG  1 
ATOM   10051 N ND1 . HIS E  1 292 ? 42.957  65.317 49.610  1.00 27.64  ? 292  HIS E ND1 1 
ATOM   10052 C CD2 . HIS E  1 292 ? 40.961  65.541 48.761  1.00 27.10  ? 292  HIS E CD2 1 
ATOM   10053 C CE1 . HIS E  1 292 ? 42.093  65.134 50.592  1.00 28.16  ? 292  HIS E CE1 1 
ATOM   10054 N NE2 . HIS E  1 292 ? 40.874  65.264 50.104  1.00 27.97  ? 292  HIS E NE2 1 
ATOM   10055 N N   . ASN E  1 293 ? 44.353  63.115 47.068  1.00 25.67  ? 293  ASN E N   1 
ATOM   10056 C CA  . ASN E  1 293 ? 44.765  61.865 47.704  1.00 26.34  ? 293  ASN E CA  1 
ATOM   10057 C C   . ASN E  1 293 ? 45.719  62.079 48.882  1.00 27.88  ? 293  ASN E C   1 
ATOM   10058 O O   . ASN E  1 293 ? 46.534  61.208 49.200  1.00 29.15  ? 293  ASN E O   1 
ATOM   10059 C CB  . ASN E  1 293 ? 45.406  60.942 46.667  1.00 26.38  ? 293  ASN E CB  1 
ATOM   10060 C CG  . ASN E  1 293 ? 46.737  61.462 46.161  1.00 27.28  ? 293  ASN E CG  1 
ATOM   10061 O OD1 . ASN E  1 293 ? 47.013  62.657 46.219  1.00 27.54  ? 293  ASN E OD1 1 
ATOM   10062 N ND2 . ASN E  1 293 ? 47.570  60.562 45.661  1.00 28.35  ? 293  ASN E ND2 1 
ATOM   10063 N N   . ILE E  1 294 ? 45.590  63.226 49.543  1.00 28.17  ? 294  ILE E N   1 
ATOM   10064 C CA  . ILE E  1 294 ? 46.519  63.619 50.605  1.00 29.84  ? 294  ILE E CA  1 
ATOM   10065 C C   . ILE E  1 294 ? 46.208  62.894 51.915  1.00 30.44  ? 294  ILE E C   1 
ATOM   10066 O O   . ILE E  1 294 ? 47.050  62.167 52.440  1.00 31.82  ? 294  ILE E O   1 
ATOM   10067 C CB  . ILE E  1 294 ? 46.509  65.152 50.849  1.00 30.46  ? 294  ILE E CB  1 
ATOM   10068 C CG1 . ILE E  1 294 ? 46.724  65.936 49.545  1.00 30.31  ? 294  ILE E CG1 1 
ATOM   10069 C CG2 . ILE E  1 294 ? 47.580  65.540 51.859  1.00 32.57  ? 294  ILE E CG2 1 
ATOM   10070 C CD1 . ILE E  1 294 ? 47.933  65.515 48.736  1.00 31.09  ? 294  ILE E CD1 1 
ATOM   10071 N N   . HIS E  1 295 ? 44.999  63.093 52.433  1.00 29.89  ? 295  HIS E N   1 
ATOM   10072 C CA  . HIS E  1 295 ? 44.610  62.545 53.732  1.00 30.82  ? 295  HIS E CA  1 
ATOM   10073 C C   . HIS E  1 295 ? 43.081  62.604 53.897  1.00 30.40  ? 295  HIS E C   1 
ATOM   10074 O O   . HIS E  1 295 ? 42.475  63.632 53.596  1.00 30.02  ? 295  HIS E O   1 
ATOM   10075 C CB  . HIS E  1 295 ? 45.295  63.348 54.843  1.00 32.16  ? 295  HIS E CB  1 
ATOM   10076 C CG  . HIS E  1 295 ? 45.314  62.664 56.173  1.00 33.48  ? 295  HIS E CG  1 
ATOM   10077 N ND1 . HIS E  1 295 ? 44.198  62.568 56.972  1.00 33.76  ? 295  HIS E ND1 1 
ATOM   10078 C CD2 . HIS E  1 295 ? 46.317  62.065 56.856  1.00 35.03  ? 295  HIS E CD2 1 
ATOM   10079 C CE1 . HIS E  1 295 ? 44.505  61.923 58.083  1.00 35.24  ? 295  HIS E CE1 1 
ATOM   10080 N NE2 . HIS E  1 295 ? 45.786  61.610 58.040  1.00 36.00  ? 295  HIS E NE2 1 
ATOM   10081 N N   . PRO E  1 296 ? 42.455  61.509 54.384  1.00 31.07  ? 296  PRO E N   1 
ATOM   10082 C CA  . PRO E  1 296 ? 40.986  61.443 54.485  1.00 31.39  ? 296  PRO E CA  1 
ATOM   10083 C C   . PRO E  1 296 ? 40.347  62.511 55.376  1.00 32.26  ? 296  PRO E C   1 
ATOM   10084 O O   . PRO E  1 296 ? 39.333  63.097 55.007  1.00 32.39  ? 296  PRO E O   1 
ATOM   10085 C CB  . PRO E  1 296 ? 40.732  60.047 55.075  1.00 32.87  ? 296  PRO E CB  1 
ATOM   10086 C CG  . PRO E  1 296 ? 42.015  59.643 55.707  1.00 33.56  ? 296  PRO E CG  1 
ATOM   10087 C CD  . PRO E  1 296 ? 43.084  60.264 54.862  1.00 32.25  ? 296  PRO E CD  1 
ATOM   10088 N N   . LEU E  1 297 ? 40.926  62.735 56.548  1.00 33.26  ? 297  LEU E N   1 
ATOM   10089 C CA  . LEU E  1 297 ? 40.402  63.710 57.508  1.00 34.50  ? 297  LEU E CA  1 
ATOM   10090 C C   . LEU E  1 297 ? 40.784  65.143 57.142  1.00 34.19  ? 297  LEU E C   1 
ATOM   10091 O O   . LEU E  1 297 ? 41.907  65.580 57.399  1.00 34.32  ? 297  LEU E O   1 
ATOM   10092 C CB  . LEU E  1 297 ? 40.898  63.381 58.920  1.00 35.87  ? 297  LEU E CB  1 
ATOM   10093 C CG  . LEU E  1 297 ? 40.583  61.969 59.426  1.00 36.97  ? 297  LEU E CG  1 
ATOM   10094 C CD1 . LEU E  1 297 ? 41.347  61.672 60.709  1.00 38.33  ? 297  LEU E CD1 1 
ATOM   10095 C CD2 . LEU E  1 297 ? 39.086  61.790 59.636  1.00 38.37  ? 297  LEU E CD2 1 
ATOM   10096 N N   . THR E  1 298 ? 39.845  65.866 56.538  1.00 34.35  ? 298  THR E N   1 
ATOM   10097 C CA  . THR E  1 298 ? 40.058  67.266 56.187  1.00 34.80  ? 298  THR E CA  1 
ATOM   10098 C C   . THR E  1 298 ? 38.987  68.142 56.816  1.00 37.01  ? 298  THR E C   1 
ATOM   10099 O O   . THR E  1 298 ? 37.964  67.650 57.294  1.00 37.98  ? 298  THR E O   1 
ATOM   10100 C CB  . THR E  1 298 ? 40.051  67.497 54.657  1.00 33.51  ? 298  THR E CB  1 
ATOM   10101 O OG1 . THR E  1 298 ? 38.705  67.479 54.159  1.00 33.92  ? 298  THR E OG1 1 
ATOM   10102 C CG2 . THR E  1 298 ? 40.877  66.438 53.945  1.00 31.65  ? 298  THR E CG2 1 
ATOM   10103 N N   . ILE E  1 299 ? 39.244  69.445 56.804  1.00 38.33  ? 299  ILE E N   1 
ATOM   10104 C CA  . ILE E  1 299 ? 38.311  70.440 57.318  1.00 41.11  ? 299  ILE E CA  1 
ATOM   10105 C C   . ILE E  1 299 ? 38.242  71.571 56.294  1.00 42.06  ? 299  ILE E C   1 
ATOM   10106 O O   . ILE E  1 299 ? 39.266  71.964 55.727  1.00 41.34  ? 299  ILE E O   1 
ATOM   10107 C CB  . ILE E  1 299 ? 38.733  70.946 58.730  1.00 42.94  ? 299  ILE E CB  1 
ATOM   10108 C CG1 . ILE E  1 299 ? 37.844  72.103 59.226  1.00 46.35  ? 299  ILE E CG1 1 
ATOM   10109 C CG2 . ILE E  1 299 ? 40.195  71.373 58.754  1.00 42.53  ? 299  ILE E CG2 1 
ATOM   10110 C CD1 . ILE E  1 299 ? 36.461  71.683 59.680  1.00 47.92  ? 299  ILE E CD1 1 
ATOM   10111 N N   . GLY E  1 300 ? 37.027  72.055 56.038  1.00 44.15  ? 300  GLY E N   1 
ATOM   10112 C CA  . GLY E  1 300 ? 36.802  73.178 55.133  1.00 45.93  ? 300  GLY E CA  1 
ATOM   10113 C C   . GLY E  1 300 ? 36.251  72.767 53.780  1.00 44.71  ? 300  GLY E C   1 
ATOM   10114 O O   . GLY E  1 300 ? 35.749  71.653 53.613  1.00 43.12  ? 300  GLY E O   1 
ATOM   10115 N N   . GLU E  1 301 ? 36.351  73.683 52.818  1.00 45.88  ? 301  GLU E N   1 
ATOM   10116 C CA  . GLU E  1 301 ? 35.883  73.458 51.447  1.00 45.01  ? 301  GLU E CA  1 
ATOM   10117 C C   . GLU E  1 301 ? 36.937  72.673 50.680  1.00 41.38  ? 301  GLU E C   1 
ATOM   10118 O O   . GLU E  1 301 ? 37.888  73.250 50.147  1.00 41.26  ? 301  GLU E O   1 
ATOM   10119 C CB  . GLU E  1 301 ? 35.621  74.800 50.752  1.00 48.16  ? 301  GLU E CB  1 
ATOM   10120 C CG  . GLU E  1 301 ? 35.059  74.697 49.337  1.00 47.79  ? 301  GLU E CG  1 
ATOM   10121 C CD  . GLU E  1 301 ? 33.575  74.351 49.298  1.00 49.47  ? 301  GLU E CD  1 
ATOM   10122 O OE1 . GLU E  1 301 ? 32.962  74.153 50.378  1.00 51.04  ? 301  GLU E OE1 1 
ATOM   10123 O OE2 . GLU E  1 301 ? 33.020  74.286 48.174  1.00 49.58  ? 301  GLU E OE2 1 
ATOM   10124 N N   . CYS E  1 302 ? 36.758  71.356 50.619  1.00 38.99  ? 302  CYS E N   1 
ATOM   10125 C CA  . CYS E  1 302 ? 37.774  70.468 50.066  1.00 35.97  ? 302  CYS E CA  1 
ATOM   10126 C C   . CYS E  1 302 ? 37.267  69.604 48.914  1.00 34.17  ? 302  CYS E C   1 
ATOM   10127 O O   . CYS E  1 302 ? 36.075  69.299 48.836  1.00 35.01  ? 302  CYS E O   1 
ATOM   10128 C CB  . CYS E  1 302 ? 38.306  69.551 51.166  1.00 35.03  ? 302  CYS E CB  1 
ATOM   10129 S SG  . CYS E  1 302 ? 39.183  70.422 52.479  1.00 36.86  ? 302  CYS E SG  1 
ATOM   10130 N N   . PRO E  1 303 ? 38.183  69.197 48.017  1.00 32.02  ? 303  PRO E N   1 
ATOM   10131 C CA  . PRO E  1 303 ? 37.847  68.148 47.062  1.00 30.22  ? 303  PRO E CA  1 
ATOM   10132 C C   . PRO E  1 303 ? 37.688  66.813 47.787  1.00 29.40  ? 303  PRO E C   1 
ATOM   10133 O O   . PRO E  1 303 ? 38.064  66.704 48.954  1.00 29.90  ? 303  PRO E O   1 
ATOM   10134 C CB  . PRO E  1 303 ? 39.052  68.124 46.114  1.00 28.75  ? 303  PRO E CB  1 
ATOM   10135 C CG  . PRO E  1 303 ? 40.172  68.738 46.877  1.00 29.54  ? 303  PRO E CG  1 
ATOM   10136 C CD  . PRO E  1 303 ? 39.550  69.717 47.822  1.00 31.78  ? 303  PRO E CD  1 
ATOM   10137 N N   . LYS E  1 304 ? 37.143  65.808 47.108  1.00 28.51  ? 304  LYS E N   1 
ATOM   10138 C CA  . LYS E  1 304 ? 36.890  64.518 47.747  1.00 28.49  ? 304  LYS E CA  1 
ATOM   10139 C C   . LYS E  1 304 ? 38.161  63.693 47.802  1.00 26.94  ? 304  LYS E C   1 
ATOM   10140 O O   . LYS E  1 304 ? 38.966  63.696 46.866  1.00 25.64  ? 304  LYS E O   1 
ATOM   10141 C CB  . LYS E  1 304 ? 35.802  63.734 47.011  1.00 29.00  ? 304  LYS E CB  1 
ATOM   10142 C CG  . LYS E  1 304 ? 34.509  64.507 46.795  1.00 31.05  ? 304  LYS E CG  1 
ATOM   10143 C CD  . LYS E  1 304 ? 33.782  64.802 48.103  1.00 33.61  ? 304  LYS E CD  1 
ATOM   10144 C CE  . LYS E  1 304 ? 33.319  66.251 48.182  1.00 35.48  ? 304  LYS E CE  1 
ATOM   10145 N NZ  . LYS E  1 304 ? 32.271  66.441 49.228  1.00 38.74  ? 304  LYS E NZ  1 
ATOM   10146 N N   . TYR E  1 305 ? 38.339  62.986 48.911  1.00 27.44  ? 305  TYR E N   1 
ATOM   10147 C CA  . TYR E  1 305 ? 39.503  62.144 49.082  1.00 26.74  ? 305  TYR E CA  1 
ATOM   10148 C C   . TYR E  1 305 ? 39.303  60.807 48.382  1.00 26.51  ? 305  TYR E C   1 
ATOM   10149 O O   . TYR E  1 305 ? 38.250  60.178 48.507  1.00 27.56  ? 305  TYR E O   1 
ATOM   10150 C CB  . TYR E  1 305 ? 39.789  61.901 50.559  1.00 27.90  ? 305  TYR E CB  1 
ATOM   10151 C CG  . TYR E  1 305 ? 40.963  60.982 50.773  1.00 27.93  ? 305  TYR E CG  1 
ATOM   10152 C CD1 . TYR E  1 305 ? 42.263  61.436 50.597  1.00 27.51  ? 305  TYR E CD1 1 
ATOM   10153 C CD2 . TYR E  1 305 ? 40.774  59.654 51.128  1.00 29.05  ? 305  TYR E CD2 1 
ATOM   10154 C CE1 . TYR E  1 305 ? 43.345  60.594 50.785  1.00 28.23  ? 305  TYR E CE1 1 
ATOM   10155 C CE2 . TYR E  1 305 ? 41.850  58.803 51.318  1.00 29.76  ? 305  TYR E CE2 1 
ATOM   10156 C CZ  . TYR E  1 305 ? 43.135  59.280 51.147  1.00 29.35  ? 305  TYR E CZ  1 
ATOM   10157 O OH  . TYR E  1 305 ? 44.214  58.449 51.332  1.00 30.64  ? 305  TYR E OH  1 
ATOM   10158 N N   . VAL E  1 306 ? 40.326  60.384 47.647  1.00 25.57  ? 306  VAL E N   1 
ATOM   10159 C CA  . VAL E  1 306 ? 40.396  59.028 47.126  1.00 25.93  ? 306  VAL E CA  1 
ATOM   10160 C C   . VAL E  1 306 ? 41.804  58.492 47.350  1.00 26.40  ? 306  VAL E C   1 
ATOM   10161 O O   . VAL E  1 306 ? 42.746  59.263 47.520  1.00 26.05  ? 306  VAL E O   1 
ATOM   10162 C CB  . VAL E  1 306 ? 40.023  58.952 45.627  1.00 24.88  ? 306  VAL E CB  1 
ATOM   10163 C CG1 . VAL E  1 306 ? 38.546  59.258 45.432  1.00 25.18  ? 306  VAL E CG1 1 
ATOM   10164 C CG2 . VAL E  1 306 ? 40.884  59.892 44.790  1.00 23.49  ? 306  VAL E CG2 1 
ATOM   10165 N N   . LYS E  1 307 ? 41.932  57.169 47.354  1.00 27.78  ? 307  LYS E N   1 
ATOM   10166 C CA  . LYS E  1 307 ? 43.224  56.507 47.537  1.00 29.08  ? 307  LYS E CA  1 
ATOM   10167 C C   . LYS E  1 307 ? 44.057  56.404 46.251  1.00 28.60  ? 307  LYS E C   1 
ATOM   10168 O O   . LYS E  1 307 ? 45.163  55.868 46.274  1.00 30.20  ? 307  LYS E O   1 
ATOM   10169 C CB  . LYS E  1 307 ? 43.019  55.096 48.096  1.00 31.59  ? 307  LYS E CB  1 
ATOM   10170 C CG  . LYS E  1 307 ? 42.591  55.043 49.546  1.00 32.90  ? 307  LYS E CG  1 
ATOM   10171 C CD  . LYS E  1 307 ? 42.722  53.623 50.068  1.00 36.07  ? 307  LYS E CD  1 
ATOM   10172 C CE  . LYS E  1 307 ? 41.954  53.415 51.362  1.00 37.77  ? 307  LYS E CE  1 
ATOM   10173 N NZ  . LYS E  1 307 ? 42.030  51.994 51.810  1.00 41.45  ? 307  LYS E NZ  1 
ATOM   10174 N N   . SER E  1 308 ? 43.539  56.907 45.136  1.00 26.85  ? 308  SER E N   1 
ATOM   10175 C CA  . SER E  1 308 ? 44.218  56.767 43.852  1.00 26.51  ? 308  SER E CA  1 
ATOM   10176 C C   . SER E  1 308 ? 45.549  57.514 43.818  1.00 26.80  ? 308  SER E C   1 
ATOM   10177 O O   . SER E  1 308 ? 45.717  58.542 44.479  1.00 26.37  ? 308  SER E O   1 
ATOM   10178 C CB  . SER E  1 308 ? 43.326  57.283 42.719  1.00 24.64  ? 308  SER E CB  1 
ATOM   10179 O OG  . SER E  1 308 ? 41.993  56.845 42.883  1.00 24.71  ? 308  SER E OG  1 
ATOM   10180 N N   . ASN E  1 309 ? 46.490  56.971 43.048  1.00 28.00  ? 309  ASN E N   1 
ATOM   10181 C CA  . ASN E  1 309 ? 47.712  57.679 42.681  1.00 28.73  ? 309  ASN E CA  1 
ATOM   10182 C C   . ASN E  1 309 ? 47.494  58.517 41.431  1.00 27.05  ? 309  ASN E C   1 
ATOM   10183 O O   . ASN E  1 309 ? 48.217  59.487 41.200  1.00 27.47  ? 309  ASN E O   1 
ATOM   10184 C CB  . ASN E  1 309 ? 48.847  56.691 42.419  1.00 31.56  ? 309  ASN E CB  1 
ATOM   10185 C CG  . ASN E  1 309 ? 49.298  55.973 43.677  1.00 33.98  ? 309  ASN E CG  1 
ATOM   10186 O OD1 . ASN E  1 309 ? 49.535  56.601 44.714  1.00 34.18  ? 309  ASN E OD1 1 
ATOM   10187 N ND2 . ASN E  1 309 ? 49.430  54.649 43.592  1.00 36.21  ? 309  ASN E ND2 1 
ATOM   10188 N N   . ARG E  1 310 ? 46.495  58.143 40.632  1.00 25.56  ? 310  ARG E N   1 
ATOM   10189 C CA  . ARG E  1 310 ? 46.304  58.740 39.313  1.00 24.28  ? 310  ARG E CA  1 
ATOM   10190 C C   . ARG E  1 310 ? 44.840  58.705 38.837  1.00 22.39  ? 310  ARG E C   1 
ATOM   10191 O O   . ARG E  1 310 ? 44.217  57.642 38.803  1.00 22.60  ? 310  ARG E O   1 
ATOM   10192 C CB  . ARG E  1 310 ? 47.182  57.993 38.310  1.00 25.73  ? 310  ARG E CB  1 
ATOM   10193 C CG  . ARG E  1 310 ? 47.531  58.790 37.068  1.00 25.38  ? 310  ARG E CG  1 
ATOM   10194 C CD  . ARG E  1 310 ? 48.276  57.934 36.058  1.00 27.02  ? 310  ARG E CD  1 
ATOM   10195 N NE  . ARG E  1 310 ? 47.874  58.264 34.692  1.00 25.83  ? 310  ARG E NE  1 
ATOM   10196 C CZ  . ARG E  1 310 ? 48.324  59.303 33.991  1.00 25.99  ? 310  ARG E CZ  1 
ATOM   10197 N NH1 . ARG E  1 310 ? 49.215  60.149 34.506  1.00 27.53  ? 310  ARG E NH1 1 
ATOM   10198 N NH2 . ARG E  1 310 ? 47.879  59.498 32.756  1.00 24.99  ? 310  ARG E NH2 1 
ATOM   10199 N N   . LEU E  1 311 ? 44.307  59.875 38.480  1.00 21.05  ? 311  LEU E N   1 
ATOM   10200 C CA  . LEU E  1 311 ? 43.004  59.988 37.811  1.00 19.76  ? 311  LEU E CA  1 
ATOM   10201 C C   . LEU E  1 311 ? 43.075  61.025 36.691  1.00 19.10  ? 311  LEU E C   1 
ATOM   10202 O O   . LEU E  1 311 ? 43.076  62.232 36.951  1.00 19.23  ? 311  LEU E O   1 
ATOM   10203 C CB  . LEU E  1 311 ? 41.903  60.384 38.795  1.00 19.56  ? 311  LEU E CB  1 
ATOM   10204 C CG  . LEU E  1 311 ? 41.512  59.379 39.879  1.00 20.40  ? 311  LEU E CG  1 
ATOM   10205 C CD1 . LEU E  1 311 ? 40.474  60.008 40.790  1.00 20.54  ? 311  LEU E CD1 1 
ATOM   10206 C CD2 . LEU E  1 311 ? 40.978  58.086 39.289  1.00 20.89  ? 311  LEU E CD2 1 
ATOM   10207 N N   . VAL E  1 312 ? 43.132  60.545 35.450  1.00 18.75  ? 312  VAL E N   1 
ATOM   10208 C CA  . VAL E  1 312 ? 43.247  61.403 34.275  1.00 18.39  ? 312  VAL E CA  1 
ATOM   10209 C C   . VAL E  1 312 ? 42.168  61.041 33.264  1.00 17.46  ? 312  VAL E C   1 
ATOM   10210 O O   . VAL E  1 312 ? 42.070  59.895 32.845  1.00 17.48  ? 312  VAL E O   1 
ATOM   10211 C CB  . VAL E  1 312 ? 44.627  61.248 33.602  1.00 19.46  ? 312  VAL E CB  1 
ATOM   10212 C CG1 . VAL E  1 312 ? 44.774  62.216 32.433  1.00 19.57  ? 312  VAL E CG1 1 
ATOM   10213 C CG2 . VAL E  1 312 ? 45.738  61.468 34.619  1.00 20.92  ? 312  VAL E CG2 1 
ATOM   10214 N N   . LEU E  1 313 ? 41.373  62.032 32.874  1.00 17.08  ? 313  LEU E N   1 
ATOM   10215 C CA  . LEU E  1 313 ? 40.331  61.851 31.874  1.00 16.58  ? 313  LEU E CA  1 
ATOM   10216 C C   . LEU E  1 313 ? 40.824  62.242 30.491  1.00 16.53  ? 313  LEU E C   1 
ATOM   10217 O O   . LEU E  1 313 ? 41.404  63.309 30.318  1.00 17.14  ? 313  LEU E O   1 
ATOM   10218 C CB  . LEU E  1 313 ? 39.113  62.710 32.211  1.00 16.90  ? 313  LEU E CB  1 
ATOM   10219 C CG  . LEU E  1 313 ? 38.195  62.180 33.305  1.00 17.30  ? 313  LEU E CG  1 
ATOM   10220 C CD1 . LEU E  1 313 ? 37.201  63.256 33.712  1.00 18.29  ? 313  LEU E CD1 1 
ATOM   10221 C CD2 . LEU E  1 313 ? 37.471  60.926 32.839  1.00 17.41  ? 313  LEU E CD2 1 
ATOM   10222 N N   . ALA E  1 314 ? 40.581  61.380 29.508  1.00 16.18  ? 314  ALA E N   1 
ATOM   10223 C CA  . ALA E  1 314 ? 40.796  61.738 28.113  1.00 16.17  ? 314  ALA E CA  1 
ATOM   10224 C C   . ALA E  1 314 ? 39.762  62.772 27.733  1.00 16.33  ? 314  ALA E C   1 
ATOM   10225 O O   . ALA E  1 314 ? 38.571  62.588 27.986  1.00 16.33  ? 314  ALA E O   1 
ATOM   10226 C CB  . ALA E  1 314 ? 40.665  60.524 27.214  1.00 15.95  ? 314  ALA E CB  1 
ATOM   10227 N N   . THR E  1 315 ? 40.229  63.875 27.160  1.00 17.07  ? 315  THR E N   1 
ATOM   10228 C CA  . THR E  1 315 ? 39.357  64.860 26.537  1.00 17.83  ? 315  THR E CA  1 
ATOM   10229 C C   . THR E  1 315 ? 39.530  64.805 25.022  1.00 17.93  ? 315  THR E C   1 
ATOM   10230 O O   . THR E  1 315 ? 38.559  64.842 24.281  1.00 18.05  ? 315  THR E O   1 
ATOM   10231 C CB  . THR E  1 315 ? 39.642  66.282 27.058  1.00 19.38  ? 315  THR E CB  1 
ATOM   10232 O OG1 . THR E  1 315 ? 41.056  66.509 27.122  1.00 19.98  ? 315  THR E OG1 1 
ATOM   10233 C CG2 . THR E  1 315 ? 39.047  66.462 28.446  1.00 19.59  ? 315  THR E CG2 1 
ATOM   10234 N N   . GLY E  1 316 ? 40.772  64.704 24.569  1.00 18.23  ? 316  GLY E N   1 
ATOM   10235 C CA  . GLY E  1 316 ? 41.063  64.588 23.152  1.00 18.55  ? 316  GLY E CA  1 
ATOM   10236 C C   . GLY E  1 316 ? 40.975  63.156 22.673  1.00 17.50  ? 316  GLY E C   1 
ATOM   10237 O O   . GLY E  1 316 ? 40.362  62.307 23.316  1.00 16.66  ? 316  GLY E O   1 
ATOM   10238 N N   . LEU E  1 317 ? 41.613  62.892 21.543  1.00 18.01  ? 317  LEU E N   1 
ATOM   10239 C CA  . LEU E  1 317 ? 41.508  61.606 20.872  1.00 17.58  ? 317  LEU E CA  1 
ATOM   10240 C C   . LEU E  1 317 ? 42.867  60.924 20.832  1.00 18.62  ? 317  LEU E C   1 
ATOM   10241 O O   . LEU E  1 317 ? 43.877  61.514 21.209  1.00 19.73  ? 317  LEU E O   1 
ATOM   10242 C CB  . LEU E  1 317 ? 40.922  61.780 19.459  1.00 17.64  ? 317  LEU E CB  1 
ATOM   10243 C CG  . LEU E  1 317 ? 41.493  62.858 18.528  1.00 18.86  ? 317  LEU E CG  1 
ATOM   10244 C CD1 . LEU E  1 317 ? 42.697  62.325 17.776  1.00 19.86  ? 317  LEU E CD1 1 
ATOM   10245 C CD2 . LEU E  1 317 ? 40.449  63.376 17.549  1.00 18.97  ? 317  LEU E CD2 1 
ATOM   10246 N N   . ARG E  1 318 ? 42.879  59.673 20.391  1.00 18.84  ? 318  ARG E N   1 
ATOM   10247 C CA  . ARG E  1 318 ? 44.099  58.891 20.340  1.00 20.49  ? 318  ARG E CA  1 
ATOM   10248 C C   . ARG E  1 318 ? 45.128  59.596 19.468  1.00 22.27  ? 318  ARG E C   1 
ATOM   10249 O O   . ARG E  1 318 ? 44.880  59.869 18.292  1.00 22.34  ? 318  ARG E O   1 
ATOM   10250 C CB  . ARG E  1 318 ? 43.806  57.496 19.802  1.00 20.80  ? 318  ARG E CB  1 
ATOM   10251 C CG  . ARG E  1 318 ? 45.013  56.582 19.739  1.00 23.05  ? 318  ARG E CG  1 
ATOM   10252 C CD  . ARG E  1 318 ? 44.630  55.232 19.160  1.00 23.84  ? 318  ARG E CD  1 
ATOM   10253 N NE  . ARG E  1 318 ? 43.868  54.431 20.115  1.00 23.50  ? 318  ARG E NE  1 
ATOM   10254 C CZ  . ARG E  1 318 ? 44.382  53.483 20.895  1.00 25.25  ? 318  ARG E CZ  1 
ATOM   10255 N NH1 . ARG E  1 318 ? 45.680  53.189 20.854  1.00 27.58  ? 318  ARG E NH1 1 
ATOM   10256 N NH2 . ARG E  1 318 ? 43.588  52.822 21.729  1.00 25.18  ? 318  ARG E NH2 1 
ATOM   10257 N N   . ASN E  1 319 ? 46.279  59.899 20.060  1.00 24.17  ? 319  ASN E N   1 
ATOM   10258 C CA  . ASN E  1 319 ? 47.327  60.634 19.379  1.00 26.66  ? 319  ASN E CA  1 
ATOM   10259 C C   . ASN E  1 319 ? 48.255  59.683 18.636  1.00 29.18  ? 319  ASN E C   1 
ATOM   10260 O O   . ASN E  1 319 ? 48.531  58.577 19.098  1.00 29.83  ? 319  ASN E O   1 
ATOM   10261 C CB  . ASN E  1 319 ? 48.108  61.473 20.382  1.00 28.03  ? 319  ASN E CB  1 
ATOM   10262 C CG  . ASN E  1 319 ? 48.990  62.504 19.720  1.00 30.74  ? 319  ASN E CG  1 
ATOM   10263 O OD1 . ASN E  1 319 ? 48.948  62.690 18.509  1.00 31.37  ? 319  ASN E OD1 1 
ATOM   10264 N ND2 . ASN E  1 319 ? 49.795  63.184 20.517  1.00 32.73  ? 319  ASN E ND2 1 
ATOM   10265 N N   . SER E  1 320 ? 48.747  60.135 17.488  1.00 31.26  ? 320  SER E N   1 
ATOM   10266 C CA  . SER E  1 320 ? 49.435  59.268 16.532  1.00 33.76  ? 320  SER E CA  1 
ATOM   10267 C C   . SER E  1 320 ? 50.953  59.213 16.760  1.00 38.03  ? 320  SER E C   1 
ATOM   10268 O O   . SER E  1 320 ? 51.556  60.211 17.164  1.00 39.66  ? 320  SER E O   1 
ATOM   10269 C CB  . SER E  1 320 ? 49.140  59.749 15.106  1.00 33.85  ? 320  SER E CB  1 
ATOM   10270 O OG  . SER E  1 320 ? 47.738  59.906 14.918  1.00 30.69  ? 320  SER E OG  1 
ATOM   10271 N N   . PRO E  1 321 ? 51.573  58.040 16.504  1.00 40.51  ? 321  PRO E N   1 
ATOM   10272 C CA  . PRO E  1 321 ? 53.031  57.897 16.569  1.00 45.26  ? 321  PRO E CA  1 
ATOM   10273 C C   . PRO E  1 321 ? 53.713  58.326 15.273  1.00 48.38  ? 321  PRO E C   1 
ATOM   10274 O O   . PRO E  1 321 ? 53.715  59.510 14.939  1.00 48.64  ? 321  PRO E O   1 
ATOM   10275 C CB  . PRO E  1 321 ? 53.219  56.394 16.784  1.00 46.60  ? 321  PRO E CB  1 
ATOM   10276 C CG  . PRO E  1 321 ? 52.055  55.779 16.078  1.00 43.65  ? 321  PRO E CG  1 
ATOM   10277 C CD  . PRO E  1 321 ? 50.908  56.742 16.258  1.00 39.36  ? 321  PRO E CD  1 
ATOM   10278 N N   . GLY F  2 1   ? 39.976  51.053 17.238  1.00 18.26  ? 1    GLY F N   1 
ATOM   10279 C CA  . GLY F  2 1   ? 38.735  51.624 17.833  1.00 16.49  ? 1    GLY F CA  1 
ATOM   10280 C C   . GLY F  2 1   ? 37.488  51.008 17.243  1.00 16.97  ? 1    GLY F C   1 
ATOM   10281 O O   . GLY F  2 1   ? 37.521  50.452 16.150  1.00 18.32  ? 1    GLY F O   1 
ATOM   10282 N N   . LEU F  2 2   ? 36.380  51.134 17.965  1.00 16.23  ? 2    LEU F N   1 
ATOM   10283 C CA  . LEU F  2 2   ? 35.133  50.467 17.602  1.00 17.30  ? 2    LEU F CA  1 
ATOM   10284 C C   . LEU F  2 2   ? 34.620  50.815 16.212  1.00 17.83  ? 2    LEU F C   1 
ATOM   10285 O O   . LEU F  2 2   ? 34.014  49.973 15.550  1.00 19.63  ? 2    LEU F O   1 
ATOM   10286 C CB  . LEU F  2 2   ? 34.044  50.780 18.631  1.00 16.64  ? 2    LEU F CB  1 
ATOM   10287 C CG  . LEU F  2 2   ? 34.094  49.997 19.937  1.00 16.85  ? 2    LEU F CG  1 
ATOM   10288 C CD1 . LEU F  2 2   ? 33.017  50.502 20.876  1.00 16.28  ? 2    LEU F CD1 1 
ATOM   10289 C CD2 . LEU F  2 2   ? 33.932  48.507 19.692  1.00 19.10  ? 2    LEU F CD2 1 
ATOM   10290 N N   . PHE F  2 3   ? 34.859  52.046 15.772  1.00 16.58  ? 3    PHE F N   1 
ATOM   10291 C CA  . PHE F  2 3   ? 34.251  52.547 14.542  1.00 16.97  ? 3    PHE F CA  1 
ATOM   10292 C C   . PHE F  2 3   ? 35.182  52.499 13.339  1.00 17.52  ? 3    PHE F C   1 
ATOM   10293 O O   . PHE F  2 3   ? 34.776  52.823 12.231  1.00 17.97  ? 3    PHE F O   1 
ATOM   10294 C CB  . PHE F  2 3   ? 33.652  53.930 14.801  1.00 15.80  ? 3    PHE F CB  1 
ATOM   10295 C CG  . PHE F  2 3   ? 32.550  53.889 15.820  1.00 15.96  ? 3    PHE F CG  1 
ATOM   10296 C CD1 . PHE F  2 3   ? 31.251  53.568 15.444  1.00 17.50  ? 3    PHE F CD1 1 
ATOM   10297 C CD2 . PHE F  2 3   ? 32.827  54.072 17.166  1.00 14.99  ? 3    PHE F CD2 1 
ATOM   10298 C CE1 . PHE F  2 3   ? 30.245  53.480 16.385  1.00 18.15  ? 3    PHE F CE1 1 
ATOM   10299 C CE2 . PHE F  2 3   ? 31.825  53.981 18.112  1.00 15.37  ? 3    PHE F CE2 1 
ATOM   10300 C CZ  . PHE F  2 3   ? 30.532  53.686 17.722  1.00 17.00  ? 3    PHE F CZ  1 
ATOM   10301 N N   . GLY F  2 4   ? 36.422  52.073 13.569  1.00 17.81  ? 4    GLY F N   1 
ATOM   10302 C CA  . GLY F  2 4   ? 37.335  51.684 12.501  1.00 19.14  ? 4    GLY F CA  1 
ATOM   10303 C C   . GLY F  2 4   ? 38.008  52.800 11.733  1.00 18.52  ? 4    GLY F C   1 
ATOM   10304 O O   . GLY F  2 4   ? 38.744  52.526 10.790  1.00 19.79  ? 4    GLY F O   1 
ATOM   10305 N N   . ALA F  2 5   ? 37.767  54.049 12.124  1.00 16.97  ? 5    ALA F N   1 
ATOM   10306 C CA  . ALA F  2 5   ? 38.286  55.201 11.394  1.00 16.65  ? 5    ALA F CA  1 
ATOM   10307 C C   . ALA F  2 5   ? 39.642  55.617 11.937  1.00 16.84  ? 5    ALA F C   1 
ATOM   10308 O O   . ALA F  2 5   ? 40.643  55.551 11.230  1.00 17.99  ? 5    ALA F O   1 
ATOM   10309 C CB  . ALA F  2 5   ? 37.301  56.355 11.461  1.00 15.57  ? 5    ALA F CB  1 
ATOM   10310 N N   . ILE F  2 6   ? 39.670  56.027 13.201  1.00 16.10  ? 6    ILE F N   1 
ATOM   10311 C CA  . ILE F  2 6   ? 40.905  56.461 13.848  1.00 16.69  ? 6    ILE F CA  1 
ATOM   10312 C C   . ILE F  2 6   ? 41.855  55.282 14.009  1.00 18.30  ? 6    ILE F C   1 
ATOM   10313 O O   . ILE F  2 6   ? 41.476  54.254 14.555  1.00 18.40  ? 6    ILE F O   1 
ATOM   10314 C CB  . ILE F  2 6   ? 40.624  57.107 15.221  1.00 15.74  ? 6    ILE F CB  1 
ATOM   10315 C CG1 . ILE F  2 6   ? 39.907  58.444 15.018  1.00 15.03  ? 6    ILE F CG1 1 
ATOM   10316 C CG2 . ILE F  2 6   ? 41.916  57.315 16.001  1.00 16.80  ? 6    ILE F CG2 1 
ATOM   10317 C CD1 . ILE F  2 6   ? 39.508  59.150 16.295  1.00 14.51  ? 6    ILE F CD1 1 
ATOM   10318 N N   . ALA F  2 7   ? 43.085  55.440 13.529  1.00 20.01  ? 7    ALA F N   1 
ATOM   10319 C CA  . ALA F  2 7   ? 44.075  54.371 13.544  1.00 22.28  ? 7    ALA F CA  1 
ATOM   10320 C C   . ALA F  2 7   ? 43.546  53.122 12.855  1.00 23.07  ? 7    ALA F C   1 
ATOM   10321 O O   . ALA F  2 7   ? 43.899  52.008 13.225  1.00 24.66  ? 7    ALA F O   1 
ATOM   10322 C CB  . ALA F  2 7   ? 44.488  54.054 14.974  1.00 22.57  ? 7    ALA F CB  1 
ATOM   10323 N N   . GLY F  2 8   ? 42.697  53.316 11.853  1.00 22.35  ? 8    GLY F N   1 
ATOM   10324 C CA  . GLY F  2 8   ? 42.025  52.215 11.184  1.00 23.32  ? 8    GLY F CA  1 
ATOM   10325 C C   . GLY F  2 8   ? 42.218  52.332 9.693   1.00 24.49  ? 8    GLY F C   1 
ATOM   10326 O O   . GLY F  2 8   ? 43.304  52.063 9.194   1.00 26.63  ? 8    GLY F O   1 
ATOM   10327 N N   . PHE F  2 9   ? 41.170  52.727 8.978   1.00 23.46  ? 9    PHE F N   1 
ATOM   10328 C CA  . PHE F  2 9   ? 41.299  52.973 7.554   1.00 24.39  ? 9    PHE F CA  1 
ATOM   10329 C C   . PHE F  2 9   ? 41.901  54.359 7.324   1.00 23.62  ? 9    PHE F C   1 
ATOM   10330 O O   . PHE F  2 9   ? 42.447  54.619 6.260   1.00 24.77  ? 9    PHE F O   1 
ATOM   10331 C CB  . PHE F  2 9   ? 39.970  52.760 6.805   1.00 24.15  ? 9    PHE F CB  1 
ATOM   10332 C CG  . PHE F  2 9   ? 38.967  53.868 6.975   1.00 21.98  ? 9    PHE F CG  1 
ATOM   10333 C CD1 . PHE F  2 9   ? 38.974  54.959 6.128   1.00 21.39  ? 9    PHE F CD1 1 
ATOM   10334 C CD2 . PHE F  2 9   ? 37.988  53.791 7.950   1.00 20.94  ? 9    PHE F CD2 1 
ATOM   10335 C CE1 . PHE F  2 9   ? 38.041  55.969 6.271   1.00 19.97  ? 9    PHE F CE1 1 
ATOM   10336 C CE2 . PHE F  2 9   ? 37.052  54.797 8.099   1.00 19.57  ? 9    PHE F CE2 1 
ATOM   10337 C CZ  . PHE F  2 9   ? 37.080  55.888 7.261   1.00 19.17  ? 9    PHE F CZ  1 
ATOM   10338 N N   . ILE F  2 10  ? 41.800  55.237 8.322   1.00 22.10  ? 10   ILE F N   1 
ATOM   10339 C CA  . ILE F  2 10  ? 42.593  56.466 8.366   1.00 22.10  ? 10   ILE F CA  1 
ATOM   10340 C C   . ILE F  2 10  ? 43.766  56.211 9.302   1.00 23.45  ? 10   ILE F C   1 
ATOM   10341 O O   . ILE F  2 10  ? 43.627  56.284 10.521  1.00 22.60  ? 10   ILE F O   1 
ATOM   10342 C CB  . ILE F  2 10  ? 41.780  57.668 8.871   1.00 20.23  ? 10   ILE F CB  1 
ATOM   10343 C CG1 . ILE F  2 10  ? 40.543  57.875 7.998   1.00 19.42  ? 10   ILE F CG1 1 
ATOM   10344 C CG2 . ILE F  2 10  ? 42.641  58.924 8.860   1.00 20.80  ? 10   ILE F CG2 1 
ATOM   10345 C CD1 . ILE F  2 10  ? 39.559  58.888 8.545   1.00 18.10  ? 10   ILE F CD1 1 
ATOM   10346 N N   . GLU F  2 11  ? 44.923  55.916 8.726   1.00 25.94  ? 11   GLU F N   1 
ATOM   10347 C CA  . GLU F  2 11  ? 46.040  55.356 9.492   1.00 28.10  ? 11   GLU F CA  1 
ATOM   10348 C C   . GLU F  2 11  ? 46.586  56.246 10.596  1.00 28.01  ? 11   GLU F C   1 
ATOM   10349 O O   . GLU F  2 11  ? 47.060  55.741 11.609  1.00 28.90  ? 11   GLU F O   1 
ATOM   10350 C CB  . GLU F  2 11  ? 47.186  54.981 8.559   1.00 31.36  ? 11   GLU F CB  1 
ATOM   10351 C CG  . GLU F  2 11  ? 46.864  53.851 7.599   1.00 32.53  ? 11   GLU F CG  1 
ATOM   10352 C CD  . GLU F  2 11  ? 48.121  53.150 7.116   1.00 36.55  ? 11   GLU F CD  1 
ATOM   10353 O OE1 . GLU F  2 11  ? 48.889  53.776 6.347   1.00 38.16  ? 11   GLU F OE1 1 
ATOM   10354 O OE2 . GLU F  2 11  ? 48.344  51.981 7.515   1.00 38.44  ? 11   GLU F OE2 1 
ATOM   10355 N N   . GLY F  2 12  ? 46.524  57.561 10.402  1.00 27.33  ? 12   GLY F N   1 
ATOM   10356 C CA  . GLY F  2 12  ? 47.085  58.512 11.366  1.00 27.90  ? 12   GLY F CA  1 
ATOM   10357 C C   . GLY F  2 12  ? 46.485  59.907 11.310  1.00 26.58  ? 12   GLY F C   1 
ATOM   10358 O O   . GLY F  2 12  ? 45.828  60.279 10.333  1.00 25.58  ? 12   GLY F O   1 
ATOM   10359 N N   . GLY F  2 13  ? 46.723  60.679 12.367  1.00 26.98  ? 13   GLY F N   1 
ATOM   10360 C CA  . GLY F  2 13  ? 46.215  62.045 12.477  1.00 26.45  ? 13   GLY F CA  1 
ATOM   10361 C C   . GLY F  2 13  ? 47.063  63.061 11.730  1.00 28.86  ? 13   GLY F C   1 
ATOM   10362 O O   . GLY F  2 13  ? 48.070  62.712 11.114  1.00 30.99  ? 13   GLY F O   1 
ATOM   10363 N N   . TRP F  2 14  ? 46.647  64.324 11.793  1.00 28.93  ? 14   TRP F N   1 
ATOM   10364 C CA  . TRP F  2 14  ? 47.305  65.410 11.077  1.00 31.35  ? 14   TRP F CA  1 
ATOM   10365 C C   . TRP F  2 14  ? 47.852  66.462 12.025  1.00 33.69  ? 14   TRP F C   1 
ATOM   10366 O O   . TRP F  2 14  ? 47.095  67.238 12.606  1.00 33.02  ? 14   TRP F O   1 
ATOM   10367 C CB  . TRP F  2 14  ? 46.322  66.082 10.123  1.00 30.08  ? 14   TRP F CB  1 
ATOM   10368 C CG  . TRP F  2 14  ? 45.871  65.220 8.998   1.00 28.57  ? 14   TRP F CG  1 
ATOM   10369 C CD1 . TRP F  2 14  ? 46.536  64.165 8.456   1.00 29.23  ? 14   TRP F CD1 1 
ATOM   10370 C CD2 . TRP F  2 14  ? 44.660  65.363 8.243   1.00 26.73  ? 14   TRP F CD2 1 
ATOM   10371 N NE1 . TRP F  2 14  ? 45.813  63.633 7.422   1.00 27.82  ? 14   TRP F NE1 1 
ATOM   10372 C CE2 . TRP F  2 14  ? 44.658  64.352 7.266   1.00 26.22  ? 14   TRP F CE2 1 
ATOM   10373 C CE3 . TRP F  2 14  ? 43.580  66.248 8.300   1.00 25.89  ? 14   TRP F CE3 1 
ATOM   10374 C CZ2 . TRP F  2 14  ? 43.615  64.194 6.354   1.00 24.80  ? 14   TRP F CZ2 1 
ATOM   10375 C CZ3 . TRP F  2 14  ? 42.547  66.092 7.393   1.00 24.52  ? 14   TRP F CZ3 1 
ATOM   10376 C CH2 . TRP F  2 14  ? 42.571  65.071 6.435   1.00 23.92  ? 14   TRP F CH2 1 
ATOM   10377 N N   . GLN F  2 15  ? 49.176  66.493 12.158  1.00 36.92  ? 15   GLN F N   1 
ATOM   10378 C CA  . GLN F  2 15  ? 49.863  67.565 12.876  1.00 40.21  ? 15   GLN F CA  1 
ATOM   10379 C C   . GLN F  2 15  ? 49.506  68.927 12.271  1.00 41.17  ? 15   GLN F C   1 
ATOM   10380 O O   . GLN F  2 15  ? 49.415  69.920 12.987  1.00 42.82  ? 15   GLN F O   1 
ATOM   10381 C CB  . GLN F  2 15  ? 51.380  67.371 12.808  1.00 44.27  ? 15   GLN F CB  1 
ATOM   10382 C CG  . GLN F  2 15  ? 51.910  66.119 13.495  1.00 44.42  ? 15   GLN F CG  1 
ATOM   10383 C CD  . GLN F  2 15  ? 52.306  66.340 14.946  1.00 46.24  ? 15   GLN F CD  1 
ATOM   10384 O OE1 . GLN F  2 15  ? 51.989  65.526 15.815  1.00 44.47  ? 15   GLN F OE1 1 
ATOM   10385 N NE2 . GLN F  2 15  ? 53.010  67.435 15.216  1.00 50.14  ? 15   GLN F NE2 1 
ATOM   10386 N N   . GLY F  2 16  ? 49.297  68.957 10.953  1.00 40.36  ? 16   GLY F N   1 
ATOM   10387 C CA  . GLY F  2 16  ? 48.996  70.188 10.226  1.00 41.48  ? 16   GLY F CA  1 
ATOM   10388 C C   . GLY F  2 16  ? 47.606  70.779 10.395  1.00 39.27  ? 16   GLY F C   1 
ATOM   10389 O O   . GLY F  2 16  ? 47.350  71.885 9.931   1.00 40.76  ? 16   GLY F O   1 
ATOM   10390 N N   . MET F  2 17  ? 46.695  70.053 11.039  1.00 36.12  ? 17   MET F N   1 
ATOM   10391 C CA  . MET F  2 17  ? 45.363  70.589 11.331  1.00 34.58  ? 17   MET F CA  1 
ATOM   10392 C C   . MET F  2 17  ? 45.259  70.993 12.797  1.00 35.52  ? 17   MET F C   1 
ATOM   10393 O O   . MET F  2 17  ? 45.087  70.146 13.667  1.00 33.80  ? 17   MET F O   1 
ATOM   10394 C CB  . MET F  2 17  ? 44.281  69.566 11.002  1.00 30.88  ? 17   MET F CB  1 
ATOM   10395 C CG  . MET F  2 17  ? 42.880  70.157 11.040  1.00 29.92  ? 17   MET F CG  1 
ATOM   10396 S SD  . MET F  2 17  ? 41.659  69.002 10.422  1.00 26.46  ? 17   MET F SD  1 
ATOM   10397 C CE  . MET F  2 17  ? 41.848  67.705 11.641  1.00 24.85  ? 17   MET F CE  1 
ATOM   10398 N N   . VAL F  2 18  ? 45.343  72.295 13.054  1.00 38.50  ? 18   VAL F N   1 
ATOM   10399 C CA  . VAL F  2 18  ? 45.443  72.818 14.420  1.00 40.41  ? 18   VAL F CA  1 
ATOM   10400 C C   . VAL F  2 18  ? 44.166  73.498 14.932  1.00 40.14  ? 18   VAL F C   1 
ATOM   10401 O O   . VAL F  2 18  ? 43.999  73.668 16.137  1.00 40.90  ? 18   VAL F O   1 
ATOM   10402 C CB  . VAL F  2 18  ? 46.625  73.809 14.545  1.00 45.21  ? 18   VAL F CB  1 
ATOM   10403 C CG1 . VAL F  2 18  ? 47.898  73.194 13.982  1.00 46.18  ? 18   VAL F CG1 1 
ATOM   10404 C CG2 . VAL F  2 18  ? 46.318  75.134 13.857  1.00 47.79  ? 18   VAL F CG2 1 
ATOM   10405 N N   . ASP F  2 19  ? 43.274  73.885 14.025  1.00 39.38  ? 19   ASP F N   1 
ATOM   10406 C CA  . ASP F  2 19  ? 42.087  74.667 14.388  1.00 40.10  ? 19   ASP F CA  1 
ATOM   10407 C C   . ASP F  2 19  ? 40.832  73.804 14.611  1.00 36.61  ? 19   ASP F C   1 
ATOM   10408 O O   . ASP F  2 19  ? 39.719  74.328 14.695  1.00 37.16  ? 19   ASP F O   1 
ATOM   10409 C CB  . ASP F  2 19  ? 41.823  75.759 13.333  1.00 42.35  ? 19   ASP F CB  1 
ATOM   10410 C CG  . ASP F  2 19  ? 41.744  75.212 11.912  1.00 40.11  ? 19   ASP F CG  1 
ATOM   10411 O OD1 . ASP F  2 19  ? 41.961  73.995 11.716  1.00 37.13  ? 19   ASP F OD1 1 
ATOM   10412 O OD2 . ASP F  2 19  ? 41.476  76.005 10.984  1.00 41.62  ? 19   ASP F OD2 1 
ATOM   10413 N N   . GLY F  2 20  ? 41.007  72.489 14.716  1.00 33.52  ? 20   GLY F N   1 
ATOM   10414 C CA  . GLY F  2 20  ? 39.888  71.603 15.009  1.00 30.64  ? 20   GLY F CA  1 
ATOM   10415 C C   . GLY F  2 20  ? 40.298  70.164 15.242  1.00 27.98  ? 20   GLY F C   1 
ATOM   10416 O O   . GLY F  2 20  ? 41.449  69.791 15.003  1.00 28.25  ? 20   GLY F O   1 
ATOM   10417 N N   . TRP F  2 21  ? 39.342  69.356 15.698  1.00 25.82  ? 21   TRP F N   1 
ATOM   10418 C CA  . TRP F  2 21  ? 39.578  67.937 15.967  1.00 23.51  ? 21   TRP F CA  1 
ATOM   10419 C C   . TRP F  2 21  ? 39.415  67.078 14.715  1.00 21.82  ? 21   TRP F C   1 
ATOM   10420 O O   . TRP F  2 21  ? 40.186  66.142 14.496  1.00 21.07  ? 21   TRP F O   1 
ATOM   10421 C CB  . TRP F  2 21  ? 38.638  67.424 17.067  1.00 22.38  ? 21   TRP F CB  1 
ATOM   10422 C CG  . TRP F  2 21  ? 39.226  67.428 18.448  1.00 23.07  ? 21   TRP F CG  1 
ATOM   10423 C CD1 . TRP F  2 21  ? 40.537  67.231 18.796  1.00 23.84  ? 21   TRP F CD1 1 
ATOM   10424 C CD2 . TRP F  2 21  ? 38.514  67.596 19.672  1.00 23.34  ? 21   TRP F CD2 1 
ATOM   10425 N NE1 . TRP F  2 21  ? 40.684  67.291 20.158  1.00 24.49  ? 21   TRP F NE1 1 
ATOM   10426 C CE2 . TRP F  2 21  ? 39.456  67.511 20.722  1.00 24.08  ? 21   TRP F CE2 1 
ATOM   10427 C CE3 . TRP F  2 21  ? 37.169  67.816 19.985  1.00 23.37  ? 21   TRP F CE3 1 
ATOM   10428 C CZ2 . TRP F  2 21  ? 39.096  67.638 22.058  1.00 24.59  ? 21   TRP F CZ2 1 
ATOM   10429 C CZ3 . TRP F  2 21  ? 36.811  67.946 21.314  1.00 24.00  ? 21   TRP F CZ3 1 
ATOM   10430 C CH2 . TRP F  2 21  ? 37.770  67.855 22.336  1.00 24.47  ? 21   TRP F CH2 1 
ATOM   10431 N N   . TYR F  2 22  ? 38.396  67.386 13.918  1.00 21.59  ? 22   TYR F N   1 
ATOM   10432 C CA  . TYR F  2 22  ? 38.125  66.660 12.682  1.00 20.39  ? 22   TYR F CA  1 
ATOM   10433 C C   . TYR F  2 22  ? 38.041  67.658 11.540  1.00 21.70  ? 22   TYR F C   1 
ATOM   10434 O O   . TYR F  2 22  ? 37.610  68.794 11.734  1.00 23.27  ? 22   TYR F O   1 
ATOM   10435 C CB  . TYR F  2 22  ? 36.805  65.881 12.777  1.00 19.10  ? 22   TYR F CB  1 
ATOM   10436 C CG  . TYR F  2 22  ? 36.437  65.419 14.171  1.00 18.48  ? 22   TYR F CG  1 
ATOM   10437 C CD1 . TYR F  2 22  ? 37.132  64.392 14.790  1.00 17.43  ? 22   TYR F CD1 1 
ATOM   10438 C CD2 . TYR F  2 22  ? 35.397  66.019 14.871  1.00 19.27  ? 22   TYR F CD2 1 
ATOM   10439 C CE1 . TYR F  2 22  ? 36.799  63.972 16.065  1.00 16.94  ? 22   TYR F CE1 1 
ATOM   10440 C CE2 . TYR F  2 22  ? 35.060  65.604 16.144  1.00 18.86  ? 22   TYR F CE2 1 
ATOM   10441 C CZ  . TYR F  2 22  ? 35.761  64.583 16.731  1.00 17.55  ? 22   TYR F CZ  1 
ATOM   10442 O OH  . TYR F  2 22  ? 35.426  64.172 17.992  1.00 17.21  ? 22   TYR F OH  1 
ATOM   10443 N N   . GLY F  2 23  ? 38.442  67.234 10.348  1.00 21.34  ? 23   GLY F N   1 
ATOM   10444 C CA  . GLY F  2 23  ? 38.336  68.097 9.189   1.00 22.54  ? 23   GLY F CA  1 
ATOM   10445 C C   . GLY F  2 23  ? 38.786  67.459 7.898   1.00 22.06  ? 23   GLY F C   1 
ATOM   10446 O O   . GLY F  2 23  ? 38.913  66.237 7.806   1.00 20.76  ? 23   GLY F O   1 
ATOM   10447 N N   . TYR F  2 24  ? 39.043  68.315 6.911   1.00 23.46  ? 24   TYR F N   1 
ATOM   10448 C CA  . TYR F  2 24  ? 39.364  67.894 5.553   1.00 23.37  ? 24   TYR F CA  1 
ATOM   10449 C C   . TYR F  2 24  ? 40.747  68.372 5.130   1.00 25.00  ? 24   TYR F C   1 
ATOM   10450 O O   . TYR F  2 24  ? 41.220  69.413 5.581   1.00 26.73  ? 24   TYR F O   1 
ATOM   10451 C CB  . TYR F  2 24  ? 38.347  68.461 4.560   1.00 23.80  ? 24   TYR F CB  1 
ATOM   10452 C CG  . TYR F  2 24  ? 36.920  68.474 5.046   1.00 23.51  ? 24   TYR F CG  1 
ATOM   10453 C CD1 . TYR F  2 24  ? 36.473  69.463 5.911   1.00 24.76  ? 24   TYR F CD1 1 
ATOM   10454 C CD2 . TYR F  2 24  ? 36.009  67.515 4.622   1.00 22.55  ? 24   TYR F CD2 1 
ATOM   10455 C CE1 . TYR F  2 24  ? 35.165  69.487 6.355   1.00 24.99  ? 24   TYR F CE1 1 
ATOM   10456 C CE2 . TYR F  2 24  ? 34.695  67.526 5.066   1.00 22.83  ? 24   TYR F CE2 1 
ATOM   10457 C CZ  . TYR F  2 24  ? 34.279  68.517 5.933   1.00 24.03  ? 24   TYR F CZ  1 
ATOM   10458 O OH  . TYR F  2 24  ? 32.979  68.555 6.382   1.00 24.82  ? 24   TYR F OH  1 
ATOM   10459 N N   . HIS F  2 25  ? 41.384  67.598 4.257   1.00 24.93  ? 25   HIS F N   1 
ATOM   10460 C CA  . HIS F  2 25  ? 42.564  68.053 3.536   1.00 26.88  ? 25   HIS F CA  1 
ATOM   10461 C C   . HIS F  2 25  ? 42.344  67.869 2.043   1.00 26.79  ? 25   HIS F C   1 
ATOM   10462 O O   . HIS F  2 25  ? 42.067  66.764 1.584   1.00 25.66  ? 25   HIS F O   1 
ATOM   10463 C CB  . HIS F  2 25  ? 43.814  67.293 3.961   1.00 27.68  ? 25   HIS F CB  1 
ATOM   10464 C CG  . HIS F  2 25  ? 45.056  67.763 3.272   1.00 30.25  ? 25   HIS F CG  1 
ATOM   10465 N ND1 . HIS F  2 25  ? 45.520  67.195 2.106   1.00 30.84  ? 25   HIS F ND1 1 
ATOM   10466 C CD2 . HIS F  2 25  ? 45.913  68.767 3.567   1.00 32.86  ? 25   HIS F CD2 1 
ATOM   10467 C CE1 . HIS F  2 25  ? 46.621  67.815 1.723   1.00 33.54  ? 25   HIS F CE1 1 
ATOM   10468 N NE2 . HIS F  2 25  ? 46.880  68.776 2.592   1.00 34.88  ? 25   HIS F NE2 1 
ATOM   10469 N N   . HIS F  2 26  ? 42.482  68.958 1.295   1.00 28.34  ? 26   HIS F N   1 
ATOM   10470 C CA  . HIS F  2 26  ? 42.269  68.949 -0.149  1.00 28.49  ? 26   HIS F CA  1 
ATOM   10471 C C   . HIS F  2 26  ? 43.593  69.127 -0.876  1.00 30.47  ? 26   HIS F C   1 
ATOM   10472 O O   . HIS F  2 26  ? 44.525  69.689 -0.322  1.00 32.28  ? 26   HIS F O   1 
ATOM   10473 C CB  . HIS F  2 26  ? 41.303  70.069 -0.541  1.00 28.98  ? 26   HIS F CB  1 
ATOM   10474 C CG  . HIS F  2 26  ? 41.891  71.442 -0.448  1.00 31.42  ? 26   HIS F CG  1 
ATOM   10475 N ND1 . HIS F  2 26  ? 41.790  72.222 0.684   1.00 32.45  ? 26   HIS F ND1 1 
ATOM   10476 C CD2 . HIS F  2 26  ? 42.581  72.179 -1.350  1.00 33.42  ? 26   HIS F CD2 1 
ATOM   10477 C CE1 . HIS F  2 26  ? 42.393  73.379 0.476   1.00 35.11  ? 26   HIS F CE1 1 
ATOM   10478 N NE2 . HIS F  2 26  ? 42.883  73.377 -0.750  1.00 35.73  ? 26   HIS F NE2 1 
ATOM   10479 N N   . SER F  2 27  ? 43.672  68.630 -2.107  1.00 30.46  ? 27   SER F N   1 
ATOM   10480 C CA  . SER F  2 27  ? 44.828  68.881 -2.972  1.00 32.66  ? 27   SER F CA  1 
ATOM   10481 C C   . SER F  2 27  ? 44.394  68.927 -4.438  1.00 32.60  ? 27   SER F C   1 
ATOM   10482 O O   . SER F  2 27  ? 43.815  67.971 -4.951  1.00 31.25  ? 27   SER F O   1 
ATOM   10483 C CB  . SER F  2 27  ? 45.918  67.827 -2.759  1.00 33.51  ? 27   SER F CB  1 
ATOM   10484 O OG  . SER F  2 27  ? 45.568  66.595 -3.350  1.00 32.39  ? 27   SER F OG  1 
ATOM   10485 N N   . ASN F  2 28  ? 44.667  70.054 -5.094  1.00 34.34  ? 28   ASN F N   1 
ATOM   10486 C CA  . ASN F  2 28  ? 44.295  70.268 -6.488  1.00 34.55  ? 28   ASN F CA  1 
ATOM   10487 C C   . ASN F  2 28  ? 45.351  71.131 -7.187  1.00 37.39  ? 28   ASN F C   1 
ATOM   10488 O O   . ASN F  2 28  ? 46.424  71.358 -6.627  1.00 39.33  ? 28   ASN F O   1 
ATOM   10489 C CB  . ASN F  2 28  ? 42.887  70.882 -6.569  1.00 33.41  ? 28   ASN F CB  1 
ATOM   10490 C CG  . ASN F  2 28  ? 42.788  72.239 -5.901  1.00 34.71  ? 28   ASN F CG  1 
ATOM   10491 O OD1 . ASN F  2 28  ? 43.791  72.870 -5.597  1.00 36.73  ? 28   ASN F OD1 1 
ATOM   10492 N ND2 . ASN F  2 28  ? 41.565  72.693 -5.671  1.00 34.05  ? 28   ASN F ND2 1 
ATOM   10493 N N   . GLU F  2 29  ? 45.063  71.594 -8.403  1.00 37.99  ? 29   GLU F N   1 
ATOM   10494 C CA  . GLU F  2 29  ? 46.017  72.408 -9.159  1.00 40.86  ? 29   GLU F CA  1 
ATOM   10495 C C   . GLU F  2 29  ? 46.428  73.685 -8.421  1.00 43.07  ? 29   GLU F C   1 
ATOM   10496 O O   . GLU F  2 29  ? 47.593  74.077 -8.458  1.00 45.94  ? 29   GLU F O   1 
ATOM   10497 C CB  . GLU F  2 29  ? 45.446  72.787 -10.528 1.00 40.98  ? 29   GLU F CB  1 
ATOM   10498 C CG  . GLU F  2 29  ? 45.313  71.625 -11.503 1.00 39.96  ? 29   GLU F CG  1 
ATOM   10499 C CD  . GLU F  2 29  ? 45.167  72.080 -12.952 1.00 40.97  ? 29   GLU F CD  1 
ATOM   10500 O OE1 . GLU F  2 29  ? 44.872  73.274 -13.195 1.00 42.01  ? 29   GLU F OE1 1 
ATOM   10501 O OE2 . GLU F  2 29  ? 45.337  71.239 -13.857 1.00 40.97  ? 29   GLU F OE2 1 
ATOM   10502 N N   . GLN F  2 30  ? 45.466  74.330 -7.764  1.00 42.22  ? 30   GLN F N   1 
ATOM   10503 C CA  . GLN F  2 30  ? 45.706  75.595 -7.056  1.00 44.67  ? 30   GLN F CA  1 
ATOM   10504 C C   . GLN F  2 30  ? 46.515  75.439 -5.765  1.00 45.54  ? 30   GLN F C   1 
ATOM   10505 O O   . GLN F  2 30  ? 47.195  76.369 -5.347  1.00 48.67  ? 30   GLN F O   1 
ATOM   10506 C CB  . GLN F  2 30  ? 44.374  76.275 -6.745  1.00 43.93  ? 30   GLN F CB  1 
ATOM   10507 C CG  . GLN F  2 30  ? 43.614  76.714 -7.989  1.00 44.03  ? 30   GLN F CG  1 
ATOM   10508 C CD  . GLN F  2 30  ? 42.166  76.259 -7.979  1.00 41.55  ? 30   GLN F CD  1 
ATOM   10509 O OE1 . GLN F  2 30  ? 41.844  75.154 -8.440  1.00 39.31  ? 30   GLN F OE1 1 
ATOM   10510 N NE2 . GLN F  2 30  ? 41.281  77.113 -7.460  1.00 42.45  ? 30   GLN F NE2 1 
ATOM   10511 N N   . GLY F  2 31  ? 46.434  74.276 -5.130  1.00 43.09  ? 31   GLY F N   1 
ATOM   10512 C CA  . GLY F  2 31  ? 47.207  74.016 -3.917  1.00 43.91  ? 31   GLY F CA  1 
ATOM   10513 C C   . GLY F  2 31  ? 46.597  72.955 -3.029  1.00 40.74  ? 31   GLY F C   1 
ATOM   10514 O O   . GLY F  2 31  ? 45.752  72.186 -3.466  1.00 38.09  ? 31   GLY F O   1 
ATOM   10515 N N   . SER F  2 32  ? 47.043  72.916 -1.779  1.00 41.34  ? 32   SER F N   1 
ATOM   10516 C CA  . SER F  2 32  ? 46.493  72.007 -0.782  1.00 38.65  ? 32   SER F CA  1 
ATOM   10517 C C   . SER F  2 32  ? 46.343  72.708 0.557   1.00 39.39  ? 32   SER F C   1 
ATOM   10518 O O   . SER F  2 32  ? 46.935  73.760 0.779   1.00 42.46  ? 32   SER F O   1 
ATOM   10519 C CB  . SER F  2 32  ? 47.393  70.784 -0.630  1.00 38.64  ? 32   SER F CB  1 
ATOM   10520 O OG  . SER F  2 32  ? 48.714  71.163 -0.312  1.00 42.05  ? 32   SER F OG  1 
ATOM   10521 N N   . GLY F  2 33  ? 45.550  72.128 1.452   1.00 36.92  ? 33   GLY F N   1 
ATOM   10522 C CA  . GLY F  2 33  ? 45.364  72.715 2.774   1.00 37.61  ? 33   GLY F CA  1 
ATOM   10523 C C   . GLY F  2 33  ? 44.428  71.970 3.704   1.00 34.76  ? 33   GLY F C   1 
ATOM   10524 O O   . GLY F  2 33  ? 43.626  71.150 3.270   1.00 32.22  ? 33   GLY F O   1 
ATOM   10525 N N   . TYR F  2 34  ? 44.540  72.279 4.994   1.00 35.55  ? 34   TYR F N   1 
ATOM   10526 C CA  . TYR F  2 34  ? 43.688  71.705 6.025   1.00 33.31  ? 34   TYR F CA  1 
ATOM   10527 C C   . TYR F  2 34  ? 42.566  72.669 6.380   1.00 33.78  ? 34   TYR F C   1 
ATOM   10528 O O   . TYR F  2 34  ? 42.791  73.864 6.517   1.00 36.61  ? 34   TYR F O   1 
ATOM   10529 C CB  . TYR F  2 34  ? 44.503  71.408 7.280   1.00 34.08  ? 34   TYR F CB  1 
ATOM   10530 C CG  . TYR F  2 34  ? 45.629  70.421 7.073   1.00 34.22  ? 34   TYR F CG  1 
ATOM   10531 C CD1 . TYR F  2 34  ? 45.390  69.053 7.070   1.00 31.68  ? 34   TYR F CD1 1 
ATOM   10532 C CD2 . TYR F  2 34  ? 46.937  70.856 6.885   1.00 37.45  ? 34   TYR F CD2 1 
ATOM   10533 C CE1 . TYR F  2 34  ? 46.421  68.149 6.882   1.00 32.39  ? 34   TYR F CE1 1 
ATOM   10534 C CE2 . TYR F  2 34  ? 47.972  69.957 6.697   1.00 38.19  ? 34   TYR F CE2 1 
ATOM   10535 C CZ  . TYR F  2 34  ? 47.709  68.607 6.697   1.00 35.67  ? 34   TYR F CZ  1 
ATOM   10536 O OH  . TYR F  2 34  ? 48.734  67.711 6.513   1.00 36.94  ? 34   TYR F OH  1 
ATOM   10537 N N   . ALA F  2 35  ? 41.355  72.141 6.518   1.00 31.53  ? 35   ALA F N   1 
ATOM   10538 C CA  . ALA F  2 35  ? 40.208  72.925 6.959   1.00 32.25  ? 35   ALA F CA  1 
ATOM   10539 C C   . ALA F  2 35  ? 39.434  72.132 8.002   1.00 30.35  ? 35   ALA F C   1 
ATOM   10540 O O   . ALA F  2 35  ? 38.940  71.045 7.724   1.00 28.02  ? 35   ALA F O   1 
ATOM   10541 C CB  . ALA F  2 35  ? 39.314  73.260 5.782   1.00 32.26  ? 35   ALA F CB  1 
ATOM   10542 N N   . ALA F  2 36  ? 39.347  72.669 9.212   1.00 31.70  ? 36   ALA F N   1 
ATOM   10543 C CA  . ALA F  2 36  ? 38.646  71.997 10.292  1.00 30.21  ? 36   ALA F CA  1 
ATOM   10544 C C   . ALA F  2 36  ? 37.138  72.075 10.087  1.00 30.01  ? 36   ALA F C   1 
ATOM   10545 O O   . ALA F  2 36  ? 36.608  73.127 9.742   1.00 32.20  ? 36   ALA F O   1 
ATOM   10546 C CB  . ALA F  2 36  ? 39.021  72.615 11.628  1.00 32.03  ? 36   ALA F CB  1 
ATOM   10547 N N   . ASP F  2 37  ? 36.456  70.953 10.298  1.00 27.89  ? 37   ASP F N   1 
ATOM   10548 C CA  . ASP F  2 37  ? 34.999  70.914 10.299  1.00 28.14  ? 37   ASP F CA  1 
ATOM   10549 C C   . ASP F  2 37  ? 34.492  71.419 11.658  1.00 29.64  ? 37   ASP F C   1 
ATOM   10550 O O   . ASP F  2 37  ? 34.665  70.752 12.686  1.00 28.39  ? 37   ASP F O   1 
ATOM   10551 C CB  . ASP F  2 37  ? 34.509  69.490 10.023  1.00 25.75  ? 37   ASP F CB  1 
ATOM   10552 C CG  . ASP F  2 37  ? 33.009  69.413 9.851   1.00 26.45  ? 37   ASP F CG  1 
ATOM   10553 O OD1 . ASP F  2 37  ? 32.296  69.292 10.873  1.00 26.81  ? 37   ASP F OD1 1 
ATOM   10554 O OD2 . ASP F  2 37  ? 32.543  69.484 8.694   1.00 26.89  ? 37   ASP F OD2 1 
ATOM   10555 N N   . LYS F  2 38  ? 33.876  72.602 11.651  1.00 32.61  ? 38   LYS F N   1 
ATOM   10556 C CA  . LYS F  2 38  ? 33.444  73.264 12.885  1.00 34.84  ? 38   LYS F CA  1 
ATOM   10557 C C   . LYS F  2 38  ? 32.300  72.540 13.587  1.00 34.19  ? 38   LYS F C   1 
ATOM   10558 O O   . LYS F  2 38  ? 32.354  72.325 14.799  1.00 34.01  ? 38   LYS F O   1 
ATOM   10559 C CB  . LYS F  2 38  ? 33.030  74.714 12.610  1.00 38.75  ? 38   LYS F CB  1 
ATOM   10560 C CG  . LYS F  2 38  ? 34.199  75.670 12.419  1.00 40.69  ? 38   LYS F CG  1 
ATOM   10561 C CD  . LYS F  2 38  ? 33.738  77.122 12.370  1.00 45.21  ? 38   LYS F CD  1 
ATOM   10562 C CE  . LYS F  2 38  ? 33.179  77.496 11.003  1.00 46.12  ? 38   LYS F CE  1 
ATOM   10563 N NZ  . LYS F  2 38  ? 32.550  78.851 11.015  1.00 50.93  ? 38   LYS F NZ  1 
ATOM   10564 N N   . GLU F  2 39  ? 31.268  72.178 12.825  1.00 34.20  ? 39   GLU F N   1 
ATOM   10565 C CA  . GLU F  2 39  ? 30.076  71.523 13.380  1.00 34.28  ? 39   GLU F CA  1 
ATOM   10566 C C   . GLU F  2 39  ? 30.414  70.270 14.194  1.00 31.34  ? 39   GLU F C   1 
ATOM   10567 O O   . GLU F  2 39  ? 30.069  70.187 15.371  1.00 31.82  ? 39   GLU F O   1 
ATOM   10568 C CB  . GLU F  2 39  ? 29.071  71.184 12.263  1.00 34.88  ? 39   GLU F CB  1 
ATOM   10569 C CG  . GLU F  2 39  ? 27.973  70.196 12.667  1.00 34.82  ? 39   GLU F CG  1 
ATOM   10570 C CD  . GLU F  2 39  ? 26.582  70.625 12.217  1.00 38.23  ? 39   GLU F CD  1 
ATOM   10571 O OE1 . GLU F  2 39  ? 26.413  70.992 11.030  1.00 39.25  ? 39   GLU F OE1 1 
ATOM   10572 O OE2 . GLU F  2 39  ? 25.655  70.611 13.064  1.00 40.28  ? 39   GLU F OE2 1 
ATOM   10573 N N   . SER F  2 40  ? 31.084  69.306 13.570  1.00 28.57  ? 40   SER F N   1 
ATOM   10574 C CA  . SER F  2 40  ? 31.432  68.063 14.255  1.00 26.12  ? 40   SER F CA  1 
ATOM   10575 C C   . SER F  2 40  ? 32.392  68.302 15.415  1.00 25.73  ? 40   SER F C   1 
ATOM   10576 O O   . SER F  2 40  ? 32.322  67.611 16.433  1.00 24.77  ? 40   SER F O   1 
ATOM   10577 C CB  . SER F  2 40  ? 32.032  67.045 13.284  1.00 24.01  ? 40   SER F CB  1 
ATOM   10578 O OG  . SER F  2 40  ? 33.222  67.531 12.692  1.00 23.82  ? 40   SER F OG  1 
ATOM   10579 N N   . THR F  2 41  ? 33.278  69.284 15.261  1.00 26.76  ? 41   THR F N   1 
ATOM   10580 C CA  . THR F  2 41  ? 34.245  69.618 16.307  1.00 27.09  ? 41   THR F CA  1 
ATOM   10581 C C   . THR F  2 41  ? 33.572  70.235 17.534  1.00 28.94  ? 41   THR F C   1 
ATOM   10582 O O   . THR F  2 41  ? 33.856  69.840 18.665  1.00 28.32  ? 41   THR F O   1 
ATOM   10583 C CB  . THR F  2 41  ? 35.337  70.571 15.782  1.00 28.54  ? 41   THR F CB  1 
ATOM   10584 O OG1 . THR F  2 41  ? 36.055  69.930 14.724  1.00 26.89  ? 41   THR F OG1 1 
ATOM   10585 C CG2 . THR F  2 41  ? 36.319  70.929 16.881  1.00 29.58  ? 41   THR F CG2 1 
ATOM   10586 N N   . GLN F  2 42  ? 32.687  71.201 17.309  1.00 31.49  ? 42   GLN F N   1 
ATOM   10587 C CA  . GLN F  2 42  ? 31.989  71.867 18.408  1.00 33.96  ? 42   GLN F CA  1 
ATOM   10588 C C   . GLN F  2 42  ? 31.075  70.896 19.138  1.00 32.75  ? 42   GLN F C   1 
ATOM   10589 O O   . GLN F  2 42  ? 30.900  70.993 20.347  1.00 33.61  ? 42   GLN F O   1 
ATOM   10590 C CB  . GLN F  2 42  ? 31.173  73.054 17.894  1.00 37.49  ? 42   GLN F CB  1 
ATOM   10591 C CG  . GLN F  2 42  ? 30.527  73.887 18.993  1.00 40.96  ? 42   GLN F CG  1 
ATOM   10592 C CD  . GLN F  2 42  ? 31.534  74.421 19.995  1.00 42.01  ? 42   GLN F CD  1 
ATOM   10593 O OE1 . GLN F  2 42  ? 31.445  74.147 21.191  1.00 41.94  ? 42   GLN F OE1 1 
ATOM   10594 N NE2 . GLN F  2 42  ? 32.506  75.181 19.507  1.00 43.22  ? 42   GLN F NE2 1 
ATOM   10595 N N   . LYS F  2 43  ? 30.494  69.964 18.389  1.00 31.05  ? 43   LYS F N   1 
ATOM   10596 C CA  . LYS F  2 43  ? 29.638  68.924 18.960  1.00 30.12  ? 43   LYS F CA  1 
ATOM   10597 C C   . LYS F  2 43  ? 30.433  68.001 19.876  1.00 27.52  ? 43   LYS F C   1 
ATOM   10598 O O   . LYS F  2 43  ? 29.928  67.567 20.912  1.00 27.58  ? 43   LYS F O   1 
ATOM   10599 C CB  . LYS F  2 43  ? 28.979  68.104 17.844  1.00 29.32  ? 43   LYS F CB  1 
ATOM   10600 C CG  . LYS F  2 43  ? 27.484  67.893 18.018  1.00 31.44  ? 43   LYS F CG  1 
ATOM   10601 C CD  . LYS F  2 43  ? 26.832  67.629 16.670  1.00 32.06  ? 43   LYS F CD  1 
ATOM   10602 C CE  . LYS F  2 43  ? 25.364  67.246 16.797  1.00 34.47  ? 43   LYS F CE  1 
ATOM   10603 N NZ  . LYS F  2 43  ? 24.925  66.501 15.580  1.00 34.30  ? 43   LYS F NZ  1 
ATOM   10604 N N   . ALA F  2 44  ? 31.672  67.704 19.484  1.00 25.53  ? 44   ALA F N   1 
ATOM   10605 C CA  . ALA F  2 44  ? 32.570  66.888 20.297  1.00 23.52  ? 44   ALA F CA  1 
ATOM   10606 C C   . ALA F  2 44  ? 33.011  67.640 21.541  1.00 24.86  ? 44   ALA F C   1 
ATOM   10607 O O   . ALA F  2 44  ? 33.077  67.069 22.625  1.00 24.13  ? 44   ALA F O   1 
ATOM   10608 C CB  . ALA F  2 44  ? 33.783  66.461 19.491  1.00 21.94  ? 44   ALA F CB  1 
ATOM   10609 N N   . ILE F  2 45  ? 33.317  68.924 21.383  1.00 27.11  ? 45   ILE F N   1 
ATOM   10610 C CA  . ILE F  2 45  ? 33.698  69.763 22.520  1.00 29.18  ? 45   ILE F CA  1 
ATOM   10611 C C   . ILE F  2 45  ? 32.581  69.814 23.567  1.00 30.39  ? 45   ILE F C   1 
ATOM   10612 O O   . ILE F  2 45  ? 32.852  69.744 24.765  1.00 30.66  ? 45   ILE F O   1 
ATOM   10613 C CB  . ILE F  2 45  ? 34.096  71.186 22.061  1.00 32.16  ? 45   ILE F CB  1 
ATOM   10614 C CG1 . ILE F  2 45  ? 35.491  71.152 21.427  1.00 31.41  ? 45   ILE F CG1 1 
ATOM   10615 C CG2 . ILE F  2 45  ? 34.082  72.167 23.227  1.00 35.35  ? 45   ILE F CG2 1 
ATOM   10616 C CD1 . ILE F  2 45  ? 35.841  72.389 20.626  1.00 34.12  ? 45   ILE F CD1 1 
ATOM   10617 N N   . ASP F  2 46  ? 31.335  69.926 23.111  1.00 31.39  ? 46   ASP F N   1 
ATOM   10618 C CA  . ASP F  2 46  ? 30.184  69.974 24.013  1.00 33.09  ? 46   ASP F CA  1 
ATOM   10619 C C   . ASP F  2 46  ? 29.976  68.654 24.740  1.00 30.62  ? 46   ASP F C   1 
ATOM   10620 O O   . ASP F  2 46  ? 29.744  68.632 25.942  1.00 31.39  ? 46   ASP F O   1 
ATOM   10621 C CB  . ASP F  2 46  ? 28.913  70.344 23.245  1.00 35.25  ? 46   ASP F CB  1 
ATOM   10622 C CG  . ASP F  2 46  ? 28.984  71.723 22.626  1.00 38.31  ? 46   ASP F CG  1 
ATOM   10623 O OD1 . ASP F  2 46  ? 29.975  72.438 22.879  1.00 39.12  ? 46   ASP F OD1 1 
ATOM   10624 O OD2 . ASP F  2 46  ? 28.052  72.091 21.882  1.00 40.30  ? 46   ASP F OD2 1 
ATOM   10625 N N   . GLY F  2 47  ? 30.058  67.555 24.005  1.00 27.91  ? 47   GLY F N   1 
ATOM   10626 C CA  . GLY F  2 47  ? 29.882  66.235 24.592  1.00 25.86  ? 47   GLY F CA  1 
ATOM   10627 C C   . GLY F  2 47  ? 30.904  65.904 25.666  1.00 24.53  ? 47   GLY F C   1 
ATOM   10628 O O   . GLY F  2 47  ? 30.559  65.341 26.707  1.00 24.30  ? 47   GLY F O   1 
ATOM   10629 N N   . VAL F  2 48  ? 32.161  66.262 25.419  1.00 23.98  ? 48   VAL F N   1 
ATOM   10630 C CA  . VAL F  2 48  ? 33.242  66.003 26.371  1.00 23.21  ? 48   VAL F CA  1 
ATOM   10631 C C   . VAL F  2 48  ? 33.165  66.931 27.588  1.00 25.57  ? 48   VAL F C   1 
ATOM   10632 O O   . VAL F  2 48  ? 33.427  66.506 28.709  1.00 25.16  ? 48   VAL F O   1 
ATOM   10633 C CB  . VAL F  2 48  ? 34.622  66.116 25.687  1.00 22.61  ? 48   VAL F CB  1 
ATOM   10634 C CG1 . VAL F  2 48  ? 35.750  66.143 26.712  1.00 22.97  ? 48   VAL F CG1 1 
ATOM   10635 C CG2 . VAL F  2 48  ? 34.815  64.963 24.710  1.00 20.29  ? 48   VAL F CG2 1 
ATOM   10636 N N   . THR F  2 49  ? 32.812  68.192 27.369  1.00 28.33  ? 49   THR F N   1 
ATOM   10637 C CA  . THR F  2 49  ? 32.673  69.139 28.463  1.00 31.28  ? 49   THR F CA  1 
ATOM   10638 C C   . THR F  2 49  ? 31.590  68.679 29.437  1.00 31.62  ? 49   THR F C   1 
ATOM   10639 O O   . THR F  2 49  ? 31.828  68.600 30.646  1.00 32.03  ? 49   THR F O   1 
ATOM   10640 C CB  . THR F  2 49  ? 32.344  70.548 27.944  1.00 34.73  ? 49   THR F CB  1 
ATOM   10641 O OG1 . THR F  2 49  ? 33.392  70.994 27.078  1.00 34.71  ? 49   THR F OG1 1 
ATOM   10642 C CG2 . THR F  2 49  ? 32.199  71.529 29.088  1.00 38.33  ? 49   THR F CG2 1 
ATOM   10643 N N   . ASN F  2 50  ? 30.409  68.371 28.907  1.00 31.75  ? 50   ASN F N   1 
ATOM   10644 C CA  . ASN F  2 50  ? 29.297  67.875 29.726  1.00 32.43  ? 50   ASN F CA  1 
ATOM   10645 C C   . ASN F  2 50  ? 29.676  66.626 30.507  1.00 29.73  ? 50   ASN F C   1 
ATOM   10646 O O   . ASN F  2 50  ? 29.352  66.490 31.680  1.00 30.51  ? 50   ASN F O   1 
ATOM   10647 C CB  . ASN F  2 50  ? 28.094  67.555 28.845  1.00 32.91  ? 50   ASN F CB  1 
ATOM   10648 C CG  . ASN F  2 50  ? 27.439  68.795 28.281  1.00 36.47  ? 50   ASN F CG  1 
ATOM   10649 O OD1 . ASN F  2 50  ? 27.126  69.725 29.016  1.00 39.75  ? 50   ASN F OD1 1 
ATOM   10650 N ND2 . ASN F  2 50  ? 27.217  68.812 26.976  1.00 36.19  ? 50   ASN F ND2 1 
ATOM   10651 N N   . LYS F  2 51  ? 30.363  65.718 29.830  1.00 26.88  ? 51   LYS F N   1 
ATOM   10652 C CA  . LYS F  2 51  ? 30.846  64.478 30.428  1.00 24.50  ? 51   LYS F CA  1 
ATOM   10653 C C   . LYS F  2 51  ? 31.750  64.713 31.630  1.00 24.82  ? 51   LYS F C   1 
ATOM   10654 O O   . LYS F  2 51  ? 31.621  64.045 32.654  1.00 24.28  ? 51   LYS F O   1 
ATOM   10655 C CB  . LYS F  2 51  ? 31.605  63.699 29.366  1.00 22.10  ? 51   LYS F CB  1 
ATOM   10656 C CG  . LYS F  2 51  ? 32.322  62.453 29.833  1.00 19.94  ? 51   LYS F CG  1 
ATOM   10657 C CD  . LYS F  2 51  ? 32.971  61.803 28.622  1.00 18.36  ? 51   LYS F CD  1 
ATOM   10658 C CE  . LYS F  2 51  ? 32.816  60.301 28.619  1.00 16.86  ? 51   LYS F CE  1 
ATOM   10659 N NZ  . LYS F  2 51  ? 32.510  59.773 27.264  1.00 16.37  ? 51   LYS F NZ  1 
ATOM   10660 N N   . VAL F  2 52  ? 32.675  65.655 31.496  1.00 26.03  ? 52   VAL F N   1 
ATOM   10661 C CA  . VAL F  2 52  ? 33.606  65.962 32.571  1.00 26.92  ? 52   VAL F CA  1 
ATOM   10662 C C   . VAL F  2 52  ? 32.850  66.555 33.762  1.00 29.41  ? 52   VAL F C   1 
ATOM   10663 O O   . VAL F  2 52  ? 33.098  66.170 34.904  1.00 29.24  ? 52   VAL F O   1 
ATOM   10664 C CB  . VAL F  2 52  ? 34.719  66.917 32.090  1.00 28.37  ? 52   VAL F CB  1 
ATOM   10665 C CG1 . VAL F  2 52  ? 35.545  67.437 33.260  1.00 30.31  ? 52   VAL F CG1 1 
ATOM   10666 C CG2 . VAL F  2 52  ? 35.621  66.210 31.088  1.00 26.16  ? 52   VAL F CG2 1 
ATOM   10667 N N   . ASN F  2 53  ? 31.922  67.470 33.486  1.00 32.02  ? 53   ASN F N   1 
ATOM   10668 C CA  . ASN F  2 53  ? 31.099  68.089 34.530  1.00 35.06  ? 53   ASN F CA  1 
ATOM   10669 C C   . ASN F  2 53  ? 30.136  67.089 35.166  1.00 34.12  ? 53   ASN F C   1 
ATOM   10670 O O   . ASN F  2 53  ? 29.910  67.116 36.375  1.00 35.31  ? 53   ASN F O   1 
ATOM   10671 C CB  . ASN F  2 53  ? 30.307  69.269 33.966  1.00 38.49  ? 53   ASN F CB  1 
ATOM   10672 C CG  . ASN F  2 53  ? 31.198  70.319 33.324  1.00 40.07  ? 53   ASN F CG  1 
ATOM   10673 O OD1 . ASN F  2 53  ? 32.365  70.460 33.684  1.00 39.94  ? 53   ASN F OD1 1 
ATOM   10674 N ND2 . ASN F  2 53  ? 30.651  71.056 32.360  1.00 41.92  ? 53   ASN F ND2 1 
ATOM   10675 N N   . SER F  2 54  ? 29.573  66.211 34.340  1.00 32.32  ? 54   SER F N   1 
ATOM   10676 C CA  . SER F  2 54  ? 28.700  65.139 34.819  1.00 31.58  ? 54   SER F CA  1 
ATOM   10677 C C   . SER F  2 54  ? 29.441  64.227 35.777  1.00 29.59  ? 54   SER F C   1 
ATOM   10678 O O   . SER F  2 54  ? 28.901  63.839 36.812  1.00 30.19  ? 54   SER F O   1 
ATOM   10679 C CB  . SER F  2 54  ? 28.153  64.310 33.653  1.00 30.05  ? 54   SER F CB  1 
ATOM   10680 O OG  . SER F  2 54  ? 27.099  64.988 32.998  1.00 32.63  ? 54   SER F OG  1 
ATOM   10681 N N   . ILE F  2 55  ? 30.676  63.887 35.416  1.00 27.63  ? 55   ILE F N   1 
ATOM   10682 C CA  . ILE F  2 55  ? 31.539  63.062 36.258  1.00 26.09  ? 55   ILE F CA  1 
ATOM   10683 C C   . ILE F  2 55  ? 31.870  63.775 37.566  1.00 28.19  ? 55   ILE F C   1 
ATOM   10684 O O   . ILE F  2 55  ? 31.708  63.206 38.645  1.00 28.00  ? 55   ILE F O   1 
ATOM   10685 C CB  . ILE F  2 55  ? 32.841  62.678 35.521  1.00 24.18  ? 55   ILE F CB  1 
ATOM   10686 C CG1 . ILE F  2 55  ? 32.533  61.626 34.452  1.00 22.19  ? 55   ILE F CG1 1 
ATOM   10687 C CG2 . ILE F  2 55  ? 33.882  62.136 36.495  1.00 23.45  ? 55   ILE F CG2 1 
ATOM   10688 C CD1 . ILE F  2 55  ? 33.687  61.311 33.523  1.00 20.80  ? 55   ILE F CD1 1 
ATOM   10689 N N   . ILE F  2 56  ? 32.336  65.014 37.463  1.00 30.58  ? 56   ILE F N   1 
ATOM   10690 C CA  . ILE F  2 56  ? 32.643  65.820 38.642  1.00 33.32  ? 56   ILE F CA  1 
ATOM   10691 C C   . ILE F  2 56  ? 31.453  65.856 39.610  1.00 35.20  ? 56   ILE F C   1 
ATOM   10692 O O   . ILE F  2 56  ? 31.617  65.601 40.807  1.00 35.53  ? 56   ILE F O   1 
ATOM   10693 C CB  . ILE F  2 56  ? 33.045  67.260 38.242  1.00 36.31  ? 56   ILE F CB  1 
ATOM   10694 C CG1 . ILE F  2 56  ? 34.450  67.264 37.628  1.00 35.34  ? 56   ILE F CG1 1 
ATOM   10695 C CG2 . ILE F  2 56  ? 32.993  68.204 39.442  1.00 39.94  ? 56   ILE F CG2 1 
ATOM   10696 C CD1 . ILE F  2 56  ? 34.819  68.561 36.937  1.00 38.08  ? 56   ILE F CD1 1 
ATOM   10697 N N   . ASP F  2 57  ? 30.263  66.161 39.087  1.00 36.81  ? 57   ASP F N   1 
ATOM   10698 C CA  . ASP F  2 57  ? 29.072  66.367 39.925  1.00 39.55  ? 57   ASP F CA  1 
ATOM   10699 C C   . ASP F  2 57  ? 28.560  65.104 40.611  1.00 37.94  ? 57   ASP F C   1 
ATOM   10700 O O   . ASP F  2 57  ? 28.092  65.159 41.745  1.00 39.68  ? 57   ASP F O   1 
ATOM   10701 C CB  . ASP F  2 57  ? 27.945  67.014 39.118  1.00 42.05  ? 57   ASP F CB  1 
ATOM   10702 C CG  . ASP F  2 57  ? 28.129  68.511 38.969  1.00 45.76  ? 57   ASP F CG  1 
ATOM   10703 O OD1 . ASP F  2 57  ? 28.309  69.186 40.012  1.00 48.51  ? 57   ASP F OD1 1 
ATOM   10704 O OD2 . ASP F  2 57  ? 28.096  69.013 37.820  1.00 46.23  ? 57   ASP F OD2 1 
ATOM   10705 N N   . LYS F  2 58  ? 28.645  63.968 39.933  1.00 35.03  ? 58   LYS F N   1 
ATOM   10706 C CA  . LYS F  2 58  ? 28.237  62.706 40.544  1.00 33.71  ? 58   LYS F CA  1 
ATOM   10707 C C   . LYS F  2 58  ? 29.123  62.324 41.728  1.00 32.99  ? 58   LYS F C   1 
ATOM   10708 O O   . LYS F  2 58  ? 28.652  61.705 42.681  1.00 33.17  ? 58   LYS F O   1 
ATOM   10709 C CB  . LYS F  2 58  ? 28.189  61.580 39.499  1.00 31.08  ? 58   LYS F CB  1 
ATOM   10710 C CG  . LYS F  2 58  ? 26.782  61.167 39.079  1.00 32.30  ? 58   LYS F CG  1 
ATOM   10711 C CD  . LYS F  2 58  ? 25.828  62.349 38.923  1.00 35.83  ? 58   LYS F CD  1 
ATOM   10712 C CE  . LYS F  2 58  ? 24.405  61.883 38.704  1.00 37.73  ? 58   LYS F CE  1 
ATOM   10713 N NZ  . LYS F  2 58  ? 23.442  63.013 38.791  1.00 41.96  ? 58   LYS F NZ  1 
ATOM   10714 N N   . MET F  2 59  ? 30.390  62.717 41.677  1.00 32.69  ? 59   MET F N   1 
ATOM   10715 C CA  . MET F  2 59  ? 31.326  62.442 42.766  1.00 32.45  ? 59   MET F CA  1 
ATOM   10716 C C   . MET F  2 59  ? 31.278  63.526 43.852  1.00 35.80  ? 59   MET F C   1 
ATOM   10717 O O   . MET F  2 59  ? 31.688  63.284 44.988  1.00 35.97  ? 59   MET F O   1 
ATOM   10718 C CB  . MET F  2 59  ? 32.744  62.313 42.206  1.00 30.96  ? 59   MET F CB  1 
ATOM   10719 C CG  . MET F  2 59  ? 32.873  61.287 41.086  1.00 28.30  ? 59   MET F CG  1 
ATOM   10720 S SD  . MET F  2 59  ? 32.505  59.599 41.607  1.00 26.43  ? 59   MET F SD  1 
ATOM   10721 C CE  . MET F  2 59  ? 33.749  59.264 42.847  1.00 26.19  ? 59   MET F CE  1 
ATOM   10722 N N   . ASN F  2 60  ? 30.764  64.705 43.495  1.00 38.82  ? 60   ASN F N   1 
ATOM   10723 C CA  . ASN F  2 60  ? 30.688  65.866 44.402  1.00 42.86  ? 60   ASN F CA  1 
ATOM   10724 C C   . ASN F  2 60  ? 30.086  65.581 45.795  1.00 44.23  ? 60   ASN F C   1 
ATOM   10725 O O   . ASN F  2 60  ? 30.590  66.100 46.795  1.00 46.22  ? 60   ASN F O   1 
ATOM   10726 C CB  . ASN F  2 60  ? 29.980  67.050 43.698  1.00 46.06  ? 60   ASN F CB  1 
ATOM   10727 C CG  . ASN F  2 60  ? 29.172  67.921 44.648  1.00 50.51  ? 60   ASN F CG  1 
ATOM   10728 O OD1 . ASN F  2 60  ? 28.109  67.518 45.115  1.00 51.25  ? 60   ASN F OD1 1 
ATOM   10729 N ND2 . ASN F  2 60  ? 29.657  69.132 44.913  1.00 54.04  ? 60   ASN F ND2 1 
ATOM   10730 N N   . THR F  2 61  ? 29.024  64.776 45.870  1.00 43.57  ? 61   THR F N   1 
ATOM   10731 C CA  . THR F  2 61  ? 28.533  64.294 47.176  1.00 44.41  ? 61   THR F CA  1 
ATOM   10732 C C   . THR F  2 61  ? 29.028  62.862 47.377  1.00 40.59  ? 61   THR F C   1 
ATOM   10733 O O   . THR F  2 61  ? 28.655  61.948 46.630  1.00 38.46  ? 61   THR F O   1 
ATOM   10734 C CB  . THR F  2 61  ? 26.989  64.340 47.333  1.00 46.97  ? 61   THR F CB  1 
ATOM   10735 O OG1 . THR F  2 61  ? 26.398  63.183 46.729  1.00 44.84  ? 61   THR F OG1 1 
ATOM   10736 C CG2 . THR F  2 61  ? 26.388  65.600 46.713  1.00 50.58  ? 61   THR F CG2 1 
ATOM   10737 N N   . GLN F  2 62  ? 29.889  62.681 48.371  1.00 40.14  ? 62   GLN F N   1 
ATOM   10738 C CA  . GLN F  2 62  ? 30.471  61.374 48.658  1.00 37.04  ? 62   GLN F CA  1 
ATOM   10739 C C   . GLN F  2 62  ? 30.965  61.351 50.104  1.00 37.85  ? 62   GLN F C   1 
ATOM   10740 O O   . GLN F  2 62  ? 31.039  62.399 50.759  1.00 40.89  ? 62   GLN F O   1 
ATOM   10741 C CB  . GLN F  2 62  ? 31.601  61.063 47.663  1.00 34.75  ? 62   GLN F CB  1 
ATOM   10742 C CG  . GLN F  2 62  ? 33.025  61.105 48.212  1.00 34.72  ? 62   GLN F CG  1 
ATOM   10743 C CD  . GLN F  2 62  ? 34.050  60.724 47.162  1.00 32.93  ? 62   GLN F CD  1 
ATOM   10744 O OE1 . GLN F  2 62  ? 33.775  60.782 45.959  1.00 32.17  ? 62   GLN F OE1 1 
ATOM   10745 N NE2 . GLN F  2 62  ? 35.242  60.326 47.610  1.00 32.61  ? 62   GLN F NE2 1 
ATOM   10746 N N   . PHE F  2 63  ? 31.306  60.161 50.595  1.00 35.44  ? 63   PHE F N   1 
ATOM   10747 C CA  . PHE F  2 63  ? 31.651  59.978 52.007  1.00 36.04  ? 63   PHE F CA  1 
ATOM   10748 C C   . PHE F  2 63  ? 32.773  60.916 52.471  1.00 37.71  ? 63   PHE F C   1 
ATOM   10749 O O   . PHE F  2 63  ? 33.732  61.164 51.736  1.00 37.32  ? 63   PHE F O   1 
ATOM   10750 C CB  . PHE F  2 63  ? 32.040  58.520 52.294  1.00 33.39  ? 63   PHE F CB  1 
ATOM   10751 C CG  . PHE F  2 63  ? 32.255  58.239 53.753  1.00 34.15  ? 63   PHE F CG  1 
ATOM   10752 C CD1 . PHE F  2 63  ? 31.175  58.202 54.631  1.00 35.52  ? 63   PHE F CD1 1 
ATOM   10753 C CD2 . PHE F  2 63  ? 33.537  58.043 54.257  1.00 33.87  ? 63   PHE F CD2 1 
ATOM   10754 C CE1 . PHE F  2 63  ? 31.369  57.962 55.981  1.00 36.29  ? 63   PHE F CE1 1 
ATOM   10755 C CE2 . PHE F  2 63  ? 33.738  57.801 55.606  1.00 34.75  ? 63   PHE F CE2 1 
ATOM   10756 C CZ  . PHE F  2 63  ? 32.654  57.760 56.469  1.00 35.79  ? 63   PHE F CZ  1 
ATOM   10757 N N   . GLU F  2 64  ? 32.625  61.442 53.685  1.00 39.96  ? 64   GLU F N   1 
ATOM   10758 C CA  . GLU F  2 64  ? 33.651  62.257 54.325  1.00 42.12  ? 64   GLU F CA  1 
ATOM   10759 C C   . GLU F  2 64  ? 34.016  61.640 55.666  1.00 41.98  ? 64   GLU F C   1 
ATOM   10760 O O   . GLU F  2 64  ? 33.135  61.344 56.477  1.00 42.45  ? 64   GLU F O   1 
ATOM   10761 C CB  . GLU F  2 64  ? 33.139  63.674 54.561  1.00 46.18  ? 64   GLU F CB  1 
ATOM   10762 C CG  . GLU F  2 64  ? 32.862  64.463 53.294  1.00 46.86  ? 64   GLU F CG  1 
ATOM   10763 C CD  . GLU F  2 64  ? 32.314  65.848 53.583  1.00 51.46  ? 64   GLU F CD  1 
ATOM   10764 O OE1 . GLU F  2 64  ? 32.452  66.328 54.734  1.00 54.38  ? 64   GLU F OE1 1 
ATOM   10765 O OE2 . GLU F  2 64  ? 31.741  66.456 52.655  1.00 52.42  ? 64   GLU F OE2 1 
ATOM   10766 N N   . ALA F  2 65  ? 35.311  61.459 55.905  1.00 41.64  ? 65   ALA F N   1 
ATOM   10767 C CA  . ALA F  2 65  ? 35.783  60.898 57.169  1.00 41.76  ? 65   ALA F CA  1 
ATOM   10768 C C   . ALA F  2 65  ? 35.685  61.935 58.287  1.00 45.50  ? 65   ALA F C   1 
ATOM   10769 O O   . ALA F  2 65  ? 35.812  63.138 58.038  1.00 48.39  ? 65   ALA F O   1 
ATOM   10770 C CB  . ALA F  2 65  ? 37.214  60.400 57.029  1.00 41.04  ? 65   ALA F CB  1 
ATOM   10771 N N   . VAL F  2 66  ? 35.435  61.461 59.508  1.00 45.61  ? 66   VAL F N   1 
ATOM   10772 C CA  . VAL F  2 66  ? 35.436  62.319 60.699  1.00 49.33  ? 66   VAL F CA  1 
ATOM   10773 C C   . VAL F  2 66  ? 36.245  61.644 61.807  1.00 49.14  ? 66   VAL F C   1 
ATOM   10774 O O   . VAL F  2 66  ? 36.252  60.412 61.931  1.00 46.16  ? 66   VAL F O   1 
ATOM   10775 C CB  . VAL F  2 66  ? 34.003  62.625 61.199  1.00 50.78  ? 66   VAL F CB  1 
ATOM   10776 C CG1 . VAL F  2 66  ? 34.027  63.641 62.338  1.00 55.42  ? 66   VAL F CG1 1 
ATOM   10777 C CG2 . VAL F  2 66  ? 33.127  63.130 60.056  1.00 50.76  ? 66   VAL F CG2 1 
ATOM   10778 N N   . GLY F  2 67  ? 36.935  62.462 62.598  1.00 52.62  ? 67   GLY F N   1 
ATOM   10779 C CA  . GLY F  2 67  ? 37.784  61.973 63.673  1.00 53.19  ? 67   GLY F CA  1 
ATOM   10780 C C   . GLY F  2 67  ? 36.972  61.630 64.903  1.00 53.38  ? 67   GLY F C   1 
ATOM   10781 O O   . GLY F  2 67  ? 36.204  62.458 65.399  1.00 56.19  ? 67   GLY F O   1 
ATOM   10782 N N   . ARG F  2 68  ? 37.142  60.403 65.392  1.00 50.64  ? 68   ARG F N   1 
ATOM   10783 C CA  . ARG F  2 68  ? 36.431  59.921 66.571  1.00 50.56  ? 68   ARG F CA  1 
ATOM   10784 C C   . ARG F  2 68  ? 37.383  59.118 67.445  1.00 50.22  ? 68   ARG F C   1 
ATOM   10785 O O   . ARG F  2 68  ? 38.118  58.262 66.949  1.00 47.96  ? 68   ARG F O   1 
ATOM   10786 C CB  . ARG F  2 68  ? 35.222  59.080 66.150  1.00 47.38  ? 68   ARG F CB  1 
ATOM   10787 C CG  . ARG F  2 68  ? 34.031  59.931 65.737  1.00 48.76  ? 68   ARG F CG  1 
ATOM   10788 C CD  . ARG F  2 68  ? 32.789  59.116 65.428  1.00 46.42  ? 68   ARG F CD  1 
ATOM   10789 N NE  . ARG F  2 68  ? 32.937  58.238 64.277  1.00 42.79  ? 68   ARG F NE  1 
ATOM   10790 C CZ  . ARG F  2 68  ? 32.809  58.597 63.001  1.00 41.95  ? 68   ARG F CZ  1 
ATOM   10791 N NH1 . ARG F  2 68  ? 32.531  59.841 62.641  1.00 44.43  ? 68   ARG F NH1 1 
ATOM   10792 N NH2 . ARG F  2 68  ? 32.975  57.689 62.057  1.00 38.83  ? 68   ARG F NH2 1 
ATOM   10793 N N   . GLU F  2 69  ? 37.363  59.406 68.744  1.00 52.75  ? 69   GLU F N   1 
ATOM   10794 C CA  . GLU F  2 69  ? 38.327  58.858 69.691  1.00 53.45  ? 69   GLU F CA  1 
ATOM   10795 C C   . GLU F  2 69  ? 37.673  57.814 70.580  1.00 51.47  ? 69   GLU F C   1 
ATOM   10796 O O   . GLU F  2 69  ? 36.520  57.967 70.977  1.00 51.69  ? 69   GLU F O   1 
ATOM   10797 C CB  . GLU F  2 69  ? 38.877  59.978 70.574  1.00 58.49  ? 69   GLU F CB  1 
ATOM   10798 C CG  . GLU F  2 69  ? 39.588  61.096 69.820  1.00 61.28  ? 69   GLU F CG  1 
ATOM   10799 C CD  . GLU F  2 69  ? 41.083  60.868 69.712  1.00 62.42  ? 69   GLU F CD  1 
ATOM   10800 O OE1 . GLU F  2 69  ? 41.488  59.784 69.231  1.00 59.33  ? 69   GLU F OE1 1 
ATOM   10801 O OE2 . GLU F  2 69  ? 41.849  61.774 70.111  1.00 66.98  ? 69   GLU F OE2 1 
ATOM   10802 N N   . PHE F  2 70  ? 38.421  56.763 70.904  1.00 49.90  ? 70   PHE F N   1 
ATOM   10803 C CA  . PHE F  2 70  ? 37.929  55.689 71.766  1.00 48.24  ? 70   PHE F CA  1 
ATOM   10804 C C   . PHE F  2 70  ? 38.999  55.283 72.776  1.00 49.79  ? 70   PHE F C   1 
ATOM   10805 O O   . PHE F  2 70  ? 40.186  55.260 72.456  1.00 50.62  ? 70   PHE F O   1 
ATOM   10806 C CB  . PHE F  2 70  ? 37.532  54.477 70.922  1.00 44.25  ? 70   PHE F CB  1 
ATOM   10807 C CG  . PHE F  2 70  ? 36.622  54.806 69.773  1.00 42.63  ? 70   PHE F CG  1 
ATOM   10808 C CD1 . PHE F  2 70  ? 37.144  55.155 68.533  1.00 41.88  ? 70   PHE F CD1 1 
ATOM   10809 C CD2 . PHE F  2 70  ? 35.245  54.764 69.928  1.00 42.17  ? 70   PHE F CD2 1 
ATOM   10810 C CE1 . PHE F  2 70  ? 36.307  55.455 67.473  1.00 40.53  ? 70   PHE F CE1 1 
ATOM   10811 C CE2 . PHE F  2 70  ? 34.402  55.063 68.869  1.00 41.11  ? 70   PHE F CE2 1 
ATOM   10812 C CZ  . PHE F  2 70  ? 34.934  55.410 67.641  1.00 40.20  ? 70   PHE F CZ  1 
ATOM   10813 N N   . ASN F  2 71  ? 38.582  54.954 73.994  1.00 50.41  ? 71   ASN F N   1 
ATOM   10814 C CA  . ASN F  2 71  ? 39.536  54.565 75.033  1.00 52.16  ? 71   ASN F CA  1 
ATOM   10815 C C   . ASN F  2 71  ? 39.981  53.101 74.878  1.00 49.55  ? 71   ASN F C   1 
ATOM   10816 O O   . ASN F  2 71  ? 39.654  52.447 73.885  1.00 46.52  ? 71   ASN F O   1 
ATOM   10817 C CB  . ASN F  2 71  ? 38.992  54.886 76.442  1.00 54.48  ? 71   ASN F CB  1 
ATOM   10818 C CG  . ASN F  2 71  ? 37.850  53.978 76.869  1.00 52.12  ? 71   ASN F CG  1 
ATOM   10819 O OD1 . ASN F  2 71  ? 37.968  52.754 76.841  1.00 49.79  ? 71   ASN F OD1 1 
ATOM   10820 N ND2 . ASN F  2 71  ? 36.742  54.578 77.292  1.00 53.23  ? 71   ASN F ND2 1 
ATOM   10821 N N   . ASN F  2 72  ? 40.727  52.603 75.862  1.00 51.07  ? 72   ASN F N   1 
ATOM   10822 C CA  . ASN F  2 72  ? 41.404  51.309 75.764  1.00 49.73  ? 72   ASN F CA  1 
ATOM   10823 C C   . ASN F  2 72  ? 40.479  50.089 75.883  1.00 46.71  ? 72   ASN F C   1 
ATOM   10824 O O   . ASN F  2 72  ? 40.843  48.990 75.463  1.00 45.27  ? 72   ASN F O   1 
ATOM   10825 C CB  . ASN F  2 72  ? 42.514  51.233 76.824  1.00 53.06  ? 72   ASN F CB  1 
ATOM   10826 C CG  . ASN F  2 72  ? 43.566  50.189 76.500  1.00 53.05  ? 72   ASN F CG  1 
ATOM   10827 O OD1 . ASN F  2 72  ? 44.001  50.065 75.354  1.00 52.14  ? 72   ASN F OD1 1 
ATOM   10828 N ND2 . ASN F  2 72  ? 43.985  49.435 77.511  1.00 54.38  ? 72   ASN F ND2 1 
ATOM   10829 N N   . LEU F  2 73  ? 39.296  50.282 76.463  1.00 46.21  ? 73   LEU F N   1 
ATOM   10830 C CA  . LEU F  2 73  ? 38.287  49.229 76.542  1.00 43.83  ? 73   LEU F CA  1 
ATOM   10831 C C   . LEU F  2 73  ? 37.079  49.566 75.659  1.00 42.01  ? 73   LEU F C   1 
ATOM   10832 O O   . LEU F  2 73  ? 35.935  49.252 75.993  1.00 41.38  ? 73   LEU F O   1 
ATOM   10833 C CB  . LEU F  2 73  ? 37.871  49.008 77.994  1.00 45.19  ? 73   LEU F CB  1 
ATOM   10834 C CG  . LEU F  2 73  ? 38.959  48.392 78.887  1.00 46.78  ? 73   LEU F CG  1 
ATOM   10835 C CD1 . LEU F  2 73  ? 38.632  48.596 80.359  1.00 48.79  ? 73   LEU F CD1 1 
ATOM   10836 C CD2 . LEU F  2 73  ? 39.151  46.912 78.574  1.00 45.00  ? 73   LEU F CD2 1 
ATOM   10837 N N   . GLU F  2 74  ? 37.362  50.207 74.526  1.00 41.46  ? 74   GLU F N   1 
ATOM   10838 C CA  . GLU F  2 74  ? 36.384  50.453 73.474  1.00 39.73  ? 74   GLU F CA  1 
ATOM   10839 C C   . GLU F  2 74  ? 36.994  50.076 72.125  1.00 37.93  ? 74   GLU F C   1 
ATOM   10840 O O   . GLU F  2 74  ? 36.786  50.754 71.126  1.00 37.34  ? 74   GLU F O   1 
ATOM   10841 C CB  . GLU F  2 74  ? 35.980  51.923 73.471  1.00 41.56  ? 74   GLU F CB  1 
ATOM   10842 C CG  . GLU F  2 74  ? 35.162  52.326 74.675  1.00 43.54  ? 74   GLU F CG  1 
ATOM   10843 C CD  . GLU F  2 74  ? 34.616  53.723 74.545  1.00 45.69  ? 74   GLU F CD  1 
ATOM   10844 O OE1 . GLU F  2 74  ? 35.419  54.653 74.334  1.00 47.42  ? 74   GLU F OE1 1 
ATOM   10845 O OE2 . GLU F  2 74  ? 33.385  53.885 74.645  1.00 46.04  ? 74   GLU F OE2 1 
ATOM   10846 N N   . ARG F  2 75  ? 37.746  48.979 72.113  1.00 37.33  ? 75   ARG F N   1 
ATOM   10847 C CA  . ARG F  2 75  ? 38.512  48.566 70.940  1.00 36.28  ? 75   ARG F CA  1 
ATOM   10848 C C   . ARG F  2 75  ? 37.632  48.023 69.826  1.00 33.84  ? 75   ARG F C   1 
ATOM   10849 O O   . ARG F  2 75  ? 37.946  48.192 68.646  1.00 32.94  ? 75   ARG F O   1 
ATOM   10850 C CB  . ARG F  2 75  ? 39.550  47.511 71.329  1.00 37.07  ? 75   ARG F CB  1 
ATOM   10851 C CG  . ARG F  2 75  ? 40.713  48.061 72.135  1.00 39.96  ? 75   ARG F CG  1 
ATOM   10852 C CD  . ARG F  2 75  ? 41.829  48.556 71.233  1.00 41.03  ? 75   ARG F CD  1 
ATOM   10853 N NE  . ARG F  2 75  ? 42.775  49.404 71.964  1.00 44.41  ? 75   ARG F NE  1 
ATOM   10854 C CZ  . ARG F  2 75  ? 42.695  50.733 72.075  1.00 45.97  ? 75   ARG F CZ  1 
ATOM   10855 N NH1 . ARG F  2 75  ? 41.701  51.412 71.499  1.00 44.43  ? 75   ARG F NH1 1 
ATOM   10856 N NH2 . ARG F  2 75  ? 43.622  51.392 72.772  1.00 49.55  ? 75   ARG F NH2 1 
ATOM   10857 N N   . ARG F  2 76  ? 36.542  47.361 70.199  1.00 33.08  ? 76   ARG F N   1 
ATOM   10858 C CA  . ARG F  2 76  ? 35.607  46.818 69.216  1.00 31.36  ? 76   ARG F CA  1 
ATOM   10859 C C   . ARG F  2 76  ? 34.975  47.918 68.371  1.00 30.94  ? 76   ARG F C   1 
ATOM   10860 O O   . ARG F  2 76  ? 34.992  47.837 67.145  1.00 29.68  ? 76   ARG F O   1 
ATOM   10861 C CB  . ARG F  2 76  ? 34.506  46.018 69.899  1.00 31.42  ? 76   ARG F CB  1 
ATOM   10862 C CG  . ARG F  2 76  ? 34.950  44.679 70.457  1.00 31.68  ? 76   ARG F CG  1 
ATOM   10863 C CD  . ARG F  2 76  ? 33.831  44.088 71.292  1.00 32.23  ? 76   ARG F CD  1 
ATOM   10864 N NE  . ARG F  2 76  ? 33.530  44.948 72.438  1.00 33.50  ? 76   ARG F NE  1 
ATOM   10865 C CZ  . ARG F  2 76  ? 32.397  44.934 73.138  1.00 34.35  ? 76   ARG F CZ  1 
ATOM   10866 N NH1 . ARG F  2 76  ? 31.409  44.100 72.833  1.00 34.19  ? 76   ARG F NH1 1 
ATOM   10867 N NH2 . ARG F  2 76  ? 32.251  45.772 74.158  1.00 35.81  ? 76   ARG F NH2 1 
ATOM   10868 N N   . ILE F  2 77  ? 34.418  48.937 69.025  1.00 32.27  ? 77   ILE F N   1 
ATOM   10869 C CA  . ILE F  2 77  ? 33.794  50.051 68.303  1.00 32.50  ? 77   ILE F CA  1 
ATOM   10870 C C   . ILE F  2 77  ? 34.816  50.935 67.586  1.00 32.75  ? 77   ILE F C   1 
ATOM   10871 O O   . ILE F  2 77  ? 34.507  51.521 66.548  1.00 32.21  ? 77   ILE F O   1 
ATOM   10872 C CB  . ILE F  2 77  ? 32.867  50.910 69.193  1.00 34.53  ? 77   ILE F CB  1 
ATOM   10873 C CG1 . ILE F  2 77  ? 33.631  51.570 70.341  1.00 36.66  ? 77   ILE F CG1 1 
ATOM   10874 C CG2 . ILE F  2 77  ? 31.726  50.059 69.726  1.00 34.53  ? 77   ILE F CG2 1 
ATOM   10875 C CD1 . ILE F  2 77  ? 32.836  52.651 71.045  1.00 39.21  ? 77   ILE F CD1 1 
ATOM   10876 N N   . GLU F  2 78  ? 36.025  51.030 68.132  1.00 33.86  ? 78   GLU F N   1 
ATOM   10877 C CA  . GLU F  2 78  ? 37.116  51.707 67.443  1.00 34.49  ? 78   GLU F CA  1 
ATOM   10878 C C   . GLU F  2 78  ? 37.413  50.997 66.132  1.00 32.40  ? 78   GLU F C   1 
ATOM   10879 O O   . GLU F  2 78  ? 37.635  51.633 65.110  1.00 32.13  ? 78   GLU F O   1 
ATOM   10880 C CB  . GLU F  2 78  ? 38.374  51.736 68.310  1.00 36.56  ? 78   GLU F CB  1 
ATOM   10881 C CG  . GLU F  2 78  ? 39.575  52.404 67.653  1.00 37.89  ? 78   GLU F CG  1 
ATOM   10882 C CD  . GLU F  2 78  ? 40.696  52.690 68.638  1.00 40.96  ? 78   GLU F CD  1 
ATOM   10883 O OE1 . GLU F  2 78  ? 41.150  51.742 69.319  1.00 41.18  ? 78   GLU F OE1 1 
ATOM   10884 O OE2 . GLU F  2 78  ? 41.127  53.863 68.729  1.00 43.53  ? 78   GLU F OE2 1 
ATOM   10885 N N   . ASN F  2 79  ? 37.415  49.673 66.177  1.00 31.22  ? 79   ASN F N   1 
ATOM   10886 C CA  . ASN F  2 79  ? 37.704  48.865 65.007  1.00 29.71  ? 79   ASN F CA  1 
ATOM   10887 C C   . ASN F  2 79  ? 36.553  48.882 64.002  1.00 28.05  ? 79   ASN F C   1 
ATOM   10888 O O   . ASN F  2 79  ? 36.777  48.914 62.792  1.00 27.10  ? 79   ASN F O   1 
ATOM   10889 C CB  . ASN F  2 79  ? 38.008  47.435 65.437  1.00 29.65  ? 79   ASN F CB  1 
ATOM   10890 C CG  . ASN F  2 79  ? 38.376  46.550 64.274  1.00 28.74  ? 79   ASN F CG  1 
ATOM   10891 O OD1 . ASN F  2 79  ? 39.493  46.611 63.762  1.00 29.47  ? 79   ASN F OD1 1 
ATOM   10892 N ND2 . ASN F  2 79  ? 37.434  45.735 63.838  1.00 27.58  ? 79   ASN F ND2 1 
ATOM   10893 N N   . LEU F  2 80  ? 35.325  48.849 64.513  1.00 28.01  ? 80   LEU F N   1 
ATOM   10894 C CA  . LEU F  2 80  ? 34.123  49.000 63.691  1.00 27.17  ? 80   LEU F CA  1 
ATOM   10895 C C   . LEU F  2 80  ? 34.192  50.331 62.966  1.00 27.42  ? 80   LEU F C   1 
ATOM   10896 O O   . LEU F  2 80  ? 33.980  50.402 61.759  1.00 26.38  ? 80   LEU F O   1 
ATOM   10897 C CB  . LEU F  2 80  ? 32.869  48.948 64.572  1.00 28.07  ? 80   LEU F CB  1 
ATOM   10898 C CG  . LEU F  2 80  ? 31.462  48.849 63.965  1.00 27.99  ? 80   LEU F CG  1 
ATOM   10899 C CD1 . LEU F  2 80  ? 30.452  48.591 65.074  1.00 29.43  ? 80   LEU F CD1 1 
ATOM   10900 C CD2 . LEU F  2 80  ? 31.063  50.095 63.193  1.00 28.39  ? 80   LEU F CD2 1 
ATOM   10901 N N   . ASN F  2 81  ? 34.503  51.380 63.715  1.00 29.10  ? 81   ASN F N   1 
ATOM   10902 C CA  . ASN F  2 81  ? 34.648  52.712 63.155  1.00 30.02  ? 81   ASN F CA  1 
ATOM   10903 C C   . ASN F  2 81  ? 35.688  52.777 62.038  1.00 29.21  ? 81   ASN F C   1 
ATOM   10904 O O   . ASN F  2 81  ? 35.437  53.385 61.004  1.00 28.81  ? 81   ASN F O   1 
ATOM   10905 C CB  . ASN F  2 81  ? 35.024  53.700 64.252  1.00 32.55  ? 81   ASN F CB  1 
ATOM   10906 C CG  . ASN F  2 81  ? 35.153  55.111 63.736  1.00 34.13  ? 81   ASN F CG  1 
ATOM   10907 O OD1 . ASN F  2 81  ? 34.230  55.632 63.125  1.00 34.16  ? 81   ASN F OD1 1 
ATOM   10908 N ND2 . ASN F  2 81  ? 36.299  55.734 63.972  1.00 35.84  ? 81   ASN F ND2 1 
ATOM   10909 N N   . LYS F  2 82  ? 36.846  52.154 62.248  1.00 29.29  ? 82   LYS F N   1 
ATOM   10910 C CA  . LYS F  2 82  ? 37.919  52.177 61.254  1.00 29.09  ? 82   LYS F CA  1 
ATOM   10911 C C   . LYS F  2 82  ? 37.475  51.500 59.972  1.00 26.94  ? 82   LYS F C   1 
ATOM   10912 O O   . LYS F  2 82  ? 37.616  52.065 58.890  1.00 26.54  ? 82   LYS F O   1 
ATOM   10913 C CB  . LYS F  2 82  ? 39.195  51.502 61.771  1.00 30.12  ? 82   LYS F CB  1 
ATOM   10914 C CG  . LYS F  2 82  ? 40.294  51.400 60.709  1.00 30.28  ? 82   LYS F CG  1 
ATOM   10915 C CD  . LYS F  2 82  ? 41.673  51.105 61.296  1.00 32.52  ? 82   LYS F CD  1 
ATOM   10916 C CE  . LYS F  2 82  ? 41.994  49.612 61.324  1.00 32.01  ? 82   LYS F CE  1 
ATOM   10917 N NZ  . LYS F  2 82  ? 43.220  49.312 62.125  1.00 34.66  ? 82   LYS F NZ  1 
ATOM   10918 N N   . LYS F  2 83  ? 36.941  50.289 60.109  1.00 48.35  ? 83   LYS F N   1 
ATOM   10919 C CA  . LYS F  2 83  ? 36.447  49.523 58.965  1.00 46.14  ? 83   LYS F CA  1 
ATOM   10920 C C   . LYS F  2 83  ? 35.341  50.242 58.208  1.00 42.93  ? 83   LYS F C   1 
ATOM   10921 O O   . LYS F  2 83  ? 35.283  50.173 56.981  1.00 40.76  ? 83   LYS F O   1 
ATOM   10922 C CB  . LYS F  2 83  ? 35.977  48.132 59.411  1.00 47.80  ? 83   LYS F CB  1 
ATOM   10923 C CG  . LYS F  2 83  ? 37.054  47.051 59.356  1.00 50.50  ? 83   LYS F CG  1 
ATOM   10924 C CD  . LYS F  2 83  ? 38.462  47.569 59.642  1.00 52.59  ? 83   LYS F CD  1 
ATOM   10925 C CE  . LYS F  2 83  ? 39.521  46.490 59.473  1.00 55.74  ? 83   LYS F CE  1 
ATOM   10926 N NZ  . LYS F  2 83  ? 39.804  45.786 60.755  1.00 59.84  ? 83   LYS F NZ  1 
ATOM   10927 N N   . MET F  2 84  ? 34.475  50.938 58.933  1.00 43.02  ? 84   MET F N   1 
ATOM   10928 C CA  . MET F  2 84  ? 33.423  51.712 58.298  1.00 40.79  ? 84   MET F CA  1 
ATOM   10929 C C   . MET F  2 84  ? 34.028  52.814 57.436  1.00 39.27  ? 84   MET F C   1 
ATOM   10930 O O   . MET F  2 84  ? 33.685  52.934 56.261  1.00 36.97  ? 84   MET F O   1 
ATOM   10931 C CB  . MET F  2 84  ? 32.489  52.321 59.340  1.00 42.10  ? 84   MET F CB  1 
ATOM   10932 C CG  . MET F  2 84  ? 31.160  52.784 58.766  1.00 40.71  ? 84   MET F CG  1 
ATOM   10933 S SD  . MET F  2 84  ? 30.643  54.370 59.435  1.00 42.04  ? 84   MET F SD  1 
ATOM   10934 C CE  . MET F  2 84  ? 31.783  55.446 58.579  1.00 40.89  ? 84   MET F CE  1 
ATOM   10935 N N   . GLU F  2 85  ? 34.936  53.599 58.016  1.00 40.91  ? 85   GLU F N   1 
ATOM   10936 C CA  . GLU F  2 85  ? 35.549  54.721 57.301  1.00 40.23  ? 85   GLU F CA  1 
ATOM   10937 C C   . GLU F  2 85  ? 36.383  54.223 56.122  1.00 38.86  ? 85   GLU F C   1 
ATOM   10938 O O   . GLU F  2 85  ? 36.247  54.725 55.012  1.00 36.77  ? 85   GLU F O   1 
ATOM   10939 C CB  . GLU F  2 85  ? 36.396  55.598 58.234  1.00 43.20  ? 85   GLU F CB  1 
ATOM   10940 C CG  . GLU F  2 85  ? 35.631  56.147 59.438  1.00 45.03  ? 85   GLU F CG  1 
ATOM   10941 C CD  . GLU F  2 85  ? 35.782  57.649 59.639  1.00 46.67  ? 85   GLU F CD  1 
ATOM   10942 O OE1 . GLU F  2 85  ? 36.773  58.081 60.272  1.00 49.57  ? 85   GLU F OE1 1 
ATOM   10943 O OE2 . GLU F  2 85  ? 34.888  58.401 59.191  1.00 45.64  ? 85   GLU F OE2 1 
ATOM   10944 N N   . ASP F  2 86  ? 37.228  53.225 56.365  1.00 40.36  ? 86   ASP F N   1 
ATOM   10945 C CA  . ASP F  2 86  ? 38.034  52.612 55.303  1.00 39.73  ? 86   ASP F CA  1 
ATOM   10946 C C   . ASP F  2 86  ? 37.197  51.974 54.209  1.00 36.92  ? 86   ASP F C   1 
ATOM   10947 O O   . ASP F  2 86  ? 37.544  52.060 53.031  1.00 35.41  ? 86   ASP F O   1 
ATOM   10948 C CB  . ASP F  2 86  ? 38.976  51.546 55.877  1.00 42.72  ? 86   ASP F CB  1 
ATOM   10949 C CG  . ASP F  2 86  ? 40.343  52.094 56.196  1.00 45.62  ? 86   ASP F CG  1 
ATOM   10950 O OD1 . ASP F  2 86  ? 40.891  52.825 55.338  1.00 44.95  ? 86   ASP F OD1 1 
ATOM   10951 O OD2 . ASP F  2 86  ? 40.873  51.786 57.288  1.00 48.91  ? 86   ASP F OD2 1 
ATOM   10952 N N   . GLY F  2 87  ? 36.116  51.313 54.607  1.00 36.61  ? 87   GLY F N   1 
ATOM   10953 C CA  . GLY F  2 87  ? 35.236  50.628 53.670  1.00 34.71  ? 87   GLY F CA  1 
ATOM   10954 C C   . GLY F  2 87  ? 34.621  51.559 52.644  1.00 32.05  ? 87   GLY F C   1 
ATOM   10955 O O   . GLY F  2 87  ? 34.550  51.224 51.460  1.00 30.48  ? 87   GLY F O   1 
ATOM   10956 N N   . PHE F  2 88  ? 34.184  52.731 53.103  1.00 31.92  ? 88   PHE F N   1 
ATOM   10957 C CA  . PHE F  2 88  ? 33.619  53.747 52.219  1.00 30.06  ? 88   PHE F CA  1 
ATOM   10958 C C   . PHE F  2 88  ? 34.670  54.365 51.291  1.00 29.25  ? 88   PHE F C   1 
ATOM   10959 O O   . PHE F  2 88  ? 34.366  54.688 50.140  1.00 27.40  ? 88   PHE F O   1 
ATOM   10960 C CB  . PHE F  2 88  ? 32.915  54.846 53.023  1.00 31.00  ? 88   PHE F CB  1 
ATOM   10961 C CG  . PHE F  2 88  ? 31.546  54.460 53.522  1.00 31.48  ? 88   PHE F CG  1 
ATOM   10962 C CD1 . PHE F  2 88  ? 30.541  54.103 52.634  1.00 30.22  ? 88   PHE F CD1 1 
ATOM   10963 C CD2 . PHE F  2 88  ? 31.255  54.467 54.877  1.00 33.60  ? 88   PHE F CD2 1 
ATOM   10964 C CE1 . PHE F  2 88  ? 29.281  53.750 53.086  1.00 31.30  ? 88   PHE F CE1 1 
ATOM   10965 C CE2 . PHE F  2 88  ? 29.995  54.120 55.335  1.00 34.47  ? 88   PHE F CE2 1 
ATOM   10966 C CZ  . PHE F  2 88  ? 29.006  53.760 54.437  1.00 33.45  ? 88   PHE F CZ  1 
ATOM   10967 N N   . LEU F  2 89  ? 35.899  54.527 51.778  1.00 31.01  ? 89   LEU F N   1 
ATOM   10968 C CA  . LEU F  2 89  ? 36.990  55.015 50.927  1.00 30.92  ? 89   LEU F CA  1 
ATOM   10969 C C   . LEU F  2 89  ? 37.296  54.062 49.776  1.00 29.59  ? 89   LEU F C   1 
ATOM   10970 O O   . LEU F  2 89  ? 37.597  54.505 48.679  1.00 28.32  ? 89   LEU F O   1 
ATOM   10971 C CB  . LEU F  2 89  ? 38.264  55.240 51.731  1.00 33.90  ? 89   LEU F CB  1 
ATOM   10972 C CG  . LEU F  2 89  ? 38.192  56.349 52.781  1.00 35.87  ? 89   LEU F CG  1 
ATOM   10973 C CD1 . LEU F  2 89  ? 39.493  56.395 53.576  1.00 39.35  ? 89   LEU F CD1 1 
ATOM   10974 C CD2 . LEU F  2 89  ? 37.868  57.697 52.141  1.00 35.06  ? 89   LEU F CD2 1 
ATOM   10975 N N   . ASP F  2 90  ? 37.226  52.759 50.035  1.00 30.27  ? 90   ASP F N   1 
ATOM   10976 C CA  . ASP F  2 90  ? 37.443  51.760 48.990  1.00 29.62  ? 90   ASP F CA  1 
ATOM   10977 C C   . ASP F  2 90  ? 36.325  51.783 47.966  1.00 27.05  ? 90   ASP F C   1 
ATOM   10978 O O   . ASP F  2 90  ? 36.576  51.641 46.768  1.00 25.92  ? 90   ASP F O   1 
ATOM   10979 C CB  . ASP F  2 90  ? 37.554  50.360 49.582  1.00 31.66  ? 90   ASP F CB  1 
ATOM   10980 C CG  . ASP F  2 90  ? 38.778  50.195 50.444  1.00 34.78  ? 90   ASP F CG  1 
ATOM   10981 O OD1 . ASP F  2 90  ? 39.682  51.056 50.359  1.00 35.42  ? 90   ASP F OD1 1 
ATOM   10982 O OD2 . ASP F  2 90  ? 38.829  49.207 51.212  1.00 37.00  ? 90   ASP F OD2 1 
ATOM   10983 N N   . VAL F  2 91  ? 35.096  51.961 48.442  1.00 26.54  ? 91   VAL F N   1 
ATOM   10984 C CA  . VAL F  2 91  ? 33.940  52.062 47.559  1.00 24.75  ? 91   VAL F CA  1 
ATOM   10985 C C   . VAL F  2 91  ? 34.045  53.292 46.663  1.00 23.17  ? 91   VAL F C   1 
ATOM   10986 O O   . VAL F  2 91  ? 33.859  53.192 45.449  1.00 21.77  ? 91   VAL F O   1 
ATOM   10987 C CB  . VAL F  2 91  ? 32.616  52.096 48.351  1.00 25.30  ? 91   VAL F CB  1 
ATOM   10988 C CG1 . VAL F  2 91  ? 31.452  52.516 47.461  1.00 24.02  ? 91   VAL F CG1 1 
ATOM   10989 C CG2 . VAL F  2 91  ? 32.338  50.731 48.967  1.00 26.93  ? 91   VAL F CG2 1 
ATOM   10990 N N   . TRP F  2 92  ? 34.349  54.444 47.251  1.00 23.77  ? 92   TRP F N   1 
ATOM   10991 C CA  . TRP F  2 92  ? 34.444  55.678 46.470  1.00 22.89  ? 92   TRP F CA  1 
ATOM   10992 C C   . TRP F  2 92  ? 35.702  55.741 45.608  1.00 22.58  ? 92   TRP F C   1 
ATOM   10993 O O   . TRP F  2 92  ? 35.672  56.317 44.521  1.00 21.37  ? 92   TRP F O   1 
ATOM   10994 C CB  . TRP F  2 92  ? 34.312  56.909 47.369  1.00 24.36  ? 92   TRP F CB  1 
ATOM   10995 C CG  . TRP F  2 92  ? 32.893  57.124 47.790  1.00 24.61  ? 92   TRP F CG  1 
ATOM   10996 C CD1 . TRP F  2 92  ? 32.370  56.969 49.041  1.00 26.20  ? 92   TRP F CD1 1 
ATOM   10997 C CD2 . TRP F  2 92  ? 31.801  57.490 46.942  1.00 23.72  ? 92   TRP F CD2 1 
ATOM   10998 N NE1 . TRP F  2 92  ? 31.021  57.235 49.029  1.00 26.43  ? 92   TRP F NE1 1 
ATOM   10999 C CE2 . TRP F  2 92  ? 30.647  57.558 47.750  1.00 25.05  ? 92   TRP F CE2 1 
ATOM   11000 C CE3 . TRP F  2 92  ? 31.689  57.783 45.578  1.00 22.26  ? 92   TRP F CE3 1 
ATOM   11001 C CZ2 . TRP F  2 92  ? 29.395  57.908 47.240  1.00 25.23  ? 92   TRP F CZ2 1 
ATOM   11002 C CZ3 . TRP F  2 92  ? 30.445  58.127 45.071  1.00 22.27  ? 92   TRP F CZ3 1 
ATOM   11003 C CH2 . TRP F  2 92  ? 29.314  58.189 45.903  1.00 23.89  ? 92   TRP F CH2 1 
ATOM   11004 N N   . THR F  2 93  ? 36.797  55.147 46.076  1.00 24.05  ? 93   THR F N   1 
ATOM   11005 C CA  . THR F  2 93  ? 38.001  55.028 45.257  1.00 24.36  ? 93   THR F CA  1 
ATOM   11006 C C   . THR F  2 93  ? 37.705  54.164 44.031  1.00 22.69  ? 93   THR F C   1 
ATOM   11007 O O   . THR F  2 93  ? 38.075  54.518 42.912  1.00 21.83  ? 93   THR F O   1 
ATOM   11008 C CB  . THR F  2 93  ? 39.178  54.415 46.040  1.00 27.03  ? 93   THR F CB  1 
ATOM   11009 O OG1 . THR F  2 93  ? 39.504  55.258 47.147  1.00 28.95  ? 93   THR F OG1 1 
ATOM   11010 C CG2 . THR F  2 93  ? 40.406  54.276 45.156  1.00 27.94  ? 93   THR F CG2 1 
ATOM   11011 N N   . TYR F  2 94  ? 37.036  53.037 44.254  1.00 22.62  ? 94   TYR F N   1 
ATOM   11012 C CA  . TYR F  2 94  ? 36.670  52.121 43.177  1.00 21.66  ? 94   TYR F CA  1 
ATOM   11013 C C   . TYR F  2 94  ? 35.771  52.796 42.140  1.00 19.46  ? 94   TYR F C   1 
ATOM   11014 O O   . TYR F  2 94  ? 35.987  52.654 40.940  1.00 18.55  ? 94   TYR F O   1 
ATOM   11015 C CB  . TYR F  2 94  ? 35.985  50.883 43.763  1.00 22.69  ? 94   TYR F CB  1 
ATOM   11016 C CG  . TYR F  2 94  ? 35.274  50.002 42.760  1.00 22.15  ? 94   TYR F CG  1 
ATOM   11017 C CD1 . TYR F  2 94  ? 33.939  50.226 42.431  1.00 20.97  ? 94   TYR F CD1 1 
ATOM   11018 C CD2 . TYR F  2 94  ? 35.927  48.932 42.155  1.00 23.42  ? 94   TYR F CD2 1 
ATOM   11019 C CE1 . TYR F  2 94  ? 33.285  49.419 41.517  1.00 21.00  ? 94   TYR F CE1 1 
ATOM   11020 C CE2 . TYR F  2 94  ? 35.279  48.123 41.238  1.00 23.41  ? 94   TYR F CE2 1 
ATOM   11021 C CZ  . TYR F  2 94  ? 33.960  48.370 40.924  1.00 22.15  ? 94   TYR F CZ  1 
ATOM   11022 O OH  . TYR F  2 94  ? 33.311  47.570 40.017  1.00 22.61  ? 94   TYR F OH  1 
ATOM   11023 N N   . ASN F  2 95  ? 34.771  53.528 42.618  1.00 18.98  ? 95   ASN F N   1 
ATOM   11024 C CA  . ASN F  2 95  ? 33.838  54.243 41.747  1.00 17.58  ? 95   ASN F CA  1 
ATOM   11025 C C   . ASN F  2 95  ? 34.532  55.233 40.827  1.00 16.79  ? 95   ASN F C   1 
ATOM   11026 O O   . ASN F  2 95  ? 34.254  55.279 39.624  1.00 15.65  ? 95   ASN F O   1 
ATOM   11027 C CB  . ASN F  2 95  ? 32.799  54.994 42.584  1.00 18.09  ? 95   ASN F CB  1 
ATOM   11028 C CG  . ASN F  2 95  ? 31.797  54.066 43.237  1.00 18.94  ? 95   ASN F CG  1 
ATOM   11029 O OD1 . ASN F  2 95  ? 31.763  52.873 42.945  1.00 19.19  ? 95   ASN F OD1 1 
ATOM   11030 N ND2 . ASN F  2 95  ? 30.975  54.610 44.125  1.00 19.91  ? 95   ASN F ND2 1 
ATOM   11031 N N   . ALA F  2 96  ? 35.423  56.027 41.412  1.00 17.76  ? 96   ALA F N   1 
ATOM   11032 C CA  . ALA F  2 96  ? 36.190  57.032 40.681  1.00 17.69  ? 96   ALA F CA  1 
ATOM   11033 C C   . ALA F  2 96  ? 37.079  56.402 39.621  1.00 17.25  ? 96   ALA F C   1 
ATOM   11034 O O   . ALA F  2 96  ? 37.056  56.814 38.467  1.00 16.25  ? 96   ALA F O   1 
ATOM   11035 C CB  . ALA F  2 96  ? 37.037  57.841 41.650  1.00 19.69  ? 96   ALA F CB  1 
ATOM   11036 N N   . GLU F  2 97  ? 37.858  55.399 40.012  1.00 18.37  ? 97   GLU F N   1 
ATOM   11037 C CA  . GLU F  2 97  ? 38.810  54.778 39.087  1.00 18.76  ? 97   GLU F CA  1 
ATOM   11038 C C   . GLU F  2 97  ? 38.111  54.021 37.962  1.00 17.20  ? 97   GLU F C   1 
ATOM   11039 O O   . GLU F  2 97  ? 38.570  54.041 36.820  1.00 16.85  ? 97   GLU F O   1 
ATOM   11040 C CB  . GLU F  2 97  ? 39.768  53.853 39.835  1.00 21.14  ? 97   GLU F CB  1 
ATOM   11041 C CG  . GLU F  2 97  ? 40.690  54.595 40.792  1.00 23.33  ? 97   GLU F CG  1 
ATOM   11042 C CD  . GLU F  2 97  ? 41.721  53.703 41.455  1.00 26.29  ? 97   GLU F CD  1 
ATOM   11043 O OE1 . GLU F  2 97  ? 41.746  52.485 41.176  1.00 26.78  ? 97   GLU F OE1 1 
ATOM   11044 O OE2 . GLU F  2 97  ? 42.520  54.226 42.259  1.00 28.64  ? 97   GLU F OE2 1 
ATOM   11045 N N   . LEU F  2 98  ? 37.000  53.364 38.285  1.00 16.65  ? 98   LEU F N   1 
ATOM   11046 C CA  . LEU F  2 98  ? 36.234  52.622 37.297  1.00 15.76  ? 98   LEU F CA  1 
ATOM   11047 C C   . LEU F  2 98  ? 35.554  53.566 36.319  1.00 14.07  ? 98   LEU F C   1 
ATOM   11048 O O   . LEU F  2 98  ? 35.592  53.344 35.119  1.00 13.46  ? 98   LEU F O   1 
ATOM   11049 C CB  . LEU F  2 98  ? 35.183  51.749 37.970  1.00 16.30  ? 98   LEU F CB  1 
ATOM   11050 C CG  . LEU F  2 98  ? 34.457  50.781 37.036  1.00 16.39  ? 98   LEU F CG  1 
ATOM   11051 C CD1 . LEU F  2 98  ? 35.402  49.696 36.542  1.00 17.85  ? 98   LEU F CD1 1 
ATOM   11052 C CD2 . LEU F  2 98  ? 33.261  50.161 37.739  1.00 17.29  ? 98   LEU F CD2 1 
ATOM   11053 N N   . LEU F  2 99  ? 34.934  54.619 36.837  1.00 13.65  ? 99   LEU F N   1 
ATOM   11054 C CA  . LEU F  2 99  ? 34.246  55.579 35.990  1.00 12.68  ? 99   LEU F CA  1 
ATOM   11055 C C   . LEU F  2 99  ? 35.202  56.212 34.985  1.00 12.24  ? 99   LEU F C   1 
ATOM   11056 O O   . LEU F  2 99  ? 34.874  56.346 33.810  1.00 11.43  ? 99   LEU F O   1 
ATOM   11057 C CB  . LEU F  2 99  ? 33.588  56.672 36.833  1.00 13.19  ? 99   LEU F CB  1 
ATOM   11058 C CG  . LEU F  2 99  ? 32.707  57.675 36.077  1.00 12.98  ? 99   LEU F CG  1 
ATOM   11059 C CD1 . LEU F  2 99  ? 31.574  56.968 35.346  1.00 12.72  ? 99   LEU F CD1 1 
ATOM   11060 C CD2 . LEU F  2 99  ? 32.150  58.719 37.027  1.00 14.21  ? 99   LEU F CD2 1 
ATOM   11061 N N   . VAL F  2 100 ? 36.381  56.603 35.453  1.00 13.10  ? 100  VAL F N   1 
ATOM   11062 C CA  . VAL F  2 100 ? 37.397  57.164 34.570  1.00 13.26  ? 100  VAL F CA  1 
ATOM   11063 C C   . VAL F  2 100 ? 37.770  56.152 33.473  1.00 12.84  ? 100  VAL F C   1 
ATOM   11064 O O   . VAL F  2 100 ? 37.751  56.488 32.296  1.00 12.12  ? 100  VAL F O   1 
ATOM   11065 C CB  . VAL F  2 100 ? 38.642  57.633 35.367  1.00 15.14  ? 100  VAL F CB  1 
ATOM   11066 C CG1 . VAL F  2 100 ? 39.832  57.894 34.448  1.00 16.01  ? 100  VAL F CG1 1 
ATOM   11067 C CG2 . VAL F  2 100 ? 38.307  58.886 36.162  1.00 15.85  ? 100  VAL F CG2 1 
ATOM   11068 N N   . LEU F  2 101 ? 38.097  54.925 33.870  1.00 13.62  ? 101  LEU F N   1 
ATOM   11069 C CA  . LEU F  2 101 ? 38.415  53.844 32.928  1.00 13.91  ? 101  LEU F CA  1 
ATOM   11070 C C   . LEU F  2 101 ? 37.333  53.606 31.867  1.00 12.52  ? 101  LEU F C   1 
ATOM   11071 O O   . LEU F  2 101 ? 37.630  53.498 30.672  1.00 12.36  ? 101  LEU F O   1 
ATOM   11072 C CB  . LEU F  2 101 ? 38.644  52.537 33.694  1.00 15.53  ? 101  LEU F CB  1 
ATOM   11073 C CG  . LEU F  2 101 ? 40.061  51.971 33.806  1.00 17.97  ? 101  LEU F CG  1 
ATOM   11074 C CD1 . LEU F  2 101 ? 41.125  53.038 34.010  1.00 18.84  ? 101  LEU F CD1 1 
ATOM   11075 C CD2 . LEU F  2 101 ? 40.092  50.959 34.939  1.00 19.76  ? 101  LEU F CD2 1 
ATOM   11076 N N   . MET F  2 102 ? 36.086  53.504 32.316  1.00 11.92  ? 102  MET F N   1 
ATOM   11077 C CA  . MET F  2 102 ? 34.967  53.206 31.432  1.00 11.31  ? 102  MET F CA  1 
ATOM   11078 C C   . MET F  2 102 ? 34.661  54.372 30.504  1.00 10.20  ? 102  MET F C   1 
ATOM   11079 O O   . MET F  2 102 ? 34.426  54.180 29.306  1.00 9.95   ? 102  MET F O   1 
ATOM   11080 C CB  . MET F  2 102 ? 33.722  52.857 32.246  1.00 11.67  ? 102  MET F CB  1 
ATOM   11081 C CG  . MET F  2 102 ? 33.816  51.527 32.975  1.00 13.15  ? 102  MET F CG  1 
ATOM   11082 S SD  . MET F  2 102 ? 32.242  50.949 33.646  1.00 14.15  ? 102  MET F SD  1 
ATOM   11083 C CE  . MET F  2 102 ? 31.771  52.348 34.668  1.00 13.36  ? 102  MET F CE  1 
ATOM   11084 N N   . GLU F  2 103 ? 34.673  55.581 31.055  1.00 9.93   ? 103  GLU F N   1 
ATOM   11085 C CA  . GLU F  2 103 ? 34.341  56.764 30.279  1.00 9.46   ? 103  GLU F CA  1 
ATOM   11086 C C   . GLU F  2 103 ? 35.490  57.242 29.385  1.00 9.42   ? 103  GLU F C   1 
ATOM   11087 O O   . GLU F  2 103 ? 35.240  57.835 28.339  1.00 9.10   ? 103  GLU F O   1 
ATOM   11088 C CB  . GLU F  2 103 ? 33.840  57.880 31.191  1.00 9.90   ? 103  GLU F CB  1 
ATOM   11089 C CG  . GLU F  2 103 ? 32.460  57.609 31.788  1.00 10.31  ? 103  GLU F CG  1 
ATOM   11090 C CD  . GLU F  2 103 ? 31.339  57.517 30.756  1.00 10.38  ? 103  GLU F CD  1 
ATOM   11091 O OE1 . GLU F  2 103 ? 31.532  57.935 29.604  1.00 10.00  ? 103  GLU F OE1 1 
ATOM   11092 O OE2 . GLU F  2 103 ? 30.247  57.015 31.099  1.00 11.18  ? 103  GLU F OE2 1 
ATOM   11093 N N   . ASN F  2 104 ? 36.734  56.987 29.782  1.00 10.16  ? 104  ASN F N   1 
ATOM   11094 C CA  . ASN F  2 104 ? 37.876  57.200 28.891  1.00 10.67  ? 104  ASN F CA  1 
ATOM   11095 C C   . ASN F  2 104 ? 37.761  56.362 27.629  1.00 10.34  ? 104  ASN F C   1 
ATOM   11096 O O   . ASN F  2 104 ? 38.034  56.840 26.533  1.00 10.17  ? 104  ASN F O   1 
ATOM   11097 C CB  . ASN F  2 104 ? 39.191  56.829 29.574  1.00 12.22  ? 104  ASN F CB  1 
ATOM   11098 C CG  . ASN F  2 104 ? 39.729  57.929 30.458  1.00 13.30  ? 104  ASN F CG  1 
ATOM   11099 O OD1 . ASN F  2 104 ? 39.257  59.061 30.420  1.00 13.00  ? 104  ASN F OD1 1 
ATOM   11100 N ND2 . ASN F  2 104 ? 40.732  57.596 31.259  1.00 15.06  ? 104  ASN F ND2 1 
ATOM   11101 N N   . GLU F  2 105 ? 37.366  55.105 27.794  1.00 10.60  ? 105  GLU F N   1 
ATOM   11102 C CA  . GLU F  2 105 ? 37.203  54.211 26.664  1.00 10.85  ? 105  GLU F CA  1 
ATOM   11103 C C   . GLU F  2 105 ? 36.085  54.684 25.755  1.00 9.86   ? 105  GLU F C   1 
ATOM   11104 O O   . GLU F  2 105 ? 36.189  54.594 24.534  1.00 9.89   ? 105  GLU F O   1 
ATOM   11105 C CB  . GLU F  2 105 ? 36.898  52.793 27.135  1.00 11.94  ? 105  GLU F CB  1 
ATOM   11106 C CG  . GLU F  2 105 ? 37.049  51.765 26.029  1.00 13.10  ? 105  GLU F CG  1 
ATOM   11107 C CD  . GLU F  2 105 ? 37.313  50.381 26.568  1.00 15.20  ? 105  GLU F CD  1 
ATOM   11108 O OE1 . GLU F  2 105 ? 36.533  49.929 27.426  1.00 15.52  ? 105  GLU F OE1 1 
ATOM   11109 O OE2 . GLU F  2 105 ? 38.307  49.745 26.139  1.00 17.05  ? 105  GLU F OE2 1 
ATOM   11110 N N   . ARG F  2 106 ? 35.010  55.174 26.358  1.00 9.38   ? 106  ARG F N   1 
ATOM   11111 C CA  . ARG F  2 106 ? 33.895  55.693 25.586  1.00 9.09   ? 106  ARG F CA  1 
ATOM   11112 C C   . ARG F  2 106 ? 34.266  56.992 24.880  1.00 8.57   ? 106  ARG F C   1 
ATOM   11113 O O   . ARG F  2 106 ? 33.803  57.242 23.769  1.00 8.58   ? 106  ARG F O   1 
ATOM   11114 C CB  . ARG F  2 106 ? 32.667  55.907 26.471  1.00 9.52   ? 106  ARG F CB  1 
ATOM   11115 C CG  . ARG F  2 106 ? 32.010  54.625 26.961  1.00 10.49  ? 106  ARG F CG  1 
ATOM   11116 C CD  . ARG F  2 106 ? 30.508  54.805 27.148  1.00 11.50  ? 106  ARG F CD  1 
ATOM   11117 N NE  . ARG F  2 106 ? 29.722  54.331 25.995  1.00 12.57  ? 106  ARG F NE  1 
ATOM   11118 C CZ  . ARG F  2 106 ? 28.553  54.847 25.589  1.00 13.76  ? 106  ARG F CZ  1 
ATOM   11119 N NH1 . ARG F  2 106 ? 28.003  55.896 26.201  1.00 14.06  ? 106  ARG F NH1 1 
ATOM   11120 N NH2 . ARG F  2 106 ? 27.922  54.315 24.541  1.00 15.14  ? 106  ARG F NH2 1 
ATOM   11121 N N   . THR F  2 107 ? 35.104  57.809 25.514  1.00 8.46   ? 107  THR F N   1 
ATOM   11122 C CA  . THR F  2 107 ? 35.540  59.072 24.916  1.00 8.56   ? 107  THR F CA  1 
ATOM   11123 C C   . THR F  2 107 ? 36.358  58.853 23.643  1.00 8.50   ? 107  THR F C   1 
ATOM   11124 O O   . THR F  2 107 ? 36.168  59.554 22.655  1.00 8.56   ? 107  THR F O   1 
ATOM   11125 C CB  . THR F  2 107 ? 36.348  59.940 25.906  1.00 9.31   ? 107  THR F CB  1 
ATOM   11126 O OG1 . THR F  2 107 ? 35.523  60.302 27.018  1.00 9.52   ? 107  THR F OG1 1 
ATOM   11127 C CG2 . THR F  2 107 ? 36.825  61.215 25.238  1.00 10.17  ? 107  THR F CG2 1 
ATOM   11128 N N   . LEU F  2 108 ? 37.256  57.879 23.658  1.00 8.67   ? 108  LEU F N   1 
ATOM   11129 C CA  . LEU F  2 108 ? 38.072  57.604 22.483  1.00 9.07   ? 108  LEU F CA  1 
ATOM   11130 C C   . LEU F  2 108 ? 37.234  57.029 21.339  1.00 8.59   ? 108  LEU F C   1 
ATOM   11131 O O   . LEU F  2 108 ? 37.450  57.356 20.175  1.00 8.73   ? 108  LEU F O   1 
ATOM   11132 C CB  . LEU F  2 108 ? 39.214  56.653 22.834  1.00 10.23  ? 108  LEU F CB  1 
ATOM   11133 C CG  . LEU F  2 108 ? 40.159  57.112 23.946  1.00 11.26  ? 108  LEU F CG  1 
ATOM   11134 C CD1 . LEU F  2 108 ? 41.263  56.086 24.117  1.00 13.03  ? 108  LEU F CD1 1 
ATOM   11135 C CD2 . LEU F  2 108 ? 40.740  58.491 23.677  1.00 11.92  ? 108  LEU F CD2 1 
ATOM   11136 N N   . ASP F  2 109 ? 36.284  56.167 21.678  1.00 8.34   ? 109  ASP F N   1 
ATOM   11137 C CA  . ASP F  2 109 ? 35.363  55.628 20.687  1.00 8.48   ? 109  ASP F CA  1 
ATOM   11138 C C   . ASP F  2 109 ? 34.390  56.690 20.158  1.00 8.11   ? 109  ASP F C   1 
ATOM   11139 O O   . ASP F  2 109 ? 33.954  56.612 19.022  1.00 8.50   ? 109  ASP F O   1 
ATOM   11140 C CB  . ASP F  2 109 ? 34.602  54.439 21.268  1.00 9.09   ? 109  ASP F CB  1 
ATOM   11141 C CG  . ASP F  2 109 ? 35.493  53.225 21.487  1.00 10.16  ? 109  ASP F CG  1 
ATOM   11142 O OD1 . ASP F  2 109 ? 36.459  53.034 20.708  1.00 10.78  ? 109  ASP F OD1 1 
ATOM   11143 O OD2 . ASP F  2 109 ? 35.216  52.452 22.442  1.00 10.78  ? 109  ASP F OD2 1 
ATOM   11144 N N   . PHE F  2 110 ? 34.067  57.679 20.983  1.00 7.74   ? 110  PHE F N   1 
ATOM   11145 C CA  . PHE F  2 110 ? 33.249  58.817 20.572  1.00 8.04   ? 110  PHE F CA  1 
ATOM   11146 C C   . PHE F  2 110 ? 33.948  59.600 19.458  1.00 8.16   ? 110  PHE F C   1 
ATOM   11147 O O   . PHE F  2 110 ? 33.350  59.908 18.428  1.00 8.72   ? 110  PHE F O   1 
ATOM   11148 C CB  . PHE F  2 110 ? 32.988  59.701 21.795  1.00 8.21   ? 110  PHE F CB  1 
ATOM   11149 C CG  . PHE F  2 110 ? 32.200  60.946 21.512  1.00 9.29   ? 110  PHE F CG  1 
ATOM   11150 C CD1 . PHE F  2 110 ? 30.924  60.883 20.979  1.00 10.30  ? 110  PHE F CD1 1 
ATOM   11151 C CD2 . PHE F  2 110 ? 32.722  62.192 21.829  1.00 9.93   ? 110  PHE F CD2 1 
ATOM   11152 C CE1 . PHE F  2 110 ? 30.201  62.042 20.735  1.00 11.93  ? 110  PHE F CE1 1 
ATOM   11153 C CE2 . PHE F  2 110 ? 32.000  63.351 21.596  1.00 11.55  ? 110  PHE F CE2 1 
ATOM   11154 C CZ  . PHE F  2 110 ? 30.738  63.279 21.047  1.00 12.55  ? 110  PHE F CZ  1 
ATOM   11155 N N   . HIS F  2 111 ? 35.226  59.900 19.661  1.00 7.99   ? 111  HIS F N   1 
ATOM   11156 C CA  . HIS F  2 111 ? 36.036  60.563 18.648  1.00 8.46   ? 111  HIS F CA  1 
ATOM   11157 C C   . HIS F  2 111 ? 36.129  59.744 17.366  1.00 8.42   ? 111  HIS F C   1 
ATOM   11158 O O   . HIS F  2 111 ? 36.065  60.286 16.266  1.00 8.88   ? 111  HIS F O   1 
ATOM   11159 C CB  . HIS F  2 111 ? 37.442  60.829 19.181  1.00 8.96   ? 111  HIS F CB  1 
ATOM   11160 C CG  . HIS F  2 111 ? 37.502  61.930 20.191  1.00 9.63   ? 111  HIS F CG  1 
ATOM   11161 N ND1 . HIS F  2 111 ? 37.173  63.233 19.889  1.00 10.66  ? 111  HIS F ND1 1 
ATOM   11162 C CD2 . HIS F  2 111 ? 37.868  61.927 21.494  1.00 9.85   ? 111  HIS F CD2 1 
ATOM   11163 C CE1 . HIS F  2 111 ? 37.322  63.982 20.966  1.00 11.58  ? 111  HIS F CE1 1 
ATOM   11164 N NE2 . HIS F  2 111 ? 37.745  63.214 21.953  1.00 11.00  ? 111  HIS F NE2 1 
ATOM   11165 N N   . ASP F  2 112 ? 36.284  58.436 17.520  1.00 8.19   ? 112  ASP F N   1 
ATOM   11166 C CA  . ASP F  2 112 ? 36.342  57.527 16.387  1.00 8.65   ? 112  ASP F CA  1 
ATOM   11167 C C   . ASP F  2 112 ? 35.022  57.566 15.607  1.00 8.90   ? 112  ASP F C   1 
ATOM   11168 O O   . ASP F  2 112 ? 35.013  57.597 14.380  1.00 9.48   ? 112  ASP F O   1 
ATOM   11169 C CB  . ASP F  2 112 ? 36.639  56.114 16.895  1.00 9.03   ? 112  ASP F CB  1 
ATOM   11170 C CG  . ASP F  2 112 ? 37.023  55.162 15.795  1.00 10.17  ? 112  ASP F CG  1 
ATOM   11171 O OD1 . ASP F  2 112 ? 37.274  55.609 14.658  1.00 10.48  ? 112  ASP F OD1 1 
ATOM   11172 O OD2 . ASP F  2 112 ? 37.077  53.950 16.077  1.00 11.08  ? 112  ASP F OD2 1 
ATOM   11173 N N   . SER F  2 113 ? 33.915  57.578 16.343  1.00 8.83   ? 113  SER F N   1 
ATOM   11174 C CA  . SER F  2 113 ? 32.578  57.682 15.770  1.00 9.72   ? 113  SER F CA  1 
ATOM   11175 C C   . SER F  2 113 ? 32.373  58.966 14.975  1.00 10.22  ? 113  SER F C   1 
ATOM   11176 O O   . SER F  2 113 ? 31.804  58.937 13.884  1.00 11.26  ? 113  SER F O   1 
ATOM   11177 C CB  . SER F  2 113 ? 31.527  57.599 16.881  1.00 9.98   ? 113  SER F CB  1 
ATOM   11178 O OG  . SER F  2 113 ? 30.251  57.973 16.408  1.00 11.42  ? 113  SER F OG  1 
ATOM   11179 N N   . ASN F  2 114 ? 32.829  60.088 15.527  1.00 9.89   ? 114  ASN F N   1 
ATOM   11180 C CA  . ASN F  2 114 ? 32.653  61.396 14.888  1.00 10.89  ? 114  ASN F CA  1 
ATOM   11181 C C   . ASN F  2 114 ? 33.404  61.533 13.571  1.00 11.16  ? 114  ASN F C   1 
ATOM   11182 O O   . ASN F  2 114 ? 32.912  62.166 12.640  1.00 12.34  ? 114  ASN F O   1 
ATOM   11183 C CB  . ASN F  2 114 ? 33.095  62.512 15.829  1.00 11.00  ? 114  ASN F CB  1 
ATOM   11184 C CG  . ASN F  2 114 ? 32.188  62.656 17.029  1.00 11.31  ? 114  ASN F CG  1 
ATOM   11185 O OD1 . ASN F  2 114 ? 30.995  62.367 16.966  1.00 12.11  ? 114  ASN F OD1 1 
ATOM   11186 N ND2 . ASN F  2 114 ? 32.744  63.132 18.127  1.00 11.10  ? 114  ASN F ND2 1 
ATOM   11187 N N   . VAL F  2 115 ? 34.589  60.936 13.505  1.00 10.45  ? 115  VAL F N   1 
ATOM   11188 C CA  . VAL F  2 115 ? 35.395  60.927 12.289  1.00 10.96  ? 115  VAL F CA  1 
ATOM   11189 C C   . VAL F  2 115 ? 34.706  60.095 11.209  1.00 11.57  ? 115  VAL F C   1 
ATOM   11190 O O   . VAL F  2 115 ? 34.648  60.487 10.040  1.00 12.46  ? 115  VAL F O   1 
ATOM   11191 C CB  . VAL F  2 115 ? 36.799  60.337 12.551  1.00 10.64  ? 115  VAL F CB  1 
ATOM   11192 C CG1 . VAL F  2 115 ? 37.553  60.121 11.250  1.00 11.50  ? 115  VAL F CG1 1 
ATOM   11193 C CG2 . VAL F  2 115 ? 37.604  61.241 13.464  1.00 10.77  ? 115  VAL F CG2 1 
ATOM   11194 N N   . LYS F  2 116 ? 34.193  58.940 11.619  1.00 11.45  ? 116  LYS F N   1 
ATOM   11195 C CA  . LYS F  2 116 ? 33.548  58.010 10.705  1.00 12.57  ? 116  LYS F CA  1 
ATOM   11196 C C   . LYS F  2 116 ? 32.262  58.577 10.138  1.00 13.84  ? 116  LYS F C   1 
ATOM   11197 O O   . LYS F  2 116 ? 31.966  58.405 8.956   1.00 15.12  ? 116  LYS F O   1 
ATOM   11198 C CB  . LYS F  2 116 ? 33.241  56.706 11.424  1.00 12.70  ? 116  LYS F CB  1 
ATOM   11199 C CG  . LYS F  2 116 ? 33.549  55.484 10.596  1.00 13.97  ? 116  LYS F CG  1 
ATOM   11200 C CD  . LYS F  2 116 ? 32.314  54.758 10.126  1.00 15.82  ? 116  LYS F CD  1 
ATOM   11201 C CE  . LYS F  2 116 ? 32.721  53.672 9.148   1.00 17.55  ? 116  LYS F CE  1 
ATOM   11202 N NZ  . LYS F  2 116 ? 31.776  52.530 9.239   1.00 19.70  ? 116  LYS F NZ  1 
ATOM   11203 N N   . ASN F  2 117 ? 31.492  59.248 10.984  1.00 13.91  ? 117  ASN F N   1 
ATOM   11204 C CA  . ASN F  2 117 ? 30.248  59.859 10.543  1.00 15.78  ? 117  ASN F CA  1 
ATOM   11205 C C   . ASN F  2 117 ? 30.497  61.019 9.586   1.00 16.60  ? 117  ASN F C   1 
ATOM   11206 O O   . ASN F  2 117 ? 29.726  61.235 8.647   1.00 18.53  ? 117  ASN F O   1 
ATOM   11207 C CB  . ASN F  2 117 ? 29.417  60.306 11.746  1.00 16.10  ? 117  ASN F CB  1 
ATOM   11208 C CG  . ASN F  2 117 ? 28.928  59.136 12.582  1.00 15.98  ? 117  ASN F CG  1 
ATOM   11209 O OD1 . ASN F  2 117 ? 28.859  58.004 12.108  1.00 16.45  ? 117  ASN F OD1 1 
ATOM   11210 N ND2 . ASN F  2 117 ? 28.591  59.408 13.839  1.00 15.67  ? 117  ASN F ND2 1 
ATOM   11211 N N   . LEU F  2 118 ? 31.580  61.749 9.823   1.00 15.57  ? 118  LEU F N   1 
ATOM   11212 C CA  . LEU F  2 118 ? 31.997  62.825 8.935   1.00 16.57  ? 118  LEU F CA  1 
ATOM   11213 C C   . LEU F  2 118 ? 32.488  62.261 7.601   1.00 16.88  ? 118  LEU F C   1 
ATOM   11214 O O   . LEU F  2 118 ? 32.223  62.831 6.542   1.00 18.42  ? 118  LEU F O   1 
ATOM   11215 C CB  . LEU F  2 118 ? 33.097  63.655 9.597   1.00 15.85  ? 118  LEU F CB  1 
ATOM   11216 C CG  . LEU F  2 118 ? 33.691  64.824 8.814   1.00 17.19  ? 118  LEU F CG  1 
ATOM   11217 C CD1 . LEU F  2 118 ? 32.610  65.773 8.328   1.00 19.51  ? 118  LEU F CD1 1 
ATOM   11218 C CD2 . LEU F  2 118 ? 34.693  65.563 9.681   1.00 17.01  ? 118  LEU F CD2 1 
ATOM   11219 N N   . TYR F  2 119 ? 33.205  61.144 7.653   1.00 15.81  ? 119  TYR F N   1 
ATOM   11220 C CA  . TYR F  2 119 ? 33.688  60.503 6.442   1.00 16.44  ? 119  TYR F CA  1 
ATOM   11221 C C   . TYR F  2 119 ? 32.529  59.982 5.611   1.00 18.12  ? 119  TYR F C   1 
ATOM   11222 O O   . TYR F  2 119 ? 32.517  60.137 4.393   1.00 19.43  ? 119  TYR F O   1 
ATOM   11223 C CB  . TYR F  2 119 ? 34.642  59.359 6.779   1.00 15.58  ? 119  TYR F CB  1 
ATOM   11224 C CG  . TYR F  2 119 ? 35.055  58.550 5.572   1.00 16.72  ? 119  TYR F CG  1 
ATOM   11225 C CD1 . TYR F  2 119 ? 36.060  59.000 4.725   1.00 17.24  ? 119  TYR F CD1 1 
ATOM   11226 C CD2 . TYR F  2 119 ? 34.437  57.342 5.271   1.00 17.75  ? 119  TYR F CD2 1 
ATOM   11227 C CE1 . TYR F  2 119 ? 36.445  58.267 3.618   1.00 18.58  ? 119  TYR F CE1 1 
ATOM   11228 C CE2 . TYR F  2 119 ? 34.815  56.603 4.160   1.00 19.25  ? 119  TYR F CE2 1 
ATOM   11229 C CZ  . TYR F  2 119 ? 35.820  57.070 3.337   1.00 19.58  ? 119  TYR F CZ  1 
ATOM   11230 O OH  . TYR F  2 119 ? 36.210  56.350 2.232   1.00 21.34  ? 119  TYR F OH  1 
ATOM   11231 N N   . ASP F  2 120 ? 31.559  59.355 6.269   1.00 18.48  ? 120  ASP F N   1 
ATOM   11232 C CA  . ASP F  2 120 ? 30.386  58.836 5.574   1.00 20.75  ? 120  ASP F CA  1 
ATOM   11233 C C   . ASP F  2 120 ? 29.540  59.967 4.990   1.00 22.62  ? 120  ASP F C   1 
ATOM   11234 O O   . ASP F  2 120 ? 29.002  59.841 3.897   1.00 24.78  ? 120  ASP F O   1 
ATOM   11235 C CB  . ASP F  2 120 ? 29.544  57.965 6.512   1.00 21.16  ? 120  ASP F CB  1 
ATOM   11236 C CG  . ASP F  2 120 ? 30.157  56.587 6.753   1.00 20.64  ? 120  ASP F CG  1 
ATOM   11237 O OD1 . ASP F  2 120 ? 30.802  56.029 5.831   1.00 21.19  ? 120  ASP F OD1 1 
ATOM   11238 O OD2 . ASP F  2 120 ? 29.969  56.049 7.866   1.00 20.06  ? 120  ASP F OD2 1 
ATOM   11239 N N   . LYS F  2 121 ? 29.440  61.071 5.720   1.00 22.25  ? 121  LYS F N   1 
ATOM   11240 C CA  . LYS F  2 121 ? 28.710  62.254 5.269   1.00 24.52  ? 121  LYS F CA  1 
ATOM   11241 C C   . LYS F  2 121 ? 29.207  62.715 3.909   1.00 25.46  ? 121  LYS F C   1 
ATOM   11242 O O   . LYS F  2 121 ? 28.418  62.990 3.007   1.00 28.11  ? 121  LYS F O   1 
ATOM   11243 C CB  . LYS F  2 121 ? 28.889  63.376 6.291   1.00 23.95  ? 121  LYS F CB  1 
ATOM   11244 C CG  . LYS F  2 121 ? 28.056  64.622 6.059   1.00 26.88  ? 121  LYS F CG  1 
ATOM   11245 C CD  . LYS F  2 121 ? 28.225  65.575 7.240   1.00 26.61  ? 121  LYS F CD  1 
ATOM   11246 C CE  . LYS F  2 121 ? 27.233  66.730 7.211   1.00 30.25  ? 121  LYS F CE  1 
ATOM   11247 N NZ  . LYS F  2 121 ? 27.746  67.904 6.448   1.00 31.82  ? 121  LYS F NZ  1 
ATOM   11248 N N   . VAL F  2 122 ? 30.525  62.792 3.773   1.00 23.66  ? 122  VAL F N   1 
ATOM   11249 C CA  . VAL F  2 122 ? 31.160  63.177 2.526   1.00 24.47  ? 122  VAL F CA  1 
ATOM   11250 C C   . VAL F  2 122 ? 30.948  62.094 1.469   1.00 25.51  ? 122  VAL F C   1 
ATOM   11251 O O   . VAL F  2 122 ? 30.625  62.394 0.320   1.00 27.56  ? 122  VAL F O   1 
ATOM   11252 C CB  . VAL F  2 122 ? 32.666  63.441 2.736   1.00 22.69  ? 122  VAL F CB  1 
ATOM   11253 C CG1 . VAL F  2 122 ? 33.380  63.674 1.409   1.00 23.68  ? 122  VAL F CG1 1 
ATOM   11254 C CG2 . VAL F  2 122 ? 32.856  64.634 3.657   1.00 22.54  ? 122  VAL F CG2 1 
ATOM   11255 N N   . ARG F  2 123 ? 31.125  60.838 1.864   1.00 24.52  ? 123  ARG F N   1 
ATOM   11256 C CA  . ARG F  2 123 ? 30.954  59.710 0.956   1.00 25.94  ? 123  ARG F CA  1 
ATOM   11257 C C   . ARG F  2 123 ? 29.571  59.736 0.316   1.00 29.00  ? 123  ARG F C   1 
ATOM   11258 O O   . ARG F  2 123 ? 29.436  59.525 -0.893  1.00 30.98  ? 123  ARG F O   1 
ATOM   11259 C CB  . ARG F  2 123 ? 31.141  58.400 1.716   1.00 24.99  ? 123  ARG F CB  1 
ATOM   11260 C CG  . ARG F  2 123 ? 31.233  57.166 0.837   1.00 26.65  ? 123  ARG F CG  1 
ATOM   11261 C CD  . ARG F  2 123 ? 31.339  55.898 1.675   1.00 26.33  ? 123  ARG F CD  1 
ATOM   11262 N NE  . ARG F  2 123 ? 30.295  55.803 2.701   1.00 26.41  ? 123  ARG F NE  1 
ATOM   11263 C CZ  . ARG F  2 123 ? 29.013  55.514 2.467   1.00 29.00  ? 123  ARG F CZ  1 
ATOM   11264 N NH1 . ARG F  2 123 ? 28.565  55.287 1.231   1.00 31.76  ? 123  ARG F NH1 1 
ATOM   11265 N NH2 . ARG F  2 123 ? 28.160  55.459 3.481   1.00 29.20  ? 123  ARG F NH2 1 
ATOM   11266 N N   . LEU F  2 124 ? 28.552  60.000 1.135   1.00 29.79  ? 124  LEU F N   1 
ATOM   11267 C CA  . LEU F  2 124 ? 27.156  60.015 0.684   1.00 33.35  ? 124  LEU F CA  1 
ATOM   11268 C C   . LEU F  2 124 ? 26.830  61.173 -0.264  1.00 35.69  ? 124  LEU F C   1 
ATOM   11269 O O   . LEU F  2 124 ? 25.907  61.070 -1.074  1.00 39.12  ? 124  LEU F O   1 
ATOM   11270 C CB  . LEU F  2 124 ? 26.208  60.038 1.887   1.00 33.84  ? 124  LEU F CB  1 
ATOM   11271 C CG  . LEU F  2 124 ? 26.195  58.743 2.708   1.00 32.86  ? 124  LEU F CG  1 
ATOM   11272 C CD1 . LEU F  2 124 ? 25.602  58.960 4.096   1.00 32.42  ? 124  LEU F CD1 1 
ATOM   11273 C CD2 . LEU F  2 124 ? 25.451  57.638 1.971   1.00 36.05  ? 124  LEU F CD2 1 
ATOM   11274 N N   . GLN F  2 125 ? 27.582  62.267 -0.158  1.00 34.37  ? 125  GLN F N   1 
ATOM   11275 C CA  . GLN F  2 125 ? 27.448  63.394 -1.078  1.00 36.68  ? 125  GLN F CA  1 
ATOM   11276 C C   . GLN F  2 125 ? 28.060  63.067 -2.420  1.00 37.17  ? 125  GLN F C   1 
ATOM   11277 O O   . GLN F  2 125 ? 27.421  63.217 -3.457  1.00 40.26  ? 125  GLN F O   1 
ATOM   11278 C CB  . GLN F  2 125 ? 28.140  64.639 -0.527  1.00 35.49  ? 125  GLN F CB  1 
ATOM   11279 C CG  . GLN F  2 125 ? 27.352  65.359 0.543   1.00 36.55  ? 125  GLN F CG  1 
ATOM   11280 C CD  . GLN F  2 125 ? 28.110  66.542 1.098   1.00 35.76  ? 125  GLN F CD  1 
ATOM   11281 O OE1 . GLN F  2 125 ? 28.239  67.569 0.434   1.00 37.90  ? 125  GLN F OE1 1 
ATOM   11282 N NE2 . GLN F  2 125 ? 28.619  66.405 2.315   1.00 33.17  ? 125  GLN F NE2 1 
ATOM   11283 N N   . LEU F  2 126 ? 29.313  62.632 -2.388  1.00 34.53  ? 126  LEU F N   1 
ATOM   11284 C CA  . LEU F  2 126 ? 30.073  62.395 -3.602  1.00 35.00  ? 126  LEU F CA  1 
ATOM   11285 C C   . LEU F  2 126 ? 29.493  61.254 -4.424  1.00 37.15  ? 126  LEU F C   1 
ATOM   11286 O O   . LEU F  2 126 ? 29.482  61.327 -5.643  1.00 39.18  ? 126  LEU F O   1 
ATOM   11287 C CB  . LEU F  2 126 ? 31.547  62.128 -3.277  1.00 32.17  ? 126  LEU F CB  1 
ATOM   11288 C CG  . LEU F  2 126 ? 32.310  63.235 -2.538  1.00 30.58  ? 126  LEU F CG  1 
ATOM   11289 C CD1 . LEU F  2 126 ? 33.796  62.920 -2.509  1.00 28.88  ? 126  LEU F CD1 1 
ATOM   11290 C CD2 . LEU F  2 126 ? 32.076  64.597 -3.167  1.00 32.67  ? 126  LEU F CD2 1 
ATOM   11291 N N   . ARG F  2 127 ? 29.002  60.209 -3.762  1.00 37.15  ? 127  ARG F N   1 
ATOM   11292 C CA  . ARG F  2 127 ? 28.405  59.062 -4.461  1.00 39.86  ? 127  ARG F CA  1 
ATOM   11293 C C   . ARG F  2 127 ? 29.405  58.498 -5.494  1.00 40.04  ? 127  ARG F C   1 
ATOM   11294 O O   . ARG F  2 127 ? 30.579  58.325 -5.163  1.00 37.58  ? 127  ARG F O   1 
ATOM   11295 C CB  . ARG F  2 127 ? 27.023  59.443 -5.049  1.00 43.82  ? 127  ARG F CB  1 
ATOM   11296 C CG  . ARG F  2 127 ? 25.894  59.334 -4.026  1.00 44.88  ? 127  ARG F CG  1 
ATOM   11297 C CD  . ARG F  2 127 ? 24.860  60.463 -4.074  1.00 47.65  ? 127  ARG F CD  1 
ATOM   11298 N NE  . ARG F  2 127 ? 24.052  60.670 -5.293  1.00 52.19  ? 127  ARG F NE  1 
ATOM   11299 C CZ  . ARG F  2 127 ? 23.551  59.739 -6.116  1.00 55.38  ? 127  ARG F CZ  1 
ATOM   11300 N NH1 . ARG F  2 127 ? 23.739  58.434 -5.931  1.00 54.89  ? 127  ARG F NH1 1 
ATOM   11301 N NH2 . ARG F  2 127 ? 22.826  60.131 -7.161  1.00 59.68  ? 127  ARG F NH2 1 
ATOM   11302 N N   . ASP F  2 128 ? 28.979  58.230 -6.728  1.00 43.31  ? 128  ASP F N   1 
ATOM   11303 C CA  . ASP F  2 128 ? 29.881  57.649 -7.725  1.00 43.96  ? 128  ASP F CA  1 
ATOM   11304 C C   . ASP F  2 128 ? 30.635  58.702 -8.560  1.00 43.63  ? 128  ASP F C   1 
ATOM   11305 O O   . ASP F  2 128 ? 31.205  58.368 -9.596  1.00 44.92  ? 128  ASP F O   1 
ATOM   11306 C CB  . ASP F  2 128 ? 29.113  56.682 -8.641  1.00 48.01  ? 128  ASP F CB  1 
ATOM   11307 C CG  . ASP F  2 128 ? 28.054  57.379 -9.480  1.00 51.35  ? 128  ASP F CG  1 
ATOM   11308 O OD1 . ASP F  2 128 ? 27.597  58.468 -9.068  1.00 50.91  ? 128  ASP F OD1 1 
ATOM   11309 O OD2 . ASP F  2 128 ? 27.684  56.841 -10.550 1.00 54.91  ? 128  ASP F OD2 1 
ATOM   11310 N N   . ASN F  2 129 ? 30.644  59.958 -8.106  1.00 42.33  ? 129  ASN F N   1 
ATOM   11311 C CA  . ASN F  2 129 ? 31.409  61.030 -8.764  1.00 42.21  ? 129  ASN F CA  1 
ATOM   11312 C C   . ASN F  2 129 ? 32.891  61.119 -8.343  1.00 39.44  ? 129  ASN F C   1 
ATOM   11313 O O   . ASN F  2 129 ? 33.623  61.973 -8.854  1.00 39.60  ? 129  ASN F O   1 
ATOM   11314 C CB  . ASN F  2 129 ? 30.730  62.394 -8.542  1.00 43.10  ? 129  ASN F CB  1 
ATOM   11315 C CG  . ASN F  2 129 ? 29.528  62.618 -9.453  1.00 47.08  ? 129  ASN F CG  1 
ATOM   11316 O OD1 . ASN F  2 129 ? 28.969  61.678 -10.024 1.00 49.20  ? 129  ASN F OD1 1 
ATOM   11317 N ND2 . ASN F  2 129 ? 29.124  63.881 -9.589  1.00 48.71  ? 129  ASN F ND2 1 
ATOM   11318 N N   . ALA F  2 130 ? 33.329  60.249 -7.428  1.00 37.40  ? 130  ALA F N   1 
ATOM   11319 C CA  . ALA F  2 130 ? 34.739  60.186 -7.011  1.00 35.42  ? 130  ALA F CA  1 
ATOM   11320 C C   . ALA F  2 130 ? 35.147  58.759 -6.671  1.00 35.07  ? 130  ALA F C   1 
ATOM   11321 O O   . ALA F  2 130 ? 34.288  57.925 -6.410  1.00 35.76  ? 130  ALA F O   1 
ATOM   11322 C CB  . ALA F  2 130 ? 34.971  61.088 -5.814  1.00 33.22  ? 130  ALA F CB  1 
ATOM   11323 N N   . LYS F  2 131 ? 36.452  58.482 -6.669  1.00 34.59  ? 131  LYS F N   1 
ATOM   11324 C CA  . LYS F  2 131 ? 36.976  57.163 -6.280  1.00 34.74  ? 131  LYS F CA  1 
ATOM   11325 C C   . LYS F  2 131 ? 37.204  57.080 -4.772  1.00 32.29  ? 131  LYS F C   1 
ATOM   11326 O O   . LYS F  2 131 ? 37.930  57.892 -4.211  1.00 30.81  ? 131  LYS F O   1 
ATOM   11327 C CB  . LYS F  2 131 ? 38.308  56.878 -6.977  1.00 36.15  ? 131  LYS F CB  1 
ATOM   11328 C CG  . LYS F  2 131 ? 38.248  56.789 -8.494  1.00 38.90  ? 131  LYS F CG  1 
ATOM   11329 C CD  . LYS F  2 131 ? 39.656  56.756 -9.086  1.00 40.32  ? 131  LYS F CD  1 
ATOM   11330 C CE  . LYS F  2 131 ? 39.726  56.074 -10.453 1.00 43.63  ? 131  LYS F CE  1 
ATOM   11331 N NZ  . LYS F  2 131 ? 39.531  54.591 -10.378 1.00 45.45  ? 131  LYS F NZ  1 
ATOM   11332 N N   . GLU F  2 132 ? 36.594  56.096 -4.116  1.00 32.20  ? 132  GLU F N   1 
ATOM   11333 C CA  . GLU F  2 132 ? 36.871  55.832 -2.708  1.00 30.24  ? 132  GLU F CA  1 
ATOM   11334 C C   . GLU F  2 132 ? 38.210  55.096 -2.603  1.00 30.95  ? 132  GLU F C   1 
ATOM   11335 O O   . GLU F  2 132 ? 38.284  53.891 -2.833  1.00 32.87  ? 132  GLU F O   1 
ATOM   11336 C CB  . GLU F  2 132 ? 35.741  55.008 -2.081  1.00 30.45  ? 132  GLU F CB  1 
ATOM   11337 C CG  . GLU F  2 132 ? 35.813  54.920 -0.561  1.00 28.31  ? 132  GLU F CG  1 
ATOM   11338 C CD  . GLU F  2 132 ? 34.570  54.315 0.073   1.00 28.64  ? 132  GLU F CD  1 
ATOM   11339 O OE1 . GLU F  2 132 ? 33.835  53.565 -0.600  1.00 31.08  ? 132  GLU F OE1 1 
ATOM   11340 O OE2 . GLU F  2 132 ? 34.325  54.591 1.262   1.00 26.82  ? 132  GLU F OE2 1 
ATOM   11341 N N   . LEU F  2 133 ? 39.266  55.832 -2.264  1.00 29.98  ? 133  LEU F N   1 
ATOM   11342 C CA  . LEU F  2 133 ? 40.633  55.285 -2.252  1.00 31.33  ? 133  LEU F CA  1 
ATOM   11343 C C   . LEU F  2 133 ? 40.897  54.243 -1.160  1.00 31.38  ? 133  LEU F C   1 
ATOM   11344 O O   . LEU F  2 133 ? 41.740  53.365 -1.344  1.00 33.67  ? 133  LEU F O   1 
ATOM   11345 C CB  . LEU F  2 133 ? 41.666  56.416 -2.145  1.00 30.84  ? 133  LEU F CB  1 
ATOM   11346 C CG  . LEU F  2 133 ? 42.225  56.977 -3.459  1.00 32.66  ? 133  LEU F CG  1 
ATOM   11347 C CD1 . LEU F  2 133 ? 41.175  57.072 -4.555  1.00 33.18  ? 133  LEU F CD1 1 
ATOM   11348 C CD2 . LEU F  2 133 ? 42.863  58.336 -3.217  1.00 32.06  ? 133  LEU F CD2 1 
ATOM   11349 N N   . GLY F  2 134 ? 40.193  54.347 -0.035  1.00 29.24  ? 134  GLY F N   1 
ATOM   11350 C CA  . GLY F  2 134 ? 40.339  53.390 1.066   1.00 29.30  ? 134  GLY F CA  1 
ATOM   11351 C C   . GLY F  2 134 ? 41.133  53.898 2.260   1.00 27.88  ? 134  GLY F C   1 
ATOM   11352 O O   . GLY F  2 134 ? 41.295  53.181 3.252   1.00 27.94  ? 134  GLY F O   1 
ATOM   11353 N N   . ASN F  2 135 ? 41.607  55.141 2.184   1.00 26.95  ? 135  ASN F N   1 
ATOM   11354 C CA  . ASN F  2 135 ? 42.489  55.708 3.211   1.00 26.30  ? 135  ASN F CA  1 
ATOM   11355 C C   . ASN F  2 135 ? 41.933  56.973 3.863   1.00 23.74  ? 135  ASN F C   1 
ATOM   11356 O O   . ASN F  2 135 ? 42.649  57.671 4.581   1.00 23.48  ? 135  ASN F O   1 
ATOM   11357 C CB  . ASN F  2 135 ? 43.854  56.011 2.599   1.00 28.76  ? 135  ASN F CB  1 
ATOM   11358 C CG  . ASN F  2 135 ? 43.760  56.907 1.386   1.00 29.26  ? 135  ASN F CG  1 
ATOM   11359 O OD1 . ASN F  2 135 ? 42.722  57.514 1.128   1.00 27.70  ? 135  ASN F OD1 1 
ATOM   11360 N ND2 . ASN F  2 135 ? 44.838  56.981 0.622   1.00 31.96  ? 135  ASN F ND2 1 
ATOM   11361 N N   . GLY F  2 136 ? 40.659  57.258 3.608   1.00 22.32  ? 136  GLY F N   1 
ATOM   11362 C CA  . GLY F  2 136 ? 40.030  58.493 4.061   1.00 20.64  ? 136  GLY F CA  1 
ATOM   11363 C C   . GLY F  2 136 ? 39.889  59.515 2.949   1.00 21.24  ? 136  GLY F C   1 
ATOM   11364 O O   . GLY F  2 136 ? 39.237  60.545 3.131   1.00 20.55  ? 136  GLY F O   1 
ATOM   11365 N N   . CYS F  2 137 ? 40.489  59.223 1.795   1.00 22.82  ? 137  CYS F N   1 
ATOM   11366 C CA  . CYS F  2 137 ? 40.514  60.158 0.682   1.00 23.83  ? 137  CYS F CA  1 
ATOM   11367 C C   . CYS F  2 137 ? 39.563  59.760 -0.434  1.00 24.60  ? 137  CYS F C   1 
ATOM   11368 O O   . CYS F  2 137 ? 39.335  58.578 -0.693  1.00 25.17  ? 137  CYS F O   1 
ATOM   11369 C CB  . CYS F  2 137 ? 41.932  60.302 0.120   1.00 25.62  ? 137  CYS F CB  1 
ATOM   11370 S SG  . CYS F  2 137 ? 43.149  60.912 1.307   1.00 25.75  ? 137  CYS F SG  1 
ATOM   11371 N N   . PHE F  2 138 ? 39.023  60.781 -1.091  1.00 25.11  ? 138  PHE F N   1 
ATOM   11372 C CA  . PHE F  2 138 ? 38.186  60.620 -2.260  1.00 26.41  ? 138  PHE F CA  1 
ATOM   11373 C C   . PHE F  2 138 ? 38.849  61.342 -3.412  1.00 28.19  ? 138  PHE F C   1 
ATOM   11374 O O   . PHE F  2 138 ? 39.146  62.524 -3.305  1.00 28.38  ? 138  PHE F O   1 
ATOM   11375 C CB  . PHE F  2 138 ? 36.811  61.222 -2.007  1.00 26.06  ? 138  PHE F CB  1 
ATOM   11376 C CG  . PHE F  2 138 ? 36.016  60.484 -0.972  1.00 24.84  ? 138  PHE F CG  1 
ATOM   11377 C CD1 . PHE F  2 138 ? 35.279  59.359 -1.322  1.00 25.69  ? 138  PHE F CD1 1 
ATOM   11378 C CD2 . PHE F  2 138 ? 36.013  60.906 0.355   1.00 23.17  ? 138  PHE F CD2 1 
ATOM   11379 C CE1 . PHE F  2 138 ? 34.548  58.673 -0.373  1.00 25.01  ? 138  PHE F CE1 1 
ATOM   11380 C CE2 . PHE F  2 138 ? 35.280  60.224 1.307   1.00 22.24  ? 138  PHE F CE2 1 
ATOM   11381 C CZ  . PHE F  2 138 ? 34.549  59.104 0.943   1.00 23.18  ? 138  PHE F CZ  1 
ATOM   11382 N N   . GLU F  2 139 ? 39.069  60.627 -4.510  1.00 29.89  ? 139  GLU F N   1 
ATOM   11383 C CA  . GLU F  2 139 ? 39.745  61.170 -5.677  1.00 31.87  ? 139  GLU F CA  1 
ATOM   11384 C C   . GLU F  2 139 ? 38.723  61.437 -6.780  1.00 33.34  ? 139  GLU F C   1 
ATOM   11385 O O   . GLU F  2 139 ? 38.051  60.521 -7.246  1.00 34.09  ? 139  GLU F O   1 
ATOM   11386 C CB  . GLU F  2 139 ? 40.796  60.174 -6.148  1.00 33.28  ? 139  GLU F CB  1 
ATOM   11387 C CG  . GLU F  2 139 ? 41.752  60.697 -7.201  1.00 35.46  ? 139  GLU F CG  1 
ATOM   11388 C CD  . GLU F  2 139 ? 42.533  59.572 -7.842  1.00 37.52  ? 139  GLU F CD  1 
ATOM   11389 O OE1 . GLU F  2 139 ? 43.470  59.049 -7.198  1.00 37.83  ? 139  GLU F OE1 1 
ATOM   11390 O OE2 . GLU F  2 139 ? 42.185  59.188 -8.980  1.00 39.23  ? 139  GLU F OE2 1 
ATOM   11391 N N   . PHE F  2 140 ? 38.626  62.694 -7.205  1.00 34.29  ? 140  PHE F N   1 
ATOM   11392 C CA  . PHE F  2 140 ? 37.553  63.140 -8.101  1.00 35.96  ? 140  PHE F CA  1 
ATOM   11393 C C   . PHE F  2 140 ? 37.777  62.744 -9.556  1.00 38.34  ? 140  PHE F C   1 
ATOM   11394 O O   . PHE F  2 140 ? 38.905  62.769 -10.044 1.00 39.19  ? 140  PHE F O   1 
ATOM   11395 C CB  . PHE F  2 140 ? 37.396  64.661 -8.019  1.00 36.58  ? 140  PHE F CB  1 
ATOM   11396 C CG  . PHE F  2 140 ? 36.942  65.148 -6.677  1.00 34.96  ? 140  PHE F CG  1 
ATOM   11397 C CD1 . PHE F  2 140 ? 37.859  65.426 -5.677  1.00 33.60  ? 140  PHE F CD1 1 
ATOM   11398 C CD2 . PHE F  2 140 ? 35.594  65.322 -6.413  1.00 35.24  ? 140  PHE F CD2 1 
ATOM   11399 C CE1 . PHE F  2 140 ? 37.439  65.874 -4.436  1.00 32.36  ? 140  PHE F CE1 1 
ATOM   11400 C CE2 . PHE F  2 140 ? 35.167  65.769 -5.177  1.00 34.10  ? 140  PHE F CE2 1 
ATOM   11401 C CZ  . PHE F  2 140 ? 36.091  66.044 -4.186  1.00 32.55  ? 140  PHE F CZ  1 
ATOM   11402 N N   . TYR F  2 141 ? 36.697  62.392 -10.248 1.00 39.92  ? 141  TYR F N   1 
ATOM   11403 C CA  . TYR F  2 141 ? 36.767  62.127 -11.687 1.00 42.62  ? 141  TYR F CA  1 
ATOM   11404 C C   . TYR F  2 141 ? 36.864  63.428 -12.471 1.00 44.38  ? 141  TYR F C   1 
ATOM   11405 O O   . TYR F  2 141 ? 37.517  63.490 -13.515 1.00 46.20  ? 141  TYR F O   1 
ATOM   11406 C CB  . TYR F  2 141 ? 35.551  61.329 -12.158 1.00 44.18  ? 141  TYR F CB  1 
ATOM   11407 C CG  . TYR F  2 141 ? 35.506  59.937 -11.584 1.00 43.49  ? 141  TYR F CG  1 
ATOM   11408 C CD1 . TYR F  2 141 ? 36.546  59.043 -11.806 1.00 43.82  ? 141  TYR F CD1 1 
ATOM   11409 C CD2 . TYR F  2 141 ? 34.437  59.519 -10.808 1.00 43.00  ? 141  TYR F CD2 1 
ATOM   11410 C CE1 . TYR F  2 141 ? 36.514  57.767 -11.280 1.00 43.74  ? 141  TYR F CE1 1 
ATOM   11411 C CE2 . TYR F  2 141 ? 34.396  58.244 -10.277 1.00 42.78  ? 141  TYR F CE2 1 
ATOM   11412 C CZ  . TYR F  2 141 ? 35.436  57.371 -10.516 1.00 43.18  ? 141  TYR F CZ  1 
ATOM   11413 O OH  . TYR F  2 141 ? 35.398  56.100 -9.983  1.00 43.50  ? 141  TYR F OH  1 
ATOM   11414 N N   . HIS F  2 142 ? 36.201  64.458 -11.958 1.00 44.31  ? 142  HIS F N   1 
ATOM   11415 C CA  . HIS F  2 142 ? 36.264  65.800 -12.524 1.00 46.28  ? 142  HIS F CA  1 
ATOM   11416 C C   . HIS F  2 142 ? 37.322  66.616 -11.797 1.00 45.30  ? 142  HIS F C   1 
ATOM   11417 O O   . HIS F  2 142 ? 37.724  66.279 -10.681 1.00 43.01  ? 142  HIS F O   1 
ATOM   11418 C CB  . HIS F  2 142 ? 34.905  66.498 -12.409 1.00 47.69  ? 142  HIS F CB  1 
ATOM   11419 C CG  . HIS F  2 142 ? 34.373  66.565 -11.011 1.00 45.79  ? 142  HIS F CG  1 
ATOM   11420 N ND1 . HIS F  2 142 ? 34.492  67.688 -10.222 1.00 45.65  ? 142  HIS F ND1 1 
ATOM   11421 C CD2 . HIS F  2 142 ? 33.733  65.639 -10.256 1.00 44.31  ? 142  HIS F CD2 1 
ATOM   11422 C CE1 . HIS F  2 142 ? 33.940  67.454 -9.044  1.00 43.95  ? 142  HIS F CE1 1 
ATOM   11423 N NE2 . HIS F  2 142 ? 33.474  66.218 -9.038  1.00 43.04  ? 142  HIS F NE2 1 
ATOM   11424 N N   . LYS F  2 143 ? 37.774  67.686 -12.437 1.00 47.47  ? 143  LYS F N   1 
ATOM   11425 C CA  . LYS F  2 143 ? 38.667  68.637 -11.792 1.00 47.51  ? 143  LYS F CA  1 
ATOM   11426 C C   . LYS F  2 143 ? 37.856  69.379 -10.735 1.00 47.00  ? 143  LYS F C   1 
ATOM   11427 O O   . LYS F  2 143 ? 36.742  69.827 -11.011 1.00 48.52  ? 143  LYS F O   1 
ATOM   11428 C CB  . LYS F  2 143 ? 39.233  69.609 -12.822 1.00 50.66  ? 143  LYS F CB  1 
ATOM   11429 C CG  . LYS F  2 143 ? 40.442  70.398 -12.357 1.00 51.46  ? 143  LYS F CG  1 
ATOM   11430 C CD  . LYS F  2 143 ? 40.882  71.386 -13.434 1.00 55.16  ? 143  LYS F CD  1 
ATOM   11431 C CE  . LYS F  2 143 ? 41.783  72.475 -12.872 1.00 56.90  ? 143  LYS F CE  1 
ATOM   11432 N NZ  . LYS F  2 143 ? 41.067  73.437 -11.983 1.00 57.36  ? 143  LYS F NZ  1 
ATOM   11433 N N   . CYS F  2 144 ? 38.408  69.493 -9.529  1.00 45.28  ? 144  CYS F N   1 
ATOM   11434 C CA  . CYS F  2 144 ? 37.693  70.079 -8.395  1.00 44.71  ? 144  CYS F CA  1 
ATOM   11435 C C   . CYS F  2 144 ? 38.475  71.256 -7.806  1.00 45.99  ? 144  CYS F C   1 
ATOM   11436 O O   . CYS F  2 144 ? 39.400  71.065 -7.018  1.00 44.68  ? 144  CYS F O   1 
ATOM   11437 C CB  . CYS F  2 144 ? 37.450  69.003 -7.333  1.00 41.52  ? 144  CYS F CB  1 
ATOM   11438 S SG  . CYS F  2 144 ? 36.400  69.495 -5.946  1.00 40.81  ? 144  CYS F SG  1 
ATOM   11439 N N   . ASP F  2 145 ? 38.098  72.472 -8.196  1.00 49.11  ? 145  ASP F N   1 
ATOM   11440 C CA  . ASP F  2 145 ? 38.766  73.692 -7.723  1.00 51.32  ? 145  ASP F CA  1 
ATOM   11441 C C   . ASP F  2 145 ? 38.403  73.998 -6.258  1.00 50.27  ? 145  ASP F C   1 
ATOM   11442 O O   . ASP F  2 145 ? 37.704  73.218 -5.611  1.00 47.55  ? 145  ASP F O   1 
ATOM   11443 C CB  . ASP F  2 145 ? 38.455  74.880 -8.656  1.00 55.63  ? 145  ASP F CB  1 
ATOM   11444 C CG  . ASP F  2 145 ? 36.976  75.243 -8.698  1.00 57.02  ? 145  ASP F CG  1 
ATOM   11445 O OD1 . ASP F  2 145 ? 36.178  74.670 -7.932  1.00 54.80  ? 145  ASP F OD1 1 
ATOM   11446 O OD2 . ASP F  2 145 ? 36.607  76.113 -9.510  1.00 60.81  ? 145  ASP F OD2 1 
ATOM   11447 N N   . ASN F  2 146 ? 38.882  75.126 -5.737  1.00 52.77  ? 146  ASN F N   1 
ATOM   11448 C CA  . ASN F  2 146 ? 38.664  75.474 -4.330  1.00 52.22  ? 146  ASN F CA  1 
ATOM   11449 C C   . ASN F  2 146 ? 37.205  75.759 -3.974  1.00 52.89  ? 146  ASN F C   1 
ATOM   11450 O O   . ASN F  2 146 ? 36.809  75.597 -2.824  1.00 51.31  ? 146  ASN F O   1 
ATOM   11451 C CB  . ASN F  2 146 ? 39.543  76.660 -3.926  1.00 55.57  ? 146  ASN F CB  1 
ATOM   11452 C CG  . ASN F  2 146 ? 41.026  76.342 -4.002  1.00 55.24  ? 146  ASN F CG  1 
ATOM   11453 O OD1 . ASN F  2 146 ? 41.436  75.184 -3.927  1.00 51.93  ? 146  ASN F OD1 1 
ATOM   11454 N ND2 . ASN F  2 146 ? 41.838  77.376 -4.151  1.00 59.26  ? 146  ASN F ND2 1 
ATOM   11455 N N   . GLU F  2 147 ? 36.409  76.176 -4.954  1.00 55.64  ? 147  GLU F N   1 
ATOM   11456 C CA  . GLU F  2 147 ? 34.968  76.337 -4.748  1.00 56.88  ? 147  GLU F CA  1 
ATOM   11457 C C   . GLU F  2 147 ? 34.299  74.964 -4.719  1.00 53.32  ? 147  GLU F C   1 
ATOM   11458 O O   . GLU F  2 147 ? 33.424  74.707 -3.891  1.00 52.44  ? 147  GLU F O   1 
ATOM   11459 C CB  . GLU F  2 147 ? 34.339  77.204 -5.842  1.00 61.54  ? 147  GLU F CB  1 
ATOM   11460 C CG  . GLU F  2 147 ? 34.897  78.617 -5.919  1.00 66.07  ? 147  GLU F CG  1 
ATOM   11461 C CD  . GLU F  2 147 ? 36.096  78.722 -6.845  1.00 66.75  ? 147  GLU F CD  1 
ATOM   11462 O OE1 . GLU F  2 147 ? 35.895  78.915 -8.065  1.00 69.09  ? 147  GLU F OE1 1 
ATOM   11463 O OE2 . GLU F  2 147 ? 37.240  78.611 -6.351  1.00 65.30  ? 147  GLU F OE2 1 
ATOM   11464 N N   . CYS F  2 148 ? 34.718  74.093 -5.635  1.00 51.75  ? 148  CYS F N   1 
ATOM   11465 C CA  . CYS F  2 148 ? 34.270  72.704 -5.658  1.00 48.72  ? 148  CYS F CA  1 
ATOM   11466 C C   . CYS F  2 148 ? 34.606  71.998 -4.342  1.00 45.32  ? 148  CYS F C   1 
ATOM   11467 O O   . CYS F  2 148 ? 33.774  71.280 -3.785  1.00 43.85  ? 148  CYS F O   1 
ATOM   11468 C CB  . CYS F  2 148 ? 34.910  71.966 -6.836  1.00 47.99  ? 148  CYS F CB  1 
ATOM   11469 S SG  . CYS F  2 148 ? 34.693  70.176 -6.810  1.00 44.43  ? 148  CYS F SG  1 
ATOM   11470 N N   . MET F  2 149 ? 35.822  72.211 -3.845  1.00 44.62  ? 149  MET F N   1 
ATOM   11471 C CA  . MET F  2 149 ? 36.229  71.655 -2.558  1.00 41.85  ? 149  MET F CA  1 
ATOM   11472 C C   . MET F  2 149 ? 35.372  72.230 -1.438  1.00 42.74  ? 149  MET F C   1 
ATOM   11473 O O   . MET F  2 149 ? 34.992  71.518 -0.511  1.00 40.39  ? 149  MET F O   1 
ATOM   11474 C CB  . MET F  2 149 ? 37.702  71.958 -2.280  1.00 41.77  ? 149  MET F CB  1 
ATOM   11475 C CG  . MET F  2 149 ? 38.683  71.290 -3.230  1.00 41.25  ? 149  MET F CG  1 
ATOM   11476 S SD  . MET F  2 149 ? 38.579  69.495 -3.208  1.00 37.60  ? 149  MET F SD  1 
ATOM   11477 C CE  . MET F  2 149 ? 40.040  69.047 -4.145  1.00 38.32  ? 149  MET F CE  1 
ATOM   11478 N N   . GLU F  2 150 ? 35.075  73.522 -1.527  1.00 46.74  ? 150  GLU F N   1 
ATOM   11479 C CA  . GLU F  2 150 ? 34.263  74.196 -0.518  1.00 48.59  ? 150  GLU F CA  1 
ATOM   11480 C C   . GLU F  2 150 ? 32.829  73.670 -0.484  1.00 48.85  ? 150  GLU F C   1 
ATOM   11481 O O   . GLU F  2 150 ? 32.231  73.594 0.587   1.00 48.39  ? 150  GLU F O   1 
ATOM   11482 C CB  . GLU F  2 150 ? 34.282  75.716 -0.748  1.00 53.40  ? 150  GLU F CB  1 
ATOM   11483 C CG  . GLU F  2 150 ? 33.411  76.547 0.193   1.00 56.05  ? 150  GLU F CG  1 
ATOM   11484 C CD  . GLU F  2 150 ? 33.738  76.349 1.662   1.00 53.90  ? 150  GLU F CD  1 
ATOM   11485 O OE1 . GLU F  2 150 ? 34.874  75.945 1.987   1.00 51.55  ? 150  GLU F OE1 1 
ATOM   11486 O OE2 . GLU F  2 150 ? 32.853  76.605 2.504   1.00 55.04  ? 150  GLU F OE2 1 
ATOM   11487 N N   . SER F  2 151 ? 32.286  73.297 -1.642  1.00 50.19  ? 151  SER F N   1 
ATOM   11488 C CA  . SER F  2 151 ? 30.922  72.759 -1.714  1.00 51.20  ? 151  SER F CA  1 
ATOM   11489 C C   . SER F  2 151 ? 30.804  71.417 -0.982  1.00 47.82  ? 151  SER F C   1 
ATOM   11490 O O   . SER F  2 151 ? 29.752  71.091 -0.421  1.00 48.31  ? 151  SER F O   1 
ATOM   11491 C CB  . SER F  2 151 ? 30.473  72.602 -3.166  1.00 53.27  ? 151  SER F CB  1 
ATOM   11492 O OG  . SER F  2 151 ? 31.148  71.536 -3.805  1.00 50.48  ? 151  SER F OG  1 
ATOM   11493 N N   . VAL F  2 152 ? 31.892  70.649 -0.985  1.00 45.11  ? 152  VAL F N   1 
ATOM   11494 C CA  . VAL F  2 152 ? 31.945  69.373 -0.279  1.00 42.04  ? 152  VAL F CA  1 
ATOM   11495 C C   . VAL F  2 152 ? 31.946  69.621 1.229   1.00 41.47  ? 152  VAL F C   1 
ATOM   11496 O O   . VAL F  2 152 ? 31.239  68.938 1.971   1.00 40.37  ? 152  VAL F O   1 
ATOM   11497 C CB  . VAL F  2 152 ? 33.188  68.548 -0.679  1.00 39.51  ? 152  VAL F CB  1 
ATOM   11498 C CG1 . VAL F  2 152 ? 33.222  67.225 0.072   1.00 36.52  ? 152  VAL F CG1 1 
ATOM   11499 C CG2 . VAL F  2 152 ? 33.204  68.300 -2.184  1.00 40.84  ? 152  VAL F CG2 1 
ATOM   11500 N N   . ARG F  2 153 ? 32.732  70.598 1.676   1.00 42.92  ? 153  ARG F N   1 
ATOM   11501 C CA  . ARG F  2 153 ? 32.748  70.978 3.092   1.00 43.18  ? 153  ARG F CA  1 
ATOM   11502 C C   . ARG F  2 153 ? 31.437  71.670 3.490   1.00 47.07  ? 153  ARG F C   1 
ATOM   11503 O O   . ARG F  2 153 ? 30.918  71.442 4.583   1.00 46.28  ? 153  ARG F O   1 
ATOM   11504 C CB  . ARG F  2 153 ? 33.935  71.895 3.406   1.00 43.81  ? 153  ARG F CB  1 
ATOM   11505 C CG  . ARG F  2 153 ? 35.300  71.309 3.083   1.00 41.60  ? 153  ARG F CG  1 
ATOM   11506 C CD  . ARG F  2 153 ? 36.430  72.227 3.539   1.00 42.96  ? 153  ARG F CD  1 
ATOM   11507 N NE  . ARG F  2 153 ? 37.456  72.358 2.503   1.00 43.90  ? 153  ARG F NE  1 
ATOM   11508 C CZ  . ARG F  2 153 ? 37.590  73.396 1.677   1.00 47.22  ? 153  ARG F CZ  1 
ATOM   11509 N NH1 . ARG F  2 153 ? 36.783  74.451 1.756   1.00 50.13  ? 153  ARG F NH1 1 
ATOM   11510 N NH2 . ARG F  2 153 ? 38.557  73.386 0.763   1.00 48.07  ? 153  ARG F NH2 1 
ATOM   11511 N N   . ASN F  2 154 ? 30.927  72.526 2.601   1.00 52.33  ? 154  ASN F N   1 
ATOM   11512 C CA  . ASN F  2 154 ? 29.588  73.128 2.728   1.00 57.21  ? 154  ASN F CA  1 
ATOM   11513 C C   . ASN F  2 154 ? 28.495  72.126 3.098   1.00 55.55  ? 154  ASN F C   1 
ATOM   11514 O O   . ASN F  2 154 ? 27.658  72.401 3.959   1.00 57.18  ? 154  ASN F O   1 
ATOM   11515 C CB  . ASN F  2 154 ? 29.164  73.777 1.397   1.00 62.98  ? 154  ASN F CB  1 
ATOM   11516 C CG  . ASN F  2 154 ? 29.439  75.268 1.335   1.00 69.79  ? 154  ASN F CG  1 
ATOM   11517 O OD1 . ASN F  2 154 ? 29.908  75.871 2.299   1.00 70.59  ? 154  ASN F OD1 1 
ATOM   11518 N ND2 . ASN F  2 154 ? 29.136  75.874 0.179   1.00 77.12  ? 154  ASN F ND2 1 
ATOM   11519 N N   . GLY F  2 155 ? 28.518  70.970 2.436   1.00 52.48  ? 155  GLY F N   1 
ATOM   11520 C CA  . GLY F  2 155 ? 27.385  70.048 2.405   1.00 52.06  ? 155  GLY F CA  1 
ATOM   11521 C C   . GLY F  2 155 ? 26.574  70.249 1.134   1.00 55.08  ? 155  GLY F C   1 
ATOM   11522 O O   . GLY F  2 155 ? 25.538  69.614 0.949   1.00 56.52  ? 155  GLY F O   1 
ATOM   11523 N N   . THR F  2 156 ? 27.070  71.114 0.249   1.00 56.32  ? 156  THR F N   1 
ATOM   11524 C CA  . THR F  2 156 ? 26.321  71.589 -0.915  1.00 60.25  ? 156  THR F CA  1 
ATOM   11525 C C   . THR F  2 156 ? 26.898  71.065 -2.232  1.00 59.05  ? 156  THR F C   1 
ATOM   11526 O O   . THR F  2 156 ? 26.649  71.638 -3.292  1.00 62.38  ? 156  THR F O   1 
ATOM   11527 C CB  . THR F  2 156 ? 26.333  73.134 -0.949  1.00 64.10  ? 156  THR F CB  1 
ATOM   11528 O OG1 . THR F  2 156 ? 25.955  73.643 0.335   1.00 64.99  ? 156  THR F OG1 1 
ATOM   11529 C CG2 . THR F  2 156 ? 25.375  73.693 -2.009  1.00 69.52  ? 156  THR F CG2 1 
ATOM   11530 N N   . TYR F  2 157 ? 27.659  69.974 -2.178  1.00 54.67  ? 157  TYR F N   1 
ATOM   11531 C CA  . TYR F  2 157 ? 28.269  69.424 -3.390  1.00 53.70  ? 157  TYR F CA  1 
ATOM   11532 C C   . TYR F  2 157 ? 27.192  69.051 -4.402  1.00 56.98  ? 157  TYR F C   1 
ATOM   11533 O O   . TYR F  2 157 ? 26.417  68.122 -4.179  1.00 56.94  ? 157  TYR F O   1 
ATOM   11534 C CB  . TYR F  2 157 ? 29.125  68.199 -3.072  1.00 49.26  ? 157  TYR F CB  1 
ATOM   11535 C CG  . TYR F  2 157 ? 29.714  67.550 -4.307  1.00 48.72  ? 157  TYR F CG  1 
ATOM   11536 C CD1 . TYR F  2 157 ? 30.787  68.132 -4.979  1.00 48.62  ? 157  TYR F CD1 1 
ATOM   11537 C CD2 . TYR F  2 157 ? 29.196  66.358 -4.809  1.00 48.81  ? 157  TYR F CD2 1 
ATOM   11538 C CE1 . TYR F  2 157 ? 31.328  67.545 -6.112  1.00 48.52  ? 157  TYR F CE1 1 
ATOM   11539 C CE2 . TYR F  2 157 ? 29.731  65.764 -5.941  1.00 48.84  ? 157  TYR F CE2 1 
ATOM   11540 C CZ  . TYR F  2 157 ? 30.796  66.360 -6.588  1.00 48.60  ? 157  TYR F CZ  1 
ATOM   11541 O OH  . TYR F  2 157 ? 31.327  65.769 -7.711  1.00 48.91  ? 157  TYR F OH  1 
ATOM   11542 N N   . ASP F  2 158 ? 27.150  69.783 -5.512  1.00 60.26  ? 158  ASP F N   1 
ATOM   11543 C CA  . ASP F  2 158 ? 26.103  69.593 -6.510  1.00 64.34  ? 158  ASP F CA  1 
ATOM   11544 C C   . ASP F  2 158 ? 26.406  68.387 -7.401  1.00 63.16  ? 158  ASP F C   1 
ATOM   11545 O O   . ASP F  2 158 ? 26.996  68.522 -8.480  1.00 63.80  ? 158  ASP F O   1 
ATOM   11546 C CB  . ASP F  2 158 ? 25.923  70.857 -7.356  1.00 68.63  ? 158  ASP F CB  1 
ATOM   11547 C CG  . ASP F  2 158 ? 24.593  70.884 -8.077  1.00 73.76  ? 158  ASP F CG  1 
ATOM   11548 O OD1 . ASP F  2 158 ? 23.548  70.817 -7.392  1.00 75.78  ? 158  ASP F OD1 1 
ATOM   11549 O OD2 . ASP F  2 158 ? 24.588  70.973 -9.323  1.00 76.11  ? 158  ASP F OD2 1 
ATOM   11550 N N   . TYR F  2 159 ? 25.984  67.212 -6.934  1.00 61.96  ? 159  TYR F N   1 
ATOM   11551 C CA  . TYR F  2 159 ? 26.208  65.950 -7.644  1.00 61.13  ? 159  TYR F CA  1 
ATOM   11552 C C   . TYR F  2 159 ? 25.749  66.003 -9.114  1.00 65.26  ? 159  TYR F C   1 
ATOM   11553 O O   . TYR F  2 159 ? 26.540  65.685 -10.006 1.00 64.61  ? 159  TYR F O   1 
ATOM   11554 C CB  . TYR F  2 159 ? 25.560  64.777 -6.877  1.00 60.32  ? 159  TYR F CB  1 
ATOM   11555 C CG  . TYR F  2 159 ? 25.524  63.468 -7.637  1.00 60.75  ? 159  TYR F CG  1 
ATOM   11556 C CD1 . TYR F  2 159 ? 24.471  63.167 -8.503  1.00 65.20  ? 159  TYR F CD1 1 
ATOM   11557 C CD2 . TYR F  2 159 ? 26.541  62.530 -7.489  1.00 57.26  ? 159  TYR F CD2 1 
ATOM   11558 C CE1 . TYR F  2 159 ? 24.439  61.973 -9.204  1.00 66.19  ? 159  TYR F CE1 1 
ATOM   11559 C CE2 . TYR F  2 159 ? 26.516  61.333 -8.180  1.00 58.27  ? 159  TYR F CE2 1 
ATOM   11560 C CZ  . TYR F  2 159 ? 25.462  61.059 -9.036  1.00 62.80  ? 159  TYR F CZ  1 
ATOM   11561 O OH  . TYR F  2 159 ? 25.422  59.872 -9.731  1.00 64.48  ? 159  TYR F OH  1 
ATOM   11562 N N   . PRO F  2 160 ? 24.488  66.421 -9.375  1.00 70.05  ? 160  PRO F N   1 
ATOM   11563 C CA  . PRO F  2 160 ? 23.995  66.497 -10.763 1.00 74.46  ? 160  PRO F CA  1 
ATOM   11564 C C   . PRO F  2 160 ? 24.818  67.347 -11.748 1.00 75.04  ? 160  PRO F C   1 
ATOM   11565 O O   . PRO F  2 160 ? 24.745  67.107 -12.958 1.00 77.58  ? 160  PRO F O   1 
ATOM   11566 C CB  . PRO F  2 160 ? 22.591  67.093 -10.601 1.00 79.47  ? 160  PRO F CB  1 
ATOM   11567 C CG  . PRO F  2 160 ? 22.159  66.654 -9.249  1.00 77.78  ? 160  PRO F CG  1 
ATOM   11568 C CD  . PRO F  2 160 ? 23.404  66.690 -8.406  1.00 71.96  ? 160  PRO F CD  1 
ATOM   11569 N N   . GLN F  2 161 ? 25.565  68.334 -11.252 1.00 73.41  ? 161  GLN F N   1 
ATOM   11570 C CA  . GLN F  2 161 ? 26.404  69.178 -12.120 1.00 74.26  ? 161  GLN F CA  1 
ATOM   11571 C C   . GLN F  2 161 ? 27.637  68.423 -12.619 1.00 71.02  ? 161  GLN F C   1 
ATOM   11572 O O   . GLN F  2 161 ? 27.985  68.500 -13.801 1.00 72.59  ? 161  GLN F O   1 
ATOM   11573 C CB  . GLN F  2 161 ? 26.844  70.454 -11.388 1.00 73.96  ? 161  GLN F CB  1 
ATOM   11574 C CG  . GLN F  2 161 ? 27.806  71.347 -12.168 1.00 74.68  ? 161  GLN F CG  1 
ATOM   11575 C CD  . GLN F  2 161 ? 28.313  72.524 -11.350 1.00 74.55  ? 161  GLN F CD  1 
ATOM   11576 O OE1 . GLN F  2 161 ? 28.436  72.442 -10.126 1.00 71.91  ? 161  GLN F OE1 1 
ATOM   11577 N NE2 . GLN F  2 161 ? 28.617  73.626 -12.028 1.00 77.69  ? 161  GLN F NE2 1 
ATOM   11578 N N   . TYR F  2 162 ? 28.292  67.705 -11.710 1.00 66.87  ? 162  TYR F N   1 
ATOM   11579 C CA  . TYR F  2 162 ? 29.517  66.976 -12.034 1.00 64.11  ? 162  TYR F CA  1 
ATOM   11580 C C   . TYR F  2 162 ? 29.252  65.537 -12.504 1.00 64.39  ? 162  TYR F C   1 
ATOM   11581 O O   . TYR F  2 162 ? 30.188  64.752 -12.667 1.00 62.43  ? 162  TYR F O   1 
ATOM   11582 C CB  . TYR F  2 162 ? 30.453  66.977 -10.822 1.00 60.03  ? 162  TYR F CB  1 
ATOM   11583 C CG  . TYR F  2 162 ? 30.825  68.366 -10.332 1.00 60.29  ? 162  TYR F CG  1 
ATOM   11584 C CD1 . TYR F  2 162 ? 31.759  69.145 -11.019 1.00 61.09  ? 162  TYR F CD1 1 
ATOM   11585 C CD2 . TYR F  2 162 ? 30.244  68.900 -9.180  1.00 60.16  ? 162  TYR F CD2 1 
ATOM   11586 C CE1 . TYR F  2 162 ? 32.104  70.412 -10.571 1.00 62.00  ? 162  TYR F CE1 1 
ATOM   11587 C CE2 . TYR F  2 162 ? 30.582  70.166 -8.724  1.00 60.93  ? 162  TYR F CE2 1 
ATOM   11588 C CZ  . TYR F  2 162 ? 31.512  70.918 -9.421  1.00 61.98  ? 162  TYR F CZ  1 
ATOM   11589 O OH  . TYR F  2 162 ? 31.847  72.175 -8.970  1.00 63.44  ? 162  TYR F OH  1 
ATOM   11590 N N   . SER F  2 163 ? 27.981  65.198 -12.718 1.00 67.65  ? 163  SER F N   1 
ATOM   11591 C CA  . SER F  2 163 ? 27.594  63.893 -13.257 1.00 69.05  ? 163  SER F CA  1 
ATOM   11592 C C   . SER F  2 163 ? 27.331  64.010 -14.751 1.00 72.86  ? 163  SER F C   1 
ATOM   11593 O O   . SER F  2 163 ? 26.724  63.131 -15.351 1.00 75.54  ? 163  SER F O   1 
ATOM   11594 C CB  . SER F  2 163 ? 26.355  63.371 -12.527 1.00 70.60  ? 163  SER F CB  1 
ATOM   11595 O OG  . SER F  2 163 ? 26.034  62.028 -12.868 1.00 72.03  ? 163  SER F OG  1 
HETATM 11596 C C1  . NAG G  3 .   ? 17.269  71.026 31.942  1.00 22.84  ? 1023 NAG A C1  1 
HETATM 11597 C C2  . NAG G  3 .   ? 18.093  72.263 32.349  1.00 26.41  ? 1023 NAG A C2  1 
HETATM 11598 C C3  . NAG G  3 .   ? 17.703  72.860 33.711  1.00 27.41  ? 1023 NAG A C3  1 
HETATM 11599 C C4  . NAG G  3 .   ? 16.182  72.963 33.805  1.00 27.30  ? 1023 NAG A C4  1 
HETATM 11600 C C5  . NAG G  3 .   ? 15.664  71.531 33.703  1.00 26.74  ? 1023 NAG A C5  1 
HETATM 11601 C C6  . NAG G  3 .   ? 14.181  71.349 34.068  1.00 27.20  ? 1023 NAG A C6  1 
HETATM 11602 C C7  . NAG G  3 .   ? 20.259  72.095 31.192  1.00 27.79  ? 1023 NAG A C7  1 
HETATM 11603 C C8  . NAG G  3 .   ? 21.734  71.806 31.290  1.00 27.32  ? 1023 NAG A C8  1 
HETATM 11604 N N2  . NAG G  3 .   ? 19.532  71.997 32.315  1.00 27.22  ? 1023 NAG A N2  1 
HETATM 11605 O O3  . NAG G  3 .   ? 18.307  74.127 33.897  1.00 28.36  ? 1023 NAG A O3  1 
HETATM 11606 O O4  . NAG G  3 .   ? 15.788  73.612 34.999  1.00 28.37  ? 1023 NAG A O4  1 
HETATM 11607 O O5  . NAG G  3 .   ? 15.913  71.114 32.372  1.00 24.55  ? 1023 NAG A O5  1 
HETATM 11608 O O6  . NAG G  3 .   ? 13.340  71.615 32.963  1.00 28.07  ? 1023 NAG A O6  1 
HETATM 11609 O O7  . NAG G  3 .   ? 19.776  72.403 30.097  1.00 28.41  ? 1023 NAG A O7  1 
HETATM 11610 C C1  . NAG H  3 .   ? 9.463   27.474 89.454  1.00 26.03  ? 1165 NAG A C1  1 
HETATM 11611 C C2  . NAG H  3 .   ? 9.084   26.242 88.612  1.00 28.76  ? 1165 NAG A C2  1 
HETATM 11612 C C3  . NAG H  3 .   ? 10.068  25.092 88.894  1.00 29.09  ? 1165 NAG A C3  1 
HETATM 11613 C C4  . NAG H  3 .   ? 11.489  25.607 88.642  1.00 29.34  ? 1165 NAG A C4  1 
HETATM 11614 C C5  . NAG H  3 .   ? 11.738  26.814 89.556  1.00 29.26  ? 1165 NAG A C5  1 
HETATM 11615 C C6  . NAG H  3 .   ? 13.170  27.353 89.496  1.00 29.46  ? 1165 NAG A C6  1 
HETATM 11616 C C7  . NAG H  3 .   ? 7.036   25.537 89.867  1.00 33.14  ? 1165 NAG A C7  1 
HETATM 11617 C C8  . NAG H  3 .   ? 5.564   25.218 89.758  1.00 33.29  ? 1165 NAG A C8  1 
HETATM 11618 N N2  . NAG H  3 .   ? 7.666   25.889 88.730  1.00 30.57  ? 1165 NAG A N2  1 
HETATM 11619 O O3  . NAG H  3 .   ? 9.832   23.949 88.098  1.00 29.73  ? 1165 NAG A O3  1 
HETATM 11620 O O4  . NAG H  3 .   ? 12.454  24.585 88.804  1.00 29.85  ? 1165 NAG A O4  1 
HETATM 11621 O O5  . NAG H  3 .   ? 10.812  27.825 89.186  1.00 27.55  ? 1165 NAG A O5  1 
HETATM 11622 O O6  . NAG H  3 .   ? 13.239  28.582 90.193  1.00 30.13  ? 1165 NAG A O6  1 
HETATM 11623 O O7  . NAG H  3 .   ? 7.582   25.453 90.975  1.00 34.85  ? 1165 NAG A O7  1 
HETATM 11624 C C1  . SIA I  4 .   ? 5.067   65.290 96.500  1.00 47.47  ? 1322 SIA A C1  1 
HETATM 11625 C C2  . SIA I  4 .   ? 5.473   65.530 97.943  1.00 46.44  ? 1322 SIA A C2  1 
HETATM 11626 C C3  . SIA I  4 .   ? 4.292   65.129 98.831  1.00 45.03  ? 1322 SIA A C3  1 
HETATM 11627 C C4  . SIA I  4 .   ? 4.047   63.629 98.727  1.00 43.99  ? 1322 SIA A C4  1 
HETATM 11628 C C5  . SIA I  4 .   ? 5.330   62.879 99.077  1.00 42.77  ? 1322 SIA A C5  1 
HETATM 11629 C C6  . SIA I  4 .   ? 6.508   63.346 98.214  1.00 41.81  ? 1322 SIA A C6  1 
HETATM 11630 C C7  . SIA I  4 .   ? 7.854   62.712 98.580  1.00 40.24  ? 1322 SIA A C7  1 
HETATM 11631 C C8  . SIA I  4 .   ? 9.048   63.343 97.848  1.00 39.37  ? 1322 SIA A C8  1 
HETATM 11632 C C9  . SIA I  4 .   ? 10.245  62.394 97.873  1.00 38.33  ? 1322 SIA A C9  1 
HETATM 11633 C C10 . SIA I  4 .   ? 5.598   60.476 99.417  1.00 41.76  ? 1322 SIA A C10 1 
HETATM 11634 C C11 . SIA I  4 .   ? 5.185   59.100 98.985  1.00 41.45  ? 1322 SIA A C11 1 
HETATM 11635 N N5  . SIA I  4 .   ? 5.034   61.485 98.762  1.00 41.87  ? 1322 SIA A N5  1 
HETATM 11636 O O1A . SIA I  4 .   ? 5.906   64.844 95.684  1.00 49.43  ? 1322 SIA A O1A 1 
HETATM 11637 O O1B . SIA I  4 .   ? 3.889   65.548 96.159  1.00 48.42  ? 1322 SIA A O1B 1 
HETATM 11638 O O4  . SIA I  4 .   ? 2.988   63.241 99.611  1.00 44.50  ? 1322 SIA A O4  1 
HETATM 11639 O O6  . SIA I  4 .   ? 6.634   64.772 98.313  1.00 43.56  ? 1322 SIA A O6  1 
HETATM 11640 O O7  . SIA I  4 .   ? 8.067   62.819 99.990  1.00 39.07  ? 1322 SIA A O7  1 
HETATM 11641 O O8  . SIA I  4 .   ? 8.731   63.647 96.479  1.00 38.88  ? 1322 SIA A O8  1 
HETATM 11642 O O9  . SIA I  4 .   ? 11.460  63.100 97.582  1.00 38.27  ? 1322 SIA A O9  1 
HETATM 11643 O O10 . SIA I  4 .   ? 6.411   60.657 100.306 1.00 40.82  ? 1322 SIA A O10 1 
HETATM 11644 C C1  . GLA J  5 .   ? 6.164   69.816 100.350 1.00 60.28  ? 1323 GLA A C1  1 
HETATM 11645 C C2  . GLA J  5 .   ? 5.473   68.786 99.457  1.00 57.37  ? 1323 GLA A C2  1 
HETATM 11646 C C3  . GLA J  5 .   ? 6.221   67.455 99.302  1.00 54.72  ? 1323 GLA A C3  1 
HETATM 11647 C C4  . GLA J  5 .   ? 7.751   67.559 99.306  1.00 55.47  ? 1323 GLA A C4  1 
HETATM 11648 C C5  . GLA J  5 .   ? 8.271   68.689 100.210 1.00 55.98  ? 1323 GLA A C5  1 
HETATM 11649 C C6  . GLA J  5 .   ? 9.769   68.970 100.045 1.00 54.37  ? 1323 GLA A C6  1 
HETATM 11650 O O2  . GLA J  5 .   ? 4.149   68.541 99.951  1.00 57.01  ? 1323 GLA A O2  1 
HETATM 11651 O O3  . GLA J  5 .   ? 5.786   66.925 98.042  1.00 50.23  ? 1323 GLA A O3  1 
HETATM 11652 O O4  . GLA J  5 .   ? 8.197   67.726 97.951  1.00 54.23  ? 1323 GLA A O4  1 
HETATM 11653 O O5  . GLA J  5 .   ? 7.539   69.894 99.954  1.00 58.58  ? 1323 GLA A O5  1 
HETATM 11654 O O6  . GLA J  5 .   ? 10.535  67.964 100.712 1.00 52.07  ? 1323 GLA A O6  1 
HETATM 11655 C C1  . NGS K  6 .   ? 4.706   72.844 104.048 1.00 74.01  ? 1324 NGS A C1  1 
HETATM 11656 C C2  . NGS K  6 .   ? 6.120   72.961 103.461 1.00 72.49  ? 1324 NGS A C2  1 
HETATM 11657 C C3  . NGS K  6 .   ? 6.310   72.026 102.253 1.00 71.07  ? 1324 NGS A C3  1 
HETATM 11658 C C4  . NGS K  6 .   ? 5.903   70.607 102.699 1.00 70.33  ? 1324 NGS A C4  1 
HETATM 11659 C C5  . NGS K  6 .   ? 4.436   70.663 103.144 1.00 73.71  ? 1324 NGS A C5  1 
HETATM 11660 C C6  . NGS K  6 .   ? 3.817   69.301 103.457 1.00 75.15  ? 1324 NGS A C6  1 
HETATM 11661 O O1  . NGS K  6 .   ? 4.615   73.593 105.268 1.00 73.91  ? 1324 NGS A O1  1 
HETATM 11662 O O3  . NGS K  6 .   ? 7.651   72.066 101.713 1.00 70.63  ? 1324 NGS A O3  1 
HETATM 11663 O O5  . NGS K  6 .   ? 4.364   71.480 104.313 1.00 75.03  ? 1324 NGS A O5  1 
HETATM 11664 O O6  . NGS K  6 .   ? 4.733   68.525 104.229 1.00 78.15  ? 1324 NGS A O6  1 
HETATM 11665 N N   . NGS K  6 .   ? 6.183   74.356 103.019 1.00 72.44  ? 1324 NGS A N   1 
HETATM 11666 C C   . NGS K  6 .   ? 7.125   75.227 103.396 1.00 71.10  ? 1324 NGS A C   1 
HETATM 11667 O O   . NGS K  6 .   ? 8.047   74.926 104.140 1.00 71.02  ? 1324 NGS A O   1 
HETATM 11668 C CH3 . NGS K  6 .   ? 6.995   76.609 102.817 1.00 69.48  ? 1324 NGS A CH3 1 
HETATM 11669 S S   . NGS K  6 .   ? 5.099   67.067 103.893 1.00 82.02  ? 1324 NGS A S   1 
HETATM 11670 O O7  . NGS K  6 .   ? 6.569   66.924 104.010 1.00 79.28  ? 1324 NGS A O7  1 
HETATM 11671 O O8  . NGS K  6 .   ? 4.434   66.161 104.860 1.00 81.97  ? 1324 NGS A O8  1 
HETATM 11672 O O9  . NGS K  6 .   ? 4.676   66.697 102.520 1.00 81.74  ? 1324 NGS A O9  1 
HETATM 11673 O O4  . NGS K  6 .   ? 6.069   69.524 101.753 1.00 66.06  ? 1324 NGS A O4  1 
HETATM 11674 C C1  . FUC L  7 .   ? 8.049   73.287 101.044 1.00 70.75  ? 1325 FUC A C1  1 
HETATM 11675 C C2  . FUC L  7 .   ? 9.340   73.153 100.228 1.00 70.08  ? 1325 FUC A C2  1 
HETATM 11676 C C3  . FUC L  7 .   ? 9.163   72.543 98.835  1.00 69.85  ? 1325 FUC A C3  1 
HETATM 11677 C C4  . FUC L  7 .   ? 7.886   72.971 98.106  1.00 70.95  ? 1325 FUC A C4  1 
HETATM 11678 C C5  . FUC L  7 .   ? 6.692   73.050 99.056  1.00 71.37  ? 1325 FUC A C5  1 
HETATM 11679 C C6  . FUC L  7 .   ? 5.430   73.596 98.388  1.00 70.67  ? 1325 FUC A C6  1 
HETATM 11680 O O2  . FUC L  7 .   ? 10.292  72.380 100.972 1.00 70.00  ? 1325 FUC A O2  1 
HETATM 11681 O O3  . FUC L  7 .   ? 10.295  72.940 98.056  1.00 66.87  ? 1325 FUC A O3  1 
HETATM 11682 O O4  . FUC L  7 .   ? 8.086   74.239 97.465  1.00 72.00  ? 1325 FUC A O4  1 
HETATM 11683 O O5  . FUC L  7 .   ? 7.014   73.834 100.210 1.00 71.18  ? 1325 FUC A O5  1 
HETATM 11684 C C1  . NAG M  3 .   ? 6.992   38.561 -0.108  1.00 34.72  ? 1154 NAG B C1  1 
HETATM 11685 C C2  . NAG M  3 .   ? 6.873   37.027 -0.138  1.00 38.28  ? 1154 NAG B C2  1 
HETATM 11686 C C3  . NAG M  3 .   ? 6.795   36.424 -1.537  1.00 39.61  ? 1154 NAG B C3  1 
HETATM 11687 C C4  . NAG M  3 .   ? 5.756   37.172 -2.357  1.00 40.34  ? 1154 NAG B C4  1 
HETATM 11688 C C5  . NAG M  3 .   ? 6.183   38.639 -2.435  1.00 40.36  ? 1154 NAG B C5  1 
HETATM 11689 C C6  . NAG M  3 .   ? 5.189   39.445 -3.273  1.00 41.24  ? 1154 NAG B C6  1 
HETATM 11690 C C7  . NAG M  3 .   ? 7.930   36.307 1.942   1.00 38.55  ? 1154 NAG B C7  1 
HETATM 11691 C C8  . NAG M  3 .   ? 9.094   35.637 2.621   1.00 38.37  ? 1154 NAG B C8  1 
HETATM 11692 N N2  . NAG M  3 .   ? 7.954   36.395 0.609   1.00 38.28  ? 1154 NAG B N2  1 
HETATM 11693 O O3  . NAG M  3 .   ? 6.431   35.066 -1.421  1.00 40.83  ? 1154 NAG B O3  1 
HETATM 11694 O O4  . NAG M  3 .   ? 5.629   36.587 -3.642  1.00 40.48  ? 1154 NAG B O4  1 
HETATM 11695 O O5  . NAG M  3 .   ? 6.267   39.228 -1.141  1.00 37.68  ? 1154 NAG B O5  1 
HETATM 11696 O O6  . NAG M  3 .   ? 5.487   40.822 -3.175  1.00 42.42  ? 1154 NAG B O6  1 
HETATM 11697 O O7  . NAG M  3 .   ? 7.005   36.754 2.620   1.00 38.74  ? 1154 NAG B O7  1 
HETATM 11698 N N1  . EPE N  8 .   ? 12.401  61.974 3.462   1.00 41.90  ? 1164 EPE B N1  1 
HETATM 11699 C C2  . EPE N  8 .   ? 12.777  62.208 2.075   1.00 42.22  ? 1164 EPE B C2  1 
HETATM 11700 C C3  . EPE N  8 .   ? 14.162  62.843 2.100   1.00 41.75  ? 1164 EPE B C3  1 
HETATM 11701 N N4  . EPE N  8 .   ? 14.056  64.032 2.932   1.00 41.42  ? 1164 EPE B N4  1 
HETATM 11702 C C5  . EPE N  8 .   ? 13.664  63.877 4.332   1.00 41.94  ? 1164 EPE B C5  1 
HETATM 11703 C C6  . EPE N  8 .   ? 12.339  63.105 4.387   1.00 42.11  ? 1164 EPE B C6  1 
HETATM 11704 C C7  . EPE N  8 .   ? 14.339  65.346 2.354   1.00 40.93  ? 1164 EPE B C7  1 
HETATM 11705 C C8  . EPE N  8 .   ? 15.815  65.380 1.944   1.00 40.43  ? 1164 EPE B C8  1 
HETATM 11706 O O8  . EPE N  8 .   ? 15.933  65.327 0.512   1.00 39.92  ? 1164 EPE B O8  1 
HETATM 11707 C C9  . EPE N  8 .   ? 12.082  60.620 3.895   1.00 43.53  ? 1164 EPE B C9  1 
HETATM 11708 C C10 . EPE N  8 .   ? 10.769  60.198 3.227   1.00 46.55  ? 1164 EPE B C10 1 
HETATM 11709 S S   . EPE N  8 .   ? 9.410   60.919 3.882   1.00 52.01  ? 1164 EPE B S   1 
HETATM 11710 O O1S . EPE N  8 .   ? 9.713   61.644 5.145   1.00 52.72  ? 1164 EPE B O1S 1 
HETATM 11711 O O2S . EPE N  8 .   ? 8.409   59.862 4.166   1.00 51.26  ? 1164 EPE B O2S 1 
HETATM 11712 O O3S . EPE N  8 .   ? 8.819   61.876 2.909   1.00 52.62  ? 1164 EPE B O3S 1 
HETATM 11713 C C1  . NAG O  3 .   ? 18.464  31.178 31.921  1.00 24.47  ? 1023 NAG C C1  1 
HETATM 11714 C C2  . NAG O  3 .   ? 16.976  31.164 32.311  1.00 28.15  ? 1023 NAG C C2  1 
HETATM 11715 C C3  . NAG O  3 .   ? 16.710  30.475 33.663  1.00 28.98  ? 1023 NAG C C3  1 
HETATM 11716 C C4  . NAG O  3 .   ? 17.446  29.146 33.764  1.00 29.06  ? 1023 NAG C C4  1 
HETATM 11717 C C5  . NAG O  3 .   ? 18.921  29.456 33.558  1.00 28.49  ? 1023 NAG C C5  1 
HETATM 11718 C C6  . NAG O  3 .   ? 19.845  28.259 33.827  1.00 29.12  ? 1023 NAG C C6  1 
HETATM 11719 C C7  . NAG O  3 .   ? 16.029  33.162 31.228  1.00 29.68  ? 1023 NAG C C7  1 
HETATM 11720 C C8  . NAG O  3 .   ? 15.491  34.558 31.383  1.00 29.15  ? 1023 NAG C C8  1 
HETATM 11721 N N2  . NAG O  3 .   ? 16.439  32.526 32.335  1.00 29.21  ? 1023 NAG C N2  1 
HETATM 11722 O O3  . NAG O  3 .   ? 15.328  30.258 33.870  1.00 29.77  ? 1023 NAG C O3  1 
HETATM 11723 O O4  . NAG O  3 .   ? 17.194  28.541 35.019  1.00 30.55  ? 1023 NAG C O4  1 
HETATM 11724 O O5  . NAG O  3 .   ? 19.045  29.910 32.221  1.00 26.34  ? 1023 NAG C O5  1 
HETATM 11725 O O6  . NAG O  3 .   ? 19.672  27.242 32.859  1.00 29.89  ? 1023 NAG C O6  1 
HETATM 11726 O O7  . NAG O  3 .   ? 16.073  32.656 30.103  1.00 30.44  ? 1023 NAG C O7  1 
HETATM 11727 C C1  . NAG P  3 .   ? 60.062  46.356 89.472  1.00 23.43  ? 1165 NAG C C1  1 
HETATM 11728 C C2  . NAG P  3 .   ? 61.331  46.660 88.651  1.00 25.85  ? 1165 NAG C C2  1 
HETATM 11729 C C3  . NAG P  3 .   ? 61.850  48.064 88.992  1.00 26.11  ? 1165 NAG C C3  1 
HETATM 11730 C C4  . NAG P  3 .   ? 60.717  49.044 88.690  1.00 26.43  ? 1165 NAG C C4  1 
HETATM 11731 C C5  . NAG P  3 .   ? 59.512  48.675 89.563  1.00 26.22  ? 1165 NAG C C5  1 
HETATM 11732 C C6  . NAG P  3 .   ? 58.347  49.666 89.438  1.00 26.38  ? 1165 NAG C C6  1 
HETATM 11733 C C7  . NAG P  3 .   ? 62.912  45.093 89.817  1.00 29.17  ? 1165 NAG C C7  1 
HETATM 11734 C C8  . NAG P  3 .   ? 63.938  44.002 89.628  1.00 29.26  ? 1165 NAG C C8  1 
HETATM 11735 N N2  . NAG P  3 .   ? 62.349  45.601 88.703  1.00 27.20  ? 1165 NAG C N2  1 
HETATM 11736 O O3  . NAG P  3 .   ? 62.990  48.443 88.248  1.00 26.72  ? 1165 NAG C O3  1 
HETATM 11737 O O4  . NAG P  3 .   ? 61.130  50.386 88.855  1.00 27.24  ? 1165 NAG C O4  1 
HETATM 11738 O O5  . NAG P  3 .   ? 59.096  47.365 89.200  1.00 24.69  ? 1165 NAG C O5  1 
HETATM 11739 O O6  . NAG P  3 .   ? 57.348  49.351 90.387  1.00 26.86  ? 1165 NAG C O6  1 
HETATM 11740 O O7  . NAG P  3 .   ? 62.650  45.458 90.970  1.00 30.54  ? 1165 NAG C O7  1 
HETATM 11741 C C1  . SIA Q  4 .   ? 29.463  23.502 96.513  1.00 47.77  ? 1322 SIA C C1  1 
HETATM 11742 C C2  . SIA Q  4 .   ? 29.104  23.734 97.969  1.00 47.10  ? 1322 SIA C C2  1 
HETATM 11743 C C3  . SIA Q  4 .   ? 30.067  22.923 98.841  1.00 45.68  ? 1322 SIA C C3  1 
HETATM 11744 C C4  . SIA Q  4 .   ? 31.482  23.478 98.713  1.00 44.55  ? 1322 SIA C C4  1 
HETATM 11745 C C5  . SIA Q  4 .   ? 31.478  24.955 99.097  1.00 43.39  ? 1322 SIA C C5  1 
HETATM 11746 C C6  . SIA Q  4 .   ? 30.485  25.729 98.223  1.00 42.98  ? 1322 SIA C C6  1 
HETATM 11747 C C7  . SIA Q  4 .   ? 30.367  27.223 98.546  1.00 41.95  ? 1322 SIA C C7  1 
HETATM 11748 C C8  . SIA Q  4 .   ? 29.222  27.912 97.792  1.00 41.97  ? 1322 SIA C C8  1 
HETATM 11749 C C9  . SIA Q  4 .   ? 29.374  29.433 97.843  1.00 41.33  ? 1322 SIA C C9  1 
HETATM 11750 C C10 . SIA Q  4 .   ? 33.390  26.447 99.395  1.00 42.06  ? 1322 SIA C C10 1 
HETATM 11751 C C11 . SIA Q  4 .   ? 34.787  26.776 98.960  1.00 41.79  ? 1322 SIA C C11 1 
HETATM 11752 N N5  . SIA Q  4 .   ? 32.826  25.410 98.788  1.00 42.47  ? 1322 SIA C N5  1 
HETATM 11753 O O1A . SIA Q  4 .   ? 29.502  24.471 95.718  1.00 48.78  ? 1322 SIA C O1A 1 
HETATM 11754 O O1B . SIA Q  4 .   ? 29.710  22.331 96.139  1.00 49.05  ? 1322 SIA C O1B 1 
HETATM 11755 O O4  . SIA Q  4 .   ? 32.395  22.741 99.536  1.00 44.69  ? 1322 SIA C O4  1 
HETATM 11756 O O6  . SIA Q  4 .   ? 29.184  25.125 98.327  1.00 44.73  ? 1322 SIA C O6  1 
HETATM 11757 O O7  . SIA Q  4 .   ? 30.183  27.404 99.953  1.00 40.82  ? 1322 SIA C O7  1 
HETATM 11758 O O8  . SIA Q  4 .   ? 29.194  27.495 96.417  1.00 42.42  ? 1322 SIA C O8  1 
HETATM 11759 O O9  . SIA Q  4 .   ? 28.159  30.078 97.438  1.00 40.38  ? 1322 SIA C O9  1 
HETATM 11760 O O10 . SIA Q  4 .   ? 32.805  27.094 100.242 1.00 41.18  ? 1322 SIA C O10 1 
HETATM 11761 C C1  . GLA R  5 .   ? 24.971  22.414 100.458 1.00 59.22  ? 1323 GLA C C1  1 
HETATM 11762 C C2  . GLA R  5 .   ? 26.150  22.242 99.493  1.00 56.78  ? 1323 GLA C C2  1 
HETATM 11763 C C3  . GLA R  5 .   ? 27.038  23.479 99.315  1.00 54.69  ? 1323 GLA C C3  1 
HETATM 11764 C C4  . GLA R  5 .   ? 26.244  24.780 99.216  1.00 55.19  ? 1323 GLA C C4  1 
HETATM 11765 C C5  . GLA R  5 .   ? 25.171  24.878 100.306 1.00 55.38  ? 1323 GLA C C5  1 
HETATM 11766 C C6  . GLA R  5 .   ? 24.248  26.086 100.093 1.00 54.12  ? 1323 GLA C C6  1 
HETATM 11767 O O2  . GLA R  5 .   ? 26.950  21.129 99.922  1.00 56.26  ? 1323 GLA C O2  1 
HETATM 11768 O O3  . GLA R  5 .   ? 27.756  23.261 98.095  1.00 50.70  ? 1323 GLA C O3  1 
HETATM 11769 O O4  . GLA R  5 .   ? 25.670  24.867 97.902  1.00 53.70  ? 1323 GLA C O4  1 
HETATM 11770 O O5  . GLA R  5 .   ? 24.353  23.704 100.340 1.00 57.69  ? 1323 GLA C O5  1 
HETATM 11771 O O6  . GLA R  5 .   ? 24.453  27.069 101.111 1.00 51.83  ? 1323 GLA C O6  1 
HETATM 11772 C C1  . NGS S  6 .   ? 23.269  19.082 103.841 1.00 73.54  ? 1324 NGS C C1  1 
HETATM 11773 C C2  . NGS S  6 .   ? 22.411  20.255 103.347 1.00 71.54  ? 1324 NGS C C2  1 
HETATM 11774 C C3  . NGS S  6 .   ? 23.120  20.966 102.182 1.00 69.68  ? 1324 NGS C C3  1 
HETATM 11775 C C4  . NGS S  6 .   ? 24.491  21.435 102.710 1.00 69.30  ? 1324 NGS C C4  1 
HETATM 11776 C C5  . NGS S  6 .   ? 25.270  20.193 103.171 1.00 72.97  ? 1324 NGS C C5  1 
HETATM 11777 C C6  . NGS S  6 .   ? 26.696  20.486 103.642 1.00 74.59  ? 1324 NGS C C6  1 
HETATM 11778 O O1  . NGS S  6 .   ? 22.641  18.413 104.947 1.00 72.99  ? 1324 NGS C O1  1 
HETATM 11779 O O3  . NGS S  6 .   ? 22.334  22.045 101.649 1.00 67.89  ? 1324 NGS C O3  1 
HETATM 11780 O O5  . NGS S  6 .   ? 24.559  19.560 104.239 1.00 74.63  ? 1324 NGS C O5  1 
HETATM 11781 O O6  . NGS S  6 .   ? 26.764  21.774 104.259 1.00 77.23  ? 1324 NGS C O6  1 
HETATM 11782 N N   . NGS S  6 .   ? 21.158  19.649 102.888 1.00 70.99  ? 1324 NGS C N   1 
HETATM 11783 C C   . NGS S  6 .   ? 19.936  20.091 103.217 1.00 68.87  ? 1324 NGS C C   1 
HETATM 11784 O O   . NGS S  6 .   ? 19.746  21.066 103.933 1.00 67.28  ? 1324 NGS C O   1 
HETATM 11785 C CH3 . NGS S  6 .   ? 18.792  19.315 102.628 1.00 67.51  ? 1324 NGS C CH3 1 
HETATM 11786 S S   . NGS S  6 .   ? 27.865  22.795 103.919 1.00 79.34  ? 1324 NGS C S   1 
HETATM 11787 O O7  . NGS S  6 .   ? 27.337  24.148 104.215 1.00 76.24  ? 1324 NGS C O7  1 
HETATM 11788 O O8  . NGS S  6 .   ? 29.064  22.525 104.749 1.00 79.35  ? 1324 NGS C O8  1 
HETATM 11789 O O9  . NGS S  6 .   ? 28.241  22.710 102.488 1.00 78.11  ? 1324 NGS C O9  1 
HETATM 11790 O O4  . NGS S  6 .   ? 25.343  22.201 101.826 1.00 65.08  ? 1324 NGS C O4  1 
HETATM 11791 C C1  . FUC T  7 .   ? 21.389  21.662 100.630 1.00 67.16  ? 1325 FUC C C1  1 
HETATM 11792 C C2  . FUC T  7 .   ? 20.181  22.601 100.683 1.00 67.34  ? 1325 FUC C C2  1 
HETATM 11793 C C3  . FUC T  7 .   ? 20.538  23.959 100.096 1.00 67.06  ? 1325 FUC C C3  1 
HETATM 11794 C C4  . FUC T  7 .   ? 20.962  23.770 98.646  1.00 66.55  ? 1325 FUC C C4  1 
HETATM 11795 C C5  . FUC T  7 .   ? 22.186  22.853 98.607  1.00 66.48  ? 1325 FUC C C5  1 
HETATM 11796 C C6  . FUC T  7 .   ? 22.639  22.537 97.182  1.00 65.67  ? 1325 FUC C C6  1 
HETATM 11797 O O2  . FUC T  7 .   ? 19.725  22.774 102.031 1.00 68.31  ? 1325 FUC C O2  1 
HETATM 11798 O O3  . FUC T  7 .   ? 19.427  24.858 100.188 1.00 67.75  ? 1325 FUC C O3  1 
HETATM 11799 O O4  . FUC T  7 .   ? 19.878  23.227 97.878  1.00 63.97  ? 1325 FUC C O4  1 
HETATM 11800 O O5  . FUC T  7 .   ? 21.972  21.618 99.314  1.00 66.68  ? 1325 FUC C O5  1 
HETATM 11801 C C1  . NAG U  3 .   ? 51.693  38.590 -0.110  1.00 33.80  ? 1154 NAG D C1  1 
HETATM 11802 C C2  . NAG U  3 .   ? 53.139  39.104 -0.124  1.00 37.69  ? 1154 NAG D C2  1 
HETATM 11803 C C3  . NAG U  3 .   ? 53.813  39.143 -1.497  1.00 39.37  ? 1154 NAG D C3  1 
HETATM 11804 C C4  . NAG U  3 .   ? 53.482  37.904 -2.323  1.00 40.01  ? 1154 NAG D C4  1 
HETATM 11805 C C5  . NAG U  3 .   ? 51.966  37.703 -2.377  1.00 39.63  ? 1154 NAG D C5  1 
HETATM 11806 C C6  . NAG U  3 .   ? 51.620  36.429 -3.157  1.00 40.18  ? 1154 NAG D C6  1 
HETATM 11807 C C7  . NAG U  3 .   ? 53.238  40.548 1.847   1.00 38.01  ? 1154 NAG D C7  1 
HETATM 11808 C C8  . NAG U  3 .   ? 53.309  41.947 2.396   1.00 38.16  ? 1154 NAG D C8  1 
HETATM 11809 N N2  . NAG U  3 .   ? 53.206  40.413 0.515   1.00 37.65  ? 1154 NAG D N2  1 
HETATM 11810 O O3  . NAG U  3 .   ? 55.212  39.204 -1.306  1.00 40.26  ? 1154 NAG D O3  1 
HETATM 11811 O O4  . NAG U  3 .   ? 54.036  38.032 -3.623  1.00 40.18  ? 1154 NAG D O4  1 
HETATM 11812 O O5  . NAG U  3 .   ? 51.426  37.577 -1.070  1.00 36.50  ? 1154 NAG D O5  1 
HETATM 11813 O O6  . NAG U  3 .   ? 50.226  36.335 -3.366  1.00 39.85  ? 1154 NAG D O6  1 
HETATM 11814 O O7  . NAG U  3 .   ? 53.211  39.593 2.627   1.00 37.26  ? 1154 NAG D O7  1 
HETATM 11815 N N1  . EPE V  8 .   ? 28.729  31.859 3.838   1.00 43.40  ? 1164 EPE D N1  1 
HETATM 11816 C C2  . EPE V  8 .   ? 27.997  30.593 3.978   1.00 43.93  ? 1164 EPE D C2  1 
HETATM 11817 C C3  . EPE V  8 .   ? 26.488  30.871 3.982   1.00 43.77  ? 1164 EPE D C3  1 
HETATM 11818 N N4  . EPE V  8 .   ? 26.195  31.761 2.856   1.00 43.34  ? 1164 EPE D N4  1 
HETATM 11819 C C5  . EPE V  8 .   ? 26.963  32.990 2.683   1.00 42.85  ? 1164 EPE D C5  1 
HETATM 11820 C C6  . EPE V  8 .   ? 27.972  33.098 3.823   1.00 43.45  ? 1164 EPE D C6  1 
HETATM 11821 C C7  . EPE V  8 .   ? 25.151  31.419 1.881   1.00 43.28  ? 1164 EPE D C7  1 
HETATM 11822 C C8  . EPE V  8 .   ? 24.079  32.518 1.854   1.00 43.04  ? 1164 EPE D C8  1 
HETATM 11823 O O8  . EPE V  8 .   ? 24.085  33.191 0.584   1.00 42.50  ? 1164 EPE D O8  1 
HETATM 11824 C C9  . EPE V  8 .   ? 30.187  31.962 3.753   1.00 44.62  ? 1164 EPE D C9  1 
HETATM 11825 C C10 . EPE V  8 .   ? 30.761  30.826 2.916   1.00 47.98  ? 1164 EPE D C10 1 
HETATM 11826 S S   . EPE V  8 .   ? 31.268  29.547 3.861   1.00 53.24  ? 1164 EPE D S   1 
HETATM 11827 O O1S . EPE V  8 .   ? 30.665  29.593 5.218   1.00 54.63  ? 1164 EPE D O1S 1 
HETATM 11828 O O2S . EPE V  8 .   ? 32.742  29.622 3.998   1.00 52.49  ? 1164 EPE D O2S 1 
HETATM 11829 O O3S . EPE V  8 .   ? 30.887  28.257 3.223   1.00 53.60  ? 1164 EPE D O3S 1 
HETATM 11830 C C1  . NAG W  3 .   ? 52.343  52.172 31.881  1.00 23.58  ? 1023 NAG E C1  1 
HETATM 11831 C C2  . NAG W  3 .   ? 52.931  50.787 32.208  1.00 26.99  ? 1023 NAG E C2  1 
HETATM 11832 C C3  . NAG W  3 .   ? 53.642  50.728 33.564  1.00 27.75  ? 1023 NAG E C3  1 
HETATM 11833 C C4  . NAG W  3 .   ? 54.609  51.902 33.661  1.00 27.67  ? 1023 NAG E C4  1 
HETATM 11834 C C5  . NAG W  3 .   ? 53.757  53.169 33.603  1.00 27.06  ? 1023 NAG E C5  1 
HETATM 11835 C C6  . NAG W  3 .   ? 54.570  54.427 33.931  1.00 27.58  ? 1023 NAG E C6  1 
HETATM 11836 C C7  . NAG W  3 .   ? 51.850  48.849 31.130  1.00 28.79  ? 1023 NAG E C7  1 
HETATM 11837 C C8  . NAG W  3 .   ? 50.779  47.792 31.209  1.00 28.43  ? 1023 NAG E C8  1 
HETATM 11838 N N2  . NAG W  3 .   ? 51.930  49.720 32.148  1.00 28.11  ? 1023 NAG E N2  1 
HETATM 11839 O O3  . NAG W  3 .   ? 54.331  49.500 33.705  1.00 28.45  ? 1023 NAG E O3  1 
HETATM 11840 O O4  . NAG W  3 .   ? 55.408  51.806 34.828  1.00 28.22  ? 1023 NAG E O4  1 
HETATM 11841 O O5  . NAG W  3 .   ? 53.182  53.248 32.306  1.00 24.94  ? 1023 NAG E O5  1 
HETATM 11842 O O6  . NAG W  3 .   ? 54.303  55.484 33.032  1.00 28.64  ? 1023 NAG E O6  1 
HETATM 11843 O O7  . NAG W  3 .   ? 52.599  48.880 30.148  1.00 29.36  ? 1023 NAG E O7  1 
HETATM 11844 C C1  . NAG X  3 .   ? 18.373  80.616 89.507  1.00 24.80  ? 1165 NAG E C1  1 
HETATM 11845 C C2  . NAG X  3 .   ? 17.512  81.576 88.663  1.00 27.47  ? 1165 NAG E C2  1 
HETATM 11846 C C3  . NAG X  3 .   ? 16.017  81.329 88.920  1.00 27.77  ? 1165 NAG E C3  1 
HETATM 11847 C C4  . NAG X  3 .   ? 15.734  79.852 88.635  1.00 28.01  ? 1165 NAG E C4  1 
HETATM 11848 C C5  . NAG X  3 .   ? 16.620  78.999 89.558  1.00 27.51  ? 1165 NAG E C5  1 
HETATM 11849 C C6  . NAG X  3 .   ? 16.375  77.489 89.444  1.00 27.64  ? 1165 NAG E C6  1 
HETATM 11850 C C7  . NAG X  3 .   ? 17.934  83.716 89.917  1.00 31.23  ? 1165 NAG E C7  1 
HETATM 11851 C C8  . NAG X  3 .   ? 18.347  85.165 89.794  1.00 31.29  ? 1165 NAG E C8  1 
HETATM 11852 N N2  . NAG X  3 .   ? 17.886  82.993 88.779  1.00 29.11  ? 1165 NAG E N2  1 
HETATM 11853 O O3  . NAG X  3 .   ? 15.181  82.146 88.123  1.00 28.43  ? 1165 NAG E O3  1 
HETATM 11854 O O4  . NAG X  3 .   ? 14.350  79.568 88.753  1.00 28.84  ? 1165 NAG E O4  1 
HETATM 11855 O O5  . NAG X  3 .   ? 17.976  79.275 89.246  1.00 26.02  ? 1165 NAG E O5  1 
HETATM 11856 O O6  . NAG X  3 .   ? 16.880  76.829 90.587  1.00 27.74  ? 1165 NAG E O6  1 
HETATM 11857 O O7  . NAG X  3 .   ? 17.663  83.275 91.042  1.00 32.51  ? 1165 NAG E O7  1 
HETATM 11858 C C1  . SIA Y  4 .   ? 53.418  65.566 96.510  1.00 46.28  ? 1322 SIA E C1  1 
HETATM 11859 C C2  . SIA Y  4 .   ? 53.394  65.085 97.947  1.00 45.29  ? 1322 SIA E C2  1 
HETATM 11860 C C3  . SIA Y  4 .   ? 53.594  66.314 98.840  1.00 44.00  ? 1322 SIA E C3  1 
HETATM 11861 C C4  . SIA Y  4 .   ? 52.401  67.253 98.704  1.00 42.59  ? 1322 SIA E C4  1 
HETATM 11862 C C5  . SIA Y  4 .   ? 51.131  66.495 99.066  1.00 41.40  ? 1322 SIA E C5  1 
HETATM 11863 C C6  . SIA Y  4 .   ? 50.972  65.244 98.200  1.00 41.15  ? 1322 SIA E C6  1 
HETATM 11864 C C7  . SIA Y  4 .   ? 49.746  64.401 98.562  1.00 40.28  ? 1322 SIA E C7  1 
HETATM 11865 C C8  . SIA Y  4 .   ? 49.707  63.050 97.836  1.00 39.72  ? 1322 SIA E C8  1 
HETATM 11866 C C9  . SIA Y  4 .   ? 48.281  62.501 97.841  1.00 39.03  ? 1322 SIA E C9  1 
HETATM 11867 C C10 . SIA Y  4 .   ? 48.913  67.448 99.443  1.00 39.82  ? 1322 SIA E C10 1 
HETATM 11868 C C11 . SIA Y  4 .   ? 47.891  68.463 99.020  1.00 39.19  ? 1322 SIA E C11 1 
HETATM 11869 N N5  . SIA Y  4 .   ? 50.050  67.423 98.752  1.00 40.60  ? 1322 SIA E N5  1 
HETATM 11870 O O1A . SIA Y  4 .   ? 52.534  65.174 95.711  1.00 47.21  ? 1322 SIA E O1A 1 
HETATM 11871 O O1B . SIA Y  4 .   ? 54.339  66.350 96.167  1.00 47.54  ? 1322 SIA E O1B 1 
HETATM 11872 O O4  . SIA Y  4 .   ? 52.552  68.394 99.555  1.00 42.48  ? 1322 SIA E O4  1 
HETATM 11873 O O6  . SIA Y  4 .   ? 52.157  64.432 98.284  1.00 42.68  ? 1322 SIA E O6  1 
HETATM 11874 O O7  . SIA Y  4 .   ? 49.702  64.176 99.974  1.00 39.65  ? 1322 SIA E O7  1 
HETATM 11875 O O8  . SIA Y  4 .   ? 50.157  63.176 96.476  1.00 39.26  ? 1322 SIA E O8  1 
HETATM 11876 O O9  . SIA Y  4 .   ? 48.258  61.131 97.416  1.00 39.30  ? 1322 SIA E O9  1 
HETATM 11877 O O10 . SIA Y  4 .   ? 48.712  66.678 100.362 1.00 39.35  ? 1322 SIA E O10 1 
HETATM 11878 C C1  . GLA Z  5 .   ? 56.701  62.221 100.355 1.00 56.97  ? 1323 GLA E C1  1 
HETATM 11879 C C2  . GLA Z  5 .   ? 56.198  63.381 99.486  1.00 54.64  ? 1323 GLA E C2  1 
HETATM 11880 C C3  . GLA Z  5 .   ? 54.679  63.429 99.269  1.00 52.02  ? 1323 GLA E C3  1 
HETATM 11881 C C4  . GLA Z  5 .   ? 54.030  62.052 99.128  1.00 51.91  ? 1323 GLA E C4  1 
HETATM 11882 C C5  . GLA Z  5 .   ? 54.622  61.030 100.107 1.00 52.25  ? 1323 GLA E C5  1 
HETATM 11883 C C6  . GLA Z  5 .   ? 54.062  59.619 99.900  1.00 50.38  ? 1323 GLA E C6  1 
HETATM 11884 O O2  . GLA Z  5 .   ? 56.643  64.625 100.045 1.00 54.76  ? 1323 GLA E O2  1 
HETATM 11885 O O3  . GLA Z  5 .   ? 54.487  64.162 98.052  1.00 48.21  ? 1323 GLA E O3  1 
HETATM 11886 O O4  . GLA Z  5 .   ? 54.199  61.621 97.771  1.00 49.82  ? 1323 GLA E O4  1 
HETATM 11887 O O5  . GLA Z  5 .   ? 56.049  61.003 99.967  1.00 55.05  ? 1323 GLA E O5  1 
HETATM 11888 O O6  . GLA Z  5 .   ? 53.154  59.287 100.955 1.00 47.81  ? 1323 GLA E O6  1 
HETATM 11889 C C1  . NGS AA 6 .   ? 60.168  61.998 103.935 1.00 72.39  ? 1324 NGS E C1  1 
HETATM 11890 C C2  . NGS AA 6 .   ? 59.519  60.710 103.413 1.00 70.67  ? 1324 NGS E C2  1 
HETATM 11891 C C3  . NGS AA 6 .   ? 58.609  61.016 102.211 1.00 69.17  ? 1324 NGS E C3  1 
HETATM 11892 C C4  . NGS AA 6 .   ? 57.588  62.082 102.671 1.00 68.19  ? 1324 NGS E C4  1 
HETATM 11893 C C5  . NGS AA 6 .   ? 58.398  63.330 103.049 1.00 70.80  ? 1324 NGS E C5  1 
HETATM 11894 C C6  . NGS AA 6 .   ? 57.567  64.573 103.369 1.00 71.77  ? 1324 NGS E C6  1 
HETATM 11895 O O1  . NGS AA 6 .   ? 60.896  61.727 105.142 1.00 73.90  ? 1324 NGS E O1  1 
HETATM 11896 O O3  . NGS AA 6 .   ? 57.989  59.834 101.664 1.00 68.76  ? 1324 NGS E O3  1 
HETATM 11897 O O5  . NGS AA 6 .   ? 59.185  63.005 104.196 1.00 72.66  ? 1324 NGS E O5  1 
HETATM 11898 O O6  . NGS AA 6 .   ? 56.392  64.207 104.093 1.00 73.65  ? 1324 NGS E O6  1 
HETATM 11899 N N   . NGS AA 6 .   ? 60.658  59.896 102.980 1.00 70.50  ? 1324 NGS E N   1 
HETATM 11900 C C   . NGS AA 6 .   ? 60.874  58.628 103.347 1.00 69.02  ? 1324 NGS E C   1 
HETATM 11901 O O   . NGS AA 6 .   ? 60.118  58.005 104.080 1.00 68.59  ? 1324 NGS E O   1 
HETATM 11902 C CH3 . NGS AA 6 .   ? 62.109  57.999 102.767 1.00 67.88  ? 1324 NGS E CH3 1 
HETATM 11903 S S   . NGS AA 6 .   ? 54.997  64.784 103.785 1.00 76.22  ? 1324 NGS E S   1 
HETATM 11904 O O7  . NGS AA 6 .   ? 54.045  63.653 103.704 1.00 74.73  ? 1324 NGS E O7  1 
HETATM 11905 O O8  . NGS AA 6 .   ? 54.595  65.696 104.885 1.00 75.48  ? 1324 NGS E O8  1 
HETATM 11906 O O9  . NGS AA 6 .   ? 54.978  65.532 102.503 1.00 75.41  ? 1324 NGS E O9  1 
HETATM 11907 O O4  . NGS AA 6 .   ? 56.519  62.439 101.761 1.00 62.99  ? 1324 NGS E O4  1 
HETATM 11908 C C1  . FUC BA 7 .   ? 58.856  58.972 100.890 1.00 68.93  ? 1325 FUC E C1  1 
HETATM 11909 C C2  . FUC BA 7 .   ? 58.076  57.904 100.109 1.00 68.16  ? 1325 FUC E C2  1 
HETATM 11910 C C3  . FUC BA 7 .   ? 57.703  58.276 98.672  1.00 68.59  ? 1325 FUC E C3  1 
HETATM 11911 C C4  . FUC BA 7 .   ? 58.789  59.076 97.956  1.00 70.08  ? 1325 FUC E C4  1 
HETATM 11912 C C5  . FUC BA 7 .   ? 59.186  60.244 98.844  1.00 70.17  ? 1325 FUC E C5  1 
HETATM 11913 C C6  . FUC BA 7 .   ? 60.154  61.218 98.172  1.00 69.23  ? 1325 FUC E C6  1 
HETATM 11914 O O2  . FUC BA 7 .   ? 56.884  57.580 100.835 1.00 67.66  ? 1325 FUC E O2  1 
HETATM 11915 O O3  . FUC BA 7 .   ? 57.455  57.059 97.965  1.00 64.84  ? 1325 FUC E O3  1 
HETATM 11916 O O4  . FUC BA 7 .   ? 59.931  58.253 97.676  1.00 71.25  ? 1325 FUC E O4  1 
HETATM 11917 O O5  . FUC BA 7 .   ? 59.755  59.721 100.048 1.00 69.78  ? 1325 FUC E O5  1 
HETATM 11918 C C1  . NAG CA 3 .   ? 29.304  77.289 -0.083  1.00 33.45  ? 1154 NAG F C1  1 
HETATM 11919 C C2  . NAG CA 3 .   ? 28.064  78.193 -0.161  1.00 36.76  ? 1154 NAG F C2  1 
HETATM 11920 C C3  . NAG CA 3 .   ? 27.617  78.517 -1.584  1.00 38.06  ? 1154 NAG F C3  1 
HETATM 11921 C C4  . NAG CA 3 .   ? 28.804  78.963 -2.430  1.00 38.72  ? 1154 NAG F C4  1 
HETATM 11922 C C5  . NAG CA 3 .   ? 29.888  77.884 -2.395  1.00 38.66  ? 1154 NAG F C5  1 
HETATM 11923 C C6  . NAG CA 3 .   ? 31.131  78.347 -3.161  1.00 39.61  ? 1154 NAG F C6  1 
HETATM 11924 C C7  . NAG CA 3 .   ? 26.949  77.629 1.941   1.00 37.16  ? 1154 NAG F C7  1 
HETATM 11925 C C8  . NAG CA 3 .   ? 25.757  77.032 2.639   1.00 36.75  ? 1154 NAG F C8  1 
HETATM 11926 N N2  . NAG CA 3 .   ? 26.952  77.632 0.602   1.00 36.81  ? 1154 NAG F N2  1 
HETATM 11927 O O3  . NAG CA 3 .   ? 26.676  79.566 -1.521  1.00 38.98  ? 1154 NAG F O3  1 
HETATM 11928 O O4  . NAG CA 3 .   ? 28.382  79.227 -3.757  1.00 38.34  ? 1154 NAG F O4  1 
HETATM 11929 O O5  . NAG CA 3 .   ? 30.288  77.588 -1.066  1.00 35.90  ? 1154 NAG F O5  1 
HETATM 11930 O O6  . NAG CA 3 .   ? 32.054  77.285 -3.281  1.00 40.69  ? 1154 NAG F O6  1 
HETATM 11931 O O7  . NAG CA 3 .   ? 27.875  78.087 2.613   1.00 37.39  ? 1154 NAG F O7  1 
HETATM 11932 N N1  . EPE DA 8 .   ? 47.005  60.603 3.699   1.00 39.12  ? 1164 EPE F N1  1 
HETATM 11933 C C2  . EPE DA 8 .   ? 48.417  60.459 4.057   1.00 39.62  ? 1164 EPE F C2  1 
HETATM 11934 C C3  . EPE DA 8 .   ? 48.788  58.972 3.965   1.00 39.47  ? 1164 EPE F C3  1 
HETATM 11935 N N4  . EPE DA 8 .   ? 48.057  58.403 2.831   1.00 39.00  ? 1164 EPE F N4  1 
HETATM 11936 C C5  . EPE DA 8 .   ? 46.600  58.484 2.777   1.00 38.71  ? 1164 EPE F C5  1 
HETATM 11937 C C6  . EPE DA 8 .   ? 46.124  59.465 3.845   1.00 38.99  ? 1164 EPE F C6  1 
HETATM 11938 C C7  . EPE DA 8 .   ? 48.771  57.763 1.726   1.00 39.16  ? 1164 EPE F C7  1 
HETATM 11939 C C8  . EPE DA 8 .   ? 48.364  56.286 1.652   1.00 39.03  ? 1164 EPE F C8  1 
HETATM 11940 O O8  . EPE DA 8 .   ? 47.846  55.998 0.346   1.00 38.79  ? 1164 EPE F O8  1 
HETATM 11941 C C9  . EPE DA 8 .   ? 46.473  61.852 3.185   1.00 39.65  ? 1164 EPE F C9  1 
HETATM 11942 C C10 . EPE DA 8 .   ? 46.563  62.831 4.345   1.00 42.00  ? 1164 EPE F C10 1 
HETATM 11943 S S   . EPE DA 8 .   ? 47.435  64.172 3.899   1.00 46.32  ? 1164 EPE F S   1 
HETATM 11944 O O1S . EPE DA 8 .   ? 47.536  65.116 5.040   1.00 47.03  ? 1164 EPE F O1S 1 
HETATM 11945 O O2S . EPE DA 8 .   ? 46.696  64.816 2.789   1.00 46.24  ? 1164 EPE F O2S 1 
HETATM 11946 O O3S . EPE DA 8 .   ? 48.809  63.796 3.470   1.00 47.31  ? 1164 EPE F O3S 1 
HETATM 11947 O O   . HOH EA 9 .   ? 11.340  58.388 -7.193  1.00 16.76  ? 2001 HOH A O   1 
HETATM 11948 O O   . HOH EA 9 .   ? 5.060   52.482 -9.753  1.00 21.34  ? 2002 HOH A O   1 
HETATM 11949 O O   . HOH EA 9 .   ? 9.285   56.950 -0.176  1.00 10.33  ? 2003 HOH A O   1 
HETATM 11950 O O   . HOH EA 9 .   ? 14.064  61.350 -1.039  1.00 24.68  ? 2004 HOH A O   1 
HETATM 11951 O O   . HOH EA 9 .   ? 14.501  58.484 5.155   1.00 14.92  ? 2005 HOH A O   1 
HETATM 11952 O O   . HOH EA 9 .   ? 12.837  58.873 9.887   1.00 4.33   ? 2006 HOH A O   1 
HETATM 11953 O O   . HOH EA 9 .   ? 12.167  60.801 16.347  1.00 5.01   ? 2007 HOH A O   1 
HETATM 11954 O O   . HOH EA 9 .   ? 3.588   57.361 20.454  1.00 19.23  ? 2008 HOH A O   1 
HETATM 11955 O O   . HOH EA 9 .   ? 4.190   66.054 17.302  1.00 20.25  ? 2009 HOH A O   1 
HETATM 11956 O O   . HOH EA 9 .   ? 0.421   65.759 17.646  1.00 31.10  ? 2010 HOH A O   1 
HETATM 11957 O O   . HOH EA 9 .   ? 8.850   66.749 20.886  1.00 23.20  ? 2011 HOH A O   1 
HETATM 11958 O O   . HOH EA 9 .   ? 5.450   59.085 25.185  1.00 14.57  ? 2012 HOH A O   1 
HETATM 11959 O O   . HOH EA 9 .   ? 10.808  68.184 26.037  1.00 12.80  ? 2013 HOH A O   1 
HETATM 11960 O O   . HOH EA 9 .   ? 15.989  65.391 31.471  1.00 12.75  ? 2014 HOH A O   1 
HETATM 11961 O O   . HOH EA 9 .   ? 17.074  60.686 32.809  1.00 4.24   ? 2015 HOH A O   1 
HETATM 11962 O O   . HOH EA 9 .   ? 18.905  68.474 33.763  1.00 21.33  ? 2016 HOH A O   1 
HETATM 11963 O O   . HOH EA 9 .   ? 24.480  64.949 32.743  1.00 8.68   ? 2017 HOH A O   1 
HETATM 11964 O O   . HOH EA 9 .   ? 24.526  63.212 23.238  1.00 12.48  ? 2018 HOH A O   1 
HETATM 11965 O O   . HOH EA 9 .   ? 7.728   51.473 24.900  1.00 24.18  ? 2019 HOH A O   1 
HETATM 11966 O O   . HOH EA 9 .   ? 7.628   52.257 29.897  1.00 21.97  ? 2020 HOH A O   1 
HETATM 11967 O O   . HOH EA 9 .   ? 6.504   56.184 33.382  1.00 26.22  ? 2021 HOH A O   1 
HETATM 11968 O O   . HOH EA 9 .   ? 11.766  60.870 38.370  1.00 8.65   ? 2022 HOH A O   1 
HETATM 11969 O O   . HOH EA 9 .   ? 2.971   56.800 47.291  1.00 16.95  ? 2023 HOH A O   1 
HETATM 11970 O O   . HOH EA 9 .   ? 1.390   44.813 58.912  1.00 18.76  ? 2024 HOH A O   1 
HETATM 11971 O O   . HOH EA 9 .   ? -8.187  51.840 84.690  1.00 31.36  ? 2025 HOH A O   1 
HETATM 11972 O O   . HOH EA 9 .   ? -2.757  50.551 69.810  1.00 17.23  ? 2026 HOH A O   1 
HETATM 11973 O O   . HOH EA 9 .   ? 4.666   58.556 78.391  1.00 28.48  ? 2027 HOH A O   1 
HETATM 11974 O O   . HOH EA 9 .   ? -4.996  50.056 75.588  1.00 30.39  ? 2028 HOH A O   1 
HETATM 11975 O O   . HOH EA 9 .   ? -6.606  46.977 74.213  1.00 32.83  ? 2029 HOH A O   1 
HETATM 11976 O O   . HOH EA 9 .   ? -4.387  45.349 84.187  1.00 27.72  ? 2030 HOH A O   1 
HETATM 11977 O O   . HOH EA 9 .   ? 8.116   66.669 78.910  1.00 32.39  ? 2031 HOH A O   1 
HETATM 11978 O O   . HOH EA 9 .   ? 10.864  65.432 96.203  1.00 17.68  ? 2032 HOH A O   1 
HETATM 11979 O O   . HOH EA 9 .   ? 17.849  48.337 83.439  1.00 22.64  ? 2033 HOH A O   1 
HETATM 11980 O O   . HOH EA 9 .   ? 22.892  51.509 77.897  1.00 18.49  ? 2034 HOH A O   1 
HETATM 11981 O O   . HOH EA 9 .   ? 20.483  51.698 76.514  1.00 14.74  ? 2035 HOH A O   1 
HETATM 11982 O O   . HOH EA 9 .   ? 18.622  45.363 73.685  1.00 12.03  ? 2036 HOH A O   1 
HETATM 11983 O O   . HOH EA 9 .   ? 24.822  49.189 72.384  1.00 6.29   ? 2037 HOH A O   1 
HETATM 11984 O O   . HOH EA 9 .   ? 14.599  64.429 58.325  1.00 31.20  ? 2038 HOH A O   1 
HETATM 11985 O O   . HOH EA 9 .   ? 12.047  49.694 67.968  1.00 18.25  ? 2039 HOH A O   1 
HETATM 11986 O O   . HOH EA 9 .   ? -0.743  48.996 102.578 1.00 26.90  ? 2040 HOH A O   1 
HETATM 11987 O O   . HOH EA 9 .   ? 7.774   41.639 102.862 1.00 30.16  ? 2041 HOH A O   1 
HETATM 11988 O O   . HOH EA 9 .   ? 2.468   53.696 100.208 1.00 27.73  ? 2042 HOH A O   1 
HETATM 11989 O O   . HOH EA 9 .   ? -1.470  66.172 92.264  1.00 22.10  ? 2043 HOH A O   1 
HETATM 11990 O O   . HOH EA 9 .   ? -7.416  53.729 86.636  1.00 26.74  ? 2044 HOH A O   1 
HETATM 11991 O O   . HOH EA 9 .   ? 0.116   50.432 115.448 1.00 28.80  ? 2045 HOH A O   1 
HETATM 11992 O O   . HOH EA 9 .   ? 17.974  39.049 96.050  1.00 28.57  ? 2046 HOH A O   1 
HETATM 11993 O O   . HOH EA 9 .   ? 22.170  35.951 89.146  1.00 24.37  ? 2047 HOH A O   1 
HETATM 11994 O O   . HOH EA 9 .   ? 26.564  54.004 89.098  1.00 27.76  ? 2048 HOH A O   1 
HETATM 11995 O O   . HOH EA 9 .   ? 24.291  67.459 96.127  1.00 18.90  ? 2049 HOH A O   1 
HETATM 11996 O O   . HOH EA 9 .   ? -4.163  52.920 42.373  1.00 39.59  ? 2050 HOH A O   1 
HETATM 11997 O O   . HOH EA 9 .   ? 0.223   51.101 41.593  1.00 39.21  ? 2051 HOH A O   1 
HETATM 11998 O O   . HOH EA 9 .   ? 12.323  64.539 48.867  1.00 27.25  ? 2052 HOH A O   1 
HETATM 11999 O O   . HOH EA 9 .   ? 10.537  63.953 51.122  1.00 18.13  ? 2053 HOH A O   1 
HETATM 12000 O O   . HOH EA 9 .   ? 11.908  62.947 60.218  1.00 26.24  ? 2054 HOH A O   1 
HETATM 12001 O O   . HOH EA 9 .   ? 17.746  53.473 29.269  1.00 3.26   ? 2055 HOH A O   1 
HETATM 12002 O O   . HOH EA 9 .   ? 9.013   49.611 26.291  1.00 18.70  ? 2056 HOH A O   1 
HETATM 12003 O O   . HOH EA 9 .   ? 18.064  57.503 19.732  1.00 2.69   ? 2057 HOH A O   1 
HETATM 12004 O O   . HOH EA 9 .   ? 20.395  59.232 19.345  1.00 7.54   ? 2058 HOH A O   1 
HETATM 12005 O O   . HOH EA 9 .   ? 15.787  65.382 17.134  1.00 20.67  ? 2059 HOH A O   1 
HETATM 12006 O O   . HOH EA 9 .   ? 7.531   69.639 15.778  1.00 29.04  ? 2060 HOH A O   1 
HETATM 12007 O O   . HOH FA 9 .   ? 23.445  59.411 14.894  1.00 4.47   ? 2001 HOH B O   1 
HETATM 12008 O O   . HOH FA 9 .   ? 29.169  60.223 17.538  1.00 2.01   ? 2002 HOH B O   1 
HETATM 12009 O O   . HOH FA 9 .   ? 29.224  55.267 13.098  1.00 4.42   ? 2003 HOH B O   1 
HETATM 12010 O O   . HOH FA 9 .   ? 20.612  65.390 10.646  1.00 10.87  ? 2004 HOH B O   1 
HETATM 12011 O O   . HOH FA 9 .   ? 20.489  64.089 5.644   1.00 14.69  ? 2005 HOH B O   1 
HETATM 12012 O O   . HOH FA 9 .   ? 16.989  62.812 5.535   1.00 24.01  ? 2006 HOH B O   1 
HETATM 12013 O O   . HOH FA 9 .   ? 14.662  62.592 7.457   1.00 21.29  ? 2007 HOH B O   1 
HETATM 12014 O O   . HOH FA 9 .   ? 5.976   61.194 8.963   1.00 14.86  ? 2008 HOH B O   1 
HETATM 12015 O O   . HOH FA 9 .   ? 5.373   49.004 18.847  1.00 22.64  ? 2009 HOH B O   1 
HETATM 12016 O O   . HOH FA 9 .   ? 6.425   51.830 19.102  1.00 10.01  ? 2010 HOH B O   1 
HETATM 12017 O O   . HOH FA 9 .   ? 6.361   50.232 21.098  1.00 33.20  ? 2011 HOH B O   1 
HETATM 12018 O O   . HOH FA 9 .   ? 2.033   52.579 -3.331  1.00 16.09  ? 2012 HOH B O   1 
HETATM 12019 O O   . HOH FA 9 .   ? 9.464   42.827 10.007  1.00 33.41  ? 2013 HOH B O   1 
HETATM 12020 O O   . HOH FA 9 .   ? 7.378   38.721 24.104  1.00 19.06  ? 2014 HOH B O   1 
HETATM 12021 O O   . HOH FA 9 .   ? 20.308  40.428 32.921  1.00 11.34  ? 2015 HOH B O   1 
HETATM 12022 O O   . HOH FA 9 .   ? 23.446  47.611 51.384  1.00 12.79  ? 2016 HOH B O   1 
HETATM 12023 O O   . HOH FA 9 .   ? 20.599  49.822 58.995  1.00 13.57  ? 2017 HOH B O   1 
HETATM 12024 O O   . HOH FA 9 .   ? 17.328  59.098 71.484  1.00 23.49  ? 2018 HOH B O   1 
HETATM 12025 O O   . HOH FA 9 .   ? 30.120  57.132 75.229  1.00 14.68  ? 2019 HOH B O   1 
HETATM 12026 O O   . HOH FA 9 .   ? 26.731  50.658 74.056  1.00 16.98  ? 2020 HOH B O   1 
HETATM 12027 O O   . HOH FA 9 .   ? 34.072  58.764 76.582  1.00 10.26  ? 2021 HOH B O   1 
HETATM 12028 O O   . HOH FA 9 .   ? 29.534  56.701 72.467  1.00 6.85   ? 2022 HOH B O   1 
HETATM 12029 O O   . HOH FA 9 .   ? 20.632  63.821 63.050  1.00 30.13  ? 2023 HOH B O   1 
HETATM 12030 O O   . HOH FA 9 .   ? 28.964  58.297 51.319  1.00 12.73  ? 2024 HOH B O   1 
HETATM 12031 O O   . HOH FA 9 .   ? 25.500  51.847 39.081  1.00 4.86   ? 2025 HOH B O   1 
HETATM 12032 O O   . HOH FA 9 .   ? 28.810  52.085 44.328  1.00 14.36  ? 2026 HOH B O   1 
HETATM 12033 O O   . HOH FA 9 .   ? 20.459  60.282 36.725  1.00 9.36   ? 2027 HOH B O   1 
HETATM 12034 O O   . HOH FA 9 .   ? 27.931  52.757 28.772  1.00 22.72  ? 2028 HOH B O   1 
HETATM 12035 O O   . HOH FA 9 .   ? 29.642  48.387 22.883  1.00 15.24  ? 2029 HOH B O   1 
HETATM 12036 O O   . HOH FA 9 .   ? 21.858  47.187 17.579  1.00 6.64   ? 2030 HOH B O   1 
HETATM 12037 O O   . HOH FA 9 .   ? 26.126  49.612 13.096  1.00 6.25   ? 2031 HOH B O   1 
HETATM 12038 O O   . HOH FA 9 .   ? 20.295  57.000 1.213   1.00 7.24   ? 2032 HOH B O   1 
HETATM 12039 O O   . HOH FA 9 .   ? 20.101  42.231 3.225   1.00 15.95  ? 2033 HOH B O   1 
HETATM 12040 O O   . HOH FA 9 .   ? 26.386  48.927 -5.439  1.00 15.47  ? 2034 HOH B O   1 
HETATM 12041 O O   . HOH FA 9 .   ? 28.540  45.223 -5.684  1.00 21.56  ? 2035 HOH B O   1 
HETATM 12042 O O   . HOH FA 9 .   ? 24.352  54.937 -5.742  1.00 26.37  ? 2036 HOH B O   1 
HETATM 12043 O O   . HOH FA 9 .   ? 14.577  43.347 -17.373 1.00 36.06  ? 2037 HOH B O   1 
HETATM 12044 O O   . HOH GA 9 .   ? 32.315  32.166 -7.164  1.00 19.76  ? 2001 HOH C O   1 
HETATM 12045 O O   . HOH GA 9 .   ? 40.128  29.955 -9.895  1.00 11.95  ? 2002 HOH C O   1 
HETATM 12046 O O   . HOH GA 9 .   ? 34.501  31.359 -0.245  1.00 7.90   ? 2003 HOH C O   1 
HETATM 12047 O O   . HOH GA 9 .   ? 30.639  35.114 5.161   1.00 9.35   ? 2004 HOH C O   1 
HETATM 12048 O O   . HOH GA 9 .   ? 31.161  33.577 9.783   1.00 4.05   ? 2005 HOH C O   1 
HETATM 12049 O O   . HOH GA 9 .   ? 29.867  31.789 16.251  1.00 6.56   ? 2006 HOH C O   1 
HETATM 12050 O O   . HOH GA 9 .   ? 36.673  26.352 20.263  1.00 25.47  ? 2007 HOH C O   1 
HETATM 12051 O O   . HOH GA 9 .   ? 31.367  19.358 17.424  1.00 37.29  ? 2008 HOH C O   1 
HETATM 12052 O O   . HOH GA 9 .   ? 26.412  26.082 20.834  1.00 22.00  ? 2009 HOH C O   1 
HETATM 12053 O O   . HOH GA 9 .   ? 33.824  27.148 25.493  1.00 17.16  ? 2010 HOH C O   1 
HETATM 12054 O O   . HOH GA 9 .   ? 23.959  32.950 31.213  1.00 20.50  ? 2011 HOH C O   1 
HETATM 12055 O O   . HOH GA 9 .   ? 27.418  36.240 32.968  1.00 4.49   ? 2012 HOH C O   1 
HETATM 12056 O O   . HOH GA 9 .   ? 19.721  33.935 33.802  1.00 21.35  ? 2013 HOH C O   1 
HETATM 12057 O O   . HOH GA 9 .   ? 21.455  38.911 35.121  1.00 16.09  ? 2014 HOH C O   1 
HETATM 12058 O O   . HOH GA 9 .   ? 21.476  41.638 23.188  1.00 17.19  ? 2015 HOH C O   1 
HETATM 12059 O O   . HOH GA 9 .   ? 23.952  32.767 21.204  1.00 22.02  ? 2016 HOH C O   1 
HETATM 12060 O O   . HOH GA 9 .   ? 39.354  32.419 29.725  1.00 19.17  ? 2017 HOH C O   1 
HETATM 12061 O O   . HOH GA 9 .   ? 36.598  29.405 33.475  1.00 27.56  ? 2018 HOH C O   1 
HETATM 12062 O O   . HOH GA 9 .   ? 29.940  31.744 38.366  1.00 7.28   ? 2019 HOH C O   1 
HETATM 12063 O O   . HOH GA 9 .   ? 37.797  25.909 47.281  1.00 14.04  ? 2020 HOH C O   1 
HETATM 12064 O O   . HOH GA 9 .   ? 51.113  22.564 74.262  1.00 25.89  ? 2021 HOH C O   1 
HETATM 12065 O O   . HOH GA 9 .   ? 52.150  25.860 83.908  1.00 33.06  ? 2022 HOH C O   1 
HETATM 12066 O O   . HOH GA 9 .   ? 46.586  24.879 70.059  1.00 19.86  ? 2023 HOH C O   1 
HETATM 12067 O O   . HOH GA 9 .   ? 26.458  28.566 96.198  1.00 15.50  ? 2024 HOH C O   1 
HETATM 12068 O O   . HOH GA 9 .   ? 37.786  43.354 83.656  1.00 16.96  ? 2025 HOH C O   1 
HETATM 12069 O O   . HOH GA 9 .   ? 32.989  46.242 77.875  1.00 13.35  ? 2026 HOH C O   1 
HETATM 12070 O O   . HOH GA 9 .   ? 33.405  43.899 76.528  1.00 8.84   ? 2027 HOH C O   1 
HETATM 12071 O O   . HOH GA 9 .   ? 34.657  40.977 70.258  1.00 12.17  ? 2028 HOH C O   1 
HETATM 12072 O O   . HOH GA 9 .   ? 40.110  45.395 73.907  1.00 7.71   ? 2029 HOH C O   1 
HETATM 12073 O O   . HOH GA 9 .   ? 48.692  37.797 102.799 1.00 31.27  ? 2030 HOH C O   1 
HETATM 12074 O O   . HOH GA 9 .   ? 40.743  27.195 100.280 1.00 25.91  ? 2031 HOH C O   1 
HETATM 12075 O O   . HOH GA 9 .   ? 46.067  18.694 86.523  1.00 30.88  ? 2032 HOH C O   1 
HETATM 12076 O O   . HOH GA 9 .   ? 45.386  27.008 115.301 1.00 33.71  ? 2033 HOH C O   1 
HETATM 12077 O O   . HOH GA 9 .   ? 45.798  47.762 96.062  1.00 23.11  ? 2034 HOH C O   1 
HETATM 12078 O O   . HOH GA 9 .   ? 46.415  53.155 89.186  1.00 21.43  ? 2035 HOH C O   1 
HETATM 12079 O O   . HOH GA 9 .   ? 47.778  47.484 84.399  1.00 19.02  ? 2036 HOH C O   1 
HETATM 12080 O O   . HOH GA 9 .   ? 44.604  22.437 42.277  1.00 47.46  ? 2037 HOH C O   1 
HETATM 12081 O O   . HOH GA 9 .   ? 43.573  26.674 41.633  1.00 42.06  ? 2038 HOH C O   1 
HETATM 12082 O O   . HOH GA 9 .   ? 26.336  30.116 48.978  1.00 28.69  ? 2039 HOH C O   1 
HETATM 12083 O O   . HOH GA 9 .   ? 27.939  28.885 51.177  1.00 16.88  ? 2040 HOH C O   1 
HETATM 12084 O O   . HOH GA 9 .   ? 26.977  31.308 59.868  1.00 31.36  ? 2041 HOH C O   1 
HETATM 12085 O O   . HOH GA 9 .   ? 24.482  33.544 54.624  1.00 26.39  ? 2042 HOH C O   1 
HETATM 12086 O O   . HOH GA 9 .   ? 27.429  36.847 35.816  1.00 10.46  ? 2043 HOH C O   1 
HETATM 12087 O O   . HOH GA 9 .   ? 33.451  40.486 29.233  1.00 3.01   ? 2044 HOH C O   1 
HETATM 12088 O O   . HOH GA 9 .   ? 39.854  32.694 24.935  1.00 17.65  ? 2045 HOH C O   1 
HETATM 12089 O O   . HOH GA 9 .   ? 41.080  34.833 26.206  1.00 14.15  ? 2046 HOH C O   1 
HETATM 12090 O O   . HOH GA 9 .   ? 29.895  38.783 19.704  1.00 3.56   ? 2047 HOH C O   1 
HETATM 12091 O O   . HOH GA 9 .   ? 27.208  39.690 19.083  1.00 9.03   ? 2048 HOH C O   1 
HETATM 12092 O O   . HOH GA 9 .   ? 49.643  20.682 89.555  1.00 39.47  ? 2049 HOH C O   1 
HETATM 12093 O O   . HOH GA 9 .   ? 48.197  19.732 84.775  1.00 45.53  ? 2050 HOH C O   1 
HETATM 12094 O O   . HOH GA 9 .   ? 37.946  17.088 23.478  1.00 41.57  ? 2051 HOH C O   1 
HETATM 12095 O O   . HOH GA 9 .   ? 29.350  48.531 89.935  1.00 41.89  ? 2052 HOH C O   1 
HETATM 12096 O O   . HOH HA 9 .   ? 25.422  42.418 14.915  1.00 3.65   ? 2001 HOH D O   1 
HETATM 12097 O O   . HOH HA 9 .   ? 23.277  45.069 20.750  1.00 11.43  ? 2002 HOH D O   1 
HETATM 12098 O O   . HOH HA 9 .   ? 21.093  37.226 17.476  1.00 32.24  ? 2003 HOH D O   1 
HETATM 12099 O O   . HOH HA 9 .   ? 22.893  43.594 10.203  1.00 17.29  ? 2004 HOH D O   1 
HETATM 12100 O O   . HOH HA 9 .   ? 19.974  36.778 14.840  1.00 24.24  ? 2005 HOH D O   1 
HETATM 12101 O O   . HOH HA 9 .   ? 21.683  36.864 10.889  1.00 16.15  ? 2006 HOH D O   1 
HETATM 12102 O O   . HOH HA 9 .   ? 22.466  37.733 5.776   1.00 22.64  ? 2007 HOH D O   1 
HETATM 12103 O O   . HOH HA 9 .   ? 25.977  35.252 5.650   1.00 23.51  ? 2008 HOH D O   1 
HETATM 12104 O O   . HOH HA 9 .   ? 32.786  26.200 8.943   1.00 12.27  ? 2009 HOH D O   1 
HETATM 12105 O O   . HOH HA 9 .   ? 28.487  22.311 17.582  1.00 29.75  ? 2010 HOH D O   1 
HETATM 12106 O O   . HOH HA 9 .   ? 45.115  25.848 15.233  1.00 20.72  ? 2011 HOH D O   1 
HETATM 12107 O O   . HOH HA 9 .   ? 43.574  32.014 18.799  1.00 17.57  ? 2012 HOH D O   1 
HETATM 12108 O O   . HOH HA 9 .   ? 40.408  31.272 18.897  1.00 8.23   ? 2013 HOH D O   1 
HETATM 12109 O O   . HOH HA 9 .   ? 41.794  32.416 20.702  1.00 24.07  ? 2014 HOH D O   1 
HETATM 12110 O O   . HOH HA 9 .   ? 29.480  50.140 29.108  1.00 13.60  ? 2015 HOH D O   1 
HETATM 12111 O O   . HOH HA 9 .   ? 46.805  38.829 10.141  1.00 33.23  ? 2016 HOH D O   1 
HETATM 12112 O O   . HOH HA 9 .   ? 51.469  39.012 24.366  1.00 26.88  ? 2017 HOH D O   1 
HETATM 12113 O O   . HOH HA 9 .   ? 44.303  40.457 37.214  1.00 31.49  ? 2018 HOH D O   1 
HETATM 12114 O O   . HOH HA 9 .   ? 43.376  49.077 32.810  1.00 8.91   ? 2019 HOH D O   1 
HETATM 12115 O O   . HOH HA 9 .   ? 35.403  48.344 51.290  1.00 11.69  ? 2020 HOH D O   1 
HETATM 12116 O O   . HOH HA 9 .   ? 35.075  44.729 59.082  1.00 14.04  ? 2021 HOH D O   1 
HETATM 12117 O O   . HOH HA 9 .   ? 28.699  37.112 71.678  1.00 29.37  ? 2022 HOH D O   1 
HETATM 12118 O O   . HOH HA 9 .   ? 26.067  46.950 78.356  1.00 18.90  ? 2023 HOH D O   1 
HETATM 12119 O O   . HOH HA 9 .   ? 23.937  37.516 63.083  1.00 42.43  ? 2024 HOH D O   1 
HETATM 12120 O O   . HOH HA 9 .   ? 30.787  47.946 38.924  1.00 8.99   ? 2025 HOH D O   1 
HETATM 12121 O O   . HOH HA 9 .   ? 30.447  50.918 44.322  1.00 19.96  ? 2026 HOH D O   1 
HETATM 12122 O O   . HOH HA 9 .   ? 26.254  39.427 36.673  1.00 9.61   ? 2027 HOH D O   1 
HETATM 12123 O O   . HOH HA 9 .   ? 31.971  52.140 28.703  1.00 19.09  ? 2028 HOH D O   1 
HETATM 12124 O O   . HOH HA 9 .   ? 31.921  53.322 22.783  1.00 13.58  ? 2029 HOH D O   1 
HETATM 12125 O O   . HOH HA 9 .   ? 26.474  41.980 20.042  1.00 8.68   ? 2030 HOH D O   1 
HETATM 12126 O O   . HOH HA 9 .   ? 37.153  47.395 17.529  1.00 2.99   ? 2031 HOH D O   1 
HETATM 12127 O O   . HOH HA 9 .   ? 32.648  49.632 13.130  1.00 5.37   ? 2032 HOH D O   1 
HETATM 12128 O O   . HOH HA 9 .   ? 28.970  40.831 1.397   1.00 9.62   ? 2033 HOH D O   1 
HETATM 12129 O O   . HOH HA 9 .   ? 41.794  48.442 3.137   1.00 14.87  ? 2034 HOH D O   1 
HETATM 12130 O O   . HOH HA 9 .   ? 32.886  49.928 -5.530  1.00 11.58  ? 2035 HOH D O   1 
HETATM 12131 O O   . HOH HA 9 .   ? 34.974  54.025 -5.554  1.00 16.66  ? 2036 HOH D O   1 
HETATM 12132 O O   . HOH HA 9 .   ? 23.018  36.621 -0.215  1.00 24.57  ? 2037 HOH D O   1 
HETATM 12133 O O   . HOH HA 9 .   ? 44.206  42.795 -17.574 1.00 36.37  ? 2038 HOH D O   1 
HETATM 12134 O O   . HOH IA 9 .   ? 44.612  63.734 -7.292  1.00 23.91  ? 2001 HOH E O   1 
HETATM 12135 O O   . HOH IA 9 .   ? 42.421  71.835 -9.731  1.00 15.84  ? 2002 HOH E O   1 
HETATM 12136 O O   . HOH IA 9 .   ? 44.049  66.120 -0.311  1.00 9.93   ? 2003 HOH E O   1 
HETATM 12137 O O   . HOH IA 9 .   ? 42.750  60.826 5.072   1.00 8.98   ? 2004 HOH E O   1 
HETATM 12138 O O   . HOH IA 9 .   ? 43.913  62.135 9.909   1.00 4.77   ? 2005 HOH E O   1 
HETATM 12139 O O   . HOH IA 9 .   ? 46.022  61.805 16.376  1.00 8.57   ? 2006 HOH E O   1 
HETATM 12140 O O   . HOH IA 9 .   ? 46.931  71.093 20.540  1.00 26.49  ? 2007 HOH E O   1 
HETATM 12141 O O   . HOH IA 9 .   ? 51.521  62.831 16.463  1.00 26.97  ? 2008 HOH E O   1 
HETATM 12142 O O   . HOH IA 9 .   ? 37.888  69.884 26.177  1.00 19.47  ? 2009 HOH E O   1 
HETATM 12143 O O   . HOH IA 9 .   ? 54.811  66.131 17.331  1.00 23.21  ? 2010 HOH E O   1 
HETATM 12144 O O   . HOH IA 9 .   ? 56.238  69.319 17.489  1.00 36.85  ? 2011 HOH E O   1 
HETATM 12145 O O   . HOH IA 9 .   ? 52.715  61.490 20.918  1.00 26.89  ? 2012 HOH E O   1 
HETATM 12146 O O   . HOH IA 9 .   ? 47.959  67.682 25.818  1.00 21.62  ? 2013 HOH E O   1 
HETATM 12147 O O   . HOH IA 9 .   ? 49.789  62.047 31.122  1.00 17.12  ? 2014 HOH E O   1 
HETATM 12148 O O   . HOH IA 9 .   ? 48.111  56.161 31.350  1.00 23.11  ? 2015 HOH E O   1 
HETATM 12149 O O   . HOH IA 9 .   ? 50.625  56.503 32.438  1.00 25.69  ? 2016 HOH E O   1 
HETATM 12150 O O   . HOH IA 9 .   ? 43.637  57.651 32.761  1.00 5.14   ? 2017 HOH E O   1 
HETATM 12151 O O   . HOH IA 9 .   ? 49.276  52.152 33.690  1.00 19.55  ? 2018 HOH E O   1 
HETATM 12152 O O   . HOH IA 9 .   ? 41.936  49.825 23.256  1.00 17.16  ? 2019 HOH E O   1 
HETATM 12153 O O   . HOH IA 9 .   ? 48.242  56.332 21.028  1.00 19.17  ? 2020 HOH E O   1 
HETATM 12154 O O   . HOH IA 9 .   ? 40.530  69.492 29.168  1.00 21.97  ? 2021 HOH E O   1 
HETATM 12155 O O   . HOH IA 9 .   ? 44.692  68.970 33.610  1.00 41.21  ? 2022 HOH E O   1 
HETATM 12156 O O   . HOH IA 9 .   ? 46.340  61.958 38.271  1.00 8.54   ? 2023 HOH E O   1 
HETATM 12157 O O   . HOH IA 9 .   ? 48.685  64.164 35.172  1.00 31.49  ? 2024 HOH E O   1 
HETATM 12158 O O   . HOH IA 9 .   ? 47.215  71.695 47.086  1.00 15.49  ? 2025 HOH E O   1 
HETATM 12159 O O   . HOH IA 9 .   ? 44.281  79.615 69.945  1.00 20.25  ? 2026 HOH E O   1 
HETATM 12160 O O   . HOH IA 9 .   ? 40.642  84.204 83.732  1.00 27.91  ? 2027 HOH E O   1 
HETATM 12161 O O   . HOH IA 9 .   ? 50.560  60.478 96.181  1.00 16.57  ? 2028 HOH E O   1 
HETATM 12162 O O   . HOH IA 9 .   ? 32.474  62.930 83.460  1.00 17.25  ? 2029 HOH E O   1 
HETATM 12163 O O   . HOH IA 9 .   ? 35.684  61.204 70.409  1.00 8.38   ? 2030 HOH E O   1 
HETATM 12164 O O   . HOH IA 9 .   ? 29.344  63.766 73.643  1.00 9.68   ? 2031 HOH E O   1 
HETATM 12165 O O   . HOH IA 9 .   ? 40.427  55.424 19.151  1.00 5.35   ? 2032 HOH E O   1 
HETATM 12166 O O   . HOH IA 9 .   ? 44.672  73.505 100.266 1.00 26.81  ? 2033 HOH E O   1 
HETATM 12167 O O   . HOH IA 9 .   ? 49.476  82.311 86.638  1.00 28.88  ? 2034 HOH E O   1 
HETATM 12168 O O   . HOH IA 9 .   ? 42.250  77.441 115.343 1.00 29.33  ? 2035 HOH E O   1 
HETATM 12169 O O   . HOH IA 9 .   ? 31.272  74.856 102.997 1.00 28.25  ? 2036 HOH E O   1 
HETATM 12170 O O   . HOH IA 9 .   ? 27.282  58.544 91.310  1.00 25.88  ? 2037 HOH E O   1 
HETATM 12171 O O   . HOH IA 9 .   ? 44.523  63.342 61.987  1.00 27.36  ? 2038 HOH E O   1 
HETATM 12172 O O   . HOH IA 9 .   ? 43.439  76.692 42.408  1.00 41.33  ? 2039 HOH E O   1 
HETATM 12173 O O   . HOH IA 9 .   ? 47.233  78.517 42.135  1.00 31.92  ? 2040 HOH E O   1 
HETATM 12174 O O   . HOH IA 9 .   ? 49.182  59.840 48.841  1.00 23.63  ? 2041 HOH E O   1 
HETATM 12175 O O   . HOH IA 9 .   ? 49.583  61.496 51.200  1.00 16.66  ? 2042 HOH E O   1 
HETATM 12176 O O   . HOH IA 9 .   ? 48.357  61.708 60.464  1.00 26.77  ? 2043 HOH E O   1 
HETATM 12177 O O   . HOH IA 9 .   ? 36.769  60.510 29.291  1.00 2.63   ? 2044 HOH E O   1 
HETATM 12178 O O   . HOH IA 9 .   ? 40.300  58.212 19.772  1.00 3.12   ? 2045 HOH E O   1 
HETATM 12179 O O   . HOH IA 9 .   ? 47.931  55.174 18.129  1.00 32.32  ? 2046 HOH E O   1 
HETATM 12180 O O   . HOH IA 9 .   ? 56.081  61.368 15.239  1.00 29.59  ? 2047 HOH E O   1 
HETATM 12181 O O   . HOH IA 9 .   ? 48.725  83.522 84.317  1.00 25.24  ? 2048 HOH E O   1 
HETATM 12182 O O   . HOH IA 9 .   ? 32.289  52.982 89.522  1.00 36.72  ? 2049 HOH E O   1 
HETATM 12183 O O   . HOH JA 9 .   ? 39.242  52.608 14.931  1.00 2.95   ? 2001 HOH F O   1 
HETATM 12184 O O   . HOH JA 9 .   ? 41.522  53.918 17.131  1.00 10.71  ? 2002 HOH F O   1 
HETATM 12185 O O   . HOH JA 9 .   ? 45.747  51.989 10.729  1.00 12.00  ? 2003 HOH F O   1 
HETATM 12186 O O   . HOH JA 9 .   ? 44.717  53.041 5.156   1.00 20.16  ? 2004 HOH F O   1 
HETATM 12187 O O   . HOH JA 9 .   ? 45.353  56.547 5.365   1.00 14.82  ? 2005 HOH F O   1 
HETATM 12188 O O   . HOH JA 9 .   ? 49.533  67.077 8.903   1.00 10.87  ? 2006 HOH F O   1 
HETATM 12189 O O   . HOH JA 9 .   ? 45.525  74.202 10.368  1.00 14.73  ? 2007 HOH F O   1 
HETATM 12190 O O   . HOH JA 9 .   ? 42.830  73.591 9.525   1.00 9.49   ? 2008 HOH F O   1 
HETATM 12191 O O   . HOH JA 9 .   ? 38.982  73.307 18.740  1.00 26.94  ? 2009 HOH F O   1 
HETATM 12192 O O   . HOH JA 9 .   ? 41.339  71.202 18.801  1.00 7.58   ? 2010 HOH F O   1 
HETATM 12193 O O   . HOH JA 9 .   ? 39.879  71.576 20.579  1.00 27.17  ? 2011 HOH F O   1 
HETATM 12194 O O   . HOH JA 9 .   ? 40.431  71.657 2.966   1.00 17.86  ? 2012 HOH F O   1 
HETATM 12195 O O   . HOH JA 9 .   ? 41.678  52.385 64.819  1.00 30.14  ? 2013 HOH F O   1 
HETATM 12196 O O   . HOH JA 9 .   ? 44.877  76.452 0.001   1.00 13.04  ? 2014 HOH F O   1 
HETATM 12197 O O   . HOH JA 9 .   ? 29.180  76.811 24.083  1.00 19.32  ? 2015 HOH F O   1 
HETATM 12198 O O   . HOH JA 9 .   ? 30.351  72.789 25.811  1.00 17.98  ? 2016 HOH F O   1 
HETATM 12199 O O   . HOH JA 9 .   ? 32.309  59.860 58.937  1.00 12.53  ? 2017 HOH F O   1 
HETATM 12200 O O   . HOH JA 9 .   ? 42.376  58.066 71.561  1.00 26.21  ? 2018 HOH F O   1 
HETATM 12201 O O   . HOH JA 9 .   ? 38.905  54.025 64.699  1.00 12.08  ? 2019 HOH F O   1 
HETATM 12202 O O   . HOH JA 9 .   ? 44.269  52.436 63.313  1.00 28.69  ? 2020 HOH F O   1 
HETATM 12203 O O   . HOH JA 9 .   ? 30.499  52.057 40.291  0.33 2.00   ? 2021 HOH F O   1 
HETATM 12204 O O   . HOH JA 9 .   ? 38.548  53.278 23.572  1.00 13.19  ? 2022 HOH F O   1 
HETATM 12205 O O   . HOH JA 9 .   ? 26.746  52.545 22.800  1.00 19.07  ? 2023 HOH F O   1 
HETATM 12206 O O   . HOH JA 9 .   ? 38.670  56.571 1.329   1.00 9.83   ? 2024 HOH F O   1 
HETATM 12207 O O   . HOH JA 9 .   ? 25.791  64.166 3.313   1.00 11.31  ? 2025 HOH F O   1 
HETATM 12208 O O   . HOH JA 9 .   ? 28.462  55.222 -5.470  1.00 21.67  ? 2026 HOH F O   1 
HETATM 12209 O O   . HOH JA 9 .   ? 29.487  68.622 -18.025 1.00 21.92  ? 2027 HOH F O   1 
HETATM 12210 O O   . HOH JA 9 .   ? -3.827  60.758 23.606  1.00 29.53  ? 2030 HOH F O   1 
HETATM 12211 O O   . HOH JA 9 .   ? 54.411  75.808 23.295  1.00 36.53  ? 2031 HOH F O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ASP A 1   ? 0.1096 0.8862 0.3138 -0.0053 -0.0974 -0.1405 1   ASP A N   
2     C CA  . ASP A 1   ? 0.1137 0.8949 0.3173 -0.0420 -0.0933 -0.1493 1   ASP A CA  
3     C C   . ASP A 1   ? 0.1126 0.7834 0.3119 -0.0407 -0.0887 -0.1453 1   ASP A C   
4     O O   . ASP A 1   ? 0.1141 0.7049 0.3057 -0.0355 -0.0878 -0.1418 1   ASP A O   
5     C CB  . ASP A 1   ? 0.1362 0.9429 0.3231 -0.1044 -0.0910 -0.1669 1   ASP A CB  
6     C CG  . ASP A 1   ? 0.1387 1.0697 0.3294 -0.1135 -0.0960 -0.1723 1   ASP A CG  
7     O OD1 . ASP A 1   ? 0.1216 1.1236 0.3292 -0.0652 -0.1008 -0.1611 1   ASP A OD1 
8     O OD2 . ASP A 1   ? 0.1640 1.1208 0.3353 -0.1692 -0.0939 -0.1878 1   ASP A OD2 
9     N N   . GLN A 2   ? 0.1094 0.7843 0.3138 -0.0445 -0.0857 -0.1452 2   GLN A N   
10    C CA  . GLN A 2   ? 0.1081 0.6904 0.3090 -0.0431 -0.0814 -0.1411 2   GLN A CA  
11    C C   . GLN A 2   ? 0.1128 0.7043 0.3127 -0.0699 -0.0768 -0.1473 2   GLN A C   
12    O O   . GLN A 2   ? 0.1101 0.7867 0.3183 -0.0747 -0.0776 -0.1505 2   GLN A O   
13    C CB  . GLN A 2   ? 0.0966 0.6446 0.3041 0.0064  -0.0830 -0.1265 2   GLN A CB  
14    C CG  . GLN A 2   ? 0.0938 0.6977 0.3081 0.0376  -0.0831 -0.1203 2   GLN A CG  
15    C CD  . GLN A 2   ? 0.0982 0.6398 0.3042 0.0778  -0.0813 -0.1077 2   GLN A CD  
16    O OE1 . GLN A 2   ? 0.1025 0.6456 0.3069 0.0930  -0.0784 -0.1040 2   GLN A OE1 
17    N NE2 . GLN A 2   ? 0.1033 0.5892 0.2994 0.0926  -0.0821 -0.1013 2   GLN A NE2 
18    N N   . ILE A 3   ? 0.1214 0.6286 0.3095 -0.0853 -0.0714 -0.1479 3   ILE A N   
19    C CA  . ILE A 3   ? 0.1280 0.6259 0.3124 -0.1057 -0.0661 -0.1516 3   ILE A CA  
20    C C   . ILE A 3   ? 0.1144 0.5472 0.3054 -0.0773 -0.0652 -0.1407 3   ILE A C   
21    O O   . ILE A 3   ? 0.1132 0.4824 0.2992 -0.0643 -0.0652 -0.1347 3   ILE A O   
22    C CB  . ILE A 3   ? 0.1652 0.6213 0.3174 -0.1566 -0.0577 -0.1637 3   ILE A CB  
23    C CG1 . ILE A 3   ? 0.1770 0.6420 0.3228 -0.1821 -0.0517 -0.1687 3   ILE A CG1 
24    C CG2 . ILE A 3   ? 0.1807 0.5336 0.3120 -0.1517 -0.0528 -0.1597 3   ILE A CG2 
25    C CD1 . ILE A 3   ? 0.2276 0.6664 0.3313 -0.2393 -0.0417 -0.1828 3   ILE A CD1 
26    N N   . CYS A 4   ? 0.1063 0.5613 0.3071 -0.0693 -0.0643 -0.1384 4   CYS A N   
27    C CA  . CYS A 4   ? 0.0970 0.4979 0.3017 -0.0456 -0.0634 -0.1292 4   CYS A CA  
28    C C   . CYS A 4   ? 0.1041 0.4813 0.3025 -0.0691 -0.0574 -0.1329 4   CYS A C   
29    O O   . CYS A 4   ? 0.1153 0.5337 0.3092 -0.0979 -0.0543 -0.1416 4   CYS A O   
30    C CB  . CYS A 4   ? 0.0881 0.5244 0.3030 -0.0065 -0.0666 -0.1212 4   CYS A CB  
31    S SG  . CYS A 4   ? 0.0898 0.5575 0.3041 0.0274  -0.0716 -0.1153 4   CYS A SG  
32    N N   . ILE A 5   ? 0.0998 0.4142 0.2955 -0.0584 -0.0555 -0.1261 5   ILE A N   
33    C CA  . ILE A 5   ? 0.1056 0.3959 0.2957 -0.0724 -0.0499 -0.1271 5   ILE A CA  
34    C C   . ILE A 5   ? 0.0890 0.3872 0.2922 -0.0457 -0.0522 -0.1201 5   ILE A C   
35    O O   . ILE A 5   ? 0.0817 0.3588 0.2872 -0.0197 -0.0556 -0.1125 5   ILE A O   
36    C CB  . ILE A 5   ? 0.1199 0.3360 0.2919 -0.0790 -0.0446 -0.1239 5   ILE A CB  
37    C CG1 . ILE A 5   ? 0.1464 0.3401 0.2951 -0.0996 -0.0405 -0.1299 5   ILE A CG1 
38    C CG2 . ILE A 5   ? 0.1321 0.3235 0.2939 -0.0919 -0.0377 -0.1244 5   ILE A CG2 
39    C CD1 . ILE A 5   ? 0.1785 0.3840 0.3044 -0.1387 -0.0333 -0.1418 5   ILE A CD1 
40    N N   . GLY A 6   ? 0.0891 0.4142 0.2952 -0.0547 -0.0493 -0.1232 6   GLY A N   
41    C CA  . GLY A 6   ? 0.0800 0.4134 0.2931 -0.0295 -0.0502 -0.1176 6   GLY A CA  
42    C C   . GLY A 6   ? 0.0825 0.4261 0.2959 -0.0455 -0.0455 -0.1209 6   GLY A C   
43    O O   . GLY A 6   ? 0.0943 0.4332 0.2992 -0.0780 -0.0407 -0.1273 6   GLY A O   
44    N N   . TYR A 7   ? 0.0781 0.4306 0.2950 -0.0227 -0.0455 -0.1165 7   TYR A N   
45    C CA  . TYR A 7   ? 0.0798 0.4336 0.2969 -0.0337 -0.0412 -0.1179 7   TYR A CA  
46    C C   . TYR A 7   ? 0.0797 0.4927 0.3019 -0.0118 -0.0408 -0.1169 7   TYR A C   
47    O O   . TYR A 7   ? 0.0825 0.5217 0.3027 0.0198  -0.0431 -0.1128 7   TYR A O   
48    C CB  . TYR A 7   ? 0.0796 0.3642 0.2900 -0.0288 -0.0399 -0.1123 7   TYR A CB  
49    C CG  . TYR A 7   ? 0.0805 0.3352 0.2846 0.0008  -0.0429 -0.1052 7   TYR A CG  
50    C CD1 . TYR A 7   ? 0.0806 0.3038 0.2798 0.0063  -0.0461 -0.1016 7   TYR A CD1 
51    C CD2 . TYR A 7   ? 0.0891 0.3416 0.2853 0.0210  -0.0413 -0.1023 7   TYR A CD2 
52    C CE1 . TYR A 7   ? 0.0916 0.2817 0.2764 0.0266  -0.0472 -0.0959 7   TYR A CE1 
53    C CE2 . TYR A 7   ? 0.1052 0.3168 0.2822 0.0429  -0.0415 -0.0969 7   TYR A CE2 
54    C CZ  . TYR A 7   ? 0.1076 0.2877 0.2780 0.0433  -0.0444 -0.0940 7   TYR A CZ  
55    O OH  . TYR A 7   ? 0.1333 0.2678 0.2765 0.0589  -0.0431 -0.0893 7   TYR A OH  
56    N N   . HIS A 8   ? 0.0814 0.5133 0.3059 -0.0263 -0.0368 -0.1197 8   HIS A N   
57    C CA  . HIS A 8   ? 0.0830 0.5831 0.3121 -0.0088 -0.0353 -0.1191 8   HIS A CA  
58    C C   . HIS A 8   ? 0.0924 0.5612 0.3099 0.0342  -0.0345 -0.1111 8   HIS A C   
59    O O   . HIS A 8   ? 0.0962 0.4913 0.3042 0.0359  -0.0341 -0.1081 8   HIS A O   
60    C CB  . HIS A 8   ? 0.0847 0.6055 0.3164 -0.0417 -0.0303 -0.1246 8   HIS A CB  
61    C CG  . HIS A 8   ? 0.0849 0.6884 0.3230 -0.0280 -0.0283 -0.1243 8   HIS A CG  
62    N ND1 . HIS A 8   ? 0.0838 0.7882 0.3299 -0.0247 -0.0296 -0.1264 8   HIS A ND1 
63    C CD2 . HIS A 8   ? 0.0873 0.6944 0.3240 -0.0161 -0.0247 -0.1218 8   HIS A CD2 
64    C CE1 . HIS A 8   ? 0.0855 0.8558 0.3351 -0.0086 -0.0266 -0.1243 8   HIS A CE1 
65    N NE2 . HIS A 8   ? 0.0880 0.7968 0.3316 -0.0032 -0.0235 -0.1218 8   HIS A NE2 
66    N N   . ALA A 9   ? 0.1031 0.6289 0.3157 0.0694  -0.0334 -0.1075 9   ALA A N   
67    C CA  . ALA A 9   ? 0.1269 0.6240 0.3165 0.1111  -0.0291 -0.1006 9   ALA A CA  
68    C C   . ALA A 9   ? 0.1327 0.7206 0.3255 0.1307  -0.0254 -0.0996 9   ALA A C   
69    O O   . ALA A 9   ? 0.1183 0.7981 0.3307 0.1149  -0.0271 -0.1035 9   ALA A O   
70    C CB  . ALA A 9   ? 0.1520 0.6070 0.3151 0.1489  -0.0286 -0.0939 9   ALA A CB  
71    N N   . ASN A 10  ? 0.1576 0.7232 0.3284 0.1630  -0.0196 -0.0947 10  ASN A N   
72    C CA  . ASN A 10  ? 0.1672 0.8209 0.3376 0.1889  -0.0150 -0.0921 10  ASN A CA  
73    C C   . ASN A 10  ? 0.2132 0.8188 0.3414 0.2421  -0.0067 -0.0841 10  ASN A C   
74    O O   . ASN A 10  ? 0.2410 0.7426 0.3372 0.2540  -0.0044 -0.0815 10  ASN A O   
75    C CB  . ASN A 10  ? 0.1410 0.8434 0.3391 0.1442  -0.0154 -0.0993 10  ASN A CB  
76    C CG  . ASN A 10  ? 0.1424 0.7605 0.3337 0.1283  -0.0132 -0.1007 10  ASN A CG  
77    O OD1 . ASN A 10  ? 0.1637 0.6950 0.3291 0.1498  -0.0113 -0.0968 10  ASN A OD1 
78    N ND2 . ASN A 10  ? 0.1244 0.7686 0.3348 0.0879  -0.0128 -0.1065 10  ASN A ND2 
79    N N   . ASN A 11  ? 0.2277 0.9091 0.3511 0.2721  -0.0011 -0.0803 11  ASN A N   
80    C CA  . ASN A 11  ? 0.2827 0.9216 0.3567 0.3294  0.0092  -0.0721 11  ASN A CA  
81    C C   . ASN A 11  ? 0.2893 0.8651 0.3541 0.3141  0.0126  -0.0752 11  ASN A C   
82    O O   . ASN A 11  ? 0.3319 0.8922 0.3589 0.3567  0.0221  -0.0698 11  ASN A O   
83    C CB  . ASN A 11  ? 0.3010 1.0587 0.3678 0.3811  0.0149  -0.0642 11  ASN A CB  
84    C CG  . ASN A 11  ? 0.2626 1.1416 0.3724 0.3516  0.0123  -0.0688 11  ASN A CG  
85    O OD1 . ASN A 11  ? 0.2292 1.0907 0.3683 0.2946  0.0077  -0.0778 11  ASN A OD1 
86    N ND2 . ASN A 11  ? 0.2722 1.2778 0.3817 0.3913  0.0163  -0.0620 11  ASN A ND2 
87    N N   . SER A 12  ? 0.2525 0.7904 0.3470 0.2569  0.0060  -0.0832 12  SER A N   
88    C CA  . SER A 12  ? 0.2542 0.7370 0.3438 0.2378  0.0081  -0.0863 12  SER A CA  
89    C C   . SER A 12  ? 0.3027 0.6640 0.3412 0.2563  0.0133  -0.0838 12  SER A C   
90    O O   . SER A 12  ? 0.3180 0.6211 0.3384 0.2575  0.0118  -0.0827 12  SER A O   
91    C CB  . SER A 12  ? 0.2074 0.6847 0.3373 0.1760  0.0007  -0.0939 12  SER A CB  
92    O OG  . SER A 12  ? 0.2085 0.6367 0.3337 0.1593  0.0028  -0.0958 12  SER A OG  
93    N N   . THR A 13  ? 0.3313 0.6559 0.3435 0.2675  0.0199  -0.0835 13  THR A N   
94    C CA  . THR A 13  ? 0.3838 0.5904 0.3415 0.2740  0.0258  -0.0833 13  THR A CA  
95    C C   . THR A 13  ? 0.3635 0.5345 0.3358 0.2315  0.0227  -0.0890 13  THR A C   
96    O O   . THR A 13  ? 0.4067 0.4911 0.3347 0.2300  0.0276  -0.0901 13  THR A O   
97    C CB  . THR A 13  ? 0.4580 0.6335 0.3500 0.3330  0.0398  -0.0773 13  THR A CB  
98    O OG1 . THR A 13  ? 0.4433 0.7005 0.3548 0.3483  0.0426  -0.0762 13  THR A OG1 
99    C CG2 . THR A 13  ? 0.4979 0.6791 0.3561 0.3820  0.0454  -0.0698 13  THR A CG2 
100   N N   . GLU A 14  ? 0.3053 0.5405 0.3334 0.1962  0.0156  -0.0925 14  GLU A N   
101   C CA  . GLU A 14  ? 0.2857 0.4932 0.3282 0.1590  0.0130  -0.0964 14  GLU A CA  
102   C C   . GLU A 14  ? 0.2851 0.4208 0.3198 0.1313  0.0083  -0.0978 14  GLU A C   
103   O O   . GLU A 14  ? 0.2672 0.4060 0.3177 0.1202  0.0030  -0.0975 14  GLU A O   
104   C CB  . GLU A 14  ? 0.2346 0.5154 0.3290 0.1270  0.0083  -0.0991 14  GLU A CB  
105   C CG  . GLU A 14  ? 0.2334 0.5934 0.3377 0.1427  0.0128  -0.0986 14  GLU A CG  
106   C CD  . GLU A 14  ? 0.2074 0.5922 0.3385 0.1071  0.0123  -0.1018 14  GLU A CD  
107   O OE1 . GLU A 14  ? 0.2198 0.5586 0.3363 0.1043  0.0148  -0.1020 14  GLU A OE1 
108   O OE2 . GLU A 14  ? 0.1808 0.6267 0.3422 0.0799  0.0104  -0.1043 14  GLU A OE2 
109   N N   . GLN A 15  ? 0.3058 0.3839 0.3156 0.1191  0.0105  -0.0994 15  GLN A N   
110   C CA  . GLN A 15  ? 0.3097 0.3310 0.3083 0.0912  0.0067  -0.1004 15  GLN A CA  
111   C C   . GLN A 15  ? 0.2753 0.3080 0.3018 0.0579  0.0024  -0.1015 15  GLN A C   
112   O O   . GLN A 15  ? 0.2665 0.3233 0.3027 0.0582  0.0048  -0.1023 15  GLN A O   
113   C CB  . GLN A 15  ? 0.3792 0.3178 0.3108 0.1021  0.0143  -0.1014 15  GLN A CB  
114   C CG  . GLN A 15  ? 0.4304 0.3426 0.3180 0.1434  0.0221  -0.0987 15  GLN A CG  
115   C CD  . GLN A 15  ? 0.5156 0.3259 0.3214 0.1505  0.0326  -0.1001 15  GLN A CD  
116   O OE1 . GLN A 15  ? 0.5616 0.3207 0.3246 0.1635  0.0373  -0.0983 15  GLN A OE1 
117   N NE2 . GLN A 15  ? 0.5442 0.3194 0.3219 0.1398  0.0373  -0.1037 15  GLN A NE2 
118   N N   . VAL A 16  ? 0.2579 0.2763 0.2948 0.0318  -0.0032 -0.1007 16  VAL A N   
119   C CA  . VAL A 16  ? 0.2338 0.2610 0.2892 0.0056  -0.0063 -0.0997 16  VAL A CA  
120   C C   . VAL A 16  ? 0.2535 0.2426 0.2846 -0.0143 -0.0086 -0.0993 16  VAL A C   
121   O O   . VAL A 16  ? 0.2741 0.2354 0.2851 -0.0136 -0.0092 -0.0995 16  VAL A O   
122   C CB  . VAL A 16  ? 0.1886 0.2585 0.2870 -0.0058 -0.0103 -0.0970 16  VAL A CB  
123   C CG1 . VAL A 16  ? 0.1745 0.2873 0.2928 0.0043  -0.0075 -0.0986 16  VAL A CG1 
124   C CG2 . VAL A 16  ? 0.1785 0.2442 0.2843 -0.0106 -0.0148 -0.0951 16  VAL A CG2 
125   N N   . ASP A 17  ? 0.2499 0.2426 0.2811 -0.0334 -0.0097 -0.0986 17  ASP A N   
126   C CA  . ASP A 17  ? 0.2652 0.2415 0.2766 -0.0584 -0.0124 -0.0980 17  ASP A CA  
127   C C   . ASP A 17  ? 0.2241 0.2434 0.2715 -0.0695 -0.0182 -0.0914 17  ASP A C   
128   O O   . ASP A 17  ? 0.1920 0.2425 0.2705 -0.0622 -0.0183 -0.0878 17  ASP A O   
129   C CB  . ASP A 17  ? 0.2939 0.2541 0.2766 -0.0730 -0.0094 -0.1010 17  ASP A CB  
130   C CG  . ASP A 17  ? 0.3549 0.2541 0.2827 -0.0636 -0.0014 -0.1076 17  ASP A CG  
131   O OD1 . ASP A 17  ? 0.3897 0.2470 0.2864 -0.0543 0.0018  -0.1093 17  ASP A OD1 
132   O OD2 . ASP A 17  ? 0.3745 0.2629 0.2844 -0.0636 0.0026  -0.1105 17  ASP A OD2 
133   N N   . THR A 18  ? 0.2330 0.2507 0.2691 -0.0869 -0.0216 -0.0897 18  THR A N   
134   C CA  . THR A 18  ? 0.2041 0.2651 0.2649 -0.0950 -0.0262 -0.0821 18  THR A CA  
135   C C   . THR A 18  ? 0.2272 0.2993 0.2636 -0.1231 -0.0282 -0.0816 18  THR A C   
136   O O   . THR A 18  ? 0.2686 0.3046 0.2660 -0.1394 -0.0255 -0.0885 18  THR A O   
137   C CB  . THR A 18  ? 0.1884 0.2521 0.2636 -0.0877 -0.0289 -0.0795 18  THR A CB  
138   O OG1 . THR A 18  ? 0.2185 0.2536 0.2638 -0.1016 -0.0297 -0.0829 18  THR A OG1 
139   C CG2 . THR A 18  ? 0.1751 0.2293 0.2670 -0.0662 -0.0269 -0.0820 18  THR A CG2 
140   N N   . ILE A 19  ? 0.2081 0.3308 0.2616 -0.1291 -0.0320 -0.0735 19  ILE A N   
141   C CA  . ILE A 19  ? 0.2277 0.3824 0.2610 -0.1591 -0.0346 -0.0723 19  ILE A CA  
142   C C   . ILE A 19  ? 0.2683 0.3876 0.2651 -0.1853 -0.0346 -0.0788 19  ILE A C   
143   O O   . ILE A 19  ? 0.3117 0.4085 0.2664 -0.2160 -0.0324 -0.0856 19  ILE A O   
144   C CB  . ILE A 19  ? 0.1977 0.4257 0.2568 -0.1527 -0.0380 -0.0599 19  ILE A CB  
145   C CG1 . ILE A 19  ? 0.1752 0.4291 0.2562 -0.1273 -0.0353 -0.0524 19  ILE A CG1 
146   C CG2 . ILE A 19  ? 0.2157 0.4944 0.2549 -0.1868 -0.0413 -0.0583 19  ILE A CG2 
147   C CD1 . ILE A 19  ? 0.1871 0.4640 0.2556 -0.1407 -0.0347 -0.0531 19  ILE A CD1 
148   N N   . MET A 20  ? 0.2614 0.3699 0.2686 -0.1747 -0.0360 -0.0770 20  MET A N   
149   C CA  . MET A 20  ? 0.3011 0.3783 0.2732 -0.1986 -0.0355 -0.0812 20  MET A CA  
150   C C   . MET A 20  ? 0.3502 0.3410 0.2825 -0.1927 -0.0291 -0.0901 20  MET A C   
151   O O   . MET A 20  ? 0.4018 0.3472 0.2859 -0.2164 -0.0255 -0.0950 20  MET A O   
152   C CB  . MET A 20  ? 0.2710 0.3784 0.2704 -0.1882 -0.0396 -0.0743 20  MET A CB  
153   C CG  . MET A 20  ? 0.2386 0.4306 0.2658 -0.1904 -0.0442 -0.0638 20  MET A CG  
154   S SD  . MET A 20  ? 0.2222 0.4399 0.2646 -0.1851 -0.0475 -0.0571 20  MET A SD  
155   C CE  . MET A 20  ? 0.1832 0.4937 0.2608 -0.1630 -0.0497 -0.0421 20  MET A CE  
156   N N   . GLU A 21  ? 0.3416 0.3107 0.2892 -0.1604 -0.0265 -0.0916 21  GLU A N   
157   C CA  . GLU A 21  ? 0.3879 0.2863 0.2994 -0.1436 -0.0197 -0.0975 21  GLU A CA  
158   C C   . GLU A 21  ? 0.3933 0.2799 0.3076 -0.1203 -0.0155 -0.1002 21  GLU A C   
159   O O   . GLU A 21  ? 0.3436 0.2769 0.3047 -0.1052 -0.0188 -0.0966 21  GLU A O   
160   C CB  . GLU A 21  ? 0.3668 0.2641 0.2994 -0.1197 -0.0214 -0.0946 21  GLU A CB  
161   C CG  . GLU A 21  ? 0.4238 0.2488 0.3058 -0.1055 -0.0138 -0.0987 21  GLU A CG  
162   C CD  . GLU A 21  ? 0.4028 0.2349 0.3061 -0.0832 -0.0161 -0.0954 21  GLU A CD  
163   O OE1 . GLU A 21  ? 0.3490 0.2348 0.3004 -0.0855 -0.0236 -0.0908 21  GLU A OE1 
164   O OE2 . GLU A 21  ? 0.4444 0.2266 0.3114 -0.0608 -0.0095 -0.0969 21  GLU A OE2 
165   N N   . LYS A 22  ? 0.4636 0.2830 0.3208 -0.1173 -0.0069 -0.1063 22  LYS A N   
166   C CA  . LYS A 22  ? 0.4792 0.2851 0.3311 -0.0926 -0.0016 -0.1088 22  LYS A CA  
167   C C   . LYS A 22  ? 0.5102 0.2806 0.3437 -0.0535 0.0047  -0.1089 22  LYS A C   
168   O O   . LYS A 22  ? 0.5445 0.2751 0.3470 -0.0495 0.0077  -0.1087 22  LYS A O   
169   C CB  . LYS A 22  ? 0.5401 0.2997 0.3348 -0.1157 0.0049  -0.1150 22  LYS A CB  
170   C CG  . LYS A 22  ? 0.5075 0.3239 0.3305 -0.1453 -0.0015 -0.1138 22  LYS A CG  
171   C CD  . LYS A 22  ? 0.5755 0.3506 0.3348 -0.1848 0.0035  -0.1209 22  LYS A CD  
172   C CE  . LYS A 22  ? 0.6444 0.3422 0.3435 -0.1698 0.0152  -0.1278 22  LYS A CE  
173   N NZ  . LYS A 22  ? 0.7034 0.3697 0.3458 -0.2101 0.0200  -0.1354 22  LYS A NZ  
174   N N   . ASN A 23  ? 0.5035 0.2945 0.3553 -0.0239 0.0071  -0.1085 23  ASN A N   
175   C CA  . ASN A 23  ? 0.5326 0.3091 0.3689 0.0184  0.0135  -0.1074 23  ASN A CA  
176   C C   . ASN A 23  ? 0.4874 0.2950 0.3563 0.0310  0.0083  -0.1034 23  ASN A C   
177   O O   . ASN A 23  ? 0.5267 0.2968 0.3588 0.0545  0.0141  -0.1022 23  ASN A O   
178   C CB  . ASN A 23  ? 0.6483 0.3302 0.3951 0.0311  0.0268  -0.1105 23  ASN A CB  
179   C CG  . ASN A 23  ? 0.7133 0.3632 0.4234 0.0258  0.0336  -0.1149 23  ASN A CG  
180   O OD1 . ASN A 23  ? 0.6666 0.3725 0.4224 0.0248  0.0290  -0.1147 23  ASN A OD1 
181   N ND2 . ASN A 23  ? 0.8449 0.3971 0.4649 0.0212  0.0460  -0.1193 23  ASN A ND2 
182   N N   . VAL A 24  ? 0.4075 0.2794 0.3397 0.0165  -0.0012 -0.1011 24  VAL A N   
183   C CA  . VAL A 24  ? 0.3643 0.2713 0.3311 0.0251  -0.0064 -0.0982 24  VAL A CA  
184   C C   . VAL A 24  ? 0.3357 0.2919 0.3291 0.0542  -0.0053 -0.0975 24  VAL A C   
185   O O   . VAL A 24  ? 0.3014 0.3016 0.3278 0.0494  -0.0068 -0.0981 24  VAL A O   
186   C CB  . VAL A 24  ? 0.3095 0.2580 0.3233 -0.0014 -0.0150 -0.0959 24  VAL A CB  
187   C CG1 . VAL A 24  ? 0.2758 0.2588 0.3228 0.0072  -0.0192 -0.0939 24  VAL A CG1 
188   C CG2 . VAL A 24  ? 0.3273 0.2481 0.3190 -0.0300 -0.0169 -0.0954 24  VAL A CG2 
189   N N   . THR A 25  ? 0.3508 0.3037 0.3273 0.0831  -0.0021 -0.0960 25  THR A N   
190   C CA  . THR A 25  ? 0.3288 0.3431 0.3278 0.1108  -0.0009 -0.0949 25  THR A CA  
191   C C   . THR A 25  ? 0.2661 0.3452 0.3216 0.0923  -0.0089 -0.0955 25  THR A C   
192   O O   . THR A 25  ? 0.2537 0.3272 0.3184 0.0825  -0.0135 -0.0946 25  THR A O   
193   C CB  . THR A 25  ? 0.3726 0.3724 0.3336 0.1521  0.0053  -0.0915 25  THR A CB  
194   O OG1 . THR A 25  ? 0.4460 0.3596 0.3371 0.1671  0.0153  -0.0910 25  THR A OG1 
195   C CG2 . THR A 25  ? 0.3613 0.4367 0.3397 0.1837  0.0079  -0.0896 25  THR A CG2 
196   N N   . VAL A 26  ? 0.2323 0.3681 0.3193 0.0861  -0.0094 -0.0972 26  VAL A N   
197   C CA  . VAL A 26  ? 0.1869 0.3733 0.3155 0.0632  -0.0142 -0.0989 26  VAL A CA  
198   C C   . VAL A 26  ? 0.1757 0.4374 0.3203 0.0752  -0.0126 -0.1003 26  VAL A C   
199   O O   . VAL A 26  ? 0.1947 0.4797 0.3251 0.1021  -0.0078 -0.0990 26  VAL A O   
200   C CB  . VAL A 26  ? 0.1649 0.3473 0.3113 0.0329  -0.0150 -0.1001 26  VAL A CB  
201   C CG1 . VAL A 26  ? 0.1691 0.2977 0.3044 0.0196  -0.0175 -0.0977 26  VAL A CG1 
202   C CG2 . VAL A 26  ? 0.1712 0.3693 0.3145 0.0371  -0.0103 -0.1011 26  VAL A CG2 
203   N N   . THR A 27  ? 0.1484 0.4507 0.3189 0.0542  -0.0160 -0.1029 27  THR A N   
204   C CA  . THR A 27  ? 0.1391 0.5250 0.3249 0.0564  -0.0152 -0.1052 27  THR A CA  
205   C C   . THR A 27  ? 0.1306 0.5574 0.3280 0.0374  -0.0114 -0.1083 27  THR A C   
206   O O   . THR A 27  ? 0.1333 0.6339 0.3355 0.0489  -0.0089 -0.1087 27  THR A O   
207   C CB  . THR A 27  ? 0.1225 0.5355 0.3250 0.0335  -0.0191 -0.1086 27  THR A CB  
208   O OG1 . THR A 27  ? 0.1120 0.4972 0.3225 -0.0057 -0.0188 -0.1120 27  THR A OG1 
209   C CG2 . THR A 27  ? 0.1288 0.5038 0.3210 0.0513  -0.0228 -0.1054 27  THR A CG2 
210   N N   . HIS A 28  ? 0.1231 0.5073 0.3231 0.0095  -0.0106 -0.1096 28  HIS A N   
211   C CA  . HIS A 28  ? 0.1204 0.5309 0.3261 -0.0105 -0.0059 -0.1120 28  HIS A CA  
212   C C   . HIS A 28  ? 0.1243 0.4716 0.3209 -0.0149 -0.0044 -0.1096 28  HIS A C   
213   O O   . HIS A 28  ? 0.1238 0.4146 0.3151 -0.0192 -0.0070 -0.1073 28  HIS A O   
214   C CB  . HIS A 28  ? 0.1160 0.5528 0.3299 -0.0520 -0.0040 -0.1174 28  HIS A CB  
215   C CG  . HIS A 28  ? 0.1126 0.6187 0.3350 -0.0559 -0.0059 -0.1209 28  HIS A CG  
216   N ND1 . HIS A 28  ? 0.1086 0.6001 0.3318 -0.0520 -0.0105 -0.1209 28  HIS A ND1 
217   C CD2 . HIS A 28  ? 0.1126 0.7116 0.3431 -0.0635 -0.0039 -0.1243 28  HIS A CD2 
218   C CE1 . HIS A 28  ? 0.1069 0.6769 0.3380 -0.0570 -0.0115 -0.1244 28  HIS A CE1 
219   N NE2 . HIS A 28  ? 0.1090 0.7496 0.3449 -0.0646 -0.0076 -0.1264 28  HIS A NE2 
220   N N   . ALA A 29  ? 0.1290 0.4937 0.3241 -0.0141 -0.0002 -0.1097 29  ALA A N   
221   C CA  . ALA A 29  ? 0.1338 0.4480 0.3200 -0.0179 0.0014  -0.1074 29  ALA A CA  
222   C C   . ALA A 29  ? 0.1354 0.4801 0.3256 -0.0351 0.0072  -0.1091 29  ALA A C   
223   O O   . ALA A 29  ? 0.1346 0.5428 0.3331 -0.0438 0.0098  -0.1123 29  ALA A O   
224   C CB  . ALA A 29  ? 0.1495 0.4317 0.3168 0.0127  0.0007  -0.1049 29  ALA A CB  
225   N N   . GLN A 30  ? 0.1398 0.4442 0.3227 -0.0417 0.0093  -0.1068 30  GLN A N   
226   C CA  . GLN A 30  ? 0.1449 0.4699 0.3276 -0.0563 0.0154  -0.1076 30  GLN A CA  
227   C C   . GLN A 30  ? 0.1505 0.4433 0.3233 -0.0429 0.0161  -0.1046 30  GLN A C   
228   O O   . GLN A 30  ? 0.1513 0.3968 0.3172 -0.0481 0.0151  -0.1012 30  GLN A O   
229   C CB  . GLN A 30  ? 0.1532 0.4596 0.3304 -0.0909 0.0206  -0.1081 30  GLN A CB  
230   C CG  . GLN A 30  ? 0.1656 0.4943 0.3371 -0.1113 0.0287  -0.1095 30  GLN A CG  
231   C CD  . GLN A 30  ? 0.1901 0.4956 0.3428 -0.1486 0.0370  -0.1111 30  GLN A CD  
232   O OE1 . GLN A 30  ? 0.1981 0.4928 0.3448 -0.1623 0.0369  -0.1135 30  GLN A OE1 
233   N NE2 . GLN A 30  ? 0.2103 0.5017 0.3470 -0.1656 0.0455  -0.1100 30  GLN A NE2 
234   N N   . ASP A 31  ? 0.1568 0.4804 0.3268 -0.0244 0.0183  -0.1055 31  ASP A N   
235   C CA  . ASP A 31  ? 0.1672 0.4649 0.3244 -0.0147 0.0204  -0.1040 31  ASP A CA  
236   C C   . ASP A 31  ? 0.1647 0.4633 0.3257 -0.0405 0.0252  -0.1029 31  ASP A C   
237   O O   . ASP A 31  ? 0.1638 0.5041 0.3323 -0.0588 0.0298  -0.1048 31  ASP A O   
238   C CB  . ASP A 31  ? 0.1818 0.5129 0.3295 0.0145  0.0236  -0.1049 31  ASP A CB  
239   C CG  . ASP A 31  ? 0.2023 0.4915 0.3268 0.0287  0.0256  -0.1043 31  ASP A CG  
240   O OD1 . ASP A 31  ? 0.1991 0.4539 0.3223 0.0106  0.0248  -0.1032 31  ASP A OD1 
241   O OD2 . ASP A 31  ? 0.2279 0.5181 0.3305 0.0598  0.0290  -0.1046 31  ASP A OD2 
242   N N   . ILE A 32  ? 0.1680 0.4221 0.3197 -0.0435 0.0249  -0.0995 32  ILE A N   
243   C CA  . ILE A 32  ? 0.1730 0.4181 0.3211 -0.0622 0.0306  -0.0966 32  ILE A CA  
244   C C   . ILE A 32  ? 0.1803 0.4197 0.3198 -0.0531 0.0324  -0.0954 32  ILE A C   
245   O O   . ILE A 32  ? 0.1867 0.4163 0.3205 -0.0647 0.0373  -0.0921 32  ILE A O   
246   C CB  . ILE A 32  ? 0.1752 0.3778 0.3164 -0.0727 0.0304  -0.0914 32  ILE A CB  
247   C CG1 . ILE A 32  ? 0.1696 0.3459 0.3080 -0.0587 0.0229  -0.0890 32  ILE A CG1 
248   C CG2 . ILE A 32  ? 0.1777 0.3820 0.3204 -0.0878 0.0322  -0.0930 32  ILE A CG2 
249   C CD1 . ILE A 32  ? 0.1735 0.3217 0.3035 -0.0625 0.0234  -0.0815 32  ILE A CD1 
250   N N   . LEU A 33  ? 0.1865 0.4271 0.3190 -0.0315 0.0298  -0.0981 33  LEU A N   
251   C CA  . LEU A 33  ? 0.2000 0.4300 0.3182 -0.0223 0.0318  -0.0982 33  LEU A CA  
252   C C   . LEU A 33  ? 0.2089 0.4810 0.3263 -0.0075 0.0369  -0.1009 33  LEU A C   
253   O O   . LEU A 33  ? 0.2170 0.5058 0.3294 0.0140  0.0368  -0.1030 33  LEU A O   
254   C CB  . LEU A 33  ? 0.2157 0.4031 0.3121 -0.0104 0.0275  -0.0997 33  LEU A CB  
255   C CG  . LEU A 33  ? 0.2371 0.4026 0.3100 -0.0059 0.0295  -0.1010 33  LEU A CG  
256   C CD1 . LEU A 33  ? 0.2267 0.3900 0.3061 -0.0243 0.0291  -0.0965 33  LEU A CD1 
257   C CD2 . LEU A 33  ? 0.2674 0.3858 0.3069 0.0012  0.0274  -0.1046 33  LEU A CD2 
258   N N   . GLU A 34  ? 0.2113 0.5031 0.3310 -0.0161 0.0421  -0.0999 34  GLU A N   
259   C CA  . GLU A 34  ? 0.2208 0.5592 0.3388 -0.0008 0.0474  -0.1015 34  GLU A CA  
260   C C   . GLU A 34  ? 0.2467 0.5529 0.3372 0.0251  0.0485  -0.1029 34  GLU A C   
261   O O   . GLU A 34  ? 0.2535 0.5242 0.3329 0.0172  0.0482  -0.1023 34  GLU A O   
262   C CB  . GLU A 34  ? 0.2164 0.5874 0.3439 -0.0236 0.0536  -0.1001 34  GLU A CB  
263   C CG  . GLU A 34  ? 0.2236 0.6556 0.3516 -0.0097 0.0593  -0.1012 34  GLU A CG  
264   C CD  . GLU A 34  ? 0.2236 0.7106 0.3569 0.0121  0.0588  -0.1027 34  GLU A CD  
265   O OE1 . GLU A 34  ? 0.2112 0.7414 0.3613 -0.0078 0.0584  -0.1037 34  GLU A OE1 
266   O OE2 . GLU A 34  ? 0.2425 0.7264 0.3576 0.0505  0.0598  -0.1026 34  GLU A OE2 
267   N N   . LYS A 35  ? 0.2684 0.5863 0.3424 0.0572  0.0508  -0.1044 35  LYS A N   
268   C CA  . LYS A 35  ? 0.3104 0.5785 0.3424 0.0842  0.0541  -0.1064 35  LYS A CA  
269   C C   . LYS A 35  ? 0.3335 0.6347 0.3500 0.1114  0.0625  -0.1060 35  LYS A C   
270   O O   . LYS A 35  ? 0.3759 0.6278 0.3501 0.1319  0.0672  -0.1080 35  LYS A O   
271   C CB  . LYS A 35  ? 0.3371 0.5675 0.3423 0.1072  0.0534  -0.1074 35  LYS A CB  
272   C CG  . LYS A 35  ? 0.3373 0.5057 0.3346 0.0851  0.0469  -0.1090 35  LYS A CG  
273   C CD  . LYS A 35  ? 0.3647 0.4987 0.3357 0.1050  0.0470  -0.1097 35  LYS A CD  
274   C CE  . LYS A 35  ? 0.3256 0.4898 0.3340 0.0910  0.0400  -0.1078 35  LYS A CE  
275   N NZ  . LYS A 35  ? 0.2877 0.5335 0.3383 0.0865  0.0398  -0.1057 35  LYS A NZ  
276   N N   . THR A 36  ? 0.3116 0.6949 0.3572 0.1091  0.0651  -0.1038 36  THR A N   
277   C CA  . THR A 36  ? 0.3320 0.7653 0.3656 0.1391  0.0733  -0.1022 36  THR A CA  
278   C C   . THR A 36  ? 0.3145 0.7913 0.3692 0.1149  0.0761  -0.1014 36  THR A C   
279   O O   . THR A 36  ? 0.2858 0.7703 0.3676 0.0745  0.0729  -0.1013 36  THR A O   
280   C CB  . THR A 36  ? 0.3299 0.8458 0.3732 0.1657  0.0760  -0.0993 36  THR A CB  
281   O OG1 . THR A 36  ? 0.2876 0.8731 0.3748 0.1274  0.0722  -0.0993 36  THR A OG1 
282   C CG2 . THR A 36  ? 0.3552 0.8277 0.3723 0.1954  0.0749  -0.0989 36  THR A CG2 
283   N N   . HIS A 37  ? 0.3405 0.8404 0.3758 0.1428  0.0835  -0.1004 37  HIS A N   
284   C CA  . HIS A 37  ? 0.3292 0.8804 0.3806 0.1260  0.0878  -0.0991 37  HIS A CA  
285   C C   . HIS A 37  ? 0.3532 0.9750 0.3911 0.1681  0.0964  -0.0962 37  HIS A C   
286   O O   . HIS A 37  ? 0.3885 0.9955 0.3937 0.2152  0.1002  -0.0950 37  HIS A O   
287   C CB  . HIS A 37  ? 0.3385 0.8199 0.3742 0.1117  0.0875  -0.1008 37  HIS A CB  
288   C CG  . HIS A 37  ? 0.3849 0.7964 0.3719 0.1456  0.0906  -0.1033 37  HIS A CG  
289   N ND1 . HIS A 37  ? 0.4160 0.8286 0.3755 0.1699  0.0984  -0.1034 37  HIS A ND1 
290   C CD2 . HIS A 37  ? 0.4137 0.7468 0.3675 0.1561  0.0883  -0.1064 37  HIS A CD2 
291   C CE1 . HIS A 37  ? 0.4667 0.7981 0.3737 0.1936  0.1015  -0.1069 37  HIS A CE1 
292   N NE2 . HIS A 37  ? 0.4675 0.7494 0.3692 0.1837  0.0956  -0.1090 37  HIS A NE2 
293   N N   . ASN A 38  ? 0.3408 1.0382 0.3984 0.1532  0.1008  -0.0944 38  ASN A N   
294   C CA  . ASN A 38  ? 0.3611 1.1431 0.4087 0.1936  0.1094  -0.0905 38  ASN A CA  
295   C C   . ASN A 38  ? 0.4051 1.1357 0.4098 0.2321  0.1165  -0.0902 38  ASN A C   
296   O O   . ASN A 38  ? 0.4342 1.2173 0.4176 0.2793  0.1251  -0.0860 38  ASN A O   
297   C CB  . ASN A 38  ? 0.3323 1.2291 0.4160 0.1592  0.1120  -0.0888 38  ASN A CB  
298   C CG  . ASN A 38  ? 0.3229 1.1942 0.4135 0.1191  0.1136  -0.0902 38  ASN A CG  
299   O OD1 . ASN A 38  ? 0.3370 1.1205 0.4069 0.1246  0.1130  -0.0917 38  ASN A OD1 
300   N ND2 . ASN A 38  ? 0.3042 1.2536 0.4197 0.0766  0.1164  -0.0899 38  ASN A ND2 
301   N N   . GLY A 39  ? 0.4138 1.0465 0.4032 0.2123  0.1136  -0.0943 39  GLY A N   
302   C CA  . GLY A 39  ? 0.4624 1.0290 0.4036 0.2421  0.1200  -0.0959 39  GLY A CA  
303   C C   . GLY A 39  ? 0.4601 1.0718 0.4083 0.2364  0.1255  -0.0944 39  GLY A C   
304   O O   . GLY A 39  ? 0.5034 1.0827 0.4099 0.2691  0.1331  -0.0950 39  GLY A O   
305   N N   . LYS A 40  ? 0.4170 1.0955 0.4115 0.1931  0.1227  -0.0928 40  LYS A N   
306   C CA  . LYS A 40  ? 0.4137 1.1523 0.4183 0.1845  0.1289  -0.0904 40  LYS A CA  
307   C C   . LYS A 40  ? 0.3882 1.1029 0.4155 0.1293  0.1254  -0.0912 40  LYS A C   
308   O O   . LYS A 40  ? 0.3648 1.0548 0.4120 0.0930  0.1193  -0.0920 40  LYS A O   
309   C CB  . LYS A 40  ? 0.3997 1.2703 0.4291 0.1904  0.1335  -0.0860 40  LYS A CB  
310   C CG  . LYS A 40  ? 0.4355 1.3495 0.4360 0.2576  0.1406  -0.0821 40  LYS A CG  
311   C CD  . LYS A 40  ? 0.4165 1.4645 0.4455 0.2618  0.1418  -0.0775 40  LYS A CD  
312   C CE  . LYS A 40  ? 0.4587 1.5430 0.4524 0.3387  0.1495  -0.0716 40  LYS A CE  
313   N NZ  . LYS A 40  ? 0.4402 1.6662 0.4615 0.3466  0.1499  -0.0663 40  LYS A NZ  
314   N N   . LEU A 41  ? 0.3991 1.1204 0.4189 0.1270  0.1307  -0.0902 41  LEU A N   
315   C CA  . LEU A 41  ? 0.3827 1.0933 0.4185 0.0805  0.1307  -0.0890 41  LEU A CA  
316   C C   . LEU A 41  ? 0.3677 1.1793 0.4291 0.0524  0.1364  -0.0860 41  LEU A C   
317   O O   . LEU A 41  ? 0.3746 1.2721 0.4369 0.0757  0.1424  -0.0841 41  LEU A O   
318   C CB  . LEU A 41  ? 0.4041 1.0742 0.4162 0.0917  0.1341  -0.0893 41  LEU A CB  
319   C CG  . LEU A 41  ? 0.4262 0.9952 0.4075 0.1053  0.1290  -0.0935 41  LEU A CG  
320   C CD1 . LEU A 41  ? 0.4139 0.9343 0.4010 0.0693  0.1250  -0.0922 41  LEU A CD1 
321   C CD2 . LEU A 41  ? 0.4331 0.9585 0.4039 0.1201  0.1232  -0.0968 41  LEU A CD2 
322   N N   . CYS A 42  ? 0.3541 1.1554 0.4300 0.0021  0.1359  -0.0853 42  CYS A N   
323   C CA  . CYS A 42  ? 0.3472 1.2346 0.4406 -0.0343 0.1409  -0.0845 42  CYS A CA  
324   C C   . CYS A 42  ? 0.3535 1.2172 0.4427 -0.0904 0.1469  -0.0830 42  CYS A C   
325   O O   . CYS A 42  ? 0.3599 1.1333 0.4364 -0.1007 0.1455  -0.0814 42  CYS A O   
326   C CB  . CYS A 42  ? 0.3361 1.2387 0.4424 -0.0373 0.1352  -0.0869 42  CYS A CB  
327   S SG  . CYS A 42  ? 0.3395 1.3010 0.4456 0.0271  0.1326  -0.0868 42  CYS A SG  
328   N N   . ASP A 43  ? 0.3579 1.3052 0.4524 -0.1268 0.1547  -0.0830 43  ASP A N   
329   C CA  . ASP A 43  ? 0.3794 1.3013 0.4577 -0.1858 0.1638  -0.0820 43  ASP A CA  
330   C C   . ASP A 43  ? 0.3850 1.2277 0.4538 -0.2124 0.1613  -0.0833 43  ASP A C   
331   O O   . ASP A 43  ? 0.3704 1.2356 0.4529 -0.2093 0.1552  -0.0867 43  ASP A O   
332   C CB  . ASP A 43  ? 0.3907 1.4266 0.4721 -0.2259 0.1730  -0.0834 43  ASP A CB  
333   C CG  . ASP A 43  ? 0.3886 1.5092 0.4765 -0.2021 0.1774  -0.0808 43  ASP A CG  
334   O OD1 . ASP A 43  ? 0.3810 1.4660 0.4683 -0.1529 0.1737  -0.0786 43  ASP A OD1 
335   O OD2 . ASP A 43  ? 0.3977 1.6235 0.4884 -0.2345 0.1852  -0.0813 43  ASP A OD2 
336   N N   . LEU A 44  ? 0.4095 1.1598 0.4518 -0.2344 0.1667  -0.0797 44  LEU A N   
337   C CA  . LEU A 44  ? 0.4254 1.0925 0.4499 -0.2557 0.1668  -0.0793 44  LEU A CA  
338   C C   . LEU A 44  ? 0.4723 1.1336 0.4634 -0.3186 0.1814  -0.0802 44  LEU A C   
339   O O   . LEU A 44  ? 0.5092 1.1400 0.4693 -0.3424 0.1934  -0.0763 44  LEU A O   
340   C CB  . LEU A 44  ? 0.4316 0.9969 0.4399 -0.2331 0.1647  -0.0731 44  LEU A CB  
341   C CG  . LEU A 44  ? 0.4427 0.9255 0.4356 -0.2382 0.1628  -0.0711 44  LEU A CG  
342   C CD1 . LEU A 44  ? 0.4029 0.8946 0.4262 -0.2045 0.1478  -0.0749 44  LEU A CD1 
343   C CD2 . LEU A 44  ? 0.4668 0.8620 0.4307 -0.2279 0.1670  -0.0624 44  LEU A CD2 
344   N N   . ASP A 45  ? 0.4769 1.1635 0.4688 -0.3471 0.1812  -0.0856 45  ASP A N   
345   C CA  . ASP A 45  ? 0.5316 1.2072 0.4826 -0.4144 0.1960  -0.0887 45  ASP A CA  
346   C C   . ASP A 45  ? 0.5491 1.3123 0.4939 -0.4498 0.2063  -0.0903 45  ASP A C   
347   O O   . ASP A 45  ? 0.6094 1.3345 0.5052 -0.5039 0.2226  -0.0903 45  ASP A O   
348   C CB  . ASP A 45  ? 0.5873 1.1237 0.4838 -0.4292 0.2071  -0.0828 45  ASP A CB  
349   C CG  . ASP A 45  ? 0.6430 1.1274 0.4939 -0.4818 0.2178  -0.0871 45  ASP A CG  
350   O OD1 . ASP A 45  ? 0.6276 1.0817 0.4884 -0.4666 0.2096  -0.0887 45  ASP A OD1 
351   O OD2 . ASP A 45  ? 0.7080 1.1762 0.5081 -0.5398 0.2354  -0.0890 45  ASP A OD2 
352   N N   . GLY A 46  ? 0.5023 1.3796 0.4911 -0.4175 0.1980  -0.0912 46  GLY A N   
353   C CA  . GLY A 46  ? 0.5107 1.4881 0.5005 -0.4405 0.2063  -0.0914 46  GLY A CA  
354   C C   . GLY A 46  ? 0.5095 1.4586 0.4955 -0.4121 0.2092  -0.0850 46  GLY A C   
355   O O   . GLY A 46  ? 0.4967 1.5428 0.4997 -0.4030 0.2108  -0.0842 46  GLY A O   
356   N N   . VAL A 47  ? 0.5231 1.3460 0.4863 -0.3960 0.2100  -0.0798 47  VAL A N   
357   C CA  . VAL A 47  ? 0.5306 1.3154 0.4821 -0.3763 0.2143  -0.0734 47  VAL A CA  
358   C C   . VAL A 47  ? 0.4791 1.2846 0.4686 -0.3072 0.2003  -0.0720 47  VAL A C   
359   O O   . VAL A 47  ? 0.4557 1.2084 0.4572 -0.2717 0.1892  -0.0719 47  VAL A O   
360   C CB  . VAL A 47  ? 0.5753 1.2212 0.4798 -0.3872 0.2227  -0.0671 47  VAL A CB  
361   C CG1 . VAL A 47  ? 0.5859 1.2006 0.4772 -0.3680 0.2276  -0.0599 47  VAL A CG1 
362   C CG2 . VAL A 47  ? 0.6433 1.2464 0.4940 -0.4552 0.2396  -0.0688 47  VAL A CG2 
363   N N   . LYS A 48  ? 0.4688 1.3466 0.4706 -0.2907 0.2021  -0.0709 48  LYS A N   
364   C CA  . LYS A 48  ? 0.4330 1.3352 0.4606 -0.2274 0.1916  -0.0708 48  LYS A CA  
365   C C   . LYS A 48  ? 0.4324 1.2321 0.4482 -0.1972 0.1871  -0.0670 48  LYS A C   
366   O O   . LYS A 48  ? 0.4594 1.2002 0.4492 -0.2184 0.1950  -0.0621 48  LYS A O   
367   C CB  . LYS A 48  ? 0.4315 1.4376 0.4681 -0.2179 0.1970  -0.0700 48  LYS A CB  
368   C CG  . LYS A 48  ? 0.4066 1.4510 0.4618 -0.1513 0.1888  -0.0707 48  LYS A CG  
369   C CD  . LYS A 48  ? 0.4128 1.5338 0.4677 -0.1349 0.1957  -0.0681 48  LYS A CD  
370   C CE  . LYS A 48  ? 0.4011 1.5642 0.4643 -0.0667 0.1905  -0.0687 48  LYS A CE  
371   N NZ  . LYS A 48  ? 0.4126 1.6181 0.4674 -0.0398 0.1970  -0.0657 48  LYS A NZ  
372   N N   . PRO A 49  ? 0.4070 1.1863 0.4371 -0.1484 0.1753  -0.0691 49  PRO A N   
373   C CA  . PRO A 49  ? 0.4077 1.1088 0.4261 -0.1223 0.1709  -0.0665 49  PRO A CA  
374   C C   . PRO A 49  ? 0.4142 1.1411 0.4261 -0.1045 0.1753  -0.0649 49  PRO A C   
375   O O   . PRO A 49  ? 0.4104 1.2174 0.4318 -0.0905 0.1781  -0.0669 49  PRO A O   
376   C CB  . PRO A 49  ? 0.3874 1.0686 0.4168 -0.0828 0.1586  -0.0711 49  PRO A CB  
377   C CG  . PRO A 49  ? 0.3775 1.1448 0.4235 -0.0701 0.1585  -0.0748 49  PRO A CG  
378   C CD  . PRO A 49  ? 0.3840 1.2018 0.4345 -0.1189 0.1664  -0.0737 49  PRO A CD  
379   N N   . LEU A 50  ? 0.4250 1.0889 0.4197 -0.1023 0.1762  -0.0608 50  LEU A N   
380   C CA  . LEU A 50  ? 0.4314 1.1076 0.4179 -0.0812 0.1787  -0.0599 50  LEU A CA  
381   C C   . LEU A 50  ? 0.4220 1.0813 0.4087 -0.0366 0.1690  -0.0656 50  LEU A C   
382   O O   . LEU A 50  ? 0.4217 1.0157 0.3997 -0.0276 0.1617  -0.0663 50  LEU A O   
383   C CB  . LEU A 50  ? 0.4505 1.0671 0.4153 -0.0950 0.1835  -0.0529 50  LEU A CB  
384   C CG  . LEU A 50  ? 0.4580 1.0733 0.4117 -0.0733 0.1846  -0.0519 50  LEU A CG  
385   C CD1 . LEU A 50  ? 0.4602 1.1545 0.4198 -0.0659 0.1911  -0.0541 50  LEU A CD1 
386   C CD2 . LEU A 50  ? 0.4809 1.0480 0.4118 -0.0912 0.1917  -0.0429 50  LEU A CD2 
387   N N   . ILE A 51  ? 0.4215 1.1396 0.4123 -0.0090 0.1702  -0.0695 51  ILE A N   
388   C CA  . ILE A 51  ? 0.4304 1.1216 0.4064 0.0347  0.1647  -0.0751 51  ILE A CA  
389   C C   . ILE A 51  ? 0.4515 1.1364 0.4058 0.0541  0.1691  -0.0754 51  ILE A C   
390   O O   . ILE A 51  ? 0.4599 1.2091 0.4134 0.0672  0.1770  -0.0741 51  ILE A O   
391   C CB  . ILE A 51  ? 0.4303 1.1783 0.4116 0.0639  0.1653  -0.0779 51  ILE A CB  
392   C CG1 . ILE A 51  ? 0.4094 1.1624 0.4121 0.0423  0.1602  -0.0780 51  ILE A CG1 
393   C CG2 . ILE A 51  ? 0.4573 1.1596 0.4069 0.1116  0.1632  -0.0833 51  ILE A CG2 
394   C CD1 . ILE A 51  ? 0.4104 1.2015 0.4150 0.0755  0.1584  -0.0806 51  ILE A CD1 
395   N N   . LEU A 52  ? 0.4614 1.0745 0.3971 0.0554  0.1642  -0.0773 52  LEU A N   
396   C CA  . LEU A 52  ? 0.4840 1.0828 0.3956 0.0696  0.1677  -0.0784 52  LEU A CA  
397   C C   . LEU A 52  ? 0.5168 1.1104 0.3976 0.1131  0.1703  -0.0853 52  LEU A C   
398   O O   . LEU A 52  ? 0.5420 1.1307 0.3983 0.1289  0.1753  -0.0868 52  LEU A O   
399   C CB  . LEU A 52  ? 0.4866 1.0188 0.3855 0.0552  0.1612  -0.0783 52  LEU A CB  
400   C CG  . LEU A 52  ? 0.4679 0.9914 0.3840 0.0215  0.1608  -0.0696 52  LEU A CG  
401   C CD1 . LEU A 52  ? 0.4728 0.9435 0.3744 0.0168  0.1539  -0.0688 52  LEU A CD1 
402   C CD2 . LEU A 52  ? 0.4710 1.0351 0.3920 0.0053  0.1714  -0.0623 52  LEU A CD2 
403   N N   . ARG A 53  ? 0.5234 1.1128 0.3995 0.1342  0.1682  -0.0889 53  ARG A N   
404   C CA  . ARG A 53  ? 0.5687 1.1374 0.4030 0.1807  0.1730  -0.0945 53  ARG A CA  
405   C C   . ARG A 53  ? 0.6095 1.0880 0.3969 0.1841  0.1713  -0.1020 53  ARG A C   
406   O O   . ARG A 53  ? 0.6080 1.0272 0.3902 0.1635  0.1628  -0.1059 53  ARG A O   
407   C CB  . ARG A 53  ? 0.5811 1.2313 0.4136 0.2113  0.1842  -0.0904 53  ARG A CB  
408   C CG  . ARG A 53  ? 0.6317 1.2709 0.4191 0.2691  0.1916  -0.0933 53  ARG A CG  
409   C CD  . ARG A 53  ? 0.6483 1.3742 0.4296 0.3057  0.2035  -0.0879 53  ARG A CD  
410   N NE  . ARG A 53  ? 0.6226 1.4561 0.4380 0.3159  0.2057  -0.0813 53  ARG A NE  
411   C CZ  . ARG A 53  ? 0.5779 1.5134 0.4431 0.2813  0.2057  -0.0753 53  ARG A CZ  
412   N NH1 . ARG A 53  ? 0.5554 1.4942 0.4413 0.2366  0.2047  -0.0741 53  ARG A NH1 
413   N NH2 . ARG A 53  ? 0.5611 1.5971 0.4509 0.2903  0.2076  -0.0705 53  ARG A NH2 
414   N N   . ASP A 54  ? 0.6482 1.1198 0.4003 0.2067  0.1793  -0.1043 54  ASP A N   
415   C CA  . ASP A 54  ? 0.6954 1.0824 0.3953 0.2059  0.1789  -0.1129 54  ASP A CA  
416   C C   . ASP A 54  ? 0.6745 1.0642 0.3898 0.1717  0.1748  -0.1109 54  ASP A C   
417   O O   . ASP A 54  ? 0.7080 1.0388 0.3850 0.1627  0.1729  -0.1179 54  ASP A O   
418   C CB  . ASP A 54  ? 0.7644 1.1255 0.4023 0.2531  0.1916  -0.1177 54  ASP A CB  
419   C CG  . ASP A 54  ? 0.8098 1.1320 0.4073 0.2913  0.1968  -0.1210 54  ASP A CG  
420   O OD1 . ASP A 54  ? 0.8293 1.0771 0.4025 0.2772  0.1913  -0.1276 54  ASP A OD1 
421   O OD2 . ASP A 54  ? 0.8295 1.1986 0.4168 0.3368  0.2070  -0.1163 54  ASP A OD2 
422   N N   . CYS A 55  ? 0.6266 1.0830 0.3916 0.1518  0.1744  -0.1013 55  CYS A N   
423   C CA  . CYS A 55  ? 0.6084 1.0657 0.3869 0.1216  0.1714  -0.0970 55  CYS A CA  
424   C C   . CYS A 55  ? 0.5816 1.0086 0.3780 0.0912  0.1607  -0.0952 55  CYS A C   
425   O O   . CYS A 55  ? 0.5612 0.9888 0.3777 0.0863  0.1565  -0.0943 55  CYS A O   
426   C CB  . CYS A 55  ? 0.5814 1.1105 0.3939 0.1116  0.1780  -0.0870 55  CYS A CB  
427   S SG  . CYS A 55  ? 0.6125 1.1833 0.4025 0.1414  0.1902  -0.0874 55  CYS A SG  
428   N N   . SER A 56  ? 0.5833 0.9891 0.3707 0.0733  0.1566  -0.0943 56  SER A N   
429   C CA  . SER A 56  ? 0.5586 0.9496 0.3624 0.0485  0.1478  -0.0897 56  SER A CA  
430   C C   . SER A 56  ? 0.5296 0.9557 0.3639 0.0336  0.1514  -0.0763 56  SER A C   
431   O O   . SER A 56  ? 0.5282 0.9892 0.3707 0.0368  0.1602  -0.0718 56  SER A O   
432   C CB  . SER A 56  ? 0.5824 0.9403 0.3547 0.0383  0.1418  -0.0953 56  SER A CB  
433   O OG  . SER A 56  ? 0.5817 0.9621 0.3538 0.0327  0.1446  -0.0888 56  SER A OG  
434   N N   . VAL A 57  ? 0.5131 0.9275 0.3579 0.0178  0.1459  -0.0694 57  VAL A N   
435   C CA  . VAL A 57  ? 0.5014 0.9300 0.3601 0.0060  0.1516  -0.0556 57  VAL A CA  
436   C C   . VAL A 57  ? 0.5172 0.9566 0.3601 0.0079  0.1566  -0.0507 57  VAL A C   
437   O O   . VAL A 57  ? 0.5211 0.9771 0.3666 0.0032  0.1667  -0.0423 57  VAL A O   
438   C CB  . VAL A 57  ? 0.4900 0.8989 0.3547 -0.0029 0.1457  -0.0483 57  VAL A CB  
439   C CG1 . VAL A 57  ? 0.4957 0.9036 0.3590 -0.0099 0.1549  -0.0330 57  VAL A CG1 
440   C CG2 . VAL A 57  ? 0.4740 0.8721 0.3549 -0.0057 0.1410  -0.0529 57  VAL A CG2 
441   N N   . ALA A 58  ? 0.5302 0.9599 0.3528 0.0117  0.1502  -0.0564 58  ALA A N   
442   C CA  . ALA A 58  ? 0.5467 0.9889 0.3518 0.0143  0.1538  -0.0531 58  ALA A CA  
443   C C   . ALA A 58  ? 0.5578 1.0179 0.3589 0.0236  0.1631  -0.0565 58  ALA A C   
444   O O   . ALA A 58  ? 0.5618 1.0409 0.3631 0.0222  0.1715  -0.0476 58  ALA A O   
445   C CB  . ALA A 58  ? 0.5636 0.9950 0.3437 0.0117  0.1448  -0.0620 58  ALA A CB  
446   N N   . GLY A 59  ? 0.5673 1.0211 0.3604 0.0355  0.1628  -0.0685 59  GLY A N   
447   C CA  . GLY A 59  ? 0.5807 1.0588 0.3676 0.0508  0.1720  -0.0714 59  GLY A CA  
448   C C   . GLY A 59  ? 0.5615 1.0815 0.3756 0.0437  0.1810  -0.0615 59  GLY A C   
449   O O   . GLY A 59  ? 0.5699 1.1203 0.3815 0.0454  0.1897  -0.0574 59  GLY A O   
450   N N   . TRP A 60  ? 0.5399 1.0615 0.3764 0.0323  0.1794  -0.0583 60  TRP A N   
451   C CA  . TRP A 60  ? 0.5295 1.0861 0.3850 0.0157  0.1885  -0.0500 60  TRP A CA  
452   C C   . TRP A 60  ? 0.5395 1.0883 0.3866 -0.0014 0.1957  -0.0380 60  TRP A C   
453   O O   . TRP A 60  ? 0.5502 1.1299 0.3945 -0.0093 0.2063  -0.0333 60  TRP A O   
454   C CB  . TRP A 60  ? 0.5112 1.0617 0.3859 0.0037  0.1850  -0.0497 60  TRP A CB  
455   C CG  . TRP A 60  ? 0.5113 1.0728 0.3939 -0.0250 0.1940  -0.0403 60  TRP A CG  
456   C CD1 . TRP A 60  ? 0.5228 1.1244 0.4041 -0.0412 0.2061  -0.0357 60  TRP A CD1 
457   C CD2 . TRP A 60  ? 0.5085 1.0354 0.3935 -0.0435 0.1931  -0.0349 60  TRP A CD2 
458   N NE1 . TRP A 60  ? 0.5334 1.1202 0.4107 -0.0728 0.2136  -0.0286 60  TRP A NE1 
459   C CE2 . TRP A 60  ? 0.5259 1.0641 0.4043 -0.0723 0.2061  -0.0278 60  TRP A CE2 
460   C CE3 . TRP A 60  ? 0.4979 0.9842 0.3856 -0.0394 0.1835  -0.0353 60  TRP A CE3 
461   C CZ2 . TRP A 60  ? 0.5396 1.0393 0.4080 -0.0957 0.2109  -0.0215 60  TRP A CZ2 
462   C CZ3 . TRP A 60  ? 0.5040 0.9610 0.3884 -0.0584 0.1873  -0.0281 60  TRP A CZ3 
463   C CH2 . TRP A 60  ? 0.5278 0.9866 0.3998 -0.0854 0.2013  -0.0215 60  TRP A CH2 
464   N N   . LEU A 61  ? 0.5404 1.0498 0.3795 -0.0051 0.1907  -0.0323 61  LEU A N   
465   C CA  . LEU A 61  ? 0.5582 1.0512 0.3815 -0.0153 0.1991  -0.0185 61  LEU A CA  
466   C C   . LEU A 61  ? 0.5748 1.0808 0.3811 -0.0066 0.2033  -0.0159 61  LEU A C   
467   O O   . LEU A 61  ? 0.5953 1.1022 0.3879 -0.0162 0.2153  -0.0058 61  LEU A O   
468   C CB  . LEU A 61  ? 0.5578 1.0136 0.3745 -0.0132 0.1931  -0.0115 61  LEU A CB  
469   C CG  . LEU A 61  ? 0.5489 0.9835 0.3761 -0.0241 0.1921  -0.0102 61  LEU A CG  
470   C CD1 . LEU A 61  ? 0.5539 0.9572 0.3698 -0.0163 0.1877  -0.0011 61  LEU A CD1 
471   C CD2 . LEU A 61  ? 0.5678 0.9985 0.3883 -0.0470 0.2067  -0.0040 61  LEU A CD2 
472   N N   . LEU A 62  ? 0.5723 1.0835 0.3736 0.0093  0.1946  -0.0253 62  LEU A N   
473   C CA  . LEU A 62  ? 0.5889 1.1146 0.3728 0.0177  0.1983  -0.0249 62  LEU A CA  
474   C C   . LEU A 62  ? 0.5946 1.1560 0.3817 0.0205  0.2074  -0.0288 62  LEU A C   
475   O O   . LEU A 62  ? 0.6097 1.1870 0.3838 0.0245  0.2136  -0.0260 62  LEU A O   
476   C CB  . LEU A 62  ? 0.5935 1.1090 0.3625 0.0288  0.1872  -0.0352 62  LEU A CB  
477   C CG  . LEU A 62  ? 0.5907 1.0911 0.3540 0.0253  0.1788  -0.0296 62  LEU A CG  
478   C CD1 . LEU A 62  ? 0.5980 1.0901 0.3455 0.0260  0.1672  -0.0435 62  LEU A CD1 
479   C CD2 . LEU A 62  ? 0.6048 1.1143 0.3545 0.0277  0.1851  -0.0147 62  LEU A CD2 
480   N N   . GLY A 63  ? 0.5833 1.1642 0.3873 0.0200  0.2082  -0.0345 63  GLY A N   
481   C CA  . GLY A 63  ? 0.5880 1.2188 0.3967 0.0254  0.2169  -0.0371 63  GLY A CA  
482   C C   . GLY A 63  ? 0.6020 1.2380 0.3944 0.0547  0.2142  -0.0482 63  GLY A C   
483   O O   . GLY A 63  ? 0.6164 1.2828 0.3987 0.0647  0.2217  -0.0479 63  GLY A O   
484   N N   . ASN A 64  ? 0.6049 1.2052 0.3883 0.0679  0.2047  -0.0580 64  ASN A N   
485   C CA  . ASN A 64  ? 0.6334 1.2211 0.3879 0.0965  0.2045  -0.0698 64  ASN A CA  
486   C C   . ASN A 64  ? 0.6387 1.2824 0.3989 0.1175  0.2142  -0.0699 64  ASN A C   
487   O O   . ASN A 64  ? 0.6175 1.2972 0.4044 0.1119  0.2155  -0.0666 64  ASN A O   
488   C CB  . ASN A 64  ? 0.6408 1.1754 0.3809 0.1010  0.1948  -0.0796 64  ASN A CB  
489   C CG  . ASN A 64  ? 0.6841 1.1899 0.3821 0.1321  0.1977  -0.0920 64  ASN A CG  
490   O OD1 . ASN A 64  ? 0.6964 1.2356 0.3900 0.1585  0.2065  -0.0921 64  ASN A OD1 
491   N ND2 . ASN A 64  ? 0.7144 1.1571 0.3753 0.1289  0.1916  -0.1022 64  ASN A ND2 
492   N N   . PRO A 65  ? 0.6693 1.3266 0.4031 0.1422  0.2214  -0.0733 65  PRO A N   
493   C CA  . PRO A 65  ? 0.6757 1.4022 0.4142 0.1660  0.2319  -0.0711 65  PRO A CA  
494   C C   . PRO A 65  ? 0.6817 1.4210 0.4188 0.1934  0.2321  -0.0754 65  PRO A C   
495   O O   . PRO A 65  ? 0.6740 1.4915 0.4283 0.2059  0.2393  -0.0706 65  PRO A O   
496   C CB  . PRO A 65  ? 0.7162 1.4329 0.4148 0.1931  0.2385  -0.0756 65  PRO A CB  
497   C CG  . PRO A 65  ? 0.7407 1.3708 0.4046 0.1884  0.2305  -0.0846 65  PRO A CG  
498   C CD  . PRO A 65  ? 0.7029 1.3156 0.3978 0.1499  0.2205  -0.0796 65  PRO A CD  
499   N N   . MET A 66  ? 0.6992 1.3670 0.4135 0.2023  0.2249  -0.0838 66  MET A N   
500   C CA  . MET A 66  ? 0.7074 1.3764 0.4174 0.2277  0.2249  -0.0870 66  MET A CA  
501   C C   . MET A 66  ? 0.6587 1.3658 0.4190 0.1986  0.2191  -0.0810 66  MET A C   
502   O O   . MET A 66  ? 0.6554 1.3907 0.4233 0.2166  0.2198  -0.0811 66  MET A O   
503   C CB  . MET A 66  ? 0.7495 1.3187 0.4109 0.2409  0.2201  -0.0984 66  MET A CB  
504   C CG  . MET A 66  ? 0.8141 1.3272 0.4110 0.2667  0.2270  -0.1068 66  MET A CG  
505   S SD  . MET A 66  ? 0.8696 1.4119 0.4231 0.3336  0.2436  -0.1065 66  MET A SD  
506   C CE  . MET A 66  ? 0.9602 1.3926 0.4212 0.3527  0.2506  -0.1196 66  MET A CE  
507   N N   . CYS A 67  ? 0.6275 1.3315 0.4163 0.1556  0.2144  -0.0755 67  CYS A N   
508   C CA  . CYS A 67  ? 0.5905 1.3170 0.4180 0.1237  0.2106  -0.0700 67  CYS A CA  
509   C C   . CYS A 67  ? 0.5742 1.3804 0.4275 0.0999  0.2194  -0.0610 67  CYS A C   
510   O O   . CYS A 67  ? 0.5573 1.3606 0.4285 0.0610  0.2194  -0.0549 67  CYS A O   
511   C CB  . CYS A 67  ? 0.5790 1.2397 0.4094 0.0948  0.2016  -0.0689 67  CYS A CB  
512   S SG  . CYS A 67  ? 0.6060 1.1803 0.3998 0.1124  0.1919  -0.0804 67  CYS A SG  
513   N N   . ASP A 68  ? 0.5869 1.4616 0.4353 0.1236  0.2283  -0.0602 68  ASP A N   
514   C CA  . ASP A 68  ? 0.5765 1.5411 0.4457 0.0996  0.2379  -0.0526 68  ASP A CA  
515   C C   . ASP A 68  ? 0.5538 1.5719 0.4518 0.0739  0.2377  -0.0504 68  ASP A C   
516   O O   . ASP A 68  ? 0.5477 1.6164 0.4597 0.0328  0.2445  -0.0447 68  ASP A O   
517   C CB  . ASP A 68  ? 0.5961 1.6341 0.4530 0.1372  0.2472  -0.0522 68  ASP A CB  
518   C CG  . ASP A 68  ? 0.6186 1.6247 0.4502 0.1473  0.2510  -0.0522 68  ASP A CG  
519   O OD1 . ASP A 68  ? 0.6159 1.5583 0.4435 0.1202  0.2472  -0.0511 68  ASP A OD1 
520   O OD2 . ASP A 68  ? 0.6419 1.6900 0.4551 0.1852  0.2584  -0.0528 68  ASP A OD2 
521   N N   . GLU A 69  ? 0.5469 1.5521 0.4486 0.0953  0.2308  -0.0551 69  GLU A N   
522   C CA  . GLU A 69  ? 0.5256 1.5750 0.4536 0.0695  0.2292  -0.0538 69  GLU A CA  
523   C C   . GLU A 69  ? 0.5156 1.5146 0.4521 0.0143  0.2276  -0.0507 69  GLU A C   
524   O O   . GLU A 69  ? 0.5101 1.5563 0.4609 -0.0254 0.2321  -0.0478 69  GLU A O   
525   C CB  . GLU A 69  ? 0.5227 1.5458 0.4486 0.1037  0.2213  -0.0594 69  GLU A CB  
526   C CG  . GLU A 69  ? 0.5001 1.5705 0.4531 0.0790  0.2189  -0.0585 69  GLU A CG  
527   C CD  . GLU A 69  ? 0.5000 1.5454 0.4487 0.1158  0.2118  -0.0632 69  GLU A CD  
528   O OE1 . GLU A 69  ? 0.5258 1.5312 0.4451 0.1652  0.2116  -0.0668 69  GLU A OE1 
529   O OE2 . GLU A 69  ? 0.4802 1.5411 0.4496 0.0941  0.2075  -0.0634 69  GLU A OE2 
530   N N   . PHE A 70  ? 0.5206 1.4249 0.4425 0.0126  0.2222  -0.0510 70  PHE A N   
531   C CA  . PHE A 70  ? 0.5176 1.3603 0.4397 -0.0263 0.2205  -0.0470 70  PHE A CA  
532   C C   . PHE A 70  ? 0.5380 1.3623 0.4441 -0.0554 0.2299  -0.0391 70  PHE A C   
533   O O   . PHE A 70  ? 0.5462 1.2997 0.4395 -0.0708 0.2289  -0.0345 70  PHE A O   
534   C CB  . PHE A 70  ? 0.5107 1.2698 0.4266 -0.0081 0.2085  -0.0509 70  PHE A CB  
535   C CG  . PHE A 70  ? 0.5011 1.2669 0.4228 0.0231  0.2010  -0.0586 70  PHE A CG  
536   C CD1 . PHE A 70  ? 0.4851 1.2835 0.4263 0.0124  0.1995  -0.0594 70  PHE A CD1 
537   C CD2 . PHE A 70  ? 0.5158 1.2530 0.4167 0.0627  0.1971  -0.0651 70  PHE A CD2 
538   C CE1 . PHE A 70  ? 0.4813 1.2850 0.4240 0.0445  0.1938  -0.0653 70  PHE A CE1 
539   C CE2 . PHE A 70  ? 0.5201 1.2521 0.4151 0.0932  0.1929  -0.0714 70  PHE A CE2 
540   C CZ  . PHE A 70  ? 0.5011 1.2681 0.4186 0.0862  0.1911  -0.0709 70  PHE A CZ  
541   N N   . ILE A 71  ? 0.5503 1.4406 0.4543 -0.0600 0.2398  -0.0367 71  ILE A N   
542   C CA  . ILE A 71  ? 0.5760 1.4602 0.4623 -0.0967 0.2519  -0.0287 71  ILE A CA  
543   C C   . ILE A 71  ? 0.5897 1.4945 0.4746 -0.1486 0.2605  -0.0260 71  ILE A C   
544   O O   . ILE A 71  ? 0.5793 1.5650 0.4829 -0.1572 0.2614  -0.0299 71  ILE A O   
545   C CB  . ILE A 71  ? 0.5863 1.5359 0.4682 -0.0859 0.2601  -0.0272 71  ILE A CB  
546   C CG1 . ILE A 71  ? 0.6179 1.5587 0.4770 -0.1288 0.2743  -0.0185 71  ILE A CG1 
547   C CG2 . ILE A 71  ? 0.5752 1.6377 0.4769 -0.0765 0.2629  -0.0307 71  ILE A CG2 
548   C CD1 . ILE A 71  ? 0.6290 1.6078 0.4793 -0.1143 0.2809  -0.0160 71  ILE A CD1 
549   N N   . ASN A 72  ? 0.6203 1.4509 0.4773 -0.1821 0.2679  -0.0192 72  ASN A N   
550   C CA  . ASN A 72  ? 0.6491 1.4727 0.4888 -0.2364 0.2785  -0.0172 72  ASN A CA  
551   C C   . ASN A 72  ? 0.6247 1.4715 0.4879 -0.2411 0.2702  -0.0241 72  ASN A C   
552   O O   . ASN A 72  ? 0.6286 1.5495 0.4991 -0.2741 0.2756  -0.0274 72  ASN A O   
553   C CB  . ASN A 72  ? 0.6771 1.5753 0.5043 -0.2778 0.2939  -0.0154 72  ASN A CB  
554   C CG  . ASN A 72  ? 0.7231 1.5664 0.5092 -0.2944 0.3074  -0.0064 72  ASN A CG  
555   O OD1 . ASN A 72  ? 0.7446 1.4872 0.5039 -0.2841 0.3081  0.0000  72  ASN A OD1 
556   N ND2 . ASN A 72  ? 0.7414 1.6554 0.5202 -0.3190 0.3189  -0.0049 72  ASN A ND2 
557   N N   . VAL A 73  ? 0.6011 1.3898 0.4752 -0.2100 0.2573  -0.0262 73  VAL A N   
558   C CA  . VAL A 73  ? 0.5772 1.3801 0.4730 -0.2100 0.2486  -0.0324 73  VAL A CA  
559   C C   . VAL A 73  ? 0.6095 1.3818 0.4820 -0.2641 0.2582  -0.0308 73  VAL A C   
560   O O   . VAL A 73  ? 0.6534 1.3430 0.4858 -0.2870 0.2684  -0.0238 73  VAL A O   
561   C CB  . VAL A 73  ? 0.5508 1.2906 0.4581 -0.1690 0.2334  -0.0347 73  VAL A CB  
562   C CG1 . VAL A 73  ? 0.5267 1.2949 0.4498 -0.1196 0.2244  -0.0392 73  VAL A CG1 
563   C CG2 . VAL A 73  ? 0.5742 1.2131 0.4529 -0.1725 0.2353  -0.0271 73  VAL A CG2 
564   N N   . PRO A 74  ? 0.5946 1.4300 0.4861 -0.2830 0.2561  -0.0370 74  PRO A N   
565   C CA  . PRO A 74  ? 0.6287 1.4280 0.4938 -0.3357 0.2647  -0.0374 74  PRO A CA  
566   C C   . PRO A 74  ? 0.6240 1.3239 0.4830 -0.3181 0.2567  -0.0363 74  PRO A C   
567   O O   . PRO A 74  ? 0.5870 1.2651 0.4689 -0.2683 0.2431  -0.0365 74  PRO A O   
568   C CB  . PRO A 74  ? 0.6062 1.5217 0.5010 -0.3525 0.2618  -0.0450 74  PRO A CB  
569   C CG  . PRO A 74  ? 0.5522 1.5224 0.4906 -0.2884 0.2466  -0.0480 74  PRO A CG  
570   C CD  . PRO A 74  ? 0.5509 1.4853 0.4838 -0.2516 0.2458  -0.0436 74  PRO A CD  
571   N N   . GLU A 75  ? 0.6654 1.3056 0.4891 -0.3601 0.2660  -0.0353 75  GLU A N   
572   C CA  . GLU A 75  ? 0.6668 1.2136 0.4799 -0.3434 0.2604  -0.0330 75  GLU A CA  
573   C C   . GLU A 75  ? 0.6072 1.1974 0.4694 -0.3133 0.2422  -0.0405 75  GLU A C   
574   O O   . GLU A 75  ? 0.5812 1.2653 0.4730 -0.3211 0.2383  -0.0476 75  GLU A O   
575   C CB  . GLU A 75  ? 0.7369 1.2037 0.4915 -0.3942 0.2769  -0.0304 75  GLU A CB  
576   C CG  . GLU A 75  ? 0.7388 1.2463 0.4992 -0.4341 0.2770  -0.0394 75  GLU A CG  
577   C CD  . GLU A 75  ? 0.8169 1.2180 0.5093 -0.4775 0.2933  -0.0369 75  GLU A CD  
578   O OE1 . GLU A 75  ? 0.8914 1.2547 0.5240 -0.5258 0.3138  -0.0343 75  GLU A OE1 
579   O OE2 . GLU A 75  ? 0.8109 1.1608 0.5038 -0.4632 0.2869  -0.0375 75  GLU A OE2 
580   N N   . TRP A 76  ? 0.5891 1.1133 0.4563 -0.2783 0.2321  -0.0381 76  TRP A N   
581   C CA  . TRP A 76  ? 0.5375 1.0880 0.4456 -0.2453 0.2150  -0.0444 76  TRP A CA  
582   C C   . TRP A 76  ? 0.5460 1.0257 0.4418 -0.2503 0.2124  -0.0432 76  TRP A C   
583   O O   . TRP A 76  ? 0.5858 0.9820 0.4427 -0.2577 0.2208  -0.0353 76  TRP A O   
584   C CB  . TRP A 76  ? 0.5049 1.0531 0.4328 -0.1947 0.2033  -0.0440 76  TRP A CB  
585   C CG  . TRP A 76  ? 0.5243 0.9910 0.4266 -0.1811 0.2046  -0.0354 76  TRP A CG  
586   C CD1 . TRP A 76  ? 0.5198 0.9265 0.4179 -0.1640 0.1974  -0.0323 76  TRP A CD1 
587   C CD2 . TRP A 76  ? 0.5526 0.9975 0.4287 -0.1819 0.2141  -0.0278 76  TRP A CD2 
588   N NE1 . TRP A 76  ? 0.5433 0.8994 0.4146 -0.1520 0.2018  -0.0226 76  TRP A NE1 
589   C CE2 . TRP A 76  ? 0.5643 0.9393 0.4211 -0.1621 0.2120  -0.0197 76  TRP A CE2 
590   C CE3 . TRP A 76  ? 0.5700 1.0529 0.4367 -0.1963 0.2243  -0.0264 76  TRP A CE3 
591   C CZ2 . TRP A 76  ? 0.5934 0.9354 0.4211 -0.1540 0.2199  -0.0099 76  TRP A CZ2 
592   C CZ3 . TRP A 76  ? 0.5990 1.0414 0.4364 -0.1908 0.2322  -0.0174 76  TRP A CZ3 
593   C CH2 . TRP A 76  ? 0.6108 0.9832 0.4287 -0.1687 0.2299  -0.0091 76  TRP A CH2 
594   N N   . SER A 77  ? 0.5120 1.0259 0.4379 -0.2425 0.2017  -0.0502 77  SER A N   
595   C CA  . SER A 77  ? 0.5109 0.9657 0.4323 -0.2399 0.1966  -0.0499 77  SER A CA  
596   C C   . SER A 77  ? 0.4868 0.8967 0.4174 -0.1956 0.1850  -0.0463 77  SER A C   
597   O O   . SER A 77  ? 0.5068 0.8455 0.4139 -0.1912 0.1869  -0.0393 77  SER A O   
598   C CB  . SER A 77  ? 0.4815 0.9952 0.4335 -0.2439 0.1884  -0.0585 77  SER A CB  
599   O OG  . SER A 77  ? 0.4435 1.0359 0.4305 -0.2134 0.1795  -0.0633 77  SER A OG  
600   N N   . TYR A 78  ? 0.4494 0.9033 0.4093 -0.1634 0.1742  -0.0509 78  TYR A N   
601   C CA  . TYR A 78  ? 0.4314 0.8524 0.3961 -0.1282 0.1636  -0.0495 78  TYR A CA  
602   C C   . TYR A 78  ? 0.4190 0.8806 0.3934 -0.1049 0.1606  -0.0532 78  TYR A C   
603   O O   . TYR A 78  ? 0.4182 0.9390 0.4007 -0.1096 0.1653  -0.0565 78  TYR A O   
604   C CB  . TYR A 78  ? 0.4056 0.8145 0.3880 -0.1134 0.1513  -0.0542 78  TYR A CB  
605   C CG  . TYR A 78  ? 0.3821 0.8485 0.3891 -0.1041 0.1457  -0.0631 78  TYR A CG  
606   C CD1 . TYR A 78  ? 0.3826 0.8912 0.3978 -0.1280 0.1503  -0.0658 78  TYR A CD1 
607   C CD2 . TYR A 78  ? 0.3670 0.8442 0.3824 -0.0710 0.1370  -0.0685 78  TYR A CD2 
608   C CE1 . TYR A 78  ? 0.3631 0.9341 0.3994 -0.1137 0.1456  -0.0722 78  TYR A CE1 
609   C CE2 . TYR A 78  ? 0.3559 0.8800 0.3847 -0.0546 0.1341  -0.0747 78  TYR A CE2 
610   C CZ  . TYR A 78  ? 0.3510 0.9274 0.3930 -0.0732 0.1379  -0.0758 78  TYR A CZ  
611   O OH  . TYR A 78  ? 0.3414 0.9735 0.3955 -0.0511 0.1354  -0.0803 78  TYR A OH  
612   N N   . ILE A 79  ? 0.4137 0.8467 0.3836 -0.0807 0.1535  -0.0525 79  ILE A N   
613   C CA  . ILE A 79  ? 0.4118 0.8687 0.3810 -0.0589 0.1515  -0.0566 79  ILE A CA  
614   C C   . ILE A 79  ? 0.3994 0.8501 0.3737 -0.0332 0.1406  -0.0651 79  ILE A C   
615   O O   . ILE A 79  ? 0.3921 0.8076 0.3672 -0.0316 0.1327  -0.0658 79  ILE A O   
616   C CB  . ILE A 79  ? 0.4267 0.8548 0.3768 -0.0554 0.1537  -0.0502 79  ILE A CB  
617   C CG1 . ILE A 79  ? 0.4506 0.8784 0.3857 -0.0783 0.1674  -0.0414 79  ILE A CG1 
618   C CG2 . ILE A 79  ? 0.4285 0.8727 0.3733 -0.0334 0.1508  -0.0560 79  ILE A CG2 
619   C CD1 . ILE A 79  ? 0.4710 0.8601 0.3824 -0.0741 0.1710  -0.0315 79  ILE A CD1 
620   N N   . VAL A 80  ? 0.4043 0.8861 0.3759 -0.0124 0.1415  -0.0712 80  VAL A N   
621   C CA  . VAL A 80  ? 0.4106 0.8728 0.3714 0.0141  0.1347  -0.0794 80  VAL A CA  
622   C C   . VAL A 80  ? 0.4354 0.8810 0.3692 0.0324  0.1359  -0.0833 80  VAL A C   
623   O O   . VAL A 80  ? 0.4461 0.9268 0.3745 0.0438  0.1432  -0.0832 80  VAL A O   
624   C CB  . VAL A 80  ? 0.4083 0.9137 0.3777 0.0314  0.1366  -0.0832 80  VAL A CB  
625   C CG1 . VAL A 80  ? 0.4268 0.8938 0.3734 0.0604  0.1317  -0.0906 80  VAL A CG1 
626   C CG2 . VAL A 80  ? 0.3866 0.9156 0.3813 0.0082  0.1361  -0.0802 80  VAL A CG2 
627   N N   . GLU A 81  ? 0.4474 0.8419 0.3617 0.0330  0.1289  -0.0870 81  GLU A N   
628   C CA  . GLU A 81  ? 0.4779 0.8471 0.3592 0.0431  0.1295  -0.0923 81  GLU A CA  
629   C C   . GLU A 81  ? 0.5087 0.8279 0.3569 0.0557  0.1254  -0.1024 81  GLU A C   
630   O O   . GLU A 81  ? 0.5001 0.7955 0.3531 0.0453  0.1183  -0.1036 81  GLU A O   
631   C CB  . GLU A 81  ? 0.4726 0.8298 0.3531 0.0234  0.1260  -0.0870 81  GLU A CB  
632   C CG  . GLU A 81  ? 0.5031 0.8419 0.3499 0.0274  0.1264  -0.0923 81  GLU A CG  
633   C CD  . GLU A 81  ? 0.4973 0.8347 0.3435 0.0097  0.1217  -0.0864 81  GLU A CD  
634   O OE1 . GLU A 81  ? 0.4818 0.8119 0.3384 -0.0021 0.1148  -0.0829 81  GLU A OE1 
635   O OE2 . GLU A 81  ? 0.5094 0.8578 0.3435 0.0101  0.1253  -0.0846 81  GLU A OE2 
636   N N   . LYS A 82  ? 0.5528 0.8507 0.3610 0.0777  0.1312  -0.1097 82  LYS A N   
637   C CA  . LYS A 82  ? 0.6022 0.8343 0.3605 0.0874  0.1306  -0.1201 82  LYS A CA  
638   C C   . LYS A 82  ? 0.6173 0.8085 0.3540 0.0578  0.1231  -0.1248 82  LYS A C   
639   O O   . LYS A 82  ? 0.5918 0.8099 0.3491 0.0379  0.1193  -0.1193 82  LYS A O   
640   C CB  . LYS A 82  ? 0.6588 0.8688 0.3670 0.1214  0.1417  -0.1260 82  LYS A CB  
641   C CG  . LYS A 82  ? 0.6598 0.9069 0.3754 0.1586  0.1493  -0.1226 82  LYS A CG  
642   C CD  . LYS A 82  ? 0.7262 0.9461 0.3822 0.1999  0.1621  -0.1272 82  LYS A CD  
643   C CE  . LYS A 82  ? 0.7425 0.9881 0.3906 0.2447  0.1698  -0.1241 82  LYS A CE  
644   N NZ  . LYS A 82  ? 0.6892 1.0456 0.3959 0.2509  0.1713  -0.1142 82  LYS A NZ  
645   N N   . ALA A 83  ? 0.6643 0.7929 0.3549 0.0547  0.1220  -0.1345 83  ALA A N   
646   C CA  . ALA A 83  ? 0.6869 0.7826 0.3502 0.0213  0.1153  -0.1407 83  ALA A CA  
647   C C   . ALA A 83  ? 0.7279 0.8101 0.3519 0.0144  0.1194  -0.1462 83  ALA A C   
648   O O   . ALA A 83  ? 0.7112 0.8208 0.3472 -0.0117 0.1130  -0.1438 83  ALA A O   
649   C CB  . ALA A 83  ? 0.7353 0.7622 0.3503 0.0152  0.1152  -0.1507 83  ALA A CB  
650   N N   . ASN A 84  ? 0.7855 0.8285 0.3604 0.0407  0.1308  -0.1529 84  ASN A N   
651   C CA  . ASN A 84  ? 0.8328 0.8556 0.3629 0.0368  0.1363  -0.1593 84  ASN A CA  
652   C C   . ASN A 84  ? 0.8351 0.8851 0.3700 0.0748  0.1468  -0.1548 84  ASN A C   
653   O O   . ASN A 84  ? 0.9037 0.9017 0.3768 0.1015  0.1585  -0.1622 84  ASN A O   
654   C CB  . ASN A 84  ? 0.9290 0.8545 0.3664 0.0262  0.1425  -0.1752 84  ASN A CB  
655   C CG  . ASN A 84  ? 0.9358 0.8350 0.3626 -0.0128 0.1335  -0.1805 84  ASN A CG  
656   O OD1 . ASN A 84  ? 0.8848 0.8388 0.3563 -0.0443 0.1216  -0.1754 84  ASN A OD1 
657   N ND2 . ASN A 84  ? 1.0049 0.8202 0.3676 -0.0089 0.1404  -0.1900 84  ASN A ND2 
658   N N   . PRO A 85  ? 0.7679 0.8971 0.3698 0.0775  0.1441  -0.1425 85  PRO A N   
659   C CA  . PRO A 85  ? 0.7664 0.9345 0.3768 0.1090  0.1539  -0.1376 85  PRO A CA  
660   C C   . PRO A 85  ? 0.8188 0.9601 0.3788 0.1139  0.1609  -0.1441 85  PRO A C   
661   O O   . PRO A 85  ? 0.8173 0.9576 0.3739 0.0843  0.1554  -0.1459 85  PRO A O   
662   C CB  . PRO A 85  ? 0.6918 0.9384 0.3749 0.0949  0.1490  -0.1242 85  PRO A CB  
663   C CG  . PRO A 85  ? 0.6556 0.9005 0.3687 0.0687  0.1383  -0.1212 85  PRO A CG  
664   C CD  . PRO A 85  ? 0.6991 0.8816 0.3637 0.0516  0.1337  -0.1322 85  PRO A CD  
665   N N   . VAL A 86  ? 0.8674 0.9913 0.3870 0.1531  0.1736  -0.1471 86  VAL A N   
666   C CA  . VAL A 86  ? 0.9285 1.0160 0.3893 0.1622  0.1824  -0.1544 86  VAL A CA  
667   C C   . VAL A 86  ? 0.8854 1.0419 0.3875 0.1543  0.1815  -0.1465 86  VAL A C   
668   O O   . VAL A 86  ? 0.9127 1.0484 0.3853 0.1369  0.1813  -0.1518 86  VAL A O   
669   C CB  . VAL A 86  ? 1.0029 1.0481 0.3995 0.2148  0.1986  -0.1584 86  VAL A CB  
670   C CG1 . VAL A 86  ? 1.0616 1.0224 0.4019 0.2250  0.2021  -0.1662 86  VAL A CG1 
671   C CG2 . VAL A 86  ? 0.9608 1.0955 0.4061 0.2527  0.2042  -0.1461 86  VAL A CG2 
672   N N   . ASN A 87  ? 0.8238 1.0610 0.3892 0.1643  0.1816  -0.1341 87  ASN A N   
673   C CA  . ASN A 87  ? 0.7863 1.0869 0.3884 0.1560  0.1826  -0.1255 87  ASN A CA  
674   C C   . ASN A 87  ? 0.7343 1.0571 0.3800 0.1161  0.1716  -0.1188 87  ASN A C   
675   O O   . ASN A 87  ? 0.6840 1.0564 0.3821 0.1065  0.1694  -0.1082 87  ASN A O   
676   C CB  . ASN A 87  ? 0.7541 1.1318 0.3964 0.1787  0.1896  -0.1155 87  ASN A CB  
677   C CG  . ASN A 87  ? 0.8061 1.1834 0.4053 0.2259  0.2026  -0.1188 87  ASN A CG  
678   O OD1 . ASN A 87  ? 0.8649 1.1918 0.4065 0.2402  0.2088  -0.1265 87  ASN A OD1 
679   N ND2 . ASN A 87  ? 0.7890 1.2267 0.4127 0.2513  0.2077  -0.1124 87  ASN A ND2 
680   N N   . ASP A 88  ? 0.7536 1.0395 0.3715 0.0932  0.1658  -0.1249 88  ASP A N   
681   C CA  . ASP A 88  ? 0.7117 1.0233 0.3628 0.0624  0.1564  -0.1172 88  ASP A CA  
682   C C   . ASP A 88  ? 0.7140 1.0525 0.3612 0.0585  0.1595  -0.1130 88  ASP A C   
683   O O   . ASP A 88  ? 0.6982 1.0761 0.3664 0.0719  0.1670  -0.1052 88  ASP A O   
684   C CB  . ASP A 88  ? 0.7283 0.9982 0.3555 0.0379  0.1468  -0.1254 88  ASP A CB  
685   C CG  . ASP A 88  ? 0.6846 0.9909 0.3487 0.0133  0.1371  -0.1152 88  ASP A CG  
686   O OD1 . ASP A 88  ? 0.6445 0.9945 0.3497 0.0168  0.1388  -0.1014 88  ASP A OD1 
687   O OD2 . ASP A 88  ? 0.6968 0.9872 0.3429 -0.0092 0.1290  -0.1207 88  ASP A OD2 
688   N N   . LEU A 89  ? 0.7349 1.0574 0.3540 0.0384  0.1541  -0.1183 89  LEU A N   
689   C CA  . LEU A 89  ? 0.7417 1.0889 0.3521 0.0351  0.1566  -0.1151 89  LEU A CA  
690   C C   . LEU A 89  ? 0.8000 1.1100 0.3554 0.0506  0.1653  -0.1278 89  LEU A C   
691   O O   . LEU A 89  ? 0.8524 1.1124 0.3530 0.0375  0.1640  -0.1417 89  LEU A O   
692   C CB  . LEU A 89  ? 0.7396 1.0989 0.3439 0.0067  0.1467  -0.1143 89  LEU A CB  
693   C CG  . LEU A 89  ? 0.6905 1.1022 0.3405 0.0011  0.1424  -0.0963 89  LEU A CG  
694   C CD1 . LEU A 89  ? 0.6502 1.0715 0.3439 0.0114  0.1449  -0.0853 89  LEU A CD1 
695   C CD2 . LEU A 89  ? 0.6901 1.1154 0.3328 -0.0225 0.1313  -0.0967 89  LEU A CD2 
696   N N   . CYS A 90  ? 0.7965 1.1301 0.3612 0.0772  0.1754  -0.1231 90  CYS A N   
697   C CA  . CYS A 90  ? 0.8547 1.1568 0.3658 0.0999  0.1858  -0.1330 90  CYS A CA  
698   C C   . CYS A 90  ? 0.8907 1.1759 0.3613 0.0810  0.1843  -0.1400 90  CYS A C   
699   O O   . CYS A 90  ? 0.9587 1.1804 0.3618 0.0790  0.1878  -0.1551 90  CYS A O   
700   C CB  . CYS A 90  ? 0.8381 1.1900 0.3735 0.1302  0.1964  -0.1241 90  CYS A CB  
701   S SG  . CYS A 90  ? 0.7764 1.2078 0.3734 0.1160  0.1961  -0.1061 90  CYS A SG  
702   N N   . TYR A 91  ? 0.7288 0.9228 0.5652 0.2119  0.1192  -0.2209 91  TYR A N   
703   C CA  . TYR A 91  ? 0.7627 0.9275 0.5611 0.2028  0.1123  -0.2434 91  TYR A CA  
704   C C   . TYR A 91  ? 0.7456 0.8703 0.5457 0.1799  0.0908  -0.2339 91  TYR A C   
705   O O   . TYR A 91  ? 0.7012 0.8410 0.5108 0.1609  0.0851  -0.2082 91  TYR A O   
706   C CB  . TYR A 91  ? 0.7601 0.9691 0.5281 0.1925  0.1214  -0.2421 91  TYR A CB  
707   C CG  . TYR A 91  ? 0.8075 1.0020 0.5328 0.1906  0.1185  -0.2700 91  TYR A CG  
708   C CD1 . TYR A 91  ? 0.8071 0.9784 0.5135 0.1681  0.1004  -0.2690 91  TYR A CD1 
709   C CD2 . TYR A 91  ? 0.8555 1.0640 0.5592 0.2114  0.1339  -0.2980 91  TYR A CD2 
710   C CE1 . TYR A 91  ? 0.8527 1.0189 0.5193 0.1642  0.0959  -0.2949 91  TYR A CE1 
711   C CE2 . TYR A 91  ? 0.9035 1.1033 0.5647 0.2080  0.1309  -0.3266 91  TYR A CE2 
712   C CZ  . TYR A 91  ? 0.9019 1.0823 0.5443 0.1833  0.1109  -0.3250 91  TYR A CZ  
713   O OH  . TYR A 91  ? 0.9520 1.1318 0.5513 0.1778  0.1063  -0.3537 91  TYR A OH  
714   N N   . PRO A 92  ? 0.7844 0.8578 0.5758 0.1806  0.0799  -0.2556 92  PRO A N   
715   C CA  . PRO A 92  ? 0.7716 0.8081 0.5690 0.1597  0.0595  -0.2461 92  PRO A CA  
716   C C   . PRO A 92  ? 0.7410 0.7991 0.5206 0.1341  0.0510  -0.2292 92  PRO A C   
717   O O   . PRO A 92  ? 0.7498 0.8387 0.5006 0.1307  0.0575  -0.2347 92  PRO A O   
718   C CB  . PRO A 92  ? 0.8310 0.8191 0.6113 0.1617  0.0526  -0.2800 92  PRO A CB  
719   C CG  . PRO A 92  ? 0.8742 0.8613 0.6520 0.1899  0.0708  -0.3049 92  PRO A CG  
720   C CD  . PRO A 92  ? 0.8476 0.8961 0.6213 0.1992  0.0874  -0.2924 92  PRO A CD  
721   N N   . GLY A 93  ? 0.7085 0.7518 0.5060 0.1178  0.0379  -0.2071 93  GLY A N   
722   C CA  . GLY A 93  ? 0.6815 0.7416 0.4672 0.0961  0.0312  -0.1885 93  GLY A CA  
723   C C   . GLY A 93  ? 0.6410 0.6909 0.4530 0.0830  0.0224  -0.1615 93  GLY A C   
724   O O   . GLY A 93  ? 0.6374 0.6624 0.4743 0.0876  0.0167  -0.1581 93  GLY A O   
725   N N   . ASP A 94  ? 0.6141 0.6840 0.4204 0.0677  0.0227  -0.1413 94  ASP A N   
726   C CA  . ASP A 94  ? 0.5766 0.6416 0.4046 0.0551  0.0181  -0.1162 94  ASP A CA  
727   C C   . ASP A 94  ? 0.5471 0.6445 0.3789 0.0500  0.0336  -0.0988 94  ASP A C   
728   O O   . ASP A 94  ? 0.5555 0.6779 0.3695 0.0512  0.0448  -0.1005 94  ASP A O   
729   C CB  . ASP A 94  ? 0.5781 0.6297 0.3983 0.0397  0.0040  -0.1079 94  ASP A CB  
730   C CG  . ASP A 94  ? 0.6121 0.6323 0.4285 0.0391  -0.0120 -0.1266 94  ASP A CG  
731   O OD1 . ASP A 94  ? 0.6109 0.6038 0.4504 0.0408  -0.0189 -0.1255 94  ASP A OD1 
732   O OD2 . ASP A 94  ? 0.6435 0.6675 0.4338 0.0355  -0.0177 -0.1421 94  ASP A OD2 
733   N N   . PHE A 95  ? 0.5160 0.6130 0.3708 0.0433  0.0347  -0.0825 95  PHE A N   
734   C CA  . PHE A 95  ? 0.4910 0.6112 0.3515 0.0332  0.0489  -0.0674 95  PHE A CA  
735   C C   . PHE A 95  ? 0.4757 0.5807 0.3393 0.0190  0.0443  -0.0497 95  PHE A C   
736   O O   . PHE A 95  ? 0.4637 0.5515 0.3424 0.0156  0.0348  -0.0436 95  PHE A O   
737   C CB  . PHE A 95  ? 0.4724 0.6093 0.3555 0.0355  0.0550  -0.0657 95  PHE A CB  
738   C CG  . PHE A 95  ? 0.4601 0.6289 0.3462 0.0268  0.0726  -0.0602 95  PHE A CG  
739   C CD1 . PHE A 95  ? 0.4476 0.6140 0.3342 0.0096  0.0809  -0.0466 95  PHE A CD1 
740   C CD2 . PHE A 95  ? 0.4646 0.6652 0.3552 0.0356  0.0823  -0.0683 95  PHE A CD2 
741   C CE1 . PHE A 95  ? 0.4423 0.6332 0.3338 -0.0011 0.0984  -0.0429 95  PHE A CE1 
742   C CE2 . PHE A 95  ? 0.4556 0.6875 0.3515 0.0242  0.0985  -0.0633 95  PHE A CE2 
743   C CZ  . PHE A 95  ? 0.4457 0.6705 0.3419 0.0045  0.1065  -0.0513 95  PHE A CZ  
744   N N   . ASN A 96  ? 0.4782 0.5914 0.3286 0.0123  0.0524  -0.0393 96  ASN A N   
745   C CA  . ASN A 96  ? 0.4684 0.5694 0.3225 0.0023  0.0505  -0.0203 96  ASN A CA  
746   C C   . ASN A 96  ? 0.4440 0.5415 0.3182 -0.0071 0.0612  -0.0092 96  ASN A C   
747   O O   . ASN A 96  ? 0.4389 0.5509 0.3174 -0.0117 0.0771  -0.0097 96  ASN A O   
748   C CB  . ASN A 96  ? 0.4830 0.5972 0.3195 0.0007  0.0584  -0.0085 96  ASN A CB  
749   C CG  . ASN A 96  ? 0.4809 0.5853 0.3202 -0.0046 0.0530  0.0118  96  ASN A CG  
750   O OD1 . ASN A 96  ? 0.4850 0.5797 0.3238 -0.0047 0.0349  0.0096  96  ASN A OD1 
751   N ND2 . ASN A 96  ? 0.4774 0.5844 0.3220 -0.0092 0.0696  0.0327  96  ASN A ND2 
752   N N   . ASP A 97  ? 0.4315 0.5119 0.3177 -0.0114 0.0527  -0.0004 97  ASP A N   
753   C CA  . ASP A 97  ? 0.4123 0.4889 0.3153 -0.0203 0.0617  0.0068  97  ASP A CA  
754   C C   . ASP A 97  ? 0.4018 0.4956 0.3134 -0.0215 0.0673  -0.0053 97  ASP A C   
755   O O   . ASP A 97  ? 0.3970 0.5009 0.3138 -0.0317 0.0831  -0.0054 97  ASP A O   
756   C CB  . ASP A 97  ? 0.4152 0.4878 0.3185 -0.0283 0.0800  0.0214  97  ASP A CB  
757   C CG  . ASP A 97  ? 0.4210 0.4816 0.3228 -0.0261 0.0745  0.0393  97  ASP A CG  
758   O OD1 . ASP A 97  ? 0.4192 0.4741 0.3230 -0.0229 0.0562  0.0399  97  ASP A OD1 
759   O OD2 . ASP A 97  ? 0.4299 0.4883 0.3306 -0.0277 0.0892  0.0547  97  ASP A OD2 
760   N N   . TYR A 98  ? 0.4013 0.4993 0.3155 -0.0114 0.0547  -0.0153 98  TYR A N   
761   C CA  . TYR A 98  ? 0.3934 0.5149 0.3177 -0.0086 0.0577  -0.0239 98  TYR A CA  
762   C C   . TYR A 98  ? 0.3758 0.5051 0.3152 -0.0182 0.0591  -0.0183 98  TYR A C   
763   O O   . TYR A 98  ? 0.3690 0.5251 0.3148 -0.0257 0.0685  -0.0229 98  TYR A O   
764   C CB  . TYR A 98  ? 0.4041 0.5221 0.3304 0.0081  0.0445  -0.0323 98  TYR A CB  
765   C CG  . TYR A 98  ? 0.4018 0.5484 0.3400 0.0171  0.0474  -0.0385 98  TYR A CG  
766   C CD1 . TYR A 98  ? 0.3982 0.5780 0.3365 0.0128  0.0616  -0.0431 98  TYR A CD1 
767   C CD2 . TYR A 98  ? 0.4062 0.5485 0.3581 0.0306  0.0365  -0.0377 98  TYR A CD2 
768   C CE1 . TYR A 98  ? 0.3964 0.6102 0.3483 0.0218  0.0637  -0.0466 98  TYR A CE1 
769   C CE2 . TYR A 98  ? 0.4060 0.5790 0.3717 0.0420  0.0396  -0.0394 98  TYR A CE2 
770   C CZ  . TYR A 98  ? 0.4000 0.6115 0.3655 0.0378  0.0526  -0.0440 98  TYR A CZ  
771   O OH  . TYR A 98  ? 0.3999 0.6494 0.3816 0.0496  0.0551  -0.0436 98  TYR A OH  
772   N N   . GLU A 99  ? 0.3699 0.4796 0.3142 -0.0192 0.0496  -0.0089 99  GLU A N   
773   C CA  . GLU A 99  ? 0.3567 0.4753 0.3127 -0.0268 0.0500  -0.0032 99  GLU A CA  
774   C C   . GLU A 99  ? 0.3536 0.4743 0.3071 -0.0431 0.0676  -0.0039 99  GLU A C   
775   O O   . GLU A 99  ? 0.3478 0.4902 0.3066 -0.0532 0.0745  -0.0090 99  GLU A O   
776   C CB  . GLU A 99  ? 0.3548 0.4527 0.3173 -0.0233 0.0365  0.0088  99  GLU A CB  
777   C CG  . GLU A 99  ? 0.3620 0.4542 0.3324 -0.0098 0.0204  0.0097  99  GLU A CG  
778   C CD  . GLU A 99  ? 0.3797 0.4529 0.3398 -0.0011 0.0143  0.0009  99  GLU A CD  
779   O OE1 . GLU A 99  ? 0.3846 0.4436 0.3334 -0.0058 0.0147  0.0021  99  GLU A OE1 
780   O OE2 . GLU A 99  ? 0.3911 0.4659 0.3544 0.0112  0.0097  -0.0069 99  GLU A OE2 
781   N N   . GLU A 100 ? 0.3609 0.4600 0.3067 -0.0456 0.0757  0.0012  100 GLU A N   
782   C CA  . GLU A 100 ? 0.3661 0.4588 0.3113 -0.0593 0.0961  0.0013  100 GLU A CA  
783   C C   . GLU A 100 ? 0.3711 0.4851 0.3158 -0.0694 0.1097  -0.0112 100 GLU A C   
784   O O   . GLU A 100 ? 0.3758 0.4937 0.3244 -0.0853 0.1246  -0.0182 100 GLU A O   
785   C CB  . GLU A 100 ? 0.3762 0.4440 0.3159 -0.0560 0.1022  0.0145  100 GLU A CB  
786   C CG  . GLU A 100 ? 0.3724 0.4231 0.3170 -0.0512 0.0942  0.0286  100 GLU A CG  
787   C CD  . GLU A 100 ? 0.3718 0.4157 0.3247 -0.0601 0.1075  0.0296  100 GLU A CD  
788   O OE1 . GLU A 100 ? 0.3840 0.4193 0.3372 -0.0694 0.1289  0.0259  100 GLU A OE1 
789   O OE2 . GLU A 100 ? 0.3629 0.4093 0.3222 -0.0583 0.0978  0.0336  100 GLU A OE2 
790   N N   . LEU A 101 ? 0.3734 0.5025 0.3136 -0.0613 0.1054  -0.0154 101 LEU A N   
791   C CA  . LEU A 101 ? 0.3776 0.5341 0.3200 -0.0705 0.1173  -0.0256 101 LEU A CA  
792   C C   . LEU A 101 ? 0.3672 0.5578 0.3201 -0.0764 0.1125  -0.0351 101 LEU A C   
793   O O   . LEU A 101 ? 0.3705 0.5812 0.3287 -0.0947 0.1248  -0.0441 101 LEU A O   
794   C CB  . LEU A 101 ? 0.3841 0.5527 0.3190 -0.0576 0.1146  -0.0270 101 LEU A CB  
795   C CG  . LEU A 101 ? 0.3890 0.5906 0.3280 -0.0663 0.1281  -0.0349 101 LEU A CG  
796   C CD1 . LEU A 101 ? 0.4000 0.5919 0.3420 -0.0878 0.1498  -0.0331 101 LEU A CD1 
797   C CD2 . LEU A 101 ? 0.3987 0.6107 0.3276 -0.0509 0.1269  -0.0351 101 LEU A CD2 
798   N N   . LYS A 102 ? 0.3581 0.5570 0.3150 -0.0616 0.0947  -0.0321 102 LYS A N   
799   C CA  . LYS A 102 ? 0.3496 0.5851 0.3175 -0.0640 0.0882  -0.0351 102 LYS A CA  
800   C C   . LYS A 102 ? 0.3482 0.5873 0.3172 -0.0835 0.0954  -0.0386 102 LYS A C   
801   O O   . LYS A 102 ? 0.3467 0.6252 0.3212 -0.0964 0.0981  -0.0470 102 LYS A O   
802   C CB  . LYS A 102 ? 0.3450 0.5776 0.3187 -0.0437 0.0696  -0.0257 102 LYS A CB  
803   C CG  . LYS A 102 ? 0.3502 0.5994 0.3289 -0.0248 0.0635  -0.0273 102 LYS A CG  
804   C CD  . LYS A 102 ? 0.3536 0.5847 0.3391 -0.0054 0.0475  -0.0180 102 LYS A CD  
805   C CE  . LYS A 102 ? 0.3561 0.6220 0.3574 0.0109  0.0422  -0.0146 102 LYS A CE  
806   N NZ  . LYS A 102 ? 0.3647 0.6058 0.3755 0.0285  0.0289  -0.0034 102 LYS A NZ  
807   N N   . HIS A 103 ? 0.3512 0.5526 0.3149 -0.0856 0.0988  -0.0329 103 HIS A N   
808   C CA  . HIS A 103 ? 0.3563 0.5554 0.3192 -0.1026 0.1090  -0.0383 103 HIS A CA  
809   C C   . HIS A 103 ? 0.3729 0.5745 0.3342 -0.1249 0.1302  -0.0537 103 HIS A C   
810   O O   . HIS A 103 ? 0.3808 0.6015 0.3425 -0.1437 0.1380  -0.0673 103 HIS A O   
811   C CB  . HIS A 103 ? 0.3577 0.5157 0.3176 -0.0967 0.1101  -0.0267 103 HIS A CB  
812   C CG  . HIS A 103 ? 0.3664 0.5188 0.3249 -0.1112 0.1234  -0.0333 103 HIS A CG  
813   N ND1 . HIS A 103 ? 0.3607 0.5349 0.3203 -0.1124 0.1159  -0.0325 103 HIS A ND1 
814   C CD2 . HIS A 103 ? 0.3848 0.5117 0.3409 -0.1244 0.1455  -0.0410 103 HIS A CD2 
815   C CE1 . HIS A 103 ? 0.3752 0.5393 0.3306 -0.1260 0.1326  -0.0423 103 HIS A CE1 
816   N NE2 . HIS A 103 ? 0.3912 0.5234 0.3454 -0.1333 0.1513  -0.0483 103 HIS A NE2 
817   N N   . LEU A 104 ? 0.3822 0.5657 0.3418 -0.1240 0.1397  -0.0517 104 LEU A N   
818   C CA  . LEU A 104 ? 0.4021 0.5843 0.3635 -0.1455 0.1613  -0.0633 104 LEU A CA  
819   C C   . LEU A 104 ? 0.4018 0.6371 0.3698 -0.1609 0.1602  -0.0784 104 LEU A C   
820   O O   . LEU A 104 ? 0.4186 0.6614 0.3897 -0.1867 0.1757  -0.0941 104 LEU A O   
821   C CB  . LEU A 104 ? 0.4110 0.5713 0.3699 -0.1380 0.1697  -0.0526 104 LEU A CB  
822   C CG  . LEU A 104 ? 0.4350 0.5533 0.3945 -0.1482 0.1933  -0.0480 104 LEU A CG  
823   C CD1 . LEU A 104 ? 0.4361 0.5174 0.3931 -0.1376 0.1928  -0.0364 104 LEU A CD1 
824   C CD2 . LEU A 104 ? 0.4432 0.5555 0.4003 -0.1408 0.2001  -0.0351 104 LEU A CD2 
825   N N   . LEU A 105 ? 0.3861 0.6584 0.3579 -0.1452 0.1425  -0.0736 105 LEU A N   
826   C CA  . LEU A 105 ? 0.3835 0.7165 0.3647 -0.1550 0.1386  -0.0831 105 LEU A CA  
827   C C   . LEU A 105 ? 0.3848 0.7516 0.3673 -0.1709 0.1345  -0.0933 105 LEU A C   
828   O O   . LEU A 105 ? 0.3876 0.8082 0.3776 -0.1876 0.1349  -0.1042 105 LEU A O   
829   C CB  . LEU A 105 ? 0.3687 0.7294 0.3556 -0.1284 0.1219  -0.0721 105 LEU A CB  
830   C CG  . LEU A 105 ? 0.3726 0.7336 0.3602 -0.1184 0.1275  -0.0693 105 LEU A CG  
831   C CD1 . LEU A 105 ? 0.3637 0.7415 0.3556 -0.0886 0.1119  -0.0606 105 LEU A CD1 
832   C CD2 . LEU A 105 ? 0.3814 0.7833 0.3784 -0.1413 0.1410  -0.0800 105 LEU A CD2 
833   N N   . SER A 106 ? 0.3841 0.7261 0.3596 -0.1661 0.1302  -0.0891 106 SER A N   
834   C CA  . SER A 106 ? 0.3900 0.7633 0.3628 -0.1820 0.1284  -0.0996 106 SER A CA  
835   C C   . SER A 106 ? 0.4168 0.7841 0.3851 -0.2159 0.1496  -0.1244 106 SER A C   
836   O O   . SER A 106 ? 0.4273 0.8348 0.3925 -0.2363 0.1498  -0.1405 106 SER A O   
837   C CB  . SER A 106 ? 0.3841 0.7316 0.3506 -0.1676 0.1207  -0.0874 106 SER A CB  
838   O OG  . SER A 106 ? 0.3963 0.6843 0.3560 -0.1702 0.1355  -0.0889 106 SER A OG  
839   N N   . ARG A 107 ? 0.4327 0.7502 0.4008 -0.2223 0.1680  -0.1274 107 ARG A N   
840   C CA  . ARG A 107 ? 0.4655 0.7673 0.4332 -0.2549 0.1918  -0.1506 107 ARG A CA  
841   C C   . ARG A 107 ? 0.4726 0.8026 0.4514 -0.2730 0.1992  -0.1586 107 ARG A C   
842   O O   . ARG A 107 ? 0.5028 0.8131 0.4847 -0.3009 0.2208  -0.1757 107 ARG A O   
843   C CB  . ARG A 107 ? 0.4856 0.7121 0.4501 -0.2511 0.2117  -0.1457 107 ARG A CB  
844   C CG  . ARG A 107 ? 0.4957 0.6940 0.4512 -0.2481 0.2161  -0.1490 107 ARG A CG  
845   C CD  . ARG A 107 ? 0.5289 0.6596 0.4856 -0.2537 0.2439  -0.1514 107 ARG A CD  
846   N NE  . ARG A 107 ? 0.5297 0.6257 0.4814 -0.2359 0.2461  -0.1408 107 ARG A NE  
847   C CZ  . ARG A 107 ? 0.5589 0.6306 0.5057 -0.2467 0.2643  -0.1573 107 ARG A CZ  
848   N NH1 . ARG A 107 ? 0.5947 0.6682 0.5387 -0.2781 0.2827  -0.1894 107 ARG A NH1 
849   N NH2 . ARG A 107 ? 0.5551 0.6010 0.4999 -0.2264 0.2648  -0.1426 107 ARG A NH2 
850   N N   . ILE A 108 ? 0.4478 0.8227 0.4342 -0.2575 0.1832  -0.1461 108 ILE A N   
851   C CA  . ILE A 108 ? 0.4520 0.8563 0.4505 -0.2698 0.1902  -0.1489 108 ILE A CA  
852   C C   . ILE A 108 ? 0.4393 0.9287 0.4481 -0.2764 0.1755  -0.1539 108 ILE A C   
853   O O   . ILE A 108 ? 0.4155 0.9376 0.4256 -0.2513 0.1555  -0.1402 108 ILE A O   
854   C CB  . ILE A 108 ? 0.4400 0.8197 0.4397 -0.2424 0.1894  -0.1274 108 ILE A CB  
855   C CG1 . ILE A 108 ? 0.4550 0.7597 0.4468 -0.2382 0.2053  -0.1197 108 ILE A CG1 
856   C CG2 . ILE A 108 ? 0.4446 0.8632 0.4574 -0.2532 0.1968  -0.1285 108 ILE A CG2 
857   C CD1 . ILE A 108 ? 0.4431 0.7248 0.4302 -0.2081 0.2000  -0.0977 108 ILE A CD1 
858   N N   . ASN A 109 ? 0.4576 0.9831 0.4762 -0.3105 0.1863  -0.1720 109 ASN A N   
859   C CA  . ASN A 109 ? 0.4492 1.0652 0.4810 -0.3210 0.1739  -0.1764 109 ASN A CA  
860   C C   . ASN A 109 ? 0.4440 1.0953 0.4936 -0.3188 0.1776  -0.1675 109 ASN A C   
861   O O   . ASN A 109 ? 0.4287 1.1554 0.4918 -0.3115 0.1642  -0.1607 109 ASN A O   
862   C CB  . ASN A 109 ? 0.4761 1.1257 0.5071 -0.3655 0.1804  -0.2060 109 ASN A CB  
863   C CG  . ASN A 109 ? 0.4703 1.1518 0.4892 -0.3630 0.1647  -0.2107 109 ASN A CG  
864   O OD1 . ASN A 109 ? 0.4690 1.2335 0.4937 -0.3763 0.1520  -0.2167 109 ASN A OD1 
865   N ND2 . ASN A 109 ? 0.4675 1.0894 0.4705 -0.3453 0.1651  -0.2055 109 ASN A ND2 
866   N N   . HIS A 110 ? 0.4578 1.0597 0.5087 -0.3240 0.1966  -0.1653 110 HIS A N   
867   C CA  . HIS A 110 ? 0.4550 1.0907 0.5217 -0.3213 0.2022  -0.1554 110 HIS A CA  
868   C C   . HIS A 110 ? 0.4621 1.0360 0.5237 -0.3074 0.2176  -0.1413 110 HIS A C   
869   O O   . HIS A 110 ? 0.4846 0.9965 0.5404 -0.3231 0.2355  -0.1455 110 HIS A O   
870   C CB  . HIS A 110 ? 0.4766 1.1656 0.5611 -0.3657 0.2127  -0.1737 110 HIS A CB  
871   C CG  . HIS A 110 ? 0.4686 1.2204 0.5736 -0.3617 0.2135  -0.1623 110 HIS A CG  
872   N ND1 . HIS A 110 ? 0.4917 1.2672 0.6145 -0.3978 0.2307  -0.1707 110 HIS A ND1 
873   C CD2 . HIS A 110 ? 0.4432 1.2377 0.5550 -0.3253 0.2009  -0.1430 110 HIS A CD2 
874   C CE1 . HIS A 110 ? 0.4780 1.3140 0.6177 -0.3834 0.2280  -0.1559 110 HIS A CE1 
875   N NE2 . HIS A 110 ? 0.4495 1.2969 0.5823 -0.3384 0.2106  -0.1398 110 HIS A NE2 
876   N N   . PHE A 111 ? 0.4455 1.0408 0.5100 -0.2769 0.2113  -0.1239 111 PHE A N   
877   C CA  . PHE A 111 ? 0.4536 1.0133 0.5140 -0.2644 0.2251  -0.1096 111 PHE A CA  
878   C C   . PHE A 111 ? 0.4628 1.0788 0.5428 -0.2802 0.2367  -0.1081 111 PHE A C   
879   O O   . PHE A 111 ? 0.4512 1.1405 0.5466 -0.2811 0.2268  -0.1112 111 PHE A O   
880   C CB  . PHE A 111 ? 0.4338 0.9801 0.4810 -0.2193 0.2112  -0.0940 111 PHE A CB  
881   C CG  . PHE A 111 ? 0.4301 0.9081 0.4576 -0.2029 0.2050  -0.0895 111 PHE A CG  
882   C CD1 . PHE A 111 ? 0.4487 0.8661 0.4682 -0.2164 0.2206  -0.0877 111 PHE A CD1 
883   C CD2 . PHE A 111 ? 0.4105 0.8855 0.4300 -0.1729 0.1848  -0.0847 111 PHE A CD2 
884   C CE1 . PHE A 111 ? 0.4449 0.8070 0.4490 -0.2002 0.2147  -0.0813 111 PHE A CE1 
885   C CE2 . PHE A 111 ? 0.4078 0.8251 0.4116 -0.1596 0.1786  -0.0796 111 PHE A CE2 
886   C CZ  . PHE A 111 ? 0.4234 0.7874 0.4196 -0.1730 0.1931  -0.0777 111 PHE A CZ  
887   N N   . GLU A 112 ? 0.4848 1.0704 0.5662 -0.2917 0.2579  -0.1006 112 GLU A N   
888   C CA  . GLU A 112 ? 0.4933 1.1286 0.5917 -0.2993 0.2702  -0.0927 112 GLU A CA  
889   C C   . GLU A 112 ? 0.4947 1.1014 0.5787 -0.2688 0.2771  -0.0722 112 GLU A C   
890   O O   . GLU A 112 ? 0.5095 1.0520 0.5803 -0.2678 0.2878  -0.0635 112 GLU A O   
891   C CB  . GLU A 112 ? 0.5253 1.1598 0.6420 -0.3474 0.2925  -0.1012 112 GLU A CB  
892   C CG  . GLU A 112 ? 0.5307 1.2399 0.6721 -0.3624 0.3011  -0.0966 112 GLU A CG  
893   C CD  . GLU A 112 ? 0.5673 1.2525 0.7222 -0.3952 0.3297  -0.0904 112 GLU A CD  
894   O OE1 . GLU A 112 ? 0.5957 1.2304 0.7533 -0.4280 0.3426  -0.1028 112 GLU A OE1 
895   O OE2 . GLU A 112 ? 0.5711 1.2873 0.7348 -0.3879 0.3408  -0.0726 112 GLU A OE2 
896   N N   . LYS A 113 ? 0.4823 1.1398 0.5688 -0.2431 0.2717  -0.0642 113 LYS A N   
897   C CA  . LYS A 113 ? 0.4861 1.1249 0.5550 -0.2124 0.2765  -0.0484 113 LYS A CA  
898   C C   . LYS A 113 ? 0.5114 1.1562 0.5884 -0.2310 0.3018  -0.0348 113 LYS A C   
899   O O   . LYS A 113 ? 0.5197 1.2142 0.6215 -0.2579 0.3126  -0.0368 113 LYS A O   
900   C CB  . LYS A 113 ? 0.4696 1.1588 0.5379 -0.1769 0.2634  -0.0481 113 LYS A CB  
901   C CG  . LYS A 113 ? 0.4748 1.1398 0.5181 -0.1410 0.2633  -0.0389 113 LYS A CG  
902   C CD  . LYS A 113 ? 0.4594 1.1250 0.4931 -0.1045 0.2427  -0.0460 113 LYS A CD  
903   C CE  . LYS A 113 ? 0.4496 1.1877 0.5061 -0.0927 0.2379  -0.0497 113 LYS A CE  
904   N NZ  . LYS A 113 ? 0.4396 1.1664 0.4893 -0.0577 0.2193  -0.0548 113 LYS A NZ  
905   N N   . ILE A 114 ? 0.5254 1.1231 0.5829 -0.2180 0.3111  -0.0192 114 ILE A N   
906   C CA  . ILE A 114 ? 0.5516 1.1571 0.6145 -0.2294 0.3354  -0.0001 114 ILE A CA  
907   C C   . ILE A 114 ? 0.5572 1.1522 0.5927 -0.1949 0.3362  0.0164  114 ILE A C   
908   O O   . ILE A 114 ? 0.5481 1.1058 0.5595 -0.1699 0.3209  0.0142  114 ILE A O   
909   C CB  . ILE A 114 ? 0.5795 1.1317 0.6526 -0.2638 0.3555  0.0069  114 ILE A CB  
910   C CG1 . ILE A 114 ? 0.5795 1.0565 0.6322 -0.2517 0.3489  0.0090  114 ILE A CG1 
911   C CG2 . ILE A 114 ? 0.5852 1.1575 0.6869 -0.3054 0.3602  -0.0116 114 ILE A CG2 
912   C CD1 . ILE A 114 ? 0.6140 1.0351 0.6716 -0.2697 0.3733  0.0276  114 ILE A CD1 
913   N N   . GLN A 115 ? 0.5750 1.2067 0.6142 -0.1955 0.3544  0.0327  115 GLN A N   
914   C CA  . GLN A 115 ? 0.5864 1.2183 0.5980 -0.1660 0.3579  0.0487  115 GLN A CA  
915   C C   . GLN A 115 ? 0.6127 1.1949 0.6171 -0.1766 0.3745  0.0736  115 GLN A C   
916   O O   . GLN A 115 ? 0.6342 1.2142 0.6612 -0.2064 0.3965  0.0876  115 GLN A O   
917   C CB  . GLN A 115 ? 0.5939 1.2988 0.6120 -0.1581 0.3699  0.0548  115 GLN A CB  
918   C CG  . GLN A 115 ? 0.6197 1.3323 0.6159 -0.1432 0.3853  0.0785  115 GLN A CG  
919   C CD  . GLN A 115 ? 0.6254 1.4132 0.6225 -0.1273 0.3944  0.0798  115 GLN A CD  
920   O OE1 . GLN A 115 ? 0.6103 1.4277 0.6016 -0.1021 0.3809  0.0603  115 GLN A OE1 
921   N NE2 . GLN A 115 ? 0.6504 1.4690 0.6561 -0.1407 0.4190  0.1044  115 GLN A NE2 
922   N N   . ILE A 116 ? 0.6136 1.1576 0.5888 -0.1527 0.3643  0.0802  116 ILE A N   
923   C CA  . ILE A 116 ? 0.6397 1.1422 0.6071 -0.1563 0.3789  0.1087  116 ILE A CA  
924   C C   . ILE A 116 ? 0.6589 1.1923 0.6000 -0.1327 0.3852  0.1298  116 ILE A C   
925   O O   . ILE A 116 ? 0.6878 1.2217 0.6330 -0.1414 0.4073  0.1604  116 ILE A O   
926   C CB  . ILE A 116 ? 0.6316 1.0693 0.5890 -0.1510 0.3655  0.1062  116 ILE A CB  
927   C CG1 . ILE A 116 ? 0.6045 1.0429 0.5386 -0.1235 0.3360  0.0840  116 ILE A CG1 
928   C CG2 . ILE A 116 ? 0.6300 1.0310 0.6152 -0.1815 0.3713  0.0949  116 ILE A CG2 
929   C CD1 . ILE A 116 ? 0.6006 0.9854 0.5203 -0.1133 0.3234  0.0885  116 ILE A CD1 
930   N N   . ILE A 117 ? 0.6473 1.2066 0.5615 -0.1033 0.3669  0.1135  117 ILE A N   
931   C CA  . ILE A 117 ? 0.6677 1.2667 0.5533 -0.0807 0.3718  0.1256  117 ILE A CA  
932   C C   . ILE A 117 ? 0.6625 1.3231 0.5509 -0.0703 0.3729  0.1071  117 ILE A C   
933   O O   . ILE A 117 ? 0.6427 1.3065 0.5272 -0.0550 0.3544  0.0786  117 ILE A O   
934   C CB  . ILE A 117 ? 0.6676 1.2444 0.5154 -0.0539 0.3507  0.1191  117 ILE A CB  
935   C CG1 . ILE A 117 ? 0.6823 1.2174 0.5243 -0.0589 0.3549  0.1486  117 ILE A CG1 
936   C CG2 . ILE A 117 ? 0.6861 1.3127 0.5008 -0.0284 0.3503  0.1147  117 ILE A CG2 
937   C CD1 . ILE A 117 ? 0.6672 1.1435 0.5341 -0.0775 0.3521  0.1476  117 ILE A CD1 
938   N N   . PRO A 118 ? 0.6824 1.3932 0.5805 -0.0777 0.3960  0.1252  118 PRO A N   
939   C CA  . PRO A 118 ? 0.6807 1.4562 0.5803 -0.0633 0.3990  0.1099  118 PRO A CA  
940   C C   . PRO A 118 ? 0.6920 1.4842 0.5495 -0.0261 0.3881  0.0951  118 PRO A C   
941   O O   . PRO A 118 ? 0.7127 1.4923 0.5384 -0.0158 0.3878  0.1083  118 PRO A O   
942   C CB  . PRO A 118 ? 0.7040 1.5265 0.6221 -0.0815 0.4283  0.1386  118 PRO A CB  
943   C CG  . PRO A 118 ? 0.7136 1.4881 0.6518 -0.1127 0.4401  0.1635  118 PRO A CG  
944   C CD  . PRO A 118 ? 0.7080 1.4180 0.6224 -0.1015 0.4221  0.1610  118 PRO A CD  
945   N N   . LYS A 119 ? 0.6823 1.5035 0.5404 -0.0063 0.3799  0.0675  119 LYS A N   
946   C CA  . LYS A 119 ? 0.6989 1.5326 0.5191 0.0285  0.3715  0.0468  119 LYS A CA  
947   C C   . LYS A 119 ? 0.7339 1.6233 0.5316 0.0391  0.3926  0.0621  119 LYS A C   
948   O O   . LYS A 119 ? 0.7593 1.6500 0.5150 0.0597  0.3885  0.0554  119 LYS A O   
949   C CB  . LYS A 119 ? 0.6844 1.5349 0.5179 0.0478  0.3622  0.0166  119 LYS A CB  
950   C CG  . LYS A 119 ? 0.7024 1.5417 0.4998 0.0823  0.3499  -0.0118 119 LYS A CG  
951   C CD  . LYS A 119 ? 0.6887 1.5337 0.5066 0.1009  0.3414  -0.0374 119 LYS A CD  
952   C CE  . LYS A 119 ? 0.7187 1.5623 0.5045 0.1372  0.3379  -0.0667 119 LYS A CE  
953   N NZ  . LYS A 119 ? 0.7122 1.5708 0.5235 0.1593  0.3363  -0.0858 119 LYS A NZ  
954   N N   . SER A 120 ? 0.7377 1.6767 0.5633 0.0235  0.4153  0.0823  120 SER A N   
955   C CA  . SER A 120 ? 0.7705 1.7676 0.5804 0.0292  0.4389  0.1037  120 SER A CA  
956   C C   . SER A 120 ? 0.7928 1.7682 0.5781 0.0210  0.4437  0.1343  120 SER A C   
957   O O   . SER A 120 ? 0.8245 1.8348 0.5742 0.0375  0.4522  0.1432  120 SER A O   
958   C CB  . SER A 120 ? 0.7675 1.8165 0.6207 0.0068  0.4619  0.1236  120 SER A CB  
959   O OG  . SER A 120 ? 0.7550 1.7664 0.6409 -0.0301 0.4652  0.1449  120 SER A OG  
960   N N   . SER A 121 ? 0.7789 1.6987 0.5834 -0.0033 0.4386  0.1507  121 SER A N   
961   C CA  . SER A 121 ? 0.8002 1.6976 0.5921 -0.0128 0.4461  0.1869  121 SER A CA  
962   C C   . SER A 121 ? 0.8204 1.7127 0.5608 0.0117  0.4322  0.1843  121 SER A C   
963   O O   . SER A 121 ? 0.8442 1.7394 0.5704 0.0090  0.4411  0.2191  121 SER A O   
964   C CB  . SER A 121 ? 0.7814 1.6124 0.6052 -0.0400 0.4422  0.1976  121 SER A CB  
965   O OG  . SER A 121 ? 0.7931 1.5827 0.5976 -0.0374 0.4361  0.2180  121 SER A OG  
966   N N   . TRP A 122 ? 0.8142 1.7009 0.5285 0.0345  0.4112  0.1445  122 TRP A N   
967   C CA  . TRP A 122 ? 0.8385 1.7276 0.5022 0.0558  0.3973  0.1352  122 TRP A CA  
968   C C   . TRP A 122 ? 0.8773 1.8389 0.5087 0.0733  0.4140  0.1375  122 TRP A C   
969   O O   . TRP A 122 ? 0.8892 1.8734 0.4970 0.0954  0.4091  0.1010  122 TRP A O   
970   C CB  . TRP A 122 ? 0.8225 1.6727 0.4730 0.0706  0.3700  0.0899  122 TRP A CB  
971   C CG  . TRP A 122 ? 0.7880 1.5716 0.4655 0.0548  0.3534  0.0895  122 TRP A CG  
972   C CD1 . TRP A 122 ? 0.7548 1.5118 0.4685 0.0460  0.3479  0.0732  122 TRP A CD1 
973   C CD2 . TRP A 122 ? 0.7852 1.5257 0.4560 0.0464  0.3414  0.1081  122 TRP A CD2 
974   N NE1 . TRP A 122 ? 0.7326 1.4309 0.4601 0.0323  0.3335  0.0781  122 TRP A NE1 
975   C CE2 . TRP A 122 ? 0.7501 1.4360 0.4532 0.0329  0.3298  0.0996  122 TRP A CE2 
976   C CE3 . TRP A 122 ? 0.8101 1.5580 0.4513 0.0499  0.3393  0.1324  122 TRP A CE3 
977   C CZ2 . TRP A 122 ? 0.7396 1.3755 0.4467 0.0239  0.3179  0.1134  122 TRP A CZ2 
978   C CZ3 . TRP A 122 ? 0.7986 1.4986 0.4462 0.0413  0.3266  0.1483  122 TRP A CZ3 
979   C CH2 . TRP A 122 ? 0.7636 1.4068 0.4443 0.0289  0.3168  0.1380  122 TRP A CH2 
980   N N   . SER A 123 ? 1.0995 1.5583 0.4852 -0.1009 0.4520  0.0398  123 SER A N   
981   C CA  . SER A 123 ? 1.1561 1.6288 0.5025 -0.0880 0.4827  0.0476  123 SER A CA  
982   C C   . SER A 123 ? 1.2063 1.6275 0.4783 -0.0609 0.4726  0.0388  123 SER A C   
983   O O   . SER A 123 ? 1.2514 1.6825 0.4869 -0.0387 0.4932  0.0360  123 SER A O   
984   C CB  . SER A 123 ? 1.1818 1.6622 0.5270 -0.1166 0.5067  0.0737  123 SER A CB  
985   O OG  . SER A 123 ? 1.1936 1.6171 0.5085 -0.1312 0.4884  0.0828  123 SER A OG  
986   N N   . SER A 124 ? 1.2013 1.5680 0.4513 -0.0625 0.4407  0.0344  124 SER A N   
987   C CA  . SER A 124 ? 1.2479 1.5611 0.4298 -0.0396 0.4239  0.0259  124 SER A CA  
988   C C   . SER A 124 ? 1.2299 1.5293 0.4129 -0.0151 0.3969  0.0007  124 SER A C   
989   O O   . SER A 124 ? 1.2674 1.5224 0.3972 0.0043  0.3789  -0.0089 124 SER A O   
990   C CB  . SER A 124 ? 1.2582 1.5199 0.4159 -0.0557 0.4040  0.0380  124 SER A CB  
991   O OG  . SER A 124 ? 1.3040 1.5142 0.3980 -0.0352 0.3844  0.0307  124 SER A OG  
992   N N   . HIS A 125 ? 1.1766 1.5123 0.4191 -0.0166 0.3929  -0.0091 125 HIS A N   
993   C CA  . HIS A 125 ? 1.1577 1.4822 0.4072 0.0042  0.3680  -0.0314 125 HIS A CA  
994   C C   . HIS A 125 ? 1.1379 1.5153 0.4265 0.0167  0.3843  -0.0412 125 HIS A C   
995   O O   . HIS A 125 ? 1.1195 1.5470 0.4496 0.0022  0.4082  -0.0303 125 HIS A O   
996   C CB  . HIS A 125 ? 1.1056 1.4099 0.3912 -0.0111 0.3369  -0.0338 125 HIS A CB  
997   C CG  . HIS A 125 ? 1.1238 1.3751 0.3753 -0.0185 0.3159  -0.0271 125 HIS A CG  
998   N ND1 . HIS A 125 ? 1.1203 1.3639 0.3775 -0.0432 0.3208  -0.0084 125 HIS A ND1 
999   C CD2 . HIS A 125 ? 1.1476 1.3510 0.3608 -0.0044 0.2885  -0.0363 125 HIS A CD2 
1000  C CE1 . HIS A 125 ? 1.1405 1.3351 0.3647 -0.0421 0.2981  -0.0061 125 HIS A CE1 
1001  N NE2 . HIS A 125 ? 1.1564 1.3275 0.3550 -0.0195 0.2777  -0.0226 125 HIS A NE2 
1002  N N   . GLU A 126 ? 1.1456 1.5111 0.4218 0.0436  0.3701  -0.0613 126 GLU A N   
1003  C CA  . GLU A 126 ? 1.1263 1.5373 0.4403 0.0589  0.3809  -0.0722 126 GLU A CA  
1004  C C   . GLU A 126 ? 1.0611 1.4844 0.4358 0.0452  0.3595  -0.0761 126 GLU A C   
1005  O O   . GLU A 126 ? 1.0468 1.4298 0.4171 0.0438  0.3291  -0.0833 126 GLU A O   
1006  C CB  . GLU A 126 ? 1.1699 1.5573 0.4393 0.0953  0.3750  -0.0925 126 GLU A CB  
1007  C CG  . GLU A 126 ? 1.1578 1.5892 0.4614 0.1159  0.3868  -0.1042 126 GLU A CG  
1008  C CD  . GLU A 126 ? 1.1633 1.6588 0.4926 0.1137  0.4273  -0.0918 126 GLU A CD  
1009  O OE1 . GLU A 126 ? 1.2180 1.7138 0.5018 0.1256  0.4527  -0.0872 126 GLU A OE1 
1010  O OE2 . GLU A 126 ? 1.1146 1.6607 0.5099 0.0999  0.4333  -0.0862 126 GLU A OE2 
1011  N N   . ALA A 127 ? 1.0254 1.5048 0.4565 0.0349  0.3753  -0.0706 127 ALA A N   
1012  C CA  . ALA A 127 ? 0.9654 1.4589 0.4530 0.0183  0.3574  -0.0715 127 ALA A CA  
1013  C C   . ALA A 127 ? 0.9419 1.4754 0.4706 0.0344  0.3578  -0.0829 127 ALA A C   
1014  O O   . ALA A 127 ? 0.8996 1.4358 0.4657 0.0262  0.3387  -0.0865 127 ALA A O   
1015  C CB  . ALA A 127 ? 0.9404 1.4580 0.4618 -0.0156 0.3685  -0.0528 127 ALA A CB  
1016  N N   . SER A 128 ? 0.9713 1.5343 0.4916 0.0583  0.3794  -0.0881 128 SER A N   
1017  C CA  . SER A 128 ? 0.9515 1.5607 0.5154 0.0741  0.3838  -0.0964 128 SER A CA  
1018  C C   . SER A 128 ? 0.9718 1.5534 0.5105 0.1090  0.3686  -0.1172 128 SER A C   
1019  O O   . SER A 128 ? 0.9616 1.5760 0.5316 0.1266  0.3708  -0.1251 128 SER A O   
1020  C CB  . SER A 128 ? 0.9672 1.6395 0.5528 0.0766  0.4205  -0.0866 128 SER A CB  
1021  O OG  . SER A 128 ? 0.9343 1.6438 0.5667 0.0425  0.4289  -0.0692 128 SER A OG  
1022  N N   . LEU A 129 ? 1.0027 1.5229 0.4857 0.1190  0.3517  -0.1257 129 LEU A N   
1023  C CA  . LEU A 129 ? 1.0265 1.5104 0.4821 0.1491  0.3326  -0.1458 129 LEU A CA  
1024  C C   . LEU A 129 ? 1.0015 1.4357 0.4570 0.1381  0.2956  -0.1506 129 LEU A C   
1025  O O   . LEU A 129 ? 1.0308 1.4171 0.4503 0.1561  0.2749  -0.1647 129 LEU A O   
1026  C CB  . LEU A 129 ? 1.0956 1.5479 0.4820 0.1744  0.3429  -0.1544 129 LEU A CB  
1027  C CG  . LEU A 129 ? 1.1306 1.6293 0.5114 0.1947  0.3809  -0.1533 129 LEU A CG  
1028  C CD1 . LEU A 129 ? 1.1348 1.6633 0.5163 0.1723  0.4094  -0.1325 129 LEU A CD1 
1029  C CD2 . LEU A 129 ? 1.2009 1.6598 0.5137 0.2313  0.3824  -0.1709 129 LEU A CD2 
1030  N N   . GLY A 130 ? 0.9511 1.3968 0.4473 0.1086  0.2876  -0.1387 130 GLY A N   
1031  C CA  . GLY A 130 ? 0.9233 1.3299 0.4273 0.0966  0.2562  -0.1407 130 GLY A CA  
1032  C C   . GLY A 130 ? 0.8890 1.3111 0.4357 0.1012  0.2429  -0.1469 130 GLY A C   
1033  O O   . GLY A 130 ? 0.8445 1.2808 0.4305 0.0797  0.2362  -0.1386 130 GLY A O   
1034  N N   . VAL A 131 ? 0.9141 1.3299 0.4493 0.1303  0.2388  -0.1616 131 VAL A N   
1035  C CA  . VAL A 131 ? 0.8899 1.3196 0.4616 0.1394  0.2269  -0.1678 131 VAL A CA  
1036  C C   . VAL A 131 ? 0.9142 1.2904 0.4596 0.1585  0.2004  -0.1825 131 VAL A C   
1037  O O   . VAL A 131 ? 0.9553 1.2872 0.4534 0.1678  0.1921  -0.1900 131 VAL A O   
1038  C CB  . VAL A 131 ? 0.8950 1.3804 0.4913 0.1582  0.2496  -0.1703 131 VAL A CB  
1039  C CG1 . VAL A 131 ? 0.8741 1.4141 0.4998 0.1374  0.2754  -0.1548 131 VAL A CG1 
1040  C CG2 . VAL A 131 ? 0.9523 1.4239 0.5052 0.1928  0.2597  -0.1843 131 VAL A CG2 
1041  N N   . SER A 132 ? 0.8926 1.2720 0.4684 0.1634  0.1859  -0.1861 132 SER A N   
1042  C CA  . SER A 132 ? 0.9153 1.2460 0.4723 0.1806  0.1605  -0.1989 132 SER A CA  
1043  C C   . SER A 132 ? 0.9080 1.2602 0.4946 0.1987  0.1578  -0.2043 132 SER A C   
1044  O O   . SER A 132 ? 0.8735 1.2758 0.5026 0.1908  0.1690  -0.1959 132 SER A O   
1045  C CB  . SER A 132 ? 0.8928 1.1840 0.4539 0.1577  0.1353  -0.1929 132 SER A CB  
1046  O OG  . SER A 132 ? 0.9083 1.1597 0.4643 0.1701  0.1107  -0.2021 132 SER A OG  
1047  N N   . SER A 133 ? 0.9434 1.2552 0.5067 0.2227  0.1410  -0.2183 133 SER A N   
1048  C CA  . SER A 133 ? 0.9426 1.2647 0.5293 0.2424  0.1344  -0.2240 133 SER A CA  
1049  C C   . SER A 133 ? 0.8996 1.2172 0.5218 0.2221  0.1152  -0.2141 133 SER A C   
1050  O O   . SER A 133 ? 0.8882 1.2267 0.5391 0.2319  0.1121  -0.2136 133 SER A O   
1051  C CB  . SER A 133 ? 1.0002 1.2713 0.5463 0.2735  0.1203  -0.2421 133 SER A CB  
1052  O OG  . SER A 133 ? 1.0130 1.2221 0.5336 0.2620  0.0938  -0.2445 133 SER A OG  
1053  N N   . ALA A 134 ? 0.8782 1.1689 0.4977 0.1952  0.1029  -0.2058 134 ALA A N   
1054  C CA  . ALA A 134 ? 0.8407 1.1250 0.4898 0.1750  0.0872  -0.1953 134 ALA A CA  
1055  C C   . ALA A 134 ? 0.7954 1.1353 0.4863 0.1593  0.1008  -0.1833 134 ALA A C   
1056  O O   . ALA A 134 ? 0.7743 1.1182 0.4901 0.1538  0.0903  -0.1777 134 ALA A O   
1057  C CB  . ALA A 134 ? 0.8327 1.0784 0.4697 0.1518  0.0736  -0.1892 134 ALA A CB  
1058  N N   . CYS A 135 ? 0.7842 1.1644 0.4809 0.1515  0.1231  -0.1790 135 CYS A N   
1059  C CA  . CYS A 135 ? 0.7485 1.1842 0.4846 0.1377  0.1362  -0.1690 135 CYS A CA  
1060  C C   . CYS A 135 ? 0.7614 1.2459 0.5102 0.1591  0.1554  -0.1739 135 CYS A C   
1061  O O   . CYS A 135 ? 0.7670 1.2780 0.5110 0.1562  0.1766  -0.1718 135 CYS A O   
1062  C CB  . CYS A 135 ? 0.7248 1.1717 0.4643 0.1077  0.1472  -0.1577 135 CYS A CB  
1063  S SG  . CYS A 135 ? 0.7168 1.1089 0.4368 0.0857  0.1305  -0.1521 135 CYS A SG  
1064  N N   . PRO A 136 ? 0.7681 1.2648 0.5336 0.1814  0.1486  -0.1796 136 PRO A N   
1065  C CA  . PRO A 136 ? 0.7806 1.3283 0.5646 0.2039  0.1668  -0.1836 136 PRO A CA  
1066  C C   . PRO A 136 ? 0.7448 1.3562 0.5798 0.1899  0.1745  -0.1728 136 PRO A C   
1067  O O   . PRO A 136 ? 0.7190 1.3292 0.5751 0.1758  0.1582  -0.1666 136 PRO A O   
1068  C CB  . PRO A 136 ? 0.8111 1.3330 0.5858 0.2365  0.1520  -0.1955 136 PRO A CB  
1069  C CG  . PRO A 136 ? 0.7936 1.2768 0.5710 0.2222  0.1260  -0.1910 136 PRO A CG  
1070  C CD  . PRO A 136 ? 0.7748 1.2316 0.5367 0.1912  0.1238  -0.1836 136 PRO A CD  
1071  N N   . TYR A 137 ? 0.7467 1.4126 0.6005 0.1938  0.1989  -0.1704 137 TYR A N   
1072  C CA  . TYR A 137 ? 0.7186 1.4509 0.6249 0.1824  0.2064  -0.1608 137 TYR A CA  
1073  C C   . TYR A 137 ? 0.7388 1.5241 0.6681 0.2122  0.2247  -0.1652 137 TYR A C   
1074  O O   . TYR A 137 ? 0.7635 1.5607 0.6762 0.2233  0.2481  -0.1679 137 TYR A O   
1075  C CB  . TYR A 137 ? 0.6956 1.4495 0.6115 0.1471  0.2201  -0.1485 137 TYR A CB  
1076  C CG  . TYR A 137 ? 0.6731 1.4974 0.6428 0.1328  0.2295  -0.1384 137 TYR A CG  
1077  C CD1 . TYR A 137 ? 0.6483 1.4887 0.6515 0.1220  0.2104  -0.1341 137 TYR A CD1 
1078  C CD2 . TYR A 137 ? 0.6797 1.5535 0.6662 0.1287  0.2570  -0.1324 137 TYR A CD2 
1079  C CE1 . TYR A 137 ? 0.6307 1.5345 0.6836 0.1075  0.2158  -0.1253 137 TYR A CE1 
1080  C CE2 . TYR A 137 ? 0.6605 1.5999 0.7003 0.1130  0.2642  -0.1223 137 TYR A CE2 
1081  C CZ  . TYR A 137 ? 0.6359 1.5899 0.7093 0.1022  0.2422  -0.1193 137 TYR A CZ  
1082  O OH  . TYR A 137 ? 0.6198 1.6381 0.7467 0.0856  0.2463  -0.1097 137 TYR A OH  
1083  N N   . GLN A 138 ? 0.7308 1.5477 0.6976 0.2260  0.2143  -0.1654 138 GLN A N   
1084  C CA  . GLN A 138 ? 0.7494 1.6201 0.7452 0.2574  0.2294  -0.1693 138 GLN A CA  
1085  C C   . GLN A 138 ? 0.7969 1.6376 0.7510 0.2946  0.2406  -0.1838 138 GLN A C   
1086  O O   . GLN A 138 ? 0.8185 1.7014 0.7819 0.3146  0.2665  -0.1858 138 GLN A O   
1087  C CB  . GLN A 138 ? 0.7335 1.6791 0.7722 0.2409  0.2546  -0.1578 138 GLN A CB  
1088  C CG  . GLN A 138 ? 0.6920 1.6640 0.7683 0.2022  0.2431  -0.1445 138 GLN A CG  
1089  C CD  . GLN A 138 ? 0.6794 1.7352 0.8132 0.1915  0.2618  -0.1335 138 GLN A CD  
1090  O OE1 . GLN A 138 ? 0.6968 1.7873 0.8354 0.2010  0.2906  -0.1321 138 GLN A OE1 
1091  N NE2 . GLN A 138 ? 0.6517 1.7402 0.8292 0.1710  0.2452  -0.1254 138 GLN A NE2 
1092  N N   . GLY A 139 ? 0.8159 1.5829 0.7236 0.3034  0.2212  -0.1936 139 GLY A N   
1093  C CA  . GLY A 139 ? 0.8670 1.5933 0.7289 0.3387  0.2256  -0.2095 139 GLY A CA  
1094  C C   . GLY A 139 ? 0.8891 1.5790 0.6998 0.3317  0.2383  -0.2133 139 GLY A C   
1095  O O   . GLY A 139 ? 0.9306 1.5633 0.6917 0.3525  0.2312  -0.2269 139 GLY A O   
1096  N N   . LYS A 140 ? 0.8651 1.5857 0.6861 0.3024  0.2556  -0.2012 140 LYS A N   
1097  C CA  . LYS A 140 ? 0.8871 1.5772 0.6603 0.2944  0.2686  -0.2025 140 LYS A CA  
1098  C C   . LYS A 140 ? 0.8647 1.5023 0.6163 0.2623  0.2475  -0.1976 140 LYS A C   
1099  O O   . LYS A 140 ? 0.8241 1.4657 0.6056 0.2389  0.2312  -0.1890 140 LYS A O   
1100  C CB  . LYS A 140 ? 0.8814 1.6327 0.6747 0.2824  0.3019  -0.1909 140 LYS A CB  
1101  C CG  . LYS A 140 ? 0.9117 1.7152 0.7206 0.3162  0.3289  -0.1954 140 LYS A CG  
1102  C CD  . LYS A 140 ? 0.8773 1.7579 0.7598 0.3121  0.3341  -0.1853 140 LYS A CD  
1103  C CE  . LYS A 140 ? 0.9088 1.8332 0.8104 0.3544  0.3523  -0.1930 140 LYS A CE  
1104  N NZ  . LYS A 140 ? 0.9466 1.8975 0.8285 0.3690  0.3901  -0.1926 140 LYS A NZ  
1105  N N   . SER A 141 ? 0.8948 1.4836 0.5934 0.2627  0.2479  -0.2031 141 SER A N   
1106  C CA  . SER A 141 ? 0.8785 1.4190 0.5556 0.2344  0.2298  -0.1982 141 SER A CA  
1107  C C   . SER A 141 ? 0.8408 1.4158 0.5426 0.1987  0.2427  -0.1812 141 SER A C   
1108  O O   . SER A 141 ? 0.8499 1.4622 0.5536 0.1965  0.2690  -0.1754 141 SER A O   
1109  C CB  . SER A 141 ? 0.9260 1.4089 0.5403 0.2461  0.2265  -0.2087 141 SER A CB  
1110  O OG  . SER A 141 ? 0.9623 1.4016 0.5510 0.2750  0.2087  -0.2249 141 SER A OG  
1111  N N   . SER A 142 ? 0.8024 1.3628 0.5217 0.1714  0.2246  -0.1731 142 SER A N   
1112  C CA  . SER A 142 ? 0.7670 1.3545 0.5109 0.1371  0.2329  -0.1579 142 SER A CA  
1113  C C   . SER A 142 ? 0.7529 1.2898 0.4769 0.1141  0.2151  -0.1536 142 SER A C   
1114  O O   . SER A 142 ? 0.7746 1.2599 0.4636 0.1241  0.2000  -0.1617 142 SER A O   
1115  C CB  . SER A 142 ? 0.7317 1.3678 0.5299 0.1280  0.2307  -0.1513 142 SER A CB  
1116  O OG  . SER A 142 ? 0.7030 1.3640 0.5241 0.0951  0.2380  -0.1377 142 SER A OG  
1117  N N   . PHE A 143 ? 0.7196 1.2708 0.4662 0.0837  0.2164  -0.1411 143 PHE A N   
1118  C CA  . PHE A 143 ? 0.7054 1.2136 0.4378 0.0624  0.2018  -0.1360 143 PHE A CA  
1119  C C   . PHE A 143 ? 0.6675 1.1952 0.4332 0.0340  0.1999  -0.1247 143 PHE A C   
1120  O O   . PHE A 143 ? 0.6541 1.2292 0.4524 0.0279  0.2099  -0.1203 143 PHE A O   
1121  C CB  . PHE A 143 ? 0.7289 1.2136 0.4238 0.0570  0.2113  -0.1333 143 PHE A CB  
1122  C CG  . PHE A 143 ? 0.7273 1.1589 0.3997 0.0465  0.1926  -0.1321 143 PHE A CG  
1123  C CD1 . PHE A 143 ? 0.7423 1.1321 0.3960 0.0619  0.1717  -0.1419 143 PHE A CD1 
1124  C CD2 . PHE A 143 ? 0.7132 1.1364 0.3847 0.0213  0.1953  -0.1207 143 PHE A CD2 
1125  C CE1 . PHE A 143 ? 0.7408 1.0863 0.3797 0.0514  0.1542  -0.1396 143 PHE A CE1 
1126  C CE2 . PHE A 143 ? 0.7122 1.0905 0.3673 0.0132  0.1784  -0.1190 143 PHE A CE2 
1127  C CZ  . PHE A 143 ? 0.7248 1.0666 0.3656 0.0278  0.1580  -0.1280 143 PHE A CZ  
1128  N N   . PHE A 144 ? 0.6531 1.1439 0.4108 0.0175  0.1862  -0.1205 144 PHE A N   
1129  C CA  . PHE A 144 ? 0.6246 1.1238 0.4036 -0.0096 0.1854  -0.1104 144 PHE A CA  
1130  C C   . PHE A 144 ? 0.6245 1.1590 0.4136 -0.0259 0.2060  -0.1022 144 PHE A C   
1131  O O   . PHE A 144 ? 0.6408 1.1626 0.4066 -0.0310 0.2164  -0.0983 144 PHE A O   
1132  C CB  . PHE A 144 ? 0.6190 1.0715 0.3801 -0.0227 0.1740  -0.1064 144 PHE A CB  
1133  C CG  . PHE A 144 ? 0.6199 1.0364 0.3735 -0.0109 0.1540  -0.1119 144 PHE A CG  
1134  C CD1 . PHE A 144 ? 0.6030 1.0223 0.3771 -0.0110 0.1426  -0.1119 144 PHE A CD1 
1135  C CD2 . PHE A 144 ? 0.6409 1.0192 0.3662 -0.0008 0.1457  -0.1163 144 PHE A CD2 
1136  C CE1 . PHE A 144 ? 0.6066 0.9919 0.3744 -0.0018 0.1252  -0.1150 144 PHE A CE1 
1137  C CE2 . PHE A 144 ? 0.6437 0.9888 0.3653 0.0074  0.1264  -0.1203 144 PHE A CE2 
1138  C CZ  . PHE A 144 ? 0.6262 0.9750 0.3697 0.0065  0.1171  -0.1190 144 PHE A CZ  
1139  N N   . ARG A 145 ? 0.6090 1.1866 0.4327 -0.0349 0.2106  -0.0987 145 ARG A N   
1140  C CA  . ARG A 145 ? 0.6116 1.2297 0.4517 -0.0499 0.2302  -0.0905 145 ARG A CA  
1141  C C   . ARG A 145 ? 0.6100 1.2101 0.4404 -0.0779 0.2355  -0.0803 145 ARG A C   
1142  O O   . ARG A 145 ? 0.6212 1.2438 0.4547 -0.0894 0.2533  -0.0726 145 ARG A O   
1143  C CB  . ARG A 145 ? 0.5952 1.2630 0.4791 -0.0554 0.2291  -0.0890 145 ARG A CB  
1144  C CG  . ARG A 145 ? 0.5992 1.2927 0.4984 -0.0272 0.2257  -0.0976 145 ARG A CG  
1145  C CD  . ARG A 145 ? 0.5921 1.3496 0.5369 -0.0321 0.2337  -0.0934 145 ARG A CD  
1146  N NE  . ARG A 145 ? 0.5930 1.3737 0.5573 -0.0058 0.2255  -0.1011 145 ARG A NE  
1147  C CZ  . ARG A 145 ? 0.6118 1.4177 0.5790 0.0215  0.2380  -0.1066 145 ARG A CZ  
1148  N NH1 . ARG A 145 ? 0.6330 1.4453 0.5827 0.0267  0.2606  -0.1052 145 ARG A NH1 
1149  N NH2 . ARG A 145 ? 0.6132 1.4363 0.5989 0.0453  0.2280  -0.1133 145 ARG A NH2 
1150  N N   . ASN A 146 ? 0.5990 1.1589 0.4184 -0.0884 0.2210  -0.0794 146 ASN A N   
1151  C CA  . ASN A 146 ? 0.5988 1.1389 0.4102 -0.1136 0.2244  -0.0703 146 ASN A CA  
1152  C C   . ASN A 146 ? 0.6184 1.1223 0.3941 -0.1119 0.2294  -0.0671 146 ASN A C   
1153  O O   . ASN A 146 ? 0.6246 1.1144 0.3915 -0.1306 0.2355  -0.0583 146 ASN A O   
1154  C CB  . ASN A 146 ? 0.5803 1.0966 0.3978 -0.1253 0.2083  -0.0703 146 ASN A CB  
1155  C CG  . ASN A 146 ? 0.5668 1.1170 0.4162 -0.1345 0.2036  -0.0708 146 ASN A CG  
1156  O OD1 . ASN A 146 ? 0.5702 1.1581 0.4403 -0.1461 0.2137  -0.0666 146 ASN A OD1 
1157  N ND2 . ASN A 146 ? 0.5542 1.0917 0.4081 -0.1298 0.1877  -0.0752 146 ASN A ND2 
1158  N N   . VAL A 147 ? 0.6319 1.1189 0.3858 -0.0892 0.2254  -0.0742 147 VAL A N   
1159  C CA  . VAL A 147 ? 0.6552 1.1066 0.3726 -0.0853 0.2266  -0.0722 147 VAL A CA  
1160  C C   . VAL A 147 ? 0.6850 1.1462 0.3803 -0.0647 0.2377  -0.0770 147 VAL A C   
1161  O O   . VAL A 147 ? 0.6867 1.1698 0.3914 -0.0461 0.2382  -0.0856 147 VAL A O   
1162  C CB  . VAL A 147 ? 0.6492 1.0557 0.3534 -0.0795 0.2061  -0.0760 147 VAL A CB  
1163  C CG1 . VAL A 147 ? 0.6290 1.0197 0.3458 -0.0998 0.1999  -0.0692 147 VAL A CG1 
1164  C CG2 . VAL A 147 ? 0.6422 1.0489 0.3547 -0.0600 0.1927  -0.0869 147 VAL A CG2 
1165  N N   . VAL A 148 ? 0.7127 1.1552 0.3760 -0.0667 0.2465  -0.0714 148 VAL A N   
1166  C CA  . VAL A 148 ? 0.7493 1.1974 0.3833 -0.0480 0.2597  -0.0748 148 VAL A CA  
1167  C C   . VAL A 148 ? 0.7741 1.1744 0.3675 -0.0305 0.2436  -0.0828 148 VAL A C   
1168  O O   . VAL A 148 ? 0.7804 1.1448 0.3540 -0.0396 0.2342  -0.0773 148 VAL A O   
1169  C CB  . VAL A 148 ? 0.7719 1.2320 0.3926 -0.0623 0.2824  -0.0615 148 VAL A CB  
1170  C CG1 . VAL A 148 ? 0.8122 1.2847 0.4037 -0.0418 0.3004  -0.0644 148 VAL A CG1 
1171  C CG2 . VAL A 148 ? 0.7494 1.2514 0.4120 -0.0852 0.2949  -0.0520 148 VAL A CG2 
1172  N N   . TRP A 149 ? 0.7909 1.1902 0.3726 -0.0052 0.2392  -0.0958 149 TRP A N   
1173  C CA  . TRP A 149 ? 0.8235 1.1773 0.3633 0.0121  0.2234  -0.1048 149 TRP A CA  
1174  C C   . TRP A 149 ? 0.8716 1.2198 0.3663 0.0209  0.2401  -0.1028 149 TRP A C   
1175  O O   . TRP A 149 ? 0.8962 1.2670 0.3798 0.0389  0.2568  -0.1085 149 TRP A O   
1176  C CB  . TRP A 149 ? 0.8274 1.1763 0.3700 0.0355  0.2102  -0.1203 149 TRP A CB  
1177  C CG  . TRP A 149 ? 0.8583 1.1555 0.3633 0.0504  0.1875  -0.1306 149 TRP A CG  
1178  C CD1 . TRP A 149 ? 0.8846 1.1436 0.3531 0.0469  0.1782  -0.1278 149 TRP A CD1 
1179  C CD2 . TRP A 149 ? 0.8702 1.1471 0.3703 0.0707  0.1697  -0.1451 149 TRP A CD2 
1180  N NE1 . TRP A 149 ? 0.9107 1.1287 0.3540 0.0624  0.1545  -0.1399 149 TRP A NE1 
1181  C CE2 . TRP A 149 ? 0.9033 1.1298 0.3646 0.0768  0.1492  -0.1508 149 TRP A CE2 
1182  C CE3 . TRP A 149 ? 0.8589 1.1537 0.3834 0.0842  0.1675  -0.1534 149 TRP A CE3 
1183  C CZ2 . TRP A 149 ? 0.9261 1.1184 0.3728 0.0942  0.1268  -0.1647 149 TRP A CZ2 
1184  C CZ3 . TRP A 149 ? 0.8824 1.1417 0.3908 0.1028  0.1464  -0.1669 149 TRP A CZ3 
1185  C CH2 . TRP A 149 ? 0.9157 1.1236 0.3855 0.1069  0.1263  -0.1725 149 TRP A CH2 
1186  N N   . LEU A 150 ? 0.8876 1.2052 0.3554 0.0093  0.2360  -0.0940 150 LEU A N   
1187  C CA  . LEU A 150 ? 0.9356 1.2448 0.3575 0.0142  0.2521  -0.0887 150 LEU A CA  
1188  C C   . LEU A 150 ? 0.9842 1.2522 0.3535 0.0384  0.2377  -0.1016 150 LEU A C   
1189  O O   . LEU A 150 ? 0.9815 1.2124 0.3451 0.0412  0.2095  -0.1084 150 LEU A O   
1190  C CB  . LEU A 150 ? 0.9351 1.2275 0.3497 -0.0090 0.2532  -0.0723 150 LEU A CB  
1191  C CG  . LEU A 150 ? 0.9024 1.2294 0.3576 -0.0347 0.2700  -0.0582 150 LEU A CG  
1192  C CD1 . LEU A 150 ? 0.9090 1.2075 0.3505 -0.0543 0.2668  -0.0437 150 LEU A CD1 
1193  C CD2 . LEU A 150 ? 0.9162 1.2894 0.3776 -0.0340 0.3012  -0.0532 150 LEU A CD2 
1194  N N   . ILE A 151 ? 1.0320 1.3069 0.3629 0.0555  0.2576  -0.1044 151 ILE A N   
1195  C CA  . ILE A 151 ? 1.0906 1.3233 0.3605 0.0794  0.2465  -0.1167 151 ILE A CA  
1196  C C   . ILE A 151 ? 1.1439 1.3683 0.3612 0.0813  0.2667  -0.1073 151 ILE A C   
1197  O O   . ILE A 151 ? 1.1361 1.3929 0.3673 0.0658  0.2929  -0.0914 151 ILE A O   
1198  C CB  . ILE A 151 ? 1.1089 1.3497 0.3731 0.1082  0.2484  -0.1354 151 ILE A CB  
1199  C CG1 . ILE A 151 ? 1.1236 1.4145 0.3918 0.1182  0.2864  -0.1323 151 ILE A CG1 
1200  C CG2 . ILE A 151 ? 1.0594 1.3072 0.3743 0.1058  0.2290  -0.1429 151 ILE A CG2 
1201  C CD1 . ILE A 151 ? 1.1363 1.4430 0.4087 0.1471  0.2912  -0.1494 151 ILE A CD1 
1202  N N   . LYS A 152 ? 1.2017 1.3804 0.3571 0.0998  0.2532  -0.1168 152 LYS A N   
1203  C CA  . LYS A 152 ? 1.2633 1.4245 0.3569 0.1048  0.2688  -0.1089 152 LYS A CA  
1204  C C   . LYS A 152 ? 1.2935 1.4948 0.3739 0.1184  0.3093  -0.1070 152 LYS A C   
1205  O O   . LYS A 152 ? 1.2891 1.5161 0.3863 0.1367  0.3186  -0.1198 152 LYS A O   
1206  C CB  . LYS A 152 ? 1.3222 1.4224 0.3500 0.1239  0.2409  -0.1225 152 LYS A CB  
1207  C CG  . LYS A 152 ? 1.3525 1.4406 0.3583 0.1539  0.2342  -0.1460 152 LYS A CG  
1208  C CD  . LYS A 152 ? 1.4090 1.4318 0.3540 0.1687  0.2000  -0.1601 152 LYS A CD  
1209  C CE  . LYS A 152 ? 1.4545 1.4613 0.3654 0.2011  0.1982  -0.1837 152 LYS A CE  
1210  N NZ  . LYS A 152 ? 1.5157 1.4556 0.3654 0.2162  0.1624  -0.2000 152 LYS A NZ  
1211  N N   . LYS A 153 ? 1.3263 1.5330 0.3776 0.1098  0.3335  -0.0900 153 LYS A N   
1212  C CA  . LYS A 153 ? 1.3651 1.6078 0.3970 0.1225  0.3745  -0.0853 153 LYS A CA  
1213  C C   . LYS A 153 ? 1.4517 1.6500 0.3935 0.1437  0.3781  -0.0888 153 LYS A C   
1214  O O   . LYS A 153 ? 1.4790 1.6406 0.3820 0.1325  0.3684  -0.0774 153 LYS A O   
1215  C CB  . LYS A 153 ? 1.3391 1.6271 0.4098 0.0942  0.4041  -0.0607 153 LYS A CB  
1216  C CG  . LYS A 153 ? 1.3516 1.6995 0.4389 0.1031  0.4470  -0.0558 153 LYS A CG  
1217  C CD  . LYS A 153 ? 1.3618 1.7394 0.4559 0.0792  0.4798  -0.0294 153 LYS A CD  
1218  C CE  . LYS A 153 ? 1.2970 1.7335 0.4754 0.0523  0.4916  -0.0177 153 LYS A CE  
1219  N NZ  . LYS A 153 ? 1.2372 1.6578 0.4581 0.0273  0.4605  -0.0165 153 LYS A NZ  
1220  N N   . ASN A 154 ? 1.4981 1.6986 0.4051 0.1756  0.3916  -0.1048 154 ASN A N   
1221  C CA  . ASN A 154 ? 1.5888 1.7438 0.4033 0.2011  0.3943  -0.1125 154 ASN A CA  
1222  C C   . ASN A 154 ? 1.6160 1.6989 0.3817 0.2006  0.3498  -0.1199 154 ASN A C   
1223  O O   . ASN A 154 ? 1.6699 1.7171 0.3744 0.1991  0.3486  -0.1105 154 ASN A O   
1224  C CB  . ASN A 154 ? 1.6342 1.8096 0.4152 0.1966  0.4356  -0.0913 154 ASN A CB  
1225  C CG  . ASN A 154 ? 1.7305 1.8786 0.4224 0.2309  0.4525  -0.1016 154 ASN A CG  
1226  O OD1 . ASN A 154 ? 1.7548 1.8966 0.4293 0.2612  0.4504  -0.1243 154 ASN A OD1 
1227  N ND2 . ASN A 154 ? 1.7898 1.9191 0.4220 0.2272  0.4699  -0.0850 154 ASN A ND2 
1228  N N   . SER A 155 ? 1.5792 1.6424 0.3747 0.2013  0.3131  -0.1358 155 SER A N   
1229  C CA  . SER A 155 ? 1.6025 1.6010 0.3613 0.2025  0.2674  -0.1456 155 SER A CA  
1230  C C   . SER A 155 ? 1.5884 1.5674 0.3492 0.1752  0.2512  -0.1259 155 SER A C   
1231  O O   . SER A 155 ? 1.6385 1.5646 0.3431 0.1795  0.2250  -0.1280 155 SER A O   
1232  C CB  . SER A 155 ? 1.6980 1.6463 0.3639 0.2346  0.2612  -0.1632 155 SER A CB  
1233  O OG  . SER A 155 ? 1.7082 1.6578 0.3750 0.2605  0.2604  -0.1864 155 SER A OG  
1234  N N   . THR A 156 ? 1.5239 1.5441 0.3486 0.1479  0.2654  -0.1070 156 THR A N   
1235  C CA  . THR A 156 ? 1.5035 1.5066 0.3398 0.1222  0.2493  -0.0889 156 THR A CA  
1236  C C   . THR A 156 ? 1.4161 1.4586 0.3399 0.0968  0.2499  -0.0802 156 THR A C   
1237  O O   . THR A 156 ? 1.3844 1.4775 0.3489 0.0896  0.2806  -0.0738 156 THR A O   
1238  C CB  . THR A 156 ? 1.5468 1.5496 0.3416 0.1139  0.2763  -0.0670 156 THR A CB  
1239  O OG1 . THR A 156 ? 1.5055 1.5651 0.3516 0.0965  0.3130  -0.0515 156 THR A OG1 
1240  C CG2 . THR A 156 ? 1.6377 1.6154 0.3450 0.1408  0.2906  -0.0736 156 THR A CG2 
1241  N N   . TYR A 157 ? 1.3807 1.4007 0.3330 0.0838  0.2161  -0.0800 157 TYR A N   
1242  C CA  . TYR A 157 ? 1.3044 1.3547 0.3320 0.0595  0.2156  -0.0706 157 TYR A CA  
1243  C C   . TYR A 157 ? 1.3026 1.3344 0.3291 0.0386  0.2089  -0.0508 157 TYR A C   
1244  O O   . TYR A 157 ? 1.2962 1.2955 0.3254 0.0348  0.1767  -0.0512 157 TYR A O   
1245  C CB  . TYR A 157 ? 1.2606 1.3049 0.3301 0.0615  0.1857  -0.0854 157 TYR A CB  
1246  C CG  . TYR A 157 ? 1.1850 1.2676 0.3301 0.0414  0.1914  -0.0791 157 TYR A CG  
1247  C CD1 . TYR A 157 ? 1.1548 1.2837 0.3363 0.0428  0.2147  -0.0829 157 TYR A CD1 
1248  C CD2 . TYR A 157 ? 1.1476 1.2195 0.3263 0.0222  0.1733  -0.0695 157 TYR A CD2 
1249  C CE1 . TYR A 157 ? 1.0915 1.2524 0.3371 0.0246  0.2179  -0.0776 157 TYR A CE1 
1250  C CE2 . TYR A 157 ? 1.0852 1.1881 0.3266 0.0050  0.1787  -0.0646 157 TYR A CE2 
1251  C CZ  . TYR A 157 ? 1.0581 1.2041 0.3311 0.0058  0.2001  -0.0689 157 TYR A CZ  
1252  O OH  . TYR A 157 ? 1.0009 1.1752 0.3317 -0.0110 0.2035  -0.0646 157 TYR A OH  
1253  N N   . PRO A 158 ? 1.3113 1.3637 0.3347 0.0253  0.2393  -0.0326 158 PRO A N   
1254  C CA  . PRO A 158 ? 1.3154 1.3475 0.3349 0.0063  0.2346  -0.0130 158 PRO A CA  
1255  C C   . PRO A 158 ? 1.2479 1.2917 0.3347 -0.0142 0.2225  -0.0083 158 PRO A C   
1256  O O   . PRO A 158 ? 1.1964 1.2740 0.3352 -0.0183 0.2274  -0.0161 158 PRO A O   
1257  C CB  . PRO A 158 ? 1.3422 1.3975 0.3446 -0.0026 0.2737  0.0041  158 PRO A CB  
1258  C CG  . PRO A 158 ? 1.3181 1.4238 0.3522 0.0025  0.2993  -0.0045 158 PRO A CG  
1259  C CD  . PRO A 158 ? 1.3213 1.4163 0.3452 0.0273  0.2793  -0.0286 158 PRO A CD  
1260  N N   . THR A 159 ? 1.2530 1.2675 0.3360 -0.0256 0.2068  0.0043  159 THR A N   
1261  C CA  . THR A 159 ? 1.1975 1.2170 0.3379 -0.0428 0.1949  0.0089  159 THR A CA  
1262  C C   . THR A 159 ? 1.1619 1.2208 0.3452 -0.0624 0.2234  0.0178  159 THR A C   
1263  O O   . THR A 159 ? 1.1885 1.2583 0.3527 -0.0704 0.2498  0.0303  159 THR A O   
1264  C CB  . THR A 159 ? 1.2169 1.1969 0.3413 -0.0491 0.1755  0.0226  159 THR A CB  
1265  O OG1 . THR A 159 ? 1.2568 1.2006 0.3398 -0.0315 0.1471  0.0151  159 THR A OG1 
1266  C CG2 . THR A 159 ? 1.1609 1.1448 0.3440 -0.0628 0.1626  0.0253  159 THR A CG2 
1267  N N   . ILE A 160 ? 1.1053 1.1848 0.3456 -0.0705 0.2171  0.0113  160 ILE A N   
1268  C CA  . ILE A 160 ? 1.0687 1.1831 0.3539 -0.0900 0.2377  0.0175  160 ILE A CA  
1269  C C   . ILE A 160 ? 1.0542 1.1488 0.3597 -0.1077 0.2296  0.0296  160 ILE A C   
1270  O O   . ILE A 160 ? 1.0368 1.1101 0.3554 -0.1040 0.2055  0.0258  160 ILE A O   
1271  C CB  . ILE A 160 ? 1.0180 1.1651 0.3501 -0.0866 0.2348  0.0023  160 ILE A CB  
1272  C CG1 . ILE A 160 ? 1.0355 1.2043 0.3502 -0.0679 0.2455  -0.0097 160 ILE A CG1 
1273  C CG2 . ILE A 160 ? 0.9787 1.1568 0.3580 -0.1080 0.2499  0.0084  160 ILE A CG2 
1274  C CD1 . ILE A 160 ? 0.9972 1.1852 0.3465 -0.0578 0.2348  -0.0265 160 ILE A CD1 
1275  N N   . LYS A 161 ? 1.0648 1.1661 0.3734 -0.1267 0.2499  0.0445  161 LYS A N   
1276  C CA  . LYS A 161 ? 1.0535 1.1355 0.3818 -0.1440 0.2449  0.0554  161 LYS A CA  
1277  C C   . LYS A 161 ? 1.0321 1.1446 0.3961 -0.1658 0.2654  0.0601  161 LYS A C   
1278  O O   . LYS A 161 ? 1.0598 1.1752 0.4105 -0.1801 0.2851  0.0739  161 LYS A O   
1279  C CB  . LYS A 161 ? 1.1040 1.1456 0.3886 -0.1461 0.2431  0.0719  161 LYS A CB  
1280  C CG  . LYS A 161 ? 1.1244 1.1303 0.3810 -0.1276 0.2157  0.0688  161 LYS A CG  
1281  C CD  . LYS A 161 ? 1.1822 1.1499 0.3892 -0.1279 0.2150  0.0859  161 LYS A CD  
1282  C CE  . LYS A 161 ? 1.2050 1.1384 0.3856 -0.1097 0.1846  0.0828  161 LYS A CE  
1283  N NZ  . LYS A 161 ? 1.2707 1.1678 0.3925 -0.1061 0.1835  0.0983  161 LYS A NZ  
1284  N N   . ARG A 162 ? 0.9870 1.1210 0.3957 -0.1690 0.2597  0.0491  162 ARG A N   
1285  C CA  . ARG A 162 ? 0.9658 1.1318 0.4107 -0.1883 0.2751  0.0504  162 ARG A CA  
1286  C C   . ARG A 162 ? 0.9433 1.0927 0.4164 -0.2010 0.2645  0.0507  162 ARG A C   
1287  O O   . ARG A 162 ? 0.9208 1.0556 0.4048 -0.1906 0.2460  0.0426  162 ARG A O   
1288  C CB  . ARG A 162 ? 0.9367 1.1474 0.4067 -0.1795 0.2799  0.0364  162 ARG A CB  
1289  C CG  . ARG A 162 ? 0.9645 1.2016 0.4141 -0.1721 0.2996  0.0382  162 ARG A CG  
1290  C CD  . ARG A 162 ? 0.9881 1.2409 0.4376 -0.1938 0.3242  0.0547  162 ARG A CD  
1291  N NE  . ARG A 162 ? 0.9712 1.2784 0.4543 -0.1991 0.3419  0.0518  162 ARG A NE  
1292  C CZ  . ARG A 162 ? 0.9821 1.3197 0.4570 -0.1822 0.3549  0.0464  162 ARG A CZ  
1293  N NH1 . ARG A 162 ? 1.0125 1.3279 0.4424 -0.1595 0.3517  0.0422  162 ARG A NH1 
1294  N NH2 . ARG A 162 ? 0.9654 1.3552 0.4770 -0.1871 0.3704  0.0448  162 ARG A NH2 
1295  N N   . SER A 163 ? 0.9553 1.1055 0.4386 -0.2237 0.2767  0.0605  163 SER A N   
1296  C CA  . SER A 163 ? 0.9432 1.0743 0.4478 -0.2366 0.2690  0.0607  163 SER A CA  
1297  C C   . SER A 163 ? 0.9322 1.0945 0.4686 -0.2571 0.2798  0.0590  163 SER A C   
1298  O O   . SER A 163 ? 0.9487 1.1351 0.4854 -0.2697 0.2967  0.0666  163 SER A O   
1299  C CB  . SER A 163 ? 0.9808 1.0663 0.4589 -0.2450 0.2686  0.0756  163 SER A CB  
1300  O OG  . SER A 163 ? 0.9719 1.0357 0.4672 -0.2563 0.2627  0.0752  163 SER A OG  
1301  N N   . TYR A 164 ? 0.9095 1.0723 0.4729 -0.2604 0.2700  0.0496  164 TYR A N   
1302  C CA  . TYR A 164 ? 0.9048 1.0899 0.4961 -0.2813 0.2757  0.0477  164 TYR A CA  
1303  C C   . TYR A 164 ? 0.9183 1.0673 0.5125 -0.2937 0.2679  0.0480  164 TYR A C   
1304  O O   . TYR A 164 ? 0.9017 1.0307 0.4981 -0.2812 0.2555  0.0405  164 TYR A O   
1305  C CB  . TYR A 164 ? 0.8646 1.0922 0.4860 -0.2736 0.2720  0.0338  164 TYR A CB  
1306  C CG  . TYR A 164 ? 0.8526 1.0959 0.5017 -0.2939 0.2717  0.0306  164 TYR A CG  
1307  C CD1 . TYR A 164 ? 0.8666 1.1364 0.5291 -0.3156 0.2843  0.0383  164 TYR A CD1 
1308  C CD2 . TYR A 164 ? 0.8315 1.0615 0.4924 -0.2923 0.2585  0.0208  164 TYR A CD2 
1309  C CE1 . TYR A 164 ? 0.8600 1.1426 0.5479 -0.3356 0.2808  0.0351  164 TYR A CE1 
1310  C CE2 . TYR A 164 ? 0.8267 1.0668 0.5076 -0.3107 0.2561  0.0171  164 TYR A CE2 
1311  C CZ  . TYR A 164 ? 0.8410 1.1069 0.5357 -0.3327 0.2657  0.0238  164 TYR A CZ  
1312  O OH  . TYR A 164 ? 0.8398 1.1147 0.5545 -0.3520 0.2601  0.0197  164 TYR A OH  
1313  N N   . ASN A 165 ? 0.9552 1.0966 0.5502 -0.3183 0.2759  0.0566  165 ASN A N   
1314  C CA  . ASN A 165 ? 0.9797 1.0841 0.5742 -0.3319 0.2694  0.0562  165 ASN A CA  
1315  C C   . ASN A 165 ? 0.9493 1.0778 0.5724 -0.3443 0.2650  0.0453  165 ASN A C   
1316  O O   . ASN A 165 ? 0.9478 1.1132 0.5901 -0.3604 0.2721  0.0471  165 ASN A O   
1317  C CB  . ASN A 165 ? 1.0459 1.1219 0.6220 -0.3534 0.2784  0.0720  165 ASN A CB  
1318  C CG  . ASN A 165 ? 1.0955 1.1188 0.6602 -0.3618 0.2708  0.0724  165 ASN A CG  
1319  O OD1 . ASN A 165 ? 1.0769 1.0901 0.6506 -0.3557 0.2607  0.0601  165 ASN A OD1 
1320  N ND2 . ASN A 165 ? 1.1743 1.1614 0.7165 -0.3753 0.2763  0.0869  165 ASN A ND2 
1321  N N   . ASN A 166 ? 0.9256 1.0338 0.5515 -0.3368 0.2535  0.0347  166 ASN A N   
1322  C CA  . ASN A 166 ? 0.9027 1.0273 0.5494 -0.3472 0.2471  0.0239  166 ASN A CA  
1323  C C   . ASN A 166 ? 0.9310 1.0301 0.5736 -0.3747 0.2469  0.0274  166 ASN A C   
1324  O O   . ASN A 166 ? 0.9489 1.0024 0.5754 -0.3757 0.2408  0.0241  166 ASN A O   
1325  C CB  . ASN A 166 ? 0.8789 0.9899 0.5262 -0.3285 0.2364  0.0119  166 ASN A CB  
1326  C CG  . ASN A 166 ? 0.8614 0.9953 0.5278 -0.3350 0.2291  0.0004  166 ASN A CG  
1327  O OD1 . ASN A 166 ? 0.8593 1.0279 0.5441 -0.3506 0.2305  0.0004  166 ASN A OD1 
1328  N ND2 . ASN A 166 ? 0.8508 0.9662 0.5133 -0.3228 0.2214  -0.0086 166 ASN A ND2 
1329  N N   . THR A 167 ? 0.9344 1.0629 0.5921 -0.3968 0.2537  0.0341  167 THR A N   
1330  C CA  . THR A 167 ? 0.9655 1.0730 0.6228 -0.4270 0.2525  0.0387  167 THR A CA  
1331  C C   . THR A 167 ? 0.9539 1.0713 0.6286 -0.4392 0.2396  0.0257  167 THR A C   
1332  O O   . THR A 167 ? 0.9878 1.0757 0.6566 -0.4622 0.2339  0.0259  167 THR A O   
1333  C CB  . THR A 167 ? 0.9833 1.1199 0.6528 -0.4486 0.2659  0.0538  167 THR A CB  
1334  O OG1 . THR A 167 ? 0.9497 1.1520 0.6500 -0.4433 0.2708  0.0512  167 THR A OG1 
1335  C CG2 . THR A 167 ? 1.0070 1.1180 0.6489 -0.4417 0.2777  0.0686  167 THR A CG2 
1336  N N   . ASN A 168 ? 0.9090 1.0647 0.6027 -0.4240 0.2339  0.0147  168 ASN A N   
1337  C CA  . ASN A 168 ? 0.8995 1.0618 0.6048 -0.4319 0.2197  0.0019  168 ASN A CA  
1338  C C   . ASN A 168 ? 0.9122 1.0164 0.5877 -0.4236 0.2114  -0.0066 168 ASN A C   
1339  O O   . ASN A 168 ? 0.9073 0.9844 0.5639 -0.4026 0.2158  -0.0054 168 ASN A O   
1340  C CB  . ASN A 168 ? 0.8561 1.0689 0.5854 -0.4147 0.2151  -0.0070 168 ASN A CB  
1341  C CG  . ASN A 168 ? 0.8323 1.0937 0.5802 -0.4040 0.2272  0.0000  168 ASN A CG  
1342  O OD1 . ASN A 168 ? 0.8278 1.1369 0.6046 -0.4162 0.2306  0.0036  168 ASN A OD1 
1343  N ND2 . ASN A 168 ? 0.8193 1.0693 0.5511 -0.3801 0.2333  0.0017  168 ASN A ND2 
1344  N N   . GLN A 169 ? 0.9297 1.0147 0.6005 -0.4391 0.1993  -0.0154 169 GLN A N   
1345  C CA  . GLN A 169 ? 0.9457 0.9766 0.5859 -0.4288 0.1927  -0.0253 169 GLN A CA  
1346  C C   . GLN A 169 ? 0.9109 0.9608 0.5553 -0.4077 0.1859  -0.0373 169 GLN A C   
1347  O O   . GLN A 169 ? 0.9259 0.9584 0.5585 -0.4111 0.1749  -0.0484 169 GLN A O   
1348  C CB  . GLN A 169 ? 0.9964 0.9840 0.6192 -0.4545 0.1833  -0.0292 169 GLN A CB  
1349  C CG  . GLN A 169 ? 1.0024 1.0186 0.6447 -0.4777 0.1691  -0.0359 169 GLN A CG  
1350  C CD  . GLN A 169 ? 1.0513 1.0135 0.6644 -0.4911 0.1547  -0.0475 169 GLN A CD  
1351  O OE1 . GLN A 169 ? 1.0788 1.0437 0.7007 -0.5196 0.1424  -0.0493 169 GLN A OE1 
1352  N NE2 . GLN A 169 ? 1.0652 0.9777 0.6432 -0.4703 0.1560  -0.0556 169 GLN A NE2 
1353  N N   . GLU A 170 ? 0.8671 0.9500 0.5256 -0.3860 0.1923  -0.0346 170 GLU A N   
1354  C CA  . GLU A 170 ? 0.8330 0.9348 0.4970 -0.3648 0.1875  -0.0431 170 GLU A CA  
1355  C C   . GLU A 170 ? 0.8055 0.9067 0.4679 -0.3390 0.1959  -0.0387 170 GLU A C   
1356  O O   . GLU A 170 ? 0.8058 0.9068 0.4685 -0.3377 0.2043  -0.0291 170 GLU A O   
1357  C CB  . GLU A 170 ? 0.8055 0.9662 0.5005 -0.3688 0.1817  -0.0454 170 GLU A CB  
1358  C CG  . GLU A 170 ? 0.8242 0.9923 0.5248 -0.3897 0.1679  -0.0526 170 GLU A CG  
1359  C CD  . GLU A 170 ? 0.8377 1.0324 0.5610 -0.4172 0.1681  -0.0455 170 GLU A CD  
1360  O OE1 . GLU A 170 ? 0.8488 1.0353 0.5708 -0.4249 0.1798  -0.0349 170 GLU A OE1 
1361  O OE2 . GLU A 170 ? 0.8389 1.0636 0.5823 -0.4315 0.1561  -0.0497 170 GLU A OE2 
1362  N N   . ASP A 171 ? 0.7847 0.8843 0.4445 -0.3192 0.1929  -0.0450 171 ASP A N   
1363  C CA  . ASP A 171 ? 0.7534 0.8645 0.4205 -0.2961 0.1973  -0.0415 171 ASP A CA  
1364  C C   . ASP A 171 ? 0.7234 0.8861 0.4151 -0.2945 0.1966  -0.0402 171 ASP A C   
1365  O O   . ASP A 171 ? 0.7198 0.9121 0.4256 -0.3058 0.1912  -0.0440 171 ASP A O   
1366  C CB  . ASP A 171 ? 0.7427 0.8422 0.4042 -0.2779 0.1945  -0.0474 171 ASP A CB  
1367  C CG  . ASP A 171 ? 0.7710 0.8205 0.4085 -0.2738 0.1984  -0.0483 171 ASP A CG  
1368  O OD1 . ASP A 171 ? 0.7889 0.8117 0.4168 -0.2752 0.2041  -0.0421 171 ASP A OD1 
1369  O OD2 . ASP A 171 ? 0.7778 0.8139 0.4045 -0.2676 0.1963  -0.0551 171 ASP A OD2 
1370  N N   . LEU A 172 ? 0.7042 0.8771 0.4006 -0.2797 0.2012  -0.0350 172 LEU A N   
1371  C CA  . LEU A 172 ? 0.6816 0.8986 0.3966 -0.2750 0.2022  -0.0342 172 LEU A CA  
1372  C C   . LEU A 172 ? 0.6557 0.8790 0.3746 -0.2513 0.1995  -0.0359 172 LEU A C   
1373  O O   . LEU A 172 ? 0.6575 0.8575 0.3662 -0.2409 0.2012  -0.0315 172 LEU A O   
1374  C CB  . LEU A 172 ? 0.6962 0.9188 0.4086 -0.2845 0.2117  -0.0250 172 LEU A CB  
1375  C CG  . LEU A 172 ? 0.6827 0.9517 0.4119 -0.2809 0.2163  -0.0237 172 LEU A CG  
1376  C CD1 . LEU A 172 ? 0.6793 0.9860 0.4315 -0.2954 0.2140  -0.0271 172 LEU A CD1 
1377  C CD2 . LEU A 172 ? 0.7019 0.9670 0.4197 -0.2854 0.2277  -0.0132 172 LEU A CD2 
1378  N N   . LEU A 173 ? 0.6336 0.8873 0.3679 -0.2432 0.1937  -0.0418 173 LEU A N   
1379  C CA  . LEU A 173 ? 0.6122 0.8730 0.3515 -0.2223 0.1897  -0.0436 173 LEU A CA  
1380  C C   . LEU A 173 ? 0.6085 0.8915 0.3511 -0.2156 0.1940  -0.0413 173 LEU A C   
1381  O O   . LEU A 173 ? 0.6038 0.9220 0.3596 -0.2176 0.1957  -0.0435 173 LEU A O   
1382  C CB  . LEU A 173 ? 0.5963 0.8764 0.3478 -0.2155 0.1812  -0.0505 173 LEU A CB  
1383  C CG  . LEU A 173 ? 0.5782 0.8665 0.3364 -0.1950 0.1757  -0.0525 173 LEU A CG  
1384  C CD1 . LEU A 173 ? 0.5769 0.8329 0.3270 -0.1853 0.1743  -0.0492 173 LEU A CD1 
1385  C CD2 . LEU A 173 ? 0.5677 0.8769 0.3374 -0.1899 0.1674  -0.0581 173 LEU A CD2 
1386  N N   . VAL A 174 ? 0.6127 0.8754 0.3431 -0.2066 0.1954  -0.0369 174 VAL A N   
1387  C CA  . VAL A 174 ? 0.6155 0.8919 0.3411 -0.1978 0.1987  -0.0352 174 VAL A CA  
1388  C C   . VAL A 174 ? 0.6014 0.8787 0.3298 -0.1774 0.1893  -0.0403 174 VAL A C   
1389  O O   . VAL A 174 ? 0.5942 0.8495 0.3232 -0.1707 0.1817  -0.0403 174 VAL A O   
1390  C CB  . VAL A 174 ? 0.6369 0.8868 0.3422 -0.2011 0.2040  -0.0266 174 VAL A CB  
1391  C CG1 . VAL A 174 ? 0.6477 0.9117 0.3422 -0.1930 0.2089  -0.0249 174 VAL A CG1 
1392  C CG2 . VAL A 174 ? 0.6550 0.8938 0.3555 -0.2221 0.2118  -0.0208 174 VAL A CG2 
1393  N N   . LEU A 175 ? 0.6003 0.9030 0.3311 -0.1675 0.1902  -0.0444 175 LEU A N   
1394  C CA  . LEU A 175 ? 0.5938 0.8949 0.3242 -0.1481 0.1804  -0.0501 175 LEU A CA  
1395  C C   . LEU A 175 ? 0.6126 0.9131 0.3243 -0.1382 0.1834  -0.0500 175 LEU A C   
1396  O O   . LEU A 175 ? 0.6247 0.9454 0.3316 -0.1424 0.1954  -0.0483 175 LEU A O   
1397  C CB  . LEU A 175 ? 0.5800 0.9098 0.3278 -0.1411 0.1769  -0.0576 175 LEU A CB  
1398  C CG  . LEU A 175 ? 0.5659 0.8995 0.3290 -0.1492 0.1727  -0.0586 175 LEU A CG  
1399  C CD1 . LEU A 175 ? 0.5581 0.9266 0.3378 -0.1437 0.1707  -0.0646 175 LEU A CD1 
1400  C CD2 . LEU A 175 ? 0.5579 0.8635 0.3204 -0.1429 0.1629  -0.0580 175 LEU A CD2 
1401  N N   . TRP A 176 ? 0.6179 0.8952 0.3188 -0.1253 0.1723  -0.0516 176 TRP A N   
1402  C CA  . TRP A 176 ? 0.6404 0.9130 0.3186 -0.1126 0.1715  -0.0540 176 TRP A CA  
1403  C C   . TRP A 176 ? 0.6406 0.8967 0.3174 -0.0964 0.1541  -0.0608 176 TRP A C   
1404  O O   . TRP A 176 ? 0.6217 0.8725 0.3173 -0.0963 0.1448  -0.0619 176 TRP A O   
1405  C CB  . TRP A 176 ? 0.6624 0.9129 0.3178 -0.1189 0.1755  -0.0452 176 TRP A CB  
1406  C CG  . TRP A 176 ? 0.6595 0.8780 0.3156 -0.1200 0.1632  -0.0403 176 TRP A CG  
1407  C CD1 . TRP A 176 ? 0.6718 0.8666 0.3157 -0.1091 0.1485  -0.0407 176 TRP A CD1 
1408  C CD2 . TRP A 176 ? 0.6462 0.8539 0.3170 -0.1320 0.1644  -0.0341 176 TRP A CD2 
1409  N NE1 . TRP A 176 ? 0.6644 0.8385 0.3194 -0.1137 0.1410  -0.0341 176 TRP A NE1 
1410  C CE2 . TRP A 176 ? 0.6494 0.8303 0.3195 -0.1266 0.1518  -0.0302 176 TRP A CE2 
1411  C CE3 . TRP A 176 ? 0.6352 0.8525 0.3189 -0.1464 0.1742  -0.0320 176 TRP A CE3 
1412  C CZ2 . TRP A 176 ? 0.6413 0.8066 0.3243 -0.1332 0.1514  -0.0239 176 TRP A CZ2 
1413  C CZ3 . TRP A 176 ? 0.6303 0.8272 0.3213 -0.1531 0.1728  -0.0270 176 TRP A CZ3 
1414  C CH2 . TRP A 176 ? 0.6329 0.8050 0.3240 -0.1455 0.1628  -0.0229 176 TRP A CH2 
1415  N N   . GLY A 177 ? 0.6661 0.9123 0.3188 -0.0832 0.1497  -0.0651 177 GLY A N   
1416  C CA  . GLY A 177 ? 0.6731 0.9004 0.3219 -0.0685 0.1313  -0.0725 177 GLY A CA  
1417  C C   . GLY A 177 ? 0.7079 0.9104 0.3238 -0.0582 0.1223  -0.0747 177 GLY A C   
1418  O O   . GLY A 177 ? 0.7304 0.9329 0.3215 -0.0592 0.1328  -0.0713 177 GLY A O   
1419  N N   . ILE A 178 ? 0.7158 0.8955 0.3307 -0.0488 0.1018  -0.0801 178 ILE A N   
1420  C CA  . ILE A 178 ? 0.7535 0.9057 0.3357 -0.0374 0.0876  -0.0848 178 ILE A CA  
1421  C C   . ILE A 178 ? 0.7687 0.9148 0.3439 -0.0207 0.0764  -0.0984 178 ILE A C   
1422  O O   . ILE A 178 ? 0.7469 0.8984 0.3489 -0.0205 0.0705  -0.1008 178 ILE A O   
1423  C CB  . ILE A 178 ? 0.7546 0.8791 0.3431 -0.0435 0.0684  -0.0776 178 ILE A CB  
1424  C CG1 . ILE A 178 ? 0.7985 0.8937 0.3485 -0.0331 0.0524  -0.0818 178 ILE A CG1 
1425  C CG2 . ILE A 178 ? 0.7302 0.8503 0.3535 -0.0458 0.0539  -0.0777 178 ILE A CG2 
1426  C CD1 . ILE A 178 ? 0.8038 0.8722 0.3642 -0.0352 0.0258  -0.0783 178 ILE A CD1 
1427  N N   . HIS A 179 ? 0.8107 0.9431 0.3470 -0.0060 0.0737  -0.1071 179 HIS A N   
1428  C CA  . HIS A 179 ? 0.8352 0.9534 0.3580 0.0119  0.0608  -0.1214 179 HIS A CA  
1429  C C   . HIS A 179 ? 0.8637 0.9396 0.3694 0.0159  0.0316  -0.1255 179 HIS A C   
1430  O O   . HIS A 179 ? 0.8897 0.9463 0.3685 0.0147  0.0249  -0.1225 179 HIS A O   
1431  C CB  . HIS A 179 ? 0.8692 0.9985 0.3579 0.0290  0.0771  -0.1307 179 HIS A CB  
1432  C CG  . HIS A 179 ? 0.9031 1.0121 0.3715 0.0504  0.0639  -0.1469 179 HIS A CG  
1433  N ND1 . HIS A 179 ? 0.9583 1.0422 0.3762 0.0679  0.0597  -0.1575 179 HIS A ND1 
1434  C CD2 . HIS A 179 ? 0.8948 1.0004 0.3833 0.0575  0.0529  -0.1542 179 HIS A CD2 
1435  C CE1 . HIS A 179 ? 0.9822 1.0477 0.3904 0.0854  0.0468  -0.1718 179 HIS A CE1 
1436  N NE2 . HIS A 179 ? 0.9442 1.0224 0.3957 0.0792  0.0422  -0.1696 179 HIS A NE2 
1437  N N   . HIS A 180 ? 0.8611 0.9222 0.3827 0.0201  0.0132  -0.1318 180 HIS A N   
1438  C CA  . HIS A 180 ? 0.8900 0.9111 0.4002 0.0229  -0.0172 -0.1367 180 HIS A CA  
1439  C C   . HIS A 180 ? 0.9349 0.9336 0.4091 0.0443  -0.0262 -0.1546 180 HIS A C   
1440  O O   . HIS A 180 ? 0.9280 0.9307 0.4164 0.0517  -0.0262 -0.1610 180 HIS A O   
1441  C CB  . HIS A 180 ? 0.8587 0.8767 0.4151 0.0103  -0.0320 -0.1294 180 HIS A CB  
1442  C CG  . HIS A 180 ? 0.8177 0.8557 0.4094 -0.0081 -0.0226 -0.1128 180 HIS A CG  
1443  N ND1 . HIS A 180 ? 0.8148 0.8384 0.4243 -0.0190 -0.0397 -0.1035 180 HIS A ND1 
1444  C CD2 . HIS A 180 ? 0.7811 0.8513 0.3937 -0.0169 0.0013  -0.1045 180 HIS A CD2 
1445  C CE1 . HIS A 180 ? 0.7788 0.8240 0.4169 -0.0318 -0.0250 -0.0903 180 HIS A CE1 
1446  N NE2 . HIS A 180 ? 0.7591 0.8305 0.3976 -0.0313 -0.0006 -0.0912 180 HIS A NE2 
1447  N N   . PRO A 181 ? 0.9851 0.9577 0.4093 0.0557  -0.0338 -0.1628 181 PRO A N   
1448  C CA  . PRO A 181 ? 1.0358 0.9834 0.4180 0.0786  -0.0407 -0.1813 181 PRO A CA  
1449  C C   . PRO A 181 ? 1.0621 0.9659 0.4429 0.0807  -0.0763 -0.1902 181 PRO A C   
1450  O O   . PRO A 181 ? 1.0452 0.9382 0.4549 0.0637  -0.0966 -0.1808 181 PRO A O   
1451  C CB  . PRO A 181 ? 1.0826 1.0172 0.4094 0.0877  -0.0351 -0.1847 181 PRO A CB  
1452  C CG  . PRO A 181 ? 1.0689 0.9982 0.4071 0.0686  -0.0460 -0.1702 181 PRO A CG  
1453  C CD  . PRO A 181 ? 1.0023 0.9643 0.4033 0.0489  -0.0372 -0.1553 181 PRO A CD  
1454  N N   . ASN A 182 ? 1.1058 0.9844 0.4540 0.1017  -0.0835 -0.2078 182 ASN A N   
1455  C CA  . ASN A 182 ? 1.1356 0.9696 0.4818 0.1042  -0.1173 -0.2174 182 ASN A CA  
1456  C C   . ASN A 182 ? 1.1846 0.9731 0.4970 0.1015  -0.1492 -0.2222 182 ASN A C   
1457  O O   . ASN A 182 ? 1.1827 0.9488 0.5207 0.0872  -0.1783 -0.2180 182 ASN A O   
1458  C CB  . ASN A 182 ? 1.1724 0.9905 0.4916 0.1295  -0.1147 -0.2357 182 ASN A CB  
1459  C CG  . ASN A 182 ? 1.1255 0.9826 0.4861 0.1310  -0.0929 -0.2308 182 ASN A CG  
1460  O OD1 . ASN A 182 ? 1.1133 0.9595 0.5033 0.1268  -0.1068 -0.2298 182 ASN A OD1 
1461  N ND2 . ASN A 182 ? 1.1006 1.0034 0.4645 0.1359  -0.0595 -0.2266 182 ASN A ND2 
1462  N N   . ASP A 183 ? 1.2307 1.0062 0.4859 0.1152  -0.1438 -0.2303 183 ASP A N   
1463  C CA  . ASP A 183 ? 1.2858 1.0164 0.4993 0.1150  -0.1746 -0.2359 183 ASP A CA  
1464  C C   . ASP A 183 ? 1.3038 1.0439 0.4767 0.1184  -0.1579 -0.2310 183 ASP A C   
1465  O O   . ASP A 183 ? 1.2786 1.0580 0.4527 0.1222  -0.1216 -0.2250 183 ASP A O   
1466  C CB  . ASP A 183 ? 1.3595 1.0356 0.5217 0.1355  -0.1986 -0.2592 183 ASP A CB  
1467  C CG  . ASP A 183 ? 1.3883 1.0701 0.5094 0.1639  -0.1705 -0.2741 183 ASP A CG  
1468  O OD1 . ASP A 183 ? 1.3810 1.0952 0.4845 0.1708  -0.1380 -0.2695 183 ASP A OD1 
1469  O OD2 . ASP A 183 ? 1.4207 1.0741 0.5282 0.1796  -0.1810 -0.2899 183 ASP A OD2 
1470  N N   . ALA A 184 ? 1.3501 1.0534 0.4876 0.1163  -0.1857 -0.2329 184 ALA A N   
1471  C CA  . ALA A 184 ? 1.3770 1.0810 0.4696 0.1196  -0.1746 -0.2275 184 ALA A CA  
1472  C C   . ALA A 184 ? 1.4243 1.1264 0.4533 0.1451  -0.1469 -0.2402 184 ALA A C   
1473  O O   . ALA A 184 ? 1.4272 1.1492 0.4327 0.1467  -0.1212 -0.2313 184 ALA A O   
1474  C CB  . ALA A 184 ? 1.4266 1.0855 0.4893 0.1148  -0.2154 -0.2292 184 ALA A CB  
1475  N N   . ALA A 185 ? 1.4636 1.1413 0.4657 0.1653  -0.1514 -0.2601 185 ALA A N   
1476  C CA  . ALA A 185 ? 1.5102 1.1882 0.4560 0.1929  -0.1232 -0.2734 185 ALA A CA  
1477  C C   . ALA A 185 ? 1.4536 1.1948 0.4372 0.1932  -0.0771 -0.2630 185 ALA A C   
1478  O O   . ALA A 185 ? 1.4746 1.2348 0.4233 0.2057  -0.0457 -0.2620 185 ALA A O   
1479  C CB  . ALA A 185 ? 1.5658 1.1998 0.4781 0.2152  -0.1415 -0.2977 185 ALA A CB  
1480  N N   . GLU A 186 ? 1.3853 1.1588 0.4396 0.1789  -0.0737 -0.2548 186 GLU A N   
1481  C CA  . GLU A 186 ? 1.3293 1.1631 0.4252 0.1759  -0.0347 -0.2442 186 GLU A CA  
1482  C C   . GLU A 186 ? 1.2895 1.1577 0.4059 0.1549  -0.0163 -0.2228 186 GLU A C   
1483  O O   . GLU A 186 ? 1.2728 1.1819 0.3931 0.1566  0.0188  -0.2155 186 GLU A O   
1484  C CB  . GLU A 186 ? 1.2745 1.1275 0.4343 0.1678  -0.0391 -0.2423 186 GLU A CB  
1485  C CG  . GLU A 186 ? 1.2290 1.1394 0.4248 0.1702  -0.0024 -0.2361 186 GLU A CG  
1486  C CD  . GLU A 186 ? 1.1886 1.1113 0.4362 0.1673  -0.0086 -0.2367 186 GLU A CD  
1487  O OE1 . GLU A 186 ? 1.1462 1.0687 0.4370 0.1454  -0.0249 -0.2260 186 GLU A OE1 
1488  O OE2 . GLU A 186 ? 1.2001 1.1334 0.4450 0.1878  0.0036  -0.2474 186 GLU A OE2 
1489  N N   . GLN A 187 ? 1.2764 1.1279 0.4078 0.1351  -0.0405 -0.2124 187 GLN A N   
1490  C CA  . GLN A 187 ? 1.2491 1.1231 0.3935 0.1166  -0.0278 -0.1928 187 GLN A CA  
1491  C C   . GLN A 187 ? 1.2997 1.1713 0.3830 0.1286  -0.0064 -0.1923 187 GLN A C   
1492  O O   . GLN A 187 ? 1.2758 1.1854 0.3696 0.1223  0.0259  -0.1798 187 GLN A O   
1493  C CB  . GLN A 187 ? 1.2444 1.0916 0.4035 0.0997  -0.0621 -0.1848 187 GLN A CB  
1494  C CG  . GLN A 187 ? 1.2337 1.0909 0.3923 0.0851  -0.0548 -0.1663 187 GLN A CG  
1495  C CD  . GLN A 187 ? 1.1672 1.0737 0.3780 0.0689  -0.0247 -0.1502 187 GLN A CD  
1496  O OE1 . GLN A 187 ? 1.1147 1.0421 0.3808 0.0590  -0.0246 -0.1474 187 GLN A OE1 
1497  N NE2 . GLN A 187 ? 1.1733 1.0956 0.3641 0.0657  0.0000  -0.1391 187 GLN A NE2 
1498  N N   . THR A 188 ? 1.3737 1.1988 0.3916 0.1455  -0.0251 -0.2057 188 THR A N   
1499  C CA  . THR A 188 ? 1.4334 1.2495 0.3836 0.1596  -0.0061 -0.2061 188 THR A CA  
1500  C C   . THR A 188 ? 1.4405 1.2900 0.3801 0.1777  0.0337  -0.2121 188 THR A C   
1501  O O   . THR A 188 ? 1.4499 1.3241 0.3703 0.1784  0.0658  -0.2018 188 THR A O   
1502  C CB  . THR A 188 ? 1.5182 1.2719 0.3950 0.1758  -0.0377 -0.2216 188 THR A CB  
1503  O OG1 . THR A 188 ? 1.5436 1.2720 0.4116 0.1927  -0.0543 -0.2433 188 THR A OG1 
1504  C CG2 . THR A 188 ? 1.5171 1.2419 0.4025 0.1576  -0.0762 -0.2130 188 THR A CG2 
1505  N N   . LYS A 189 ? 1.4372 1.2884 0.3918 0.1920  0.0318  -0.2276 189 LYS A N   
1506  C CA  . LYS A 189 ? 1.4420 1.3286 0.3946 0.2110  0.0681  -0.2335 189 LYS A CA  
1507  C C   . LYS A 189 ? 1.3757 1.3275 0.3852 0.1936  0.1028  -0.2144 189 LYS A C   
1508  O O   . LYS A 189 ? 1.3883 1.3733 0.3853 0.2033  0.1385  -0.2110 189 LYS A O   
1509  C CB  . LYS A 189 ? 1.4426 1.3199 0.4116 0.2274  0.0562  -0.2517 189 LYS A CB  
1510  C CG  . LYS A 189 ? 1.4381 1.3596 0.4188 0.2466  0.0930  -0.2562 189 LYS A CG  
1511  C CD  . LYS A 189 ? 1.4474 1.3543 0.4385 0.2662  0.0801  -0.2746 189 LYS A CD  
1512  C CE  . LYS A 189 ? 1.4494 1.4017 0.4496 0.2886  0.1173  -0.2789 189 LYS A CE  
1513  N NZ  . LYS A 189 ? 1.4146 1.3809 0.4652 0.2940  0.1102  -0.2852 189 LYS A NZ  
1514  N N   . LEU A 190 ? 1.3084 1.2779 0.3804 0.1682  0.0921  -0.2021 190 LEU A N   
1515  C CA  . LEU A 190 ? 1.2459 1.2724 0.3739 0.1500  0.1199  -0.1855 190 LEU A CA  
1516  C C   . LEU A 190 ? 1.2408 1.2766 0.3612 0.1312  0.1334  -0.1662 190 LEU A C   
1517  O O   . LEU A 190 ? 1.2306 1.3063 0.3597 0.1266  0.1665  -0.1556 190 LEU A O   
1518  C CB  . LEU A 190 ? 1.1809 1.2197 0.3757 0.1327  0.1036  -0.1818 190 LEU A CB  
1519  C CG  . LEU A 190 ? 1.1675 1.2198 0.3892 0.1470  0.1034  -0.1944 190 LEU A CG  
1520  C CD1 . LEU A 190 ? 1.1184 1.1657 0.3916 0.1313  0.0794  -0.1917 190 LEU A CD1 
1521  C CD2 . LEU A 190 ? 1.1447 1.2544 0.3927 0.1503  0.1398  -0.1895 190 LEU A CD2 
1522  N N   . TYR A 191 ? 1.2483 1.2477 0.3553 0.1197  0.1067  -0.1610 191 TYR A N   
1523  C CA  . TYR A 191 ? 1.2387 1.2424 0.3453 0.1000  0.1141  -0.1414 191 TYR A CA  
1524  C C   . TYR A 191 ? 1.3043 1.2630 0.3428 0.1070  0.1005  -0.1406 191 TYR A C   
1525  O O   . TYR A 191 ? 1.3074 1.2650 0.3368 0.0935  0.1069  -0.1241 191 TYR A O   
1526  C CB  . TYR A 191 ? 1.1780 1.1863 0.3433 0.0766  0.0962  -0.1312 191 TYR A CB  
1527  C CG  . TYR A 191 ? 1.1203 1.1607 0.3462 0.0719  0.1000  -0.1348 191 TYR A CG  
1528  C CD1 . TYR A 191 ? 1.0804 1.1690 0.3434 0.0623  0.1296  -0.1263 191 TYR A CD1 
1529  C CD2 . TYR A 191 ? 1.1096 1.1309 0.3544 0.0767  0.0729  -0.1463 191 TYR A CD2 
1530  C CE1 . TYR A 191 ? 1.0317 1.1480 0.3465 0.0587  0.1312  -0.1295 191 TYR A CE1 
1531  C CE2 . TYR A 191 ? 1.0615 1.1096 0.3576 0.0730  0.0762  -0.1485 191 TYR A CE2 
1532  C CZ  . TYR A 191 ? 1.0230 1.1183 0.3525 0.0647  0.1051  -0.1404 191 TYR A CZ  
1533  O OH  . TYR A 191 ? 0.9792 1.0998 0.3562 0.0617  0.1068  -0.1424 191 TYR A OH  
1534  N N   . GLN A 192 ? 1.3597 1.2788 0.3485 0.1282  0.0807  -0.1585 192 GLN A N   
1535  C CA  . GLN A 192 ? 1.4300 1.2998 0.3484 0.1371  0.0615  -0.1608 192 GLN A CA  
1536  C C   . GLN A 192 ? 1.4200 1.2620 0.3502 0.1201  0.0267  -0.1513 192 GLN A C   
1537  O O   . GLN A 192 ? 1.4546 1.2539 0.3610 0.1266  -0.0098 -0.1625 192 GLN A O   
1538  C CB  . GLN A 192 ? 1.4771 1.3539 0.3416 0.1442  0.0943  -0.1518 192 GLN A CB  
1539  C CG  . GLN A 192 ? 1.5475 1.4069 0.3468 0.1744  0.1053  -0.1699 192 GLN A CG  
1540  C CD  . GLN A 192 ? 1.6120 1.4650 0.3427 0.1839  0.1318  -0.1617 192 GLN A CD  
1541  O OE1 . GLN A 192 ? 1.6656 1.5157 0.3479 0.2084  0.1516  -0.1734 192 GLN A OE1 
1542  N NE2 . GLN A 192 ? 1.6118 1.4607 0.3358 0.1659  0.1328  -0.1412 192 GLN A NE2 
1543  N N   . ASN A 193 ? 1.3764 1.2416 0.3432 0.0988  0.0374  -0.1309 193 ASN A N   
1544  C CA  . ASN A 193 ? 1.3645 1.2084 0.3480 0.0838  0.0076  -0.1200 193 ASN A CA  
1545  C C   . ASN A 193 ? 1.3352 1.1672 0.3613 0.0805  -0.0269 -0.1300 193 ASN A C   
1546  O O   . ASN A 193 ? 1.2794 1.1404 0.3609 0.0744  -0.0190 -0.1323 193 ASN A O   
1547  C CB  . ASN A 193 ? 1.3123 1.1879 0.3413 0.0620  0.0274  -0.0983 193 ASN A CB  
1548  C CG  . ASN A 193 ? 1.3346 1.2278 0.3315 0.0617  0.0651  -0.0868 193 ASN A CG  
1549  O OD1 . ASN A 193 ? 1.3652 1.2676 0.3291 0.0762  0.0874  -0.0952 193 ASN A OD1 
1550  N ND2 . ASN A 193 ? 1.3216 1.2194 0.3295 0.0452  0.0733  -0.0671 193 ASN A ND2 
1551  N N   . PRO A 194 ? 1.3758 1.1647 0.3754 0.0843  -0.0660 -0.1356 194 PRO A N   
1552  C CA  . PRO A 194 ? 1.3571 1.1321 0.3941 0.0812  -0.0999 -0.1454 194 PRO A CA  
1553  C C   . PRO A 194 ? 1.2839 1.0857 0.4000 0.0595  -0.1047 -0.1306 194 PRO A C   
1554  O O   . PRO A 194 ? 1.2413 1.0578 0.4070 0.0546  -0.1085 -0.1352 194 PRO A O   
1555  C CB  . PRO A 194 ? 1.4258 1.1491 0.4114 0.0886  -0.1400 -0.1522 194 PRO A CB  
1556  C CG  . PRO A 194 ? 1.4579 1.1741 0.4015 0.0879  -0.1308 -0.1380 194 PRO A CG  
1557  C CD  . PRO A 194 ? 1.4409 1.1926 0.3780 0.0897  -0.0820 -0.1311 194 PRO A CD  
1558  N N   . THR A 195 ? 1.2735 1.0797 0.3981 0.0482  -0.1037 -0.1129 195 THR A N   
1559  C CA  . THR A 195 ? 1.2100 1.0407 0.4042 0.0297  -0.1045 -0.0979 195 THR A CA  
1560  C C   . THR A 195 ? 1.1727 1.0390 0.3829 0.0215  -0.0642 -0.0855 195 THR A C   
1561  O O   . THR A 195 ? 1.2027 1.0647 0.3719 0.0236  -0.0479 -0.0779 195 THR A O   
1562  C CB  . THR A 195 ? 1.2278 1.0366 0.4232 0.0238  -0.1342 -0.0863 195 THR A CB  
1563  O OG1 . THR A 195 ? 1.2802 1.0507 0.4433 0.0328  -0.1725 -0.0986 195 THR A OG1 
1564  C CG2 . THR A 195 ? 1.1663 0.9981 0.4381 0.0079  -0.1398 -0.0739 195 THR A CG2 
1565  N N   . THR A 196 ? 1.1116 1.0108 0.3790 0.0118  -0.0488 -0.0835 196 THR A N   
1566  C CA  . THR A 196 ? 1.0768 1.0099 0.3622 0.0028  -0.0124 -0.0737 196 THR A CA  
1567  C C   . THR A 196 ? 1.0172 0.9719 0.3667 -0.0134 -0.0095 -0.0626 196 THR A C   
1568  O O   . THR A 196 ? 0.9971 0.9469 0.3828 -0.0168 -0.0317 -0.0634 196 THR A O   
1569  C CB  . THR A 196 ? 1.0697 1.0265 0.3500 0.0106  0.0121  -0.0850 196 THR A CB  
1570  O OG1 . THR A 196 ? 1.0422 1.0042 0.3574 0.0128  -0.0003 -0.0959 196 THR A OG1 
1571  C CG2 . THR A 196 ? 1.1328 1.0707 0.3459 0.0285  0.0161  -0.0949 196 THR A CG2 
1572  N N   . TYR A 197 ? 0.9930 0.9706 0.3553 -0.0236 0.0183  -0.0521 197 TYR A N   
1573  C CA  . TYR A 197 ? 0.9430 0.9381 0.3583 -0.0380 0.0242  -0.0419 197 TYR A CA  
1574  C C   . TYR A 197 ? 0.9176 0.9419 0.3448 -0.0476 0.0570  -0.0373 197 TYR A C   
1575  O O   . TYR A 197 ? 0.9398 0.9716 0.3351 -0.0448 0.0761  -0.0384 197 TYR A O   
1576  C CB  . TYR A 197 ? 0.9539 0.9296 0.3703 -0.0431 0.0114  -0.0278 197 TYR A CB  
1577  C CG  . TYR A 197 ? 0.9833 0.9517 0.3622 -0.0460 0.0287  -0.0170 197 TYR A CG  
1578  C CD1 . TYR A 197 ? 1.0399 0.9832 0.3616 -0.0361 0.0210  -0.0173 197 TYR A CD1 
1579  C CD2 . TYR A 197 ? 0.9592 0.9428 0.3569 -0.0589 0.0523  -0.0063 197 TYR A CD2 
1580  C CE1 . TYR A 197 ? 1.0708 1.0059 0.3563 -0.0394 0.0379  -0.0055 197 TYR A CE1 
1581  C CE2 . TYR A 197 ? 0.9896 0.9641 0.3536 -0.0632 0.0679  0.0048  197 TYR A CE2 
1582  C CZ  . TYR A 197 ? 1.0450 0.9958 0.3533 -0.0536 0.0613  0.0060  197 TYR A CZ  
1583  O OH  . TYR A 197 ? 1.0786 1.0190 0.3515 -0.0584 0.0778  0.0189  197 TYR A OH  
1584  N N   . ILE A 198 ? 0.8736 0.9141 0.3471 -0.0590 0.0632  -0.0321 198 ILE A N   
1585  C CA  . ILE A 198 ? 0.8505 0.9145 0.3385 -0.0712 0.0900  -0.0263 198 ILE A CA  
1586  C C   . ILE A 198 ? 0.8292 0.8878 0.3463 -0.0824 0.0895  -0.0147 198 ILE A C   
1587  O O   . ILE A 198 ? 0.8005 0.8621 0.3538 -0.0836 0.0797  -0.0157 198 ILE A O   
1588  C CB  . ILE A 198 ? 0.8168 0.9105 0.3323 -0.0721 0.1008  -0.0357 198 ILE A CB  
1589  C CG1 . ILE A 198 ? 0.8351 0.9303 0.3304 -0.0568 0.0947  -0.0496 198 ILE A CG1 
1590  C CG2 . ILE A 198 ? 0.8051 0.9232 0.3262 -0.0841 0.1275  -0.0308 198 ILE A CG2 
1591  C CD1 . ILE A 198 ? 0.8047 0.9263 0.3278 -0.0552 0.1016  -0.0586 198 ILE A CD1 
1592  N N   . SER A 199 ? 0.8467 0.8962 0.3470 -0.0900 0.1010  -0.0034 199 SER A N   
1593  C CA  . SER A 199 ? 0.8323 0.8735 0.3559 -0.0992 0.1026  0.0071  199 SER A CA  
1594  C C   . SER A 199 ? 0.8140 0.8725 0.3499 -0.1134 0.1266  0.0096  199 SER A C   
1595  O O   . SER A 199 ? 0.8321 0.8967 0.3451 -0.1195 0.1429  0.0123  199 SER A O   
1596  C CB  . SER A 199 ? 0.8695 0.8813 0.3661 -0.0973 0.0946  0.0191  199 SER A CB  
1597  O OG  . SER A 199 ? 0.9053 0.9120 0.3593 -0.0989 0.1075  0.0230  199 SER A OG  
1598  N N   . VAL A 200 ? 0.7810 0.8472 0.3529 -0.1188 0.1282  0.0087  200 VAL A N   
1599  C CA  . VAL A 200 ? 0.7650 0.8443 0.3499 -0.1327 0.1470  0.0097  200 VAL A CA  
1600  C C   . VAL A 200 ? 0.7642 0.8234 0.3616 -0.1382 0.1476  0.0183  200 VAL A C   
1601  O O   . VAL A 200 ? 0.7510 0.8031 0.3701 -0.1313 0.1364  0.0188  200 VAL A O   
1602  C CB  . VAL A 200 ? 0.7302 0.8362 0.3425 -0.1333 0.1496  -0.0008 200 VAL A CB  
1603  C CG1 . VAL A 200 ? 0.7216 0.8436 0.3405 -0.1481 0.1675  -0.0009 200 VAL A CG1 
1604  C CG2 . VAL A 200 ? 0.7311 0.8522 0.3351 -0.1224 0.1438  -0.0105 200 VAL A CG2 
1605  N N   . GLY A 201 ? 0.7812 0.8309 0.3654 -0.1504 0.1614  0.0253  201 GLY A N   
1606  C CA  . GLY A 201 ? 0.7884 0.8137 0.3786 -0.1547 0.1632  0.0330  201 GLY A CA  
1607  C C   . GLY A 201 ? 0.7851 0.8133 0.3799 -0.1709 0.1790  0.0322  201 GLY A C   
1608  O O   . GLY A 201 ? 0.7904 0.8343 0.3757 -0.1821 0.1899  0.0310  201 GLY A O   
1609  N N   . THR A 202 ? 0.7786 0.7924 0.3887 -0.1717 0.1799  0.0325  202 THR A N   
1610  C CA  . THR A 202 ? 0.7861 0.7905 0.3947 -0.1868 0.1920  0.0322  202 THR A CA  
1611  C C   . THR A 202 ? 0.8061 0.7742 0.4124 -0.1821 0.1905  0.0391  202 THR A C   
1612  O O   . THR A 202 ? 0.8187 0.7718 0.4214 -0.1698 0.1814  0.0463  202 THR A O   
1613  C CB  . THR A 202 ? 0.7561 0.7834 0.3858 -0.1910 0.1954  0.0210  202 THR A CB  
1614  O OG1 . THR A 202 ? 0.7389 0.7610 0.3877 -0.1786 0.1899  0.0184  202 THR A OG1 
1615  C CG2 . THR A 202 ? 0.7348 0.7988 0.3709 -0.1906 0.1945  0.0140  202 THR A CG2 
1616  N N   . SER A 203 ? 0.8131 0.7658 0.4204 -0.1907 0.1984  0.0366  203 SER A N   
1617  C CA  . SER A 203 ? 0.8319 0.7502 0.4387 -0.1827 0.1982  0.0412  203 SER A CA  
1618  C C   . SER A 203 ? 0.8066 0.7349 0.4399 -0.1641 0.1916  0.0388  203 SER A C   
1619  O O   . SER A 203 ? 0.8191 0.7286 0.4578 -0.1509 0.1871  0.0458  203 SER A O   
1620  C CB  . SER A 203 ? 0.8490 0.7463 0.4476 -0.1953 0.2078  0.0368  203 SER A CB  
1621  O OG  . SER A 203 ? 0.8223 0.7430 0.4354 -0.1986 0.2104  0.0254  203 SER A OG  
1622  N N   . THR A 204 ? 0.7728 0.7317 0.4244 -0.1632 0.1909  0.0301  204 THR A N   
1623  C CA  . THR A 204 ? 0.7490 0.7198 0.4279 -0.1483 0.1860  0.0288  204 THR A CA  
1624  C C   . THR A 204 ? 0.7289 0.7242 0.4202 -0.1410 0.1732  0.0290  204 THR A C   
1625  O O   . THR A 204 ? 0.7242 0.7198 0.4337 -0.1282 0.1637  0.0341  204 THR A O   
1626  C CB  . THR A 204 ? 0.7307 0.7129 0.4203 -0.1511 0.1938  0.0196  204 THR A CB  
1627  O OG1 . THR A 204 ? 0.7122 0.7210 0.3999 -0.1611 0.1931  0.0122  204 THR A OG1 
1628  C CG2 . THR A 204 ? 0.7565 0.7099 0.4297 -0.1577 0.2048  0.0175  204 THR A CG2 
1629  N N   . LEU A 205 ? 0.7193 0.7347 0.4014 -0.1489 0.1724  0.0235  205 LEU A N   
1630  C CA  . LEU A 205 ? 0.7032 0.7393 0.3934 -0.1416 0.1604  0.0211  205 LEU A CA  
1631  C C   . LEU A 205 ? 0.7246 0.7480 0.4017 -0.1344 0.1486  0.0286  205 LEU A C   
1632  O O   . LEU A 205 ? 0.7512 0.7600 0.4019 -0.1400 0.1523  0.0336  205 LEU A O   
1633  C CB  . LEU A 205 ? 0.6921 0.7521 0.3742 -0.1497 0.1644  0.0127  205 LEU A CB  
1634  C CG  . LEU A 205 ? 0.6762 0.7567 0.3657 -0.1413 0.1532  0.0071  205 LEU A CG  
1635  C CD1 . LEU A 205 ? 0.6535 0.7404 0.3719 -0.1331 0.1460  0.0053  205 LEU A CD1 
1636  C CD2 . LEU A 205 ? 0.6686 0.7727 0.3506 -0.1478 0.1597  -0.0008 205 LEU A CD2 
1637  N N   . ASN A 206 ? 0.7154 0.7434 0.4105 -0.1227 0.1335  0.0300  206 ASN A N   
1638  C CA  . ASN A 206 ? 0.7361 0.7535 0.4185 -0.1150 0.1176  0.0355  206 ASN A CA  
1639  C C   . ASN A 206 ? 0.7225 0.7559 0.4155 -0.1084 0.1018  0.0293  206 ASN A C   
1640  O O   . ASN A 206 ? 0.7141 0.7493 0.4334 -0.1006 0.0879  0.0321  206 ASN A O   
1641  C CB  . ASN A 206 ? 0.7501 0.7483 0.4452 -0.1065 0.1104  0.0463  206 ASN A CB  
1642  C CG  . ASN A 206 ? 0.7761 0.7616 0.4561 -0.0985 0.0911  0.0526  206 ASN A CG  
1643  O OD1 . ASN A 206 ? 0.7958 0.7765 0.4420 -0.1011 0.0888  0.0512  206 ASN A OD1 
1644  N ND2 . ASN A 206 ? 0.7789 0.7593 0.4837 -0.0882 0.0771  0.0602  206 ASN A ND2 
1645  N N   . GLN A 207 ? 0.7231 0.7678 0.3961 -0.1115 0.1041  0.0213  207 GLN A N   
1646  C CA  . GLN A 207 ? 0.7125 0.7705 0.3922 -0.1055 0.0913  0.0129  207 GLN A CA  
1647  C C   . GLN A 207 ? 0.7424 0.7907 0.3886 -0.0996 0.0793  0.0110  207 GLN A C   
1648  O O   . GLN A 207 ? 0.7667 0.8069 0.3806 -0.1026 0.0880  0.0139  207 GLN A O   
1649  C CB  . GLN A 207 ? 0.6897 0.7696 0.3752 -0.1110 0.1041  0.0034  207 GLN A CB  
1650  C CG  . GLN A 207 ? 0.6877 0.7790 0.3673 -0.1049 0.0950  -0.0066 207 GLN A CG  
1651  C CD  . GLN A 207 ? 0.6674 0.7811 0.3535 -0.1092 0.1078  -0.0147 207 GLN A CD  
1652  O OE1 . GLN A 207 ? 0.6758 0.8003 0.3425 -0.1083 0.1135  -0.0210 207 GLN A OE1 
1653  N NE2 . GLN A 207 ? 0.6433 0.7645 0.3561 -0.1131 0.1127  -0.0141 207 GLN A NE2 
1654  N N   . ARG A 208 ? 0.7442 0.7914 0.3968 -0.0914 0.0590  0.0064  208 ARG A N   
1655  C CA  . ARG A 208 ? 0.7754 0.8120 0.3927 -0.0840 0.0461  0.0012  208 ARG A CA  
1656  C C   . ARG A 208 ? 0.7669 0.8099 0.3951 -0.0781 0.0315  -0.0097 208 ARG A C   
1657  O O   . ARG A 208 ? 0.7606 0.7994 0.4154 -0.0757 0.0124  -0.0081 208 ARG A O   
1658  C CB  . ARG A 208 ? 0.8073 0.8201 0.4102 -0.0786 0.0276  0.0098  208 ARG A CB  
1659  C CG  . ARG A 208 ? 0.8498 0.8466 0.4033 -0.0713 0.0179  0.0054  208 ARG A CG  
1660  C CD  . ARG A 208 ? 0.8820 0.8547 0.4250 -0.0644 -0.0086 0.0120  208 ARG A CD  
1661  N NE  . ARG A 208 ? 0.9311 0.8835 0.4166 -0.0579 -0.0136 0.0105  208 ARG A NE  
1662  C CZ  . ARG A 208 ? 0.9572 0.8993 0.4074 -0.0602 0.0017  0.0189  208 ARG A CZ  
1663  N NH1 . ARG A 208 ? 0.9393 0.8876 0.4061 -0.0695 0.0218  0.0285  208 ARG A NH1 
1664  N NH2 . ARG A 208 ? 1.0059 0.9290 0.4014 -0.0531 -0.0027 0.0177  208 ARG A NH2 
1665  N N   . LEU A 209 ? 0.7687 0.8221 0.3780 -0.0759 0.0406  -0.0202 209 LEU A N   
1666  C CA  . LEU A 209 ? 0.7646 0.8213 0.3805 -0.0693 0.0283  -0.0315 209 LEU A CA  
1667  C C   . LEU A 209 ? 0.8067 0.8429 0.3833 -0.0583 0.0107  -0.0391 209 LEU A C   
1668  O O   . LEU A 209 ? 0.8365 0.8649 0.3733 -0.0551 0.0178  -0.0385 209 LEU A O   
1669  C CB  . LEU A 209 ? 0.7448 0.8247 0.3637 -0.0706 0.0476  -0.0393 209 LEU A CB  
1670  C CG  . LEU A 209 ? 0.7087 0.8076 0.3592 -0.0814 0.0652  -0.0340 209 LEU A CG  
1671  C CD1 . LEU A 209 ? 0.6966 0.8187 0.3443 -0.0823 0.0822  -0.0415 209 LEU A CD1 
1672  C CD2 . LEU A 209 ? 0.6849 0.7836 0.3747 -0.0833 0.0546  -0.0307 209 LEU A CD2 
1673  N N   . VAL A 210 ? 0.8129 0.8384 0.3990 -0.0530 -0.0124 -0.0458 210 VAL A N   
1674  C CA  . VAL A 210 ? 0.8573 0.8594 0.4039 -0.0415 -0.0317 -0.0563 210 VAL A CA  
1675  C C   . VAL A 210 ? 0.8542 0.8578 0.4064 -0.0354 -0.0376 -0.0697 210 VAL A C   
1676  O O   . VAL A 210 ? 0.8225 0.8362 0.4166 -0.0412 -0.0407 -0.0679 210 VAL A O   
1677  C CB  . VAL A 210 ? 0.8825 0.8597 0.4291 -0.0407 -0.0627 -0.0515 210 VAL A CB  
1678  C CG1 . VAL A 210 ? 0.8902 0.8638 0.4289 -0.0446 -0.0576 -0.0378 210 VAL A CG1 
1679  C CG2 . VAL A 210 ? 0.8562 0.8372 0.4560 -0.0471 -0.0805 -0.0478 210 VAL A CG2 
1680  N N   . PRO A 211 ? 0.8902 0.8826 0.3989 -0.0226 -0.0381 -0.0828 211 PRO A N   
1681  C CA  . PRO A 211 ? 0.8920 0.8819 0.4041 -0.0146 -0.0447 -0.0959 211 PRO A CA  
1682  C C   . PRO A 211 ? 0.9092 0.8717 0.4324 -0.0142 -0.0790 -0.0999 211 PRO A C   
1683  O O   . PRO A 211 ? 0.9466 0.8826 0.4455 -0.0115 -0.1016 -0.1010 211 PRO A O   
1684  C CB  . PRO A 211 ? 0.9327 0.9159 0.3910 0.0011  -0.0348 -0.1085 211 PRO A CB  
1685  C CG  . PRO A 211 ? 0.9404 0.9329 0.3754 -0.0020 -0.0151 -0.0994 211 PRO A CG  
1686  C CD  . PRO A 211 ? 0.9305 0.9142 0.3852 -0.0140 -0.0283 -0.0855 211 PRO A CD  
1687  N N   . ARG A 212 ? 0.8844 0.8529 0.4440 -0.0178 -0.0835 -0.1013 212 ARG A N   
1688  C CA  . ARG A 212 ? 0.8995 0.8437 0.4755 -0.0197 -0.1149 -0.1043 212 ARG A CA  
1689  C C   . ARG A 212 ? 0.9329 0.8559 0.4793 -0.0057 -0.1239 -0.1220 212 ARG A C   
1690  O O   . ARG A 212 ? 0.9152 0.8536 0.4684 -0.0008 -0.1069 -0.1266 212 ARG A O   
1691  C CB  . ARG A 212 ? 0.8540 0.8164 0.4906 -0.0337 -0.1135 -0.0921 212 ARG A CB  
1692  C CG  . ARG A 212 ? 0.8205 0.8051 0.4878 -0.0452 -0.1004 -0.0754 212 ARG A CG  
1693  C CD  . ARG A 212 ? 0.7839 0.7832 0.5084 -0.0572 -0.1005 -0.0634 212 ARG A CD  
1694  N NE  . ARG A 212 ? 0.7648 0.7740 0.5015 -0.0565 -0.0886 -0.0673 212 ARG A NE  
1695  C CZ  . ARG A 212 ? 0.7355 0.7689 0.4767 -0.0573 -0.0611 -0.0655 212 ARG A CZ  
1696  N NH1 . ARG A 212 ? 0.7210 0.7709 0.4563 -0.0600 -0.0411 -0.0599 212 ARG A NH1 
1697  N NH2 . ARG A 212 ? 0.7235 0.7628 0.4746 -0.0556 -0.0550 -0.0690 212 ARG A NH2 
1698  N N   . ILE A 213 ? 0.9847 0.8707 0.4968 0.0016  -0.1517 -0.1322 213 ILE A N   
1699  C CA  . ILE A 213 ? 1.0270 0.8849 0.5038 0.0172  -0.1628 -0.1509 213 ILE A CA  
1700  C C   . ILE A 213 ? 1.0286 0.8665 0.5382 0.0100  -0.1893 -0.1519 213 ILE A C   
1701  O O   . ILE A 213 ? 1.0265 0.8555 0.5654 -0.0039 -0.2128 -0.1428 213 ILE A O   
1702  C CB  . ILE A 213 ? 1.0926 0.9150 0.5047 0.0309  -0.1788 -0.1636 213 ILE A CB  
1703  C CG1 . ILE A 213 ? 1.0951 0.9376 0.4720 0.0388  -0.1485 -0.1618 213 ILE A CG1 
1704  C CG2 . ILE A 213 ? 1.1430 0.9306 0.5158 0.0486  -0.1921 -0.1843 213 ILE A CG2 
1705  C CD1 . ILE A 213 ? 1.1504 0.9637 0.4728 0.0455  -0.1632 -0.1653 213 ILE A CD1 
1706  N N   . ALA A 214 ? 1.0337 0.8656 0.5400 0.0195  -0.1852 -0.1620 214 ALA A N   
1707  C CA  . ALA A 214 ? 1.0427 0.8507 0.5743 0.0138  -0.2095 -0.1637 214 ALA A CA  
1708  C C   . ALA A 214 ? 1.0694 0.8598 0.5741 0.0322  -0.2065 -0.1801 214 ALA A C   
1709  O O   . ALA A 214 ? 1.0581 0.8715 0.5465 0.0456  -0.1785 -0.1850 214 ALA A O   
1710  C CB  . ALA A 214 ? 0.9855 0.8235 0.5825 -0.0052 -0.2009 -0.1445 214 ALA A CB  
1711  N N   . THR A 215 ? 1.1070 0.8564 0.6088 0.0326  -0.2362 -0.1881 215 THR A N   
1712  C CA  . THR A 215 ? 1.1350 0.8625 0.6161 0.0498  -0.2368 -0.2027 215 THR A CA  
1713  C C   . THR A 215 ? 1.0853 0.8399 0.6173 0.0408  -0.2219 -0.1898 215 THR A C   
1714  O O   . THR A 215 ? 1.0671 0.8189 0.6427 0.0216  -0.2359 -0.1764 215 THR A O   
1715  C CB  . THR A 215 ? 1.1998 0.8669 0.6570 0.0525  -0.2766 -0.2161 215 THR A CB  
1716  O OG1 . THR A 215 ? 1.2475 0.8877 0.6585 0.0577  -0.2944 -0.2262 215 THR A OG1 
1717  C CG2 . THR A 215 ? 1.2378 0.8772 0.6641 0.0751  -0.2761 -0.2336 215 THR A CG2 
1718  N N   . ARG A 216 ? 1.0655 0.8476 0.5922 0.0548  -0.1935 -0.1929 216 ARG A N   
1719  C CA  . ARG A 216 ? 1.0187 0.8300 0.5889 0.0474  -0.1771 -0.1803 216 ARG A CA  
1720  C C   . ARG A 216 ? 1.0427 0.8397 0.5972 0.0674  -0.1753 -0.1922 216 ARG A C   
1721  O O   . ARG A 216 ? 1.0852 0.8639 0.5950 0.0901  -0.1756 -0.2103 216 ARG A O   
1722  C CB  . ARG A 216 ? 0.9650 0.8300 0.5521 0.0425  -0.1440 -0.1695 216 ARG A CB  
1723  C CG  . ARG A 216 ? 0.9415 0.8212 0.5447 0.0244  -0.1436 -0.1569 216 ARG A CG  
1724  C CD  . ARG A 216 ? 0.9010 0.8261 0.5093 0.0226  -0.1116 -0.1499 216 ARG A CD  
1725  N NE  . ARG A 216 ? 0.9272 0.8543 0.4902 0.0378  -0.1010 -0.1615 216 ARG A NE  
1726  C CZ  . ARG A 216 ? 0.9401 0.8638 0.4819 0.0349  -0.1024 -0.1602 216 ARG A CZ  
1727  N NH1 . ARG A 216 ? 0.9279 0.8474 0.4916 0.0179  -0.1154 -0.1484 216 ARG A NH1 
1728  N NH2 . ARG A 216 ? 0.9675 0.8929 0.4658 0.0498  -0.0901 -0.1701 216 ARG A NH2 
1729  N N   . SER A 217 ? 1.0183 0.8229 0.6084 0.0601  -0.1730 -0.1815 217 SER A N   
1730  C CA  . SER A 217 ? 1.0374 0.8311 0.6182 0.0787  -0.1711 -0.1899 217 SER A CA  
1731  C C   . SER A 217 ? 1.0158 0.8530 0.5876 0.0954  -0.1402 -0.1944 217 SER A C   
1732  O O   . SER A 217 ? 0.9720 0.8524 0.5601 0.0853  -0.1188 -0.1847 217 SER A O   
1733  C CB  . SER A 217 ? 1.0163 0.8078 0.6375 0.0646  -0.1762 -0.1743 217 SER A CB  
1734  O OG  . SER A 217 ? 1.0288 0.7902 0.6687 0.0443  -0.2013 -0.1658 217 SER A OG  
1735  N N   . LYS A 218 ? 1.0499 0.8753 0.5969 0.1209  -0.1385 -0.2089 218 LYS A N   
1736  C CA  . LYS A 218 ? 1.0328 0.9022 0.5763 0.1379  -0.1103 -0.2128 218 LYS A CA  
1737  C C   . LYS A 218 ? 0.9828 0.8891 0.5683 0.1280  -0.0968 -0.1974 218 LYS A C   
1738  O O   . LYS A 218 ? 0.9894 0.8766 0.5890 0.1284  -0.1086 -0.1932 218 LYS A O   
1739  C CB  . LYS A 218 ? 1.0865 0.9339 0.5942 0.1706  -0.1123 -0.2325 218 LYS A CB  
1740  C CG  . LYS A 218 ? 1.1315 0.9648 0.5910 0.1870  -0.1099 -0.2491 218 LYS A CG  
1741  C CD  . LYS A 218 ? 1.1832 1.0018 0.6094 0.2225  -0.1060 -0.2682 218 LYS A CD  
1742  C CE  . LYS A 218 ? 1.2387 1.0358 0.6096 0.2409  -0.1043 -0.2857 218 LYS A CE  
1743  N NZ  . LYS A 218 ? 1.2947 1.0234 0.6317 0.2381  -0.1384 -0.2959 218 LYS A NZ  
1744  N N   . VAL A 219 ? 0.9367 0.8929 0.5397 0.1184  -0.0731 -0.1885 219 VAL A N   
1745  C CA  . VAL A 219 ? 0.8933 0.8881 0.5294 0.1118  -0.0582 -0.1765 219 VAL A CA  
1746  C C   . VAL A 219 ? 0.8858 0.9237 0.5158 0.1284  -0.0350 -0.1835 219 VAL A C   
1747  O O   . VAL A 219 ? 0.8843 0.9400 0.4999 0.1284  -0.0217 -0.1872 219 VAL A O   
1748  C CB  . VAL A 219 ? 0.8480 0.8627 0.5125 0.0834  -0.0516 -0.1590 219 VAL A CB  
1749  C CG1 . VAL A 219 ? 0.8082 0.8626 0.5001 0.0771  -0.0353 -0.1482 219 VAL A CG1 
1750  C CG2 . VAL A 219 ? 0.8561 0.8328 0.5322 0.0675  -0.0733 -0.1506 219 VAL A CG2 
1751  N N   . ASN A 220 ? 0.8841 0.9387 0.5256 0.1427  -0.0306 -0.1848 220 ASN A N   
1752  C CA  . ASN A 220 ? 0.8831 0.9796 0.5229 0.1616  -0.0105 -0.1921 220 ASN A CA  
1753  C C   . ASN A 220 ? 0.9260 1.0097 0.5281 0.1836  -0.0066 -0.2089 220 ASN A C   
1754  O O   . ASN A 220 ? 0.9203 1.0418 0.5183 0.1898  0.0149  -0.2117 220 ASN A O   
1755  C CB  . ASN A 220 ? 0.8354 0.9854 0.4995 0.1434  0.0111  -0.1809 220 ASN A CB  
1756  C CG  . ASN A 220 ? 0.8027 0.9774 0.4997 0.1340  0.0124  -0.1691 220 ASN A CG  
1757  O OD1 . ASN A 220 ? 0.8085 0.9566 0.5122 0.1330  -0.0032 -0.1646 220 ASN A OD1 
1758  N ND2 . ASN A 220 ? 0.7718 0.9964 0.4881 0.1265  0.0308  -0.1637 220 ASN A ND2 
1759  N N   . GLY A 221 ? 0.9723 1.0010 0.5456 0.1948  -0.0276 -0.2197 221 GLY A N   
1760  C CA  . GLY A 221 ? 1.0241 1.0303 0.5537 0.2181  -0.0270 -0.2375 221 GLY A CA  
1761  C C   . GLY A 221 ? 1.0295 1.0311 0.5348 0.2068  -0.0227 -0.2383 221 GLY A C   
1762  O O   . GLY A 221 ? 1.0714 1.0619 0.5375 0.2261  -0.0170 -0.2520 221 GLY A O   
1763  N N   . GLN A 222 ? 0.9912 0.9999 0.5174 0.1772  -0.0252 -0.2237 222 GLN A N   
1764  C CA  . GLN A 222 ? 0.9947 0.9993 0.5006 0.1651  -0.0226 -0.2221 222 GLN A CA  
1765  C C   . GLN A 222 ? 0.9818 0.9567 0.5002 0.1401  -0.0447 -0.2123 222 GLN A C   
1766  O O   . GLN A 222 ? 0.9447 0.9282 0.5006 0.1231  -0.0486 -0.1992 222 GLN A O   
1767  C CB  . GLN A 222 ? 0.9553 1.0161 0.4780 0.1547  0.0063  -0.2119 222 GLN A CB  
1768  C CG  . GLN A 222 ? 0.9672 1.0652 0.4822 0.1771  0.0310  -0.2195 222 GLN A CG  
1769  C CD  . GLN A 222 ? 1.0295 1.1016 0.4926 0.2024  0.0322  -0.2364 222 GLN A CD  
1770  O OE1 . GLN A 222 ? 1.0580 1.0965 0.4877 0.1981  0.0217  -0.2397 222 GLN A OE1 
1771  N NE2 . GLN A 222 ? 1.0543 1.1419 0.5096 0.2302  0.0449  -0.2471 222 GLN A NE2 
1772  N N   . SER A 223 ? 1.0150 0.9557 0.5014 0.1388  -0.0590 -0.2182 223 SER A N   
1773  C CA  . SER A 223 ? 1.0071 0.9219 0.5064 0.1160  -0.0812 -0.2090 223 SER A CA  
1774  C C   . SER A 223 ? 0.9779 0.9171 0.4829 0.0982  -0.0696 -0.1975 223 SER A C   
1775  O O   . SER A 223 ? 0.9675 0.8930 0.4877 0.0794  -0.0850 -0.1881 223 SER A O   
1776  C CB  . SER A 223 ? 1.0685 0.9240 0.5313 0.1250  -0.1114 -0.2230 223 SER A CB  
1777  O OG  . SER A 223 ? 1.0897 0.9161 0.5577 0.1337  -0.1276 -0.2289 223 SER A OG  
1778  N N   . GLY A 224 ? 0.9665 0.9418 0.4609 0.1042  -0.0426 -0.1975 224 GLY A N   
1779  C CA  . GLY A 224 ? 0.9370 0.9381 0.4393 0.0871  -0.0282 -0.1850 224 GLY A CA  
1780  C C   . GLY A 224 ? 0.8777 0.9136 0.4293 0.0676  -0.0165 -0.1690 224 GLY A C   
1781  O O   . GLY A 224 ? 0.8589 0.9086 0.4342 0.0704  -0.0128 -0.1682 224 GLY A O   
1782  N N   . ARG A 225 ? 0.8521 0.8996 0.4162 0.0491  -0.0111 -0.1564 225 ARG A N   
1783  C CA  . ARG A 225 ? 0.8013 0.8767 0.4074 0.0305  -0.0004 -0.1416 225 ARG A CA  
1784  C C   . ARG A 225 ? 0.7795 0.8859 0.3866 0.0206  0.0226  -0.1333 225 ARG A C   
1785  O O   . ARG A 225 ? 0.8009 0.9007 0.3804 0.0220  0.0255  -0.1342 225 ARG A O   
1786  C CB  . ARG A 225 ? 0.7900 0.8441 0.4202 0.0148  -0.0196 -0.1317 225 ARG A CB  
1787  C CG  . ARG A 225 ? 0.8079 0.8319 0.4451 0.0193  -0.0427 -0.1363 225 ARG A CG  
1788  C CD  . ARG A 225 ? 0.7850 0.8247 0.4473 0.0202  -0.0354 -0.1333 225 ARG A CD  
1789  N NE  . ARG A 225 ? 0.8047 0.8123 0.4743 0.0226  -0.0576 -0.1353 225 ARG A NE  
1790  C CZ  . ARG A 225 ? 0.8404 0.8250 0.4885 0.0406  -0.0685 -0.1487 225 ARG A CZ  
1791  N NH1 . ARG A 225 ? 0.8608 0.8534 0.4789 0.0601  -0.0578 -0.1620 225 ARG A NH1 
1792  N NH2 . ARG A 225 ? 0.8587 0.8110 0.5158 0.0393  -0.0897 -0.1483 225 ARG A NH2 
1793  N N   . MET A 226 ? 0.7408 0.8781 0.3776 0.0104  0.0378  -0.1250 226 MET A N   
1794  C CA  . MET A 226 ? 0.7189 0.8830 0.3616 -0.0024 0.0580  -0.1160 226 MET A CA  
1795  C C   . MET A 226 ? 0.6843 0.8508 0.3585 -0.0205 0.0571  -0.1035 226 MET A C   
1796  O O   . MET A 226 ? 0.6665 0.8373 0.3637 -0.0226 0.0541  -0.1015 226 MET A O   
1797  C CB  . MET A 226 ? 0.7095 0.9110 0.3573 0.0024  0.0783  -0.1189 226 MET A CB  
1798  C CG  . MET A 226 ? 0.7433 0.9502 0.3608 0.0206  0.0864  -0.1295 226 MET A CG  
1799  S SD  . MET A 226 ? 0.7615 0.9743 0.3510 0.0146  0.1030  -0.1243 226 MET A SD  
1800  C CE  . MET A 226 ? 0.8017 1.0249 0.3593 0.0401  0.1148  -0.1375 226 MET A CE  
1801  N N   . GLU A 227 ? 0.6783 0.8406 0.3515 -0.0324 0.0604  -0.0948 227 GLU A N   
1802  C CA  . GLU A 227 ? 0.6499 0.8132 0.3506 -0.0475 0.0615  -0.0831 227 GLU A CA  
1803  C C   . GLU A 227 ? 0.6333 0.8183 0.3362 -0.0587 0.0820  -0.0768 227 GLU A C   
1804  O O   . GLU A 227 ? 0.6461 0.8288 0.3310 -0.0614 0.0883  -0.0742 227 GLU A O   
1805  C CB  . GLU A 227 ? 0.6595 0.7967 0.3621 -0.0513 0.0453  -0.0773 227 GLU A CB  
1806  C CG  . GLU A 227 ? 0.6354 0.7710 0.3714 -0.0623 0.0429  -0.0664 227 GLU A CG  
1807  C CD  . GLU A 227 ? 0.6460 0.7596 0.3910 -0.0645 0.0242  -0.0608 227 GLU A CD  
1808  O OE1 . GLU A 227 ? 0.6742 0.7699 0.3974 -0.0576 0.0093  -0.0666 227 GLU A OE1 
1809  O OE2 . GLU A 227 ? 0.6284 0.7430 0.4026 -0.0729 0.0242  -0.0503 227 GLU A OE2 
1810  N N   . PHE A 228 ? 0.6086 0.8121 0.3316 -0.0655 0.0914  -0.0741 228 PHE A N   
1811  C CA  . PHE A 228 ? 0.5967 0.8206 0.3215 -0.0767 0.1093  -0.0700 228 PHE A CA  
1812  C C   . PHE A 228 ? 0.5824 0.7971 0.3200 -0.0900 0.1127  -0.0600 228 PHE A C   
1813  O O   . PHE A 228 ? 0.5707 0.7768 0.3254 -0.0913 0.1064  -0.0564 228 PHE A O   
1814  C CB  . PHE A 228 ? 0.5850 0.8361 0.3204 -0.0753 0.1165  -0.0746 228 PHE A CB  
1815  C CG  . PHE A 228 ? 0.6003 0.8656 0.3238 -0.0610 0.1178  -0.0840 228 PHE A CG  
1816  C CD1 . PHE A 228 ? 0.6111 0.8955 0.3223 -0.0619 0.1320  -0.0848 228 PHE A CD1 
1817  C CD2 . PHE A 228 ? 0.6077 0.8658 0.3316 -0.0459 0.1055  -0.0915 228 PHE A CD2 
1818  C CE1 . PHE A 228 ? 0.6280 0.9275 0.3284 -0.0466 0.1358  -0.0932 228 PHE A CE1 
1819  C CE2 . PHE A 228 ? 0.6260 0.8953 0.3372 -0.0299 0.1075  -0.1010 228 PHE A CE2 
1820  C CZ  . PHE A 228 ? 0.6359 0.9274 0.3356 -0.0295 0.1236  -0.1020 228 PHE A CZ  
1821  N N   . PHE A 229 ? 0.5868 0.8023 0.3148 -0.0991 0.1235  -0.0552 229 PHE A N   
1822  C CA  . PHE A 229 ? 0.5798 0.7836 0.3154 -0.1099 0.1281  -0.0464 229 PHE A CA  
1823  C C   . PHE A 229 ? 0.5761 0.7938 0.3101 -0.1223 0.1433  -0.0450 229 PHE A C   
1824  O O   . PHE A 229 ? 0.5802 0.8177 0.3073 -0.1239 0.1507  -0.0488 229 PHE A O   
1825  C CB  . PHE A 229 ? 0.5963 0.7792 0.3197 -0.1090 0.1232  -0.0407 229 PHE A CB  
1826  C CG  . PHE A 229 ? 0.6018 0.7687 0.3300 -0.0995 0.1051  -0.0411 229 PHE A CG  
1827  C CD1 . PHE A 229 ? 0.6173 0.7820 0.3306 -0.0887 0.0948  -0.0490 229 PHE A CD1 
1828  C CD2 . PHE A 229 ? 0.5946 0.7484 0.3427 -0.1011 0.0982  -0.0336 229 PHE A CD2 
1829  C CE1 . PHE A 229 ? 0.6265 0.7735 0.3436 -0.0815 0.0753  -0.0499 229 PHE A CE1 
1830  C CE2 . PHE A 229 ? 0.6007 0.7418 0.3577 -0.0946 0.0799  -0.0329 229 PHE A CE2 
1831  C CZ  . PHE A 229 ? 0.6174 0.7535 0.3582 -0.0857 0.0671  -0.0414 229 PHE A CZ  
1832  N N   . TRP A 230 ? 0.5705 0.7776 0.3117 -0.1311 0.1480  -0.0394 230 TRP A N   
1833  C CA  . TRP A 230 ? 0.5711 0.7856 0.3100 -0.1444 0.1597  -0.0387 230 TRP A CA  
1834  C C   . TRP A 230 ? 0.5791 0.7700 0.3142 -0.1520 0.1649  -0.0317 230 TRP A C   
1835  O O   . TRP A 230 ? 0.5784 0.7515 0.3191 -0.1460 0.1601  -0.0271 230 TRP A O   
1836  C CB  . TRP A 230 ? 0.5577 0.7874 0.3084 -0.1459 0.1595  -0.0435 230 TRP A CB  
1837  C CG  . TRP A 230 ? 0.5493 0.7649 0.3102 -0.1418 0.1551  -0.0411 230 TRP A CG  
1838  C CD1 . TRP A 230 ? 0.5412 0.7556 0.3126 -0.1311 0.1457  -0.0416 230 TRP A CD1 
1839  C CD2 . TRP A 230 ? 0.5521 0.7519 0.3127 -0.1483 0.1613  -0.0373 230 TRP A CD2 
1840  N NE1 . TRP A 230 ? 0.5371 0.7390 0.3169 -0.1313 0.1468  -0.0369 230 TRP A NE1 
1841  C CE2 . TRP A 230 ? 0.5444 0.7373 0.3166 -0.1405 0.1570  -0.0347 230 TRP A CE2 
1842  C CE3 . TRP A 230 ? 0.5642 0.7529 0.3144 -0.1595 0.1702  -0.0359 230 TRP A CE3 
1843  C CZ2 . TRP A 230 ? 0.5484 0.7262 0.3213 -0.1423 0.1636  -0.0306 230 TRP A CZ2 
1844  C CZ3 . TRP A 230 ? 0.5697 0.7398 0.3184 -0.1605 0.1750  -0.0334 230 TRP A CZ3 
1845  C CH2 . TRP A 230 ? 0.5616 0.7277 0.3213 -0.1512 0.1727  -0.0307 230 TRP A CH2 
1846  N N   . THR A 231 ? 0.5890 0.7801 0.3160 -0.1651 0.1744  -0.0308 231 THR A N   
1847  C CA  . THR A 231 ? 0.6017 0.7675 0.3226 -0.1725 0.1800  -0.0257 231 THR A CA  
1848  C C   . THR A 231 ? 0.6102 0.7800 0.3263 -0.1879 0.1871  -0.0285 231 THR A C   
1849  O O   . THR A 231 ? 0.6067 0.8018 0.3258 -0.1943 0.1883  -0.0324 231 THR A O   
1850  C CB  . THR A 231 ? 0.6204 0.7671 0.3278 -0.1727 0.1813  -0.0182 231 THR A CB  
1851  O OG1 . THR A 231 ? 0.6325 0.7513 0.3367 -0.1749 0.1850  -0.0132 231 THR A OG1 
1852  C CG2 . THR A 231 ? 0.6355 0.7919 0.3292 -0.1839 0.1884  -0.0170 231 THR A CG2 
1853  N N   . ILE A 232 ? 0.6240 0.7688 0.3334 -0.1933 0.1913  -0.0268 232 ILE A N   
1854  C CA  . ILE A 232 ? 0.6415 0.7809 0.3415 -0.2100 0.1962  -0.0292 232 ILE A CA  
1855  C C   . ILE A 232 ? 0.6676 0.7835 0.3530 -0.2183 0.2017  -0.0223 232 ILE A C   
1856  O O   . ILE A 232 ? 0.6792 0.7664 0.3580 -0.2117 0.2030  -0.0175 232 ILE A O   
1857  C CB  . ILE A 232 ? 0.6469 0.7693 0.3428 -0.2104 0.1968  -0.0335 232 ILE A CB  
1858  C CG1 . ILE A 232 ? 0.6324 0.7808 0.3366 -0.2113 0.1914  -0.0407 232 ILE A CG1 
1859  C CG2 . ILE A 232 ? 0.6771 0.7727 0.3553 -0.2253 0.2014  -0.0342 232 ILE A CG2 
1860  C CD1 . ILE A 232 ? 0.6066 0.7804 0.3270 -0.1978 0.1857  -0.0411 232 ILE A CD1 
1861  N N   . LEU A 233 ? 0.6790 0.8082 0.3609 -0.2323 0.2051  -0.0208 233 LEU A N   
1862  C CA  . LEU A 233 ? 0.7079 0.8150 0.3744 -0.2427 0.2108  -0.0127 233 LEU A CA  
1863  C C   . LEU A 233 ? 0.7334 0.8185 0.3906 -0.2602 0.2132  -0.0146 233 LEU A C   
1864  O O   . LEU A 233 ? 0.7333 0.8380 0.3973 -0.2746 0.2124  -0.0192 233 LEU A O   
1865  C CB  . LEU A 233 ? 0.7099 0.8436 0.3771 -0.2490 0.2152  -0.0084 233 LEU A CB  
1866  C CG  . LEU A 233 ? 0.7411 0.8541 0.3900 -0.2587 0.2220  0.0024  233 LEU A CG  
1867  C CD1 . LEU A 233 ? 0.7497 0.8334 0.3854 -0.2434 0.2188  0.0087  233 LEU A CD1 
1868  C CD2 . LEU A 233 ? 0.7432 0.8892 0.3943 -0.2653 0.2292  0.0062  233 LEU A CD2 
1869  N N   . LYS A 234 ? 0.7581 0.8017 0.4001 -0.2583 0.2149  -0.0115 234 LYS A N   
1870  C CA  . LYS A 234 ? 0.7897 0.8033 0.4177 -0.2728 0.2160  -0.0147 234 LYS A CA  
1871  C C   . LYS A 234 ? 0.8186 0.8265 0.4385 -0.2950 0.2194  -0.0083 234 LYS A C   
1872  O O   . LYS A 234 ? 0.8197 0.8376 0.4395 -0.2955 0.2233  0.0007  234 LYS A O   
1873  C CB  . LYS A 234 ? 0.8093 0.7788 0.4232 -0.2603 0.2178  -0.0136 234 LYS A CB  
1874  C CG  . LYS A 234 ? 0.7851 0.7617 0.4096 -0.2402 0.2165  -0.0184 234 LYS A CG  
1875  C CD  . LYS A 234 ? 0.8082 0.7442 0.4204 -0.2287 0.2208  -0.0185 234 LYS A CD  
1876  C CE  . LYS A 234 ? 0.7873 0.7338 0.4108 -0.2120 0.2218  -0.0229 234 LYS A CE  
1877  N NZ  . LYS A 234 ? 0.8130 0.7226 0.4243 -0.2000 0.2290  -0.0238 234 LYS A NZ  
1878  N N   . PRO A 235 ? 0.8465 0.8373 0.4582 -0.3142 0.2176  -0.0126 235 PRO A N   
1879  C CA  . PRO A 235 ? 0.8751 0.8624 0.4829 -0.3385 0.2206  -0.0053 235 PRO A CA  
1880  C C   . PRO A 235 ? 0.9066 0.8553 0.4948 -0.3376 0.2262  0.0065  235 PRO A C   
1881  O O   . PRO A 235 ? 0.9195 0.8302 0.4931 -0.3228 0.2257  0.0062  235 PRO A O   
1882  C CB  . PRO A 235 ? 0.9026 0.8684 0.5024 -0.3574 0.2143  -0.0137 235 PRO A CB  
1883  C CG  . PRO A 235 ? 0.8850 0.8523 0.4848 -0.3425 0.2085  -0.0261 235 PRO A CG  
1884  C CD  . PRO A 235 ? 0.8581 0.8280 0.4608 -0.3148 0.2126  -0.0238 235 PRO A CD  
1885  N N   . ASN A 236 ? 0.9209 0.8806 0.5095 -0.3523 0.2319  0.0176  236 ASN A N   
1886  C CA  . ASN A 236 ? 0.9568 0.8792 0.5240 -0.3540 0.2369  0.0308  236 ASN A CA  
1887  C C   . ASN A 236 ? 0.9419 0.8622 0.5038 -0.3278 0.2374  0.0360  236 ASN A C   
1888  O O   . ASN A 236 ? 0.9719 0.8558 0.5142 -0.3233 0.2387  0.0461  236 ASN A O   
1889  C CB  . ASN A 236 ? 1.0013 0.8643 0.5467 -0.3612 0.2337  0.0292  236 ASN A CB  
1890  C CG  . ASN A 236 ? 1.0504 0.8831 0.5797 -0.3845 0.2378  0.0420  236 ASN A CG  
1891  O OD1 . ASN A 236 ? 1.0554 0.9097 0.5878 -0.3938 0.2448  0.0542  236 ASN A OD1 
1892  N ND2 . ASN A 236 ? 1.0935 0.8735 0.6034 -0.3940 0.2340  0.0393  236 ASN A ND2 
1893  N N   . ASP A 237 ? 0.8994 0.8574 0.4785 -0.3110 0.2348  0.0295  237 ASP A N   
1894  C CA  . ASP A 237 ? 0.8839 0.8441 0.4611 -0.2876 0.2323  0.0332  237 ASP A CA  
1895  C C   . ASP A 237 ? 0.8656 0.8683 0.4497 -0.2862 0.2356  0.0360  237 ASP A C   
1896  O O   . ASP A 237 ? 0.8470 0.8875 0.4474 -0.2951 0.2382  0.0304  237 ASP A O   
1897  C CB  . ASP A 237 ? 0.8546 0.8179 0.4451 -0.2676 0.2256  0.0233  237 ASP A CB  
1898  C CG  . ASP A 237 ? 0.8437 0.8041 0.4348 -0.2449 0.2204  0.0279  237 ASP A CG  
1899  O OD1 . ASP A 237 ? 0.8681 0.8075 0.4428 -0.2425 0.2204  0.0387  237 ASP A OD1 
1900  O OD2 . ASP A 237 ? 0.8125 0.7909 0.4206 -0.2301 0.2152  0.0213  237 ASP A OD2 
1901  N N   . ALA A 238 ? 0.8741 0.8693 0.4443 -0.2737 0.2350  0.0444  238 ALA A N   
1902  C CA  . ALA A 238 ? 0.8659 0.8942 0.4346 -0.2695 0.2387  0.0469  238 ALA A CA  
1903  C C   . ALA A 238 ? 0.8366 0.8791 0.4130 -0.2457 0.2289  0.0399  238 ALA A C   
1904  O O   . ALA A 238 ? 0.8354 0.8540 0.4106 -0.2318 0.2197  0.0402  238 ALA A O   
1905  C CB  . ALA A 238 ? 0.9055 0.9130 0.4463 -0.2744 0.2449  0.0620  238 ALA A CB  
1906  N N   . ILE A 239 ? 0.8151 0.8966 0.4011 -0.2412 0.2305  0.0339  239 ILE A N   
1907  C CA  . ILE A 239 ? 0.7951 0.8879 0.3838 -0.2199 0.2207  0.0280  239 ILE A CA  
1908  C C   . ILE A 239 ? 0.8188 0.9138 0.3822 -0.2136 0.2237  0.0345  239 ILE A C   
1909  O O   . ILE A 239 ? 0.8338 0.9460 0.3891 -0.2242 0.2368  0.0390  239 ILE A O   
1910  C CB  . ILE A 239 ? 0.7588 0.8879 0.3726 -0.2153 0.2183  0.0153  239 ILE A CB  
1911  C CG1 . ILE A 239 ? 0.7424 0.8749 0.3590 -0.1942 0.2058  0.0094  239 ILE A CG1 
1912  C CG2 . ILE A 239 ? 0.7584 0.9245 0.3769 -0.2246 0.2297  0.0140  239 ILE A CG2 
1913  C CD1 . ILE A 239 ? 0.7090 0.8652 0.3505 -0.1882 0.2005  -0.0017 239 ILE A CD1 
1914  N N   . ASN A 240 ? 0.8249 0.9023 0.3756 -0.1966 0.2115  0.0355  240 ASN A N   
1915  C CA  . ASN A 240 ? 0.8542 0.9263 0.3737 -0.1884 0.2115  0.0412  240 ASN A CA  
1916  C C   . ASN A 240 ? 0.8409 0.9257 0.3603 -0.1692 0.1992  0.0311  240 ASN A C   
1917  O O   . ASN A 240 ? 0.8235 0.8989 0.3572 -0.1586 0.1834  0.0264  240 ASN A O   
1918  C CB  . ASN A 240 ? 0.8876 0.9185 0.3833 -0.1860 0.2047  0.0535  240 ASN A CB  
1919  C CG  . ASN A 240 ? 0.9064 0.9160 0.3997 -0.2037 0.2147  0.0635  240 ASN A CG  
1920  O OD1 . ASN A 240 ? 0.9248 0.9421 0.4085 -0.2195 0.2300  0.0697  240 ASN A OD1 
1921  N ND2 . ASN A 240 ? 0.9052 0.8872 0.4076 -0.2011 0.2062  0.0655  240 ASN A ND2 
1922  N N   . PHE A 241 ? 0.8526 0.9577 0.3557 -0.1649 0.2071  0.0282  241 PHE A N   
1923  C CA  . PHE A 241 ? 0.8502 0.9627 0.3455 -0.1461 0.1958  0.0179  241 PHE A CA  
1924  C C   . PHE A 241 ? 0.8950 0.9859 0.3456 -0.1362 0.1925  0.0236  241 PHE A C   
1925  O O   . PHE A 241 ? 0.9262 1.0156 0.3515 -0.1435 0.2082  0.0333  241 PHE A O   
1926  C CB  . PHE A 241 ? 0.8334 0.9852 0.3417 -0.1445 0.2072  0.0081  241 PHE A CB  
1927  C CG  . PHE A 241 ? 0.7914 0.9638 0.3402 -0.1500 0.2057  0.0005  241 PHE A CG  
1928  C CD1 . PHE A 241 ? 0.7673 0.9402 0.3332 -0.1378 0.1898  -0.0097 241 PHE A CD1 
1929  C CD2 . PHE A 241 ? 0.7801 0.9694 0.3483 -0.1681 0.2191  0.0041  241 PHE A CD2 
1930  C CE1 . PHE A 241 ? 0.7330 0.9228 0.3321 -0.1423 0.1887  -0.0156 241 PHE A CE1 
1931  C CE2 . PHE A 241 ? 0.7466 0.9524 0.3473 -0.1725 0.2162  -0.0031 241 PHE A CE2 
1932  C CZ  . PHE A 241 ? 0.7232 0.9291 0.3381 -0.1590 0.2017  -0.0126 241 PHE A CZ  
1933  N N   . GLU A 242 ? 0.9014 0.9745 0.3418 -0.1203 0.1713  0.0181  242 GLU A N   
1934  C CA  . GLU A 242 ? 0.9469 1.0001 0.3411 -0.1078 0.1646  0.0198  242 GLU A CA  
1935  C C   . GLU A 242 ? 0.9431 0.9980 0.3352 -0.0904 0.1468  0.0048  242 GLU A C   
1936  O O   . GLU A 242 ? 0.9180 0.9675 0.3377 -0.0868 0.1277  -0.0003 242 GLU A O   
1937  C CB  . GLU A 242 ? 0.9751 0.9906 0.3498 -0.1077 0.1509  0.0322  242 GLU A CB  
1938  C CG  . GLU A 242 ? 1.0307 1.0220 0.3504 -0.0963 0.1445  0.0361  242 GLU A CG  
1939  C CD  . GLU A 242 ? 1.0591 1.0131 0.3618 -0.0947 0.1274  0.0487  242 GLU A CD  
1940  O OE1 . GLU A 242 ? 1.0649 1.0083 0.3702 -0.1068 0.1376  0.0622  242 GLU A OE1 
1941  O OE2 . GLU A 242 ? 1.0787 1.0127 0.3651 -0.0812 0.1024  0.0452  242 GLU A OE2 
1942  N N   . SER A 243 ? 0.9709 1.0322 0.3301 -0.0795 0.1538  -0.0017 243 SER A N   
1943  C CA  . SER A 243 ? 0.9747 1.0332 0.3265 -0.0621 0.1371  -0.0173 243 SER A CA  
1944  C C   . SER A 243 ? 1.0288 1.0757 0.3243 -0.0469 0.1404  -0.0219 243 SER A C   
1945  O O   . SER A 243 ? 1.0499 1.1119 0.3240 -0.0488 0.1657  -0.0169 243 SER A O   
1946  C CB  . SER A 243 ? 0.9327 1.0245 0.3231 -0.0619 0.1444  -0.0286 243 SER A CB  
1947  O OG  . SER A 243 ? 0.9382 1.0226 0.3226 -0.0455 0.1266  -0.0433 243 SER A OG  
1948  N N   . ASN A 244 ? 1.0533 1.0732 0.3255 -0.0320 0.1146  -0.0313 244 ASN A N   
1949  C CA  . ASN A 244 ? 1.1094 1.1126 0.3238 -0.0142 0.1134  -0.0396 244 ASN A CA  
1950  C C   . ASN A 244 ? 1.1056 1.1145 0.3235 0.0013  0.1049  -0.0593 244 ASN A C   
1951  O O   . ASN A 244 ? 1.1543 1.1405 0.3245 0.0187  0.0955  -0.0698 244 ASN A O   
1952  C CB  . ASN A 244 ? 1.1557 1.1150 0.3289 -0.0081 0.0870  -0.0355 244 ASN A CB  
1953  C CG  . ASN A 244 ? 1.1372 1.0787 0.3381 -0.0062 0.0513  -0.0422 244 ASN A CG  
1954  O OD1 . ASN A 244 ? 1.0834 1.0433 0.3408 -0.0157 0.0485  -0.0421 244 ASN A OD1 
1955  N ND2 . ASN A 244 ? 1.1844 1.0899 0.3455 0.0053  0.0235  -0.0473 244 ASN A ND2 
1956  N N   . GLY A 245 ? 1.0521 1.0881 0.3231 -0.0043 0.1076  -0.0643 245 GLY A N   
1957  C CA  . GLY A 245 ? 1.0470 1.0885 0.3252 0.0097  0.1002  -0.0818 245 GLY A CA  
1958  C C   . GLY A 245 ? 0.9882 1.0516 0.3267 0.0015  0.0961  -0.0844 245 GLY A C   
1959  O O   . GLY A 245 ? 0.9536 1.0176 0.3276 -0.0133 0.0888  -0.0751 245 GLY A O   
1960  N N   . ASN A 246 ? 0.9812 1.0615 0.3283 0.0127  0.1017  -0.0971 246 ASN A N   
1961  C CA  . ASN A 246 ? 0.9363 1.0308 0.3317 0.0096  0.0938  -0.1022 246 ASN A CA  
1962  C C   . ASN A 246 ? 0.8841 1.0126 0.3272 -0.0086 0.1105  -0.0917 246 ASN A C   
1963  O O   . ASN A 246 ? 0.8476 0.9801 0.3293 -0.0155 0.1005  -0.0914 246 ASN A O   
1964  C CB  . ASN A 246 ? 0.9352 0.9971 0.3405 0.0092  0.0605  -0.1052 246 ASN A CB  
1965  C CG  . ASN A 246 ? 0.9901 1.0148 0.3482 0.0265  0.0395  -0.1177 246 ASN A CG  
1966  O OD1 . ASN A 246 ? 1.0311 1.0345 0.3466 0.0302  0.0361  -0.1152 246 ASN A OD1 
1967  N ND2 . ASN A 246 ? 0.9951 1.0086 0.3580 0.0374  0.0243  -0.1311 246 ASN A ND2 
1968  N N   . PHE A 247 ? 0.8849 1.0369 0.3234 -0.0164 0.1359  -0.0831 247 PHE A N   
1969  C CA  . PHE A 247 ? 0.8442 1.0223 0.3209 -0.0361 0.1503  -0.0724 247 PHE A CA  
1970  C C   . PHE A 247 ? 0.8212 1.0408 0.3239 -0.0358 0.1683  -0.0765 247 PHE A C   
1971  O O   . PHE A 247 ? 0.8428 1.0814 0.3286 -0.0258 0.1846  -0.0803 247 PHE A O   
1972  C CB  . PHE A 247 ? 0.8625 1.0365 0.3198 -0.0484 0.1643  -0.0583 247 PHE A CB  
1973  C CG  . PHE A 247 ? 0.8305 1.0259 0.3209 -0.0693 0.1788  -0.0476 247 PHE A CG  
1974  C CD1 . PHE A 247 ? 0.7945 0.9858 0.3197 -0.0796 0.1681  -0.0454 247 PHE A CD1 
1975  C CD2 . PHE A 247 ? 0.8411 1.0586 0.3260 -0.0793 0.2032  -0.0392 247 PHE A CD2 
1976  C CE1 . PHE A 247 ? 0.7719 0.9775 0.3217 -0.0979 0.1802  -0.0371 247 PHE A CE1 
1977  C CE2 . PHE A 247 ? 0.8169 1.0497 0.3302 -0.0998 0.2139  -0.0300 247 PHE A CE2 
1978  C CZ  . PHE A 247 ? 0.7837 1.0087 0.3273 -0.1086 0.2018  -0.0299 247 PHE A CZ  
1979  N N   . ILE A 248 ? 0.7798 1.0139 0.3236 -0.0460 0.1654  -0.0754 248 ILE A N   
1980  C CA  . ILE A 248 ? 0.7562 1.0304 0.3290 -0.0486 0.1799  -0.0775 248 ILE A CA  
1981  C C   . ILE A 248 ? 0.7388 1.0296 0.3300 -0.0714 0.1942  -0.0652 248 ILE A C   
1982  O O   . ILE A 248 ? 0.7144 0.9961 0.3262 -0.0844 0.1869  -0.0605 248 ILE A O   
1983  C CB  . ILE A 248 ? 0.7276 1.0047 0.3297 -0.0438 0.1655  -0.0852 248 ILE A CB  
1984  C CG1 . ILE A 248 ? 0.7470 0.9948 0.3309 -0.0251 0.1455  -0.0958 248 ILE A CG1 
1985  C CG2 . ILE A 248 ? 0.7124 1.0309 0.3388 -0.0411 0.1782  -0.0890 248 ILE A CG2 
1986  C CD1 . ILE A 248 ? 0.7797 1.0337 0.3378 -0.0037 0.1513  -0.1069 248 ILE A CD1 
1987  N N   . ALA A 249 ? 0.7554 1.0689 0.3380 -0.0763 0.2152  -0.0596 249 ALA A N   
1988  C CA  . ALA A 249 ? 0.7489 1.0725 0.3432 -0.0993 0.2284  -0.0470 249 ALA A CA  
1989  C C   . ALA A 249 ? 0.7160 1.0727 0.3517 -0.1116 0.2326  -0.0475 249 ALA A C   
1990  O O   . ALA A 249 ? 0.7047 1.0896 0.3580 -0.1011 0.2335  -0.0556 249 ALA A O   
1991  C CB  . ALA A 249 ? 0.7824 1.1182 0.3531 -0.1017 0.2496  -0.0391 249 ALA A CB  
1992  N N   . PRO A 250 ? 0.7041 1.0550 0.3535 -0.1330 0.2339  -0.0390 250 PRO A N   
1993  C CA  . PRO A 250 ? 0.6810 1.0614 0.3648 -0.1472 0.2376  -0.0388 250 PRO A CA  
1994  C C   . PRO A 250 ? 0.6927 1.1122 0.3873 -0.1579 0.2576  -0.0327 250 PRO A C   
1995  O O   . PRO A 250 ? 0.7147 1.1267 0.3947 -0.1710 0.2694  -0.0220 250 PRO A O   
1996  C CB  . PRO A 250 ? 0.6738 1.0256 0.3599 -0.1651 0.2317  -0.0323 250 PRO A CB  
1997  C CG  . PRO A 250 ? 0.6990 1.0167 0.3539 -0.1650 0.2328  -0.0247 250 PRO A CG  
1998  C CD  . PRO A 250 ? 0.7132 1.0252 0.3461 -0.1429 0.2283  -0.0306 250 PRO A CD  
1999  N N   . GLU A 251 ? 0.6804 1.1416 0.4015 -0.1523 0.2612  -0.0385 251 GLU A N   
2000  C CA  . GLU A 251 ? 0.6854 1.1915 0.4297 -0.1657 0.2786  -0.0319 251 GLU A CA  
2001  C C   . GLU A 251 ? 0.6684 1.1802 0.4399 -0.1907 0.2728  -0.0282 251 GLU A C   
2002  O O   . GLU A 251 ? 0.6807 1.1948 0.4555 -0.2134 0.2825  -0.0177 251 GLU A O   
2003  C CB  . GLU A 251 ? 0.6810 1.2324 0.4453 -0.1470 0.2842  -0.0396 251 GLU A CB  
2004  C CG  . GLU A 251 ? 0.7092 1.2889 0.4644 -0.1395 0.3075  -0.0346 251 GLU A CG  
2005  C CD  . GLU A 251 ? 0.7062 1.3431 0.5019 -0.1544 0.3233  -0.0271 251 GLU A CD  
2006  O OE1 . GLU A 251 ? 0.6863 1.3592 0.5170 -0.1479 0.3177  -0.0336 251 GLU A OE1 
2007  O OE2 . GLU A 251 ? 0.7259 1.3723 0.5197 -0.1726 0.3406  -0.0140 251 GLU A OE2 
2008  N N   . TYR A 252 ? 0.6441 1.1545 0.4320 -0.1862 0.2563  -0.0368 252 TYR A N   
2009  C CA  . TYR A 252 ? 0.6313 1.1433 0.4402 -0.2065 0.2477  -0.0360 252 TYR A CA  
2010  C C   . TYR A 252 ? 0.6230 1.0877 0.4161 -0.2071 0.2328  -0.0390 252 TYR A C   
2011  O O   . TYR A 252 ? 0.6165 1.0590 0.3957 -0.1886 0.2243  -0.0444 252 TYR A O   
2012  C CB  . TYR A 252 ? 0.6138 1.1685 0.4564 -0.2015 0.2415  -0.0426 252 TYR A CB  
2013  C CG  . TYR A 252 ? 0.6204 1.2294 0.4875 -0.2009 0.2566  -0.0392 252 TYR A CG  
2014  C CD1 . TYR A 252 ? 0.6269 1.2657 0.5193 -0.2260 0.2643  -0.0307 252 TYR A CD1 
2015  C CD2 . TYR A 252 ? 0.6234 1.2539 0.4893 -0.1750 0.2634  -0.0443 252 TYR A CD2 
2016  C CE1 . TYR A 252 ? 0.6332 1.3269 0.5535 -0.2258 0.2799  -0.0260 252 TYR A CE1 
2017  C CE2 . TYR A 252 ? 0.6316 1.3145 0.5212 -0.1721 0.2799  -0.0408 252 TYR A CE2 
2018  C CZ  . TYR A 252 ? 0.6349 1.3519 0.5540 -0.1978 0.2888  -0.0309 252 TYR A CZ  
2019  O OH  . TYR A 252 ? 0.6424 1.4164 0.5903 -0.1953 0.3066  -0.0259 252 TYR A OH  
2020  N N   . ALA A 253 ? 0.6262 1.0757 0.4221 -0.2286 0.2299  -0.0352 253 ALA A N   
2021  C CA  . ALA A 253 ? 0.6209 1.0296 0.4047 -0.2300 0.2180  -0.0379 253 ALA A CA  
2022  C C   . ALA A 253 ? 0.6169 1.0340 0.4173 -0.2459 0.2101  -0.0408 253 ALA A C   
2023  O O   . ALA A 253 ? 0.6287 1.0630 0.4413 -0.2661 0.2147  -0.0366 253 ALA A O   
2024  C CB  . ALA A 253 ? 0.6398 1.0075 0.3990 -0.2385 0.2228  -0.0303 253 ALA A CB  
2025  N N   . TYR A 254 ? 0.6035 1.0079 0.4035 -0.2371 0.1977  -0.0476 254 TYR A N   
2026  C CA  . TYR A 254 ? 0.6032 1.0125 0.4133 -0.2492 0.1879  -0.0516 254 TYR A CA  
2027  C C   . TYR A 254 ? 0.6230 0.9941 0.4159 -0.2678 0.1876  -0.0492 254 TYR A C   
2028  O O   . TYR A 254 ? 0.6287 0.9606 0.4005 -0.2630 0.1898  -0.0472 254 TYR A O   
2029  C CB  . TYR A 254 ? 0.5879 0.9928 0.3980 -0.2324 0.1759  -0.0584 254 TYR A CB  
2030  C CG  . TYR A 254 ? 0.5727 1.0157 0.4019 -0.2156 0.1728  -0.0622 254 TYR A CG  
2031  C CD1 . TYR A 254 ? 0.5698 1.0512 0.4227 -0.2199 0.1664  -0.0649 254 TYR A CD1 
2032  C CD2 . TYR A 254 ? 0.5646 1.0038 0.3881 -0.1947 0.1748  -0.0633 254 TYR A CD2 
2033  C CE1 . TYR A 254 ? 0.5587 1.0743 0.4297 -0.2020 0.1635  -0.0683 254 TYR A CE1 
2034  C CE2 . TYR A 254 ? 0.5559 1.0254 0.3941 -0.1775 0.1717  -0.0677 254 TYR A CE2 
2035  C CZ  . TYR A 254 ? 0.5527 1.0607 0.4149 -0.1802 0.1669  -0.0700 254 TYR A CZ  
2036  O OH  . TYR A 254 ? 0.5464 1.0840 0.4238 -0.1608 0.1640  -0.0743 254 TYR A OH  
2037  N N   . LYS A 255 ? 0.6360 1.0185 0.4389 -0.2885 0.1837  -0.0496 255 LYS A N   
2038  C CA  . LYS A 255 ? 0.6618 1.0069 0.4475 -0.3081 0.1822  -0.0485 255 LYS A CA  
2039  C C   . LYS A 255 ? 0.6663 0.9954 0.4437 -0.3085 0.1683  -0.0570 255 LYS A C   
2040  O O   . LYS A 255 ? 0.6582 1.0186 0.4530 -0.3087 0.1583  -0.0615 255 LYS A O   
2041  C CB  . LYS A 255 ? 0.6799 1.0457 0.4812 -0.3337 0.1860  -0.0429 255 LYS A CB  
2042  C CG  . LYS A 255 ? 0.7110 1.0341 0.4912 -0.3520 0.1911  -0.0373 255 LYS A CG  
2043  C CD  . LYS A 255 ? 0.7261 1.0731 0.5229 -0.3735 0.2005  -0.0273 255 LYS A CD  
2044  C CE  . LYS A 255 ? 0.7387 1.1105 0.5590 -0.3984 0.1905  -0.0290 255 LYS A CE  
2045  N NZ  . LYS A 255 ? 0.7630 1.1436 0.5948 -0.4245 0.1999  -0.0173 255 LYS A NZ  
2046  N N   . ILE A 256 ? 0.6820 0.9625 0.4318 -0.3075 0.1681  -0.0588 256 ILE A N   
2047  C CA  . ILE A 256 ? 0.6904 0.9499 0.4247 -0.3037 0.1576  -0.0665 256 ILE A CA  
2048  C C   . ILE A 256 ? 0.7244 0.9651 0.4475 -0.3272 0.1495  -0.0706 256 ILE A C   
2049  O O   . ILE A 256 ? 0.7514 0.9469 0.4492 -0.3338 0.1527  -0.0711 256 ILE A O   
2050  C CB  . ILE A 256 ? 0.6915 0.9096 0.4019 -0.2867 0.1631  -0.0665 256 ILE A CB  
2051  C CG1 . ILE A 256 ? 0.6686 0.8931 0.3870 -0.2706 0.1725  -0.0600 256 ILE A CG1 
2052  C CG2 . ILE A 256 ? 0.6891 0.9027 0.3908 -0.2749 0.1549  -0.0725 256 ILE A CG2 
2053  C CD1 . ILE A 256 ? 0.6640 0.8592 0.3693 -0.2525 0.1759  -0.0591 256 ILE A CD1 
2054  N N   . VAL A 257 ? 0.7257 1.0004 0.4681 -0.3395 0.1378  -0.0737 257 VAL A N   
2055  C CA  . VAL A 257 ? 0.7609 1.0212 0.4964 -0.3649 0.1268  -0.0776 257 VAL A CA  
2056  C C   . VAL A 257 ? 0.7876 1.0074 0.4891 -0.3623 0.1154  -0.0875 257 VAL A C   
2057  O O   . VAL A 257 ? 0.8256 1.0014 0.5005 -0.3759 0.1129  -0.0912 257 VAL A O   
2058  C CB  . VAL A 257 ? 0.7559 1.0705 0.5290 -0.3818 0.1170  -0.0763 257 VAL A CB  
2059  C CG1 . VAL A 257 ? 0.7406 1.0887 0.5417 -0.3875 0.1318  -0.0657 257 VAL A CG1 
2060  C CG2 . VAL A 257 ? 0.7334 1.0864 0.5238 -0.3666 0.1057  -0.0806 257 VAL A CG2 
2061  N N   . LYS A 258 ? 0.7720 1.0035 0.4714 -0.3441 0.1091  -0.0914 258 LYS A N   
2062  C CA  . LYS A 258 ? 0.7995 0.9947 0.4636 -0.3393 0.0995  -0.0999 258 LYS A CA  
2063  C C   . LYS A 258 ? 0.7858 0.9602 0.4314 -0.3131 0.1099  -0.0988 258 LYS A C   
2064  O O   . LYS A 258 ? 0.7510 0.9547 0.4168 -0.2967 0.1138  -0.0942 258 LYS A O   
2065  C CB  . LYS A 258 ? 0.8051 1.0295 0.4787 -0.3446 0.0787  -0.1053 258 LYS A CB  
2066  C CG  . LYS A 258 ? 0.8499 1.0555 0.5091 -0.3699 0.0616  -0.1127 258 LYS A CG  
2067  C CD  . LYS A 258 ? 0.8769 1.0678 0.5081 -0.3653 0.0431  -0.1216 258 LYS A CD  
2068  C CE  . LYS A 258 ? 0.8519 1.0972 0.5144 -0.3583 0.0292  -0.1200 258 LYS A CE  
2069  N NZ  . LYS A 258 ? 0.8896 1.1228 0.5277 -0.3638 0.0048  -0.1286 258 LYS A NZ  
2070  N N   . LYS A 259 ? 0.8167 0.9398 0.4243 -0.3094 0.1145  -0.1029 259 LYS A N   
2071  C CA  . LYS A 259 ? 0.8114 0.9131 0.4002 -0.2862 0.1246  -0.1014 259 LYS A CA  
2072  C C   . LYS A 259 ? 0.8462 0.9225 0.3994 -0.2835 0.1149  -0.1094 259 LYS A C   
2073  O O   . LYS A 259 ? 0.8903 0.9277 0.4112 -0.2938 0.1111  -0.1169 259 LYS A O   
2074  C CB  . LYS A 259 ? 0.8209 0.8842 0.3948 -0.2802 0.1416  -0.0982 259 LYS A CB  
2075  C CG  . LYS A 259 ? 0.7928 0.8740 0.3947 -0.2816 0.1510  -0.0898 259 LYS A CG  
2076  C CD  . LYS A 259 ? 0.8048 0.8471 0.3917 -0.2733 0.1658  -0.0861 259 LYS A CD  
2077  C CE  . LYS A 259 ? 0.7824 0.8399 0.3926 -0.2751 0.1730  -0.0774 259 LYS A CE  
2078  N NZ  . LYS A 259 ? 0.7975 0.8171 0.3943 -0.2678 0.1849  -0.0731 259 LYS A NZ  
2079  N N   . GLY A 260 ? 1.3589 0.7303 0.4466 -0.2032 0.2353  0.0329  260 GLY A N   
2080  C CA  . GLY A 260 ? 1.3237 0.7087 0.4456 -0.2015 0.2263  0.0289  260 GLY A CA  
2081  C C   . GLY A 260 ? 1.1691 0.6869 0.4330 -0.1424 0.2102  0.0256  260 GLY A C   
2082  O O   . GLY A 260 ? 1.0987 0.6907 0.4246 -0.1017 0.2064  0.0268  260 GLY A O   
2083  N N   . ASP A 261 ? 1.1249 0.6685 0.4320 -0.1425 0.2014  0.0211  261 ASP A N   
2084  C CA  . ASP A 261 ? 0.9874 0.6511 0.4220 -0.0989 0.1872  0.0164  261 ASP A CA  
2085  C C   . ASP A 261 ? 0.8683 0.6704 0.4272 -0.1302 0.1845  0.0026  261 ASP A C   
2086  O O   . ASP A 261 ? 0.8570 0.6955 0.4396 -0.1856 0.1870  -0.0063 261 ASP A O   
2087  C CB  . ASP A 261 ? 0.9820 0.6281 0.4211 -0.0932 0.1794  0.0154  261 ASP A CB  
2088  C CG  . ASP A 261 ? 1.0836 0.6111 0.4136 -0.0385 0.1803  0.0294  261 ASP A CG  
2089  O OD1 . ASP A 261 ? 1.1329 0.6220 0.4067 0.0115  0.1841  0.0403  261 ASP A OD1 
2090  O OD2 . ASP A 261 ? 1.1185 0.5944 0.4152 -0.0411 0.1777  0.0300  261 ASP A OD2 
2091  N N   . SER A 262 ? 0.7894 0.6695 0.4184 -0.0934 0.1805  0.0010  262 SER A N   
2092  C CA  . SER A 262 ? 0.6900 0.6866 0.4235 -0.1103 0.1795  -0.0114 262 SER A CA  
2093  C C   . SER A 262 ? 0.6071 0.6708 0.4114 -0.0634 0.1706  -0.0137 262 SER A C   
2094  O O   . SER A 262 ? 0.6218 0.6587 0.3996 -0.0224 0.1649  -0.0055 262 SER A O   
2095  C CB  . SER A 262 ? 0.7151 0.7182 0.4295 -0.1362 0.1902  -0.0126 262 SER A CB  
2096  O OG  . SER A 262 ? 0.6279 0.7379 0.4339 -0.1420 0.1906  -0.0242 262 SER A OG  
2097  N N   . THR A 263 ? 0.5305 0.6806 0.4150 -0.0703 0.1706  -0.0250 263 THR A N   
2098  C CA  . THR A 263 ? 0.4674 0.6716 0.4046 -0.0393 0.1647  -0.0293 263 THR A CA  
2099  C C   . THR A 263 ? 0.4208 0.6893 0.4119 -0.0514 0.1705  -0.0411 263 THR A C   
2100  O O   . THR A 263 ? 0.4133 0.7081 0.4260 -0.0750 0.1755  -0.0476 263 THR A O   
2101  C CB  . THR A 263 ? 0.4331 0.6469 0.4004 -0.0248 0.1548  -0.0312 263 THR A CB  
2102  O OG1 . THR A 263 ? 0.4017 0.6477 0.3872 0.0026  0.1493  -0.0316 263 THR A OG1 
2103  C CG2 . THR A 263 ? 0.3890 0.6477 0.4126 -0.0424 0.1550  -0.0422 263 THR A CG2 
2104  N N   . ILE A 264 ? 0.3973 0.6947 0.4031 -0.0350 0.1705  -0.0440 264 ILE A N   
2105  C CA  . ILE A 264 ? 0.3658 0.7080 0.4096 -0.0420 0.1770  -0.0561 264 ILE A CA  
2106  C C   . ILE A 264 ? 0.3327 0.6913 0.4087 -0.0317 0.1727  -0.0643 264 ILE A C   
2107  O O   . ILE A 264 ? 0.3240 0.6880 0.3966 -0.0226 0.1681  -0.0650 264 ILE A O   
2108  C CB  . ILE A 264 ? 0.3729 0.7296 0.4023 -0.0394 0.1818  -0.0564 264 ILE A CB  
2109  C CG1 . ILE A 264 ? 0.4155 0.7471 0.4055 -0.0491 0.1874  -0.0480 264 ILE A CG1 
2110  C CG2 . ILE A 264 ? 0.3533 0.7406 0.4092 -0.0463 0.1900  -0.0700 264 ILE A CG2 
2111  C CD1 . ILE A 264 ? 0.4323 0.7717 0.3953 -0.0378 0.1891  -0.0431 264 ILE A CD1 
2112  N N   . MET A 265 ? 0.3210 0.6918 0.4223 -0.0344 0.1746  -0.0701 265 MET A N   
2113  C CA  . MET A 265 ? 0.3039 0.6777 0.4250 -0.0213 0.1721  -0.0772 265 MET A CA  
2114  C C   . MET A 265 ? 0.3120 0.6902 0.4300 -0.0160 0.1819  -0.0883 265 MET A C   
2115  O O   . MET A 265 ? 0.3208 0.7170 0.4390 -0.0182 0.1916  -0.0922 265 MET A O   
2116  C CB  . MET A 265 ? 0.2970 0.6887 0.4391 -0.0204 0.1711  -0.0778 265 MET A CB  
2117  C CG  . MET A 265 ? 0.2852 0.6694 0.4402 -0.0035 0.1655  -0.0809 265 MET A CG  
2118  S SD  . MET A 265 ? 0.2775 0.6977 0.4553 -0.0061 0.1621  -0.0786 265 MET A SD  
2119  C CE  . MET A 265 ? 0.2882 0.6707 0.4437 -0.0286 0.1524  -0.0674 265 MET A CE  
2120  N N   . LYS A 266 ? 0.3189 0.6748 0.4246 -0.0115 0.1805  -0.0937 266 LYS A N   
2121  C CA  . LYS A 266 ? 0.3505 0.6846 0.4298 -0.0106 0.1915  -0.1052 266 LYS A CA  
2122  C C   . LYS A 266 ? 0.3720 0.6809 0.4445 0.0121  0.1957  -0.1111 266 LYS A C   
2123  O O   . LYS A 266 ? 0.3734 0.6591 0.4408 0.0152  0.1893  -0.1107 266 LYS A O   
2124  C CB  . LYS A 266 ? 0.3642 0.6845 0.4143 -0.0306 0.1893  -0.1082 266 LYS A CB  
2125  C CG  . LYS A 266 ? 0.3594 0.7111 0.4040 -0.0463 0.1896  -0.1049 266 LYS A CG  
2126  C CD  . LYS A 266 ? 0.3892 0.7308 0.4119 -0.0534 0.2036  -0.1140 266 LYS A CD  
2127  C CE  . LYS A 266 ? 0.3898 0.7642 0.4001 -0.0725 0.2037  -0.1120 266 LYS A CE  
2128  N NZ  . LYS A 266 ? 0.4163 0.7818 0.4091 -0.0782 0.2174  -0.1198 266 LYS A NZ  
2129  N N   . SER A 267 ? 0.3943 0.7111 0.4625 0.0325  0.2071  -0.1161 267 SER A N   
2130  C CA  . SER A 267 ? 0.4229 0.7254 0.4793 0.0677  0.2123  -0.1198 267 SER A CA  
2131  C C   . SER A 267 ? 0.4700 0.7697 0.4973 0.0970  0.2290  -0.1273 267 SER A C   
2132  O O   . SER A 267 ? 0.4554 0.8037 0.5017 0.0922  0.2338  -0.1270 267 SER A O   
2133  C CB  . SER A 267 ? 0.3814 0.7424 0.4859 0.0766  0.2027  -0.1119 267 SER A CB  
2134  O OG  . SER A 267 ? 0.4074 0.7732 0.5028 0.1170  0.2075  -0.1143 267 SER A OG  
2135  N N   . GLU A 268 ? 0.5367 0.7730 0.5085 0.1299  0.2388  -0.1338 268 GLU A N   
2136  C CA  . GLU A 268 ? 0.6004 0.8219 0.5280 0.1733  0.2565  -0.1403 268 GLU A CA  
2137  C C   . GLU A 268 ? 0.5816 0.8919 0.5471 0.2190  0.2566  -0.1354 268 GLU A C   
2138  O O   . GLU A 268 ? 0.6167 0.9584 0.5646 0.2585  0.2698  -0.1385 268 GLU A O   
2139  C CB  . GLU A 268 ? 0.7056 0.8016 0.5331 0.1946  0.2696  -0.1488 268 GLU A CB  
2140  C CG  . GLU A 268 ? 0.7375 0.7521 0.5160 0.1401  0.2703  -0.1554 268 GLU A CG  
2141  C CD  . GLU A 268 ? 0.7256 0.7622 0.5094 0.1076  0.2751  -0.1593 268 GLU A CD  
2142  O OE1 . GLU A 268 ? 0.7728 0.7968 0.5226 0.1354  0.2904  -0.1647 268 GLU A OE1 
2143  O OE2 . GLU A 268 ? 0.6723 0.7418 0.4909 0.0586  0.2638  -0.1565 268 GLU A OE2 
2144  N N   . LEU A 269 ? 0.5305 0.8893 0.5452 0.2131  0.2422  -0.1278 269 LEU A N   
2145  C CA  . LEU A 269 ? 0.5131 0.9701 0.5631 0.2499  0.2408  -0.1232 269 LEU A CA  
2146  C C   . LEU A 269 ? 0.4696 1.0436 0.5704 0.2323  0.2417  -0.1213 269 LEU A C   
2147  O O   . LEU A 269 ? 0.4379 1.0125 0.5578 0.1840  0.2386  -0.1207 269 LEU A O   
2148  C CB  . LEU A 269 ? 0.4711 0.9463 0.5568 0.2373  0.2248  -0.1164 269 LEU A CB  
2149  C CG  . LEU A 269 ? 0.5237 0.9167 0.5594 0.2746  0.2258  -0.1172 269 LEU A CG  
2150  C CD1 . LEU A 269 ? 0.4771 0.8644 0.5462 0.2443  0.2087  -0.1114 269 LEU A CD1 
2151  C CD2 . LEU A 269 ? 0.5699 1.0091 0.5834 0.3472  0.2353  -0.1166 269 LEU A CD2 
2152  N N   . GLU A 270 ? 0.4744 1.1520 0.5918 0.2718  0.2462  -0.1200 270 GLU A N   
2153  C CA  . GLU A 270 ? 0.4463 1.2503 0.6032 0.2554  0.2497  -0.1196 270 GLU A CA  
2154  C C   . GLU A 270 ? 0.3904 1.2940 0.6037 0.2092  0.2362  -0.1133 270 GLU A C   
2155  O O   . GLU A 270 ? 0.3606 1.2156 0.5875 0.1540  0.2251  -0.1096 270 GLU A O   
2156  C CB  . GLU A 270 ? 0.4958 1.3682 0.6269 0.3260  0.2662  -0.1235 270 GLU A CB  
2157  C CG  . GLU A 270 ? 0.5479 1.4153 0.6421 0.4050  0.2706  -0.1222 270 GLU A CG  
2158  C CD  . GLU A 270 ? 0.6074 1.5477 0.6668 0.4853  0.2883  -0.1248 270 GLU A CD  
2159  O OE1 . GLU A 270 ? 0.5945 1.6165 0.6727 0.4739  0.2958  -0.1276 270 GLU A OE1 
2160  O OE2 . GLU A 270 ? 0.6744 1.5886 0.6810 0.5646  0.2956  -0.1234 270 GLU A OE2 
2161  N N   . TYR A 271 ? 0.3860 1.4272 0.6236 0.2309  0.2379  -0.1120 271 TYR A N   
2162  C CA  . TYR A 271 ? 0.3454 1.4899 0.6257 0.1742  0.2276  -0.1079 271 TYR A CA  
2163  C C   . TYR A 271 ? 0.3464 1.6067 0.6437 0.2148  0.2250  -0.1056 271 TYR A C   
2164  O O   . TYR A 271 ? 0.3688 1.7357 0.6634 0.2722  0.2352  -0.1073 271 TYR A O   
2165  C CB  . TYR A 271 ? 0.3366 1.5757 0.6317 0.1269  0.2340  -0.1099 271 TYR A CB  
2166  C CG  . TYR A 271 ? 0.3151 1.6394 0.6328 0.0503  0.2261  -0.1070 271 TYR A CG  
2167  C CD1 . TYR A 271 ? 0.3084 1.5327 0.6147 -0.0123 0.2159  -0.1030 271 TYR A CD1 
2168  C CD2 . TYR A 271 ? 0.3128 1.8181 0.6524 0.0393  0.2300  -0.1086 271 TYR A CD2 
2169  C CE1 . TYR A 271 ? 0.3118 1.5893 0.6165 -0.0861 0.2111  -0.1010 271 TYR A CE1 
2170  C CE2 . TYR A 271 ? 0.3084 1.8850 0.6540 -0.0435 0.2243  -0.1075 271 TYR A CE2 
2171  C CZ  . TYR A 271 ? 0.3138 1.7637 0.6361 -0.1074 0.2155  -0.1039 271 TYR A CZ  
2172  O OH  . TYR A 271 ? 0.3314 1.8288 0.6385 -0.1929 0.2121  -0.1033 271 TYR A OH  
2173  N N   . GLY A 272 ? 0.3260 1.5704 0.6377 0.1890  0.2117  -0.1013 272 GLY A N   
2174  C CA  . GLY A 272 ? 0.3251 1.6791 0.6535 0.2237  0.2074  -0.0984 272 GLY A CA  
2175  C C   . GLY A 272 ? 0.3038 1.8416 0.6673 0.1740  0.2050  -0.0982 272 GLY A C   
2176  O O   . GLY A 272 ? 0.3032 1.9720 0.6829 0.2068  0.2032  -0.0963 272 GLY A O   
2177  N N   . ASN A 273 ? 0.2945 1.8433 0.6620 0.0929  0.2058  -0.1002 273 ASN A N   
2178  C CA  . ASN A 273 ? 0.2879 1.9874 0.6724 0.0190  0.2040  -0.1011 273 ASN A CA  
2179  C C   . ASN A 273 ? 0.2793 1.9870 0.6697 -0.0187 0.1910  -0.0979 273 ASN A C   
2180  O O   . ASN A 273 ? 0.2763 2.1481 0.6843 -0.0412 0.1890  -0.0986 273 ASN A O   
2181  C CB  . ASN A 273 ? 0.2921 2.2022 0.6970 0.0569  0.2140  -0.1040 273 ASN A CB  
2182  C CG  . ASN A 273 ? 0.2947 2.3491 0.7057 -0.0368 0.2170  -0.1076 273 ASN A CG  
2183  O OD1 . ASN A 273 ? 0.3024 2.4410 0.7148 -0.0388 0.2281  -0.1114 273 ASN A OD1 
2184  N ND2 . ASN A 273 ? 0.2971 2.3740 0.7030 -0.1198 0.2081  -0.1070 273 ASN A ND2 
2185  N N   . CYS A 274 ? 0.2775 1.8134 0.6512 -0.0267 0.1823  -0.0947 274 CYS A N   
2186  C CA  . CYS A 274 ? 0.2733 1.7866 0.6462 -0.0586 0.1702  -0.0915 274 CYS A CA  
2187  C C   . CYS A 274 ? 0.2919 1.6805 0.6279 -0.1434 0.1665  -0.0903 274 CYS A C   
2188  O O   . CYS A 274 ? 0.3052 1.6098 0.6188 -0.1612 0.1722  -0.0907 274 CYS A O   
2189  C CB  . CYS A 274 ? 0.2639 1.6851 0.6407 0.0165  0.1639  -0.0881 274 CYS A CB  
2190  S SG  . CYS A 274 ? 0.2660 1.4710 0.6167 -0.0065 0.1543  -0.0846 274 CYS A SG  
2191  N N   . ASN A 275 ? 0.3015 1.6765 0.6231 -0.1921 0.1578  -0.0885 275 ASN A N   
2192  C CA  . ASN A 275 ? 0.3394 1.5784 0.6072 -0.2632 0.1553  -0.0864 275 ASN A CA  
2193  C C   . ASN A 275 ? 0.3300 1.4420 0.5909 -0.2374 0.1443  -0.0816 275 ASN A C   
2194  O O   . ASN A 275 ? 0.3031 1.4643 0.5952 -0.1999 0.1372  -0.0808 275 ASN A O   
2195  C CB  . ASN A 275 ? 0.3851 1.7046 0.6179 -0.3591 0.1574  -0.0895 275 ASN A CB  
2196  C CG  . ASN A 275 ? 0.4554 1.6165 0.6056 -0.4332 0.1595  -0.0873 275 ASN A CG  
2197  O OD1 . ASN A 275 ? 0.4815 1.5583 0.5989 -0.4429 0.1666  -0.0861 275 ASN A OD1 
2198  N ND2 . ASN A 275 ? 0.4963 1.6103 0.6036 -0.4822 0.1542  -0.0865 275 ASN A ND2 
2199  N N   . THR A 276 ? 0.3554 1.3102 0.5723 -0.2540 0.1433  -0.0778 276 THR A N   
2200  C CA  . THR A 276 ? 0.3492 1.1882 0.5559 -0.2297 0.1336  -0.0731 276 THR A CA  
2201  C C   . THR A 276 ? 0.4096 1.1086 0.5426 -0.2763 0.1342  -0.0687 276 THR A C   
2202  O O   . THR A 276 ? 0.4613 1.1393 0.5457 -0.3267 0.1428  -0.0691 276 THR A O   
2203  C CB  . THR A 276 ? 0.3062 1.0960 0.5457 -0.1530 0.1316  -0.0720 276 THR A CB  
2204  O OG1 . THR A 276 ? 0.2993 1.0005 0.5324 -0.1327 0.1219  -0.0680 276 THR A OG1 
2205  C CG2 . THR A 276 ? 0.3159 1.0393 0.5367 -0.1483 0.1389  -0.0715 276 THR A CG2 
2206  N N   . LYS A 277 ? 0.4124 1.0140 0.5289 -0.2567 0.1261  -0.0641 277 LYS A N   
2207  C CA  . LYS A 277 ? 0.4769 0.9340 0.5156 -0.2783 0.1272  -0.0583 277 LYS A CA  
2208  C C   . LYS A 277 ? 0.4474 0.8217 0.4963 -0.2165 0.1220  -0.0531 277 LYS A C   
2209  O O   . LYS A 277 ? 0.4967 0.7594 0.4843 -0.2149 0.1220  -0.0468 277 LYS A O   
2210  C CB  . LYS A 277 ? 0.5332 0.9495 0.5191 -0.3240 0.1238  -0.0574 277 LYS A CB  
2211  C CG  . LYS A 277 ? 0.6466 0.9624 0.5218 -0.3911 0.1336  -0.0555 277 LYS A CG  
2212  C CD  . LYS A 277 ? 0.7175 0.9802 0.5259 -0.4410 0.1320  -0.0558 277 LYS A CD  
2213  C CE  . LYS A 277 ? 0.7499 0.8686 0.5107 -0.3986 0.1270  -0.0481 277 LYS A CE  
2214  N NZ  . LYS A 277 ? 0.8927 0.8566 0.5115 -0.4489 0.1358  -0.0448 277 LYS A NZ  
2215  N N   . CYS A 278 ? 0.3771 0.8082 0.4939 -0.1660 0.1188  -0.0559 278 CYS A N   
2216  C CA  . CYS A 278 ? 0.3491 0.7251 0.4778 -0.1169 0.1149  -0.0532 278 CYS A CA  
2217  C C   . CYS A 278 ? 0.3033 0.7408 0.4819 -0.0831 0.1188  -0.0587 278 CYS A C   
2218  O O   . CYS A 278 ? 0.2753 0.7799 0.4924 -0.0639 0.1176  -0.0628 278 CYS A O   
2219  C CB  . CYS A 278 ? 0.3312 0.6813 0.4702 -0.0945 0.1045  -0.0512 278 CYS A CB  
2220  S SG  . CYS A 278 ? 0.2977 0.6063 0.4527 -0.0436 0.0998  -0.0496 278 CYS A SG  
2221  N N   . GLN A 279 ? 0.3054 0.7156 0.4744 -0.0731 0.1243  -0.0585 279 GLN A N   
2222  C CA  . GLN A 279 ? 0.2788 0.7329 0.4790 -0.0463 0.1306  -0.0645 279 GLN A CA  
2223  C C   . GLN A 279 ? 0.2665 0.6709 0.4642 -0.0170 0.1292  -0.0649 279 GLN A C   
2224  O O   . GLN A 279 ? 0.2782 0.6310 0.4496 -0.0207 0.1264  -0.0597 279 GLN A O   
2225  C CB  . GLN A 279 ? 0.2961 0.7810 0.4866 -0.0693 0.1407  -0.0662 279 GLN A CB  
2226  C CG  . GLN A 279 ? 0.2791 0.8081 0.4939 -0.0408 0.1491  -0.0728 279 GLN A CG  
2227  C CD  . GLN A 279 ? 0.2664 0.8811 0.5119 -0.0183 0.1515  -0.0776 279 GLN A CD  
2228  O OE1 . GLN A 279 ? 0.2710 0.9622 0.5255 -0.0425 0.1525  -0.0779 279 GLN A OE1 
2229  N NE2 . GLN A 279 ? 0.2612 0.8643 0.5134 0.0280  0.1534  -0.0814 279 GLN A NE2 
2230  N N   . THR A 280 ? 0.2531 0.6747 0.4690 0.0119  0.1322  -0.0710 280 THR A N   
2231  C CA  . THR A 280 ? 0.2548 0.6348 0.4583 0.0284  0.1339  -0.0741 280 THR A CA  
2232  C C   . THR A 280 ? 0.2686 0.6646 0.4684 0.0418  0.1460  -0.0813 280 THR A C   
2233  O O   . THR A 280 ? 0.2710 0.7179 0.4837 0.0509  0.1520  -0.0837 280 THR A O   
2234  C CB  . THR A 280 ? 0.2519 0.6052 0.4544 0.0472  0.1281  -0.0757 280 THR A CB  
2235  O OG1 . THR A 280 ? 0.2661 0.6329 0.4687 0.0745  0.1347  -0.0815 280 THR A OG1 
2236  C CG2 . THR A 280 ? 0.2392 0.5914 0.4511 0.0399  0.1171  -0.0697 280 THR A CG2 
2237  N N   . PRO A 281 ? 0.2825 0.6410 0.4601 0.0427  0.1503  -0.0851 281 PRO A N   
2238  C CA  . PRO A 281 ? 0.3102 0.6636 0.4694 0.0566  0.1632  -0.0932 281 PRO A CA  
2239  C C   . PRO A 281 ? 0.3422 0.6819 0.4850 0.0920  0.1693  -0.0986 281 PRO A C   
2240  O O   . PRO A 281 ? 0.3740 0.7172 0.4978 0.1147  0.1816  -0.1041 281 PRO A O   
2241  C CB  . PRO A 281 ? 0.3239 0.6348 0.4538 0.0410  0.1646  -0.0963 281 PRO A CB  
2242  C CG  . PRO A 281 ? 0.3002 0.6074 0.4373 0.0263  0.1520  -0.0892 281 PRO A CG  
2243  C CD  . PRO A 281 ? 0.2773 0.6074 0.4410 0.0274  0.1441  -0.0814 281 PRO A CD  
2244  N N   . MET A 282 ? 0.3419 0.6619 0.4846 0.1012  0.1616  -0.0965 282 MET A N   
2245  C CA  . MET A 282 ? 0.3824 0.6792 0.4990 0.1404  0.1668  -0.0998 282 MET A CA  
2246  C C   . MET A 282 ? 0.3643 0.7425 0.5153 0.1657  0.1654  -0.0959 282 MET A C   
2247  O O   . MET A 282 ? 0.4029 0.7885 0.5316 0.2115  0.1735  -0.0980 282 MET A O   
2248  C CB  . MET A 282 ? 0.3924 0.6343 0.4909 0.1355  0.1589  -0.0988 282 MET A CB  
2249  C CG  . MET A 282 ? 0.4074 0.5941 0.4747 0.1018  0.1584  -0.1025 282 MET A CG  
2250  S SD  . MET A 282 ? 0.5080 0.5880 0.4819 0.1094  0.1732  -0.1130 282 MET A SD  
2251  C CE  . MET A 282 ? 0.5233 0.5681 0.4838 0.1267  0.1658  -0.1098 282 MET A CE  
2252  N N   . GLY A 283 ? 0.3158 0.7540 0.5114 0.1360  0.1558  -0.0902 283 GLY A N   
2253  C CA  . GLY A 283 ? 0.2984 0.8288 0.5259 0.1434  0.1532  -0.0871 283 GLY A CA  
2254  C C   . GLY A 283 ? 0.2643 0.8172 0.5175 0.0978  0.1416  -0.0814 283 GLY A C   
2255  O O   . GLY A 283 ? 0.2572 0.7547 0.5016 0.0694  0.1368  -0.0789 283 GLY A O   
2256  N N   . ALA A 284 ? 0.2532 0.8871 0.5291 0.0919  0.1380  -0.0792 284 ALA A N   
2257  C CA  . ALA A 284 ? 0.2406 0.8850 0.5236 0.0432  0.1292  -0.0747 284 ALA A CA  
2258  C C   . ALA A 284 ? 0.2323 0.8559 0.5198 0.0497  0.1183  -0.0716 284 ALA A C   
2259  O O   . ALA A 284 ? 0.2342 0.8678 0.5263 0.0918  0.1178  -0.0725 284 ALA A O   
2260  C CB  . ALA A 284 ? 0.2431 0.9951 0.5394 0.0140  0.1329  -0.0756 284 ALA A CB  
2261  N N   . ILE A 285 ? 0.2329 0.8198 0.5095 0.0103  0.1108  -0.0675 285 ILE A N   
2262  C CA  . ILE A 285 ? 0.2266 0.7869 0.5037 0.0111  0.1003  -0.0644 285 ILE A CA  
2263  C C   . ILE A 285 ? 0.2382 0.8444 0.5112 -0.0330 0.0963  -0.0627 285 ILE A C   
2264  O O   . ILE A 285 ? 0.2652 0.8574 0.5103 -0.0786 0.0996  -0.0618 285 ILE A O   
2265  C CB  . ILE A 285 ? 0.2281 0.6885 0.4828 0.0103  0.0951  -0.0611 285 ILE A CB  
2266  C CG1 . ILE A 285 ? 0.2195 0.6452 0.4768 0.0492  0.0954  -0.0637 285 ILE A CG1 
2267  C CG2 . ILE A 285 ? 0.2349 0.6648 0.4768 -0.0085 0.0856  -0.0567 285 ILE A CG2 
2268  C CD1 . ILE A 285 ? 0.2214 0.5803 0.4582 0.0460  0.0937  -0.0622 285 ILE A CD1 
2269  N N   . ASN A 286 ? 0.2275 0.8822 0.5188 -0.0216 0.0900  -0.0624 286 ASN A N   
2270  C CA  . ASN A 286 ? 0.2422 0.9412 0.5255 -0.0673 0.0854  -0.0617 286 ASN A CA  
2271  C C   . ASN A 286 ? 0.2324 0.8993 0.5198 -0.0516 0.0749  -0.0590 286 ASN A C   
2272  O O   . ASN A 286 ? 0.2147 0.9486 0.5296 -0.0195 0.0715  -0.0593 286 ASN A O   
2273  C CB  . ASN A 286 ? 0.2382 1.0845 0.5466 -0.0744 0.0895  -0.0650 286 ASN A CB  
2274  C CG  . ASN A 286 ? 0.2579 1.1672 0.5552 -0.1306 0.0849  -0.0655 286 ASN A CG  
2275  O OD1 . ASN A 286 ? 0.2955 1.1263 0.5474 -0.1849 0.0835  -0.0646 286 ASN A OD1 
2276  N ND2 . ASN A 286 ? 0.2427 1.2935 0.5723 -0.1168 0.0834  -0.0669 286 ASN A ND2 
2277  N N   . SER A 287 ? 0.2489 0.8135 0.5041 -0.0688 0.0704  -0.0559 287 SER A N   
2278  C CA  . SER A 287 ? 0.2426 0.7730 0.4976 -0.0583 0.0607  -0.0534 287 SER A CA  
2279  C C   . SER A 287 ? 0.2834 0.7224 0.4862 -0.0943 0.0582  -0.0502 287 SER A C   
2280  O O   . SER A 287 ? 0.3208 0.7032 0.4810 -0.1178 0.0643  -0.0489 287 SER A O   
2281  C CB  . SER A 287 ? 0.2152 0.7034 0.4880 -0.0049 0.0579  -0.0527 287 SER A CB  
2282  O OG  . SER A 287 ? 0.2225 0.6238 0.4710 -0.0026 0.0584  -0.0506 287 SER A OG  
2283  N N   . SER A 288 ? 0.2845 0.7039 0.4826 -0.0941 0.0500  -0.0486 288 SER A N   
2284  C CA  . SER A 288 ? 0.3324 0.6543 0.4721 -0.1164 0.0480  -0.0452 288 SER A CA  
2285  C C   . SER A 288 ? 0.3119 0.5686 0.4545 -0.0716 0.0423  -0.0414 288 SER A C   
2286  O O   . SER A 288 ? 0.3509 0.5287 0.4449 -0.0744 0.0406  -0.0377 288 SER A O   
2287  C CB  . SER A 288 ? 0.3596 0.7066 0.4818 -0.1564 0.0438  -0.0468 288 SER A CB  
2288  O OG  . SER A 288 ? 0.3081 0.7520 0.4909 -0.1331 0.0370  -0.0485 288 SER A OG  
2289  N N   . MET A 289 ? 0.2607 0.5492 0.4504 -0.0316 0.0407  -0.0426 289 MET A N   
2290  C CA  . MET A 289 ? 0.2426 0.4870 0.4345 0.0019  0.0362  -0.0404 289 MET A CA  
2291  C C   . MET A 289 ? 0.2717 0.4530 0.4210 0.0051  0.0399  -0.0364 289 MET A C   
2292  O O   . MET A 289 ? 0.2919 0.4672 0.4237 -0.0070 0.0473  -0.0363 289 MET A O   
2293  C CB  . MET A 289 ? 0.2066 0.4824 0.4349 0.0319  0.0378  -0.0438 289 MET A CB  
2294  C CG  . MET A 289 ? 0.1892 0.5202 0.4483 0.0465  0.0360  -0.0464 289 MET A CG  
2295  S SD  . MET A 289 ? 0.1828 0.5009 0.4456 0.0564  0.0253  -0.0443 289 MET A SD  
2296  C CE  . MET A 289 ? 0.1765 0.5267 0.4570 0.0964  0.0277  -0.0467 289 MET A CE  
2297  N N   . PRO A 290 ? 0.2771 0.4176 0.4068 0.0254  0.0350  -0.0326 290 PRO A N   
2298  C CA  . PRO A 290 ? 0.3063 0.4031 0.3941 0.0422  0.0386  -0.0275 290 PRO A CA  
2299  C C   . PRO A 290 ? 0.2722 0.4042 0.3863 0.0597  0.0413  -0.0294 290 PRO A C   
2300  O O   . PRO A 290 ? 0.2954 0.4099 0.3785 0.0726  0.0453  -0.0252 290 PRO A O   
2301  C CB  . PRO A 290 ? 0.3201 0.3859 0.3838 0.0635  0.0322  -0.0233 290 PRO A CB  
2302  C CG  . PRO A 290 ? 0.2731 0.3799 0.3867 0.0622  0.0248  -0.0277 290 PRO A CG  
2303  C CD  . PRO A 290 ? 0.2638 0.4014 0.4029 0.0356  0.0264  -0.0321 290 PRO A CD  
2304  N N   . PHE A 291 ? 0.2292 0.4046 0.3891 0.0607  0.0401  -0.0354 291 PHE A N   
2305  C CA  . PHE A 291 ? 0.2091 0.4084 0.3826 0.0688  0.0438  -0.0390 291 PHE A CA  
2306  C C   . PHE A 291 ? 0.1938 0.4168 0.3931 0.0632  0.0495  -0.0454 291 PHE A C   
2307  O O   . PHE A 291 ? 0.1892 0.4267 0.4052 0.0610  0.0484  -0.0470 291 PHE A O   
2308  C CB  . PHE A 291 ? 0.1949 0.4043 0.3734 0.0783  0.0386  -0.0406 291 PHE A CB  
2309  C CG  . PHE A 291 ? 0.2073 0.4142 0.3608 0.0928  0.0340  -0.0345 291 PHE A CG  
2310  C CD1 . PHE A 291 ? 0.2168 0.4444 0.3513 0.1035  0.0370  -0.0318 291 PHE A CD1 
2311  C CD2 . PHE A 291 ? 0.2135 0.4043 0.3595 0.1005  0.0270  -0.0313 291 PHE A CD2 
2312  C CE1 . PHE A 291 ? 0.2337 0.4726 0.3405 0.1279  0.0334  -0.0251 291 PHE A CE1 
2313  C CE2 . PHE A 291 ? 0.2315 0.4236 0.3484 0.1225  0.0239  -0.0253 291 PHE A CE2 
2314  C CZ  . PHE A 291 ? 0.2428 0.4623 0.3393 0.1394  0.0272  -0.0219 291 PHE A CZ  
2315  N N   . HIS A 292 ? 0.1905 0.4217 0.3879 0.0641  0.0558  -0.0489 292 HIS A N   
2316  C CA  . HIS A 292 ? 0.1898 0.4301 0.3969 0.0668  0.0630  -0.0556 292 HIS A CA  
2317  C C   . HIS A 292 ? 0.1985 0.4290 0.3869 0.0633  0.0677  -0.0606 292 HIS A C   
2318  O O   . HIS A 292 ? 0.1956 0.4347 0.3729 0.0574  0.0651  -0.0584 292 HIS A O   
2319  C CB  . HIS A 292 ? 0.1930 0.4541 0.4079 0.0615  0.0700  -0.0561 292 HIS A CB  
2320  C CG  . HIS A 292 ? 0.1991 0.4571 0.4000 0.0536  0.0750  -0.0550 292 HIS A CG  
2321  N ND1 . HIS A 292 ? 0.2042 0.4697 0.4029 0.0537  0.0839  -0.0602 292 HIS A ND1 
2322  C CD2 . HIS A 292 ? 0.2091 0.4536 0.3897 0.0498  0.0731  -0.0488 292 HIS A CD2 
2323  C CE1 . HIS A 292 ? 0.2092 0.4743 0.3945 0.0467  0.0863  -0.0574 292 HIS A CE1 
2324  N NE2 . HIS A 292 ? 0.2147 0.4664 0.3866 0.0473  0.0799  -0.0500 292 HIS A NE2 
2325  N N   . ASN A 293 ? 0.2184 0.4323 0.3947 0.0675  0.0755  -0.0672 293 ASN A N   
2326  C CA  . ASN A 293 ? 0.2454 0.4376 0.3879 0.0540  0.0823  -0.0738 293 ASN A CA  
2327  C C   . ASN A 293 ? 0.2738 0.4502 0.3986 0.0581  0.0949  -0.0797 293 ASN A C   
2328  O O   . ASN A 293 ? 0.3198 0.4534 0.3993 0.0495  0.1036  -0.0871 293 ASN A O   
2329  C CB  . ASN A 293 ? 0.2741 0.4281 0.3862 0.0493  0.0813  -0.0776 293 ASN A CB  
2330  C CG  . ASN A 293 ? 0.3082 0.4217 0.4033 0.0743  0.0866  -0.0797 293 ASN A CG  
2331  O OD1 . ASN A 293 ? 0.2934 0.4322 0.4158 0.0976  0.0870  -0.0767 293 ASN A OD1 
2332  N ND2 . ASN A 293 ? 0.3635 0.4160 0.4049 0.0698  0.0917  -0.0848 293 ASN A ND2 
2333  N N   . ILE A 294 ? 0.2553 0.4622 0.4069 0.0677  0.0969  -0.0770 294 ILE A N   
2334  C CA  . ILE A 294 ? 0.2802 0.4827 0.4196 0.0780  0.1090  -0.0819 294 ILE A CA  
2335  C C   . ILE A 294 ? 0.2904 0.4887 0.4107 0.0573  0.1154  -0.0858 294 ILE A C   
2336  O O   . ILE A 294 ? 0.3367 0.4941 0.4137 0.0532  0.1255  -0.0935 294 ILE A O   
2337  C CB  . ILE A 294 ? 0.2574 0.5106 0.4323 0.0897  0.1092  -0.0781 294 ILE A CB  
2338  C CG1 . ILE A 294 ? 0.2453 0.5215 0.4412 0.1043  0.1020  -0.0742 294 ILE A CG1 
2339  C CG2 . ILE A 294 ? 0.2856 0.5441 0.4467 0.1076  0.1222  -0.0834 294 ILE A CG2 
2340  C CD1 . ILE A 294 ? 0.2809 0.5233 0.4501 0.1332  0.1049  -0.0771 294 ILE A CD1 
2341  N N   . HIS A 295 ? 0.2586 0.4927 0.4009 0.0451  0.1104  -0.0803 295 HIS A N   
2342  C CA  . HIS A 295 ? 0.2644 0.5092 0.3929 0.0293  0.1157  -0.0824 295 HIS A CA  
2343  C C   . HIS A 295 ? 0.2385 0.5159 0.3801 0.0257  0.1077  -0.0734 295 HIS A C   
2344  O O   . HIS A 295 ? 0.2260 0.5076 0.3835 0.0338  0.1036  -0.0665 295 HIS A O   
2345  C CB  . HIS A 295 ? 0.2763 0.5241 0.4061 0.0364  0.1264  -0.0858 295 HIS A CB  
2346  C CG  . HIS A 295 ? 0.2948 0.5411 0.4008 0.0204  0.1345  -0.0908 295 HIS A CG  
2347  N ND1 . HIS A 295 ? 0.2763 0.5555 0.3900 0.0094  0.1317  -0.0857 295 HIS A ND1 
2348  C CD2 . HIS A 295 ? 0.3393 0.5506 0.4056 0.0144  0.1463  -0.1004 295 HIS A CD2 
2349  C CE1 . HIS A 295 ? 0.2982 0.5761 0.3875 -0.0050 0.1401  -0.0920 295 HIS A CE1 
2350  N NE2 . HIS A 295 ? 0.3384 0.5716 0.3969 -0.0053 0.1494  -0.1016 295 HIS A NE2 
2351  N N   . PRO A 296 ? 0.2412 0.5409 0.3659 0.0142  0.1067  -0.0733 296 PRO A N   
2352  C CA  . PRO A 296 ? 0.2299 0.5604 0.3539 0.0242  0.0999  -0.0633 296 PRO A CA  
2353  C C   . PRO A 296 ? 0.2352 0.5596 0.3580 0.0333  0.1031  -0.0566 296 PRO A C   
2354  O O   . PRO A 296 ? 0.2432 0.5536 0.3559 0.0476  0.0986  -0.0473 296 PRO A O   
2355  C CB  . PRO A 296 ? 0.2365 0.6124 0.3410 0.0096  0.1007  -0.0664 296 PRO A CB  
2356  C CG  . PRO A 296 ? 0.2583 0.6126 0.3476 -0.0156 0.1108  -0.0786 296 PRO A CG  
2357  C CD  . PRO A 296 ? 0.2663 0.5658 0.3612 -0.0090 0.1129  -0.0827 296 PRO A CD  
2358  N N   . LEU A 297 ? 0.2418 0.5681 0.3642 0.0233  0.1120  -0.0616 297 LEU A N   
2359  C CA  . LEU A 297 ? 0.2532 0.5734 0.3691 0.0256  0.1165  -0.0563 297 LEU A CA  
2360  C C   . LEU A 297 ? 0.2545 0.5545 0.3840 0.0217  0.1184  -0.0561 297 LEU A C   
2361  O O   . LEU A 297 ? 0.2500 0.5586 0.3963 0.0166  0.1248  -0.0635 297 LEU A O   
2362  C CB  . LEU A 297 ? 0.2594 0.5967 0.3701 0.0145  0.1256  -0.0623 297 LEU A CB  
2363  C CG  . LEU A 297 ? 0.2623 0.6364 0.3565 0.0086  0.1248  -0.0640 297 LEU A CG  
2364  C CD1 . LEU A 297 ? 0.2738 0.6556 0.3595 -0.0093 0.1351  -0.0728 297 LEU A CD1 
2365  C CD2 . LEU A 297 ? 0.2704 0.6691 0.3453 0.0293  0.1192  -0.0516 297 LEU A CD2 
2366  N N   . THR A 298 ? 0.2697 0.5454 0.3836 0.0243  0.1138  -0.0478 298 THR A N   
2367  C CA  . THR A 298 ? 0.2792 0.5456 0.3974 0.0093  0.1156  -0.0477 298 THR A CA  
2368  C C   . THR A 298 ? 0.3255 0.5560 0.3988 -0.0028 0.1197  -0.0401 298 THR A C   
2369  O O   . THR A 298 ? 0.3529 0.5556 0.3876 0.0118  0.1197  -0.0327 298 THR A O   
2370  C CB  . THR A 298 ? 0.2727 0.5288 0.3993 0.0111  0.1076  -0.0465 298 THR A CB  
2371  O OG1 . THR A 298 ? 0.3053 0.5162 0.3903 0.0177  0.1029  -0.0373 298 THR A OG1 
2372  C CG2 . THR A 298 ? 0.2420 0.5151 0.3953 0.0252  0.1033  -0.0521 298 THR A CG2 
2373  N N   . ILE A 299 ? 0.3423 0.5761 0.4133 -0.0298 0.1240  -0.0418 299 ILE A N   
2374  C CA  . ILE A 299 ? 0.4050 0.5917 0.4180 -0.0543 0.1299  -0.0359 299 ILE A CA  
2375  C C   . ILE A 299 ? 0.4319 0.6072 0.4294 -0.0855 0.1284  -0.0363 299 ILE A C   
2376  O O   . ILE A 299 ? 0.3922 0.6317 0.4393 -0.0945 0.1265  -0.0431 299 ILE A O   
2377  C CB  . ILE A 299 ? 0.4091 0.6246 0.4255 -0.0724 0.1399  -0.0394 299 ILE A CB  
2378  C CG1 . ILE A 299 ? 0.4860 0.6468 0.4317 -0.1085 0.1475  -0.0341 299 ILE A CG1 
2379  C CG2 . ILE A 299 ? 0.3621 0.6599 0.4390 -0.0804 0.1426  -0.0496 299 ILE A CG2 
2380  C CD1 . ILE A 299 ? 0.5525 0.6238 0.4204 -0.0891 0.1494  -0.0230 299 ILE A CD1 
2381  N N   . GLY A 300 ? 0.5093 0.5999 0.4287 -0.0996 0.1302  -0.0288 300 GLY A N   
2382  C CA  . GLY A 300 ? 0.5566 0.6217 0.4400 -0.1410 0.1307  -0.0295 300 GLY A CA  
2383  C C   . GLY A 300 ? 0.5698 0.5878 0.4345 -0.1220 0.1224  -0.0256 300 GLY A C   
2384  O O   . GLY A 300 ? 0.5602 0.5507 0.4212 -0.0757 0.1175  -0.0201 300 GLY A O   
2385  N N   . GLU A 301 ? 0.5939 0.6131 0.4459 -0.1602 0.1212  -0.0287 301 GLU A N   
2386  C CA  . GLU A 301 ? 0.6105 0.5861 0.4428 -0.1493 0.1138  -0.0260 301 GLU A CA  
2387  C C   . GLU A 301 ? 0.5105 0.5741 0.4401 -0.1179 0.1031  -0.0307 301 GLU A C   
2388  O O   . GLU A 301 ? 0.4720 0.6119 0.4508 -0.1385 0.1005  -0.0371 301 GLU A O   
2389  C CB  . GLU A 301 ? 0.6818 0.6270 0.4563 -0.2116 0.1176  -0.0287 301 GLU A CB  
2390  C CG  . GLU A 301 ? 0.7137 0.6011 0.4538 -0.2064 0.1114  -0.0262 301 GLU A CG  
2391  C CD  . GLU A 301 ? 0.8181 0.5575 0.4453 -0.1804 0.1162  -0.0164 301 GLU A CD  
2392  O OE1 . GLU A 301 ? 0.8662 0.5487 0.4413 -0.1624 0.1238  -0.0105 301 GLU A OE1 
2393  O OE2 . GLU A 301 ? 0.8584 0.5377 0.4435 -0.1737 0.1128  -0.0141 301 GLU A OE2 
2394  N N   . CYS A 302 ? 0.4772 0.5323 0.4265 -0.0684 0.0977  -0.0273 302 CYS A N   
2395  C CA  . CYS A 302 ? 0.3963 0.5204 0.4235 -0.0415 0.0898  -0.0320 302 CYS A CA  
2396  C C   . CYS A 302 ? 0.3903 0.4855 0.4114 -0.0133 0.0811  -0.0282 302 CYS A C   
2397  O O   . CYS A 302 ? 0.4402 0.4701 0.4023 0.0040  0.0814  -0.0207 302 CYS A O   
2398  C CB  . CYS A 302 ? 0.3570 0.5185 0.4188 -0.0185 0.0925  -0.0343 302 CYS A CB  
2399  S SG  . CYS A 302 ? 0.3509 0.5638 0.4340 -0.0436 0.1025  -0.0403 302 CYS A SG  
2400  N N   . PRO A 303 ? 0.3355 0.4788 0.4117 -0.0045 0.0741  -0.0329 303 PRO A N   
2401  C CA  . PRO A 303 ? 0.3202 0.4507 0.3994 0.0230  0.0661  -0.0303 303 PRO A CA  
2402  C C   . PRO A 303 ? 0.3003 0.4462 0.3855 0.0502  0.0664  -0.0292 303 PRO A C   
2403  O O   . PRO A 303 ? 0.2915 0.4593 0.3871 0.0470  0.0724  -0.0317 303 PRO A O   
2404  C CB  . PRO A 303 ? 0.2744 0.4523 0.4065 0.0215  0.0606  -0.0362 303 PRO A CB  
2405  C CG  . PRO A 303 ? 0.2558 0.4839 0.4197 0.0099  0.0666  -0.0420 303 PRO A CG  
2406  C CD  . PRO A 303 ? 0.2955 0.5070 0.4249 -0.0160 0.0740  -0.0401 303 PRO A CD  
2407  N N   . LYS A 304 ? 0.2949 0.4388 0.3722 0.0740  0.0604  -0.0259 304 LYS A N   
2408  C CA  . LYS A 304 ? 0.2805 0.4583 0.3587 0.0943  0.0604  -0.0248 304 LYS A CA  
2409  C C   . LYS A 304 ? 0.2324 0.4576 0.3561 0.0832  0.0599  -0.0340 304 LYS A C   
2410  O O   . LYS A 304 ? 0.2131 0.4402 0.3605 0.0762  0.0562  -0.0384 304 LYS A O   
2411  C CB  . LYS A 304 ? 0.2999 0.4754 0.3480 0.1246  0.0548  -0.0178 304 LYS A CB  
2412  C CG  . LYS A 304 ? 0.3708 0.4735 0.3504 0.1430  0.0571  -0.0083 304 LYS A CG  
2413  C CD  . LYS A 304 ? 0.4209 0.4947 0.3512 0.1550  0.0654  -0.0021 304 LYS A CD  
2414  C CE  . LYS A 304 ? 0.4935 0.4736 0.3633 0.1351  0.0723  0.0009  304 LYS A CE  
2415  N NZ  . LYS A 304 ? 0.5710 0.4951 0.3622 0.1582  0.0810  0.0100  304 LYS A NZ  
2416  N N   . TYR A 305 ? 0.2236 0.4791 0.3485 0.0813  0.0646  -0.0366 305 TYR A N   
2417  C CA  . TYR A 305 ? 0.2019 0.4827 0.3468 0.0660  0.0669  -0.0460 305 TYR A CA  
2418  C C   . TYR A 305 ? 0.1942 0.5067 0.3336 0.0657  0.0614  -0.0471 305 TYR A C   
2419  O O   . TYR A 305 ? 0.1987 0.5474 0.3218 0.0801  0.0584  -0.0413 305 TYR A O   
2420  C CB  . TYR A 305 ? 0.2059 0.5040 0.3462 0.0567  0.0752  -0.0496 305 TYR A CB  
2421  C CG  . TYR A 305 ? 0.2068 0.5120 0.3464 0.0370  0.0799  -0.0601 305 TYR A CG  
2422  C CD1 . TYR A 305 ? 0.2145 0.4863 0.3598 0.0329  0.0851  -0.0668 305 TYR A CD1 
2423  C CD2 . TYR A 305 ? 0.2124 0.5564 0.3344 0.0225  0.0804  -0.0633 305 TYR A CD2 
2424  C CE1 . TYR A 305 ? 0.2409 0.4924 0.3619 0.0174  0.0920  -0.0763 305 TYR A CE1 
2425  C CE2 . TYR A 305 ? 0.2345 0.5670 0.3359 -0.0054 0.0868  -0.0741 305 TYR A CE2 
2426  C CZ  . TYR A 305 ? 0.2550 0.5283 0.3499 -0.0065 0.0934  -0.0805 305 TYR A CZ  
2427  O OH  . TYR A 305 ? 0.3008 0.5366 0.3528 -0.0313 0.1023  -0.0910 305 TYR A OH  
2428  N N   . VAL A 306 ? 0.1893 0.4906 0.3358 0.0511  0.0609  -0.0542 306 VAL A N   
2429  C CA  . VAL A 306 ? 0.1913 0.5223 0.3249 0.0363  0.0582  -0.0581 306 VAL A CA  
2430  C C   . VAL A 306 ? 0.2152 0.5157 0.3305 0.0086  0.0661  -0.0691 306 VAL A C   
2431  O O   . VAL A 306 ? 0.2262 0.4804 0.3440 0.0141  0.0717  -0.0721 306 VAL A O   
2432  C CB  . VAL A 306 ? 0.1825 0.5107 0.3216 0.0467  0.0491  -0.0543 306 VAL A CB  
2433  C CG1 . VAL A 306 ? 0.1788 0.5276 0.3143 0.0769  0.0434  -0.0437 306 VAL A CG1 
2434  C CG2 . VAL A 306 ? 0.1817 0.4564 0.3350 0.0505  0.0482  -0.0557 306 VAL A CG2 
2435  N N   . LYS A 307 ? 0.2338 0.5604 0.3211 -0.0210 0.0677  -0.0752 307 LYS A N   
2436  C CA  . LYS A 307 ? 0.2835 0.5596 0.3267 -0.0540 0.0776  -0.0865 307 LYS A CA  
2437  C C   . LYS A 307 ? 0.3106 0.5253 0.3327 -0.0566 0.0769  -0.0893 307 LYS A C   
2438  O O   . LYS A 307 ? 0.3732 0.5220 0.3395 -0.0798 0.0867  -0.0980 307 LYS A O   
2439  C CB  . LYS A 307 ? 0.3085 0.6367 0.3155 -0.0984 0.0811  -0.0932 307 LYS A CB  
2440  C CG  . LYS A 307 ? 0.3009 0.6771 0.3117 -0.1026 0.0855  -0.0933 307 LYS A CG  
2441  C CD  . LYS A 307 ? 0.3405 0.7627 0.3035 -0.1585 0.0912  -0.1030 307 LYS A CD  
2442  C CE  . LYS A 307 ? 0.3219 0.8293 0.2962 -0.1592 0.0918  -0.1007 307 LYS A CE  
2443  N NZ  . LYS A 307 ? 0.3606 0.9347 0.2878 -0.2211 0.0966  -0.1106 307 LYS A NZ  
2444  N N   . SER A 308 ? 0.2753 0.5017 0.3310 -0.0325 0.0666  -0.0819 308 SER A N   
2445  C CA  . SER A 308 ? 0.2981 0.4754 0.3352 -0.0335 0.0646  -0.0834 308 SER A CA  
2446  C C   . SER A 308 ? 0.3354 0.4328 0.3525 -0.0138 0.0725  -0.0859 308 SER A C   
2447  O O   . SER A 308 ? 0.3192 0.4182 0.3616 0.0111  0.0752  -0.0835 308 SER A O   
2448  C CB  . SER A 308 ? 0.2513 0.4606 0.3308 -0.0089 0.0519  -0.0746 308 SER A CB  
2449  O OG  . SER A 308 ? 0.2201 0.5045 0.3163 -0.0083 0.0456  -0.0698 308 SER A OG  
2450  N N   . ASN A 309 ? 0.3934 0.4234 0.3575 -0.0235 0.0770  -0.0905 309 ASN A N   
2451  C CA  . ASN A 309 ? 0.4364 0.3935 0.3748 0.0099  0.0831  -0.0903 309 ASN A CA  
2452  C C   . ASN A 309 ? 0.3934 0.3725 0.3781 0.0411  0.0715  -0.0822 309 ASN A C   
2453  O O   . ASN A 309 ? 0.4018 0.3647 0.3933 0.0793  0.0731  -0.0791 309 ASN A O   
2454  C CB  . ASN A 309 ? 0.5421 0.3959 0.3803 -0.0112 0.0953  -0.0982 309 ASN A CB  
2455  C CG  . ASN A 309 ? 0.6072 0.4183 0.3808 -0.0439 0.1099  -0.1077 309 ASN A CG  
2456  O OD1 . ASN A 309 ? 0.6020 0.4172 0.3879 -0.0230 0.1160  -0.1081 309 ASN A OD1 
2457  N ND2 . ASN A 309 ? 0.6746 0.4460 0.3734 -0.1005 0.1161  -0.1161 309 ASN A ND2 
2458  N N   . ARG A 310 ? 0.3504 0.3746 0.3643 0.0260  0.0601  -0.0788 310 ARG A N   
2459  C CA  . ARG A 310 ? 0.3213 0.3558 0.3661 0.0475  0.0497  -0.0724 310 ARG A CA  
2460  C C   . ARG A 310 ? 0.2601 0.3609 0.3506 0.0409  0.0375  -0.0672 310 ARG A C   
2461  O O   . ARG A 310 ? 0.2591 0.3871 0.3366 0.0153  0.0357  -0.0692 310 ARG A O   
2462  C CB  . ARG A 310 ? 0.3837 0.3500 0.3701 0.0403  0.0526  -0.0754 310 ARG A CB  
2463  C CG  . ARG A 310 ? 0.3760 0.3335 0.3802 0.0738  0.0455  -0.0693 310 ARG A CG  
2464  C CD  . ARG A 310 ? 0.4441 0.3284 0.3824 0.0644  0.0484  -0.0716 310 ARG A CD  
2465  N NE  . ARG A 310 ? 0.4080 0.3189 0.3809 0.0760  0.0360  -0.0656 310 ARG A NE  
2466  C CZ  . ARG A 310 ? 0.3990 0.3151 0.3937 0.1158  0.0316  -0.0597 310 ARG A CZ  
2467  N NH1 . ARG A 310 ? 0.4228 0.3291 0.4102 0.1533  0.0384  -0.0583 310 ARG A NH1 
2468  N NH2 . ARG A 310 ? 0.3678 0.3086 0.3906 0.1188  0.0203  -0.0552 310 ARG A NH2 
2469  N N   . LEU A 311 ? 0.2183 0.3460 0.3534 0.0639  0.0302  -0.0606 311 LEU A N   
2470  C CA  . LEU A 311 ? 0.1815 0.3463 0.3421 0.0660  0.0200  -0.0549 311 LEU A CA  
2471  C C   . LEU A 311 ? 0.1682 0.3266 0.3500 0.0827  0.0129  -0.0504 311 LEU A C   
2472  O O   . LEU A 311 ? 0.1581 0.3265 0.3599 0.0920  0.0130  -0.0480 311 LEU A O   
2473  C CB  . LEU A 311 ? 0.1610 0.3584 0.3362 0.0698  0.0204  -0.0513 311 LEU A CB  
2474  C CG  . LEU A 311 ? 0.1663 0.3924 0.3254 0.0560  0.0254  -0.0540 311 LEU A CG  
2475  C CD1 . LEU A 311 ? 0.1550 0.4017 0.3228 0.0695  0.0261  -0.0486 311 LEU A CD1 
2476  C CD2 . LEU A 311 ? 0.1680 0.4300 0.3117 0.0433  0.0213  -0.0548 311 LEU A CD2 
2477  N N   . VAL A 312 ? 0.1712 0.3191 0.3455 0.0814  0.0069  -0.0498 312 VAL A N   
2478  C CA  . VAL A 312 ? 0.1615 0.3066 0.3524 0.0944  -0.0002 -0.0460 312 VAL A CA  
2479  C C   . VAL A 312 ? 0.1464 0.3026 0.3398 0.0913  -0.0089 -0.0427 312 VAL A C   
2480  O O   . VAL A 312 ? 0.1534 0.3109 0.3296 0.0812  -0.0100 -0.0446 312 VAL A O   
2481  C CB  . VAL A 312 ? 0.1931 0.3038 0.3634 0.1044  0.0018  -0.0478 312 VAL A CB  
2482  C CG1 . VAL A 312 ? 0.1816 0.3056 0.3724 0.1200  -0.0059 -0.0433 312 VAL A CG1 
2483  C CG2 . VAL A 312 ? 0.2234 0.3142 0.3756 0.1162  0.0126  -0.0509 312 VAL A CG2 
2484  N N   . LEU A 313 ? 0.1338 0.2971 0.3407 0.0973  -0.0139 -0.0384 313 LEU A N   
2485  C CA  . LEU A 313 ? 0.1312 0.2942 0.3312 0.1006  -0.0210 -0.0349 313 LEU A CA  
2486  C C   . LEU A 313 ? 0.1299 0.2836 0.3375 0.1018  -0.0278 -0.0341 313 LEU A C   
2487  O O   . LEU A 313 ? 0.1297 0.2866 0.3505 0.1020  -0.0285 -0.0337 313 LEU A O   
2488  C CB  . LEU A 313 ? 0.1427 0.2950 0.3298 0.1050  -0.0205 -0.0308 313 LEU A CB  
2489  C CG  . LEU A 313 ? 0.1520 0.3123 0.3198 0.1142  -0.0154 -0.0290 313 LEU A CG  
2490  C CD1 . LEU A 313 ? 0.1854 0.3094 0.3232 0.1182  -0.0122 -0.0247 313 LEU A CD1 
2491  C CD2 . LEU A 313 ? 0.1515 0.3386 0.3055 0.1274  -0.0184 -0.0274 313 LEU A CD2 
2492  N N   . ALA A 314 ? 0.1296 0.2827 0.3286 0.1022  -0.0327 -0.0338 314 ALA A N   
2493  C CA  . ALA A 314 ? 0.1294 0.2735 0.3329 0.1044  -0.0401 -0.0322 314 ALA A CA  
2494  C C   . ALA A 314 ? 0.1348 0.2714 0.3343 0.1053  -0.0435 -0.0289 314 ALA A C   
2495  O O   . ALA A 314 ? 0.1469 0.2746 0.3249 0.1117  -0.0422 -0.0268 314 ALA A O   
2496  C CB  . ALA A 314 ? 0.1314 0.2777 0.3222 0.1015  -0.0438 -0.0329 314 ALA A CB  
2497  N N   . THR A 315 ? 0.1368 0.2757 0.3471 0.0993  -0.0468 -0.0284 315 THR A N   
2498  C CA  . THR A 315 ? 0.1569 0.2798 0.3503 0.0889  -0.0499 -0.0266 315 THR A CA  
2499  C C   . THR A 315 ? 0.1549 0.2783 0.3515 0.0894  -0.0582 -0.0258 315 THR A C   
2500  O O   . THR A 315 ? 0.1750 0.2711 0.3457 0.0883  -0.0609 -0.0245 315 THR A O   
2501  C CB  . THR A 315 ? 0.1671 0.3067 0.3646 0.0692  -0.0469 -0.0276 315 THR A CB  
2502  O OG1 . THR A 315 ? 0.1453 0.3320 0.3765 0.0758  -0.0475 -0.0287 315 THR A OG1 
2503  C CG2 . THR A 315 ? 0.1832 0.3056 0.3624 0.0644  -0.0386 -0.0278 315 THR A CG2 
2504  N N   . GLY A 316 ? 0.1394 0.2877 0.3596 0.0955  -0.0612 -0.0261 316 GLY A N   
2505  C CA  . GLY A 316 ? 0.1389 0.2887 0.3613 0.0987  -0.0689 -0.0248 316 GLY A CA  
2506  C C   . GLY A 316 ? 0.1370 0.2680 0.3493 0.1072  -0.0703 -0.0250 316 GLY A C   
2507  O O   . GLY A 316 ? 0.1362 0.2614 0.3377 0.1081  -0.0663 -0.0260 316 GLY A O   
2508  N N   . LEU A 317 ? 0.1401 0.2696 0.3530 0.1119  -0.0758 -0.0238 317 LEU A N   
2509  C CA  . LEU A 317 ? 0.1454 0.2602 0.3430 0.1115  -0.0776 -0.0244 317 LEU A CA  
2510  C C   . LEU A 317 ? 0.1677 0.2622 0.3499 0.1157  -0.0743 -0.0249 317 LEU A C   
2511  O O   . LEU A 317 ? 0.1797 0.2714 0.3630 0.1290  -0.0713 -0.0239 317 LEU A O   
2512  C CB  . LEU A 317 ? 0.1448 0.2581 0.3397 0.1104  -0.0858 -0.0226 317 LEU A CB  
2513  C CG  . LEU A 317 ? 0.1466 0.2697 0.3525 0.1118  -0.0922 -0.0203 317 LEU A CG  
2514  C CD1 . LEU A 317 ? 0.1585 0.2728 0.3577 0.1228  -0.0945 -0.0184 317 LEU A CD1 
2515  C CD2 . LEU A 317 ? 0.1515 0.2695 0.3491 0.1030  -0.0981 -0.0199 317 LEU A CD2 
2516  N N   . ARG A 318 ? 0.1848 0.2627 0.3423 0.1046  -0.0737 -0.0267 318 ARG A N   
2517  C CA  . ARG A 318 ? 0.2311 0.2650 0.3490 0.1012  -0.0682 -0.0279 318 ARG A CA  
2518  C C   . ARG A 318 ? 0.2563 0.2681 0.3665 0.1250  -0.0715 -0.0233 318 ARG A C   
2519  O O   . ARG A 318 ? 0.2454 0.2688 0.3663 0.1282  -0.0799 -0.0205 318 ARG A O   
2520  C CB  . ARG A 318 ? 0.2490 0.2756 0.3358 0.0745  -0.0676 -0.0310 318 ARG A CB  
2521  C CG  . ARG A 318 ? 0.3184 0.2783 0.3403 0.0592  -0.0594 -0.0335 318 ARG A CG  
2522  C CD  . ARG A 318 ? 0.3382 0.3046 0.3273 0.0210  -0.0590 -0.0375 318 ARG A CD  
2523  N NE  . ARG A 318 ? 0.3221 0.3413 0.3148 -0.0065 -0.0545 -0.0428 318 ARG A NE  
2524  C CZ  . ARG A 318 ? 0.3722 0.3667 0.3130 -0.0421 -0.0439 -0.0490 318 ARG A CZ  
2525  N NH1 . ARG A 318 ? 0.4548 0.3511 0.3232 -0.0538 -0.0349 -0.0508 318 ARG A NH1 
2526  N NH2 . ARG A 318 ? 0.3497 0.4153 0.3016 -0.0651 -0.0414 -0.0533 318 ARG A NH2 
2527  N N   . ASN A 319 ? 0.2962 0.2797 0.3836 0.1459  -0.0645 -0.0222 319 ASN A N   
2528  C CA  . ASN A 319 ? 0.3277 0.3033 0.4032 0.1810  -0.0665 -0.0164 319 ASN A CA  
2529  C C   . ASN A 319 ? 0.4064 0.3010 0.4101 0.1865  -0.0621 -0.0149 319 ASN A C   
2530  O O   . ASN A 319 ? 0.4583 0.2883 0.4059 0.1650  -0.0525 -0.0193 319 ASN A O   
2531  C CB  . ASN A 319 ? 0.3387 0.3304 0.4175 0.2110  -0.0599 -0.0149 319 ASN A CB  
2532  C CG  . ASN A 319 ? 0.3529 0.3794 0.4350 0.2538  -0.0637 -0.0080 319 ASN A CG  
2533  O OD1 . ASN A 319 ? 0.3483 0.3894 0.4359 0.2583  -0.0723 -0.0043 319 ASN A OD1 
2534  N ND2 . ASN A 319 ? 0.3719 0.4215 0.4498 0.2877  -0.0572 -0.0061 319 ASN A ND2 
2535  N N   . SER A 320 ? 0.4267 0.3228 0.4240 0.2124  -0.0683 -0.0088 320 SER A N   
2536  C CA  . SER A 320 ? 0.5040 0.3197 0.4298 0.2151  -0.0657 -0.0065 320 SER A CA  
2537  C C   . SER A 320 ? 0.6098 0.3420 0.4510 0.2604  -0.0540 -0.0017 320 SER A C   
2538  O O   . SER A 320 ? 0.6096 0.3805 0.4662 0.3071  -0.0530 0.0029  320 SER A O   
2539  C CB  . SER A 320 ? 0.4736 0.3304 0.4301 0.2220  -0.0786 -0.0016 320 SER A CB  
2540  O OG  . SER A 320 ? 0.3937 0.3171 0.4161 0.1886  -0.0878 -0.0055 320 SER A OG  
2541  N N   . PRO A 321 ? 0.7132 0.3282 0.4541 0.2467  -0.0439 -0.0031 321 PRO A N   
2542  C CA  . PRO A 321 ? 0.8428 0.3460 0.4734 0.2945  -0.0305 0.0022  321 PRO A CA  
2543  C C   . PRO A 321 ? 0.8855 0.3744 0.4865 0.3433  -0.0358 0.0125  321 PRO A C   
2544  O O   . PRO A 321 ? 0.8247 0.4180 0.4968 0.3838  -0.0466 0.0189  321 PRO A O   
2545  C CB  . PRO A 321 ? 0.9416 0.3170 0.4660 0.2415  -0.0167 -0.0051 321 PRO A CB  
2546  C CG  . PRO A 321 ? 0.8703 0.3010 0.4463 0.1790  -0.0273 -0.0103 321 PRO A CG  
2547  C CD  . PRO A 321 ? 0.7242 0.3032 0.4380 0.1814  -0.0423 -0.0105 321 PRO A CD  
2548  N N   . GLY B 1   ? 0.2760 0.1659 0.2129 -0.1431 -0.0766 -0.0015 1   GLY B N   
2549  C CA  . GLY B 1   ? 0.2216 0.1632 0.2047 -0.1199 -0.0519 -0.0095 1   GLY B CA  
2550  C C   . GLY B 1   ? 0.1977 0.2094 0.1962 -0.1299 -0.0399 -0.0041 1   GLY B C   
2551  O O   . GLY B 1   ? 0.2097 0.2433 0.1958 -0.1522 -0.0461 0.0033  1   GLY B O   
2552  N N   . LEU B 2   ? 0.1692 0.2171 0.1905 -0.1105 -0.0241 -0.0092 2   LEU B N   
2553  C CA  . LEU B 2   ? 0.1538 0.2746 0.1842 -0.1090 -0.0147 -0.0075 2   LEU B CA  
2554  C C   . LEU B 2   ? 0.1452 0.2942 0.1830 -0.1026 -0.0099 -0.0110 2   LEU B C   
2555  O O   . LEU B 2   ? 0.1445 0.3607 0.1798 -0.1119 -0.0090 -0.0073 2   LEU B O   
2556  C CB  . LEU B 2   ? 0.1363 0.2722 0.1812 -0.0782 -0.0012 -0.0153 2   LEU B CB  
2557  C CG  . LEU B 2   ? 0.1407 0.2852 0.1799 -0.0855 -0.0035 -0.0104 2   LEU B CG  
2558  C CD1 . LEU B 2   ? 0.1291 0.2764 0.1783 -0.0515 0.0085  -0.0190 2   LEU B CD1 
2559  C CD2 . LEU B 2   ? 0.1501 0.3642 0.1770 -0.1140 -0.0096 0.0003  2   LEU B CD2 
2560  N N   . PHE B 3   ? 0.1402 0.2461 0.1861 -0.0877 -0.0070 -0.0189 3   PHE B N   
2561  C CA  . PHE B 3   ? 0.1336 0.2590 0.1855 -0.0774 -0.0012 -0.0243 3   PHE B CA  
2562  C C   . PHE B 3   ? 0.1452 0.2596 0.1886 -0.1006 -0.0120 -0.0186 3   PHE B C   
2563  O O   . PHE B 3   ? 0.1407 0.2739 0.1879 -0.0961 -0.0084 -0.0221 3   PHE B O   
2564  C CB  . PHE B 3   ? 0.1276 0.2178 0.1868 -0.0491 0.0090  -0.0364 3   PHE B CB  
2565  C CG  . PHE B 3   ? 0.1291 0.2261 0.1849 -0.0259 0.0171  -0.0412 3   PHE B CG  
2566  C CD1 . PHE B 3   ? 0.1371 0.2714 0.1834 -0.0023 0.0218  -0.0469 3   PHE B CD1 
2567  C CD2 . PHE B 3   ? 0.1281 0.1970 0.1856 -0.0246 0.0179  -0.0408 3   PHE B CD2 
2568  C CE1 . PHE B 3   ? 0.1492 0.2840 0.1837 0.0242  0.0258  -0.0521 3   PHE B CE1 
2569  C CE2 . PHE B 3   ? 0.1347 0.2066 0.1845 -0.0040 0.0236  -0.0442 3   PHE B CE2 
2570  C CZ  . PHE B 3   ? 0.1476 0.2491 0.1839 0.0213  0.0267  -0.0498 3   PHE B CZ  
2571  N N   . GLY B 4   ? 0.1687 0.2462 0.1934 -0.1240 -0.0272 -0.0102 4   GLY B N   
2572  C CA  . GLY B 4   ? 0.1968 0.2584 0.1977 -0.1516 -0.0429 -0.0014 4   GLY B CA  
2573  C C   . GLY B 4   ? 0.2003 0.2201 0.2037 -0.1397 -0.0467 -0.0079 4   GLY B C   
2574  O O   . GLY B 4   ? 0.2281 0.2294 0.2079 -0.1597 -0.0611 -0.0010 4   GLY B O   
2575  N N   . ALA B 5   ? 0.1779 0.1847 0.2051 -0.1106 -0.0353 -0.0205 5   ALA B N   
2576  C CA  . ALA B 5   ? 0.1774 0.1622 0.2105 -0.0997 -0.0368 -0.0280 5   ALA B CA  
2577  C C   . ALA B 5   ? 0.2018 0.1383 0.2201 -0.0908 -0.0513 -0.0317 5   ALA B C   
2578  O O   . ALA B 5   ? 0.2328 0.1388 0.2271 -0.0956 -0.0684 -0.0292 5   ALA B O   
2579  C CB  . ALA B 5   ? 0.1505 0.1511 0.2077 -0.0801 -0.0188 -0.0391 5   ALA B CB  
2580  N N   . ILE B 6   ? 0.1940 0.1237 0.2219 -0.0750 -0.0460 -0.0385 6   ILE B N   
2581  C CA  . ILE B 6   ? 0.2186 0.1135 0.2322 -0.0581 -0.0593 -0.0457 6   ILE B CA  
2582  C C   . ILE B 6   ? 0.2711 0.1159 0.2390 -0.0702 -0.0829 -0.0367 6   ILE B C   
2583  O O   . ILE B 6   ? 0.2773 0.1221 0.2346 -0.0888 -0.0831 -0.0273 6   ILE B O   
2584  C CB  . ILE B 6   ? 0.1977 0.1065 0.2312 -0.0417 -0.0471 -0.0548 6   ILE B CB  
2585  C CG1 . ILE B 6   ? 0.1666 0.1105 0.2289 -0.0358 -0.0294 -0.0634 6   ILE B CG1 
2586  C CG2 . ILE B 6   ? 0.2279 0.1081 0.2418 -0.0208 -0.0627 -0.0634 6   ILE B CG2 
2587  C CD1 . ILE B 6   ? 0.1520 0.1113 0.2279 -0.0285 -0.0171 -0.0703 6   ILE B CD1 
2588  N N   . ALA B 7   ? 0.3177 0.1166 0.2514 -0.0599 -0.1048 -0.0398 7   ALA B N   
2589  C CA  . ALA B 7   ? 0.3911 0.1191 0.2612 -0.0736 -0.1336 -0.0307 7   ALA B CA  
2590  C C   . ALA B 7   ? 0.4043 0.1383 0.2555 -0.1203 -0.1363 -0.0115 7   ALA B C   
2591  O O   . ALA B 7   ? 0.4548 0.1479 0.2585 -0.1470 -0.1533 0.0000  7   ALA B O   
2592  C CB  . ALA B 7   ? 0.4150 0.1110 0.2655 -0.0613 -0.1408 -0.0348 7   ALA B CB  
2593  N N   . GLY B 8   ? 0.3640 0.1533 0.2485 -0.1316 -0.1204 -0.0086 8   GLY B N   
2594  C CA  . GLY B 8   ? 0.3665 0.1906 0.2423 -0.1727 -0.1187 0.0068  8   GLY B CA  
2595  C C   . GLY B 8   ? 0.3805 0.2058 0.2454 -0.1859 -0.1255 0.0112  8   GLY B C   
2596  O O   . GLY B 8   ? 0.4454 0.2045 0.2562 -0.1974 -0.1516 0.0173  8   GLY B O   
2597  N N   . PHE B 9   ? 0.3290 0.2222 0.2378 -0.1825 -0.1042 0.0078  9   PHE B N   
2598  C CA  . PHE B 9   ? 0.3363 0.2359 0.2403 -0.1914 -0.1083 0.0100  9   PHE B CA  
2599  C C   . PHE B 9   ? 0.3305 0.2015 0.2483 -0.1560 -0.1092 -0.0038 9   PHE B C   
2600  O O   . PHE B 9   ? 0.3530 0.2058 0.2542 -0.1592 -0.1203 -0.0025 9   PHE B O   
2601  C CB  . PHE B 9   ? 0.2930 0.2764 0.2295 -0.2011 -0.0881 0.0110  9   PHE B CB  
2602  C CG  . PHE B 9   ? 0.2392 0.2573 0.2240 -0.1659 -0.0642 -0.0043 9   PHE B CG  
2603  C CD1 . PHE B 9   ? 0.2258 0.2407 0.2259 -0.1504 -0.0594 -0.0130 9   PHE B CD1 
2604  C CD2 . PHE B 9   ? 0.2110 0.2608 0.2179 -0.1513 -0.0484 -0.0094 9   PHE B CD2 
2605  C CE1 . PHE B 9   ? 0.1918 0.2272 0.2224 -0.1258 -0.0406 -0.0256 9   PHE B CE1 
2606  C CE2 . PHE B 9   ? 0.1802 0.2444 0.2150 -0.1228 -0.0307 -0.0224 9   PHE B CE2 
2607  C CZ  . PHE B 9   ? 0.1736 0.2276 0.2174 -0.1127 -0.0272 -0.0300 9   PHE B CZ  
2608  N N   . ILE B 10  ? 0.3032 0.1778 0.2497 -0.1248 -0.0977 -0.0170 10  ILE B N   
2609  C CA  . ILE B 10  ? 0.3072 0.1628 0.2594 -0.0929 -0.1023 -0.0307 10  ILE B CA  
2610  C C   . ILE B 10  ? 0.3582 0.1549 0.2716 -0.0772 -0.1238 -0.0334 10  ILE B C   
2611  O O   . ILE B 10  ? 0.3447 0.1461 0.2702 -0.0648 -0.1168 -0.0388 10  ILE B O   
2612  C CB  . ILE B 10  ? 0.2534 0.1563 0.2542 -0.0733 -0.0779 -0.0437 10  ILE B CB  
2613  C CG1 . ILE B 10  ? 0.2193 0.1649 0.2451 -0.0855 -0.0596 -0.0422 10  ILE B CG1 
2614  C CG2 . ILE B 10  ? 0.2577 0.1616 0.2637 -0.0460 -0.0830 -0.0577 10  ILE B CG2 
2615  C CD1 . ILE B 10  ? 0.1849 0.1589 0.2407 -0.0744 -0.0386 -0.0521 10  ILE B CD1 
2616  N N   . GLU B 11  ? 0.4251 0.1603 0.2852 -0.0757 -0.1521 -0.0303 11  GLU B N   
2617  C CA  . GLU B 11  ? 0.4992 0.1561 0.2989 -0.0648 -0.1798 -0.0304 11  GLU B CA  
2618  C C   . GLU B 11  ? 0.4945 0.1543 0.3060 -0.0174 -0.1795 -0.0498 11  GLU B C   
2619  O O   . GLU B 11  ? 0.5343 0.1488 0.3120 -0.0093 -0.1925 -0.0511 11  GLU B O   
2620  C CB  . GLU B 11  ? 0.5882 0.1641 0.3147 -0.0677 -0.2144 -0.0246 11  GLU B CB  
2621  C CG  . GLU B 11  ? 0.6164 0.1776 0.3110 -0.1236 -0.2218 -0.0025 11  GLU B CG  
2622  C CD  . GLU B 11  ? 0.7359 0.1831 0.3286 -0.1364 -0.2644 0.0072  11  GLU B CD  
2623  O OE1 . GLU B 11  ? 0.7737 0.1851 0.3406 -0.1094 -0.2817 0.0000  11  GLU B OE1 
2624  O OE2 . GLU B 11  ? 0.7994 0.1894 0.3316 -0.1742 -0.2825 0.0221  11  GLU B OE2 
2625  N N   . GLY B 12  ? 0.4500 0.1678 0.3059 0.0110  -0.1655 -0.0650 12  GLY B N   
2626  C CA  . GLY B 12  ? 0.4451 0.1873 0.3134 0.0549  -0.1651 -0.0849 12  GLY B CA  
2627  C C   . GLY B 12  ? 0.3759 0.2110 0.3074 0.0641  -0.1388 -0.0968 12  GLY B C   
2628  O O   . GLY B 12  ? 0.3419 0.2101 0.3002 0.0442  -0.1255 -0.0920 12  GLY B O   
2629  N N   . GLY B 13  ? 0.3612 0.2383 0.3107 0.0914  -0.1326 -0.1123 13  GLY B N   
2630  C CA  . GLY B 13  ? 0.3068 0.2745 0.3067 0.0927  -0.1097 -0.1231 13  GLY B CA  
2631  C C   . GLY B 13  ? 0.3196 0.3294 0.3182 0.1212  -0.1198 -0.1377 13  GLY B C   
2632  O O   . GLY B 13  ? 0.3744 0.3360 0.3302 0.1469  -0.1462 -0.1406 13  GLY B O   
2633  N N   . TRP B 14  ? 0.2764 0.3751 0.3153 0.1149  -0.1004 -0.1466 14  TRP B N   
2634  C CA  . TRP B 14  ? 0.2800 0.4429 0.3249 0.1363  -0.1061 -0.1606 14  TRP B CA  
2635  C C   . TRP B 14  ? 0.2746 0.5306 0.3338 0.1647  -0.1036 -0.1814 14  TRP B C   
2636  O O   . TRP B 14  ? 0.2346 0.5583 0.3264 0.1361  -0.0810 -0.1820 14  TRP B O   
2637  C CB  . TRP B 14  ? 0.2397 0.4405 0.3150 0.0955  -0.0864 -0.1527 14  TRP B CB  
2638  C CG  . TRP B 14  ? 0.2451 0.3777 0.3081 0.0732  -0.0895 -0.1362 14  TRP B CG  
2639  C CD1 . TRP B 14  ? 0.2887 0.3457 0.3133 0.0863  -0.1122 -0.1294 14  TRP B CD1 
2640  C CD2 . TRP B 14  ? 0.2135 0.3494 0.2960 0.0326  -0.0711 -0.1249 14  TRP B CD2 
2641  N NE1 . TRP B 14  ? 0.2789 0.3055 0.3043 0.0535  -0.1069 -0.1141 14  TRP B NE1 
2642  C CE2 . TRP B 14  ? 0.2317 0.3067 0.2937 0.0249  -0.0817 -0.1125 14  TRP B CE2 
2643  C CE3 . TRP B 14  ? 0.1818 0.3608 0.2884 0.0015  -0.0488 -0.1244 14  TRP B CE3 
2644  C CZ2 . TRP B 14  ? 0.2118 0.2798 0.2835 -0.0065 -0.0692 -0.1018 14  TRP B CZ2 
2645  C CZ3 . TRP B 14  ? 0.1712 0.3262 0.2795 -0.0275 -0.0389 -0.1139 14  TRP B CZ3 
2646  C CH2 . TRP B 14  ? 0.1823 0.2884 0.2769 -0.0282 -0.0482 -0.1038 14  TRP B CH2 
2647  N N   . GLN B 15  ? 0.3231 0.5824 0.3509 0.2215  -0.1288 -0.1989 15  GLN B N   
2648  C CA  . GLN B 15  ? 0.3233 0.6932 0.3626 0.2585  -0.1295 -0.2230 15  GLN B CA  
2649  C C   . GLN B 15  ? 0.2819 0.7708 0.3606 0.2336  -0.1120 -0.2281 15  GLN B C   
2650  O O   . GLN B 15  ? 0.2572 0.8581 0.3617 0.2269  -0.0982 -0.2395 15  GLN B O   
2651  C CB  . GLN B 15  ? 0.3961 0.7430 0.3843 0.3336  -0.1648 -0.2433 15  GLN B CB  
2652  C CG  . GLN B 15  ? 0.4572 0.6828 0.3906 0.3610  -0.1877 -0.2412 15  GLN B CG  
2653  C CD  . GLN B 15  ? 0.4658 0.7382 0.3975 0.3951  -0.1881 -0.2592 15  GLN B CD  
2654  O OE1 . GLN B 15  ? 0.4712 0.6782 0.3920 0.3804  -0.1858 -0.2499 15  GLN B OE1 
2655  N NE2 . GLN B 15  ? 0.4689 0.8630 0.4107 0.4416  -0.1915 -0.2859 15  GLN B NE2 
2656  N N   . GLY B 16  ? 0.2787 0.7439 0.3577 0.2155  -0.1133 -0.2187 16  GLY B N   
2657  C CA  . GLY B 16  ? 0.2485 0.8145 0.3568 0.1893  -0.0998 -0.2222 16  GLY B CA  
2658  C C   . GLY B 16  ? 0.2029 0.8003 0.3417 0.1191  -0.0701 -0.2087 16  GLY B C   
2659  O O   . GLY B 16  ? 0.1863 0.8703 0.3420 0.0908  -0.0596 -0.2119 16  GLY B O   
2660  N N   . MET B 17  ? 0.1911 0.7147 0.3298 0.0901  -0.0586 -0.1937 17  MET B N   
2661  C CA  . MET B 17  ? 0.1651 0.7021 0.3181 0.0295  -0.0346 -0.1822 17  MET B CA  
2662  C C   . MET B 17  ? 0.1589 0.7499 0.3185 0.0227  -0.0252 -0.1884 17  MET B C   
2663  O O   . MET B 17  ? 0.1608 0.6929 0.3144 0.0320  -0.0253 -0.1836 17  MET B O   
2664  C CB  . MET B 17  ? 0.1606 0.5850 0.3051 0.0031  -0.0282 -0.1622 17  MET B CB  
2665  C CG  . MET B 17  ? 0.1514 0.5716 0.2957 -0.0529 -0.0087 -0.1516 17  MET B CG  
2666  S SD  . MET B 17  ? 0.1519 0.4559 0.2829 -0.0705 -0.0042 -0.1330 17  MET B SD  
2667  C CE  . MET B 17  ? 0.1513 0.4045 0.2804 -0.0438 -0.0087 -0.1298 17  MET B CE  
2668  N N   . VAL B 18  ? 0.1535 0.8621 0.3237 0.0021  -0.0171 -0.1983 18  VAL B N   
2669  C CA  . VAL B 18  ? 0.1507 0.9371 0.3265 -0.0031 -0.0099 -0.2070 18  VAL B CA  
2670  C C   . VAL B 18  ? 0.1489 0.9426 0.3179 -0.0761 0.0094  -0.1936 18  VAL B C   
2671  O O   . VAL B 18  ? 0.1496 0.9735 0.3172 -0.0885 0.0162  -0.1949 18  VAL B O   
2672  C CB  . VAL B 18  ? 0.1543 1.0926 0.3412 0.0301  -0.0175 -0.2312 18  VAL B CB  
2673  C CG1 . VAL B 18  ? 0.1741 1.0917 0.3528 0.1075  -0.0416 -0.2459 18  VAL B CG1 
2674  C CG2 . VAL B 18  ? 0.1494 1.1896 0.3429 -0.0195 -0.0081 -0.2314 18  VAL B CG2 
2675  N N   . ASP B 19  ? 0.1556 0.9138 0.3127 -0.1238 0.0161  -0.1808 19  ASP B N   
2676  C CA  . ASP B 19  ? 0.1754 0.9291 0.3080 -0.1957 0.0294  -0.1686 19  ASP B CA  
2677  C C   . ASP B 19  ? 0.1889 0.8008 0.2972 -0.2136 0.0342  -0.1509 19  ASP B C   
2678  O O   . ASP B 19  ? 0.2211 0.7927 0.2941 -0.2687 0.0407  -0.1394 19  ASP B O   
2679  C CB  . ASP B 19  ? 0.1910 0.9917 0.3112 -0.2413 0.0314  -0.1668 19  ASP B CB  
2680  C CG  . ASP B 19  ? 0.1863 0.9130 0.3086 -0.2223 0.0252  -0.1623 19  ASP B CG  
2681  O OD1 . ASP B 19  ? 0.1717 0.8192 0.3048 -0.1754 0.0187  -0.1605 19  ASP B OD1 
2682  O OD2 . ASP B 19  ? 0.2006 0.9518 0.3107 -0.2582 0.0263  -0.1601 19  ASP B OD2 
2683  N N   . GLY B 20  ? 0.1726 0.7091 0.2928 -0.1672 0.0289  -0.1491 20  GLY B N   
2684  C CA  . GLY B 20  ? 0.1829 0.6050 0.2835 -0.1762 0.0329  -0.1348 20  GLY B CA  
2685  C C   . GLY B 20  ? 0.1641 0.5306 0.2801 -0.1270 0.0260  -0.1343 20  GLY B C   
2686  O O   . GLY B 20  ? 0.1515 0.5456 0.2853 -0.0856 0.0154  -0.1438 20  GLY B O   
2687  N N   . TRP B 21  ? 0.1711 0.4558 0.2726 -0.1326 0.0301  -0.1233 21  TRP B N   
2688  C CA  . TRP B 21  ? 0.1581 0.3900 0.2685 -0.0965 0.0241  -0.1202 21  TRP B CA  
2689  C C   . TRP B 21  ? 0.1547 0.3331 0.2643 -0.0849 0.0184  -0.1137 21  TRP B C   
2690  O O   . TRP B 21  ? 0.1483 0.3102 0.2652 -0.0556 0.0077  -0.1143 21  TRP B O   
2691  C CB  . TRP B 21  ? 0.1665 0.3495 0.2628 -0.1063 0.0308  -0.1120 21  TRP B CB  
2692  C CG  . TRP B 21  ? 0.1608 0.3808 0.2659 -0.0947 0.0311  -0.1182 21  TRP B CG  
2693  C CD1 . TRP B 21  ? 0.1503 0.4139 0.2725 -0.0597 0.0220  -0.1298 21  TRP B CD1 
2694  C CD2 . TRP B 21  ? 0.1731 0.3827 0.2638 -0.1145 0.0388  -0.1139 21  TRP B CD2 
2695  N NE1 . TRP B 21  ? 0.1506 0.4392 0.2738 -0.0565 0.0251  -0.1339 21  TRP B NE1 
2696  C CE2 . TRP B 21  ? 0.1615 0.4198 0.2680 -0.0923 0.0361  -0.1234 21  TRP B CE2 
2697  C CE3 . TRP B 21  ? 0.2014 0.3590 0.2602 -0.1465 0.0455  -0.1037 21  TRP B CE3 
2698  C CZ2 . TRP B 21  ? 0.1688 0.4337 0.2669 -0.1052 0.0422  -0.1218 21  TRP B CZ2 
2699  C CZ3 . TRP B 21  ? 0.2144 0.3708 0.2600 -0.1595 0.0499  -0.1014 21  TRP B CZ3 
2700  C CH2 . TRP B 21  ? 0.1939 0.4079 0.2627 -0.1409 0.0494  -0.1099 21  TRP B CH2 
2701  N N   . TYR B 22  ? 0.1671 0.3150 0.2605 -0.1097 0.0239  -0.1074 22  TYR B N   
2702  C CA  . TYR B 22  ? 0.1651 0.2733 0.2567 -0.1018 0.0199  -0.1020 22  TYR B CA  
2703  C C   . TYR B 22  ? 0.1750 0.3045 0.2606 -0.1214 0.0207  -0.1047 22  TYR B C   
2704  O O   . TYR B 22  ? 0.1940 0.3421 0.2634 -0.1518 0.0264  -0.1064 22  TYR B O   
2705  C CB  . TYR B 22  ? 0.1770 0.2225 0.2489 -0.1050 0.0248  -0.0933 22  TYR B CB  
2706  C CG  . TYR B 22  ? 0.1785 0.2067 0.2457 -0.1004 0.0283  -0.0907 22  TYR B CG  
2707  C CD1 . TYR B 22  ? 0.1598 0.1911 0.2438 -0.0783 0.0232  -0.0897 22  TYR B CD1 
2708  C CD2 . TYR B 22  ? 0.2074 0.2085 0.2454 -0.1203 0.0346  -0.0888 22  TYR B CD2 
2709  C CE1 . TYR B 22  ? 0.1609 0.1789 0.2411 -0.0748 0.0265  -0.0874 22  TYR B CE1 
2710  C CE2 . TYR B 22  ? 0.2109 0.1956 0.2430 -0.1156 0.0371  -0.0862 22  TYR B CE2 
2711  C CZ  . TYR B 22  ? 0.1830 0.1810 0.2403 -0.0922 0.0342  -0.0858 22  TYR B CZ  
2712  O OH  . TYR B 22  ? 0.1864 0.1702 0.2381 -0.0882 0.0368  -0.0833 22  TYR B OH  
2713  N N   . GLY B 23  ? 0.1679 0.2930 0.2616 -0.1088 0.0140  -0.1040 23  GLY B N   
2714  C CA  . GLY B 23  ? 0.1775 0.3198 0.2654 -0.1266 0.0144  -0.1061 23  GLY B CA  
2715  C C   . GLY B 23  ? 0.1702 0.3030 0.2661 -0.1108 0.0061  -0.1042 23  GLY B C   
2716  O O   . GLY B 23  ? 0.1637 0.2648 0.2622 -0.0928 0.0006  -0.0986 23  GLY B O   
2717  N N   . TYR B 24  ? 0.1755 0.3396 0.2720 -0.1220 0.0045  -0.1082 24  TYR B N   
2718  C CA  . TYR B 24  ? 0.1739 0.3291 0.2733 -0.1131 -0.0029 -0.1061 24  TYR B CA  
2719  C C   . TYR B 24  ? 0.1700 0.3783 0.2828 -0.0957 -0.0144 -0.1140 24  TYR B C   
2720  O O   . TYR B 24  ? 0.1688 0.4385 0.2886 -0.0990 -0.0131 -0.1231 24  TYR B O   
2721  C CB  . TYR B 24  ? 0.1903 0.3279 0.2717 -0.1389 0.0035  -0.1043 24  TYR B CB  
2722  C CG  . TYR B 24  ? 0.2148 0.3020 0.2681 -0.1552 0.0125  -0.1010 24  TYR B CG  
2723  C CD1 . TYR B 24  ? 0.2381 0.3282 0.2717 -0.1805 0.0180  -0.1031 24  TYR B CD1 
2724  C CD2 . TYR B 24  ? 0.2229 0.2613 0.2624 -0.1448 0.0135  -0.0965 24  TYR B CD2 
2725  C CE1 . TYR B 24  ? 0.2760 0.3036 0.2699 -0.1933 0.0221  -0.1001 24  TYR B CE1 
2726  C CE2 . TYR B 24  ? 0.2559 0.2435 0.2608 -0.1501 0.0185  -0.0960 24  TYR B CE2 
2727  C CZ  . TYR B 24  ? 0.2865 0.2596 0.2650 -0.1736 0.0216  -0.0975 24  TYR B CZ  
2728  O OH  . TYR B 24  ? 0.3349 0.2418 0.2656 -0.1773 0.0224  -0.0970 24  TYR B OH  
2729  N N   . HIS B 25  ? 0.1742 0.3612 0.2854 -0.0772 -0.0269 -0.1108 25  HIS B N   
2730  C CA  . HIS B 25  ? 0.1829 0.4072 0.2965 -0.0584 -0.0406 -0.1181 25  HIS B CA  
2731  C C   . HIS B 25  ? 0.1877 0.3925 0.2950 -0.0690 -0.0437 -0.1121 25  HIS B C   
2732  O O   . HIS B 25  ? 0.1924 0.3465 0.2895 -0.0705 -0.0473 -0.1020 25  HIS B O   
2733  C CB  . HIS B 25  ? 0.2018 0.4071 0.3048 -0.0201 -0.0601 -0.1209 25  HIS B CB  
2734  C CG  . HIS B 25  ? 0.2231 0.4598 0.3183 0.0086  -0.0782 -0.1307 25  HIS B CG  
2735  N ND1 . HIS B 25  ? 0.2460 0.4418 0.3212 0.0160  -0.0940 -0.1247 25  HIS B ND1 
2736  C CD2 . HIS B 25  ? 0.2276 0.5388 0.3295 0.0335  -0.0840 -0.1468 25  HIS B CD2 
2737  C CE1 . HIS B 25  ? 0.2674 0.5006 0.3344 0.0475  -0.1101 -0.1368 25  HIS B CE1 
2738  N NE2 . HIS B 25  ? 0.2552 0.5646 0.3398 0.0610  -0.1041 -0.1513 25  HIS B NE2 
2739  N N   . HIS B 26  ? 0.1883 0.4416 0.3009 -0.0788 -0.0423 -0.1185 26  HIS B N   
2740  C CA  . HIS B 26  ? 0.1932 0.4349 0.3002 -0.0905 -0.0444 -0.1141 26  HIS B CA  
2741  C C   . HIS B 26  ? 0.2070 0.4755 0.3116 -0.0641 -0.0628 -0.1196 26  HIS B C   
2742  O O   . HIS B 26  ? 0.2124 0.5294 0.3213 -0.0394 -0.0709 -0.1308 26  HIS B O   
2743  C CB  . HIS B 26  ? 0.1922 0.4585 0.2977 -0.1260 -0.0300 -0.1164 26  HIS B CB  
2744  C CG  . HIS B 26  ? 0.1927 0.5407 0.3067 -0.1328 -0.0302 -0.1271 26  HIS B CG  
2745  N ND1 . HIS B 26  ? 0.1922 0.5850 0.3093 -0.1461 -0.0225 -0.1328 26  HIS B ND1 
2746  C CD2 . HIS B 26  ? 0.1952 0.5984 0.3141 -0.1301 -0.0373 -0.1333 26  HIS B CD2 
2747  C CE1 . HIS B 26  ? 0.1931 0.6740 0.3175 -0.1533 -0.0244 -0.1423 26  HIS B CE1 
2748  N NE2 . HIS B 26  ? 0.1943 0.6834 0.3208 -0.1417 -0.0334 -0.1432 26  HIS B NE2 
2749  N N   . SER B 27  ? 0.2180 0.4565 0.3118 -0.0663 -0.0709 -0.1128 27  SER B N   
2750  C CA  . SER B 27  ? 0.2393 0.4964 0.3235 -0.0430 -0.0899 -0.1175 27  SER B CA  
2751  C C   . SER B 27  ? 0.2397 0.4891 0.3205 -0.0649 -0.0881 -0.1112 27  SER B C   
2752  O O   . SER B 27  ? 0.2418 0.4411 0.3126 -0.0800 -0.0864 -0.0997 27  SER B O   
2753  C CB  . SER B 27  ? 0.2762 0.4777 0.3312 -0.0093 -0.1143 -0.1145 27  SER B CB  
2754  O OG  . SER B 27  ? 0.2898 0.4230 0.3247 -0.0269 -0.1188 -0.0987 27  SER B OG  
2755  N N   . ASN B 28  ? 0.2384 0.5474 0.3277 -0.0674 -0.0881 -0.1196 28  ASN B N   
2756  C CA  . ASN B 28  ? 0.2394 0.5489 0.3258 -0.0882 -0.0862 -0.1156 28  ASN B CA  
2757  C C   . ASN B 28  ? 0.2528 0.6209 0.3393 -0.0687 -0.1001 -0.1251 28  ASN B C   
2758  O O   . ASN B 28  ? 0.2668 0.6665 0.3505 -0.0318 -0.1142 -0.1349 28  ASN B O   
2759  C CB  . ASN B 28  ? 0.2233 0.5400 0.3163 -0.1287 -0.0640 -0.1149 28  ASN B CB  
2760  C CG  . ASN B 28  ? 0.2173 0.6011 0.3202 -0.1442 -0.0546 -0.1251 28  ASN B CG  
2761  O OD1 . ASN B 28  ? 0.2175 0.6670 0.3302 -0.1242 -0.0630 -0.1347 28  ASN B OD1 
2762  N ND2 . ASN B 28  ? 0.2203 0.5884 0.3137 -0.1803 -0.0390 -0.1236 28  ASN B ND2 
2763  N N   . GLU B 29  ? 0.2529 0.6376 0.3396 -0.0890 -0.0975 -0.1237 29  GLU B N   
2764  C CA  . GLU B 29  ? 0.2660 0.7115 0.3525 -0.0708 -0.1108 -0.1326 29  GLU B CA  
2765  C C   . GLU B 29  ? 0.2563 0.8042 0.3607 -0.0638 -0.1070 -0.1480 29  GLU B C   
2766  O O   . GLU B 29  ? 0.2724 0.8748 0.3740 -0.0237 -0.1242 -0.1595 29  GLU B O   
2767  C CB  . GLU B 29  ? 0.2641 0.7149 0.3498 -0.1018 -0.1049 -0.1283 29  GLU B CB  
2768  C CG  . GLU B 29  ? 0.2792 0.6537 0.3457 -0.1045 -0.1128 -0.1150 29  GLU B CG  
2769  C CD  . GLU B 29  ? 0.2835 0.6760 0.3469 -0.1224 -0.1134 -0.1137 29  GLU B CD  
2770  O OE1 . GLU B 29  ? 0.2733 0.7281 0.3488 -0.1420 -0.1037 -0.1218 29  GLU B OE1 
2771  O OE2 . GLU B 29  ? 0.3013 0.6464 0.3464 -0.1213 -0.1242 -0.1039 29  GLU B OE2 
2772  N N   . GLN B 30  ? 0.2371 0.8123 0.3536 -0.1026 -0.0863 -0.1488 30  GLN B N   
2773  C CA  . GLN B 30  ? 0.2296 0.9128 0.3600 -0.1109 -0.0805 -0.1615 30  GLN B CA  
2774  C C   . GLN B 30  ? 0.2290 0.9440 0.3660 -0.0698 -0.0878 -0.1711 30  GLN B C   
2775  O O   . GLN B 30  ? 0.2283 1.0529 0.3761 -0.0555 -0.0909 -0.1855 30  GLN B O   
2776  C CB  . GLN B 30  ? 0.2261 0.9091 0.3522 -0.1726 -0.0592 -0.1567 30  GLN B CB  
2777  C CG  . GLN B 30  ? 0.2370 0.9022 0.3491 -0.2133 -0.0536 -0.1513 30  GLN B CG  
2778  C CD  . GLN B 30  ? 0.2492 0.8149 0.3386 -0.2476 -0.0409 -0.1408 30  GLN B CD  
2779  O OE1 . GLN B 30  ? 0.2480 0.7343 0.3325 -0.2318 -0.0428 -0.1333 30  GLN B OE1 
2780  N NE2 . GLN B 30  ? 0.2693 0.8403 0.3378 -0.2950 -0.0298 -0.1407 30  GLN B NE2 
2781  N N   . GLY B 31  ? 0.2312 0.8585 0.3600 -0.0512 -0.0907 -0.1640 31  GLY B N   
2782  C CA  . GLY B 31  ? 0.2372 0.8802 0.3662 -0.0095 -0.0996 -0.1731 31  GLY B CA  
2783  C C   . GLY B 31  ? 0.2317 0.7853 0.3553 -0.0157 -0.0929 -0.1626 31  GLY B C   
2784  O O   . GLY B 31  ? 0.2280 0.7011 0.3446 -0.0408 -0.0862 -0.1483 31  GLY B O   
2785  N N   . SER B 32  ? 0.2319 0.8085 0.3583 0.0094  -0.0953 -0.1708 32  SER B N   
2786  C CA  . SER B 32  ? 0.2255 0.7305 0.3485 0.0034  -0.0884 -0.1622 32  SER B CA  
2787  C C   . SER B 32  ? 0.2102 0.7835 0.3486 -0.0037 -0.0763 -0.1711 32  SER B C   
2788  O O   . SER B 32  ? 0.2091 0.8897 0.3581 0.0064  -0.0777 -0.1858 32  SER B O   
2789  C CB  . SER B 32  ? 0.2579 0.6855 0.3542 0.0490  -0.1112 -0.1605 32  SER B CB  
2790  O OG  . SER B 32  ? 0.2861 0.7632 0.3706 0.1032  -0.1314 -0.1779 32  SER B OG  
2791  N N   . GLY B 33  ? 0.2002 0.7193 0.3384 -0.0222 -0.0647 -0.1625 33  GLY B N   
2792  C CA  . GLY B 33  ? 0.1897 0.7648 0.3383 -0.0325 -0.0537 -0.1690 33  GLY B CA  
2793  C C   . GLY B 33  ? 0.1826 0.6849 0.3272 -0.0514 -0.0422 -0.1581 33  GLY B C   
2794  O O   . GLY B 33  ? 0.1823 0.6001 0.3179 -0.0666 -0.0383 -0.1449 33  GLY B O   
2795  N N   . TYR B 34  ? 0.1782 0.7231 0.3290 -0.0484 -0.0373 -0.1647 34  TYR B N   
2796  C CA  . TYR B 34  ? 0.1733 0.6609 0.3197 -0.0653 -0.0265 -0.1559 34  TYR B CA  
2797  C C   . TYR B 34  ? 0.1756 0.6861 0.3153 -0.1215 -0.0092 -0.1515 34  TYR B C   
2798  O O   . TYR B 34  ? 0.1786 0.7826 0.3215 -0.1425 -0.0057 -0.1595 34  TYR B O   
2799  C CB  . TYR B 34  ? 0.1743 0.6858 0.3250 -0.0282 -0.0333 -0.1654 34  TYR B CB  
2800  C CG  . TYR B 34  ? 0.1926 0.6603 0.3319 0.0269  -0.0552 -0.1697 34  TYR B CG  
2801  C CD1 . TYR B 34  ? 0.2010 0.5640 0.3251 0.0323  -0.0608 -0.1570 34  TYR B CD1 
2802  C CD2 . TYR B 34  ? 0.2111 0.7409 0.3463 0.0731  -0.0728 -0.1868 34  TYR B CD2 
2803  C CE1 . TYR B 34  ? 0.2341 0.5439 0.3330 0.0740  -0.0843 -0.1589 34  TYR B CE1 
2804  C CE2 . TYR B 34  ? 0.2480 0.7168 0.3552 0.1243  -0.0979 -0.1906 34  TYR B CE2 
2805  C CZ  . TYR B 34  ? 0.2626 0.6155 0.3486 0.1204  -0.1040 -0.1755 34  TYR B CZ  
2806  O OH  . TYR B 34  ? 0.3146 0.5947 0.3591 0.1625  -0.1320 -0.1773 34  TYR B OH  
2807  N N   . ALA B 35  ? 0.1831 0.6079 0.3064 -0.1462 -0.0004 -0.1390 35  ALA B N   
2808  C CA  . ALA B 35  ? 0.2054 0.6206 0.3042 -0.1975 0.0115  -0.1336 35  ALA B CA  
2809  C C   . ALA B 35  ? 0.2115 0.5548 0.2985 -0.1959 0.0166  -0.1262 35  ALA B C   
2810  O O   . ALA B 35  ? 0.2094 0.4760 0.2922 -0.1792 0.0155  -0.1192 35  ALA B O   
2811  C CB  . ALA B 35  ? 0.2280 0.5983 0.3017 -0.2295 0.0138  -0.1273 35  ALA B CB  
2812  N N   . ALA B 36  ? 0.2204 0.5977 0.3015 -0.2140 0.0219  -0.1281 36  ALA B N   
2813  C CA  . ALA B 36  ? 0.2285 0.5438 0.2970 -0.2129 0.0263  -0.1216 36  ALA B CA  
2814  C C   . ALA B 36  ? 0.2720 0.4976 0.2943 -0.2465 0.0304  -0.1115 36  ALA B C   
2815  O O   . ALA B 36  ? 0.3100 0.5374 0.2984 -0.2906 0.0316  -0.1098 36  ALA B O   
2816  C CB  . ALA B 36  ? 0.2285 0.6110 0.3009 -0.2244 0.0300  -0.1268 36  ALA B CB  
2817  N N   . ASP B 37  ? 0.2753 0.4223 0.2900 -0.2246 0.0306  -0.1056 37  ASP B N   
2818  C CA  . ASP B 37  ? 0.3263 0.3827 0.2897 -0.2431 0.0316  -0.0988 37  ASP B CA  
2819  C C   . ASP B 37  ? 0.3621 0.4037 0.2940 -0.2700 0.0343  -0.0957 37  ASP B C   
2820  O O   . ASP B 37  ? 0.3403 0.3838 0.2902 -0.2490 0.0364  -0.0950 37  ASP B O   
2821  C CB  . ASP B 37  ? 0.3134 0.3120 0.2827 -0.2041 0.0302  -0.0957 37  ASP B CB  
2822  C CG  . ASP B 37  ? 0.3706 0.2794 0.2827 -0.2098 0.0285  -0.0926 37  ASP B CG  
2823  O OD1 . ASP B 37  ? 0.4011 0.2650 0.2829 -0.2113 0.0286  -0.0898 37  ASP B OD1 
2824  O OD2 . ASP B 37  ? 0.3906 0.2711 0.2829 -0.2097 0.0254  -0.0940 37  ASP B OD2 
2825  N N   . LYS B 38  ? 0.4234 0.4477 0.3029 -0.3207 0.0329  -0.0929 38  LYS B N   
2826  C CA  . LYS B 38  ? 0.4687 0.4829 0.3082 -0.3591 0.0336  -0.0884 38  LYS B CA  
2827  C C   . LYS B 38  ? 0.5105 0.4178 0.3066 -0.3447 0.0305  -0.0825 38  LYS B C   
2828  O O   . LYS B 38  ? 0.5040 0.4194 0.3052 -0.3424 0.0332  -0.0806 38  LYS B O   
2829  C CB  . LYS B 38  ? 0.5385 0.5512 0.3179 -0.4268 0.0297  -0.0848 38  LYS B CB  
2830  C CG  . LYS B 38  ? 0.5041 0.6542 0.3227 -0.4520 0.0338  -0.0910 38  LYS B CG  
2831  C CD  . LYS B 38  ? 0.5802 0.7378 0.3319 -0.5320 0.0298  -0.0853 38  LYS B CD  
2832  C CE  . LYS B 38  ? 0.6252 0.7222 0.3355 -0.5514 0.0230  -0.0834 38  LYS B CE  
2833  N NZ  . LYS B 38  ? 0.7214 0.7961 0.3453 -0.6373 0.0155  -0.0753 38  LYS B NZ  
2834  N N   . GLU B 39  ? 0.5564 0.3679 0.3078 -0.3317 0.0239  -0.0811 39  GLU B N   
2835  C CA  . GLU B 39  ? 0.6088 0.3166 0.3085 -0.3107 0.0180  -0.0780 39  GLU B CA  
2836  C C   . GLU B 39  ? 0.5446 0.2801 0.2988 -0.2641 0.0240  -0.0788 39  GLU B C   
2837  O O   . GLU B 39  ? 0.5663 0.2762 0.2993 -0.2680 0.0235  -0.0751 39  GLU B O   
2838  C CB  . GLU B 39  ? 0.6600 0.2812 0.3127 -0.2878 0.0094  -0.0810 39  GLU B CB  
2839  C CG  . GLU B 39  ? 0.6995 0.2367 0.3142 -0.2429 0.0030  -0.0823 39  GLU B CG  
2840  C CD  . GLU B 39  ? 0.8198 0.2288 0.3262 -0.2463 -0.0132 -0.0842 39  GLU B CD  
2841  O OE1 . GLU B 39  ? 0.8455 0.2352 0.3301 -0.2521 -0.0177 -0.0882 39  GLU B OE1 
2842  O OE2 . GLU B 39  ? 0.8982 0.2187 0.3338 -0.2421 -0.0236 -0.0822 39  GLU B OE2 
2843  N N   . SER B 40  ? 0.4723 0.2565 0.2899 -0.2245 0.0282  -0.0826 40  SER B N   
2844  C CA  . SER B 40  ? 0.4191 0.2272 0.2820 -0.1858 0.0319  -0.0823 40  SER B CA  
2845  C C   . SER B 40  ? 0.3829 0.2538 0.2806 -0.1968 0.0369  -0.0821 40  SER B C   
2846  O O   . SER B 40  ? 0.3713 0.2358 0.2776 -0.1797 0.0385  -0.0801 40  SER B O   
2847  C CB  . SER B 40  ? 0.3631 0.2086 0.2761 -0.1525 0.0327  -0.0846 40  SER B CB  
2848  O OG  . SER B 40  ? 0.3257 0.2366 0.2772 -0.1630 0.0337  -0.0875 40  SER B OG  
2849  N N   . THR B 41  ? 0.3670 0.3045 0.2828 -0.2232 0.0389  -0.0854 41  THR B N   
2850  C CA  . THR B 41  ? 0.3363 0.3482 0.2829 -0.2296 0.0427  -0.0886 41  THR B CA  
2851  C C   . THR B 41  ? 0.3823 0.3691 0.2851 -0.2635 0.0440  -0.0836 41  THR B C   
2852  O O   . THR B 41  ? 0.3627 0.3692 0.2827 -0.2518 0.0468  -0.0839 41  THR B O   
2853  C CB  . THR B 41  ? 0.3140 0.4187 0.2875 -0.2450 0.0433  -0.0960 41  THR B CB  
2854  O OG1 . THR B 41  ? 0.2747 0.3971 0.2855 -0.2106 0.0399  -0.1002 41  THR B OG1 
2855  C CG2 . THR B 41  ? 0.2889 0.4813 0.2905 -0.2444 0.0462  -0.1027 41  THR B CG2 
2856  N N   . GLN B 42  ? 0.4506 0.3883 0.2899 -0.3081 0.0402  -0.0787 42  GLN B N   
2857  C CA  . GLN B 42  ? 0.5128 0.4129 0.2937 -0.3496 0.0380  -0.0718 42  GLN B CA  
2858  C C   . GLN B 42  ? 0.5360 0.3473 0.2904 -0.3199 0.0347  -0.0672 42  GLN B C   
2859  O O   . GLN B 42  ? 0.5545 0.3596 0.2911 -0.3339 0.0352  -0.0632 42  GLN B O   
2860  C CB  . GLN B 42  ? 0.6015 0.4452 0.3020 -0.4074 0.0300  -0.0660 42  GLN B CB  
2861  C CG  . GLN B 42  ? 0.6819 0.4851 0.3088 -0.4638 0.0247  -0.0569 42  GLN B CG  
2862  C CD  . GLN B 42  ? 0.6392 0.5682 0.3086 -0.4893 0.0338  -0.0590 42  GLN B CD  
2863  O OE1 . GLN B 42  ? 0.6396 0.5656 0.3068 -0.4868 0.0357  -0.0561 42  GLN B OE1 
2864  N NE2 . GLN B 42  ? 0.6022 0.6495 0.3107 -0.5103 0.0391  -0.0655 42  GLN B NE2 
2865  N N   . LYS B 43  ? 0.5354 0.2870 0.2871 -0.2784 0.0310  -0.0685 43  LYS B N   
2866  C CA  . LYS B 43  ? 0.5526 0.2362 0.2843 -0.2410 0.0274  -0.0665 43  LYS B CA  
2867  C C   . LYS B 43  ? 0.4778 0.2248 0.2750 -0.2122 0.0353  -0.0677 43  LYS B C   
2868  O O   . LYS B 43  ? 0.4957 0.2089 0.2740 -0.2025 0.0340  -0.0643 43  LYS B O   
2869  C CB  . LYS B 43  ? 0.5611 0.1978 0.2843 -0.2000 0.0227  -0.0702 43  LYS B CB  
2870  C CG  . LYS B 43  ? 0.6519 0.1756 0.2917 -0.1827 0.0106  -0.0694 43  LYS B CG  
2871  C CD  . LYS B 43  ? 0.6816 0.1634 0.2953 -0.1558 0.0038  -0.0756 43  LYS B CD  
2872  C CE  . LYS B 43  ? 0.7737 0.1486 0.3036 -0.1205 -0.0106 -0.0791 43  LYS B CE  
2873  N NZ  . LYS B 43  ? 0.7698 0.1450 0.3035 -0.0738 -0.0135 -0.0885 43  LYS B NZ  
2874  N N   . ALA B 44  ? 0.4021 0.2333 0.2686 -0.1981 0.0411  -0.0728 44  ALA B N   
2875  C CA  . ALA B 44  ? 0.3422 0.2274 0.2622 -0.1730 0.0455  -0.0749 44  ALA B CA  
2876  C C   . ALA B 44  ? 0.3449 0.2719 0.2641 -0.1995 0.0490  -0.0753 44  ALA B C   
2877  O O   . ALA B 44  ? 0.3323 0.2612 0.2614 -0.1861 0.0508  -0.0742 44  ALA B O   
2878  C CB  . ALA B 44  ? 0.2843 0.2306 0.2598 -0.1514 0.0457  -0.0806 44  ALA B CB  
2879  N N   . ILE B 45  ? 0.3619 0.3308 0.2686 -0.2391 0.0502  -0.0772 45  ILE B N   
2880  C CA  . ILE B 45  ? 0.3696 0.3951 0.2714 -0.2712 0.0538  -0.0781 45  ILE B CA  
2881  C C   . ILE B 45  ? 0.4276 0.3780 0.2717 -0.2930 0.0514  -0.0685 45  ILE B C   
2882  O O   . ILE B 45  ? 0.4174 0.3990 0.2712 -0.2951 0.0548  -0.0686 45  ILE B O   
2883  C CB  . ILE B 45  ? 0.3870 0.4804 0.2779 -0.3179 0.0547  -0.0810 45  ILE B CB  
2884  C CG1 . ILE B 45  ? 0.3238 0.5173 0.2784 -0.2880 0.0566  -0.0936 45  ILE B CG1 
2885  C CG2 . ILE B 45  ? 0.4194 0.5596 0.2826 -0.3669 0.0573  -0.0785 45  ILE B CG2 
2886  C CD1 . ILE B 45  ? 0.3360 0.5975 0.2846 -0.3245 0.0565  -0.0975 45  ILE B CD1 
2887  N N   . ASP B 46  ? 0.4946 0.3420 0.2734 -0.3058 0.0437  -0.0612 46  ASP B N   
2888  C CA  . ASP B 46  ? 0.5683 0.3236 0.2761 -0.3218 0.0367  -0.0523 46  ASP B CA  
2889  C C   . ASP B 46  ? 0.5376 0.2698 0.2693 -0.2718 0.0380  -0.0525 46  ASP B C   
2890  O O   . ASP B 46  ? 0.5573 0.2767 0.2699 -0.2811 0.0378  -0.0481 46  ASP B O   
2891  C CB  . ASP B 46  ? 0.6616 0.2990 0.2829 -0.3361 0.0237  -0.0473 46  ASP B CB  
2892  C CG  . ASP B 46  ? 0.7093 0.3567 0.2902 -0.3971 0.0203  -0.0448 46  ASP B CG  
2893  O OD1 . ASP B 46  ? 0.6696 0.4265 0.2900 -0.4300 0.0287  -0.0470 46  ASP B OD1 
2894  O OD2 . ASP B 46  ? 0.7908 0.3399 0.2969 -0.4109 0.0080  -0.0417 46  ASP B OD2 
2895  N N   . GLY B 47  ? 0.4918 0.2236 0.2632 -0.2227 0.0389  -0.0569 47  GLY B N   
2896  C CA  . GLY B 47  ? 0.4624 0.1844 0.2574 -0.1785 0.0398  -0.0568 47  GLY B CA  
2897  C C   . GLY B 47  ? 0.4054 0.2003 0.2531 -0.1742 0.0472  -0.0588 47  GLY B C   
2898  O O   . GLY B 47  ? 0.4110 0.1865 0.2512 -0.1622 0.0470  -0.0556 47  GLY B O   
2899  N N   . VAL B 48  ? 0.3560 0.2335 0.2527 -0.1805 0.0523  -0.0652 48  VAL B N   
2900  C CA  . VAL B 48  ? 0.3096 0.2565 0.2508 -0.1701 0.0568  -0.0705 48  VAL B CA  
2901  C C   . VAL B 48  ? 0.3387 0.3074 0.2548 -0.2065 0.0597  -0.0687 48  VAL B C   
2902  O O   . VAL B 48  ? 0.3233 0.3099 0.2527 -0.1961 0.0619  -0.0694 48  VAL B O   
2903  C CB  . VAL B 48  ? 0.2615 0.2847 0.2519 -0.1567 0.0573  -0.0806 48  VAL B CB  
2904  C CG1 . VAL B 48  ? 0.2326 0.3269 0.2537 -0.1461 0.0591  -0.0893 48  VAL B CG1 
2905  C CG2 . VAL B 48  ? 0.2332 0.2343 0.2476 -0.1216 0.0531  -0.0807 48  VAL B CG2 
2906  N N   . THR B 49  ? 0.3851 0.3535 0.2608 -0.2531 0.0589  -0.0657 49  THR B N   
2907  C CA  . THR B 49  ? 0.4238 0.4153 0.2657 -0.2991 0.0604  -0.0619 49  THR B CA  
2908  C C   . THR B 49  ? 0.4726 0.3756 0.2662 -0.3000 0.0560  -0.0519 49  THR B C   
2909  O O   . THR B 49  ? 0.4644 0.3983 0.2656 -0.3039 0.0595  -0.0517 49  THR B O   
2910  C CB  . THR B 49  ? 0.4803 0.4752 0.2727 -0.3591 0.0576  -0.0577 49  THR B CB  
2911  O OG1 . THR B 49  ? 0.4334 0.5233 0.2735 -0.3555 0.0617  -0.0682 49  THR B OG1 
2912  C CG2 . THR B 49  ? 0.5271 0.5522 0.2777 -0.4166 0.0582  -0.0519 49  THR B CG2 
2913  N N   . ASN B 50  ? 0.5272 0.3219 0.2687 -0.2918 0.0473  -0.0450 50  ASN B N   
2914  C CA  . ASN B 50  ? 0.5833 0.2854 0.2709 -0.2822 0.0398  -0.0371 50  ASN B CA  
2915  C C   . ASN B 50  ? 0.5228 0.2566 0.2646 -0.2366 0.0454  -0.0403 50  ASN B C   
2916  O O   . ASN B 50  ? 0.5448 0.2595 0.2651 -0.2415 0.0443  -0.0356 50  ASN B O   
2917  C CB  . ASN B 50  ? 0.6438 0.2366 0.2745 -0.2605 0.0280  -0.0345 50  ASN B CB  
2918  C CG  . ASN B 50  ? 0.7365 0.2614 0.2842 -0.3102 0.0174  -0.0290 50  ASN B CG  
2919  O OD1 . ASN B 50  ? 0.8061 0.3010 0.2913 -0.3633 0.0116  -0.0207 50  ASN B OD1 
2920  N ND2 . ASN B 50  ? 0.7448 0.2428 0.2855 -0.2973 0.0136  -0.0329 50  ASN B ND2 
2921  N N   . LYS B 51  ? 0.4540 0.2319 0.2598 -0.1961 0.0499  -0.0475 51  LYS B N   
2922  C CA  . LYS B 51  ? 0.3997 0.2087 0.2544 -0.1575 0.0535  -0.0503 51  LYS B CA  
2923  C C   . LYS B 51  ? 0.3731 0.2481 0.2554 -0.1695 0.0594  -0.0537 51  LYS B C   
2924  O O   . LYS B 51  ? 0.3679 0.2357 0.2530 -0.1557 0.0599  -0.0515 51  LYS B O   
2925  C CB  . LYS B 51  ? 0.3419 0.1884 0.2498 -0.1268 0.0549  -0.0565 51  LYS B CB  
2926  C CG  . LYS B 51  ? 0.2907 0.1713 0.2442 -0.0956 0.0561  -0.0591 51  LYS B CG  
2927  C CD  . LYS B 51  ? 0.2540 0.1561 0.2418 -0.0754 0.0538  -0.0627 51  LYS B CD  
2928  C CE  . LYS B 51  ? 0.2350 0.1294 0.2366 -0.0482 0.0508  -0.0593 51  LYS B CE  
2929  N NZ  . LYS B 51  ? 0.2307 0.1171 0.2350 -0.0362 0.0477  -0.0582 51  LYS B NZ  
2930  N N   . VAL B 52  ? 0.3581 0.3044 0.2601 -0.1925 0.0635  -0.0603 52  VAL B N   
2931  C CA  . VAL B 52  ? 0.3348 0.3593 0.2625 -0.1990 0.0686  -0.0671 52  VAL B CA  
2932  C C   . VAL B 52  ? 0.3877 0.3886 0.2669 -0.2364 0.0689  -0.0585 52  VAL B C   
2933  O O   . VAL B 52  ? 0.3746 0.3970 0.2657 -0.2277 0.0714  -0.0598 52  VAL B O   
2934  C CB  . VAL B 52  ? 0.3115 0.4315 0.2669 -0.2111 0.0716  -0.0786 52  VAL B CB  
2935  C CG1 . VAL B 52  ? 0.2991 0.5103 0.2701 -0.2199 0.0761  -0.0875 52  VAL B CG1 
2936  C CG2 . VAL B 52  ? 0.2650 0.4039 0.2653 -0.1682 0.0686  -0.0878 52  VAL B CG2 
2937  N N   . ASN B 53  ? 0.4566 0.4052 0.2741 -0.2797 0.0645  -0.0492 53  ASN B N   
2938  C CA  . ASN B 53  ? 0.5282 0.4338 0.2805 -0.3232 0.0607  -0.0384 53  ASN B CA  
2939  C C   . ASN B 53  ? 0.5568 0.3701 0.2804 -0.2942 0.0547  -0.0309 53  ASN B C   
2940  O O   . ASN B 53  ? 0.5797 0.3863 0.2811 -0.3084 0.0543  -0.0259 53  ASN B O   
2941  C CB  . ASN B 53  ? 0.6123 0.4628 0.2885 -0.3794 0.0527  -0.0291 53  ASN B CB  
2942  C CG  . ASN B 53  ? 0.5901 0.5420 0.2914 -0.4131 0.0584  -0.0361 53  ASN B CG  
2943  O OD1 . ASN B 53  ? 0.5289 0.6023 0.2903 -0.4058 0.0678  -0.0474 53  ASN B OD1 
2944  N ND2 . ASN B 53  ? 0.6452 0.5485 0.2967 -0.4470 0.0514  -0.0306 53  ASN B ND2 
2945  N N   . SER B 54  ? 0.5577 0.3082 0.2809 -0.2530 0.0496  -0.0308 54  SER B N   
2946  C CA  . SER B 54  ? 0.5789 0.2603 0.2815 -0.2156 0.0436  -0.0264 54  SER B CA  
2947  C C   . SER B 54  ? 0.5164 0.2600 0.2777 -0.1896 0.0513  -0.0306 54  SER B C   
2948  O O   . SER B 54  ? 0.5419 0.2528 0.2785 -0.1841 0.0484  -0.0253 54  SER B O   
2949  C CB  . SER B 54  ? 0.5746 0.2124 0.2795 -0.1722 0.0385  -0.0290 54  SER B CB  
2950  O OG  . SER B 54  ? 0.6607 0.2071 0.2873 -0.1873 0.0266  -0.0245 54  SER B OG  
2951  N N   . ILE B 55  ? 0.4448 0.2704 0.2764 -0.1728 0.0590  -0.0403 55  ILE B N   
2952  C CA  . ILE B 55  ? 0.3938 0.2737 0.2746 -0.1492 0.0638  -0.0458 55  ILE B CA  
2953  C C   . ILE B 55  ? 0.4081 0.3283 0.2802 -0.1783 0.0679  -0.0463 55  ILE B C   
2954  O O   . ILE B 55  ? 0.4093 0.3215 0.2792 -0.1691 0.0681  -0.0436 55  ILE B O   
2955  C CB  . ILE B 55  ? 0.3327 0.2757 0.2725 -0.1265 0.0663  -0.0569 55  ILE B CB  
2956  C CG1 . ILE B 55  ? 0.3178 0.2263 0.2691 -0.0963 0.0620  -0.0548 55  ILE B CG1 
2957  C CG2 . ILE B 55  ? 0.2964 0.2914 0.2713 -0.1092 0.0682  -0.0646 55  ILE B CG2 
2958  C CD1 . ILE B 55  ? 0.2752 0.2255 0.2686 -0.0798 0.0609  -0.0632 55  ILE B CD1 
2959  N N   . ILE B 56  ? 0.4214 0.3937 0.2883 -0.2148 0.0712  -0.0499 56  ILE B N   
2960  C CA  . ILE B 56  ? 0.4384 0.4665 0.2941 -0.2491 0.0754  -0.0508 56  ILE B CA  
2961  C C   . ILE B 56  ? 0.5059 0.4567 0.2991 -0.2731 0.0704  -0.0365 56  ILE B C   
2962  O O   . ILE B 56  ? 0.4994 0.4731 0.2981 -0.2718 0.0731  -0.0367 56  ILE B O   
2963  C CB  . ILE B 56  ? 0.4548 0.5507 0.2999 -0.2953 0.0783  -0.0542 56  ILE B CB  
2964  C CG1 . ILE B 56  ? 0.3906 0.5858 0.2997 -0.2651 0.0826  -0.0720 56  ILE B CG1 
2965  C CG2 . ILE B 56  ? 0.4913 0.6352 0.3042 -0.3461 0.0810  -0.0505 56  ILE B CG2 
2966  C CD1 . ILE B 56  ? 0.4009 0.6678 0.3050 -0.3022 0.0846  -0.0765 56  ILE B CD1 
2967  N N   . ASP B 57  ? 0.5790 0.4322 0.3071 -0.2916 0.0612  -0.0251 57  ASP B N   
2968  C CA  . ASP B 57  ? 0.6675 0.4293 0.3153 -0.3167 0.0515  -0.0113 57  ASP B CA  
2969  C C   . ASP B 57  ? 0.6630 0.3773 0.3142 -0.2706 0.0483  -0.0090 57  ASP B C   
2970  O O   . ASP B 57  ? 0.7048 0.3900 0.3172 -0.2861 0.0446  -0.0016 57  ASP B O   
2971  C CB  . ASP B 57  ? 0.7609 0.4149 0.3238 -0.3423 0.0377  -0.0016 57  ASP B CB  
2972  C CG  . ASP B 57  ? 0.8090 0.4922 0.3320 -0.4143 0.0371  0.0026  57  ASP B CG  
2973  O OD1 . ASP B 57  ? 0.8347 0.5590 0.3360 -0.4615 0.0391  0.0075  57  ASP B OD1 
2974  O OD2 . ASP B 57  ? 0.8230 0.4952 0.3353 -0.4266 0.0345  0.0013  57  ASP B OD2 
2975  N N   . LYS B 58  ? 0.6166 0.3292 0.3122 -0.2174 0.0492  -0.0149 58  LYS B N   
2976  C CA  . LYS B 58  ? 0.6055 0.2947 0.3108 -0.1749 0.0470  -0.0136 58  LYS B CA  
2977  C C   . LYS B 58  ? 0.5581 0.3196 0.3100 -0.1731 0.0556  -0.0177 58  LYS B C   
2978  O O   . LYS B 58  ? 0.5730 0.3100 0.3103 -0.1598 0.0528  -0.0131 58  LYS B O   
2979  C CB  . LYS B 58  ? 0.5638 0.2526 0.3057 -0.1262 0.0462  -0.0187 58  LYS B CB  
2980  C CG  . LYS B 58  ? 0.6270 0.2261 0.3097 -0.0984 0.0335  -0.0140 58  LYS B CG  
2981  C CD  . LYS B 58  ? 0.7283 0.2341 0.3195 -0.1303 0.0214  -0.0070 58  LYS B CD  
2982  C CE  . LYS B 58  ? 0.8072 0.2133 0.3262 -0.0916 0.0046  -0.0049 58  LYS B CE  
2983  N NZ  . LYS B 58  ? 0.9309 0.2212 0.3388 -0.1250 -0.0124 0.0031  58  LYS B NZ  
2984  N N   . MET B 59  ? 0.5100 0.3596 0.3127 -0.1837 0.0646  -0.0275 59  MET B N   
2985  C CA  . MET B 59  ? 0.4714 0.3909 0.3131 -0.1783 0.0711  -0.0347 59  MET B CA  
2986  C C   . MET B 59  ? 0.5117 0.4575 0.3200 -0.2245 0.0736  -0.0313 59  MET B C   
2987  O O   . MET B 59  ? 0.4959 0.4811 0.3189 -0.2219 0.0773  -0.0344 59  MET B O   
2988  C CB  . MET B 59  ? 0.4095 0.4075 0.3120 -0.1583 0.0759  -0.0497 59  MET B CB  
2989  C CG  . MET B 59  ? 0.3793 0.3534 0.3091 -0.1218 0.0722  -0.0517 59  MET B CG  
2990  S SD  . MET B 59  ? 0.3676 0.3070 0.3064 -0.0870 0.0682  -0.0467 59  MET B SD  
2991  C CE  . MET B 59  ? 0.3373 0.3357 0.3059 -0.0782 0.0704  -0.0572 59  MET B CE  
2992  N N   . ASN B 60  ? 0.5697 0.4937 0.3284 -0.2704 0.0707  -0.0243 60  ASN B N   
2993  C CA  . ASN B 60  ? 0.6189 0.5734 0.3359 -0.3284 0.0718  -0.0189 60  ASN B CA  
2994  C C   . ASN B 60  ? 0.6571 0.5736 0.3376 -0.3373 0.0685  -0.0096 60  ASN B C   
2995  O O   . ASN B 60  ? 0.6532 0.6425 0.3378 -0.3659 0.0743  -0.0120 60  ASN B O   
2996  C CB  . ASN B 60  ? 0.6949 0.6009 0.3438 -0.3822 0.0645  -0.0086 60  ASN B CB  
2997  C CG  . ASN B 60  ? 0.7893 0.6494 0.3519 -0.4453 0.0567  0.0067  60  ASN B CG  
2998  O OD1 . ASN B 60  ? 0.8538 0.6035 0.3559 -0.4400 0.0451  0.0185  60  ASN B OD1 
2999  N ND2 . ASN B 60  ? 0.8064 0.7522 0.3565 -0.5065 0.0613  0.0067  60  ASN B ND2 
3000  N N   . THR B 61  ? 0.6953 0.5064 0.3390 -0.3112 0.0588  -0.0001 61  THR B N   
3001  C CA  . THR B 61  ? 0.7216 0.5011 0.3399 -0.3075 0.0554  0.0069  61  THR B CA  
3002  C C   . THR B 61  ? 0.6454 0.4564 0.3316 -0.2478 0.0608  -0.0021 61  THR B C   
3003  O O   . THR B 61  ? 0.6317 0.4018 0.3302 -0.2061 0.0567  -0.0028 61  THR B O   
3004  C CB  . THR B 61  ? 0.8277 0.4694 0.3479 -0.3156 0.0378  0.0229  61  THR B CB  
3005  O OG1 . THR B 61  ? 0.8192 0.4041 0.3478 -0.2550 0.0316  0.0210  61  THR B OG1 
3006  C CG2 . THR B 61  ? 0.9176 0.4954 0.3571 -0.3694 0.0272  0.0323  61  THR B CG2 
3007  N N   . GLN B 62  ? 0.6013 0.4892 0.3277 -0.2466 0.0691  -0.0094 62  GLN B N   
3008  C CA  . GLN B 62  ? 0.5385 0.4553 0.3208 -0.1986 0.0725  -0.0177 62  GLN B CA  
3009  C C   . GLN B 62  ? 0.5268 0.4948 0.3186 -0.2075 0.0773  -0.0210 62  GLN B C   
3010  O O   . GLN B 62  ? 0.5569 0.5585 0.3229 -0.2500 0.0801  -0.0192 62  GLN B O   
3011  C CB  . GLN B 62  ? 0.4756 0.4488 0.3190 -0.1720 0.0771  -0.0320 62  GLN B CB  
3012  C CG  . GLN B 62  ? 0.4308 0.4965 0.3201 -0.1630 0.0834  -0.0483 62  GLN B CG  
3013  C CD  . GLN B 62  ? 0.3884 0.4847 0.3217 -0.1319 0.0826  -0.0614 62  GLN B CD  
3014  O OE1 . GLN B 62  ? 0.3901 0.4574 0.3231 -0.1295 0.0804  -0.0584 62  GLN B OE1 
3015  N NE2 . GLN B 62  ? 0.3593 0.5077 0.3236 -0.1068 0.0824  -0.0765 62  GLN B NE2 
3016  N N   . PHE B 63  ? 0.4865 0.4642 0.3118 -0.1710 0.0778  -0.0256 63  PHE B N   
3017  C CA  . PHE B 63  ? 0.4796 0.4934 0.3093 -0.1746 0.0809  -0.0282 63  PHE B CA  
3018  C C   . PHE B 63  ? 0.4610 0.5713 0.3109 -0.1944 0.0887  -0.0419 63  PHE B C   
3019  O O   . PHE B 63  ? 0.4308 0.5945 0.3148 -0.1817 0.0913  -0.0559 63  PHE B O   
3020  C CB  . PHE B 63  ? 0.4389 0.4537 0.3036 -0.1331 0.0792  -0.0331 63  PHE B CB  
3021  C CG  . PHE B 63  ? 0.4387 0.4787 0.3023 -0.1352 0.0811  -0.0346 63  PHE B CG  
3022  C CD1 . PHE B 63  ? 0.4808 0.4748 0.3020 -0.1494 0.0779  -0.0204 63  PHE B CD1 
3023  C CD2 . PHE B 63  ? 0.4047 0.5096 0.3025 -0.1207 0.0842  -0.0510 63  PHE B CD2 
3024  C CE1 . PHE B 63  ? 0.4807 0.4996 0.3006 -0.1529 0.0799  -0.0215 63  PHE B CE1 
3025  C CE2 . PHE B 63  ? 0.4071 0.5355 0.3015 -0.1219 0.0857  -0.0534 63  PHE B CE2 
3026  C CZ  . PHE B 63  ? 0.4410 0.5300 0.2999 -0.1402 0.0846  -0.0380 63  PHE B CZ  
3027  N N   . GLU B 64  ? 0.4841 0.6202 0.3091 -0.2241 0.0913  -0.0385 64  GLU B N   
3028  C CA  . GLU B 64  ? 0.4675 0.7123 0.3103 -0.2401 0.0987  -0.0531 64  GLU B CA  
3029  C C   . GLU B 64  ? 0.4522 0.7240 0.3057 -0.2242 0.1003  -0.0588 64  GLU B C   
3030  O O   . GLU B 64  ? 0.4841 0.7023 0.3046 -0.2383 0.0976  -0.0442 64  GLU B O   
3031  C CB  . GLU B 64  ? 0.5213 0.7891 0.3163 -0.3045 0.1006  -0.0430 64  GLU B CB  
3032  C CG  . GLU B 64  ? 0.5424 0.7930 0.3205 -0.3287 0.0986  -0.0383 64  GLU B CG  
3033  C CD  . GLU B 64  ? 0.6102 0.8755 0.3272 -0.4032 0.0978  -0.0257 64  GLU B CD  
3034  O OE1 . GLU B 64  ? 0.6273 0.9533 0.3284 -0.4360 0.1015  -0.0253 64  GLU B OE1 
3035  O OE2 . GLU B 64  ? 0.6520 0.8669 0.3319 -0.4325 0.0925  -0.0157 64  GLU B OE2 
3036  N N   . ALA B 65  ? 0.4099 0.7604 0.3032 -0.1924 0.1029  -0.0808 65  ALA B N   
3037  C CA  . ALA B 65  ? 0.3979 0.7772 0.2989 -0.1747 0.1035  -0.0892 65  ALA B CA  
3038  C C   . ALA B 65  ? 0.4212 0.8732 0.2989 -0.2182 0.1101  -0.0883 65  ALA B C   
3039  O O   . ALA B 65  ? 0.4335 0.9546 0.3028 -0.2528 0.1149  -0.0909 65  ALA B O   
3040  C CB  . ALA B 65  ? 0.3655 0.7925 0.3020 -0.1232 0.1000  -0.1148 65  ALA B CB  
3041  N N   . VAL B 66  ? 0.4281 0.8685 0.2931 -0.2207 0.1102  -0.0837 66  VAL B N   
3042  C CA  . VAL B 66  ? 0.4500 0.9655 0.2932 -0.2606 0.1161  -0.0839 66  VAL B CA  
3043  C C   . VAL B 66  ? 0.4264 0.9857 0.2903 -0.2252 0.1167  -0.1004 66  VAL B C   
3044  O O   . VAL B 66  ? 0.4125 0.9040 0.2866 -0.1888 0.1110  -0.0996 66  VAL B O   
3045  C CB  . VAL B 66  ? 0.5079 0.9473 0.2922 -0.3150 0.1133  -0.0554 66  VAL B CB  
3046  C CG1 . VAL B 66  ? 0.5405 1.0640 0.2957 -0.3679 0.1187  -0.0539 66  VAL B CG1 
3047  C CG2 . VAL B 66  ? 0.5420 0.9093 0.2940 -0.3428 0.1084  -0.0391 66  VAL B CG2 
3048  N N   . GLY B 67  ? 0.4245 1.1028 0.2912 -0.2378 0.1230  -0.1160 67  GLY B N   
3049  C CA  . GLY B 67  ? 0.4084 1.1399 0.2897 -0.2025 0.1230  -0.1356 67  GLY B CA  
3050  C C   . GLY B 67  ? 0.4290 1.1206 0.2823 -0.2308 0.1239  -0.1182 67  GLY B C   
3051  O O   . GLY B 67  ? 0.4642 1.1723 0.2827 -0.2900 0.1280  -0.1015 67  GLY B O   
3052  N N   . ARG B 68  ? 0.4127 1.0487 0.2751 -0.1914 0.1184  -0.1215 68  ARG B N   
3053  C CA  . ARG B 68  ? 0.4289 1.0248 0.2677 -0.2098 0.1181  -0.1066 68  ARG B CA  
3054  C C   . ARG B 68  ? 0.4111 1.0367 0.2663 -0.1652 0.1153  -0.1278 68  ARG B C   
3055  O O   . ARG B 68  ? 0.3937 0.9885 0.2675 -0.1163 0.1076  -0.1422 68  ARG B O   
3056  C CB  . ARG B 68  ? 0.4402 0.9063 0.2617 -0.2141 0.1116  -0.0806 68  ARG B CB  
3057  C CG  . ARG B 68  ? 0.4813 0.9033 0.2619 -0.2659 0.1115  -0.0566 68  ARG B CG  
3058  C CD  . ARG B 68  ? 0.5016 0.7983 0.2578 -0.2606 0.1026  -0.0342 68  ARG B CD  
3059  N NE  . ARG B 68  ? 0.4995 0.7607 0.2586 -0.2584 0.1004  -0.0310 68  ARG B NE  
3060  C CZ  . ARG B 68  ? 0.4639 0.6952 0.2562 -0.2174 0.0974  -0.0371 68  ARG B CZ  
3061  N NH1 . ARG B 68  ? 0.4312 0.6581 0.2534 -0.1770 0.0950  -0.0460 68  ARG B NH1 
3062  N NH2 . ARG B 68  ? 0.4669 0.6713 0.2574 -0.2211 0.0959  -0.0336 68  ARG B NH2 
3063  N N   . GLU B 69  ? 0.4229 1.1033 0.2636 -0.1851 0.1199  -0.1293 69  GLU B N   
3064  C CA  . GLU B 69  ? 0.4148 1.1392 0.2645 -0.1453 0.1174  -0.1527 69  GLU B CA  
3065  C C   . GLU B 69  ? 0.4205 1.0680 0.2554 -0.1479 0.1136  -0.1373 69  GLU B C   
3066  O O   . GLU B 69  ? 0.4394 1.0478 0.2504 -0.1909 0.1162  -0.1116 69  GLU B O   
3067  C CB  . GLU B 69  ? 0.4255 1.2907 0.2713 -0.1633 0.1260  -0.1695 69  GLU B CB  
3068  C CG  . GLU B 69  ? 0.4185 1.3908 0.2792 -0.1610 0.1302  -0.1878 69  GLU B CG  
3069  C CD  . GLU B 69  ? 0.4098 1.4447 0.2893 -0.0879 0.1233  -0.2269 69  GLU B CD  
3070  O OE1 . GLU B 69  ? 0.4083 1.3490 0.2916 -0.0385 0.1112  -0.2335 69  GLU B OE1 
3071  O OE2 . GLU B 69  ? 0.4133 1.5918 0.2971 -0.0799 0.1281  -0.2513 69  GLU B OE2 
3072  N N   . PHE B 70  ? 0.4115 1.0349 0.2533 -0.1021 0.1053  -0.1532 70  PHE B N   
3073  C CA  . PHE B 70  ? 0.4167 0.9770 0.2458 -0.1022 0.1009  -0.1411 70  PHE B CA  
3074  C C   . PHE B 70  ? 0.4247 1.0264 0.2494 -0.0678 0.0962  -0.1669 70  PHE B C   
3075  O O   . PHE B 70  ? 0.4284 1.0567 0.2568 -0.0243 0.0891  -0.1945 70  PHE B O   
3076  C CB  . PHE B 70  ? 0.4077 0.8625 0.2408 -0.0862 0.0916  -0.1277 70  PHE B CB  
3077  C CG  . PHE B 70  ? 0.4001 0.8126 0.2366 -0.1071 0.0939  -0.1077 70  PHE B CG  
3078  C CD1 . PHE B 70  ? 0.3865 0.8048 0.2392 -0.0918 0.0926  -0.1174 70  PHE B CD1 
3079  C CD2 . PHE B 70  ? 0.4135 0.7758 0.2311 -0.1384 0.0955  -0.0804 70  PHE B CD2 
3080  C CE1 . PHE B 70  ? 0.3827 0.7608 0.2360 -0.1103 0.0942  -0.0998 70  PHE B CE1 
3081  C CE2 . PHE B 70  ? 0.4174 0.7334 0.2292 -0.1523 0.0951  -0.0641 70  PHE B CE2 
3082  C CZ  . PHE B 70  ? 0.3998 0.7252 0.2312 -0.1398 0.0952  -0.0737 70  PHE B CZ  
3083  N N   . ASN B 71  ? 0.4339 1.0347 0.2444 -0.0841 0.0981  -0.1588 71  ASN B N   
3084  C CA  . ASN B 71  ? 0.4477 1.0840 0.2487 -0.0528 0.0931  -0.1831 71  ASN B CA  
3085  C C   . ASN B 71  ? 0.4581 1.0015 0.2487 -0.0177 0.0773  -0.1878 71  ASN B C   
3086  O O   . ASN B 71  ? 0.4494 0.9167 0.2450 -0.0167 0.0713  -0.1745 71  ASN B O   
3087  C CB  . ASN B 71  ? 0.4578 1.1408 0.2455 -0.0867 0.1015  -0.1741 71  ASN B CB  
3088  C CG  . ASN B 71  ? 0.4611 1.0574 0.2371 -0.1108 0.0994  -0.1448 71  ASN B CG  
3089  O OD1 . ASN B 71  ? 0.4622 0.9894 0.2356 -0.0879 0.0893  -0.1441 71  ASN B OD1 
3090  N ND2 . ASN B 71  ? 0.4708 1.0717 0.2327 -0.1584 0.1070  -0.1207 71  ASN B ND2 
3091  N N   . ASN B 72  ? 0.4817 1.0337 0.2529 0.0076  0.0698  -0.2068 72  ASN B N   
3092  C CA  . ASN B 72  ? 0.5098 0.9764 0.2567 0.0401  0.0510  -0.2165 72  ASN B CA  
3093  C C   . ASN B 72  ? 0.5047 0.8886 0.2470 0.0131  0.0474  -0.1881 72  ASN B C   
3094  O O   . ASN B 72  ? 0.5263 0.8333 0.2489 0.0258  0.0318  -0.1886 72  ASN B O   
3095  C CB  . ASN B 72  ? 0.5498 1.0493 0.2672 0.0774  0.0419  -0.2480 72  ASN B CB  
3096  C CG  . ASN B 72  ? 0.6023 1.0109 0.2776 0.1196  0.0170  -0.2667 72  ASN B CG  
3097  O OD1 . ASN B 72  ? 0.6135 0.9754 0.2825 0.1387  0.0065  -0.2716 72  ASN B OD1 
3098  N ND2 . ASN B 72  ? 0.6435 1.0199 0.2821 0.1321  0.0054  -0.2770 72  ASN B ND2 
3099  N N   . LEU B 73  ? 0.4833 0.8852 0.2374 -0.0247 0.0599  -0.1639 73  LEU B N   
3100  C CA  . LEU B 73  ? 0.4772 0.8176 0.2291 -0.0467 0.0572  -0.1370 73  LEU B CA  
3101  C C   . LEU B 73  ? 0.4524 0.7759 0.2221 -0.0708 0.0650  -0.1113 73  LEU B C   
3102  O O   . LEU B 73  ? 0.4496 0.7534 0.2160 -0.0921 0.0677  -0.0881 73  LEU B O   
3103  C CB  . LEU B 73  ? 0.4869 0.8475 0.2262 -0.0627 0.0607  -0.1308 73  LEU B CB  
3104  C CG  . LEU B 73  ? 0.5188 0.8777 0.2329 -0.0384 0.0498  -0.1542 73  LEU B CG  
3105  C CD1 . LEU B 73  ? 0.5247 0.9290 0.2307 -0.0543 0.0571  -0.1520 73  LEU B CD1 
3106  C CD2 . LEU B 73  ? 0.5389 0.8173 0.2331 -0.0333 0.0332  -0.1495 73  LEU B CD2 
3107  N N   . GLU B 74  ? 0.4407 0.7699 0.2241 -0.0629 0.0667  -0.1171 74  GLU B N   
3108  C CA  . GLU B 74  ? 0.4238 0.7255 0.2192 -0.0789 0.0708  -0.0965 74  GLU B CA  
3109  C C   . GLU B 74  ? 0.4167 0.6848 0.2223 -0.0577 0.0629  -0.1043 74  GLU B C   
3110  O O   . GLU B 74  ? 0.4036 0.6748 0.2219 -0.0610 0.0672  -0.1011 74  GLU B O   
3111  C CB  . GLU B 74  ? 0.4221 0.7722 0.2190 -0.1024 0.0826  -0.0930 74  GLU B CB  
3112  C CG  . GLU B 74  ? 0.4391 0.8080 0.2161 -0.1330 0.0886  -0.0791 74  GLU B CG  
3113  C CD  . GLU B 74  ? 0.4517 0.8520 0.2168 -0.1682 0.0970  -0.0701 74  GLU B CD  
3114  O OE1 . GLU B 74  ? 0.4455 0.9149 0.2209 -0.1687 0.1026  -0.0877 74  GLU B OE1 
3115  O OE2 . GLU B 74  ? 0.4752 0.8300 0.2142 -0.1952 0.0962  -0.0458 74  GLU B OE2 
3116  N N   . ARG B 75  ? 0.4332 0.6643 0.2263 -0.0392 0.0496  -0.1137 75  ARG B N   
3117  C CA  . ARG B 75  ? 0.4416 0.6334 0.2317 -0.0201 0.0382  -0.1232 75  ARG B CA  
3118  C C   . ARG B 75  ? 0.4222 0.5771 0.2255 -0.0340 0.0378  -0.1014 75  ARG B C   
3119  O O   . ARG B 75  ? 0.4169 0.5556 0.2275 -0.0253 0.0347  -0.1048 75  ARG B O   
3120  C CB  . ARG B 75  ? 0.4839 0.6318 0.2394 -0.0033 0.0200  -0.1378 75  ARG B CB  
3121  C CG  . ARG B 75  ? 0.5153 0.6928 0.2501 0.0260  0.0155  -0.1675 75  ARG B CG  
3122  C CD  . ARG B 75  ? 0.5372 0.7078 0.2612 0.0610  0.0058  -0.1909 75  ARG B CD  
3123  N NE  . ARG B 75  ? 0.5599 0.7902 0.2721 0.0951  0.0053  -0.2212 75  ARG B NE  
3124  C CZ  . ARG B 75  ? 0.5317 0.8574 0.2726 0.0968  0.0214  -0.2293 75  ARG B CZ  
3125  N NH1 . ARG B 75  ? 0.4863 0.8436 0.2638 0.0638  0.0381  -0.2082 75  ARG B NH1 
3126  N NH2 . ARG B 75  ? 0.5557 0.9481 0.2827 0.1311  0.0193  -0.2595 75  ARG B NH2 
3127  N N   . ARG B 76  ? 0.4142 0.5608 0.2187 -0.0522 0.0401  -0.0803 76  ARG B N   
3128  C CA  . ARG B 76  ? 0.3985 0.5238 0.2137 -0.0602 0.0394  -0.0612 76  ARG B CA  
3129  C C   . ARG B 76  ? 0.3811 0.5144 0.2125 -0.0615 0.0492  -0.0553 76  ARG B C   
3130  O O   . ARG B 76  ? 0.3712 0.4874 0.2123 -0.0567 0.0467  -0.0535 76  ARG B O   
3131  C CB  . ARG B 76  ? 0.3978 0.5268 0.2081 -0.0717 0.0396  -0.0426 76  ARG B CB  
3132  C CG  . ARG B 76  ? 0.4152 0.5348 0.2084 -0.0777 0.0282  -0.0433 76  ARG B CG  
3133  C CD  . ARG B 76  ? 0.4132 0.5527 0.2036 -0.0864 0.0302  -0.0267 76  ARG B CD  
3134  N NE  . ARG B 76  ? 0.4174 0.5730 0.2032 -0.0873 0.0389  -0.0276 76  ARG B NE  
3135  C CZ  . ARG B 76  ? 0.4208 0.5869 0.2001 -0.0909 0.0422  -0.0128 76  ARG B CZ  
3136  N NH1 . ARG B 76  ? 0.4186 0.5884 0.1974 -0.0870 0.0378  0.0022  76  ARG B NH1 
3137  N NH2 . ARG B 76  ? 0.4320 0.6084 0.2007 -0.0972 0.0486  -0.0139 76  ARG B NH2 
3138  N N   . ILE B 77  ? 0.3842 0.5402 0.2124 -0.0721 0.0589  -0.0514 77  ILE B N   
3139  C CA  . ILE B 77  ? 0.3820 0.5378 0.2131 -0.0810 0.0661  -0.0445 77  ILE B CA  
3140  C C   . ILE B 77  ? 0.3736 0.5542 0.2179 -0.0744 0.0688  -0.0623 77  ILE B C   
3141  O O   . ILE B 77  ? 0.3675 0.5392 0.2182 -0.0779 0.0713  -0.0580 77  ILE B O   
3142  C CB  . ILE B 77  ? 0.4038 0.5663 0.2128 -0.1032 0.0724  -0.0327 77  ILE B CB  
3143  C CG1 . ILE B 77  ? 0.4107 0.6247 0.2158 -0.1129 0.0778  -0.0464 77  ILE B CG1 
3144  C CG2 . ILE B 77  ? 0.4187 0.5502 0.2098 -0.1024 0.0673  -0.0147 77  ILE B CG2 
3145  C CD1 . ILE B 77  ? 0.4390 0.6639 0.2167 -0.1450 0.0837  -0.0347 77  ILE B CD1 
3146  N N   . GLU B 78  ? 0.3782 0.5908 0.2231 -0.0614 0.0668  -0.0833 78  GLU B N   
3147  C CA  . GLU B 78  ? 0.3757 0.6153 0.2299 -0.0440 0.0659  -0.1040 78  GLU B CA  
3148  C C   . GLU B 78  ? 0.3706 0.5623 0.2305 -0.0288 0.0564  -0.1038 78  GLU B C   
3149  O O   . GLU B 78  ? 0.3612 0.5601 0.2324 -0.0238 0.0580  -0.1084 78  GLU B O   
3150  C CB  . GLU B 78  ? 0.3936 0.6688 0.2374 -0.0210 0.0610  -0.1296 78  GLU B CB  
3151  C CG  . GLU B 78  ? 0.3996 0.7076 0.2466 0.0079  0.0569  -0.1550 78  GLU B CG  
3152  C CD  . GLU B 78  ? 0.4244 0.7844 0.2562 0.0358  0.0527  -0.1831 78  GLU B CD  
3153  O OE1 . GLU B 78  ? 0.4514 0.7722 0.2591 0.0514  0.0412  -0.1900 78  GLU B OE1 
3154  O OE2 . GLU B 78  ? 0.4208 0.8656 0.2615 0.0423  0.0602  -0.1992 78  GLU B OE2 
3155  N N   . ASN B 79  ? 0.3798 0.5267 0.2292 -0.0257 0.0460  -0.0977 79  ASN B N   
3156  C CA  . ASN B 79  ? 0.3831 0.4854 0.2305 -0.0190 0.0351  -0.0956 79  ASN B CA  
3157  C C   . ASN B 79  ? 0.3594 0.4520 0.2242 -0.0319 0.0412  -0.0758 79  ASN B C   
3158  O O   . ASN B 79  ? 0.3535 0.4299 0.2255 -0.0265 0.0378  -0.0769 79  ASN B O   
3159  C CB  . ASN B 79  ? 0.4086 0.4730 0.2316 -0.0220 0.0212  -0.0932 79  ASN B CB  
3160  C CG  . ASN B 79  ? 0.4229 0.4415 0.2339 -0.0238 0.0075  -0.0900 79  ASN B CG  
3161  O OD1 . ASN B 79  ? 0.4520 0.4403 0.2428 -0.0072 -0.0045 -0.1059 79  ASN B OD1 
3162  N ND2 . ASN B 79  ? 0.4082 0.4244 0.2273 -0.0426 0.0082  -0.0699 79  ASN B ND2 
3163  N N   . LEU B 80  ? 0.3529 0.4521 0.2190 -0.0455 0.0483  -0.0588 80  LEU B N   
3164  C CA  . LEU B 80  ? 0.3426 0.4300 0.2151 -0.0507 0.0524  -0.0422 80  LEU B CA  
3165  C C   . LEU B 80  ? 0.3383 0.4333 0.2180 -0.0529 0.0594  -0.0470 80  LEU B C   
3166  O O   . LEU B 80  ? 0.3297 0.4092 0.2178 -0.0494 0.0586  -0.0435 80  LEU B O   
3167  C CB  . LEU B 80  ? 0.3534 0.4399 0.2119 -0.0585 0.0559  -0.0268 80  LEU B CB  
3168  C CG  . LEU B 80  ? 0.3601 0.4249 0.2097 -0.0545 0.0552  -0.0102 80  LEU B CG  
3169  C CD1 . LEU B 80  ? 0.3826 0.4427 0.2088 -0.0552 0.0538  0.0014  80  LEU B CD1 
3170  C CD2 . LEU B 80  ? 0.3696 0.4157 0.2121 -0.0596 0.0597  -0.0083 80  LEU B CD2 
3171  N N   . ASN B 81  ? 0.3464 0.4727 0.2217 -0.0614 0.0661  -0.0552 81  ASN B N   
3172  C CA  . ASN B 81  ? 0.3465 0.4960 0.2258 -0.0703 0.0728  -0.0606 81  ASN B CA  
3173  C C   . ASN B 81  ? 0.3343 0.4901 0.2310 -0.0519 0.0689  -0.0756 81  ASN B C   
3174  O O   . ASN B 81  ? 0.3281 0.4794 0.2311 -0.0567 0.0715  -0.0724 81  ASN B O   
3175  C CB  . ASN B 81  ? 0.3571 0.5608 0.2287 -0.0843 0.0797  -0.0698 81  ASN B CB  
3176  C CG  . ASN B 81  ? 0.3594 0.6031 0.2321 -0.1014 0.0867  -0.0744 81  ASN B CG  
3177  O OD1 . ASN B 81  ? 0.3716 0.5859 0.2312 -0.1219 0.0885  -0.0595 81  ASN B OD1 
3178  N ND2 . ASN B 81  ? 0.3537 0.6667 0.2373 -0.0919 0.0892  -0.0961 81  ASN B ND2 
3179  N N   . LYS B 82  ? 0.3401 0.4987 0.2371 -0.0302 0.0604  -0.0919 82  LYS B N   
3180  C CA  . LYS B 82  ? 0.3430 0.4964 0.2447 -0.0082 0.0525  -0.1076 82  LYS B CA  
3181  C C   . LYS B 82  ? 0.3352 0.4419 0.2426 -0.0104 0.0477  -0.0946 82  LYS B C   
3182  O O   . LYS B 82  ? 0.3263 0.4354 0.2442 -0.0070 0.0488  -0.0972 82  LYS B O   
3183  C CB  . LYS B 82  ? 0.3705 0.5113 0.2525 0.0175  0.0386  -0.1269 82  LYS B CB  
3184  C CG  . LYS B 82  ? 0.3890 0.5038 0.2613 0.0437  0.0251  -0.1423 82  LYS B CG  
3185  C CD  . LYS B 82  ? 0.4351 0.5365 0.2734 0.0774  0.0085  -0.1674 82  LYS B CD  
3186  C CE  . LYS B 82  ? 0.4753 0.4936 0.2758 0.0753  -0.0106 -0.1622 82  LYS B CE  
3187  N NZ  . LYS B 82  ? 0.5345 0.5261 0.2881 0.1067  -0.0289 -0.1862 82  LYS B NZ  
3188  N N   . LYS B 83  ? 0.3399 0.4134 0.2401 -0.0171 0.0423  -0.0810 83  LYS B N   
3189  C CA  . LYS B 83  ? 0.3336 0.3776 0.2384 -0.0212 0.0377  -0.0682 83  LYS B CA  
3190  C C   . LYS B 83  ? 0.3173 0.3659 0.2350 -0.0282 0.0475  -0.0564 83  LYS B C   
3191  O O   . LYS B 83  ? 0.3097 0.3452 0.2352 -0.0256 0.0454  -0.0538 83  LYS B O   
3192  C CB  . LYS B 83  ? 0.3414 0.3720 0.2354 -0.0304 0.0313  -0.0558 83  LYS B CB  
3193  C CG  . LYS B 83  ? 0.3706 0.3707 0.2412 -0.0311 0.0147  -0.0625 83  LYS B CG  
3194  C CD  . LYS B 83  ? 0.3988 0.3840 0.2513 -0.0123 0.0067  -0.0850 83  LYS B CD  
3195  C CE  . LYS B 83  ? 0.4485 0.3779 0.2590 -0.0128 -0.0153 -0.0912 83  LYS B CE  
3196  N NZ  . LYS B 83  ? 0.4792 0.3958 0.2613 -0.0180 -0.0230 -0.0939 83  LYS B NZ  
3197  N N   . MET B 84  ? 0.3220 0.3821 0.2343 -0.0382 0.0563  -0.0492 84  MET B N   
3198  C CA  . MET B 84  ? 0.3263 0.3742 0.2342 -0.0461 0.0619  -0.0386 84  MET B CA  
3199  C C   . MET B 84  ? 0.3203 0.3823 0.2381 -0.0487 0.0655  -0.0486 84  MET B C   
3200  O O   . MET B 84  ? 0.3151 0.3590 0.2372 -0.0467 0.0649  -0.0442 84  MET B O   
3201  C CB  . MET B 84  ? 0.3506 0.3948 0.2347 -0.0609 0.0667  -0.0293 84  MET B CB  
3202  C CG  . MET B 84  ? 0.3765 0.3809 0.2359 -0.0657 0.0661  -0.0152 84  MET B CG  
3203  S SD  . MET B 84  ? 0.4214 0.4163 0.2421 -0.0989 0.0705  -0.0098 84  MET B SD  
3204  C CE  . MET B 84  ? 0.3993 0.4395 0.2451 -0.1106 0.0770  -0.0246 84  MET B CE  
3205  N N   . GLU B 85  ? 0.3217 0.4237 0.2427 -0.0512 0.0689  -0.0630 85  GLU B N   
3206  C CA  . GLU B 85  ? 0.3171 0.4513 0.2475 -0.0532 0.0726  -0.0743 85  GLU B CA  
3207  C C   . GLU B 85  ? 0.3043 0.4245 0.2493 -0.0307 0.0646  -0.0834 85  GLU B C   
3208  O O   . GLU B 85  ? 0.2973 0.4135 0.2494 -0.0335 0.0661  -0.0818 85  GLU B O   
3209  C CB  . GLU B 85  ? 0.3228 0.5231 0.2534 -0.0556 0.0771  -0.0907 85  GLU B CB  
3210  C CG  . GLU B 85  ? 0.3418 0.5594 0.2530 -0.0846 0.0842  -0.0810 85  GLU B CG  
3211  C CD  . GLU B 85  ? 0.3534 0.6383 0.2582 -0.1120 0.0925  -0.0865 85  GLU B CD  
3212  O OE1 . GLU B 85  ? 0.3500 0.7099 0.2636 -0.1031 0.0948  -0.1056 85  GLU B OE1 
3213  O OE2 . GLU B 85  ? 0.3729 0.6379 0.2583 -0.1438 0.0954  -0.0721 85  GLU B OE2 
3214  N N   . ASP B 86  ? 0.3091 0.4146 0.2511 -0.0114 0.0544  -0.0920 86  ASP B N   
3215  C CA  . ASP B 86  ? 0.3126 0.3886 0.2543 0.0058  0.0426  -0.0986 86  ASP B CA  
3216  C C   . ASP B 86  ? 0.3008 0.3420 0.2481 -0.0036 0.0416  -0.0817 86  ASP B C   
3217  O O   . ASP B 86  ? 0.2975 0.3272 0.2501 0.0022  0.0375  -0.0843 86  ASP B O   
3218  C CB  . ASP B 86  ? 0.3400 0.3873 0.2595 0.0208  0.0278  -0.1077 86  ASP B CB  
3219  C CG  . ASP B 86  ? 0.3648 0.4317 0.2710 0.0493  0.0200  -0.1333 86  ASP B CG  
3220  O OD1 . ASP B 86  ? 0.3654 0.4495 0.2780 0.0641  0.0186  -0.1445 86  ASP B OD1 
3221  O OD2 . ASP B 86  ? 0.3884 0.4558 0.2753 0.0603  0.0140  -0.1435 86  ASP B OD2 
3222  N N   . GLY B 87  ? 0.2969 0.3269 0.2414 -0.0152 0.0445  -0.0656 87  GLY B N   
3223  C CA  . GLY B 87  ? 0.2887 0.3003 0.2366 -0.0191 0.0431  -0.0512 87  GLY B CA  
3224  C C   . GLY B 87  ? 0.2806 0.2906 0.2362 -0.0209 0.0498  -0.0478 87  GLY B C   
3225  O O   . GLY B 87  ? 0.2735 0.2725 0.2353 -0.0178 0.0463  -0.0446 87  GLY B O   
3226  N N   . PHE B 88  ? 0.2870 0.3069 0.2369 -0.0299 0.0583  -0.0478 88  PHE B N   
3227  C CA  . PHE B 88  ? 0.2909 0.3027 0.2375 -0.0379 0.0630  -0.0444 88  PHE B CA  
3228  C C   . PHE B 88  ? 0.2786 0.3098 0.2417 -0.0340 0.0626  -0.0572 88  PHE B C   
3229  O O   . PHE B 88  ? 0.2755 0.2941 0.2416 -0.0353 0.0630  -0.0542 88  PHE B O   
3230  C CB  . PHE B 88  ? 0.3157 0.3277 0.2387 -0.0585 0.0693  -0.0393 88  PHE B CB  
3231  C CG  . PHE B 88  ? 0.3429 0.3154 0.2365 -0.0591 0.0670  -0.0244 88  PHE B CG  
3232  C CD1 . PHE B 88  ? 0.3560 0.2906 0.2358 -0.0468 0.0624  -0.0155 88  PHE B CD1 
3233  C CD2 . PHE B 88  ? 0.3609 0.3352 0.2367 -0.0677 0.0679  -0.0205 88  PHE B CD2 
3234  C CE1 . PHE B 88  ? 0.3909 0.2889 0.2363 -0.0376 0.0573  -0.0046 88  PHE B CE1 
3235  C CE2 . PHE B 88  ? 0.3944 0.3280 0.2366 -0.0632 0.0632  -0.0076 88  PHE B CE2 
3236  C CZ  . PHE B 88  ? 0.4117 0.3064 0.2370 -0.0453 0.0570  -0.0004 88  PHE B CZ  
3237  N N   . LEU B 89  ? 0.2759 0.3377 0.2461 -0.0252 0.0603  -0.0727 89  LEU B N   
3238  C CA  . LEU B 89  ? 0.2712 0.3525 0.2523 -0.0123 0.0566  -0.0875 89  LEU B CA  
3239  C C   . LEU B 89  ? 0.2674 0.3110 0.2512 -0.0002 0.0465  -0.0853 89  LEU B C   
3240  O O   . LEU B 89  ? 0.2620 0.3073 0.2533 0.0038  0.0452  -0.0893 89  LEU B O   
3241  C CB  . LEU B 89  ? 0.2814 0.3996 0.2602 0.0058  0.0522  -0.1076 89  LEU B CB  
3242  C CG  . LEU B 89  ? 0.2849 0.4637 0.2631 -0.0074 0.0625  -0.1134 89  LEU B CG  
3243  C CD1 . LEU B 89  ? 0.2973 0.5170 0.2713 0.0202  0.0561  -0.1364 89  LEU B CD1 
3244  C CD2 . LEU B 89  ? 0.2807 0.4990 0.2646 -0.0286 0.0715  -0.1124 89  LEU B CD2 
3245  N N   . ASP B 90  ? 0.2735 0.2871 0.2482 0.0014  0.0387  -0.0784 90  ASP B N   
3246  C CA  . ASP B 90  ? 0.2770 0.2589 0.2475 0.0029  0.0281  -0.0735 90  ASP B CA  
3247  C C   . ASP B 90  ? 0.2595 0.2391 0.2412 -0.0056 0.0345  -0.0602 90  ASP B C   
3248  O O   . ASP B 90  ? 0.2574 0.2259 0.2423 -0.0042 0.0296  -0.0599 90  ASP B O   
3249  C CB  . ASP B 90  ? 0.2938 0.2542 0.2466 -0.0027 0.0181  -0.0674 90  ASP B CB  
3250  C CG  . ASP B 90  ? 0.3248 0.2704 0.2547 0.0090  0.0069  -0.0820 90  ASP B CG  
3251  O OD1 . ASP B 90  ? 0.3344 0.2879 0.2619 0.0284  0.0043  -0.0989 90  ASP B OD1 
3252  O OD2 . ASP B 90  ? 0.3436 0.2728 0.2547 0.0009  -0.0002 -0.0775 90  ASP B OD2 
3253  N N   . VAL B 91  ? 0.2540 0.2396 0.2354 -0.0120 0.0434  -0.0501 91  VAL B N   
3254  C CA  . VAL B 91  ? 0.2496 0.2269 0.2313 -0.0127 0.0473  -0.0400 91  VAL B CA  
3255  C C   . VAL B 91  ? 0.2468 0.2226 0.2331 -0.0155 0.0517  -0.0450 91  VAL B C   
3256  O O   . VAL B 91  ? 0.2414 0.2091 0.2326 -0.0127 0.0500  -0.0426 91  VAL B O   
3257  C CB  . VAL B 91  ? 0.2639 0.2341 0.2292 -0.0127 0.0518  -0.0302 91  VAL B CB  
3258  C CG1 . VAL B 91  ? 0.2775 0.2264 0.2293 -0.0073 0.0533  -0.0237 91  VAL B CG1 
3259  C CG2 . VAL B 91  ? 0.2629 0.2448 0.2260 -0.0081 0.0470  -0.0239 91  VAL B CG2 
3260  N N   . TRP B 92  ? 0.2511 0.2422 0.2348 -0.0237 0.0573  -0.0519 92  TRP B N   
3261  C CA  . TRP B 92  ? 0.2517 0.2520 0.2371 -0.0326 0.0616  -0.0563 92  TRP B CA  
3262  C C   . TRP B 92  ? 0.2364 0.2547 0.2397 -0.0208 0.0566  -0.0687 92  TRP B C   
3263  O O   . TRP B 92  ? 0.2326 0.2512 0.2407 -0.0237 0.0576  -0.0696 92  TRP B O   
3264  C CB  . TRP B 92  ? 0.2680 0.2918 0.2400 -0.0529 0.0687  -0.0584 92  TRP B CB  
3265  C CG  . TRP B 92  ? 0.2999 0.2842 0.2389 -0.0683 0.0704  -0.0441 92  TRP B CG  
3266  C CD1 . TRP B 92  ? 0.3193 0.2943 0.2386 -0.0749 0.0710  -0.0381 92  TRP B CD1 
3267  C CD2 . TRP B 92  ? 0.3273 0.2654 0.2397 -0.0749 0.0686  -0.0346 92  TRP B CD2 
3268  N NE1 . TRP B 92  ? 0.3620 0.2831 0.2397 -0.0841 0.0683  -0.0253 92  TRP B NE1 
3269  C CE2 . TRP B 92  ? 0.3707 0.2656 0.2409 -0.0829 0.0661  -0.0236 92  TRP B CE2 
3270  C CE3 . TRP B 92  ? 0.3259 0.2503 0.2406 -0.0732 0.0674  -0.0350 92  TRP B CE3 
3271  C CZ2 . TRP B 92  ? 0.4215 0.2516 0.2442 -0.0857 0.0601  -0.0141 92  TRP B CZ2 
3272  C CZ3 . TRP B 92  ? 0.3696 0.2364 0.2429 -0.0781 0.0634  -0.0256 92  TRP B CZ3 
3273  C CH2 . TRP B 92  ? 0.4209 0.2373 0.2452 -0.0826 0.0587  -0.0159 92  TRP B CH2 
3274  N N   . THR B 93  ? 0.2353 0.2611 0.2414 -0.0058 0.0489  -0.0787 93  THR B N   
3275  C CA  . THR B 93  ? 0.2369 0.2610 0.2460 0.0112  0.0386  -0.0905 93  THR B CA  
3276  C C   . THR B 93  ? 0.2328 0.2214 0.2419 0.0092  0.0326  -0.0802 93  THR B C   
3277  O O   . THR B 93  ? 0.2306 0.2178 0.2447 0.0134  0.0296  -0.0840 93  THR B O   
3278  C CB  . THR B 93  ? 0.2572 0.2742 0.2514 0.0303  0.0264  -0.1030 93  THR B CB  
3279  O OG1 . THR B 93  ? 0.2595 0.3225 0.2551 0.0355  0.0323  -0.1150 93  THR B OG1 
3280  C CG2 . THR B 93  ? 0.2778 0.2749 0.2597 0.0520  0.0109  -0.1154 93  THR B CG2 
3281  N N   . TYR B 94  ? 0.2320 0.2011 0.2350 0.0020  0.0307  -0.0678 94  TYR B N   
3282  C CA  . TYR B 94  ? 0.2288 0.1816 0.2310 -0.0033 0.0254  -0.0576 94  TYR B CA  
3283  C C   . TYR B 94  ? 0.2148 0.1731 0.2279 -0.0055 0.0338  -0.0527 94  TYR B C   
3284  O O   . TYR B 94  ? 0.2114 0.1636 0.2279 -0.0055 0.0295  -0.0520 94  TYR B O   
3285  C CB  . TYR B 94  ? 0.2312 0.1850 0.2259 -0.0112 0.0236  -0.0460 94  TYR B CB  
3286  C CG  . TYR B 94  ? 0.2252 0.1876 0.2215 -0.0180 0.0215  -0.0349 94  TYR B CG  
3287  C CD1 . TYR B 94  ? 0.2145 0.1924 0.2173 -0.0113 0.0305  -0.0286 94  TYR B CD1 
3288  C CD2 . TYR B 94  ? 0.2393 0.1938 0.2226 -0.0312 0.0086  -0.0310 94  TYR B CD2 
3289  C CE1 . TYR B 94  ? 0.2101 0.2097 0.2140 -0.0117 0.0284  -0.0212 94  TYR B CE1 
3290  C CE2 . TYR B 94  ? 0.2335 0.2129 0.2186 -0.0410 0.0073  -0.0211 94  TYR B CE2 
3291  C CZ  . TYR B 94  ? 0.2146 0.2238 0.2139 -0.0282 0.0181  -0.0173 94  TYR B CZ  
3292  O OH  . TYR B 94  ? 0.2101 0.2572 0.2110 -0.0321 0.0167  -0.0101 94  TYR B OH  
3293  N N   . ASN B 95  ? 0.2150 0.1777 0.2259 -0.0085 0.0439  -0.0491 95  ASN B N   
3294  C CA  . ASN B 95  ? 0.2182 0.1714 0.2254 -0.0109 0.0493  -0.0450 95  ASN B CA  
3295  C C   . ASN B 95  ? 0.2128 0.1731 0.2290 -0.0143 0.0501  -0.0531 95  ASN B C   
3296  O O   . ASN B 95  ? 0.2100 0.1618 0.2285 -0.0132 0.0493  -0.0508 95  ASN B O   
3297  C CB  . ASN B 95  ? 0.2403 0.1798 0.2261 -0.0178 0.0556  -0.0404 95  ASN B CB  
3298  C CG  . ASN B 95  ? 0.2523 0.1810 0.2238 -0.0080 0.0538  -0.0316 95  ASN B CG  
3299  O OD1 . ASN B 95  ? 0.2404 0.1830 0.2211 0.0016  0.0494  -0.0285 95  ASN B OD1 
3300  N ND2 . ASN B 95  ? 0.2812 0.1881 0.2253 -0.0125 0.0559  -0.0274 95  ASN B ND2 
3301  N N   . ALA B 96  ? 0.2120 0.1959 0.2327 -0.0166 0.0515  -0.0636 96  ALA B N   
3302  C CA  . ALA B 96  ? 0.2072 0.2147 0.2369 -0.0171 0.0519  -0.0738 96  ALA B CA  
3303  C C   . ALA B 96  ? 0.2005 0.1982 0.2381 -0.0023 0.0415  -0.0783 96  ALA B C   
3304  O O   . ALA B 96  ? 0.1962 0.1933 0.2390 -0.0041 0.0416  -0.0785 96  ALA B O   
3305  C CB  . ALA B 96  ? 0.2101 0.2625 0.2424 -0.0162 0.0539  -0.0869 96  ALA B CB  
3306  N N   . GLU B 97  ? 0.2077 0.1910 0.2389 0.0094  0.0309  -0.0812 97  GLU B N   
3307  C CA  . GLU B 97  ? 0.2194 0.1793 0.2427 0.0198  0.0165  -0.0849 97  GLU B CA  
3308  C C   . GLU B 97  ? 0.2120 0.1523 0.2364 0.0081  0.0153  -0.0714 97  GLU B C   
3309  O O   . GLU B 97  ? 0.2165 0.1467 0.2395 0.0102  0.0086  -0.0729 97  GLU B O   
3310  C CB  . GLU B 97  ? 0.2484 0.1814 0.2480 0.0302  0.0016  -0.0901 97  GLU B CB  
3311  C CG  . GLU B 97  ? 0.2619 0.2182 0.2562 0.0515  -0.0007 -0.1082 97  GLU B CG  
3312  C CD  . GLU B 97  ? 0.3052 0.2204 0.2639 0.0672  -0.0196 -0.1159 97  GLU B CD  
3313  O OE1 . GLU B 97  ? 0.3285 0.1934 0.2631 0.0541  -0.0317 -0.1050 97  GLU B OE1 
3314  O OE2 . GLU B 97  ? 0.3227 0.2575 0.2720 0.0916  -0.0237 -0.1334 97  GLU B OE2 
3315  N N   . LEU B 98  ? 0.2028 0.1441 0.2282 -0.0017 0.0213  -0.0594 98  LEU B N   
3316  C CA  . LEU B 98  ? 0.1956 0.1366 0.2222 -0.0089 0.0210  -0.0485 98  LEU B CA  
3317  C C   . LEU B 98  ? 0.1842 0.1303 0.2201 -0.0072 0.0293  -0.0487 98  LEU B C   
3318  O O   . LEU B 98  ? 0.1811 0.1260 0.2194 -0.0091 0.0258  -0.0465 98  LEU B O   
3319  C CB  . LEU B 98  ? 0.1935 0.1474 0.2167 -0.0119 0.0246  -0.0387 98  LEU B CB  
3320  C CG  . LEU B 98  ? 0.1899 0.1635 0.2128 -0.0162 0.0226  -0.0293 98  LEU B CG  
3321  C CD1 . LEU B 98  ? 0.2034 0.1735 0.2144 -0.0340 0.0088  -0.0253 98  LEU B CD1 
3322  C CD2 . LEU B 98  ? 0.1893 0.1883 0.2088 -0.0095 0.0273  -0.0230 98  LEU B CD2 
3323  N N   . LEU B 99  ? 0.1843 0.1323 0.2194 -0.0073 0.0390  -0.0508 99  LEU B N   
3324  C CA  . LEU B 99  ? 0.1872 0.1289 0.2193 -0.0105 0.0448  -0.0506 99  LEU B CA  
3325  C C   . LEU B 99  ? 0.1788 0.1294 0.2222 -0.0118 0.0419  -0.0582 99  LEU B C   
3326  O O   . LEU B 99  ? 0.1770 0.1219 0.2213 -0.0126 0.0419  -0.0562 99  LEU B O   
3327  C CB  . LEU B 99  ? 0.2055 0.1394 0.2215 -0.0199 0.0521  -0.0508 99  LEU B CB  
3328  C CG  . LEU B 99  ? 0.2284 0.1391 0.2239 -0.0293 0.0552  -0.0486 99  LEU B CG  
3329  C CD1 . LEU B 99  ? 0.2419 0.1263 0.2220 -0.0141 0.0523  -0.0424 99  LEU B CD1 
3330  C CD2 . LEU B 99  ? 0.2609 0.1559 0.2271 -0.0485 0.0591  -0.0467 99  LEU B CD2 
3331  N N   . VAL B 100 ? 0.1765 0.1438 0.2259 -0.0080 0.0385  -0.0683 100 VAL B N   
3332  C CA  . VAL B 100 ? 0.1740 0.1542 0.2307 -0.0017 0.0331  -0.0778 100 VAL B CA  
3333  C C   . VAL B 100 ? 0.1759 0.1322 0.2295 0.0027  0.0221  -0.0735 100 VAL B C   
3334  O O   . VAL B 100 ? 0.1717 0.1283 0.2299 0.0008  0.0217  -0.0734 100 VAL B O   
3335  C CB  . VAL B 100 ? 0.1809 0.1878 0.2379 0.0122  0.0282  -0.0927 100 VAL B CB  
3336  C CG1 . VAL B 100 ? 0.1891 0.2026 0.2456 0.0298  0.0169  -0.1041 100 VAL B CG1 
3337  C CG2 . VAL B 100 ? 0.1780 0.2270 0.2388 0.0000  0.0400  -0.0972 100 VAL B CG2 
3338  N N   . LEU B 101 ? 0.1863 0.1224 0.2280 0.0038  0.0125  -0.0691 101 LEU B N   
3339  C CA  . LEU B 101 ? 0.1983 0.1116 0.2273 -0.0025 0.0002  -0.0620 101 LEU B CA  
3340  C C   . LEU B 101 ? 0.1819 0.1073 0.2204 -0.0126 0.0071  -0.0521 101 LEU B C   
3341  O O   . LEU B 101 ? 0.1854 0.1051 0.2217 -0.0163 0.0012  -0.0507 101 LEU B O   
3342  C CB  . LEU B 101 ? 0.2185 0.1133 0.2269 -0.0108 -0.0096 -0.0556 101 LEU B CB  
3343  C CG  . LEU B 101 ? 0.2638 0.1139 0.2364 -0.0075 -0.0312 -0.0606 101 LEU B CG  
3344  C CD1 . LEU B 101 ? 0.2779 0.1221 0.2461 0.0203  -0.0366 -0.0787 101 LEU B CD1 
3345  C CD2 . LEU B 101 ? 0.2835 0.1191 0.2355 -0.0178 -0.0373 -0.0554 101 LEU B CD2 
3346  N N   . MET B 102 ? 0.1695 0.1103 0.2138 -0.0134 0.0180  -0.0464 102 MET B N   
3347  C CA  . MET B 102 ? 0.1621 0.1171 0.2088 -0.0139 0.0229  -0.0399 102 MET B CA  
3348  C C   . MET B 102 ? 0.1585 0.1076 0.2098 -0.0103 0.0287  -0.0446 102 MET B C   
3349  O O   . MET B 102 ? 0.1561 0.1115 0.2088 -0.0113 0.0273  -0.0423 102 MET B O   
3350  C CB  . MET B 102 ? 0.1637 0.1304 0.2052 -0.0062 0.0297  -0.0355 102 MET B CB  
3351  C CG  . MET B 102 ? 0.1658 0.1518 0.2031 -0.0126 0.0243  -0.0291 102 MET B CG  
3352  S SD  . MET B 102 ? 0.1694 0.1843 0.1996 0.0035  0.0303  -0.0246 102 MET B SD  
3353  C CE  . MET B 102 ? 0.1825 0.1559 0.2026 0.0142  0.0380  -0.0300 102 MET B CE  
3354  N N   . GLU B 103 ? 0.1609 0.1024 0.2120 -0.0100 0.0348  -0.0507 103 GLU B N   
3355  C CA  . GLU B 103 ? 0.1652 0.1008 0.2137 -0.0138 0.0398  -0.0542 103 GLU B CA  
3356  C C   . GLU B 103 ? 0.1567 0.1030 0.2173 -0.0158 0.0350  -0.0607 103 GLU B C   
3357  O O   . GLU B 103 ? 0.1578 0.1027 0.2182 -0.0195 0.0368  -0.0616 103 GLU B O   
3358  C CB  . GLU B 103 ? 0.1815 0.1084 0.2159 -0.0223 0.0469  -0.0562 103 GLU B CB  
3359  C CG  . GLU B 103 ? 0.2053 0.1050 0.2140 -0.0173 0.0492  -0.0498 103 GLU B CG  
3360  C CD  . GLU B 103 ? 0.2259 0.1016 0.2139 -0.0071 0.0477  -0.0472 103 GLU B CD  
3361  O OE1 . GLU B 103 ? 0.2227 0.0993 0.2152 -0.0111 0.0472  -0.0497 103 GLU B OE1 
3362  O OE2 . GLU B 103 ? 0.2492 0.1063 0.2135 0.0089  0.0460  -0.0440 103 GLU B OE2 
3363  N N   . ASN B 104 ? 0.1550 0.1077 0.2204 -0.0101 0.0270  -0.0662 104 ASN B N   
3364  C CA  . ASN B 104 ? 0.1576 0.1127 0.2256 -0.0039 0.0174  -0.0729 104 ASN B CA  
3365  C C   . ASN B 104 ? 0.1592 0.0995 0.2233 -0.0087 0.0110  -0.0650 104 ASN B C   
3366  O O   . ASN B 104 ? 0.1577 0.1007 0.2252 -0.0087 0.0088  -0.0676 104 ASN B O   
3367  C CB  . ASN B 104 ? 0.1742 0.1214 0.2319 0.0101  0.0044  -0.0806 104 ASN B CB  
3368  C CG  . ASN B 104 ? 0.1737 0.1544 0.2373 0.0210  0.0082  -0.0942 104 ASN B CG  
3369  O OD1 . ASN B 104 ? 0.1614 0.1753 0.2365 0.0115  0.0198  -0.0970 104 ASN B OD1 
3370  N ND2 . ASN B 104 ? 0.1934 0.1673 0.2435 0.0393  -0.0029 -0.1030 104 ASN B ND2 
3371  N N   . GLU B 105 ? 0.2504 0.3173 0.1421 -0.0136 -0.0176 -0.0160 105 GLU B N   
3372  C CA  . GLU B 105 ? 0.2328 0.3117 0.1453 -0.0310 -0.0287 -0.0120 105 GLU B CA  
3373  C C   . GLU B 105 ? 0.1937 0.2928 0.1383 -0.0135 -0.0191 0.0072  105 GLU B C   
3374  O O   . GLU B 105 ? 0.1730 0.2647 0.1386 -0.0197 -0.0193 0.0084  105 GLU B O   
3375  C CB  . GLU B 105 ? 0.2534 0.3803 0.1533 -0.0543 -0.0477 -0.0123 105 GLU B CB  
3376  C CG  . GLU B 105 ? 0.2486 0.3899 0.1636 -0.0841 -0.0595 -0.0107 105 GLU B CG  
3377  C CD  . GLU B 105 ? 0.2889 0.4614 0.1811 -0.1242 -0.0807 -0.0189 105 GLU B CD  
3378  O OE1 . GLU B 105 ? 0.2927 0.5316 0.1816 -0.1210 -0.0876 -0.0136 105 GLU B OE1 
3379  O OE2 . GLU B 105 ? 0.3260 0.4541 0.1993 -0.1606 -0.0917 -0.0299 105 GLU B OE2 
3380  N N   . ARG B 106 ? 0.1943 0.3124 0.1355 0.0094  -0.0115 0.0223  106 ARG B N   
3381  C CA  . ARG B 106 ? 0.1778 0.2966 0.1366 0.0306  -0.0028 0.0381  106 ARG B CA  
3382  C C   . ARG B 106 ? 0.1650 0.2337 0.1347 0.0319  0.0117  0.0348  106 ARG B C   
3383  O O   . ARG B 106 ? 0.1499 0.2101 0.1368 0.0375  0.0152  0.0383  106 ARG B O   
3384  C CB  . ARG B 106 ? 0.2039 0.3373 0.1436 0.0571  -0.0001 0.0569  106 ARG B CB  
3385  C CG  . ARG B 106 ? 0.2141 0.4172 0.1497 0.0640  -0.0161 0.0637  106 ARG B CG  
3386  C CD  . ARG B 106 ? 0.2397 0.4545 0.1642 0.1050  -0.0142 0.0860  106 ARG B CD  
3387  N NE  . ARG B 106 ? 0.2265 0.4715 0.1744 0.1240  -0.0161 0.0892  106 ARG B NE  
3388  C CZ  . ARG B 106 ? 0.2535 0.4719 0.1917 0.1639  -0.0094 0.1020  106 ARG B CZ  
3389  N NH1 . ARG B 106 ? 0.3000 0.4501 0.2033 0.1839  -0.0008 0.1165  106 ARG B NH1 
3390  N NH2 . ARG B 106 ? 0.2441 0.4999 0.2021 0.1837  -0.0109 0.1002  106 ARG B NH2 
3391  N N   . THR B 107 ? 0.1739 0.2187 0.1330 0.0270  0.0199  0.0268  107 THR B N   
3392  C CA  . THR B 107 ? 0.1630 0.1795 0.1359 0.0253  0.0328  0.0232  107 THR B CA  
3393  C C   . THR B 107 ? 0.1392 0.1468 0.1340 0.0167  0.0268  0.0115  107 THR B C   
3394  O O   . THR B 107 ? 0.1245 0.1212 0.1366 0.0169  0.0323  0.0134  107 THR B O   
3395  C CB  . THR B 107 ? 0.1801 0.1945 0.1398 0.0243  0.0437  0.0161  107 THR B CB  
3396  O OG1 . THR B 107 ? 0.2075 0.2276 0.1426 0.0295  0.0514  0.0318  107 THR B OG1 
3397  C CG2 . THR B 107 ? 0.1686 0.1753 0.1484 0.0203  0.0557  0.0123  107 THR B CG2 
3398  N N   . LEU B 108 ? 0.1448 0.1517 0.1327 0.0070  0.0142  0.0001  108 LEU B N   
3399  C CA  . LEU B 108 ? 0.1368 0.1259 0.1357 -0.0017 0.0069  -0.0067 108 LEU B CA  
3400  C C   . LEU B 108 ? 0.1153 0.1239 0.1311 -0.0073 0.0028  0.0038  108 LEU B C   
3401  O O   . LEU B 108 ? 0.1015 0.1010 0.1318 -0.0084 0.0037  0.0038  108 LEU B O   
3402  C CB  . LEU B 108 ? 0.1709 0.1362 0.1448 -0.0143 -0.0068 -0.0198 108 LEU B CB  
3403  C CG  . LEU B 108 ? 0.2040 0.1475 0.1535 -0.0026 -0.0034 -0.0361 108 LEU B CG  
3404  C CD1 . LEU B 108 ? 0.2565 0.1551 0.1705 -0.0156 -0.0200 -0.0515 108 LEU B CD1 
3405  C CD2 . LEU B 108 ? 0.1944 0.1343 0.1592 0.0177  0.0096  -0.0410 108 LEU B CD2 
3406  N N   . ASP B 109 ? 0.1151 0.1595 0.1284 -0.0078 -0.0017 0.0124  109 ASP B N   
3407  C CA  . ASP B 109 ? 0.0987 0.1770 0.1278 -0.0052 -0.0030 0.0214  109 ASP B CA  
3408  C C   . ASP B 109 ? 0.0912 0.1561 0.1283 0.0177  0.0095  0.0263  109 ASP B C   
3409  O O   . ASP B 109 ? 0.0817 0.1569 0.1297 0.0219  0.0108  0.0273  109 ASP B O   
3410  C CB  . ASP B 109 ? 0.1054 0.2414 0.1308 -0.0062 -0.0116 0.0286  109 ASP B CB  
3411  C CG  . ASP B 109 ? 0.1219 0.2729 0.1371 -0.0414 -0.0268 0.0231  109 ASP B CG  
3412  O OD1 . ASP B 109 ? 0.1286 0.2486 0.1413 -0.0635 -0.0313 0.0184  109 ASP B OD1 
3413  O OD2 . ASP B 109 ? 0.1372 0.3279 0.1420 -0.0485 -0.0358 0.0241  109 ASP B OD2 
3414  N N   . PHE B 110 ? 0.1053 0.1439 0.1311 0.0294  0.0186  0.0291  110 PHE B N   
3415  C CA  . PHE B 110 ? 0.1171 0.1234 0.1399 0.0420  0.0296  0.0331  110 PHE B CA  
3416  C C   . PHE B 110 ? 0.1019 0.0895 0.1403 0.0291  0.0325  0.0232  110 PHE B C   
3417  O O   . PHE B 110 ? 0.1051 0.0820 0.1461 0.0340  0.0348  0.0214  110 PHE B O   
3418  C CB  . PHE B 110 ? 0.1451 0.1258 0.1474 0.0452  0.0383  0.0408  110 PHE B CB  
3419  C CG  . PHE B 110 ? 0.1759 0.1094 0.1652 0.0473  0.0490  0.0465  110 PHE B CG  
3420  C CD1 . PHE B 110 ? 0.2066 0.1145 0.1799 0.0683  0.0489  0.0524  110 PHE B CD1 
3421  C CD2 . PHE B 110 ? 0.1853 0.0999 0.1734 0.0277  0.0590  0.0455  110 PHE B CD2 
3422  C CE1 . PHE B 110 ? 0.2548 0.0997 0.2042 0.0657  0.0570  0.0561  110 PHE B CE1 
3423  C CE2 . PHE B 110 ? 0.2257 0.0934 0.1965 0.0184  0.0677  0.0514  110 PHE B CE2 
3424  C CZ  . PHE B 110 ? 0.2653 0.0883 0.2130 0.0355  0.0660  0.0564  110 PHE B CZ  
3425  N N   . HIS B 111 ? 0.0917 0.0777 0.1372 0.0163  0.0314  0.0154  111 HIS B N   
3426  C CA  . HIS B 111 ? 0.0793 0.0594 0.1402 0.0084  0.0312  0.0071  111 HIS B CA  
3427  C C   . HIS B 111 ? 0.0669 0.0577 0.1352 0.0054  0.0222  0.0064  111 HIS B C   
3428  O O   . HIS B 111 ? 0.0620 0.0503 0.1384 0.0035  0.0230  0.0030  111 HIS B O   
3429  C CB  . HIS B 111 ? 0.0802 0.0613 0.1431 0.0064  0.0297  -0.0010 111 HIS B CB  
3430  C CG  . HIS B 111 ? 0.0913 0.0769 0.1516 0.0071  0.0419  -0.0016 111 HIS B CG  
3431  N ND1 . HIS B 111 ? 0.0941 0.0832 0.1641 -0.0015 0.0517  -0.0001 111 HIS B ND1 
3432  C CD2 . HIS B 111 ? 0.1059 0.0978 0.1524 0.0114  0.0463  -0.0033 111 HIS B CD2 
3433  C CE1 . HIS B 111 ? 0.1086 0.1106 0.1728 -0.0050 0.0628  0.0017  111 HIS B CE1 
3434  N NE2 . HIS B 111 ? 0.1143 0.1194 0.1642 0.0058  0.0603  -0.0005 111 HIS B NE2 
3435  N N   . ASP B 112 ? 0.0669 0.0740 0.1298 0.0005  0.0134  0.0099  112 ASP B N   
3436  C CA  . ASP B 112 ? 0.0615 0.0877 0.1279 -0.0087 0.0060  0.0131  112 ASP B CA  
3437  C C   . ASP B 112 ? 0.0572 0.1054 0.1284 0.0045  0.0122  0.0153  112 ASP B C   
3438  O O   . ASP B 112 ? 0.0532 0.1090 0.1283 0.0023  0.0119  0.0136  112 ASP B O   
3439  C CB  . ASP B 112 ? 0.0718 0.1174 0.1286 -0.0250 -0.0041 0.0176  112 ASP B CB  
3440  C CG  . ASP B 112 ? 0.0770 0.1389 0.1322 -0.0459 -0.0123 0.0238  112 ASP B CG  
3441  O OD1 . ASP B 112 ? 0.0725 0.1251 0.1318 -0.0447 -0.0111 0.0242  112 ASP B OD1 
3442  O OD2 . ASP B 112 ? 0.0906 0.1786 0.1380 -0.0675 -0.0204 0.0292  112 ASP B OD2 
3443  N N   . SER B 113 ? 0.0672 0.1214 0.1321 0.0224  0.0176  0.0186  113 SER B N   
3444  C CA  . SER B 113 ? 0.0815 0.1420 0.1408 0.0460  0.0237  0.0184  113 SER B CA  
3445  C C   . SER B 113 ? 0.0963 0.1118 0.1496 0.0479  0.0300  0.0092  113 SER B C   
3446  O O   . SER B 113 ? 0.1062 0.1278 0.1552 0.0579  0.0318  0.0029  113 SER B O   
3447  C CB  . SER B 113 ? 0.1048 0.1634 0.1496 0.0702  0.0265  0.0258  113 SER B CB  
3448  O OG  . SER B 113 ? 0.1383 0.1764 0.1663 0.1004  0.0325  0.0240  113 SER B OG  
3449  N N   . ASN B 114 ? 0.1029 0.0803 0.1543 0.0365  0.0334  0.0072  114 ASN B N   
3450  C CA  . ASN B 114 ? 0.1233 0.0636 0.1684 0.0288  0.0381  -0.0015 114 ASN B CA  
3451  C C   . ASN B 114 ? 0.1052 0.0638 0.1639 0.0165  0.0328  -0.0103 114 ASN B C   
3452  O O   . ASN B 114 ? 0.1262 0.0674 0.1750 0.0151  0.0340  -0.0203 114 ASN B O   
3453  C CB  . ASN B 114 ? 0.1321 0.0499 0.1769 0.0127  0.0435  0.0005  114 ASN B CB  
3454  C CG  . ASN B 114 ? 0.1676 0.0542 0.1882 0.0225  0.0499  0.0115  114 ASN B CG  
3455  O OD1 . ASN B 114 ? 0.2023 0.0631 0.1995 0.0441  0.0509  0.0151  114 ASN B OD1 
3456  N ND2 . ASN B 114 ? 0.1662 0.0562 0.1884 0.0105  0.0545  0.0175  114 ASN B ND2 
3457  N N   . VAL B 115 ? 0.0773 0.0643 0.1518 0.0077  0.0255  -0.0066 115 VAL B N   
3458  C CA  . VAL B 115 ? 0.0675 0.0707 0.1496 -0.0009 0.0182  -0.0099 115 VAL B CA  
3459  C C   . VAL B 115 ? 0.0725 0.0982 0.1466 0.0053  0.0175  -0.0099 115 VAL B C   
3460  O O   . VAL B 115 ? 0.0803 0.1107 0.1500 0.0031  0.0160  -0.0172 115 VAL B O   
3461  C CB  . VAL B 115 ? 0.0561 0.0666 0.1443 -0.0077 0.0092  -0.0031 115 VAL B CB  
3462  C CG1 . VAL B 115 ? 0.0581 0.0792 0.1448 -0.0136 0.0000  -0.0006 115 VAL B CG1 
3463  C CG2 . VAL B 115 ? 0.0560 0.0553 0.1517 -0.0071 0.0107  -0.0069 115 VAL B CG2 
3464  N N   . LYS B 116 ? 0.0709 0.1206 0.1428 0.0130  0.0187  -0.0022 116 LYS B N   
3465  C CA  . LYS B 116 ? 0.0750 0.1676 0.1425 0.0204  0.0201  -0.0009 116 LYS B CA  
3466  C C   . LYS B 116 ? 0.1029 0.1825 0.1547 0.0448  0.0281  -0.0144 116 LYS B C   
3467  O O   . LYS B 116 ? 0.1127 0.2157 0.1565 0.0499  0.0297  -0.0211 116 LYS B O   
3468  C CB  . LYS B 116 ? 0.0687 0.2053 0.1410 0.0221  0.0192  0.0099  116 LYS B CB  
3469  C CG  . LYS B 116 ? 0.0645 0.2597 0.1397 0.0045  0.0155  0.0193  116 LYS B CG  
3470  C CD  . LYS B 116 ? 0.0718 0.3342 0.1474 0.0270  0.0232  0.0179  116 LYS B CD  
3471  C CE  . LYS B 116 ? 0.0705 0.3987 0.1481 0.0011  0.0215  0.0289  116 LYS B CE  
3472  N NZ  . LYS B 116 ? 0.0717 0.4955 0.1590 0.0132  0.0267  0.0336  116 LYS B NZ  
3473  N N   . ASN B 117 ? 0.1269 0.1624 0.1671 0.0602  0.0331  -0.0183 117 ASN B N   
3474  C CA  . ASN B 117 ? 0.1763 0.1730 0.1885 0.0846  0.0393  -0.0321 117 ASN B CA  
3475  C C   . ASN B 117 ? 0.1958 0.1560 0.1972 0.0667  0.0377  -0.0475 117 ASN B C   
3476  O O   . ASN B 117 ? 0.2359 0.1802 0.2120 0.0813  0.0402  -0.0636 117 ASN B O   
3477  C CB  . ASN B 117 ? 0.2125 0.1562 0.2056 0.1017  0.0433  -0.0278 117 ASN B CB  
3478  C CG  . ASN B 117 ? 0.2035 0.1928 0.2025 0.1268  0.0433  -0.0145 117 ASN B CG  
3479  O OD1 . ASN B 117 ? 0.1827 0.2444 0.1953 0.1370  0.0423  -0.0124 117 ASN B OD1 
3480  N ND2 . ASN B 117 ? 0.2229 0.1780 0.2107 0.1345  0.0441  -0.0043 117 ASN B ND2 
3481  N N   . LEU B 118 ? 0.1725 0.1258 0.1915 0.0370  0.0329  -0.0443 118 LEU B N   
3482  C CA  . LEU B 118 ? 0.1847 0.1253 0.2006 0.0158  0.0286  -0.0572 118 LEU B CA  
3483  C C   . LEU B 118 ? 0.1687 0.1570 0.1887 0.0147  0.0228  -0.0598 118 LEU B C   
3484  O O   . LEU B 118 ? 0.1965 0.1782 0.1989 0.0107  0.0206  -0.0757 118 LEU B O   
3485  C CB  . LEU B 118 ? 0.1612 0.1047 0.2001 -0.0090 0.0250  -0.0513 118 LEU B CB  
3486  C CG  . LEU B 118 ? 0.1681 0.1203 0.2122 -0.0330 0.0185  -0.0625 118 LEU B CG  
3487  C CD1 . LEU B 118 ? 0.2284 0.1313 0.2400 -0.0438 0.0207  -0.0809 118 LEU B CD1 
3488  C CD2 . LEU B 118 ? 0.1463 0.1172 0.2161 -0.0491 0.0176  -0.0555 118 LEU B CD2 
3489  N N   . TYR B 119 ? 0.1333 0.1661 0.1705 0.0146  0.0198  -0.0437 119 TYR B N   
3490  C CA  . TYR B 119 ? 0.1264 0.2026 0.1617 0.0098  0.0149  -0.0398 119 TYR B CA  
3491  C C   . TYR B 119 ? 0.1530 0.2513 0.1671 0.0303  0.0226  -0.0506 119 TYR B C   
3492  O O   . TYR B 119 ? 0.1698 0.2859 0.1688 0.0285  0.0208  -0.0597 119 TYR B O   
3493  C CB  . TYR B 119 ? 0.1002 0.2054 0.1492 -0.0008 0.0098  -0.0180 119 TYR B CB  
3494  C CG  . TYR B 119 ? 0.1050 0.2518 0.1444 -0.0104 0.0058  -0.0081 119 TYR B CG  
3495  C CD1 . TYR B 119 ? 0.1115 0.2553 0.1453 -0.0222 -0.0046 -0.0037 119 TYR B CD1 
3496  C CD2 . TYR B 119 ? 0.1078 0.3050 0.1425 -0.0075 0.0125  -0.0012 119 TYR B CD2 
3497  C CE1 . TYR B 119 ? 0.1254 0.3027 0.1433 -0.0328 -0.0084 0.0094  119 TYR B CE1 
3498  C CE2 . TYR B 119 ? 0.1182 0.3590 0.1408 -0.0221 0.0105  0.0108  119 TYR B CE2 
3499  C CZ  . TYR B 119 ? 0.1292 0.3536 0.1406 -0.0357 0.0000  0.0171  119 TYR B CZ  
3500  O OH  . TYR B 119 ? 0.1487 0.4113 0.1413 -0.0519 -0.0023 0.0331  119 TYR B OH  
3501  N N   . ASP B 120 ? 0.1617 0.2650 0.1725 0.0536  0.0309  -0.0500 120 ASP B N   
3502  C CA  . ASP B 120 ? 0.1939 0.3255 0.1837 0.0844  0.0397  -0.0621 120 ASP B CA  
3503  C C   . ASP B 120 ? 0.2522 0.3217 0.2063 0.0991  0.0419  -0.0893 120 ASP B C   
3504  O O   . ASP B 120 ? 0.2842 0.3734 0.2143 0.1154  0.0458  -0.1055 120 ASP B O   
3505  C CB  . ASP B 120 ? 0.1951 0.3515 0.1902 0.1129  0.0462  -0.0547 120 ASP B CB  
3506  C CG  . ASP B 120 ? 0.1529 0.3912 0.1754 0.0960  0.0443  -0.0323 120 ASP B CG  
3507  O OD1 . ASP B 120 ? 0.1401 0.4275 0.1664 0.0737  0.0425  -0.0245 120 ASP B OD1 
3508  O OD2 . ASP B 120 ? 0.1409 0.3933 0.1765 0.1019  0.0438  -0.0215 120 ASP B OD2 
3509  N N   . LYS B 121 ? 0.2742 0.2682 0.2206 0.0897  0.0394  -0.0948 121 LYS B N   
3510  C CA  . LYS B 121 ? 0.3439 0.2626 0.2501 0.0906  0.0391  -0.1201 121 LYS B CA  
3511  C C   . LYS B 121 ? 0.3498 0.2898 0.2476 0.0699  0.0325  -0.1350 121 LYS B C   
3512  O O   . LYS B 121 ? 0.4105 0.3258 0.2678 0.0848  0.0342  -0.1601 121 LYS B O   
3513  C CB  . LYS B 121 ? 0.3570 0.2086 0.2641 0.0646  0.0362  -0.1162 121 LYS B CB  
3514  C CG  . LYS B 121 ? 0.4453 0.2037 0.3042 0.0555  0.0352  -0.1393 121 LYS B CG  
3515  C CD  . LYS B 121 ? 0.4575 0.1632 0.3197 0.0254  0.0348  -0.1281 121 LYS B CD  
3516  C CE  . LYS B 121 ? 0.5663 0.1607 0.3696 0.0116  0.0344  -0.1464 121 LYS B CE  
3517  N NZ  . LYS B 121 ? 0.5848 0.1776 0.3849 -0.0389 0.0255  -0.1633 121 LYS B NZ  
3518  N N   . VAL B 122 ? 0.2950 0.2787 0.2262 0.0393  0.0239  -0.1200 122 VAL B N   
3519  C CA  . VAL B 122 ? 0.2965 0.3119 0.2224 0.0208  0.0149  -0.1283 122 VAL B CA  
3520  C C   . VAL B 122 ? 0.2983 0.3733 0.2114 0.0400  0.0195  -0.1280 122 VAL B C   
3521  O O   . VAL B 122 ? 0.3376 0.4191 0.2199 0.0424  0.0179  -0.1484 122 VAL B O   
3522  C CB  . VAL B 122 ? 0.2446 0.2922 0.2072 -0.0064 0.0037  -0.1083 122 VAL B CB  
3523  C CG1 . VAL B 122 ? 0.2477 0.3380 0.2034 -0.0191 -0.0076 -0.1112 122 VAL B CG1 
3524  C CG2 . VAL B 122 ? 0.2484 0.2555 0.2232 -0.0267 0.0009  -0.1117 122 VAL B CG2 
3525  N N   . ARG B 123 ? 0.2611 0.3846 0.1955 0.0502  0.0254  -0.1055 123 ARG B N   
3526  C CA  . ARG B 123 ? 0.2623 0.4584 0.1881 0.0621  0.0318  -0.1002 123 ARG B CA  
3527  C C   . ARG B 123 ? 0.3221 0.5141 0.2093 0.0989  0.0426  -0.1297 123 ARG B C   
3528  O O   . ARG B 123 ? 0.3461 0.5812 0.2096 0.1042  0.0452  -0.1403 123 ARG B O   
3529  C CB  . ARG B 123 ? 0.2233 0.4688 0.1767 0.0629  0.0369  -0.0737 123 ARG B CB  
3530  C CG  . ARG B 123 ? 0.2195 0.5551 0.1701 0.0594  0.0428  -0.0599 123 ARG B CG  
3531  C CD  . ARG B 123 ? 0.1894 0.5764 0.1662 0.0522  0.0465  -0.0355 123 ARG B CD  
3532  N NE  . ARG B 123 ? 0.1930 0.5705 0.1775 0.0856  0.0537  -0.0452 123 ARG B NE  
3533  C CZ  . ARG B 123 ? 0.2245 0.6374 0.1944 0.1295  0.0658  -0.0626 123 ARG B CZ  
3534  N NH1 . ARG B 123 ? 0.2537 0.7186 0.2008 0.1452  0.0743  -0.0757 123 ARG B NH1 
3535  N NH2 . ARG B 123 ? 0.2343 0.6300 0.2080 0.1626  0.0694  -0.0672 123 ARG B NH2 
3536  N N   . LEU B 124 ? 0.3558 0.4914 0.2308 0.1272  0.0486  -0.1428 124 LEU B N   
3537  C CA  . LEU B 124 ? 0.4308 0.5436 0.2606 0.1736  0.0584  -0.1724 124 LEU B CA  
3538  C C   . LEU B 124 ? 0.5024 0.5497 0.2835 0.1679  0.0530  -0.2066 124 LEU B C   
3539  O O   . LEU B 124 ? 0.5691 0.6136 0.3054 0.2038  0.0603  -0.2345 124 LEU B O   
3540  C CB  . LEU B 124 ? 0.4609 0.5143 0.2829 0.2076  0.0633  -0.1734 124 LEU B CB  
3541  C CG  . LEU B 124 ? 0.4088 0.5425 0.2695 0.2248  0.0695  -0.1466 124 LEU B CG  
3542  C CD1 . LEU B 124 ? 0.4274 0.4964 0.2861 0.2455  0.0692  -0.1399 124 LEU B CD1 
3543  C CD2 . LEU B 124 ? 0.4259 0.6558 0.2781 0.2677  0.0819  -0.1538 124 LEU B CD2 
3544  N N   . GLN B 125 ? 0.4952 0.4952 0.2832 0.1237  0.0400  -0.2064 125 GLN B N   
3545  C CA  . GLN B 125 ? 0.5596 0.5111 0.3056 0.1051  0.0311  -0.2374 125 GLN B CA  
3546  C C   . GLN B 125 ? 0.5434 0.5771 0.2866 0.0951  0.0274  -0.2388 125 GLN B C   
3547  O O   . GLN B 125 ? 0.6092 0.6381 0.3038 0.1115  0.0294  -0.2694 125 GLN B O   
3548  C CB  . GLN B 125 ? 0.5512 0.4530 0.3133 0.0566  0.0178  -0.2335 125 GLN B CB  
3549  C CG  . GLN B 125 ? 0.6065 0.4032 0.3472 0.0568  0.0201  -0.2407 125 GLN B CG  
3550  C CD  . GLN B 125 ? 0.5929 0.3652 0.3555 0.0035  0.0092  -0.2336 125 GLN B CD  
3551  O OE1 . GLN B 125 ? 0.6371 0.3902 0.3779 -0.0313 -0.0017 -0.2544 125 GLN B OE1 
3552  N NE2 . GLN B 125 ? 0.5356 0.3178 0.3411 -0.0038 0.0119  -0.2052 125 GLN B NE2 
3553  N N   . LEU B 126 ? 0.4664 0.5689 0.2554 0.0694  0.0214  -0.2057 126 LEU B N   
3554  C CA  . LEU B 126 ? 0.4550 0.6289 0.2394 0.0545  0.0149  -0.1992 126 LEU B CA  
3555  C C   . LEU B 126 ? 0.4734 0.7161 0.2358 0.0849  0.0295  -0.2018 126 LEU B C   
3556  O O   . LEU B 126 ? 0.5078 0.7862 0.2369 0.0844  0.0278  -0.2160 126 LEU B O   
3557  C CB  . LEU B 126 ? 0.3839 0.5985 0.2140 0.0257  0.0045  -0.1598 126 LEU B CB  
3558  C CG  . LEU B 126 ? 0.3624 0.5351 0.2191 -0.0013 -0.0094 -0.1554 126 LEU B CG  
3559  C CD1 . LEU B 126 ? 0.3121 0.5276 0.2006 -0.0181 -0.0207 -0.1204 126 LEU B CD1 
3560  C CD2 . LEU B 126 ? 0.4141 0.5563 0.2427 -0.0193 -0.0206 -0.1872 126 LEU B CD2 
3561  N N   . ARG B 127 ? 0.4540 0.7258 0.2345 0.1110  0.0438  -0.1884 127 ARG B N   
3562  C CA  . ARG B 127 ? 0.4702 0.8290 0.2359 0.1407  0.0601  -0.1895 127 ARG B CA  
3563  C C   . ARG B 127 ? 0.4478 0.8917 0.2155 0.1103  0.0566  -0.1647 127 ARG B C   
3564  O O   . ARG B 127 ? 0.3988 0.8493 0.1978 0.0742  0.0459  -0.1301 127 ARG B O   
3565  C CB  . ARG B 127 ? 0.5588 0.8837 0.2679 0.1876  0.0696  -0.2362 127 ARG B CB  
3566  C CG  . ARG B 127 ? 0.5886 0.8608 0.2935 0.2332  0.0789  -0.2486 127 ARG B CG  
3567  C CD  . ARG B 127 ? 0.6898 0.8374 0.3344 0.2593  0.0760  -0.2928 127 ARG B CD  
3568  N NE  . ARG B 127 ? 0.7829 0.9234 0.3610 0.2923  0.0816  -0.3356 127 ARG B NE  
3569  C CZ  . ARG B 127 ? 0.8035 1.0407 0.3641 0.3340  0.0976  -0.3456 127 ARG B CZ  
3570  N NH1 . ARG B 127 ? 0.7364 1.1003 0.3437 0.3449  0.1105  -0.3138 127 ARG B NH1 
3571  N NH2 . ARG B 127 ? 0.9012 1.1113 0.3926 0.3638  0.1010  -0.3905 127 ARG B NH2 
3572  N N   . ASP B 128 ? 0.4931 0.9955 0.2219 0.1256  0.0651  -0.1813 128 ASP B N   
3573  C CA  . ASP B 128 ? 0.4828 1.0664 0.2059 0.0960  0.0627  -0.1535 128 ASP B CA  
3574  C C   . ASP B 128 ? 0.5048 1.0563 0.2027 0.0702  0.0430  -0.1604 128 ASP B C   
3575  O O   . ASP B 128 ? 0.5173 1.1306 0.1939 0.0536  0.0405  -0.1439 128 ASP B O   
3576  C CB  . ASP B 128 ? 0.5178 1.2057 0.2134 0.1229  0.0839  -0.1618 128 ASP B CB  
3577  C CG  . ASP B 128 ? 0.5964 1.2621 0.2353 0.1631  0.0895  -0.2149 128 ASP B CG  
3578  O OD1 . ASP B 128 ? 0.6288 1.1880 0.2524 0.1757  0.0803  -0.2475 128 ASP B OD1 
3579  O OD2 . ASP B 128 ? 0.6350 1.3875 0.2398 0.1798  0.1033  -0.2246 128 ASP B OD2 
3580  N N   . ASN B 129 ? 0.5138 0.9766 0.2132 0.0647  0.0287  -0.1824 129 ASN B N   
3581  C CA  . ASN B 129 ? 0.5302 0.9738 0.2141 0.0375  0.0071  -0.1883 129 ASN B CA  
3582  C C   . ASN B 129 ? 0.4755 0.9197 0.1987 0.0056  -0.0103 -0.1462 129 ASN B C   
3583  O O   . ASN B 129 ? 0.4860 0.9289 0.2018 -0.0127 -0.0298 -0.1467 129 ASN B O   
3584  C CB  . ASN B 129 ? 0.5772 0.9346 0.2407 0.0391  -0.0009 -0.2329 129 ASN B CB  
3585  C CG  . ASN B 129 ? 0.6655 1.0111 0.2651 0.0660  0.0074  -0.2812 129 ASN B CG  
3586  O OD1 . ASN B 129 ? 0.6866 1.0909 0.2637 0.0958  0.0249  -0.2848 129 ASN B OD1 
3587  N ND2 . ASN B 129 ? 0.7267 0.9974 0.2933 0.0540  -0.0050 -0.3201 129 ASN B ND2 
3588  N N   . ALA B 130 ? 0.4253 0.8731 0.1864 0.0016  -0.0045 -0.1119 130 ALA B N   
3589  C CA  . ALA B 130 ? 0.3882 0.8272 0.1772 -0.0216 -0.0200 -0.0725 130 ALA B CA  
3590  C C   . ALA B 130 ? 0.3659 0.8350 0.1675 -0.0309 -0.0110 -0.0329 130 ALA B C   
3591  O O   . ALA B 130 ? 0.3622 0.8612 0.1677 -0.0195 0.0074  -0.0372 130 ALA B O   
3592  C CB  . ALA B 130 ? 0.3585 0.7331 0.1832 -0.0244 -0.0284 -0.0800 130 ALA B CB  
3593  N N   . LYS B 131 ? 0.3608 0.8215 0.1652 -0.0513 -0.0252 0.0050  131 LYS B N   
3594  C CA  . LYS B 131 ? 0.3545 0.8255 0.1638 -0.0707 -0.0204 0.0443  131 LYS B CA  
3595  C C   . LYS B 131 ? 0.3159 0.7323 0.1639 -0.0715 -0.0214 0.0489  131 LYS B C   
3596  O O   . LYS B 131 ? 0.3037 0.6668 0.1671 -0.0678 -0.0358 0.0483  131 LYS B O   
3597  C CB  . LYS B 131 ? 0.3910 0.8555 0.1710 -0.0918 -0.0372 0.0845  131 LYS B CB  
3598  C CG  . LYS B 131 ? 0.4367 0.9603 0.1713 -0.0962 -0.0374 0.0897  131 LYS B CG  
3599  C CD  . LYS B 131 ? 0.4819 0.9799 0.1837 -0.1106 -0.0592 0.1308  131 LYS B CD  
3600  C CE  . LYS B 131 ? 0.5378 1.0965 0.1869 -0.1282 -0.0556 0.1558  131 LYS B CE  
3601  N NZ  . LYS B 131 ? 0.5526 1.1454 0.1920 -0.1599 -0.0376 0.1852  131 LYS B NZ  
3602  N N   . GLU B 132 ? 0.2986 0.7381 0.1621 -0.0751 -0.0063 0.0531  132 GLU B N   
3603  C CA  . GLU B 132 ? 0.2690 0.6634 0.1628 -0.0802 -0.0080 0.0610  132 GLU B CA  
3604  C C   . GLU B 132 ? 0.2934 0.6564 0.1728 -0.1115 -0.0210 0.1009  132 GLU B C   
3605  O O   . GLU B 132 ? 0.3152 0.7139 0.1797 -0.1397 -0.0156 0.1260  132 GLU B O   
3606  C CB  . GLU B 132 ? 0.2490 0.6888 0.1616 -0.0725 0.0100  0.0521  132 GLU B CB  
3607  C CG  . GLU B 132 ? 0.2186 0.6147 0.1617 -0.0721 0.0083  0.0526  132 GLU B CG  
3608  C CD  . GLU B 132 ? 0.2011 0.6456 0.1629 -0.0540 0.0241  0.0399  132 GLU B CD  
3609  O OE1 . GLU B 132 ? 0.2130 0.7394 0.1670 -0.0491 0.0371  0.0393  132 GLU B OE1 
3610  O OE2 . GLU B 132 ? 0.1793 0.5859 0.1626 -0.0417 0.0236  0.0311  132 GLU B OE2 
3611  N N   . LEU B 133 ? 0.2997 0.5954 0.1793 -0.1065 -0.0384 0.1066  133 LEU B N   
3612  C CA  . LEU B 133 ? 0.3450 0.5879 0.1971 -0.1271 -0.0542 0.1426  133 LEU B CA  
3613  C C   . LEU B 133 ? 0.3517 0.5603 0.2076 -0.1513 -0.0527 0.1580  133 LEU B C   
3614  O O   . LEU B 133 ? 0.4082 0.5819 0.2281 -0.1818 -0.0615 0.1905  133 LEU B O   
3615  C CB  . LEU B 133 ? 0.3549 0.5420 0.2065 -0.1032 -0.0733 0.1405  133 LEU B CB  
3616  C CG  . LEU B 133 ? 0.3922 0.5948 0.2132 -0.0946 -0.0870 0.1509  133 LEU B CG  
3617  C CD1 . LEU B 133 ? 0.3839 0.6636 0.1974 -0.0971 -0.0753 0.1353  133 LEU B CD1 
3618  C CD2 . LEU B 133 ? 0.3817 0.5636 0.2209 -0.0636 -0.1023 0.1362  133 LEU B CD2 
3619  N N   . GLY B 134 ? 0.3043 0.5173 0.1973 -0.1403 -0.0433 0.1355  134 GLY B N   
3620  C CA  . GLY B 134 ? 0.3090 0.4997 0.2070 -0.1635 -0.0426 0.1454  134 GLY B CA  
3621  C C   . GLY B 134 ? 0.3090 0.4184 0.2150 -0.1500 -0.0535 0.1386  134 GLY B C   
3622  O O   . GLY B 134 ? 0.3182 0.4017 0.2242 -0.1683 -0.0548 0.1430  134 GLY B O   
3623  N N   . ASN B 135 ? 0.3015 0.3800 0.2140 -0.1184 -0.0613 0.1265  135 ASN B N   
3624  C CA  . ASN B 135 ? 0.3086 0.3200 0.2257 -0.0999 -0.0713 0.1205  135 ASN B CA  
3625  C C   . ASN B 135 ? 0.2508 0.2809 0.2088 -0.0705 -0.0640 0.0908  135 ASN B C   
3626  O O   . ASN B 135 ? 0.2522 0.2462 0.2179 -0.0506 -0.0705 0.0837  135 ASN B O   
3627  C CB  . ASN B 135 ? 0.3708 0.3280 0.2527 -0.0880 -0.0903 0.1387  135 ASN B CB  
3628  C CG  . ASN B 135 ? 0.3652 0.3680 0.2491 -0.0709 -0.0937 0.1358  135 ASN B CG  
3629  O OD1 . ASN B 135 ? 0.3149 0.3779 0.2277 -0.0655 -0.0823 0.1140  135 ASN B OD1 
3630  N ND2 . ASN B 135 ? 0.4286 0.3978 0.2754 -0.0621 -0.1109 0.1577  135 ASN B ND2 
3631  N N   . GLY B 136 ? 0.2091 0.2934 0.1882 -0.0679 -0.0504 0.0739  136 GLY B N   
3632  C CA  . GLY B 136 ? 0.1711 0.2652 0.1789 -0.0480 -0.0437 0.0480  136 GLY B CA  
3633  C C   . GLY B 136 ? 0.1716 0.2932 0.1780 -0.0398 -0.0474 0.0369  136 GLY B C   
3634  O O   . GLY B 136 ? 0.1527 0.2830 0.1760 -0.0325 -0.0421 0.0146  136 GLY B O   
3635  N N   . CYS B 137 ? 0.2012 0.3340 0.1821 -0.0450 -0.0574 0.0530  137 CYS B N   
3636  C CA  . CYS B 137 ? 0.2098 0.3733 0.1843 -0.0385 -0.0647 0.0439  137 CYS B CA  
3637  C C   . CYS B 137 ? 0.2195 0.4256 0.1741 -0.0467 -0.0565 0.0385  137 CYS B C   
3638  O O   . CYS B 137 ? 0.2306 0.4513 0.1691 -0.0592 -0.0494 0.0543  137 CYS B O   
3639  C CB  . CYS B 137 ? 0.2463 0.3963 0.2011 -0.0304 -0.0844 0.0656  137 CYS B CB  
3640  S SG  . CYS B 137 ? 0.2483 0.3566 0.2216 -0.0072 -0.0949 0.0674  137 CYS B SG  
3641  N N   . PHE B 138 ? 0.2209 0.4510 0.1749 -0.0415 -0.0574 0.0144  138 PHE B N   
3642  C CA  . PHE B 138 ? 0.2415 0.5108 0.1697 -0.0435 -0.0512 0.0028  138 PHE B CA  
3643  C C   . PHE B 138 ? 0.2695 0.5643 0.1782 -0.0444 -0.0681 0.0040  138 PHE B C   
3644  O O   . PHE B 138 ? 0.2659 0.5599 0.1893 -0.0418 -0.0789 -0.0103 138 PHE B O   
3645  C CB  . PHE B 138 ? 0.2372 0.4996 0.1701 -0.0358 -0.0384 -0.0328 138 PHE B CB  
3646  C CG  . PHE B 138 ? 0.2176 0.4638 0.1646 -0.0282 -0.0224 -0.0336 138 PHE B CG  
3647  C CD1 . PHE B 138 ? 0.2248 0.5083 0.1584 -0.0223 -0.0090 -0.0300 138 PHE B CD1 
3648  C CD2 . PHE B 138 ? 0.1938 0.3990 0.1674 -0.0260 -0.0208 -0.0371 138 PHE B CD2 
3649  C CE1 . PHE B 138 ? 0.2086 0.4913 0.1571 -0.0120 0.0036  -0.0302 138 PHE B CE1 
3650  C CE2 . PHE B 138 ? 0.1801 0.3750 0.1637 -0.0171 -0.0081 -0.0364 138 PHE B CE2 
3651  C CZ  . PHE B 138 ? 0.1870 0.4220 0.1592 -0.0089 0.0030  -0.0330 138 PHE B CZ  
3652  N N   . GLU B 139 ? 0.3010 0.6268 0.1760 -0.0501 -0.0704 0.0226  139 GLU B N   
3653  C CA  . GLU B 139 ? 0.3352 0.6901 0.1846 -0.0495 -0.0880 0.0293  139 GLU B CA  
3654  C C   . GLU B 139 ? 0.3587 0.7580 0.1806 -0.0511 -0.0815 0.0015  139 GLU B C   
3655  O O   . GLU B 139 ? 0.3718 0.7972 0.1718 -0.0536 -0.0662 0.0035  139 GLU B O   
3656  C CB  . GLU B 139 ? 0.3707 0.7196 0.1900 -0.0560 -0.0967 0.0741  139 GLU B CB  
3657  C CG  . GLU B 139 ? 0.4134 0.7823 0.2036 -0.0490 -0.1193 0.0905  139 GLU B CG  
3658  C CD  . GLU B 139 ? 0.4680 0.8241 0.2121 -0.0600 -0.1247 0.1367  139 GLU B CD  
3659  O OE1 . GLU B 139 ? 0.4883 0.7836 0.2278 -0.0595 -0.1322 0.1660  139 GLU B OE1 
3660  O OE2 . GLU B 139 ? 0.4997 0.9022 0.2069 -0.0714 -0.1208 0.1433  139 GLU B OE2 
3661  N N   . PHE B 140 ? 0.3706 0.7836 0.1912 -0.0505 -0.0936 -0.0256 140 PHE B N   
3662  C CA  . PHE B 140 ? 0.4033 0.8410 0.1934 -0.0524 -0.0884 -0.0626 140 PHE B CA  
3663  C C   . PHE B 140 ? 0.4474 0.9393 0.1907 -0.0540 -0.0942 -0.0510 140 PHE B C   
3664  O O   . PHE B 140 ? 0.4611 0.9734 0.1950 -0.0556 -0.1126 -0.0208 140 PHE B O   
3665  C CB  . PHE B 140 ? 0.4108 0.8414 0.2114 -0.0614 -0.1017 -0.0966 140 PHE B CB  
3666  C CG  . PHE B 140 ? 0.3816 0.7600 0.2183 -0.0645 -0.0932 -0.1120 140 PHE B CG  
3667  C CD1 . PHE B 140 ? 0.3431 0.7109 0.2222 -0.0645 -0.1002 -0.0920 140 PHE B CD1 
3668  C CD2 . PHE B 140 ? 0.4027 0.7392 0.2250 -0.0639 -0.0779 -0.1461 140 PHE B CD2 
3669  C CE1 . PHE B 140 ? 0.3200 0.6453 0.2288 -0.0692 -0.0911 -0.1042 140 PHE B CE1 
3670  C CE2 . PHE B 140 ? 0.3864 0.6692 0.2346 -0.0679 -0.0705 -0.1560 140 PHE B CE2 
3671  C CZ  . PHE B 140 ? 0.3418 0.6235 0.2347 -0.0732 -0.0766 -0.1342 140 PHE B CZ  
3672  N N   . TYR B 141 ? 0.4782 0.9935 0.1878 -0.0496 -0.0787 -0.0751 141 TYR B N   
3673  C CA  . TYR B 141 ? 0.5277 1.1023 0.1869 -0.0514 -0.0824 -0.0707 141 TYR B CA  
3674  C C   . TYR B 141 ? 0.5639 1.1559 0.2015 -0.0576 -0.1040 -0.0995 141 TYR B C   
3675  O O   . TYR B 141 ? 0.5973 1.2374 0.2029 -0.0616 -0.1194 -0.0832 141 TYR B O   
3676  C CB  . TYR B 141 ? 0.5528 1.1573 0.1814 -0.0395 -0.0568 -0.0911 141 TYR B CB  
3677  C CG  . TYR B 141 ? 0.5245 1.1418 0.1715 -0.0389 -0.0370 -0.0587 141 TYR B CG  
3678  C CD1 . TYR B 141 ? 0.5255 1.1661 0.1670 -0.0573 -0.0415 -0.0061 141 TYR B CD1 
3679  C CD2 . TYR B 141 ? 0.5061 1.1096 0.1724 -0.0218 -0.0157 -0.0793 141 TYR B CD2 
3680  C CE1 . TYR B 141 ? 0.5078 1.1620 0.1636 -0.0671 -0.0251 0.0230  141 TYR B CE1 
3681  C CE2 . TYR B 141 ? 0.4805 1.1108 0.1667 -0.0250 0.0004  -0.0502 141 TYR B CE2 
3682  C CZ  . TYR B 141 ? 0.4807 1.1384 0.1625 -0.0519 -0.0042 0.0000  141 TYR B CZ  
3683  O OH  . TYR B 141 ? 0.4631 1.1496 0.1621 -0.0649 0.0104  0.0282  141 TYR B OH  
3684  N N   . HIS B 142 ? 0.5654 1.1181 0.2172 -0.0617 -0.1058 -0.1413 142 HIS B N   
3685  C CA  . HIS B 142 ? 0.6014 1.1687 0.2382 -0.0776 -0.1279 -0.1722 142 HIS B CA  
3686  C C   . HIS B 142 ? 0.5638 1.1321 0.2501 -0.0879 -0.1481 -0.1543 142 HIS B C   
3687  O O   . HIS B 142 ? 0.5145 1.0503 0.2444 -0.0811 -0.1413 -0.1305 142 HIS B O   
3688  C CB  . HIS B 142 ? 0.6439 1.1599 0.2578 -0.0834 -0.1191 -0.2293 142 HIS B CB  
3689  C CG  . HIS B 142 ? 0.6124 1.0551 0.2636 -0.0812 -0.1050 -0.2358 142 HIS B CG  
3690  N ND1 . HIS B 142 ? 0.6042 1.0122 0.2852 -0.1044 -0.1161 -0.2487 142 HIS B ND1 
3691  C CD2 . HIS B 142 ? 0.5906 0.9965 0.2532 -0.0593 -0.0811 -0.2290 142 HIS B CD2 
3692  C CE1 . HIS B 142 ? 0.5813 0.9257 0.2859 -0.0964 -0.0992 -0.2488 142 HIS B CE1 
3693  N NE2 . HIS B 142 ? 0.5717 0.9138 0.2663 -0.0672 -0.0789 -0.2374 142 HIS B NE2 
3694  N N   . LYS B 143 ? 0.5914 1.2058 0.2699 -0.1029 -0.1732 -0.1673 143 LYS B N   
3695  C CA  . LYS B 143 ? 0.5625 1.1975 0.2893 -0.1116 -0.1925 -0.1583 143 LYS B CA  
3696  C C   . LYS B 143 ? 0.5519 1.1320 0.3056 -0.1325 -0.1822 -0.1916 143 LYS B C   
3697  O O   . LYS B 143 ? 0.5993 1.1451 0.3191 -0.1513 -0.1768 -0.2343 143 LYS B O   
3698  C CB  . LYS B 143 ? 0.6010 1.3166 0.3107 -0.1242 -0.2226 -0.1671 143 LYS B CB  
3699  C CG  . LYS B 143 ? 0.5726 1.3423 0.3322 -0.1205 -0.2452 -0.1461 143 LYS B CG  
3700  C CD  . LYS B 143 ? 0.6157 1.4804 0.3574 -0.1339 -0.2766 -0.1585 143 LYS B CD  
3701  C CE  . LYS B 143 ? 0.5913 1.5259 0.3895 -0.1370 -0.2976 -0.1529 143 LYS B CE  
3702  N NZ  . LYS B 143 ? 0.5797 1.4954 0.4113 -0.1782 -0.2898 -0.1901 143 LYS B NZ  
3703  N N   . CYS B 144 ? 0.5008 1.0655 0.3081 -0.1282 -0.1794 -0.1717 144 CYS B N   
3704  C CA  . CYS B 144 ? 0.4906 0.9992 0.3226 -0.1478 -0.1671 -0.1945 144 CYS B CA  
3705  C C   . CYS B 144 ? 0.4693 1.0279 0.3490 -0.1668 -0.1833 -0.1924 144 CYS B C   
3706  O O   . CYS B 144 ? 0.4216 0.9970 0.3445 -0.1466 -0.1833 -0.1622 144 CYS B O   
3707  C CB  . CYS B 144 ? 0.4494 0.8949 0.3001 -0.1249 -0.1429 -0.1739 144 CYS B CB  
3708  S SG  . CYS B 144 ? 0.4485 0.8117 0.3160 -0.1422 -0.1247 -0.1973 144 CYS B SG  
3709  N N   . ASP B 145 ? 0.5122 1.0978 0.3809 -0.2068 -0.1970 -0.2264 145 ASP B N   
3710  C CA  . ASP B 145 ? 0.4984 1.1545 0.4132 -0.2330 -0.2126 -0.2276 145 ASP B CA  
3711  C C   . ASP B 145 ? 0.4739 1.0773 0.4235 -0.2493 -0.1943 -0.2288 145 ASP B C   
3712  O O   . ASP B 145 ? 0.4648 0.9762 0.4030 -0.2350 -0.1718 -0.2260 145 ASP B O   
3713  C CB  . ASP B 145 ? 0.5608 1.2701 0.4493 -0.2808 -0.2347 -0.2640 145 ASP B CB  
3714  C CG  . ASP B 145 ? 0.6315 1.2424 0.4684 -0.3221 -0.2243 -0.3080 145 ASP B CG  
3715  O OD1 . ASP B 145 ? 0.6297 1.1372 0.4562 -0.3113 -0.2001 -0.3094 145 ASP B OD1 
3716  O OD2 . ASP B 145 ? 0.6990 1.3328 0.5004 -0.3644 -0.2420 -0.3424 145 ASP B OD2 
3717  N N   . ASN B 146 ? 0.4659 1.1371 0.4572 -0.2789 -0.2041 -0.2316 146 ASN B N   
3718  C CA  . ASN B 146 ? 0.4442 1.0809 0.4690 -0.2961 -0.1870 -0.2283 146 ASN B CA  
3719  C C   . ASN B 146 ? 0.5037 1.0277 0.4866 -0.3382 -0.1723 -0.2574 146 ASN B C   
3720  O O   . ASN B 146 ? 0.4903 0.9493 0.4842 -0.3385 -0.1529 -0.2494 146 ASN B O   
3721  C CB  . ASN B 146 ? 0.4264 1.1832 0.5057 -0.3202 -0.2003 -0.2243 146 ASN B CB  
3722  C CG  . ASN B 146 ? 0.3741 1.2280 0.4949 -0.2641 -0.2124 -0.1924 146 ASN B CG  
3723  O OD1 . ASN B 146 ? 0.3452 1.1539 0.4599 -0.2110 -0.2054 -0.1676 146 ASN B OD1 
3724  N ND2 . ASN B 146 ? 0.3715 1.3589 0.5311 -0.2758 -0.2315 -0.1927 146 ASN B ND2 
3725  N N   . GLU B 147 ? 0.5802 1.0745 0.5086 -0.3708 -0.1823 -0.2912 147 GLU B N   
3726  C CA  . GLU B 147 ? 0.6603 1.0234 0.5312 -0.4006 -0.1698 -0.3209 147 GLU B CA  
3727  C C   . GLU B 147 ? 0.6537 0.9235 0.4931 -0.3458 -0.1498 -0.3151 147 GLU B C   
3728  O O   . GLU B 147 ? 0.6760 0.8435 0.4970 -0.3415 -0.1313 -0.3174 147 GLU B O   
3729  C CB  . GLU B 147 ? 0.7594 1.1116 0.5721 -0.4507 -0.1884 -0.3635 147 GLU B CB  
3730  C CG  . GLU B 147 ? 0.7787 1.2332 0.6196 -0.5159 -0.2102 -0.3728 147 GLU B CG  
3731  C CD  . GLU B 147 ? 0.7336 1.3420 0.6087 -0.4987 -0.2341 -0.3617 147 GLU B CD  
3732  O OE1 . GLU B 147 ? 0.7895 1.4166 0.6189 -0.5121 -0.2523 -0.3877 147 GLU B OE1 
3733  O OE2 . GLU B 147 ? 0.6506 1.3577 0.5932 -0.4679 -0.2353 -0.3272 147 GLU B OE2 
3734  N N   . CYS B 148 ? 0.6280 0.9409 0.4602 -0.3047 -0.1541 -0.3058 148 CYS B N   
3735  C CA  . CYS B 148 ? 0.6109 0.8699 0.4235 -0.2535 -0.1354 -0.2946 148 CYS B CA  
3736  C C   . CYS B 148 ? 0.5417 0.7827 0.4017 -0.2263 -0.1182 -0.2603 148 CYS B C   
3737  O O   . CYS B 148 ? 0.5491 0.7131 0.3923 -0.2042 -0.0992 -0.2602 148 CYS B O   
3738  C CB  . CYS B 148 ? 0.5906 0.9207 0.3937 -0.2236 -0.1445 -0.2821 148 CYS B CB  
3739  S SG  . CYS B 148 ? 0.5529 0.8551 0.3474 -0.1677 -0.1222 -0.2568 148 CYS B SG  
3740  N N   . MET B 149 ? 0.4826 0.7975 0.3987 -0.2246 -0.1258 -0.2329 149 MET B N   
3741  C CA  . MET B 149 ? 0.4246 0.7244 0.3824 -0.2020 -0.1115 -0.2040 149 MET B CA  
3742  C C   . MET B 149 ? 0.4536 0.6824 0.4095 -0.2285 -0.0980 -0.2154 149 MET B C   
3743  O O   . MET B 149 ? 0.4346 0.6067 0.3943 -0.2070 -0.0809 -0.2026 149 MET B O   
3744  C CB  . MET B 149 ? 0.3711 0.7623 0.3814 -0.1929 -0.1238 -0.1788 149 MET B CB  
3745  C CG  . MET B 149 ? 0.3527 0.8002 0.3611 -0.1600 -0.1377 -0.1583 149 MET B CG  
3746  S SD  . MET B 149 ? 0.3298 0.7195 0.3184 -0.1191 -0.1223 -0.1334 149 MET B SD  
3747  C CE  . MET B 149 ? 0.3242 0.7804 0.3115 -0.0905 -0.1431 -0.1020 149 MET B CE  
3748  N N   . GLU B 150 ? 0.5102 0.7430 0.4562 -0.2788 -0.1070 -0.2380 150 GLU B N   
3749  C CA  . GLU B 150 ? 0.5581 0.7166 0.4923 -0.3139 -0.0959 -0.2466 150 GLU B CA  
3750  C C   . GLU B 150 ? 0.6283 0.6564 0.5007 -0.3004 -0.0823 -0.2636 150 GLU B C   
3751  O O   . GLU B 150 ? 0.6443 0.5985 0.5098 -0.2996 -0.0678 -0.2558 150 GLU B O   
3752  C CB  . GLU B 150 ? 0.6134 0.8091 0.5445 -0.3815 -0.1107 -0.2671 150 GLU B CB  
3753  C CG  . GLU B 150 ? 0.6816 0.7929 0.5886 -0.4321 -0.1011 -0.2753 150 GLU B CG  
3754  C CD  . GLU B 150 ? 0.6270 0.7419 0.5768 -0.4194 -0.0837 -0.2447 150 GLU B CD  
3755  O OE1 . GLU B 150 ? 0.5385 0.7473 0.5468 -0.3854 -0.0830 -0.2209 150 GLU B OE1 
3756  O OE2 . GLU B 150 ? 0.6841 0.7009 0.6023 -0.4422 -0.0711 -0.2447 150 GLU B OE2 
3757  N N   . SER B 151 ? 0.6781 0.6821 0.5031 -0.2852 -0.0872 -0.2863 151 SER B N   
3758  C CA  . SER B 151 ? 0.7540 0.6426 0.5164 -0.2604 -0.0745 -0.3058 151 SER B CA  
3759  C C   . SER B 151 ? 0.7005 0.5755 0.4837 -0.2042 -0.0560 -0.2793 151 SER B C   
3760  O O   . SER B 151 ? 0.7486 0.5309 0.4972 -0.1833 -0.0429 -0.2846 151 SER B O   
3761  C CB  . SER B 151 ? 0.8114 0.6967 0.5200 -0.2501 -0.0827 -0.3372 151 SER B CB  
3762  O OG  . SER B 151 ? 0.7397 0.7092 0.4732 -0.2089 -0.0818 -0.3190 151 SER B OG  
3763  N N   . VAL B 152 ? 0.6128 0.5783 0.4480 -0.1805 -0.0566 -0.2505 152 VAL B N   
3764  C CA  . VAL B 152 ? 0.5596 0.5256 0.4182 -0.1375 -0.0419 -0.2240 152 VAL B CA  
3765  C C   . VAL B 152 ? 0.5479 0.4790 0.4327 -0.1459 -0.0330 -0.2069 152 VAL B C   
3766  O O   . VAL B 152 ? 0.5534 0.4327 0.4281 -0.1189 -0.0195 -0.1997 152 VAL B O   
3767  C CB  . VAL B 152 ? 0.4810 0.5386 0.3787 -0.1188 -0.0474 -0.1971 152 VAL B CB  
3768  C CG1 . VAL B 152 ? 0.4315 0.4864 0.3487 -0.0846 -0.0337 -0.1713 152 VAL B CG1 
3769  C CG2 . VAL B 152 ? 0.5051 0.6017 0.3723 -0.1123 -0.0558 -0.2100 152 VAL B CG2 
3770  N N   . ARG B 153 ? 0.5385 0.5079 0.4565 -0.1816 -0.0406 -0.2002 153 ARG B N   
3771  C CA  . ARG B 153 ? 0.5367 0.4814 0.4761 -0.1952 -0.0314 -0.1851 153 ARG B CA  
3772  C C   . ARG B 153 ? 0.6444 0.4807 0.5314 -0.2198 -0.0252 -0.2023 153 ARG B C   
3773  O O   . ARG B 153 ? 0.6541 0.4330 0.5342 -0.2093 -0.0130 -0.1892 153 ARG B O   
3774  C CB  . ARG B 153 ? 0.4950 0.5253 0.4828 -0.2256 -0.0398 -0.1753 153 ARG B CB  
3775  C CG  . ARG B 153 ? 0.4170 0.5394 0.4483 -0.1966 -0.0480 -0.1570 153 ARG B CG  
3776  C CD  . ARG B 153 ? 0.3848 0.5936 0.4630 -0.2149 -0.0548 -0.1482 153 ARG B CD  
3777  N NE  . ARG B 153 ? 0.3639 0.6597 0.4598 -0.2053 -0.0732 -0.1471 153 ARG B NE  
3778  C CZ  . ARG B 153 ? 0.3923 0.7456 0.4875 -0.2382 -0.0886 -0.1637 153 ARG B CZ  
3779  N NH1 . ARG B 153 ? 0.4474 0.7768 0.5238 -0.2912 -0.0882 -0.1843 153 ARG B NH1 
3780  N NH2 . ARG B 153 ? 0.3749 0.8089 0.4842 -0.2202 -0.1064 -0.1584 153 ARG B NH2 
3781  N N   . ASN B 154 ? 0.7439 0.5478 0.5885 -0.2536 -0.0354 -0.2311 154 ASN B N   
3782  C CA  . ASN B 154 ? 0.8797 0.5545 0.6538 -0.2753 -0.0325 -0.2524 154 ASN B CA  
3783  C C   . ASN B 154 ? 0.9046 0.4867 0.6386 -0.2197 -0.0189 -0.2510 154 ASN B C   
3784  O O   . ASN B 154 ? 0.9744 0.4560 0.6711 -0.2244 -0.0115 -0.2472 154 ASN B O   
3785  C CB  . ASN B 154 ? 0.9889 0.6386 0.7113 -0.3028 -0.0469 -0.2901 154 ASN B CB  
3786  C CG  . ASN B 154 ? 1.0754 0.7411 0.7957 -0.3814 -0.0602 -0.3017 154 ASN B CG  
3787  O OD1 . ASN B 154 ? 1.0544 0.7525 0.8118 -0.4162 -0.0567 -0.2810 154 ASN B OD1 
3788  N ND2 . ASN B 154 ? 1.2030 0.8533 0.8776 -0.4120 -0.0755 -0.3364 154 ASN B ND2 
3789  N N   . GLY B 155 ? 0.8491 0.4722 0.5897 -0.1675 -0.0160 -0.2523 155 GLY B N   
3790  C CA  . GLY B 155 ? 0.8858 0.4407 0.5821 -0.1111 -0.0054 -0.2602 155 GLY B CA  
3791  C C   . GLY B 155 ? 0.9732 0.4766 0.6023 -0.1028 -0.0108 -0.2998 155 GLY B C   
3792  O O   . GLY B 155 ? 1.0324 0.4764 0.6141 -0.0520 -0.0025 -0.3139 155 GLY B O   
3793  N N   . THR B 156 ? 0.9821 0.5170 0.6067 -0.1494 -0.0252 -0.3188 156 THR B N   
3794  C CA  . THR B 156 ? 1.0872 0.5613 0.6384 -0.1564 -0.0336 -0.3619 156 THR B CA  
3795  C C   . THR B 156 ? 1.0356 0.6150 0.6001 -0.1403 -0.0395 -0.3719 156 THR B C   
3796  O O   . THR B 156 ? 1.1099 0.6727 0.6257 -0.1606 -0.0510 -0.4065 156 THR B O   
3797  C CB  . THR B 156 ? 1.1673 0.5897 0.6901 -0.2343 -0.0487 -0.3803 156 THR B CB  
3798  O OG1 . THR B 156 ? 1.2056 0.5429 0.7208 -0.2582 -0.0425 -0.3631 156 THR B OG1 
3799  C CG2 . THR B 156 ? 1.3142 0.6381 0.7425 -0.2460 -0.0583 -0.4300 156 THR B CG2 
3800  N N   . TYR B 157 ? 0.9189 0.6020 0.5425 -0.1069 -0.0326 -0.3413 157 TYR B N   
3801  C CA  . TYR B 157 ? 0.8743 0.6569 0.5078 -0.0944 -0.0377 -0.3431 157 TYR B CA  
3802  C C   . TYR B 157 ? 0.9635 0.7055 0.5252 -0.0580 -0.0322 -0.3799 157 TYR B C   
3803  O O   . TYR B 157 ? 0.9754 0.6951 0.5212 -0.0048 -0.0159 -0.3795 157 TYR B O   
3804  C CB  . TYR B 157 ? 0.7578 0.6348 0.4540 -0.0653 -0.0295 -0.3020 157 TYR B CB  
3805  C CG  . TYR B 157 ? 0.7259 0.6965 0.4236 -0.0536 -0.0337 -0.2981 157 TYR B CG  
3806  C CD1 . TYR B 157 ? 0.7003 0.7382 0.4162 -0.0863 -0.0519 -0.2926 157 TYR B CD1 
3807  C CD2 . TYR B 157 ? 0.7276 0.7267 0.4066 -0.0094 -0.0195 -0.2984 157 TYR B CD2 
3808  C CE1 . TYR B 157 ? 0.6830 0.8005 0.3926 -0.0757 -0.0566 -0.2850 157 TYR B CE1 
3809  C CE2 . TYR B 157 ? 0.7078 0.7937 0.3830 -0.0038 -0.0221 -0.2913 157 TYR B CE2 
3810  C CZ  . TYR B 157 ? 0.6881 0.8263 0.3758 -0.0373 -0.0410 -0.2836 157 TYR B CZ  
3811  O OH  . TYR B 157 ? 0.6780 0.8966 0.3546 -0.0316 -0.0444 -0.2728 157 TYR B OH  
3812  N N   . ASP B 158 ? 1.0293 0.7701 0.5470 -0.0847 -0.0462 -0.4131 158 ASP B N   
3813  C CA  . ASP B 158 ? 1.1344 0.8277 0.5725 -0.0518 -0.0420 -0.4558 158 ASP B CA  
3814  C C   . ASP B 158 ? 1.0801 0.8860 0.5309 -0.0095 -0.0327 -0.4453 158 ASP B C   
3815  O O   . ASP B 158 ? 1.0755 0.9558 0.5197 -0.0274 -0.0439 -0.4519 158 ASP B O   
3816  C CB  . ASP B 158 ? 1.2377 0.8831 0.6160 -0.1016 -0.0619 -0.4987 158 ASP B CB  
3817  C CG  . ASP B 158 ? 1.3837 0.9264 0.6608 -0.0685 -0.0575 -0.5512 158 ASP B CG  
3818  O OD1 . ASP B 158 ? 1.4619 0.8831 0.6965 -0.0374 -0.0466 -0.5626 158 ASP B OD1 
3819  O OD2 . ASP B 158 ? 1.4294 1.0095 0.6641 -0.0697 -0.0653 -0.5816 158 ASP B OD2 
3820  N N   . TYR B 159 ? 1.0450 0.8680 0.5120 0.0440  -0.0126 -0.4274 159 TYR B N   
3821  C CA  . TYR B 159 ? 0.9927 0.9287 0.4740 0.0804  -0.0003 -0.4122 159 TYR B CA  
3822  C C   . TYR B 159 ? 1.0752 1.0318 0.4882 0.0952  -0.0011 -0.4524 159 TYR B C   
3823  O O   . TYR B 159 ? 1.0340 1.0922 0.4594 0.0817  -0.0058 -0.4386 159 TYR B O   
3824  C CB  . TYR B 159 ? 0.9664 0.9120 0.4659 0.1353  0.0213  -0.3954 159 TYR B CB  
3825  C CG  . TYR B 159 ? 0.9365 0.9986 0.4399 0.1728  0.0370  -0.3857 159 TYR B CG  
3826  C CD1 . TYR B 159 ? 1.0253 1.0885 0.4646 0.2221  0.0493  -0.4247 159 TYR B CD1 
3827  C CD2 . TYR B 159 ? 0.8292 0.9993 0.3956 0.1578  0.0400  -0.3379 159 TYR B CD2 
3828  C CE1 . TYR B 159 ? 0.9996 1.1864 0.4440 0.2534  0.0659  -0.4145 159 TYR B CE1 
3829  C CE2 . TYR B 159 ? 0.8099 1.0906 0.3776 0.1820  0.0549  -0.3257 159 TYR B CE2 
3830  C CZ  . TYR B 159 ? 0.8913 1.1891 0.4013 0.2289  0.0687  -0.3632 159 TYR B CZ  
3831  O OH  . TYR B 159 ? 0.8748 1.2985 0.3870 0.2508  0.0858  -0.3504 159 TYR B OH  
3832  N N   . PRO B 160 ? 1.2028 1.0566 0.5367 0.1236  0.0026  -0.5023 160 PRO B N   
3833  C CA  . PRO B 160 ? 1.2954 1.1618 0.5548 0.1413  0.0022  -0.5470 160 PRO B CA  
3834  C C   . PRO B 160 ? 1.3034 1.2101 0.5500 0.0836  -0.0207 -0.5580 160 PRO B C   
3835  O O   . PRO B 160 ? 1.3438 1.3105 0.5471 0.0973  -0.0197 -0.5798 160 PRO B O   
3836  C CB  . PRO B 160 ? 1.4467 1.1544 0.6191 0.1714  0.0044  -0.5993 160 PRO B CB  
3837  C CG  . PRO B 160 ? 1.4177 1.0743 0.6237 0.2029  0.0168  -0.5734 160 PRO B CG  
3838  C CD  . PRO B 160 ? 1.2778 0.9974 0.5794 0.1507  0.0091  -0.5189 160 PRO B CD  
3839  N N   . GLN B 161 ? 1.2715 1.1548 0.5535 0.0221  -0.0412 -0.5440 161 GLN B N   
3840  C CA  . GLN B 161 ? 1.2747 1.2120 0.5520 -0.0320 -0.0658 -0.5514 161 GLN B CA  
3841  C C   . GLN B 161 ? 1.1645 1.2503 0.4977 -0.0326 -0.0675 -0.5052 161 GLN B C   
3842  O O   . GLN B 161 ? 1.1879 1.3428 0.4908 -0.0413 -0.0780 -0.5158 161 GLN B O   
3843  C CB  . GLN B 161 ? 1.2727 1.1586 0.5766 -0.0963 -0.0862 -0.5484 161 GLN B CB  
3844  C CG  . GLN B 161 ? 1.2644 1.2280 0.5766 -0.1523 -0.1139 -0.5511 161 GLN B CG  
3845  C CD  . GLN B 161 ? 1.2488 1.1909 0.6008 -0.2146 -0.1314 -0.5423 161 GLN B CD  
3846  O OE1 . GLN B 161 ? 1.1918 1.1045 0.5948 -0.2145 -0.1218 -0.5130 161 GLN B OE1 
3847  N NE2 . GLN B 161 ? 1.3014 1.2692 0.6304 -0.2697 -0.1571 -0.5677 161 GLN B NE2 
3848  N N   . TYR B 162 ? 1.0556 1.1822 0.4634 -0.0243 -0.0585 -0.4538 162 TYR B N   
3849  C CA  . TYR B 162 ? 0.9635 1.2071 0.4200 -0.0277 -0.0614 -0.4049 162 TYR B CA  
3850  C C   . TYR B 162 ? 0.9485 1.2589 0.3960 0.0159  -0.0385 -0.3889 162 TYR B C   
3851  O O   . TYR B 162 ? 0.8828 1.2769 0.3653 0.0122  -0.0380 -0.3432 162 TYR B O   
3852  C CB  . TYR B 162 ? 0.8668 1.1148 0.4019 -0.0457 -0.0656 -0.3593 162 TYR B CB  
3853  C CG  . TYR B 162 ? 0.8739 1.0833 0.4270 -0.0910 -0.0862 -0.3694 162 TYR B CG  
3854  C CD1 . TYR B 162 ? 0.8706 1.1442 0.4298 -0.1249 -0.1111 -0.3665 162 TYR B CD1 
3855  C CD2 . TYR B 162 ? 0.8881 1.0059 0.4515 -0.1007 -0.0810 -0.3797 162 TYR B CD2 
3856  C CE1 . TYR B 162 ? 0.8772 1.1373 0.4578 -0.1688 -0.1295 -0.3754 162 TYR B CE1 
3857  C CE2 . TYR B 162 ? 0.8981 0.9928 0.4784 -0.1488 -0.0980 -0.3868 162 TYR B CE2 
3858  C CZ  . TYR B 162 ? 0.8902 1.0624 0.4819 -0.1836 -0.1218 -0.3855 162 TYR B CZ  
3859  O OH  . TYR B 162 ? 0.8991 1.0691 0.5124 -0.2336 -0.1382 -0.3923 162 TYR B OH  
3860  N N   . SER B 163 ? 1.0196 1.2929 0.4169 0.0571  -0.0199 -0.4256 163 SER B N   
3861  C CA  . SER B 163 ? 1.0140 1.3670 0.4007 0.1004  0.0040  -0.4157 163 SER B CA  
3862  C C   . SER B 163 ? 1.0994 1.4928 0.4111 0.1142  0.0051  -0.4539 163 SER B C   
3863  O O   . SER B 163 ? 1.1255 1.5785 0.4098 0.1564  0.0273  -0.4621 163 SER B O   
3864  C CB  . SER B 163 ? 1.0310 1.3343 0.4188 0.1496  0.0264  -0.4278 163 SER B CB  
3865  O OG  . SER B 163 ? 1.1512 1.3865 0.4612 0.1877  0.0330  -0.4867 163 SER B OG  
3866  N N   . ASP C 1   ? 0.7718 0.2479 0.3110 0.2726  0.1652  -0.0263 1   ASP C N   
3867  C CA  . ASP C 1   ? 0.7477 0.2747 0.3144 0.2891  0.1717  -0.0209 1   ASP C CA  
3868  C C   . ASP C 1   ? 0.6795 0.2565 0.3080 0.2557  0.1670  -0.0185 1   ASP C C   
3869  O O   . ASP C 1   ? 0.6406 0.2408 0.3010 0.2296  0.1643  -0.0197 1   ASP C O   
3870  C CB  . ASP C 1   ? 0.7413 0.3299 0.3191 0.3212  0.1868  -0.0170 1   ASP C CB  
3871  C CG  . ASP C 1   ? 0.8124 0.3560 0.3264 0.3613  0.1925  -0.0195 1   ASP C CG  
3872  O OD1 . ASP C 1   ? 0.8718 0.3271 0.3275 0.3636  0.1839  -0.0242 1   ASP C OD1 
3873  O OD2 . ASP C 1   ? 0.8126 0.4100 0.3317 0.3900  0.2053  -0.0165 1   ASP C OD2 
3874  N N   . GLN C 2   ? 0.6704 0.2597 0.3106 0.2589  0.1657  -0.0153 2   GLN C N   
3875  C CA  . GLN C 2   ? 0.6113 0.2445 0.3052 0.2304  0.1611  -0.0131 2   GLN C CA  
3876  C C   . GLN C 2   ? 0.5958 0.2674 0.3092 0.2445  0.1652  -0.0079 2   GLN C C   
3877  O O   . GLN C 2   ? 0.6391 0.2837 0.3161 0.2729  0.1673  -0.0069 2   GLN C O   
3878  C CB  . GLN C 2   ? 0.6139 0.2029 0.3010 0.1994  0.1476  -0.0170 2   GLN C CB  
3879  C CG  . GLN C 2   ? 0.6617 0.1934 0.3061 0.2036  0.1413  -0.0171 2   GLN C CG  
3880  C CD  . GLN C 2   ? 0.6538 0.1644 0.3027 0.1670  0.1286  -0.0192 2   GLN C CD  
3881  O OE1 . GLN C 2   ? 0.6626 0.1598 0.3050 0.1604  0.1241  -0.0172 2   GLN C OE1 
3882  N NE2 . GLN C 2   ? 0.6392 0.1503 0.2980 0.1437  0.1227  -0.0230 2   GLN C NE2 
3883  N N   . ILE C 3   ? 0.5388 0.2696 0.3052 0.2252  0.1655  -0.0048 3   ILE C N   
3884  C CA  . ILE C 3   ? 0.5179 0.2875 0.3082 0.2314  0.1673  0.0000  3   ILE C CA  
3885  C C   . ILE C 3   ? 0.4824 0.2524 0.3018 0.1994  0.1575  -0.0006 3   ILE C C   
3886  O O   . ILE C 3   ? 0.4530 0.2325 0.2948 0.1743  0.1531  -0.0028 3   ILE C O   
3887  C CB  . ILE C 3   ? 0.4868 0.3365 0.3111 0.2400  0.1776  0.0058  3   ILE C CB  
3888  C CG1 . ILE C 3   ? 0.4771 0.3643 0.3164 0.2543  0.1799  0.0109  3   ILE C CG1 
3889  C CG2 . ILE C 3   ? 0.4404 0.3261 0.3037 0.2066  0.1757  0.0064  3   ILE C CG2 
3890  C CD1 . ILE C 3   ? 0.4620 0.4299 0.3230 0.2702  0.1908  0.0172  3   ILE C CD1 
3891  N N   . CYS C 4   ? 0.4901 0.2485 0.3050 0.2030  0.1541  0.0010  4   CYS C N   
3892  C CA  . CYS C 4   ? 0.4614 0.2211 0.3002 0.1756  0.1454  0.0004  4   CYS C CA  
3893  C C   . CYS C 4   ? 0.4289 0.2376 0.3001 0.1788  0.1480  0.0056  4   CYS C C   
3894  O O   . CYS C 4   ? 0.4422 0.2698 0.3064 0.2049  0.1547  0.0094  4   CYS C O   
3895  C CB  . CYS C 4   ? 0.5037 0.1993 0.3036 0.1690  0.1371  -0.0020 4   CYS C CB  
3896  S SG  . CYS C 4   ? 0.5556 0.1851 0.3062 0.1641  0.1325  -0.0076 4   CYS C SG  
3897  N N   . ILE C 5   ? 0.3885 0.2185 0.2928 0.1539  0.1422  0.0055  5   ILE C N   
3898  C CA  . ILE C 5   ? 0.3604 0.2287 0.2924 0.1528  0.1425  0.0099  5   ILE C CA  
3899  C C   . ILE C 5   ? 0.3674 0.2041 0.2907 0.1419  0.1348  0.0088  5   ILE C C   
3900  O O   . ILE C 5   ? 0.3676 0.1800 0.2865 0.1220  0.1277  0.0047  5   ILE C O   
3901  C CB  . ILE C 5   ? 0.3156 0.2301 0.2865 0.1329  0.1416  0.0109  5   ILE C CB  
3902  C CG1 . ILE C 5   ? 0.3134 0.2552 0.2878 0.1365  0.1485  0.0124  5   ILE C CG1 
3903  C CG2 . ILE C 5   ? 0.2915 0.2442 0.2876 0.1314  0.1417  0.0157  5   ILE C CG2 
3904  C CD1 . ILE C 5   ? 0.3197 0.3035 0.2960 0.1584  0.1578  0.0182  5   ILE C CD1 
3905  N N   . GLY C 6   ? 0.3743 0.2157 0.2943 0.1547  0.1361  0.0126  6   GLY C N   
3906  C CA  . GLY C 6   ? 0.3880 0.1973 0.2940 0.1445  0.1293  0.0125  6   GLY C CA  
3907  C C   . GLY C 6   ? 0.3799 0.2123 0.2968 0.1556  0.1309  0.0174  6   GLY C C   
3908  O O   . GLY C 6   ? 0.3608 0.2399 0.2989 0.1705  0.1369  0.0210  6   GLY C O   
3909  N N   . TYR C 7   ? 0.3973 0.1985 0.2974 0.1468  0.1253  0.0179  7   TYR C N   
3910  C CA  . TYR C 7   ? 0.3867 0.2087 0.2994 0.1525  0.1253  0.0222  7   TYR C CA  
3911  C C   . TYR C 7   ? 0.4431 0.2069 0.3062 0.1619  0.1221  0.0238  7   TYR C C   
3912  O O   . TYR C 7   ? 0.4890 0.1933 0.3080 0.1553  0.1182  0.0214  7   TYR C O   
3913  C CB  . TYR C 7   ? 0.3387 0.1945 0.2919 0.1252  0.1207  0.0218  7   TYR C CB  
3914  C CG  . TYR C 7   ? 0.3429 0.1719 0.2876 0.0982  0.1135  0.0181  7   TYR C CG  
3915  C CD1 . TYR C 7   ? 0.3283 0.1623 0.2826 0.0844  0.1115  0.0136  7   TYR C CD1 
3916  C CD2 . TYR C 7   ? 0.3631 0.1666 0.2893 0.0858  0.1085  0.0195  7   TYR C CD2 
3917  C CE1 . TYR C 7   ? 0.3322 0.1530 0.2803 0.0608  0.1046  0.0105  7   TYR C CE1 
3918  C CE2 . TYR C 7   ? 0.3675 0.1582 0.2871 0.0585  0.1021  0.0169  7   TYR C CE2 
3919  C CZ  . TYR C 7   ? 0.3509 0.1539 0.2829 0.0470  0.1001  0.0124  7   TYR C CZ  
3920  O OH  . TYR C 7   ? 0.3556 0.1562 0.2822 0.0208  0.0934  0.0101  7   TYR C OH  
3921  N N   . HIS C 8   ? 0.4437 0.2225 0.3105 0.1756  0.1231  0.0280  8   HIS C N   
3922  C CA  . HIS C 8   ? 0.5040 0.2262 0.3182 0.1906  0.1203  0.0303  8   HIS C CA  
3923  C C   . HIS C 8   ? 0.5240 0.2019 0.3171 0.1580  0.1122  0.0298  8   HIS C C   
3924  O O   . HIS C 8   ? 0.4780 0.1914 0.3111 0.1302  0.1095  0.0293  8   HIS C O   
3925  C CB  . HIS C 8   ? 0.4920 0.2532 0.3221 0.2141  0.1234  0.0351  8   HIS C CB  
3926  C CG  . HIS C 8   ? 0.5578 0.2609 0.3301 0.2364  0.1207  0.0376  8   HIS C CG  
3927  N ND1 . HIS C 8   ? 0.6273 0.2752 0.3379 0.2695  0.1219  0.0369  8   HIS C ND1 
3928  C CD2 . HIS C 8   ? 0.5702 0.2578 0.3316 0.2322  0.1165  0.0408  8   HIS C CD2 
3929  C CE1 . HIS C 8   ? 0.6837 0.2796 0.3439 0.2853  0.1179  0.0395  8   HIS C CE1 
3930  N NE2 . HIS C 8   ? 0.6488 0.2688 0.3402 0.2618  0.1147  0.0421  8   HIS C NE2 
3931  N N   . ALA C 9   ? 0.5989 0.1982 0.3241 0.1614  0.1079  0.0300  9   ALA C N   
3932  C CA  . ALA C 9   ? 0.6319 0.1859 0.3258 0.1311  0.1001  0.0315  9   ALA C CA  
3933  C C   . ALA C 9   ? 0.7111 0.1949 0.3355 0.1548  0.0978  0.0348  9   ALA C C   
3934  O O   . ALA C 9   ? 0.7466 0.2103 0.3409 0.1951  0.1017  0.0347  9   ALA C O   
3935  C CB  . ALA C 9   ? 0.6558 0.1725 0.3247 0.0984  0.0944  0.0283  9   ALA C CB  
3936  N N   . ASN C 10  ? 0.7427 0.1904 0.3387 0.1316  0.0915  0.0378  10  ASN C N   
3937  C CA  . ASN C 10  ? 0.8282 0.1981 0.3485 0.1520  0.0879  0.0411  10  ASN C CA  
3938  C C   . ASN C 10  ? 0.8771 0.1906 0.3521 0.1104  0.0791  0.0441  10  ASN C C   
3939  O O   . ASN C 10  ? 0.8428 0.1849 0.3477 0.0666  0.0762  0.0434  10  ASN C O   
3940  C CB  . ASN C 10  ? 0.8044 0.2172 0.3503 0.1902  0.0929  0.0442  10  ASN C CB  
3941  C CG  . ASN C 10  ? 0.7390 0.2149 0.3450 0.1669  0.0929  0.0468  10  ASN C CG  
3942  O OD1 . ASN C 10  ? 0.7170 0.2015 0.3405 0.1244  0.0891  0.0466  10  ASN C OD1 
3943  N ND2 . ASN C 10  ? 0.7102 0.2336 0.3464 0.1958  0.0969  0.0493  10  ASN C ND2 
3944  N N   . ASN C 11  ? 0.9613 0.1966 0.3614 0.1247  0.0746  0.0476  11  ASN C N   
3945  C CA  . ASN C 11  ? 1.0245 0.1938 0.3665 0.0836  0.0655  0.0514  11  ASN C CA  
3946  C C   . ASN C 11  ? 0.9813 0.1988 0.3644 0.0666  0.0657  0.0556  11  ASN C C   
3947  O O   . ASN C 11  ? 1.0413 0.2008 0.3689 0.0421  0.0591  0.0599  11  ASN C O   
3948  C CB  . ASN C 11  ? 1.1537 0.1959 0.3773 0.1046  0.0589  0.0531  11  ASN C CB  
3949  C CG  . ASN C 11  ? 1.1782 0.2092 0.3823 0.1616  0.0621  0.0549  11  ASN C CG  
3950  O OD1 . ASN C 11  ? 1.0982 0.2187 0.3786 0.1805  0.0688  0.0556  11  ASN C OD1 
3951  N ND2 . ASN C 11  ? 1.2951 0.2141 0.3918 0.1902  0.0564  0.0557  11  ASN C ND2 
3952  N N   . SER C 12  ? 0.8823 0.2020 0.3578 0.0776  0.0729  0.0544  12  SER C N   
3953  C CA  . SER C 12  ? 0.8349 0.2069 0.3549 0.0648  0.0736  0.0577  12  SER C CA  
3954  C C   . SER C 12  ? 0.8115 0.2086 0.3519 0.0097  0.0699  0.0585  12  SER C C   
3955  O O   . SER C 12  ? 0.7864 0.2080 0.3490 -0.0127 0.0696  0.0550  12  SER C O   
3956  C CB  . SER C 12  ? 0.7421 0.2117 0.3489 0.0909  0.0815  0.0560  12  SER C CB  
3957  O OG  . SER C 12  ? 0.6974 0.2154 0.3453 0.0791  0.0818  0.0589  12  SER C OG  
3958  N N   . THR C 13  ? 0.8222 0.2164 0.3537 -0.0102 0.0671  0.0631  13  THR C N   
3959  C CA  . THR C 13  ? 0.7953 0.2291 0.3512 -0.0600 0.0646  0.0645  13  THR C CA  
3960  C C   . THR C 13  ? 0.7197 0.2352 0.3454 -0.0575 0.0688  0.0655  13  THR C C   
3961  O O   . THR C 13  ? 0.6985 0.2518 0.3439 -0.0930 0.0673  0.0671  13  THR C O   
3962  C CB  . THR C 13  ? 0.8874 0.2405 0.3593 -0.0974 0.0565  0.0701  13  THR C CB  
3963  O OG1 . THR C 13  ? 0.9423 0.2354 0.3641 -0.0726 0.0550  0.0743  13  THR C OG1 
3964  C CG2 . THR C 13  ? 0.9623 0.2391 0.3651 -0.1142 0.0506  0.0691  13  THR C CG2 
3965  N N   . GLU C 14  ? 0.6821 0.2272 0.3429 -0.0164 0.0738  0.0646  14  GLU C N   
3966  C CA  . GLU C 14  ? 0.6139 0.2320 0.3373 -0.0123 0.0771  0.0652  14  GLU C CA  
3967  C C   . GLU C 14  ? 0.5384 0.2352 0.3286 -0.0303 0.0794  0.0609  14  GLU C C   
3968  O O   . GLU C 14  ? 0.5141 0.2290 0.3260 -0.0228 0.0813  0.0564  14  GLU C O   
3969  C CB  . GLU C 14  ? 0.5913 0.2296 0.3380 0.0327  0.0813  0.0651  14  GLU C CB  
3970  C CG  . GLU C 14  ? 0.6601 0.2346 0.3471 0.0580  0.0790  0.0695  14  GLU C CG  
3971  C CD  . GLU C 14  ? 0.6238 0.2446 0.3473 0.0848  0.0815  0.0717  14  GLU C CD  
3972  O OE1 . GLU C 14  ? 0.6001 0.2477 0.3449 0.0663  0.0806  0.0740  14  GLU C OE1 
3973  O OE2 . GLU C 14  ? 0.6193 0.2544 0.3507 0.1236  0.0844  0.0712  14  GLU C OE2 
3974  N N   . GLN C 15  ? 0.5056 0.2475 0.3245 -0.0515 0.0791  0.0622  15  GLN C N   
3975  C CA  . GLN C 15  ? 0.4424 0.2571 0.3170 -0.0653 0.0804  0.0580  15  GLN C CA  
3976  C C   . GLN C 15  ? 0.3840 0.2555 0.3100 -0.0486 0.0834  0.0573  15  GLN C C   
3977  O O   . GLN C 15  ? 0.3924 0.2537 0.3109 -0.0390 0.0836  0.0611  15  GLN C O   
3978  C CB  . GLN C 15  ? 0.4594 0.2855 0.3196 -0.1067 0.0770  0.0598  15  GLN C CB  
3979  C CG  . GLN C 15  ? 0.5268 0.2916 0.3269 -0.1319 0.0725  0.0617  15  GLN C CG  
3980  C CD  . GLN C 15  ? 0.5418 0.3309 0.3306 -0.1781 0.0688  0.0642  15  GLN C CD  
3981  O OE1 . GLN C 15  ? 0.5605 0.3474 0.3339 -0.2022 0.0655  0.0630  15  GLN C OE1 
3982  N NE2 . GLN C 15  ? 0.5347 0.3518 0.3310 -0.1918 0.0693  0.0681  15  GLN C NE2 
3983  N N   . VAL C 16  ? 0.3296 0.2563 0.3028 -0.0450 0.0848  0.0522  16  VAL C N   
3984  C CA  . VAL C 16  ? 0.2807 0.2573 0.2965 -0.0330 0.0863  0.0509  16  VAL C CA  
3985  C C   . VAL C 16  ? 0.2481 0.2769 0.2919 -0.0468 0.0854  0.0467  16  VAL C C   
3986  O O   . VAL C 16  ? 0.2519 0.2857 0.2924 -0.0587 0.0842  0.0438  16  VAL C O   
3987  C CB  . VAL C 16  ? 0.2536 0.2397 0.2932 -0.0051 0.0885  0.0490  16  VAL C CB  
3988  C CG1 . VAL C 16  ? 0.2865 0.2314 0.2989 0.0138  0.0897  0.0530  16  VAL C CG1 
3989  C CG2 . VAL C 16  ? 0.2368 0.2338 0.2901 -0.0033 0.0890  0.0437  16  VAL C CG2 
3990  N N   . ASP C 17  ? 0.2198 0.2874 0.2883 -0.0429 0.0856  0.0462  17  ASP C N   
3991  C CA  . ASP C 17  ? 0.1914 0.3112 0.2840 -0.0474 0.0847  0.0416  17  ASP C CA  
3992  C C   . ASP C 17  ? 0.1587 0.2962 0.2775 -0.0248 0.0844  0.0365  17  ASP C C   
3993  O O   . ASP C 17  ? 0.1513 0.2742 0.2755 -0.0097 0.0851  0.0378  17  ASP C O   
3994  C CB  . ASP C 17  ? 0.1886 0.3385 0.2847 -0.0565 0.0847  0.0440  17  ASP C CB  
3995  C CG  . ASP C 17  ? 0.2242 0.3658 0.2921 -0.0865 0.0843  0.0491  17  ASP C CG  
3996  O OD1 . ASP C 17  ? 0.2452 0.3778 0.2965 -0.1047 0.0829  0.0490  17  ASP C OD1 
3997  O OD2 . ASP C 17  ? 0.2349 0.3782 0.2943 -0.0944 0.0849  0.0535  17  ASP C OD2 
3998  N N   . THR C 18  ? 0.1440 0.3129 0.2748 -0.0237 0.0829  0.0310  18  THR C N   
3999  C CA  . THR C 18  ? 0.1228 0.3047 0.2689 -0.0044 0.0812  0.0257  18  THR C CA  
4000  C C   . THR C 18  ? 0.1144 0.3414 0.2679 -0.0010 0.0791  0.0214  18  THR C C   
4001  O O   . THR C 18  ? 0.1207 0.3757 0.2720 -0.0152 0.0797  0.0231  18  THR C O   
4002  C CB  . THR C 18  ? 0.1223 0.2889 0.2673 -0.0001 0.0808  0.0221  18  THR C CB  
4003  O OG1 . THR C 18  ? 0.1261 0.3142 0.2685 -0.0102 0.0793  0.0191  18  THR C OG1 
4004  C CG2 . THR C 18  ? 0.1369 0.2638 0.2708 -0.0021 0.0834  0.0261  18  THR C CG2 
4005  N N   . ILE C 19  ? 0.1066 0.3407 0.2643 0.0178  0.0764  0.0161  19  ILE C N   
4006  C CA  . ILE C 19  ? 0.1049 0.3797 0.2636 0.0292  0.0739  0.0112  19  ILE C CA  
4007  C C   . ILE C 19  ? 0.1084 0.4198 0.2688 0.0216  0.0734  0.0085  19  ILE C C   
4008  O O   . ILE C 19  ? 0.1074 0.4661 0.2708 0.0160  0.0738  0.0088  19  ILE C O   
4009  C CB  . ILE C 19  ? 0.1069 0.3671 0.2575 0.0530  0.0696  0.0055  19  ILE C CB  
4010  C CG1 . ILE C 19  ? 0.1087 0.3398 0.2552 0.0568  0.0689  0.0084  19  ILE C CG1 
4011  C CG2 . ILE C 19  ? 0.1119 0.4107 0.2559 0.0717  0.0665  -0.0005 19  ILE C CG2 
4012  C CD1 . ILE C 19  ? 0.1093 0.3609 0.2548 0.0610  0.0688  0.0096  19  ILE C CD1 
4013  N N   . MET C 20  ? 0.1137 0.4070 0.2718 0.0205  0.0724  0.0063  20  MET C N   
4014  C CA  . MET C 20  ? 0.1186 0.4465 0.2773 0.0151  0.0706  0.0031  20  MET C CA  
4015  C C   . MET C 20  ? 0.1330 0.4646 0.2882 -0.0160 0.0724  0.0083  20  MET C C   
4016  O O   . MET C 20  ? 0.1365 0.5095 0.2921 -0.0274 0.0706  0.0071  20  MET C O   
4017  C CB  . MET C 20  ? 0.1195 0.4235 0.2734 0.0281  0.0680  -0.0018 20  MET C CB  
4018  C CG  . MET C 20  ? 0.1209 0.4160 0.2669 0.0569  0.0643  -0.0075 20  MET C CG  
4019  S SD  . MET C 20  ? 0.1293 0.4060 0.2645 0.0692  0.0604  -0.0136 20  MET C SD  
4020  C CE  . MET C 20  ? 0.1444 0.3794 0.2582 0.0944  0.0562  -0.0173 20  MET C CE  
4021  N N   . GLU C 21  ? 0.1485 0.4353 0.2955 -0.0298 0.0752  0.0141  21  GLU C N   
4022  C CA  . GLU C 21  ? 0.1764 0.4474 0.3072 -0.0590 0.0758  0.0190  21  GLU C CA  
4023  C C   . GLU C 21  ? 0.1984 0.4359 0.3158 -0.0705 0.0783  0.0259  21  GLU C C   
4024  O O   . GLU C 21  ? 0.1917 0.3977 0.3117 -0.0546 0.0801  0.0271  21  GLU C O   
4025  C CB  . GLU C 21  ? 0.1864 0.4165 0.3069 -0.0595 0.0751  0.0175  21  GLU C CB  
4026  C CG  . GLU C 21  ? 0.2161 0.4364 0.3141 -0.0897 0.0734  0.0205  21  GLU C CG  
4027  C CD  . GLU C 21  ? 0.2286 0.4084 0.3142 -0.0877 0.0725  0.0183  21  GLU C CD  
4028  O OE1 . GLU C 21  ? 0.2094 0.3799 0.3079 -0.0634 0.0734  0.0140  21  GLU C OE1 
4029  O OE2 . GLU C 21  ? 0.2613 0.4157 0.3200 -0.1120 0.0706  0.0211  21  GLU C OE2 
4030  N N   . LYS C 22  ? 0.2307 0.4760 0.3309 -0.0997 0.0779  0.0308  22  LYS C N   
4031  C CA  . LYS C 22  ? 0.2635 0.4718 0.3423 -0.1129 0.0794  0.0377  22  LYS C CA  
4032  C C   . LYS C 22  ? 0.3154 0.4657 0.3555 -0.1347 0.0778  0.0418  22  LYS C C   
4033  O O   . LYS C 22  ? 0.3281 0.4811 0.3586 -0.1495 0.0753  0.0401  22  LYS C O   
4034  C CB  . LYS C 22  ? 0.2660 0.5225 0.3467 -0.1306 0.0798  0.0410  22  LYS C CB  
4035  C CG  . LYS C 22  ? 0.2342 0.5280 0.3423 -0.1048 0.0815  0.0381  22  LYS C CG  
4036  C CD  . LYS C 22  ? 0.2312 0.5955 0.3477 -0.1166 0.0820  0.0388  22  LYS C CD  
4037  C CE  . LYS C 22  ? 0.2667 0.6227 0.3573 -0.1525 0.0828  0.0471  22  LYS C CE  
4038  N NZ  . LYS C 22  ? 0.2601 0.6853 0.3606 -0.1606 0.0846  0.0488  22  LYS C NZ  
4039  N N   . ASN C 23  ? 0.3543 0.4490 0.3681 -0.1346 0.0787  0.0469  23  ASN C N   
4040  C CA  . ASN C 23  ? 0.4183 0.4439 0.3829 -0.1509 0.0766  0.0509  23  ASN C CA  
4041  C C   . ASN C 23  ? 0.4095 0.4045 0.3692 -0.1376 0.0761  0.0468  23  ASN C C   
4042  O O   . ASN C 23  ? 0.4448 0.4111 0.3720 -0.1589 0.0729  0.0475  23  ASN C O   
4043  C CB  . ASN C 23  ? 0.4786 0.5101 0.4112 -0.1952 0.0730  0.0555  23  ASN C CB  
4044  C CG  . ASN C 23  ? 0.5166 0.5633 0.4418 -0.2110 0.0737  0.0612  23  ASN C CG  
4045  O OD1 . ASN C 23  ? 0.5086 0.5406 0.4411 -0.1890 0.0763  0.0624  23  ASN C OD1 
4046  N ND2 . ASN C 23  ? 0.5771 0.6565 0.4868 -0.2513 0.0713  0.0650  23  ASN C ND2 
4047  N N   . VAL C 24  ? 0.3616 0.3628 0.3510 -0.1044 0.0791  0.0429  24  VAL C N   
4048  C CA  . VAL C 24  ? 0.3544 0.3290 0.3411 -0.0884 0.0798  0.0394  24  VAL C CA  
4049  C C   . VAL C 24  ? 0.3905 0.2961 0.3385 -0.0756 0.0808  0.0429  24  VAL C C   
4050  O O   . VAL C 24  ? 0.3827 0.2816 0.3365 -0.0550 0.0833  0.0452  24  VAL C O   
4051  C CB  . VAL C 24  ? 0.3023 0.3131 0.3327 -0.0609 0.0824  0.0345  24  VAL C CB  
4052  C CG1 . VAL C 24  ? 0.3064 0.2888 0.3318 -0.0445 0.0839  0.0319  24  VAL C CG1 
4053  C CG2 . VAL C 24  ? 0.2684 0.3394 0.3284 -0.0662 0.0806  0.0299  24  VAL C CG2 
4054  N N   . THR C 25  ? 0.4308 0.2858 0.3366 -0.0858 0.0785  0.0433  25  THR C N   
4055  C CA  . THR C 25  ? 0.4781 0.2613 0.3367 -0.0695 0.0788  0.0462  25  THR C CA  
4056  C C   . THR C 25  ? 0.4489 0.2372 0.3296 -0.0328 0.0835  0.0433  25  THR C C   
4057  O O   . THR C 25  ? 0.4253 0.2322 0.3257 -0.0295 0.0845  0.0388  25  THR C O   
4058  C CB  . THR C 25  ? 0.5449 0.2643 0.3428 -0.0908 0.0741  0.0471  25  THR C CB  
4059  O OG1 . THR C 25  ? 0.5649 0.2929 0.3460 -0.1331 0.0692  0.0499  25  THR C OG1 
4060  C CG2 . THR C 25  ? 0.6133 0.2495 0.3489 -0.0726 0.0733  0.0507  25  THR C CG2 
4061  N N   . VAL C 26  ? 0.4511 0.2256 0.3269 -0.0062 0.0862  0.0461  26  VAL C N   
4062  C CA  . VAL C 26  ? 0.4246 0.2151 0.3223 0.0271  0.0909  0.0446  26  VAL C CA  
4063  C C   . VAL C 26  ? 0.4797 0.2124 0.3276 0.0534  0.0918  0.0471  26  VAL C C   
4064  O O   . VAL C 26  ? 0.5368 0.2142 0.3334 0.0495  0.0884  0.0506  26  VAL C O   
4065  C CB  . VAL C 26  ? 0.3707 0.2180 0.3172 0.0394  0.0935  0.0455  26  VAL C CB  
4066  C CG1 . VAL C 26  ? 0.3195 0.2193 0.3095 0.0211  0.0925  0.0419  26  VAL C CG1 
4067  C CG2 . VAL C 26  ? 0.3906 0.2240 0.3206 0.0429  0.0922  0.0506  26  VAL C CG2 
4068  N N   . THR C 27  ? 0.4660 0.2119 0.3257 0.0812  0.0963  0.0455  27  THR C N   
4069  C CA  . THR C 27  ? 0.5189 0.2180 0.3317 0.1137  0.0978  0.0472  27  THR C CA  
4070  C C   . THR C 27  ? 0.5231 0.2325 0.3346 0.1390  0.0989  0.0516  27  THR C C   
4071  O O   . THR C 27  ? 0.5871 0.2413 0.3429 0.1614  0.0974  0.0540  27  THR C O   
4072  C CB  . THR C 27  ? 0.5048 0.2237 0.3312 0.1363  0.1030  0.0442  27  THR C CB  
4073  O OG1 . THR C 27  ? 0.4421 0.2359 0.3272 0.1462  0.1074  0.0447  27  THR C OG1 
4074  C CG2 . THR C 27  ? 0.4999 0.2088 0.3273 0.1130  0.1016  0.0396  27  THR C CG2 
4075  N N   . HIS C 28  ? 0.4609 0.2375 0.3287 0.1369  0.1008  0.0526  28  HIS C N   
4076  C CA  . HIS C 28  ? 0.4590 0.2546 0.3313 0.1578  0.1011  0.0570  28  HIS C CA  
4077  C C   . HIS C 28  ? 0.4096 0.2495 0.3252 0.1352  0.0994  0.0580  28  HIS C C   
4078  O O   . HIS C 28  ? 0.3614 0.2408 0.3183 0.1149  0.0998  0.0550  28  HIS C O   
4079  C CB  . HIS C 28  ? 0.4393 0.2826 0.3342 0.1908  0.1062  0.0579  28  HIS C CB  
4080  C CG  . HIS C 28  ? 0.4850 0.2938 0.3400 0.2182  0.1089  0.0566  28  HIS C CG  
4081  N ND1 . HIS C 28  ? 0.4755 0.2837 0.3367 0.2105  0.1113  0.0525  28  HIS C ND1 
4082  C CD2 . HIS C 28  ? 0.5452 0.3158 0.3487 0.2559  0.1093  0.0585  28  HIS C CD2 
4083  C CE1 . HIS C 28  ? 0.5264 0.2987 0.3433 0.2411  0.1135  0.0521  28  HIS C CE1 
4084  N NE2 . HIS C 28  ? 0.5709 0.3193 0.3508 0.2706  0.1122  0.0555  28  HIS C NE2 
4085  N N   . ALA C 29  ? 0.4268 0.2573 0.3285 0.1414  0.0972  0.0621  29  ALA C N   
4086  C CA  . ALA C 29  ? 0.3872 0.2552 0.3239 0.1227  0.0955  0.0633  29  ALA C CA  
4087  C C   . ALA C 29  ? 0.3956 0.2753 0.3292 0.1452  0.0948  0.0680  29  ALA C C   
4088  O O   . ALA C 29  ? 0.4372 0.2928 0.3372 0.1759  0.0953  0.0703  29  ALA C O   
4089  C CB  . ALA C 29  ? 0.4059 0.2407 0.3218 0.0908  0.0920  0.0631  29  ALA C CB  
4090  N N   . GLN C 30  ? 0.3593 0.2767 0.3257 0.1324  0.0934  0.0693  30  GLN C N   
4091  C CA  . GLN C 30  ? 0.3658 0.2964 0.3305 0.1502  0.0918  0.0739  30  GLN C CA  
4092  C C   . GLN C 30  ? 0.3543 0.2861 0.3260 0.1275  0.0888  0.0752  30  GLN C C   
4093  O O   . GLN C 30  ? 0.3068 0.2813 0.3191 0.1101  0.0887  0.0733  30  GLN C O   
4094  C CB  . GLN C 30  ? 0.3252 0.3230 0.3318 0.1658  0.0936  0.0748  30  GLN C CB  
4095  C CG  . GLN C 30  ? 0.3362 0.3525 0.3385 0.1882  0.0916  0.0799  30  GLN C CG  
4096  C CD  . GLN C 30  ? 0.3070 0.3922 0.3425 0.2047  0.0931  0.0819  30  GLN C CD  
4097  O OE1 . GLN C 30  ? 0.2959 0.4038 0.3440 0.2091  0.0966  0.0802  30  GLN C OE1 
4098  N NE2 . GLN C 30  ? 0.2972 0.4186 0.3459 0.2121  0.0903  0.0860  30  GLN C NE2 
4099  N N   . ASP C 31  ? 0.4040 0.2848 0.3303 0.1285  0.0862  0.0786  31  ASP C N   
4100  C CA  . ASP C 31  ? 0.4004 0.2819 0.3279 0.1104  0.0838  0.0810  31  ASP C CA  
4101  C C   . ASP C 31  ? 0.3706 0.2995 0.3282 0.1274  0.0829  0.0835  31  ASP C C   
4102  O O   . ASP C 31  ? 0.3879 0.3204 0.3347 0.1579  0.0825  0.0861  31  ASP C O   
4103  C CB  . ASP C 31  ? 0.4718 0.2799 0.3341 0.1076  0.0807  0.0847  31  ASP C CB  
4104  C CG  . ASP C 31  ? 0.4717 0.2779 0.3316 0.0795  0.0789  0.0871  31  ASP C CG  
4105  O OD1 . ASP C 31  ? 0.4201 0.2811 0.3262 0.0727  0.0796  0.0864  31  ASP C OD1 
4106  O OD2 . ASP C 31  ? 0.5285 0.2758 0.3356 0.0630  0.0764  0.0899  31  ASP C OD2 
4107  N N   . ILE C 32  ? 0.3286 0.2960 0.3217 0.1087  0.0821  0.0827  32  ILE C N   
4108  C CA  . ILE C 32  ? 0.3011 0.3128 0.3218 0.1185  0.0802  0.0850  32  ILE C CA  
4109  C C   . ILE C 32  ? 0.3088 0.3120 0.3209 0.1076  0.0776  0.0878  32  ILE C C   
4110  O O   . ILE C 32  ? 0.2883 0.3248 0.3207 0.1124  0.0752  0.0897  32  ILE C O   
4111  C CB  . ILE C 32  ? 0.2470 0.3132 0.3154 0.1089  0.0807  0.0815  32  ILE C CB  
4112  C CG1 . ILE C 32  ? 0.2268 0.2923 0.3072 0.0829  0.0815  0.0767  32  ILE C CG1 
4113  C CG2 . ILE C 32  ? 0.2407 0.3250 0.3186 0.1236  0.0830  0.0806  32  ILE C CG2 
4114  C CD1 . ILE C 32  ? 0.1852 0.2925 0.3007 0.0739  0.0800  0.0735  32  ILE C CD1 
4115  N N   . LEU C 33  ? 0.3424 0.3011 0.3214 0.0911  0.0777  0.0885  33  LEU C N   
4116  C CA  . LEU C 33  ? 0.3546 0.3034 0.3211 0.0775  0.0759  0.0915  33  LEU C CA  
4117  C C   . LEU C 33  ? 0.4203 0.3096 0.3302 0.0896  0.0734  0.0968  33  LEU C C   
4118  O O   . LEU C 33  ? 0.4685 0.3033 0.3341 0.0852  0.0734  0.0974  33  LEU C O   
4119  C CB  . LEU C 33  ? 0.3473 0.2962 0.3158 0.0451  0.0777  0.0891  33  LEU C CB  
4120  C CG  . LEU C 33  ? 0.3538 0.3043 0.3143 0.0269  0.0770  0.0919  33  LEU C CG  
4121  C CD1 . LEU C 33  ? 0.3085 0.3093 0.3092 0.0331  0.0762  0.0905  33  LEU C CD1 
4122  C CD2 . LEU C 33  ? 0.3567 0.3100 0.3120 -0.0045 0.0791  0.0903  33  LEU C CD2 
4123  N N   . GLU C 34  ? 0.4285 0.3234 0.3343 0.1046  0.0706  0.1006  34  GLU C N   
4124  C CA  . GLU C 34  ? 0.4963 0.3306 0.3427 0.1174  0.0673  0.1058  34  GLU C CA  
4125  C C   . GLU C 34  ? 0.5228 0.3246 0.3415 0.0851  0.0669  0.1083  34  GLU C C   
4126  O O   . GLU C 34  ? 0.4895 0.3283 0.3372 0.0704  0.0673  0.1085  34  GLU C O   
4127  C CB  . GLU C 34  ? 0.4949 0.3523 0.3474 0.1477  0.0640  0.1090  34  GLU C CB  
4128  C CG  . GLU C 34  ? 0.5698 0.3618 0.3561 0.1670  0.0597  0.1142  34  GLU C CG  
4129  C CD  . GLU C 34  ? 0.6374 0.3567 0.3624 0.1784  0.0592  0.1142  34  GLU C CD  
4130  O OE1 . GLU C 34  ? 0.6401 0.3693 0.3665 0.2087  0.0599  0.1125  34  GLU C OE1 
4131  O OE2 . GLU C 34  ? 0.6912 0.3433 0.3637 0.1549  0.0579  0.1162  34  GLU C OE2 
4132  N N   . LYS C 35  ? 0.5886 0.3202 0.3469 0.0734  0.0656  0.1105  35  LYS C N   
4133  C CA  . LYS C 35  ? 0.6188 0.3219 0.3469 0.0346  0.0654  0.1134  35  LYS C CA  
4134  C C   . LYS C 35  ? 0.6963 0.3287 0.3546 0.0367  0.0608  0.1200  35  LYS C C   
4135  O O   . LYS C 35  ? 0.7218 0.3355 0.3548 0.0027  0.0605  0.1236  35  LYS C O   
4136  C CB  . LYS C 35  ? 0.6391 0.3167 0.3470 0.0063  0.0667  0.1116  35  LYS C CB  
4137  C CG  . LYS C 35  ? 0.5673 0.3173 0.3389 -0.0137 0.0713  0.1062  35  LYS C CG  
4138  C CD  . LYS C 35  ? 0.5883 0.3158 0.3400 -0.0375 0.0718  0.1044  35  LYS C CD  
4139  C CE  . LYS C 35  ? 0.5575 0.3020 0.3378 -0.0152 0.0734  0.0988  35  LYS C CE  
4140  N NZ  . LYS C 35  ? 0.5785 0.2946 0.3421 0.0265  0.0719  0.0994  35  LYS C NZ  
4141  N N   . THR C 36  ? 0.7364 0.3323 0.3617 0.0768  0.0570  0.1218  36  THR C N   
4142  C CA  . THR C 36  ? 0.8255 0.3387 0.3703 0.0846  0.0514  0.1278  36  THR C CA  
4143  C C   . THR C 36  ? 0.8208 0.3531 0.3734 0.1166  0.0485  0.1305  36  THR C C   
4144  O O   . THR C 36  ? 0.7587 0.3616 0.3712 0.1417  0.0498  0.1278  36  THR C O   
4145  C CB  . THR C 36  ? 0.9091 0.3358 0.3784 0.1087  0.0473  0.1283  36  THR C CB  
4146  O OG1 . THR C 36  ? 0.8845 0.3448 0.3801 0.1585  0.0477  0.1252  36  THR C OG1 
4147  C CG2 . THR C 36  ? 0.9250 0.3239 0.3773 0.0753  0.0489  0.1261  36  THR C CG2 
4148  N N   . HIS C 37  ? 0.8924 0.3592 0.3798 0.1127  0.0438  0.1362  37  HIS C N   
4149  C CA  . HIS C 37  ? 0.9072 0.3751 0.3845 0.1446  0.0396  0.1395  37  HIS C CA  
4150  C C   . HIS C 37  ? 1.0253 0.3796 0.3950 0.1546  0.0326  0.1450  37  HIS C C   
4151  O O   . HIS C 37  ? 1.0901 0.3698 0.3978 0.1246  0.0314  0.1469  37  HIS C O   
4152  C CB  . HIS C 37  ? 0.8500 0.3777 0.3776 0.1197  0.0419  0.1407  37  HIS C CB  
4153  C CG  . HIS C 37  ? 0.8755 0.3732 0.3755 0.0691  0.0436  0.1439  37  HIS C CG  
4154  N ND1 . HIS C 37  ? 0.9342 0.3808 0.3793 0.0572  0.0401  0.1501  37  HIS C ND1 
4155  C CD2 . HIS C 37  ? 0.8524 0.3689 0.3709 0.0267  0.0484  0.1421  37  HIS C CD2 
4156  C CE1 . HIS C 37  ? 0.9456 0.3835 0.3772 0.0074  0.0430  0.1524  37  HIS C CE1 
4157  N NE2 . HIS C 37  ? 0.8959 0.3788 0.3726 -0.0110 0.0480  0.1476  37  HIS C NE2 
4158  N N   . ASN C 38  ? 1.0588 0.3979 0.4019 0.1960  0.0273  0.1477  38  ASN C N   
4159  C CA  . ASN C 38  ? 1.1798 0.4036 0.4122 0.2125  0.0195  0.1528  38  ASN C CA  
4160  C C   . ASN C 38  ? 1.2229 0.4000 0.4127 0.1716  0.0174  0.1589  38  ASN C C   
4161  O O   . ASN C 38  ? 1.3326 0.4007 0.4202 0.1716  0.0107  0.1637  38  ASN C O   
4162  C CB  . ASN C 38  ? 1.2082 0.4312 0.4200 0.2794  0.0139  0.1533  38  ASN C CB  
4163  C CG  . ASN C 38  ? 1.1489 0.4489 0.4175 0.2909  0.0133  0.1549  38  ASN C CG  
4164  O OD1 . ASN C 38  ? 1.1036 0.4380 0.4107 0.2508  0.0162  0.1562  38  ASN C OD1 
4165  N ND2 . ASN C 38  ? 1.1525 0.4819 0.4241 0.3471  0.0092  0.1547  38  ASN C ND2 
4166  N N   . GLY C 39  ? 1.1419 0.3994 0.4054 0.1382  0.0228  0.1586  39  GLY C N   
4167  C CA  . GLY C 39  ? 1.1704 0.4014 0.4050 0.0939  0.0228  0.1642  39  GLY C CA  
4168  C C   . GLY C 39  ? 1.2018 0.4150 0.4094 0.1172  0.0176  0.1687  39  GLY C C   
4169  O O   . GLY C 39  ? 1.2541 0.4181 0.4109 0.0869  0.0158  0.1745  39  GLY C O   
4170  N N   . LYS C 40  ? 1.1700 0.4282 0.4123 0.1692  0.0151  0.1663  40  LYS C N   
4171  C CA  . LYS C 40  ? 1.2091 0.4467 0.4187 0.2013  0.0085  0.1704  40  LYS C CA  
4172  C C   . LYS C 40  ? 1.1141 0.4623 0.4151 0.2202  0.0100  0.1680  40  LYS C C   
4173  O O   . LYS C 40  ? 1.0335 0.4646 0.4113 0.2284  0.0141  0.1628  40  LYS C O   
4174  C CB  . LYS C 40  ? 1.3002 0.4607 0.4299 0.2567  0.0005  0.1712  40  LYS C CB  
4175  C CG  . LYS C 40  ? 1.4267 0.4493 0.4367 0.2413  -0.0044 0.1753  40  LYS C CG  
4176  C CD  . LYS C 40  ? 1.5062 0.4597 0.4463 0.2957  -0.0105 0.1735  40  LYS C CD  
4177  C CE  . LYS C 40  ? 1.6363 0.4450 0.4526 0.2730  -0.0159 0.1771  40  LYS C CE  
4178  N NZ  . LYS C 40  ? 1.7206 0.4542 0.4619 0.3267  -0.0218 0.1747  40  LYS C NZ  
4179  N N   . LEU C 41  ? 1.1315 0.4754 0.4179 0.2252  0.0060  0.1721  41  LEU C N   
4180  C CA  . LEU C 41  ? 1.0617 0.4957 0.4168 0.2469  0.0047  0.1709  41  LEU C CA  
4181  C C   . LEU C 41  ? 1.1014 0.5278 0.4275 0.3094  -0.0031 0.1717  41  LEU C C   
4182  O O   . LEU C 41  ? 1.2009 0.5353 0.4361 0.3343  -0.0095 0.1754  41  LEU C O   
4183  C CB  . LEU C 41  ? 1.0645 0.4964 0.4144 0.2220  0.0040  0.1751  41  LEU C CB  
4184  C CG  . LEU C 41  ? 1.0166 0.4791 0.4050 0.1647  0.0123  0.1744  41  LEU C CG  
4185  C CD1 . LEU C 41  ? 0.9227 0.4853 0.3976 0.1605  0.0148  0.1712  41  LEU C CD1 
4186  C CD2 . LEU C 41  ? 1.0006 0.4612 0.4012 0.1348  0.0190  0.1709  41  LEU C CD2 
4187  N N   . CYS C 42  ? 1.0289 0.5518 0.4276 0.3347  -0.0030 0.1684  42  CYS C N   
4188  C CA  . CYS C 42  ? 1.0567 0.5914 0.4383 0.3937  -0.0085 0.1681  42  CYS C CA  
4189  C C   . CYS C 42  ? 0.9907 0.6336 0.4397 0.4195  -0.0118 0.1678  42  CYS C C   
4190  O O   . CYS C 42  ? 0.9100 0.6278 0.4321 0.3892  -0.0088 0.1662  42  CYS C O   
4191  C CB  . CYS C 42  ? 1.0509 0.5854 0.4399 0.3994  -0.0037 0.1637  42  CYS C CB  
4192  S SG  . CYS C 42  ? 1.1592 0.5522 0.4436 0.3853  -0.0035 0.1648  42  CYS C SG  
4193  N N   . ASP C 43  ? 1.0313 0.6812 0.4502 0.4765  -0.0184 0.1693  43  ASP C N   
4194  C CA  . ASP C 43  ? 0.9774 0.7367 0.4547 0.5042  -0.0226 0.1698  43  ASP C CA  
4195  C C   . ASP C 43  ? 0.8889 0.7420 0.4497 0.4877  -0.0164 0.1656  43  ASP C C   
4196  O O   . ASP C 43  ? 0.8948 0.7302 0.4495 0.4912  -0.0114 0.1625  43  ASP C O   
4197  C CB  . ASP C 43  ? 1.0471 0.7977 0.4699 0.5735  -0.0305 0.1722  43  ASP C CB  
4198  C CG  . ASP C 43  ? 1.1396 0.7989 0.4756 0.5951  -0.0384 0.1766  43  ASP C CG  
4199  O OD1 . ASP C 43  ? 1.1506 0.7520 0.4677 0.5533  -0.0372 0.1784  43  ASP C OD1 
4200  O OD2 . ASP C 43  ? 1.2048 0.8509 0.4883 0.6555  -0.0459 0.1786  43  ASP C OD2 
4201  N N   . LEU C 44  ? 0.8126 0.7597 0.4460 0.4680  -0.0174 0.1656  44  LEU C N   
4202  C CA  . LEU C 44  ? 0.7333 0.7688 0.4422 0.4489  -0.0128 0.1623  44  LEU C CA  
4203  C C   . LEU C 44  ? 0.7181 0.8489 0.4543 0.4881  -0.0181 0.1643  44  LEU C C   
4204  O O   . LEU C 44  ? 0.7060 0.8911 0.4587 0.4961  -0.0253 0.1678  44  LEU C O   
4205  C CB  . LEU C 44  ? 0.6654 0.7383 0.4307 0.3971  -0.0110 0.1608  44  LEU C CB  
4206  C CG  . LEU C 44  ? 0.5929 0.7320 0.4245 0.3685  -0.0059 0.1567  44  LEU C CG  
4207  C CD1 . LEU C 44  ? 0.5926 0.6753 0.4159 0.3445  0.0028  0.1523  44  LEU C CD1 
4208  C CD2 . LEU C 44  ? 0.5368 0.7279 0.4174 0.3322  -0.0084 0.1563  44  LEU C CD2 
4209  N N   . ASP C 45  ? 0.7198 0.8748 0.4600 0.5118  -0.0146 0.1625  45  ASP C N   
4210  C CA  . ASP C 45  ? 0.7064 0.9621 0.4730 0.5498  -0.0184 0.1647  45  ASP C CA  
4211  C C   . ASP C 45  ? 0.7706 1.0205 0.4859 0.6051  -0.0272 0.1690  45  ASP C C   
4212  O O   . ASP C 45  ? 0.7518 1.0994 0.4963 0.6268  -0.0333 0.1725  45  ASP C O   
4213  C CB  . ASP C 45  ? 0.6253 0.9898 0.4709 0.5129  -0.0200 0.1656  45  ASP C CB  
4214  C CG  . ASP C 45  ? 0.5908 1.0568 0.4793 0.5253  -0.0183 0.1659  45  ASP C CG  
4215  O OD1 . ASP C 45  ? 0.5614 1.0252 0.4733 0.5020  -0.0108 0.1622  45  ASP C OD1 
4216  O OD2 . ASP C 45  ? 0.5938 1.1454 0.4926 0.5571  -0.0246 0.1702  45  ASP C OD2 
4217  N N   . GLY C 46  ? 0.8505 0.9849 0.4860 0.6263  -0.0285 0.1692  46  GLY C N   
4218  C CA  . GLY C 46  ? 0.9249 1.0302 0.4971 0.6791  -0.0376 0.1730  46  GLY C CA  
4219  C C   . GLY C 46  ? 0.9284 1.0086 0.4926 0.6573  -0.0434 0.1762  46  GLY C C   
4220  O O   . GLY C 46  ? 1.0067 1.0134 0.4982 0.6893  -0.0496 0.1788  46  GLY C O   
4221  N N   . VAL C 47  ? 0.8495 0.9851 0.4824 0.6039  -0.0417 0.1759  47  VAL C N   
4222  C CA  . VAL C 47  ? 0.8433 0.9740 0.4786 0.5828  -0.0474 0.1788  47  VAL C CA  
4223  C C   . VAL C 47  ? 0.8730 0.8896 0.4670 0.5465  -0.0431 0.1778  47  VAL C C   
4224  O O   . VAL C 47  ? 0.8339 0.8336 0.4554 0.5016  -0.0349 0.1743  47  VAL C O   
4225  C CB  . VAL C 47  ? 0.7532 0.9902 0.4735 0.5422  -0.0484 0.1788  47  VAL C CB  
4226  C CG1 . VAL C 47  ? 0.7520 0.9831 0.4707 0.5238  -0.0548 0.1817  47  VAL C CG1 
4227  C CG2 . VAL C 47  ? 0.7240 1.0819 0.4859 0.5701  -0.0526 0.1807  47  VAL C CG2 
4228  N N   . LYS C 48  ? 0.9439 0.8873 0.4711 0.5657  -0.0489 0.1813  48  LYS C N   
4229  C CA  . LYS C 48  ? 0.9891 0.8194 0.4629 0.5346  -0.0455 0.1817  48  LYS C CA  
4230  C C   . LYS C 48  ? 0.9265 0.7779 0.4500 0.4763  -0.0416 0.1810  48  LYS C C   
4231  O O   . LYS C 48  ? 0.8797 0.8047 0.4495 0.4704  -0.0461 0.1821  48  LYS C O   
4232  C CB  . LYS C 48  ? 1.0887 0.8349 0.4719 0.5717  -0.0539 0.1863  48  LYS C CB  
4233  C CG  . LYS C 48  ? 1.1595 0.7748 0.4668 0.5450  -0.0509 0.1876  48  LYS C CG  
4234  C CD  . LYS C 48  ? 1.2493 0.7863 0.4736 0.5690  -0.0598 0.1928  48  LYS C CD  
4235  C CE  . LYS C 48  ? 1.3365 0.7355 0.4710 0.5443  -0.0576 0.1948  48  LYS C CE  
4236  N NZ  . LYS C 48  ? 1.4131 0.7366 0.4747 0.5490  -0.0649 0.2003  48  LYS C NZ  
4237  N N   . PRO C 49  ? 0.9292 0.7170 0.4400 0.4336  -0.0337 0.1792  49  PRO C N   
4238  C CA  . PRO C 49  ? 0.8837 0.6831 0.4287 0.3844  -0.0300 0.1788  49  PRO C CA  
4239  C C   . PRO C 49  ? 0.9341 0.6833 0.4299 0.3853  -0.0354 0.1837  49  PRO C C   
4240  O O   . PRO C 49  ? 1.0196 0.6871 0.4368 0.4103  -0.0394 0.1872  49  PRO C O   
4241  C CB  . PRO C 49  ? 0.8843 0.6307 0.4199 0.3454  -0.0203 0.1761  49  PRO C CB  
4242  C CG  . PRO C 49  ? 0.9663 0.6304 0.4279 0.3730  -0.0214 0.1774  49  PRO C CG  
4243  C CD  . PRO C 49  ? 0.9688 0.6825 0.4386 0.4269  -0.0276 0.1773  49  PRO C CD  
4244  N N   . LEU C 50  ? 0.8863 0.6789 0.4230 0.3583  -0.0357 0.1837  50  LEU C N   
4245  C CA  . LEU C 50  ? 0.9272 0.6727 0.4222 0.3499  -0.0389 0.1880  50  LEU C CA  
4246  C C   . LEU C 50  ? 0.9494 0.6253 0.4138 0.3075  -0.0301 0.1882  50  LEU C C   
4247  O O   . LEU C 50  ? 0.8927 0.6023 0.4039 0.2685  -0.0228 0.1850  50  LEU C O   
4248  C CB  . LEU C 50  ? 0.8696 0.6883 0.4185 0.3365  -0.0425 0.1877  50  LEU C CB  
4249  C CG  . LEU C 50  ? 0.8973 0.6792 0.4157 0.3204  -0.0443 0.1913  50  LEU C CG  
4250  C CD1 . LEU C 50  ? 0.9906 0.6939 0.4253 0.3519  -0.0510 0.1971  50  LEU C CD1 
4251  C CD2 . LEU C 50  ? 0.8453 0.7037 0.4141 0.3164  -0.0503 0.1908  50  LEU C CD2 
4252  N N   . ILE C 51  ? 1.0369 0.6163 0.4187 0.3155  -0.0312 0.1920  51  ILE C N   
4253  C CA  . ILE C 51  ? 1.0700 0.5818 0.4132 0.2718  -0.0238 0.1936  51  ILE C CA  
4254  C C   . ILE C 51  ? 1.1094 0.5832 0.4128 0.2565  -0.0260 0.1989  51  ILE C C   
4255  O O   . ILE C 51  ? 1.1924 0.5959 0.4210 0.2809  -0.0336 0.2040  51  ILE C O   
4256  C CB  . ILE C 51  ? 1.1524 0.5713 0.4194 0.2804  -0.0241 0.1952  51  ILE C CB  
4257  C CG1 . ILE C 51  ? 1.1097 0.5709 0.4197 0.2954  -0.0211 0.1897  51  ILE C CG1 
4258  C CG2 . ILE C 51  ? 1.1925 0.5443 0.4150 0.2287  -0.0175 0.1981  51  ILE C CG2 
4259  C CD1 . ILE C 51  ? 1.1762 0.5537 0.4233 0.2920  -0.0193 0.1899  51  ILE C CD1 
4260  N N   . LEU C 52  ? 1.0538 0.5720 0.4033 0.2176  -0.0195 0.1976  52  LEU C N   
4261  C CA  . LEU C 52  ? 1.0811 0.5755 0.4017 0.1999  -0.0202 0.2023  52  LEU C CA  
4262  C C   . LEU C 52  ? 1.1654 0.5646 0.4039 0.1698  -0.0169 0.2081  52  LEU C C   
4263  O O   . LEU C 52  ? 1.2078 0.5710 0.4046 0.1571  -0.0183 0.2133  52  LEU C O   
4264  C CB  . LEU C 52  ? 0.9985 0.5711 0.3909 0.1702  -0.0138 0.1986  52  LEU C CB  
4265  C CG  . LEU C 52  ? 0.9206 0.5830 0.3885 0.1900  -0.0178 0.1934  52  LEU C CG  
4266  C CD1 . LEU C 52  ? 0.8553 0.5757 0.3780 0.1588  -0.0114 0.1894  52  LEU C CD1 
4267  C CD2 . LEU C 52  ? 0.9431 0.6119 0.3961 0.2277  -0.0297 0.1965  52  LEU C CD2 
4268  N N   . ARG C 53  ? 1.1924 0.5508 0.4055 0.1560  -0.0129 0.2075  53  ARG C N   
4269  C CA  . ARG C 53  ? 1.2757 0.5443 0.4086 0.1200  -0.0102 0.2132  53  ARG C CA  
4270  C C   . ARG C 53  ? 1.2464 0.5483 0.4014 0.0685  -0.0011 0.2151  53  ARG C C   
4271  O O   . ARG C 53  ? 1.1681 0.5453 0.3941 0.0453  0.0075  0.2101  53  ARG C O   
4272  C CB  . ARG C 53  ? 1.3925 0.5528 0.4196 0.1469  -0.0208 0.2198  53  ARG C CB  
4273  C CG  . ARG C 53  ? 1.4961 0.5459 0.4249 0.1127  -0.0203 0.2256  53  ARG C CG  
4274  C CD  . ARG C 53  ? 1.6234 0.5545 0.4359 0.1379  -0.0317 0.2324  53  ARG C CD  
4275  N NE  . ARG C 53  ? 1.6873 0.5533 0.4447 0.1848  -0.0399 0.2308  53  ARG C NE  
4276  C CZ  . ARG C 53  ? 1.6891 0.5693 0.4505 0.2505  -0.0484 0.2282  53  ARG C CZ  
4277  N NH1 . ARG C 53  ? 1.6307 0.5872 0.4490 0.2762  -0.0510 0.2271  53  ARG C NH1 
4278  N NH2 . ARG C 53  ? 1.7536 0.5728 0.4587 0.2917  -0.0548 0.2267  53  ARG C NH2 
4279  N N   . ASP C 54  ? 1.3098 0.5592 0.4041 0.0527  -0.0031 0.2221  54  ASP C N   
4280  C CA  . ASP C 54  ? 1.2886 0.5717 0.3983 0.0049  0.0059  0.2246  54  ASP C CA  
4281  C C   . ASP C 54  ? 1.2266 0.5808 0.3925 0.0180  0.0060  0.2224  54  ASP C C   
4282  O O   . ASP C 54  ? 1.2009 0.5949 0.3875 -0.0150 0.0139  0.2233  54  ASP C O   
4283  C CB  . ASP C 54  ? 1.3974 0.5836 0.4050 -0.0289 0.0049  0.2344  54  ASP C CB  
4284  C CG  . ASP C 54  ? 1.4532 0.5806 0.4094 -0.0622 0.0072  0.2369  54  ASP C CG  
4285  O OD1 . ASP C 54  ? 1.3956 0.5847 0.4040 -0.0946 0.0167  0.2336  54  ASP C OD1 
4286  O OD2 . ASP C 54  ? 1.5598 0.5766 0.4188 -0.0556 -0.0009 0.2422  54  ASP C OD2 
4287  N N   . CYS C 55  ? 1.2064 0.5784 0.3941 0.0655  -0.0029 0.2197  55  CYS C N   
4288  C CA  . CYS C 55  ? 1.1448 0.5873 0.3888 0.0780  -0.0043 0.2168  55  CYS C CA  
4289  C C   . CYS C 55  ? 1.0420 0.5800 0.3794 0.0742  0.0016  0.2083  55  CYS C C   
4290  O O   . CYS C 55  ? 1.0151 0.5684 0.3791 0.0803  0.0030  0.2041  55  CYS C O   
4291  C CB  . CYS C 55  ? 1.1669 0.5967 0.3957 0.1275  -0.0173 0.2179  55  CYS C CB  
4292  S SG  . CYS C 55  ? 1.2801 0.6107 0.4051 0.1347  -0.0252 0.2274  55  CYS C SG  
4293  N N   . SER C 56  ? 0.9909 0.5872 0.3717 0.0644  0.0047  0.2059  56  SER C N   
4294  C CA  . SER C 56  ? 0.9030 0.5818 0.3630 0.0649  0.0081  0.1977  56  SER C CA  
4295  C C   . SER C 56  ? 0.8715 0.5855 0.3640 0.1003  -0.0026 0.1950  56  SER C C   
4296  O O   . SER C 56  ? 0.9138 0.5954 0.3713 0.1260  -0.0121 0.1993  56  SER C O   
4297  C CB  . SER C 56  ? 0.8732 0.5929 0.3552 0.0362  0.0171  0.1961  56  SER C CB  
4298  O OG  . SER C 56  ? 0.8701 0.6038 0.3541 0.0477  0.0118  0.1968  56  SER C OG  
4299  N N   . VAL C 57  ? 0.8013 0.5819 0.3572 0.1008  -0.0017 0.1881  57  VAL C N   
4300  C CA  . VAL C 57  ? 0.7691 0.5914 0.3580 0.1261  -0.0122 0.1858  57  VAL C CA  
4301  C C   . VAL C 57  ? 0.7838 0.6061 0.3575 0.1281  -0.0174 0.1885  57  VAL C C   
4302  O O   . VAL C 57  ? 0.7983 0.6232 0.3638 0.1525  -0.0285 0.1910  57  VAL C O   
4303  C CB  . VAL C 57  ? 0.6998 0.5843 0.3511 0.1198  -0.0103 0.1780  57  VAL C CB  
4304  C CG1 . VAL C 57  ? 0.6738 0.6010 0.3534 0.1383  -0.0220 0.1766  57  VAL C CG1 
4305  C CG2 . VAL C 57  ? 0.6845 0.5703 0.3517 0.1190  -0.0055 0.1753  57  VAL C CG2 
4306  N N   . ALA C 58  ? 0.7813 0.6044 0.3505 0.1033  -0.0093 0.1879  58  ALA C N   
4307  C CA  . ALA C 58  ? 0.7988 0.6181 0.3492 0.1025  -0.0127 0.1905  58  ALA C CA  
4308  C C   . ALA C 58  ? 0.8664 0.6270 0.3570 0.1151  -0.0186 0.1986  58  ALA C C   
4309  O O   . ALA C 58  ? 0.8795 0.6413 0.3607 0.1347  -0.0290 0.2007  58  ALA C O   
4310  C CB  . ALA C 58  ? 0.7909 0.6208 0.3413 0.0746  -0.0009 0.1889  58  ALA C CB  
4311  N N   . GLY C 59  ? 0.9138 0.6205 0.3597 0.1033  -0.0128 0.2031  59  GLY C N   
4312  C CA  . GLY C 59  ? 0.9916 0.6276 0.3677 0.1145  -0.0185 0.2110  59  GLY C CA  
4313  C C   . GLY C 59  ? 1.0074 0.6366 0.3763 0.1566  -0.0320 0.2119  59  GLY C C   
4314  O O   . GLY C 59  ? 1.0506 0.6530 0.3825 0.1768  -0.0410 0.2164  59  GLY C O   
4315  N N   . TRP C 60  ? 0.9739 0.6312 0.3774 0.1712  -0.0332 0.2078  60  TRP C N   
4316  C CA  . TRP C 60  ? 0.9818 0.6506 0.3861 0.2131  -0.0452 0.2083  60  TRP C CA  
4317  C C   . TRP C 60  ? 0.9475 0.6751 0.3869 0.2271  -0.0548 0.2072  60  TRP C C   
4318  O O   . TRP C 60  ? 0.9864 0.7013 0.3952 0.2557  -0.0656 0.2114  60  TRP C O   
4319  C CB  . TRP C 60  ? 0.9453 0.6440 0.3868 0.2216  -0.0431 0.2037  60  TRP C CB  
4320  C CG  . TRP C 60  ? 0.9214 0.6738 0.3938 0.2581  -0.0538 0.2023  60  TRP C CG  
4321  C CD1 . TRP C 60  ? 0.9621 0.7087 0.4043 0.2965  -0.0656 0.2064  60  TRP C CD1 
4322  C CD2 . TRP C 60  ? 0.8546 0.6789 0.3920 0.2587  -0.0537 0.1969  60  TRP C CD2 
4323  N NE1 . TRP C 60  ? 0.9215 0.7408 0.4095 0.3200  -0.0726 0.2042  60  TRP C NE1 
4324  C CE2 . TRP C 60  ? 0.8564 0.7220 0.4021 0.2955  -0.0654 0.1985  60  TRP C CE2 
4325  C CE3 . TRP C 60  ? 0.7963 0.6553 0.3832 0.2318  -0.0451 0.1911  60  TRP C CE3 
4326  C CZ2 . TRP C 60  ? 0.8020 0.7439 0.4042 0.3018  -0.0683 0.1950  60  TRP C CZ2 
4327  C CZ3 . TRP C 60  ? 0.7450 0.6706 0.3845 0.2396  -0.0484 0.1873  60  TRP C CZ3 
4328  C CH2 . TRP C 60  ? 0.7481 0.7151 0.3949 0.2721  -0.0598 0.1895  60  TRP C CH2 
4329  N N   . LEU C 61  ? 0.8811 0.6693 0.3788 0.2069  -0.0517 0.2017  61  LEU C N   
4330  C CA  . LEU C 61  ? 0.8484 0.6932 0.3795 0.2151  -0.0617 0.2002  61  LEU C CA  
4331  C C   . LEU C 61  ? 0.8798 0.7037 0.3793 0.2127  -0.0659 0.2039  61  LEU C C   
4332  O O   . LEU C 61  ? 0.8855 0.7336 0.3853 0.2323  -0.0782 0.2059  61  LEU C O   
4333  C CB  . LEU C 61  ? 0.7807 0.6819 0.3708 0.1926  -0.0578 0.1931  61  LEU C CB  
4334  C CG  . LEU C 61  ? 0.7425 0.6794 0.3719 0.1970  -0.0566 0.1892  61  LEU C CG  
4335  C CD1 . LEU C 61  ? 0.6862 0.6698 0.3636 0.1744  -0.0545 0.1826  61  LEU C CD1 
4336  C CD2 . LEU C 61  ? 0.7492 0.7173 0.3835 0.2294  -0.0686 0.1920  61  LEU C CD2 
4337  N N   . LEU C 62  ? 0.9010 0.6846 0.3733 0.1883  -0.0560 0.2051  62  LEU C N   
4338  C CA  . LEU C 62  ? 0.9377 0.6949 0.3732 0.1855  -0.0589 0.2093  62  LEU C CA  
4339  C C   . LEU C 62  ? 1.0127 0.7084 0.3834 0.2092  -0.0657 0.2167  62  LEU C C   
4340  O O   . LEU C 62  ? 1.0469 0.7228 0.3857 0.2156  -0.0717 0.2207  62  LEU C O   
4341  C CB  . LEU C 62  ? 0.9377 0.6787 0.3638 0.1514  -0.0454 0.2086  62  LEU C CB  
4342  C CG  . LEU C 62  ? 0.8749 0.6720 0.3539 0.1336  -0.0402 0.2010  62  LEU C CG  
4343  C CD1 . LEU C 62  ? 0.8753 0.6639 0.3463 0.1041  -0.0248 0.2002  62  LEU C CD1 
4344  C CD2 . LEU C 62  ? 0.8631 0.6881 0.3529 0.1406  -0.0501 0.1996  62  LEU C CD2 
4345  N N   . GLY C 63  ? 1.0434 0.7047 0.3901 0.2240  -0.0654 0.2185  63  GLY C N   
4346  C CA  . GLY C 63  ? 1.1254 0.7184 0.4008 0.2514  -0.0728 0.2250  63  GLY C CA  
4347  C C   . GLY C 63  ? 1.1911 0.7032 0.3996 0.2260  -0.0652 0.2305  63  GLY C C   
4348  O O   . GLY C 63  ? 1.2541 0.7158 0.4046 0.2369  -0.0714 0.2362  63  GLY C O   
4349  N N   . ASN C 64  ? 1.1782 0.6808 0.3936 0.1902  -0.0520 0.2290  64  ASN C N   
4350  C CA  . ASN C 64  ? 1.2443 0.6733 0.3939 0.1598  -0.0442 0.2349  64  ASN C CA  
4351  C C   . ASN C 64  ? 1.3421 0.6779 0.4055 0.1847  -0.0527 0.2412  64  ASN C C   
4352  O O   . ASN C 64  ? 1.3491 0.6767 0.4111 0.2125  -0.0575 0.2393  64  ASN C O   
4353  C CB  . ASN C 64  ? 1.2096 0.6566 0.3871 0.1212  -0.0301 0.2319  64  ASN C CB  
4354  C CG  . ASN C 64  ? 1.2829 0.6554 0.3890 0.0856  -0.0226 0.2388  64  ASN C CG  
4355  O OD1 . ASN C 64  ? 1.3689 0.6559 0.3975 0.0957  -0.0289 0.2447  64  ASN C OD1 
4356  N ND2 . ASN C 64  ? 1.2534 0.6589 0.3821 0.0432  -0.0096 0.2380  64  ASN C ND2 
4357  N N   . PRO C 65  ? 1.4236 0.6859 0.4099 0.1768  -0.0550 0.2486  65  PRO C N   
4358  C CA  . PRO C 65  ? 1.5301 0.6927 0.4216 0.2054  -0.0652 0.2546  65  PRO C CA  
4359  C C   . PRO C 65  ? 1.5832 0.6781 0.4263 0.1981  -0.0624 0.2558  65  PRO C C   
4360  O O   . PRO C 65  ? 1.6604 0.6843 0.4363 0.2351  -0.0725 0.2583  65  PRO C O   
4361  C CB  . PRO C 65  ? 1.6013 0.7000 0.4224 0.1824  -0.0649 0.2624  65  PRO C CB  
4362  C CG  . PRO C 65  ? 1.5409 0.6957 0.4117 0.1310  -0.0505 0.2610  65  PRO C CG  
4363  C CD  . PRO C 65  ? 1.4263 0.6914 0.4044 0.1408  -0.0480 0.2518  65  PRO C CD  
4364  N N   . MET C 66  ? 1.5472 0.6631 0.4201 0.1526  -0.0495 0.2540  66  MET C N   
4365  C CA  . MET C 66  ? 1.5865 0.6493 0.4236 0.1417  -0.0466 0.2543  66  MET C CA  
4366  C C   . MET C 66  ? 1.5298 0.6440 0.4248 0.1794  -0.0497 0.2469  66  MET C C   
4367  O O   . MET C 66  ? 1.5702 0.6345 0.4291 0.1859  -0.0505 0.2467  66  MET C O   
4368  C CB  . MET C 66  ? 1.5603 0.6426 0.4166 0.0793  -0.0319 0.2548  66  MET C CB  
4369  C CG  . MET C 66  ? 1.6156 0.6568 0.4164 0.0345  -0.0268 0.2627  66  MET C CG  
4370  S SD  . MET C 66  ? 1.7785 0.6592 0.4283 0.0227  -0.0345 0.2734  66  MET C SD  
4371  C CE  . MET C 66  ? 1.8101 0.6834 0.4257 -0.0456 -0.0239 0.2819  66  MET C CE  
4372  N N   . CYS C 67  ? 1.4399 0.6527 0.4212 0.2016  -0.0516 0.2411  67  CYS C N   
4373  C CA  . CYS C 67  ? 1.3803 0.6551 0.4224 0.2345  -0.0546 0.2345  67  CYS C CA  
4374  C C   . CYS C 67  ? 1.4093 0.6841 0.4325 0.2941  -0.0690 0.2354  67  CYS C C   
4375  O O   . CYS C 67  ? 1.3411 0.7021 0.4329 0.3196  -0.0732 0.2307  67  CYS C O   
4376  C CB  . CYS C 67  ? 1.2655 0.6508 0.4123 0.2151  -0.0476 0.2279  67  CYS C CB  
4377  S SG  . CYS C 67  ? 1.2337 0.6305 0.4017 0.1506  -0.0309 0.2270  67  CYS C SG  
4378  N N   . ASP C 68  ? 1.5158 0.6938 0.4414 0.3154  -0.0771 0.2416  68  ASP C N   
4379  C CA  . ASP C 68  ? 1.5607 0.7284 0.4526 0.3774  -0.0915 0.2429  68  ASP C CA  
4380  C C   . ASP C 68  ? 1.5544 0.7423 0.4590 0.4190  -0.0950 0.2389  68  ASP C C   
4381  O O   . ASP C 68  ? 1.5506 0.7827 0.4674 0.4706  -0.1052 0.2379  68  ASP C O   
4382  C CB  . ASP C 68  ? 1.6907 0.7333 0.4608 0.3911  -0.0992 0.2505  68  ASP C CB  
4383  C CG  . ASP C 68  ? 1.7011 0.7372 0.4579 0.3704  -0.1003 0.2549  68  ASP C CG  
4384  O OD1 . ASP C 68  ? 1.6101 0.7414 0.4506 0.3554  -0.0972 0.2519  68  ASP C OD1 
4385  O OD2 . ASP C 68  ? 1.8069 0.7370 0.4633 0.3690  -0.1048 0.2616  68  ASP C OD2 
4386  N N   . GLU C 69  ? 1.5557 0.7145 0.4557 0.3972  -0.0867 0.2368  69  GLU C N   
4387  C CA  . GLU C 69  ? 1.5417 0.7263 0.4606 0.4329  -0.0884 0.2324  69  GLU C CA  
4388  C C   . GLU C 69  ? 1.4270 0.7496 0.4580 0.4452  -0.0883 0.2268  69  GLU C C   
4389  O O   . GLU C 69  ? 1.4206 0.7859 0.4662 0.4926  -0.0948 0.2248  69  GLU C O   
4390  C CB  . GLU C 69  ? 1.5482 0.6891 0.4558 0.3973  -0.0783 0.2306  69  GLU C CB  
4391  C CG  . GLU C 69  ? 1.5356 0.6993 0.4605 0.4326  -0.0791 0.2259  69  GLU C CG  
4392  C CD  . GLU C 69  ? 1.5477 0.6632 0.4563 0.3969  -0.0700 0.2243  69  GLU C CD  
4393  O OE1 . GLU C 69  ? 1.5918 0.6363 0.4524 0.3494  -0.0650 0.2281  69  GLU C OE1 
4394  O OE2 . GLU C 69  ? 1.5141 0.6660 0.4572 0.4151  -0.0680 0.2195  69  GLU C OE2 
4395  N N   . PHE C 70  ? 1.3431 0.7334 0.4472 0.4023  -0.0815 0.2247  70  PHE C N   
4396  C CA  . PHE C 70  ? 1.2370 0.7476 0.4431 0.4006  -0.0803 0.2193  70  PHE C CA  
4397  C C   . PHE C 70  ? 1.2071 0.7856 0.4462 0.4168  -0.0898 0.2204  70  PHE C C   
4398  O O   . PHE C 70  ? 1.1241 0.7889 0.4399 0.3970  -0.0883 0.2168  70  PHE C O   
4399  C CB  . PHE C 70  ? 1.1667 0.7066 0.4294 0.3452  -0.0671 0.2152  70  PHE C CB  
4400  C CG  . PHE C 70  ? 1.2005 0.6729 0.4265 0.3237  -0.0584 0.2149  70  PHE C CG  
4401  C CD1 . PHE C 70  ? 1.2032 0.6749 0.4304 0.3464  -0.0582 0.2122  70  PHE C CD1 
4402  C CD2 . PHE C 70  ? 1.2353 0.6451 0.4208 0.2807  -0.0508 0.2180  70  PHE C CD2 
4403  C CE1 . PHE C 70  ? 1.2398 0.6458 0.4287 0.3257  -0.0513 0.2121  70  PHE C CE1 
4404  C CE2 . PHE C 70  ? 1.2714 0.6211 0.4197 0.2572  -0.0439 0.2184  70  PHE C CE2 
4405  C CZ  . PHE C 70  ? 1.2747 0.6193 0.4235 0.2797  -0.0445 0.2153  70  PHE C CZ  
4406  N N   . ILE C 71  ? 1.2811 0.8159 0.4568 0.4529  -0.1003 0.2253  71  ILE C N   
4407  C CA  . ILE C 71  ? 1.2626 0.8668 0.4638 0.4810  -0.1122 0.2267  71  ILE C CA  
4408  C C   . ILE C 71  ? 1.2442 0.9218 0.4755 0.5276  -0.1194 0.2249  71  ILE C C   
4409  O O   . ILE C 71  ? 1.3028 0.9350 0.4840 0.5654  -0.1212 0.2255  71  ILE C O   
4410  C CB  . ILE C 71  ? 1.3505 0.8833 0.4705 0.5050  -0.1215 0.2328  71  ILE C CB  
4411  C CG1 . ILE C 71  ? 1.3305 0.9432 0.4784 0.5370  -0.1348 0.2342  71  ILE C CG1 
4412  C CG2 . ILE C 71  ? 1.4581 0.8908 0.4807 0.5468  -0.1260 0.2360  71  ILE C CG2 
4413  C CD1 . ILE C 71  ? 1.3957 0.9522 0.4814 0.5467  -0.1427 0.2396  71  ILE C CD1 
4414  N N   . ASN C 72  ? 1.1677 0.9579 0.4766 0.5237  -0.1236 0.2228  72  ASN C N   
4415  C CA  . ASN C 72  ? 1.1393 1.0203 0.4876 0.5604  -0.1299 0.2216  72  ASN C CA  
4416  C C   . ASN C 72  ? 1.1332 1.0050 0.4875 0.5670  -0.1216 0.2181  72  ASN C C   
4417  O O   . ASN C 72  ? 1.1780 1.0466 0.4993 0.6173  -0.1262 0.2190  72  ASN C O   
4418  C CB  . ASN C 72  ? 1.2043 1.0913 0.5039 0.6223  -0.1441 0.2261  72  ASN C CB  
4419  C CG  . ASN C 72  ? 1.1824 1.1336 0.5075 0.6196  -0.1548 0.2288  72  ASN C CG  
4420  O OD1 . ASN C 72  ? 1.1108 1.1235 0.5003 0.5760  -0.1530 0.2269  72  ASN C OD1 
4421  N ND2 . ASN C 72  ? 1.2497 1.1837 0.5195 0.6676  -0.1667 0.2333  72  ASN C ND2 
4422  N N   . VAL C 73  ? 1.0803 0.9489 0.4747 0.5185  -0.1097 0.2140  73  VAL C N   
4423  C CA  . VAL C 73  ? 1.0706 0.9294 0.4734 0.5189  -0.1013 0.2105  73  VAL C CA  
4424  C C   . VAL C 73  ? 1.0234 0.9885 0.4817 0.5448  -0.1051 0.2087  73  VAL C C   
4425  O O   . VAL C 73  ? 0.9646 1.0251 0.4832 0.5329  -0.1101 0.2086  73  VAL C O   
4426  C CB  . VAL C 73  ? 1.0189 0.8621 0.4579 0.4607  -0.0880 0.2063  73  VAL C CB  
4427  C CG1 . VAL C 73  ? 1.0723 0.8110 0.4511 0.4349  -0.0825 0.2085  73  VAL C CG1 
4428  C CG2 . VAL C 73  ? 0.9325 0.8637 0.4506 0.4246  -0.0876 0.2035  73  VAL C CG2 
4429  N N   . PRO C 74  ? 1.0531 1.0016 0.4878 0.5783  -0.1029 0.2075  74  PRO C N   
4430  C CA  . PRO C 74  ? 1.0053 1.0580 0.4946 0.5986  -0.1045 0.2059  74  PRO C CA  
4431  C C   . PRO C 74  ? 0.9202 1.0190 0.4823 0.5471  -0.0948 0.2012  74  PRO C C   
4432  O O   . PRO C 74  ? 0.9053 0.9481 0.4686 0.5029  -0.0864 0.1989  74  PRO C O   
4433  C CB  . PRO C 74  ? 1.0750 1.0733 0.5037 0.6492  -0.1038 0.2057  74  PRO C CB  
4434  C CG  . PRO C 74  ? 1.1291 0.9944 0.4950 0.6262  -0.0966 0.2050  74  PRO C CG  
4435  C CD  . PRO C 74  ? 1.1313 0.9623 0.4880 0.5919  -0.0982 0.2076  74  PRO C CD  
4436  N N   . GLU C 75  ? 0.8679 1.0689 0.4870 0.5532  -0.0961 0.2001  75  GLU C N   
4437  C CA  . GLU C 75  ? 0.7920 1.0370 0.4763 0.5060  -0.0883 0.1959  75  GLU C CA  
4438  C C   . GLU C 75  ? 0.8010 0.9729 0.4676 0.4947  -0.0764 0.1918  75  GLU C C   
4439  O O   . GLU C 75  ? 0.8594 0.9749 0.4729 0.5315  -0.0752 0.1923  75  GLU C O   
4440  C CB  . GLU C 75  ? 0.7428 1.1122 0.4855 0.5132  -0.0929 0.1965  75  GLU C CB  
4441  C CG  . GLU C 75  ? 0.7533 1.1464 0.4939 0.5486  -0.0891 0.1954  75  GLU C CG  
4442  C CD  . GLU C 75  ? 0.6955 1.2166 0.5012 0.5409  -0.0918 0.1962  75  GLU C CD  
4443  O OE1 . GLU C 75  ? 0.6963 1.3041 0.5145 0.5633  -0.1021 0.2007  75  GLU C OE1 
4444  O OE2 . GLU C 75  ? 0.6518 1.1884 0.4945 0.5107  -0.0839 0.1926  75  GLU C OE2 
4445  N N   . TRP C 76  ? 0.7467 0.9191 0.4541 0.4446  -0.0684 0.1878  76  TRP C N   
4446  C CA  . TRP C 76  ? 0.7507 0.8565 0.4451 0.4254  -0.0572 0.1839  76  TRP C CA  
4447  C C   . TRP C 76  ? 0.6836 0.8500 0.4397 0.4005  -0.0514 0.1795  76  TRP C C   
4448  O O   . TRP C 76  ? 0.6301 0.8713 0.4383 0.3788  -0.0547 0.1790  76  TRP C O   
4449  C CB  . TRP C 76  ? 0.7590 0.7935 0.4333 0.3871  -0.0520 0.1832  76  TRP C CB  
4450  C CG  . TRP C 76  ? 0.7006 0.7840 0.4252 0.3482  -0.0527 0.1816  76  TRP C CG  
4451  C CD1 . TRP C 76  ? 0.6429 0.7541 0.4153 0.3105  -0.0463 0.1767  76  TRP C CD1 
4452  C CD2 . TRP C 76  ? 0.7009 0.8065 0.4267 0.3456  -0.0609 0.1845  76  TRP C CD2 
4453  N NE1 . TRP C 76  ? 0.6118 0.7559 0.4104 0.2858  -0.0503 0.1763  76  TRP C NE1 
4454  C CE2 . TRP C 76  ? 0.6449 0.7872 0.4172 0.3053  -0.0591 0.1811  76  TRP C CE2 
4455  C CE3 . TRP C 76  ? 0.7475 0.8421 0.4356 0.3749  -0.0702 0.1896  76  TRP C CE3 
4456  C CZ2 . TRP C 76  ? 0.6349 0.8011 0.4159 0.2921  -0.0663 0.1825  76  TRP C CZ2 
4457  C CZ3 . TRP C 76  ? 0.7324 0.8562 0.4341 0.3607  -0.0770 0.1912  76  TRP C CZ3 
4458  C CH2 . TRP C 76  ? 0.6769 0.8353 0.4243 0.3190  -0.0750 0.1876  76  TRP C CH2 
4459  N N   . SER C 77  ? 0.6927 0.8210 0.4371 0.4027  -0.0434 0.1766  77  SER C N   
4460  C CA  . SER C 77  ? 0.6350 0.8038 0.4305 0.3765  -0.0367 0.1721  77  SER C CA  
4461  C C   . SER C 77  ? 0.5992 0.7431 0.4154 0.3265  -0.0305 0.1685  77  SER C C   
4462  O O   . SER C 77  ? 0.5444 0.7418 0.4101 0.2986  -0.0302 0.1659  77  SER C O   
4463  C CB  . SER C 77  ? 0.6634 0.7919 0.4331 0.3964  -0.0304 0.1701  77  SER C CB  
4464  O OG  . SER C 77  ? 0.7302 0.7555 0.4324 0.4032  -0.0283 0.1712  77  SER C OG  
4465  N N   . TYR C 78  ? 0.6363 0.6980 0.4093 0.3161  -0.0260 0.1687  78  TYR C N   
4466  C CA  . TYR C 78  ? 0.6111 0.6499 0.3962 0.2735  -0.0199 0.1659  78  TYR C CA  
4467  C C   . TYR C 78  ? 0.6648 0.6312 0.3950 0.2703  -0.0198 0.1694  78  TYR C C   
4468  O O   . TYR C 78  ? 0.7256 0.6471 0.4033 0.3000  -0.0240 0.1736  78  TYR C O   
4469  C CB  . TYR C 78  ? 0.5884 0.6122 0.3886 0.2521  -0.0102 0.1611  78  TYR C CB  
4470  C CG  . TYR C 78  ? 0.6425 0.5964 0.3917 0.2659  -0.0063 0.1621  78  TYR C CG  
4471  C CD1 . TYR C 78  ? 0.6664 0.6229 0.4006 0.3023  -0.0087 0.1628  78  TYR C CD1 
4472  C CD2 . TYR C 78  ? 0.6745 0.5599 0.3863 0.2417  -0.0005 0.1625  78  TYR C CD2 
4473  C CE1 . TYR C 78  ? 0.7253 0.6079 0.4039 0.3157  -0.0060 0.1634  78  TYR C CE1 
4474  C CE2 . TYR C 78  ? 0.7328 0.5471 0.3901 0.2496  0.0017  0.1638  78  TYR C CE2 
4475  C CZ  . TYR C 78  ? 0.7604 0.5683 0.3987 0.2873  -0.0013 0.1640  78  TYR C CZ  
4476  O OH  . TYR C 78  ? 0.8275 0.5547 0.4026 0.2955  0.0000  0.1651  78  TYR C OH  
4477  N N   . ILE C 79  ? 0.6468 0.6017 0.3852 0.2356  -0.0152 0.1680  79  ILE C N   
4478  C CA  . ILE C 79  ? 0.6951 0.5884 0.3842 0.2261  -0.0142 0.1717  79  ILE C CA  
4479  C C   . ILE C 79  ? 0.7098 0.5534 0.3781 0.1967  -0.0043 0.1705  79  ILE C C   
4480  O O   . ILE C 79  ? 0.6635 0.5362 0.3711 0.1747  0.0022  0.1656  79  ILE C O   
4481  C CB  . ILE C 79  ? 0.6700 0.5928 0.3791 0.2098  -0.0169 0.1719  79  ILE C CB  
4482  C CG1 . ILE C 79  ? 0.6664 0.6340 0.3867 0.2369  -0.0283 0.1744  79  ILE C CG1 
4483  C CG2 . ILE C 79  ? 0.7161 0.5791 0.3769 0.1945  -0.0140 0.1756  79  ILE C CG2 
4484  C CD1 . ILE C 79  ? 0.6301 0.6409 0.3817 0.2191  -0.0322 0.1731  79  ILE C CD1 
4485  N N   . VAL C 80  ? 0.7786 0.5475 0.3819 0.1952  -0.0038 0.1752  80  VAL C N   
4486  C CA  . VAL C 80  ? 0.8027 0.5240 0.3783 0.1621  0.0046  0.1755  80  VAL C CA  
4487  C C   . VAL C 80  ? 0.8351 0.5241 0.3766 0.1369  0.0066  0.1798  80  VAL C C   
4488  O O   . VAL C 80  ? 0.8976 0.5342 0.3829 0.1501  0.0009  0.1855  80  VAL C O   
4489  C CB  . VAL C 80  ? 0.8696 0.5188 0.3856 0.1753  0.0036  0.1779  80  VAL C CB  
4490  C CG1 . VAL C 80  ? 0.8908 0.4990 0.3819 0.1345  0.0118  0.1782  80  VAL C CG1 
4491  C CG2 . VAL C 80  ? 0.8419 0.5256 0.3889 0.2049  0.0017  0.1739  80  VAL C CG2 
4492  N N   . GLU C 81  ? 0.7955 0.5173 0.3687 0.1022  0.0147  0.1772  81  GLU C N   
4493  C CA  . GLU C 81  ? 0.8169 0.5245 0.3666 0.0752  0.0185  0.1808  81  GLU C CA  
4494  C C   . GLU C 81  ? 0.8269 0.5219 0.3645 0.0361  0.0282  0.1811  81  GLU C C   
4495  O O   . GLU C 81  ? 0.7805 0.5149 0.3604 0.0266  0.0335  0.1757  81  GLU C O   
4496  C CB  . GLU C 81  ? 0.7570 0.5315 0.3596 0.0733  0.0189  0.1770  81  GLU C CB  
4497  C CG  . GLU C 81  ? 0.7752 0.5439 0.3568 0.0506  0.0228  0.1804  81  GLU C CG  
4498  C CD  . GLU C 81  ? 0.7191 0.5505 0.3495 0.0495  0.0236  0.1755  81  GLU C CD  
4499  O OE1 . GLU C 81  ? 0.6644 0.5440 0.3436 0.0476  0.0266  0.1688  81  GLU C OE1 
4500  O OE2 . GLU C 81  ? 0.7349 0.5625 0.3496 0.0510  0.0208  0.1783  81  GLU C OE2 
4501  N N   . LYS C 82  ? 0.8908 0.5329 0.3690 0.0118  0.0302  0.1877  82  LYS C N   
4502  C CA  . LYS C 82  ? 0.9039 0.5430 0.3683 -0.0317 0.0392  0.1893  82  LYS C CA  
4503  C C   . LYS C 82  ? 0.8404 0.5606 0.3611 -0.0514 0.0477  0.1851  82  LYS C C   
4504  O O   . LYS C 82  ? 0.7985 0.5615 0.3558 -0.0341 0.0460  0.1820  82  LYS C O   
4505  C CB  . LYS C 82  ? 0.9953 0.5563 0.3750 -0.0566 0.0383  0.1986  82  LYS C CB  
4506  C CG  . LYS C 82  ? 1.0752 0.5428 0.3836 -0.0457 0.0312  0.2025  82  LYS C CG  
4507  C CD  . LYS C 82  ? 1.1750 0.5570 0.3902 -0.0764 0.0297  0.2121  82  LYS C CD  
4508  C CE  . LYS C 82  ? 1.2625 0.5458 0.3985 -0.0770 0.0240  0.2155  82  LYS C CE  
4509  N NZ  . LYS C 82  ? 1.3027 0.5306 0.4042 -0.0219 0.0131  0.2151  82  LYS C NZ  
4510  N N   . ALA C 83  ? 0.8382 0.5790 0.3616 -0.0866 0.0562  0.1852  83  ALA C N   
4511  C CA  . ALA C 83  ? 0.7855 0.6054 0.3563 -0.1028 0.0649  0.1811  83  ALA C CA  
4512  C C   . ALA C 83  ? 0.8086 0.6349 0.3575 -0.1159 0.0674  0.1860  83  ALA C C   
4513  O O   . ALA C 83  ? 0.7656 0.6442 0.3524 -0.1031 0.0692  0.1816  83  ALA C O   
4514  C CB  . ALA C 83  ? 0.7809 0.6259 0.3565 -0.1364 0.0729  0.1807  83  ALA C CB  
4515  N N   . ASN C 84  ? 0.8831 0.6510 0.3655 -0.1416 0.0672  0.1950  84  ASN C N   
4516  C CA  . ASN C 84  ? 0.9139 0.6816 0.3673 -0.1577 0.0698  0.2009  84  ASN C CA  
4517  C C   . ASN C 84  ? 0.9912 0.6679 0.3740 -0.1502 0.0610  0.2086  84  ASN C C   
4518  O O   . ASN C 84  ? 1.0638 0.6885 0.3807 -0.1836 0.0621  0.2172  84  ASN C O   
4519  C CB  . ASN C 84  ? 0.9342 0.7328 0.3706 -0.2072 0.0803  0.2056  84  ASN C CB  
4520  C CG  . ASN C 84  ? 0.8680 0.7538 0.3665 -0.2132 0.0885  0.1983  84  ASN C CG  
4521  O OD1 . ASN C 84  ? 0.8038 0.7474 0.3599 -0.1847 0.0896  0.1899  84  ASN C OD1 
4522  N ND2 . ASN C 84  ? 0.8894 0.7819 0.3713 -0.2510 0.0935  0.2015  84  ASN C ND2 
4523  N N   . PRO C 85  ? 0.9803 0.6381 0.3730 -0.1072 0.0516  0.2059  85  PRO C N   
4524  C CA  . PRO C 85  ? 1.0551 0.6286 0.3798 -0.0926 0.0422  0.2127  85  PRO C CA  
4525  C C   . PRO C 85  ? 1.0979 0.6554 0.3812 -0.1140 0.0444  0.2197  85  PRO C C   
4526  O O   . PRO C 85  ? 1.0513 0.6713 0.3759 -0.1130 0.0487  0.2169  85  PRO C O   
4527  C CB  . PRO C 85  ? 1.0148 0.6058 0.3780 -0.0425 0.0332  0.2073  85  PRO C CB  
4528  C CG  . PRO C 85  ? 0.9321 0.5952 0.3714 -0.0344 0.0369  0.1983  85  PRO C CG  
4529  C CD  . PRO C 85  ? 0.9037 0.6183 0.3664 -0.0713 0.0487  0.1970  85  PRO C CD  
4530  N N   . VAL C 86  ? 1.1911 0.6615 0.3886 -0.1330 0.0410  0.2287  86  VAL C N   
4531  C CA  . VAL C 86  ? 1.2421 0.6900 0.3905 -0.1595 0.0433  0.2367  86  VAL C CA  
4532  C C   . VAL C 86  ? 1.2400 0.6817 0.3889 -0.1236 0.0360  0.2366  86  VAL C C   
4533  O O   . VAL C 86  ? 1.2285 0.7052 0.3857 -0.1359 0.0407  0.2383  86  VAL C O   
4534  C CB  . VAL C 86  ? 1.3561 0.7008 0.4002 -0.1942 0.0405  0.2472  86  VAL C CB  
4535  C CG1 . VAL C 86  ? 1.3625 0.7161 0.4022 -0.2372 0.0474  0.2482  86  VAL C CG1 
4536  C CG2 . VAL C 86  ? 1.4280 0.6698 0.4071 -0.1566 0.0267  0.2494  86  VAL C CG2 
4537  N N   . ASN C 87  ? 1.2518 0.6533 0.3912 -0.0788 0.0244  0.2347  87  ASN C N   
4538  C CA  . ASN C 87  ? 1.2514 0.6491 0.3905 -0.0423 0.0157  0.2348  87  ASN C CA  
4539  C C   . ASN C 87  ? 1.1511 0.6430 0.3817 -0.0182 0.0162  0.2258  87  ASN C C   
4540  O O   . ASN C 87  ? 1.1211 0.6277 0.3825 0.0191  0.0083  0.2212  87  ASN C O   
4541  C CB  . ASN C 87  ? 1.3139 0.6337 0.3992 -0.0022 0.0024  0.2371  87  ASN C CB  
4542  C CG  . ASN C 87  ? 1.4328 0.6402 0.4083 -0.0200 -0.0013 0.2467  87  ASN C CG  
4543  O OD1 . ASN C 87  ? 1.4736 0.6599 0.4092 -0.0559 0.0031  0.2532  87  ASN C OD1 
4544  N ND2 . ASN C 87  ? 1.4953 0.6269 0.4159 0.0058  -0.0101 0.2479  87  ASN C ND2 
4545  N N   . ASP C 88  ? 1.1046 0.6596 0.3737 -0.0401 0.0252  0.2237  88  ASP C N   
4546  C CA  . ASP C 88  ? 1.0218 0.6557 0.3652 -0.0205 0.0252  0.2154  88  ASP C CA  
4547  C C   . ASP C 88  ? 1.0331 0.6678 0.3640 -0.0098 0.0207  0.2176  88  ASP C C   
4548  O O   . ASP C 88  ? 1.0715 0.6621 0.3694 0.0152  0.0097  0.2211  88  ASP C O   
4549  C CB  . ASP C 88  ? 0.9650 0.6680 0.3578 -0.0455 0.0377  0.2100  88  ASP C CB  
4550  C CG  . ASP C 88  ? 0.8878 0.6606 0.3501 -0.0238 0.0365  0.2006  88  ASP C CG  
4551  O OD1 . ASP C 88  ? 0.8727 0.6448 0.3506 0.0066  0.0259  0.1982  88  ASP C OD1 
4552  O OD2 . ASP C 88  ? 0.8464 0.6750 0.3443 -0.0378 0.0458  0.1957  88  ASP C OD2 
4553  N N   . LEU C 89  ? 1.0031 0.6875 0.3570 -0.0264 0.0289  0.2156  89  LEU C N   
4554  C CA  . LEU C 89  ? 1.0159 0.7009 0.3555 -0.0193 0.0257  0.2177  89  LEU C CA  
4555  C C   . LEU C 89  ? 1.0905 0.7226 0.3601 -0.0470 0.0299  0.2276  89  LEU C C   
4556  O O   . LEU C 89  ? 1.0933 0.7514 0.3579 -0.0803 0.0420  0.2296  89  LEU C O   
4557  C CB  . LEU C 89  ? 0.9564 0.7154 0.3466 -0.0212 0.0324  0.2106  89  LEU C CB  
4558  C CG  . LEU C 89  ? 0.9029 0.6991 0.3419 0.0093  0.0233  0.2025  89  LEU C CG  
4559  C CD1 . LEU C 89  ? 0.8849 0.6725 0.3450 0.0310  0.0138  0.2001  89  LEU C CD1 
4560  C CD2 . LEU C 89  ? 0.8502 0.7104 0.3334 0.0042  0.0317  0.1944  89  LEU C CD2 
4561  N N   . CYS C 90  ? 1.1544 0.7136 0.3669 -0.0331 0.0197  0.2340  90  CYS C N   
4562  C CA  . CYS C 90  ? 1.2380 0.7323 0.3721 -0.0590 0.0217  0.2441  90  CYS C CA  
4563  C C   . CYS C 90  ? 1.2309 0.7626 0.3678 -0.0759 0.0290  0.2455  90  CYS C C   
4564  O O   . CYS C 90  ? 1.2601 0.7937 0.3686 -0.1155 0.0398  0.2510  90  CYS C O   
4565  C CB  . CYS C 90  ? 1.3103 0.7182 0.3801 -0.0318 0.0075  0.2497  90  CYS C CB  
4566  S SG  . CYS C 90  ? 1.2787 0.7083 0.3798 0.0217  -0.0072 0.2452  90  CYS C SG  
4567  N N   . TYR C 91  ? 1.1939 0.7584 0.3639 -0.0472 0.0230  0.2408  91  TYR C N   
4568  C CA  . TYR C 91  ? 1.1766 0.7865 0.3590 -0.0574 0.0301  0.2399  91  TYR C CA  
4569  C C   . TYR C 91  ? 1.0986 0.7940 0.3505 -0.0599 0.0395  0.2306  91  TYR C C   
4570  O O   . TYR C 91  ? 1.0462 0.7699 0.3475 -0.0346 0.0334  0.2227  91  TYR C O   
4571  C CB  . TYR C 91  ? 1.1801 0.7803 0.3593 -0.0261 0.0183  0.2390  91  TYR C CB  
4572  C CG  . TYR C 91  ? 1.1908 0.8115 0.3565 -0.0385 0.0246  0.2409  91  TYR C CG  
4573  C CD1 . TYR C 91  ? 1.1338 0.8259 0.3488 -0.0357 0.0312  0.2332  91  TYR C CD1 
4574  C CD2 . TYR C 91  ? 1.2640 0.8287 0.3619 -0.0519 0.0238  0.2504  91  TYR C CD2 
4575  C CE1 . TYR C 91  ? 1.1468 0.8580 0.3464 -0.0438 0.0373  0.2346  91  TYR C CE1 
4576  C CE2 . TYR C 91  ? 1.2746 0.8601 0.3593 -0.0632 0.0302  0.2523  91  TYR C CE2 
4577  C CZ  . TYR C 91  ? 1.2147 0.8756 0.3516 -0.0582 0.0371  0.2443  91  TYR C CZ  
4578  O OH  . TYR C 91  ? 1.2293 0.9110 0.3502 -0.0662 0.0437  0.2459  91  TYR C OH  
4579  N N   . PRO C 92  ? 1.0946 0.8329 0.3477 -0.0897 0.0540  0.2318  92  PRO C N   
4580  C CA  . PRO C 92  ? 1.0291 0.8475 0.3405 -0.0902 0.0635  0.2231  92  PRO C CA  
4581  C C   . PRO C 92  ? 0.9773 0.8311 0.3334 -0.0555 0.0571  0.2133  92  PRO C C   
4582  O O   . PRO C 92  ? 0.9924 0.8276 0.3330 -0.0395 0.0495  0.2140  92  PRO C O   
4583  C CB  . PRO C 92  ? 1.0475 0.9060 0.3406 -0.1211 0.0783  0.2274  92  PRO C CB  
4584  C CG  . PRO C 92  ? 1.1246 0.9185 0.3487 -0.1497 0.0780  0.2395  92  PRO C CG  
4585  C CD  . PRO C 92  ? 1.1552 0.8726 0.3518 -0.1231 0.0619  0.2414  92  PRO C CD  
4586  N N   . GLY C 93  ? 0.9218 0.8228 0.3282 -0.0457 0.0594  0.2045  93  GLY C N   
4587  C CA  . GLY C 93  ? 0.8800 0.8083 0.3217 -0.0167 0.0527  0.1952  93  GLY C CA  
4588  C C   . GLY C 93  ? 0.8283 0.7895 0.3177 -0.0066 0.0525  0.1865  93  GLY C C   
4589  O O   . GLY C 93  ? 0.8166 0.7956 0.3183 -0.0222 0.0607  0.1866  93  GLY C O   
4590  N N   . ASP C 94  ? 0.8009 0.7686 0.3135 0.0176  0.0424  0.1793  94  ASP C N   
4591  C CA  . ASP C 94  ? 0.7563 0.7472 0.3094 0.0286  0.0396  0.1711  94  ASP C CA  
4592  C C   . ASP C 94  ? 0.7474 0.7128 0.3111 0.0449  0.0235  0.1705  94  ASP C C   
4593  O O   . ASP C 94  ? 0.7696 0.7111 0.3135 0.0533  0.0138  0.1737  94  ASP C O   
4594  C CB  . ASP C 94  ? 0.7369 0.7652 0.3028 0.0409  0.0428  0.1621  94  ASP C CB  
4595  C CG  . ASP C 94  ? 0.7443 0.8121 0.3013 0.0298  0.0589  0.1622  94  ASP C CG  
4596  O OD1 . ASP C 94  ? 0.7285 0.8251 0.3021 0.0174  0.0684  0.1618  94  ASP C OD1 
4597  O OD2 . ASP C 94  ? 0.7670 0.8414 0.3003 0.0335  0.0619  0.1628  94  ASP C OD2 
4598  N N   . PHE C 95  ? 0.7148 0.6902 0.3098 0.0488  0.0208  0.1665  95  PHE C N   
4599  C CA  . PHE C 95  ? 0.7000 0.6671 0.3114 0.0632  0.0063  0.1650  95  PHE C CA  
4600  C C   . PHE C 95  ? 0.6682 0.6616 0.3046 0.0700  0.0033  0.1557  95  PHE C C   
4601  O O   . PHE C 95  ? 0.6433 0.6573 0.3008 0.0667  0.0104  0.1507  95  PHE C O   
4602  C CB  . PHE C 95  ? 0.6944 0.6497 0.3168 0.0625  0.0053  0.1683  95  PHE C CB  
4603  C CG  . PHE C 95  ? 0.6981 0.6416 0.3231 0.0784  -0.0092 0.1709  95  PHE C CG  
4604  C CD1 . PHE C 95  ? 0.6717 0.6388 0.3224 0.0872  -0.0198 0.1660  95  PHE C CD1 
4605  C CD2 . PHE C 95  ? 0.7333 0.6430 0.3308 0.0846  -0.0128 0.1786  95  PHE C CD2 
4606  C CE1 . PHE C 95  ? 0.6745 0.6438 0.3297 0.1004  -0.0331 0.1691  95  PHE C CE1 
4607  C CE2 . PHE C 95  ? 0.7380 0.6460 0.3378 0.1037  -0.0261 0.1810  95  PHE C CE2 
4608  C CZ  . PHE C 95  ? 0.7056 0.6495 0.3376 0.1110  -0.0360 0.1764  95  PHE C CZ  
4609  N N   . ASN C 96  ? 0.6746 0.6631 0.3029 0.0787  -0.0080 0.1535  96  ASN C N   
4610  C CA  . ASN C 96  ? 0.6597 0.6596 0.2970 0.0838  -0.0130 0.1450  96  ASN C CA  
4611  C C   . ASN C 96  ? 0.6305 0.6398 0.2976 0.0835  -0.0201 0.1423  96  ASN C C   
4612  O O   . ASN C 96  ? 0.6279 0.6357 0.3040 0.0846  -0.0297 0.1468  96  ASN C O   
4613  C CB  . ASN C 96  ? 0.6848 0.6695 0.2971 0.0893  -0.0248 0.1442  96  ASN C CB  
4614  C CG  . ASN C 96  ? 0.6883 0.6716 0.2911 0.0943  -0.0283 0.1352  96  ASN C CG  
4615  O OD1 . ASN C 96  ? 0.6909 0.6824 0.2856 0.0996  -0.0172 0.1301  96  ASN C OD1 
4616  N ND2 . ASN C 96  ? 0.6941 0.6668 0.2932 0.0928  -0.0441 0.1332  96  ASN C ND2 
4617  N N   . ASP C 97  ? 0.6107 0.6325 0.2911 0.0836  -0.0153 0.1350  97  ASP C N   
4618  C CA  . ASP C 97  ? 0.5836 0.6147 0.2910 0.0815  -0.0202 0.1321  97  ASP C CA  
4619  C C   . ASP C 97  ? 0.5674 0.6043 0.2961 0.0788  -0.0186 0.1383  97  ASP C C   
4620  O O   . ASP C 97  ? 0.5586 0.6013 0.3015 0.0798  -0.0287 0.1404  97  ASP C O   
4621  C CB  . ASP C 97  ? 0.5915 0.6153 0.2928 0.0803  -0.0368 0.1298  97  ASP C CB  
4622  C CG  . ASP C 97  ? 0.6126 0.6202 0.2864 0.0840  -0.0393 0.1219  97  ASP C CG  
4623  O OD1 . ASP C 97  ? 0.6131 0.6238 0.2807 0.0913  -0.0276 0.1169  97  ASP C OD1 
4624  O OD2 . ASP C 97  ? 0.6335 0.6252 0.2879 0.0801  -0.0535 0.1208  97  ASP C OD2 
4625  N N   . TYR C 98  ? 0.5681 0.6036 0.2944 0.0752  -0.0061 0.1415  98  TYR C N   
4626  C CA  . TYR C 98  ? 0.5657 0.5943 0.2993 0.0736  -0.0040 0.1474  98  TYR C CA  
4627  C C   . TYR C 98  ? 0.5345 0.5779 0.2986 0.0732  -0.0036 0.1439  98  TYR C C   
4628  O O   . TYR C 98  ? 0.5305 0.5724 0.3045 0.0783  -0.0088 0.1474  98  TYR C O   
4629  C CB  . TYR C 98  ? 0.5835 0.6021 0.2987 0.0637  0.0091  0.1513  98  TYR C CB  
4630  C CG  . TYR C 98  ? 0.6004 0.5952 0.3052 0.0607  0.0109  0.1583  98  TYR C CG  
4631  C CD1 . TYR C 98  ? 0.6176 0.5924 0.3124 0.0734  0.0004  0.1634  98  TYR C CD1 
4632  C CD2 . TYR C 98  ? 0.6060 0.5970 0.3048 0.0457  0.0227  0.1599  98  TYR C CD2 
4633  C CE1 . TYR C 98  ? 0.6438 0.5879 0.3188 0.0752  0.0015  0.1693  98  TYR C CE1 
4634  C CE2 . TYR C 98  ? 0.6331 0.5906 0.3113 0.0419  0.0234  0.1662  98  TYR C CE2 
4635  C CZ  . TYR C 98  ? 0.6542 0.5844 0.3181 0.0586  0.0127  0.1706  98  TYR C CZ  
4636  O OH  . TYR C 98  ? 0.6909 0.5795 0.3249 0.0592  0.0128  0.1764  98  TYR C OH  
4637  N N   . GLU C 99  ? 0.5147 0.5734 0.2912 0.0696  0.0025  0.1370  99  GLU C N   
4638  C CA  . GLU C 99  ? 0.4867 0.5584 0.2900 0.0682  0.0041  0.1331  99  GLU C CA  
4639  C C   . GLU C 99  ? 0.4751 0.5529 0.2918 0.0717  -0.0089 0.1313  99  GLU C C   
4640  O O   . GLU C 99  ? 0.4585 0.5451 0.2954 0.0723  -0.0112 0.1324  99  GLU C O   
4641  C CB  . GLU C 99  ? 0.4745 0.5614 0.2829 0.0661  0.0135  0.1260  99  GLU C CB  
4642  C CG  . GLU C 99  ? 0.4802 0.5755 0.2821 0.0578  0.0274  0.1282  99  GLU C CG  
4643  C CD  . GLU C 99  ? 0.5071 0.5985 0.2816 0.0560  0.0310  0.1315  99  GLU C CD  
4644  O OE1 . GLU C 99  ? 0.5162 0.6075 0.2780 0.0649  0.0266  0.1278  99  GLU C OE1 
4645  O OE2 . GLU C 99  ? 0.5236 0.6089 0.2849 0.0445  0.0380  0.1379  99  GLU C OE2 
4646  N N   . GLU C 100 ? 0.4874 0.5610 0.2896 0.0724  -0.0177 0.1289  100 GLU C N   
4647  C CA  . GLU C 100 ? 0.4846 0.5646 0.2928 0.0696  -0.0318 0.1285  100 GLU C CA  
4648  C C   . GLU C 100 ? 0.4857 0.5773 0.3023 0.0732  -0.0395 0.1362  100 GLU C C   
4649  O O   . GLU C 100 ? 0.4729 0.5851 0.3076 0.0709  -0.0470 0.1372  100 GLU C O   
4650  C CB  . GLU C 100 ? 0.5086 0.5738 0.2894 0.0672  -0.0407 0.1250  100 GLU C CB  
4651  C CG  . GLU C 100 ? 0.5132 0.5658 0.2813 0.0679  -0.0373 0.1162  100 GLU C CG  
4652  C CD  . GLU C 100 ? 0.5007 0.5567 0.2814 0.0603  -0.0429 0.1125  100 GLU C CD  
4653  O OE1 . GLU C 100 ? 0.5048 0.5656 0.2870 0.0497  -0.0558 0.1152  100 GLU C OE1 
4654  O OE2 . GLU C 100 ? 0.4885 0.5451 0.2768 0.0639  -0.0346 0.1072  100 GLU C OE2 
4655  N N   . LEU C 101 ? 0.5044 0.5845 0.3052 0.0801  -0.0376 0.1417  101 LEU C N   
4656  C CA  . LEU C 101 ? 0.5126 0.6008 0.3148 0.0899  -0.0446 0.1489  101 LEU C CA  
4657  C C   . LEU C 101 ? 0.4995 0.5921 0.3183 0.0965  -0.0384 0.1506  101 LEU C C   
4658  O O   . LEU C 101 ? 0.4924 0.6078 0.3257 0.1046  -0.0454 0.1534  101 LEU C O   
4659  C CB  . LEU C 101 ? 0.5440 0.6095 0.3169 0.0970  -0.0443 0.1543  101 LEU C CB  
4660  C CG  . LEU C 101 ? 0.5614 0.6312 0.3274 0.1127  -0.0529 0.1616  101 LEU C CG  
4661  C CD1 . LEU C 101 ? 0.5513 0.6600 0.3339 0.1139  -0.0678 0.1624  101 LEU C CD1 
4662  C CD2 . LEU C 101 ? 0.5977 0.6385 0.3288 0.1183  -0.0531 0.1664  101 LEU C CD2 
4663  N N   . LYS C 102 ? 0.4992 0.5725 0.3137 0.0928  -0.0255 0.1493  102 LYS C N   
4664  C CA  . LYS C 102 ? 0.4909 0.5616 0.3165 0.0963  -0.0192 0.1501  102 LYS C CA  
4665  C C   . LYS C 102 ? 0.4590 0.5590 0.3165 0.0948  -0.0223 0.1461  102 LYS C C   
4666  O O   . LYS C 102 ? 0.4538 0.5623 0.3220 0.1041  -0.0232 0.1483  102 LYS C O   
4667  C CB  . LYS C 102 ? 0.4944 0.5460 0.3112 0.0853  -0.0054 0.1484  102 LYS C CB  
4668  C CG  . LYS C 102 ? 0.5331 0.5498 0.3149 0.0852  -0.0008 0.1548  102 LYS C CG  
4669  C CD  . LYS C 102 ? 0.5362 0.5455 0.3101 0.0674  0.0122  0.1534  102 LYS C CD  
4670  C CE  . LYS C 102 ? 0.5689 0.5424 0.3154 0.0621  0.0176  0.1590  102 LYS C CE  
4671  N NZ  . LYS C 102 ? 0.5697 0.5468 0.3115 0.0396  0.0299  0.1580  102 LYS C NZ  
4672  N N   . HIS C 103 ? 0.4430 0.5550 0.3106 0.0838  -0.0242 0.1402  103 HIS C N   
4673  C CA  . HIS C 103 ? 0.4194 0.5549 0.3113 0.0787  -0.0283 0.1367  103 HIS C CA  
4674  C C   . HIS C 103 ? 0.4206 0.5853 0.3211 0.0826  -0.0411 0.1411  103 HIS C C   
4675  O O   . HIS C 103 ? 0.4041 0.5942 0.3255 0.0835  -0.0431 0.1416  103 HIS C O   
4676  C CB  . HIS C 103 ? 0.4149 0.5456 0.3030 0.0671  -0.0291 0.1295  103 HIS C CB  
4677  C CG  . HIS C 103 ? 0.3979 0.5445 0.3027 0.0587  -0.0340 0.1260  103 HIS C CG  
4678  N ND1 . HIS C 103 ? 0.3779 0.5266 0.2994 0.0576  -0.0261 0.1222  103 HIS C ND1 
4679  C CD2 . HIS C 103 ? 0.4016 0.5622 0.3061 0.0482  -0.0465 0.1262  103 HIS C CD2 
4680  C CE1 . HIS C 103 ? 0.3701 0.5312 0.3004 0.0482  -0.0331 0.1201  103 HIS C CE1 
4681  N NE2 . HIS C 103 ? 0.3854 0.5541 0.3047 0.0406  -0.0456 0.1227  103 HIS C NE2 
4682  N N   . LEU C 104 ? 0.4411 0.6069 0.3254 0.0846  -0.0498 0.1447  104 LEU C N   
4683  C CA  . LEU C 104 ? 0.4453 0.6476 0.3366 0.0881  -0.0629 0.1497  104 LEU C CA  
4684  C C   . LEU C 104 ? 0.4467 0.6658 0.3464 0.1098  -0.0614 0.1550  104 LEU C C   
4685  O O   . LEU C 104 ? 0.4379 0.7016 0.3549 0.1143  -0.0689 0.1579  104 LEU C O   
4686  C CB  . LEU C 104 ? 0.4705 0.6668 0.3388 0.0878  -0.0718 0.1526  104 LEU C CB  
4687  C CG  . LEU C 104 ? 0.4754 0.6978 0.3426 0.0708  -0.0867 0.1528  104 LEU C CG  
4688  C CD1 . LEU C 104 ? 0.4745 0.6744 0.3337 0.0502  -0.0863 0.1456  104 LEU C CD1 
4689  C CD2 . LEU C 104 ? 0.5022 0.7184 0.3458 0.0745  -0.0951 0.1566  104 LEU C CD2 
4690  N N   . LEU C 105 ? 0.5019 0.6967 0.3274 0.2262  -0.0198 0.1559  105 LEU C N   
4691  C CA  . LEU C 105 ? 0.5107 0.7064 0.3331 0.2391  -0.0155 0.1564  105 LEU C CA  
4692  C C   . LEU C 105 ? 0.5166 0.7156 0.3348 0.2458  -0.0108 0.1550  105 LEU C C   
4693  O O   . LEU C 105 ? 0.5235 0.7295 0.3420 0.2563  -0.0061 0.1556  105 LEU C O   
4694  C CB  . LEU C 105 ? 0.5179 0.6920 0.3320 0.2423  -0.0152 0.1496  105 LEU C CB  
4695  C CG  . LEU C 105 ? 0.5234 0.6928 0.3357 0.2412  -0.0175 0.1534  105 LEU C CG  
4696  C CD1 . LEU C 105 ? 0.5341 0.6779 0.3357 0.2406  -0.0154 0.1463  105 LEU C CD1 
4697  C CD2 . LEU C 105 ? 0.5300 0.7133 0.3475 0.2526  -0.0178 0.1612  105 LEU C CD2 
4698  N N   . SER C 106 ? 0.5174 0.7103 0.3304 0.2404  -0.0125 0.1526  106 SER C N   
4699  C CA  . SER C 106 ? 0.5277 0.7229 0.3320 0.2452  -0.0088 0.1527  106 SER C CA  
4700  C C   . SER C 106 ? 0.5309 0.7483 0.3403 0.2438  -0.0032 0.1620  106 SER C C   
4701  O O   . SER C 106 ? 0.5418 0.7653 0.3437 0.2489  0.0031  0.1625  106 SER C O   
4702  C CB  . SER C 106 ? 0.5312 0.7123 0.3268 0.2403  -0.0144 0.1491  106 SER C CB  
4703  O OG  . SER C 106 ? 0.5277 0.7117 0.3281 0.2300  -0.0180 0.1555  106 SER C OG  
4704  N N   . ARG C 107 ? 0.5238 0.7541 0.3461 0.2359  -0.0049 0.1681  107 ARG C N   
4705  C CA  . ARG C 107 ? 0.5263 0.7815 0.3587 0.2330  0.0008  0.1755  107 ARG C CA  
4706  C C   . ARG C 107 ? 0.5224 0.7973 0.3695 0.2412  0.0027  0.1761  107 ARG C C   
4707  O O   . ARG C 107 ? 0.5212 0.8213 0.3826 0.2386  0.0063  0.1805  107 ARG C O   
4708  C CB  . ARG C 107 ? 0.5230 0.7823 0.3625 0.2182  -0.0027 0.1810  107 ARG C CB  
4709  C CG  . ARG C 107 ? 0.5349 0.7815 0.3621 0.2102  -0.0024 0.1843  107 ARG C CG  
4710  C CD  . ARG C 107 ? 0.5366 0.7928 0.3738 0.1957  -0.0023 0.1911  107 ARG C CD  
4711  N NE  . ARG C 107 ? 0.5476 0.7818 0.3739 0.1872  -0.0070 0.1935  107 ARG C NE  
4712  C CZ  . ARG C 107 ? 0.5662 0.7961 0.3829 0.1795  -0.0027 0.2013  107 ARG C CZ  
4713  N NH1 . ARG C 107 ? 0.5757 0.8246 0.3925 0.1772  0.0085  0.2069  107 ARG C NH1 
4714  N NH2 . ARG C 107 ? 0.5780 0.7833 0.3845 0.1738  -0.0096 0.2032  107 ARG C NH2 
4715  N N   . ILE C 108 ? 0.5225 0.7857 0.3671 0.2511  -0.0001 0.1715  108 ILE C N   
4716  C CA  . ILE C 108 ? 0.5231 0.7992 0.3798 0.2604  -0.0015 0.1728  108 ILE C CA  
4717  C C   . ILE C 108 ? 0.5341 0.8047 0.3872 0.2765  0.0031  0.1676  108 ILE C C   
4718  O O   . ILE C 108 ? 0.5395 0.7856 0.3786 0.2799  0.0031  0.1618  108 ILE C O   
4719  C CB  . ILE C 108 ? 0.5193 0.7833 0.3750 0.2567  -0.0106 0.1740  108 ILE C CB  
4720  C CG1 . ILE C 108 ? 0.5098 0.7824 0.3714 0.2414  -0.0152 0.1776  108 ILE C CG1 
4721  C CG2 . ILE C 108 ? 0.5260 0.7989 0.3900 0.2684  -0.0143 0.1766  108 ILE C CG2 
4722  C CD1 . ILE C 108 ? 0.5083 0.7653 0.3636 0.2347  -0.0226 0.1766  108 ILE C CD1 
4723  N N   . ASN C 109 ? 0.5385 0.8329 0.4063 0.2862  0.0070  0.1684  109 ASN C N   
4724  C CA  . ASN C 109 ? 0.5513 0.8429 0.4194 0.3032  0.0116  0.1625  109 ASN C CA  
4725  C C   . ASN C 109 ? 0.5581 0.8479 0.4354 0.3156  0.0044  0.1642  109 ASN C C   
4726  O O   . ASN C 109 ? 0.5715 0.8455 0.4442 0.3291  0.0056  0.1593  109 ASN C O   
4727  C CB  . ASN C 109 ? 0.5561 0.8752 0.4341 0.3077  0.0227  0.1598  109 ASN C CB  
4728  C CG  . ASN C 109 ? 0.5640 0.8715 0.4229 0.3056  0.0310  0.1544  109 ASN C CG  
4729  O OD1 . ASN C 109 ? 0.5770 0.8846 0.4327 0.3172  0.0382  0.1468  109 ASN C OD1 
4730  N ND2 . ASN C 109 ? 0.5592 0.8557 0.4045 0.2916  0.0291  0.1578  109 ASN C ND2 
4731  N N   . HIS C 110 ? 0.5520 0.8564 0.4410 0.3114  -0.0036 0.1709  110 HIS C N   
4732  C CA  . HIS C 110 ? 0.5631 0.8642 0.4576 0.3236  -0.0129 0.1740  110 HIS C CA  
4733  C C   . HIS C 110 ? 0.5590 0.8623 0.4538 0.3144  -0.0245 0.1814  110 HIS C C   
4734  O O   . HIS C 110 ? 0.5463 0.8749 0.4537 0.3037  -0.0259 0.1838  110 HIS C O   
4735  C CB  . HIS C 110 ? 0.5697 0.9006 0.4880 0.3399  -0.0109 0.1716  110 HIS C CB  
4736  C CG  . HIS C 110 ? 0.5883 0.9081 0.5091 0.3578  -0.0205 0.1736  110 HIS C CG  
4737  N ND1 . HIS C 110 ? 0.5937 0.9429 0.5396 0.3714  -0.0265 0.1742  110 HIS C ND1 
4738  C CD2 . HIS C 110 ? 0.6057 0.8867 0.5069 0.3644  -0.0256 0.1752  110 HIS C CD2 
4739  C CE1 . HIS C 110 ? 0.6152 0.9422 0.5552 0.3871  -0.0362 0.1771  110 HIS C CE1 
4740  N NE2 . HIS C 110 ? 0.6237 0.9079 0.5354 0.3823  -0.0351 0.1783  110 HIS C NE2 
4741  N N   . PHE C 111 ? 0.5732 0.8482 0.4523 0.3181  -0.0321 0.1846  111 PHE C N   
4742  C CA  . PHE C 111 ? 0.5777 0.8520 0.4528 0.3127  -0.0440 0.1916  111 PHE C CA  
4743  C C   . PHE C 111 ? 0.5976 0.8777 0.4808 0.3313  -0.0538 0.1960  111 PHE C C   
4744  O O   . PHE C 111 ? 0.6134 0.8784 0.4946 0.3472  -0.0517 0.1940  111 PHE C O   
4745  C CB  . PHE C 111 ? 0.5856 0.8218 0.4335 0.3029  -0.0455 0.1927  111 PHE C CB  
4746  C CG  . PHE C 111 ? 0.5676 0.8015 0.4099 0.2833  -0.0412 0.1893  111 PHE C CG  
4747  C CD1 . PHE C 111 ? 0.5524 0.8119 0.4069 0.2718  -0.0439 0.1905  111 PHE C CD1 
4748  C CD2 . PHE C 111 ? 0.5681 0.7734 0.3941 0.2765  -0.0352 0.1839  111 PHE C CD2 
4749  C CE1 . PHE C 111 ? 0.5394 0.7936 0.3892 0.2553  -0.0408 0.1869  111 PHE C CE1 
4750  C CE2 . PHE C 111 ? 0.5535 0.7569 0.3768 0.2606  -0.0326 0.1797  111 PHE C CE2 
4751  C CZ  . PHE C 111 ? 0.5399 0.7663 0.3745 0.2506  -0.0356 0.1815  111 PHE C CZ  
4752  N N   . GLU C 112 ? 0.5991 0.9004 0.4916 0.3299  -0.0655 0.2012  112 GLU C N   
4753  C CA  . GLU C 112 ? 0.6232 0.9245 0.5179 0.3470  -0.0794 0.2071  112 GLU C CA  
4754  C C   . GLU C 112 ? 0.6362 0.9193 0.5074 0.3373  -0.0913 0.2149  112 GLU C C   
4755  O O   . GLU C 112 ? 0.6222 0.9228 0.4963 0.3215  -0.0942 0.2149  112 GLU C O   
4756  C CB  . GLU C 112 ? 0.6175 0.9666 0.5475 0.3572  -0.0849 0.2050  112 GLU C CB  
4757  C CG  . GLU C 112 ? 0.6445 0.9935 0.5819 0.3817  -0.0982 0.2086  112 GLU C CG  
4758  C CD  . GLU C 112 ? 0.6448 1.0365 0.6088 0.3868  -0.1127 0.2097  112 GLU C CD  
4759  O OE1 . GLU C 112 ? 0.6224 1.0569 0.6158 0.3791  -0.1065 0.2030  112 GLU C OE1 
4760  O OE2 . GLU C 112 ? 0.6700 1.0524 0.6253 0.3981  -0.1306 0.2171  112 GLU C OE2 
4761  N N   . LYS C 113 ? 0.6660 0.9123 0.5124 0.3458  -0.0976 0.2214  113 LYS C N   
4762  C CA  . LYS C 113 ? 0.6849 0.9085 0.5023 0.3356  -0.1069 0.2291  113 LYS C CA  
4763  C C   . LYS C 113 ? 0.6995 0.9462 0.5241 0.3439  -0.1260 0.2358  113 LYS C C   
4764  O O   . LYS C 113 ? 0.7112 0.9725 0.5541 0.3649  -0.1346 0.2374  113 LYS C O   
4765  C CB  . LYS C 113 ? 0.7167 0.8891 0.5020 0.3400  -0.1051 0.2342  113 LYS C CB  
4766  C CG  . LYS C 113 ? 0.7369 0.8798 0.4865 0.3243  -0.1084 0.2406  113 LYS C CG  
4767  C CD  . LYS C 113 ? 0.7453 0.8466 0.4711 0.3141  -0.0944 0.2375  113 LYS C CD  
4768  C CE  . LYS C 113 ? 0.7740 0.8418 0.4911 0.3309  -0.0928 0.2406  113 LYS C CE  
4769  N NZ  . LYS C 113 ? 0.7778 0.8105 0.4770 0.3182  -0.0778 0.2347  113 LYS C NZ  
4770  N N   . ILE C 114 ? 0.6995 0.9513 0.5114 0.3280  -0.1329 0.2382  114 ILE C N   
4771  C CA  . ILE C 114 ? 0.7187 0.9890 0.5313 0.3342  -0.1530 0.2444  114 ILE C CA  
4772  C C   . ILE C 114 ? 0.7420 0.9860 0.5153 0.3195  -0.1598 0.2507  114 ILE C C   
4773  O O   . ILE C 114 ? 0.7318 0.9589 0.4884 0.2996  -0.1477 0.2467  114 ILE C O   
4774  C CB  . ILE C 114 ? 0.6911 1.0164 0.5416 0.3296  -0.1571 0.2373  114 ILE C CB  
4775  C CG1 . ILE C 114 ? 0.6613 0.9947 0.5136 0.3041  -0.1444 0.2298  114 ILE C CG1 
4776  C CG2 . ILE C 114 ? 0.6771 1.0331 0.5667 0.3467  -0.1529 0.2318  114 ILE C CG2 
4777  C CD1 . ILE C 114 ? 0.6469 1.0235 0.5228 0.2938  -0.1524 0.2251  114 ILE C CD1 
4778  N N   . GLN C 115 ? 0.7757 1.0174 0.5347 0.3298  -0.1795 0.2600  115 GLN C N   
4779  C CA  . GLN C 115 ? 0.8046 1.0229 0.5228 0.3167  -0.1877 0.2667  115 GLN C CA  
4780  C C   . GLN C 115 ? 0.7889 1.0469 0.5202 0.3033  -0.1964 0.2608  115 GLN C C   
4781  O O   . GLN C 115 ? 0.7842 1.0813 0.5444 0.3141  -0.2106 0.2594  115 GLN C O   
4782  C CB  . GLN C 115 ? 0.8569 1.0463 0.5460 0.3351  -0.2058 0.2813  115 GLN C CB  
4783  C CG  . GLN C 115 ? 0.8909 1.0745 0.5457 0.3272  -0.2228 0.2889  115 GLN C CG  
4784  C CD  . GLN C 115 ? 0.9503 1.0918 0.5655 0.3432  -0.2381 0.3056  115 GLN C CD  
4785  O OE1 . GLN C 115 ? 0.9733 1.0671 0.5610 0.3439  -0.2277 0.3121  115 GLN C OE1 
4786  N NE2 . GLN C 115 ? 0.9786 1.1364 0.5899 0.3558  -0.2637 0.3126  115 GLN C NE2 
4787  N N   . ILE C 116 ? 0.7821 1.0307 0.4940 0.2795  -0.1877 0.2559  116 ILE C N   
4788  C CA  . ILE C 116 ? 0.7717 1.0525 0.4918 0.2644  -0.1953 0.2490  116 ILE C CA  
4789  C C   . ILE C 116 ? 0.8130 1.0739 0.4887 0.2565  -0.2081 0.2554  116 ILE C C   
4790  O O   . ILE C 116 ? 0.8233 1.1110 0.5022 0.2562  -0.2258 0.2549  116 ILE C O   
4791  C CB  . ILE C 116 ? 0.7320 1.0241 0.4692 0.2431  -0.1772 0.2359  116 ILE C CB  
4792  C CG1 . ILE C 116 ? 0.7315 0.9828 0.4437 0.2326  -0.1586 0.2344  116 ILE C CG1 
4793  C CG2 . ILE C 116 ? 0.6955 1.0216 0.4795 0.2494  -0.1705 0.2296  116 ILE C CG2 
4794  C CD1 . ILE C 116 ? 0.7029 0.9605 0.4235 0.2111  -0.1450 0.2219  116 ILE C CD1 
4795  N N   . ILE C 117 ? 0.8388 1.0534 0.4726 0.2494  -0.1989 0.2609  117 ILE C N   
4796  C CA  . ILE C 117 ? 0.8867 1.0750 0.4706 0.2425  -0.2091 0.2691  117 ILE C CA  
4797  C C   . ILE C 117 ? 0.9316 1.0776 0.4843 0.2596  -0.2146 0.2853  117 ILE C C   
4798  O O   . ILE C 117 ? 0.9329 1.0452 0.4752 0.2582  -0.1979 0.2868  117 ILE C O   
4799  C CB  . ILE C 117 ? 0.8856 1.0529 0.4425 0.2159  -0.1914 0.2610  117 ILE C CB  
4800  C CG1 . ILE C 117 ? 0.8586 1.0624 0.4348 0.1988  -0.1921 0.2466  117 ILE C CG1 
4801  C CG2 . ILE C 117 ? 0.9423 1.0683 0.4396 0.2096  -0.1952 0.2717  117 ILE C CG2 
4802  C CD1 . ILE C 117 ? 0.8049 1.0414 0.4330 0.1979  -0.1825 0.2350  117 ILE C CD1 
4803  N N   . PRO C 118 ? 0.9709 1.1178 0.5093 0.2764  -0.2390 0.2972  118 PRO C N   
4804  C CA  . PRO C 118 ? 1.0225 1.1220 0.5247 0.2919  -0.2456 0.3142  118 PRO C CA  
4805  C C   . PRO C 118 ? 1.0648 1.1138 0.5067 0.2729  -0.2355 0.3212  118 PRO C C   
4806  O O   . PRO C 118 ? 1.0727 1.1271 0.4914 0.2530  -0.2353 0.3167  118 PRO C O   
4807  C CB  . PRO C 118 ? 1.0552 1.1727 0.5569 0.3130  -0.2770 0.3239  118 PRO C CB  
4808  C CG  . PRO C 118 ? 1.0092 1.1902 0.5626 0.3124  -0.2838 0.3098  118 PRO C CG  
4809  C CD  . PRO C 118 ? 0.9696 1.1617 0.5295 0.2840  -0.2622 0.2951  118 PRO C CD  
4810  N N   . LYS C 119 ? 1.0934 1.0939 0.5108 0.2779  -0.2261 0.3310  119 LYS C N   
4811  C CA  . LYS C 119 ? 1.1377 1.0873 0.4979 0.2591  -0.2139 0.3380  119 LYS C CA  
4812  C C   . LYS C 119 ? 1.2034 1.1323 0.5104 0.2607  -0.2353 0.3538  119 LYS C C   
4813  O O   . LYS C 119 ? 1.2336 1.1413 0.4953 0.2386  -0.2280 0.3549  119 LYS C O   
4814  C CB  . LYS C 119 ? 1.1552 1.0579 0.5052 0.2653  -0.1999 0.3448  119 LYS C CB  
4815  C CG  . LYS C 119 ? 1.1870 1.0427 0.4899 0.2407  -0.1791 0.3465  119 LYS C CG  
4816  C CD  . LYS C 119 ? 1.1959 1.0116 0.4990 0.2457  -0.1638 0.3494  119 LYS C CD  
4817  C CE  . LYS C 119 ? 1.2456 1.0069 0.4944 0.2237  -0.1467 0.3557  119 LYS C CE  
4818  N NZ  . LYS C 119 ? 1.2663 0.9833 0.5110 0.2306  -0.1358 0.3610  119 LYS C NZ  
4819  N N   . SER C 120 ? 1.2278 1.1635 0.5405 0.2875  -0.2620 0.3656  120 SER C N   
4820  C CA  . SER C 120 ? 1.2900 1.2121 0.5566 0.2935  -0.2880 0.3809  120 SER C CA  
4821  C C   . SER C 120 ? 1.2766 1.2396 0.5421 0.2768  -0.2957 0.3701  120 SER C C   
4822  O O   . SER C 120 ? 1.3278 1.2702 0.5389 0.2659  -0.3044 0.3783  120 SER C O   
4823  C CB  . SER C 120 ? 1.3082 1.2409 0.5957 0.3286  -0.3168 0.3915  120 SER C CB  
4824  O OG  . SER C 120 ? 1.2478 1.2453 0.6021 0.3386  -0.3232 0.3761  120 SER C OG  
4825  N N   . SER C 121 ? 1.2110 1.2299 0.5348 0.2742  -0.2917 0.3516  121 SER C N   
4826  C CA  . SER C 121 ? 1.1942 1.2572 0.5268 0.2605  -0.3007 0.3392  121 SER C CA  
4827  C C   . SER C 121 ? 1.2119 1.2570 0.4992 0.2297  -0.2864 0.3334  121 SER C C   
4828  O O   . SER C 121 ? 1.2153 1.2877 0.4960 0.2189  -0.2973 0.3257  121 SER C O   
4829  C CB  . SER C 121 ? 1.1203 1.2397 0.5236 0.2598  -0.2935 0.3201  121 SER C CB  
4830  O OG  . SER C 121 ? 1.1086 1.2593 0.5544 0.2866  -0.3123 0.3226  121 SER C OG  
4831  N N   . TRP C 122 ? 1.2235 1.2251 0.4817 0.2152  -0.2616 0.3354  122 TRP C N   
4832  C CA  . TRP C 122 ? 1.2464 1.2286 0.4597 0.1862  -0.2460 0.3296  122 TRP C CA  
4833  C C   . TRP C 122 ? 1.3291 1.2722 0.4701 0.1858  -0.2617 0.3484  122 TRP C C   
4834  O O   . TRP C 122 ? 1.3749 1.2655 0.4689 0.1790  -0.2495 0.3605  122 TRP C O   
4835  C CB  . TRP C 122 ? 1.2278 1.1820 0.4413 0.1704  -0.2132 0.3228  122 TRP C CB  
4836  C CG  . TRP C 122 ? 1.1525 1.1430 0.4308 0.1695  -0.1987 0.3045  122 TRP C CG  
4837  C CD1 . TRP C 122 ? 1.1179 1.1099 0.4362 0.1847  -0.1922 0.3047  122 TRP C CD1 
4838  C CD2 . TRP C 122 ? 1.1063 1.1354 0.4150 0.1528  -0.1899 0.2835  122 TRP C CD2 
4839  N NE1 . TRP C 122 ? 1.0547 1.0831 0.4237 0.1781  -0.1799 0.2863  122 TRP C NE1 
4840  C CE2 . TRP C 122 ? 1.0464 1.0970 0.4113 0.1589  -0.1785 0.2735  122 TRP C CE2 
4841  C CE3 . TRP C 122 ? 1.1127 1.1585 0.4052 0.1333  -0.1904 0.2719  122 TRP C CE3 
4842  C CZ2 . TRP C 122 ? 0.9950 1.0804 0.3990 0.1467  -0.1685 0.2540  122 TRP C CZ2 
4843  C CZ3 . TRP C 122 ? 1.0598 1.1411 0.3943 0.1214  -0.1801 0.2511  122 TRP C CZ3 
4844  C CH2 . TRP C 122 ? 1.0026 1.1019 0.3916 0.1283  -0.1695 0.2431  122 TRP C CH2 
4845  N N   . SER C 123 ? 1.3506 1.3195 0.4824 0.1923  -0.2891 0.3505  123 SER C N   
4846  C CA  . SER C 123 ? 1.4326 1.3683 0.4955 0.1954  -0.3100 0.3695  123 SER C CA  
4847  C C   . SER C 123 ? 1.4703 1.3848 0.4744 0.1643  -0.2952 0.3647  123 SER C C   
4848  O O   . SER C 123 ? 1.5455 1.4141 0.4798 0.1605  -0.3008 0.3824  123 SER C O   
4849  C CB  . SER C 123 ? 1.4413 1.4170 0.5192 0.2149  -0.3470 0.3718  123 SER C CB  
4850  O OG  . SER C 123 ? 1.3982 1.4270 0.5081 0.2005  -0.3473 0.3498  123 SER C OG  
4851  N N   . SER C 124 ? 1.4214 1.3684 0.4529 0.1425  -0.2764 0.3408  124 SER C N   
4852  C CA  . SER C 124 ? 1.4493 1.3839 0.4340 0.1122  -0.2596 0.3309  124 SER C CA  
4853  C C   . SER C 124 ? 1.4409 1.3435 0.4170 0.0918  -0.2222 0.3246  124 SER C C   
4854  O O   . SER C 124 ? 1.4632 1.3542 0.4029 0.0658  -0.2039 0.3147  124 SER C O   
4855  C CB  . SER C 124 ? 1.4057 1.3947 0.4255 0.1003  -0.2623 0.3064  124 SER C CB  
4856  O OG  . SER C 124 ? 1.4316 1.4116 0.4096 0.0717  -0.2459 0.2939  124 SER C OG  
4857  N N   . HIS C 125 ? 1.4103 1.3004 0.4208 0.1036  -0.2108 0.3287  125 HIS C N   
4858  C CA  . HIS C 125 ? 1.3994 1.2621 0.4089 0.0864  -0.1768 0.3219  125 HIS C CA  
4859  C C   . HIS C 125 ? 1.4284 1.2446 0.4237 0.1005  -0.1746 0.3422  125 HIS C C   
4860  O O   . HIS C 125 ? 1.4325 1.2487 0.4422 0.1275  -0.1970 0.3567  125 HIS C O   
4861  C CB  . HIS C 125 ? 1.3150 1.2180 0.3957 0.0827  -0.1602 0.2981  125 HIS C CB  
4862  C CG  . HIS C 125 ? 1.2873 1.2296 0.3831 0.0656  -0.1570 0.2758  125 HIS C CG  
4863  N ND1 . HIS C 125 ? 1.2556 1.2437 0.3872 0.0754  -0.1777 0.2686  125 HIS C ND1 
4864  C CD2 . HIS C 125 ? 1.2881 1.2306 0.3697 0.0391  -0.1348 0.2578  125 HIS C CD2 
4865  C CE1 . HIS C 125 ? 1.2396 1.2516 0.3767 0.0556  -0.1690 0.2478  125 HIS C CE1 
4866  N NE2 . HIS C 125 ? 1.2584 1.2439 0.3660 0.0343  -0.1432 0.2405  125 HIS C NE2 
4867  N N   . GLU C 126 ? 1.4505 1.2277 0.4191 0.0820  -0.1471 0.3419  126 GLU C N   
4868  C CA  . GLU C 126 ? 1.4759 1.2069 0.4340 0.0919  -0.1408 0.3582  126 GLU C CA  
4869  C C   . GLU C 126 ? 1.4029 1.1563 0.4308 0.1004  -0.1278 0.3443  126 GLU C C   
4870  O O   . GLU C 126 ? 1.3564 1.1335 0.4157 0.0836  -0.1062 0.3224  126 GLU C O   
4871  C CB  . GLU C 126 ? 1.5357 1.2144 0.4333 0.0659  -0.1162 0.3635  126 GLU C CB  
4872  C CG  . GLU C 126 ? 1.5710 1.1956 0.4517 0.0731  -0.1088 0.3807  126 GLU C CG  
4873  C CD  . GLU C 126 ? 1.6220 1.2182 0.4762 0.1014  -0.1399 0.4083  126 GLU C CD  
4874  O OE1 . GLU C 126 ? 1.6918 1.2624 0.4832 0.0992  -0.1552 0.4252  126 GLU C OE1 
4875  O OE2 . GLU C 126 ? 1.5942 1.1932 0.4899 0.1264  -0.1493 0.4124  126 GLU C OE2 
4876  N N   . ALA C 127 ? 1.3967 1.1424 0.4479 0.1270  -0.1414 0.3564  127 ALA C N   
4877  C CA  . ALA C 127 ? 1.3276 1.0988 0.4454 0.1387  -0.1334 0.3440  127 ALA C CA  
4878  C C   . ALA C 127 ? 1.3426 1.0714 0.4599 0.1463  -0.1221 0.3525  127 ALA C C   
4879  O O   . ALA C 127 ? 1.2900 1.0350 0.4559 0.1506  -0.1103 0.3400  127 ALA C O   
4880  C CB  . ALA C 127 ? 1.2898 1.1060 0.4531 0.1645  -0.1588 0.3440  127 ALA C CB  
4881  N N   . SER C 128 ? 1.4160 1.0893 0.4772 0.1476  -0.1260 0.3735  128 SER C N   
4882  C CA  . SER C 128 ? 1.4383 1.0671 0.4968 0.1580  -0.1195 0.3838  128 SER C CA  
4883  C C   . SER C 128 ? 1.4679 1.0526 0.4948 0.1305  -0.0892 0.3811  128 SER C C   
4884  O O   . SER C 128 ? 1.4918 1.0353 0.5130 0.1353  -0.0816 0.3886  128 SER C O   
4885  C CB  . SER C 128 ? 1.5028 1.0955 0.5259 0.1825  -0.1465 0.4103  128 SER C CB  
4886  O OG  . SER C 128 ? 1.4654 1.0979 0.5360 0.2128  -0.1705 0.4098  128 SER C OG  
4887  N N   . LEU C 129 ? 1.4672 1.0614 0.4756 0.1016  -0.0715 0.3688  129 LEU C N   
4888  C CA  . LEU C 129 ? 1.4898 1.0511 0.4752 0.0729  -0.0402 0.3618  129 LEU C CA  
4889  C C   . LEU C 129 ? 1.4173 1.0227 0.4556 0.0572  -0.0183 0.3321  129 LEU C C   
4890  O O   . LEU C 129 ? 1.4285 1.0249 0.4524 0.0294  0.0071  0.3199  129 LEU C O   
4891  C CB  . LEU C 129 ? 1.5639 1.0916 0.4758 0.0497  -0.0346 0.3727  129 LEU C CB  
4892  C CG  . LEU C 129 ? 1.6519 1.1207 0.4994 0.0604  -0.0520 0.4042  129 LEU C CG  
4893  C CD1 . LEU C 129 ? 1.6622 1.1515 0.5006 0.0842  -0.0876 0.4174  129 LEU C CD1 
4894  C CD2 . LEU C 129 ? 1.7290 1.1498 0.5036 0.0291  -0.0322 0.4123  129 LEU C CD2 
4895  N N   . GLY C 130 ? 1.3467 0.9992 0.4461 0.0754  -0.0282 0.3204  130 GLY C N   
4896  C CA  . GLY C 130 ? 1.2777 0.9710 0.4297 0.0650  -0.0113 0.2938  130 GLY C CA  
4897  C C   . GLY C 130 ? 1.2513 0.9346 0.4379 0.0699  0.0015  0.2864  130 GLY C C   
4898  O O   . GLY C 130 ? 1.1945 0.9100 0.4327 0.0865  -0.0047 0.2777  130 GLY C O   
4899  N N   . VAL C 131 ? 1.2949 0.9331 0.4516 0.0540  0.0201  0.2895  131 VAL C N   
4900  C CA  . VAL C 131 ? 1.2806 0.9026 0.4638 0.0567  0.0327  0.2830  131 VAL C CA  
4901  C C   . VAL C 131 ? 1.2814 0.8963 0.4656 0.0267  0.0627  0.2642  131 VAL C C   
4902  O O   . VAL C 131 ? 1.3037 0.9192 0.4611 0.0033  0.0752  0.2586  131 VAL C O   
4903  C CB  . VAL C 131 ? 1.3383 0.9054 0.4891 0.0705  0.0245  0.3061  131 VAL C CB  
4904  C CG1 . VAL C 131 ? 1.3398 0.9157 0.4924 0.1016  -0.0059 0.3235  131 VAL C CG1 
4905  C CG2 . VAL C 131 ? 1.4190 0.9313 0.5032 0.0483  0.0365  0.3201  131 VAL C CG2 
4906  N N   . SER C 132 ? 1.2585 0.8688 0.4749 0.0277  0.0740  0.2531  132 SER C N   
4907  C CA  . SER C 132 ? 1.2584 0.8629 0.4823 0.0009  0.1018  0.2338  132 SER C CA  
4908  C C   . SER C 132 ? 1.2734 0.8436 0.5048 0.0036  0.1099  0.2344  132 SER C C   
4909  O O   . SER C 132 ? 1.2625 0.8273 0.5098 0.0288  0.0944  0.2432  132 SER C O   
4910  C CB  . SER C 132 ? 1.1876 0.8482 0.4655 -0.0033 0.1080  0.2063  132 SER C CB  
4911  O OG  . SER C 132 ? 1.1804 0.8401 0.4778 -0.0236 0.1318  0.1854  132 SER C OG  
4912  N N   . SER C 133 ? 1.2986 0.8473 0.5204 -0.0231 0.1352  0.2233  133 SER C N   
4913  C CA  . SER C 133 ? 1.3128 0.8303 0.5442 -0.0253 0.1459  0.2196  133 SER C CA  
4914  C C   . SER C 133 ? 1.2425 0.8007 0.5384 -0.0139 0.1448  0.1969  133 SER C C   
4915  O O   . SER C 133 ? 1.2455 0.7842 0.5558 -0.0068 0.1464  0.1946  133 SER C O   
4916  C CB  . SER C 133 ? 1.3609 0.8475 0.5653 -0.0605 0.1748  0.2121  133 SER C CB  
4917  O OG  . SER C 133 ? 1.3229 0.8533 0.5561 -0.0804 0.1910  0.1858  133 SER C OG  
4918  N N   . ALA C 134 ? 1.1828 0.7955 0.5152 -0.0121 0.1416  0.1802  134 ALA C N   
4919  C CA  . ALA C 134 ? 1.1178 0.7704 0.5082 -0.0008 0.1387  0.1596  134 ALA C CA  
4920  C C   . ALA C 134 ? 1.0936 0.7511 0.5017 0.0311  0.1170  0.1705  134 ALA C C   
4921  O O   . ALA C 134 ? 1.0627 0.7319 0.5061 0.0402  0.1167  0.1580  134 ALA C O   
4922  C CB  . ALA C 134 ? 1.0681 0.7726 0.4883 -0.0063 0.1394  0.1414  134 ALA C CB  
4923  N N   . CYS C 135 ? 1.1089 0.7590 0.4929 0.0479  0.0991  0.1925  135 CYS C N   
4924  C CA  . CYS C 135 ? 1.0962 0.7470 0.4929 0.0781  0.0796  0.2043  135 CYS C CA  
4925  C C   . CYS C 135 ? 1.1600 0.7553 0.5147 0.0856  0.0744  0.2272  135 CYS C C   
4926  O O   . CYS C 135 ? 1.1881 0.7725 0.5122 0.0940  0.0607  0.2468  135 CYS C O   
4927  C CB  . CYS C 135 ? 1.0610 0.7522 0.4708 0.0949  0.0604  0.2101  135 CYS C CB  
4928  S SG  . CYS C 135 ? 1.0004 0.7492 0.4465 0.0839  0.0645  0.1881  135 CYS C SG  
4929  N N   . PRO C 136 ? 1.1852 0.7440 0.5379 0.0827  0.0846  0.2246  136 PRO C N   
4930  C CA  . PRO C 136 ? 1.2498 0.7510 0.5638 0.0910  0.0795  0.2460  136 PRO C CA  
4931  C C   . PRO C 136 ? 1.2400 0.7399 0.5727 0.1243  0.0610  0.2536  136 PRO C C   
4932  O O   . PRO C 136 ? 1.1936 0.7213 0.5686 0.1346  0.0610  0.2376  136 PRO C O   
4933  C CB  . PRO C 136 ? 1.2825 0.7461 0.5883 0.0678  0.1024  0.2359  136 PRO C CB  
4934  C CG  . PRO C 136 ? 1.2199 0.7275 0.5782 0.0639  0.1108  0.2080  136 PRO C CG  
4935  C CD  . PRO C 136 ? 1.1647 0.7295 0.5457 0.0666  0.1032  0.2009  136 PRO C CD  
4936  N N   . TYR C 137 ? 1.2864 0.7539 0.5867 0.1409  0.0453  0.2773  137 TYR C N   
4937  C CA  . TYR C 137 ? 1.2884 0.7486 0.6031 0.1732  0.0281  0.2853  137 TYR C CA  
4938  C C   . TYR C 137 ? 1.3679 0.7579 0.6389 0.1784  0.0250  0.3057  137 TYR C C   
4939  O O   . TYR C 137 ? 1.4185 0.7797 0.6444 0.1747  0.0181  0.3259  137 TYR C O   
4940  C CB  . TYR C 137 ? 1.2574 0.7606 0.5865 0.1961  0.0057  0.2934  137 TYR C CB  
4941  C CG  . TYR C 137 ? 1.2666 0.7639 0.6084 0.2302  -0.0131 0.3029  137 TYR C CG  
4942  C CD1 . TYR C 137 ? 1.2328 0.7460 0.6151 0.2455  -0.0113 0.2885  137 TYR C CD1 
4943  C CD2 . TYR C 137 ? 1.3105 0.7879 0.6242 0.2479  -0.0334 0.3254  137 TYR C CD2 
4944  C CE1 . TYR C 137 ? 1.2418 0.7519 0.6376 0.2767  -0.0271 0.2950  137 TYR C CE1 
4945  C CE2 . TYR C 137 ? 1.3189 0.7940 0.6484 0.2804  -0.0510 0.3322  137 TYR C CE2 
4946  C CZ  . TYR C 137 ? 1.2838 0.7759 0.6553 0.2945  -0.0469 0.3165  137 TYR C CZ  
4947  O OH  . TYR C 137 ? 1.2932 0.7849 0.6821 0.3268  -0.0629 0.3213  137 TYR C OH  
4948  N N   . GLN C 138 ? 1.3814 0.7426 0.6645 0.1871  0.0295  0.3001  138 GLN C N   
4949  C CA  . GLN C 138 ? 1.4592 0.7486 0.7042 0.1926  0.0276  0.3176  138 GLN C CA  
4950  C C   . GLN C 138 ? 1.5229 0.7616 0.7138 0.1619  0.0424  0.3293  138 GLN C C   
4951  O O   . GLN C 138 ? 1.5943 0.7791 0.7378 0.1668  0.0336  0.3534  138 GLN C O   
4952  C CB  . GLN C 138 ? 1.4847 0.7649 0.7197 0.2266  0.0005  0.3385  138 GLN C CB  
4953  C CG  . GLN C 138 ? 1.4241 0.7575 0.7119 0.2563  -0.0132 0.3272  138 GLN C CG  
4954  C CD  . GLN C 138 ? 1.4593 0.7725 0.7433 0.2917  -0.0365 0.3436  138 GLN C CD  
4955  O OE1 . GLN C 138 ? 1.5166 0.7941 0.7596 0.2976  -0.0501 0.3665  138 GLN C OE1 
4956  N NE2 . GLN C 138 ? 1.4271 0.7639 0.7538 0.3160  -0.0417 0.3313  138 GLN C NE2 
4957  N N   . GLY C 139 ? 1.4990 0.7554 0.6967 0.1303  0.0647  0.3119  139 GLY C N   
4958  C CA  . GLY C 139 ? 1.5560 0.7692 0.7067 0.0967  0.0840  0.3185  139 GLY C CA  
4959  C C   . GLY C 139 ? 1.5609 0.7917 0.6809 0.0826  0.0826  0.3280  139 GLY C C   
4960  O O   . GLY C 139 ? 1.5839 0.8025 0.6795 0.0500  0.1036  0.3237  139 GLY C O   
4961  N N   . LYS C 140 ? 1.5405 0.8012 0.6626 0.1062  0.0587  0.3393  140 LYS C N   
4962  C CA  . LYS C 140 ? 1.5465 0.8253 0.6391 0.0954  0.0543  0.3482  140 LYS C CA  
4963  C C   . LYS C 140 ? 1.4633 0.8164 0.6016 0.0898  0.0577  0.3255  140 LYS C C   
4964  O O   . LYS C 140 ? 1.3998 0.7939 0.5915 0.1041  0.0544  0.3091  140 LYS C O   
4965  C CB  . LYS C 140 ? 1.5796 0.8464 0.6449 0.1231  0.0248  0.3739  140 LYS C CB  
4966  C CG  . LYS C 140 ? 1.6741 0.8619 0.6829 0.1277  0.0190  0.4003  140 LYS C CG  
4967  C CD  . LYS C 140 ? 1.6806 0.8475 0.7122 0.1604  0.0040  0.4051  140 LYS C CD  
4968  C CE  . LYS C 140 ? 1.7742 0.8547 0.7559 0.1582  0.0068  0.4251  140 LYS C CE  
4969  N NZ  . LYS C 140 ? 1.8529 0.8892 0.7682 0.1606  -0.0088 0.4554  140 LYS C NZ  
4970  N N   . SER C 141 ? 1.4683 0.8359 0.5828 0.0685  0.0646  0.3250  141 SER C N   
4971  C CA  . SER C 141 ? 1.3979 0.8314 0.5500 0.0623  0.0670  0.3050  141 SER C CA  
4972  C C   . SER C 141 ? 1.3574 0.8326 0.5333 0.0917  0.0399  0.3107  141 SER C C   
4973  O O   . SER C 141 ? 1.3956 0.8542 0.5392 0.1059  0.0205  0.3320  141 SER C O   
4974  C CB  . SER C 141 ? 1.4233 0.8564 0.5391 0.0322  0.0814  0.3033  141 SER C CB  
4975  O OG  . SER C 141 ? 1.4502 0.8562 0.5543 0.0023  0.1098  0.2925  141 SER C OG  
4976  N N   . SER C 142 ? 1.2826 0.8118 0.5148 0.1002  0.0385  0.2914  142 SER C N   
4977  C CA  . SER C 142 ? 1.2388 0.8110 0.5013 0.1267  0.0157  0.2937  142 SER C CA  
4978  C C   . SER C 142 ? 1.1727 0.8037 0.4725 0.1178  0.0200  0.2736  142 SER C C   
4979  O O   . SER C 142 ? 1.1689 0.8053 0.4636 0.0924  0.0377  0.2607  142 SER C O   
4980  C CB  . SER C 142 ? 1.2206 0.7914 0.5160 0.1525  0.0077  0.2930  142 SER C CB  
4981  O OG  . SER C 142 ? 1.1827 0.7945 0.5074 0.1775  -0.0127 0.2953  142 SER C OG  
4982  N N   . PHE C 143 ? 1.1233 0.7976 0.4608 0.1385  0.0043  0.2705  143 PHE C N   
4983  C CA  . PHE C 143 ? 1.0631 0.7904 0.4365 0.1322  0.0065  0.2528  143 PHE C CA  
4984  C C   . PHE C 143 ? 1.0110 0.7771 0.4311 0.1557  -0.0062 0.2482  143 PHE C C   
4985  O O   . PHE C 143 ? 1.0218 0.7779 0.4460 0.1779  -0.0180 0.2588  143 PHE C O   
4986  C CB  . PHE C 143 ? 1.0745 0.8161 0.4235 0.1222  -0.0002 0.2578  143 PHE C CB  
4987  C CG  . PHE C 143 ? 1.0289 0.8107 0.4031 0.1062  0.0091  0.2376  143 PHE C CG  
4988  C CD1 . PHE C 143 ? 1.0266 0.8028 0.4020 0.0828  0.0313  0.2211  143 PHE C CD1 
4989  C CD2 . PHE C 143 ? 0.9903 0.8156 0.3887 0.1145  -0.0043 0.2341  143 PHE C CD2 
4990  C CE1 . PHE C 143 ? 0.9871 0.7996 0.3876 0.0701  0.0389  0.2016  143 PHE C CE1 
4991  C CE2 . PHE C 143 ? 0.9524 0.8108 0.3736 0.1005  0.0035  0.2156  143 PHE C CE2 
4992  C CZ  . PHE C 143 ? 0.9509 0.8026 0.3733 0.0793  0.0247  0.1993  143 PHE C CZ  
4993  N N   . PHE C 144 ? 0.9574 0.7665 0.4121 0.1505  -0.0029 0.2319  144 PHE C N   
4994  C CA  . PHE C 144 ? 0.9095 0.7587 0.4048 0.1691  -0.0143 0.2280  144 PHE C CA  
4995  C C   . PHE C 144 ? 0.9235 0.7807 0.4116 0.1882  -0.0352 0.2447  144 PHE C C   
4996  O O   . PHE C 144 ? 0.9333 0.8012 0.4052 0.1826  -0.0435 0.2501  144 PHE C O   
4997  C CB  . PHE C 144 ? 0.8630 0.7528 0.3848 0.1578  -0.0106 0.2123  144 PHE C CB  
4998  C CG  . PHE C 144 ? 0.8460 0.7348 0.3804 0.1406  0.0076  0.1937  144 PHE C CG  
4999  C CD1 . PHE C 144 ? 0.8232 0.7137 0.3841 0.1471  0.0134  0.1838  144 PHE C CD1 
5000  C CD2 . PHE C 144 ? 0.8535 0.7419 0.3745 0.1181  0.0185  0.1846  144 PHE C CD2 
5001  C CE1 . PHE C 144 ? 0.8084 0.7007 0.3831 0.1322  0.0281  0.1656  144 PHE C CE1 
5002  C CE2 . PHE C 144 ? 0.8377 0.7288 0.3748 0.1033  0.0345  0.1657  144 PHE C CE2 
5003  C CZ  . PHE C 144 ? 0.8149 0.7084 0.3795 0.1106  0.0385  0.1563  144 PHE C CZ  
5004  N N   . ARG C 145 ? 0.9253 0.7790 0.4270 0.2108  -0.0438 0.2513  145 ARG C N   
5005  C CA  . ARG C 145 ? 0.9464 0.8036 0.4419 0.2314  -0.0641 0.2670  145 ARG C CA  
5006  C C   . ARG C 145 ? 0.9130 0.8196 0.4328 0.2368  -0.0773 0.2653  145 ARG C C   
5007  O O   . ARG C 145 ? 0.9343 0.8466 0.4445 0.2486  -0.0949 0.2773  145 ARG C O   
5008  C CB  . ARG C 145 ? 0.9523 0.7983 0.4636 0.2552  -0.0686 0.2707  145 ARG C CB  
5009  C CG  . ARG C 145 ? 0.9929 0.7861 0.4800 0.2527  -0.0582 0.2739  145 ARG C CG  
5010  C CD  . ARG C 145 ? 1.0208 0.7947 0.5099 0.2797  -0.0700 0.2842  145 ARG C CD  
5011  N NE  . ARG C 145 ? 1.0523 0.7788 0.5275 0.2782  -0.0583 0.2833  145 ARG C NE  
5012  C CZ  . ARG C 145 ? 1.1129 0.7851 0.5460 0.2730  -0.0572 0.2963  145 ARG C CZ  
5013  N NH1 . ARG C 145 ? 1.1523 0.8085 0.5484 0.2693  -0.0678 0.3126  145 ARG C NH1 
5014  N NH2 . ARG C 145 ? 1.1378 0.7695 0.5636 0.2707  -0.0453 0.2930  145 ARG C NH2 
5015  N N   . ASN C 146 ? 0.8641 0.8056 0.4155 0.2285  -0.0697 0.2505  146 ASN C N   
5016  C CA  . ASN C 146 ? 0.8315 0.8194 0.4097 0.2326  -0.0803 0.2477  146 ASN C CA  
5017  C C   . ASN C 146 ? 0.8346 0.8343 0.3970 0.2149  -0.0833 0.2461  146 ASN C C   
5018  O O   . ASN C 146 ? 0.8175 0.8515 0.3961 0.2177  -0.0947 0.2457  146 ASN C O   
5019  C CB  . ASN C 146 ? 0.7815 0.7990 0.4000 0.2336  -0.0719 0.2340  146 ASN C CB  
5020  C CG  . ASN C 146 ? 0.7767 0.7941 0.4151 0.2543  -0.0726 0.2351  146 ASN C CG  
5021  O OD1 . ASN C 146 ? 0.7961 0.8141 0.4350 0.2726  -0.0850 0.2451  146 ASN C OD1 
5022  N ND2 . ASN C 146 ? 0.7529 0.7705 0.4082 0.2523  -0.0599 0.2240  146 ASN C ND2 
5023  N N   . VAL C 147 ? 0.8583 0.8304 0.3898 0.1961  -0.0723 0.2440  147 VAL C N   
5024  C CA  . VAL C 147 ? 0.8659 0.8466 0.3792 0.1779  -0.0728 0.2405  147 VAL C CA  
5025  C C   . VAL C 147 ? 0.9245 0.8666 0.3855 0.1692  -0.0734 0.2521  147 VAL C C   
5026  O O   . VAL C 147 ? 0.9555 0.8589 0.3946 0.1691  -0.0654 0.2582  147 VAL C O   
5027  C CB  . VAL C 147 ? 0.8328 0.8259 0.3629 0.1588  -0.0561 0.2217  147 VAL C CB  
5028  C CG1 . VAL C 147 ? 0.7816 0.8144 0.3569 0.1651  -0.0589 0.2122  147 VAL C CG1 
5029  C CG2 . VAL C 147 ? 0.8389 0.8028 0.3637 0.1512  -0.0380 0.2153  147 VAL C CG2 
5030  N N   . VAL C 148 ? 0.9426 0.8944 0.3822 0.1609  -0.0826 0.2547  148 VAL C N   
5031  C CA  . VAL C 148 ? 1.0036 0.9206 0.3881 0.1524  -0.0854 0.2672  148 VAL C CA  
5032  C C   . VAL C 148 ? 1.0121 0.9224 0.3747 0.1244  -0.0677 0.2549  148 VAL C C   
5033  O O   . VAL C 148 ? 0.9863 0.9280 0.3632 0.1141  -0.0677 0.2422  148 VAL C O   
5034  C CB  . VAL C 148 ? 1.0266 0.9583 0.3964 0.1633  -0.1104 0.2792  148 VAL C CB  
5035  C CG1 . VAL C 148 ? 1.0975 0.9875 0.4051 0.1578  -0.1158 0.2953  148 VAL C CG1 
5036  C CG2 . VAL C 148 ? 1.0114 0.9606 0.4128 0.1913  -0.1279 0.2872  148 VAL C CG2 
5037  N N   . TRP C 149 ? 1.0499 0.9194 0.3792 0.1115  -0.0519 0.2576  149 TRP C N   
5038  C CA  . TRP C 149 ? 1.0676 0.9285 0.3716 0.0841  -0.0337 0.2463  149 TRP C CA  
5039  C C   . TRP C 149 ? 1.1245 0.9698 0.3739 0.0769  -0.0440 0.2590  149 TRP C C   
5040  O O   . TRP C 149 ? 1.1823 0.9855 0.3856 0.0775  -0.0462 0.2768  149 TRP C O   
5041  C CB  . TRP C 149 ? 1.0857 0.9115 0.3786 0.0713  -0.0108 0.2425  149 TRP C CB  
5042  C CG  . TRP C 149 ? 1.0946 0.9185 0.3736 0.0425  0.0118  0.2257  149 TRP C CG  
5043  C CD1 . TRP C 149 ? 1.0944 0.9397 0.3641 0.0277  0.0135  0.2150  149 TRP C CD1 
5044  C CD2 . TRP C 149 ? 1.1076 0.9077 0.3816 0.0249  0.0365  0.2161  149 TRP C CD2 
5045  N NE1 . TRP C 149 ? 1.1050 0.9425 0.3656 0.0029  0.0382  0.1990  149 TRP C NE1 
5046  C CE2 . TRP C 149 ? 1.1128 0.9238 0.3766 0.0003  0.0527  0.1993  149 TRP C CE2 
5047  C CE3 . TRP C 149 ? 1.1160 0.8879 0.3950 0.0270  0.0467  0.2185  149 TRP C CE3 
5048  C CZ2 . TRP C 149 ? 1.1248 0.9221 0.3856 -0.0219 0.0790  0.1847  149 TRP C CZ2 
5049  C CZ3 . TRP C 149 ? 1.1287 0.8858 0.4038 0.0039  0.0723  0.2044  149 TRP C CZ3 
5050  C CH2 . TRP C 149 ? 1.1322 0.9032 0.3992 -0.0201 0.0883  0.1876  149 TRP C CH2 
5051  N N   . LEU C 150 ? 1.1107 0.9885 0.3642 0.0699  -0.0508 0.2498  150 LEU C N   
5052  C CA  . LEU C 150 ? 1.1612 1.0314 0.3659 0.0647  -0.0641 0.2601  150 LEU C CA  
5053  C C   . LEU C 150 ? 1.2032 1.0503 0.3621 0.0363  -0.0439 0.2535  150 LEU C C   
5054  O O   . LEU C 150 ? 1.1751 1.0362 0.3547 0.0190  -0.0230 0.2321  150 LEU C O   
5055  C CB  . LEU C 150 ? 1.1292 1.0462 0.3596 0.0695  -0.0814 0.2518  150 LEU C CB  
5056  C CG  . LEU C 150 ? 1.0977 1.0417 0.3674 0.0962  -0.1043 0.2594  150 LEU C CG  
5057  C CD1 . LEU C 150 ? 1.0671 1.0573 0.3628 0.0947  -0.1167 0.2475  150 LEU C CD1 
5058  C CD2 . LEU C 150 ? 1.1473 1.0657 0.3845 0.1151  -0.1250 0.2839  150 LEU C CD2 
5059  N N   . ILE C 151 ? 1.2734 1.0851 0.3697 0.0321  -0.0504 0.2716  151 ILE C N   
5060  C CA  . ILE C 151 ? 1.3246 1.1126 0.3675 0.0043  -0.0323 0.2677  151 ILE C CA  
5061  C C   . ILE C 151 ? 1.3771 1.1619 0.3675 0.0026  -0.0518 0.2793  151 ILE C C   
5062  O O   . ILE C 151 ? 1.3802 1.1753 0.3726 0.0244  -0.0804 0.2931  151 ILE C O   
5063  C CB  . ILE C 151 ? 1.3735 1.1079 0.3793 -0.0061 -0.0132 0.2790  151 ILE C CB  
5064  C CG1 . ILE C 151 ? 1.4347 1.1266 0.3950 0.0110  -0.0338 0.3101  151 ILE C CG1 
5065  C CG2 . ILE C 151 ? 1.3223 1.0617 0.3810 -0.0038 0.0040  0.2665  151 ILE C CG2 
5066  C CD1 . ILE C 151 ? 1.4824 1.1180 0.4107 0.0038  -0.0173 0.3230  151 ILE C CD1 
5067  N N   . LYS C 152 ? 1.4196 1.1915 0.3635 -0.0235 -0.0359 0.2723  152 LYS C N   
5068  C CA  . LYS C 152 ? 1.4757 1.2434 0.3629 -0.0295 -0.0516 0.2806  152 LYS C CA  
5069  C C   . LYS C 152 ? 1.5495 1.2711 0.3771 -0.0167 -0.0715 0.3131  152 LYS C C   
5070  O O   . LYS C 152 ? 1.5796 1.2574 0.3880 -0.0156 -0.0619 0.3279  152 LYS C O   
5071  C CB  . LYS C 152 ? 1.5078 1.2693 0.3568 -0.0626 -0.0253 0.2642  152 LYS C CB  
5072  C CG  . LYS C 152 ? 1.5565 1.2694 0.3649 -0.0821 0.0025  0.2705  152 LYS C CG  
5073  C CD  . LYS C 152 ? 1.5788 1.2944 0.3611 -0.1155 0.0320  0.2491  152 LYS C CD  
5074  C CE  . LYS C 152 ? 1.6427 1.3058 0.3730 -0.1367 0.0581  0.2591  152 LYS C CE  
5075  N NZ  . LYS C 152 ? 1.6688 1.3336 0.3732 -0.1710 0.0904  0.2375  152 LYS C NZ  
5076  N N   . LYS C 153 ? 1.5805 1.3115 0.3796 -0.0069 -0.1000 0.3234  153 LYS C N   
5077  C CA  . LYS C 153 ? 1.6593 1.3469 0.3953 0.0053  -0.1226 0.3541  153 LYS C CA  
5078  C C   . LYS C 153 ? 1.7349 1.4018 0.3918 -0.0175 -0.1205 0.3577  153 LYS C C   
5079  O O   . LYS C 153 ? 1.7256 1.4288 0.3824 -0.0247 -0.1286 0.3430  153 LYS C O   
5080  C CB  . LYS C 153 ? 1.6417 1.3564 0.4061 0.0380  -0.1613 0.3648  153 LYS C CB  
5081  C CG  . LYS C 153 ? 1.7071 1.3756 0.4294 0.0602  -0.1849 0.3970  153 LYS C CG  
5082  C CD  . LYS C 153 ? 1.7173 1.4130 0.4422 0.0849  -0.2258 0.4062  153 LYS C CD  
5083  C CE  . LYS C 153 ? 1.6327 1.3850 0.4449 0.1079  -0.2391 0.3934  153 LYS C CE  
5084  N NZ  . LYS C 153 ? 1.5962 1.3368 0.4536 0.1247  -0.2304 0.3976  153 LYS C NZ  
5085  N N   . ASN C 154 ? 1.8125 1.4195 0.4010 -0.0294 -0.1091 0.3770  154 ASN C N   
5086  C CA  . ASN C 154 ? 1.8949 1.4735 0.3991 -0.0545 -0.1022 0.3822  154 ASN C CA  
5087  C C   . ASN C 154 ? 1.8676 1.4818 0.3813 -0.0841 -0.0760 0.3501  154 ASN C C   
5088  O O   . ASN C 154 ? 1.8950 1.5261 0.3749 -0.0933 -0.0859 0.3435  154 ASN C O   
5089  C CB  . ASN C 154 ? 1.9537 1.5259 0.4080 -0.0375 -0.1419 0.4032  154 ASN C CB  
5090  C CG  . ASN C 154 ? 2.0632 1.5816 0.4134 -0.0580 -0.1378 0.4215  154 ASN C CG  
5091  O OD1 . ASN C 154 ? 2.1104 1.5774 0.4197 -0.0752 -0.1124 0.4320  154 ASN C OD1 
5092  N ND2 . ASN C 154 ? 2.1070 1.6366 0.4125 -0.0571 -0.1629 0.4252  154 ASN C ND2 
5093  N N   . SER C 155 ? 1.8144 1.4401 0.3758 -0.0978 -0.0436 0.3291  155 SER C N   
5094  C CA  . SER C 155 ? 1.7897 1.4446 0.3643 -0.1261 -0.0142 0.2971  155 SER C CA  
5095  C C   . SER C 155 ? 1.7350 1.4500 0.3530 -0.1212 -0.0285 0.2737  155 SER C C   
5096  O O   . SER C 155 ? 1.7494 1.4809 0.3472 -0.1432 -0.0158 0.2539  155 SER C O   
5097  C CB  . SER C 155 ? 1.8793 1.4955 0.3670 -0.1573 0.0064  0.3010  155 SER C CB  
5098  O OG  . SER C 155 ? 1.9143 1.4826 0.3782 -0.1704 0.0322  0.3119  155 SER C OG  
5099  N N   . THR C 156 ? 1.6752 1.4220 0.3526 -0.0934 -0.0539 0.2754  156 THR C N   
5100  C CA  . THR C 156 ? 1.6167 1.4204 0.3447 -0.0887 -0.0659 0.2526  156 THR C CA  
5101  C C   . THR C 156 ? 1.5335 1.3673 0.3452 -0.0651 -0.0744 0.2487  156 THR C C   
5102  O O   . THR C 156 ? 1.5335 1.3552 0.3535 -0.0411 -0.0943 0.2703  156 THR C O   
5103  C CB  . THR C 156 ? 1.6536 1.4698 0.3473 -0.0790 -0.1006 0.2623  156 THR C CB  
5104  O OG1 . THR C 156 ? 1.6399 1.4590 0.3570 -0.0474 -0.1320 0.2832  156 THR C OG1 
5105  C CG2 . THR C 156 ? 1.7531 1.5281 0.3501 -0.0957 -0.1006 0.2770  156 THR C CG2 
5106  N N   . TYR C 157 ? 1.4666 1.3381 0.3385 -0.0717 -0.0594 0.2210  157 TYR C N   
5107  C CA  . TYR C 157 ? 1.3887 1.2922 0.3381 -0.0511 -0.0678 0.2155  157 TYR C CA  
5108  C C   . TYR C 157 ? 1.3521 1.3036 0.3363 -0.0476 -0.0847 0.1990  157 TYR C C   
5109  O O   . TYR C 157 ? 1.3151 1.2923 0.3315 -0.0609 -0.0695 0.1729  157 TYR C O   
5110  C CB  . TYR C 157 ? 1.3401 1.2456 0.3350 -0.0589 -0.0386 0.1988  157 TYR C CB  
5111  C CG  . TYR C 157 ? 1.2729 1.1981 0.3356 -0.0361 -0.0466 0.2002  157 TYR C CG  
5112  C CD1 . TYR C 157 ? 1.2786 1.1784 0.3418 -0.0182 -0.0532 0.2219  157 TYR C CD1 
5113  C CD2 . TYR C 157 ? 1.2076 1.1748 0.3317 -0.0329 -0.0472 0.1797  157 TYR C CD2 
5114  C CE1 . TYR C 157 ? 1.2204 1.1387 0.3430 0.0017  -0.0594 0.2220  157 TYR C CE1 
5115  C CE2 . TYR C 157 ? 1.1507 1.1348 0.3325 -0.0134 -0.0535 0.1814  157 TYR C CE2 
5116  C CZ  . TYR C 157 ? 1.1567 1.1176 0.3375 0.0037  -0.0592 0.2021  157 TYR C CZ  
5117  O OH  . TYR C 157 ? 1.1029 1.0809 0.3384 0.0224  -0.0645 0.2028  157 TYR C OH  
5118  N N   . PRO C 158 ? 1.3651 1.3286 0.3435 -0.0298 -0.1168 0.2135  158 PRO C N   
5119  C CA  . PRO C 158 ? 1.3345 1.3434 0.3454 -0.0275 -0.1340 0.1982  158 PRO C CA  
5120  C C   . PRO C 158 ? 1.2540 1.2971 0.3458 -0.0164 -0.1319 0.1856  158 PRO C C   
5121  O O   . PRO C 158 ? 1.2241 1.2576 0.3455 -0.0035 -0.1259 0.1943  158 PRO C O   
5122  C CB  . PRO C 158 ? 1.3730 1.3826 0.3567 -0.0094 -0.1691 0.2196  158 PRO C CB  
5123  C CG  . PRO C 158 ? 1.3940 1.3669 0.3624 0.0074  -0.1721 0.2458  158 PRO C CG  
5124  C CD  . PRO C 158 ? 1.4118 1.3470 0.3536 -0.0110 -0.1392 0.2438  158 PRO C CD  
5125  N N   . THR C 159 ? 1.2236 1.3041 0.3480 -0.0224 -0.1366 0.1651  159 THR C N   
5126  C CA  . THR C 159 ? 1.1530 1.2645 0.3500 -0.0148 -0.1339 0.1523  159 THR C CA  
5127  C C   . THR C 159 ? 1.1302 1.2540 0.3596 0.0109  -0.1552 0.1703  159 THR C C   
5128  O O   . THR C 159 ? 1.1596 1.2888 0.3690 0.0221  -0.1803 0.1841  159 THR C O   
5129  C CB  . THR C 159 ? 1.1330 1.2793 0.3540 -0.0266 -0.1375 0.1282  159 THR C CB  
5130  O OG1 . THR C 159 ? 1.1601 1.2956 0.3492 -0.0500 -0.1180 0.1100  159 THR C OG1 
5131  C CG2 . THR C 159 ? 1.0644 1.2360 0.3565 -0.0210 -0.1317 0.1155  159 THR C CG2 
5132  N N   . ILE C 160 ? 1.0801 1.2090 0.3592 0.0203  -0.1448 0.1689  160 ILE C N   
5133  C CA  . ILE C 160 ? 1.0521 1.1952 0.3691 0.0438  -0.1601 0.1824  160 ILE C CA  
5134  C C   . ILE C 160 ? 1.0037 1.1890 0.3772 0.0448  -0.1661 0.1676  160 ILE C C   
5135  O O   . ILE C 160 ? 0.9711 1.1640 0.3718 0.0331  -0.1495 0.1497  160 ILE C O   
5136  C CB  . ILE C 160 ? 1.0285 1.1497 0.3631 0.0529  -0.1439 0.1898  160 ILE C CB  
5137  C CG1 . ILE C 160 ? 1.0814 1.1578 0.3609 0.0524  -0.1385 0.2064  160 ILE C CG1 
5138  C CG2 . ILE C 160 ? 0.9923 1.1332 0.3726 0.0758  -0.1567 0.1992  160 ILE C CG2 
5139  C CD1 . ILE C 160 ? 1.0651 1.1160 0.3551 0.0532  -0.1169 0.2079  160 ILE C CD1 
5140  N N   . LYS C 161 ? 1.0026 1.2146 0.3940 0.0585  -0.1899 0.1748  161 LYS C N   
5141  C CA  . LYS C 161 ? 0.9587 1.2106 0.4058 0.0598  -0.1958 0.1630  161 LYS C CA  
5142  C C   . LYS C 161 ? 0.9417 1.2111 0.4219 0.0829  -0.2103 0.1771  161 LYS C C   
5143  O O   . LYS C 161 ? 0.9601 1.2491 0.4384 0.0929  -0.2336 0.1840  161 LYS C O   
5144  C CB  . LYS C 161 ? 0.9756 1.2529 0.4155 0.0474  -0.2102 0.1502  161 LYS C CB  
5145  C CG  . LYS C 161 ? 0.9830 1.2520 0.4059 0.0237  -0.1938 0.1299  161 LYS C CG  
5146  C CD  . LYS C 161 ? 1.0098 1.3004 0.4169 0.0119  -0.2098 0.1180  161 LYS C CD  
5147  C CE  . LYS C 161 ? 1.0196 1.3019 0.4100 -0.0113 -0.1925 0.0957  161 LYS C CE  
5148  N NZ  . LYS C 161 ? 1.0590 1.3552 0.4191 -0.0235 -0.2077 0.0851  161 LYS C NZ  
5149  N N   . ARG C 162 ? 0.9087 1.1724 0.4202 0.0915  -0.1965 0.1799  162 ARG C N   
5150  C CA  . ARG C 162 ? 0.8941 1.1704 0.4356 0.1137  -0.2059 0.1925  162 ARG C CA  
5151  C C   . ARG C 162 ? 0.8448 1.1502 0.4438 0.1139  -0.1986 0.1827  162 ARG C C   
5152  O O   . ARG C 162 ? 0.8190 1.1169 0.4316 0.1027  -0.1799 0.1720  162 ARG C O   
5153  C CB  . ARG C 162 ? 0.9069 1.1458 0.4273 0.1257  -0.1969 0.2071  162 ARG C CB  
5154  C CG  . ARG C 162 ? 0.9639 1.1759 0.4320 0.1327  -0.2103 0.2231  162 ARG C CG  
5155  C CD  . ARG C 162 ? 0.9814 1.2179 0.4561 0.1507  -0.2389 0.2330  162 ARG C CD  
5156  N NE  . ARG C 162 ? 1.0007 1.2169 0.4681 0.1741  -0.2468 0.2514  162 ARG C NE  
5157  C CZ  . ARG C 162 ? 1.0509 1.2240 0.4664 0.1778  -0.2490 0.2664  162 ARG C CZ  
5158  N NH1 . ARG C 162 ? 1.0869 1.2342 0.4521 0.1587  -0.2426 0.2653  162 ARG C NH1 
5159  N NH2 . ARG C 162 ? 1.0679 1.2221 0.4811 0.2000  -0.2567 0.2822  162 ARG C NH2 
5160  N N   . SER C 163 ? 0.8370 1.1759 0.4689 0.1263  -0.2137 0.1860  163 SER C N   
5161  C CA  . SER C 163 ? 0.7965 1.1643 0.4810 0.1262  -0.2076 0.1785  163 SER C CA  
5162  C C   . SER C 163 ? 0.7900 1.1712 0.5010 0.1486  -0.2131 0.1898  163 SER C C   
5163  O O   . SER C 163 ? 0.8151 1.2026 0.5164 0.1637  -0.2312 0.1998  163 SER C O   
5164  C CB  . SER C 163 ? 0.7915 1.1958 0.4971 0.1139  -0.2189 0.1660  163 SER C CB  
5165  O OG  . SER C 163 ? 0.7538 1.1849 0.5086 0.1123  -0.2126 0.1598  163 SER C OG  
5166  N N   . TYR C 164 ? 0.7618 1.1466 0.5050 0.1513  -0.1981 0.1879  164 TYR C N   
5167  C CA  . TYR C 164 ? 0.7539 1.1569 0.5277 0.1708  -0.2010 0.1953  164 TYR C CA  
5168  C C   . TYR C 164 ? 0.7266 1.1635 0.5480 0.1651  -0.1941 0.1866  164 TYR C C   
5169  O O   . TYR C 164 ? 0.7034 1.1307 0.5333 0.1530  -0.1777 0.1800  164 TYR C O   
5170  C CB  . TYR C 164 ? 0.7511 1.1212 0.5132 0.1834  -0.1885 0.2041  164 TYR C CB  
5171  C CG  . TYR C 164 ? 0.7304 1.1210 0.5287 0.2007  -0.1870 0.2076  164 TYR C CG  
5172  C CD1 . TYR C 164 ? 0.7455 1.1552 0.5542 0.2203  -0.2038 0.2148  164 TYR C CD1 
5173  C CD2 . TYR C 164 ? 0.6976 1.0901 0.5204 0.1975  -0.1693 0.2029  164 TYR C CD2 
5174  C CE1 . TYR C 164 ? 0.7277 1.1589 0.5717 0.2360  -0.2010 0.2158  164 TYR C CE1 
5175  C CE2 . TYR C 164 ? 0.6814 1.0939 0.5354 0.2120  -0.1664 0.2050  164 TYR C CE2 
5176  C CZ  . TYR C 164 ? 0.6956 1.1282 0.5612 0.2310  -0.1814 0.2107  164 TYR C CZ  
5177  O OH  . TYR C 164 ? 0.6806 1.1349 0.5788 0.2454  -0.1770 0.2108  164 TYR C OH  
5178  N N   . ASN C 165 ? 0.7357 1.2114 0.5878 0.1744  -0.2069 0.1870  165 ASN C N   
5179  C CA  . ASN C 165 ? 0.7178 1.2285 0.6158 0.1689  -0.2002 0.1797  165 ASN C CA  
5180  C C   . ASN C 165 ? 0.6940 1.2079 0.6135 0.1856  -0.1901 0.1856  165 ASN C C   
5181  O O   . ASN C 165 ? 0.7064 1.2262 0.6279 0.2061  -0.1998 0.1929  165 ASN C O   
5182  C CB  . ASN C 165 ? 0.7424 1.2986 0.6657 0.1681  -0.2189 0.1743  165 ASN C CB  
5183  C CG  . ASN C 165 ? 0.7398 1.3308 0.7068 0.1542  -0.2107 0.1641  165 ASN C CG  
5184  O OD1 . ASN C 165 ? 0.7169 1.3001 0.6976 0.1496  -0.1920 0.1637  165 ASN C OD1 
5185  N ND2 . ASN C 165 ? 0.7752 1.4041 0.7633 0.1466  -0.2253 0.1558  165 ASN C ND2 
5186  N N   . ASN C 166 ? 0.6609 1.1704 0.5957 0.1772  -0.1713 0.1821  166 ASN C N   
5187  C CA  . ASN C 166 ? 0.6400 1.1530 0.5935 0.1908  -0.1600 0.1862  166 ASN C CA  
5188  C C   . ASN C 166 ? 0.6258 1.1876 0.6229 0.1951  -0.1633 0.1825  166 ASN C C   
5189  O O   . ASN C 166 ? 0.6075 1.1882 0.6295 0.1812  -0.1527 0.1766  166 ASN C O   
5190  C CB  . ASN C 166 ? 0.6197 1.1088 0.5698 0.1805  -0.1398 0.1843  166 ASN C CB  
5191  C CG  . ASN C 166 ? 0.6096 1.0939 0.5682 0.1955  -0.1282 0.1888  166 ASN C CG  
5192  O OD1 . ASN C 166 ? 0.6177 1.1091 0.5803 0.2148  -0.1343 0.1935  166 ASN C OD1 
5193  N ND2 . ASN C 166 ? 0.5937 1.0649 0.5542 0.1874  -0.1121 0.1869  166 ASN C ND2 
5194  N N   . THR C 167 ? 0.6341 1.2154 0.6403 0.2145  -0.1780 0.1860  167 THR C N   
5195  C CA  . THR C 167 ? 0.6237 1.2558 0.6747 0.2212  -0.1825 0.1809  167 THR C CA  
5196  C C   . THR C 167 ? 0.6057 1.2461 0.6790 0.2334  -0.1667 0.1816  167 THR C C   
5197  O O   . THR C 167 ? 0.5966 1.2803 0.7101 0.2341  -0.1638 0.1753  167 THR C O   
5198  C CB  . THR C 167 ? 0.6469 1.3000 0.7019 0.2391  -0.2075 0.1830  167 THR C CB  
5199  O OG1 . THR C 167 ? 0.6664 1.2834 0.6907 0.2599  -0.2126 0.1936  167 THR C OG1 
5200  C CG2 . THR C 167 ? 0.6615 1.3202 0.7025 0.2248  -0.2241 0.1793  167 THR C CG2 
5201  N N   . ASN C 168 ? 0.6007 1.2014 0.6486 0.2420  -0.1559 0.1880  168 ASN C N   
5202  C CA  . ASN C 168 ? 0.5848 1.1895 0.6490 0.2517  -0.1392 0.1876  168 ASN C CA  
5203  C C   . ASN C 168 ? 0.5610 1.1748 0.6389 0.2305  -0.1210 0.1826  168 ASN C C   
5204  O O   . ASN C 168 ? 0.5570 1.1531 0.6192 0.2112  -0.1186 0.1818  168 ASN C O   
5205  C CB  . ASN C 168 ? 0.5910 1.1489 0.6231 0.2638  -0.1320 0.1943  168 ASN C CB  
5206  C CG  . ASN C 168 ? 0.6148 1.1406 0.6131 0.2729  -0.1472 0.2015  168 ASN C CG  
5207  O OD1 . ASN C 168 ? 0.6338 1.1575 0.6313 0.2944  -0.1576 0.2059  168 ASN C OD1 
5208  N ND2 . ASN C 168 ? 0.6177 1.1163 0.5866 0.2566  -0.1479 0.2028  168 ASN C ND2 
5209  N N   . GLN C 169 ? 0.5471 1.1862 0.6523 0.2341  -0.1077 0.1791  169 GLN C N   
5210  C CA  . GLN C 169 ? 0.5308 1.1727 0.6434 0.2144  -0.0890 0.1765  169 GLN C CA  
5211  C C   . GLN C 169 ? 0.5249 1.1252 0.6092 0.2168  -0.0744 0.1812  169 GLN C C   
5212  O O   . GLN C 169 ? 0.5202 1.1268 0.6127 0.2174  -0.0585 0.1801  169 GLN C O   
5213  C CB  . GLN C 169 ? 0.5253 1.2176 0.6805 0.2120  -0.0805 0.1697  169 GLN C CB  
5214  C CG  . GLN C 169 ? 0.5275 1.2380 0.7000 0.2347  -0.0749 0.1678  169 GLN C CG  
5215  C CD  . GLN C 169 ? 0.5217 1.2674 0.7246 0.2261  -0.0553 0.1615  169 GLN C CD  
5216  O OE1 . GLN C 169 ? 0.5173 1.2548 0.7138 0.2046  -0.0407 0.1626  169 GLN C OE1 
5217  N NE2 . GLN C 169 ? 0.5243 1.3083 0.7595 0.2430  -0.0545 0.1549  169 GLN C NE2 
5218  N N   . GLU C 170 ? 0.5259 1.0849 0.5763 0.2176  -0.0800 0.1854  170 GLU C N   
5219  C CA  . GLU C 170 ? 0.5212 1.0397 0.5442 0.2193  -0.0692 0.1885  170 GLU C CA  
5220  C C   . GLU C 170 ? 0.5192 1.0041 0.5154 0.2057  -0.0728 0.1893  170 GLU C C   
5221  O O   . GLU C 170 ? 0.5244 1.0122 0.5170 0.1998  -0.0851 0.1885  170 GLU C O   
5222  C CB  . GLU C 170 ? 0.5300 1.0313 0.5407 0.2423  -0.0718 0.1913  170 GLU C CB  
5223  C CG  . GLU C 170 ? 0.5304 1.0547 0.5625 0.2577  -0.0634 0.1888  170 GLU C CG  
5224  C CD  . GLU C 170 ? 0.5396 1.0948 0.5954 0.2750  -0.0761 0.1875  170 GLU C CD  
5225  O OE1 . GLU C 170 ? 0.5430 1.1158 0.6075 0.2706  -0.0906 0.1876  170 GLU C OE1 
5226  O OE2 . GLU C 170 ? 0.5450 1.1072 0.6112 0.2939  -0.0725 0.1855  170 GLU C OE2 
5227  N N   . ASP C 171 ? 0.5128 0.9674 0.4907 0.2010  -0.0624 0.1899  171 ASP C N   
5228  C CA  . ASP C 171 ? 0.5125 0.9323 0.4646 0.1931  -0.0650 0.1892  171 ASP C CA  
5229  C C   . ASP C 171 ? 0.5221 0.9220 0.4548 0.2076  -0.0721 0.1918  171 ASP C C   
5230  O O   . ASP C 171 ? 0.5268 0.9298 0.4625 0.2245  -0.0714 0.1943  171 ASP C O   
5231  C CB  . ASP C 171 ? 0.5065 0.9008 0.4466 0.1874  -0.0534 0.1884  171 ASP C CB  
5232  C CG  . ASP C 171 ? 0.5017 0.9063 0.4544 0.1713  -0.0469 0.1875  171 ASP C CG  
5233  O OD1 . ASP C 171 ? 0.5017 0.9213 0.4659 0.1583  -0.0521 0.1853  171 ASP C OD1 
5234  O OD2 . ASP C 171 ? 0.5010 0.8963 0.4499 0.1711  -0.0367 0.1890  171 ASP C OD2 
5235  N N   . LEU C 172 ? 0.5270 0.9053 0.4392 0.2003  -0.0780 0.1908  172 LEU C N   
5236  C CA  . LEU C 172 ? 0.5416 0.8978 0.4313 0.2105  -0.0842 0.1942  172 LEU C CA  
5237  C C   . LEU C 172 ? 0.5421 0.8629 0.4072 0.2018  -0.0789 0.1909  172 LEU C C   
5238  O O   . LEU C 172 ? 0.5389 0.8559 0.3995 0.1866  -0.0796 0.1859  172 LEU C O   
5239  C CB  . LEU C 172 ? 0.5562 0.9271 0.4443 0.2107  -0.0994 0.1965  172 LEU C CB  
5240  C CG  . LEU C 172 ? 0.5808 0.9291 0.4433 0.2223  -0.1078 0.2026  172 LEU C CG  
5241  C CD1 . LEU C 172 ? 0.5882 0.9399 0.4592 0.2442  -0.1091 0.2078  172 LEU C CD1 
5242  C CD2 . LEU C 172 ? 0.5981 0.9575 0.4526 0.2179  -0.1235 0.2042  172 LEU C CD2 
5243  N N   . LEU C 173 ? 0.5466 0.8424 0.3975 0.2114  -0.0733 0.1921  173 LEU C N   
5244  C CA  . LEU C 173 ? 0.5496 0.8135 0.3791 0.2041  -0.0679 0.1878  173 LEU C CA  
5245  C C   . LEU C 173 ? 0.5719 0.8199 0.3776 0.2028  -0.0749 0.1909  173 LEU C C   
5246  O O   . LEU C 173 ? 0.5896 0.8259 0.3838 0.2152  -0.0782 0.1974  173 LEU C O   
5247  C CB  . LEU C 173 ? 0.5483 0.7927 0.3731 0.2136  -0.0589 0.1867  173 LEU C CB  
5248  C CG  . LEU C 173 ? 0.5542 0.7671 0.3593 0.2070  -0.0530 0.1810  173 LEU C CG  
5249  C CD1 . LEU C 173 ? 0.5401 0.7521 0.3497 0.1921  -0.0492 0.1722  173 LEU C CD1 
5250  C CD2 . LEU C 173 ? 0.5568 0.7526 0.3584 0.2178  -0.0460 0.1797  173 LEU C CD2 
5251  N N   . VAL C 174 ? 0.5738 0.8194 0.3706 0.1875  -0.0767 0.1860  174 VAL C N   
5252  C CA  . VAL C 174 ? 0.5982 0.8273 0.3675 0.1827  -0.0818 0.1881  174 VAL C CA  
5253  C C   . VAL C 174 ? 0.6027 0.8021 0.3537 0.1734  -0.0708 0.1811  174 VAL C C   
5254  O O   . VAL C 174 ? 0.5848 0.7838 0.3465 0.1645  -0.0632 0.1714  174 VAL C O   
5255  C CB  . VAL C 174 ? 0.6015 0.8489 0.3710 0.1706  -0.0906 0.1852  174 VAL C CB  
5256  C CG1 . VAL C 174 ? 0.6333 0.8643 0.3699 0.1671  -0.0970 0.1889  174 VAL C CG1 
5257  C CG2 . VAL C 174 ? 0.5928 0.8750 0.3876 0.1770  -0.1003 0.1889  174 VAL C CG2 
5258  N N   . LEU C 175 ? 0.6292 0.8036 0.3531 0.1754  -0.0703 0.1860  175 LEU C N   
5259  C CA  . LEU C 175 ? 0.6386 0.7855 0.3440 0.1648  -0.0590 0.1789  175 LEU C CA  
5260  C C   . LEU C 175 ? 0.6701 0.8033 0.3436 0.1543  -0.0616 0.1811  175 LEU C C   
5261  O O   . LEU C 175 ? 0.6947 0.8248 0.3510 0.1616  -0.0720 0.1928  175 LEU C O   
5262  C CB  . LEU C 175 ? 0.6473 0.7707 0.3462 0.1751  -0.0525 0.1825  175 LEU C CB  
5263  C CG  . LEU C 175 ? 0.6233 0.7561 0.3476 0.1868  -0.0493 0.1807  175 LEU C CG  
5264  C CD1 . LEU C 175 ? 0.6404 0.7502 0.3547 0.1992  -0.0462 0.1860  175 LEU C CD1 
5265  C CD2 . LEU C 175 ? 0.5997 0.7350 0.3387 0.1774  -0.0404 0.1674  175 LEU C CD2 
5266  N N   . TRP C 176 ? 0.6715 0.7964 0.3366 0.1376  -0.0522 0.1694  176 TRP C N   
5267  C CA  . TRP C 176 ? 0.7052 0.8132 0.3356 0.1251  -0.0505 0.1697  176 TRP C CA  
5268  C C   . TRP C 176 ? 0.7068 0.7979 0.3315 0.1106  -0.0337 0.1559  176 TRP C C   
5269  O O   . TRP C 176 ? 0.6812 0.7747 0.3301 0.1119  -0.0258 0.1465  176 TRP C O   
5270  C CB  . TRP C 176 ? 0.7091 0.8376 0.3361 0.1170  -0.0604 0.1675  176 TRP C CB  
5271  C CG  . TRP C 176 ? 0.6821 0.8283 0.3331 0.1058  -0.0555 0.1513  176 TRP C CG  
5272  C CD1 . TRP C 176 ? 0.6881 0.8297 0.3306 0.0889  -0.0464 0.1368  176 TRP C CD1 
5273  C CD2 . TRP C 176 ? 0.6484 0.8180 0.3355 0.1107  -0.0591 0.1476  176 TRP C CD2 
5274  N NE1 . TRP C 176 ? 0.6603 0.8198 0.3326 0.0846  -0.0455 0.1244  176 TRP C NE1 
5275  C CE2 . TRP C 176 ? 0.6368 0.8120 0.3351 0.0972  -0.0533 0.1317  176 TRP C CE2 
5276  C CE3 . TRP C 176 ? 0.6295 0.8151 0.3398 0.1248  -0.0660 0.1560  176 TRP C CE3 
5277  C CZ2 . TRP C 176 ? 0.6096 0.8020 0.3392 0.0974  -0.0551 0.1257  176 TRP C CZ2 
5278  C CZ3 . TRP C 176 ? 0.6022 0.8066 0.3424 0.1234  -0.0662 0.1499  176 TRP C CZ3 
5279  C CH2 . TRP C 176 ? 0.5936 0.7994 0.3422 0.1098  -0.0613 0.1357  176 TRP C CH2 
5280  N N   . GLY C 177 ? 0.7393 0.8141 0.3317 0.0966  -0.0281 0.1541  177 GLY C N   
5281  C CA  . GLY C 177 ? 0.7451 0.8055 0.3321 0.0813  -0.0105 0.1396  177 GLY C CA  
5282  C C   . GLY C 177 ? 0.7740 0.8291 0.3322 0.0624  -0.0043 0.1324  177 GLY C C   
5283  O O   . GLY C 177 ? 0.7984 0.8546 0.3314 0.0609  -0.0145 0.1414  177 GLY C O   
5284  N N   . ILE C 178 ? 0.7727 0.8235 0.3356 0.0480  0.0123  0.1150  178 ILE C N   
5285  C CA  . ILE C 178 ? 0.8028 0.8473 0.3384 0.0279  0.0231  0.1048  178 ILE C CA  
5286  C C   . ILE C 178 ? 0.8275 0.8462 0.3459 0.0169  0.0418  0.1011  178 ILE C C   
5287  O O   . ILE C 178 ? 0.8066 0.8229 0.3502 0.0215  0.0487  0.0952  178 ILE C O   
5288  C CB  . ILE C 178 ? 0.7782 0.8470 0.3410 0.0186  0.0275  0.0822  178 ILE C CB  
5289  C CG1 . ILE C 178 ? 0.8123 0.8772 0.3442 -0.0018 0.0378  0.0713  178 ILE C CG1 
5290  C CG2 . ILE C 178 ? 0.7461 0.8210 0.3478 0.0201  0.0377  0.0659  178 ILE C CG2 
5291  C CD1 . ILE C 178 ? 0.7950 0.8772 0.3533 -0.0132 0.0490  0.0443  178 ILE C CD1 
5292  N N   . HIS C 179 ? 0.8748 0.8738 0.3491 0.0016  0.0500  0.1044  179 HIS C N   
5293  C CA  . HIS C 179 ? 0.9040 0.8782 0.3597 -0.0133 0.0706  0.0993  179 HIS C CA  
5294  C C   . HIS C 179 ? 0.9066 0.8926 0.3673 -0.0347 0.0895  0.0740  179 HIS C C   
5295  O O   . HIS C 179 ? 0.9197 0.9163 0.3647 -0.0441 0.0884  0.0680  179 HIS C O   
5296  C CB  . HIS C 179 ? 0.9625 0.9012 0.3619 -0.0177 0.0701  0.1207  179 HIS C CB  
5297  C CG  . HIS C 179 ? 0.9996 0.9101 0.3753 -0.0367 0.0931  0.1160  179 HIS C CG  
5298  N ND1 . HIS C 179 ? 1.0547 0.9442 0.3799 -0.0570 0.1047  0.1186  179 HIS C ND1 
5299  C CD2 . HIS C 179 ? 0.9914 0.8923 0.3872 -0.0400 0.1075  0.1077  179 HIS C CD2 
5300  C CE1 . HIS C 179 ? 1.0789 0.9461 0.3943 -0.0728 0.1264  0.1128  179 HIS C CE1 
5301  N NE2 . HIS C 179 ? 1.0409 0.9153 0.4001 -0.0628 0.1281  0.1056  179 HIS C NE2 
5302  N N   . HIS C 180 ? 0.8952 0.8806 0.3792 -0.0420 0.1065  0.0579  180 HIS C N   
5303  C CA  . HIS C 180 ? 0.8982 0.8957 0.3923 -0.0619 0.1266  0.0315  180 HIS C CA  
5304  C C   . HIS C 180 ? 0.9466 0.9155 0.4037 -0.0823 0.1481  0.0325  180 HIS C C   
5305  O O   . HIS C 180 ? 0.9468 0.9015 0.4134 -0.0821 0.1561  0.0333  180 HIS C O   
5306  C CB  . HIS C 180 ? 0.8509 0.8719 0.4031 -0.0554 0.1297  0.0102  180 HIS C CB  
5307  C CG  . HIS C 180 ? 0.8072 0.8524 0.3948 -0.0367 0.1102  0.0096  180 HIS C CG  
5308  N ND1 . HIS C 180 ? 0.7843 0.8549 0.4027 -0.0387 0.1107  -0.0118 180 HIS C ND1 
5309  C CD2 . HIS C 180 ? 0.7851 0.8317 0.3822 -0.0163 0.0908  0.0274  180 HIS C CD2 
5310  C CE1 . HIS C 180 ? 0.7514 0.8355 0.3945 -0.0213 0.0923  -0.0059 180 HIS C CE1 
5311  N NE2 . HIS C 180 ? 0.7506 0.8221 0.3816 -0.0081 0.0807  0.0175  180 HIS C NE2 
5312  N N   . PRO C 181 ? 0.9907 0.9498 0.4036 -0.1009 0.1579  0.0324  181 PRO C N   
5313  C CA  . PRO C 181 ? 1.0447 0.9729 0.4151 -0.1226 0.1793  0.0356  181 PRO C CA  
5314  C C   . PRO C 181 ? 1.0403 0.9823 0.4368 -0.1429 0.2065  0.0054  181 PRO C C   
5315  O O   . PRO C 181 ? 0.9996 0.9761 0.4430 -0.1403 0.2077  -0.0190 181 PRO C O   
5316  C CB  . PRO C 181 ? 1.0934 1.0100 0.4068 -0.1336 0.1771  0.0461  181 PRO C CB  
5317  C CG  . PRO C 181 ? 1.0589 1.0122 0.3996 -0.1281 0.1669  0.0304  181 PRO C CG  
5318  C CD  . PRO C 181 ? 0.9961 0.9717 0.3947 -0.1040 0.1500  0.0285  181 PRO C CD  
5319  N N   . ASN C 182 ? 1.0844 0.9992 0.4511 -0.1630 0.2281  0.0068  182 ASN C N   
5320  C CA  . ASN C 182 ? 1.0827 1.0106 0.4766 -0.1833 0.2556  -0.0220 182 ASN C CA  
5321  C C   . ASN C 182 ? 1.0981 1.0473 0.4859 -0.2042 0.2736  -0.0462 182 ASN C C   
5322  O O   . ASN C 182 ? 1.0662 1.0490 0.5037 -0.2081 0.2843  -0.0770 182 ASN C O   
5323  C CB  . ASN C 182 ? 1.1295 1.0196 0.4924 -0.2003 0.2743  -0.0123 182 ASN C CB  
5324  C CG  . ASN C 182 ? 1.1085 0.9828 0.4911 -0.1815 0.2612  0.0022  182 ASN C CG  
5325  O OD1 . ASN C 182 ? 1.0815 0.9688 0.5086 -0.1822 0.2696  -0.0153 182 ASN C OD1 
5326  N ND2 . ASN C 182 ? 1.1211 0.9693 0.4725 -0.1638 0.2399  0.0330  182 ASN C ND2 
5327  N N   . ASP C 183 ? 1.1494 1.0788 0.4759 -0.2169 0.2764  -0.0330 183 ASP C N   
5328  C CA  . ASP C 183 ? 1.1726 1.1190 0.4836 -0.2380 0.2940  -0.0547 183 ASP C CA  
5329  C C   . ASP C 183 ? 1.2021 1.1390 0.4611 -0.2354 0.2780  -0.0371 183 ASP C C   
5330  O O   . ASP C 183 ? 1.2094 1.1246 0.4415 -0.2189 0.2546  -0.0070 183 ASP C O   
5331  C CB  . ASP C 183 ? 1.2255 1.1551 0.5079 -0.2705 0.3290  -0.0654 183 ASP C CB  
5332  C CG  . ASP C 183 ? 1.2849 1.1620 0.5040 -0.2787 0.3315  -0.0329 183 ASP C CG  
5333  O OD1 . ASP C 183 ? 1.3090 1.1612 0.4819 -0.2670 0.3102  -0.0034 183 ASP C OD1 
5334  O OD2 . ASP C 183 ? 1.3097 1.1698 0.5260 -0.2970 0.3548  -0.0375 183 ASP C OD2 
5335  N N   . ALA C 184 ? 1.2195 1.1746 0.4663 -0.2516 0.2903  -0.0577 184 ALA C N   
5336  C CA  . ALA C 184 ? 1.2505 1.2005 0.4480 -0.2519 0.2765  -0.0459 184 ALA C CA  
5337  C C   . ALA C 184 ? 1.3219 1.2255 0.4386 -0.2615 0.2755  -0.0137 184 ALA C C   
5338  O O   . ALA C 184 ? 1.3421 1.2354 0.4201 -0.2520 0.2531  0.0067  184 ALA C O   
5339  C CB  . ALA C 184 ? 1.2615 1.2383 0.4601 -0.2707 0.2946  -0.0778 184 ALA C CB  
5340  N N   . ALA C 185 ? 1.3621 1.2373 0.4541 -0.2804 0.2991  -0.0096 185 ALA C N   
5341  C CA  . ALA C 185 ? 1.4357 1.2599 0.4501 -0.2900 0.2995  0.0223  185 ALA C CA  
5342  C C   . ALA C 185 ? 1.4252 1.2245 0.4353 -0.2621 0.2691  0.0563  185 ALA C C   
5343  O O   . ALA C 185 ? 1.4733 1.2413 0.4241 -0.2574 0.2527  0.0849  185 ALA C O   
5344  C CB  . ALA C 185 ? 1.4795 1.2796 0.4749 -0.3184 0.3344  0.0161  185 ALA C CB  
5345  N N   . GLU C 186 ? 1.3649 1.1784 0.4374 -0.2431 0.2613  0.0525  186 GLU C N   
5346  C CA  . GLU C 186 ? 1.3491 1.1444 0.4258 -0.2153 0.2335  0.0809  186 GLU C CA  
5347  C C   . GLU C 186 ? 1.3162 1.1354 0.4049 -0.1910 0.2015  0.0885  186 GLU C C   
5348  O O   . GLU C 186 ? 1.3319 1.1307 0.3946 -0.1732 0.1774  0.1164  186 GLU C O   
5349  C CB  . GLU C 186 ? 1.2971 1.1012 0.4352 -0.2039 0.2363  0.0726  186 GLU C CB  
5350  C CG  . GLU C 186 ? 1.2936 1.0710 0.4286 -0.1795 0.2139  0.1016  186 GLU C CG  
5351  C CD  . GLU C 186 ? 1.2546 1.0346 0.4406 -0.1724 0.2201  0.0932  186 GLU C CD  
5352  O OE1 . GLU C 186 ? 1.1911 1.0109 0.4391 -0.1627 0.2175  0.0717  186 GLU C OE1 
5353  O OE2 . GLU C 186 ? 1.2905 1.0310 0.4530 -0.1763 0.2267  0.1083  186 GLU C OE2 
5354  N N   . GLN C 187 ? 1.2722 1.1346 0.4022 -0.1904 0.2014  0.0627  187 GLN C N   
5355  C CA  . GLN C 187 ? 1.2445 1.1318 0.3861 -0.1722 0.1742  0.0659  187 GLN C CA  
5356  C C   . GLN C 187 ? 1.3066 1.1720 0.3776 -0.1765 0.1617  0.0867  187 GLN C C   
5357  O O   . GLN C 187 ? 1.3056 1.1662 0.3665 -0.1561 0.1338  0.1091  187 GLN C O   
5358  C CB  . GLN C 187 ? 1.2031 1.1336 0.3899 -0.1777 0.1816  0.0324  187 GLN C CB  
5359  C CG  . GLN C 187 ? 1.1860 1.1405 0.3771 -0.1662 0.1583  0.0317  187 GLN C CG  
5360  C CD  . GLN C 187 ? 1.1406 1.1041 0.3653 -0.1372 0.1294  0.0487  187 GLN C CD  
5361  O OE1 . GLN C 187 ? 1.0932 1.0659 0.3680 -0.1243 0.1287  0.0451  187 GLN C OE1 
5362  N NE2 . GLN C 187 ? 1.1564 1.1191 0.3540 -0.1272 0.1055  0.0663  187 GLN C NE2 
5363  N N   . THR C 188 ? 1.3627 1.2160 0.3851 -0.2031 0.1825  0.0786  188 THR C N   
5364  C CA  . THR C 188 ? 1.4307 1.2608 0.3787 -0.2101 0.1724  0.0973  188 THR C CA  
5365  C C   . THR C 188 ? 1.4809 1.2621 0.3796 -0.2022 0.1613  0.1337  188 THR C C   
5366  O O   . THR C 188 ? 1.5109 1.2790 0.3711 -0.1894 0.1353  0.1567  188 THR C O   
5367  C CB  . THR C 188 ? 1.4846 1.3103 0.3879 -0.2429 0.2009  0.0795  188 THR C CB  
5368  O OG1 . THR C 188 ? 1.5070 1.3110 0.4052 -0.2624 0.2320  0.0743  188 THR C OG1 
5369  C CG2 . THR C 188 ? 1.4431 1.3161 0.3895 -0.2488 0.2082  0.0437  188 THR C CG2 
5370  N N   . LYS C 189 ? 1.4911 1.2456 0.3928 -0.2090 0.1798  0.1380  189 LYS C N   
5371  C CA  . LYS C 189 ? 1.5399 1.2440 0.3985 -0.2012 0.1707  0.1714  189 LYS C CA  
5372  C C   . LYS C 189 ? 1.5048 1.2133 0.3891 -0.1659 0.1354  0.1917  189 LYS C C   
5373  O O   . LYS C 189 ? 1.5520 1.2272 0.3898 -0.1543 0.1156  0.2208  189 LYS C O   
5374  C CB  . LYS C 189 ? 1.5466 1.2262 0.4173 -0.2139 0.1971  0.1680  189 LYS C CB  
5375  C CG  . LYS C 189 ? 1.5912 1.2179 0.4267 -0.2028 0.1866  0.2012  189 LYS C CG  
5376  C CD  . LYS C 189 ? 1.6044 1.2043 0.4485 -0.2185 0.2140  0.1969  189 LYS C CD  
5377  C CE  . LYS C 189 ? 1.6582 1.1997 0.4607 -0.2082 0.2031  0.2307  189 LYS C CE  
5378  N NZ  . LYS C 189 ? 1.6328 1.1635 0.4779 -0.2058 0.2150  0.2257  189 LYS C NZ  
5379  N N   . LEU C 190 ? 1.4247 1.1738 0.3829 -0.1490 0.1279  0.1760  190 LEU C N   
5380  C CA  . LEU C 190 ? 1.3862 1.1439 0.3765 -0.1168 0.0983  0.1919  190 LEU C CA  
5381  C C   . LEU C 190 ? 1.3725 1.1590 0.3631 -0.1030 0.0709  0.1948  190 LEU C C   
5382  O O   . LEU C 190 ? 1.3883 1.1638 0.3618 -0.0829 0.0446  0.2181  190 LEU C O   
5383  C CB  . LEU C 190 ? 1.3109 1.0969 0.3776 -0.1056 0.1032  0.1748  190 LEU C CB  
5384  C CG  . LEU C 190 ? 1.3168 1.0733 0.3920 -0.1068 0.1180  0.1796  190 LEU C CG  
5385  C CD1 . LEU C 190 ? 1.2460 1.0352 0.3933 -0.1026 0.1277  0.1557  190 LEU C CD1 
5386  C CD2 . LEU C 190 ? 1.3381 1.0638 0.3962 -0.0836 0.0962  0.2095  190 LEU C CD2 
5387  N N   . TYR C 191 ? 1.3429 1.1669 0.3559 -0.1135 0.0771  0.1697  191 TYR C N   
5388  C CA  . TYR C 191 ? 1.3191 1.1769 0.3458 -0.1016 0.0528  0.1668  191 TYR C CA  
5389  C C   . TYR C 191 ? 1.3593 1.2241 0.3427 -0.1217 0.0567  0.1559  191 TYR C C   
5390  O O   . TYR C 191 ? 1.3495 1.2398 0.3371 -0.1142 0.0363  0.1534  191 TYR C O   
5391  C CB  . TYR C 191 ? 1.2377 1.1383 0.3422 -0.0909 0.0517  0.1458  191 TYR C CB  
5392  C CG  . TYR C 191 ? 1.1972 1.0927 0.3455 -0.0767 0.0552  0.1497  191 TYR C CG  
5393  C CD1 . TYR C 191 ? 1.1836 1.0741 0.3443 -0.0514 0.0330  0.1710  191 TYR C CD1 
5394  C CD2 . TYR C 191 ? 1.1750 1.0716 0.3521 -0.0885 0.0807  0.1310  191 TYR C CD2 
5395  C CE1 . TYR C 191 ? 1.1495 1.0350 0.3478 -0.0388 0.0367  0.1734  191 TYR C CE1 
5396  C CE2 . TYR C 191 ? 1.1409 1.0330 0.3559 -0.0759 0.0829  0.1337  191 TYR C CE2 
5397  C CZ  . TYR C 191 ? 1.1289 1.0146 0.3528 -0.0513 0.0612  0.1550  191 TYR C CZ  
5398  O OH  . TYR C 191 ? 1.0975 0.9787 0.3568 -0.0390 0.0636  0.1566  191 TYR C OH  
5399  N N   . GLN C 192 ? 1.4059 1.2487 0.3479 -0.1478 0.0834  0.1485  192 GLN C N   
5400  C CA  . GLN C 192 ? 1.4485 1.2965 0.3465 -0.1704 0.0928  0.1348  192 GLN C CA  
5401  C C   . GLN C 192 ? 1.3993 1.2938 0.3445 -0.1760 0.0982  0.1016  192 GLN C C   
5402  O O   . GLN C 192 ? 1.4073 1.3089 0.3520 -0.1983 0.1254  0.0770  192 GLN C O   
5403  C CB  . GLN C 192 ? 1.5097 1.3395 0.3419 -0.1658 0.0676  0.1585  192 GLN C CB  
5404  C CG  . GLN C 192 ? 1.5977 1.3766 0.3483 -0.1840 0.0810  0.1770  192 GLN C CG  
5405  C CD  . GLN C 192 ? 1.6683 1.4301 0.3452 -0.1850 0.0596  0.1954  192 GLN C CD  
5406  O OE1 . GLN C 192 ? 1.7447 1.4597 0.3512 -0.1942 0.0631  0.2176  192 GLN C OE1 
5407  N NE2 . GLN C 192 ? 1.6475 1.4453 0.3381 -0.1764 0.0373  0.1862  192 GLN C NE2 
5408  N N   . ASN C 193 ? 1.3520 1.2771 0.3376 -0.1564 0.0730  0.1001  193 ASN C N   
5409  C CA  . ASN C 193 ? 1.3069 1.2728 0.3383 -0.1599 0.0754  0.0701  193 ASN C CA  
5410  C C   . ASN C 193 ? 1.2642 1.2422 0.3471 -0.1677 0.1025  0.0450  193 ASN C C   
5411  O O   . ASN C 193 ? 1.2249 1.2005 0.3479 -0.1546 0.1032  0.0509  193 ASN C O   
5412  C CB  . ASN C 193 ? 1.2567 1.2504 0.3331 -0.1361 0.0458  0.0749  193 ASN C CB  
5413  C CG  . ASN C 193 ? 1.2937 1.2782 0.3280 -0.1243 0.0163  0.1007  193 ASN C CG  
5414  O OD1 . ASN C 193 ? 1.3478 1.2980 0.3279 -0.1251 0.0138  0.1237  193 ASN C OD1 
5415  N ND2 . ASN C 193 ? 1.2670 1.2816 0.3271 -0.1132 -0.0068 0.0970  193 ASN C ND2 
5416  N N   . PRO C 194 ? 1.2743 1.2656 0.3558 -0.1889 0.1248  0.0161  194 PRO C N   
5417  C CA  . PRO C 194 ? 1.2411 1.2439 0.3692 -0.1972 0.1513  -0.0090 194 PRO C CA  
5418  C C   . PRO C 194 ? 1.1652 1.1984 0.3714 -0.1784 0.1411  -0.0225 194 PRO C C   
5419  O O   . PRO C 194 ? 1.1293 1.1637 0.3773 -0.1718 0.1497  -0.0262 194 PRO C O   
5420  C CB  . PRO C 194 ? 1.2762 1.2887 0.3806 -0.2229 0.1739  -0.0370 194 PRO C CB  
5421  C CG  . PRO C 194 ? 1.3005 1.3205 0.3716 -0.2222 0.1534  -0.0337 194 PRO C CG  
5422  C CD  . PRO C 194 ? 1.3146 1.3146 0.3562 -0.2047 0.1249  0.0031  194 PRO C CD  
5423  N N   . THR C 195 ? 1.1447 1.2008 0.3677 -0.1707 0.1227  -0.0294 195 THR C N   
5424  C CA  . THR C 195 ? 1.0798 1.1615 0.3705 -0.1533 0.1108  -0.0395 195 THR C CA  
5425  C C   . THR C 195 ? 1.0625 1.1436 0.3564 -0.1320 0.0810  -0.0122 195 THR C C   
5426  O O   . THR C 195 ? 1.0913 1.1714 0.3492 -0.1319 0.0643  -0.0008 195 THR C O   
5427  C CB  . THR C 195 ? 1.0707 1.1781 0.3818 -0.1610 0.1125  -0.0689 195 THR C CB  
5428  O OG1 . THR C 195 ? 1.1018 1.2090 0.3955 -0.1834 0.1400  -0.0935 195 THR C OG1 
5429  C CG2 . THR C 195 ? 1.0086 1.1373 0.3910 -0.1460 0.1063  -0.0826 195 THR C CG2 
5430  N N   . THR C 196 ? 1.0178 1.1005 0.3542 -0.1140 0.0745  -0.0027 196 THR C N   
5431  C CA  . THR C 196 ? 1.0010 1.0839 0.3437 -0.0933 0.0489  0.0226  196 THR C CA  
5432  C C   . THR C 196 ? 0.9402 1.0442 0.3465 -0.0768 0.0398  0.0172  196 THR C C   
5433  O O   . THR C 196 ? 0.9113 1.0246 0.3562 -0.0791 0.0528  -0.0028 196 THR C O   
5434  C CB  . THR C 196 ? 1.0222 1.0762 0.3370 -0.0861 0.0481  0.0490  196 THR C CB  
5435  O OG1 . THR C 196 ? 1.0005 1.0470 0.3424 -0.0866 0.0664  0.0420  196 THR C OG1 
5436  C CG2 . THR C 196 ? 1.0903 1.1187 0.3352 -0.1013 0.0535  0.0593  196 THR C CG2 
5437  N N   . TYR C 197 ? 0.9241 1.0356 0.3402 -0.0603 0.0171  0.0353  197 TYR C N   
5438  C CA  . TYR C 197 ? 0.8718 1.0021 0.3426 -0.0455 0.0075  0.0331  197 TYR C CA  
5439  C C   . TYR C 197 ? 0.8610 0.9919 0.3360 -0.0264 -0.0120 0.0586  197 TYR C C   
5440  O O   . TYR C 197 ? 0.8937 1.0140 0.3308 -0.0237 -0.0223 0.0766  197 TYR C O   
5441  C CB  . TYR C 197 ? 0.8599 1.0128 0.3510 -0.0511 0.0009  0.0151  197 TYR C CB  
5442  C CG  . TYR C 197 ? 0.8811 1.0436 0.3483 -0.0506 -0.0190 0.0253  197 TYR C CG  
5443  C CD1 . TYR C 197 ? 0.9280 1.0859 0.3479 -0.0653 -0.0182 0.0209  197 TYR C CD1 
5444  C CD2 . TYR C 197 ? 0.8562 1.0337 0.3480 -0.0358 -0.0388 0.0385  197 TYR C CD2 
5445  C CE1 . TYR C 197 ? 0.9496 1.1177 0.3476 -0.0643 -0.0386 0.0295  197 TYR C CE1 
5446  C CE2 . TYR C 197 ? 0.8757 1.0655 0.3496 -0.0353 -0.0581 0.0462  197 TYR C CE2 
5447  C CZ  . TYR C 197 ? 0.9222 1.1075 0.3493 -0.0490 -0.0590 0.0416  197 TYR C CZ  
5448  O OH  . TYR C 197 ? 0.9433 1.1422 0.3524 -0.0480 -0.0801 0.0484  197 TYR C OH  
5449  N N   . ILE C 198 ? 0.8173 0.9605 0.3383 -0.0130 -0.0172 0.0593  198 ILE C N   
5450  C CA  . ILE C 198 ? 0.8013 0.9523 0.3356 0.0047  -0.0351 0.0791  198 ILE C CA  
5451  C C   . ILE C 198 ? 0.7632 0.9379 0.3427 0.0095  -0.0427 0.0709  198 ILE C C   
5452  O O   . ILE C 198 ? 0.7336 0.9096 0.3459 0.0118  -0.0342 0.0611  198 ILE C O   
5453  C CB  . ILE C 198 ? 0.7896 0.9251 0.3309 0.0182  -0.0311 0.0931  198 ILE C CB  
5454  C CG1 . ILE C 198 ? 0.8248 0.9320 0.3283 0.0098  -0.0168 0.0961  198 ILE C CG1 
5455  C CG2 . ILE C 198 ? 0.7860 0.9278 0.3301 0.0358  -0.0494 0.1142  198 ILE C CG2 
5456  C CD1 . ILE C 198 ? 0.8149 0.9051 0.3267 0.0209  -0.0111 0.1064  198 ILE C CD1 
5457  N N   . SER C 199 ? 0.7668 0.9598 0.3475 0.0107  -0.0591 0.0748  199 SER C N   
5458  C CA  . SER C 199 ? 0.7354 0.9494 0.3569 0.0136  -0.0664 0.0687  199 SER C CA  
5459  C C   . SER C 199 ? 0.7184 0.9441 0.3574 0.0301  -0.0796 0.0874  199 SER C C   
5460  O O   . SER C 199 ? 0.7377 0.9687 0.3575 0.0358  -0.0927 0.1008  199 SER C O   
5461  C CB  . SER C 199 ? 0.7498 0.9791 0.3670 0.0005  -0.0737 0.0554  199 SER C CB  
5462  O OG  . SER C 199 ? 0.7824 1.0158 0.3653 -0.0003 -0.0868 0.0654  199 SER C OG  
5463  N N   . VAL C 200 ? 0.6850 0.9148 0.3598 0.0381  -0.0763 0.0877  200 VAL C N   
5464  C CA  . VAL C 200 ? 0.6669 0.9094 0.3623 0.0529  -0.0856 0.1030  200 VAL C CA  
5465  C C   . VAL C 200 ? 0.6435 0.9052 0.3749 0.0502  -0.0895 0.0965  200 VAL C C   
5466  O O   . VAL C 200 ? 0.6286 0.8841 0.3781 0.0449  -0.0809 0.0848  200 VAL C O   
5467  C CB  . VAL C 200 ? 0.6516 0.8792 0.3539 0.0655  -0.0770 0.1114  200 VAL C CB  
5468  C CG1 . VAL C 200 ? 0.6417 0.8818 0.3569 0.0815  -0.0867 0.1278  200 VAL C CG1 
5469  C CG2 . VAL C 200 ? 0.6754 0.8783 0.3444 0.0638  -0.0683 0.1133  200 VAL C CG2 
5470  N N   . GLY C 201 ? 0.6430 0.9274 0.3851 0.0537  -0.1027 0.1041  201 GLY C N   
5471  C CA  . GLY C 201 ? 0.6257 0.9288 0.4005 0.0487  -0.1062 0.0988  201 GLY C CA  
5472  C C   . GLY C 201 ? 0.6110 0.9332 0.4080 0.0607  -0.1125 0.1124  201 GLY C C   
5473  O O   . GLY C 201 ? 0.6202 0.9504 0.4073 0.0716  -0.1206 0.1241  201 GLY C O   
5474  N N   . THR C 202 ? 0.5909 0.9190 0.4174 0.0590  -0.1082 0.1107  202 THR C N   
5475  C CA  . THR C 202 ? 0.5779 0.9290 0.4295 0.0659  -0.1125 0.1203  202 THR C CA  
5476  C C   . THR C 202 ? 0.5718 0.9333 0.4485 0.0519  -0.1119 0.1117  202 THR C C   
5477  O O   . THR C 202 ? 0.5821 0.9367 0.4544 0.0384  -0.1122 0.0987  202 THR C O   
5478  C CB  . THR C 202 ? 0.5617 0.9031 0.4200 0.0803  -0.1038 0.1306  202 THR C CB  
5479  O OG1 . THR C 202 ? 0.5495 0.8731 0.4172 0.0756  -0.0935 0.1251  202 THR C OG1 
5480  C CG2 . THR C 202 ? 0.5704 0.8944 0.4029 0.0920  -0.1024 0.1371  202 THR C CG2 
5481  N N   . SER C 203 ? 0.5586 0.9351 0.4606 0.0541  -0.1101 0.1181  203 SER C N   
5482  C CA  . SER C 203 ? 0.5554 0.9350 0.4795 0.0399  -0.1071 0.1116  203 SER C CA  
5483  C C   . SER C 203 ? 0.5520 0.8990 0.4723 0.0367  -0.0972 0.1060  203 SER C C   
5484  O O   . SER C 203 ? 0.5587 0.8972 0.4868 0.0234  -0.0964 0.0957  203 SER C O   
5485  C CB  . SER C 203 ? 0.5454 0.9466 0.4948 0.0423  -0.1049 0.1207  203 SER C CB  
5486  O OG  . SER C 203 ? 0.5344 0.9239 0.4809 0.0563  -0.0964 0.1310  203 SER C OG  
5487  N N   . THR C 204 ? 0.5436 0.8722 0.4528 0.0494  -0.0906 0.1119  204 THR C N   
5488  C CA  . THR C 204 ? 0.5404 0.8403 0.4479 0.0492  -0.0828 0.1065  204 THR C CA  
5489  C C   . THR C 204 ? 0.5461 0.8288 0.4334 0.0506  -0.0808 0.0972  204 THR C C   
5490  O O   . THR C 204 ? 0.5512 0.8176 0.4394 0.0436  -0.0779 0.0845  204 THR C O   
5491  C CB  . THR C 204 ? 0.5284 0.8198 0.4399 0.0613  -0.0763 0.1177  204 THR C CB  
5492  O OG1 . THR C 204 ? 0.5232 0.8167 0.4214 0.0751  -0.0756 0.1249  204 THR C OG1 
5493  C CG2 . THR C 204 ? 0.5256 0.8340 0.4557 0.0582  -0.0756 0.1265  204 THR C CG2 
5494  N N   . LEU C 205 ? 0.5479 0.8336 0.4175 0.0595  -0.0817 0.1029  205 LEU C N   
5495  C CA  . LEU C 205 ? 0.5553 0.8235 0.4043 0.0602  -0.0772 0.0955  205 LEU C CA  
5496  C C   . LEU C 205 ? 0.5732 0.8426 0.4102 0.0466  -0.0799 0.0819  205 LEU C C   
5497  O O   . LEU C 205 ? 0.5843 0.8712 0.4160 0.0417  -0.0886 0.0834  205 LEU C O   
5498  C CB  . LEU C 205 ? 0.5577 0.8253 0.3886 0.0722  -0.0772 0.1069  205 LEU C CB  
5499  C CG  . LEU C 205 ? 0.5660 0.8130 0.3754 0.0732  -0.0698 0.1016  205 LEU C CG  
5500  C CD1 . LEU C 205 ? 0.5538 0.7840 0.3746 0.0748  -0.0607 0.0935  205 LEU C CD1 
5501  C CD2 . LEU C 205 ? 0.5721 0.8162 0.3642 0.0850  -0.0707 0.1148  205 LEU C CD2 
5502  N N   . ASN C 206 ? 0.5768 0.8292 0.4108 0.0409  -0.0728 0.0674  206 ASN C N   
5503  C CA  . ASN C 206 ? 0.5955 0.8469 0.4151 0.0281  -0.0724 0.0520  206 ASN C CA  
5504  C C   . ASN C 206 ? 0.6012 0.8354 0.4053 0.0283  -0.0617 0.0428  206 ASN C C   
5505  O O   . ASN C 206 ? 0.5987 0.8220 0.4140 0.0246  -0.0548 0.0276  206 ASN C O   
5506  C CB  . ASN C 206 ? 0.5980 0.8492 0.4368 0.0169  -0.0738 0.0376  206 ASN C CB  
5507  C CG  . ASN C 206 ? 0.6195 0.8708 0.4437 0.0033  -0.0731 0.0195  206 ASN C CG  
5508  O OD1 . ASN C 206 ? 0.6358 0.8945 0.4342 0.0000  -0.0758 0.0210  206 ASN C OD1 
5509  N ND2 . ASN C 206 ? 0.6229 0.8648 0.4621 -0.0042 -0.0696 0.0020  206 ASN C ND2 
5510  N N   . GLN C 207 ? 0.6111 0.8431 0.3901 0.0324  -0.0603 0.0517  207 GLN C N   
5511  C CA  . GLN C 207 ? 0.6176 0.8335 0.3818 0.0325  -0.0487 0.0458  207 GLN C CA  
5512  C C   . GLN C 207 ? 0.6474 0.8608 0.3785 0.0211  -0.0457 0.0393  207 GLN C C   
5513  O O   . GLN C 207 ? 0.6639 0.8865 0.3763 0.0185  -0.0553 0.0470  207 GLN C O   
5514  C CB  . GLN C 207 ? 0.6084 0.8178 0.3690 0.0464  -0.0474 0.0623  207 GLN C CB  
5515  C CG  . GLN C 207 ? 0.6226 0.8160 0.3599 0.0455  -0.0370 0.0612  207 GLN C CG  
5516  C CD  . GLN C 207 ? 0.6159 0.8019 0.3504 0.0593  -0.0369 0.0773  207 GLN C CD  
5517  O OE1 . GLN C 207 ? 0.6353 0.8138 0.3437 0.0615  -0.0377 0.0882  207 GLN C OE1 
5518  N NE2 . GLN C 207 ? 0.5918 0.7782 0.3517 0.0690  -0.0364 0.0789  207 GLN C NE2 
5519  N N   . ARG C 208 ? 0.6565 0.8583 0.3805 0.0139  -0.0326 0.0242  208 ARG C N   
5520  C CA  . ARG C 208 ? 0.6887 0.8845 0.3768 0.0022  -0.0258 0.0185  208 ARG C CA  
5521  C C   . ARG C 208 ? 0.6923 0.8732 0.3751 0.0004  -0.0093 0.0111  208 ARG C C   
5522  O O   . ARG C 208 ? 0.6833 0.8635 0.3869 -0.0036 0.0004  -0.0080 208 ARG C O   
5523  C CB  . ARG C 208 ? 0.7045 0.9080 0.3894 -0.0123 -0.0254 -0.0009 208 ARG C CB  
5524  C CG  . ARG C 208 ? 0.7435 0.9429 0.3844 -0.0250 -0.0214 -0.0037 208 ARG C CG  
5525  C CD  . ARG C 208 ? 0.7599 0.9646 0.3988 -0.0405 -0.0156 -0.0287 208 ARG C CD  
5526  N NE  . ARG C 208 ? 0.8007 1.0047 0.3937 -0.0528 -0.0163 -0.0291 208 ARG C NE  
5527  C CZ  . ARG C 208 ? 0.8169 1.0308 0.3916 -0.0537 -0.0327 -0.0194 208 ARG C CZ  
5528  N NH1 . ARG C 208 ? 0.7941 1.0214 0.3951 -0.0441 -0.0486 -0.0092 208 ARG C NH1 
5529  N NH2 . ARG C 208 ? 0.8587 1.0697 0.3877 -0.0649 -0.0334 -0.0203 208 ARG C NH2 
5530  N N   . LEU C 209 ? 0.7074 0.8763 0.3637 0.0034  -0.0065 0.0259  209 LEU C N   
5531  C CA  . LEU C 209 ? 0.7132 0.8673 0.3636 0.0005  0.0094  0.0204  209 LEU C CA  
5532  C C   . LEU C 209 ? 0.7518 0.8974 0.3653 -0.0168 0.0216  0.0113  209 LEU C C   
5533  O O   . LEU C 209 ? 0.7797 0.9239 0.3592 -0.0222 0.0149  0.0199  209 LEU C O   
5534  C CB  . LEU C 209 ? 0.7108 0.8528 0.3531 0.0129  0.0067  0.0414  209 LEU C CB  
5535  C CG  . LEU C 209 ? 0.6775 0.8272 0.3509 0.0303  -0.0041 0.0522  209 LEU C CG  
5536  C CD1 . LEU C 209 ? 0.6826 0.8202 0.3421 0.0419  -0.0071 0.0724  209 LEU C CD1 
5537  C CD2 . LEU C 209 ? 0.6496 0.8026 0.3598 0.0334  0.0020  0.0373  209 LEU C CD2 
5538  N N   . VAL C 210 ? 0.7552 0.8960 0.3754 -0.0256 0.0396  -0.0065 210 VAL C N   
5539  C CA  . VAL C 210 ? 0.7945 0.9258 0.3793 -0.0438 0.0557  -0.0159 210 VAL C CA  
5540  C C   . VAL C 210 ? 0.7999 0.9163 0.3826 -0.0462 0.0717  -0.0160 210 VAL C C   
5541  O O   . VAL C 210 ? 0.7693 0.8903 0.3898 -0.0378 0.0744  -0.0233 210 VAL C O   
5542  C CB  . VAL C 210 ? 0.7996 0.9440 0.3954 -0.0575 0.0657  -0.0447 210 VAL C CB  
5543  C CG1 . VAL C 210 ? 0.7984 0.9557 0.3950 -0.0568 0.0500  -0.0454 210 VAL C CG1 
5544  C CG2 . VAL C 210 ? 0.7684 0.9220 0.4131 -0.0534 0.0741  -0.0659 210 VAL C CG2 
5545  N N   . PRO C 211 ? 0.8421 0.9394 0.3795 -0.0580 0.0818  -0.0077 211 PRO C N   
5546  C CA  . PRO C 211 ? 0.8504 0.9322 0.3860 -0.0626 0.0982  -0.0087 211 PRO C CA  
5547  C C   . PRO C 211 ? 0.8475 0.9402 0.4070 -0.0765 0.1195  -0.0390 211 PRO C C   
5548  O O   . PRO C 211 ? 0.8677 0.9683 0.4153 -0.0916 0.1295  -0.0561 211 PRO C O   
5549  C CB  . PRO C 211 ? 0.9028 0.9585 0.3787 -0.0733 0.1028  0.0091  211 PRO C CB  
5550  C CG  . PRO C 211 ? 0.9151 0.9735 0.3661 -0.0674 0.0827  0.0246  211 PRO C CG  
5551  C CD  . PRO C 211 ? 0.8855 0.9720 0.3703 -0.0661 0.0765  0.0059  211 PRO C CD  
5552  N N   . ARG C 212 ? 0.8234 0.9181 0.4175 -0.0707 0.1258  -0.0465 212 ARG C N   
5553  C CA  . ARG C 212 ? 0.8185 0.9258 0.4418 -0.0816 0.1451  -0.0758 212 ARG C CA  
5554  C C   . ARG C 212 ? 0.8504 0.9397 0.4498 -0.0973 0.1659  -0.0756 212 ARG C C   
5555  O O   . ARG C 212 ? 0.8479 0.9215 0.4451 -0.0903 0.1635  -0.0602 212 ARG C O   
5556  C CB  . ARG C 212 ? 0.7720 0.8953 0.4521 -0.0647 0.1368  -0.0863 212 ARG C CB  
5557  C CG  . ARG C 212 ? 0.7430 0.8790 0.4459 -0.0487 0.1160  -0.0831 212 ARG C CG  
5558  C CD  . ARG C 212 ? 0.7045 0.8539 0.4601 -0.0338 0.1091  -0.0953 212 ARG C CD  
5559  N NE  . ARG C 212 ? 0.6931 0.8345 0.4584 -0.0254 0.1090  -0.0866 212 ARG C NE  
5560  C CZ  . ARG C 212 ? 0.6802 0.8123 0.4409 -0.0105 0.0947  -0.0631 212 ARG C CZ  
5561  N NH1 . ARG C 212 ? 0.6755 0.8064 0.4239 -0.0019 0.0790  -0.0448 212 ARG C NH1 
5562  N NH2 . ARG C 212 ? 0.6728 0.7979 0.4427 -0.0046 0.0966  -0.0593 212 ARG C NH2 
5563  N N   . ILE C 213 ? 0.8828 0.9740 0.4641 -0.1195 0.1873  -0.0935 213 ILE C N   
5564  C CA  . ILE C 213 ? 0.9199 0.9933 0.4753 -0.1388 0.2103  -0.0947 213 ILE C CA  
5565  C C   . ILE C 213 ? 0.8993 0.9914 0.5042 -0.1438 0.2269  -0.1233 213 ILE C C   
5566  O O   . ILE C 213 ? 0.8770 0.9968 0.5215 -0.1430 0.2298  -0.1503 213 ILE C O   
5567  C CB  . ILE C 213 ? 0.9737 1.0372 0.4763 -0.1627 0.2267  -0.0976 213 ILE C CB  
5568  C CG1 . ILE C 213 ? 0.9994 1.0422 0.4499 -0.1569 0.2082  -0.0672 213 ILE C CG1 
5569  C CG2 . ILE C 213 ? 1.0159 1.0599 0.4913 -0.1856 0.2534  -0.1000 213 ILE C CG2 
5570  C CD1 . ILE C 213 ? 1.0402 1.0838 0.4484 -0.1741 0.2151  -0.0736 213 ILE C CD1 
5571  N N   . ALA C 214 ? 0.9084 0.9851 0.5120 -0.1484 0.2366  -0.1180 214 ALA C N   
5572  C CA  . ALA C 214 ? 0.8936 0.9879 0.5425 -0.1550 0.2528  -0.1450 214 ALA C CA  
5573  C C   . ALA C 214 ? 0.9233 0.9924 0.5509 -0.1687 0.2686  -0.1362 214 ALA C C   
5574  O O   . ALA C 214 ? 0.9407 0.9786 0.5315 -0.1634 0.2596  -0.1067 214 ALA C O   
5575  C CB  . ALA C 214 ? 0.8390 0.9546 0.5461 -0.1303 0.2335  -0.1524 214 ALA C CB  
5576  N N   . THR C 215 ? 0.9312 1.0139 0.5834 -0.1866 0.2924  -0.1631 215 THR C N   
5577  C CA  . THR C 215 ? 0.9568 1.0185 0.5979 -0.2013 0.3091  -0.1596 215 THR C CA  
5578  C C   . THR C 215 ? 0.9149 0.9828 0.6005 -0.1806 0.2931  -0.1590 215 THR C C   
5579  O O   . THR C 215 ? 0.8763 0.9774 0.6191 -0.1715 0.2893  -0.1839 215 THR C O   
5580  C CB  . THR C 215 ? 0.9806 1.0588 0.6359 -0.2300 0.3420  -0.1915 215 THR C CB  
5581  O OG1 . THR C 215 ? 1.0162 1.0943 0.6339 -0.2481 0.3566  -0.1963 215 THR C OG1 
5582  C CG2 . THR C 215 ? 1.0170 1.0676 0.6524 -0.2494 0.3614  -0.1854 215 THR C CG2 
5583  N N   . ARG C 216 ? 0.9250 0.9605 0.5835 -0.1724 0.2830  -0.1309 216 ARG C N   
5584  C CA  . ARG C 216 ? 0.8882 0.9267 0.5817 -0.1510 0.2657  -0.1271 216 ARG C CA  
5585  C C   . ARG C 216 ? 0.9150 0.9271 0.5976 -0.1628 0.2786  -0.1224 216 ARG C C   
5586  O O   . ARG C 216 ? 0.9652 0.9459 0.6007 -0.1831 0.2954  -0.1106 216 ARG C O   
5587  C CB  . ARG C 216 ? 0.8691 0.8960 0.5467 -0.1250 0.2375  -0.0983 216 ARG C CB  
5588  C CG  . ARG C 216 ? 0.8435 0.8942 0.5321 -0.1133 0.2234  -0.1017 216 ARG C CG  
5589  C CD  . ARG C 216 ? 0.8350 0.8717 0.5001 -0.0927 0.1991  -0.0717 216 ARG C CD  
5590  N NE  . ARG C 216 ? 0.8791 0.8888 0.4853 -0.1026 0.2019  -0.0500 216 ARG C NE  
5591  C CZ  . ARG C 216 ? 0.8901 0.9057 0.4740 -0.1063 0.1986  -0.0476 216 ARG C CZ  
5592  N NH1 . ARG C 216 ? 0.8605 0.9068 0.4762 -0.1017 0.1935  -0.0658 216 ARG C NH1 
5593  N NH2 . ARG C 216 ? 0.9342 0.9231 0.4621 -0.1146 0.1996  -0.0268 216 ARG C NH2 
5594  N N   . SER C 217 ? 0.8841 0.9076 0.6090 -0.1505 0.2704  -0.1318 217 SER C N   
5595  C CA  . SER C 217 ? 0.9056 0.9051 0.6258 -0.1594 0.2800  -0.1289 217 SER C CA  
5596  C C   . SER C 217 ? 0.9276 0.8842 0.6010 -0.1481 0.2674  -0.0928 217 SER C C   
5597  O O   . SER C 217 ? 0.9077 0.8638 0.5717 -0.1259 0.2452  -0.0738 217 SER C O   
5598  C CB  . SER C 217 ? 0.8650 0.8910 0.6436 -0.1467 0.2712  -0.1496 217 SER C CB  
5599  O OG  . SER C 217 ? 0.8400 0.9091 0.6666 -0.1507 0.2769  -0.1824 217 SER C OG  
5600  N N   . LYS C 218 ? 0.9713 0.8918 0.6163 -0.1638 0.2819  -0.0840 218 LYS C N   
5601  C CA  . LYS C 218 ? 0.9976 0.8745 0.5999 -0.1527 0.2704  -0.0512 218 LYS C CA  
5602  C C   . LYS C 218 ? 0.9585 0.8411 0.5921 -0.1264 0.2495  -0.0482 218 LYS C C   
5603  O O   . LYS C 218 ? 0.9454 0.8381 0.6144 -0.1291 0.2544  -0.0669 218 LYS C O   
5604  C CB  . LYS C 218 ? 1.0613 0.8934 0.6237 -0.1774 0.2923  -0.0430 218 LYS C CB  
5605  C CG  . LYS C 218 ? 1.1169 0.9228 0.6207 -0.1967 0.3055  -0.0280 218 LYS C CG  
5606  C CD  . LYS C 218 ? 1.1855 0.9389 0.6447 -0.2187 0.3245  -0.0150 218 LYS C CD  
5607  C CE  . LYS C 218 ? 1.2475 0.9735 0.6445 -0.2409 0.3397  -0.0011 218 LYS C CE  
5608  N NZ  . LYS C 218 ? 1.2548 1.0090 0.6649 -0.2700 0.3672  -0.0299 218 LYS C NZ  
5609  N N   . VAL C 219 ? 0.9406 0.8190 0.5616 -0.1017 0.2264  -0.0258 219 VAL C N   
5610  C CA  . VAL C 219 ? 0.9125 0.7897 0.5519 -0.0768 0.2073  -0.0179 219 VAL C CA  
5611  C C   . VAL C 219 ? 0.9485 0.7819 0.5406 -0.0685 0.2001  0.0134  219 VAL C C   
5612  O O   . VAL C 219 ? 0.9659 0.7889 0.5234 -0.0663 0.1944  0.0322  219 VAL C O   
5613  C CB  . VAL C 219 ? 0.8591 0.7739 0.5300 -0.0536 0.1862  -0.0209 219 VAL C CB  
5614  C CG1 . VAL C 219 ? 0.8361 0.7478 0.5188 -0.0281 0.1669  -0.0099 219 VAL C CG1 
5615  C CG2 . VAL C 219 ? 0.8273 0.7824 0.5455 -0.0600 0.1917  -0.0522 219 VAL C CG2 
5616  N N   . ASN C 220 ? 0.9623 0.7697 0.5532 -0.0639 0.1999  0.0182  220 ASN C N   
5617  C CA  . ASN C 220 ? 1.0050 0.7653 0.5515 -0.0573 0.1951  0.0462  220 ASN C CA  
5618  C C   . ASN C 220 ? 1.0633 0.7892 0.5576 -0.0789 0.2096  0.0600  220 ASN C C   
5619  O O   . ASN C 220 ? 1.0929 0.7910 0.5463 -0.0697 0.1994  0.0862  220 ASN C O   
5620  C CB  . ASN C 220 ? 0.9807 0.7482 0.5248 -0.0271 0.1697  0.0660  220 ASN C CB  
5621  C CG  . ASN C 220 ? 0.9483 0.7255 0.5247 -0.0056 0.1570  0.0617  220 ASN C CG  
5622  O OD1 . ASN C 220 ? 0.9283 0.7212 0.5386 -0.0103 0.1631  0.0398  220 ASN C OD1 
5623  N ND2 . ASN C 220 ? 0.9448 0.7139 0.5108 0.0181  0.1392  0.0816  220 ASN C ND2 
5624  N N   . GLY C 221 ? 1.0815 0.8102 0.5772 -0.1077 0.2333  0.0416  221 GLY C N   
5625  C CA  . GLY C 221 ? 1.1425 0.8378 0.5867 -0.1325 0.2511  0.0521  221 GLY C CA  
5626  C C   . GLY C 221 ? 1.1445 0.8546 0.5644 -0.1344 0.2473  0.0593  221 GLY C C   
5627  O O   . GLY C 221 ? 1.1997 0.8788 0.5681 -0.1514 0.2578  0.0731  221 GLY C O   
5628  N N   . GLN C 222 ? 1.0882 0.8438 0.5430 -0.1179 0.2323  0.0499  222 GLN C N   
5629  C CA  . GLN C 222 ? 1.0863 0.8592 0.5228 -0.1185 0.2269  0.0543  222 GLN C CA  
5630  C C   . GLN C 222 ? 1.0330 0.8587 0.5189 -0.1192 0.2285  0.0260  222 GLN C C   
5631  O O   . GLN C 222 ? 0.9837 0.8367 0.5182 -0.1039 0.2188  0.0130  222 GLN C O   
5632  C CB  . GLN C 222 ? 1.0797 0.8464 0.4981 -0.0915 0.1997  0.0807  222 GLN C CB  
5633  C CG  . GLN C 222 ? 1.1360 0.8501 0.5036 -0.0871 0.1944  0.1103  222 GLN C CG  
5634  C CD  . GLN C 222 ? 1.2059 0.8845 0.5150 -0.1127 0.2112  0.1202  222 GLN C CD  
5635  O OE1 . GLN C 222 ? 1.2113 0.9072 0.5076 -0.1271 0.2188  0.1124  222 GLN C OE1 
5636  N NE2 . GLN C 222 ? 1.2626 0.8894 0.5339 -0.1186 0.2172  0.1375  222 GLN C NE2 
5637  N N   . SER C 223 ? 1.0465 0.8847 0.5179 -0.1368 0.2405  0.0166  223 SER C N   
5638  C CA  . SER C 223 ? 1.0027 0.8885 0.5178 -0.1379 0.2424  -0.0104 223 SER C CA  
5639  C C   . SER C 223 ? 0.9801 0.8846 0.4904 -0.1221 0.2226  -0.0017 223 SER C C   
5640  O O   . SER C 223 ? 0.9451 0.8862 0.4899 -0.1200 0.2209  -0.0218 223 SER C O   
5641  C CB  . SER C 223 ? 1.0315 0.9237 0.5418 -0.1693 0.2717  -0.0330 223 SER C CB  
5642  O OG  . SER C 223 ? 1.0346 0.9255 0.5710 -0.1823 0.2888  -0.0503 223 SER C OG  
5643  N N   . GLY C 224 ? 1.0015 0.8808 0.4707 -0.1108 0.2071  0.0274  224 GLY C N   
5644  C CA  . GLY C 224 ? 0.9788 0.8756 0.4465 -0.0936 0.1855  0.0375  224 GLY C CA  
5645  C C   . GLY C 224 ? 0.9242 0.8417 0.4355 -0.0666 0.1646  0.0390  224 GLY C C   
5646  O O   . GLY C 224 ? 0.9128 0.8219 0.4426 -0.0583 0.1636  0.0399  224 GLY C O   
5647  N N   . ARG C 225 ? 0.8931 0.8365 0.4193 -0.0540 0.1486  0.0389  225 ARG C N   
5648  C CA  . ARG C 225 ? 0.8434 0.8077 0.4093 -0.0301 0.1298  0.0401  225 ARG C CA  
5649  C C   . ARG C 225 ? 0.8373 0.8047 0.3892 -0.0135 0.1082  0.0608  225 ARG C C   
5650  O O   . ARG C 225 ? 0.8591 0.8259 0.3826 -0.0204 0.1059  0.0665  225 ARG C O   
5651  C CB  . ARG C 225 ? 0.8029 0.8024 0.4163 -0.0305 0.1320  0.0136  225 ARG C CB  
5652  C CG  . ARG C 225 ? 0.8007 0.8053 0.4398 -0.0435 0.1504  -0.0101 225 ARG C CG  
5653  C CD  . ARG C 225 ? 0.7844 0.7825 0.4451 -0.0313 0.1460  -0.0081 225 ARG C CD  
5654  N NE  . ARG C 225 ? 0.7804 0.7881 0.4705 -0.0435 0.1619  -0.0334 225 ARG C NE  
5655  C CZ  . ARG C 225 ? 0.8134 0.8012 0.4886 -0.0617 0.1808  -0.0378 225 ARG C CZ  
5656  N NH1 . ARG C 225 ? 0.8571 0.8093 0.4841 -0.0699 0.1865  -0.0169 225 ARG C NH1 
5657  N NH2 . ARG C 225 ? 0.8049 0.8082 0.5144 -0.0720 0.1939  -0.0636 225 ARG C NH2 
5658  N N   . MET C 226 ? 0.8086 0.7809 0.3814 0.0077  0.0929  0.0707  226 MET C N   
5659  C CA  . MET C 226 ? 0.7961 0.7779 0.3662 0.0246  0.0726  0.0873  226 MET C CA  
5660  C C   . MET C 226 ? 0.7458 0.7572 0.3612 0.0380  0.0629  0.0778  226 MET C C   
5661  O O   . MET C 226 ? 0.7253 0.7388 0.3664 0.0455  0.0642  0.0716  226 MET C O   
5662  C CB  . MET C 226 ? 0.8153 0.7731 0.3651 0.0389  0.0634  0.1104  226 MET C CB  
5663  C CG  . MET C 226 ? 0.8711 0.7953 0.3701 0.0290  0.0680  0.1253  226 MET C CG  
5664  S SD  . MET C 226 ? 0.8937 0.8231 0.3597 0.0305  0.0525  0.1404  226 MET C SD  
5665  C CE  . MET C 226 ? 0.9656 0.8465 0.3697 0.0206  0.0586  0.1593  226 MET C CE  
5666  N N   . GLU C 227 ? 0.7294 0.7618 0.3525 0.0404  0.0529  0.0769  227 GLU C N   
5667  C CA  . GLU C 227 ? 0.6870 0.7440 0.3492 0.0517  0.0436  0.0696  227 GLU C CA  
5668  C C   . GLU C 227 ? 0.6767 0.7419 0.3380 0.0670  0.0261  0.0878  227 GLU C C   
5669  O O   . GLU C 227 ? 0.6884 0.7591 0.3335 0.0640  0.0191  0.0943  227 GLU C O   
5670  C CB  . GLU C 227 ? 0.6764 0.7516 0.3548 0.0406  0.0480  0.0496  227 GLU C CB  
5671  C CG  . GLU C 227 ? 0.6393 0.7331 0.3596 0.0497  0.0426  0.0375  227 GLU C CG  
5672  C CD  . GLU C 227 ? 0.6333 0.7412 0.3716 0.0392  0.0485  0.0150  227 GLU C CD  
5673  O OE1 . GLU C 227 ? 0.6567 0.7617 0.3763 0.0233  0.0594  0.0064  227 GLU C OE1 
5674  O OE2 . GLU C 227 ? 0.6076 0.7285 0.3781 0.0470  0.0421  0.0058  227 GLU C OE2 
5675  N N   . PHE C 228 ? 0.6561 0.7235 0.3352 0.0829  0.0195  0.0948  228 PHE C N   
5676  C CA  . PHE C 228 ? 0.6488 0.7244 0.3284 0.0977  0.0050  0.1118  228 PHE C CA  
5677  C C   . PHE C 228 ? 0.6158 0.7160 0.3256 0.1038  -0.0031 0.1077  228 PHE C C   
5678  O O   . PHE C 228 ? 0.5945 0.7002 0.3282 0.1055  -0.0001 0.0966  228 PHE C O   
5679  C CB  . PHE C 228 ? 0.6538 0.7148 0.3298 0.1113  0.0039  0.1232  228 PHE C CB  
5680  C CG  . PHE C 228 ? 0.6922 0.7246 0.3346 0.1067  0.0095  0.1316  228 PHE C CG  
5681  C CD1 . PHE C 228 ? 0.7185 0.7432 0.3346 0.1110  0.0003  0.1483  228 PHE C CD1 
5682  C CD2 . PHE C 228 ? 0.7054 0.7180 0.3421 0.0973  0.0237  0.1226  228 PHE C CD2 
5683  C CE1 . PHE C 228 ? 0.7601 0.7537 0.3411 0.1069  0.0046  0.1579  228 PHE C CE1 
5684  C CE2 . PHE C 228 ? 0.7460 0.7282 0.3490 0.0912  0.0300  0.1313  228 PHE C CE2 
5685  C CZ  . PHE C 228 ? 0.7748 0.7455 0.3482 0.0963  0.0203  0.1499  228 PHE C CZ  
5686  N N   . PHE C 229 ? 0.6149 0.7289 0.3224 0.1066  -0.0140 0.1168  229 PHE C N   
5687  C CA  . PHE C 229 ? 0.5897 0.7253 0.3224 0.1098  -0.0216 0.1145  229 PHE C CA  
5688  C C   . PHE C 229 ? 0.5839 0.7311 0.3215 0.1234  -0.0322 0.1302  229 PHE C C   
5689  O O   . PHE C 229 ? 0.6015 0.7420 0.3214 0.1298  -0.0361 0.1423  229 PHE C O   
5690  C CB  . PHE C 229 ? 0.5948 0.7404 0.3249 0.0967  -0.0235 0.1062  229 PHE C CB  
5691  C CG  . PHE C 229 ? 0.5979 0.7371 0.3296 0.0837  -0.0124 0.0875  229 PHE C CG  
5692  C CD1 . PHE C 229 ? 0.6231 0.7468 0.3299 0.0736  -0.0024 0.0835  229 PHE C CD1 
5693  C CD2 . PHE C 229 ? 0.5785 0.7267 0.3367 0.0814  -0.0118 0.0735  229 PHE C CD2 
5694  C CE1 . PHE C 229 ? 0.6263 0.7477 0.3375 0.0609  0.0094  0.0642  229 PHE C CE1 
5695  C CE2 . PHE C 229 ? 0.5817 0.7265 0.3454 0.0709  -0.0019 0.0543  229 PHE C CE2 
5696  C CZ  . PHE C 229 ? 0.6044 0.7379 0.3460 0.0604  0.0093  0.0487  229 PHE C CZ  
5697  N N   . TRP C 230 ? 0.5613 0.7252 0.3230 0.1278  -0.0366 0.1297  230 TRP C N   
5698  C CA  . TRP C 230 ? 0.5540 0.7326 0.3251 0.1396  -0.0444 0.1423  230 TRP C CA  
5699  C C   . TRP C 230 ? 0.5383 0.7378 0.3300 0.1360  -0.0497 0.1408  230 TRP C C   
5700  O O   . TRP C 230 ? 0.5302 0.7290 0.3314 0.1271  -0.0473 0.1303  230 TRP C O   
5701  C CB  . TRP C 230 ? 0.5458 0.7177 0.3238 0.1525  -0.0405 0.1457  230 TRP C CB  
5702  C CG  . TRP C 230 ? 0.5284 0.6985 0.3227 0.1515  -0.0357 0.1363  230 TRP C CG  
5703  C CD1 . TRP C 230 ? 0.5280 0.6832 0.3215 0.1477  -0.0287 0.1250  230 TRP C CD1 
5704  C CD2 . TRP C 230 ? 0.5123 0.6956 0.3254 0.1547  -0.0383 0.1375  230 TRP C CD2 
5705  N NE1 . TRP C 230 ? 0.5127 0.6711 0.3234 0.1500  -0.0289 0.1192  230 TRP C NE1 
5706  C CE2 . TRP C 230 ? 0.5047 0.6781 0.3252 0.1539  -0.0344 0.1277  230 TRP C CE2 
5707  C CE3 . TRP C 230 ? 0.5062 0.7088 0.3303 0.1574  -0.0434 0.1458  230 TRP C CE3 
5708  C CZ2 . TRP C 230 ? 0.4943 0.6726 0.3285 0.1565  -0.0363 0.1277  230 TRP C CZ2 
5709  C CZ3 . TRP C 230 ? 0.4954 0.7032 0.3337 0.1579  -0.0429 0.1455  230 TRP C CZ3 
5710  C CH2 . TRP C 230 ? 0.4911 0.6850 0.3321 0.1578  -0.0399 0.1374  230 TRP C CH2 
5711  N N   . THR C 231 ? 0.5361 0.7538 0.3356 0.1430  -0.0567 0.1509  231 THR C N   
5712  C CA  . THR C 231 ? 0.5231 0.7612 0.3438 0.1395  -0.0603 0.1509  231 THR C CA  
5713  C C   . THR C 231 ? 0.5185 0.7745 0.3511 0.1514  -0.0633 0.1615  231 THR C C   
5714  O O   . THR C 231 ? 0.5271 0.7817 0.3514 0.1627  -0.0654 0.1686  231 THR C O   
5715  C CB  . THR C 231 ? 0.5306 0.7806 0.3502 0.1270  -0.0670 0.1468  231 THR C CB  
5716  O OG1 . THR C 231 ? 0.5192 0.7834 0.3600 0.1203  -0.0684 0.1442  231 THR C OG1 
5717  C CG2 . THR C 231 ? 0.5448 0.8085 0.3556 0.1319  -0.0766 0.1554  231 THR C CG2 
5718  N N   . ILE C 232 ? 0.5074 0.7790 0.3596 0.1487  -0.0629 0.1622  232 ILE C N   
5719  C CA  . ILE C 232 ? 0.5043 0.7996 0.3715 0.1568  -0.0648 0.1702  232 ILE C CA  
5720  C C   . ILE C 232 ? 0.5076 0.8273 0.3861 0.1477  -0.0729 0.1697  232 ILE C C   
5721  O O   . ILE C 232 ? 0.5045 0.8271 0.3915 0.1342  -0.0727 0.1643  232 ILE C O   
5722  C CB  . ILE C 232 ? 0.4935 0.7907 0.3731 0.1590  -0.0571 0.1717  232 ILE C CB  
5723  C CG1 . ILE C 232 ? 0.4934 0.7788 0.3653 0.1736  -0.0517 0.1746  232 ILE C CG1 
5724  C CG2 . ILE C 232 ? 0.4903 0.8173 0.3905 0.1575  -0.0577 0.1763  232 ILE C CG2 
5725  C CD1 . ILE C 232 ? 0.4981 0.7560 0.3516 0.1754  -0.0500 0.1698  232 ILE C CD1 
5726  N N   . LEU C 233 ? 0.5167 0.8528 0.3955 0.1554  -0.0811 0.1748  233 LEU C N   
5727  C CA  . LEU C 233 ? 0.5217 0.8847 0.4123 0.1484  -0.0909 0.1737  233 LEU C CA  
5728  C C   . LEU C 233 ? 0.5128 0.9066 0.4318 0.1517  -0.0894 0.1768  233 LEU C C   
5729  O O   . LEU C 233 ? 0.5130 0.9173 0.4385 0.1669  -0.0893 0.1823  233 LEU C O   
5730  C CB  . LEU C 233 ? 0.5402 0.9046 0.4145 0.1559  -0.1027 0.1774  233 LEU C CB  
5731  C CG  . LEU C 233 ? 0.5500 0.9406 0.4312 0.1489  -0.1162 0.1751  233 LEU C CG  
5732  C CD1 . LEU C 233 ? 0.5514 0.9358 0.4268 0.1292  -0.1159 0.1652  233 LEU C CD1 
5733  C CD2 . LEU C 233 ? 0.5730 0.9609 0.4340 0.1604  -0.1289 0.1815  233 LEU C CD2 
5734  N N   . LYS C 234 ? 0.6806 1.3117 0.4255 0.2544  -0.1317 0.3099  234 LYS C N   
5735  C CA  . LYS C 234 ? 0.6744 1.3679 0.4330 0.2419  -0.1370 0.3170  234 LYS C CA  
5736  C C   . LYS C 234 ? 0.6808 1.4225 0.4366 0.2602  -0.1383 0.3134  234 LYS C C   
5737  O O   . LYS C 234 ? 0.6888 1.4121 0.4360 0.2752  -0.1400 0.3085  234 LYS C O   
5738  C CB  . LYS C 234 ? 0.6674 1.3685 0.4471 0.2041  -0.1552 0.3266  234 LYS C CB  
5739  C CG  . LYS C 234 ? 0.6644 1.3196 0.4480 0.1868  -0.1571 0.3292  234 LYS C CG  
5740  C CD  . LYS C 234 ? 0.6647 1.3290 0.4664 0.1481  -0.1793 0.3411  234 LYS C CD  
5741  C CE  . LYS C 234 ? 0.6641 1.2874 0.4683 0.1331  -0.1816 0.3439  234 LYS C CE  
5742  N NZ  . LYS C 234 ? 0.6714 1.3008 0.4891 0.0932  -0.2067 0.3582  234 LYS C NZ  
5743  N N   . PRO C 235 ? 0.6785 1.4864 0.4415 0.2591  -0.1379 0.3144  235 PRO C N   
5744  C CA  . PRO C 235 ? 0.6851 1.5439 0.4468 0.2796  -0.1397 0.3077  235 PRO C CA  
5745  C C   . PRO C 235 ? 0.6841 1.5559 0.4561 0.2645  -0.1534 0.3121  235 PRO C C   
5746  O O   . PRO C 235 ? 0.6776 1.5466 0.4638 0.2306  -0.1651 0.3219  235 PRO C O   
5747  C CB  . PRO C 235 ? 0.6790 1.6169 0.4517 0.2728  -0.1380 0.3065  235 PRO C CB  
5748  C CG  . PRO C 235 ? 0.6719 1.5932 0.4467 0.2539  -0.1327 0.3125  235 PRO C CG  
5749  C CD  . PRO C 235 ? 0.6700 1.5155 0.4435 0.2367  -0.1370 0.3207  235 PRO C CD  
5750  N N   . ASN C 236 ? 0.6942 1.5764 0.4581 0.2899  -0.1541 0.3046  236 ASN C N   
5751  C CA  . ASN C 236 ? 0.6943 1.5941 0.4672 0.2795  -0.1665 0.3070  236 ASN C CA  
5752  C C   . ASN C 236 ? 0.6945 1.5311 0.4669 0.2679  -0.1726 0.3089  236 ASN C C   
5753  O O   . ASN C 236 ? 0.6942 1.5399 0.4776 0.2530  -0.1858 0.3110  236 ASN C O   
5754  C CB  . ASN C 236 ? 0.6862 1.6536 0.4798 0.2462  -0.1775 0.3155  236 ASN C CB  
5755  C CG  . ASN C 236 ? 0.6898 1.7190 0.4891 0.2529  -0.1841 0.3117  236 ASN C CG  
5756  O OD1 . ASN C 236 ? 0.7005 1.7174 0.4897 0.2815  -0.1828 0.3033  236 ASN C OD1 
5757  N ND2 . ASN C 236 ? 0.6850 1.7838 0.4993 0.2243  -0.1921 0.3183  236 ASN C ND2 
5758  N N   . ASP C 237 ? 0.6968 1.4734 0.4569 0.2749  -0.1638 0.3063  237 ASP C N   
5759  C CA  . ASP C 237 ? 0.6973 1.4200 0.4567 0.2672  -0.1681 0.3030  237 ASP C CA  
5760  C C   . ASP C 237 ? 0.7118 1.3972 0.4452 0.2949  -0.1573 0.2954  237 ASP C C   
5761  O O   . ASP C 237 ? 0.7221 1.3992 0.4366 0.3162  -0.1465 0.2945  237 ASP C O   
5762  C CB  . ASP C 237 ? 0.6899 1.3768 0.4573 0.2469  -0.1687 0.3054  237 ASP C CB  
5763  C CG  . ASP C 237 ? 0.6906 1.3323 0.4636 0.2376  -0.1769 0.2975  237 ASP C CG  
5764  O OD1 . ASP C 237 ? 0.6934 1.3414 0.4722 0.2366  -0.1875 0.2926  237 ASP C OD1 
5765  O OD2 . ASP C 237 ? 0.6884 1.2914 0.4611 0.2319  -0.1734 0.2942  237 ASP C OD2 
5766  N N   . ALA C 238 ? 0.7155 1.3791 0.4470 0.2930  -0.1624 0.2896  238 ALA C N   
5767  C CA  . ALA C 238 ? 0.7331 1.3644 0.4373 0.3125  -0.1543 0.2841  238 ALA C CA  
5768  C C   . ALA C 238 ? 0.7332 1.3170 0.4317 0.3031  -0.1489 0.2775  238 ALA C C   
5769  O O   . ALA C 238 ? 0.7203 1.2989 0.4405 0.2837  -0.1571 0.2723  238 ALA C O   
5770  C CB  . ALA C 238 ? 0.7396 1.3903 0.4428 0.3179  -0.1628 0.2807  238 ALA C CB  
5771  N N   . ILE C 239 ? 0.7508 1.3005 0.4193 0.3164  -0.1372 0.2770  239 ILE C N   
5772  C CA  . ILE C 239 ? 0.7551 1.2667 0.4131 0.3075  -0.1306 0.2692  239 ILE C CA  
5773  C C   . ILE C 239 ? 0.7743 1.2801 0.4104 0.3125  -0.1308 0.2641  239 ILE C C   
5774  O O   . ILE C 239 ? 0.7953 1.3023 0.4076 0.3288  -0.1310 0.2708  239 ILE C O   
5775  C CB  . ILE C 239 ? 0.7645 1.2407 0.4020 0.3120  -0.1178 0.2732  239 ILE C CB  
5776  C CG1 . ILE C 239 ? 0.7660 1.2118 0.3976 0.2983  -0.1113 0.2633  239 ILE C CG1 
5777  C CG2 . ILE C 239 ? 0.7943 1.2553 0.3962 0.3339  -0.1138 0.2808  239 ILE C CG2 
5778  C CD1 . ILE C 239 ? 0.7680 1.1828 0.3895 0.2963  -0.1004 0.2660  239 ILE C CD1 
5779  N N   . ASN C 240 ? 0.7689 1.2710 0.4134 0.2987  -0.1325 0.2508  240 ASN C N   
5780  C CA  . ASN C 240 ? 0.7856 1.2908 0.4116 0.2990  -0.1328 0.2437  240 ASN C CA  
5781  C C   . ASN C 240 ? 0.7969 1.2785 0.4033 0.2883  -0.1225 0.2341  240 ASN C C   
5782  O O   . ASN C 240 ? 0.7804 1.2598 0.4077 0.2764  -0.1221 0.2208  240 ASN C O   
5783  C CB  . ASN C 240 ? 0.7708 1.3078 0.4265 0.2919  -0.1465 0.2315  240 ASN C CB  
5784  C CG  . ASN C 240 ? 0.7592 1.3245 0.4358 0.2969  -0.1577 0.2406  240 ASN C CG  
5785  O OD1 . ASN C 240 ? 0.7713 1.3486 0.4322 0.3110  -0.1574 0.2510  240 ASN C OD1 
5786  N ND2 . ASN C 240 ? 0.7394 1.3161 0.4505 0.2841  -0.1700 0.2363  240 ASN C ND2 
5787  N N   . PHE C 241 ? 0.8275 1.2932 0.3930 0.2915  -0.1163 0.2407  241 PHE C N   
5788  C CA  . PHE C 241 ? 0.8447 1.2943 0.3848 0.2771  -0.1066 0.2334  241 PHE C CA  
5789  C C   . PHE C 241 ? 0.8578 1.3317 0.3861 0.2689  -0.1093 0.2231  241 PHE C C   
5790  O O   . PHE C 241 ? 0.8728 1.3549 0.3872 0.2779  -0.1159 0.2320  241 PHE C O   
5791  C CB  . PHE C 241 ? 0.8790 1.2870 0.3739 0.2812  -0.0995 0.2513  241 PHE C CB  
5792  C CG  . PHE C 241 ? 0.8681 1.2523 0.3713 0.2867  -0.0945 0.2577  241 PHE C CG  
5793  C CD1 . PHE C 241 ? 0.8606 1.2305 0.3666 0.2726  -0.0848 0.2498  241 PHE C CD1 
5794  C CD2 . PHE C 241 ? 0.8655 1.2468 0.3743 0.3060  -0.0996 0.2698  241 PHE C CD2 
5795  C CE1 . PHE C 241 ? 0.8510 1.1996 0.3642 0.2771  -0.0802 0.2558  241 PHE C CE1 
5796  C CE2 . PHE C 241 ? 0.8559 1.2205 0.3723 0.3104  -0.0947 0.2742  241 PHE C CE2 
5797  C CZ  . PHE C 241 ? 0.8487 1.1947 0.3668 0.2957  -0.0850 0.2682  241 PHE C CZ  
5798  N N   . GLU C 242 ? 0.8521 1.3418 0.3873 0.2523  -0.1047 0.2025  242 GLU C N   
5799  C CA  . GLU C 242 ? 0.8694 1.3860 0.3871 0.2407  -0.1043 0.1907  242 GLU C CA  
5800  C C   . GLU C 242 ? 0.8835 1.3995 0.3799 0.2200  -0.0919 0.1796  242 GLU C C   
5801  O O   . GLU C 242 ? 0.8618 1.3837 0.3850 0.2147  -0.0886 0.1618  242 GLU C O   
5802  C CB  . GLU C 242 ? 0.8437 1.4036 0.4033 0.2422  -0.1157 0.1673  242 GLU C CB  
5803  C CG  . GLU C 242 ? 0.8612 1.4561 0.4045 0.2325  -0.1163 0.1544  242 GLU C CG  
5804  C CD  . GLU C 242 ? 0.8370 1.4737 0.4240 0.2356  -0.1296 0.1274  242 GLU C CD  
5805  O OE1 . GLU C 242 ? 0.8225 1.4608 0.4333 0.2485  -0.1420 0.1338  242 GLU C OE1 
5806  O OE2 . GLU C 242 ? 0.8344 1.5048 0.4320 0.2248  -0.1288 0.0983  242 GLU C OE2 
5807  N N   . SER C 243 ? 0.9228 1.4320 0.3695 0.2068  -0.0866 0.1904  243 SER C N   
5808  C CA  . SER C 243 ? 0.9420 1.4549 0.3619 0.1820  -0.0747 0.1823  243 SER C CA  
5809  C C   . SER C 243 ? 0.9842 1.5133 0.3563 0.1611  -0.0731 0.1870  243 SER C C   
5810  O O   . SER C 243 ? 1.0160 1.5213 0.3536 0.1659  -0.0806 0.2110  243 SER C O   
5811  C CB  . SER C 243 ? 0.9571 1.4179 0.3523 0.1808  -0.0677 0.2021  243 SER C CB  
5812  O OG  . SER C 243 ? 0.9747 1.4416 0.3457 0.1546  -0.0561 0.1937  243 SER C OG  
5813  N N   . ASN C 244 ? 0.9862 1.5584 0.3563 0.1372  -0.0646 0.1630  244 ASN C N   
5814  C CA  . ASN C 244 ? 1.0291 1.6248 0.3504 0.1089  -0.0611 0.1660  244 ASN C CA  
5815  C C   . ASN C 244 ? 1.0624 1.6427 0.3404 0.0792  -0.0496 0.1737  244 ASN C C   
5816  O O   . ASN C 244 ? 1.0951 1.7082 0.3362 0.0477  -0.0445 0.1699  244 ASN C O   
5817  C CB  . ASN C 244 ? 1.0097 1.6825 0.3599 0.1008  -0.0608 0.1289  244 ASN C CB  
5818  C CG  . ASN C 244 ? 0.9773 1.6914 0.3682 0.0957  -0.0533 0.0908  244 ASN C CG  
5819  O OD1 . ASN C 244 ? 0.9516 1.6372 0.3706 0.1093  -0.0526 0.0890  244 ASN C OD1 
5820  N ND2 . ASN C 244 ? 0.9796 1.7638 0.3739 0.0766  -0.0490 0.0584  244 ASN C ND2 
5821  N N   . GLY C 245 ? 1.0553 1.5890 0.3367 0.0871  -0.0457 0.1845  245 GLY C N   
5822  C CA  . GLY C 245 ? 1.0874 1.6002 0.3280 0.0598  -0.0359 0.1938  245 GLY C CA  
5823  C C   . GLY C 245 ? 1.0653 1.5400 0.3262 0.0717  -0.0304 0.1956  245 GLY C C   
5824  O O   . GLY C 245 ? 1.0163 1.5006 0.3328 0.0951  -0.0311 0.1784  245 GLY C O   
5825  N N   . ASN C 246 ? 1.1059 1.5354 0.3188 0.0536  -0.0268 0.2179  246 ASN C N   
5826  C CA  . ASN C 246 ? 1.0929 1.4907 0.3159 0.0564  -0.0192 0.2186  246 ASN C CA  
5827  C C   . ASN C 246 ? 1.0662 1.4171 0.3188 0.0931  -0.0256 0.2307  246 ASN C C   
5828  O O   . ASN C 246 ? 1.0364 1.3791 0.3183 0.1009  -0.0192 0.2218  246 ASN C O   
5829  C CB  . ASN C 246 ? 1.0551 1.5122 0.3180 0.0450  -0.0064 0.1806  246 ASN C CB  
5830  C CG  . ASN C 246 ? 1.0819 1.5964 0.3157 0.0065  0.0016  0.1648  246 ASN C CG  
5831  O OD1 . ASN C 246 ? 1.0847 1.6459 0.3194 0.0009  -0.0017 0.1532  246 ASN C OD1 
5832  N ND2 . ASN C 246 ? 1.1021 1.6179 0.3097 -0.0216 0.0126  0.1635  246 ASN C ND2 
5833  N N   . PHE C 247 ? 1.0799 1.4027 0.3224 0.1139  -0.0387 0.2509  247 PHE C N   
5834  C CA  . PHE C 247 ? 1.0516 1.3475 0.3266 0.1488  -0.0455 0.2585  247 PHE C CA  
5835  C C   . PHE C 247 ? 1.0893 1.3171 0.3266 0.1588  -0.0522 0.2863  247 PHE C C   
5836  O O   . PHE C 247 ? 1.1439 1.3370 0.3290 0.1520  -0.0625 0.3072  247 PHE C O   
5837  C CB  . PHE C 247 ? 1.0381 1.3573 0.3334 0.1683  -0.0565 0.2576  247 PHE C CB  
5838  C CG  . PHE C 247 ? 1.0122 1.3146 0.3386 0.2009  -0.0641 0.2652  247 PHE C CG  
5839  C CD1 . PHE C 247 ? 0.9674 1.2776 0.3401 0.2110  -0.0592 0.2537  247 PHE C CD1 
5840  C CD2 . PHE C 247 ? 1.0344 1.3182 0.3438 0.2203  -0.0773 0.2827  247 PHE C CD2 
5841  C CE1 . PHE C 247 ? 0.9457 1.2486 0.3450 0.2362  -0.0659 0.2608  247 PHE C CE1 
5842  C CE2 . PHE C 247 ? 1.0105 1.2903 0.3494 0.2485  -0.0836 0.2869  247 PHE C CE2 
5843  C CZ  . PHE C 247 ? 0.9662 1.2577 0.3493 0.2548  -0.0772 0.2764  247 PHE C CZ  
5844  N N   . ILE C 248 ? 1.0629 1.2711 0.3267 0.1753  -0.0486 0.2856  248 ILE C N   
5845  C CA  . ILE C 248 ? 1.0924 1.2414 0.3301 0.1914  -0.0564 0.3069  248 ILE C CA  
5846  C C   . ILE C 248 ? 1.0653 1.2205 0.3373 0.2263  -0.0654 0.3084  248 ILE C C   
5847  O O   . ILE C 248 ? 1.0175 1.1944 0.3365 0.2380  -0.0598 0.2973  248 ILE C O   
5848  C CB  . ILE C 248 ? 1.0845 1.2104 0.3254 0.1846  -0.0458 0.3047  248 ILE C CB  
5849  C CG1 . ILE C 248 ? 1.0955 1.2372 0.3177 0.1481  -0.0334 0.2952  248 ILE C CG1 
5850  C CG2 . ILE C 248 ? 1.1287 1.1895 0.3318 0.1976  -0.0564 0.3263  248 ILE C CG2 
5851  C CD1 . ILE C 248 ? 1.1642 1.2737 0.3182 0.1220  -0.0399 0.3140  248 ILE C CD1 
5852  N N   . ALA C 249 ? 1.0987 1.2372 0.3458 0.2410  -0.0807 0.3220  249 ALA C N   
5853  C CA  . ALA C 249 ? 1.0755 1.2318 0.3537 0.2721  -0.0897 0.3213  249 ALA C CA  
5854  C C   . ALA C 249 ? 1.0761 1.2039 0.3602 0.2972  -0.0942 0.3271  249 ALA C C   
5855  O O   . ALA C 249 ? 1.1154 1.1929 0.3634 0.2963  -0.0981 0.3375  249 ALA C O   
5856  C CB  . ALA C 249 ? 1.1123 1.2644 0.3622 0.2800  -0.1056 0.3313  249 ALA C CB  
5857  N N   . PRO C 250 ? 1.0345 1.1969 0.3637 0.3181  -0.0944 0.3197  250 PRO C N   
5858  C CA  . PRO C 250 ? 1.0359 1.1840 0.3722 0.3440  -0.0998 0.3225  250 PRO C CA  
5859  C C   . PRO C 250 ? 1.0802 1.2074 0.3892 0.3710  -0.1198 0.3308  250 PRO C C   
5860  O O   . PRO C 250 ? 1.0751 1.2328 0.3946 0.3812  -0.1276 0.3291  250 PRO C O   
5861  C CB  . PRO C 250 ? 0.9769 1.1803 0.3700 0.3499  -0.0936 0.3115  250 PRO C CB  
5862  C CG  . PRO C 250 ? 0.9571 1.1979 0.3673 0.3380  -0.0936 0.3054  250 PRO C CG  
5863  C CD  . PRO C 250 ? 0.9837 1.2028 0.3608 0.3146  -0.0895 0.3066  250 PRO C CD  
5864  N N   . GLU C 251 ? 1.1262 1.2004 0.4004 0.3833  -0.1303 0.3384  251 GLU C N   
5865  C CA  . GLU C 251 ? 1.1685 1.2217 0.4228 0.4163  -0.1534 0.3416  251 GLU C CA  
5866  C C   . GLU C 251 ? 1.1338 1.2257 0.4297 0.4447  -0.1525 0.3290  251 GLU C C   
5867  O O   . GLU C 251 ? 1.1235 1.2549 0.4394 0.4670  -0.1615 0.3224  251 GLU C O   
5868  C CB  . GLU C 251 ? 1.2405 1.2149 0.4375 0.4178  -0.1704 0.3540  251 GLU C CB  
5869  C CG  . GLU C 251 ? 1.3060 1.2406 0.4539 0.4203  -0.1948 0.3667  251 GLU C CG  
5870  C CD  . GLU C 251 ? 1.3538 1.2572 0.4855 0.4617  -0.2245 0.3650  251 GLU C CD  
5871  O OE1 . GLU C 251 ? 1.3880 1.2432 0.5006 0.4746  -0.2357 0.3653  251 GLU C OE1 
5872  O OE2 . GLU C 251 ? 1.3598 1.2869 0.4979 0.4825  -0.2384 0.3615  251 GLU C OE2 
5873  N N   . TYR C 252 ? 1.1162 1.2009 0.4244 0.4415  -0.1414 0.3253  252 TYR C N   
5874  C CA  . TYR C 252 ? 1.0848 1.2088 0.4300 0.4632  -0.1387 0.3133  252 TYR C CA  
5875  C C   . TYR C 252 ? 1.0216 1.1909 0.4110 0.4410  -0.1166 0.3083  252 TYR C C   
5876  O O   . TYR C 252 ? 1.0091 1.1614 0.3958 0.4131  -0.1034 0.3120  252 TYR C O   
5877  C CB  . TYR C 252 ? 1.1230 1.1997 0.4449 0.4822  -0.1483 0.3117  252 TYR C CB  
5878  C CG  . TYR C 252 ? 1.1933 1.2183 0.4715 0.5080  -0.1767 0.3151  252 TYR C CG  
5879  C CD1 . TYR C 252 ? 1.2061 1.2573 0.4953 0.5468  -0.1953 0.3025  252 TYR C CD1 
5880  C CD2 . TYR C 252 ? 1.2511 1.2016 0.4758 0.4927  -0.1875 0.3303  252 TYR C CD2 
5881  C CE1 . TYR C 252 ? 1.2759 1.2750 0.5250 0.5732  -0.2262 0.3038  252 TYR C CE1 
5882  C CE2 . TYR C 252 ? 1.3235 1.2185 0.5044 0.5146  -0.2187 0.3354  252 TYR C CE2 
5883  C CZ  . TYR C 252 ? 1.3364 1.2530 0.5301 0.5567  -0.2392 0.3215  252 TYR C CZ  
5884  O OH  . TYR C 252 ? 1.4130 1.2700 0.5632 0.5810  -0.2747 0.3249  252 TYR C OH  
5885  N N   . ALA C 253 ? 0.9855 1.2137 0.4143 0.4530  -0.1147 0.2993  253 ALA C N   
5886  C CA  . ALA C 253 ? 0.9326 1.2017 0.4017 0.4335  -0.0991 0.2958  253 ALA C CA  
5887  C C   . ALA C 253 ? 0.9215 1.2230 0.4102 0.4520  -0.0995 0.2873  253 ALA C C   
5888  O O   . ALA C 253 ? 0.9328 1.2656 0.4257 0.4784  -0.1109 0.2797  253 ALA C O   
5889  C CB  . ALA C 253 ? 0.8976 1.2176 0.3970 0.4197  -0.0976 0.2950  253 ALA C CB  
5890  N N   . TYR C 254 ? 0.9004 1.1984 0.4014 0.4383  -0.0876 0.2869  254 TYR C N   
5891  C CA  . TYR C 254 ? 0.8903 1.2204 0.4083 0.4526  -0.0864 0.2782  254 TYR C CA  
5892  C C   . TYR C 254 ? 0.8496 1.2597 0.4081 0.4450  -0.0843 0.2743  254 TYR C C   
5893  O O   . TYR C 254 ? 0.8186 1.2474 0.3981 0.4174  -0.0786 0.2806  254 TYR C O   
5894  C CB  . TYR C 254 ? 0.8824 1.1817 0.3987 0.4378  -0.0745 0.2802  254 TYR C CB  
5895  C CG  . TYR C 254 ? 0.9277 1.1531 0.4028 0.4472  -0.0783 0.2828  254 TYR C CG  
5896  C CD1 . TYR C 254 ? 0.9608 1.1696 0.4200 0.4766  -0.0885 0.2745  254 TYR C CD1 
5897  C CD2 . TYR C 254 ? 0.9405 1.1147 0.3920 0.4255  -0.0734 0.2922  254 TYR C CD2 
5898  C CE1 . TYR C 254 ? 1.0086 1.1434 0.4272 0.4830  -0.0957 0.2785  254 TYR C CE1 
5899  C CE2 . TYR C 254 ? 0.9864 1.0936 0.3966 0.4288  -0.0781 0.2968  254 TYR C CE2 
5900  C CZ  . TYR C 254 ? 1.0221 1.1054 0.4147 0.4569  -0.0902 0.2914  254 TYR C CZ  
5901  O OH  . TYR C 254 ? 1.0738 1.0843 0.4225 0.4581  -0.0986 0.2975  254 TYR C OH  
5902  N N   . LYS C 255 ? 0.8534 1.3115 0.4220 0.4692  -0.0909 0.2627  255 LYS C N   
5903  C CA  . LYS C 255 ? 0.8209 1.3638 0.4243 0.4617  -0.0903 0.2584  255 LYS C CA  
5904  C C   . LYS C 255 ? 0.8003 1.3772 0.4219 0.4529  -0.0816 0.2540  255 LYS C C   
5905  O O   . LYS C 255 ? 0.8197 1.3823 0.4298 0.4749  -0.0824 0.2439  255 LYS C O   
5906  C CB  . LYS C 255 ? 0.8403 1.4259 0.4434 0.4947  -0.1039 0.2451  255 LYS C CB  
5907  C CG  . LYS C 255 ? 0.8140 1.4755 0.4447 0.4826  -0.1061 0.2451  255 LYS C CG  
5908  C CD  . LYS C 255 ? 0.8388 1.5203 0.4617 0.5144  -0.1209 0.2347  255 LYS C CD  
5909  C CE  . LYS C 255 ? 0.8529 1.5889 0.4830 0.5492  -0.1292 0.2120  255 LYS C CE  
5910  N NZ  . LYS C 255 ? 0.8674 1.6462 0.5005 0.5748  -0.1438 0.2003  255 LYS C NZ  
5911  N N   . ILE C 256 ? 0.7645 1.3852 0.4131 0.4202  -0.0756 0.2616  256 ILE C N   
5912  C CA  . ILE C 256 ? 0.7450 1.3939 0.4089 0.4037  -0.0675 0.2614  256 ILE C CA  
5913  C C   . ILE C 256 ? 0.7356 1.4795 0.4200 0.4099  -0.0702 0.2498  256 ILE C C   
5914  O O   . ILE C 256 ? 0.7135 1.5161 0.4192 0.3831  -0.0718 0.2564  256 ILE C O   
5915  C CB  . ILE C 256 ? 0.7179 1.3561 0.3969 0.3612  -0.0631 0.2772  256 ILE C CB  
5916  C CG1 . ILE C 256 ? 0.7227 1.2946 0.3896 0.3529  -0.0643 0.2853  256 ILE C CG1 
5917  C CG2 . ILE C 256 ? 0.7097 1.3368 0.3911 0.3490  -0.0544 0.2785  256 ILE C CG2 
5918  C CD1 . ILE C 256 ? 0.7024 1.2515 0.3824 0.3180  -0.0627 0.2956  256 ILE C CD1 
5919  N N   . VAL C 257 ? 0.7552 1.5161 0.4326 0.4445  -0.0726 0.2311  257 VAL C N   
5920  C CA  . VAL C 257 ? 0.7497 1.6103 0.4467 0.4560  -0.0759 0.2138  257 VAL C CA  
5921  C C   . VAL C 257 ? 0.7252 1.6448 0.4415 0.4275  -0.0666 0.2150  257 VAL C C   
5922  O O   . VAL C 257 ? 0.7072 1.7146 0.4443 0.4065  -0.0670 0.2147  257 VAL C O   
5923  C CB  . VAL C 257 ? 0.7837 1.6482 0.4689 0.5083  -0.0864 0.1878  257 VAL C CB  
5924  C CG1 . VAL C 257 ? 0.8097 1.6306 0.4769 0.5322  -0.0992 0.1882  257 VAL C CG1 
5925  C CG2 . VAL C 257 ? 0.8046 1.6097 0.4718 0.5267  -0.0845 0.1808  257 VAL C CG2 
5926  N N   . LYS C 258 ? 0.7264 1.5990 0.4339 0.4241  -0.0588 0.2174  258 LYS C N   
5927  C CA  . LYS C 258 ? 0.7063 1.6283 0.4288 0.3971  -0.0504 0.2192  258 LYS C CA  
5928  C C   . LYS C 258 ? 0.6912 1.5524 0.4112 0.3599  -0.0439 0.2421  258 LYS C C   
5929  O O   . LYS C 258 ? 0.7020 1.4760 0.4041 0.3684  -0.0412 0.2468  258 LYS C O   
5930  C CB  . LYS C 258 ? 0.7216 1.6612 0.4403 0.4292  -0.0482 0.1956  258 LYS C CB  
5931  C CG  . LYS C 258 ? 0.7173 1.7765 0.4561 0.4389  -0.0502 0.1728  258 LYS C CG  
5932  C CD  . LYS C 258 ? 0.7107 1.8126 0.4571 0.4325  -0.0418 0.1622  258 LYS C CD  
5933  C CE  . LYS C 258 ? 0.7374 1.7784 0.4670 0.4744  -0.0436 0.1439  258 LYS C CE  
5934  N NZ  . LYS C 258 ? 0.7345 1.8500 0.4767 0.4808  -0.0389 0.1216  258 LYS C NZ  
5935  N N   . LYS C 259 ? 0.6695 1.5791 0.4064 0.3176  -0.0433 0.2557  259 LYS C N   
5936  C CA  . LYS C 259 ? 0.6573 1.5197 0.3949 0.2815  -0.0408 0.2751  259 LYS C CA  
5937  C C   . LYS C 259 ? 0.6491 1.5620 0.3945 0.2636  -0.0348 0.2734  259 LYS C C   
5938  O O   . LYS C 259 ? 0.6416 1.6431 0.4005 0.2422  -0.0374 0.2737  259 LYS C O   
5939  C CB  . LYS C 259 ? 0.6459 1.5115 0.3943 0.2427  -0.0511 0.2951  259 LYS C CB  
5940  C CG  . LYS C 259 ? 0.6519 1.4731 0.3946 0.2559  -0.0573 0.2970  259 LYS C CG  
5941  C CD  . LYS C 259 ? 0.6429 1.4643 0.3974 0.2176  -0.0701 0.3150  259 LYS C CD  
5942  C CE  . LYS C 259 ? 0.6485 1.4332 0.3984 0.2320  -0.0759 0.3143  259 LYS C CE  
5943  N NZ  . LYS C 259 ? 0.6429 1.4315 0.4055 0.1978  -0.0912 0.3288  259 LYS C NZ  
5944  N N   . GLY C 260 ? 0.6519 1.5121 0.3877 0.2702  -0.0270 0.2716  260 GLY C N   
5945  C CA  . GLY C 260 ? 0.6449 1.5470 0.3866 0.2536  -0.0208 0.2700  260 GLY C CA  
5946  C C   . GLY C 260 ? 0.6421 1.4682 0.3761 0.2394  -0.0161 0.2811  260 GLY C C   
5947  O O   . GLY C 260 ? 0.6441 1.3899 0.3700 0.2392  -0.0178 0.2900  260 GLY C O   
5948  N N   . ASP C 261 ? 0.6375 1.4942 0.3747 0.2270  -0.0101 0.2791  261 ASP C N   
5949  C CA  . ASP C 261 ? 0.6359 1.4259 0.3660 0.2165  -0.0049 0.2868  261 ASP C CA  
5950  C C   . ASP C 261 ? 0.6507 1.3744 0.3636 0.2584  0.0029  0.2715  261 ASP C C   
5951  O O   . ASP C 261 ? 0.6625 1.4147 0.3712 0.2906  0.0067  0.2512  261 ASP C O   
5952  C CB  . ASP C 261 ? 0.6290 1.4747 0.3659 0.1916  -0.0010 0.2885  261 ASP C CB  
5953  C CG  . ASP C 261 ? 0.6209 1.5091 0.3687 0.1394  -0.0124 0.3109  261 ASP C CG  
5954  O OD1 . ASP C 261 ? 0.6205 1.4743 0.3705 0.1220  -0.0243 0.3263  261 ASP C OD1 
5955  O OD2 . ASP C 261 ? 0.6183 1.5739 0.3709 0.1144  -0.0113 0.3131  261 ASP C OD2 
5956  N N   . SER C 262 ? 0.6534 1.2902 0.3558 0.2569  0.0031  0.2803  262 SER C N   
5957  C CA  . SER C 262 ? 0.6718 1.2380 0.3536 0.2881  0.0091  0.2704  262 SER C CA  
5958  C C   . SER C 262 ? 0.6666 1.1626 0.3435 0.2680  0.0128  0.2816  262 SER C C   
5959  O O   . SER C 262 ? 0.6506 1.1520 0.3411 0.2342  0.0084  0.2952  262 SER C O   
5960  C CB  . SER C 262 ? 0.6883 1.2268 0.3579 0.3140  0.0037  0.2658  262 SER C CB  
5961  O OG  . SER C 262 ? 0.7117 1.1751 0.3566 0.3373  0.0066  0.2604  262 SER C OG  
5962  N N   . THR C 263 ? 0.6836 1.1140 0.3401 0.2879  0.0187  0.2754  263 THR C N   
5963  C CA  . THR C 263 ? 0.6799 1.0471 0.3309 0.2712  0.0231  0.2825  263 THR C CA  
5964  C C   . THR C 263 ? 0.7058 1.0047 0.3294 0.2938  0.0273  0.2762  263 THR C C   
5965  O O   . THR C 263 ? 0.7293 1.0240 0.3368 0.3226  0.0270  0.2657  263 THR C O   
5966  C CB  . THR C 263 ? 0.6683 1.0473 0.3274 0.2542  0.0286  0.2842  263 THR C CB  
5967  O OG1 . THR C 263 ? 0.6582 0.9926 0.3214 0.2298  0.0281  0.2931  263 THR C OG1 
5968  C CG2 . THR C 263 ? 0.6859 1.0480 0.3284 0.2795  0.0369  0.2711  263 THR C CG2 
5969  N N   . ILE C 264 ? 0.7052 0.9523 0.3228 0.2800  0.0288  0.2818  264 ILE C N   
5970  C CA  . ILE C 264 ? 0.7315 0.9147 0.3204 0.2925  0.0333  0.2782  264 ILE C CA  
5971  C C   . ILE C 264 ? 0.7315 0.8849 0.3156 0.2837  0.0420  0.2767  264 ILE C C   
5972  O O   . ILE C 264 ? 0.7148 0.8531 0.3092 0.2610  0.0448  0.2802  264 ILE C O   
5973  C CB  . ILE C 264 ? 0.7333 0.8854 0.3163 0.2824  0.0310  0.2819  264 ILE C CB  
5974  C CG1 . ILE C 264 ? 0.7364 0.9166 0.3221 0.2931  0.0222  0.2831  264 ILE C CG1 
5975  C CG2 . ILE C 264 ? 0.7633 0.8538 0.3131 0.2886  0.0359  0.2797  264 ILE C CG2 
5976  C CD1 . ILE C 264 ? 0.7282 0.8990 0.3197 0.2781  0.0184  0.2861  264 ILE C CD1 
5977  N N   . MET C 265 ? 0.6405 0.5846 0.3818 0.1487  -0.0653 0.1902  265 MET C N   
5978  C CA  . MET C 265 ? 0.6169 0.5401 0.3822 0.1524  -0.0496 0.1943  265 MET C CA  
5979  C C   . MET C 265 ? 0.6279 0.5423 0.3851 0.1679  -0.0371 0.2112  265 MET C C   
5980  O O   . MET C 265 ? 0.6447 0.5688 0.3941 0.1812  -0.0380 0.2246  265 MET C O   
5981  C CB  . MET C 265 ? 0.5967 0.5345 0.3971 0.1546  -0.0476 0.1991  265 MET C CB  
5982  C CG  . MET C 265 ? 0.5763 0.4889 0.3967 0.1468  -0.0362 0.1971  265 MET C CG  
5983  S SD  . MET C 265 ? 0.5683 0.4914 0.4136 0.1547  -0.0365 0.1985  265 MET C SD  
5984  C CE  . MET C 265 ? 0.5485 0.5154 0.4058 0.1342  -0.0508 0.1810  265 MET C CE  
5985  N N   . LYS C 266 ? 0.6214 0.5255 0.3786 0.1652  -0.0256 0.2125  266 LYS C N   
5986  C CA  . LYS C 266 ? 0.6321 0.5459 0.3829 0.1716  -0.0134 0.2315  266 LYS C CA  
5987  C C   . LYS C 266 ? 0.6239 0.5302 0.3975 0.1546  -0.0043 0.2434  266 LYS C C   
5988  O O   . LYS C 266 ? 0.6040 0.5105 0.3937 0.1415  0.0001  0.2371  266 LYS C O   
5989  C CB  . LYS C 266 ? 0.6399 0.5652 0.3672 0.1827  -0.0064 0.2289  266 LYS C CB  
5990  C CG  . LYS C 266 ? 0.6766 0.5937 0.3575 0.2040  -0.0127 0.2235  266 LYS C CG  
5991  C CD  . LYS C 266 ? 0.6930 0.6358 0.3648 0.2166  -0.0069 0.2446  266 LYS C CD  
5992  C CE  . LYS C 266 ? 0.7354 0.6648 0.3560 0.2388  -0.0143 0.2383  266 LYS C CE  
5993  N NZ  . LYS C 266 ? 0.7502 0.7065 0.3645 0.2509  -0.0094 0.2595  266 LYS C NZ  
5994  N N   . SER C 267 ? 0.6514 0.5420 0.4160 0.1541  -0.0022 0.2605  267 SER C N   
5995  C CA  . SER C 267 ? 0.6710 0.5278 0.4340 0.1343  0.0042  0.2716  267 SER C CA  
5996  C C   . SER C 267 ? 0.7254 0.5535 0.4535 0.1305  0.0086  0.2954  267 SER C C   
5997  O O   . SER C 267 ? 0.7468 0.5696 0.4582 0.1538  0.0044  0.3004  267 SER C O   
5998  C CB  . SER C 267 ? 0.6682 0.4951 0.4408 0.1414  -0.0012 0.2593  267 SER C CB  
5999  O OG  . SER C 267 ? 0.7065 0.4798 0.4590 0.1267  0.0045  0.2689  267 SER C OG  
6000  N N   . GLU C 268 ? 0.7553 0.5642 0.4668 0.0971  0.0163  0.3109  268 GLU C N   
6001  C CA  . GLU C 268 ? 0.8267 0.5892 0.4892 0.0813  0.0203  0.3354  268 GLU C CA  
6002  C C   . GLU C 268 ? 0.8900 0.5571 0.5097 0.0902  0.0184  0.3358  268 GLU C C   
6003  O O   . GLU C 268 ? 0.9669 0.5715 0.5293 0.0915  0.0204  0.3537  268 GLU C O   
6004  C CB  . GLU C 268 ? 0.8470 0.6303 0.4976 0.0303  0.0276  0.3546  268 GLU C CB  
6005  C CG  . GLU C 268 ? 0.7932 0.6827 0.4800 0.0298  0.0324  0.3577  268 GLU C CG  
6006  C CD  . GLU C 268 ? 0.7891 0.7153 0.4722 0.0625  0.0328  0.3635  268 GLU C CD  
6007  O OE1 . GLU C 268 ? 0.8407 0.7416 0.4877 0.0540  0.0344  0.3839  268 GLU C OE1 
6008  O OE2 . GLU C 268 ? 0.7443 0.7155 0.4512 0.0959  0.0311  0.3477  268 GLU C OE2 
6009  N N   . LEU C 269 ? 0.8675 0.5199 0.5066 0.1007  0.0154  0.3173  269 LEU C N   
6010  C CA  . LEU C 269 ? 0.9343 0.4975 0.5261 0.1181  0.0154  0.3171  269 LEU C CA  
6011  C C   . LEU C 269 ? 0.9622 0.5153 0.5336 0.1720  0.0122  0.3200  269 LEU C C   
6012  O O   . LEU C 269 ? 0.9087 0.5362 0.5193 0.1930  0.0068  0.3148  269 LEU C O   
6013  C CB  . LEU C 269 ? 0.8955 0.4630 0.5188 0.1198  0.0136  0.2970  269 LEU C CB  
6014  C CG  . LEU C 269 ? 0.9096 0.4474 0.5228 0.0699  0.0173  0.2975  269 LEU C CG  
6015  C CD1 . LEU C 269 ? 0.8412 0.4188 0.5074 0.0716  0.0153  0.2757  269 LEU C CD1 
6016  C CD2 . LEU C 269 ? 1.0283 0.4396 0.5505 0.0569  0.0201  0.3100  269 LEU C CD2 
6017  N N   . GLU C 270 ? 1.0567 0.5145 0.5574 0.1957  0.0153  0.3288  270 GLU C N   
6018  C CA  . GLU C 270 ? 1.1037 0.5487 0.5696 0.2546  0.0142  0.3369  270 GLU C CA  
6019  C C   . GLU C 270 ? 1.0827 0.5619 0.5697 0.3044  0.0111  0.3238  270 GLU C C   
6020  O O   . GLU C 270 ? 0.9877 0.5685 0.5513 0.3017  0.0042  0.3078  270 GLU C O   
6021  C CB  . GLU C 270 ? 1.2412 0.5567 0.5971 0.2600  0.0209  0.3599  270 GLU C CB  
6022  C CG  . GLU C 270 ? 1.3375 0.5247 0.6156 0.2229  0.0260  0.3643  270 GLU C CG  
6023  C CD  . GLU C 270 ? 1.4974 0.5362 0.6451 0.2249  0.0313  0.3877  270 GLU C CD  
6024  O OE1 . GLU C 270 ? 1.5336 0.5684 0.6518 0.2688  0.0325  0.4002  270 GLU C OE1 
6025  O OE2 . GLU C 270 ? 1.5973 0.5165 0.6630 0.1796  0.0337  0.3940  270 GLU C OE2 
6026  N N   . TYR C 271 ? 1.1796 0.5749 0.5919 0.3498  0.0164  0.3315  271 TYR C N   
6027  C CA  . TYR C 271 ? 1.1672 0.6146 0.5947 0.4082  0.0149  0.3246  271 TYR C CA  
6028  C C   . TYR C 271 ? 1.2691 0.5999 0.6147 0.4358  0.0234  0.3260  271 TYR C C   
6029  O O   . TYR C 271 ? 1.4017 0.6009 0.6371 0.4599  0.0305  0.3413  271 TYR C O   
6030  C CB  . TYR C 271 ? 1.1887 0.6903 0.6024 0.4690  0.0126  0.3380  271 TYR C CB  
6031  C CG  . TYR C 271 ? 1.1669 0.7643 0.6056 0.5289  0.0099  0.3356  271 TYR C CG  
6032  C CD1 . TYR C 271 ? 1.0518 0.7871 0.5870 0.5063  -0.0003 0.3202  271 TYR C CD1 
6033  C CD2 . TYR C 271 ? 1.2719 0.8240 0.6291 0.6092  0.0179  0.3509  271 TYR C CD2 
6034  C CE1 . TYR C 271 ? 1.0329 0.8744 0.5921 0.5527  -0.0035 0.3216  271 TYR C CE1 
6035  C CE2 . TYR C 271 ? 1.2513 0.9160 0.6335 0.6679  0.0164  0.3526  271 TYR C CE2 
6036  C CZ  . TYR C 271 ? 1.1272 0.9449 0.6153 0.6349  0.0051  0.3387  271 TYR C CZ  
6037  O OH  . TYR C 271 ? 1.1083 1.0550 0.6221 0.6853  0.0027  0.3437  271 TYR C OH  
6038  N N   . GLY C 272 ? 1.2187 0.5876 0.6072 0.4328  0.0225  0.3100  272 GLY C N   
6039  C CA  . GLY C 272 ? 1.3136 0.5745 0.6247 0.4602  0.0303  0.3087  272 GLY C CA  
6040  C C   . GLY C 272 ? 1.3775 0.6504 0.6413 0.5553  0.0357  0.3169  272 GLY C C   
6041  O O   . GLY C 272 ? 1.4896 0.6482 0.6594 0.5945  0.0442  0.3192  272 GLY C O   
6042  N N   . ASN C 273 ? 1.3153 0.7281 0.6362 0.5938  0.0306  0.3226  273 ASN C N   
6043  C CA  . ASN C 273 ? 1.3522 0.8320 0.6501 0.6857  0.0347  0.3328  273 ASN C CA  
6044  C C   . ASN C 273 ? 1.3196 0.8466 0.6478 0.6994  0.0369  0.3209  273 ASN C C   
6045  O O   . ASN C 273 ? 1.4085 0.9036 0.6659 0.7773  0.0467  0.3292  273 ASN C O   
6046  C CB  . ASN C 273 ? 1.5250 0.8622 0.6783 0.7623  0.0465  0.3530  273 ASN C CB  
6047  C CG  . ASN C 273 ? 1.5515 0.9982 0.6913 0.8625  0.0494  0.3705  273 ASN C CG  
6048  O OD1 . ASN C 273 ? 1.6138 1.0434 0.7024 0.9033  0.0512  0.3880  273 ASN C OD1 
6049  N ND2 . ASN C 273 ? 1.5044 1.0760 0.6908 0.9025  0.0499  0.3678  273 ASN C ND2 
6050  N N   . CYS C 274 ? 1.1977 0.7996 0.6258 0.6272  0.0285  0.3024  274 CYS C N   
6051  C CA  . CYS C 274 ? 1.1531 0.8062 0.6209 0.6266  0.0294  0.2900  274 CYS C CA  
6052  C C   . CYS C 274 ? 1.0239 0.8737 0.6044 0.6056  0.0175  0.2854  274 CYS C C   
6053  O O   . CYS C 274 ? 0.9700 0.8922 0.5948 0.5777  0.0076  0.2876  274 CYS C O   
6054  C CB  . CYS C 274 ? 1.1403 0.6919 0.6110 0.5556  0.0301  0.2728  274 CYS C CB  
6055  S SG  . CYS C 274 ? 0.9812 0.6520 0.5827 0.4708  0.0186  0.2517  274 CYS C SG  
6056  N N   . ASN C 275 ? 0.9857 0.9161 0.6027 0.6167  0.0180  0.2798  275 ASN C N   
6057  C CA  . ASN C 275 ? 0.8777 0.9860 0.5901 0.5844  0.0056  0.2759  275 ASN C CA  
6058  C C   . ASN C 275 ? 0.8061 0.9091 0.5724 0.5172  0.0023  0.2548  275 ASN C C   
6059  O O   . ASN C 275 ? 0.8408 0.8501 0.5753 0.5235  0.0116  0.2471  275 ASN C O   
6060  C CB  . ASN C 275 ? 0.8964 1.1407 0.6073 0.6576  0.0084  0.2931  275 ASN C CB  
6061  C CG  . ASN C 275 ? 0.8007 1.2423 0.5995 0.6164  -0.0072 0.2948  275 ASN C CG  
6062  O OD1 . ASN C 275 ? 0.7662 1.2682 0.5932 0.5825  -0.0198 0.2973  275 ASN C OD1 
6063  N ND2 . ASN C 275 ? 0.7669 1.3061 0.6014 0.6154  -0.0071 0.2940  275 ASN C ND2 
6064  N N   . THR C 276 ? 0.7181 0.9132 0.5553 0.4538  -0.0112 0.2456  276 THR C N   
6065  C CA  . THR C 276 ? 0.6565 0.8458 0.5379 0.3923  -0.0146 0.2265  276 THR C CA  
6066  C C   . THR C 276 ? 0.5900 0.9174 0.5301 0.3467  -0.0297 0.2236  276 THR C C   
6067  O O   . THR C 276 ? 0.5879 1.0204 0.5374 0.3561  -0.0389 0.2364  276 THR C O   
6068  C CB  . THR C 276 ? 0.6465 0.7177 0.5216 0.3420  -0.0138 0.2131  276 THR C CB  
6069  O OG1 . THR C 276 ? 0.5975 0.6589 0.5064 0.2944  -0.0149 0.1960  276 THR C OG1 
6070  C CG2 . THR C 276 ? 0.6238 0.7175 0.5117 0.3119  -0.0239 0.2142  276 THR C CG2 
6071  N N   . LYS C 277 ? 0.5462 0.8699 0.5172 0.2949  -0.0329 0.2079  277 LYS C N   
6072  C CA  . LYS C 277 ? 0.5018 0.9209 0.5095 0.2360  -0.0484 0.2028  277 LYS C CA  
6073  C C   . LYS C 277 ? 0.4784 0.8129 0.4873 0.1741  -0.0533 0.1835  277 LYS C C   
6074  O O   . LYS C 277 ? 0.4610 0.8345 0.4795 0.1205  -0.0659 0.1763  277 LYS C O   
6075  C CB  . LYS C 277 ? 0.4847 0.9957 0.5179 0.2353  -0.0480 0.2055  277 LYS C CB  
6076  C CG  . LYS C 277 ? 0.4698 1.1443 0.5279 0.2053  -0.0638 0.2175  277 LYS C CG  
6077  C CD  . LYS C 277 ? 0.4622 1.2530 0.5425 0.2251  -0.0599 0.2286  277 LYS C CD  
6078  C CE  . LYS C 277 ? 0.4333 1.2634 0.5353 0.1463  -0.0709 0.2194  277 LYS C CE  
6079  N NZ  . LYS C 277 ? 0.4340 1.3687 0.5395 0.0798  -0.0927 0.2265  277 LYS C NZ  
6080  N N   . CYS C 278 ? 0.4893 0.7081 0.4789 0.1826  -0.0434 0.1771  278 CYS C N   
6081  C CA  . CYS C 278 ? 0.4743 0.6196 0.4596 0.1396  -0.0449 0.1624  278 CYS C CA  
6082  C C   . CYS C 278 ? 0.4976 0.5606 0.4588 0.1584  -0.0365 0.1665  278 CYS C C   
6083  O O   . CYS C 278 ? 0.5205 0.5262 0.4667 0.1831  -0.0252 0.1701  278 CYS C O   
6084  C CB  . CYS C 278 ? 0.4538 0.5624 0.4509 0.1198  -0.0390 0.1494  278 CYS C CB  
6085  S SG  . CYS C 278 ? 0.4445 0.4676 0.4289 0.0837  -0.0371 0.1345  278 CYS C SG  
6086  N N   . GLN C 279 ? 0.5015 0.5553 0.4510 0.1437  -0.0424 0.1669  279 GLN C N   
6087  C CA  . GLN C 279 ? 0.5259 0.5186 0.4522 0.1588  -0.0351 0.1747  279 GLN C CA  
6088  C C   . GLN C 279 ? 0.5149 0.4636 0.4351 0.1300  -0.0336 0.1663  279 GLN C C   
6089  O O   . GLN C 279 ? 0.5040 0.4677 0.4219 0.1061  -0.0417 0.1564  279 GLN C O   
6090  C CB  . GLN C 279 ? 0.5489 0.5788 0.4614 0.1817  -0.0410 0.1878  279 GLN C CB  
6091  C CG  . GLN C 279 ? 0.5821 0.5504 0.4652 0.1972  -0.0336 0.1988  279 GLN C CG  
6092  C CD  . GLN C 279 ? 0.6283 0.5338 0.4819 0.2278  -0.0218 0.2091  279 GLN C CD  
6093  O OE1 . GLN C 279 ? 0.6575 0.5827 0.4977 0.2674  -0.0203 0.2171  279 GLN C OE1 
6094  N NE2 . GLN C 279 ? 0.6467 0.4759 0.4804 0.2100  -0.0135 0.2103  279 GLN C NE2 
6095  N N   . THR C 280 ? 0.5295 0.4233 0.4373 0.1330  -0.0231 0.1720  280 THR C N   
6096  C CA  . THR C 280 ? 0.5252 0.3965 0.4252 0.1155  -0.0193 0.1706  280 THR C CA  
6097  C C   . THR C 280 ? 0.5573 0.4077 0.4346 0.1253  -0.0148 0.1871  280 THR C C   
6098  O O   . THR C 280 ? 0.5900 0.4194 0.4508 0.1435  -0.0127 0.1983  280 THR C O   
6099  C CB  . THR C 280 ? 0.5114 0.3570 0.4200 0.0990  -0.0109 0.1654  280 THR C CB  
6100  O OG1 . THR C 280 ? 0.5404 0.3466 0.4336 0.0983  -0.0030 0.1776  280 THR C OG1 
6101  C CG2 . THR C 280 ? 0.4896 0.3458 0.4181 0.0939  -0.0131 0.1525  280 THR C CG2 
6102  N N   . PRO C 281 ? 0.5573 0.4110 0.4258 0.1167  -0.0125 0.1899  281 PRO C N   
6103  C CA  . PRO C 281 ? 0.5879 0.4281 0.4351 0.1192  -0.0069 0.2078  281 PRO C CA  
6104  C C   . PRO C 281 ? 0.6180 0.4176 0.4516 0.1032  0.0017  0.2198  281 PRO C C   
6105  O O   . PRO C 281 ? 0.6611 0.4333 0.4650 0.1018  0.0050  0.2368  281 PRO C O   
6106  C CB  . PRO C 281 ? 0.5765 0.4421 0.4184 0.1156  -0.0046 0.2073  281 PRO C CB  
6107  C CG  . PRO C 281 ? 0.5529 0.4264 0.4021 0.1132  -0.0085 0.1882  281 PRO C CG  
6108  C CD  . PRO C 281 ? 0.5410 0.4108 0.4069 0.1102  -0.0159 0.1774  281 PRO C CD  
6109  N N   . MET C 282 ? 0.6053 0.3954 0.4523 0.0874  0.0046  0.2114  282 MET C N   
6110  C CA  . MET C 282 ? 0.6436 0.3883 0.4686 0.0633  0.0105  0.2205  282 MET C CA  
6111  C C   . MET C 282 ? 0.6907 0.3709 0.4858 0.0799  0.0097  0.2204  282 MET C C   
6112  O O   . MET C 282 ? 0.7574 0.3684 0.5035 0.0654  0.0132  0.2317  282 MET C O   
6113  C CB  . MET C 282 ? 0.6119 0.3791 0.4613 0.0411  0.0133  0.2111  282 MET C CB  
6114  C CG  . MET C 282 ? 0.5752 0.4071 0.4454 0.0388  0.0159  0.2105  282 MET C CG  
6115  S SD  . MET C 282 ? 0.5974 0.4673 0.4564 0.0028  0.0236  0.2326  282 MET C SD  
6116  C CE  . MET C 282 ? 0.5896 0.4490 0.4586 -0.0255 0.0247  0.2245  282 MET C CE  
6117  N N   . GLY C 283 ? 0.6660 0.3683 0.4812 0.1100  0.0051  0.2089  283 GLY C N   
6118  C CA  . GLY C 283 ? 0.7096 0.3696 0.4969 0.1399  0.0058  0.2094  283 GLY C CA  
6119  C C   . GLY C 283 ? 0.6614 0.3828 0.4886 0.1607  0.0007  0.1962  283 GLY C C   
6120  O O   . GLY C 283 ? 0.6054 0.3880 0.4723 0.1478  -0.0050 0.1867  283 GLY C O   
6121  N N   . ALA C 284 ? 0.6944 0.3968 0.5016 0.1928  0.0029  0.1967  284 ALA C N   
6122  C CA  . ALA C 284 ? 0.6537 0.4308 0.4975 0.2115  -0.0016 0.1884  284 ALA C CA  
6123  C C   . ALA C 284 ? 0.6335 0.4001 0.4930 0.1974  0.0015  0.1758  284 ALA C C   
6124  O O   . ALA C 284 ? 0.6690 0.3595 0.4978 0.1856  0.0078  0.1751  284 ALA C O   
6125  C CB  . ALA C 284 ? 0.7019 0.4939 0.5162 0.2672  -0.0004 0.2004  284 ALA C CB  
6126  N N   . ILE C 285 ? 0.5823 0.4256 0.4845 0.1938  -0.0037 0.1669  285 ILE C N   
6127  C CA  . ILE C 285 ? 0.5568 0.4022 0.4787 0.1801  -0.0012 0.1548  285 ILE C CA  
6128  C C   . ILE C 285 ? 0.5608 0.4647 0.4900 0.2145  -0.0010 0.1572  285 ILE C C   
6129  O O   . ILE C 285 ? 0.5443 0.5357 0.4929 0.2250  -0.0080 0.1632  285 ILE C O   
6130  C CB  . ILE C 285 ? 0.4980 0.3763 0.4570 0.1371  -0.0068 0.1421  285 ILE C CB  
6131  C CG1 . ILE C 285 ? 0.4966 0.3185 0.4473 0.1109  -0.0017 0.1389  285 ILE C CG1 
6132  C CG2 . ILE C 285 ? 0.4684 0.3865 0.4532 0.1285  -0.0080 0.1322  285 ILE C CG2 
6133  C CD1 . ILE C 285 ? 0.4617 0.3061 0.4279 0.0849  -0.0057 0.1313  285 ILE C CD1 
6134  N N   . ASN C 286 ? 0.5873 0.4483 0.4973 0.2308  0.0067  0.1539  286 ASN C N   
6135  C CA  . ASN C 286 ? 0.5929 0.5121 0.5076 0.2675  0.0093  0.1565  286 ASN C CA  
6136  C C   . ASN C 286 ? 0.5735 0.4705 0.5007 0.2479  0.0133  0.1434  286 ASN C C   
6137  O O   . ASN C 286 ? 0.6255 0.4362 0.5089 0.2642  0.0212  0.1411  286 ASN C O   
6138  C CB  . ASN C 286 ? 0.6803 0.5537 0.5304 0.3344  0.0177  0.1700  286 ASN C CB  
6139  C CG  . ASN C 286 ? 0.6961 0.6361 0.5433 0.3853  0.0231  0.1753  286 ASN C CG  
6140  O OD1 . ASN C 286 ? 0.6360 0.7022 0.5391 0.3737  0.0173  0.1762  286 ASN C OD1 
6141  N ND2 . ASN C 286 ? 0.7884 0.6411 0.5607 0.4414  0.0340  0.1799  286 ASN C ND2 
6142  N N   . SER C 287 ? 0.5088 0.4741 0.4863 0.2100  0.0071  0.1348  287 SER C N   
6143  C CA  . SER C 287 ? 0.4871 0.4412 0.4792 0.1917  0.0106  0.1230  287 SER C CA  
6144  C C   . SER C 287 ? 0.4376 0.4898 0.4725 0.1661  0.0038  0.1203  287 SER C C   
6145  O O   . SER C 287 ? 0.4199 0.5401 0.4710 0.1489  -0.0057 0.1255  287 SER C O   
6146  C CB  . SER C 287 ? 0.4759 0.3526 0.4648 0.1525  0.0117  0.1122  287 SER C CB  
6147  O OG  . SER C 287 ? 0.4308 0.3377 0.4475 0.1136  0.0046  0.1064  287 SER C OG  
6148  N N   . SER C 288 ? 0.4245 0.4792 0.4701 0.1594  0.0079  0.1126  288 SER C N   
6149  C CA  . SER C 288 ? 0.3878 0.5206 0.4649 0.1263  0.0019  0.1100  288 SER C CA  
6150  C C   . SER C 288 ? 0.3633 0.4414 0.4448 0.0794  0.0001  0.0950  288 SER C C   
6151  O O   . SER C 288 ? 0.3461 0.4609 0.4389 0.0460  -0.0046 0.0913  288 SER C O   
6152  C CB  . SER C 288 ? 0.3948 0.5835 0.4781 0.1573  0.0088  0.1150  288 SER C CB  
6153  O OG  . SER C 288 ? 0.4293 0.5315 0.4829 0.1917  0.0199  0.1096  288 SER C OG  
6154  N N   . MET C 289 ? 0.3692 0.3632 0.4353 0.0773  0.0041  0.0886  289 MET C N   
6155  C CA  . MET C 289 ? 0.3525 0.3024 0.4174 0.0450  0.0041  0.0772  289 MET C CA  
6156  C C   . MET C 289 ? 0.3482 0.3166 0.4068 0.0134  -0.0054 0.0755  289 MET C C   
6157  O O   . MET C 289 ? 0.3580 0.3521 0.4115 0.0132  -0.0124 0.0824  289 MET C O   
6158  C CB  . MET C 289 ? 0.3635 0.2487 0.4129 0.0478  0.0087  0.0765  289 MET C CB  
6159  C CG  . MET C 289 ? 0.3906 0.2301 0.4243 0.0669  0.0160  0.0780  289 MET C CG  
6160  S SD  . MET C 289 ? 0.3821 0.2060 0.4214 0.0589  0.0216  0.0670  289 MET C SD  
6161  C CE  . MET C 289 ? 0.4272 0.1722 0.4292 0.0565  0.0260  0.0688  289 MET C CE  
6162  N N   . PRO C 290 ? 0.3457 0.2909 0.3934 -0.0126 -0.0062 0.0662  290 PRO C N   
6163  C CA  . PRO C 290 ? 0.3687 0.2976 0.3838 -0.0422 -0.0154 0.0632  290 PRO C CA  
6164  C C   . PRO C 290 ? 0.3823 0.2594 0.3717 -0.0336 -0.0142 0.0617  290 PRO C C   
6165  O O   . PRO C 290 ? 0.4156 0.2709 0.3666 -0.0503 -0.0221 0.0601  290 PRO C O   
6166  C CB  . PRO C 290 ? 0.3792 0.2801 0.3758 -0.0640 -0.0140 0.0544  290 PRO C CB  
6167  C CG  . PRO C 290 ? 0.3521 0.2398 0.3736 -0.0404 -0.0022 0.0509  290 PRO C CG  
6168  C CD  . PRO C 290 ? 0.3345 0.2616 0.3882 -0.0150 0.0006  0.0585  290 PRO C CD  
6169  N N   . PHE C 291 ? 0.3651 0.2235 0.3685 -0.0106 -0.0050 0.0633  291 PHE C N   
6170  C CA  . PHE C 291 ? 0.3747 0.2033 0.3584 -0.0007 -0.0020 0.0654  291 PHE C CA  
6171  C C   . PHE C 291 ? 0.3635 0.1998 0.3650 0.0151  0.0019  0.0752  291 PHE C C   
6172  O O   . PHE C 291 ? 0.3571 0.1994 0.3768 0.0223  0.0048  0.0779  291 PHE C O   
6173  C CB  . PHE C 291 ? 0.3765 0.1788 0.3472 0.0038  0.0060  0.0604  291 PHE C CB  
6174  C CG  . PHE C 291 ? 0.4087 0.1770 0.3380 -0.0056 0.0037  0.0516  291 PHE C CG  
6175  C CD1 . PHE C 291 ? 0.4571 0.1853 0.3306 -0.0028 0.0001  0.0500  291 PHE C CD1 
6176  C CD2 . PHE C 291 ? 0.4045 0.1691 0.3385 -0.0162 0.0055  0.0451  291 PHE C CD2 
6177  C CE1 . PHE C 291 ? 0.5120 0.1829 0.3236 -0.0113 -0.0021 0.0419  291 PHE C CE1 
6178  C CE2 . PHE C 291 ? 0.4498 0.1675 0.3313 -0.0271 0.0034  0.0379  291 PHE C CE2 
6179  C CZ  . PHE C 291 ? 0.5097 0.1737 0.3244 -0.0250 -0.0005 0.0362  291 PHE C CZ  
6180  N N   . HIS C 292 ? 0.3723 0.1996 0.3576 0.0211  0.0025  0.0808  292 HIS C N   
6181  C CA  . HIS C 292 ? 0.3720 0.1985 0.3633 0.0285  0.0070  0.0918  292 HIS C CA  
6182  C C   . HIS C 292 ? 0.3772 0.2062 0.3517 0.0321  0.0116  0.0971  292 HIS C C   
6183  O O   . HIS C 292 ? 0.3881 0.2106 0.3385 0.0385  0.0111  0.0917  292 HIS C O   
6184  C CB  . HIS C 292 ? 0.3841 0.2178 0.3749 0.0375  0.0019  0.0998  292 HIS C CB  
6185  C CG  . HIS C 292 ? 0.3950 0.2361 0.3677 0.0390  -0.0041 0.1014  292 HIS C CG  
6186  N ND1 . HIS C 292 ? 0.4075 0.2462 0.3690 0.0470  -0.0027 0.1118  292 HIS C ND1 
6187  C CD2 . HIS C 292 ? 0.4056 0.2497 0.3605 0.0299  -0.0123 0.0942  292 HIS C CD2 
6188  C CE1 . HIS C 292 ? 0.4219 0.2633 0.3621 0.0481  -0.0093 0.1099  292 HIS C CE1 
6189  N NE2 . HIS C 292 ? 0.4258 0.2654 0.3571 0.0355  -0.0159 0.0989  292 HIS C NE2 
6190  N N   . ASN C 293 ? 0.3801 0.2169 0.3577 0.0285  0.0161  0.1092  293 ASN C N   
6191  C CA  . ASN C 293 ? 0.3847 0.2481 0.3500 0.0329  0.0214  0.1191  293 ASN C CA  
6192  C C   . ASN C 293 ? 0.4010 0.2715 0.3602 0.0292  0.0213  0.1347  293 ASN C C   
6193  O O   . ASN C 293 ? 0.4066 0.3117 0.3615 0.0225  0.0266  0.1484  293 ASN C O   
6194  C CB  . ASN C 293 ? 0.3744 0.2653 0.3482 0.0224  0.0280  0.1223  293 ASN C CB  
6195  C CG  . ASN C 293 ? 0.3843 0.2658 0.3651 -0.0058 0.0277  0.1299  293 ASN C CG  
6196  O OD1 . ASN C 293 ? 0.4008 0.2391 0.3772 -0.0095 0.0238  0.1284  293 ASN C OD1 
6197  N ND2 . ASN C 293 ? 0.3855 0.3062 0.3676 -0.0254 0.0317  0.1395  293 ASN C ND2 
6198  N N   . ILE C 294 ? 0.4119 0.2582 0.3684 0.0341  0.0155  0.1346  294 ILE C N   
6199  C CA  . ILE C 294 ? 0.4366 0.2767 0.3810 0.0319  0.0154  0.1496  294 ILE C CA  
6200  C C   . ILE C 294 ? 0.4404 0.3071 0.3719 0.0452  0.0159  0.1563  294 ILE C C   
6201  O O   . ILE C 294 ? 0.4511 0.3444 0.3753 0.0384  0.0211  0.1715  294 ILE C O   
6202  C CB  . ILE C 294 ? 0.4545 0.2628 0.3942 0.0424  0.0100  0.1490  294 ILE C CB  
6203  C CG1 . ILE C 294 ? 0.4601 0.2401 0.4034 0.0402  0.0107  0.1420  294 ILE C CG1 
6204  C CG2 . ILE C 294 ? 0.4934 0.2806 0.4088 0.0416  0.0110  0.1656  294 ILE C CG2 
6205  C CD1 . ILE C 294 ? 0.4834 0.2354 0.4122 0.0160  0.0156  0.1473  294 ILE C CD1 
6206  N N   . HIS C 295 ? 0.4398 0.3006 0.3624 0.0612  0.0099  0.1462  295 HIS C N   
6207  C CA  . HIS C 295 ? 0.4572 0.3278 0.3548 0.0772  0.0091  0.1505  295 HIS C CA  
6208  C C   . HIS C 295 ? 0.4712 0.3181 0.3435 0.0848  0.0008  0.1346  295 HIS C C   
6209  O O   . HIS C 295 ? 0.4668 0.3044 0.3487 0.0741  -0.0076 0.1266  295 HIS C O   
6210  C CB  . HIS C 295 ? 0.4723 0.3418 0.3680 0.0781  0.0065  0.1633  295 HIS C CB  
6211  C CG  . HIS C 295 ? 0.4907 0.3777 0.3627 0.0927  0.0083  0.1727  295 HIS C CG  
6212  N ND1 . HIS C 295 ? 0.5091 0.3842 0.3525 0.1083  0.0018  0.1639  295 HIS C ND1 
6213  C CD2 . HIS C 295 ? 0.5010 0.4164 0.3675 0.0921  0.0155  0.1912  295 HIS C CD2 
6214  C CE1 . HIS C 295 ? 0.5283 0.4205 0.3498 0.1237  0.0059  0.1752  295 HIS C CE1 
6215  N NE2 . HIS C 295 ? 0.5194 0.4437 0.3587 0.1146  0.0147  0.1929  295 HIS C NE2 
6216  N N   . PRO C 296 ? 0.4996 0.3356 0.3298 0.1028  0.0030  0.1317  296 PRO C N   
6217  C CA  . PRO C 296 ? 0.5387 0.3270 0.3201 0.1031  -0.0056 0.1160  296 PRO C CA  
6218  C C   . PRO C 296 ? 0.5560 0.3345 0.3260 0.0886  -0.0198 0.1129  296 PRO C C   
6219  O O   . PRO C 296 ? 0.5703 0.3300 0.3270 0.0660  -0.0306 0.1020  296 PRO C O   
6220  C CB  . PRO C 296 ? 0.5855 0.3549 0.3073 0.1364  0.0017  0.1176  296 PRO C CB  
6221  C CG  . PRO C 296 ? 0.5628 0.3911 0.3118 0.1508  0.0116  0.1370  296 PRO C CG  
6222  C CD  . PRO C 296 ? 0.5097 0.3757 0.3241 0.1250  0.0142  0.1443  296 PRO C CD  
6223  N N   . LEU C 297 ? 0.5579 0.3567 0.3308 0.0990  -0.0201 0.1241  297 LEU C N   
6224  C CA  . LEU C 297 ? 0.5757 0.3774 0.3374 0.0888  -0.0334 0.1237  297 LEU C CA  
6225  C C   . LEU C 297 ? 0.5384 0.3809 0.3525 0.0767  -0.0378 0.1290  297 LEU C C   
6226  O O   . LEU C 297 ? 0.5201 0.3835 0.3625 0.0886  -0.0318 0.1423  297 LEU C O   
6227  C CB  . LEU C 297 ? 0.5958 0.4039 0.3369 0.1096  -0.0310 0.1348  297 LEU C CB  
6228  C CG  . LEU C 297 ? 0.6430 0.4172 0.3230 0.1349  -0.0247 0.1325  297 LEU C CG  
6229  C CD1 . LEU C 297 ? 0.6508 0.4507 0.3243 0.1578  -0.0190 0.1478  297 LEU C CD1 
6230  C CD2 . LEU C 297 ? 0.7127 0.4193 0.3155 0.1258  -0.0371 0.1153  297 LEU C CD2 
6231  N N   . THR C 298 ? 0.5382 0.3900 0.3556 0.0545  -0.0481 0.1202  298 THR C N   
6232  C CA  . THR C 298 ? 0.5112 0.4140 0.3706 0.0521  -0.0520 0.1266  298 THR C CA  
6233  C C   . THR C 298 ? 0.5330 0.4745 0.3770 0.0323  -0.0689 0.1260  298 THR C C   
6234  O O   . THR C 298 ? 0.5741 0.4868 0.3689 0.0089  -0.0794 0.1172  298 THR C O   
6235  C CB  . THR C 298 ? 0.4834 0.3930 0.3727 0.0444  -0.0473 0.1212  298 THR C CB  
6236  O OG1 . THR C 298 ? 0.4993 0.4084 0.3683 0.0136  -0.0576 0.1099  298 THR C OG1 
6237  C CG2 . THR C 298 ? 0.4693 0.3421 0.3647 0.0536  -0.0333 0.1197  298 THR C CG2 
6238  N N   . ILE C 299 ? 0.5155 0.5216 0.3932 0.0425  -0.0716 0.1366  299 ILE C N   
6239  C CA  . ILE C 299 ? 0.5309 0.6066 0.4039 0.0235  -0.0880 0.1407  299 ILE C CA  
6240  C C   . ILE C 299 ? 0.5052 0.6546 0.4184 0.0282  -0.0874 0.1469  299 ILE C C   
6241  O O   . ILE C 299 ? 0.4852 0.6325 0.4249 0.0650  -0.0742 0.1535  299 ILE C O   
6242  C CB  . ILE C 299 ? 0.5449 0.6485 0.4109 0.0457  -0.0919 0.1531  299 ILE C CB  
6243  C CG1 . ILE C 299 ? 0.5573 0.7583 0.4242 0.0279  -0.1093 0.1610  299 ILE C CG1 
6244  C CG2 . ILE C 299 ? 0.5294 0.6268 0.4199 0.0934  -0.0768 0.1663  299 ILE C CG2 
6245  C CD1 . ILE C 299 ? 0.6013 0.7926 0.4186 -0.0283 -0.1284 0.1504  299 ILE C CD1 
6246  N N   . GLY C 300 ? 0.5164 0.7270 0.4249 -0.0113 -0.1019 0.1455  300 GLY C N   
6247  C CA  . GLY C 300 ? 0.4952 0.8014 0.4407 -0.0076 -0.1024 0.1545  300 GLY C CA  
6248  C C   . GLY C 300 ? 0.4871 0.7728 0.4366 -0.0374 -0.1003 0.1438  300 GLY C C   
6249  O O   . GLY C 300 ? 0.5087 0.7108 0.4224 -0.0703 -0.1025 0.1291  300 GLY C O   
6250  N N   . GLU C 301 ? 0.4636 0.8251 0.4504 -0.0198 -0.0952 0.1523  301 GLU C N   
6251  C CA  . GLU C 301 ? 0.4526 0.8095 0.4489 -0.0434 -0.0921 0.1447  301 GLU C CA  
6252  C C   . GLU C 301 ? 0.4339 0.6924 0.4379 -0.0111 -0.0741 0.1346  301 GLU C C   
6253  O O   . GLU C 301 ? 0.4185 0.6870 0.4458 0.0350  -0.0618 0.1409  301 GLU C O   
6254  C CB  . GLU C 301 ? 0.4366 0.9277 0.4686 -0.0308 -0.0927 0.1604  301 GLU C CB  
6255  C CG  . GLU C 301 ? 0.4256 0.9304 0.4691 -0.0572 -0.0902 0.1553  301 GLU C CG  
6256  C CD  . GLU C 301 ? 0.4570 0.9772 0.4688 -0.1398 -0.1082 0.1510  301 GLU C CD  
6257  O OE1 . GLU C 301 ? 0.4939 1.0042 0.4678 -0.1788 -0.1236 0.1503  301 GLU C OE1 
6258  O OE2 . GLU C 301 ? 0.4545 0.9888 0.4703 -0.1678 -0.1074 0.1486  301 GLU C OE2 
6259  N N   . CYS C 302 ? 0.4462 0.6091 0.4213 -0.0351 -0.0731 0.1199  302 CYS C N   
6260  C CA  . CYS C 302 ? 0.4315 0.5127 0.4111 -0.0098 -0.0578 0.1124  302 CYS C CA  
6261  C C   . CYS C 302 ? 0.4295 0.4648 0.3991 -0.0339 -0.0546 0.0996  302 CYS C C   
6262  O O   . CYS C 302 ? 0.4573 0.4835 0.3945 -0.0748 -0.0649 0.0933  302 CYS C O   
6263  C CB  . CYS C 302 ? 0.4484 0.4663 0.4021 0.0000  -0.0557 0.1107  302 CYS C CB  
6264  S SG  . CYS C 302 ? 0.4544 0.5063 0.4161 0.0350  -0.0559 0.1264  302 CYS C SG  
6265  N N   . PRO C 303 ? 0.4063 0.4057 0.3945 -0.0110 -0.0410 0.0961  303 PRO C N   
6266  C CA  . PRO C 303 ? 0.4077 0.3555 0.3817 -0.0269 -0.0365 0.0843  303 PRO C CA  
6267  C C   . PRO C 303 ? 0.4363 0.3170 0.3661 -0.0305 -0.0365 0.0780  303 PRO C C   
6268  O O   . PRO C 303 ? 0.4470 0.3223 0.3661 -0.0184 -0.0380 0.0832  303 PRO C O   
6269  C CB  . PRO C 303 ? 0.3804 0.3154 0.3838 0.0000  -0.0231 0.0847  303 PRO C CB  
6270  C CG  . PRO C 303 ? 0.3813 0.3233 0.3940 0.0288  -0.0198 0.0955  303 PRO C CG  
6271  C CD  . PRO C 303 ? 0.3916 0.3905 0.4034 0.0280  -0.0302 0.1036  303 PRO C CD  
6272  N N   . LYS C 304 ? 0.4552 0.2854 0.3536 -0.0413 -0.0339 0.0682  304 LYS C N   
6273  C CA  . LYS C 304 ? 0.4979 0.2624 0.3393 -0.0338 -0.0323 0.0632  304 LYS C CA  
6274  C C   . LYS C 304 ? 0.4697 0.2320 0.3311 0.0002  -0.0188 0.0680  304 LYS C C   
6275  O O   . LYS C 304 ? 0.4316 0.2138 0.3328 0.0080  -0.0103 0.0696  304 LYS C O   
6276  C CB  . LYS C 304 ? 0.5491 0.2510 0.3323 -0.0507 -0.0336 0.0526  304 LYS C CB  
6277  C CG  . LYS C 304 ? 0.5865 0.2908 0.3423 -0.0987 -0.0481 0.0497  304 LYS C CG  
6278  C CD  . LYS C 304 ? 0.6422 0.3324 0.3475 -0.1234 -0.0632 0.0509  304 LYS C CD  
6279  C CE  . LYS C 304 ? 0.6245 0.4044 0.3652 -0.1614 -0.0766 0.0591  304 LYS C CE  
6280  N NZ  . LYS C 304 ? 0.6987 0.4575 0.3708 -0.2047 -0.0953 0.0589  304 LYS C NZ  
6281  N N   . TYR C 305 ? 0.4935 0.2355 0.3225 0.0174  -0.0175 0.0714  305 TYR C N   
6282  C CA  . TYR C 305 ? 0.4727 0.2297 0.3166 0.0443  -0.0055 0.0798  305 TYR C CA  
6283  C C   . TYR C 305 ? 0.4925 0.2242 0.3038 0.0620  0.0037  0.0757  305 TYR C C   
6284  O O   . TYR C 305 ? 0.5508 0.2256 0.2946 0.0686  0.0015  0.0677  305 TYR C O   
6285  C CB  . TYR C 305 ? 0.4923 0.2510 0.3147 0.0595  -0.0064 0.0879  305 TYR C CB  
6286  C CG  . TYR C 305 ? 0.4765 0.2658 0.3116 0.0820  0.0057  0.1001  305 TYR C CG  
6287  C CD1 . TYR C 305 ? 0.4381 0.2670 0.3227 0.0736  0.0098  0.1113  305 TYR C CD1 
6288  C CD2 . TYR C 305 ? 0.5116 0.2907 0.2996 0.1111  0.0131  0.1022  305 TYR C CD2 
6289  C CE1 . TYR C 305 ? 0.4311 0.2972 0.3233 0.0814  0.0192  0.1253  305 TYR C CE1 
6290  C CE2 . TYR C 305 ? 0.4964 0.3295 0.2994 0.1292  0.0243  0.1174  305 TYR C CE2 
6291  C CZ  . TYR C 305 ? 0.4536 0.3345 0.3116 0.1081  0.0264  0.1294  305 TYR C CZ  
6292  O OH  . TYR C 305 ? 0.4449 0.3878 0.3141 0.1134  0.0356  0.1472  305 TYR C OH  
6293  N N   . VAL C 306 ? 0.4543 0.2245 0.3040 0.0698  0.0135  0.0820  306 VAL C N   
6294  C CA  . VAL C 306 ? 0.4684 0.2422 0.2934 0.0948  0.0240  0.0835  306 VAL C CA  
6295  C C   . VAL C 306 ? 0.4383 0.2803 0.2974 0.1029  0.0325  0.1000  306 VAL C C   
6296  O O   . VAL C 306 ? 0.4083 0.2758 0.3092 0.0811  0.0301  0.1072  306 VAL C O   
6297  C CB  . VAL C 306 ? 0.4586 0.2202 0.2910 0.0865  0.0262  0.0744  306 VAL C CB  
6298  C CG1 . VAL C 306 ? 0.5052 0.1971 0.2873 0.0743  0.0181  0.0608  306 VAL C CG1 
6299  C CG2 . VAL C 306 ? 0.4042 0.2016 0.3026 0.0606  0.0251  0.0757  306 VAL C CG2 
6300  N N   . LYS C 307 ? 0.4574 0.3287 0.2893 0.1343  0.0425  0.1076  307 LYS C N   
6301  C CA  . LYS C 307 ? 0.4347 0.3920 0.2948 0.1368  0.0503  0.1271  307 LYS C CA  
6302  C C   . LYS C 307 ? 0.3983 0.4033 0.3011 0.1123  0.0530  0.1310  307 LYS C C   
6303  O O   . LYS C 307 ? 0.3856 0.4681 0.3091 0.1013  0.0574  0.1486  307 LYS C O   
6304  C CB  . LYS C 307 ? 0.4740 0.4660 0.2851 0.1875  0.0609  0.1375  307 LYS C CB  
6305  C CG  . LYS C 307 ? 0.5157 0.4768 0.2818 0.2121  0.0597  0.1394  307 LYS C CG  
6306  C CD  . LYS C 307 ? 0.5536 0.5724 0.2754 0.2679  0.0730  0.1551  307 LYS C CD  
6307  C CE  . LYS C 307 ? 0.6206 0.5783 0.2690 0.3057  0.0726  0.1518  307 LYS C CE  
6308  N NZ  . LYS C 307 ? 0.6696 0.6821 0.2627 0.3738  0.0879  0.1678  307 LYS C NZ  
6309  N N   . SER C 308 ? 0.3876 0.3504 0.2993 0.0996  0.0496  0.1159  308 SER C N   
6310  C CA  . SER C 308 ? 0.3609 0.3603 0.3037 0.0791  0.0517  0.1174  308 SER C CA  
6311  C C   . SER C 308 ? 0.3433 0.3613 0.3208 0.0359  0.0472  0.1261  308 SER C C   
6312  O O   . SER C 308 ? 0.3471 0.3252 0.3288 0.0226  0.0414  0.1248  308 SER C O   
6313  C CB  . SER C 308 ? 0.3571 0.3006 0.2990 0.0751  0.0488  0.0990  308 SER C CB  
6314  O OG  . SER C 308 ? 0.3943 0.2882 0.2861 0.1056  0.0502  0.0897  308 SER C OG  
6315  N N   . ASN C 309 ? 0.3350 0.4098 0.3274 0.0140  0.0496  0.1359  309 ASN C N   
6316  C CA  . ASN C 309 ? 0.3407 0.4056 0.3454 -0.0343 0.0439  0.1410  309 ASN C CA  
6317  C C   . ASN C 309 ? 0.3358 0.3417 0.3474 -0.0458 0.0403  0.1238  309 ASN C C   
6318  O O   . ASN C 309 ? 0.3575 0.3136 0.3628 -0.0737 0.0351  0.1223  309 ASN C O   
6319  C CB  . ASN C 309 ? 0.3464 0.5027 0.3543 -0.0637 0.0459  0.1610  309 ASN C CB  
6320  C CG  . ASN C 309 ? 0.3552 0.5836 0.3572 -0.0593 0.0496  0.1828  309 ASN C CG  
6321  O OD1 . ASN C 309 ? 0.3706 0.5614 0.3640 -0.0664 0.0467  0.1868  309 ASN C OD1 
6322  N ND2 . ASN C 309 ? 0.3481 0.6888 0.3529 -0.0437 0.0567  0.1988  309 ASN C ND2 
6323  N N   . ARG C 310 ? 0.3179 0.3230 0.3328 -0.0211 0.0436  0.1117  310 ARG C N   
6324  C CA  . ARG C 310 ? 0.3107 0.2780 0.3337 -0.0312 0.0416  0.0976  310 ARG C CA  
6325  C C   . ARG C 310 ? 0.2990 0.2389 0.3175 -0.0015 0.0439  0.0829  310 ARG C C   
6326  O O   . ARG C 310 ? 0.3018 0.2669 0.3042 0.0247  0.0495  0.0842  310 ARG C O   
6327  C CB  . ARG C 310 ? 0.3117 0.3305 0.3391 -0.0557 0.0426  0.1044  310 ARG C CB  
6328  C CG  . ARG C 310 ? 0.3215 0.2927 0.3489 -0.0792 0.0386  0.0931  310 ARG C CG  
6329  C CD  . ARG C 310 ? 0.3252 0.3531 0.3529 -0.1055 0.0383  0.0994  310 ARG C CD  
6330  N NE  . ARG C 310 ? 0.3196 0.3155 0.3507 -0.1022 0.0384  0.0840  310 ARG C NE  
6331  C CZ  . ARG C 310 ? 0.3465 0.2733 0.3629 -0.1221 0.0338  0.0744  310 ARG C CZ  
6332  N NH1 . ARG C 310 ? 0.3916 0.2608 0.3800 -0.1460 0.0285  0.0782  310 ARG C NH1 
6333  N NH2 . ARG C 310 ? 0.3382 0.2473 0.3589 -0.1139 0.0351  0.0615  310 ARG C NH2 
6334  N N   . LEU C 311 ? 0.2955 0.1835 0.3195 -0.0049 0.0399  0.0707  311 LEU C N   
6335  C CA  . LEU C 311 ? 0.2915 0.1534 0.3088 0.0082  0.0405  0.0581  311 LEU C CA  
6336  C C   . LEU C 311 ? 0.2820 0.1231 0.3163 -0.0046 0.0386  0.0492  311 LEU C C   
6337  O O   . LEU C 311 ? 0.2854 0.1069 0.3264 -0.0076 0.0347  0.0477  311 LEU C O   
6338  C CB  . LEU C 311 ? 0.3058 0.1380 0.3042 0.0180  0.0366  0.0548  311 LEU C CB  
6339  C CG  . LEU C 311 ? 0.3300 0.1631 0.2941 0.0390  0.0388  0.0604  311 LEU C CG  
6340  C CD1 . LEU C 311 ? 0.3539 0.1467 0.2933 0.0375  0.0317  0.0556  311 LEU C CD1 
6341  C CD2 . LEU C 311 ? 0.3514 0.1844 0.2815 0.0634  0.0461  0.0591  311 LEU C CD2 
6342  N N   . VAL C 312 ? 0.2737 0.1246 0.3113 -0.0071 0.0421  0.0447  312 VAL C N   
6343  C CA  . VAL C 312 ? 0.2694 0.1023 0.3177 -0.0155 0.0415  0.0366  312 VAL C CA  
6344  C C   . VAL C 312 ? 0.2615 0.0925 0.3062 -0.0074 0.0448  0.0282  312 VAL C C   
6345  O O   . VAL C 312 ? 0.2617 0.1107 0.2962 0.0003  0.0490  0.0292  312 VAL C O   
6346  C CB  . VAL C 312 ? 0.2804 0.1184 0.3277 -0.0348 0.0412  0.0395  312 VAL C CB  
6347  C CG1 . VAL C 312 ? 0.2910 0.0963 0.3367 -0.0375 0.0408  0.0302  312 VAL C CG1 
6348  C CG2 . VAL C 312 ? 0.3033 0.1334 0.3397 -0.0499 0.0376  0.0501  312 VAL C CG2 
6349  N N   . LEU C 313 ? 0.2589 0.0740 0.3084 -0.0081 0.0432  0.0219  313 LEU C N   
6350  C CA  . LEU C 313 ? 0.2592 0.0676 0.3007 -0.0074 0.0457  0.0151  313 LEU C CA  
6351  C C   . LEU C 313 ? 0.2494 0.0632 0.3058 -0.0099 0.0485  0.0099  313 LEU C C   
6352  O O   . LEU C 313 ? 0.2508 0.0622 0.3184 -0.0100 0.0472  0.0094  313 LEU C O   
6353  C CB  . LEU C 313 ? 0.2683 0.0696 0.3033 -0.0156 0.0414  0.0142  313 LEU C CB  
6354  C CG  . LEU C 313 ? 0.2964 0.0733 0.2957 -0.0185 0.0377  0.0163  313 LEU C CG  
6355  C CD1 . LEU C 313 ? 0.3081 0.0920 0.3036 -0.0389 0.0301  0.0178  313 LEU C CD1 
6356  C CD2 . LEU C 313 ? 0.3292 0.0692 0.2828 -0.0104 0.0421  0.0130  313 LEU C CD2 
6357  N N   . ALA C 314 ? 0.2484 0.0648 0.2966 -0.0071 0.0528  0.0063  314 ALA C N   
6358  C CA  . ALA C 314 ? 0.2425 0.0614 0.3002 -0.0093 0.0553  0.0001  314 ALA C CA  
6359  C C   . ALA C 314 ? 0.2427 0.0595 0.3046 -0.0111 0.0553  -0.0025 314 ALA C C   
6360  O O   . ALA C 314 ? 0.2534 0.0620 0.2985 -0.0169 0.0546  -0.0015 314 ALA C O   
6361  C CB  . ALA C 314 ? 0.2432 0.0716 0.2891 -0.0035 0.0600  -0.0016 314 ALA C CB  
6362  N N   . THR C 315 ? 0.2418 0.0650 0.3167 -0.0068 0.0558  -0.0044 315 THR C N   
6363  C CA  . THR C 315 ? 0.2406 0.0857 0.3232 -0.0053 0.0574  -0.0043 315 THR C CA  
6364  C C   . THR C 315 ? 0.2410 0.0851 0.3234 -0.0001 0.0627  -0.0107 315 THR C C   
6365  O O   . THR C 315 ? 0.2388 0.0981 0.3208 -0.0059 0.0653  -0.0110 315 THR C O   
6366  C CB  . THR C 315 ? 0.2468 0.1128 0.3387 0.0085  0.0559  0.0010  315 THR C CB  
6367  O OG1 . THR C 315 ? 0.2672 0.0989 0.3468 0.0228  0.0563  -0.0008 315 THR C OG1 
6368  C CG2 . THR C 315 ? 0.2444 0.1268 0.3387 -0.0007 0.0501  0.0084  315 THR C CG2 
6369  N N   . GLY C 316 ? 0.2523 0.0743 0.3278 0.0063  0.0632  -0.0154 316 GLY C N   
6370  C CA  . GLY C 316 ? 0.2595 0.0751 0.3286 0.0097  0.0670  -0.0224 316 GLY C CA  
6371  C C   . GLY C 316 ? 0.2496 0.0680 0.3153 -0.0007 0.0678  -0.0248 316 GLY C C   
6372  O O   . GLY C 316 ? 0.2410 0.0655 0.3046 -0.0043 0.0675  -0.0207 316 GLY C O   
6373  N N   . LEU C 317 ? 0.2601 0.0726 0.3173 -0.0018 0.0689  -0.0309 317 LEU C N   
6374  C CA  . LEU C 317 ? 0.2531 0.0827 0.3066 -0.0057 0.0707  -0.0319 317 LEU C CA  
6375  C C   . LEU C 317 ? 0.2669 0.1032 0.3108 -0.0215 0.0654  -0.0314 317 LEU C C   
6376  O O   . LEU C 317 ? 0.2916 0.1015 0.3229 -0.0338 0.0602  -0.0318 317 LEU C O   
6377  C CB  . LEU C 317 ? 0.2531 0.0855 0.3047 0.0016  0.0760  -0.0375 317 LEU C CB  
6378  C CG  . LEU C 317 ? 0.2726 0.0882 0.3172 0.0072  0.0767  -0.0445 317 LEU C CG  
6379  C CD1 . LEU C 317 ? 0.2955 0.0987 0.3202 -0.0047 0.0725  -0.0504 317 LEU C CD1 
6380  C CD2 . LEU C 317 ? 0.2666 0.0971 0.3167 0.0185  0.0836  -0.0456 317 LEU C CD2 
6381  N N   . ARG C 318 ? 0.2603 0.1336 0.3029 -0.0223 0.0666  -0.0287 318 ARG C N   
6382  C CA  . ARG C 318 ? 0.2733 0.1795 0.3085 -0.0445 0.0605  -0.0242 318 ARG C CA  
6383  C C   . ARG C 318 ? 0.3114 0.1817 0.3247 -0.0674 0.0546  -0.0325 318 ARG C C   
6384  O O   . ARG C 318 ? 0.3174 0.1748 0.3245 -0.0598 0.0573  -0.0409 318 ARG C O   
6385  C CB  . ARG C 318 ? 0.2605 0.2284 0.2966 -0.0324 0.0643  -0.0184 318 ARG C CB  
6386  C CG  . ARG C 318 ? 0.2696 0.3037 0.3019 -0.0586 0.0575  -0.0094 318 ARG C CG  
6387  C CD  . ARG C 318 ? 0.2587 0.3682 0.2907 -0.0345 0.0629  -0.0015 318 ARG C CD  
6388  N NE  . ARG C 318 ? 0.2507 0.3852 0.2793 0.0029  0.0706  0.0090  318 ARG C NE  
6389  C CZ  . ARG C 318 ? 0.2496 0.4619 0.2792 0.0066  0.0700  0.0248  318 ARG C CZ  
6390  N NH1 . ARG C 318 ? 0.2525 0.5364 0.2909 -0.0346 0.0609  0.0338  318 ARG C NH1 
6391  N NH2 . ARG C 318 ? 0.2554 0.4730 0.2689 0.0504  0.0785  0.0328  318 ARG C NH2 
6392  N N   . ASN C 319 ? 0.3496 0.1941 0.3408 -0.0958 0.0465  -0.0299 319 ASN C N   
6393  C CA  . ASN C 319 ? 0.4146 0.1951 0.3596 -0.1191 0.0397  -0.0379 319 ASN C CA  
6394  C C   . ASN C 319 ? 0.4425 0.2602 0.3669 -0.1601 0.0311  -0.0355 319 ASN C C   
6395  O O   . ASN C 319 ? 0.4218 0.3185 0.3635 -0.1798 0.0278  -0.0229 319 ASN C O   
6396  C CB  . ASN C 319 ? 0.4630 0.1771 0.3743 -0.1317 0.0347  -0.0355 319 ASN C CB  
6397  C CG  . ASN C 319 ? 0.5511 0.1637 0.3925 -0.1398 0.0303  -0.0454 319 ASN C CG  
6398  O OD1 . ASN C 319 ? 0.5704 0.1634 0.3931 -0.1331 0.0314  -0.0553 319 ASN C OD1 
6399  N ND2 . ASN C 319 ? 0.6160 0.1541 0.4081 -0.1509 0.0256  -0.0427 319 ASN C ND2 
6400  N N   . SER C 320 ? 0.4967 0.2629 0.3798 -0.1721 0.0272  -0.0466 320 SER C N   
6401  C CA  . SER C 320 ? 0.5220 0.3303 0.3858 -0.2104 0.0187  -0.0459 320 SER C CA  
6402  C C   . SER C 320 ? 0.6094 0.3800 0.4094 -0.2768 0.0028  -0.0416 320 SER C C   
6403  O O   . SER C 320 ? 0.6820 0.3427 0.4251 -0.2862 -0.0008 -0.0466 320 SER C O   
6404  C CB  . SER C 320 ? 0.5398 0.3091 0.3849 -0.1915 0.0219  -0.0606 320 SER C CB  
6405  O OG  . SER C 320 ? 0.4743 0.2691 0.3688 -0.1381 0.0359  -0.0630 320 SER C OG  
6406  N N   . PRO C 321 ? 0.6129 0.4764 0.4145 -0.3241 -0.0066 -0.0305 321 PRO C N   
6407  C CA  . PRO C 321 ? 0.7065 0.5426 0.4381 -0.4037 -0.0245 -0.0247 321 PRO C CA  
6408  C C   . PRO C 321 ? 0.7963 0.5479 0.4520 -0.4351 -0.0343 -0.0395 321 PRO C C   
6409  O O   . PRO C 321 ? 0.8546 0.4712 0.4588 -0.4082 -0.0308 -0.0560 321 PRO C O   
6410  C CB  . PRO C 321 ? 0.6578 0.6641 0.4343 -0.4347 -0.0292 -0.0033 321 PRO C CB  
6411  C CG  . PRO C 321 ? 0.5707 0.6650 0.4117 -0.3735 -0.0162 -0.0052 321 PRO C CG  
6412  C CD  . PRO C 321 ? 0.5335 0.5414 0.3980 -0.3043 -0.0010 -0.0194 321 PRO C CD  
6413  N N   . GLY D 1   ? 0.0530 0.3974 0.2161 0.0308  0.0205  -0.0932 1   GLY D N   
6414  C CA  . GLY D 1   ? 0.0558 0.3381 0.2064 0.0421  0.0148  -0.0673 1   GLY D CA  
6415  C C   . GLY D 1   ? 0.0728 0.3396 0.1968 0.0765  0.0026  -0.0605 1   GLY D C   
6416  O O   . GLY D 1   ? 0.0814 0.3738 0.1966 0.0962  -0.0017 -0.0704 1   GLY D O   
6417  N N   . LEU D 2   ? 0.0862 0.3047 0.1898 0.0825  -0.0013 -0.0439 2   LEU D N   
6418  C CA  . LEU D 2   ? 0.1236 0.3057 0.1824 0.1123  -0.0094 -0.0375 2   LEU D CA  
6419  C C   . LEU D 2   ? 0.1409 0.2977 0.1804 0.1216  -0.0099 -0.0315 2   LEU D C   
6420  O O   . LEU D 2   ? 0.1803 0.3205 0.1771 0.1540  -0.0152 -0.0338 2   LEU D O   
6421  C CB  . LEU D 2   ? 0.1423 0.2673 0.1777 0.1039  -0.0096 -0.0210 2   LEU D CB  
6422  C CG  . LEU D 2   ? 0.1462 0.2805 0.1770 0.1103  -0.0122 -0.0261 2   LEU D CG  
6423  C CD1 . LEU D 2   ? 0.1653 0.2423 0.1736 0.0953  -0.0112 -0.0100 2   LEU D CD1 
6424  C CD2 . LEU D 2   ? 0.1810 0.3305 0.1752 0.1529  -0.0195 -0.0388 2   LEU D CD2 
6425  N N   . PHE D 3   ? 0.1183 0.2698 0.1828 0.0971  -0.0038 -0.0237 3   PHE D N   
6426  C CA  . PHE D 3   ? 0.1345 0.2589 0.1811 0.1009  -0.0031 -0.0157 3   PHE D CA  
6427  C C   . PHE D 3   ? 0.1201 0.2859 0.1855 0.1076  -0.0024 -0.0283 3   PHE D C   
6428  O O   . PHE D 3   ? 0.1330 0.2813 0.1842 0.1135  -0.0020 -0.0234 3   PHE D O   
6429  C CB  . PHE D 3   ? 0.1270 0.2218 0.1807 0.0736  0.0024  0.0013  3   PHE D CB  
6430  C CG  . PHE D 3   ? 0.1515 0.2065 0.1773 0.0651  0.0019  0.0113  3   PHE D CG  
6431  C CD1 . PHE D 3   ? 0.2047 0.2034 0.1740 0.0692  0.0022  0.0180  3   PHE D CD1 
6432  C CD2 . PHE D 3   ? 0.1313 0.1986 0.1781 0.0524  0.0023  0.0125  3   PHE D CD2 
6433  C CE1 . PHE D 3   ? 0.2381 0.1940 0.1728 0.0562  0.0039  0.0246  3   PHE D CE1 
6434  C CE2 . PHE D 3   ? 0.1561 0.1894 0.1756 0.0433  0.0018  0.0198  3   PHE D CE2 
6435  C CZ  . PHE D 3   ? 0.2103 0.1878 0.1734 0.0433  0.0028  0.0251  3   PHE D CZ  
6436  N N   . GLY D 4   ? 0.0980 0.3194 0.1922 0.1028  -0.0009 -0.0462 4   GLY D N   
6437  C CA  . GLY D 4   ? 0.0920 0.3648 0.1979 0.1088  -0.0006 -0.0648 4   GLY D CA  
6438  C C   . GLY D 4   ? 0.0776 0.3476 0.2039 0.0862  0.0078  -0.0636 4   GLY D C   
6439  O O   . GLY D 4   ? 0.0765 0.3864 0.2097 0.0875  0.0090  -0.0799 4   GLY D O   
6440  N N   . ALA D 5   ? 0.0715 0.2991 0.2041 0.0679  0.0139  -0.0459 5   ALA D N   
6441  C CA  . ALA D 5   ? 0.0666 0.2838 0.2092 0.0545  0.0222  -0.0423 5   ALA D CA  
6442  C C   . ALA D 5   ? 0.0655 0.2886 0.2198 0.0300  0.0344  -0.0523 5   ALA D C   
6443  O O   . ALA D 5   ? 0.0720 0.3143 0.2276 0.0190  0.0412  -0.0685 5   ALA D O   
6444  C CB  . ALA D 5   ? 0.0679 0.2462 0.2048 0.0533  0.0228  -0.0196 5   ALA D CB  
6445  N N   . ILE D 6   ? 0.0662 0.2675 0.2213 0.0198  0.0385  -0.0436 6   ILE D N   
6446  C CA  . ILE D 6   ? 0.0815 0.2690 0.2322 -0.0030 0.0530  -0.0507 6   ILE D CA  
6447  C C   . ILE D 6   ? 0.0862 0.3171 0.2402 -0.0200 0.0567  -0.0768 6   ILE D C   
6448  O O   . ILE D 6   ? 0.0742 0.3390 0.2363 -0.0119 0.0479  -0.0827 6   ILE D O   
6449  C CB  . ILE D 6   ? 0.0844 0.2398 0.2306 -0.0045 0.0556  -0.0346 6   ILE D CB  
6450  C CG1 . ILE D 6   ? 0.0849 0.2141 0.2269 0.0092  0.0547  -0.0132 6   ILE D CG1 
6451  C CG2 . ILE D 6   ? 0.1129 0.2450 0.2419 -0.0270 0.0721  -0.0435 6   ILE D CG2 
6452  C CD1 . ILE D 6   ? 0.0874 0.1993 0.2253 0.0127  0.0554  0.0020  6   ILE D CD1 
6453  N N   . ALA D 7   ? 0.1101 0.3419 0.2534 -0.0446 0.0710  -0.0940 7   ALA D N   
6454  C CA  . ALA D 7   ? 0.1191 0.4070 0.2644 -0.0698 0.0772  -0.1242 7   ALA D CA  
6455  C C   . ALA D 7   ? 0.0948 0.4599 0.2593 -0.0458 0.0605  -0.1375 7   ALA D C   
6456  O O   . ALA D 7   ? 0.0907 0.5217 0.2633 -0.0514 0.0586  -0.1586 7   ALA D O   
6457  C CB  . ALA D 7   ? 0.1285 0.4133 0.2689 -0.0898 0.0848  -0.1285 7   ALA D CB  
6458  N N   . GLY D 8   ? 0.0849 0.4425 0.2512 -0.0163 0.0493  -0.1254 8   GLY D N   
6459  C CA  . GLY D 8   ? 0.0755 0.4869 0.2452 0.0173  0.0335  -0.1329 8   GLY D CA  
6460  C C   . GLY D 8   ? 0.0804 0.5103 0.2481 0.0240  0.0325  -0.1411 8   GLY D C   
6461  O O   . GLY D 8   ? 0.0877 0.5658 0.2595 0.0005  0.0406  -0.1665 8   GLY D O   
6462  N N   . PHE D 9   ? 0.0812 0.4734 0.2394 0.0520  0.0241  -0.1212 9   PHE D N   
6463  C CA  . PHE D 9   ? 0.0871 0.4881 0.2419 0.0589  0.0238  -0.1258 9   PHE D CA  
6464  C C   . PHE D 9   ? 0.0941 0.4458 0.2493 0.0311  0.0378  -0.1181 9   PHE D C   
6465  O O   . PHE D 9   ? 0.1024 0.4646 0.2552 0.0248  0.0424  -0.1282 9   PHE D O   
6466  C CB  . PHE D 9   ? 0.0951 0.4739 0.2303 0.0991  0.0113  -0.1097 9   PHE D CB  
6467  C CG  . PHE D 9   ? 0.0969 0.4012 0.2232 0.0985  0.0128  -0.0804 9   PHE D CG  
6468  C CD1 . PHE D 9   ? 0.0966 0.3741 0.2244 0.0909  0.0184  -0.0709 9   PHE D CD1 
6469  C CD2 . PHE D 9   ? 0.1021 0.3707 0.2163 0.1051  0.0088  -0.0642 9   PHE D CD2 
6470  C CE1 . PHE D 9   ? 0.0984 0.3267 0.2195 0.0894  0.0199  -0.0472 9   PHE D CE1 
6471  C CE2 . PHE D 9   ? 0.1059 0.3213 0.2118 0.0989  0.0111  -0.0413 9   PHE D CE2 
6472  C CZ  . PHE D 9   ? 0.1024 0.3038 0.2136 0.0910  0.0165  -0.0334 9   PHE D CZ  
6473  N N   . ILE D 10  ? 0.0968 0.3954 0.2502 0.0189  0.0446  -0.1006 10  ILE D N   
6474  C CA  . ILE D 10  ? 0.1174 0.3683 0.2597 -0.0032 0.0604  -0.0962 10  ILE D CA  
6475  C C   . ILE D 10  ? 0.1389 0.3910 0.2726 -0.0364 0.0742  -0.1133 10  ILE D C   
6476  O O   . ILE D 10  ? 0.1385 0.3699 0.2712 -0.0403 0.0759  -0.1043 10  ILE D O   
6477  C CB  . ILE D 10  ? 0.1153 0.3125 0.2532 0.0092  0.0602  -0.0673 10  ILE D CB  
6478  C CG1 . ILE D 10  ? 0.1008 0.2997 0.2431 0.0340  0.0487  -0.0523 10  ILE D CG1 
6479  C CG2 . ILE D 10  ? 0.1475 0.2945 0.2628 -0.0019 0.0766  -0.0632 10  ILE D CG2 
6480  C CD1 . ILE D 10  ? 0.0960 0.2656 0.2373 0.0423  0.0470  -0.0278 10  ILE D CD1 
6481  N N   . GLU D 11  ? 0.1637 0.4391 0.2871 -0.0642 0.0857  -0.1393 11  GLU D N   
6482  C CA  . GLU D 11  ? 0.1895 0.4832 0.3017 -0.1040 0.1000  -0.1631 11  GLU D CA  
6483  C C   . GLU D 11  ? 0.2285 0.4404 0.3082 -0.1246 0.1179  -0.1521 11  GLU D C   
6484  O O   . GLU D 11  ? 0.2407 0.4621 0.3149 -0.1488 0.1256  -0.1629 11  GLU D O   
6485  C CB  . GLU D 11  ? 0.2186 0.5516 0.3184 -0.1382 0.1121  -0.1958 11  GLU D CB  
6486  C CG  . GLU D 11  ? 0.1867 0.6218 0.3156 -0.1191 0.0953  -0.2143 11  GLU D CG  
6487  C CD  . GLU D 11  ? 0.2123 0.7197 0.3342 -0.1632 0.1078  -0.2556 11  GLU D CD  
6488  O OE1 . GLU D 11  ? 0.2498 0.7237 0.3458 -0.1909 0.1229  -0.2657 11  GLU D OE1 
6489  O OE2 . GLU D 11  ? 0.1992 0.8004 0.3385 -0.1712 0.1034  -0.2793 11  GLU D OE2 
6490  N N   . GLY D 12  ? 0.2534 0.3874 0.3071 -0.1121 0.1251  -0.1314 12  GLY D N   
6491  C CA  . GLY D 12  ? 0.3059 0.3532 0.3144 -0.1223 0.1436  -0.1202 12  GLY D CA  
6492  C C   . GLY D 12  ? 0.3150 0.3016 0.3075 -0.0852 0.1420  -0.0903 12  GLY D C   
6493  O O   . GLY D 12  ? 0.2887 0.2927 0.2997 -0.0604 0.1309  -0.0809 12  GLY D O   
6494  N N   . GLY D 13  ? 0.3559 0.2763 0.3110 -0.0802 0.1536  -0.0765 13  GLY D N   
6495  C CA  . GLY D 13  ? 0.3709 0.2454 0.3062 -0.0400 0.1527  -0.0498 13  GLY D CA  
6496  C C   . GLY D 13  ? 0.4430 0.2437 0.3174 -0.0346 0.1713  -0.0501 13  GLY D C   
6497  O O   . GLY D 13  ? 0.4856 0.2623 0.3298 -0.0683 0.1866  -0.0718 13  GLY D O   
6498  N N   . TRP D 14  ? 0.4612 0.2297 0.3139 0.0084  0.1705  -0.0273 14  TRP D N   
6499  C CA  . TRP D 14  ? 0.5342 0.2306 0.3232 0.0271  0.1867  -0.0239 14  TRP D CA  
6500  C C   . TRP D 14  ? 0.6228 0.2256 0.3319 0.0540  0.2047  -0.0099 14  TRP D C   
6501  O O   . TRP D 14  ? 0.6073 0.2290 0.3241 0.0980  0.1948  0.0111  14  TRP D O   
6502  C CB  . TRP D 14  ? 0.4875 0.2352 0.3127 0.0649  0.1703  -0.0098 14  TRP D CB  
6503  C CG  . TRP D 14  ? 0.4221 0.2409 0.3056 0.0458  0.1561  -0.0221 14  TRP D CG  
6504  C CD1 . TRP D 14  ? 0.4211 0.2519 0.3112 0.0053  0.1605  -0.0465 14  TRP D CD1 
6505  C CD2 . TRP D 14  ? 0.3570 0.2452 0.2929 0.0679  0.1366  -0.0115 14  TRP D CD2 
6506  N NE1 . TRP D 14  ? 0.3597 0.2612 0.3021 0.0079  0.1435  -0.0503 14  TRP D NE1 
6507  C CE2 . TRP D 14  ? 0.3230 0.2525 0.2908 0.0441  0.1298  -0.0284 14  TRP D CE2 
6508  C CE3 . TRP D 14  ? 0.3293 0.2527 0.2844 0.1032  0.1255  0.0089  14  TRP D CE3 
6509  C CZ2 . TRP D 14  ? 0.2692 0.2573 0.2799 0.0568  0.1132  -0.0231 14  TRP D CZ2 
6510  C CZ3 . TRP D 14  ? 0.2745 0.2608 0.2748 0.1074  0.1104  0.0121  14  TRP D CZ3 
6511  C CH2 . TRP D 14  ? 0.2483 0.2580 0.2724 0.0854  0.1049  -0.0026 14  TRP D CH2 
6512  N N   . GLN D 15  ? 0.7244 0.2251 0.3493 0.0272  0.2327  -0.0230 15  GLN D N   
6513  C CA  . GLN D 15  ? 0.8396 0.2223 0.3607 0.0576  0.2552  -0.0103 15  GLN D CA  
6514  C C   . GLN D 15  ? 0.8686 0.2333 0.3587 0.1226  0.2526  0.0089  15  GLN D C   
6515  O O   . GLN D 15  ? 0.9213 0.2438 0.3597 0.1750  0.2568  0.0280  15  GLN D O   
6516  C CB  . GLN D 15  ? 0.9615 0.2231 0.3824 0.0100  0.2900  -0.0310 15  GLN D CB  
6517  C CG  . GLN D 15  ? 0.9526 0.2288 0.3886 -0.0568 0.2979  -0.0530 15  GLN D CG  
6518  C CD  . GLN D 15  ? 1.0224 0.2209 0.3951 -0.0531 0.3136  -0.0439 15  GLN D CD  
6519  O OE1 . GLN D 15  ? 0.9629 0.2225 0.3895 -0.0748 0.3035  -0.0473 15  GLN D OE1 
6520  N NE2 . GLN D 15  ? 1.1576 0.2153 0.4081 -0.0230 0.3395  -0.0325 15  GLN D NE2 
6521  N N   . GLY D 16  ? 0.8348 0.2388 0.3562 0.1219  0.2451  0.0030  16  GLY D N   
6522  C CA  . GLY D 16  ? 0.8596 0.2571 0.3550 0.1803  0.2429  0.0182  16  GLY D CA  
6523  C C   . GLY D 16  ? 0.7746 0.2815 0.3395 0.2295  0.2168  0.0384  16  GLY D C   
6524  O O   . GLY D 16  ? 0.8001 0.3115 0.3397 0.2823  0.2157  0.0508  16  GLY D O   
6525  N N   . MET D 17  ? 0.6793 0.2769 0.3275 0.2110  0.1969  0.0402  17  MET D N   
6526  C CA  . MET D 17  ? 0.6090 0.3080 0.3153 0.2476  0.1751  0.0567  17  MET D CA  
6527  C C   . MET D 17  ? 0.6348 0.3224 0.3154 0.2737  0.1764  0.0689  17  MET D C   
6528  O O   . MET D 17  ? 0.5981 0.3016 0.3111 0.2423  0.1713  0.0653  17  MET D O   
6529  C CB  . MET D 17  ? 0.4953 0.2980 0.3021 0.2113  0.1528  0.0510  17  MET D CB  
6530  C CG  . MET D 17  ? 0.4327 0.3375 0.2920 0.2383  0.1338  0.0643  17  MET D CG  
6531  S SD  . MET D 17  ? 0.3291 0.3238 0.2791 0.1960  0.1132  0.0574  17  MET D SD  
6532  C CE  . MET D 17  ? 0.3105 0.2871 0.2765 0.1586  0.1115  0.0499  17  MET D CE  
6533  N N   . VAL D 18  ? 0.7000 0.3651 0.3205 0.3359  0.1826  0.0830  18  VAL D N   
6534  C CA  . VAL D 18  ? 0.7493 0.3874 0.3233 0.3715  0.1874  0.0947  18  VAL D CA  
6535  C C   . VAL D 18  ? 0.6881 0.4516 0.3142 0.4115  0.1665  0.1071  18  VAL D C   
6536  O O   . VAL D 18  ? 0.6990 0.4716 0.3136 0.4299  0.1646  0.1144  18  VAL D O   
6537  C CB  . VAL D 18  ? 0.8975 0.4003 0.3384 0.4212  0.2139  0.1011  18  VAL D CB  
6538  C CG1 . VAL D 18  ? 0.9709 0.3468 0.3503 0.3735  0.2381  0.0856  18  VAL D CG1 
6539  C CG2 . VAL D 18  ? 0.9277 0.4643 0.3401 0.4917  0.2109  0.1117  18  VAL D CG2 
6540  N N   . ASP D 19  ? 0.6273 0.4905 0.3085 0.4210  0.1521  0.1077  19  ASP D N   
6541  C CA  . ASP D 19  ? 0.5798 0.5721 0.3031 0.4555  0.1352  0.1157  19  ASP D CA  
6542  C C   . ASP D 19  ? 0.4684 0.5653 0.2910 0.4025  0.1155  0.1105  19  ASP D C   
6543  O O   . ASP D 19  ? 0.4214 0.6356 0.2870 0.4131  0.1021  0.1127  19  ASP D O   
6544  C CB  . ASP D 19  ? 0.5935 0.6392 0.3065 0.5006  0.1338  0.1187  19  ASP D CB  
6545  C CG  . ASP D 19  ? 0.5516 0.5987 0.3038 0.4600  0.1320  0.1096  19  ASP D CG  
6546  O OD1 . ASP D 19  ? 0.5178 0.5230 0.3000 0.4013  0.1322  0.1004  19  ASP D OD1 
6547  O OD2 . ASP D 19  ? 0.5550 0.6503 0.3058 0.4902  0.1303  0.1110  19  ASP D OD2 
6548  N N   . GLY D 20  ? 0.4343 0.4892 0.2861 0.3454  0.1151  0.1023  20  GLY D N   
6549  C CA  . GLY D 20  ? 0.3478 0.4783 0.2757 0.2995  0.0989  0.0979  20  GLY D CA  
6550  C C   . GLY D 20  ? 0.3284 0.4021 0.2723 0.2493  0.1005  0.0887  20  GLY D C   
6551  O O   . GLY D 20  ? 0.3743 0.3601 0.2785 0.2403  0.1143  0.0826  20  GLY D O   
6552  N N   . TRP D 21  ? 0.2661 0.3929 0.2634 0.2158  0.0873  0.0860  21  TRP D N   
6553  C CA  . TRP D 21  ? 0.2434 0.3345 0.2593 0.1735  0.0864  0.0766  21  TRP D CA  
6554  C C   . TRP D 21  ? 0.2103 0.3064 0.2550 0.1446  0.0822  0.0666  21  TRP D C   
6555  O O   . TRP D 21  ? 0.2172 0.2693 0.2566 0.1219  0.0876  0.0554  21  TRP D O   
6556  C CB  . TRP D 21  ? 0.2035 0.3395 0.2526 0.1561  0.0749  0.0784  21  TRP D CB  
6557  C CG  . TRP D 21  ? 0.2349 0.3334 0.2561 0.1652  0.0810  0.0818  21  TRP D CG  
6558  C CD1 . TRP D 21  ? 0.2885 0.3032 0.2637 0.1660  0.0964  0.0785  21  TRP D CD1 
6559  C CD2 . TRP D 21  ? 0.2201 0.3609 0.2532 0.1698  0.0734  0.0877  21  TRP D CD2 
6560  N NE1 . TRP D 21  ? 0.3090 0.3076 0.2649 0.1742  0.0989  0.0836  21  TRP D NE1 
6561  C CE2 . TRP D 21  ? 0.2644 0.3425 0.2580 0.1788  0.0838  0.0895  21  TRP D CE2 
6562  C CE3 . TRP D 21  ? 0.1797 0.4043 0.2481 0.1634  0.0603  0.0901  21  TRP D CE3 
6563  C CZ2 . TRP D 21  ? 0.2637 0.3632 0.2566 0.1871  0.0797  0.0950  21  TRP D CZ2 
6564  C CZ3 . TRP D 21  ? 0.1791 0.4286 0.2474 0.1683  0.0564  0.0939  21  TRP D CZ3 
6565  C CH2 . TRP D 21  ? 0.2181 0.4067 0.2511 0.1828  0.0650  0.0970  21  TRP D CH2 
6566  N N   . TYR D 22  ? 0.1775 0.3326 0.2502 0.1447  0.0732  0.0692  22  TYR D N   
6567  C CA  . TYR D 22  ? 0.1524 0.3124 0.2461 0.1235  0.0691  0.0615  22  TYR D CA  
6568  C C   . TYR D 22  ? 0.1632 0.3446 0.2498 0.1441  0.0717  0.0649  22  TYR D C   
6569  O O   . TYR D 22  ? 0.1704 0.3956 0.2520 0.1689  0.0713  0.0733  22  TYR D O   
6570  C CB  . TYR D 22  ? 0.1109 0.3111 0.2369 0.0973  0.0570  0.0608  22  TYR D CB  
6571  C CG  . TYR D 22  ? 0.1008 0.3049 0.2331 0.0863  0.0527  0.0624  22  TYR D CG  
6572  C CD1 . TYR D 22  ? 0.1032 0.2673 0.2321 0.0751  0.0542  0.0555  22  TYR D CD1 
6573  C CD2 . TYR D 22  ? 0.0905 0.3454 0.2315 0.0851  0.0476  0.0691  22  TYR D CD2 
6574  C CE1 . TYR D 22  ? 0.0953 0.2627 0.2291 0.0664  0.0502  0.0571  22  TYR D CE1 
6575  C CE2 . TYR D 22  ? 0.0837 0.3413 0.2287 0.0745  0.0438  0.0701  22  TYR D CE2 
6576  C CZ  . TYR D 22  ? 0.0859 0.2960 0.2270 0.0669  0.0448  0.0650  22  TYR D CZ  
6577  O OH  . TYR D 22  ? 0.0802 0.2928 0.2243 0.0577  0.0410  0.0661  22  TYR D OH  
6578  N N   . GLY D 23  ? 0.1654 0.3242 0.2513 0.1360  0.0740  0.0573  23  GLY D N   
6579  C CA  . GLY D 23  ? 0.1748 0.3534 0.2550 0.1541  0.0763  0.0600  23  GLY D CA  
6580  C C   . GLY D 23  ? 0.1756 0.3281 0.2561 0.1417  0.0782  0.0500  23  GLY D C   
6581  O O   . GLY D 23  ? 0.1598 0.2969 0.2526 0.1174  0.0747  0.0402  23  GLY D O   
6582  N N   . TYR D 24  ? 0.1976 0.3506 0.2622 0.1623  0.0835  0.0517  24  TYR D N   
6583  C CA  . TYR D 24  ? 0.1988 0.3373 0.2639 0.1537  0.0847  0.0428  24  TYR D CA  
6584  C C   . TYR D 24  ? 0.2543 0.3312 0.2747 0.1685  0.0991  0.0370  24  TYR D C   
6585  O O   . TYR D 24  ? 0.2983 0.3494 0.2809 0.1980  0.1082  0.0443  24  TYR D O   
6586  C CB  . TYR D 24  ? 0.1788 0.3714 0.2610 0.1603  0.0794  0.0486  24  TYR D CB  
6587  C CG  . TYR D 24  ? 0.1470 0.3983 0.2556 0.1468  0.0706  0.0557  24  TYR D CG  
6588  C CD1 . TYR D 24  ? 0.1496 0.4460 0.2584 0.1620  0.0706  0.0641  24  TYR D CD1 
6589  C CD2 . TYR D 24  ? 0.1240 0.3842 0.2489 0.1194  0.0637  0.0528  24  TYR D CD2 
6590  C CE1 . TYR D 24  ? 0.1258 0.4801 0.2550 0.1416  0.0646  0.0672  24  TYR D CE1 
6591  C CE2 . TYR D 24  ? 0.1105 0.4102 0.2457 0.1003  0.0593  0.0578  24  TYR D CE2 
6592  C CZ  . TYR D 24  ? 0.1094 0.4592 0.2492 0.1073  0.0600  0.0639  24  TYR D CZ  
6593  O OH  . TYR D 24  ? 0.1013 0.4952 0.2481 0.0809  0.0575  0.0656  24  TYR D OH  
6594  N N   . HIS D 25  ? 0.2605 0.3121 0.2782 0.1491  0.1019  0.0228  25  HIS D N   
6595  C CA  . HIS D 25  ? 0.3180 0.3129 0.2901 0.1565  0.1165  0.0148  25  HIS D CA  
6596  C C   . HIS D 25  ? 0.3006 0.3203 0.2887 0.1533  0.1121  0.0086  25  HIS D C   
6597  O O   . HIS D 25  ? 0.2643 0.3117 0.2831 0.1303  0.1034  -0.0012 25  HIS D O   
6598  C CB  . HIS D 25  ? 0.3571 0.2927 0.2993 0.1278  0.1286  -0.0018 25  HIS D CB  
6599  C CG  . HIS D 25  ? 0.4315 0.2958 0.3135 0.1278  0.1474  -0.0122 25  HIS D CG  
6600  N ND1 . HIS D 25  ? 0.4324 0.2995 0.3167 0.1055  0.1494  -0.0297 25  HIS D ND1 
6601  C CD2 . HIS D 25  ? 0.5161 0.2984 0.3249 0.1488  0.1661  -0.0078 25  HIS D CD2 
6602  C CE1 . HIS D 25  ? 0.5132 0.3025 0.3302 0.1068  0.1692  -0.0369 25  HIS D CE1 
6603  N NE2 . HIS D 25  ? 0.5702 0.2999 0.3357 0.1344  0.1804  -0.0231 25  HIS D NE2 
6604  N N   . HIS D 26  ? 0.3322 0.3417 0.2944 0.1810  0.1184  0.0145  26  HIS D N   
6605  C CA  . HIS D 26  ? 0.3199 0.3520 0.2935 0.1819  0.1152  0.0102  26  HIS D CA  
6606  C C   . HIS D 26  ? 0.3816 0.3477 0.3056 0.1804  0.1304  -0.0030 26  HIS D C   
6607  O O   . HIS D 26  ? 0.4472 0.3447 0.3159 0.1899  0.1456  -0.0036 26  HIS D O   
6608  C CB  . HIS D 26  ? 0.3065 0.3896 0.2904 0.2125  0.1106  0.0257  26  HIS D CB  
6609  C CG  . HIS D 26  ? 0.3660 0.4177 0.2997 0.2535  0.1226  0.0331  26  HIS D CG  
6610  N ND1 . HIS D 26  ? 0.3867 0.4422 0.3023 0.2806  0.1249  0.0444  26  HIS D ND1 
6611  C CD2 . HIS D 26  ? 0.4169 0.4307 0.3075 0.2773  0.1331  0.0309  26  HIS D CD2 
6612  C CE1 . HIS D 26  ? 0.4509 0.4716 0.3107 0.3241  0.1363  0.0492  26  HIS D CE1 
6613  N NE2 . HIS D 26  ? 0.4719 0.4629 0.3142 0.3220  0.1419  0.0413  26  HIS D NE2 
6614  N N   . SER D 27  ? 0.3695 0.3505 0.3057 0.1676  0.1276  -0.0144 27  SER D N   
6615  C CA  . SER D 27  ? 0.4300 0.3542 0.3179 0.1643  0.1423  -0.0283 27  SER D CA  
6616  C C   . SER D 27  ? 0.4072 0.3697 0.3145 0.1719  0.1355  -0.0300 27  SER D C   
6617  O O   . SER D 27  ? 0.3559 0.3704 0.3062 0.1558  0.1227  -0.0360 27  SER D O   
6618  C CB  . SER D 27  ? 0.4554 0.3459 0.3262 0.1215  0.1511  -0.0522 27  SER D CB  
6619  O OG  . SER D 27  ? 0.4007 0.3551 0.3200 0.0983  0.1377  -0.0657 27  SER D OG  
6620  N N   . ASN D 28  ? 0.4521 0.3856 0.3215 0.2010  0.1446  -0.0243 28  ASN D N   
6621  C CA  . ASN D 28  ? 0.4376 0.4034 0.3195 0.2118  0.1400  -0.0247 28  ASN D CA  
6622  C C   . ASN D 28  ? 0.5182 0.4140 0.3338 0.2289  0.1573  -0.0308 28  ASN D C   
6623  O O   . ASN D 28  ? 0.5905 0.4044 0.3455 0.2245  0.1740  -0.0376 28  ASN D O   
6624  C CB  . ASN D 28  ? 0.3887 0.4260 0.3092 0.2367  0.1281  -0.0049 28  ASN D CB  
6625  C CG  . ASN D 28  ? 0.4204 0.4530 0.3128 0.2762  0.1344  0.0106  28  ASN D CG  
6626  O OD1 . ASN D 28  ? 0.4903 0.4525 0.3230 0.2956  0.1487  0.0091  28  ASN D OD1 
6627  N ND2 . ASN D 28  ? 0.3769 0.4853 0.3055 0.2887  0.1248  0.0245  28  ASN D ND2 
6628  N N   . GLU D 29  ? 0.5160 0.4351 0.3343 0.2470  0.1551  -0.0287 29  GLU D N   
6629  C CA  . GLU D 29  ? 0.5969 0.4471 0.3478 0.2657  0.1715  -0.0346 29  GLU D CA  
6630  C C   . GLU D 29  ? 0.6719 0.4595 0.3561 0.3090  0.1855  -0.0216 29  GLU D C   
6631  O O   . GLU D 29  ? 0.7680 0.4540 0.3699 0.3130  0.2054  -0.0301 29  GLU D O   
6632  C CB  . GLU D 29  ? 0.5746 0.4726 0.3451 0.2844  0.1650  -0.0313 29  GLU D CB  
6633  C CG  . GLU D 29  ? 0.5300 0.4676 0.3411 0.2501  0.1554  -0.0468 29  GLU D CG  
6634  C CD  . GLU D 29  ? 0.5359 0.4903 0.3421 0.2677  0.1552  -0.0474 29  GLU D CD  
6635  O OE1 . GLU D 29  ? 0.5570 0.5146 0.3439 0.3072  0.1590  -0.0331 29  GLU D OE1 
6636  O OE2 . GLU D 29  ? 0.5204 0.4919 0.3419 0.2444  0.1508  -0.0630 29  GLU D OE2 
6637  N N   . GLN D 30  ? 0.6364 0.4835 0.3487 0.3416  0.1762  -0.0022 30  GLN D N   
6638  C CA  . GLN D 30  ? 0.7040 0.5128 0.3555 0.3947  0.1866  0.0113  30  GLN D CA  
6639  C C   . GLN D 30  ? 0.7614 0.4850 0.3612 0.3874  0.1989  0.0097  30  GLN D C   
6640  O O   . GLN D 30  ? 0.8573 0.5003 0.3715 0.4291  0.2149  0.0157  30  GLN D O   
6641  C CB  . GLN D 30  ? 0.6439 0.5654 0.3475 0.4272  0.1720  0.0289  30  GLN D CB  
6642  C CG  . GLN D 30  ? 0.6079 0.6070 0.3444 0.4413  0.1646  0.0317  30  GLN D CG  
6643  C CD  . GLN D 30  ? 0.5106 0.6249 0.3331 0.4149  0.1470  0.0370  30  GLN D CD  
6644  O OE1 . GLN D 30  ? 0.4612 0.5881 0.3266 0.3703  0.1391  0.0295  30  GLN D OE1 
6645  N NE2 . GLN D 30  ? 0.4916 0.6899 0.3320 0.4428  0.1419  0.0488  30  GLN D NE2 
6646  N N   . GLY D 31  ? 0.7096 0.4482 0.3545 0.3380  0.1922  0.0018  31  GLY D N   
6647  C CA  . GLY D 31  ? 0.7619 0.4224 0.3605 0.3232  0.2046  -0.0015 31  GLY D CA  
6648  C C   . GLY D 31  ? 0.6784 0.3999 0.3489 0.2859  0.1901  -0.0024 31  GLY D C   
6649  O O   . GLY D 31  ? 0.5897 0.3965 0.3375 0.2625  0.1726  -0.0048 31  GLY D O   
6650  N N   . SER D 32  ? 0.7162 0.3856 0.3524 0.2829  0.1987  -0.0002 32  SER D N   
6651  C CA  . SER D 32  ? 0.6463 0.3674 0.3426 0.2534  0.1861  0.0002  32  SER D CA  
6652  C C   . SER D 32  ? 0.6738 0.3781 0.3427 0.2873  0.1888  0.0163  32  SER D C   
6653  O O   . SER D 32  ? 0.7644 0.3959 0.3525 0.3299  0.2041  0.0240  32  SER D O   
6654  C CB  . SER D 32  ? 0.6602 0.3389 0.3486 0.1950  0.1946  -0.0222 32  SER D CB  
6655  O OG  . SER D 32  ? 0.7753 0.3324 0.3652 0.1897  0.2209  -0.0305 32  SER D OG  
6656  N N   . GLY D 33  ? 0.6028 0.3716 0.3324 0.2720  0.1743  0.0215  33  GLY D N   
6657  C CA  . GLY D 33  ? 0.6233 0.3863 0.3323 0.3018  0.1753  0.0355  33  GLY D CA  
6658  C C   . GLY D 33  ? 0.5404 0.3781 0.3207 0.2785  0.1586  0.0392  33  GLY D C   
6659  O O   . GLY D 33  ? 0.4611 0.3690 0.3107 0.2487  0.1434  0.0349  33  GLY D O   
6660  N N   . TYR D 34  ? 0.5689 0.3836 0.3227 0.2953  0.1625  0.0476  34  TYR D N   
6661  C CA  . TYR D 34  ? 0.5022 0.3801 0.3131 0.2779  0.1482  0.0520  34  TYR D CA  
6662  C C   . TYR D 34  ? 0.4716 0.4386 0.3082 0.3172  0.1364  0.0672  34  TYR D C   
6663  O O   . TYR D 34  ? 0.5281 0.4839 0.3145 0.3695  0.1435  0.0764  34  TYR D O   
6664  C CB  . TYR D 34  ? 0.5524 0.3554 0.3188 0.2686  0.1601  0.0504  34  TYR D CB  
6665  C CG  . TYR D 34  ? 0.5871 0.3134 0.3263 0.2209  0.1740  0.0315  34  TYR D CG  
6666  C CD1 . TYR D 34  ? 0.5202 0.2900 0.3198 0.1713  0.1640  0.0183  34  TYR D CD1 
6667  C CD2 . TYR D 34  ? 0.6955 0.3070 0.3413 0.2251  0.1987  0.0250  34  TYR D CD2 
6668  C CE1 . TYR D 34  ? 0.5508 0.2720 0.3282 0.1263  0.1766  -0.0025 34  TYR D CE1 
6669  C CE2 . TYR D 34  ? 0.7323 0.2826 0.3506 0.1721  0.2137  0.0037  34  TYR D CE2 
6670  C CZ  . TYR D 34  ? 0.6549 0.2705 0.3441 0.1224  0.2019  -0.0109 34  TYR D CZ  
6671  O OH  . TYR D 34  ? 0.6897 0.2657 0.3547 0.0687  0.2165  -0.0354 34  TYR D OH  
6672  N N   . ALA D 35  ? 0.3905 0.4468 0.2988 0.2921  0.1196  0.0683  35  ALA D N   
6673  C CA  . ALA D 35  ? 0.3593 0.5129 0.2960 0.3146  0.1091  0.0784  35  ALA D CA  
6674  C C   . ALA D 35  ? 0.3091 0.5008 0.2900 0.2814  0.0985  0.0785  35  ALA D C   
6675  O O   . ALA D 35  ? 0.2623 0.4642 0.2836 0.2386  0.0910  0.0721  35  ALA D O   
6676  C CB  . ALA D 35  ? 0.3207 0.5515 0.2927 0.3124  0.1018  0.0781  35  ALA D CB  
6677  N N   . ALA D 36  ? 0.3269 0.5354 0.2931 0.3052  0.0983  0.0857  36  ALA D N   
6678  C CA  . ALA D 36  ? 0.2859 0.5273 0.2879 0.2762  0.0891  0.0858  36  ALA D CA  
6679  C C   . ALA D 36  ? 0.2301 0.5777 0.2837 0.2549  0.0769  0.0856  36  ALA D C   
6680  O O   . ALA D 36  ? 0.2320 0.6550 0.2874 0.2794  0.0756  0.0884  36  ALA D O   
6681  C CB  . ALA D 36  ? 0.3259 0.5546 0.2922 0.3106  0.0933  0.0931  36  ALA D CB  
6682  N N   . ASP D 37  ? 0.1902 0.5414 0.2782 0.2085  0.0695  0.0811  37  ASP D N   
6683  C CA  . ASP D 37  ? 0.1537 0.5856 0.2757 0.1789  0.0614  0.0798  37  ASP D CA  
6684  C C   . ASP D 37  ? 0.1527 0.6416 0.2789 0.1858  0.0577  0.0829  37  ASP D C   
6685  O O   . ASP D 37  ? 0.1494 0.6022 0.2753 0.1746  0.0558  0.0832  37  ASP D O   
6686  C CB  . ASP D 37  ? 0.1290 0.5240 0.2685 0.1331  0.0570  0.0743  37  ASP D CB  
6687  C CG  . ASP D 37  ? 0.1108 0.5642 0.2668 0.0975  0.0530  0.0723  37  ASP D CG  
6688  O OD1 . ASP D 37  ? 0.1039 0.5852 0.2661 0.0784  0.0497  0.0720  37  ASP D OD1 
6689  O OD2 . ASP D 37  ? 0.1096 0.5766 0.2666 0.0861  0.0547  0.0703  37  ASP D OD2 
6690  N N   . LYS D 38  ? 0.1558 0.7417 0.2856 0.2051  0.0567  0.0836  38  LYS D N   
6691  C CA  . LYS D 38  ? 0.1586 0.8176 0.2901 0.2195  0.0531  0.0846  38  LYS D CA  
6692  C C   . LYS D 38  ? 0.1289 0.8195 0.2865 0.1651  0.0473  0.0790  38  LYS D C   
6693  O O   . LYS D 38  ? 0.1295 0.8138 0.2853 0.1662  0.0445  0.0805  38  LYS D O   
6694  C CB  . LYS D 38  ? 0.1693 0.9459 0.2990 0.2546  0.0532  0.0833  38  LYS D CB  
6695  C CG  . LYS D 38  ? 0.2193 0.9679 0.3053 0.3274  0.0592  0.0907  38  LYS D CG  
6696  C CD  . LYS D 38  ? 0.2325 1.1157 0.3142 0.3722  0.0576  0.0886  38  LYS D CD  
6697  C CE  . LYS D 38  ? 0.2162 1.1632 0.3173 0.3582  0.0588  0.0826  38  LYS D CE  
6698  N NZ  . LYS D 38  ? 0.2214 1.3286 0.3266 0.3930  0.0565  0.0765  38  LYS D NZ  
6699  N N   . GLU D 39  ? 0.1120 0.8296 0.2859 0.1179  0.0472  0.0726  39  GLU D N   
6700  C CA  . GLU D 39  ? 0.1012 0.8381 0.2847 0.0618  0.0451  0.0661  39  GLU D CA  
6701  C C   . GLU D 39  ? 0.0970 0.7405 0.2754 0.0484  0.0421  0.0687  39  GLU D C   
6702  O O   . GLU D 39  ? 0.0948 0.7596 0.2755 0.0384  0.0389  0.0674  39  GLU D O   
6703  C CB  . GLU D 39  ? 0.1053 0.8473 0.2873 0.0138  0.0495  0.0598  39  GLU D CB  
6704  C CG  . GLU D 39  ? 0.1170 0.8262 0.2870 -0.0457 0.0509  0.0542  39  GLU D CG  
6705  C CD  . GLU D 39  ? 0.1361 0.9157 0.2965 -0.0983 0.0587  0.0437  39  GLU D CD  
6706  O OE1 . GLU D 39  ? 0.1425 0.9405 0.2999 -0.1022 0.0640  0.0422  39  GLU D OE1 
6707  O OE2 . GLU D 39  ? 0.1499 0.9678 0.3026 -0.1392 0.0608  0.0357  39  GLU D OE2 
6708  N N   . SER D 40  ? 0.0959 0.6454 0.2675 0.0491  0.0429  0.0709  40  SER D N   
6709  C CA  . SER D 40  ? 0.0930 0.5644 0.2601 0.0382  0.0401  0.0711  40  SER D CA  
6710  C C   . SER D 40  ? 0.0955 0.5533 0.2595 0.0700  0.0396  0.0755  40  SER D C   
6711  O O   . SER D 40  ? 0.0920 0.5252 0.2561 0.0572  0.0366  0.0750  40  SER D O   
6712  C CB  . SER D 40  ? 0.0946 0.4881 0.2554 0.0371  0.0411  0.0696  40  SER D CB  
6713  O OG  . SER D 40  ? 0.1008 0.4761 0.2582 0.0711  0.0450  0.0716  40  SER D OG  
6714  N N   . THR D 41  ? 0.1093 0.5769 0.2627 0.1127  0.0436  0.0800  41  THR D N   
6715  C CA  . THR D 41  ? 0.1303 0.5711 0.2643 0.1473  0.0464  0.0852  41  THR D CA  
6716  C C   . THR D 41  ? 0.1272 0.6412 0.2659 0.1531  0.0417  0.0866  41  THR D C   
6717  O O   . THR D 41  ? 0.1318 0.6168 0.2641 0.1542  0.0408  0.0885  41  THR D O   
6718  C CB  . THR D 41  ? 0.1673 0.5850 0.2700 0.1961  0.0546  0.0901  41  THR D CB  
6719  O OG1 . THR D 41  ? 0.1729 0.5200 0.2690 0.1866  0.0598  0.0867  41  THR D OG1 
6720  C CG2 . THR D 41  ? 0.2091 0.5815 0.2740 0.2326  0.0607  0.0961  41  THR D CG2 
6721  N N   . GLN D 42  ? 0.1200 0.7364 0.2699 0.1554  0.0392  0.0840  42  GLN D N   
6722  C CA  . GLN D 42  ? 0.1170 0.8254 0.2730 0.1596  0.0346  0.0818  42  GLN D CA  
6723  C C   . GLN D 42  ? 0.0965 0.8008 0.2683 0.1052  0.0302  0.0759  42  GLN D C   
6724  O O   . GLN D 42  ? 0.0978 0.8305 0.2690 0.1084  0.0267  0.0756  42  GLN D O   
6725  C CB  . GLN D 42  ? 0.1137 0.9502 0.2806 0.1658  0.0337  0.0757  42  GLN D CB  
6726  C CG  . GLN D 42  ? 0.1142 1.0694 0.2866 0.1763  0.0288  0.0704  42  GLN D CG  
6727  C CD  . GLN D 42  ? 0.1452 1.0798 0.2881 0.2423  0.0284  0.0799  42  GLN D CD  
6728  O OE1 . GLN D 42  ? 0.1448 1.0779 0.2864 0.2382  0.0249  0.0802  42  GLN D OE1 
6729  N NE2 . GLN D 42  ? 0.1811 1.0903 0.2917 0.3044  0.0335  0.0879  42  GLN D NE2 
6730  N N   . LYS D 43  ? 0.0854 0.7489 0.2639 0.0588  0.0310  0.0715  43  LYS D N   
6731  C CA  . LYS D 43  ? 0.0814 0.7170 0.2599 0.0095  0.0289  0.0663  43  LYS D CA  
6732  C C   . LYS D 43  ? 0.0795 0.6337 0.2522 0.0208  0.0267  0.0711  43  LYS D C   
6733  O O   . LYS D 43  ? 0.0797 0.6355 0.2511 0.0002  0.0236  0.0686  43  LYS D O   
6734  C CB  . LYS D 43  ? 0.0883 0.6775 0.2586 -0.0305 0.0322  0.0622  43  LYS D CB  
6735  C CG  . LYS D 43  ? 0.1061 0.7242 0.2634 -0.0878 0.0350  0.0530  43  LYS D CG  
6736  C CD  . LYS D 43  ? 0.1262 0.7190 0.2657 -0.1182 0.0417  0.0495  43  LYS D CD  
6737  C CE  . LYS D 43  ? 0.1653 0.7532 0.2714 -0.1818 0.0490  0.0399  43  LYS D CE  
6738  N NZ  . LYS D 43  ? 0.1999 0.7078 0.2703 -0.2045 0.0563  0.0399  43  LYS D NZ  
6739  N N   . ALA D 44  ? 0.0812 0.5666 0.2477 0.0499  0.0293  0.0763  44  ALA D N   
6740  C CA  . ALA D 44  ? 0.0838 0.4984 0.2426 0.0589  0.0297  0.0787  44  ALA D CA  
6741  C C   . ALA D 44  ? 0.0958 0.5352 0.2451 0.0895  0.0300  0.0838  44  ALA D C   
6742  O O   . ALA D 44  ? 0.0957 0.5115 0.2428 0.0823  0.0281  0.0840  44  ALA D O   
6743  C CB  . ALA D 44  ? 0.0922 0.4364 0.2417 0.0745  0.0353  0.0791  44  ALA D CB  
6744  N N   . ILE D 45  ? 0.1114 0.5971 0.2500 0.1284  0.0326  0.0881  45  ILE D N   
6745  C CA  . ILE D 45  ? 0.1344 0.6469 0.2534 0.1683  0.0333  0.0937  45  ILE D CA  
6746  C C   . ILE D 45  ? 0.1157 0.7054 0.2525 0.1461  0.0253  0.0890  45  ILE D C   
6747  O O   . ILE D 45  ? 0.1264 0.7044 0.2521 0.1590  0.0243  0.0921  45  ILE D O   
6748  C CB  . ILE D 45  ? 0.1640 0.7213 0.2603 0.2222  0.0371  0.0985  45  ILE D CB  
6749  C CG1 . ILE D 45  ? 0.2037 0.6572 0.2624 0.2508  0.0484  0.1042  45  ILE D CG1 
6750  C CG2 . ILE D 45  ? 0.1889 0.8077 0.2650 0.2661  0.0350  0.1024  45  ILE D CG2 
6751  C CD1 . ILE D 45  ? 0.2373 0.7179 0.2691 0.3000  0.0533  0.1081  45  ILE D CD1 
6752  N N   . ASP D 46  ? 0.0934 0.7580 0.2529 0.1088  0.0212  0.0804  46  ASP D N   
6753  C CA  . ASP D 46  ? 0.0828 0.8226 0.2542 0.0764  0.0159  0.0724  46  ASP D CA  
6754  C C   . ASP D 46  ? 0.0772 0.7433 0.2477 0.0397  0.0141  0.0710  46  ASP D C   
6755  O O   . ASP D 46  ? 0.0789 0.7676 0.2481 0.0375  0.0106  0.0697  46  ASP D O   
6756  C CB  . ASP D 46  ? 0.0741 0.8987 0.2590 0.0342  0.0162  0.0610  46  ASP D CB  
6757  C CG  . ASP D 46  ? 0.0777 1.0015 0.2663 0.0707  0.0171  0.0598  46  ASP D CG  
6758  O OD1 . ASP D 46  ? 0.0931 1.0172 0.2674 0.1342  0.0171  0.0686  46  ASP D OD1 
6759  O OD2 . ASP D 46  ? 0.0726 1.0702 0.2714 0.0367  0.0192  0.0496  46  ASP D OD2 
6760  N N   . GLY D 47  ? 0.0736 0.6555 0.2423 0.0152  0.0163  0.0708  47  GLY D N   
6761  C CA  . GLY D 47  ? 0.0742 0.5859 0.2368 -0.0124 0.0146  0.0691  47  GLY D CA  
6762  C C   . GLY D 47  ? 0.0768 0.5438 0.2345 0.0152  0.0141  0.0750  47  GLY D C   
6763  O O   . GLY D 47  ? 0.0781 0.5344 0.2328 -0.0005 0.0111  0.0730  47  GLY D O   
6764  N N   . VAL D 48  ? 0.0858 0.5206 0.2358 0.0541  0.0190  0.0817  48  VAL D N   
6765  C CA  . VAL D 48  ? 0.1012 0.4826 0.2357 0.0774  0.0226  0.0867  48  VAL D CA  
6766  C C   . VAL D 48  ? 0.1154 0.5486 0.2395 0.1040  0.0208  0.0910  48  VAL D C   
6767  O O   . VAL D 48  ? 0.1221 0.5287 0.2380 0.1049  0.0207  0.0926  48  VAL D O   
6768  C CB  . VAL D 48  ? 0.1236 0.4417 0.2383 0.1042  0.0324  0.0905  48  VAL D CB  
6769  C CG1 . VAL D 48  ? 0.1578 0.4213 0.2414 0.1282  0.0406  0.0956  48  VAL D CG1 
6770  C CG2 . VAL D 48  ? 0.1091 0.3771 0.2344 0.0773  0.0334  0.0839  48  VAL D CG2 
6771  N N   . THR D 49  ? 0.1218 0.6353 0.2450 0.1281  0.0193  0.0921  49  THR D N   
6772  C CA  . THR D 49  ? 0.1379 0.7193 0.2498 0.1600  0.0163  0.0945  49  THR D CA  
6773  C C   . THR D 49  ? 0.1182 0.7464 0.2489 0.1209  0.0085  0.0868  49  THR D C   
6774  O O   . THR D 49  ? 0.1294 0.7486 0.2485 0.1342  0.0073  0.0897  49  THR D O   
6775  C CB  . THR D 49  ? 0.1456 0.8286 0.2562 0.1928  0.0147  0.0935  49  THR D CB  
6776  O OG1 . THR D 49  ? 0.1745 0.8029 0.2583 0.2333  0.0230  0.1013  49  THR D OG1 
6777  C CG2 . THR D 49  ? 0.1649 0.9317 0.2610 0.2330  0.0105  0.0944  49  THR D CG2 
6778  N N   . ASN D 50  ? 0.0979 0.7671 0.2500 0.0710  0.0050  0.0766  50  ASN D N   
6779  C CA  . ASN D 50  ? 0.0918 0.7911 0.2507 0.0251  0.0004  0.0672  50  ASN D CA  
6780  C C   . ASN D 50  ? 0.0943 0.6994 0.2452 0.0143  0.0002  0.0705  50  ASN D C   
6781  O O   . ASN D 50  ? 0.0975 0.7203 0.2453 0.0069  -0.0032 0.0681  50  ASN D O   
6782  C CB  . ASN D 50  ? 0.0879 0.8059 0.2524 -0.0313 0.0017  0.0562  50  ASN D CB  
6783  C CG  . ASN D 50  ? 0.0865 0.9244 0.2607 -0.0341 0.0021  0.0482  50  ASN D CG  
6784  O OD1 . ASN D 50  ? 0.0877 1.0314 0.2670 -0.0212 -0.0015 0.0426  50  ASN D OD1 
6785  N ND2 . ASN D 50  ? 0.0855 0.9155 0.2617 -0.0502 0.0064  0.0463  50  ASN D ND2 
6786  N N   . LYS D 51  ? 0.0941 0.6073 0.2419 0.0136  0.0041  0.0744  51  LYS D N   
6787  C CA  . LYS D 51  ? 0.0968 0.5280 0.2379 0.0065  0.0047  0.0757  51  LYS D CA  
6788  C C   . LYS D 51  ? 0.1104 0.5282 0.2405 0.0393  0.0064  0.0825  51  LYS D C   
6789  O O   . LYS D 51  ? 0.1119 0.5099 0.2386 0.0278  0.0041  0.0810  51  LYS D O   
6790  C CB  . LYS D 51  ? 0.0941 0.4534 0.2346 0.0082  0.0092  0.0767  51  LYS D CB  
6791  C CG  . LYS D 51  ? 0.0955 0.3839 0.2303 0.0061  0.0110  0.0757  51  LYS D CG  
6792  C CD  . LYS D 51  ? 0.0927 0.3353 0.2291 0.0061  0.0149  0.0730  51  LYS D CD  
6793  C CE  . LYS D 51  ? 0.0909 0.2907 0.2244 -0.0115 0.0123  0.0659  51  LYS D CE  
6794  N NZ  . LYS D 51  ? 0.0905 0.2740 0.2228 -0.0200 0.0115  0.0614  51  LYS D NZ  
6795  N N   . VAL D 52  ? 0.1302 0.5511 0.2466 0.0818  0.0117  0.0900  52  VAL D N   
6796  C CA  . VAL D 52  ? 0.1603 0.5532 0.2504 0.1172  0.0166  0.0977  52  VAL D CA  
6797  C C   . VAL D 52  ? 0.1626 0.6322 0.2538 0.1240  0.0092  0.0966  52  VAL D C   
6798  O O   . VAL D 52  ? 0.1733 0.6170 0.2532 0.1272  0.0094  0.0988  52  VAL D O   
6799  C CB  . VAL D 52  ? 0.1992 0.5646 0.2561 0.1651  0.0266  0.1063  52  VAL D CB  
6800  C CG1 . VAL D 52  ? 0.2475 0.5826 0.2602 0.2072  0.0335  0.1152  52  VAL D CG1 
6801  C CG2 . VAL D 52  ? 0.2047 0.4862 0.2555 0.1531  0.0359  0.1051  52  VAL D CG2 
6802  N N   . ASN D 53  ? 0.1547 0.7251 0.2595 0.1238  0.0029  0.0916  53  ASN D N   
6803  C CA  . ASN D 53  ? 0.1558 0.8223 0.2645 0.1255  -0.0045 0.0863  53  ASN D CA  
6804  C C   . ASN D 53  ? 0.1394 0.8024 0.2628 0.0702  -0.0095 0.0769  53  ASN D C   
6805  O O   . ASN D 53  ? 0.1446 0.8346 0.2629 0.0725  -0.0134 0.0753  53  ASN D O   
6806  C CB  . ASN D 53  ? 0.1499 0.9406 0.2713 0.1309  -0.0087 0.0787  53  ASN D CB  
6807  C CG  . ASN D 53  ? 0.1751 0.9729 0.2753 0.1924  -0.0040 0.0878  53  ASN D CG  
6808  O OD1 . ASN D 53  ? 0.2119 0.9362 0.2760 0.2404  0.0026  0.1001  53  ASN D OD1 
6809  N ND2 . ASN D 53  ? 0.1648 1.0452 0.2798 0.1903  -0.0055 0.0813  53  ASN D ND2 
6810  N N   . SER D 54  ? 0.1282 0.7520 0.2623 0.0240  -0.0087 0.0708  54  SER D N   
6811  C CA  . SER D 54  ? 0.1291 0.7231 0.2615 -0.0250 -0.0111 0.0626  54  SER D CA  
6812  C C   . SER D 54  ? 0.1358 0.6534 0.2588 -0.0128 -0.0105 0.0686  54  SER D C   
6813  O O   . SER D 54  ? 0.1415 0.6652 0.2588 -0.0312 -0.0140 0.0640  54  SER D O   
6814  C CB  . SER D 54  ? 0.1290 0.6714 0.2589 -0.0637 -0.0082 0.0576  54  SER D CB  
6815  O OG  . SER D 54  ? 0.1330 0.7473 0.2649 -0.0943 -0.0074 0.0481  54  SER D OG  
6816  N N   . ILE D 55  ? 0.1408 0.5888 0.2596 0.0144  -0.0049 0.0772  55  ILE D N   
6817  C CA  . ILE D 55  ? 0.1512 0.5312 0.2593 0.0248  -0.0017 0.0814  55  ILE D CA  
6818  C C   . ILE D 55  ? 0.1712 0.5805 0.2657 0.0547  -0.0019 0.0870  55  ILE D C   
6819  O O   . ILE D 55  ? 0.1742 0.5711 0.2644 0.0451  -0.0043 0.0854  55  ILE D O   
6820  C CB  . ILE D 55  ? 0.1572 0.4667 0.2588 0.0416  0.0073  0.0861  55  ILE D CB  
6821  C CG1 . ILE D 55  ? 0.1420 0.4173 0.2551 0.0130  0.0063  0.0791  55  ILE D CG1 
6822  C CG2 . ILE D 55  ? 0.1749 0.4283 0.2590 0.0539  0.0142  0.0895  55  ILE D CG2 
6823  C CD1 . ILE D 55  ? 0.1455 0.3711 0.2561 0.0237  0.0145  0.0798  55  ILE D CD1 
6824  N N   . ILE D 56  ? 0.1923 0.6385 0.2744 0.0954  0.0006  0.0936  56  ILE D N   
6825  C CA  . ILE D 56  ? 0.2216 0.6987 0.2807 0.1345  0.0005  0.0996  56  ILE D CA  
6826  C C   . ILE D 56  ? 0.2100 0.7658 0.2839 0.1114  -0.0100 0.0907  56  ILE D C   
6827  O O   . ILE D 56  ? 0.2215 0.7635 0.2829 0.1187  -0.0107 0.0929  56  ILE D O   
6828  C CB  . ILE D 56  ? 0.2493 0.7722 0.2873 0.1872  0.0031  0.1062  56  ILE D CB  
6829  C CG1 . ILE D 56  ? 0.2859 0.7077 0.2890 0.2159  0.0173  0.1162  56  ILE D CG1 
6830  C CG2 . ILE D 56  ? 0.2776 0.8637 0.2917 0.2309  -0.0004 0.1096  56  ILE D CG2 
6831  C CD1 . ILE D 56  ? 0.3182 0.7683 0.2948 0.2663  0.0211  0.1223  56  ILE D CD1 
6832  N N   . ASP D 57  ? 0.1943 0.8301 0.2904 0.0794  -0.0165 0.0795  57  ASP D N   
6833  C CA  . ASP D 57  ? 0.1926 0.9160 0.2968 0.0512  -0.0244 0.0674  57  ASP D CA  
6834  C C   . ASP D 57  ? 0.1920 0.8588 0.2945 0.0072  -0.0258 0.0619  57  ASP D C   
6835  O O   . ASP D 57  ? 0.1987 0.9054 0.2965 0.0003  -0.0304 0.0567  57  ASP D O   
6836  C CB  . ASP D 57  ? 0.1830 1.0041 0.3036 0.0189  -0.0273 0.0540  57  ASP D CB  
6837  C CG  . ASP D 57  ? 0.1913 1.1213 0.3125 0.0672  -0.0296 0.0547  57  ASP D CG  
6838  O OD1 . ASP D 57  ? 0.2077 1.1978 0.3176 0.1064  -0.0337 0.0561  57  ASP D OD1 
6839  O OD2 . ASP D 57  ? 0.1865 1.1448 0.3162 0.0701  -0.0274 0.0535  57  ASP D OD2 
6840  N N   . LYS D 58  ? 0.1899 0.7670 0.2925 -0.0186 -0.0221 0.0623  58  LYS D N   
6841  C CA  . LYS D 58  ? 0.1981 0.7135 0.2908 -0.0506 -0.0229 0.0578  58  LYS D CA  
6842  C C   . LYS D 58  ? 0.2079 0.6832 0.2925 -0.0223 -0.0221 0.0656  58  LYS D C   
6843  O O   . LYS D 58  ? 0.2168 0.6806 0.2927 -0.0408 -0.0250 0.0609  58  LYS D O   
6844  C CB  . LYS D 58  ? 0.1973 0.6306 0.2855 -0.0732 -0.0193 0.0564  58  LYS D CB  
6845  C CG  . LYS D 58  ? 0.2162 0.6465 0.2869 -0.1247 -0.0192 0.0442  58  LYS D CG  
6846  C CD  . LYS D 58  ? 0.2195 0.7507 0.2942 -0.1488 -0.0201 0.0347  58  LYS D CD  
6847  C CE  . LYS D 58  ? 0.2558 0.7700 0.2977 -0.2102 -0.0160 0.0203  58  LYS D CE  
6848  N NZ  . LYS D 58  ? 0.2636 0.8916 0.3078 -0.2435 -0.0154 0.0064  58  LYS D NZ  
6849  N N   . MET D 59  ? 0.2167 0.6669 0.2972 0.0206  -0.0166 0.0770  59  MET D N   
6850  C CA  . MET D 59  ? 0.2351 0.6414 0.2987 0.0463  -0.0123 0.0846  59  MET D CA  
6851  C C   . MET D 59  ? 0.2554 0.7274 0.3057 0.0784  -0.0156 0.0882  59  MET D C   
6852  O O   . MET D 59  ? 0.2707 0.7179 0.3044 0.0921  -0.0138 0.0923  59  MET D O   
6853  C CB  . MET D 59  ? 0.2490 0.5832 0.2995 0.0711  -0.0007 0.0935  59  MET D CB  
6854  C CG  . MET D 59  ? 0.2323 0.5162 0.2970 0.0447  0.0018  0.0884  59  MET D CG  
6855  S SD  . MET D 59  ? 0.2235 0.4641 0.2928 0.0120  -0.0010 0.0798  59  MET D SD  
6856  C CE  . MET D 59  ? 0.2445 0.4406 0.2934 0.0312  0.0084  0.0851  59  MET D CE  
6857  N N   . ASN D 60  ? 0.2584 0.8200 0.3143 0.0920  -0.0203 0.0855  60  ASN D N   
6858  C CA  . ASN D 60  ? 0.2809 0.9263 0.3223 0.1317  -0.0246 0.0872  60  ASN D CA  
6859  C C   . ASN D 60  ? 0.2843 0.9616 0.3240 0.1172  -0.0311 0.0810  60  ASN D C   
6860  O O   . ASN D 60  ? 0.3099 1.0000 0.3251 0.1603  -0.0307 0.0880  60  ASN D O   
6861  C CB  . ASN D 60  ? 0.2739 1.0361 0.3292 0.1385  -0.0303 0.0795  60  ASN D CB  
6862  C CG  . ASN D 60  ? 0.2799 1.1717 0.3364 0.1477  -0.0396 0.0695  60  ASN D CG  
6863  O OD1 . ASN D 60  ? 0.2664 1.2024 0.3383 0.0969  -0.0453 0.0551  60  ASN D OD1 
6864  N ND2 . ASN D 60  ? 0.3080 1.2629 0.3422 0.2139  -0.0406 0.0757  60  ASN D ND2 
6865  N N   . THR D 61  ? 0.2680 0.9517 0.3252 0.0591  -0.0358 0.0680  61  THR D N   
6866  C CA  . THR D 61  ? 0.2758 0.9672 0.3265 0.0413  -0.0404 0.0621  61  THR D CA  
6867  C C   . THR D 61  ? 0.2756 0.8492 0.3199 0.0256  -0.0352 0.0670  61  THR D C   
6868  O O   . THR D 61  ? 0.2664 0.7890 0.3170 -0.0105 -0.0336 0.0620  61  THR D O   
6869  C CB  . THR D 61  ? 0.2726 1.0444 0.3323 -0.0143 -0.0471 0.0423  61  THR D CB  
6870  O OG1 . THR D 61  ? 0.2752 0.9711 0.3323 -0.0669 -0.0438 0.0358  61  THR D OG1 
6871  C CG2 . THR D 61  ? 0.2679 1.1638 0.3404 -0.0144 -0.0504 0.0325  61  THR D CG2 
6872  N N   . GLN D 62  ? 0.2905 0.8236 0.3175 0.0563  -0.0317 0.0764  62  GLN D N   
6873  C CA  . GLN D 62  ? 0.2908 0.7273 0.3115 0.0454  -0.0258 0.0797  62  GLN D CA  
6874  C C   . GLN D 62  ? 0.3087 0.7337 0.3086 0.0693  -0.0242 0.0854  62  GLN D C   
6875  O O   . GLN D 62  ? 0.3281 0.8088 0.3139 0.1031  -0.0265 0.0894  62  GLN D O   
6876  C CB  . GLN D 62  ? 0.2927 0.6579 0.3118 0.0584  -0.0154 0.0875  62  GLN D CB  
6877  C CG  . GLN D 62  ? 0.3254 0.6299 0.3158 0.0929  -0.0030 0.0991  62  GLN D CG  
6878  C CD  . GLN D 62  ? 0.3336 0.5710 0.3200 0.0928  0.0088  0.1022  62  GLN D CD  
6879  O OE1 . GLN D 62  ? 0.3164 0.5646 0.3218 0.0810  0.0065  0.0988  62  GLN D OE1 
6880  N NE2 . GLN D 62  ? 0.3651 0.5337 0.3237 0.1021  0.0228  0.1071  62  GLN D NE2 
6881  N N   . PHE D 63  ? 0.3052 0.6627 0.3003 0.0550  -0.0202 0.0851  63  PHE D N   
6882  C CA  . PHE D 63  ? 0.3212 0.6654 0.2968 0.0697  -0.0186 0.0887  63  PHE D CA  
6883  C C   . PHE D 63  ? 0.3559 0.6872 0.2990 0.1196  -0.0093 0.1025  63  PHE D C   
6884  O O   . PHE D 63  ? 0.3753 0.6603 0.3038 0.1376  0.0017  0.1103  63  PHE D O   
6885  C CB  . PHE D 63  ? 0.3170 0.5897 0.2917 0.0498  -0.0133 0.0861  63  PHE D CB  
6886  C CG  . PHE D 63  ? 0.3342 0.5963 0.2904 0.0590  -0.0121 0.0882  63  PHE D CG  
6887  C CD1 . PHE D 63  ? 0.3309 0.6376 0.2886 0.0446  -0.0230 0.0806  63  PHE D CD1 
6888  C CD2 . PHE D 63  ? 0.3600 0.5661 0.2920 0.0789  0.0016  0.0967  63  PHE D CD2 
6889  C CE1 . PHE D 63  ? 0.3469 0.6457 0.2873 0.0546  -0.0222 0.0826  63  PHE D CE1 
6890  C CE2 . PHE D 63  ? 0.3795 0.5747 0.2915 0.0872  0.0038  0.0990  63  PHE D CE2 
6891  C CZ  . PHE D 63  ? 0.3696 0.6130 0.2884 0.0776  -0.0091 0.0925  63  PHE D CZ  
6892  N N   . GLU D 64  ? 0.3723 0.7401 0.2964 0.1426  -0.0130 0.1050  64  GLU D N   
6893  C CA  . GLU D 64  ? 0.4213 0.7634 0.2980 0.1954  -0.0029 0.1189  64  GLU D CA  
6894  C C   . GLU D 64  ? 0.4400 0.7404 0.2938 0.1968  0.0017  0.1217  64  GLU D C   
6895  O O   . GLU D 64  ? 0.4208 0.7696 0.2915 0.1791  -0.0095 0.1135  64  GLU D O   
6896  C CB  . GLU D 64  ? 0.4354 0.8759 0.3023 0.2356  -0.0125 0.1197  64  GLU D CB  
6897  C CG  . GLU D 64  ? 0.4213 0.9136 0.3051 0.2424  -0.0162 0.1174  64  GLU D CG  
6898  C CD  . GLU D 64  ? 0.4347 1.0471 0.3106 0.2838  -0.0265 0.1149  64  GLU D CD  
6899  O OE1 . GLU D 64  ? 0.4677 1.1058 0.3116 0.3226  -0.0281 0.1191  64  GLU D OE1 
6900  O OE2 . GLU D 64  ? 0.4132 1.1010 0.3137 0.2787  -0.0330 0.1076  64  GLU D OE2 
6901  N N   . ALA D 65  ? 0.4825 0.6908 0.2926 0.2146  0.0202  0.1323  65  ALA D N   
6902  C CA  . ALA D 65  ? 0.5069 0.6697 0.2889 0.2157  0.0279  0.1355  65  ALA D CA  
6903  C C   . ALA D 65  ? 0.5461 0.7460 0.2883 0.2651  0.0244  0.1435  65  ALA D C   
6904  O O   . ALA D 65  ? 0.5786 0.8048 0.2917 0.3115  0.0244  0.1510  65  ALA D O   
6905  C CB  . ALA D 65  ? 0.5532 0.6061 0.2937 0.2113  0.0521  0.1416  65  ALA D CB  
6906  N N   . VAL D 66  ? 0.5432 0.7502 0.2822 0.2587  0.0209  0.1413  66  VAL D N   
6907  C CA  . VAL D 66  ? 0.5863 0.8226 0.2820 0.3073  0.0188  0.1488  66  VAL D CA  
6908  C C   . VAL D 66  ? 0.6266 0.7795 0.2806 0.3068  0.0337  0.1552  66  VAL D C   
6909  O O   . VAL D 66  ? 0.5962 0.7184 0.2781 0.2606  0.0361  0.1475  66  VAL D O   
6910  C CB  . VAL D 66  ? 0.5417 0.9052 0.2788 0.2996  -0.0046 0.1360  66  VAL D CB  
6911  C CG1 . VAL D 66  ? 0.5902 1.0014 0.2819 0.3577  -0.0080 0.1427  66  VAL D CG1 
6912  C CG2 . VAL D 66  ? 0.4980 0.9458 0.2794 0.2844  -0.0173 0.1260  66  VAL D CG2 
6913  N N   . GLY D 67  ? 0.7006 0.8173 0.2820 0.3615  0.0445  0.1690  67  GLY D N   
6914  C CA  . GLY D 67  ? 0.7542 0.7843 0.2819 0.3648  0.0619  0.1764  67  GLY D CA  
6915  C C   . GLY D 67  ? 0.7225 0.8172 0.2742 0.3584  0.0468  0.1698  67  GLY D C   
6916  O O   . GLY D 67  ? 0.7192 0.9052 0.2739 0.3921  0.0302  0.1684  67  GLY D O   
6917  N N   . ARG D 68  ? 0.7005 0.7542 0.2678 0.3153  0.0528  0.1640  68  ARG D N   
6918  C CA  . ARG D 68  ? 0.6733 0.7745 0.2600 0.3048  0.0404  0.1572  68  ARG D CA  
6919  C C   . ARG D 68  ? 0.7154 0.7266 0.2603 0.2940  0.0607  0.1621  68  ARG D C   
6920  O O   . ARG D 68  ? 0.7163 0.6615 0.2627 0.2586  0.0768  0.1593  68  ARG D O   
6921  C CB  . ARG D 68  ? 0.5872 0.7575 0.2529 0.2533  0.0208  0.1393  68  ARG D CB  
6922  C CG  . ARG D 68  ? 0.5513 0.8300 0.2512 0.2598  -0.0004 0.1313  68  ARG D CG  
6923  C CD  . ARG D 68  ? 0.4876 0.8169 0.2458 0.2060  -0.0163 0.1131  68  ARG D CD  
6924  N NE  . ARG D 68  ? 0.4566 0.7389 0.2437 0.1695  -0.0114 0.1087  68  ARG D NE  
6925  C CZ  . ARG D 68  ? 0.4366 0.7324 0.2442 0.1632  -0.0130 0.1074  68  ARG D CZ  
6926  N NH1 . ARG D 68  ? 0.4420 0.8004 0.2469 0.1900  -0.0193 0.1097  68  ARG D NH1 
6927  N NH2 . ARG D 68  ? 0.4125 0.6639 0.2427 0.1322  -0.0084 0.1030  68  ARG D NH2 
6928  N N   . GLU D 69  ? 0.7510 0.7674 0.2578 0.3235  0.0601  0.1678  69  GLU D N   
6929  C CA  . GLU D 69  ? 0.8083 0.7364 0.2601 0.3207  0.0819  0.1744  69  GLU D CA  
6930  C C   . GLU D 69  ? 0.7566 0.7249 0.2507 0.2880  0.0707  0.1628  69  GLU D C   
6931  O O   . GLU D 69  ? 0.7117 0.7693 0.2444 0.2912  0.0473  0.1550  69  GLU D O   
6932  C CB  . GLU D 69  ? 0.9059 0.7952 0.2671 0.3860  0.0924  0.1915  69  GLU D CB  
6933  C CG  . GLU D 69  ? 0.9786 0.8127 0.2753 0.4312  0.1061  0.2050  69  GLU D CG  
6934  C CD  . GLU D 69  ? 1.0763 0.7582 0.2867 0.4220  0.1431  0.2149  69  GLU D CD  
6935  O OE1 . GLU D 69  ? 1.0476 0.6936 0.2899 0.3599  0.1546  0.2048  69  GLU D OE1 
6936  O OE2 . GLU D 69  ? 1.1908 0.7890 0.2946 0.4771  0.1619  0.2315  69  GLU D OE2 
6937  N N   . PHE D 70  ? 0.7682 0.6719 0.2499 0.2554  0.0888  0.1602  70  PHE D N   
6938  C CA  . PHE D 70  ? 0.7290 0.6612 0.2426 0.2276  0.0810  0.1495  70  PHE D CA  
6939  C C   . PHE D 70  ? 0.7955 0.6499 0.2474 0.2265  0.1061  0.1558  70  PHE D C   
6940  O O   . PHE D 70  ? 0.8536 0.6243 0.2560 0.2176  0.1332  0.1612  70  PHE D O   
6941  C CB  . PHE D 70  ? 0.6576 0.6146 0.2380 0.1785  0.0740  0.1331  70  PHE D CB  
6942  C CG  . PHE D 70  ? 0.6020 0.6153 0.2329 0.1731  0.0549  0.1271  70  PHE D CG  
6943  C CD1 . PHE D 70  ? 0.6041 0.5917 0.2359 0.1706  0.0633  0.1301  70  PHE D CD1 
6944  C CD2 . PHE D 70  ? 0.5542 0.6417 0.2258 0.1665  0.0304  0.1174  70  PHE D CD2 
6945  C CE1 . PHE D 70  ? 0.5552 0.5940 0.2315 0.1645  0.0467  0.1246  70  PHE D CE1 
6946  C CE2 . PHE D 70  ? 0.5123 0.6464 0.2228 0.1555  0.0157  0.1107  70  PHE D CE2 
6947  C CZ  . PHE D 70  ? 0.5105 0.6221 0.2252 0.1560  0.0234  0.1149  70  PHE D CZ  
6948  N N   . ASN D 71  ? 0.7920 0.6712 0.2423 0.2315  0.0989  0.1539  71  ASN D N   
6949  C CA  . ASN D 71  ? 0.8574 0.6664 0.2474 0.2293  0.1228  0.1594  71  ASN D CA  
6950  C C   . ASN D 71  ? 0.8297 0.6257 0.2487 0.1750  0.1352  0.1449  71  ASN D C   
6951  O O   . ASN D 71  ? 0.7665 0.5990 0.2451 0.1453  0.1265  0.1324  71  ASN D O   
6952  C CB  . ASN D 71  ? 0.8744 0.7142 0.2437 0.2616  0.1114  0.1640  71  ASN D CB  
6953  C CG  . ASN D 71  ? 0.7975 0.7165 0.2349 0.2365  0.0880  0.1482  71  ASN D CG  
6954  O OD1 . ASN D 71  ? 0.7685 0.6825 0.2344 0.1977  0.0928  0.1368  71  ASN D OD1 
6955  N ND2 . ASN D 71  ? 0.7721 0.7658 0.2291 0.2596  0.0634  0.1461  71  ASN D ND2 
6956  N N   . ASN D 72  ? 0.8801 0.6289 0.2534 0.1645  0.1558  0.1459  72  ASN D N   
6957  C CA  . ASN D 72  ? 0.8722 0.6096 0.2583 0.1144  0.1738  0.1314  72  ASN D CA  
6958  C C   . ASN D 72  ? 0.7866 0.6075 0.2485 0.0939  0.1520  0.1139  72  ASN D C   
6959  O O   . ASN D 72  ? 0.7625 0.6013 0.2519 0.0575  0.1604  0.0985  72  ASN D O   
6960  C CB  . ASN D 72  ? 0.9655 0.6249 0.2695 0.1075  0.2056  0.1375  72  ASN D CB  
6961  C CG  . ASN D 72  ? 0.9844 0.6205 0.2812 0.0504  0.2339  0.1221  72  ASN D CG  
6962  O OD1 . ASN D 72  ? 0.9765 0.6055 0.2865 0.0242  0.2427  0.1148  72  ASN D OD1 
6963  N ND2 . ASN D 72  ? 1.0114 0.6427 0.2864 0.0293  0.2488  0.1156  72  ASN D ND2 
6964  N N   . LEU D 73  ? 0.7488 0.6209 0.2373 0.1183  0.1253  0.1149  73  LEU D N   
6965  C CA  . LEU D 73  ? 0.6822 0.6185 0.2285 0.1042  0.1042  0.0993  73  LEU D CA  
6966  C C   . LEU D 73  ? 0.6258 0.6094 0.2195 0.1102  0.0775  0.0955  73  LEU D C   
6967  O O   . LEU D 73  ? 0.5933 0.6186 0.2120 0.1118  0.0566  0.0879  73  LEU D O   
6968  C CB  . LEU D 73  ? 0.6958 0.6448 0.2255 0.1174  0.0981  0.0998  73  LEU D CB  
6969  C CG  . LEU D 73  ? 0.7457 0.6560 0.2338 0.1037  0.1244  0.0995  73  LEU D CG  
6970  C CD1 . LEU D 73  ? 0.7733 0.6841 0.2312 0.1268  0.1197  0.1057  73  LEU D CD1 
6971  C CD2 . LEU D 73  ? 0.7122 0.6543 0.2358 0.0702  0.1294  0.0803  73  LEU D CD2 
6972  N N   . GLU D 74  ? 0.6221 0.5928 0.2208 0.1105  0.0808  0.1002  74  GLU D N   
6973  C CA  . GLU D 74  ? 0.5721 0.5829 0.2144 0.1087  0.0602  0.0954  74  GLU D CA  
6974  C C   . GLU D 74  ? 0.5562 0.5515 0.2180 0.0877  0.0703  0.0904  74  GLU D C   
6975  O O   . GLU D 74  ? 0.5412 0.5422 0.2167 0.0920  0.0646  0.0938  74  GLU D O   
6976  C CB  . GLU D 74  ? 0.5852 0.6115 0.2126 0.1387  0.0506  0.1070  74  GLU D CB  
6977  C CG  . GLU D 74  ? 0.5921 0.6564 0.2086 0.1581  0.0361  0.1079  74  GLU D CG  
6978  C CD  . GLU D 74  ? 0.5970 0.7051 0.2078 0.1869  0.0234  0.1143  74  GLU D CD  
6979  O OE1 . GLU D 74  ? 0.6382 0.7164 0.2122 0.2160  0.0355  0.1279  74  GLU D OE1 
6980  O OE2 . GLU D 74  ? 0.5664 0.7390 0.2036 0.1801  0.0027  0.1043  74  GLU D OE2 
6981  N N   . ARG D 75  ? 0.5601 0.5441 0.2232 0.0644  0.0856  0.0808  75  ARG D N   
6982  C CA  . ARG D 75  ? 0.5533 0.5282 0.2293 0.0414  0.0990  0.0737  75  ARG D CA  
6983  C C   . ARG D 75  ? 0.4961 0.5125 0.2224 0.0355  0.0799  0.0627  75  ARG D C   
6984  O O   . ARG D 75  ? 0.4844 0.4967 0.2244 0.0266  0.0837  0.0614  75  ARG D O   
6985  C CB  . ARG D 75  ? 0.5765 0.5462 0.2388 0.0150  0.1214  0.0624  75  ARG D CB  
6986  C CG  . ARG D 75  ? 0.6520 0.5589 0.2500 0.0108  0.1491  0.0726  75  ARG D CG  
6987  C CD  . ARG D 75  ? 0.6951 0.5499 0.2616 -0.0079 0.1733  0.0750  75  ARG D CD  
6988  N NE  . ARG D 75  ? 0.7882 0.5569 0.2722 -0.0017 0.1993  0.0896  75  ARG D NE  
6989  C CZ  . ARG D 75  ? 0.8308 0.5494 0.2714 0.0361  0.1978  0.1093  75  ARG D CZ  
6990  N NH1 . ARG D 75  ? 0.7820 0.5396 0.2613 0.0662  0.1710  0.1155  75  ARG D NH1 
6991  N NH2 . ARG D 75  ? 0.9307 0.5594 0.2816 0.0454  0.2245  0.1222  75  ARG D NH2 
6992  N N   . ARG D 76  ? 0.4695 0.5174 0.2148 0.0409  0.0611  0.0549  76  ARG D N   
6993  C CA  . ARG D 76  ? 0.4328 0.5041 0.2090 0.0384  0.0444  0.0451  76  ARG D CA  
6994  C C   . ARG D 76  ? 0.4194 0.4892 0.2060 0.0428  0.0332  0.0530  76  ARG D C   
6995  O O   . ARG D 76  ? 0.3997 0.4723 0.2059 0.0357  0.0321  0.0495  76  ARG D O   
6996  C CB  . ARG D 76  ? 0.4290 0.5139 0.2030 0.0454  0.0288  0.0366  76  ARG D CB  
6997  C CG  . ARG D 76  ? 0.4353 0.5351 0.2051 0.0450  0.0365  0.0246  76  ARG D CG  
6998  C CD  . ARG D 76  ? 0.4448 0.5447 0.1993 0.0570  0.0218  0.0190  76  ARG D CD  
6999  N NE  . ARG D 76  ? 0.4614 0.5512 0.1978 0.0607  0.0189  0.0290  76  ARG D NE  
7000  C CZ  . ARG D 76  ? 0.4732 0.5588 0.1931 0.0657  0.0048  0.0266  76  ARG D CZ  
7001  N NH1 . ARG D 76  ? 0.4801 0.5551 0.1899 0.0674  -0.0063 0.0155  76  ARG D NH1 
7002  N NH2 . ARG D 76  ? 0.4873 0.5753 0.1928 0.0698  0.0029  0.0348  76  ARG D NH2 
7003  N N   . ILE D 77  ? 0.4306 0.5046 0.2042 0.0550  0.0249  0.0622  77  ILE D N   
7004  C CA  . ILE D 77  ? 0.4198 0.5091 0.2029 0.0594  0.0143  0.0677  77  ILE D CA  
7005  C C   . ILE D 77  ? 0.4317 0.5017 0.2082 0.0673  0.0278  0.0784  77  ILE D C   
7006  O O   . ILE D 77  ? 0.4149 0.4966 0.2075 0.0668  0.0220  0.0798  77  ILE D O   
7007  C CB  . ILE D 77  ? 0.4291 0.5489 0.2008 0.0701  0.0009  0.0707  77  ILE D CB  
7008  C CG1 . ILE D 77  ? 0.4645 0.5754 0.2043 0.0934  0.0107  0.0824  77  ILE D CG1 
7009  C CG2 . ILE D 77  ? 0.4256 0.5548 0.1970 0.0562  -0.0119 0.0580  77  ILE D CG2 
7010  C CD1 . ILE D 77  ? 0.4740 0.6309 0.2034 0.1106  -0.0025 0.0854  77  ILE D CD1 
7011  N N   . GLU D 78  ? 0.4693 0.5032 0.2148 0.0733  0.0475  0.0856  78  GLU D N   
7012  C CA  . GLU D 78  ? 0.4986 0.4934 0.2224 0.0771  0.0653  0.0943  78  GLU D CA  
7013  C C   . GLU D 78  ? 0.4706 0.4659 0.2241 0.0529  0.0694  0.0841  78  GLU D C   
7014  O O   . GLU D 78  ? 0.4694 0.4548 0.2259 0.0549  0.0719  0.0882  78  GLU D O   
7015  C CB  . GLU D 78  ? 0.5604 0.5002 0.2311 0.0793  0.0904  0.1011  78  GLU D CB  
7016  C CG  . GLU D 78  ? 0.6124 0.4903 0.2410 0.0798  0.1138  0.1093  78  GLU D CG  
7017  C CD  . GLU D 78  ? 0.6974 0.5033 0.2512 0.0859  0.1405  0.1187  78  GLU D CD  
7018  O OE1 . GLU D 78  ? 0.7087 0.5072 0.2550 0.0611  0.1527  0.1102  78  GLU D OE1 
7019  O OE2 . GLU D 78  ? 0.7603 0.5144 0.2562 0.1174  0.1503  0.1343  78  GLU D OE2 
7020  N N   . ASN D 79  ? 0.4510 0.4628 0.2242 0.0335  0.0699  0.0701  79  ASN D N   
7021  C CA  . ASN D 79  ? 0.4268 0.4515 0.2269 0.0143  0.0731  0.0578  79  ASN D CA  
7022  C C   . ASN D 79  ? 0.3864 0.4371 0.2197 0.0185  0.0521  0.0545  79  ASN D C   
7023  O O   . ASN D 79  ? 0.3718 0.4235 0.2210 0.0111  0.0540  0.0516  79  ASN D O   
7024  C CB  . ASN D 79  ? 0.4227 0.4712 0.2298 0.0004  0.0787  0.0423  79  ASN D CB  
7025  C CG  . ASN D 79  ? 0.4010 0.4775 0.2335 -0.0152 0.0823  0.0270  79  ASN D CG  
7026  O OD1 . ASN D 79  ? 0.4194 0.4857 0.2435 -0.0355 0.1019  0.0232  79  ASN D OD1 
7027  N ND2 . ASN D 79  ? 0.3705 0.4792 0.2270 -0.0053 0.0645  0.0176  79  ASN D ND2 
7028  N N   . LEU D 80  ? 0.3758 0.4431 0.2133 0.0270  0.0339  0.0539  80  LEU D N   
7029  C CA  . LEU D 80  ? 0.3537 0.4346 0.2080 0.0258  0.0165  0.0510  80  LEU D CA  
7030  C C   . LEU D 80  ? 0.3512 0.4338 0.2099 0.0303  0.0163  0.0613  80  LEU D C   
7031  O O   . LEU D 80  ? 0.3335 0.4193 0.2094 0.0241  0.0128  0.0589  80  LEU D O   
7032  C CB  . LEU D 80  ? 0.3602 0.4505 0.2034 0.0276  0.0015  0.0484  80  LEU D CB  
7033  C CG  . LEU D 80  ? 0.3562 0.4484 0.1995 0.0175  -0.0136 0.0413  80  LEU D CG  
7034  C CD1 . LEU D 80  ? 0.3778 0.4689 0.1974 0.0139  -0.0227 0.0359  80  LEU D CD1 
7035  C CD2 . LEU D 80  ? 0.3459 0.4571 0.2003 0.0122  -0.0185 0.0468  80  LEU D CD2 
7036  N N   . ASN D 81  ? 0.3744 0.4555 0.2131 0.0453  0.0203  0.0727  81  ASN D N   
7037  C CA  . ASN D 81  ? 0.3821 0.4684 0.2163 0.0595  0.0211  0.0831  81  ASN D CA  
7038  C C   . ASN D 81  ? 0.3883 0.4437 0.2229 0.0554  0.0357  0.0853  81  ASN D C   
7039  O O   . ASN D 81  ? 0.3742 0.4412 0.2225 0.0573  0.0310  0.0871  81  ASN D O   
7040  C CB  . ASN D 81  ? 0.4198 0.5026 0.2188 0.0864  0.0262  0.0951  81  ASN D CB  
7041  C CG  . ASN D 81  ? 0.4350 0.5286 0.2210 0.1118  0.0263  0.1057  81  ASN D CG  
7042  O OD1 . ASN D 81  ? 0.4082 0.5507 0.2184 0.1103  0.0118  0.1023  81  ASN D OD1 
7043  N ND2 . ASN D 81  ? 0.4869 0.5317 0.2273 0.1356  0.0443  0.1179  81  ASN D ND2 
7044  N N   . LYS D 82  ? 0.4139 0.4327 0.2310 0.0460  0.0546  0.0834  82  LYS D N   
7045  C CA  . LYS D 82  ? 0.4301 0.4170 0.2399 0.0349  0.0717  0.0827  82  LYS D CA  
7046  C C   . LYS D 82  ? 0.3868 0.4013 0.2385 0.0190  0.0622  0.0712  82  LYS D C   
7047  O O   . LYS D 82  ? 0.3817 0.3906 0.2399 0.0198  0.0633  0.0740  82  LYS D O   
7048  C CB  . LYS D 82  ? 0.4689 0.4194 0.2493 0.0165  0.0959  0.0777  82  LYS D CB  
7049  C CG  . LYS D 82  ? 0.4883 0.4098 0.2589 -0.0054 0.1155  0.0720  82  LYS D CG  
7050  C CD  . LYS D 82  ? 0.5513 0.4236 0.2721 -0.0285 0.1457  0.0682  82  LYS D CD  
7051  C CE  . LYS D 82  ? 0.5282 0.4456 0.2758 -0.0618 0.1511  0.0467  82  LYS D CE  
7052  N NZ  . LYS D 82  ? 0.5927 0.4710 0.2892 -0.0900 0.1812  0.0412  82  LYS D NZ  
7053  N N   . LYS D 83  ? 0.3635 0.4047 0.2371 0.0088  0.0534  0.0587  83  LYS D N   
7054  C CA  . LYS D 83  ? 0.3328 0.3962 0.2359 0.0008  0.0439  0.0476  83  LYS D CA  
7055  C C   . LYS D 83  ? 0.3147 0.3870 0.2309 0.0070  0.0279  0.0525  83  LYS D C   
7056  O O   . LYS D 83  ? 0.2988 0.3746 0.2311 0.0021  0.0259  0.0489  83  LYS D O   
7057  C CB  . LYS D 83  ? 0.3250 0.4093 0.2340 0.0000  0.0368  0.0345  83  LYS D CB  
7058  C CG  . LYS D 83  ? 0.3304 0.4327 0.2422 -0.0116 0.0514  0.0207  83  LYS D CG  
7059  C CD  . LYS D 83  ? 0.3614 0.4410 0.2533 -0.0282 0.0752  0.0242  83  LYS D CD  
7060  C CE  . LYS D 83  ? 0.3686 0.4785 0.2634 -0.0507 0.0918  0.0058  83  LYS D CE  
7061  N NZ  . LYS D 83  ? 0.3861 0.5104 0.2668 -0.0551 0.0991  -0.0004 83  LYS D NZ  
7062  N N   . MET D 84  ? 0.3204 0.4018 0.2286 0.0150  0.0173  0.0590  84  MET D N   
7063  C CA  . MET D 84  ? 0.3086 0.4090 0.2262 0.0142  0.0043  0.0612  84  MET D CA  
7064  C C   . MET D 84  ? 0.3081 0.4083 0.2293 0.0223  0.0107  0.0700  84  MET D C   
7065  O O   . MET D 84  ? 0.2908 0.3977 0.2281 0.0155  0.0064  0.0676  84  MET D O   
7066  C CB  . MET D 84  ? 0.3192 0.4436 0.2254 0.0174  -0.0060 0.0635  84  MET D CB  
7067  C CG  . MET D 84  ? 0.3122 0.4633 0.2246 0.0034  -0.0192 0.0588  84  MET D CG  
7068  S SD  . MET D 84  ? 0.3221 0.5328 0.2298 0.0133  -0.0261 0.0642  84  MET D SD  
7069  C CE  . MET D 84  ? 0.3210 0.5329 0.2338 0.0393  -0.0164 0.0770  84  MET D CE  
7070  N N   . GLU D 85  ? 0.3349 0.4200 0.2335 0.0391  0.0222  0.0804  85  GLU D N   
7071  C CA  . GLU D 85  ? 0.3502 0.4246 0.2377 0.0544  0.0300  0.0900  85  GLU D CA  
7072  C C   . GLU D 85  ? 0.3447 0.3902 0.2403 0.0398  0.0415  0.0852  85  GLU D C   
7073  O O   . GLU D 85  ? 0.3315 0.3847 0.2396 0.0411  0.0387  0.0864  85  GLU D O   
7074  C CB  . GLU D 85  ? 0.4018 0.4475 0.2439 0.0814  0.0429  0.1026  85  GLU D CB  
7075  C CG  . GLU D 85  ? 0.4097 0.4939 0.2424 0.1002  0.0312  0.1066  85  GLU D CG  
7076  C CD  . GLU D 85  ? 0.4466 0.5444 0.2470 0.1411  0.0321  0.1192  85  GLU D CD  
7077  O OE1 . GLU D 85  ? 0.5048 0.5509 0.2528 0.1670  0.0481  0.1300  85  GLU D OE1 
7078  O OE2 . GLU D 85  ? 0.4247 0.5862 0.2461 0.1487  0.0176  0.1174  85  GLU D OE2 
7079  N N   . ASP D 86  ? 0.3542 0.3748 0.2431 0.0240  0.0545  0.0779  86  ASP D N   
7080  C CA  . ASP D 86  ? 0.3493 0.3567 0.2469 0.0051  0.0658  0.0688  86  ASP D CA  
7081  C C   . ASP D 86  ? 0.3039 0.3448 0.2400 -0.0028 0.0508  0.0592  86  ASP D C   
7082  O O   . ASP D 86  ? 0.2963 0.3342 0.2423 -0.0089 0.0546  0.0564  86  ASP D O   
7083  C CB  . ASP D 86  ? 0.3677 0.3643 0.2536 -0.0147 0.0816  0.0580  86  ASP D CB  
7084  C CG  . ASP D 86  ? 0.4293 0.3689 0.2655 -0.0212 0.1079  0.0632  86  ASP D CG  
7085  O OD1 . ASP D 86  ? 0.4536 0.3606 0.2718 -0.0204 0.1178  0.0678  86  ASP D OD1 
7086  O OD2 . ASP D 86  ? 0.4627 0.3829 0.2706 -0.0280 0.1202  0.0624  86  ASP D OD2 
7087  N N   . GLY D 87  ? 0.2828 0.3475 0.2321 -0.0021 0.0353  0.0541  87  GLY D N   
7088  C CA  . GLY D 87  ? 0.2576 0.3381 0.2264 -0.0062 0.0226  0.0455  87  GLY D CA  
7089  C C   . GLY D 87  ? 0.2456 0.3305 0.2238 -0.0049 0.0153  0.0514  87  GLY D C   
7090  O O   . GLY D 87  ? 0.2325 0.3187 0.2232 -0.0092 0.0136  0.0461  87  GLY D O   
7091  N N   . PHE D 88  ? 0.2513 0.3457 0.2227 0.0023  0.0111  0.0614  88  PHE D N   
7092  C CA  . PHE D 88  ? 0.2414 0.3540 0.2216 0.0038  0.0050  0.0661  88  PHE D CA  
7093  C C   . PHE D 88  ? 0.2457 0.3440 0.2268 0.0115  0.0164  0.0714  88  PHE D C   
7094  O O   . PHE D 88  ? 0.2315 0.3391 0.2260 0.0084  0.0128  0.0709  88  PHE D O   
7095  C CB  . PHE D 88  ? 0.2488 0.3949 0.2210 0.0122  -0.0023 0.0723  88  PHE D CB  
7096  C CG  . PHE D 88  ? 0.2471 0.4116 0.2168 -0.0051 -0.0148 0.0644  88  PHE D CG  
7097  C CD1 . PHE D 88  ? 0.2423 0.4046 0.2145 -0.0256 -0.0216 0.0565  88  PHE D CD1 
7098  C CD2 . PHE D 88  ? 0.2600 0.4363 0.2164 -0.0024 -0.0180 0.0644  88  PHE D CD2 
7099  C CE1 . PHE D 88  ? 0.2588 0.4215 0.2130 -0.0464 -0.0293 0.0481  88  PHE D CE1 
7100  C CE2 . PHE D 88  ? 0.2683 0.4547 0.2143 -0.0227 -0.0275 0.0554  88  PHE D CE2 
7101  C CZ  . PHE D 88  ? 0.2720 0.4471 0.2133 -0.0464 -0.0322 0.0470  88  PHE D CZ  
7102  N N   . LEU D 89  ? 0.2729 0.3415 0.2328 0.0194  0.0319  0.0760  89  LEU D N   
7103  C CA  . LEU D 89  ? 0.2928 0.3312 0.2401 0.0225  0.0466  0.0794  89  LEU D CA  
7104  C C   . LEU D 89  ? 0.2715 0.3090 0.2403 0.0024  0.0491  0.0672  89  LEU D C   
7105  O O   . LEU D 89  ? 0.2702 0.3007 0.2422 0.0027  0.0528  0.0682  89  LEU D O   
7106  C CB  . LEU D 89  ? 0.3451 0.3345 0.2490 0.0278  0.0670  0.0845  89  LEU D CB  
7107  C CG  . LEU D 89  ? 0.3821 0.3636 0.2513 0.0581  0.0676  0.0985  89  LEU D CG  
7108  C CD1 . LEU D 89  ? 0.4476 0.3621 0.2606 0.0606  0.0913  0.1031  89  LEU D CD1 
7109  C CD2 . LEU D 89  ? 0.3887 0.3872 0.2516 0.0861  0.0621  0.1084  89  LEU D CD2 
7110  N N   . ASP D 90  ? 0.2573 0.3067 0.2383 -0.0110 0.0471  0.0552  90  ASP D N   
7111  C CA  . ASP D 90  ? 0.2387 0.3018 0.2388 -0.0236 0.0475  0.0416  90  ASP D CA  
7112  C C   . ASP D 90  ? 0.2127 0.2918 0.2317 -0.0189 0.0318  0.0414  90  ASP D C   
7113  O O   . ASP D 90  ? 0.2029 0.2860 0.2331 -0.0228 0.0334  0.0362  90  ASP D O   
7114  C CB  . ASP D 90  ? 0.2351 0.3184 0.2391 -0.0303 0.0475  0.0279  90  ASP D CB  
7115  C CG  . ASP D 90  ? 0.2642 0.3353 0.2483 -0.0436 0.0666  0.0242  90  ASP D CG  
7116  O OD1 . ASP D 90  ? 0.2956 0.3303 0.2560 -0.0501 0.0828  0.0307  90  ASP D OD1 
7117  O OD2 . ASP D 90  ? 0.2639 0.3567 0.2488 -0.0472 0.0668  0.0146  90  ASP D OD2 
7118  N N   . VAL D 91  ? 0.2074 0.2934 0.2248 -0.0139 0.0182  0.0458  91  VAL D N   
7119  C CA  . VAL D 91  ? 0.1965 0.2881 0.2196 -0.0159 0.0063  0.0453  91  VAL D CA  
7120  C C   . VAL D 91  ? 0.1898 0.2877 0.2211 -0.0142 0.0080  0.0532  91  VAL D C   
7121  O O   . VAL D 91  ? 0.1805 0.2783 0.2206 -0.0175 0.0060  0.0501  91  VAL D O   
7122  C CB  . VAL D 91  ? 0.2063 0.2998 0.2156 -0.0200 -0.0048 0.0462  91  VAL D CB  
7123  C CG1 . VAL D 91  ? 0.2082 0.3034 0.2138 -0.0307 -0.0127 0.0461  91  VAL D CG1 
7124  C CG2 . VAL D 91  ? 0.2189 0.2980 0.2132 -0.0177 -0.0077 0.0372  91  VAL D CG2 
7125  N N   . TRP D 92  ? 0.1989 0.3030 0.2230 -0.0047 0.0120  0.0633  92  TRP D N   
7126  C CA  . TRP D 92  ? 0.1988 0.3140 0.2252 0.0045  0.0135  0.0710  92  TRP D CA  
7127  C C   . TRP D 92  ? 0.2069 0.2938 0.2296 0.0075  0.0271  0.0711  92  TRP D C   
7128  O O   . TRP D 92  ? 0.2008 0.2931 0.2305 0.0105  0.0268  0.0730  92  TRP D O   
7129  C CB  . TRP D 92  ? 0.2154 0.3529 0.2274 0.0231  0.0125  0.0809  92  TRP D CB  
7130  C CG  . TRP D 92  ? 0.2052 0.3876 0.2246 0.0130  -0.0015 0.0778  92  TRP D CG  
7131  C CD1 . TRP D 92  ? 0.2129 0.4095 0.2238 0.0103  -0.0067 0.0764  92  TRP D CD1 
7132  C CD2 . TRP D 92  ? 0.1924 0.4091 0.2238 -0.0022 -0.0101 0.0735  92  TRP D CD2 
7133  N NE1 . TRP D 92  ? 0.2079 0.4459 0.2229 -0.0083 -0.0175 0.0702  92  TRP D NE1 
7134  C CE2 . TRP D 92  ? 0.1973 0.4476 0.2234 -0.0181 -0.0189 0.0681  92  TRP D CE2 
7135  C CE3 . TRP D 92  ? 0.1817 0.4036 0.2246 -0.0069 -0.0099 0.0727  92  TRP D CE3 
7136  C CZ2 . TRP D 92  ? 0.1972 0.4842 0.2247 -0.0438 -0.0255 0.0606  92  TRP D CZ2 
7137  C CZ3 . TRP D 92  ? 0.1780 0.4367 0.2250 -0.0285 -0.0174 0.0669  92  TRP D CZ3 
7138  C CH2 . TRP D 92  ? 0.1881 0.4782 0.2254 -0.0492 -0.0242 0.0603  92  TRP D CH2 
7139  N N   . THR D 93  ? 0.2245 0.2822 0.2332 0.0027  0.0403  0.0673  93  THR D N   
7140  C CA  . THR D 93  ? 0.2394 0.2693 0.2394 -0.0053 0.0557  0.0626  93  THR D CA  
7141  C C   . THR D 93  ? 0.2075 0.2589 0.2359 -0.0178 0.0489  0.0508  93  THR D C   
7142  O O   . THR D 93  ? 0.2080 0.2531 0.2392 -0.0191 0.0532  0.0500  93  THR D O   
7143  C CB  . THR D 93  ? 0.2706 0.2714 0.2464 -0.0189 0.0733  0.0562  93  THR D CB  
7144  O OG1 . THR D 93  ? 0.3112 0.2802 0.2497 -0.0033 0.0815  0.0685  93  THR D OG1 
7145  C CG2 . THR D 93  ? 0.2944 0.2685 0.2557 -0.0370 0.0917  0.0474  93  THR D CG2 
7146  N N   . TYR D 94  ? 0.1869 0.2601 0.2298 -0.0228 0.0386  0.0420  94  TYR D N   
7147  C CA  . TYR D 94  ? 0.1669 0.2579 0.2263 -0.0258 0.0314  0.0310  94  TYR D CA  
7148  C C   . TYR D 94  ? 0.1554 0.2477 0.2221 -0.0211 0.0219  0.0374  94  TYR D C   
7149  O O   . TYR D 94  ? 0.1470 0.2428 0.2224 -0.0225 0.0229  0.0325  94  TYR D O   
7150  C CB  . TYR D 94  ? 0.1634 0.2673 0.2212 -0.0219 0.0221  0.0227  94  TYR D CB  
7151  C CG  . TYR D 94  ? 0.1576 0.2692 0.2166 -0.0138 0.0123  0.0144  94  TYR D CG  
7152  C CD1 . TYR D 94  ? 0.1639 0.2565 0.2105 -0.0101 0.0013  0.0204  94  TYR D CD1 
7153  C CD2 . TYR D 94  ? 0.1540 0.2925 0.2193 -0.0100 0.0153  -0.0007 94  TYR D CD2 
7154  C CE1 . TYR D 94  ? 0.1749 0.2578 0.2070 0.0003  -0.0053 0.0139  94  TYR D CE1 
7155  C CE2 . TYR D 94  ? 0.1579 0.3011 0.2153 0.0063  0.0062  -0.0077 94  TYR D CE2 
7156  C CZ  . TYR D 94  ? 0.1721 0.2788 0.2087 0.0130  -0.0035 0.0009  94  TYR D CZ  
7157  O OH  . TYR D 94  ? 0.1912 0.2863 0.2052 0.0319  -0.0102 -0.0048 94  TYR D OH  
7158  N N   . ASN D 95  ? 0.1568 0.2519 0.2190 -0.0183 0.0136  0.0466  95  ASN D N   
7159  C CA  . ASN D 95  ? 0.1509 0.2551 0.2171 -0.0201 0.0063  0.0511  95  ASN D CA  
7160  C C   . ASN D 95  ? 0.1471 0.2540 0.2204 -0.0142 0.0132  0.0564  95  ASN D C   
7161  O O   . ASN D 95  ? 0.1384 0.2481 0.2194 -0.0170 0.0107  0.0545  95  ASN D O   
7162  C CB  . ASN D 95  ? 0.1576 0.2798 0.2166 -0.0235 -0.0009 0.0571  95  ASN D CB  
7163  C CG  . ASN D 95  ? 0.1707 0.2812 0.2140 -0.0337 -0.0082 0.0509  95  ASN D CG  
7164  O OD1 . ASN D 95  ? 0.1782 0.2654 0.2128 -0.0322 -0.0092 0.0433  95  ASN D OD1 
7165  N ND2 . ASN D 95  ? 0.1803 0.3084 0.2146 -0.0419 -0.0130 0.0531  95  ASN D ND2 
7166  N N   . ALA D 96  ? 0.1617 0.2605 0.2243 -0.0037 0.0228  0.0635  96  ALA D N   
7167  C CA  . ALA D 96  ? 0.1740 0.2619 0.2287 0.0076  0.0319  0.0695  96  ALA D CA  
7168  C C   . ALA D 96  ? 0.1727 0.2402 0.2311 -0.0027 0.0407  0.0605  96  ALA D C   
7169  O O   . ALA D 96  ? 0.1666 0.2375 0.2319 -0.0007 0.0404  0.0609  96  ALA D O   
7170  C CB  . ALA D 96  ? 0.2111 0.2748 0.2345 0.0251  0.0434  0.0785  96  ALA D CB  
7171  N N   . GLU D 97  ? 0.1792 0.2335 0.2332 -0.0154 0.0489  0.0505  97  GLU D N   
7172  C CA  . GLU D 97  ? 0.1823 0.2303 0.2383 -0.0297 0.0589  0.0379  97  GLU D CA  
7173  C C   . GLU D 97  ? 0.1499 0.2278 0.2317 -0.0311 0.0467  0.0294  97  GLU D C   
7174  O O   . GLU D 97  ? 0.1489 0.2279 0.2353 -0.0354 0.0510  0.0237  97  GLU D O   
7175  C CB  . GLU D 97  ? 0.1998 0.2434 0.2448 -0.0473 0.0713  0.0256  97  GLU D CB  
7176  C CG  . GLU D 97  ? 0.2488 0.2445 0.2533 -0.0490 0.0892  0.0331  97  GLU D CG  
7177  C CD  . GLU D 97  ? 0.2740 0.2638 0.2622 -0.0752 0.1054  0.0187  97  GLU D CD  
7178  O OE1 . GLU D 97  ? 0.2484 0.2856 0.2622 -0.0898 0.1016  0.0013  97  GLU D OE1 
7179  O OE2 . GLU D 97  ? 0.3266 0.2651 0.2705 -0.0800 0.1233  0.0240  97  GLU D OE2 
7180  N N   . LEU D 98  ? 0.1328 0.2275 0.2229 -0.0262 0.0326  0.0286  98  LEU D N   
7181  C CA  . LEU D 98  ? 0.1189 0.2266 0.2168 -0.0220 0.0221  0.0220  98  LEU D CA  
7182  C C   . LEU D 98  ? 0.1127 0.2153 0.2136 -0.0195 0.0175  0.0310  98  LEU D C   
7183  O O   . LEU D 98  ? 0.1070 0.2135 0.2131 -0.0180 0.0165  0.0260  98  LEU D O   
7184  C CB  . LEU D 98  ? 0.1236 0.2305 0.2109 -0.0157 0.0113  0.0200  98  LEU D CB  
7185  C CG  . LEU D 98  ? 0.1302 0.2353 0.2069 -0.0045 0.0028  0.0125  98  LEU D CG  
7186  C CD1 . LEU D 98  ? 0.1257 0.2626 0.2105 0.0029  0.0064  -0.0037 98  LEU D CD1 
7187  C CD2 . LEU D 98  ? 0.1539 0.2352 0.2018 0.0023  -0.0056 0.0136  98  LEU D CD2 
7188  N N   . LEU D 99  ? 0.1144 0.2163 0.2116 -0.0188 0.0147  0.0428  99  LEU D N   
7189  C CA  . LEU D 99  ? 0.1097 0.2207 0.2102 -0.0188 0.0108  0.0496  99  LEU D CA  
7190  C C   . LEU D 99  ? 0.1074 0.2156 0.2138 -0.0132 0.0193  0.0507  99  LEU D C   
7191  O O   . LEU D 99  ? 0.1004 0.2132 0.2126 -0.0141 0.0167  0.0498  99  LEU D O   
7192  C CB  . LEU D 99  ? 0.1142 0.2452 0.2109 -0.0180 0.0076  0.0589  99  LEU D CB  
7193  C CG  . LEU D 99  ? 0.1112 0.2704 0.2116 -0.0222 0.0034  0.0630  99  LEU D CG  
7194  C CD1 . LEU D 99  ? 0.1172 0.2643 0.2085 -0.0404 -0.0024 0.0569  99  LEU D CD1 
7195  C CD2 . LEU D 99  ? 0.1157 0.3153 0.2137 -0.0202 0.0003  0.0685  99  LEU D CD2 
7196  N N   . VAL D 100 ? 0.1216 0.2142 0.2188 -0.0084 0.0310  0.0524  100 VAL D N   
7197  C CA  . VAL D 100 ? 0.1348 0.2096 0.2244 -0.0050 0.0424  0.0523  100 VAL D CA  
7198  C C   . VAL D 100 ? 0.1228 0.2013 0.2243 -0.0167 0.0434  0.0385  100 VAL D C   
7199  O O   . VAL D 100 ? 0.1175 0.1987 0.2245 -0.0144 0.0429  0.0383  100 VAL D O   
7200  C CB  . VAL D 100 ? 0.1742 0.2112 0.2327 -0.0012 0.0590  0.0553  100 VAL D CB  
7201  C CG1 . VAL D 100 ? 0.2030 0.2056 0.2413 -0.0062 0.0748  0.0504  100 VAL D CG1 
7202  C CG2 . VAL D 100 ? 0.1921 0.2295 0.2327 0.0223  0.0578  0.0703  100 VAL D CG2 
7203  N N   . LEU D 101 ? 0.1188 0.2055 0.2238 -0.0267 0.0442  0.0260  101 LEU D N   
7204  C CA  . LEU D 101 ? 0.1081 0.2164 0.2241 -0.0329 0.0434  0.0100  101 LEU D CA  
7205  C C   . LEU D 101 ? 0.0914 0.2115 0.2163 -0.0220 0.0301  0.0111  101 LEU D C   
7206  O O   . LEU D 101 ? 0.0874 0.2161 0.2177 -0.0218 0.0313  0.0046  101 LEU D O   
7207  C CB  . LEU D 101 ? 0.1070 0.2390 0.2249 -0.0379 0.0429  -0.0034 101 LEU D CB  
7208  C CG  . LEU D 101 ? 0.1219 0.2697 0.2359 -0.0590 0.0586  -0.0211 101 LEU D CG  
7209  C CD1 . LEU D 101 ? 0.1562 0.2586 0.2457 -0.0752 0.0778  -0.0160 101 LEU D CD1 
7210  C CD2 . LEU D 101 ? 0.1215 0.2946 0.2358 -0.0613 0.0574  -0.0299 101 LEU D CD2 
7211  N N   . MET D 102 ? 0.0893 0.2045 0.2088 -0.0153 0.0191  0.0184  102 MET D N   
7212  C CA  . MET D 102 ? 0.0913 0.2011 0.2028 -0.0085 0.0094  0.0194  102 MET D CA  
7213  C C   . MET D 102 ? 0.0865 0.1930 0.2026 -0.0115 0.0102  0.0284  102 MET D C   
7214  O O   . MET D 102 ? 0.0875 0.1924 0.2013 -0.0077 0.0080  0.0254  102 MET D O   
7215  C CB  . MET D 102 ? 0.1075 0.1995 0.1981 -0.0079 0.0015  0.0237  102 MET D CB  
7216  C CG  . MET D 102 ? 0.1182 0.2117 0.1971 0.0023  -0.0011 0.0139  102 MET D CG  
7217  S SD  . MET D 102 ? 0.1563 0.2091 0.1923 0.0060  -0.0092 0.0174  102 MET D SD  
7218  C CE  . MET D 102 ? 0.1484 0.2032 0.1935 -0.0172 -0.0079 0.0298  102 MET D CE  
7219  N N   . GLU D 103 ? 0.0838 0.1936 0.2038 -0.0148 0.0133  0.0388  103 GLU D N   
7220  C CA  . GLU D 103 ? 0.0806 0.2000 0.2044 -0.0142 0.0137  0.0468  103 GLU D CA  
7221  C C   . GLU D 103 ? 0.0792 0.1951 0.2088 -0.0078 0.0226  0.0454  103 GLU D C   
7222  O O   . GLU D 103 ? 0.0762 0.1991 0.2091 -0.0053 0.0220  0.0482  103 GLU D O   
7223  C CB  . GLU D 103 ? 0.0833 0.2220 0.2055 -0.0139 0.0126  0.0566  103 GLU D CB  
7224  C CG  . GLU D 103 ? 0.0900 0.2349 0.2021 -0.0287 0.0046  0.0565  103 GLU D CG  
7225  C CD  . GLU D 103 ? 0.1001 0.2405 0.2004 -0.0432 0.0013  0.0544  103 GLU D CD  
7226  O OE1 . GLU D 103 ? 0.0942 0.2411 0.2017 -0.0397 0.0035  0.0552  103 GLU D OE1 
7227  O OE2 . GLU D 103 ? 0.1223 0.2455 0.1987 -0.0596 -0.0019 0.0517  103 GLU D OE2 
7228  N N   . ASN D 104 ? 0.0877 0.1896 0.2131 -0.0083 0.0323  0.0400  104 ASN D N   
7229  C CA  . ASN D 104 ? 0.0984 0.1869 0.2192 -0.0096 0.0433  0.0343  104 ASN D CA  
7230  C C   . ASN D 104 ? 0.0843 0.1878 0.2170 -0.0131 0.0386  0.0234  104 ASN D C   
7231  O O   . ASN D 104 ? 0.0860 0.1869 0.2191 -0.0109 0.0419  0.0231  104 ASN D O   
7232  C CB  . ASN D 104 ? 0.1218 0.1891 0.2269 -0.0207 0.0575  0.0257  104 ASN D CB  
7233  C CG  . ASN D 104 ? 0.1560 0.1881 0.2322 -0.0120 0.0686  0.0372  104 ASN D CG  
7234  O OD1 . ASN D 104 ? 0.1606 0.1929 0.2305 0.0074  0.0657  0.0506  104 ASN D OD1 
7235  N ND2 . ASN D 104 ? 0.1865 0.1902 0.2393 -0.0249 0.0825  0.0309  104 ASN D ND2 
7236  N N   . GLU D 105 ? 0.2646 0.2910 0.1423 -0.0004 0.0126  -0.0284 105 GLU D N   
7237  C CA  . GLU D 105 ? 0.2407 0.2986 0.1453 0.0178  0.0149  -0.0403 105 GLU D CA  
7238  C C   . GLU D 105 ? 0.2308 0.2446 0.1393 0.0241  -0.0050 -0.0380 105 GLU D C   
7239  O O   . GLU D 105 ? 0.2013 0.2309 0.1394 0.0272  -0.0057 -0.0386 105 GLU D O   
7240  C CB  . GLU D 105 ? 0.2738 0.3575 0.1536 0.0506  0.0242  -0.0583 105 GLU D CB  
7241  C CG  . GLU D 105 ? 0.2547 0.3903 0.1637 0.0747  0.0284  -0.0709 105 GLU D CG  
7242  C CD  . GLU D 105 ? 0.2817 0.4810 0.1810 0.1063  0.0450  -0.0884 105 GLU D CD  
7243  O OE1 . GLU D 105 ? 0.3343 0.4980 0.1823 0.1339  0.0436  -0.0969 105 GLU D OE1 
7244  O OE2 . GLU D 105 ? 0.2561 0.5452 0.1980 0.1034  0.0591  -0.0952 105 GLU D OE2 
7245  N N   . ARG D 106 ? 0.2622 0.2219 0.1373 0.0229  -0.0211 -0.0359 106 ARG D N   
7246  C CA  . ARG D 106 ? 0.2636 0.1825 0.1391 0.0185  -0.0381 -0.0325 106 ARG D CA  
7247  C C   . ARG D 106 ? 0.2182 0.1517 0.1371 -0.0036 -0.0419 -0.0172 106 ARG D C   
7248  O O   . ARG D 106 ? 0.2024 0.1302 0.1396 -0.0057 -0.0458 -0.0140 106 ARG D O   
7249  C CB  . ARG D 106 ? 0.3193 0.1812 0.1469 0.0138  -0.0555 -0.0360 106 ARG D CB  
7250  C CG  . ARG D 106 ? 0.3831 0.2068 0.1527 0.0422  -0.0548 -0.0535 106 ARG D CG  
7251  C CD  . ARG D 106 ? 0.4483 0.1925 0.1674 0.0320  -0.0756 -0.0580 106 ARG D CD  
7252  N NE  . ARG D 106 ? 0.4703 0.1740 0.1766 0.0404  -0.0781 -0.0596 106 ARG D NE  
7253  C CZ  . ARG D 106 ? 0.5077 0.1540 0.1934 0.0137  -0.0927 -0.0552 106 ARG D CZ  
7254  N NH1 . ARG D 106 ? 0.5203 0.1560 0.2058 -0.0244 -0.1088 -0.0508 106 ARG D NH1 
7255  N NH2 . ARG D 106 ? 0.5394 0.1409 0.2024 0.0235  -0.0916 -0.0549 106 ARG D NH2 
7256  N N   . THR D 107 ? 0.2068 0.1547 0.1345 -0.0166 -0.0395 -0.0075 107 THR D N   
7257  C CA  . THR D 107 ? 0.1767 0.1342 0.1367 -0.0283 -0.0427 0.0059  107 THR D CA  
7258  C C   . THR D 107 ? 0.1422 0.1234 0.1335 -0.0266 -0.0301 0.0050  107 THR D C   
7259  O O   . THR D 107 ? 0.1217 0.1047 0.1367 -0.0280 -0.0338 0.0106  107 THR D O   
7260  C CB  . THR D 107 ? 0.1927 0.1457 0.1394 -0.0352 -0.0434 0.0169  107 THR D CB  
7261  O OG1 . THR D 107 ? 0.2256 0.1600 0.1434 -0.0361 -0.0600 0.0175  107 THR D OG1 
7262  C CG2 . THR D 107 ? 0.1757 0.1323 0.1473 -0.0368 -0.0467 0.0292  107 THR D CG2 
7263  N N   . LEU D 108 ? 0.1393 0.1448 0.1305 -0.0247 -0.0153 -0.0029 108 LEU D N   
7264  C CA  . LEU D 108 ? 0.1137 0.1462 0.1321 -0.0268 -0.0064 -0.0068 108 LEU D CA  
7265  C C   . LEU D 108 ? 0.1009 0.1368 0.1288 -0.0095 -0.0119 -0.0140 108 LEU D C   
7266  O O   . LEU D 108 ? 0.0819 0.1227 0.1290 -0.0101 -0.0121 -0.0124 108 LEU D O   
7267  C CB  . LEU D 108 ? 0.1197 0.1924 0.1392 -0.0351 0.0098  -0.0154 108 LEU D CB  
7268  C CG  . LEU D 108 ? 0.1474 0.2084 0.1458 -0.0572 0.0197  -0.0065 108 LEU D CG  
7269  C CD1 . LEU D 108 ? 0.1557 0.2691 0.1606 -0.0738 0.0394  -0.0159 108 LEU D CD1 
7270  C CD2 . LEU D 108 ? 0.1559 0.1755 0.1498 -0.0705 0.0157  0.0077  108 LEU D CD2 
7271  N N   . ASP D 109 ? 0.1231 0.1467 0.1272 0.0081  -0.0164 -0.0219 109 ASP D N   
7272  C CA  . ASP D 109 ? 0.1329 0.1381 0.1275 0.0268  -0.0227 -0.0263 109 ASP D CA  
7273  C C   . ASP D 109 ? 0.1348 0.1012 0.1290 0.0136  -0.0319 -0.0142 109 ASP D C   
7274  O O   . ASP D 109 ? 0.1370 0.0916 0.1305 0.0199  -0.0329 -0.0125 109 ASP D O   
7275  C CB  . ASP D 109 ? 0.1774 0.1625 0.1310 0.0530  -0.0253 -0.0382 109 ASP D CB  
7276  C CG  . ASP D 109 ? 0.1751 0.2205 0.1363 0.0739  -0.0140 -0.0525 109 ASP D CG  
7277  O OD1 . ASP D 109 ? 0.1429 0.2426 0.1398 0.0708  -0.0080 -0.0556 109 ASP D OD1 
7278  O OD2 . ASP D 109 ? 0.2107 0.2534 0.1411 0.0932  -0.0114 -0.0621 109 ASP D OD2 
7279  N N   . PHE D 110 ? 0.1382 0.0915 0.1322 -0.0047 -0.0384 -0.0058 110 PHE D N   
7280  C CA  . PHE D 110 ? 0.1368 0.0781 0.1420 -0.0215 -0.0461 0.0052  110 PHE D CA  
7281  C C   . PHE D 110 ? 0.1010 0.0705 0.1419 -0.0223 -0.0386 0.0124  110 PHE D C   
7282  O O   . PHE D 110 ? 0.1011 0.0667 0.1484 -0.0251 -0.0372 0.0173  110 PHE D O   
7283  C CB  . PHE D 110 ? 0.1470 0.0882 0.1499 -0.0366 -0.0569 0.0104  110 PHE D CB  
7284  C CG  . PHE D 110 ? 0.1444 0.0979 0.1687 -0.0550 -0.0659 0.0204  110 PHE D CG  
7285  C CD1 . PHE D 110 ? 0.1713 0.1027 0.1842 -0.0711 -0.0703 0.0210  110 PHE D CD1 
7286  C CD2 . PHE D 110 ? 0.1254 0.1136 0.1770 -0.0561 -0.0700 0.0292  110 PHE D CD2 
7287  C CE1 . PHE D 110 ? 0.1700 0.1306 0.2094 -0.0941 -0.0764 0.0297  110 PHE D CE1 
7288  C CE2 . PHE D 110 ? 0.1227 0.1430 0.2012 -0.0689 -0.0783 0.0369  110 PHE D CE2 
7289  C CZ  . PHE D 110 ? 0.1409 0.1557 0.2185 -0.0911 -0.0806 0.0368  110 PHE D CZ  
7290  N N   . HIS D 111 ? 0.0816 0.0721 0.1372 -0.0208 -0.0326 0.0129  111 HIS D N   
7291  C CA  . HIS D 111 ? 0.0622 0.0665 0.1390 -0.0187 -0.0258 0.0166  111 HIS D CA  
7292  C C   . HIS D 111 ? 0.0561 0.0650 0.1335 -0.0091 -0.0204 0.0090  111 HIS D C   
7293  O O   . HIS D 111 ? 0.0501 0.0611 0.1370 -0.0059 -0.0172 0.0128  111 HIS D O   
7294  C CB  . HIS D 111 ? 0.0649 0.0707 0.1395 -0.0226 -0.0205 0.0167  111 HIS D CB  
7295  C CG  . HIS D 111 ? 0.0801 0.0753 0.1481 -0.0247 -0.0270 0.0273  111 HIS D CG  
7296  N ND1 . HIS D 111 ? 0.0795 0.0808 0.1612 -0.0172 -0.0326 0.0367  111 HIS D ND1 
7297  C CD2 . HIS D 111 ? 0.1021 0.0851 0.1482 -0.0296 -0.0290 0.0301  111 HIS D CD2 
7298  C CE1 . HIS D 111 ? 0.1003 0.0947 0.1696 -0.0142 -0.0409 0.0443  111 HIS D CE1 
7299  N NE2 . HIS D 111 ? 0.1164 0.0935 0.1603 -0.0228 -0.0388 0.0412  111 HIS D NE2 
7300  N N   . ASP D 112 ? 0.0622 0.0777 0.1275 -0.0006 -0.0195 -0.0021 112 ASP D N   
7301  C CA  . ASP D 112 ? 0.0634 0.0892 0.1252 0.0149  -0.0184 -0.0108 112 ASP D CA  
7302  C C   . ASP D 112 ? 0.0849 0.0768 0.1270 0.0227  -0.0220 -0.0043 112 ASP D C   
7303  O O   . ASP D 112 ? 0.0868 0.0774 0.1271 0.0300  -0.0198 -0.0032 112 ASP D O   
7304  C CB  . ASP D 112 ? 0.0722 0.1232 0.1254 0.0290  -0.0182 -0.0247 112 ASP D CB  
7305  C CG  . ASP D 112 ? 0.0728 0.1543 0.1284 0.0481  -0.0197 -0.0362 112 ASP D CG  
7306  O OD1 . ASP D 112 ? 0.0654 0.1454 0.1278 0.0461  -0.0203 -0.0342 112 ASP D OD1 
7307  O OD2 . ASP D 112 ? 0.0852 0.1965 0.1339 0.0689  -0.0210 -0.0485 112 ASP D OD2 
7308  N N   . SER D 113 ? 0.1108 0.0700 0.1316 0.0172  -0.0271 0.0000  113 SER D N   
7309  C CA  . SER D 113 ? 0.1475 0.0630 0.1410 0.0124  -0.0293 0.0079  113 SER D CA  
7310  C C   . SER D 113 ? 0.1324 0.0614 0.1501 -0.0052 -0.0231 0.0207  113 SER D C   
7311  O O   . SER D 113 ? 0.1553 0.0646 0.1558 -0.0042 -0.0181 0.0265  113 SER D O   
7312  C CB  . SER D 113 ? 0.1856 0.0614 0.1501 -0.0002 -0.0376 0.0084  113 SER D CB  
7313  O OG  . SER D 113 ? 0.2271 0.0606 0.1672 -0.0201 -0.0388 0.0180  113 SER D OG  
7314  N N   . ASN D 114 ? 0.1021 0.0644 0.1546 -0.0177 -0.0228 0.0254  114 ASN D N   
7315  C CA  . ASN D 114 ? 0.0903 0.0788 0.1691 -0.0276 -0.0164 0.0361  114 ASN D CA  
7316  C C   . ASN D 114 ? 0.0794 0.0794 0.1639 -0.0119 -0.0061 0.0351  114 ASN D C   
7317  O O   . ASN D 114 ? 0.0872 0.0964 0.1758 -0.0152 0.0029  0.0431  114 ASN D O   
7318  C CB  . ASN D 114 ? 0.0691 0.0905 0.1772 -0.0323 -0.0212 0.0397  114 ASN D CB  
7319  C CG  . ASN D 114 ? 0.0856 0.1034 0.1890 -0.0512 -0.0336 0.0415  114 ASN D CG  
7320  O OD1 . ASN D 114 ? 0.1159 0.1114 0.2009 -0.0700 -0.0365 0.0432  114 ASN D OD1 
7321  N ND2 . ASN D 114 ? 0.0766 0.1089 0.1887 -0.0481 -0.0417 0.0413  114 ASN D ND2 
7322  N N   . VAL D 115 ? 0.0676 0.0698 0.1505 0.0021  -0.0070 0.0244  115 VAL D N   
7323  C CA  . VAL D 115 ? 0.0663 0.0742 0.1473 0.0151  -0.0009 0.0193  115 VAL D CA  
7324  C C   . VAL D 115 ? 0.0927 0.0811 0.1453 0.0250  0.0003  0.0190  115 VAL D C   
7325  O O   . VAL D 115 ? 0.1043 0.0916 0.1487 0.0313  0.0080  0.0225  115 VAL D O   
7326  C CB  . VAL D 115 ? 0.0565 0.0734 0.1397 0.0181  -0.0043 0.0057  115 VAL D CB  
7327  C CG1 . VAL D 115 ? 0.0648 0.0847 0.1388 0.0279  -0.0024 -0.0033 115 VAL D CG1 
7328  C CG2 . VAL D 115 ? 0.0502 0.0683 0.1456 0.0092  -0.0037 0.0083  115 VAL D CG2 
7329  N N   . LYS D 116 ? 0.1124 0.0805 0.1420 0.0306  -0.0071 0.0148  116 LYS D N   
7330  C CA  . LYS D 116 ? 0.1537 0.0903 0.1422 0.0478  -0.0089 0.0147  116 LYS D CA  
7331  C C   . LYS D 116 ? 0.1914 0.0919 0.1556 0.0336  -0.0004 0.0310  116 LYS D C   
7332  O O   . LYS D 116 ? 0.2242 0.1034 0.1576 0.0436  0.0048  0.0358  116 LYS D O   
7333  C CB  . LYS D 116 ? 0.1782 0.0956 0.1406 0.0639  -0.0192 0.0062  116 LYS D CB  
7334  C CG  . LYS D 116 ? 0.2030 0.1231 0.1387 0.0980  -0.0263 -0.0043 116 LYS D CG  
7335  C CD  . LYS D 116 ? 0.2763 0.1274 0.1466 0.1177  -0.0299 0.0023  116 LYS D CD  
7336  C CE  . LYS D 116 ? 0.3029 0.1651 0.1466 0.1588  -0.0394 -0.0077 116 LYS D CE  
7337  N NZ  . LYS D 116 ? 0.3813 0.1803 0.1569 0.1938  -0.0483 -0.0079 116 LYS D NZ  
7338  N N   . ASN D 117 ? 0.1933 0.0894 0.1688 0.0071  0.0007  0.0394  117 ASN D N   
7339  C CA  . ASN D 117 ? 0.2327 0.1060 0.1910 -0.0184 0.0102  0.0548  117 ASN D CA  
7340  C C   . ASN D 117 ? 0.2134 0.1310 0.2002 -0.0229 0.0259  0.0627  117 ASN D C   
7341  O O   . ASN D 117 ? 0.2538 0.1540 0.2151 -0.0340 0.0390  0.0745  117 ASN D O   
7342  C CB  . ASN D 117 ? 0.2404 0.1108 0.2085 -0.0501 0.0044  0.0586  117 ASN D CB  
7343  C CG  . ASN D 117 ? 0.2832 0.0924 0.2048 -0.0445 -0.0089 0.0509  117 ASN D CG  
7344  O OD1 . ASN D 117 ? 0.3240 0.0839 0.1966 -0.0183 -0.0116 0.0467  117 ASN D OD1 
7345  N ND2 . ASN D 117 ? 0.2813 0.0934 0.2132 -0.0643 -0.0183 0.0481  117 ASN D ND2 
7346  N N   . LEU D 118 ? 0.1633 0.1314 0.1946 -0.0126 0.0258  0.0564  118 LEU D N   
7347  C CA  . LEU D 118 ? 0.1520 0.1586 0.2041 -0.0054 0.0400  0.0602  118 LEU D CA  
7348  C C   . LEU D 118 ? 0.1736 0.1580 0.1918 0.0173  0.0450  0.0554  118 LEU D C   
7349  O O   . LEU D 118 ? 0.1947 0.1874 0.2024 0.0195  0.0608  0.0629  118 LEU D O   
7350  C CB  . LEU D 118 ? 0.1121 0.1562 0.2028 0.0056  0.0359  0.0534  118 LEU D CB  
7351  C CG  . LEU D 118 ? 0.1092 0.1859 0.2145 0.0233  0.0488  0.0541  118 LEU D CG  
7352  C CD1 . LEU D 118 ? 0.1227 0.2415 0.2442 0.0108  0.0653  0.0678  118 LEU D CD1 
7353  C CD2 . LEU D 118 ? 0.0894 0.1811 0.2171 0.0360  0.0414  0.0486  118 LEU D CD2 
7354  N N   . TYR D 119 ? 0.1721 0.1358 0.1730 0.0344  0.0314  0.0423  119 TYR D N   
7355  C CA  . TYR D 119 ? 0.1963 0.1450 0.1640 0.0568  0.0304  0.0351  119 TYR D CA  
7356  C C   . TYR D 119 ? 0.2552 0.1596 0.1708 0.0582  0.0363  0.0474  119 TYR D C   
7357  O O   . TYR D 119 ? 0.2858 0.1813 0.1725 0.0692  0.0457  0.0509  119 TYR D O   
7358  C CB  . TYR D 119 ? 0.1827 0.1364 0.1500 0.0718  0.0126  0.0172  119 TYR D CB  
7359  C CG  . TYR D 119 ? 0.2120 0.1588 0.1445 0.0958  0.0058  0.0077  119 TYR D CG  
7360  C CD1 . TYR D 119 ? 0.2106 0.1735 0.1443 0.1020  0.0069  -0.0024 119 TYR D CD1 
7361  C CD2 . TYR D 119 ? 0.2521 0.1712 0.1428 0.1156  -0.0037 0.0079  119 TYR D CD2 
7362  C CE1 . TYR D 119 ? 0.2420 0.2025 0.1417 0.1229  -0.0026 -0.0130 119 TYR D CE1 
7363  C CE2 . TYR D 119 ? 0.2842 0.2027 0.1407 0.1425  -0.0135 -0.0010 119 TYR D CE2 
7364  C CZ  . TYR D 119 ? 0.2757 0.2195 0.1397 0.1439  -0.0136 -0.0119 119 TYR D CZ  
7365  O OH  . TYR D 119 ? 0.3116 0.2588 0.1398 0.1694  -0.0266 -0.0229 119 TYR D OH  
7366  N N   . ASP D 120 ? 0.2839 0.1503 0.1771 0.0478  0.0310  0.0539  120 ASP D N   
7367  C CA  . ASP D 120 ? 0.3612 0.1630 0.1888 0.0464  0.0364  0.0674  120 ASP D CA  
7368  C C   . ASP D 120 ? 0.3861 0.1924 0.2123 0.0155  0.0600  0.0861  120 ASP D C   
7369  O O   . ASP D 120 ? 0.4473 0.2150 0.2204 0.0175  0.0719  0.0976  120 ASP D O   
7370  C CB  . ASP D 120 ? 0.4008 0.1468 0.1951 0.0413  0.0249  0.0684  120 ASP D CB  
7371  C CG  . ASP D 120 ? 0.4047 0.1412 0.1797 0.0825  0.0049  0.0516  120 ASP D CG  
7372  O OD1 . ASP D 120 ? 0.4122 0.1595 0.1708 0.1145  -0.0009 0.0441  120 ASP D OD1 
7373  O OD2 . ASP D 120 ? 0.4056 0.1288 0.1806 0.0837  -0.0052 0.0450  120 ASP D OD2 
7374  N N   . LYS D 121 ? 0.3438 0.2033 0.2274 -0.0118 0.0670  0.0891  121 LYS D N   
7375  C CA  . LYS D 121 ? 0.3586 0.2527 0.2579 -0.0419 0.0904  0.1047  121 LYS D CA  
7376  C C   . LYS D 121 ? 0.3670 0.2826 0.2558 -0.0204 0.1077  0.1064  121 LYS D C   
7377  O O   . LYS D 121 ? 0.4215 0.3241 0.2760 -0.0361 0.1288  0.1218  121 LYS D O   
7378  C CB  . LYS D 121 ? 0.2998 0.2698 0.2727 -0.0584 0.0894  0.1021  121 LYS D CB  
7379  C CG  . LYS D 121 ? 0.3103 0.3413 0.3137 -0.0914 0.1110  0.1161  121 LYS D CG  
7380  C CD  . LYS D 121 ? 0.2570 0.3630 0.3298 -0.1003 0.1021  0.1114  121 LYS D CD  
7381  C CE  . LYS D 121 ? 0.2694 0.4533 0.3806 -0.1388 0.1192  0.1238  121 LYS D CE  
7382  N NZ  . LYS D 121 ? 0.2475 0.5159 0.3967 -0.1125 0.1395  0.1247  121 LYS D NZ  
7383  N N   . VAL D 122 ? 0.3228 0.2656 0.2344 0.0128  0.0992  0.0902  122 VAL D N   
7384  C CA  . VAL D 122 ? 0.3366 0.2911 0.2306 0.0380  0.1114  0.0867  122 VAL D CA  
7385  C C   . VAL D 122 ? 0.3996 0.2906 0.2194 0.0545  0.1084  0.0890  122 VAL D C   
7386  O O   . VAL D 122 ? 0.4473 0.3288 0.2283 0.0584  0.1275  0.0985  122 VAL D O   
7387  C CB  . VAL D 122 ? 0.2892 0.2707 0.2142 0.0645  0.0990  0.0663  122 VAL D CB  
7388  C CG1 . VAL D 122 ? 0.3175 0.2946 0.2096 0.0919  0.1073  0.0584  122 VAL D CG1 
7389  C CG2 . VAL D 122 ? 0.2456 0.2819 0.2303 0.0566  0.1033  0.0666  122 VAL D CG2 
7390  N N   . ARG D 123 ? 0.4057 0.2566 0.2030 0.0677  0.0847  0.0802  123 ARG D N   
7391  C CA  . ARG D 123 ? 0.4707 0.2636 0.1951 0.0928  0.0759  0.0808  123 ARG D CA  
7392  C C   . ARG D 123 ? 0.5561 0.2904 0.2165 0.0739  0.0956  0.1055  123 ARG D C   
7393  O O   . ARG D 123 ? 0.6184 0.3184 0.2167 0.0909  0.1035  0.1124  123 ARG D O   
7394  C CB  . ARG D 123 ? 0.4666 0.2364 0.1830 0.1104  0.0488  0.0690  123 ARG D CB  
7395  C CG  . ARG D 123 ? 0.5268 0.2549 0.1755 0.1500  0.0327  0.0640  123 ARG D CG  
7396  C CD  . ARG D 123 ? 0.5257 0.2445 0.1710 0.1725  0.0079  0.0518  123 ARG D CD  
7397  N NE  . ARG D 123 ? 0.5462 0.2196 0.1821 0.1508  0.0115  0.0631  123 ARG D NE  
7398  C CZ  . ARG D 123 ? 0.6381 0.2219 0.1984 0.1447  0.0186  0.0819  123 ARG D CZ  
7399  N NH1 . ARG D 123 ? 0.7202 0.2477 0.2043 0.1602  0.0249  0.0947  123 ARG D NH1 
7400  N NH2 . ARG D 123 ? 0.6594 0.2009 0.2115 0.1204  0.0193  0.0881  123 ARG D NH2 
7401  N N   . LEU D 124 ? 0.5683 0.2877 0.2384 0.0354  0.1035  0.1186  124 LEU D N   
7402  C CA  . LEU D 124 ? 0.6632 0.3172 0.2679 0.0034  0.1229  0.1431  124 LEU D CA  
7403  C C   . LEU D 124 ? 0.6837 0.3779 0.2918 -0.0190 0.1570  0.1582  124 LEU D C   
7404  O O   . LEU D 124 ? 0.7775 0.4125 0.3127 -0.0372 0.1764  0.1786  124 LEU D O   
7405  C CB  . LEU D 124 ? 0.6737 0.3043 0.2896 -0.0395 0.1200  0.1496  124 LEU D CB  
7406  C CG  . LEU D 124 ? 0.6931 0.2574 0.2751 -0.0161 0.0912  0.1387  124 LEU D CG  
7407  C CD1 . LEU D 124 ? 0.6775 0.2424 0.2914 -0.0545 0.0847  0.1373  124 LEU D CD1 
7408  C CD2 . LEU D 124 ? 0.8160 0.2605 0.2817 0.0030  0.0879  0.1503  124 LEU D CD2 
7409  N N   . GLN D 125 ? 0.6070 0.3981 0.2929 -0.0159 0.1657  0.1486  125 GLN D N   
7410  C CA  . GLN D 125 ? 0.6220 0.4672 0.3162 -0.0245 0.1986  0.1587  125 GLN D CA  
7411  C C   . GLN D 125 ? 0.6624 0.4786 0.2973 0.0167  0.2021  0.1547  125 GLN D C   
7412  O O   . GLN D 125 ? 0.7386 0.5284 0.3141 0.0079  0.2275  0.1721  125 GLN D O   
7413  C CB  . GLN D 125 ? 0.5374 0.4890 0.3246 -0.0205 0.2036  0.1471  125 GLN D CB  
7414  C CG  . GLN D 125 ? 0.5110 0.5180 0.3589 -0.0659 0.2089  0.1550  125 GLN D CG  
7415  C CD  . GLN D 125 ? 0.4359 0.5441 0.3678 -0.0493 0.2093  0.1430  125 GLN D CD  
7416  O OE1 . GLN D 125 ? 0.4384 0.6144 0.3906 -0.0376 0.2339  0.1451  125 GLN D OE1 
7417  N NE2 . GLN D 125 ? 0.3790 0.4946 0.3532 -0.0438 0.1828  0.1304  125 GLN D NE2 
7418  N N   . LEU D 126 ? 0.6177 0.4396 0.2660 0.0584  0.1765  0.1313  126 LEU D N   
7419  C CA  . LEU D 126 ? 0.6509 0.4559 0.2498 0.0978  0.1743  0.1215  126 LEU D CA  
7420  C C   . LEU D 126 ? 0.7452 0.4620 0.2458 0.1110  0.1678  0.1328  126 LEU D C   
7421  O O   . LEU D 126 ? 0.8081 0.5031 0.2470 0.1280  0.1815  0.1385  126 LEU D O   
7422  C CB  . LEU D 126 ? 0.5884 0.4181 0.2235 0.1290  0.1450  0.0922  126 LEU D CB  
7423  C CG  . LEU D 126 ? 0.5143 0.4120 0.2284 0.1255  0.1485  0.0798  126 LEU D CG  
7424  C CD1 . LEU D 126 ? 0.4849 0.3850 0.2081 0.1520  0.1227  0.0520  126 LEU D CD1 
7425  C CD2 . LEU D 126 ? 0.5302 0.4734 0.2527 0.1248  0.1829  0.0884  126 LEU D CD2 
7426  N N   . ARG D 127 ? 0.7663 0.4277 0.2444 0.1075  0.1472  0.1362  127 ARG D N   
7427  C CA  . ARG D 127 ? 0.8712 0.4367 0.2451 0.1282  0.1379  0.1476  127 ARG D CA  
7428  C C   . ARG D 127 ? 0.8903 0.4563 0.2248 0.1801  0.1186  0.1305  127 ARG D C   
7429  O O   . ARG D 127 ? 0.8176 0.4388 0.2070 0.2008  0.0946  0.1039  127 ARG D O   
7430  C CB  . ARG D 127 ? 0.9723 0.4775 0.2766 0.0910  0.1726  0.1802  127 ARG D CB  
7431  C CG  . ARG D 127 ? 0.9965 0.4582 0.3012 0.0445  0.1765  0.1951  127 ARG D CG  
7432  C CD  . ARG D 127 ? 1.0258 0.5092 0.3422 -0.0199 0.2168  0.2185  127 ARG D CD  
7433  N NE  . ARG D 127 ? 1.1416 0.5712 0.3679 -0.0388 0.2502  0.2450  127 ARG D NE  
7434  C CZ  . ARG D 127 ? 1.2686 0.5767 0.3694 -0.0201 0.2479  0.2607  127 ARG D CZ  
7435  N NH1 . ARG D 127 ? 1.3038 0.5288 0.3477 0.0259  0.2113  0.2518  127 ARG D NH1 
7436  N NH2 . ARG D 127 ? 1.3717 0.6419 0.3973 -0.0460 0.2843  0.2867  127 ARG D NH2 
7437  N N   . ASP D 128 ? 0.9929 0.4985 0.2308 0.1977  0.1281  0.1447  128 ASP D N   
7438  C CA  . ASP D 128 ? 1.0210 0.5266 0.2145 0.2474  0.1055  0.1273  128 ASP D CA  
7439  C C   . ASP D 128 ? 1.0017 0.5613 0.2117 0.2503  0.1237  0.1171  128 ASP D C   
7440  O O   . ASP D 128 ? 1.0489 0.5966 0.2027 0.2858  0.1109  0.1061  128 ASP D O   
7441  C CB  . ASP D 128 ? 1.1552 0.5590 0.2213 0.2763  0.0998  0.1459  128 ASP D CB  
7442  C CG  . ASP D 128 ? 1.2509 0.5985 0.2432 0.2478  0.1430  0.1784  128 ASP D CG  
7443  O OD1 . ASP D 128 ? 1.2143 0.6000 0.2609 0.1977  0.1770  0.1902  128 ASP D OD1 
7444  O OD2 . ASP D 128 ? 1.3689 0.6390 0.2476 0.2751  0.1431  0.1925  128 ASP D OD2 
7445  N N   . ASN D 129 ? 0.9408 0.5590 0.2227 0.2174  0.1515  0.1191  129 ASN D N   
7446  C CA  . ASN D 129 ? 0.9242 0.5936 0.2238 0.2266  0.1691  0.1067  129 ASN D CA  
7447  C C   . ASN D 129 ? 0.8460 0.5655 0.2075 0.2440  0.1412  0.0718  129 ASN D C   
7448  O O   . ASN D 129 ? 0.8435 0.5911 0.2102 0.2560  0.1520  0.0578  129 ASN D O   
7449  C CB  . ASN D 129 ? 0.9079 0.6244 0.2515 0.1910  0.2130  0.1246  129 ASN D CB  
7450  C CG  . ASN D 129 ? 1.0089 0.6868 0.2764 0.1728  0.2508  0.1560  129 ASN D CG  
7451  O OD1 . ASN D 129 ? 1.0974 0.6925 0.2742 0.1808  0.2438  0.1702  129 ASN D OD1 
7452  N ND2 . ASN D 129 ? 1.0047 0.7445 0.3055 0.1493  0.2921  0.1674  129 ASN D ND2 
7453  N N   . ALA D 130 ? 0.7935 0.5195 0.1946 0.2448  0.1074  0.0579  130 ALA D N   
7454  C CA  . ALA D 130 ? 0.7324 0.4991 0.1840 0.2530  0.0804  0.0259  130 ALA D CA  
7455  C C   . ALA D 130 ? 0.7226 0.4878 0.1732 0.2672  0.0404  0.0110  130 ALA D C   
7456  O O   . ALA D 130 ? 0.7465 0.4813 0.1735 0.2714  0.0343  0.0260  130 ALA D O   
7457  C CB  . ALA D 130 ? 0.6521 0.4627 0.1901 0.2267  0.0910  0.0240  130 ALA D CB  
7458  N N   . LYS D 131 ? 0.6963 0.4948 0.1693 0.2743  0.0136  -0.0191 131 LYS D N   
7459  C CA  . LYS D 131 ? 0.6796 0.5044 0.1672 0.2852  -0.0240 -0.0371 131 LYS D CA  
7460  C C   . LYS D 131 ? 0.5974 0.4595 0.1670 0.2594  -0.0282 -0.0409 131 LYS D C   
7461  O O   . LYS D 131 ? 0.5511 0.4352 0.1695 0.2359  -0.0211 -0.0506 131 LYS D O   
7462  C CB  . LYS D 131 ? 0.6971 0.5501 0.1724 0.2948  -0.0514 -0.0697 131 LYS D CB  
7463  C CG  . LYS D 131 ? 0.7858 0.6056 0.1731 0.3248  -0.0552 -0.0717 131 LYS D CG  
7464  C CD  . LYS D 131 ? 0.8038 0.6497 0.1830 0.3238  -0.0812 -0.1077 131 LYS D CD  
7465  C CE  . LYS D 131 ? 0.8914 0.7236 0.1863 0.3595  -0.1043 -0.1174 131 LYS D CE  
7466  N NZ  . LYS D 131 ? 0.9019 0.7687 0.1921 0.3857  -0.1392 -0.1210 131 LYS D NZ  
7467  N N   . GLU D 132 ? 0.5899 0.4520 0.1655 0.2676  -0.0397 -0.0334 132 GLU D N   
7468  C CA  . GLU D 132 ? 0.5204 0.4213 0.1660 0.2482  -0.0466 -0.0399 132 GLU D CA  
7469  C C   . GLU D 132 ? 0.4962 0.4615 0.1738 0.2492  -0.0761 -0.0711 132 GLU D C   
7470  O O   . GLU D 132 ? 0.5191 0.5119 0.1805 0.2768  -0.1011 -0.0817 132 GLU D O   
7471  C CB  . GLU D 132 ? 0.5362 0.4089 0.1663 0.2609  -0.0484 -0.0234 132 GLU D CB  
7472  C CG  . GLU D 132 ? 0.4713 0.3736 0.1665 0.2394  -0.0487 -0.0259 132 GLU D CG  
7473  C CD  . GLU D 132 ? 0.5005 0.3556 0.1687 0.2492  -0.0463 -0.0086 132 GLU D CD  
7474  O OE1 . GLU D 132 ? 0.5760 0.3803 0.1730 0.2814  -0.0532 0.0003  132 GLU D OE1 
7475  O OE2 . GLU D 132 ? 0.4590 0.3188 0.1688 0.2254  -0.0386 -0.0042 132 GLU D OE2 
7476  N N   . LEU D 133 ? 0.4589 0.4481 0.1780 0.2189  -0.0731 -0.0860 133 LEU D N   
7477  C CA  . LEU D 133 ? 0.4490 0.4944 0.1930 0.2060  -0.0982 -0.1165 133 LEU D CA  
7478  C C   . LEU D 133 ? 0.4063 0.5162 0.2030 0.1992  -0.1133 -0.1258 133 LEU D C   
7479  O O   . LEU D 133 ? 0.4113 0.5860 0.2219 0.1985  -0.1383 -0.1499 133 LEU D O   
7480  C CB  . LEU D 133 ? 0.4412 0.4714 0.1996 0.1724  -0.0887 -0.1280 133 LEU D CB  
7481  C CG  . LEU D 133 ? 0.5015 0.4990 0.2047 0.1794  -0.0914 -0.1414 133 LEU D CG  
7482  C CD1 . LEU D 133 ? 0.5486 0.5083 0.1915 0.2160  -0.0812 -0.1241 133 LEU D CD1 
7483  C CD2 . LEU D 133 ? 0.5048 0.4603 0.2101 0.1573  -0.0730 -0.1440 133 LEU D CD2 
7484  N N   . GLY D 134 ? 0.3682 0.4671 0.1940 0.1932  -0.0982 -0.1084 134 GLY D N   
7485  C CA  . GLY D 134 ? 0.3332 0.4898 0.2035 0.1912  -0.1080 -0.1157 134 GLY D CA  
7486  C C   . GLY D 134 ? 0.2846 0.4637 0.2096 0.1474  -0.0981 -0.1207 134 GLY D C   
7487  O O   . GLY D 134 ? 0.2562 0.4856 0.2185 0.1419  -0.1019 -0.1262 134 GLY D O   
7488  N N   . ASN D 135 ? 0.2840 0.4221 0.2073 0.1204  -0.0844 -0.1181 135 ASN D N   
7489  C CA  . ASN D 135 ? 0.2576 0.4003 0.2164 0.0802  -0.0763 -0.1225 135 ASN D CA  
7490  C C   . ASN D 135 ? 0.2384 0.3254 0.2002 0.0736  -0.0538 -0.1007 135 ASN D C   
7491  O O   . ASN D 135 ? 0.2320 0.3037 0.2077 0.0467  -0.0466 -0.1018 135 ASN D O   
7492  C CB  . ASN D 135 ? 0.2938 0.4354 0.2396 0.0528  -0.0853 -0.1446 135 ASN D CB  
7493  C CG  . ASN D 135 ? 0.3387 0.4210 0.2346 0.0688  -0.0807 -0.1432 135 ASN D CG  
7494  O OD1 . ASN D 135 ? 0.3373 0.3819 0.2158 0.0936  -0.0652 -0.1228 135 ASN D OD1 
7495  N ND2 . ASN D 135 ? 0.3864 0.4622 0.2559 0.0523  -0.0935 -0.1659 135 ASN D ND2 
7496  N N   . GLY D 136 ? 0.2370 0.2943 0.1820 0.0972  -0.0435 -0.0809 136 GLY D N   
7497  C CA  . GLY D 136 ? 0.2228 0.2434 0.1735 0.0921  -0.0236 -0.0613 136 GLY D CA  
7498  C C   . GLY D 136 ? 0.2532 0.2410 0.1721 0.1042  -0.0114 -0.0563 136 GLY D C   
7499  O O   . GLY D 136 ? 0.2469 0.2193 0.1714 0.1053  0.0060  -0.0398 136 GLY D O   
7500  N N   . CYS D 137 ? 0.2891 0.2736 0.1745 0.1142  -0.0210 -0.0717 137 CYS D N   
7501  C CA  . CYS D 137 ? 0.3290 0.2815 0.1760 0.1285  -0.0092 -0.0708 137 CYS D CA  
7502  C C   . CYS D 137 ? 0.3627 0.3055 0.1681 0.1532  -0.0061 -0.0613 137 CYS D C   
7503  O O   . CYS D 137 ? 0.3726 0.3286 0.1642 0.1644  -0.0228 -0.0651 137 CYS D O   
7504  C CB  . CYS D 137 ? 0.3660 0.3043 0.1886 0.1206  -0.0211 -0.0962 137 CYS D CB  
7505  S SG  . CYS D 137 ? 0.3570 0.2788 0.2042 0.0885  -0.0217 -0.1056 137 CYS D SG  
7506  N N   . PHE D 138 ? 0.3879 0.3085 0.1698 0.1642  0.0163  -0.0484 138 PHE D N   
7507  C CA  . PHE D 138 ? 0.4358 0.3374 0.1664 0.1844  0.0252  -0.0372 138 PHE D CA  
7508  C C   . PHE D 138 ? 0.4865 0.3693 0.1734 0.2001  0.0319  -0.0495 138 PHE D C   
7509  O O   . PHE D 138 ? 0.4862 0.3657 0.1833 0.2004  0.0492  -0.0498 138 PHE D O   
7510  C CB  . PHE D 138 ? 0.4304 0.3283 0.1695 0.1776  0.0516  -0.0087 138 PHE D CB  
7511  C CG  . PHE D 138 ? 0.4008 0.3007 0.1654 0.1633  0.0447  0.0030  138 PHE D CG  
7512  C CD1 . PHE D 138 ? 0.4382 0.3102 0.1602 0.1751  0.0351  0.0104  138 PHE D CD1 
7513  C CD2 . PHE D 138 ? 0.3468 0.2689 0.1684 0.1424  0.0465  0.0060  138 PHE D CD2 
7514  C CE1 . PHE D 138 ? 0.4260 0.2874 0.1597 0.1667  0.0285  0.0193  138 PHE D CE1 
7515  C CE2 . PHE D 138 ? 0.3288 0.2467 0.1658 0.1306  0.0396  0.0147  138 PHE D CE2 
7516  C CZ  . PHE D 138 ? 0.3698 0.2551 0.1619 0.1430  0.0310  0.0206  138 PHE D CZ  
7517  N N   . GLU D 139 ? 0.5377 0.4073 0.1709 0.2178  0.0172  -0.0606 139 GLU D N   
7518  C CA  . GLU D 139 ? 0.5984 0.4439 0.1779 0.2343  0.0195  -0.0762 139 GLU D CA  
7519  C C   . GLU D 139 ? 0.6543 0.4782 0.1765 0.2565  0.0427  -0.0568 139 GLU D C   
7520  O O   . GLU D 139 ? 0.6824 0.4958 0.1690 0.2673  0.0345  -0.0467 139 GLU D O   
7521  C CB  . GLU D 139 ? 0.6252 0.4757 0.1809 0.2349  -0.0165 -0.1053 139 GLU D CB  
7522  C CG  . GLU D 139 ? 0.6930 0.5118 0.1916 0.2447  -0.0211 -0.1292 139 GLU D CG  
7523  C CD  . GLU D 139 ? 0.7296 0.5630 0.1982 0.2450  -0.0594 -0.1561 139 GLU D CD  
7524  O OE1 . GLU D 139 ? 0.7050 0.5671 0.2112 0.2167  -0.0834 -0.1767 139 GLU D OE1 
7525  O OE2 . GLU D 139 ? 0.7870 0.6086 0.1940 0.2721  -0.0656 -0.1560 139 GLU D OE2 
7526  N N   . PHE D 140 ? 0.6797 0.4961 0.1876 0.2656  0.0725  -0.0514 140 PHE D N   
7527  C CA  . PHE D 140 ? 0.7291 0.5368 0.1923 0.2791  0.1043  -0.0285 140 PHE D CA  
7528  C C   . PHE D 140 ? 0.8151 0.5880 0.1895 0.3057  0.0975  -0.0384 140 PHE D C   
7529  O O   . PHE D 140 ? 0.8459 0.6033 0.1914 0.3179  0.0787  -0.0669 140 PHE D O   
7530  C CB  . PHE D 140 ? 0.7247 0.5560 0.2103 0.2834  0.1405  -0.0210 140 PHE D CB  
7531  C CG  . PHE D 140 ? 0.6509 0.5228 0.2179 0.2599  0.1498  -0.0069 140 PHE D CG  
7532  C CD1 . PHE D 140 ? 0.6050 0.4838 0.2196 0.2542  0.1336  -0.0228 140 PHE D CD1 
7533  C CD2 . PHE D 140 ? 0.6377 0.5364 0.2271 0.2402  0.1738  0.0221  140 PHE D CD2 
7534  C CE1 . PHE D 140 ? 0.5437 0.4592 0.2272 0.2356  0.1398  -0.0099 140 PHE D CE1 
7535  C CE2 . PHE D 140 ? 0.5752 0.5147 0.2374 0.2170  0.1788  0.0329  140 PHE D CE2 
7536  C CZ  . PHE D 140 ? 0.5262 0.4761 0.2359 0.2178  0.1610  0.0167  140 PHE D CZ  
7537  N N   . TYR D 141 ? 0.8657 0.6192 0.1891 0.3127  0.1124  -0.0147 141 TYR D N   
7538  C CA  . TYR D 141 ? 0.9603 0.6769 0.1881 0.3413  0.1109  -0.0194 141 TYR D CA  
7539  C C   . TYR D 141 ? 1.0075 0.7247 0.2027 0.3567  0.1471  -0.0204 141 TYR D C   
7540  O O   . TYR D 141 ? 1.0774 0.7672 0.2031 0.3828  0.1402  -0.0397 141 TYR D O   
7541  C CB  . TYR D 141 ? 1.0148 0.6964 0.1847 0.3450  0.1169  0.0094  141 TYR D CB  
7542  C CG  . TYR D 141 ? 0.9934 0.6675 0.1748 0.3456  0.0779  0.0068  141 TYR D CG  
7543  C CD1 . TYR D 141 ? 0.9975 0.6819 0.1686 0.3644  0.0335  -0.0234 141 TYR D CD1 
7544  C CD2 . TYR D 141 ? 0.9751 0.6362 0.1769 0.3276  0.0851  0.0325  141 TYR D CD2 
7545  C CE1 . TYR D 141 ? 0.9788 0.6733 0.1653 0.3710  -0.0008 -0.0272 141 TYR D CE1 
7546  C CE2 . TYR D 141 ? 0.9639 0.6175 0.1710 0.3367  0.0505  0.0285  141 TYR D CE2 
7547  C CZ  . TYR D 141 ? 0.9629 0.6398 0.1654 0.3613  0.0084  -0.0011 141 TYR D CZ  
7548  O OH  . TYR D 141 ? 0.9527 0.6383 0.1647 0.3762  -0.0245 -0.0063 141 TYR D OH  
7549  N N   . HIS D 142 ? 0.9750 0.7286 0.2194 0.3424  0.1851  -0.0008 142 HIS D N   
7550  C CA  . HIS D 142 ? 1.0109 0.7854 0.2400 0.3612  0.2233  -0.0018 142 HIS D CA  
7551  C C   . HIS D 142 ? 0.9670 0.7602 0.2491 0.3689  0.2156  -0.0262 142 HIS D C   
7552  O O   . HIS D 142 ? 0.8974 0.6986 0.2423 0.3487  0.1902  -0.0332 142 HIS D O   
7553  C CB  . HIS D 142 ? 1.0078 0.8273 0.2623 0.3413  0.2704  0.0334  142 HIS D CB  
7554  C CG  . HIS D 142 ? 0.9200 0.7821 0.2692 0.3053  0.2691  0.0474  142 HIS D CG  
7555  N ND1 . HIS D 142 ? 0.8661 0.7917 0.2908 0.3031  0.2855  0.0454  142 HIS D ND1 
7556  C CD2 . HIS D 142 ? 0.8855 0.7325 0.2597 0.2742  0.2514  0.0622  142 HIS D CD2 
7557  C CE1 . HIS D 142 ? 0.7989 0.7493 0.2925 0.2682  0.2772  0.0585  142 HIS D CE1 
7558  N NE2 . HIS D 142 ? 0.8100 0.7106 0.2733 0.2496  0.2574  0.0683  142 HIS D NE2 
7559  N N   . LYS D 143 ? 1.0189 0.8129 0.2670 0.4010  0.2385  -0.0388 143 LYS D N   
7560  C CA  . LYS D 143 ? 0.9994 0.8005 0.2834 0.4163  0.2374  -0.0584 143 LYS D CA  
7561  C C   . LYS D 143 ? 0.9267 0.8024 0.3017 0.4006  0.2622  -0.0346 143 LYS D C   
7562  O O   . LYS D 143 ? 0.9307 0.8608 0.3179 0.3954  0.2992  -0.0091 143 LYS D O   
7563  C CB  . LYS D 143 ? 1.0906 0.8688 0.3025 0.4633  0.2588  -0.0770 143 LYS D CB  
7564  C CG  . LYS D 143 ? 1.1078 0.8522 0.3193 0.4874  0.2471  -0.1052 143 LYS D CG  
7565  C CD  . LYS D 143 ? 1.2137 0.9298 0.3422 0.5413  0.2718  -0.1232 143 LYS D CD  
7566  C CE  . LYS D 143 ? 1.2401 0.9297 0.3700 0.5754  0.2725  -0.1433 143 LYS D CE  
7567  N NZ  . LYS D 143 ? 1.1769 0.9575 0.3940 0.5855  0.3017  -0.1206 143 LYS D NZ  
7568  N N   . CYS D 144 ? 0.8667 0.7462 0.3026 0.3895  0.2413  -0.0428 144 CYS D N   
7569  C CA  . CYS D 144 ? 0.7950 0.7450 0.3190 0.3723  0.2558  -0.0225 144 CYS D CA  
7570  C C   . CYS D 144 ? 0.7963 0.7558 0.3428 0.4046  0.2587  -0.0371 144 CYS D C   
7571  O O   . CYS D 144 ? 0.7790 0.6942 0.3355 0.3999  0.2293  -0.0527 144 CYS D O   
7572  C CB  . CYS D 144 ? 0.7232 0.6679 0.2976 0.3285  0.2264  -0.0141 144 CYS D CB  
7573  S SG  . CYS D 144 ? 0.6421 0.6673 0.3164 0.2980  0.2391  0.0114  144 CYS D SG  
7574  N N   . ASP D 145 ? 0.8261 0.8437 0.3757 0.4393  0.2953  -0.0315 145 ASP D N   
7575  C CA  . ASP D 145 ? 0.8442 0.8730 0.4054 0.4841  0.3005  -0.0445 145 ASP D CA  
7576  C C   . ASP D 145 ? 0.7633 0.8519 0.4166 0.4650  0.2924  -0.0305 145 ASP D C   
7577  O O   . ASP D 145 ? 0.6945 0.8069 0.3986 0.4143  0.2814  -0.0135 145 ASP D O   
7578  C CB  . ASP D 145 ? 0.9074 0.9930 0.4422 0.5356  0.3435  -0.0443 145 ASP D CB  
7579  C CG  . ASP D 145 ? 0.8667 1.0784 0.4660 0.5131  0.3811  -0.0141 145 ASP D CG  
7580  O OD1 . ASP D 145 ? 0.7932 1.0413 0.4560 0.4591  0.3726  0.0063  145 ASP D OD1 
7581  O OD2 . ASP D 145 ? 0.9167 1.1915 0.4993 0.5479  0.4207  -0.0114 145 ASP D OD2 
7582  N N   . ASN D 146 ? 0.7811 0.8880 0.4478 0.5093  0.2963  -0.0385 146 ASN D N   
7583  C CA  . ASN D 146 ? 0.7162 0.8732 0.4602 0.4983  0.2843  -0.0276 146 ASN D CA  
7584  C C   . ASN D 146 ? 0.6520 0.9426 0.4826 0.4695  0.3068  -0.0009 146 ASN D C   
7585  O O   . ASN D 146 ? 0.5868 0.9123 0.4814 0.4374  0.2910  0.0104  146 ASN D O   
7586  C CB  . ASN D 146 ? 0.7690 0.9064 0.4929 0.5624  0.2820  -0.0425 146 ASN D CB  
7587  C CG  . ASN D 146 ? 0.8400 0.8279 0.4763 0.5767  0.2545  -0.0682 146 ASN D CG  
7588  O OD1 . ASN D 146 ? 0.8219 0.7388 0.4396 0.5292  0.2296  -0.0737 146 ASN D OD1 
7589  N ND2 . ASN D 146 ? 0.9298 0.8701 0.5088 0.6425  0.2589  -0.0849 146 ASN D ND2 
7590  N N   . GLU D 147 ? 0.6787 1.0418 0.5069 0.4764  0.3441  0.0085  147 GLU D N   
7591  C CA  . GLU D 147 ? 0.6320 1.1164 0.5337 0.4338  0.3678  0.0344  147 GLU D CA  
7592  C C   . GLU D 147 ? 0.5998 1.0373 0.4971 0.3639  0.3555  0.0493  147 GLU D C   
7593  O O   . GLU D 147 ? 0.5456 1.0299 0.5028 0.3148  0.3501  0.0661  147 GLU D O   
7594  C CB  . GLU D 147 ? 0.6814 1.2596 0.5764 0.4584  0.4159  0.0410  147 GLU D CB  
7595  C CG  . GLU D 147 ? 0.7235 1.3625 0.6221 0.5377  0.4319  0.0260  147 GLU D CG  
7596  C CD  . GLU D 147 ? 0.8122 1.3406 0.6075 0.5991  0.4305  0.0004  147 GLU D CD  
7597  O OE1 . GLU D 147 ? 0.8727 1.4148 0.6184 0.6182  0.4635  -0.0006 147 GLU D OE1 
7598  O OE2 . GLU D 147 ? 0.8307 1.2537 0.5883 0.6252  0.3968  -0.0186 147 GLU D OE2 
7599  N N   . CYS D 148 ? 0.6433 0.9855 0.4631 0.3635  0.3495  0.0417  148 CYS D N   
7600  C CA  . CYS D 148 ? 0.6275 0.9083 0.4273 0.3121  0.3323  0.0520  148 CYS D CA  
7601  C C   . CYS D 148 ? 0.5655 0.8089 0.4041 0.2863  0.2928  0.0482  148 CYS D C   
7602  O O   . CYS D 148 ? 0.5305 0.7775 0.3963 0.2393  0.2849  0.0640  148 CYS D O   
7603  C CB  . CYS D 148 ? 0.6891 0.8773 0.3964 0.3300  0.3255  0.0386  148 CYS D CB  
7604  S SG  . CYS D 148 ? 0.6766 0.7805 0.3508 0.2867  0.2934  0.0441  148 CYS D SG  
7605  N N   . MET D 149 ? 0.5646 0.7655 0.3977 0.3167  0.2694  0.0273  149 MET D N   
7606  C CA  . MET D 149 ? 0.5126 0.6828 0.3801 0.2944  0.2358  0.0236  149 MET D CA  
7607  C C   . MET D 149 ? 0.4625 0.7177 0.4093 0.2744  0.2402  0.0402  149 MET D C   
7608  O O   . MET D 149 ? 0.4165 0.6648 0.3950 0.2357  0.2213  0.0477  149 MET D O   
7609  C CB  . MET D 149 ? 0.5377 0.6432 0.3748 0.3290  0.2156  0.0000  149 MET D CB  
7610  C CG  . MET D 149 ? 0.5922 0.6078 0.3512 0.3392  0.2028  -0.0209 149 MET D CG  
7611  S SD  . MET D 149 ? 0.5582 0.5312 0.3083 0.2911  0.1753  -0.0205 149 MET D SD  
7612  C CE  . MET D 149 ? 0.6311 0.5139 0.2973 0.3084  0.1550  -0.0522 149 MET D CE  
7613  N N   . GLU D 150 ? 0.4797 0.8201 0.4568 0.3032  0.2643  0.0441  150 GLU D N   
7614  C CA  . GLU D 150 ? 0.4391 0.8792 0.4950 0.2866  0.2674  0.0576  150 GLU D CA  
7615  C C   . GLU D 150 ? 0.4198 0.9053 0.5064 0.2234  0.2789  0.0791  150 GLU D C   
7616  O O   . GLU D 150 ? 0.3781 0.9002 0.5168 0.1884  0.2655  0.0878  150 GLU D O   
7617  C CB  . GLU D 150 ? 0.4659 1.0031 0.5471 0.3388  0.2916  0.0550  150 GLU D CB  
7618  C CG  . GLU D 150 ? 0.4248 1.0920 0.5933 0.3260  0.2951  0.0672  150 GLU D CG  
7619  C CD  . GLU D 150 ? 0.3816 1.0231 0.5804 0.3161  0.2584  0.0652  150 GLU D CD  
7620  O OE1 . GLU D 150 ? 0.3942 0.9282 0.5477 0.3375  0.2342  0.0522  150 GLU D OE1 
7621  O OE2 . GLU D 150 ? 0.3423 1.0720 0.6077 0.2835  0.2538  0.0765  150 GLU D OE2 
7622  N N   . SER D 151 ? 0.4651 0.9378 0.5099 0.2081  0.3028  0.0877  151 SER D N   
7623  C CA  . SER D 151 ? 0.4724 0.9638 0.5253 0.1457  0.3158  0.1096  151 SER D CA  
7624  C C   . SER D 151 ? 0.4541 0.8565 0.4922 0.1083  0.2833  0.1115  151 SER D C   
7625  O O   . SER D 151 ? 0.4462 0.8621 0.5063 0.0566  0.2823  0.1263  151 SER D O   
7626  C CB  . SER D 151 ? 0.5375 1.0139 0.5298 0.1424  0.3485  0.1194  151 SER D CB  
7627  O OG  . SER D 151 ? 0.5662 0.9266 0.4820 0.1578  0.3314  0.1100  151 SER D OG  
7628  N N   . VAL D 152 ? 0.4570 0.7708 0.4555 0.1342  0.2570  0.0949  152 VAL D N   
7629  C CA  . VAL D 152 ? 0.4389 0.6793 0.4255 0.1096  0.2261  0.0930  152 VAL D CA  
7630  C C   . VAL D 152 ? 0.3912 0.6643 0.4397 0.0956  0.2062  0.0916  152 VAL D C   
7631  O O   . VAL D 152 ? 0.3769 0.6323 0.4354 0.0576  0.1937  0.0996  152 VAL D O   
7632  C CB  . VAL D 152 ? 0.4482 0.6072 0.3847 0.1392  0.2039  0.0734  152 VAL D CB  
7633  C CG1 . VAL D 152 ? 0.4239 0.5270 0.3550 0.1174  0.1741  0.0708  152 VAL D CG1 
7634  C CG2 . VAL D 152 ? 0.5095 0.6353 0.3784 0.1559  0.2199  0.0733  152 VAL D CG2 
7635  N N   . ARG D 153 ? 0.3822 0.6949 0.4627 0.1295  0.2027  0.0812  153 ARG D N   
7636  C CA  . ARG D 153 ? 0.3487 0.6967 0.4827 0.1223  0.1843  0.0809  153 ARG D CA  
7637  C C   . ARG D 153 ? 0.3513 0.7968 0.5403 0.0885  0.1981  0.0967  153 ARG D C   
7638  O O   . ARG D 153 ? 0.3246 0.7813 0.5447 0.0561  0.1810  0.1010  153 ARG D O   
7639  C CB  . ARG D 153 ? 0.3484 0.7025 0.4879 0.1734  0.1772  0.0671  153 ARG D CB  
7640  C CG  . ARG D 153 ? 0.3678 0.6242 0.4509 0.1980  0.1627  0.0497  153 ARG D CG  
7641  C CD  . ARG D 153 ? 0.3874 0.6289 0.4632 0.2430  0.1545  0.0378  153 ARG D CD  
7642  N NE  . ARG D 153 ? 0.4444 0.6237 0.4577 0.2786  0.1601  0.0218  153 ARG D NE  
7643  C CZ  . ARG D 153 ? 0.4909 0.6970 0.4856 0.3236  0.1814  0.0174  153 ARG D CZ  
7644  N NH1 . ARG D 153 ? 0.4812 0.7911 0.5236 0.3409  0.2006  0.0283  153 ARG D NH1 
7645  N NH2 . ARG D 153 ? 0.5531 0.6856 0.4796 0.3523  0.1830  0.0002  153 ARG D NH2 
7646  N N   . ASN D 154 ? 0.3985 0.9188 0.5983 0.0950  0.2293  0.1039  154 ASN D N   
7647  C CA  . ASN D 154 ? 0.4159 1.0398 0.6654 0.0515  0.2483  0.1196  154 ASN D CA  
7648  C C   . ASN D 154 ? 0.4152 0.9933 0.6513 -0.0169 0.2411  0.1322  154 ASN D C   
7649  O O   . ASN D 154 ? 0.4033 1.0394 0.6854 -0.0586 0.2345  0.1385  154 ASN D O   
7650  C CB  . ASN D 154 ? 0.4829 1.1687 0.7224 0.0585  0.2895  0.1274  154 ASN D CB  
7651  C CG  . ASN D 154 ? 0.5145 1.3248 0.8052 0.1063  0.3058  0.1216  154 ASN D CG  
7652  O OD1 . ASN D 154 ? 0.4865 1.3371 0.8195 0.1354  0.2848  0.1128  154 ASN D OD1 
7653  N ND2 . ASN D 154 ? 0.6036 1.4763 0.8854 0.1187  0.3445  0.1268  154 ASN D ND2 
7654  N N   . GLY D 155 ? 0.4346 0.9048 0.6012 -0.0252 0.2406  0.1346  155 GLY D N   
7655  C CA  . GLY D 155 ? 0.4636 0.8749 0.5926 -0.0827 0.2422  0.1491  155 GLY D CA  
7656  C C   . GLY D 155 ? 0.5185 0.9438 0.6120 -0.1060 0.2800  0.1659  155 GLY D C   
7657  O O   . GLY D 155 ? 0.5732 0.9444 0.6231 -0.1568 0.2876  0.1813  155 GLY D O   
7658  N N   . THR D 156 ? 0.5139 1.0019 0.6160 -0.0669 0.3046  0.1628  156 THR D N   
7659  C CA  . THR D 156 ? 0.5672 1.0997 0.6474 -0.0866 0.3472  0.1789  156 THR D CA  
7660  C C   . THR D 156 ? 0.6107 1.0618 0.6079 -0.0480 0.3587  0.1771  156 THR D C   
7661  O O   . THR D 156 ? 0.6567 1.1517 0.6338 -0.0424 0.3954  0.1854  156 THR D O   
7662  C CB  . THR D 156 ? 0.5430 1.2345 0.6999 -0.0678 0.3718  0.1763  156 THR D CB  
7663  O OG1 . THR D 156 ? 0.4947 1.2687 0.7312 -0.0940 0.3538  0.1743  156 THR D OG1 
7664  C CG2 . THR D 156 ? 0.6059 1.3699 0.7530 -0.1013 0.4208  0.1950  156 THR D CG2 
7665  N N   . TYR D 157 ? 0.5995 0.9394 0.5480 -0.0218 0.3276  0.1655  157 TYR D N   
7666  C CA  . TYR D 157 ? 0.6426 0.9083 0.5121 0.0157  0.3316  0.1606  157 TYR D CA  
7667  C C   . TYR D 157 ? 0.7313 0.9568 0.5297 -0.0190 0.3610  0.1844  157 TYR D C   
7668  O O   . TYR D 157 ? 0.7685 0.9165 0.5252 -0.0573 0.3514  0.1978  157 TYR D O   
7669  C CB  . TYR D 157 ? 0.6213 0.7874 0.4564 0.0394  0.2907  0.1448  157 TYR D CB  
7670  C CG  . TYR D 157 ? 0.6717 0.7664 0.4246 0.0748  0.2892  0.1381  157 TYR D CG  
7671  C CD1 . TYR D 157 ? 0.6721 0.7846 0.4158 0.1227  0.2934  0.1199  157 TYR D CD1 
7672  C CD2 . TYR D 157 ? 0.7305 0.7350 0.4071 0.0634  0.2818  0.1489  157 TYR D CD2 
7673  C CE1 . TYR D 157 ? 0.7255 0.7745 0.3909 0.1528  0.2890  0.1115  157 TYR D CE1 
7674  C CE2 . TYR D 157 ? 0.7827 0.7286 0.3826 0.0987  0.2768  0.1421  157 TYR D CE2 
7675  C CZ  . TYR D 157 ? 0.7773 0.7491 0.3742 0.1407  0.2799  0.1228  157 TYR D CZ  
7676  O OH  . TYR D 157 ? 0.8344 0.7491 0.3520 0.1733  0.2719  0.1137  157 TYR D OH  
7677  N N   . ASP D 158 ? 0.7761 1.0471 0.5521 -0.0033 0.3978  0.1898  158 ASP D N   
7678  C CA  . ASP D 158 ? 0.8724 1.1131 0.5776 -0.0396 0.4329  0.2155  158 ASP D CA  
7679  C C   . ASP D 158 ? 0.9389 1.0465 0.5344 -0.0135 0.4182  0.2159  158 ASP D C   
7680  O O   . ASP D 158 ? 0.9773 1.0738 0.5224 0.0292  0.4301  0.2091  158 ASP D O   
7681  C CB  . ASP D 158 ? 0.9002 1.2513 0.6228 -0.0319 0.4816  0.2215  158 ASP D CB  
7682  C CG  . ASP D 158 ? 0.9957 1.3457 0.6680 -0.0925 0.5249  0.2529  158 ASP D CG  
7683  O OD1 . ASP D 158 ? 1.0056 1.3680 0.7038 -0.1616 0.5284  0.2694  158 ASP D OD1 
7684  O OD2 . ASP D 158 ? 1.0704 1.4019 0.6710 -0.0744 0.5556  0.2610  158 ASP D OD2 
7685  N N   . TYR D 159 ? 0.9598 0.9680 0.5151 -0.0362 0.3910  0.2227  159 TYR D N   
7686  C CA  . TYR D 159 ? 1.0241 0.9090 0.4769 -0.0075 0.3703  0.2228  159 TYR D CA  
7687  C C   . TYR D 159 ? 1.1357 0.9829 0.4910 -0.0050 0.4056  0.2420  159 TYR D C   
7688  O O   . TYR D 159 ? 1.1627 0.9749 0.4624 0.0459  0.3964  0.2297  159 TYR D O   
7689  C CB  . TYR D 159 ? 1.0481 0.8374 0.4684 -0.0343 0.3423  0.2313  159 TYR D CB  
7690  C CG  . TYR D 159 ? 1.1378 0.8004 0.4421 -0.0052 0.3240  0.2366  159 TYR D CG  
7691  C CD1 . TYR D 159 ? 1.2681 0.8467 0.4662 -0.0304 0.3498  0.2659  159 TYR D CD1 
7692  C CD2 . TYR D 159 ? 1.1004 0.7297 0.3983 0.0471  0.2808  0.2127  159 TYR D CD2 
7693  C CE1 . TYR D 159 ? 1.3616 0.8202 0.4450 0.0045  0.3304  0.2714  159 TYR D CE1 
7694  C CE2 . TYR D 159 ? 1.1842 0.7121 0.3795 0.0803  0.2608  0.2159  159 TYR D CE2 
7695  C CZ  . TYR D 159 ? 1.3169 0.7564 0.4026 0.0630  0.2845  0.2455  159 TYR D CZ  
7696  O OH  . TYR D 159 ? 1.4135 0.7474 0.3881 0.1035  0.2625  0.2497  159 TYR D OH  
7697  N N   . PRO D 160 ? 1.2079 1.0631 0.5390 -0.0633 0.4464  0.2716  160 PRO D N   
7698  C CA  . PRO D 160 ? 1.3260 1.1427 0.5567 -0.0663 0.4852  0.2933  160 PRO D CA  
7699  C C   . PRO D 160 ? 1.3198 1.2105 0.5530 -0.0169 0.5090  0.2800  160 PRO D C   
7700  O O   . PRO D 160 ? 1.4178 1.2501 0.5490 0.0021  0.5270  0.2906  160 PRO D O   
7701  C CB  . PRO D 160 ? 1.3811 1.2334 0.6206 -0.1496 0.5284  0.3237  160 PRO D CB  
7702  C CG  . PRO D 160 ? 1.3367 1.1648 0.6242 -0.1891 0.4979  0.3220  160 PRO D CG  
7703  C CD  . PRO D 160 ? 1.2013 1.0844 0.5811 -0.1354 0.4563  0.2875  160 PRO D CD  
7704  N N   . GLN D 161 ? 1.2196 1.2280 0.5570 0.0066  0.5088  0.2572  161 GLN D N   
7705  C CA  . GLN D 161 ? 1.2213 1.2911 0.5558 0.0607  0.5292  0.2406  161 GLN D CA  
7706  C C   . GLN D 161 ? 1.2251 1.2119 0.5009 0.1251  0.4895  0.2145  161 GLN D C   
7707  O O   . GLN D 161 ? 1.2955 1.2566 0.4934 0.1611  0.5044  0.2108  161 GLN D O   
7708  C CB  . GLN D 161 ? 1.1271 1.3362 0.5811 0.0735  0.5379  0.2235  161 GLN D CB  
7709  C CG  . GLN D 161 ? 1.1338 1.3961 0.5811 0.1391  0.5551  0.2020  161 GLN D CG  
7710  C CD  . GLN D 161 ? 1.0497 1.4326 0.6055 0.1631  0.5564  0.1837  161 GLN D CD  
7711  O OE1 . GLN D 161 ? 0.9689 1.3683 0.5994 0.1485  0.5256  0.1769  161 GLN D OE1 
7712  N NE2 . GLN D 161 ? 1.0771 1.5418 0.6352 0.2056  0.5918  0.1753  161 GLN D NE2 
7713  N N   . TYR D 162 ? 1.1531 1.1037 0.4660 0.1367  0.4395  0.1954  162 TYR D N   
7714  C CA  . TYR D 162 ? 1.1485 1.0373 0.4215 0.1889  0.3979  0.1674  162 TYR D CA  
7715  C C   . TYR D 162 ? 1.2185 0.9939 0.3961 0.1924  0.3713  0.1762  162 TYR D C   
7716  O O   . TYR D 162 ? 1.2133 0.9455 0.3638 0.2299  0.3309  0.1528  162 TYR D O   
7717  C CB  . TYR D 162 ? 1.0403 0.9586 0.4030 0.1995  0.3598  0.1412  162 TYR D CB  
7718  C CG  . TYR D 162 ? 0.9820 1.0010 0.4290 0.2083  0.3793  0.1306  162 TYR D CG  
7719  C CD1 . TYR D 162 ? 1.0025 1.0430 0.4314 0.2569  0.3892  0.1092  162 TYR D CD1 
7720  C CD2 . TYR D 162 ? 0.9160 1.0051 0.4539 0.1725  0.3859  0.1406  162 TYR D CD2 
7721  C CE1 . TYR D 162 ? 0.9625 1.0885 0.4590 0.2755  0.4059  0.0992  162 TYR D CE1 
7722  C CE2 . TYR D 162 ? 0.8689 1.0544 0.4809 0.1887  0.4007  0.1309  162 TYR D CE2 
7723  C CZ  . TYR D 162 ? 0.8939 1.0963 0.4839 0.2432  0.4111  0.1107  162 TYR D CZ  
7724  O OH  . TYR D 162 ? 0.8600 1.1519 0.5146 0.2691  0.4247  0.1008  162 TYR D OH  
7725  N N   . SER D 163 ? 1.2933 1.0209 0.4168 0.1535  0.3931  0.2093  163 SER D N   
7726  C CA  . SER D 163 ? 1.3823 0.9914 0.3996 0.1624  0.3706  0.2217  163 SER D CA  
7727  C C   . SER D 163 ? 1.5113 1.0715 0.4100 0.1732  0.4033  0.2412  163 SER D C   
7728  O O   . SER D 163 ? 1.6161 1.0714 0.4079 0.1743  0.3974  0.2615  163 SER D O   
7729  C CB  . SER D 163 ? 1.3987 0.9567 0.4169 0.1129  0.3677  0.2455  163 SER D CB  
7730  O OG  . SER D 163 ? 1.4984 1.0301 0.4588 0.0641  0.4146  0.2811  163 SER D OG  
7731  N N   . ASP E 1   ? 0.5118 0.3572 0.3089 -0.2644 -0.0434 0.1458  1   ASP E N   
7732  C CA  . ASP E 1   ? 0.5443 0.3335 0.3115 -0.2501 -0.0502 0.1486  1   ASP E CA  
7733  C C   . ASP E 1   ? 0.4853 0.3104 0.3047 -0.2170 -0.0505 0.1425  1   ASP E C   
7734  O O   . ASP E 1   ? 0.4391 0.3054 0.2978 -0.1965 -0.0481 0.1394  1   ASP E O   
7735  C CB  . ASP E 1   ? 0.6128 0.3221 0.3151 -0.2329 -0.0583 0.1590  1   ASP E CB  
7736  C CG  . ASP E 1   ? 0.6859 0.3436 0.3228 -0.2671 -0.0583 0.1661  1   ASP E CG  
7737  O OD1 . ASP E 1   ? 0.6809 0.3712 0.3251 -0.3084 -0.0516 0.1624  1   ASP E OD1 
7738  O OD2 . ASP E 1   ? 0.7534 0.3384 0.3275 -0.2519 -0.0650 0.1751  1   ASP E OD2 
7739  N N   . GLN E 2   ? 0.4918 0.2991 0.3070 -0.2150 -0.0529 0.1404  2   GLN E N   
7740  C CA  . GLN E 2   ? 0.4426 0.2789 0.3013 -0.1869 -0.0532 0.1346  2   GLN E CA  
7741  C C   . GLN E 2   ? 0.4722 0.2618 0.3046 -0.1774 -0.0590 0.1358  2   GLN E C   
7742  O O   . GLN E 2   ? 0.5218 0.2686 0.3114 -0.2011 -0.0608 0.1383  2   GLN E O   
7743  C CB  . GLN E 2   ? 0.3855 0.2907 0.2983 -0.1957 -0.0457 0.1255  2   GLN E CB  
7744  C CG  . GLN E 2   ? 0.3956 0.3118 0.3040 -0.2233 -0.0439 0.1219  2   GLN E CG  
7745  C CD  . GLN E 2   ? 0.3416 0.3258 0.3014 -0.2186 -0.0381 0.1125  2   GLN E CD  
7746  O OE1 . GLN E 2   ? 0.3372 0.3332 0.3039 -0.2230 -0.0386 0.1085  2   GLN E OE1 
7747  N NE2 . GLN E 2   ? 0.3065 0.3323 0.2972 -0.2082 -0.0328 0.1087  2   GLN E NE2 
7748  N N   . ILE E 3   ? 0.4443 0.2436 0.2998 -0.1451 -0.0615 0.1333  3   ILE E N   
7749  C CA  . ILE E 3   ? 0.4615 0.2285 0.3023 -0.1322 -0.0662 0.1326  3   ILE E CA  
7750  C C   . ILE E 3   ? 0.3999 0.2199 0.2965 -0.1231 -0.0624 0.1245  3   ILE E C   
7751  O O   . ILE E 3   ? 0.3551 0.2190 0.2897 -0.1103 -0.0587 0.1207  3   ILE E O   
7752  C CB  . ILE E 3   ? 0.4992 0.2219 0.3035 -0.0978 -0.0741 0.1373  3   ILE E CB  
7753  C CG1 . ILE E 3   ? 0.5344 0.2094 0.3082 -0.0880 -0.0793 0.1372  3   ILE E CG1 
7754  C CG2 . ILE E 3   ? 0.4493 0.2247 0.2955 -0.0690 -0.0733 0.1335  3   ILE E CG2 
7755  C CD1 . ILE E 3   ? 0.5964 0.2113 0.3131 -0.0546 -0.0878 0.1425  3   ILE E CD1 
7756  N N   . CYS E 4   ? 0.4045 0.2159 0.3000 -0.1316 -0.0630 0.1217  4   CYS E N   
7757  C CA  . CYS E 4   ? 0.3549 0.2096 0.2960 -0.1235 -0.0598 0.1145  4   CYS E CA  
7758  C C   . CYS E 4   ? 0.3647 0.1915 0.2954 -0.1050 -0.0648 0.1139  4   CYS E C   
7759  O O   . CYS E 4   ? 0.4161 0.1882 0.3013 -0.1054 -0.0703 0.1180  4   CYS E O   
7760  C CB  . CYS E 4   ? 0.3437 0.2305 0.3002 -0.1493 -0.0555 0.1102  4   CYS E CB  
7761  S SG  . CYS E 4   ? 0.3379 0.2640 0.3031 -0.1731 -0.0493 0.1097  4   CYS E SG  
7762  N N   . ILE E 5   ? 0.3211 0.1812 0.2886 -0.0892 -0.0627 0.1084  5   ILE E N   
7763  C CA  . ILE E 5   ? 0.3232 0.1674 0.2877 -0.0739 -0.0664 0.1063  5   ILE E CA  
7764  C C   . ILE E 5   ? 0.2996 0.1670 0.2874 -0.0856 -0.0635 0.1014  5   ILE E C   
7765  O O   . ILE E 5   ? 0.2655 0.1742 0.2843 -0.0897 -0.0579 0.0976  5   ILE E O   
7766  C CB  . ILE E 5   ? 0.2970 0.1635 0.2811 -0.0483 -0.0662 0.1032  5   ILE E CB  
7767  C CG1 . ILE E 5   ? 0.3157 0.1756 0.2810 -0.0346 -0.0690 0.1070  5   ILE E CG1 
7768  C CG2 . ILE E 5   ? 0.3025 0.1548 0.2813 -0.0324 -0.0702 0.1008  5   ILE E CG2 
7769  C CD1 . ILE E 5   ? 0.3720 0.1781 0.2879 -0.0200 -0.0770 0.1121  5   ILE E CD1 
7770  N N   . GLY E 6   ? 0.3227 0.1618 0.2912 -0.0888 -0.0674 0.1014  6   GLY E N   
7771  C CA  . GLY E 6   ? 0.3058 0.1684 0.2921 -0.1003 -0.0657 0.0969  6   GLY E CA  
7772  C C   . GLY E 6   ? 0.3269 0.1574 0.2945 -0.0958 -0.0704 0.0961  6   GLY E C   
7773  O O   . GLY E 6   ? 0.3556 0.1442 0.2954 -0.0808 -0.0750 0.0987  6   GLY E O   
7774  N N   . TYR E 7   ? 0.3152 0.1681 0.2964 -0.1070 -0.0693 0.0921  7   TYR E N   
7775  C CA  . TYR E 7   ? 0.3273 0.1586 0.2983 -0.1019 -0.0730 0.0902  7   TYR E CA  
7776  C C   . TYR E 7   ? 0.3490 0.1847 0.3060 -0.1308 -0.0735 0.0881  7   TYR E C   
7777  O O   . TYR E 7   ? 0.3435 0.2156 0.3085 -0.1526 -0.0703 0.0867  7   TYR E O   
7778  C CB  . TYR E 7   ? 0.2836 0.1454 0.2908 -0.0795 -0.0713 0.0860  7   TYR E CB  
7779  C CG  . TYR E 7   ? 0.2464 0.1605 0.2877 -0.0809 -0.0662 0.0823  7   TYR E CG  
7780  C CD1 . TYR E 7   ? 0.2243 0.1608 0.2831 -0.0735 -0.0615 0.0821  7   TYR E CD1 
7781  C CD2 . TYR E 7   ? 0.2387 0.1788 0.2902 -0.0869 -0.0662 0.0785  7   TYR E CD2 
7782  C CE1 . TYR E 7   ? 0.2012 0.1770 0.2817 -0.0698 -0.0570 0.0784  7   TYR E CE1 
7783  C CE2 . TYR E 7   ? 0.2129 0.1993 0.2889 -0.0808 -0.0623 0.0748  7   TYR E CE2 
7784  C CZ  . TYR E 7   ? 0.1970 0.1972 0.2850 -0.0709 -0.0577 0.0747  7   TYR E CZ  
7785  O OH  . TYR E 7   ? 0.1819 0.2201 0.2853 -0.0602 -0.0539 0.0707  7   TYR E OH  
7786  N N   . HIS E 8   ? 0.3753 0.1781 0.3104 -0.1314 -0.0772 0.0871  8   HIS E N   
7787  C CA  . HIS E 8   ? 0.4081 0.2056 0.3190 -0.1628 -0.0781 0.0848  8   HIS E CA  
7788  C C   . HIS E 8   ? 0.3677 0.2381 0.3193 -0.1692 -0.0755 0.0789  8   HIS E C   
7789  O O   . HIS E 8   ? 0.3255 0.2265 0.3139 -0.1431 -0.0746 0.0766  8   HIS E O   
7790  C CB  . HIS E 8   ? 0.4484 0.1857 0.3222 -0.1569 -0.0829 0.0849  8   HIS E CB  
7791  C CG  . HIS E 8   ? 0.4923 0.2126 0.3305 -0.1929 -0.0837 0.0822  8   HIS E CG  
7792  N ND1 . HIS E 8   ? 0.5507 0.2367 0.3385 -0.2307 -0.0829 0.0841  8   HIS E ND1 
7793  C CD2 . HIS E 8   ? 0.4913 0.2226 0.3323 -0.2001 -0.0850 0.0776  8   HIS E CD2 
7794  C CE1 . HIS E 8   ? 0.5847 0.2630 0.3449 -0.2624 -0.0833 0.0801  8   HIS E CE1 
7795  N NE2 . HIS E 8   ? 0.5475 0.2549 0.3412 -0.2432 -0.0847 0.0761  8   HIS E NE2 
7796  N N   . ALA E 9   ? 0.3869 0.2857 0.3271 -0.2041 -0.0741 0.0760  9   ALA E N   
7797  C CA  . ALA E 9   ? 0.3609 0.3304 0.3298 -0.2108 -0.0730 0.0694  9   ALA E CA  
7798  C C   . ALA E 9   ? 0.4094 0.3697 0.3395 -0.2529 -0.0743 0.0665  9   ALA E C   
7799  O O   . ALA E 9   ? 0.4655 0.3658 0.3448 -0.2798 -0.0748 0.0698  9   ALA E O   
7800  C CB  . ALA E 9   ? 0.3274 0.3714 0.3294 -0.2100 -0.0687 0.0665  9   ALA E CB  
7801  N N   . ASN E 10  ? 0.3951 0.4109 0.3431 -0.2592 -0.0748 0.0602  10  ASN E N   
7802  C CA  . ASN E 10  ? 0.4416 0.4582 0.3529 -0.3038 -0.0755 0.0560  10  ASN E CA  
7803  C C   . ASN E 10  ? 0.4128 0.5289 0.3573 -0.3094 -0.0751 0.0476  10  ASN E C   
7804  O O   . ASN E 10  ? 0.3615 0.5396 0.3531 -0.2751 -0.0745 0.0456  10  ASN E O   
7805  C CB  . ASN E 10  ? 0.4855 0.4125 0.3539 -0.3047 -0.0792 0.0585  10  ASN E CB  
7806  C CG  . ASN E 10  ? 0.4474 0.3838 0.3483 -0.2681 -0.0822 0.0570  10  ASN E CG  
7807  O OD1 . ASN E 10  ? 0.3941 0.3999 0.3441 -0.2445 -0.0815 0.0541  10  ASN E OD1 
7808  N ND2 . ASN E 10  ? 0.4808 0.3428 0.3486 -0.2619 -0.0854 0.0588  10  ASN E ND2 
7809  N N   . ASN E 11  ? 0.4531 0.5819 0.3672 -0.3519 -0.0755 0.0424  11  ASN E N   
7810  C CA  . ASN E 11  ? 0.4321 0.6658 0.3729 -0.3617 -0.0756 0.0333  11  ASN E CA  
7811  C C   . ASN E 11  ? 0.4115 0.6491 0.3706 -0.3342 -0.0797 0.0314  11  ASN E C   
7812  O O   . ASN E 11  ? 0.4079 0.7176 0.3754 -0.3486 -0.0807 0.0239  11  ASN E O   
7813  C CB  . ASN E 11  ? 0.4862 0.7473 0.3843 -0.4288 -0.0731 0.0270  11  ASN E CB  
7814  C CG  . ASN E 11  ? 0.5553 0.7187 0.3890 -0.4640 -0.0746 0.0286  11  ASN E CG  
7815  O OD1 . ASN E 11  ? 0.5596 0.6432 0.3850 -0.4343 -0.0779 0.0337  11  ASN E OD1 
7816  N ND2 . ASN E 11  ? 0.6160 0.7846 0.3986 -0.5290 -0.0716 0.0234  11  ASN E ND2 
7817  N N   . SER E 12  ? 0.3988 0.5651 0.3638 -0.2955 -0.0819 0.0378  12  SER E N   
7818  C CA  . SER E 12  ? 0.3807 0.5418 0.3607 -0.2684 -0.0855 0.0367  12  SER E CA  
7819  C C   . SER E 12  ? 0.3293 0.5731 0.3583 -0.2301 -0.0859 0.0336  12  SER E C   
7820  O O   . SER E 12  ? 0.3030 0.5732 0.3557 -0.2066 -0.0836 0.0350  12  SER E O   
7821  C CB  . SER E 12  ? 0.3832 0.4505 0.3536 -0.2392 -0.0871 0.0437  12  SER E CB  
7822  O OG  . SER E 12  ? 0.3660 0.4288 0.3501 -0.2145 -0.0901 0.0425  12  SER E OG  
7823  N N   . THR E 13  ? 0.3225 0.6018 0.3606 -0.2230 -0.0890 0.0292  13  THR E N   
7824  C CA  . THR E 13  ? 0.2850 0.6287 0.3589 -0.1806 -0.0905 0.0267  13  THR E CA  
7825  C C   . THR E 13  ? 0.2756 0.5716 0.3538 -0.1488 -0.0934 0.0297  13  THR E C   
7826  O O   . THR E 13  ? 0.2552 0.5907 0.3525 -0.1147 -0.0951 0.0280  13  THR E O   
7827  C CB  . THR E 13  ? 0.2845 0.7356 0.3670 -0.1961 -0.0920 0.0175  13  THR E CB  
7828  O OG1 . THR E 13  ? 0.3151 0.7549 0.3715 -0.2368 -0.0940 0.0141  13  THR E OG1 
7829  C CG2 . THR E 13  ? 0.2860 0.8075 0.3725 -0.2183 -0.0886 0.0131  13  THR E CG2 
7830  N N   . GLU E 14  ? 0.2955 0.5065 0.3518 -0.1581 -0.0940 0.0339  14  GLU E N   
7831  C CA  . GLU E 14  ? 0.2880 0.4545 0.3470 -0.1308 -0.0962 0.0363  14  GLU E CA  
7832  C C   . GLU E 14  ? 0.2587 0.4146 0.3384 -0.0887 -0.0942 0.0401  14  GLU E C   
7833  O O   . GLU E 14  ? 0.2536 0.3883 0.3355 -0.0839 -0.0910 0.0435  14  GLU E O   
7834  C CB  . GLU E 14  ? 0.3186 0.3994 0.3476 -0.1452 -0.0968 0.0392  14  GLU E CB  
7835  C CG  . GLU E 14  ? 0.3614 0.4305 0.3571 -0.1852 -0.0988 0.0353  14  GLU E CG  
7836  C CD  . GLU E 14  ? 0.3843 0.3848 0.3575 -0.1797 -0.1012 0.0360  14  GLU E CD  
7837  O OE1 . GLU E 14  ? 0.3656 0.3843 0.3553 -0.1608 -0.1034 0.0342  14  GLU E OE1 
7838  O OE2 . GLU E 14  ? 0.4251 0.3523 0.3611 -0.1915 -0.1010 0.0382  14  GLU E OE2 
7839  N N   . GLN E 15  ? 0.2450 0.4117 0.3344 -0.0605 -0.0959 0.0394  15  GLN E N   
7840  C CA  . GLN E 15  ? 0.2296 0.3796 0.3275 -0.0239 -0.0936 0.0425  15  GLN E CA  
7841  C C   . GLN E 15  ? 0.2301 0.3236 0.3205 -0.0116 -0.0941 0.0449  15  GLN E C   
7842  O O   . GLN E 15  ? 0.2377 0.3220 0.3214 -0.0216 -0.0973 0.0432  15  GLN E O   
7843  C CB  . GLN E 15  ? 0.2248 0.4342 0.3308 0.0031  -0.0947 0.0395  15  GLN E CB  
7844  C CG  . GLN E 15  ? 0.2228 0.5072 0.3382 -0.0066 -0.0946 0.0351  15  GLN E CG  
7845  C CD  . GLN E 15  ? 0.2224 0.5689 0.3423 0.0294  -0.0962 0.0314  15  GLN E CD  
7846  O OE1 . GLN E 15  ? 0.2207 0.6077 0.3456 0.0435  -0.0942 0.0294  15  GLN E OE1 
7847  N NE2 . GLN E 15  ? 0.2281 0.5816 0.3430 0.0476  -0.1002 0.0303  15  GLN E NE2 
7848  N N   . VAL E 16  ? 0.2236 0.2819 0.3131 0.0075  -0.0904 0.0480  16  VAL E N   
7849  C CA  . VAL E 16  ? 0.2252 0.2389 0.3065 0.0185  -0.0898 0.0494  16  VAL E CA  
7850  C C   . VAL E 16  ? 0.2285 0.2320 0.3026 0.0446  -0.0864 0.0507  16  VAL E C   
7851  O O   . VAL E 16  ? 0.2290 0.2457 0.3036 0.0541  -0.0836 0.0512  16  VAL E O   
7852  C CB  . VAL E 16  ? 0.2252 0.1953 0.3022 0.0073  -0.0881 0.0511  16  VAL E CB  
7853  C CG1 . VAL E 16  ? 0.2370 0.2007 0.3072 -0.0161 -0.0914 0.0501  16  VAL E CG1 
7854  C CG2 . VAL E 16  ? 0.2191 0.1814 0.2990 0.0107  -0.0835 0.0534  16  VAL E CG2 
7855  N N   . ASP E 17  ? 0.2373 0.2127 0.2989 0.0550  -0.0862 0.0509  17  ASP E N   
7856  C CA  . ASP E 17  ? 0.2546 0.2027 0.2955 0.0755  -0.0822 0.0523  17  ASP E CA  
7857  C C   . ASP E 17  ? 0.2563 0.1621 0.2886 0.0660  -0.0768 0.0533  17  ASP E C   
7858  O O   . ASP E 17  ? 0.2443 0.1424 0.2852 0.0511  -0.0775 0.0525  17  ASP E O   
7859  C CB  . ASP E 17  ? 0.2725 0.2143 0.2964 0.0914  -0.0849 0.0519  17  ASP E CB  
7860  C CG  . ASP E 17  ? 0.2768 0.2683 0.3042 0.1085  -0.0899 0.0503  17  ASP E CG  
7861  O OD1 . ASP E 17  ? 0.2762 0.3000 0.3087 0.1178  -0.0895 0.0495  17  ASP E OD1 
7862  O OD2 . ASP E 17  ? 0.2821 0.2856 0.3063 0.1135  -0.0943 0.0492  17  ASP E OD2 
7863  N N   . THR E 18  ? 0.2757 0.1562 0.2871 0.0755  -0.0714 0.0543  18  THR E N   
7864  C CA  . THR E 18  ? 0.2853 0.1302 0.2815 0.0645  -0.0653 0.0541  18  THR E CA  
7865  C C   . THR E 18  ? 0.3285 0.1311 0.2820 0.0767  -0.0610 0.0546  18  THR E C   
7866  O O   . THR E 18  ? 0.3496 0.1506 0.2869 0.0986  -0.0636 0.0554  18  THR E O   
7867  C CB  . THR E 18  ? 0.2747 0.1239 0.2796 0.0565  -0.0614 0.0546  18  THR E CB  
7868  O OG1 . THR E 18  ? 0.2940 0.1367 0.2820 0.0722  -0.0587 0.0554  18  THR E OG1 
7869  C CG2 . THR E 18  ? 0.2452 0.1280 0.2820 0.0469  -0.0658 0.0550  18  THR E CG2 
7870  N N   . ILE E 19  ? 0.3493 0.1174 0.2790 0.0624  -0.0544 0.0536  19  ILE E N   
7871  C CA  . ILE E 19  ? 0.4045 0.1180 0.2801 0.0678  -0.0491 0.0539  19  ILE E CA  
7872  C C   . ILE E 19  ? 0.4392 0.1308 0.2867 0.0904  -0.0471 0.0554  19  ILE E C   
7873  O O   . ILE E 19  ? 0.4796 0.1422 0.2900 0.1149  -0.0483 0.0567  19  ILE E O   
7874  C CB  . ILE E 19  ? 0.4216 0.1076 0.2739 0.0395  -0.0411 0.0513  19  ILE E CB  
7875  C CG1 . ILE E 19  ? 0.3970 0.1071 0.2705 0.0220  -0.0429 0.0485  19  ILE E CG1 
7876  C CG2 . ILE E 19  ? 0.4906 0.1074 0.2737 0.0395  -0.0344 0.0515  19  ILE E CG2 
7877  C CD1 . ILE E 19  ? 0.4222 0.1087 0.2705 0.0258  -0.0444 0.0487  19  ILE E CD1 
7878  N N   . MET E 20  ? 0.4271 0.1331 0.2900 0.0850  -0.0444 0.0550  20  MET E N   
7879  C CA  . MET E 20  ? 0.4635 0.1468 0.2967 0.1050  -0.0413 0.0555  20  MET E CA  
7880  C C   . MET E 20  ? 0.4478 0.1800 0.3073 0.1326  -0.0476 0.0559  20  MET E C   
7881  O O   . MET E 20  ? 0.4823 0.1995 0.3120 0.1593  -0.0463 0.0556  20  MET E O   
7882  C CB  . MET E 20  ? 0.4575 0.1356 0.2931 0.0849  -0.0348 0.0543  20  MET E CB  
7883  C CG  . MET E 20  ? 0.4852 0.1205 0.2868 0.0555  -0.0270 0.0523  20  MET E CG  
7884  S SD  . MET E 20  ? 0.4948 0.1189 0.2850 0.0379  -0.0188 0.0504  20  MET E SD  
7885  C CE  . MET E 20  ? 0.5027 0.1174 0.2777 -0.0051 -0.0120 0.0465  20  MET E CE  
7886  N N   . GLU E 21  ? 0.4023 0.1934 0.3128 0.1252  -0.0540 0.0558  21  GLU E N   
7887  C CA  . GLU E 21  ? 0.3861 0.2350 0.3232 0.1420  -0.0594 0.0550  21  GLU E CA  
7888  C C   . GLU E 21  ? 0.3624 0.2560 0.3305 0.1368  -0.0668 0.0545  21  GLU E C   
7889  O O   . GLU E 21  ? 0.3376 0.2311 0.3257 0.1127  -0.0679 0.0549  21  GLU E O   
7890  C CB  . GLU E 21  ? 0.3565 0.2347 0.3222 0.1276  -0.0575 0.0547  21  GLU E CB  
7891  C CG  . GLU E 21  ? 0.3508 0.2823 0.3294 0.1466  -0.0602 0.0527  21  GLU E CG  
7892  C CD  . GLU E 21  ? 0.3269 0.2824 0.3288 0.1307  -0.0576 0.0526  21  GLU E CD  
7893  O OE1 . GLU E 21  ? 0.3196 0.2440 0.3221 0.1101  -0.0533 0.0542  21  GLU E OE1 
7894  O OE2 . GLU E 21  ? 0.3156 0.3260 0.3342 0.1384  -0.0598 0.0504  21  GLU E OE2 
7895  N N   . LYS E 22  ? 0.3759 0.3099 0.3448 0.1606  -0.0717 0.0529  22  LYS E N   
7896  C CA  . LYS E 22  ? 0.3600 0.3422 0.3545 0.1545  -0.0786 0.0515  22  LYS E CA  
7897  C C   . LYS E 22  ? 0.3396 0.3947 0.3663 0.1469  -0.0816 0.0487  22  LYS E C   
7898  O O   . LYS E 22  ? 0.3436 0.4192 0.3693 0.1588  -0.0794 0.0474  22  LYS E O   
7899  C CB  . LYS E 22  ? 0.3922 0.3710 0.3592 0.1849  -0.0823 0.0512  22  LYS E CB  
7900  C CG  . LYS E 22  ? 0.4165 0.3289 0.3547 0.1810  -0.0803 0.0537  22  LYS E CG  
7901  C CD  . LYS E 22  ? 0.4698 0.3525 0.3604 0.2177  -0.0818 0.0546  22  LYS E CD  
7902  C CE  . LYS E 22  ? 0.4648 0.4148 0.3698 0.2389  -0.0900 0.0522  22  LYS E CE  
7903  N NZ  . LYS E 22  ? 0.5152 0.4325 0.3734 0.2730  -0.0928 0.0537  22  LYS E NZ  
7904  N N   . ASN E 23  ? 0.3261 0.4181 0.3771 0.1245  -0.0862 0.0472  23  ASN E N   
7905  C CA  . ASN E 23  ? 0.3154 0.4765 0.3908 0.1081  -0.0888 0.0437  23  ASN E CA  
7906  C C   . ASN E 23  ? 0.2908 0.4487 0.3772 0.0893  -0.0846 0.0448  23  ASN E C   
7907  O O   . ASN E 23  ? 0.2860 0.4947 0.3808 0.0918  -0.0841 0.0420  23  ASN E O   
7908  C CB  . ASN E 23  ? 0.3457 0.5747 0.4183 0.1378  -0.0921 0.0393  23  ASN E CB  
7909  C CG  . ASN E 23  ? 0.3829 0.6292 0.4476 0.1529  -0.0976 0.0378  23  ASN E CG  
7910  O OD1 . ASN E 23  ? 0.3786 0.5994 0.4465 0.1325  -0.0994 0.0392  23  ASN E OD1 
7911  N ND2 . ASN E 23  ? 0.4376 0.7294 0.4894 0.1920  -0.1006 0.0347  23  ASN E ND2 
7912  N N   . VAL E 24  ? 0.2732 0.3758 0.3587 0.0716  -0.0817 0.0483  24  VAL E N   
7913  C CA  . VAL E 24  ? 0.2548 0.3487 0.3484 0.0529  -0.0784 0.0500  24  VAL E CA  
7914  C C   . VAL E 24  ? 0.2407 0.3559 0.3453 0.0196  -0.0813 0.0492  24  VAL E C   
7915  O O   . VAL E 24  ? 0.2421 0.3301 0.3428 0.0049  -0.0837 0.0499  24  VAL E O   
7916  C CB  . VAL E 24  ? 0.2546 0.2862 0.3395 0.0496  -0.0745 0.0534  24  VAL E CB  
7917  C CG1 . VAL E 24  ? 0.2454 0.2706 0.3383 0.0306  -0.0722 0.0552  24  VAL E CG1 
7918  C CG2 . VAL E 24  ? 0.2723 0.2733 0.3361 0.0743  -0.0701 0.0539  24  VAL E CG2 
7919  N N   . THR E 25  ? 0.2307 0.3899 0.3431 0.0069  -0.0807 0.0473  25  THR E N   
7920  C CA  . THR E 25  ? 0.2307 0.4042 0.3423 -0.0297 -0.0827 0.0463  25  THR E CA  
7921  C C   . THR E 25  ? 0.2326 0.3461 0.3344 -0.0464 -0.0811 0.0509  25  THR E C   
7922  O O   . THR E 25  ? 0.2262 0.3255 0.3306 -0.0401 -0.0776 0.0534  25  THR E O   
7923  C CB  . THR E 25  ? 0.2295 0.4719 0.3486 -0.0426 -0.0817 0.0424  25  THR E CB  
7924  O OG1 . THR E 25  ? 0.2249 0.5307 0.3528 -0.0161 -0.0830 0.0376  25  THR E OG1 
7925  C CG2 . THR E 25  ? 0.2456 0.5035 0.3543 -0.0863 -0.0837 0.0401  25  THR E CG2 
7926  N N   . VAL E 26  ? 0.2439 0.3229 0.3309 -0.0660 -0.0840 0.0515  26  VAL E N   
7927  C CA  . VAL E 26  ? 0.2551 0.2748 0.3256 -0.0755 -0.0837 0.0555  26  VAL E CA  
7928  C C   . VAL E 26  ? 0.2862 0.2913 0.3306 -0.1105 -0.0854 0.0552  26  VAL E C   
7929  O O   . VAL E 26  ? 0.2982 0.3352 0.3365 -0.1319 -0.0870 0.0513  26  VAL E O   
7930  C CB  . VAL E 26  ? 0.2554 0.2288 0.3197 -0.0602 -0.0852 0.0566  26  VAL E CB  
7931  C CG1 . VAL E 26  ? 0.2325 0.2094 0.3126 -0.0325 -0.0823 0.0570  26  VAL E CG1 
7932  C CG2 . VAL E 26  ? 0.2677 0.2409 0.3230 -0.0684 -0.0891 0.0535  26  VAL E CG2 
7933  N N   . THR E 27  ? 0.3046 0.2595 0.3282 -0.1170 -0.0850 0.0592  27  THR E N   
7934  C CA  . THR E 27  ? 0.3491 0.2716 0.3341 -0.1502 -0.0862 0.0598  27  THR E CA  
7935  C C   . THR E 27  ? 0.3847 0.2580 0.3369 -0.1586 -0.0898 0.0585  27  THR E C   
7936  O O   . THR E 27  ? 0.4279 0.2869 0.3456 -0.1925 -0.0907 0.0565  27  THR E O   
7937  C CB  . THR E 27  ? 0.3677 0.2456 0.3329 -0.1501 -0.0851 0.0650  27  THR E CB  
7938  O OG1 . THR E 27  ? 0.3703 0.1994 0.3283 -0.1229 -0.0869 0.0676  27  THR E OG1 
7939  C CG2 . THR E 27  ? 0.3340 0.2573 0.3296 -0.1427 -0.0812 0.0660  27  THR E CG2 
7940  N N   . HIS E 28  ? 0.3719 0.2189 0.3307 -0.1300 -0.0915 0.0590  28  HIS E N   
7941  C CA  . HIS E 28  ? 0.4038 0.2054 0.3328 -0.1322 -0.0949 0.0571  28  HIS E CA  
7942  C C   . HIS E 28  ? 0.3691 0.1896 0.3270 -0.1053 -0.0958 0.0550  28  HIS E C   
7943  O O   . HIS E 28  ? 0.3334 0.1722 0.3204 -0.0804 -0.0938 0.0564  28  HIS E O   
7944  C CB  . HIS E 28  ? 0.4488 0.1741 0.3345 -0.1243 -0.0968 0.0602  28  HIS E CB  
7945  C CG  . HIS E 28  ? 0.4925 0.1853 0.3402 -0.1491 -0.0960 0.0633  28  HIS E CG  
7946  N ND1 . HIS E 28  ? 0.4736 0.1829 0.3369 -0.1443 -0.0936 0.0671  28  HIS E ND1 
7947  C CD2 . HIS E 28  ? 0.5596 0.2005 0.3488 -0.1819 -0.0969 0.0630  28  HIS E CD2 
7948  C CE1 . HIS E 28  ? 0.5252 0.1961 0.3436 -0.1717 -0.0933 0.0694  28  HIS E CE1 
7949  N NE2 . HIS E 28  ? 0.5810 0.2072 0.3510 -0.1961 -0.0951 0.0670  28  HIS E NE2 
7950  N N   . ALA E 29  ? 0.3856 0.1978 0.3302 -0.1133 -0.0983 0.0515  29  ALA E N   
7951  C CA  . ALA E 29  ? 0.3586 0.1857 0.3255 -0.0911 -0.0993 0.0493  29  ALA E CA  
7952  C C   . ALA E 29  ? 0.3961 0.1791 0.3302 -0.0964 -0.1025 0.0464  29  ALA E C   
7953  O O   . ALA E 29  ? 0.4472 0.1868 0.3380 -0.1191 -0.1038 0.0457  29  ALA E O   
7954  C CB  . ALA E 29  ? 0.3257 0.2189 0.3242 -0.0921 -0.0987 0.0472  29  ALA E CB  
7955  N N   . GLN E 30  ? 0.3775 0.1662 0.3264 -0.0765 -0.1034 0.0444  30  GLN E N   
7956  C CA  . GLN E 30  ? 0.4101 0.1622 0.3306 -0.0790 -0.1063 0.0407  30  GLN E CA  
7957  C C   . GLN E 30  ? 0.3812 0.1704 0.3273 -0.0711 -0.1071 0.0379  30  GLN E C   
7958  O O   . GLN E 30  ? 0.3513 0.1530 0.3204 -0.0471 -0.1059 0.0384  30  GLN E O   
7959  C CB  . GLN E 30  ? 0.4333 0.1330 0.3302 -0.0554 -0.1073 0.0407  30  GLN E CB  
7960  C CG  . GLN E 30  ? 0.4789 0.1306 0.3360 -0.0564 -0.1103 0.0365  30  GLN E CG  
7961  C CD  . GLN E 30  ? 0.5162 0.1133 0.3385 -0.0303 -0.1118 0.0358  30  GLN E CD  
7962  O OE1 . GLN E 30  ? 0.5252 0.1070 0.3386 -0.0200 -0.1114 0.0391  30  GLN E OE1 
7963  N NE2 . GLN E 30  ? 0.5410 0.1105 0.3411 -0.0172 -0.1140 0.0311  30  GLN E NE2 
7964  N N   . ASP E 31  ? 0.3947 0.2019 0.3329 -0.0939 -0.1090 0.0348  31  ASP E N   
7965  C CA  . ASP E 31  ? 0.3771 0.2139 0.3314 -0.0875 -0.1107 0.0319  31  ASP E CA  
7966  C C   . ASP E 31  ? 0.3977 0.1863 0.3306 -0.0755 -0.1121 0.0294  31  ASP E C   
7967  O O   . ASP E 31  ? 0.4443 0.1791 0.3362 -0.0860 -0.1133 0.0275  31  ASP E O   
7968  C CB  . ASP E 31  ? 0.3916 0.2645 0.3387 -0.1177 -0.1125 0.0283  31  ASP E CB  
7969  C CG  . ASP E 31  ? 0.3668 0.2878 0.3372 -0.1072 -0.1146 0.0261  31  ASP E CG  
7970  O OD1 . ASP E 31  ? 0.3515 0.2591 0.3319 -0.0823 -0.1148 0.0268  31  ASP E OD1 
7971  O OD2 . ASP E 31  ? 0.3666 0.3422 0.3429 -0.1245 -0.1160 0.0232  31  ASP E OD2 
7972  N N   . ILE E 32  ? 0.3685 0.1733 0.3239 -0.0529 -0.1118 0.0290  32  ILE E N   
7973  C CA  . ILE E 32  ? 0.3826 0.1544 0.3229 -0.0390 -0.1128 0.0257  32  ILE E CA  
7974  C C   . ILE E 32  ? 0.3752 0.1677 0.3224 -0.0401 -0.1147 0.0226  32  ILE E C   
7975  O O   . ILE E 32  ? 0.3832 0.1561 0.3211 -0.0286 -0.1153 0.0194  32  ILE E O   
7976  C CB  . ILE E 32  ? 0.3609 0.1308 0.3155 -0.0126 -0.1101 0.0269  32  ILE E CB  
7977  C CG1 . ILE E 32  ? 0.3197 0.1320 0.3082 -0.0048 -0.1072 0.0302  32  ILE E CG1 
7978  C CG2 . ILE E 32  ? 0.3801 0.1202 0.3177 -0.0081 -0.1094 0.0286  32  ILE E CG2 
7979  C CD1 . ILE E 32  ? 0.3033 0.1183 0.3012 0.0135  -0.1038 0.0296  32  ILE E CD1 
7980  N N   . LEU E 33  ? 0.3616 0.1982 0.3242 -0.0521 -0.1159 0.0233  33  LEU E N   
7981  C CA  . LEU E 33  ? 0.3552 0.2181 0.3244 -0.0518 -0.1182 0.0209  33  LEU E CA  
7982  C C   . LEU E 33  ? 0.3860 0.2544 0.3338 -0.0816 -0.1212 0.0166  33  LEU E C   
7983  O O   . LEU E 33  ? 0.3896 0.2888 0.3384 -0.1017 -0.1214 0.0166  33  LEU E O   
7984  C CB  . LEU E 33  ? 0.3222 0.2360 0.3200 -0.0379 -0.1179 0.0242  33  LEU E CB  
7985  C CG  . LEU E 33  ? 0.3157 0.2575 0.3188 -0.0302 -0.1207 0.0229  33  LEU E CG  
7986  C CD1 . LEU E 33  ? 0.3145 0.2247 0.3132 -0.0149 -0.1194 0.0225  33  LEU E CD1 
7987  C CD2 . LEU E 33  ? 0.2972 0.2853 0.3174 -0.0140 -0.1210 0.0262  33  LEU E CD2 
7988  N N   . GLU E 34  ? 0.4111 0.2526 0.3375 -0.0867 -0.1230 0.0122  34  GLU E N   
7989  C CA  . GLU E 34  ? 0.4445 0.2906 0.3461 -0.1185 -0.1253 0.0071  34  GLU E CA  
7990  C C   . GLU E 34  ? 0.4188 0.3346 0.3458 -0.1186 -0.1280 0.0062  34  GLU E C   
7991  O O   . GLU E 34  ? 0.4004 0.3247 0.3414 -0.0972 -0.1291 0.0067  34  GLU E O   
7992  C CB  . GLU E 34  ? 0.4873 0.2715 0.3499 -0.1225 -0.1261 0.0022  34  GLU E CB  
7993  C CG  . GLU E 34  ? 0.5311 0.3102 0.3589 -0.1601 -0.1278 -0.0037 34  GLU E CG  
7994  C CD  . GLU E 34  ? 0.5554 0.3464 0.3656 -0.1965 -0.1268 -0.0041 34  GLU E CD  
7995  O OE1 . GLU E 34  ? 0.5940 0.3258 0.3695 -0.2048 -0.1248 -0.0031 34  GLU E OE1 
7996  O OE2 . GLU E 34  ? 0.5377 0.4014 0.3677 -0.2155 -0.1280 -0.0057 34  GLU E OE2 
7997  N N   . LYS E 35  ? 0.4222 0.3904 0.3520 -0.1427 -0.1291 0.0044  35  LYS E N   
7998  C CA  . LYS E 35  ? 0.3977 0.4461 0.3528 -0.1367 -0.1322 0.0034  35  LYS E CA  
7999  C C   . LYS E 35  ? 0.4240 0.5046 0.3611 -0.1690 -0.1352 -0.0036 35  LYS E C   
8000  O O   . LYS E 35  ? 0.4064 0.5555 0.3619 -0.1605 -0.1386 -0.0052 35  LYS E O   
8001  C CB  . LYS E 35  ? 0.3749 0.4829 0.3532 -0.1323 -0.1315 0.0057  35  LYS E CB  
8002  C CG  . LYS E 35  ? 0.3419 0.4466 0.3452 -0.0913 -0.1299 0.0124  35  LYS E CG  
8003  C CD  . LYS E 35  ? 0.3266 0.4815 0.3468 -0.0873 -0.1287 0.0140  35  LYS E CD  
8004  C CE  . LYS E 35  ? 0.3270 0.4354 0.3443 -0.0904 -0.1243 0.0177  35  LYS E CE  
8005  N NZ  . LYS E 35  ? 0.3605 0.4133 0.3479 -0.1229 -0.1230 0.0155  35  LYS E NZ  
8006  N N   . THR E 36  ? 0.4722 0.5011 0.3682 -0.2046 -0.1339 -0.0083 36  THR E N   
8007  C CA  . THR E 36  ? 0.5068 0.5633 0.3772 -0.2454 -0.1356 -0.0161 36  THR E CA  
8008  C C   . THR E 36  ? 0.5453 0.5366 0.3803 -0.2538 -0.1362 -0.0202 36  THR E C   
8009  O O   . THR E 36  ? 0.5584 0.4711 0.3774 -0.2346 -0.1346 -0.0180 36  THR E O   
8010  C CB  . THR E 36  ? 0.5484 0.6040 0.3854 -0.2948 -0.1329 -0.0201 36  THR E CB  
8011  O OG1 . THR E 36  ? 0.5947 0.5441 0.3868 -0.3038 -0.1297 -0.0187 36  THR E OG1 
8012  C CG2 . THR E 36  ? 0.5136 0.6418 0.3846 -0.2893 -0.1322 -0.0174 36  THR E CG2 
8013  N N   . HIS E 37  ? 0.5652 0.5966 0.3874 -0.2821 -0.1384 -0.0270 37  HIS E N   
8014  C CA  . HIS E 37  ? 0.6101 0.5850 0.3920 -0.2984 -0.1388 -0.0326 37  HIS E CA  
8015  C C   . HIS E 37  ? 0.6544 0.6673 0.4034 -0.3550 -0.1391 -0.0416 37  HIS E C   
8016  O O   . HIS E 37  ? 0.6367 0.7411 0.4067 -0.3734 -0.1400 -0.0436 37  HIS E O   
8017  C CB  . HIS E 37  ? 0.5736 0.5653 0.3851 -0.2606 -0.1420 -0.0309 37  HIS E CB  
8018  C CG  . HIS E 37  ? 0.5310 0.6280 0.3835 -0.2494 -0.1462 -0.0305 37  HIS E CG  
8019  N ND1 . HIS E 37  ? 0.5406 0.6860 0.3875 -0.2671 -0.1496 -0.0365 37  HIS E ND1 
8020  C CD2 . HIS E 37  ? 0.4846 0.6462 0.3792 -0.2193 -0.1478 -0.0250 37  HIS E CD2 
8021  C CE1 . HIS E 37  ? 0.5013 0.7397 0.3858 -0.2456 -0.1537 -0.0346 37  HIS E CE1 
8022  N NE2 . HIS E 37  ? 0.4697 0.7160 0.3812 -0.2154 -0.1525 -0.0276 37  HIS E NE2 
8023  N N   . ASN E 38  ? 0.7159 0.6622 0.4106 -0.3832 -0.1381 -0.0480 38  ASN E N   
8024  C CA  . ASN E 38  ? 0.7679 0.7421 0.4212 -0.4446 -0.1375 -0.0577 38  ASN E CA  
8025  C C   . ASN E 38  ? 0.7376 0.8119 0.4223 -0.4463 -0.1420 -0.0623 38  ASN E C   
8026  O O   . ASN E 38  ? 0.7677 0.8981 0.4305 -0.4967 -0.1420 -0.0708 38  ASN E O   
8027  C CB  . ASN E 38  ? 0.8601 0.7117 0.4287 -0.4787 -0.1339 -0.0634 38  ASN E CB  
8028  C CG  . ASN E 38  ? 0.8679 0.6619 0.4257 -0.4498 -0.1356 -0.0647 38  ASN E CG  
8029  O OD1 . ASN E 38  ? 0.8079 0.6601 0.4187 -0.4146 -0.1393 -0.0624 38  ASN E OD1 
8030  N ND2 . ASN E 38  ? 0.9485 0.6237 0.4318 -0.4639 -0.1327 -0.0687 38  ASN E ND2 
8031  N N   . GLY E 39  ? 0.6838 0.7796 0.4149 -0.3933 -0.1458 -0.0570 39  GLY E N   
8032  C CA  . GLY E 39  ? 0.6510 0.8424 0.4148 -0.3837 -0.1510 -0.0594 39  GLY E CA  
8033  C C   . GLY E 39  ? 0.6900 0.8503 0.4192 -0.4047 -0.1519 -0.0665 39  GLY E C   
8034  O O   . GLY E 39  ? 0.6773 0.9198 0.4208 -0.4123 -0.1560 -0.0709 39  GLY E O   
8035  N N   . LYS E 40  ? 0.7397 0.7827 0.4216 -0.4107 -0.1484 -0.0678 40  LYS E N   
8036  C CA  . LYS E 40  ? 0.7931 0.7896 0.4278 -0.4371 -0.1481 -0.0759 40  LYS E CA  
8037  C C   . LYS E 40  ? 0.7964 0.7044 0.4234 -0.3960 -0.1477 -0.0733 40  LYS E C   
8038  O O   . LYS E 40  ? 0.7852 0.6362 0.4191 -0.3616 -0.1457 -0.0671 40  LYS E O   
8039  C CB  . LYS E 40  ? 0.8815 0.8138 0.4391 -0.5001 -0.1433 -0.0841 40  LYS E CB  
8040  C CG  . LYS E 40  ? 0.8926 0.9228 0.4466 -0.5561 -0.1433 -0.0908 40  LYS E CG  
8041  C CD  . LYS E 40  ? 0.9752 0.9382 0.4565 -0.6153 -0.1372 -0.0958 40  LYS E CD  
8042  C CE  . LYS E 40  ? 0.9778 1.0571 0.4633 -0.6710 -0.1367 -0.1027 40  LYS E CE  
8043  N NZ  . LYS E 40  ? 1.0607 1.0769 0.4729 -0.7332 -0.1302 -0.1071 40  LYS E NZ  
8044  N N   . LEU E 41  ? 0.8136 0.7169 0.4256 -0.4013 -0.1494 -0.0789 41  LEU E N   
8045  C CA  . LEU E 41  ? 0.8298 0.6507 0.4235 -0.3710 -0.1485 -0.0794 41  LEU E CA  
8046  C C   . LEU E 41  ? 0.9251 0.6339 0.4336 -0.4046 -0.1441 -0.0873 41  LEU E C   
8047  O O   . LEU E 41  ? 0.9822 0.6896 0.4432 -0.4598 -0.1429 -0.0952 41  LEU E O   
8048  C CB  . LEU E 41  ? 0.8056 0.6760 0.4211 -0.3608 -0.1524 -0.0818 41  LEU E CB  
8049  C CG  . LEU E 41  ? 0.7255 0.6858 0.4120 -0.3191 -0.1570 -0.0735 41  LEU E CG  
8050  C CD1 . LEU E 41  ? 0.7005 0.6212 0.4039 -0.2723 -0.1568 -0.0694 41  LEU E CD1 
8051  C CD2 . LEU E 41  ? 0.6817 0.6943 0.4086 -0.3046 -0.1574 -0.0657 41  LEU E CD2 
8052  N N   . CYS E 42  ? 0.9486 0.5634 0.4322 -0.3718 -0.1417 -0.0857 42  CYS E N   
8053  C CA  . CYS E 42  ? 1.0448 0.5427 0.4423 -0.3941 -0.1376 -0.0909 42  CYS E CA  
8054  C C   . CYS E 42  ? 1.0851 0.4839 0.4424 -0.3555 -0.1363 -0.0939 42  CYS E C   
8055  O O   . CYS E 42  ? 1.0286 0.4505 0.4341 -0.3059 -0.1378 -0.0903 42  CYS E O   
8056  C CB  . CYS E 42  ? 1.0455 0.5303 0.4436 -0.3959 -0.1357 -0.0847 42  CYS E CB  
8057  S SG  . CYS E 42  ? 1.0353 0.6134 0.4482 -0.4552 -0.1356 -0.0851 42  CYS E SG  
8058  N N   . ASP E 43  ? 1.1899 0.4767 0.4524 -0.3790 -0.1332 -0.1010 43  ASP E N   
8059  C CA  . ASP E 43  ? 1.2467 0.4294 0.4556 -0.3397 -0.1320 -0.1051 43  ASP E CA  
8060  C C   . ASP E 43  ? 1.2122 0.3814 0.4496 -0.2862 -0.1320 -0.0977 43  ASP E C   
8061  O O   . ASP E 43  ? 1.2093 0.3779 0.4497 -0.2957 -0.1312 -0.0918 43  ASP E O   
8062  C CB  . ASP E 43  ? 1.3833 0.4362 0.4708 -0.3766 -0.1285 -0.1137 43  ASP E CB  
8063  C CG  . ASP E 43  ? 1.4289 0.4857 0.4772 -0.4318 -0.1277 -0.1231 43  ASP E CG  
8064  O OD1 . ASP E 43  ? 1.3512 0.5179 0.4697 -0.4401 -0.1305 -0.1226 43  ASP E OD1 
8065  O OD2 . ASP E 43  ? 1.5485 0.4948 0.4899 -0.4673 -0.1243 -0.1310 43  ASP E OD2 
8066  N N   . LEU E 44  ? 1.1861 0.3510 0.4446 -0.2320 -0.1329 -0.0985 44  LEU E N   
8067  C CA  . LEU E 44  ? 1.1546 0.3153 0.4397 -0.1800 -0.1329 -0.0930 44  LEU E CA  
8068  C C   . LEU E 44  ? 1.2547 0.2955 0.4507 -0.1510 -0.1316 -0.0992 44  LEU E C   
8069  O O   . LEU E 44  ? 1.2929 0.2949 0.4545 -0.1285 -0.1316 -0.1073 44  LEU E O   
8070  C CB  . LEU E 44  ? 1.0606 0.3063 0.4275 -0.1392 -0.1343 -0.0904 44  LEU E CB  
8071  C CG  . LEU E 44  ? 1.0096 0.2808 0.4203 -0.0940 -0.1339 -0.0842 44  LEU E CG  
8072  C CD1 . LEU E 44  ? 0.9420 0.2820 0.4129 -0.1106 -0.1342 -0.0740 44  LEU E CD1 
8073  C CD2 . LEU E 44  ? 0.9554 0.2768 0.4122 -0.0535 -0.1340 -0.0861 44  LEU E CD2 
8074  N N   . ASP E 45  ? 1.3012 0.2826 0.4565 -0.1491 -0.1307 -0.0956 45  ASP E N   
8075  C CA  . ASP E 45  ? 1.4069 0.2669 0.4683 -0.1163 -0.1301 -0.1005 45  ASP E CA  
8076  C C   . ASP E 45  ? 1.5257 0.2795 0.4814 -0.1452 -0.1286 -0.1105 45  ASP E C   
8077  O O   . ASP E 45  ? 1.6067 0.2725 0.4905 -0.1068 -0.1286 -0.1179 45  ASP E O   
8078  C CB  . ASP E 45  ? 1.3710 0.2561 0.4646 -0.0455 -0.1315 -0.1027 45  ASP E CB  
8079  C CG  . ASP E 45  ? 1.4302 0.2434 0.4717 0.0005  -0.1320 -0.1020 45  ASP E CG  
8080  O OD1 . ASP E 45  ? 1.3743 0.2342 0.4656 0.0106  -0.1324 -0.0936 45  ASP E OD1 
8081  O OD2 . ASP E 45  ? 1.5351 0.2455 0.4839 0.0291  -0.1323 -0.1100 45  ASP E OD2 
8082  N N   . GLY E 46  ? 1.5385 0.3044 0.4828 -0.2125 -0.1271 -0.1115 46  GLY E N   
8083  C CA  . GLY E 46  ? 1.6470 0.3235 0.4943 -0.2523 -0.1250 -0.1215 46  GLY E CA  
8084  C C   . GLY E 46  ? 1.6064 0.3400 0.4896 -0.2552 -0.1260 -0.1280 46  GLY E C   
8085  O O   . GLY E 46  ? 1.6621 0.3686 0.4960 -0.3071 -0.1243 -0.1348 46  GLY E O   
8086  N N   . VAL E 47  ? 1.5118 0.3259 0.4782 -0.2030 -0.1284 -0.1261 47  VAL E N   
8087  C CA  . VAL E 47  ? 1.4778 0.3384 0.4739 -0.1962 -0.1293 -0.1323 47  VAL E CA  
8088  C C   . VAL E 47  ? 1.3798 0.3657 0.4635 -0.2356 -0.1309 -0.1276 47  VAL E C   
8089  O O   . VAL E 47  ? 1.2800 0.3604 0.4520 -0.2230 -0.1326 -0.1184 47  VAL E O   
8090  C CB  . VAL E 47  ? 1.4265 0.3191 0.4671 -0.1249 -0.1306 -0.1332 47  VAL E CB  
8091  C CG1 . VAL E 47  ? 1.3998 0.3345 0.4641 -0.1198 -0.1312 -0.1400 47  VAL E CG1 
8092  C CG2 . VAL E 47  ? 1.5228 0.3031 0.4780 -0.0772 -0.1299 -0.1384 47  VAL E CG2 
8093  N N   . LYS E 48  ? 1.4142 0.3985 0.4684 -0.2808 -0.1305 -0.1344 48  LYS E N   
8094  C CA  . LYS E 48  ? 1.3396 0.4381 0.4615 -0.3216 -0.1325 -0.1312 48  LYS E CA  
8095  C C   . LYS E 48  ? 1.2302 0.4336 0.4482 -0.2847 -0.1357 -0.1270 48  LYS E C   
8096  O O   . LYS E 48  ? 1.2326 0.4152 0.4469 -0.2464 -0.1356 -0.1314 48  LYS E O   
8097  C CB  . LYS E 48  ? 1.4142 0.4824 0.4714 -0.3802 -0.1312 -0.1411 48  LYS E CB  
8098  C CG  . LYS E 48  ? 1.3576 0.5405 0.4676 -0.4308 -0.1332 -0.1390 48  LYS E CG  
8099  C CD  . LYS E 48  ? 1.4129 0.5897 0.4750 -0.4805 -0.1326 -0.1496 48  LYS E CD  
8100  C CE  . LYS E 48  ? 1.3709 0.6624 0.4736 -0.5348 -0.1345 -0.1488 48  LYS E CE  
8101  N NZ  . LYS E 48  ? 1.3948 0.7175 0.4779 -0.5738 -0.1353 -0.1581 48  LYS E NZ  
8102  N N   . PRO E 49  ? 1.1400 0.4544 0.4388 -0.2956 -0.1383 -0.1187 49  PRO E N   
8103  C CA  . PRO E 49  ? 1.0509 0.4557 0.4272 -0.2676 -0.1412 -0.1147 49  PRO E CA  
8104  C C   . PRO E 49  ? 1.0629 0.4922 0.4289 -0.2924 -0.1428 -0.1217 49  PRO E C   
8105  O O   . PRO E 49  ? 1.1128 0.5330 0.4366 -0.3428 -0.1426 -0.1273 49  PRO E O   
8106  C CB  . PRO E 49  ? 0.9726 0.4734 0.4192 -0.2747 -0.1436 -0.1044 49  PRO E CB  
8107  C CG  . PRO E 49  ? 1.0222 0.5074 0.4280 -0.3258 -0.1425 -0.1065 49  PRO E CG  
8108  C CD  . PRO E 49  ? 1.1179 0.4770 0.4381 -0.3273 -0.1386 -0.1123 49  PRO E CD  
8109  N N   . LEU E 50  ? 1.0185 0.4817 0.4215 -0.2598 -0.1442 -0.1216 50  LEU E N   
8110  C CA  . LEU E 50  ? 1.0135 0.5175 0.4211 -0.2786 -0.1465 -0.1264 50  LEU E CA  
8111  C C   . LEU E 50  ? 0.9409 0.5562 0.4138 -0.2919 -0.1509 -0.1182 50  LEU E C   
8112  O O   . LEU E 50  ? 0.8700 0.5425 0.4037 -0.2585 -0.1528 -0.1098 50  LEU E O   
8113  C CB  . LEU E 50  ? 0.9955 0.4949 0.4164 -0.2382 -0.1462 -0.1291 50  LEU E CB  
8114  C CG  . LEU E 50  ? 0.9769 0.5274 0.4140 -0.2486 -0.1489 -0.1322 50  LEU E CG  
8115  C CD1 . LEU E 50  ? 1.0427 0.5713 0.4245 -0.3000 -0.1492 -0.1413 50  LEU E CD1 
8116  C CD2 . LEU E 50  ? 0.9769 0.5039 0.4113 -0.2109 -0.1472 -0.1370 50  LEU E CD2 
8117  N N   . ILE E 51  ? 0.9651 0.6103 0.4198 -0.3406 -0.1523 -0.1214 51  ILE E N   
8118  C CA  . ILE E 51  ? 0.9048 0.6630 0.4151 -0.3514 -0.1571 -0.1153 51  ILE E CA  
8119  C C   . ILE E 51  ? 0.8988 0.7072 0.4148 -0.3620 -0.1607 -0.1198 51  ILE E C   
8120  O O   . ILE E 51  ? 0.9530 0.7519 0.4232 -0.4064 -0.1603 -0.1294 51  ILE E O   
8121  C CB  . ILE E 51  ? 0.9286 0.7132 0.4219 -0.3981 -0.1567 -0.1168 51  ILE E CB  
8122  C CG1 . ILE E 51  ? 0.9338 0.6666 0.4219 -0.3851 -0.1532 -0.1116 51  ILE E CG1 
8123  C CG2 . ILE E 51  ? 0.8688 0.7818 0.4182 -0.4039 -0.1623 -0.1122 51  ILE E CG2 
8124  C CD1 . ILE E 51  ? 0.9368 0.7139 0.4261 -0.4219 -0.1531 -0.1103 51  ILE E CD1 
8125  N N   . LEU E 52  ? 0.8369 0.6971 0.4051 -0.3232 -0.1641 -0.1127 52  LEU E N   
8126  C CA  . LEU E 52  ? 0.8273 0.7353 0.4037 -0.3260 -0.1680 -0.1154 52  LEU E CA  
8127  C C   . LEU E 52  ? 0.8129 0.8224 0.4070 -0.3547 -0.1736 -0.1154 52  LEU E C   
8128  O O   . LEU E 52  ? 0.8148 0.8685 0.4079 -0.3650 -0.1773 -0.1192 52  LEU E O   
8129  C CB  . LEU E 52  ? 0.7730 0.6990 0.3925 -0.2767 -0.1696 -0.1072 52  LEU E CB  
8130  C CG  . LEU E 52  ? 0.7801 0.6284 0.3889 -0.2456 -0.1644 -0.1081 52  LEU E CG  
8131  C CD1 . LEU E 52  ? 0.7275 0.6067 0.3781 -0.2058 -0.1656 -0.0998 52  LEU E CD1 
8132  C CD2 . LEU E 52  ? 0.8420 0.6220 0.3960 -0.2600 -0.1613 -0.1205 52  LEU E CD2 
8133  N N   . ARG E 53  ? 0.7992 0.8507 0.4091 -0.3662 -0.1742 -0.1118 53  ARG E N   
8134  C CA  . ARG E 53  ? 0.7830 0.9450 0.4129 -0.3889 -0.1795 -0.1124 53  ARG E CA  
8135  C C   . ARG E 53  ? 0.7293 0.9700 0.4058 -0.3479 -0.1865 -0.1047 53  ARG E C   
8136  O O   . ARG E 53  ? 0.6867 0.9290 0.3985 -0.3021 -0.1875 -0.0939 53  ARG E O   
8137  C CB  . ARG E 53  ? 0.8449 1.0142 0.4243 -0.4521 -0.1784 -0.1258 53  ARG E CB  
8138  C CG  . ARG E 53  ? 0.8362 1.1242 0.4303 -0.4852 -0.1824 -0.1288 53  ARG E CG  
8139  C CD  . ARG E 53  ? 0.8995 1.2042 0.4416 -0.5531 -0.1811 -0.1431 53  ARG E CD  
8140  N NE  . ARG E 53  ? 0.9625 1.2115 0.4509 -0.6075 -0.1743 -0.1503 53  ARG E NE  
8141  C CZ  . ARG E 53  ? 1.0384 1.1574 0.4568 -0.6348 -0.1675 -0.1569 53  ARG E CZ  
8142  N NH1 . ARG E 53  ? 1.0591 1.0932 0.4550 -0.6122 -0.1661 -0.1584 53  ARG E NH1 
8143  N NH2 . ARG E 53  ? 1.1005 1.1715 0.4653 -0.6847 -0.1617 -0.1625 53  ARG E NH2 
8144  N N   . ASP E 54  ? 0.7377 1.0369 0.4088 -0.3636 -0.1911 -0.1100 54  ASP E N   
8145  C CA  . ASP E 54  ? 0.6971 1.0672 0.4031 -0.3239 -0.1984 -0.1026 54  ASP E CA  
8146  C C   . ASP E 54  ? 0.6972 1.0103 0.3968 -0.2991 -0.1977 -0.1008 54  ASP E C   
8147  O O   . ASP E 54  ? 0.6709 1.0239 0.3918 -0.2644 -0.2031 -0.0937 54  ASP E O   
8148  C CB  . ASP E 54  ? 0.7028 1.1867 0.4101 -0.3498 -0.2050 -0.1087 54  ASP E CB  
8149  C CG  . ASP E 54  ? 0.6876 1.2599 0.4147 -0.3585 -0.2075 -0.1082 54  ASP E CG  
8150  O OD1 . ASP E 54  ? 0.6491 1.2449 0.4097 -0.3132 -0.2100 -0.0977 54  ASP E OD1 
8151  O OD2 . ASP E 54  ? 0.7182 1.3371 0.4241 -0.4124 -0.2066 -0.1190 54  ASP E OD2 
8152  N N   . CYS E 55  ? 0.7321 0.9518 0.3978 -0.3156 -0.1913 -0.1077 55  CYS E N   
8153  C CA  . CYS E 55  ? 0.7317 0.8967 0.3919 -0.2907 -0.1895 -0.1070 55  CYS E CA  
8154  C C   . CYS E 55  ? 0.6975 0.8196 0.3820 -0.2465 -0.1865 -0.0970 55  CYS E C   
8155  O O   . CYS E 55  ? 0.6897 0.7896 0.3815 -0.2425 -0.1834 -0.0938 55  CYS E O   
8156  C CB  . CYS E 55  ? 0.7884 0.8730 0.3982 -0.3210 -0.1839 -0.1196 55  CYS E CB  
8157  S SG  . CYS E 55  ? 0.8325 0.9576 0.4079 -0.3694 -0.1871 -0.1319 55  CYS E SG  
8158  N N   . SER E 56  ? 0.6794 0.7924 0.3738 -0.2164 -0.1871 -0.0924 56  SER E N   
8159  C CA  . SER E 56  ? 0.6543 0.7247 0.3643 -0.1812 -0.1830 -0.0849 56  SER E CA  
8160  C C   . SER E 56  ? 0.6792 0.6735 0.3641 -0.1831 -0.1763 -0.0933 56  SER E C   
8161  O O   . SER E 56  ? 0.7190 0.6858 0.3709 -0.2090 -0.1749 -0.1043 56  SER E O   
8162  C CB  . SER E 56  ? 0.6300 0.7310 0.3567 -0.1503 -0.1869 -0.0753 56  SER E CB  
8163  O OG  . SER E 56  ? 0.6448 0.7239 0.3552 -0.1506 -0.1857 -0.0801 56  SER E OG  
8164  N N   . VAL E 57  ? 0.6598 0.6220 0.3565 -0.1550 -0.1719 -0.0890 57  VAL E N   
8165  C CA  . VAL E 57  ? 0.6806 0.5828 0.3563 -0.1485 -0.1657 -0.0973 57  VAL E CA  
8166  C C   . VAL E 57  ? 0.6941 0.5988 0.3555 -0.1499 -0.1663 -0.1029 57  VAL E C   
8167  O O   . VAL E 57  ? 0.7310 0.5949 0.3608 -0.1589 -0.1633 -0.1143 57  VAL E O   
8168  C CB  . VAL E 57  ? 0.6537 0.5387 0.3488 -0.1195 -0.1610 -0.0917 57  VAL E CB  
8169  C CG1 . VAL E 57  ? 0.6755 0.5143 0.3498 -0.1085 -0.1550 -0.1016 57  VAL E CG1 
8170  C CG2 . VAL E 57  ? 0.6416 0.5218 0.3497 -0.1179 -0.1602 -0.0865 57  VAL E CG2 
8171  N N   . ALA E 58  ? 0.6693 0.6175 0.3490 -0.1395 -0.1702 -0.0949 58  ALA E N   
8172  C CA  . ALA E 58  ? 0.6804 0.6371 0.3477 -0.1414 -0.1714 -0.0987 58  ALA E CA  
8173  C C   . ALA E 58  ? 0.7132 0.6770 0.3559 -0.1714 -0.1746 -0.1083 58  ALA E C   
8174  O O   . ALA E 58  ? 0.7425 0.6762 0.3590 -0.1796 -0.1719 -0.1187 58  ALA E O   
8175  C CB  . ALA E 58  ? 0.6568 0.6555 0.3407 -0.1254 -0.1760 -0.0868 58  ALA E CB  
8176  N N   . GLY E 59  ? 0.7108 0.7172 0.3595 -0.1888 -0.1799 -0.1056 59  GLY E N   
8177  C CA  . GLY E 59  ? 0.7440 0.7664 0.3675 -0.2244 -0.1827 -0.1151 59  GLY E CA  
8178  C C   . GLY E 59  ? 0.7931 0.7443 0.3752 -0.2467 -0.1767 -0.1281 59  GLY E C   
8179  O O   . GLY E 59  ? 0.8332 0.7646 0.3813 -0.2679 -0.1761 -0.1386 59  GLY E O   
8180  N N   . TRP E 60  ? 0.7966 0.7044 0.3757 -0.2407 -0.1724 -0.1275 60  TRP E N   
8181  C CA  . TRP E 60  ? 0.8531 0.6797 0.3836 -0.2543 -0.1668 -0.1390 60  TRP E CA  
8182  C C   . TRP E 60  ? 0.8740 0.6526 0.3831 -0.2338 -0.1626 -0.1467 60  TRP E C   
8183  O O   . TRP E 60  ? 0.9298 0.6645 0.3910 -0.2520 -0.1608 -0.1586 60  TRP E O   
8184  C CB  . TRP E 60  ? 0.8502 0.6423 0.3839 -0.2444 -0.1636 -0.1351 60  TRP E CB  
8185  C CG  . TRP E 60  ? 0.9026 0.6031 0.3898 -0.2357 -0.1575 -0.1443 60  TRP E CG  
8186  C CD1 . TRP E 60  ? 0.9765 0.6099 0.4000 -0.2552 -0.1548 -0.1572 60  TRP E CD1 
8187  C CD2 . TRP E 60  ? 0.8920 0.5568 0.3870 -0.2026 -0.1536 -0.1416 60  TRP E CD2 
8188  N NE1 . TRP E 60  ? 1.0155 0.5707 0.4041 -0.2312 -0.1499 -0.1625 60  TRP E NE1 
8189  C CE2 . TRP E 60  ? 0.9618 0.5402 0.3961 -0.1988 -0.1493 -0.1532 60  TRP E CE2 
8190  C CE3 . TRP E 60  ? 0.8348 0.5316 0.3782 -0.1752 -0.1534 -0.1308 60  TRP E CE3 
8191  C CZ2 . TRP E 60  ? 0.9731 0.5042 0.3970 -0.1652 -0.1454 -0.1544 60  TRP E CZ2 
8192  C CZ3 . TRP E 60  ? 0.8427 0.4948 0.3783 -0.1474 -0.1490 -0.1322 60  TRP E CZ3 
8193  C CH2 . TRP E 60  ? 0.9096 0.4838 0.3876 -0.1409 -0.1454 -0.1439 60  TRP E CH2 
8194  N N   . LEU E 61  ? 0.8330 0.6225 0.3743 -0.1977 -0.1609 -0.1407 61  LEU E N   
8195  C CA  . LEU E 61  ? 0.8487 0.6033 0.3735 -0.1753 -0.1563 -0.1487 61  LEU E CA  
8196  C C   . LEU E 61  ? 0.8587 0.6329 0.3735 -0.1840 -0.1580 -0.1540 61  LEU E C   
8197  O O   . LEU E 61  ? 0.9001 0.6319 0.3786 -0.1806 -0.1545 -0.1660 61  LEU E O   
8198  C CB  . LEU E 61  ? 0.8025 0.5742 0.3640 -0.1409 -0.1534 -0.1415 61  LEU E CB  
8199  C CG  . LEU E 61  ? 0.7984 0.5421 0.3645 -0.1261 -0.1503 -0.1390 61  LEU E CG  
8200  C CD1 . LEU E 61  ? 0.7564 0.5239 0.3555 -0.0966 -0.1469 -0.1336 61  LEU E CD1 
8201  C CD2 . LEU E 61  ? 0.8608 0.5310 0.3750 -0.1235 -0.1467 -0.1515 61  LEU E CD2 
8202  N N   . LEU E 62  ? 0.8250 0.6620 0.3683 -0.1924 -0.1636 -0.1454 62  LEU E N   
8203  C CA  . LEU E 62  ? 0.8356 0.6951 0.3683 -0.2031 -0.1661 -0.1497 62  LEU E CA  
8204  C C   . LEU E 62  ? 0.8861 0.7311 0.3788 -0.2406 -0.1679 -0.1600 62  LEU E C   
8205  O O   . LEU E 62  ? 0.9089 0.7561 0.3811 -0.2522 -0.1686 -0.1672 62  LEU E O   
8206  C CB  . LEU E 62  ? 0.7909 0.7187 0.3597 -0.1963 -0.1721 -0.1367 62  LEU E CB  
8207  C CG  . LEU E 62  ? 0.7546 0.6892 0.3494 -0.1652 -0.1696 -0.1277 62  LEU E CG  
8208  C CD1 . LEU E 62  ? 0.7232 0.7100 0.3430 -0.1568 -0.1759 -0.1131 62  LEU E CD1 
8209  C CD2 . LEU E 62  ? 0.7673 0.6849 0.3475 -0.1566 -0.1651 -0.1355 62  LEU E CD2 
8210  N N   . GLY E 63  ? 0.9078 0.7367 0.3857 -0.2626 -0.1680 -0.1611 63  GLY E N   
8211  C CA  . GLY E 63  ? 0.9651 0.7758 0.3968 -0.3060 -0.1686 -0.1716 63  GLY E CA  
8212  C C   . GLY E 63  ? 0.9447 0.8413 0.3964 -0.3312 -0.1759 -0.1676 63  GLY E C   
8213  O O   . GLY E 63  ? 0.9787 0.8830 0.4017 -0.3592 -0.1772 -0.1762 63  GLY E O   
8214  N N   . ASN E 64  ? 0.8919 0.8552 0.3909 -0.3189 -0.1807 -0.1549 64  ASN E N   
8215  C CA  . ASN E 64  ? 0.8743 0.9287 0.3920 -0.3375 -0.1883 -0.1510 64  ASN E CA  
8216  C C   . ASN E 64  ? 0.9276 0.9817 0.4041 -0.3918 -0.1877 -0.1626 64  ASN E C   
8217  O O   . ASN E 64  ? 0.9575 0.9610 0.4095 -0.4092 -0.1831 -0.1664 64  ASN E O   
8218  C CB  . ASN E 64  ? 0.8197 0.9304 0.3855 -0.3108 -0.1925 -0.1366 64  ASN E CB  
8219  C CG  . ASN E 64  ? 0.8054 1.0167 0.3882 -0.3262 -0.2006 -0.1336 64  ASN E CG  
8220  O OD1 . ASN E 64  ? 0.8374 1.0738 0.3970 -0.3696 -0.2012 -0.1429 64  ASN E OD1 
8221  N ND2 . ASN E 64  ? 0.7626 1.0323 0.3815 -0.2901 -0.2067 -0.1210 64  ASN E ND2 
8222  N N   . PRO E 65  ? 0.9450 1.0541 0.4091 -0.4212 -0.1921 -0.1686 65  PRO E N   
8223  C CA  . PRO E 65  ? 1.0058 1.1124 0.4212 -0.4812 -0.1904 -0.1818 65  PRO E CA  
8224  C C   . PRO E 65  ? 1.0058 1.1553 0.4265 -0.5088 -0.1912 -0.1805 65  PRO E C   
8225  O O   . PRO E 65  ? 1.0674 1.1831 0.4366 -0.5604 -0.1870 -0.1915 65  PRO E O   
8226  C CB  . PRO E 65  ? 1.0047 1.1909 0.4223 -0.4987 -0.1967 -0.1855 65  PRO E CB  
8227  C CG  . PRO E 65  ? 0.9362 1.1892 0.4117 -0.4469 -0.2036 -0.1711 65  PRO E CG  
8228  C CD  . PRO E 65  ? 0.9130 1.0906 0.4038 -0.4019 -0.1988 -0.1635 65  PRO E CD  
8229  N N   . MET E 66  ? 0.9440 1.1638 0.4209 -0.4762 -0.1962 -0.1677 66  MET E N   
8230  C CA  . MET E 66  ? 0.9374 1.1997 0.4250 -0.4950 -0.1966 -0.1657 66  MET E CA  
8231  C C   . MET E 66  ? 0.9572 1.1197 0.4262 -0.4906 -0.1891 -0.1648 66  MET E C   
8232  O O   . MET E 66  ? 0.9700 1.1422 0.4310 -0.5170 -0.1874 -0.1659 66  MET E O   
8233  C CB  . MET E 66  ? 0.8681 1.2333 0.4180 -0.4540 -0.2045 -0.1523 66  MET E CB  
8234  C CG  . MET E 66  ? 0.8495 1.3217 0.4179 -0.4492 -0.2134 -0.1517 66  MET E CG  
8235  S SD  . MET E 66  ? 0.8829 1.4622 0.4300 -0.5162 -0.2165 -0.1651 66  MET E SD  
8236  C CE  . MET E 66  ? 0.8443 1.5573 0.4274 -0.4830 -0.2289 -0.1596 66  MET E CE  
8237  N N   . CYS E 67  ? 0.9610 1.0333 0.4226 -0.4565 -0.1847 -0.1631 67  CYS E N   
8238  C CA  . CYS E 67  ? 0.9812 0.9584 0.4236 -0.4443 -0.1781 -0.1625 67  CYS E CA  
8239  C C   . CYS E 67  ? 1.0682 0.9360 0.4334 -0.4736 -0.1713 -0.1762 67  CYS E C   
8240  O O   . CYS E 67  ? 1.0895 0.8670 0.4333 -0.4458 -0.1664 -0.1774 67  CYS E O   
8241  C CB  . CYS E 67  ? 0.9292 0.8876 0.4131 -0.3842 -0.1777 -0.1521 67  CYS E CB  
8242  S SG  . CYS E 67  ? 0.8454 0.9149 0.4034 -0.3476 -0.1856 -0.1362 67  CYS E SG  
8243  N N   . ASP E 68  ? 1.1233 1.0010 0.4424 -0.5292 -0.1712 -0.1872 68  ASP E N   
8244  C CA  . ASP E 68  ? 1.2222 0.9894 0.4532 -0.5646 -0.1646 -0.2013 68  ASP E CA  
8245  C C   . ASP E 68  ? 1.2756 0.9499 0.4591 -0.5757 -0.1587 -0.2028 68  ASP E C   
8246  O O   . ASP E 68  ? 1.3575 0.9122 0.4671 -0.5801 -0.1529 -0.2116 68  ASP E O   
8247  C CB  . ASP E 68  ? 1.2727 1.0793 0.4623 -0.6304 -0.1655 -0.2127 68  ASP E CB  
8248  C CG  . ASP E 68  ? 1.2540 1.1085 0.4595 -0.6229 -0.1695 -0.2156 68  ASP E CG  
8249  O OD1 . ASP E 68  ? 1.2164 1.0537 0.4518 -0.5706 -0.1703 -0.2106 68  ASP E OD1 
8250  O OD2 . ASP E 68  ? 1.2793 1.1924 0.4656 -0.6720 -0.1717 -0.2236 68  ASP E OD2 
8251  N N   . GLU E 69  ? 1.2353 0.9614 0.4559 -0.5786 -0.1603 -0.1944 69  GLU E N   
8252  C CA  . GLU E 69  ? 1.2795 0.9206 0.4604 -0.5842 -0.1552 -0.1940 69  GLU E CA  
8253  C C   . GLU E 69  ? 1.2796 0.8288 0.4565 -0.5249 -0.1521 -0.1907 69  GLU E C   
8254  O O   . GLU E 69  ? 1.3552 0.7913 0.4643 -0.5276 -0.1467 -0.1957 69  GLU E O   
8255  C CB  . GLU E 69  ? 1.2198 0.9463 0.4560 -0.5872 -0.1580 -0.1841 69  GLU E CB  
8256  C CG  . GLU E 69  ? 1.2629 0.9068 0.4606 -0.5940 -0.1529 -0.1828 69  GLU E CG  
8257  C CD  . GLU E 69  ? 1.2054 0.9374 0.4569 -0.5989 -0.1555 -0.1739 69  GLU E CD  
8258  O OE1 . GLU E 69  ? 1.1492 1.0071 0.4536 -0.6085 -0.1610 -0.1713 69  GLU E OE1 
8259  O OE2 . GLU E 69  ? 1.2193 0.8950 0.4576 -0.5906 -0.1522 -0.1698 69  GLU E OE2 
8260  N N   . PHE E 70  ? 1.2007 0.7996 0.4453 -0.4719 -0.1554 -0.1828 70  PHE E N   
8261  C CA  . PHE E 70  ? 1.1826 0.7260 0.4400 -0.4142 -0.1529 -0.1787 70  PHE E CA  
8262  C C   . PHE E 70  ? 1.2179 0.7021 0.4423 -0.3896 -0.1505 -0.1874 70  PHE E C   
8263  O O   . PHE E 70  ? 1.1787 0.6609 0.4351 -0.3391 -0.1499 -0.1838 70  PHE E O   
8264  C CB  . PHE E 70  ? 1.0780 0.7105 0.4262 -0.3742 -0.1569 -0.1643 70  PHE E CB  
8265  C CG  . PHE E 70  ? 1.0420 0.7434 0.4241 -0.3956 -0.1599 -0.1565 70  PHE E CG  
8266  C CD1 . PHE E 70  ? 1.0695 0.7247 0.4280 -0.4066 -0.1567 -0.1554 70  PHE E CD1 
8267  C CD2 . PHE E 70  ? 0.9871 0.7997 0.4192 -0.4042 -0.1659 -0.1511 70  PHE E CD2 
8268  C CE1 . PHE E 70  ? 1.0384 0.7610 0.4271 -0.4272 -0.1590 -0.1493 70  PHE E CE1 
8269  C CE2 . PHE E 70  ? 0.9577 0.8400 0.4188 -0.4205 -0.1687 -0.1453 70  PHE E CE2 
8270  C CZ  . PHE E 70  ? 0.9818 0.8209 0.4227 -0.4335 -0.1650 -0.1447 70  PHE E CZ  
8271  N N   . ILE E 71  ? 1.2948 0.7339 0.4527 -0.4273 -0.1488 -0.1997 71  ILE E N   
8272  C CA  . ILE E 71  ? 1.3560 0.7114 0.4586 -0.4071 -0.1452 -0.2108 71  ILE E CA  
8273  C C   . ILE E 71  ? 1.4442 0.6718 0.4694 -0.3939 -0.1397 -0.2167 71  ILE E C   
8274  O O   . ILE E 71  ? 1.5103 0.6838 0.4786 -0.4340 -0.1376 -0.2192 71  ILE E O   
8275  C CB  . ILE E 71  ? 1.4130 0.7608 0.4660 -0.4526 -0.1451 -0.2224 71  ILE E CB  
8276  C CG1 . ILE E 71  ? 1.4855 0.7364 0.4729 -0.4289 -0.1408 -0.2349 71  ILE E CG1 
8277  C CG2 . ILE E 71  ? 1.4909 0.8048 0.4773 -0.5210 -0.1431 -0.2289 71  ILE E CG2 
8278  C CD1 . ILE E 71  ? 1.5154 0.7799 0.4763 -0.4603 -0.1414 -0.2447 71  ILE E CD1 
8279  N N   . ASN E 72  ? 1.4487 0.6313 0.4689 -0.3372 -0.1376 -0.2191 72  ASN E N   
8280  C CA  . ASN E 72  ? 1.5308 0.5960 0.4786 -0.3101 -0.1333 -0.2244 72  ASN E CA  
8281  C C   . ASN E 72  ? 1.5274 0.5786 0.4787 -0.3180 -0.1332 -0.2156 72  ASN E C   
8282  O O   . ASN E 72  ? 1.6247 0.5766 0.4901 -0.3436 -0.1302 -0.2206 72  ASN E O   
8283  C CB  . ASN E 72  ? 1.6665 0.6091 0.4949 -0.3361 -0.1293 -0.2397 72  ASN E CB  
8284  C CG  . ASN E 72  ? 1.6889 0.6109 0.4974 -0.3026 -0.1281 -0.2503 72  ASN E CG  
8285  O OD1 . ASN E 72  ? 1.6171 0.5976 0.4891 -0.2515 -0.1292 -0.2473 72  ASN E OD1 
8286  N ND2 . ASN E 72  ? 1.7938 0.6318 0.5097 -0.3336 -0.1252 -0.2635 72  ASN E ND2 
8287  N N   . VAL E 73  ? 1.4208 0.5665 0.4660 -0.2970 -0.1362 -0.2026 73  VAL E N   
8288  C CA  . VAL E 73  ? 1.4064 0.5513 0.4651 -0.3022 -0.1363 -0.1936 73  VAL E CA  
8289  C C   . VAL E 73  ? 1.4701 0.5122 0.4722 -0.2622 -0.1330 -0.1964 73  VAL E C   
8290  O O   . VAL E 73  ? 1.4721 0.4945 0.4725 -0.2095 -0.1320 -0.2007 73  VAL E O   
8291  C CB  . VAL E 73  ? 1.2812 0.5455 0.4499 -0.2829 -0.1400 -0.1793 73  VAL E CB  
8292  C CG1 . VAL E 73  ? 1.2272 0.5912 0.4444 -0.3215 -0.1441 -0.1753 73  VAL E CG1 
8293  C CG2 . VAL E 73  ? 1.2231 0.5185 0.4412 -0.2238 -0.1399 -0.1771 73  VAL E CG2 
8294  N N   . PRO E 74  ? 1.5243 0.5053 0.4786 -0.2860 -0.1314 -0.1943 74  PRO E N   
8295  C CA  . PRO E 74  ? 1.5810 0.4700 0.4846 -0.2441 -0.1292 -0.1951 74  PRO E CA  
8296  C C   . PRO E 74  ? 1.4773 0.4448 0.4720 -0.1972 -0.1312 -0.1840 74  PRO E C   
8297  O O   . PRO E 74  ? 1.3714 0.4521 0.4591 -0.2045 -0.1338 -0.1750 74  PRO E O   
8298  C CB  . PRO E 74  ? 1.6643 0.4767 0.4945 -0.2949 -0.1272 -0.1949 74  PRO E CB  
8299  C CG  . PRO E 74  ? 1.5905 0.5116 0.4870 -0.3494 -0.1294 -0.1881 74  PRO E CG  
8300  C CD  . PRO E 74  ? 1.5274 0.5356 0.4800 -0.3500 -0.1320 -0.1903 74  PRO E CD  
8301  N N   . GLU E 75  ? 1.5130 0.4189 0.4760 -0.1492 -0.1299 -0.1849 75  GLU E N   
8302  C CA  . GLU E 75  ? 1.4221 0.3999 0.4649 -0.1056 -0.1311 -0.1758 75  GLU E CA  
8303  C C   . GLU E 75  ? 1.3630 0.3937 0.4575 -0.1368 -0.1324 -0.1631 75  GLU E C   
8304  O O   . GLU E 75  ? 1.4179 0.4000 0.4641 -0.1815 -0.1317 -0.1625 75  GLU E O   
8305  C CB  . GLU E 75  ? 1.4799 0.3847 0.4724 -0.0465 -0.1298 -0.1806 75  GLU E CB  
8306  C CG  . GLU E 75  ? 1.5485 0.3679 0.4808 -0.0508 -0.1291 -0.1771 75  GLU E CG  
8307  C CD  . GLU E 75  ? 1.5849 0.3594 0.4862 0.0174  -0.1290 -0.1802 75  GLU E CD  
8308  O OE1 . GLU E 75  ? 1.6791 0.3691 0.4984 0.0511  -0.1281 -0.1918 75  GLU E OE1 
8309  O OE2 . GLU E 75  ? 1.5219 0.3485 0.4791 0.0393  -0.1300 -0.1717 75  GLU E OE2 
8310  N N   . TRP E 76  ? 1.2558 0.3848 0.4439 -0.1140 -0.1339 -0.1538 76  TRP E N   
8311  C CA  . TRP E 76  ? 1.1887 0.3828 0.4360 -0.1383 -0.1355 -0.1418 76  TRP E CA  
8312  C C   . TRP E 76  ? 1.1434 0.3569 0.4296 -0.0974 -0.1350 -0.1347 76  TRP E C   
8313  O O   . TRP E 76  ? 1.1252 0.3499 0.4268 -0.0509 -0.1342 -0.1374 76  TRP E O   
8314  C CB  . TRP E 76  ? 1.1009 0.4032 0.4253 -0.1565 -0.1381 -0.1363 76  TRP E CB  
8315  C CG  . TRP E 76  ? 1.0386 0.3975 0.4164 -0.1160 -0.1382 -0.1358 76  TRP E CG  
8316  C CD1 . TRP E 76  ? 0.9639 0.3833 0.4062 -0.0866 -0.1380 -0.1276 76  TRP E CD1 
8317  C CD2 . TRP E 76  ? 1.0515 0.4100 0.4172 -0.1042 -0.1378 -0.1443 76  TRP E CD2 
8318  N NE1 . TRP E 76  ? 0.9315 0.3887 0.4004 -0.0605 -0.1373 -0.1307 76  TRP E NE1 
8319  C CE2 . TRP E 76  ? 0.9817 0.4048 0.4068 -0.0693 -0.1372 -0.1408 76  TRP E CE2 
8320  C CE3 . TRP E 76  ? 1.1186 0.4276 0.4259 -0.1221 -0.1374 -0.1550 76  TRP E CE3 
8321  C CZ2 . TRP E 76  ? 0.9748 0.4182 0.4047 -0.0522 -0.1364 -0.1476 76  TRP E CZ2 
8322  C CZ3 . TRP E 76  ? 1.1094 0.4377 0.4236 -0.1015 -0.1369 -0.1617 76  TRP E CZ3 
8323  C CH2 . TRP E 76  ? 1.0370 0.4339 0.4130 -0.0669 -0.1364 -0.1579 76  TRP E CH2 
8324  N N   . SER E 77  ? 1.1262 0.3492 0.4274 -0.1169 -0.1354 -0.1263 77  SER E N   
8325  C CA  . SER E 77  ? 1.0731 0.3273 0.4199 -0.0853 -0.1351 -0.1182 77  SER E CA  
8326  C C   . SER E 77  ? 0.9652 0.3289 0.4048 -0.0763 -0.1363 -0.1105 77  SER E C   
8327  O O   . SER E 77  ? 0.9230 0.3190 0.3983 -0.0386 -0.1352 -0.1091 77  SER E O   
8328  C CB  . SER E 77  ? 1.0923 0.3222 0.4233 -0.1133 -0.1350 -0.1119 77  SER E CB  
8329  O OG  . SER E 77  ? 1.0868 0.3490 0.4242 -0.1667 -0.1362 -0.1102 77  SER E OG  
8330  N N   . TYR E 78  ? 0.9277 0.3468 0.3998 -0.1121 -0.1384 -0.1061 78  TYR E N   
8331  C CA  . TYR E 78  ? 0.8408 0.3521 0.3869 -0.1056 -0.1399 -0.0988 78  TYR E CA  
8332  C C   . TYR E 78  ? 0.8355 0.3852 0.3870 -0.1390 -0.1428 -0.1001 78  TYR E C   
8333  O O   . TYR E 78  ? 0.8921 0.4054 0.3958 -0.1727 -0.1433 -0.1060 78  TYR E O   
8334  C CB  . TYR E 78  ? 0.7867 0.3413 0.3797 -0.1036 -0.1402 -0.0879 78  TYR E CB  
8335  C CG  . TYR E 78  ? 0.8025 0.3581 0.3840 -0.1418 -0.1416 -0.0849 78  TYR E CG  
8336  C CD1 . TYR E 78  ? 0.8659 0.3500 0.3927 -0.1554 -0.1399 -0.0878 78  TYR E CD1 
8337  C CD2 . TYR E 78  ? 0.7590 0.3887 0.3798 -0.1635 -0.1446 -0.0795 78  TYR E CD2 
8338  C CE1 . TYR E 78  ? 0.8836 0.3730 0.3971 -0.1958 -0.1405 -0.0858 78  TYR E CE1 
8339  C CE2 . TYR E 78  ? 0.7728 0.4173 0.3845 -0.1992 -0.1456 -0.0781 78  TYR E CE2 
8340  C CZ  . TYR E 78  ? 0.8341 0.4098 0.3930 -0.2184 -0.1432 -0.0815 78  TYR E CZ  
8341  O OH  . TYR E 78  ? 0.8502 0.4455 0.3979 -0.2593 -0.1436 -0.0809 78  TYR E OH  
8342  N N   . ILE E 79  ? 0.7736 0.3946 0.3777 -0.1304 -0.1447 -0.0948 79  ILE E N   
8343  C CA  . ILE E 79  ? 0.7647 0.4316 0.3774 -0.1553 -0.1483 -0.0953 79  ILE E CA  
8344  C C   . ILE E 79  ? 0.7146 0.4544 0.3726 -0.1653 -0.1517 -0.0855 79  ILE E C   
8345  O O   . ILE E 79  ? 0.6700 0.4349 0.3654 -0.1427 -0.1511 -0.0771 79  ILE E O   
8346  C CB  . ILE E 79  ? 0.7439 0.4324 0.3719 -0.1355 -0.1485 -0.0974 79  ILE E CB  
8347  C CG1 . ILE E 79  ? 0.7995 0.4220 0.3785 -0.1258 -0.1455 -0.1091 79  ILE E CG1 
8348  C CG2 . ILE E 79  ? 0.7290 0.4729 0.3708 -0.1567 -0.1530 -0.0962 79  ILE E CG2 
8349  C CD1 . ILE E 79  ? 0.7768 0.4188 0.3726 -0.0988 -0.1441 -0.1116 79  ILE E CD1 
8350  N N   . VAL E 80  ? 0.7262 0.5021 0.3775 -0.1984 -0.1551 -0.0874 80  VAL E N   
8351  C CA  . VAL E 80  ? 0.6844 0.5398 0.3749 -0.2046 -0.1591 -0.0797 80  VAL E CA  
8352  C C   . VAL E 80  ? 0.6678 0.5858 0.3737 -0.2078 -0.1641 -0.0796 80  VAL E C   
8353  O O   . VAL E 80  ? 0.7027 0.6239 0.3804 -0.2375 -0.1655 -0.0876 80  VAL E O   
8354  C CB  . VAL E 80  ? 0.7116 0.5743 0.3827 -0.2424 -0.1592 -0.0821 80  VAL E CB  
8355  C CG1 . VAL E 80  ? 0.6654 0.6187 0.3798 -0.2413 -0.1633 -0.0747 80  VAL E CG1 
8356  C CG2 . VAL E 80  ? 0.7392 0.5297 0.3855 -0.2401 -0.1545 -0.0823 80  VAL E CG2 
8357  N N   . GLU E 81  ? 0.6211 0.5848 0.3662 -0.1775 -0.1666 -0.0705 81  GLU E N   
8358  C CA  . GLU E 81  ? 0.6065 0.6263 0.3646 -0.1714 -0.1718 -0.0685 81  GLU E CA  
8359  C C   . GLU E 81  ? 0.5745 0.6657 0.3635 -0.1575 -0.1765 -0.0596 81  GLU E C   
8360  O O   . GLU E 81  ? 0.5518 0.6371 0.3597 -0.1358 -0.1748 -0.0522 81  GLU E O   
8361  C CB  . GLU E 81  ? 0.5941 0.5877 0.3571 -0.1426 -0.1701 -0.0658 81  GLU E CB  
8362  C CG  . GLU E 81  ? 0.5868 0.6248 0.3550 -0.1349 -0.1752 -0.0635 81  GLU E CG  
8363  C CD  . GLU E 81  ? 0.5768 0.5886 0.3473 -0.1090 -0.1728 -0.0599 81  GLU E CD  
8364  O OE1 . GLU E 81  ? 0.5587 0.5491 0.3412 -0.0885 -0.1690 -0.0539 81  GLU E OE1 
8365  O OE2 . GLU E 81  ? 0.5888 0.6037 0.3472 -0.1120 -0.1743 -0.0635 81  GLU E OE2 
8366  N N   . LYS E 82  ? 0.5769 0.7378 0.3686 -0.1682 -0.1826 -0.0611 82  LYS E N   
8367  C CA  . LYS E 82  ? 0.5521 0.7881 0.3688 -0.1470 -0.1882 -0.0535 82  LYS E CA  
8368  C C   . LYS E 82  ? 0.5345 0.7623 0.3618 -0.1024 -0.1898 -0.0432 82  LYS E C   
8369  O O   . LYS E 82  ? 0.5391 0.7172 0.3565 -0.0940 -0.1871 -0.0429 82  LYS E O   
8370  C CB  . LYS E 82  ? 0.5623 0.8841 0.3760 -0.1678 -0.1948 -0.0591 82  LYS E CB  
8371  C CG  . LYS E 82  ? 0.5817 0.9322 0.3847 -0.2141 -0.1934 -0.0680 82  LYS E CG  
8372  C CD  . LYS E 82  ? 0.5898 1.0416 0.3917 -0.2358 -0.1999 -0.0744 82  LYS E CD  
8373  C CE  . LYS E 82  ? 0.6041 1.1073 0.4002 -0.2792 -0.1988 -0.0818 82  LYS E CE  
8374  N NZ  . LYS E 82  ? 0.6515 1.0849 0.4058 -0.3334 -0.1923 -0.0920 82  LYS E NZ  
8375  N N   . ALA E 83  ? 0.5209 0.7958 0.3629 -0.0746 -0.1940 -0.0354 83  ALA E N   
8376  C CA  . ALA E 83  ? 0.5183 0.7771 0.3581 -0.0327 -0.1955 -0.0250 83  ALA E CA  
8377  C C   . ALA E 83  ? 0.5347 0.8153 0.3598 -0.0231 -0.2011 -0.0247 83  ALA E C   
8378  O O   . ALA E 83  ? 0.5434 0.7745 0.3546 -0.0090 -0.1990 -0.0206 83  ALA E O   
8379  C CB  . ALA E 83  ? 0.5089 0.8074 0.3589 -0.0028 -0.1988 -0.0174 83  ALA E CB  
8380  N N   . ASN E 84  ? 0.5415 0.8996 0.3681 -0.0333 -0.2079 -0.0295 84  ASN E N   
8381  C CA  . ASN E 84  ? 0.5576 0.9467 0.3703 -0.0247 -0.2142 -0.0298 84  ASN E CA  
8382  C C   . ASN E 84  ? 0.5672 0.9969 0.3770 -0.0681 -0.2157 -0.0421 84  ASN E C   
8383  O O   . ASN E 84  ? 0.5713 1.0888 0.3836 -0.0719 -0.2228 -0.0456 84  ASN E O   
8384  C CB  . ASN E 84  ? 0.5637 1.0199 0.3741 0.0171  -0.2231 -0.0224 84  ASN E CB  
8385  C CG  . ASN E 84  ? 0.5658 0.9787 0.3705 0.0583  -0.2214 -0.0110 84  ASN E CG  
8386  O OD1 . ASN E 84  ? 0.5723 0.9021 0.3640 0.0658  -0.2156 -0.0055 84  ASN E OD1 
8387  N ND2 . ASN E 84  ? 0.5641 1.0361 0.3757 0.0839  -0.2262 -0.0081 84  ASN E ND2 
8388  N N   . PRO E 85  ? 0.5759 0.9429 0.3757 -0.1001 -0.2091 -0.0493 85  PRO E N   
8389  C CA  . PRO E 85  ? 0.5958 0.9855 0.3823 -0.1444 -0.2095 -0.0616 85  PRO E CA  
8390  C C   . PRO E 85  ? 0.6061 1.0456 0.3836 -0.1399 -0.2165 -0.0630 85  PRO E C   
8391  O O   . PRO E 85  ? 0.6076 1.0133 0.3783 -0.1137 -0.2171 -0.0572 85  PRO E O   
8392  C CB  . PRO E 85  ? 0.6105 0.9045 0.3801 -0.1637 -0.2011 -0.0672 85  PRO E CB  
8393  C CG  . PRO E 85  ? 0.5916 0.8310 0.3734 -0.1369 -0.1960 -0.0592 85  PRO E CG  
8394  C CD  . PRO E 85  ? 0.5734 0.8475 0.3690 -0.0955 -0.2010 -0.0474 85  PRO E CD  
8395  N N   . VAL E 86  ? 0.6156 1.1369 0.3909 -0.1677 -0.2213 -0.0711 86  VAL E N   
8396  C CA  . VAL E 86  ? 0.6248 1.2089 0.3927 -0.1631 -0.2289 -0.0729 86  VAL E CA  
8397  C C   . VAL E 86  ? 0.6452 1.1729 0.3907 -0.1856 -0.2257 -0.0793 86  VAL E C   
8398  O O   . VAL E 86  ? 0.6487 1.1825 0.3879 -0.1636 -0.2300 -0.0755 86  VAL E O   
8399  C CB  . VAL E 86  ? 0.6306 1.3336 0.4026 -0.1897 -0.2351 -0.0813 86  VAL E CB  
8400  C CG1 . VAL E 86  ? 0.6101 1.3816 0.4046 -0.1617 -0.2390 -0.0756 86  VAL E CG1 
8401  C CG2 . VAL E 86  ? 0.6560 1.3480 0.4094 -0.2565 -0.2292 -0.0956 86  VAL E CG2 
8402  N N   . ASN E 87  ? 0.6640 1.1340 0.3923 -0.2276 -0.2183 -0.0892 87  ASN E N   
8403  C CA  . ASN E 87  ? 0.6896 1.1008 0.3914 -0.2488 -0.2145 -0.0971 87  ASN E CA  
8404  C C   . ASN E 87  ? 0.6812 1.0007 0.3824 -0.2203 -0.2087 -0.0916 87  ASN E C   
8405  O O   . ASN E 87  ? 0.6955 0.9407 0.3831 -0.2332 -0.2012 -0.0965 87  ASN E O   
8406  C CB  . ASN E 87  ? 0.7286 1.1091 0.3998 -0.3044 -0.2090 -0.1109 87  ASN E CB  
8407  C CG  . ASN E 87  ? 0.7473 1.2198 0.4090 -0.3454 -0.2138 -0.1198 87  ASN E CG  
8408  O OD1 . ASN E 87  ? 0.7386 1.2897 0.4096 -0.3358 -0.2212 -0.1189 87  ASN E OD1 
8409  N ND2 . ASN E 87  ? 0.7782 1.2417 0.4166 -0.3932 -0.2094 -0.1290 87  ASN E ND2 
8410  N N   . ASP E 88  ? 0.6632 0.9893 0.3745 -0.1816 -0.2121 -0.0817 88  ASP E N   
8411  C CA  . ASP E 88  ? 0.6569 0.9083 0.3655 -0.1582 -0.2065 -0.0770 88  ASP E CA  
8412  C C   . ASP E 88  ? 0.6746 0.9125 0.3642 -0.1638 -0.2068 -0.0819 88  ASP E C   
8413  O O   . ASP E 88  ? 0.6991 0.9189 0.3693 -0.1955 -0.2042 -0.0938 88  ASP E O   
8414  C CB  . ASP E 88  ? 0.6343 0.8893 0.3581 -0.1158 -0.2085 -0.0626 88  ASP E CB  
8415  C CG  . ASP E 88  ? 0.6296 0.8110 0.3499 -0.0987 -0.2012 -0.0585 88  ASP E CG  
8416  O OD1 . ASP E 88  ? 0.6375 0.7703 0.3494 -0.1152 -0.1946 -0.0671 88  ASP E OD1 
8417  O OD2 . ASP E 88  ? 0.6225 0.7954 0.3441 -0.0686 -0.2020 -0.0473 88  ASP E OD2 
8418  N N   . LEU E 89  ? 0.6687 0.9103 0.3576 -0.1344 -0.2099 -0.0729 89  LEU E N   
8419  C CA  . LEU E 89  ? 0.6851 0.9192 0.3560 -0.1383 -0.2107 -0.0764 89  LEU E CA  
8420  C C   . LEU E 89  ? 0.6943 1.0058 0.3611 -0.1456 -0.2201 -0.0777 89  LEU E C   
8421  O O   . LEU E 89  ? 0.6907 1.0448 0.3595 -0.1163 -0.2275 -0.0675 89  LEU E O   
8422  C CB  . LEU E 89  ? 0.6822 0.8810 0.3472 -0.1071 -0.2091 -0.0661 89  LEU E CB  
8423  C CG  . LEU E 89  ? 0.6826 0.8128 0.3418 -0.1088 -0.1992 -0.0700 89  LEU E CG  
8424  C CD1 . LEU E 89  ? 0.6761 0.7733 0.3442 -0.1229 -0.1925 -0.0779 89  LEU E CD1 
8425  C CD2 . LEU E 89  ? 0.6790 0.7819 0.3337 -0.0814 -0.1971 -0.0579 89  LEU E CD2 
8426  N N   . CYS E 90  ? 0.7119 1.0406 0.3677 -0.1840 -0.2198 -0.0906 90  CYS E N   
8427  C CA  . CYS E 90  ? 0.7221 1.1330 0.3731 -0.1979 -0.2283 -0.0942 90  CYS E CA  
8428  C C   . CYS E 90  ? 0.7270 1.1512 0.3686 -0.1727 -0.2336 -0.0878 90  CYS E C   
8429  O O   . CYS E 90  ? 0.7247 1.2169 0.3696 -0.1499 -0.2429 -0.0807 90  CYS E O   
8430  C CB  . CYS E 90  ? 0.7506 1.1617 0.3812 -0.2500 -0.2253 -0.1105 90  CYS E CB  
8431  S SG  . CYS E 90  ? 0.7798 1.0886 0.3807 -0.2686 -0.2155 -0.1214 90  CYS E SG  
8432  N N   . TYR E 91  ? 0.7371 1.0969 0.3641 -0.1743 -0.2280 -0.0903 91  TYR E N   
8433  C CA  . TYR E 91  ? 0.7447 1.1009 0.3592 -0.1495 -0.2314 -0.0828 91  TYR E CA  
8434  C C   . TYR E 91  ? 0.7344 1.0453 0.3511 -0.1123 -0.2290 -0.0690 91  TYR E C   
8435  O O   . TYR E 91  ? 0.7261 0.9773 0.3476 -0.1148 -0.2202 -0.0705 91  TYR E O   
8436  C CB  . TYR E 91  ? 0.7632 1.0761 0.3589 -0.1705 -0.2259 -0.0928 91  TYR E CB  
8437  C CG  . TYR E 91  ? 0.7772 1.1045 0.3562 -0.1553 -0.2310 -0.0874 91  TYR E CG  
8438  C CD1 . TYR E 91  ? 0.7794 1.0630 0.3484 -0.1274 -0.2288 -0.0768 91  TYR E CD1 
8439  C CD2 . TYR E 91  ? 0.7930 1.1774 0.3617 -0.1713 -0.2379 -0.0931 91  TYR E CD2 
8440  C CE1 . TYR E 91  ? 0.7995 1.0897 0.3463 -0.1150 -0.2333 -0.0714 91  TYR E CE1 
8441  C CE2 . TYR E 91  ? 0.8083 1.2048 0.3593 -0.1561 -0.2429 -0.0878 91  TYR E CE2 
8442  C CZ  . TYR E 91  ? 0.8129 1.1592 0.3517 -0.1274 -0.2407 -0.0766 91  TYR E CZ  
8443  O OH  . TYR E 91  ? 0.8360 1.1878 0.3505 -0.1141 -0.2455 -0.0710 91  TYR E OH  
8444  N N   . PRO E 92  ? 0.7417 1.0784 0.3489 -0.0775 -0.2367 -0.0561 92  PRO E N   
8445  C CA  . PRO E 92  ? 0.7435 1.0322 0.3421 -0.0441 -0.2346 -0.0426 92  PRO E CA  
8446  C C   . PRO E 92  ? 0.7486 0.9602 0.3347 -0.0504 -0.2246 -0.0431 92  PRO E C   
8447  O O   . PRO E 92  ? 0.7591 0.9591 0.3342 -0.0675 -0.2222 -0.0501 92  PRO E O   
8448  C CB  . PRO E 92  ? 0.7704 1.0885 0.3428 -0.0088 -0.2449 -0.0310 92  PRO E CB  
8449  C CG  . PRO E 92  ? 0.7694 1.1764 0.3508 -0.0187 -0.2538 -0.0378 92  PRO E CG  
8450  C CD  . PRO E 92  ? 0.7571 1.1650 0.3533 -0.0668 -0.2478 -0.0539 92  PRO E CD  
8451  N N   . GLY E 93  ? 0.7426 0.9074 0.3295 -0.0374 -0.2188 -0.0364 93  GLY E N   
8452  C CA  . GLY E 93  ? 0.7472 0.8503 0.3226 -0.0446 -0.2089 -0.0375 93  GLY E CA  
8453  C C   . GLY E 93  ? 0.7341 0.7983 0.3185 -0.0382 -0.2017 -0.0335 93  GLY E C   
8454  O O   . GLY E 93  ? 0.7269 0.8014 0.3195 -0.0212 -0.2050 -0.0263 93  GLY E O   
8455  N N   . ASP E 94  ? 0.7316 0.7561 0.3137 -0.0514 -0.1919 -0.0389 94  ASP E N   
8456  C CA  . ASP E 94  ? 0.7182 0.7101 0.3095 -0.0500 -0.1839 -0.0376 94  ASP E CA  
8457  C C   . ASP E 94  ? 0.6979 0.6852 0.3104 -0.0689 -0.1763 -0.0522 94  ASP E C   
8458  O O   . ASP E 94  ? 0.7035 0.6967 0.3121 -0.0824 -0.1750 -0.0624 94  ASP E O   
8459  C CB  . ASP E 94  ? 0.7449 0.6938 0.3029 -0.0460 -0.1784 -0.0297 94  ASP E CB  
8460  C CG  . ASP E 94  ? 0.7813 0.7170 0.3025 -0.0234 -0.1856 -0.0147 94  ASP E CG  
8461  O OD1 . ASP E 94  ? 0.7822 0.7148 0.3036 -0.0034 -0.1891 -0.0061 94  ASP E OD1 
8462  O OD2 . ASP E 94  ? 0.8133 0.7395 0.3015 -0.0236 -0.1879 -0.0117 94  ASP E OD2 
8463  N N   . PHE E 95  ? 0.6780 0.6526 0.3091 -0.0669 -0.1716 -0.0531 95  PHE E N   
8464  C CA  . PHE E 95  ? 0.6656 0.6288 0.3098 -0.0772 -0.1640 -0.0658 95  PHE E CA  
8465  C C   . PHE E 95  ? 0.6641 0.6057 0.3027 -0.0746 -0.1554 -0.0640 95  PHE E C   
8466  O O   . PHE E 95  ? 0.6580 0.5879 0.2996 -0.0665 -0.1542 -0.0551 95  PHE E O   
8467  C CB  . PHE E 95  ? 0.6492 0.6165 0.3151 -0.0780 -0.1654 -0.0690 95  PHE E CB  
8468  C CG  . PHE E 95  ? 0.6530 0.6068 0.3203 -0.0880 -0.1610 -0.0839 95  PHE E CG  
8469  C CD1 . PHE E 95  ? 0.6517 0.5871 0.3182 -0.0834 -0.1527 -0.0912 95  PHE E CD1 
8470  C CD2 . PHE E 95  ? 0.6647 0.6236 0.3279 -0.1015 -0.1650 -0.0912 95  PHE E CD2 
8471  C CE1 . PHE E 95  ? 0.6645 0.5828 0.3244 -0.0852 -0.1493 -0.1050 95  PHE E CE1 
8472  C CE2 . PHE E 95  ? 0.6823 0.6141 0.3338 -0.1086 -0.1608 -0.1048 95  PHE E CE2 
8473  C CZ  . PHE E 95  ? 0.6834 0.5927 0.3323 -0.0969 -0.1533 -0.1115 95  PHE E CZ  
8474  N N   . ASN E 96  ? 0.6720 0.6120 0.3001 -0.0832 -0.1493 -0.0729 96  ASN E N   
8475  C CA  . ASN E 96  ? 0.6743 0.6054 0.2936 -0.0869 -0.1405 -0.0731 96  ASN E CA  
8476  C C   . ASN E 96  ? 0.6522 0.5839 0.2935 -0.0821 -0.1348 -0.0790 96  ASN E C   
8477  O O   . ASN E 96  ? 0.6440 0.5813 0.2988 -0.0782 -0.1341 -0.0903 96  ASN E O   
8478  C CB  . ASN E 96  ? 0.6893 0.6311 0.2926 -0.0983 -0.1355 -0.0831 96  ASN E CB  
8479  C CG  . ASN E 96  ? 0.7017 0.6405 0.2861 -0.1095 -0.1268 -0.0816 96  ASN E CG  
8480  O OD1 . ASN E 96  ? 0.7229 0.6382 0.2816 -0.1137 -0.1273 -0.0688 96  ASN E OD1 
8481  N ND2 . ASN E 96  ? 0.6950 0.6574 0.2862 -0.1144 -0.1186 -0.0952 96  ASN E ND2 
8482  N N   . ASP E 97  ? 0.6490 0.5704 0.2877 -0.0819 -0.1307 -0.0713 97  ASP E N   
8483  C CA  . ASP E 97  ? 0.6282 0.5524 0.2873 -0.0766 -0.1257 -0.0749 97  ASP E CA  
8484  C C   . ASP E 97  ? 0.6103 0.5322 0.2926 -0.0655 -0.1310 -0.0770 97  ASP E C   
8485  O O   . ASP E 97  ? 0.6034 0.5291 0.2970 -0.0598 -0.1281 -0.0877 97  ASP E O   
8486  C CB  . ASP E 97  ? 0.6271 0.5747 0.2871 -0.0811 -0.1169 -0.0890 97  ASP E CB  
8487  C CG  . ASP E 97  ? 0.6447 0.5983 0.2807 -0.0988 -0.1096 -0.0869 97  ASP E CG  
8488  O OD1 . ASP E 97  ? 0.6609 0.5878 0.2764 -0.1060 -0.1103 -0.0736 97  ASP E OD1 
8489  O OD2 . ASP E 97  ? 0.6485 0.6326 0.2809 -0.1060 -0.1029 -0.0992 97  ASP E OD2 
8490  N N   . TYR E 98  ? 0.6083 0.5243 0.2925 -0.0622 -0.1387 -0.0671 98  TYR E N   
8491  C CA  . TYR E 98  ? 0.5965 0.5137 0.2977 -0.0584 -0.1438 -0.0684 98  TYR E CA  
8492  C C   . TYR E 98  ? 0.5784 0.4875 0.2968 -0.0515 -0.1406 -0.0670 98  TYR E C   
8493  O O   . TYR E 98  ? 0.5747 0.4778 0.3021 -0.0501 -0.1406 -0.0739 98  TYR E O   
8494  C CB  . TYR E 98  ? 0.6000 0.5276 0.2988 -0.0564 -0.1526 -0.0581 98  TYR E CB  
8495  C CG  . TYR E 98  ? 0.5936 0.5338 0.3057 -0.0597 -0.1583 -0.0603 98  TYR E CG  
8496  C CD1 . TYR E 98  ? 0.6018 0.5357 0.3123 -0.0708 -0.1576 -0.0726 98  TYR E CD1 
8497  C CD2 . TYR E 98  ? 0.5867 0.5446 0.3067 -0.0529 -0.1644 -0.0505 98  TYR E CD2 
8498  C CE1 . TYR E 98  ? 0.6053 0.5466 0.3192 -0.0811 -0.1620 -0.0749 98  TYR E CE1 
8499  C CE2 . TYR E 98  ? 0.5830 0.5613 0.3135 -0.0613 -0.1691 -0.0533 98  TYR E CE2 
8500  C CZ  . TYR E 98  ? 0.5934 0.5618 0.3196 -0.0786 -0.1676 -0.0654 98  TYR E CZ  
8501  O OH  . TYR E 98  ? 0.5982 0.5828 0.3268 -0.0938 -0.1714 -0.0687 98  TYR E OH  
8502  N N   . GLU E 99  ? 0.5731 0.4766 0.2900 -0.0481 -0.1376 -0.0580 99  GLU E N   
8503  C CA  . GLU E 99  ? 0.5564 0.4537 0.2886 -0.0422 -0.1346 -0.0553 99  GLU E CA  
8504  C C   . GLU E 99  ? 0.5500 0.4520 0.2887 -0.0412 -0.1274 -0.0668 99  GLU E C   
8505  O O   . GLU E 99  ? 0.5393 0.4373 0.2919 -0.0341 -0.1268 -0.0700 99  GLU E O   
8506  C CB  . GLU E 99  ? 0.5623 0.4469 0.2825 -0.0405 -0.1327 -0.0431 99  GLU E CB  
8507  C CG  . GLU E 99  ? 0.5712 0.4511 0.2834 -0.0313 -0.1406 -0.0312 99  GLU E CG  
8508  C CD  . GLU E 99  ? 0.5937 0.4763 0.2835 -0.0321 -0.1454 -0.0288 99  GLU E CD  
8509  O OE1 . GLU E 99  ? 0.6122 0.4847 0.2798 -0.0413 -0.1409 -0.0307 99  GLU E OE1 
8510  O OE2 . GLU E 99  ? 0.5940 0.4933 0.2874 -0.0246 -0.1536 -0.0254 99  GLU E OE2 
8511  N N   . GLU E 100 ? 0.5592 0.4729 0.2855 -0.0471 -0.1221 -0.0735 100 GLU E N   
8512  C CA  . GLU E 100 ? 0.5560 0.4873 0.2866 -0.0421 -0.1156 -0.0865 100 GLU E CA  
8513  C C   . GLU E 100 ? 0.5629 0.4864 0.2946 -0.0305 -0.1185 -0.0974 100 GLU E C   
8514  O O   . GLU E 100 ? 0.5625 0.4872 0.2984 -0.0170 -0.1158 -0.1054 100 GLU E O   
8515  C CB  . GLU E 100 ? 0.5677 0.5221 0.2826 -0.0530 -0.1095 -0.0925 100 GLU E CB  
8516  C CG  . GLU E 100 ? 0.5710 0.5291 0.2752 -0.0680 -0.1036 -0.0852 100 GLU E CG  
8517  C CD  . GLU E 100 ? 0.5566 0.5344 0.2744 -0.0645 -0.0976 -0.0894 100 GLU E CD  
8518  O OE1 . GLU E 100 ? 0.5508 0.5606 0.2780 -0.0540 -0.0943 -0.1029 100 GLU E OE1 
8519  O OE2 . GLU E 100 ? 0.5543 0.5165 0.2709 -0.0703 -0.0963 -0.0795 100 GLU E OE2 
8520  N N   . LEU E 101 ? 0.5756 0.4875 0.2977 -0.0357 -0.1241 -0.0980 101 LEU E N   
8521  C CA  . LEU E 101 ? 0.5944 0.4865 0.3064 -0.0298 -0.1266 -0.1080 101 LEU E CA  
8522  C C   . LEU E 101 ? 0.5914 0.4603 0.3101 -0.0274 -0.1299 -0.1037 101 LEU E C   
8523  O O   . LEU E 101 ? 0.6082 0.4548 0.3164 -0.0164 -0.1287 -0.1119 101 LEU E O   
8524  C CB  . LEU E 101 ? 0.6119 0.4994 0.3091 -0.0415 -0.1315 -0.1098 101 LEU E CB  
8525  C CG  . LEU E 101 ? 0.6438 0.5022 0.3189 -0.0406 -0.1333 -0.1213 101 LEU E CG  
8526  C CD1 . LEU E 101 ? 0.6636 0.5132 0.3233 -0.0207 -0.1278 -0.1355 101 LEU E CD1 
8527  C CD2 . LEU E 101 ? 0.6604 0.5215 0.3211 -0.0556 -0.1374 -0.1233 101 LEU E CD2 
8528  N N   . LYS E 102 ? 0.5750 0.4483 0.3068 -0.0361 -0.1341 -0.0912 102 LYS E N   
8529  C CA  . LYS E 102 ? 0.5692 0.4289 0.3100 -0.0362 -0.1367 -0.0863 102 LYS E CA  
8530  C C   . LYS E 102 ? 0.5598 0.4126 0.3090 -0.0224 -0.1317 -0.0879 102 LYS E C   
8531  O O   . LYS E 102 ? 0.5694 0.3991 0.3143 -0.0190 -0.1325 -0.0902 102 LYS E O   
8532  C CB  . LYS E 102 ? 0.5511 0.4280 0.3061 -0.0419 -0.1412 -0.0728 102 LYS E CB  
8533  C CG  . LYS E 102 ? 0.5614 0.4490 0.3106 -0.0548 -0.1482 -0.0714 102 LYS E CG  
8534  C CD  . LYS E 102 ? 0.5467 0.4592 0.3069 -0.0516 -0.1529 -0.0585 102 LYS E CD  
8535  C CE  . LYS E 102 ? 0.5471 0.4794 0.3129 -0.0611 -0.1591 -0.0566 102 LYS E CE  
8536  N NZ  . LYS E 102 ? 0.5350 0.4961 0.3100 -0.0497 -0.1637 -0.0447 102 LYS E NZ  
8537  N N   . HIS E 103 ? 0.5450 0.4183 0.3027 -0.0167 -0.1265 -0.0868 103 HIS E N   
8538  C CA  . HIS E 103 ? 0.5363 0.4140 0.3023 -0.0042 -0.1216 -0.0894 103 HIS E CA  
8539  C C   . HIS E 103 ? 0.5607 0.4281 0.3104 0.0125  -0.1196 -0.1037 103 HIS E C   
8540  O O   . HIS E 103 ? 0.5653 0.4206 0.3142 0.0267  -0.1186 -0.1063 103 HIS E O   
8541  C CB  . HIS E 103 ? 0.5212 0.4281 0.2938 -0.0081 -0.1157 -0.0867 103 HIS E CB  
8542  C CG  . HIS E 103 ? 0.5106 0.4334 0.2925 0.0020  -0.1103 -0.0903 103 HIS E CG  
8543  N ND1 . HIS E 103 ? 0.4944 0.4112 0.2899 0.0019  -0.1100 -0.0817 103 HIS E ND1 
8544  C CD2 . HIS E 103 ? 0.5147 0.4654 0.2939 0.0140  -0.1051 -0.1023 103 HIS E CD2 
8545  C CE1 . HIS E 103 ? 0.4884 0.4272 0.2894 0.0115  -0.1049 -0.0878 103 HIS E CE1 
8546  N NE2 . HIS E 103 ? 0.5003 0.4633 0.2919 0.0200  -0.1020 -0.1005 103 HIS E NE2 
8547  N N   . LEU E 104 ? 0.5813 0.4514 0.3140 0.0134  -0.1193 -0.1129 104 LEU E N   
8548  C CA  . LEU E 104 ? 0.6150 0.4704 0.3234 0.0341  -0.1178 -0.1274 104 LEU E CA  
8549  C C   . LEU E 104 ? 0.6490 0.4484 0.3334 0.0377  -0.1219 -0.1290 104 LEU E C   
8550  O O   . LEU E 104 ? 0.6796 0.4537 0.3407 0.0607  -0.1207 -0.1377 104 LEU E O   
8551  C CB  . LEU E 104 ? 0.6328 0.4988 0.3251 0.0317  -0.1171 -0.1364 104 LEU E CB  
8552  C CG  . LEU E 104 ? 0.6418 0.5431 0.3267 0.0524  -0.1114 -0.1502 104 LEU E CG  
8553  C CD1 . LEU E 104 ? 0.6071 0.5647 0.3175 0.0449  -0.1059 -0.1465 104 LEU E CD1 
8554  C CD2 . LEU E 104 ? 0.6646 0.5669 0.3296 0.0492  -0.1116 -0.1591 104 LEU E CD2 
8555  N N   . LEU E 105 ? 0.8618 0.4700 0.3329 -0.0242 -0.1211 -0.1339 105 LEU E N   
8556  C CA  . LEU E 105 ? 0.8819 0.4745 0.3359 -0.0330 -0.1255 -0.1278 105 LEU E CA  
8557  C C   . LEU E 105 ? 0.8944 0.4793 0.3372 -0.0341 -0.1271 -0.1246 105 LEU E C   
8558  O O   . LEU E 105 ? 0.9145 0.4826 0.3418 -0.0391 -0.1319 -0.1191 105 LEU E O   
8559  C CB  . LEU E 105 ? 0.8763 0.4804 0.3348 -0.0436 -0.1201 -0.1208 105 LEU E CB  
8560  C CG  . LEU E 105 ? 0.8785 0.4833 0.3373 -0.0475 -0.1228 -0.1215 105 LEU E CG  
8561  C CD1 . LEU E 105 ? 0.8700 0.4932 0.3376 -0.0575 -0.1175 -0.1132 105 LEU E CD1 
8562  C CD2 . LEU E 105 ? 0.9046 0.4830 0.3458 -0.0508 -0.1320 -0.1234 105 LEU E CD2 
8563  N N   . SER E 106 ? 0.8851 0.4821 0.3351 -0.0299 -0.1227 -0.1280 106 SER E N   
8564  C CA  . SER E 106 ? 0.8996 0.4914 0.3365 -0.0301 -0.1248 -0.1267 106 SER E CA  
8565  C C   . SER E 106 ? 0.9176 0.4936 0.3430 -0.0230 -0.1362 -0.1283 106 SER E C   
8566  O O   . SER E 106 ? 0.9360 0.5039 0.3456 -0.0239 -0.1405 -0.1240 106 SER E O   
8567  C CB  . SER E 106 ? 0.8870 0.4955 0.3346 -0.0278 -0.1176 -0.1326 106 SER E CB  
8568  O OG  . SER E 106 ? 0.8769 0.4911 0.3374 -0.0193 -0.1202 -0.1414 106 SER E OG  
8569  N N   . ARG E 107 ? 0.9144 0.4873 0.3483 -0.0154 -0.1404 -0.1337 107 ARG E N   
8570  C CA  . ARG E 107 ? 0.9321 0.4898 0.3586 -0.0072 -0.1505 -0.1344 107 ARG E CA  
8571  C C   . ARG E 107 ? 0.9495 0.4850 0.3664 -0.0087 -0.1549 -0.1306 107 ARG E C   
8572  O O   . ARG E 107 ? 0.9637 0.4849 0.3774 -0.0005 -0.1619 -0.1314 107 ARG E O   
8573  C CB  . ARG E 107 ? 0.9199 0.4882 0.3635 0.0034  -0.1517 -0.1431 107 ARG E CB  
8574  C CG  . ARG E 107 ? 0.9145 0.4978 0.3650 0.0068  -0.1528 -0.1476 107 ARG E CG  
8575  C CD  . ARG E 107 ? 0.9111 0.5000 0.3763 0.0180  -0.1578 -0.1536 107 ARG E CD  
8576  N NE  . ARG E 107 ? 0.8975 0.5064 0.3790 0.0193  -0.1557 -0.1607 107 ARG E NE  
8577  C CZ  . ARG E 107 ? 0.9046 0.5201 0.3877 0.0234  -0.1637 -0.1639 107 ARG E CZ  
8578  N NH1 . ARG E 107 ? 0.9255 0.5307 0.3948 0.0282  -0.1747 -0.1589 107 ARG E NH1 
8579  N NH2 . ARG E 107 ? 0.8920 0.5252 0.3917 0.0224  -0.1609 -0.1718 107 ARG E NH2 
8580  N N   . ILE E 108 ? 0.9498 0.4824 0.3635 -0.0190 -0.1507 -0.1267 108 ILE E N   
8581  C CA  . ILE E 108 ? 0.9670 0.4790 0.3734 -0.0224 -0.1544 -0.1257 108 ILE E CA  
8582  C C   . ILE E 108 ? 0.9854 0.4841 0.3787 -0.0344 -0.1551 -0.1155 108 ILE E C   
8583  O O   . ILE E 108 ? 0.9763 0.4883 0.3712 -0.0437 -0.1491 -0.1105 108 ILE E O   
8584  C CB  . ILE E 108 ? 0.9532 0.4747 0.3693 -0.0248 -0.1501 -0.1320 108 ILE E CB  
8585  C CG1 . ILE E 108 ? 0.9385 0.4713 0.3673 -0.0125 -0.1488 -0.1408 108 ILE E CG1 
8586  C CG2 . ILE E 108 ? 0.9750 0.4746 0.3814 -0.0305 -0.1542 -0.1330 108 ILE E CG2 
8587  C CD1 . ILE E 108 ? 0.9215 0.4713 0.3608 -0.0140 -0.1427 -0.1450 108 ILE E CD1 
8588  N N   . ASN E 109 ? 1.0127 0.4850 0.3950 -0.0337 -0.1617 -0.1119 109 ASN E N   
8589  C CA  . ASN E 109 ? 1.0350 0.4910 0.4061 -0.0453 -0.1627 -0.1011 109 ASN E CA  
8590  C C   . ASN E 109 ? 1.0496 0.4879 0.4199 -0.0540 -0.1644 -0.1035 109 ASN E C   
8591  O O   . ASN E 109 ? 1.0610 0.4931 0.4274 -0.0673 -0.1635 -0.0956 109 ASN E O   
8592  C CB  . ASN E 109 ? 1.0603 0.4975 0.4192 -0.0397 -0.1687 -0.0922 109 ASN E CB  
8593  C CG  . ASN E 109 ? 1.0577 0.5098 0.4093 -0.0413 -0.1661 -0.0837 109 ASN E CG  
8594  O OD1 . ASN E 109 ? 1.0776 0.5204 0.4178 -0.0485 -0.1659 -0.0714 109 ASN E OD1 
8595  N ND2 . ASN E 109 ? 1.0354 0.5107 0.3935 -0.0351 -0.1636 -0.0906 109 ASN E ND2 
8596  N N   . HIS E 110 ? 1.0512 0.4816 0.4252 -0.0472 -0.1668 -0.1148 110 HIS E N   
8597  C CA  . HIS E 110 ? 1.0686 0.4820 0.4399 -0.0558 -0.1688 -0.1202 110 HIS E CA  
8598  C C   . HIS E 110 ? 1.0604 0.4795 0.4366 -0.0497 -0.1680 -0.1347 110 HIS E C   
8599  O O   . HIS E 110 ? 1.0577 0.4750 0.4367 -0.0352 -0.1685 -0.1414 110 HIS E O   
8600  C CB  . HIS E 110 ? 1.1056 0.4819 0.4674 -0.0559 -0.1743 -0.1164 110 HIS E CB  
8601  C CG  . HIS E 110 ? 1.1282 0.4849 0.4865 -0.0697 -0.1763 -0.1200 110 HIS E CG  
8602  N ND1 . HIS E 110 ? 1.1618 0.4830 0.5146 -0.0678 -0.1804 -0.1251 110 HIS E ND1 
8603  C CD2 . HIS E 110 ? 1.1235 0.4916 0.4842 -0.0861 -0.1751 -0.1199 110 HIS E CD2 
8604  C CE1 . HIS E 110 ? 1.1778 0.4882 0.5287 -0.0834 -0.1818 -0.1292 110 HIS E CE1 
8605  N NE2 . HIS E 110 ? 1.1545 0.4943 0.5102 -0.0949 -0.1792 -0.1257 110 HIS E NE2 
8606  N N   . PHE E 111 ? 1.0578 0.4857 0.4351 -0.0614 -0.1669 -0.1386 111 PHE E N   
8607  C CA  . PHE E 111 ? 1.0584 0.4895 0.4358 -0.0586 -0.1667 -0.1521 111 PHE E CA  
8608  C C   . PHE E 111 ? 1.0942 0.4947 0.4609 -0.0673 -0.1718 -0.1589 111 PHE E C   
8609  O O   . PHE E 111 ? 1.1097 0.4983 0.4733 -0.0814 -0.1746 -0.1518 111 PHE E O   
8610  C CB  . PHE E 111 ? 1.0332 0.4977 0.4184 -0.0663 -0.1629 -0.1516 111 PHE E CB  
8611  C CG  . PHE E 111 ? 1.0004 0.4940 0.3980 -0.0555 -0.1566 -0.1502 111 PHE E CG  
8612  C CD1 . PHE E 111 ? 0.9952 0.4886 0.3959 -0.0398 -0.1551 -0.1575 111 PHE E CD1 
8613  C CD2 . PHE E 111 ? 0.9760 0.4973 0.3842 -0.0614 -0.1517 -0.1416 111 PHE E CD2 
8614  C CE1 . PHE E 111 ? 0.9667 0.4862 0.3810 -0.0314 -0.1492 -0.1561 111 PHE E CE1 
8615  C CE2 . PHE E 111 ? 0.9488 0.4940 0.3699 -0.0522 -0.1453 -0.1407 111 PHE E CE2 
8616  C CZ  . PHE E 111 ? 0.9442 0.4884 0.3685 -0.0379 -0.1444 -0.1481 111 PHE E CZ  
8617  N N   . GLU E 112 ? 1.1091 0.4969 0.4710 -0.0590 -0.1724 -0.1730 112 GLU E N   
8618  C CA  . GLU E 112 ? 1.1434 0.5053 0.4947 -0.0682 -0.1763 -0.1841 112 GLU E CA  
8619  C C   . GLU E 112 ? 1.1366 0.5182 0.4848 -0.0687 -0.1747 -0.1972 112 GLU E C   
8620  O O   . GLU E 112 ? 1.1245 0.5175 0.4748 -0.0539 -0.1704 -0.2037 112 GLU E O   
8621  C CB  . GLU E 112 ? 1.1766 0.4995 0.5222 -0.0573 -0.1779 -0.1904 112 GLU E CB  
8622  C CG  . GLU E 112 ? 1.2183 0.5067 0.5540 -0.0700 -0.1822 -0.1991 112 GLU E CG  
8623  C CD  . GLU E 112 ? 1.2503 0.5078 0.5793 -0.0576 -0.1811 -0.2150 112 GLU E CD  
8624  O OE1 . GLU E 112 ? 1.2524 0.4993 0.5862 -0.0398 -0.1790 -0.2119 112 GLU E OE1 
8625  O OE2 . GLU E 112 ? 1.2754 0.5197 0.5945 -0.0656 -0.1824 -0.2310 112 GLU E OE2 
8626  N N   . LYS E 113 ? 1.1456 0.5328 0.4891 -0.0860 -0.1783 -0.2003 113 LYS E N   
8627  C CA  . LYS E 113 ? 1.1412 0.5512 0.4799 -0.0882 -0.1778 -0.2109 113 LYS E CA  
8628  C C   . LYS E 113 ? 1.1764 0.5601 0.5000 -0.0836 -0.1788 -0.2309 113 LYS E C   
8629  O O   . LYS E 113 ? 1.2115 0.5581 0.5276 -0.0891 -0.1827 -0.2374 113 LYS E O   
8630  C CB  . LYS E 113 ? 1.1392 0.5680 0.4793 -0.1090 -0.1825 -0.2059 113 LYS E CB  
8631  C CG  . LYS E 113 ? 1.1270 0.5903 0.4651 -0.1115 -0.1823 -0.2108 113 LYS E CG  
8632  C CD  . LYS E 113 ? 1.0988 0.5987 0.4509 -0.1222 -0.1823 -0.1949 113 LYS E CD  
8633  C CE  . LYS E 113 ? 1.1144 0.6067 0.4686 -0.1432 -0.1892 -0.1891 113 LYS E CE  
8634  N NZ  . LYS E 113 ? 1.0845 0.6142 0.4557 -0.1504 -0.1872 -0.1719 113 LYS E NZ  
8635  N N   . ILE E 114 ? 1.1690 0.5710 0.4885 -0.0731 -0.1744 -0.2404 114 ILE E N   
8636  C CA  . ILE E 114 ? 1.2038 0.5857 0.5068 -0.0689 -0.1739 -0.2611 114 ILE E CA  
8637  C C   . ILE E 114 ? 1.1976 0.6120 0.4921 -0.0702 -0.1722 -0.2689 114 ILE E C   
8638  O O   . ILE E 114 ? 1.1626 0.6146 0.4676 -0.0666 -0.1686 -0.2576 114 ILE E O   
8639  C CB  . ILE E 114 ? 1.2119 0.5730 0.5166 -0.0469 -0.1676 -0.2671 114 ILE E CB  
8640  C CG1 . ILE E 114 ? 1.1718 0.5654 0.4911 -0.0311 -0.1605 -0.2571 114 ILE E CG1 
8641  C CG2 . ILE E 114 ? 1.2308 0.5535 0.5396 -0.0456 -0.1703 -0.2618 114 ILE E CG2 
8642  C CD1 . ILE E 114 ? 1.1802 0.5658 0.4999 -0.0101 -0.1533 -0.2668 114 ILE E CD1 
8643  N N   . GLN E 115 ? 1.2347 0.6338 0.5098 -0.0753 -0.1746 -0.2883 115 GLN E N   
8644  C CA  . GLN E 115 ? 1.2368 0.6649 0.4989 -0.0766 -0.1736 -0.2974 115 GLN E CA  
8645  C C   . GLN E 115 ? 1.2401 0.6688 0.4973 -0.0549 -0.1633 -0.3072 115 GLN E C   
8646  O O   . GLN E 115 ? 1.2699 0.6637 0.5197 -0.0456 -0.1602 -0.3210 115 GLN E O   
8647  C CB  . GLN E 115 ? 1.2785 0.6919 0.5200 -0.0953 -0.1822 -0.3147 115 GLN E CB  
8648  C CG  . GLN E 115 ? 1.3007 0.7273 0.5197 -0.0923 -0.1801 -0.3330 115 GLN E CG  
8649  C CD  . GLN E 115 ? 1.3382 0.7591 0.5376 -0.1145 -0.1909 -0.3484 115 GLN E CD  
8650  O OE1 . GLN E 115 ? 1.3271 0.7683 0.5329 -0.1328 -0.2000 -0.3379 115 GLN E OE1 
8651  N NE2 . GLN E 115 ? 1.3842 0.7785 0.5602 -0.1129 -0.1898 -0.3738 115 GLN E NE2 
8652  N N   . ILE E 116 ? 1.2107 0.6793 0.4737 -0.0466 -0.1573 -0.2990 116 ILE E N   
8653  C CA  . ILE E 116 ? 1.2122 0.6878 0.4723 -0.0266 -0.1465 -0.3064 116 ILE E CA  
8654  C C   . ILE E 116 ? 1.2316 0.7288 0.4696 -0.0293 -0.1450 -0.3186 116 ILE E C   
8655  O O   . ILE E 116 ? 1.2595 0.7447 0.4822 -0.0184 -0.1383 -0.3356 116 ILE E O   
8656  C CB  . ILE E 116 ? 1.1674 0.6692 0.4524 -0.0122 -0.1387 -0.2883 116 ILE E CB  
8657  C CG1 . ILE E 116 ? 1.1311 0.6694 0.4296 -0.0225 -0.1415 -0.2693 116 ILE E CG1 
8658  C CG2 . ILE E 116 ? 1.1610 0.6361 0.4619 -0.0033 -0.1383 -0.2829 116 ILE E CG2 
8659  C CD1 . ILE E 116 ? 1.0923 0.6605 0.4124 -0.0092 -0.1325 -0.2547 116 ILE E CD1 
8660  N N   . ILE E 117 ? 1.2186 0.7487 0.4549 -0.0433 -0.1508 -0.3096 117 ILE E N   
8661  C CA  . ILE E 117 ? 1.2402 0.7932 0.4531 -0.0493 -0.1523 -0.3198 117 ILE E CA  
8662  C C   . ILE E 117 ? 1.2655 0.8109 0.4650 -0.0733 -0.1664 -0.3269 117 ILE E C   
8663  O O   . ILE E 117 ? 1.2423 0.8052 0.4566 -0.0862 -0.1735 -0.3105 117 ILE E O   
8664  C CB  . ILE E 117 ? 1.2047 0.8089 0.4281 -0.0450 -0.1476 -0.3010 117 ILE E CB  
8665  C CG1 . ILE E 117 ? 1.1918 0.8064 0.4220 -0.0225 -0.1330 -0.2992 117 ILE E CG1 
8666  C CG2 . ILE E 117 ? 1.2239 0.8570 0.4252 -0.0575 -0.1540 -0.3055 117 ILE E CG2 
8667  C CD1 . ILE E 117 ? 1.1636 0.7635 0.4209 -0.0097 -0.1270 -0.2892 117 ILE E CD1 
8668  N N   . PRO E 118 ? 1.3149 0.8342 0.4877 -0.0796 -0.1701 -0.3517 118 PRO E N   
8669  C CA  . PRO E 118 ? 1.3415 0.8574 0.5013 -0.1042 -0.1843 -0.3598 118 PRO E CA  
8670  C C   . PRO E 118 ? 1.3321 0.8990 0.4847 -0.1146 -0.1903 -0.3514 118 PRO E C   
8671  O O   . PRO E 118 ? 1.3284 0.9239 0.4708 -0.1031 -0.1832 -0.3510 118 PRO E O   
8672  C CB  . PRO E 118 ? 1.3991 0.8752 0.5308 -0.1056 -0.1845 -0.3909 118 PRO E CB  
8673  C CG  . PRO E 118 ? 1.3996 0.8491 0.5365 -0.0816 -0.1708 -0.3959 118 PRO E CG  
8674  C CD  . PRO E 118 ? 1.3503 0.8380 0.5063 -0.0651 -0.1614 -0.3740 118 PRO E CD  
8675  N N   . LYS E 119 ? 1.3289 0.9082 0.4883 -0.1357 -0.2030 -0.3432 119 LYS E N   
8676  C CA  . LYS E 119 ? 1.3210 0.9501 0.4766 -0.1468 -0.2106 -0.3330 119 LYS E CA  
8677  C C   . LYS E 119 ? 1.3690 1.0037 0.4880 -0.1538 -0.2160 -0.3568 119 LYS E C   
8678  O O   . LYS E 119 ? 1.3659 1.0436 0.4743 -0.1521 -0.2164 -0.3509 119 LYS E O   
8679  C CB  . LYS E 119 ? 1.3093 0.9479 0.4830 -0.1683 -0.2232 -0.3195 119 LYS E CB  
8680  C CG  . LYS E 119 ? 1.2877 0.9828 0.4691 -0.1763 -0.2295 -0.3003 119 LYS E CG  
8681  C CD  . LYS E 119 ? 1.2717 0.9753 0.4770 -0.1947 -0.2393 -0.2846 119 LYS E CD  
8682  C CE  . LYS E 119 ? 1.2633 1.0211 0.4728 -0.2067 -0.2490 -0.2700 119 LYS E CE  
8683  N NZ  . LYS E 119 ? 1.2566 1.0212 0.4875 -0.2273 -0.2597 -0.2585 119 LYS E NZ  
8684  N N   . SER E 120 ? 1.4160 1.0066 0.5155 -0.1616 -0.2199 -0.3837 120 SER E N   
8685  C CA  . SER E 120 ? 1.4687 1.0558 0.5303 -0.1672 -0.2236 -0.4116 120 SER E CA  
8686  C C   . SER E 120 ? 1.4724 1.0698 0.5172 -0.1438 -0.2086 -0.4180 120 SER E C   
8687  O O   . SER E 120 ? 1.4976 1.1211 0.5143 -0.1455 -0.2102 -0.4285 120 SER E O   
8688  C CB  . SER E 120 ? 1.5181 1.0472 0.5666 -0.1772 -0.2276 -0.4395 120 SER E CB  
8689  O OG  . SER E 120 ? 1.5137 1.0016 0.5728 -0.1578 -0.2143 -0.4423 120 SER E OG  
8690  N N   . SER E 121 ? 1.4483 1.0270 0.5107 -0.1221 -0.1942 -0.4108 121 SER E N   
8691  C CA  . SER E 121 ? 1.4534 1.0361 0.5040 -0.0986 -0.1781 -0.4176 121 SER E CA  
8692  C C   . SER E 121 ? 1.4347 1.0738 0.4787 -0.0918 -0.1738 -0.4029 121 SER E C   
8693  O O   . SER E 121 ? 1.4487 1.0951 0.4761 -0.0756 -0.1615 -0.4114 121 SER E O   
8694  C CB  . SER E 121 ? 1.4235 0.9827 0.5014 -0.0779 -0.1651 -0.4074 121 SER E CB  
8695  O OG  . SER E 121 ? 1.4536 0.9578 0.5299 -0.0779 -0.1650 -0.4255 121 SER E OG  
8696  N N   . TRP E 122 ? 1.4040 1.0833 0.4625 -0.1032 -0.1829 -0.3798 122 TRP E N   
8697  C CA  . TRP E 122 ? 1.3895 1.1233 0.4425 -0.0984 -0.1802 -0.3636 122 TRP E CA  
8698  C C   . TRP E 122 ? 1.4384 1.1897 0.4513 -0.1118 -0.1900 -0.3826 122 TRP E C   
8699  O O   . TRP E 122 ? 1.4389 1.2209 0.4498 -0.1296 -0.2045 -0.3740 122 TRP E O   
8700  C CB  . TRP E 122 ? 1.3403 1.1094 0.4263 -0.1044 -0.1856 -0.3311 122 TRP E CB  
8701  C CG  . TRP E 122 ? 1.2948 1.0504 0.4175 -0.0909 -0.1754 -0.3134 122 TRP E CG  
8702  C CD1 . TRP E 122 ? 1.2754 1.0052 0.4221 -0.0978 -0.1800 -0.3076 122 TRP E CD1 
8703  C CD2 . TRP E 122 ? 1.2655 1.0327 0.4042 -0.0688 -0.1590 -0.3001 122 TRP E CD2 
8704  N NE1 . TRP E 122 ? 1.2368 0.9623 0.4115 -0.0814 -0.1682 -0.2922 122 TRP E NE1 
8705  C CE2 . TRP E 122 ? 1.2295 0.9773 0.4012 -0.0639 -0.1555 -0.2876 122 TRP E CE2 
8706  C CE3 . TRP E 122 ? 1.2675 1.0609 0.3962 -0.0533 -0.1469 -0.2970 122 TRP E CE3 
8707  C CZ2 . TRP E 122 ? 1.1958 0.9491 0.3912 -0.0450 -0.1414 -0.2737 122 TRP E CZ2 
8708  C CZ3 . TRP E 122 ? 1.2330 1.0315 0.3874 -0.0343 -0.1320 -0.2818 122 TRP E CZ3 
8709  C CH2 . TRP E 122 ? 1.1977 0.9760 0.3854 -0.0308 -0.1300 -0.2711 122 TRP E CH2 
8710  N N   . SER E 123 ? 1.4811 1.2136 0.4622 -0.1028 -0.1818 -0.4087 123 SER E N   
8711  C CA  . SER E 123 ? 1.5364 1.2789 0.4737 -0.1149 -0.1902 -0.4327 123 SER E CA  
8712  C C   . SER E 123 ? 1.5327 1.3346 0.4545 -0.1100 -0.1881 -0.4176 123 SER E C   
8713  O O   . SER E 123 ? 1.5675 1.3942 0.4592 -0.1251 -0.2005 -0.4272 123 SER E O   
8714  C CB  . SER E 123 ? 1.5869 1.2847 0.4953 -0.1058 -0.1803 -0.4678 123 SER E CB  
8715  O OG  . SER E 123 ? 1.5729 1.2736 0.4855 -0.0792 -0.1596 -0.4626 123 SER E OG  
8716  N N   . SER E 124 ? 1.4926 1.3173 0.4355 -0.0893 -0.1726 -0.3935 124 SER E N   
8717  C CA  . SER E 124 ? 1.4856 1.3659 0.4187 -0.0817 -0.1677 -0.3745 124 SER E CA  
8718  C C   . SER E 124 ? 1.4384 1.3621 0.4034 -0.0882 -0.1756 -0.3379 124 SER E C   
8719  O O   . SER E 124 ? 1.4295 1.4014 0.3913 -0.0826 -0.1726 -0.3175 124 SER E O   
8720  C CB  . SER E 124 ? 1.4734 1.3539 0.4117 -0.0551 -0.1446 -0.3696 124 SER E CB  
8721  O OG  . SER E 124 ? 1.4679 1.4010 0.3982 -0.0470 -0.1381 -0.3494 124 SER E OG  
8722  N N   . HIS E 125 ? 1.4102 1.3169 0.4063 -0.0991 -0.1848 -0.3290 125 HIS E N   
8723  C CA  . HIS E 125 ? 1.3662 1.3095 0.3958 -0.1050 -0.1914 -0.2956 125 HIS E CA  
8724  C C   . HIS E 125 ? 1.3725 1.3082 0.4086 -0.1294 -0.2112 -0.2993 125 HIS E C   
8725  O O   . HIS E 125 ? 1.3983 1.2901 0.4245 -0.1394 -0.2170 -0.3241 125 HIS E O   
8726  C CB  . HIS E 125 ? 1.3117 1.2454 0.3843 -0.0889 -0.1775 -0.2736 125 HIS E CB  
8727  C CG  . HIS E 125 ? 1.2985 1.2471 0.3737 -0.0661 -0.1584 -0.2636 125 HIS E CG  
8728  N ND1 . HIS E 125 ? 1.3091 1.2249 0.3773 -0.0507 -0.1443 -0.2809 125 HIS E ND1 
8729  C CD2 . HIS E 125 ? 1.2763 1.2697 0.3628 -0.0561 -0.1505 -0.2369 125 HIS E CD2 
8730  C CE1 . HIS E 125 ? 1.2940 1.2349 0.3690 -0.0330 -0.1287 -0.2657 125 HIS E CE1 
8731  N NE2 . HIS E 125 ? 1.2743 1.2613 0.3603 -0.0360 -0.1320 -0.2388 125 HIS E NE2 
8732  N N   . GLU E 126 ? 1.3507 1.3295 0.4050 -0.1387 -0.2210 -0.2736 126 GLU E N   
8733  C CA  . GLU E 126 ? 1.3506 1.3282 0.4181 -0.1613 -0.2387 -0.2721 126 GLU E CA  
8734  C C   . GLU E 126 ? 1.3050 1.2601 0.4156 -0.1575 -0.2328 -0.2559 126 GLU E C   
8735  O O   . GLU E 126 ? 1.2640 1.2379 0.4032 -0.1429 -0.2216 -0.2301 126 GLU E O   
8736  C CB  . GLU E 126 ? 1.3485 1.3855 0.4177 -0.1724 -0.2518 -0.2509 126 GLU E CB  
8737  C CG  . GLU E 126 ? 1.3496 1.3921 0.4337 -0.1968 -0.2708 -0.2484 126 GLU E CG  
8738  C CD  . GLU E 126 ? 1.4007 1.4082 0.4549 -0.2168 -0.2842 -0.2840 126 GLU E CD  
8739  O OE1 . GLU E 126 ? 1.4464 1.4671 0.4612 -0.2240 -0.2923 -0.3033 126 GLU E OE1 
8740  O OE2 . GLU E 126 ? 1.3968 1.3635 0.4671 -0.2255 -0.2863 -0.2927 126 GLU E OE2 
8741  N N   . ALA E 127 ? 1.3158 1.2306 0.4306 -0.1708 -0.2402 -0.2713 127 ALA E N   
8742  C CA  . ALA E 127 ? 1.2786 1.1653 0.4286 -0.1667 -0.2338 -0.2601 127 ALA E CA  
8743  C C   . ALA E 127 ? 1.2691 1.1588 0.4414 -0.1872 -0.2471 -0.2505 127 ALA E C   
8744  O O   . ALA E 127 ? 1.2348 1.1121 0.4382 -0.1837 -0.2417 -0.2358 127 ALA E O   
8745  C CB  . ALA E 127 ? 1.2955 1.1249 0.4352 -0.1588 -0.2257 -0.2839 127 ALA E CB  
8746  N N   . SER E 128 ? 1.3000 1.2071 0.4568 -0.2085 -0.2643 -0.2590 128 SER E N   
8747  C CA  . SER E 128 ? 1.2982 1.2044 0.4743 -0.2304 -0.2777 -0.2538 128 SER E CA  
8748  C C   . SER E 128 ? 1.2732 1.2371 0.4729 -0.2380 -0.2858 -0.2250 128 SER E C   
8749  O O   . SER E 128 ? 1.2703 1.2409 0.4889 -0.2562 -0.2968 -0.2182 128 SER E O   
8750  C CB  . SER E 128 ? 1.3525 1.2330 0.5002 -0.2522 -0.2925 -0.2844 128 SER E CB  
8751  O OG  . SER E 128 ? 1.3690 1.1889 0.5095 -0.2484 -0.2856 -0.3056 128 SER E OG  
8752  N N   . LEU E 129 ? 1.2559 1.2617 0.4565 -0.2238 -0.2798 -0.2071 129 LEU E N   
8753  C CA  . LEU E 129 ? 1.2304 1.2917 0.4569 -0.2270 -0.2851 -0.1765 129 LEU E CA  
8754  C C   . LEU E 129 ? 1.1800 1.2517 0.4406 -0.2056 -0.2674 -0.1486 129 LEU E C   
8755  O O   . LEU E 129 ? 1.1603 1.2786 0.4388 -0.1999 -0.2663 -0.1223 129 LEU E O   
8756  C CB  . LEU E 129 ? 1.2572 1.3655 0.4576 -0.2307 -0.2952 -0.1755 129 LEU E CB  
8757  C CG  . LEU E 129 ? 1.3076 1.4181 0.4779 -0.2558 -0.3163 -0.1997 129 LEU E CG  
8758  C CD1 . LEU E 129 ? 1.3513 1.4189 0.4785 -0.2546 -0.3140 -0.2364 129 LEU E CD1 
8759  C CD2 . LEU E 129 ? 1.3203 1.4946 0.4819 -0.2628 -0.3297 -0.1850 129 LEU E CD2 
8760  N N   . GLY E 130 ? 1.1622 1.1903 0.4324 -0.1941 -0.2540 -0.1544 130 GLY E N   
8761  C CA  . GLY E 130 ? 1.1170 1.1487 0.4194 -0.1754 -0.2374 -0.1318 130 GLY E CA  
8762  C C   . GLY E 130 ? 1.0893 1.1177 0.4272 -0.1822 -0.2375 -0.1166 130 GLY E C   
8763  O O   . GLY E 130 ? 1.0723 1.0646 0.4224 -0.1759 -0.2281 -0.1197 130 GLY E O   
8764  N N   . VAL E 131 ? 1.0855 1.1537 0.4399 -0.1947 -0.2478 -0.0996 131 VAL E N   
8765  C CA  . VAL E 131 ? 1.0629 1.1335 0.4511 -0.2030 -0.2484 -0.0845 131 VAL E CA  
8766  C C   . VAL E 131 ? 1.0328 1.1529 0.4547 -0.1962 -0.2441 -0.0520 131 VAL E C   
8767  O O   . VAL E 131 ? 1.0338 1.1894 0.4521 -0.1878 -0.2435 -0.0403 131 VAL E O   
8768  C CB  . VAL E 131 ? 1.0908 1.1577 0.4723 -0.2291 -0.2664 -0.0963 131 VAL E CB  
8769  C CG1 . VAL E 131 ? 1.1247 1.1400 0.4740 -0.2360 -0.2703 -0.1286 131 VAL E CG1 
8770  C CG2 . VAL E 131 ? 1.1098 1.2272 0.4848 -0.2421 -0.2826 -0.0895 131 VAL E CG2 
8771  N N   . SER E 132 ? 1.0088 1.1305 0.4638 -0.1993 -0.2402 -0.0371 132 SER E N   
8772  C CA  . SER E 132 ? 0.9808 1.1467 0.4724 -0.1932 -0.2352 -0.0062 132 SER E CA  
8773  C C   . SER E 132 ? 0.9730 1.1467 0.4915 -0.2081 -0.2403 0.0033  132 SER E C   
8774  O O   . SER E 132 ? 0.9811 1.1191 0.4944 -0.2187 -0.2424 -0.0115 132 SER E O   
8775  C CB  . SER E 132 ? 0.9485 1.1051 0.4601 -0.1701 -0.2144 0.0061  132 SER E CB  
8776  O OG  . SER E 132 ? 0.9230 1.1127 0.4742 -0.1647 -0.2073 0.0342  132 SER E OG  
8777  N N   . SER E 133 ? 0.9576 1.1793 0.5063 -0.2081 -0.2415 0.0296  133 SER E N   
8778  C CA  . SER E 133 ? 0.9470 1.1834 0.5271 -0.2201 -0.2441 0.0429  133 SER E CA  
8779  C C   . SER E 133 ? 0.9177 1.1273 0.5222 -0.2086 -0.2250 0.0492  133 SER E C   
8780  O O   . SER E 133 ? 0.9132 1.1204 0.5372 -0.2187 -0.2248 0.0539  133 SER E O   
8781  C CB  . SER E 133 ? 0.9397 1.2381 0.5473 -0.2209 -0.2499 0.0709  133 SER E CB  
8782  O OG  . SER E 133 ? 0.9152 1.2309 0.5417 -0.1982 -0.2344 0.0912  133 SER E OG  
8783  N N   . ALA E 134 ? 0.8991 1.0899 0.5024 -0.1880 -0.2091 0.0491  134 ALA E N   
8784  C CA  . ALA E 134 ? 0.8738 1.0384 0.4968 -0.1763 -0.1910 0.0528  134 ALA E CA  
8785  C C   . ALA E 134 ? 0.8828 0.9983 0.4885 -0.1849 -0.1916 0.0314  134 ALA E C   
8786  O O   . ALA E 134 ? 0.8689 0.9704 0.4924 -0.1835 -0.1816 0.0361  134 ALA E O   
8787  C CB  . ALA E 134 ? 0.8564 1.0135 0.4814 -0.1539 -0.1757 0.0563  134 ALA E CB  
8788  N N   . CYS E 135 ? 0.9075 0.9970 0.4784 -0.1930 -0.2025 0.0086  135 CYS E N   
8789  C CA  . CYS E 135 ? 0.9222 0.9663 0.4762 -0.2031 -0.2054 -0.0108 135 CYS E CA  
8790  C C   . CYS E 135 ? 0.9506 0.9999 0.4936 -0.2274 -0.2241 -0.0193 135 CYS E C   
8791  O O   . CYS E 135 ? 0.9770 1.0141 0.4904 -0.2342 -0.2351 -0.0380 135 CYS E O   
8792  C CB  . CYS E 135 ? 0.9318 0.9349 0.4558 -0.1927 -0.2019 -0.0322 135 CYS E CB  
8793  S SG  . CYS E 135 ? 0.9043 0.9056 0.4363 -0.1657 -0.1834 -0.0255 135 CYS E SG  
8794  N N   . PRO E 136 ? 0.9461 1.0143 0.5140 -0.2409 -0.2272 -0.0061 136 PRO E N   
8795  C CA  . PRO E 136 ? 0.9741 1.0476 0.5359 -0.2660 -0.2450 -0.0135 136 PRO E CA  
8796  C C   . PRO E 136 ? 0.9917 1.0177 0.5428 -0.2784 -0.2464 -0.0291 136 PRO E C   
8797  O O   . PRO E 136 ? 0.9759 0.9812 0.5394 -0.2717 -0.2335 -0.0233 136 PRO E O   
8798  C CB  . PRO E 136 ? 0.9589 1.0812 0.5585 -0.2727 -0.2460 0.0121  136 PRO E CB  
8799  C CG  . PRO E 136 ? 0.9266 1.0446 0.5506 -0.2548 -0.2255 0.0273  136 PRO E CG  
8800  C CD  . PRO E 136 ? 0.9166 1.0108 0.5223 -0.2334 -0.2148 0.0184  136 PRO E CD  
8801  N N   . TYR E 137 ? 1.0263 1.0358 0.5543 -0.2964 -0.2619 -0.0484 137 TYR E N   
8802  C CA  . TYR E 137 ? 1.0491 1.0146 0.5684 -0.3110 -0.2652 -0.0623 137 TYR E CA  
8803  C C   . TYR E 137 ? 1.0784 1.0590 0.6004 -0.3392 -0.2838 -0.0667 137 TYR E C   
8804  O O   . TYR E 137 ? 1.1029 1.0950 0.6054 -0.3481 -0.2979 -0.0800 137 TYR E O   
8805  C CB  . TYR E 137 ? 1.0686 0.9833 0.5534 -0.3028 -0.2637 -0.0873 137 TYR E CB  
8806  C CG  . TYR E 137 ? 1.0996 0.9666 0.5727 -0.3180 -0.2686 -0.1031 137 TYR E CG  
8807  C CD1 . TYR E 137 ? 1.0907 0.9343 0.5787 -0.3184 -0.2592 -0.0941 137 TYR E CD1 
8808  C CD2 . TYR E 137 ? 1.1403 0.9846 0.5869 -0.3316 -0.2819 -0.1272 137 TYR E CD2 
8809  C CE1 . TYR E 137 ? 1.1206 0.9202 0.5991 -0.3318 -0.2632 -0.1062 137 TYR E CE1 
8810  C CE2 . TYR E 137 ? 1.1710 0.9689 0.6089 -0.3450 -0.2856 -0.1411 137 TYR E CE2 
8811  C CZ  . TYR E 137 ? 1.1604 0.9364 0.6151 -0.3449 -0.2762 -0.1294 137 TYR E CZ  
8812  O OH  . TYR E 137 ? 1.1923 0.9223 0.6396 -0.3579 -0.2794 -0.1409 137 TYR E OH  
8813  N N   . GLN E 138 ? 1.0774 1.0588 0.6233 -0.3536 -0.2834 -0.0558 138 GLN E N   
8814  C CA  . GLN E 138 ? 1.1037 1.1011 0.6590 -0.3824 -0.3004 -0.0574 138 GLN E CA  
8815  C C   . GLN E 138 ? 1.1036 1.1598 0.6675 -0.3898 -0.3141 -0.0491 138 GLN E C   
8816  O O   . GLN E 138 ? 1.1363 1.2005 0.6891 -0.4110 -0.3326 -0.0623 138 GLN E O   
8817  C CB  . GLN E 138 ? 1.1473 1.0961 0.6730 -0.3979 -0.3111 -0.0857 138 GLN E CB  
8818  C CG  . GLN E 138 ? 1.1507 1.0406 0.6661 -0.3896 -0.2986 -0.0936 138 GLN E CG  
8819  C CD  . GLN E 138 ? 1.1955 1.0402 0.6948 -0.4102 -0.3088 -0.1148 138 GLN E CD  
8820  O OE1 . GLN E 138 ? 1.2281 1.0726 0.7098 -0.4249 -0.3241 -0.1336 138 GLN E OE1 
8821  N NE2 . GLN E 138 ? 1.1997 1.0052 0.7047 -0.4113 -0.3000 -0.1119 138 GLN E NE2 
8822  N N   . GLY E 139 ? 1.0687 1.1655 0.6524 -0.3721 -0.3050 -0.0272 139 GLY E N   
8823  C CA  . GLY E 139 ? 1.0647 1.2224 0.6616 -0.3762 -0.3164 -0.0135 139 GLY E CA  
8824  C C   . GLY E 139 ? 1.0704 1.2389 0.6385 -0.3642 -0.3212 -0.0230 139 GLY E C   
8825  O O   . GLY E 139 ? 1.0568 1.2758 0.6379 -0.3576 -0.3240 -0.0054 139 GLY E O   
8826  N N   . LYS E 140 ? 1.0914 1.2139 0.6216 -0.3608 -0.3216 -0.0495 140 LYS E N   
8827  C CA  . LYS E 140 ? 1.1013 1.2306 0.6006 -0.3497 -0.3251 -0.0608 140 LYS E CA  
8828  C C   . LYS E 140 ? 1.0707 1.1847 0.5674 -0.3201 -0.3050 -0.0551 140 LYS E C   
8829  O O   . LYS E 140 ? 1.0515 1.1332 0.5584 -0.3101 -0.2902 -0.0526 140 LYS E O   
8830  C CB  . LYS E 140 ? 1.1463 1.2365 0.6053 -0.3630 -0.3369 -0.0945 140 LYS E CB  
8831  C CG  . LYS E 140 ? 1.1827 1.2910 0.6393 -0.3935 -0.3593 -0.1040 140 LYS E CG  
8832  C CD  . LYS E 140 ? 1.1996 1.2688 0.6657 -0.4131 -0.3617 -0.1132 140 LYS E CD  
8833  C CE  . LYS E 140 ? 1.2241 1.3247 0.7050 -0.4439 -0.3821 -0.1121 140 LYS E CE  
8834  N NZ  . LYS E 140 ? 1.2684 1.3767 0.7163 -0.4597 -0.4019 -0.1363 140 LYS E NZ  
8835  N N   . SER E 141 ? 1.0682 1.2070 0.5509 -0.3069 -0.3049 -0.0527 141 SER E N   
8836  C CA  . SER E 141 ? 1.0429 1.1699 0.5223 -0.2798 -0.2870 -0.0481 141 SER E CA  
8837  C C   . SER E 141 ? 1.0586 1.1273 0.5067 -0.2737 -0.2814 -0.0751 141 SER E C   
8838  O O   . SER E 141 ? 1.0948 1.1457 0.5113 -0.2843 -0.2925 -0.0988 141 SER E O   
8839  C CB  . SER E 141 ? 1.0412 1.2118 0.5133 -0.2693 -0.2894 -0.0378 141 SER E CB  
8840  O OG  . SER E 141 ? 1.0218 1.2465 0.5279 -0.2702 -0.2915 -0.0088 141 SER E OG  
8841  N N   . SER E 142 ? 1.0329 1.0728 0.4904 -0.2565 -0.2641 -0.0716 142 SER E N   
8842  C CA  . SER E 142 ? 1.0438 1.0289 0.4777 -0.2491 -0.2576 -0.0937 142 SER E CA  
8843  C C   . SER E 142 ? 1.0155 0.9945 0.4529 -0.2231 -0.2402 -0.0873 142 SER E C   
8844  O O   . SER E 142 ? 0.9941 1.0104 0.4462 -0.2120 -0.2348 -0.0690 142 SER E O   
8845  C CB  . SER E 142 ? 1.0467 0.9957 0.4902 -0.2596 -0.2564 -0.0975 142 SER E CB  
8846  O OG  . SER E 142 ? 1.0603 0.9568 0.4822 -0.2529 -0.2514 -0.1176 142 SER E OG  
8847  N N   . PHE E 143 ? 1.0165 0.9495 0.4421 -0.2138 -0.2318 -0.1015 143 PHE E N   
8848  C CA  . PHE E 143 ? 0.9915 0.9163 0.4213 -0.1906 -0.2160 -0.0972 143 PHE E CA  
8849  C C   . PHE E 143 ? 0.9891 0.8652 0.4159 -0.1842 -0.2080 -0.1078 143 PHE E C   
8850  O O   . PHE E 143 ? 1.0107 0.8566 0.4284 -0.1969 -0.2146 -0.1196 143 PHE E O   
8851  C CB  . PHE E 143 ? 1.0042 0.9367 0.4100 -0.1805 -0.2159 -0.1071 143 PHE E CB  
8852  C CG  . PHE E 143 ? 0.9755 0.9195 0.3935 -0.1585 -0.2008 -0.0950 143 PHE E CG  
8853  C CD1 . PHE E 143 ? 0.9485 0.9326 0.3942 -0.1526 -0.1951 -0.0699 143 PHE E CD1 
8854  C CD2 . PHE E 143 ? 0.9766 0.8916 0.3807 -0.1436 -0.1918 -0.1082 143 PHE E CD2 
8855  C CE1 . PHE E 143 ? 0.9245 0.9172 0.3833 -0.1332 -0.1808 -0.0589 143 PHE E CE1 
8856  C CE2 . PHE E 143 ? 0.9514 0.8775 0.3689 -0.1248 -0.1781 -0.0970 143 PHE E CE2 
8857  C CZ  . PHE E 143 ? 0.9259 0.8898 0.3706 -0.1201 -0.1725 -0.0726 143 PHE E CZ  
8858  N N   . PHE E 144 ? 0.9639 0.8337 0.3997 -0.1650 -0.1941 -0.1024 144 PHE E N   
8859  C CA  . PHE E 144 ? 0.9623 0.7893 0.3927 -0.1562 -0.1869 -0.1127 144 PHE E CA  
8860  C C   . PHE E 144 ? 0.9972 0.7887 0.3976 -0.1605 -0.1943 -0.1368 144 PHE E C   
8861  O O   . PHE E 144 ? 1.0097 0.8030 0.3920 -0.1534 -0.1945 -0.1476 144 PHE E O   
8862  C CB  . PHE E 144 ? 0.9371 0.7672 0.3763 -0.1349 -0.1732 -0.1076 144 PHE E CB  
8863  C CG  . PHE E 144 ? 0.9048 0.7655 0.3742 -0.1286 -0.1639 -0.0855 144 PHE E CG  
8864  C CD1 . PHE E 144 ? 0.8896 0.7436 0.3778 -0.1306 -0.1587 -0.0764 144 PHE E CD1 
8865  C CD2 . PHE E 144 ? 0.8917 0.7873 0.3705 -0.1200 -0.1594 -0.0737 144 PHE E CD2 
8866  C CE1 . PHE E 144 ? 0.8627 0.7429 0.3789 -0.1240 -0.1487 -0.0577 144 PHE E CE1 
8867  C CE2 . PHE E 144 ? 0.8644 0.7857 0.3729 -0.1133 -0.1499 -0.0534 144 PHE E CE2 
8868  C CZ  . PHE E 144 ? 0.8501 0.7630 0.3776 -0.1152 -0.1443 -0.0462 144 PHE E CZ  
8869  N N   . ARG E 145 ? 1.0146 0.7734 0.4103 -0.1713 -0.1992 -0.1446 145 ARG E N   
8870  C CA  . ARG E 145 ? 1.0531 0.7765 0.4228 -0.1782 -0.2070 -0.1672 145 ARG E CA  
8871  C C   . ARG E 145 ? 1.0606 0.7543 0.4145 -0.1608 -0.2000 -0.1818 145 ARG E C   
8872  O O   . ARG E 145 ? 1.0940 0.7649 0.4249 -0.1633 -0.2049 -0.2015 145 ARG E O   
8873  C CB  . ARG E 145 ? 1.0693 0.7626 0.4418 -0.1930 -0.2122 -0.1690 145 ARG E CB  
8874  C CG  . ARG E 145 ? 1.0681 0.7874 0.4563 -0.2128 -0.2199 -0.1564 145 ARG E CG  
8875  C CD  . ARG E 145 ? 1.1012 0.7878 0.4829 -0.2316 -0.2288 -0.1660 145 ARG E CD  
8876  N NE  . ARG E 145 ? 1.0961 0.8058 0.4985 -0.2495 -0.2338 -0.1507 145 ARG E NE  
8877  C CZ  . ARG E 145 ? 1.1106 0.8470 0.5150 -0.2678 -0.2458 -0.1509 145 ARG E CZ  
8878  N NH1 . ARG E 145 ? 1.1336 0.8772 0.5172 -0.2716 -0.2547 -0.1668 145 ARG E NH1 
8879  N NH2 . ARG E 145 ? 1.1035 0.8613 0.5309 -0.2827 -0.2488 -0.1351 145 ARG E NH2 
8880  N N   . ASN E 146 ? 1.0323 0.7261 0.3993 -0.1436 -0.1886 -0.1731 146 ASN E N   
8881  C CA  . ASN E 146 ? 1.0375 0.7044 0.3941 -0.1268 -0.1819 -0.1850 146 ASN E CA  
8882  C C   . ASN E 146 ? 1.0347 0.7219 0.3833 -0.1139 -0.1767 -0.1893 146 ASN E C   
8883  O O   . ASN E 146 ? 1.0450 0.7119 0.3824 -0.1012 -0.1720 -0.2017 146 ASN E O   
8884  C CB  . ASN E 146 ? 1.0118 0.6674 0.3858 -0.1156 -0.1733 -0.1750 146 ASN E CB  
8885  C CG  . ASN E 146 ? 1.0233 0.6493 0.3987 -0.1255 -0.1773 -0.1741 146 ASN E CG  
8886  O OD1 . ASN E 146 ? 1.0557 0.6522 0.4159 -0.1338 -0.1842 -0.1869 146 ASN E OD1 
8887  N ND2 . ASN E 146 ? 0.9993 0.6322 0.3929 -0.1245 -0.1724 -0.1590 146 ASN E ND2 
8888  N N   . VAL E 147 ? 1.0223 0.7505 0.3772 -0.1166 -0.1772 -0.1780 147 VAL E N   
8889  C CA  . VAL E 147 ? 1.0206 0.7725 0.3683 -0.1049 -0.1718 -0.1787 147 VAL E CA  
8890  C C   . VAL E 147 ? 1.0416 0.8215 0.3737 -0.1167 -0.1811 -0.1811 147 VAL E C   
8891  O O   . VAL E 147 ? 1.0433 0.8390 0.3813 -0.1326 -0.1902 -0.1736 147 VAL E O   
8892  C CB  . VAL E 147 ? 0.9815 0.7606 0.3552 -0.0917 -0.1604 -0.1589 147 VAL E CB  
8893  C CG1 . VAL E 147 ? 0.9663 0.7197 0.3503 -0.0778 -0.1512 -0.1608 147 VAL E CG1 
8894  C CG2 . VAL E 147 ? 0.9597 0.7651 0.3564 -0.1008 -0.1622 -0.1390 147 VAL E CG2 
8895  N N   . VAL E 148 ? 1.0591 0.8468 0.3711 -0.1088 -0.1786 -0.1911 148 VAL E N   
8896  C CA  . VAL E 148 ? 1.0852 0.8988 0.3761 -0.1189 -0.1877 -0.1963 148 VAL E CA  
8897  C C   . VAL E 148 ? 1.0650 0.9265 0.3657 -0.1103 -0.1820 -0.1766 148 VAL E C   
8898  O O   . VAL E 148 ? 1.0542 0.9204 0.3565 -0.0931 -0.1700 -0.1739 148 VAL E O   
8899  C CB  . VAL E 148 ? 1.1263 0.9155 0.3829 -0.1166 -0.1887 -0.2232 148 VAL E CB  
8900  C CG1 . VAL E 148 ? 1.1592 0.9725 0.3903 -0.1302 -0.2002 -0.2318 148 VAL E CG1 
8901  C CG2 . VAL E 148 ? 1.1469 0.8844 0.3968 -0.1213 -0.1916 -0.2416 148 VAL E CG2 
8902  N N   . TRP E 149 ? 1.0612 0.9588 0.3701 -0.1221 -0.1904 -0.1618 149 TRP E N   
8903  C CA  . TRP E 149 ? 1.0485 0.9935 0.3652 -0.1151 -0.1866 -0.1418 149 TRP E CA  
8904  C C   . TRP E 149 ? 1.0853 1.0465 0.3666 -0.1177 -0.1927 -0.1549 149 TRP E C   
8905  O O   . TRP E 149 ? 1.1111 1.0855 0.3761 -0.1346 -0.2074 -0.1614 149 TRP E O   
8906  C CB  . TRP E 149 ? 1.0298 1.0087 0.3725 -0.1254 -0.1929 -0.1187 149 TRP E CB  
8907  C CG  . TRP E 149 ? 1.0115 1.0380 0.3706 -0.1159 -0.1871 -0.0930 149 TRP E CG  
8908  C CD1 . TRP E 149 ? 1.0130 1.0564 0.3636 -0.1013 -0.1780 -0.0885 149 TRP E CD1 
8909  C CD2 . TRP E 149 ? 0.9913 1.0550 0.3795 -0.1202 -0.1894 -0.0670 149 TRP E CD2 
8910  N NE1 . TRP E 149 ? 0.9946 1.0817 0.3673 -0.0964 -0.1746 -0.0607 149 TRP E NE1 
8911  C CE2 . TRP E 149 ? 0.9811 1.0813 0.3775 -0.1073 -0.1816 -0.0472 149 TRP E CE2 
8912  C CE3 . TRP E 149 ? 0.9818 1.0518 0.3915 -0.1332 -0.1965 -0.0575 149 TRP E CE3 
8913  C CZ2 . TRP E 149 ? 0.9622 1.1034 0.3879 -0.1062 -0.1808 -0.0184 149 TRP E CZ2 
8914  C CZ3 . TRP E 149 ? 0.9626 1.0749 0.4016 -0.1320 -0.1954 -0.0296 149 TRP E CZ3 
8915  C CH2 . TRP E 149 ? 0.9533 1.1000 0.4002 -0.1183 -0.1878 -0.0104 149 TRP E CH2 
8916  N N   . LEU E 150 ? 1.0890 1.0501 0.3585 -0.1013 -0.1812 -0.1590 150 LEU E N   
8917  C CA  . LEU E 150 ? 1.1272 1.0994 0.3595 -0.1012 -0.1841 -0.1741 150 LEU E CA  
8918  C C   . LEU E 150 ? 1.1255 1.1528 0.3572 -0.1001 -0.1856 -0.1528 150 LEU E C   
8919  O O   . LEU E 150 ? 1.0927 1.1443 0.3524 -0.0887 -0.1757 -0.1271 150 LEU E O   
8920  C CB  . LEU E 150 ? 1.1343 1.0820 0.3542 -0.0833 -0.1696 -0.1881 150 LEU E CB  
8921  C CG  . LEU E 150 ? 1.1467 1.0399 0.3600 -0.0825 -0.1682 -0.2123 150 LEU E CG  
8922  C CD1 . LEU E 150 ? 1.1494 1.0277 0.3565 -0.0624 -0.1526 -0.2208 150 LEU E CD1 
8923  C CD2 . LEU E 150 ? 1.1915 1.0630 0.3737 -0.0997 -0.1823 -0.2382 150 LEU E CD2 
8924  N N   . ILE E 151 ? 1.1639 1.2100 0.3632 -0.1120 -0.1982 -0.1640 151 ILE E N   
8925  C CA  . ILE E 151 ? 1.1711 1.2712 0.3621 -0.1112 -0.2014 -0.1458 151 ILE E CA  
8926  C C   . ILE E 151 ? 1.2175 1.3226 0.3615 -0.1102 -0.2027 -0.1670 151 ILE E C   
8927  O O   . ILE E 151 ? 1.2471 1.3134 0.3649 -0.1128 -0.2032 -0.1977 151 ILE E O   
8928  C CB  . ILE E 151 ? 1.1706 1.3042 0.3725 -0.1298 -0.2191 -0.1316 151 ILE E CB  
8929  C CG1 . ILE E 151 ? 1.2143 1.3334 0.3847 -0.1517 -0.2376 -0.1597 151 ILE E CG1 
8930  C CG2 . ILE E 151 ? 1.1271 1.2548 0.3747 -0.1303 -0.2162 -0.1120 151 ILE E CG2 
8931  C CD1 . ILE E 151 ? 1.2137 1.3615 0.3984 -0.1721 -0.2559 -0.1481 151 ILE E CD1 
8932  N N   . LYS E 152 ? 1.2253 1.3787 0.3589 -0.1058 -0.2025 -0.1499 152 LYS E N   
8933  C CA  . LYS E 152 ? 1.2705 1.4371 0.3579 -0.1036 -0.2025 -0.1665 152 LYS E CA  
8934  C C   . LYS E 152 ? 1.3197 1.4804 0.3690 -0.1251 -0.2222 -0.1950 152 LYS E C   
8935  O O   . LYS E 152 ? 1.3185 1.4899 0.3782 -0.1435 -0.2392 -0.1909 152 LYS E O   
8936  C CB  . LYS E 152 ? 1.2662 1.4906 0.3539 -0.0947 -0.1987 -0.1366 152 LYS E CB  
8937  C CG  . LYS E 152 ? 1.2605 1.5308 0.3613 -0.1086 -0.2157 -0.1134 152 LYS E CG  
8938  C CD  . LYS E 152 ? 1.2517 1.5768 0.3598 -0.0965 -0.2094 -0.0791 152 LYS E CD  
8939  C CE  . LYS E 152 ? 1.2488 1.6223 0.3702 -0.1093 -0.2268 -0.0550 152 LYS E CE  
8940  N NZ  . LYS E 152 ? 1.2894 1.7124 0.3735 -0.1149 -0.2385 -0.0511 152 LYS E NZ  
8941  N N   . LYS E 153 ? 1.3646 1.5082 0.3708 -0.1229 -0.2192 -0.2242 153 LYS E N   
8942  C CA  . LYS E 153 ? 1.4193 1.5580 0.3837 -0.1427 -0.2367 -0.2545 153 LYS E CA  
8943  C C   . LYS E 153 ? 1.4565 1.6420 0.3810 -0.1411 -0.2392 -0.2534 153 LYS E C   
8944  O O   . LYS E 153 ? 1.4669 1.6548 0.3729 -0.1232 -0.2227 -0.2558 153 LYS E O   
8945  C CB  . LYS E 153 ? 1.4494 1.5268 0.3926 -0.1425 -0.2316 -0.2932 153 LYS E CB  
8946  C CG  . LYS E 153 ? 1.4968 1.5539 0.4126 -0.1674 -0.2513 -0.3244 153 LYS E CG  
8947  C CD  . LYS E 153 ? 1.5457 1.5559 0.4238 -0.1638 -0.2441 -0.3646 153 LYS E CD  
8948  C CE  . LYS E 153 ? 1.5248 1.4772 0.4263 -0.1512 -0.2296 -0.3731 153 LYS E CE  
8949  N NZ  . LYS E 153 ? 1.4960 1.4228 0.4338 -0.1638 -0.2386 -0.3661 153 LYS E NZ  
8950  N N   . ASN E 154 ? 1.4777 1.7016 0.3893 -0.1601 -0.2601 -0.2493 154 ASN E N   
8951  C CA  . ASN E 154 ? 1.5142 1.7903 0.3882 -0.1611 -0.2662 -0.2446 154 ASN E CA  
8952  C C   . ASN E 154 ? 1.4875 1.8019 0.3739 -0.1378 -0.2485 -0.2101 154 ASN E C   
8953  O O   . ASN E 154 ? 1.5168 1.8449 0.3682 -0.1263 -0.2382 -0.2164 154 ASN E O   
8954  C CB  . ASN E 154 ? 1.5799 1.8344 0.3955 -0.1664 -0.2680 -0.2874 154 ASN E CB  
8955  C CG  . ASN E 154 ? 1.6281 1.9353 0.4006 -0.1785 -0.2843 -0.2897 154 ASN E CG  
8956  O OD1 . ASN E 154 ? 1.6219 1.9708 0.4064 -0.1935 -0.3034 -0.2703 154 ASN E OD1 
8957  N ND2 . ASN E 154 ? 1.6784 1.9853 0.4002 -0.1720 -0.2769 -0.3133 154 ASN E ND2 
8958  N N   . SER E 155 ? 1.4331 1.7636 0.3703 -0.1311 -0.2442 -0.1740 155 SER E N   
8959  C CA  . SER E 155 ? 1.4043 1.7733 0.3623 -0.1112 -0.2289 -0.1361 155 SER E CA  
8960  C C   . SER E 155 ? 1.3988 1.7441 0.3532 -0.0882 -0.2032 -0.1403 155 SER E C   
8961  O O   . SER E 155 ? 1.4038 1.7833 0.3497 -0.0740 -0.1915 -0.1210 155 SER E O   
8962  C CB  . SER E 155 ? 1.4340 1.8675 0.3653 -0.1155 -0.2403 -0.1184 155 SER E CB  
8963  O OG  . SER E 155 ? 1.4219 1.8876 0.3754 -0.1316 -0.2606 -0.0996 155 SER E OG  
8964  N N   . THR E 156 ? 1.3898 1.6782 0.3520 -0.0847 -0.1944 -0.1643 156 THR E N   
8965  C CA  . THR E 156 ? 1.3782 1.6428 0.3460 -0.0630 -0.1702 -0.1668 156 THR E CA  
8966  C C   . THR E 156 ? 1.3421 1.5548 0.3463 -0.0601 -0.1640 -0.1741 156 THR E C   
8967  O O   . THR E 156 ? 1.3557 1.5307 0.3523 -0.0732 -0.1746 -0.2004 156 THR E O   
8968  C CB  . THR E 156 ? 1.4311 1.6789 0.3471 -0.0587 -0.1636 -0.2010 156 THR E CB  
8969  O OG1 . THR E 156 ? 1.4486 1.6414 0.3540 -0.0679 -0.1692 -0.2377 156 THR E OG1 
8970  C CG2 . THR E 156 ? 1.4815 1.7734 0.3491 -0.0678 -0.1755 -0.2054 156 THR E CG2 
8971  N N   . TYR E 157 ? 1.2986 1.5099 0.3424 -0.0436 -0.1471 -0.1508 157 TYR E N   
8972  C CA  . TYR E 157 ? 1.2659 1.4300 0.3421 -0.0385 -0.1395 -0.1576 157 TYR E CA  
8973  C C   . TYR E 157 ? 1.2685 1.4122 0.3414 -0.0189 -0.1184 -0.1668 157 TYR E C   
8974  O O   . TYR E 157 ? 1.2385 1.3972 0.3394 -0.0039 -0.1029 -0.1430 157 TYR E O   
8975  C CB  . TYR E 157 ? 1.2130 1.3880 0.3411 -0.0370 -0.1380 -0.1257 157 TYR E CB  
8976  C CG  . TYR E 157 ? 1.1837 1.3117 0.3409 -0.0378 -0.1364 -0.1349 157 TYR E CG  
8977  C CD1 . TYR E 157 ? 1.1953 1.2939 0.3448 -0.0544 -0.1515 -0.1555 157 TYR E CD1 
8978  C CD2 . TYR E 157 ? 1.1466 1.2605 0.3390 -0.0227 -0.1201 -0.1225 157 TYR E CD2 
8979  C CE1 . TYR E 157 ? 1.1713 1.2284 0.3457 -0.0549 -0.1499 -0.1623 157 TYR E CE1 
8980  C CE2 . TYR E 157 ? 1.1227 1.1960 0.3391 -0.0236 -0.1195 -0.1307 157 TYR E CE2 
8981  C CZ  . TYR E 157 ? 1.1351 1.1805 0.3418 -0.0392 -0.1341 -0.1498 157 TYR E CZ  
8982  O OH  . TYR E 157 ? 1.1127 1.1195 0.3422 -0.0395 -0.1330 -0.1559 157 TYR E OH  
8983  N N   . PRO E 158 ? 1.3064 1.4162 0.3463 -0.0191 -0.1174 -0.2014 158 PRO E N   
8984  C CA  . PRO E 158 ? 1.3119 1.4031 0.3487 -0.0001 -0.0973 -0.2114 158 PRO E CA  
8985  C C   . PRO E 158 ? 1.2696 1.3274 0.3499 0.0090  -0.0880 -0.2063 158 PRO E C   
8986  O O   . PRO E 158 ? 1.2462 1.2829 0.3493 -0.0009 -0.0984 -0.2053 158 PRO E O   
8987  C CB  . PRO E 158 ? 1.3655 1.4264 0.3567 -0.0051 -0.1014 -0.2513 158 PRO E CB  
8988  C CG  . PRO E 158 ? 1.3742 1.4178 0.3604 -0.0271 -0.1231 -0.2641 158 PRO E CG  
8989  C CD  . PRO E 158 ? 1.3478 1.4351 0.3532 -0.0368 -0.1343 -0.2329 158 PRO E CD  
8990  N N   . THR E 159 ? 1.2620 1.3173 0.3534 0.0277  -0.0686 -0.2028 159 THR E N   
8991  C CA  . THR E 159 ? 1.2238 1.2523 0.3564 0.0374  -0.0593 -0.1971 159 THR E CA  
8992  C C   . THR E 159 ? 1.2351 1.2117 0.3634 0.0322  -0.0664 -0.2251 159 THR E C   
8993  O O   . THR E 159 ? 1.2771 1.2330 0.3702 0.0307  -0.0683 -0.2533 159 THR E O   
8994  C CB  . THR E 159 ? 1.2185 1.2556 0.3617 0.0578  -0.0374 -0.1905 159 THR E CB  
8995  O OG1 . THR E 159 ? 1.2141 1.2993 0.3595 0.0625  -0.0300 -0.1636 159 THR E OG1 
8996  C CG2 . THR E 159 ? 1.1759 1.1909 0.3651 0.0664  -0.0294 -0.1819 159 THR E CG2 
8997  N N   . ILE E 160 ? 1.1996 1.1557 0.3638 0.0297  -0.0700 -0.2168 160 ILE E N   
8998  C CA  . ILE E 160 ? 1.2045 1.1124 0.3713 0.0257  -0.0762 -0.2376 160 ILE E CA  
8999  C C   . ILE E 160 ? 1.1899 1.0773 0.3798 0.0433  -0.0613 -0.2393 160 ILE E C   
9000  O O   . ILE E 160 ? 1.1534 1.0573 0.3767 0.0517  -0.0525 -0.2176 160 ILE E O   
9001  C CB  . ILE E 160 ? 1.1742 1.0740 0.3657 0.0117  -0.0895 -0.2263 160 ILE E CB  
9002  C CG1 . ILE E 160 ? 1.1922 1.1112 0.3628 -0.0070 -0.1058 -0.2261 160 ILE E CG1 
9003  C CG2 . ILE E 160 ? 1.1742 1.0250 0.3730 0.0099  -0.0936 -0.2434 160 ILE E CG2 
9004  C CD1 . ILE E 160 ? 1.1590 1.0859 0.3578 -0.0191 -0.1161 -0.2070 160 ILE E CD1 
9005  N N   . LYS E 161 ? 1.2207 1.0725 0.3940 0.0488  -0.0588 -0.2650 161 LYS E N   
9006  C CA  . LYS E 161 ? 1.2091 1.0391 0.4053 0.0650  -0.0467 -0.2681 161 LYS E CA  
9007  C C   . LYS E 161 ? 1.2257 1.0067 0.4187 0.0615  -0.0546 -0.2889 161 LYS E C   
9008  O O   . LYS E 161 ? 1.2659 1.0224 0.4323 0.0646  -0.0529 -0.3133 161 LYS E O   
9009  C CB  . LYS E 161 ? 1.2327 1.0744 0.4146 0.0819  -0.0296 -0.2756 161 LYS E CB  
9010  C CG  . LYS E 161 ? 1.2125 1.1005 0.4078 0.0897  -0.0177 -0.2507 161 LYS E CG  
9011  C CD  . LYS E 161 ? 1.2430 1.1444 0.4179 0.1048  -0.0008 -0.2595 161 LYS E CD  
9012  C CE  . LYS E 161 ? 1.2248 1.1727 0.4140 0.1123  0.0117  -0.2325 161 LYS E CE  
9013  N NZ  . LYS E 161 ? 1.2615 1.2285 0.4224 0.1243  0.0272  -0.2402 161 LYS E NZ  
9014  N N   . ARG E 162 ? 1.1976 0.9640 0.4180 0.0553  -0.0625 -0.2788 162 ARG E N   
9015  C CA  . ARG E 162 ? 1.2121 0.9335 0.4319 0.0511  -0.0706 -0.2942 162 ARG E CA  
9016  C C   . ARG E 162 ? 1.1860 0.8914 0.4398 0.0619  -0.0660 -0.2862 162 ARG E C   
9017  O O   . ARG E 162 ? 1.1463 0.8723 0.4291 0.0633  -0.0639 -0.2654 162 ARG E O   
9018  C CB  . ARG E 162 ? 1.2059 0.9216 0.4243 0.0307  -0.0870 -0.2902 162 ARG E CB  
9019  C CG  . ARG E 162 ? 1.2439 0.9213 0.4383 0.0194  -0.0977 -0.3132 162 ARG E CG  
9020  C CD  . ARG E 162 ? 1.2931 0.9678 0.4481 0.0166  -0.0977 -0.3359 162 ARG E CD  
9021  N NE  . ARG E 162 ? 1.3182 0.9683 0.4571 -0.0029 -0.1131 -0.3492 162 ARG E NE  
9022  C CZ  . ARG E 162 ? 1.3364 1.0029 0.4541 -0.0210 -0.1247 -0.3529 162 ARG E CZ  
9023  N NH1 . ARG E 162 ? 1.3371 1.0471 0.4415 -0.0222 -0.1237 -0.3452 162 ARG E NH1 
9024  N NH2 . ARG E 162 ? 1.3571 0.9957 0.4668 -0.0386 -0.1382 -0.3647 162 ARG E NH2 
9025  N N   . SER E 163 ? 1.2120 0.8792 0.4617 0.0682  -0.0657 -0.3033 163 SER E N   
9026  C CA  . SER E 163 ? 1.1945 0.8443 0.4733 0.0790  -0.0627 -0.2980 163 SER E CA  
9027  C C   . SER E 163 ? 1.2162 0.8222 0.4909 0.0722  -0.0735 -0.3089 163 SER E C   
9028  O O   . SER E 163 ? 1.2559 0.8364 0.5041 0.0672  -0.0773 -0.3283 163 SER E O   
9029  C CB  . SER E 163 ? 1.2055 0.8566 0.4884 0.0997  -0.0476 -0.3051 163 SER E CB  
9030  O OG  . SER E 163 ? 1.1874 0.8234 0.4990 0.1104  -0.0457 -0.3003 163 SER E OG  
9031  N N   . TYR E 164 ? 1.1943 0.7915 0.4949 0.0715  -0.0783 -0.2965 164 TYR E N   
9032  C CA  . TYR E 164 ? 1.2147 0.7710 0.5149 0.0677  -0.0870 -0.3036 164 TYR E CA  
9033  C C   . TYR E 164 ? 1.2086 0.7532 0.5346 0.0829  -0.0831 -0.2981 164 TYR E C   
9034  O O   . TYR E 164 ? 1.1709 0.7368 0.5222 0.0859  -0.0818 -0.2817 164 TYR E O   
9035  C CB  . TYR E 164 ? 1.1986 0.7520 0.5008 0.0485  -0.0999 -0.2939 164 TYR E CB  
9036  C CG  . TYR E 164 ? 1.2060 0.7212 0.5139 0.0466  -0.1072 -0.2956 164 TYR E CG  
9037  C CD1 . TYR E 164 ? 1.2477 0.7243 0.5362 0.0435  -0.1110 -0.3132 164 TYR E CD1 
9038  C CD2 . TYR E 164 ? 1.1740 0.6911 0.5065 0.0485  -0.1095 -0.2799 164 TYR E CD2 
9039  C CE1 . TYR E 164 ? 1.2570 0.6983 0.5519 0.0425  -0.1170 -0.3125 164 TYR E CE1 
9040  C CE2 . TYR E 164 ? 1.1832 0.6672 0.5196 0.0475  -0.1160 -0.2798 164 TYR E CE2 
9041  C CZ  . TYR E 164 ? 1.2241 0.6705 0.5425 0.0447  -0.1196 -0.2949 164 TYR E CZ  
9042  O OH  . TYR E 164 ? 1.2350 0.6485 0.5584 0.0441  -0.1256 -0.2924 164 TYR E OH  
9043  N N   . ASN E 165 ? 1.2517 0.7618 0.5716 0.0919  -0.0820 -0.3120 165 ASN E N   
9044  C CA  . ASN E 165 ? 1.2556 0.7523 0.5986 0.1068  -0.0798 -0.3074 165 ASN E CA  
9045  C C   . ASN E 165 ? 1.2460 0.7144 0.5942 0.0981  -0.0919 -0.3017 165 ASN E C   
9046  O O   . ASN E 165 ? 1.2767 0.7133 0.6066 0.0892  -0.0981 -0.3119 165 ASN E O   
9047  C CB  . ASN E 165 ? 1.3114 0.7867 0.6469 0.1236  -0.0706 -0.3243 165 ASN E CB  
9048  C CG  . ASN E 165 ? 1.3249 0.7991 0.6887 0.1424  -0.0657 -0.3175 165 ASN E CG  
9049  O OD1 . ASN E 165 ? 1.2953 0.7757 0.6810 0.1412  -0.0721 -0.3023 165 ASN E OD1 
9050  N ND2 . ASN E 165 ? 1.3828 0.8502 0.7459 0.1600  -0.0543 -0.3292 165 ASN E ND2 
9051  N N   . ASN E 166 ? 1.2033 0.6831 0.5759 0.1004  -0.0950 -0.2855 166 ASN E N   
9052  C CA  . ASN E 166 ? 1.1945 0.6511 0.5719 0.0933  -0.1057 -0.2780 166 ASN E CA  
9053  C C   . ASN E 166 ? 1.2159 0.6391 0.5974 0.1069  -0.1059 -0.2833 166 ASN E C   
9054  O O   . ASN E 166 ? 1.2005 0.6304 0.6036 0.1201  -0.1047 -0.2753 166 ASN E O   
9055  C CB  . ASN E 166 ? 1.1514 0.6330 0.5509 0.0905  -0.1089 -0.2599 166 ASN E CB  
9056  C CG  . ASN E 166 ? 1.1494 0.6114 0.5487 0.0799  -0.1197 -0.2514 166 ASN E CG  
9057  O OD1 . ASN E 166 ? 1.1762 0.6086 0.5591 0.0715  -0.1252 -0.2572 166 ASN E OD1 
9058  N ND2 . ASN E 166 ? 1.1190 0.5976 0.5364 0.0798  -0.1225 -0.2379 166 ASN E ND2 
9059  N N   . THR E 167 ? 1.2497 0.6373 0.6117 0.1034  -0.1078 -0.2967 167 THR E N   
9060  C CA  . THR E 167 ? 1.2769 0.6281 0.6420 0.1163  -0.1073 -0.3023 167 THR E CA  
9061  C C   . THR E 167 ? 1.2727 0.6014 0.6450 0.1110  -0.1179 -0.2894 167 THR E C   
9062  O O   . THR E 167 ? 1.2923 0.5966 0.6735 0.1239  -0.1182 -0.2880 167 THR E O   
9063  C CB  . THR E 167 ? 1.3250 0.6434 0.6665 0.1153  -0.1036 -0.3237 167 THR E CB  
9064  O OG1 . THR E 167 ? 1.3341 0.6433 0.6559 0.0927  -0.1116 -0.3275 167 THR E OG1 
9065  C CG2 . THR E 167 ? 1.3326 0.6700 0.6671 0.1264  -0.0910 -0.3372 167 THR E CG2 
9066  N N   . ASN E 168 ? 1.2471 0.5846 0.6159 0.0928  -0.1261 -0.2791 168 ASN E N   
9067  C CA  . ASN E 168 ? 1.2405 0.5619 0.6156 0.0873  -0.1353 -0.2649 168 ASN E CA  
9068  C C   . ASN E 168 ? 1.2082 0.5512 0.6060 0.1004  -0.1357 -0.2511 168 ASN E C   
9069  O O   . ASN E 168 ? 1.1791 0.5563 0.5882 0.1057  -0.1307 -0.2496 168 ASN E O   
9070  C CB  . ASN E 168 ? 1.2240 0.5543 0.5914 0.0653  -0.1423 -0.2565 168 ASN E CB  
9071  C CG  . ASN E 168 ? 1.2320 0.5678 0.5819 0.0509  -0.1412 -0.2682 168 ASN E CG  
9072  O OD1 . ASN E 168 ? 1.2632 0.5712 0.5982 0.0391  -0.1451 -0.2759 168 ASN E OD1 
9073  N ND2 . ASN E 168 ? 1.2053 0.5778 0.5576 0.0511  -0.1362 -0.2686 168 ASN E ND2 
9074  N N   . GLN E 169 ? 1.2132 0.5371 0.6180 0.1051  -0.1420 -0.2407 169 GLN E N   
9075  C CA  . GLN E 169 ? 1.1851 0.5308 0.6101 0.1153  -0.1448 -0.2273 169 GLN E CA  
9076  C C   . GLN E 169 ? 1.1537 0.5183 0.5786 0.1003  -0.1515 -0.2142 169 GLN E C   
9077  O O   . GLN E 169 ? 1.1529 0.5127 0.5818 0.1005  -0.1587 -0.2016 169 GLN E O   
9078  C CB  . GLN E 169 ? 1.2100 0.5311 0.6441 0.1308  -0.1481 -0.2217 169 GLN E CB  
9079  C CG  . GLN E 169 ? 1.2389 0.5229 0.6618 0.1231  -0.1553 -0.2148 169 GLN E CG  
9080  C CD  . GLN E 169 ? 1.2484 0.5238 0.6842 0.1361  -0.1617 -0.1999 169 GLN E CD  
9081  O OE1 . GLN E 169 ? 1.2229 0.5274 0.6741 0.1439  -0.1647 -0.1909 169 GLN E OE1 
9082  N NE2 . GLN E 169 ? 1.2864 0.5221 0.7165 0.1380  -0.1643 -0.1966 169 GLN E NE2 
9083  N N   . GLU E 170 ? 1.1287 0.5154 0.5486 0.0880  -0.1485 -0.2171 170 GLU E N   
9084  C CA  . GLU E 170 ? 1.0988 0.5055 0.5194 0.0741  -0.1522 -0.2066 170 GLU E CA  
9085  C C   . GLU E 170 ? 1.0653 0.5081 0.4940 0.0720  -0.1457 -0.2088 170 GLU E C   
9086  O O   . GLU E 170 ? 1.0684 0.5180 0.4959 0.0768  -0.1388 -0.2186 170 GLU E O   
9087  C CB  . GLU E 170 ? 1.1123 0.5004 0.5154 0.0558  -0.1562 -0.2052 170 GLU E CB  
9088  C CG  . GLU E 170 ? 1.1380 0.4944 0.5349 0.0535  -0.1632 -0.1972 170 GLU E CG  
9089  C CD  . GLU E 170 ? 1.1791 0.4969 0.5647 0.0540  -0.1633 -0.2067 170 GLU E CD  
9090  O OE1 . GLU E 170 ? 1.1915 0.5048 0.5762 0.0630  -0.1577 -0.2204 170 GLU E OE1 
9091  O OE2 . GLU E 170 ? 1.2013 0.4923 0.5790 0.0453  -0.1682 -0.2005 170 GLU E OE2 
9092  N N   . ASP E 171 ? 1.0352 0.5007 0.4721 0.0651  -0.1472 -0.1993 171 ASP E N   
9093  C CA  . ASP E 171 ? 1.0057 0.5019 0.4493 0.0594  -0.1411 -0.1991 171 ASP E CA  
9094  C C   . ASP E 171 ? 1.0124 0.5030 0.4394 0.0445  -0.1412 -0.2016 171 ASP E C   
9095  O O   . ASP E 171 ? 1.0315 0.4986 0.4454 0.0355  -0.1469 -0.2004 171 ASP E O   
9096  C CB  . ASP E 171 ? 0.9780 0.4954 0.4343 0.0551  -0.1424 -0.1892 171 ASP E CB  
9097  C CG  . ASP E 171 ? 0.9679 0.4971 0.4427 0.0680  -0.1431 -0.1874 171 ASP E CG  
9098  O OD1 . ASP E 171 ? 0.9685 0.5045 0.4537 0.0802  -0.1385 -0.1928 171 ASP E OD1 
9099  O OD2 . ASP E 171 ? 0.9604 0.4937 0.4395 0.0655  -0.1481 -0.1807 171 ASP E OD2 
9100  N N   . LEU E 172 ? 0.9967 0.5103 0.4255 0.0418  -0.1350 -0.2043 172 LEU E N   
9101  C CA  . LEU E 172 ? 1.0035 0.5172 0.4178 0.0282  -0.1357 -0.2068 172 LEU E CA  
9102  C C   . LEU E 172 ? 0.9727 0.5196 0.3967 0.0212  -0.1315 -0.1988 172 LEU E C   
9103  O O   . LEU E 172 ? 0.9552 0.5256 0.3913 0.0290  -0.1245 -0.1981 172 LEU E O   
9104  C CB  . LEU E 172 ? 1.0279 0.5331 0.4292 0.0329  -0.1326 -0.2205 172 LEU E CB  
9105  C CG  . LEU E 172 ? 1.0446 0.5469 0.4276 0.0182  -0.1354 -0.2260 172 LEU E CG  
9106  C CD1 . LEU E 172 ? 1.0702 0.5399 0.4411 0.0070  -0.1437 -0.2275 172 LEU E CD1 
9107  C CD2 . LEU E 172 ? 1.0654 0.5680 0.4359 0.0247  -0.1304 -0.2402 172 LEU E CD2 
9108  N N   . LEU E 173 ? 0.9666 0.5155 0.3873 0.0069  -0.1351 -0.1916 173 LEU E N   
9109  C CA  . LEU E 173 ? 0.9409 0.5198 0.3712 0.0000  -0.1310 -0.1830 173 LEU E CA  
9110  C C   . LEU E 173 ? 0.9496 0.5393 0.3691 -0.0062 -0.1305 -0.1873 173 LEU E C   
9111  O O   . LEU E 173 ? 0.9683 0.5461 0.3736 -0.0181 -0.1366 -0.1901 173 LEU E O   
9112  C CB  . LEU E 173 ? 0.9330 0.5114 0.3655 -0.0120 -0.1342 -0.1731 173 LEU E CB  
9113  C CG  . LEU E 173 ? 0.9106 0.5184 0.3540 -0.0198 -0.1298 -0.1634 173 LEU E CG  
9114  C CD1 . LEU E 173 ? 0.8836 0.5147 0.3476 -0.0103 -0.1215 -0.1586 173 LEU E CD1 
9115  C CD2 . LEU E 173 ? 0.9094 0.5137 0.3525 -0.0319 -0.1326 -0.1548 173 LEU E CD2 
9116  N N   . VAL E 174 ? 0.9370 0.5506 0.3636 0.0012  -0.1234 -0.1872 174 VAL E N   
9117  C CA  . VAL E 174 ? 0.9448 0.5745 0.3607 -0.0034 -0.1225 -0.1898 174 VAL E CA  
9118  C C   . VAL E 174 ? 0.9197 0.5817 0.3495 -0.0098 -0.1193 -0.1755 174 VAL E C   
9119  O O   . VAL E 174 ? 0.8941 0.5713 0.3448 -0.0040 -0.1129 -0.1663 174 VAL E O   
9120  C CB  . VAL E 174 ? 0.9512 0.5884 0.3644 0.0099  -0.1155 -0.1976 174 VAL E CB  
9121  C CG1 . VAL E 174 ? 0.9670 0.6187 0.3629 0.0044  -0.1157 -0.2020 174 VAL E CG1 
9122  C CG2 . VAL E 174 ? 0.9731 0.5799 0.3784 0.0196  -0.1166 -0.2103 174 VAL E CG2 
9123  N N   . LEU E 175 ? 0.9288 0.6010 0.3481 -0.0218 -0.1239 -0.1739 175 LEU E N   
9124  C CA  . LEU E 175 ? 0.9087 0.6133 0.3410 -0.0276 -0.1213 -0.1594 175 LEU E CA  
9125  C C   . LEU E 175 ? 0.9200 0.6468 0.3405 -0.0291 -0.1214 -0.1606 175 LEU E C   
9126  O O   . LEU E 175 ? 0.9479 0.6625 0.3454 -0.0346 -0.1280 -0.1731 175 LEU E O   
9127  C CB  . LEU E 175 ? 0.9087 0.6104 0.3420 -0.0426 -0.1280 -0.1529 175 LEU E CB  
9128  C CG  . LEU E 175 ? 0.9021 0.5829 0.3428 -0.0437 -0.1287 -0.1507 175 LEU E CG  
9129  C CD1 . LEU E 175 ? 0.9124 0.5865 0.3479 -0.0598 -0.1361 -0.1471 175 LEU E CD1 
9130  C CD2 . LEU E 175 ? 0.8722 0.5696 0.3369 -0.0365 -0.1198 -0.1396 175 LEU E CD2 
9131  N N   . TRP E 176 ? 0.9003 0.6592 0.3363 -0.0243 -0.1141 -0.1475 176 TRP E N   
9132  C CA  . TRP E 176 ? 0.9096 0.6961 0.3356 -0.0265 -0.1145 -0.1441 176 TRP E CA  
9133  C C   . TRP E 176 ? 0.8850 0.7059 0.3345 -0.0271 -0.1093 -0.1229 176 TRP E C   
9134  O O   . TRP E 176 ? 0.8621 0.6825 0.3345 -0.0259 -0.1049 -0.1134 176 TRP E O   
9135  C CB  . TRP E 176 ? 0.9211 0.7097 0.3363 -0.0139 -0.1079 -0.1527 176 TRP E CB  
9136  C CG  . TRP E 176 ? 0.8968 0.6968 0.3359 0.0000  -0.0955 -0.1436 176 TRP E CG  
9137  C CD1 . TRP E 176 ? 0.8827 0.7147 0.3360 0.0060  -0.0867 -0.1289 176 TRP E CD1 
9138  C CD2 . TRP E 176 ? 0.8852 0.6653 0.3384 0.0090  -0.0910 -0.1479 176 TRP E CD2 
9139  N NE1 . TRP E 176 ? 0.8634 0.6952 0.3398 0.0174  -0.0766 -0.1247 176 TRP E NE1 
9140  C CE2 . TRP E 176 ? 0.8645 0.6657 0.3409 0.0192  -0.0796 -0.1366 176 TRP E CE2 
9141  C CE3 . TRP E 176 ? 0.8918 0.6392 0.3408 0.0092  -0.0959 -0.1592 176 TRP E CE3 
9142  C CZ2 . TRP E 176 ? 0.8503 0.6417 0.3460 0.0285  -0.0738 -0.1380 176 TRP E CZ2 
9143  C CZ3 . TRP E 176 ? 0.8776 0.6169 0.3445 0.0195  -0.0904 -0.1595 176 TRP E CZ3 
9144  C CH2 . TRP E 176 ? 0.8570 0.6186 0.3471 0.0284  -0.0799 -0.1497 176 TRP E CH2 
9145  N N   . GLY E 177 ? 0.8922 0.7428 0.3355 -0.0287 -0.1097 -0.1156 177 GLY E N   
9146  C CA  . GLY E 177 ? 0.8724 0.7571 0.3386 -0.0288 -0.1051 -0.0937 177 GLY E CA  
9147  C C   . GLY E 177 ? 0.8792 0.7973 0.3407 -0.0237 -0.1014 -0.0842 177 GLY E C   
9148  O O   . GLY E 177 ? 0.9034 0.8212 0.3386 -0.0226 -0.1041 -0.0960 177 GLY E O   
9149  N N   . ILE E 178 ? 0.8600 0.8068 0.3472 -0.0202 -0.0945 -0.0623 178 ILE E N   
9150  C CA  . ILE E 178 ? 0.8653 0.8488 0.3521 -0.0157 -0.0908 -0.0473 178 ILE E CA  
9151  C C   . ILE E 178 ? 0.8602 0.8727 0.3601 -0.0243 -0.0963 -0.0284 178 ILE E C   
9152  O O   . ILE E 178 ? 0.8415 0.8493 0.3647 -0.0274 -0.0950 -0.0208 178 ILE E O   
9153  C CB  . ILE E 178 ? 0.8473 0.8400 0.3582 -0.0006 -0.0747 -0.0351 178 ILE E CB  
9154  C CG1 . ILE E 178 ? 0.8570 0.8867 0.3627 0.0047  -0.0705 -0.0199 178 ILE E CG1 
9155  C CG2 . ILE E 178 ? 0.8187 0.8107 0.3671 0.0015  -0.0670 -0.0207 178 ILE E CG2 
9156  C CD1 . ILE E 178 ? 0.8375 0.8846 0.3756 0.0169  -0.0548 0.0009  178 ILE E CD1 
9157  N N   . HIS E 179 ? 0.8787 0.9224 0.3634 -0.0279 -0.1024 -0.0210 179 HIS E N   
9158  C CA  . HIS E 179 ? 0.8750 0.9528 0.3745 -0.0346 -0.1076 0.0000  179 HIS E CA  
9159  C C   . HIS E 179 ? 0.8621 0.9741 0.3851 -0.0227 -0.0961 0.0265  179 HIS E C   
9160  O O   . HIS E 179 ? 0.8727 0.9972 0.3836 -0.0144 -0.0907 0.0287  179 HIS E O   
9161  C CB  . HIS E 179 ? 0.9053 0.9995 0.3744 -0.0483 -0.1243 -0.0071 179 HIS E CB  
9162  C CG  . HIS E 179 ? 0.9036 1.0382 0.3884 -0.0549 -0.1308 0.0157  179 HIS E CG  
9163  N ND1 . HIS E 179 ? 0.9237 1.0973 0.3934 -0.0569 -0.1378 0.0261  179 HIS E ND1 
9164  C CD2 . HIS E 179 ? 0.8852 1.0294 0.4006 -0.0590 -0.1310 0.0313  179 HIS E CD2 
9165  C CE1 . HIS E 179 ? 0.9165 1.1226 0.4080 -0.0622 -0.1430 0.0477  179 HIS E CE1 
9166  N NE2 . HIS E 179 ? 0.8932 1.0818 0.4135 -0.0632 -0.1384 0.0512  179 HIS E NE2 
9167  N N   . HIS E 180 ? 0.8408 0.9674 0.3981 -0.0218 -0.0916 0.0473  180 HIS E N   
9168  C CA  . HIS E 180 ? 0.8289 0.9874 0.4139 -0.0110 -0.0806 0.0755  180 HIS E CA  
9169  C C   . HIS E 180 ? 0.8365 1.0359 0.4237 -0.0182 -0.0911 0.0947  180 HIS E C   
9170  O O   . HIS E 180 ? 0.8269 1.0299 0.4319 -0.0253 -0.0955 0.1009  180 HIS E O   
9171  C CB  . HIS E 180 ? 0.8017 0.9457 0.4270 -0.0035 -0.0666 0.0851  180 HIS E CB  
9172  C CG  . HIS E 180 ? 0.7935 0.9002 0.4199 0.0026  -0.0575 0.0673  180 HIS E CG  
9173  N ND1 . HIS E 180 ? 0.7826 0.8883 0.4311 0.0152  -0.0421 0.0763  180 HIS E ND1 
9174  C CD2 . HIS E 180 ? 0.7955 0.8660 0.4056 -0.0021 -0.0620 0.0423  180 HIS E CD2 
9175  C CE1 . HIS E 180 ? 0.7775 0.8496 0.4231 0.0174  -0.0383 0.0569  180 HIS E CE1 
9176  N NE2 . HIS E 180 ? 0.7851 0.8357 0.4073 0.0076  -0.0502 0.0367  180 HIS E NE2 
9177  N N   . PRO E 181 ? 0.8545 1.0868 0.4236 -0.0165 -0.0951 0.1046  181 PRO E N   
9178  C CA  . PRO E 181 ? 0.8648 1.1399 0.4333 -0.0238 -0.1072 0.1229  181 PRO E CA  
9179  C C   . PRO E 181 ? 0.8459 1.1520 0.4572 -0.0138 -0.0970 0.1580  181 PRO E C   
9180  O O   . PRO E 181 ? 0.8286 1.1239 0.4665 -0.0007 -0.0797 0.1680  181 PRO E O   
9181  C CB  . PRO E 181 ? 0.8948 1.1908 0.4246 -0.0241 -0.1138 0.1183  181 PRO E CB  
9182  C CG  . PRO E 181 ? 0.8904 1.1695 0.4204 -0.0096 -0.0971 0.1157  181 PRO E CG  
9183  C CD  . PRO E 181 ? 0.8679 1.1014 0.4161 -0.0072 -0.0883 0.1002  181 PRO E CD  
9184  N N   . ASN E 182 ? 0.8508 1.1952 0.4697 -0.0203 -0.1079 0.1764  182 ASN E N   
9185  C CA  . ASN E 182 ? 0.8344 1.2089 0.4970 -0.0111 -0.0992 0.2109  182 ASN E CA  
9186  C C   . ASN E 182 ? 0.8400 1.2447 0.5095 0.0028  -0.0896 0.2369  182 ASN E C   
9187  O O   . ASN E 182 ? 0.8228 1.2274 0.5301 0.0162  -0.0726 0.2576  182 ASN E O   
9188  C CB  . ASN E 182 ? 0.8392 1.2480 0.5095 -0.0226 -0.1148 0.2233  182 ASN E CB  
9189  C CG  . ASN E 182 ? 0.8283 1.2101 0.5056 -0.0343 -0.1198 0.2057  182 ASN E CG  
9190  O OD1 . ASN E 182 ? 0.8082 1.1882 0.5234 -0.0301 -0.1107 0.2186  182 ASN E OD1 
9191  N ND2 . ASN E 182 ? 0.8434 1.2029 0.4842 -0.0485 -0.1330 0.1762  182 ASN E ND2 
9192  N N   . ASP E 183 ? 0.8661 1.2961 0.4989 -0.0004 -0.1002 0.2356  183 ASP E N   
9193  C CA  . ASP E 183 ? 0.8767 1.3388 0.5095 0.0120  -0.0921 0.2606  183 ASP E CA  
9194  C C   . ASP E 183 ? 0.9042 1.3659 0.4866 0.0099  -0.0971 0.2415  183 ASP E C   
9195  O O   . ASP E 183 ? 0.9170 1.3559 0.4645 -0.0019 -0.1085 0.2094  183 ASP E O   
9196  C CB  . ASP E 183 ? 0.8836 1.4007 0.5332 0.0124  -0.1003 0.2951  183 ASP E CB  
9197  C CG  . ASP E 183 ? 0.9024 1.4423 0.5251 -0.0055 -0.1250 0.2847  183 ASP E CG  
9198  O OD1 . ASP E 183 ? 0.9239 1.4515 0.5010 -0.0166 -0.1368 0.2555  183 ASP E OD1 
9199  O OD2 . ASP E 183 ? 0.8969 1.4675 0.5458 -0.0088 -0.1324 0.3058  183 ASP E OD2 
9200  N N   . ALA E 184 ? 0.9149 1.4016 0.4945 0.0218  -0.0876 0.2619  184 ALA E N   
9201  C CA  . ALA E 184 ? 0.9434 1.4341 0.4760 0.0221  -0.0894 0.2470  184 ALA E CA  
9202  C C   . ALA E 184 ? 0.9759 1.4920 0.4631 0.0071  -0.1124 0.2338  184 ALA E C   
9203  O O   . ALA E 184 ? 1.0006 1.5046 0.4433 0.0025  -0.1171 0.2070  184 ALA E O   
9204  C CB  . ALA E 184 ? 0.9494 1.4685 0.4915 0.0378  -0.0742 0.2772  184 ALA E CB  
9205  N N   . ALA E 185 ? 0.9772 1.5283 0.4769 -0.0003 -0.1264 0.2521  185 ALA E N   
9206  C CA  . ALA E 185 ? 1.0079 1.5854 0.4693 -0.0169 -0.1503 0.2402  185 ALA E CA  
9207  C C   . ALA E 185 ? 1.0114 1.5480 0.4512 -0.0335 -0.1622 0.1999  185 ALA E C   
9208  O O   . ALA E 185 ? 1.0434 1.5809 0.4375 -0.0454 -0.1765 0.1753  185 ALA E O   
9209  C CB  . ALA E 185 ? 1.0053 1.6317 0.4931 -0.0204 -0.1617 0.2723  185 ALA E CB  
9210  N N   . GLU E 186 ? 0.9808 1.4815 0.4531 -0.0342 -0.1560 0.1934  186 GLU E N   
9211  C CA  . GLU E 186 ? 0.9829 1.4417 0.4386 -0.0487 -0.1652 0.1579  186 GLU E CA  
9212  C C   . GLU E 186 ? 0.9919 1.4068 0.4182 -0.0445 -0.1565 0.1272  186 GLU E C   
9213  O O   . GLU E 186 ? 1.0125 1.4030 0.4052 -0.0567 -0.1674 0.0957  186 GLU E O   
9214  C CB  . GLU E 186 ? 0.9491 1.3856 0.4478 -0.0500 -0.1605 0.1623  186 GLU E CB  
9215  C CG  . GLU E 186 ? 0.9536 1.3563 0.4379 -0.0672 -0.1729 0.1317  186 GLU E CG  
9216  C CD  . GLU E 186 ? 0.9240 1.3138 0.4493 -0.0697 -0.1695 0.1395  186 GLU E CD  
9217  O OE1 . GLU E 186 ? 0.8974 1.2620 0.4503 -0.0573 -0.1519 0.1442  186 GLU E OE1 
9218  O OE2 . GLU E 186 ? 0.9291 1.3343 0.4588 -0.0846 -0.1844 0.1402  186 GLU E OE2 
9219  N N   . GLN E 187 ? 0.9776 1.3823 0.4191 -0.0272 -0.1365 0.1370  187 GLN E N   
9220  C CA  . GLN E 187 ? 0.9867 1.3563 0.4039 -0.0207 -0.1265 0.1124  187 GLN E CA  
9221  C C   . GLN E 187 ? 1.0298 1.4129 0.3938 -0.0265 -0.1366 0.0945  187 GLN E C   
9222  O O   . GLN E 187 ? 1.0472 1.3973 0.3805 -0.0333 -0.1414 0.0612  187 GLN E O   
9223  C CB  . GLN E 187 ? 0.9676 1.3376 0.4116 -0.0016 -0.1042 0.1323  187 GLN E CB  
9224  C CG  . GLN E 187 ? 0.9794 1.3257 0.3995 0.0069  -0.0927 0.1129  187 GLN E CG  
9225  C CD  . GLN E 187 ? 0.9720 1.2655 0.3861 0.0028  -0.0927 0.0796  187 GLN E CD  
9226  O OE1 . GLN E 187 ? 0.9439 1.2126 0.3888 0.0018  -0.0900 0.0791  187 GLN E OE1 
9227  N NE2 . GLN E 187 ? 0.9989 1.2753 0.3730 0.0012  -0.0951 0.0522  187 GLN E NE2 
9228  N N   . THR E 188 ? 1.0493 1.4810 0.4024 -0.0236 -0.1395 0.1169  188 THR E N   
9229  C CA  . THR E 188 ? 1.0942 1.5451 0.3948 -0.0289 -0.1492 0.1019  188 THR E CA  
9230  C C   . THR E 188 ? 1.1192 1.5679 0.3920 -0.0504 -0.1728 0.0779  188 THR E C   
9231  O O   . THR E 188 ? 1.1528 1.5849 0.3817 -0.0577 -0.1795 0.0466  188 THR E O   
9232  C CB  . THR E 188 ? 1.1097 1.6182 0.4056 -0.0213 -0.1480 0.1350  188 THR E CB  
9233  O OG1 . THR E 188 ? 1.0964 1.6401 0.4227 -0.0264 -0.1583 0.1636  188 THR E OG1 
9234  C CG2 . THR E 188 ? 1.0935 1.6028 0.4111 -0.0007 -0.1237 0.1563  188 THR E CG2 
9235  N N   . LYS E 189 ? 1.1042 1.5688 0.4043 -0.0606 -0.1848 0.0921  189 LYS E N   
9236  C CA  . LYS E 189 ? 1.1259 1.5893 0.4065 -0.0825 -0.2074 0.0715  189 LYS E CA  
9237  C C   . LYS E 189 ? 1.1301 1.5345 0.3956 -0.0907 -0.2083 0.0326  189 LYS E C   
9238  O O   . LYS E 189 ? 1.1641 1.5589 0.3934 -0.1062 -0.2233 0.0050  189 LYS E O   
9239  C CB  . LYS E 189 ? 1.1029 1.5907 0.4243 -0.0902 -0.2167 0.0956  189 LYS E CB  
9240  C CG  . LYS E 189 ? 1.1214 1.6039 0.4297 -0.1139 -0.2389 0.0745  189 LYS E CG  
9241  C CD  . LYS E 189 ? 1.1005 1.6130 0.4503 -0.1213 -0.2478 0.1002  189 LYS E CD  
9242  C CE  . LYS E 189 ? 1.1228 1.6338 0.4583 -0.1464 -0.2706 0.0793  189 LYS E CE  
9243  N NZ  . LYS E 189 ? 1.0933 1.6015 0.4741 -0.1528 -0.2722 0.0919  189 LYS E NZ  
9244  N N   . LEU E 190 ? 1.0975 1.4625 0.3913 -0.0804 -0.1925 0.0310  190 LEU E N   
9245  C CA  . LEU E 190 ? 1.0983 1.4077 0.3835 -0.0865 -0.1925 -0.0013 190 LEU E CA  
9246  C C   . LEU E 190 ? 1.1188 1.3987 0.3705 -0.0777 -0.1827 -0.0267 190 LEU E C   
9247  O O   . LEU E 190 ? 1.1462 1.3960 0.3670 -0.0876 -0.1906 -0.0585 190 LEU E O   
9248  C CB  . LEU E 190 ? 1.0559 1.3380 0.3862 -0.0802 -0.1812 0.0082  190 LEU E CB  
9249  C CG  . LEU E 190 ? 1.0403 1.3314 0.3992 -0.0931 -0.1920 0.0195  190 LEU E CG  
9250  C CD1 . LEU E 190 ? 0.9980 1.2732 0.4030 -0.0826 -0.1772 0.0358  190 LEU E CD1 
9251  C CD2 . LEU E 190 ? 1.0624 1.3237 0.3997 -0.1122 -0.2071 -0.0100 190 LEU E CD2 
9252  N N   . TYR E 191 ? 1.1055 1.3933 0.3663 -0.0590 -0.1647 -0.0119 191 TYR E N   
9253  C CA  . TYR E 191 ? 1.1178 1.3770 0.3568 -0.0475 -0.1515 -0.0324 191 TYR E CA  
9254  C C   . TYR E 191 ? 1.1420 1.4352 0.3553 -0.0369 -0.1439 -0.0236 191 TYR E C   
9255  O O   . TYR E 191 ? 1.1578 1.4324 0.3499 -0.0274 -0.1327 -0.0405 191 TYR E O   
9256  C CB  . TYR E 191 ? 1.0786 1.3071 0.3553 -0.0340 -0.1341 -0.0265 191 TYR E CB  
9257  C CG  . TYR E 191 ? 1.0493 1.2539 0.3576 -0.0422 -0.1393 -0.0259 191 TYR E CG  
9258  C CD1 . TYR E 191 ? 1.0578 1.2202 0.3537 -0.0524 -0.1472 -0.0542 191 TYR E CD1 
9259  C CD2 . TYR E 191 ? 1.0157 1.2401 0.3660 -0.0394 -0.1356 0.0033  191 TYR E CD2 
9260  C CE1 . TYR E 191 ? 1.0332 1.1753 0.3564 -0.0598 -0.1512 -0.0526 191 TYR E CE1 
9261  C CE2 . TYR E 191 ? 0.9916 1.1953 0.3690 -0.0465 -0.1391 0.0033  191 TYR E CE2 
9262  C CZ  . TYR E 191 ? 1.0003 1.1638 0.3631 -0.0569 -0.1470 -0.0243 191 TYR E CZ  
9263  O OH  . TYR E 191 ? 0.9785 1.1227 0.3664 -0.0638 -0.1498 -0.0233 191 TYR E OH  
9264  N N   . GLN E 192 ? 1.1459 1.4900 0.3617 -0.0382 -0.1496 0.0036  192 GLN E N   
9265  C CA  . GLN E 192 ? 1.1684 1.5521 0.3620 -0.0280 -0.1425 0.0184  192 GLN E CA  
9266  C C   . GLN E 192 ? 1.1463 1.5288 0.3636 -0.0073 -0.1184 0.0367  192 GLN E C   
9267  O O   . GLN E 192 ? 1.1352 1.5551 0.3735 0.0014  -0.1113 0.0711  192 GLN E O   
9268  C CB  . GLN E 192 ? 1.2204 1.6032 0.3552 -0.0346 -0.1501 -0.0121 192 GLN E CB  
9269  C CG  . GLN E 192 ? 1.2526 1.6801 0.3600 -0.0492 -0.1710 -0.0070 192 GLN E CG  
9270  C CD  . GLN E 192 ? 1.3083 1.7457 0.3555 -0.0532 -0.1761 -0.0320 192 GLN E CD  
9271  O OE1 . GLN E 192 ? 1.3409 1.8069 0.3596 -0.0683 -0.1956 -0.0370 192 GLN E OE1 
9272  N NE2 . GLN E 192 ? 1.3217 1.7372 0.3491 -0.0397 -0.1587 -0.0477 192 GLN E NE2 
9273  N N   . ASN E 193 ? 1.1416 1.4825 0.3567 0.0003  -0.1059 0.0148  193 ASN E N   
9274  C CA  . ASN E 193 ? 1.1213 1.4591 0.3604 0.0188  -0.0831 0.0295  193 ASN E CA  
9275  C C   . ASN E 193 ? 1.0776 1.4256 0.3719 0.0241  -0.0761 0.0630  193 ASN E C   
9276  O O   . ASN E 193 ? 1.0506 1.3744 0.3720 0.0178  -0.0813 0.0596  193 ASN E O   
9277  C CB  . ASN E 193 ? 1.1168 1.4046 0.3545 0.0242  -0.0736 0.0005  193 ASN E CB  
9278  C CG  . ASN E 193 ? 1.1601 1.4298 0.3464 0.0182  -0.0808 -0.0358 193 ASN E CG  
9279  O OD1 . ASN E 193 ? 1.1884 1.4692 0.3442 0.0042  -0.0982 -0.0470 193 ASN E OD1 
9280  N ND2 . ASN E 193 ? 1.1670 1.4086 0.3450 0.0287  -0.0674 -0.0550 193 ASN E ND2 
9281  N N   . PRO E 194 ? 1.0726 1.4565 0.3833 0.0357  -0.0639 0.0957  194 PRO E N   
9282  C CA  . PRO E 194 ? 1.0363 1.4318 0.3993 0.0408  -0.0572 0.1288  194 PRO E CA  
9283  C C   . PRO E 194 ? 1.0002 1.3558 0.4029 0.0480  -0.0428 0.1246  194 PRO E C   
9284  O O   . PRO E 194 ? 0.9711 1.3140 0.4095 0.0449  -0.0445 0.1321  194 PRO E O   
9285  C CB  . PRO E 194 ? 1.0484 1.4894 0.4134 0.0522  -0.0463 0.1623  194 PRO E CB  
9286  C CG  . PRO E 194 ? 1.0798 1.5202 0.4039 0.0580  -0.0387 0.1447  194 PRO E CG  
9287  C CD  . PRO E 194 ? 1.1017 1.5140 0.3848 0.0458  -0.0535 0.1034  194 PRO E CD  
9288  N N   . THR E 195 ? 1.0037 1.3415 0.3995 0.0575  -0.0288 0.1123  195 THR E N   
9289  C CA  . THR E 195 ? 0.9738 1.2750 0.4033 0.0639  -0.0161 0.1053  195 THR E CA  
9290  C C   . THR E 195 ? 0.9820 1.2424 0.3859 0.0585  -0.0229 0.0664  195 THR E C   
9291  O O   . THR E 195 ? 1.0122 1.2720 0.3770 0.0597  -0.0235 0.0477  195 THR E O   
9292  C CB  . THR E 195 ? 0.9718 1.2838 0.4174 0.0789  0.0051  0.1212  195 THR E CB  
9293  O OG1 . THR E 195 ? 0.9755 1.3304 0.4336 0.0840  0.0106  0.1574  195 THR E OG1 
9294  C CG2 . THR E 195 ? 0.9381 1.2191 0.4284 0.0843  0.0174  0.1208  195 THR E CG2 
9295  N N   . THR E 196 ? 0.9572 1.1836 0.3826 0.0530  -0.0276 0.0546  196 THR E N   
9296  C CA  . THR E 196 ? 0.9648 1.1512 0.3686 0.0473  -0.0353 0.0201  196 THR E CA  
9297  C C   . THR E 196 ? 0.9353 1.0859 0.3716 0.0519  -0.0273 0.0127  196 THR E C   
9298  O O   . THR E 196 ? 0.9079 1.0624 0.3842 0.0566  -0.0183 0.0324  196 THR E O   
9299  C CB  . THR E 196 ? 0.9744 1.1545 0.3592 0.0311  -0.0555 0.0076  196 THR E CB  
9300  O OG1 . THR E 196 ? 0.9457 1.1295 0.3659 0.0263  -0.0588 0.0255  196 THR E OG1 
9301  C CG2 . THR E 196 ? 1.0087 1.2230 0.3561 0.0250  -0.0657 0.0097  196 THR E CG2 
9302  N N   . TYR E 197 ? 0.9435 1.0593 0.3623 0.0505  -0.0309 -0.0159 197 TYR E N   
9303  C CA  . TYR E 197 ? 0.9199 1.0023 0.3646 0.0547  -0.0252 -0.0252 197 TYR E CA  
9304  C C   . TYR E 197 ? 0.9313 0.9757 0.3543 0.0480  -0.0363 -0.0549 197 TYR E C   
9305  O O   . TYR E 197 ? 0.9606 1.0021 0.3468 0.0417  -0.0458 -0.0710 197 TYR E O   
9306  C CB  . TYR E 197 ? 0.9179 1.0031 0.3744 0.0690  -0.0080 -0.0226 197 TYR E CB  
9307  C CG  . TYR E 197 ? 0.9492 1.0272 0.3694 0.0739  -0.0063 -0.0442 197 TYR E CG  
9308  C CD1 . TYR E 197 ? 0.9776 1.0850 0.3689 0.0770  -0.0029 -0.0396 197 TYR E CD1 
9309  C CD2 . TYR E 197 ? 0.9527 0.9948 0.3668 0.0759  -0.0079 -0.0692 197 TYR E CD2 
9310  C CE1 . TYR E 197 ? 1.0095 1.1096 0.3663 0.0820  0.0000  -0.0610 197 TYR E CE1 
9311  C CE2 . TYR E 197 ? 0.9836 1.0176 0.3660 0.0815  -0.0050 -0.0894 197 TYR E CE2 
9312  C CZ  . TYR E 197 ? 1.0123 1.0748 0.3658 0.0846  -0.0006 -0.0861 197 TYR E CZ  
9313  O OH  . TYR E 197 ? 1.0457 1.0995 0.3666 0.0908  0.0034  -0.1077 197 TYR E OH  
9314  N N   . ILE E 198 ? 0.9098 0.9250 0.3560 0.0493  -0.0348 -0.0617 198 ILE E N   
9315  C CA  . ILE E 198 ? 0.9193 0.8964 0.3500 0.0459  -0.0427 -0.0876 198 ILE E CA  
9316  C C   . ILE E 198 ? 0.9033 0.8610 0.3572 0.0565  -0.0328 -0.0924 198 ILE E C   
9317  O O   . ILE E 198 ? 0.8754 0.8303 0.3624 0.0573  -0.0291 -0.0816 198 ILE E O   
9318  C CB  . ILE E 198 ? 0.9100 0.8693 0.3441 0.0327  -0.0560 -0.0909 198 ILE E CB  
9319  C CG1 . ILE E 198 ? 0.9153 0.9017 0.3416 0.0220  -0.0648 -0.0779 198 ILE E CG1 
9320  C CG2 . ILE E 198 ? 0.9300 0.8528 0.3399 0.0280  -0.0653 -0.1171 198 ILE E CG2 
9321  C CD1 . ILE E 198 ? 0.9041 0.8779 0.3389 0.0093  -0.0760 -0.0777 198 ILE E CD1 
9322  N N   . SER E 199 ? 0.9225 0.8677 0.3597 0.0647  -0.0285 -0.1089 199 SER E N   
9323  C CA  . SER E 199 ? 0.9100 0.8383 0.3689 0.0748  -0.0204 -0.1145 199 SER E CA  
9324  C C   . SER E 199 ? 0.9195 0.8096 0.3661 0.0722  -0.0300 -0.1367 199 SER E C   
9325  O O   . SER E 199 ? 0.9489 0.8253 0.3634 0.0706  -0.0354 -0.1539 199 SER E O   
9326  C CB  . SER E 199 ? 0.9228 0.8672 0.3790 0.0881  -0.0062 -0.1142 199 SER E CB  
9327  O OG  . SER E 199 ? 0.9586 0.9021 0.3749 0.0888  -0.0083 -0.1295 199 SER E OG  
9328  N N   . VAL E 200 ? 0.8969 0.7695 0.3688 0.0719  -0.0319 -0.1358 200 VAL E N   
9329  C CA  . VAL E 200 ? 0.9036 0.7408 0.3682 0.0702  -0.0407 -0.1530 200 VAL E CA  
9330  C C   . VAL E 200 ? 0.8923 0.7209 0.3805 0.0818  -0.0336 -0.1557 200 VAL E C   
9331  O O   . VAL E 200 ? 0.8668 0.7077 0.3863 0.0841  -0.0277 -0.1430 200 VAL E O   
9332  C CB  . VAL E 200 ? 0.8891 0.7131 0.3601 0.0578  -0.0516 -0.1496 200 VAL E CB  
9333  C CG1 . VAL E 200 ? 0.9047 0.6925 0.3599 0.0546  -0.0617 -0.1669 200 VAL E CG1 
9334  C CG2 . VAL E 200 ? 0.8920 0.7342 0.3514 0.0465  -0.0569 -0.1403 200 VAL E CG2 
9335  N N   . GLY E 201 ? 0.9127 0.7202 0.3872 0.0890  -0.0344 -0.1724 201 GLY E N   
9336  C CA  . GLY E 201 ? 0.9051 0.7063 0.4016 0.1008  -0.0286 -0.1754 201 GLY E CA  
9337  C C   . GLY E 201 ? 0.9165 0.6832 0.4057 0.1016  -0.0380 -0.1899 201 GLY E C   
9338  O O   . GLY E 201 ? 0.9414 0.6871 0.4025 0.0972  -0.0452 -0.2023 201 GLY E O   
9339  N N   . THR E 202 ? 0.8995 0.6607 0.4148 0.1066  -0.0384 -0.1877 202 THR E N   
9340  C CA  . THR E 202 ? 0.9108 0.6431 0.4238 0.1113  -0.0456 -0.1990 202 THR E CA  
9341  C C   . THR E 202 ? 0.9002 0.6433 0.4426 0.1243  -0.0383 -0.1966 202 THR E C   
9342  O O   . THR E 202 ? 0.8922 0.6615 0.4496 0.1302  -0.0266 -0.1895 202 THR E O   
9343  C CB  . THR E 202 ? 0.9003 0.6139 0.4142 0.1002  -0.0583 -0.1970 202 THR E CB  
9344  O OG1 . THR E 202 ? 0.8706 0.5989 0.4141 0.0985  -0.0573 -0.1859 202 THR E OG1 
9345  C CG2 . THR E 202 ? 0.9060 0.6157 0.3975 0.0860  -0.0645 -0.1961 202 THR E CG2 
9346  N N   . SER E 203 ? 0.9012 0.6259 0.4529 0.1288  -0.0451 -0.2013 203 SER E N   
9347  C CA  . SER E 203 ? 0.8881 0.6260 0.4717 0.1392  -0.0406 -0.1976 203 SER E CA  
9348  C C   . SER E 203 ? 0.8566 0.6164 0.4682 0.1321  -0.0392 -0.1848 203 SER E C   
9349  O O   . SER E 203 ? 0.8444 0.6263 0.4836 0.1383  -0.0307 -0.1788 203 SER E O   
9350  C CB  . SER E 203 ? 0.8971 0.6120 0.4841 0.1447  -0.0503 -0.2038 203 SER E CB  
9351  O OG  . SER E 203 ? 0.8896 0.5890 0.4707 0.1330  -0.0627 -0.2016 203 SER E OG  
9352  N N   . THR E 204 ? 0.8454 0.5986 0.4507 0.1190  -0.0468 -0.1808 204 THR E N   
9353  C CA  . THR E 204 ? 0.8189 0.5886 0.4492 0.1117  -0.0454 -0.1703 204 THR E CA  
9354  C C   . THR E 204 ? 0.8111 0.5970 0.4377 0.1045  -0.0385 -0.1608 204 THR E C   
9355  O O   . THR E 204 ? 0.7953 0.6032 0.4465 0.1046  -0.0295 -0.1507 204 THR E O   
9356  C CB  . THR E 204 ? 0.8115 0.5643 0.4416 0.1031  -0.0577 -0.1715 204 THR E CB  
9357  O OG1 . THR E 204 ? 0.8210 0.5568 0.4227 0.0940  -0.0642 -0.1735 204 THR E OG1 
9358  C CG2 . THR E 204 ? 0.8201 0.5591 0.4545 0.1105  -0.0655 -0.1785 204 THR E CG2 
9359  N N   . LEU E 205 ? 0.8237 0.5994 0.4210 0.0981  -0.0428 -0.1633 205 LEU E N   
9360  C CA  . LEU E 205 ? 0.8169 0.6089 0.4103 0.0904  -0.0387 -0.1530 205 LEU E CA  
9361  C C   . LEU E 205 ? 0.8223 0.6388 0.4172 0.0973  -0.0262 -0.1469 205 LEU E C   
9362  O O   . LEU E 205 ? 0.8431 0.6572 0.4205 0.1049  -0.0234 -0.1553 205 LEU E O   
9363  C CB  . LEU E 205 ? 0.8307 0.6069 0.3931 0.0808  -0.0481 -0.1576 205 LEU E CB  
9364  C CG  . LEU E 205 ? 0.8229 0.6152 0.3821 0.0712  -0.0470 -0.1461 205 LEU E CG  
9365  C CD1 . LEU E 205 ? 0.7972 0.5983 0.3844 0.0664  -0.0446 -0.1347 205 LEU E CD1 
9366  C CD2 . LEU E 205 ? 0.8387 0.6149 0.3689 0.0611  -0.0576 -0.1522 205 LEU E CD2 
9367  N N   . ASN E 206 ? 0.8057 0.6454 0.4219 0.0952  -0.0178 -0.1320 206 ASN E N   
9368  C CA  . ASN E 206 ? 0.8106 0.6767 0.4282 0.1005  -0.0056 -0.1220 206 ASN E CA  
9369  C C   . ASN E 206 ? 0.8010 0.6839 0.4219 0.0926  -0.0034 -0.1063 206 ASN E C   
9370  O O   . ASN E 206 ? 0.7831 0.6815 0.4338 0.0924  0.0046  -0.0922 206 ASN E O   
9371  C CB  . ASN E 206 ? 0.8009 0.6829 0.4510 0.1097  0.0061  -0.1162 206 ASN E CB  
9372  C CG  . ASN E 206 ? 0.8078 0.7180 0.4592 0.1159  0.0202  -0.1043 206 ASN E CG  
9373  O OD1 . ASN E 206 ? 0.8275 0.7426 0.4483 0.1171  0.0208  -0.1066 206 ASN E OD1 
9374  N ND2 . ASN E 206 ? 0.7936 0.7227 0.4801 0.1194  0.0316  -0.0916 206 ASN E ND2 
9375  N N   . GLN E 207 ? 0.8149 0.6946 0.4062 0.0860  -0.0108 -0.1086 207 GLN E N   
9376  C CA  . GLN E 207 ? 0.8075 0.7014 0.4005 0.0777  -0.0117 -0.0943 207 GLN E CA  
9377  C C   . GLN E 207 ? 0.8239 0.7419 0.3973 0.0791  -0.0075 -0.0865 207 GLN E C   
9378  O O   . GLN E 207 ? 0.8471 0.7623 0.3925 0.0826  -0.0087 -0.0981 207 GLN E O   
9379  C CB  . GLN E 207 ? 0.8086 0.6815 0.3867 0.0668  -0.0253 -0.1018 207 GLN E CB  
9380  C CG  . GLN E 207 ? 0.8089 0.6958 0.3784 0.0577  -0.0292 -0.0907 207 GLN E CG  
9381  C CD  . GLN E 207 ? 0.8117 0.6777 0.3672 0.0469  -0.0421 -0.0987 207 GLN E CD  
9382  O OE1 . GLN E 207 ? 0.8290 0.6941 0.3584 0.0400  -0.0503 -0.1032 207 GLN E OE1 
9383  N NE2 . GLN E 207 ? 0.7967 0.6462 0.3690 0.0448  -0.0439 -0.1009 207 GLN E NE2 
9384  N N   . ARG E 208 ? 0.8136 0.7554 0.4019 0.0768  -0.0021 -0.0666 208 ARG E N   
9385  C CA  . ARG E 208 ? 0.8291 0.7969 0.3983 0.0763  -0.0004 -0.0560 208 ARG E CA  
9386  C C   . ARG E 208 ? 0.8168 0.7996 0.3987 0.0688  -0.0028 -0.0377 208 ARG E C   
9387  O O   . ARG E 208 ? 0.7989 0.7941 0.4139 0.0714  0.0066  -0.0201 208 ARG E O   
9388  C CB  . ARG E 208 ? 0.8341 0.8263 0.4123 0.0871  0.0145  -0.0449 208 ARG E CB  
9389  C CG  . ARG E 208 ? 0.8576 0.8757 0.4067 0.0879  0.0155  -0.0382 208 ARG E CG  
9390  C CD  . ARG E 208 ? 0.8590 0.9066 0.4232 0.0977  0.0320  -0.0194 208 ARG E CD  
9391  N NE  . ARG E 208 ? 0.8879 0.9582 0.4170 0.1003  0.0334  -0.0181 208 ARG E NE  
9392  C CZ  . ARG E 208 ? 0.9137 0.9777 0.4120 0.1053  0.0343  -0.0369 208 ARG E CZ  
9393  N NH1 . ARG E 208 ? 0.9132 0.9491 0.4133 0.1091  0.0338  -0.0573 208 ARG E NH1 
9394  N NH2 . ARG E 208 ? 0.9424 1.0290 0.4074 0.1070  0.0359  -0.0354 208 ARG E NH2 
9395  N N   . LEU E 209 ? 0.8279 0.8093 0.3854 0.0594  -0.0150 -0.0418 209 LEU E N   
9396  C CA  . LEU E 209 ? 0.8175 0.8138 0.3866 0.0521  -0.0186 -0.0252 209 LEU E CA  
9397  C C   . LEU E 209 ? 0.8311 0.8628 0.3887 0.0529  -0.0169 -0.0083 209 LEU E C   
9398  O O   . LEU E 209 ? 0.8549 0.8940 0.3809 0.0539  -0.0197 -0.0168 209 LEU E O   
9399  C CB  . LEU E 209 ? 0.8214 0.7984 0.3736 0.0403  -0.0334 -0.0377 209 LEU E CB  
9400  C CG  . LEU E 209 ? 0.8123 0.7543 0.3703 0.0385  -0.0371 -0.0541 209 LEU E CG  
9401  C CD1 . LEU E 209 ? 0.8225 0.7472 0.3587 0.0266  -0.0516 -0.0658 209 LEU E CD1 
9402  C CD2 . LEU E 209 ? 0.7864 0.7260 0.3822 0.0407  -0.0291 -0.0434 209 LEU E CD2 
9403  N N   . VAL E 210 ? 0.8178 0.8715 0.4011 0.0529  -0.0120 0.0155  210 VAL E N   
9404  C CA  . VAL E 210 ? 0.8301 0.9207 0.4054 0.0530  -0.0120 0.0354  210 VAL E CA  
9405  C C   . VAL E 210 ? 0.8209 0.9218 0.4085 0.0448  -0.0196 0.0487  210 VAL E C   
9406  O O   . VAL E 210 ? 0.7994 0.8868 0.4168 0.0439  -0.0163 0.0526  210 VAL E O   
9407  C CB  . VAL E 210 ? 0.8259 0.9408 0.4248 0.0644  0.0045  0.0583  210 VAL E CB  
9408  C CG1 . VAL E 210 ? 0.8364 0.9441 0.4241 0.0726  0.0128  0.0459  210 VAL E CG1 
9409  C CG2 . VAL E 210 ? 0.7995 0.9097 0.4457 0.0675  0.0150  0.0740  210 VAL E CG2 
9410  N N   . PRO E 211 ? 0.8386 0.9644 0.4036 0.0385  -0.0300 0.0550  211 PRO E N   
9411  C CA  . PRO E 211 ? 0.8299 0.9692 0.4097 0.0309  -0.0371 0.0690  211 PRO E CA  
9412  C C   . PRO E 211 ? 0.8147 0.9789 0.4336 0.0388  -0.0250 0.1004  211 PRO E C   
9413  O O   . PRO E 211 ? 0.8225 1.0124 0.4438 0.0469  -0.0168 0.1180  211 PRO E O   
9414  C CB  . PRO E 211 ? 0.8559 1.0183 0.3998 0.0221  -0.0520 0.0668  211 PRO E CB  
9415  C CG  . PRO E 211 ? 0.8791 1.0282 0.3857 0.0231  -0.0541 0.0436  211 PRO E CG  
9416  C CD  . PRO E 211 ? 0.8689 1.0094 0.3924 0.0366  -0.0371 0.0461  211 PRO E CD  
9417  N N   . ARG E 212 ? 0.7952 0.9508 0.4445 0.0367  -0.0231 0.1074  212 ARG E N   
9418  C CA  . ARG E 212 ? 0.7817 0.9566 0.4715 0.0438  -0.0114 0.1362  212 ARG E CA  
9419  C C   . ARG E 212 ? 0.7856 0.9904 0.4783 0.0381  -0.0208 0.1539  212 ARG E C   
9420  O O   . ARG E 212 ? 0.7819 0.9772 0.4711 0.0286  -0.0308 0.1442  212 ARG E O   
9421  C CB  . ARG E 212 ? 0.7595 0.9046 0.4833 0.0462  -0.0013 0.1315  212 ARG E CB  
9422  C CG  . ARG E 212 ? 0.7552 0.8703 0.4777 0.0501  0.0055  0.1121  212 ARG E CG  
9423  C CD  . ARG E 212 ? 0.7360 0.8264 0.4938 0.0525  0.0158  0.1096  212 ARG E CD  
9424  N NE  . ARG E 212 ? 0.7286 0.8071 0.4905 0.0450  0.0094  0.1038  212 ARG E NE  
9425  C CZ  . ARG E 212 ? 0.7290 0.7818 0.4704 0.0371  -0.0004 0.0802  212 ARG E CZ  
9426  N NH1 . ARG E 212 ? 0.7363 0.7707 0.4518 0.0359  -0.0059 0.0592  212 ARG E NH1 
9427  N NH2 . ARG E 212 ? 0.7230 0.7690 0.4710 0.0308  -0.0043 0.0788  212 ARG E NH2 
9428  N N   . ILE E 213 ? 0.7939 1.0365 0.4940 0.0441  -0.0175 0.1810  213 ILE E N   
9429  C CA  . ILE E 213 ? 0.7994 1.0772 0.5038 0.0398  -0.0270 0.2013  213 ILE E CA  
9430  C C   . ILE E 213 ? 0.7805 1.0642 0.5348 0.0466  -0.0151 0.2257  213 ILE E C   
9431  O O   . ILE E 213 ? 0.7720 1.0513 0.5560 0.0578  0.0016  0.2397  213 ILE E O   
9432  C CB  . ILE E 213 ? 0.8221 1.1421 0.5058 0.0428  -0.0310 0.2196  213 ILE E CB  
9433  C CG1 . ILE E 213 ? 0.8448 1.1575 0.4784 0.0379  -0.0397 0.1940  213 ILE E CG1 
9434  C CG2 . ILE E 213 ? 0.8275 1.1876 0.5185 0.0383  -0.0420 0.2424  213 ILE E CG2 
9435  C CD1 . ILE E 213 ? 0.8549 1.1741 0.4807 0.0491  -0.0269 0.1997  213 ILE E CD1 
9436  N N   . ALA E 214 ? 0.7756 1.0684 0.5402 0.0398  -0.0234 0.2305  214 ALA E N   
9437  C CA  . ALA E 214 ? 0.7606 1.0617 0.5721 0.0466  -0.0125 0.2540  214 ALA E CA  
9438  C C   . ALA E 214 ? 0.7623 1.0885 0.5775 0.0383  -0.0254 0.2632  214 ALA E C   
9439  O O   . ALA E 214 ? 0.7693 1.0918 0.5547 0.0249  -0.0416 0.2437  214 ALA E O   
9440  C CB  . ALA E 214 ? 0.7424 1.0009 0.5771 0.0492  0.0003  0.2387  214 ALA E CB  
9441  N N   . THR E 215 ? 0.7569 1.1091 0.6111 0.0463  -0.0178 0.2936  215 THR E N   
9442  C CA  . THR E 215 ? 0.7559 1.1335 0.6233 0.0401  -0.0274 0.3055  215 THR E CA  
9443  C C   . THR E 215 ? 0.7399 1.0836 0.6256 0.0370  -0.0209 0.2894  215 THR E C   
9444  O O   . THR E 215 ? 0.7278 1.0519 0.6471 0.0473  -0.0028 0.2946  215 THR E O   
9445  C CB  . THR E 215 ? 0.7567 1.1758 0.6624 0.0518  -0.0203 0.3461  215 THR E CB  
9446  O OG1 . THR E 215 ? 0.7727 1.2214 0.6618 0.0567  -0.0234 0.3626  215 THR E OG1 
9447  C CG2 . THR E 215 ? 0.7577 1.2101 0.6751 0.0446  -0.0328 0.3593  215 THR E CG2 
9448  N N   . ARG E 216 ? 0.7424 1.0786 0.6054 0.0225  -0.0355 0.2695  216 ARG E N   
9449  C CA  . ARG E 216 ? 0.7303 1.0329 0.6031 0.0182  -0.0304 0.2515  216 ARG E CA  
9450  C C   . ARG E 216 ? 0.7305 1.0564 0.6162 0.0098  -0.0391 0.2604  216 ARG E C   
9451  O O   . ARG E 216 ? 0.7416 1.1044 0.6169 0.0024  -0.0545 0.2716  216 ARG E O   
9452  C CB  . ARG E 216 ? 0.7331 0.9971 0.5666 0.0085  -0.0379 0.2164  216 ARG E CB  
9453  C CG  . ARG E 216 ? 0.7332 0.9741 0.5549 0.0164  -0.0295 0.2060  216 ARG E CG  
9454  C CD  . ARG E 216 ? 0.7402 0.9499 0.5207 0.0069  -0.0396 0.1737  216 ARG E CD  
9455  N NE  . ARG E 216 ? 0.7594 0.9887 0.5036 -0.0008 -0.0559 0.1694  216 ARG E NE  
9456  C CZ  . ARG E 216 ? 0.7706 1.0041 0.4935 0.0036  -0.0560 0.1669  216 ARG E CZ  
9457  N NH1 . ARG E 216 ? 0.7632 0.9839 0.4991 0.0157  -0.0409 0.1696  216 ARG E NH1 
9458  N NH2 . ARG E 216 ? 0.7912 1.0424 0.4793 -0.0044 -0.0711 0.1610  216 ARG E NH2 
9459  N N   . SER E 217 ? 0.7197 1.0251 0.6282 0.0107  -0.0288 0.2554  217 SER E N   
9460  C CA  . SER E 217 ? 0.7190 1.0434 0.6423 0.0028  -0.0346 0.2624  217 SER E CA  
9461  C C   . SER E 217 ? 0.7295 1.0456 0.6144 -0.0161 -0.0541 0.2394  217 SER E C   
9462  O O   . SER E 217 ? 0.7331 1.0149 0.5855 -0.0212 -0.0578 0.2134  217 SER E O   
9463  C CB  . SER E 217 ? 0.7062 1.0075 0.6611 0.0095  -0.0163 0.2607  217 SER E CB  
9464  O OG  . SER E 217 ? 0.7001 0.9988 0.6882 0.0267  0.0031  0.2766  217 SER E OG  
9465  N N   . LYS E 218 ? 0.7362 1.0842 0.6270 -0.0266 -0.0665 0.2497  218 LYS E N   
9466  C CA  . LYS E 218 ? 0.7484 1.0894 0.6073 -0.0460 -0.0848 0.2294  218 LYS E CA  
9467  C C   . LYS E 218 ? 0.7402 1.0419 0.5988 -0.0506 -0.0776 0.2099  218 LYS E C   
9468  O O   . LYS E 218 ? 0.7303 1.0357 0.6209 -0.0464 -0.0659 0.2203  218 LYS E O   
9469  C CB  . LYS E 218 ? 0.7588 1.1473 0.6276 -0.0571 -0.1004 0.2467  218 LYS E CB  
9470  C CG  . LYS E 218 ? 0.7782 1.2005 0.6245 -0.0618 -0.1175 0.2536  218 LYS E CG  
9471  C CD  . LYS E 218 ? 0.7908 1.2585 0.6446 -0.0761 -0.1356 0.2668  218 LYS E CD  
9472  C CE  . LYS E 218 ? 0.8129 1.3194 0.6449 -0.0802 -0.1528 0.2756  218 LYS E CE  
9473  N NZ  . LYS E 218 ? 0.8087 1.3517 0.6686 -0.0624 -0.1439 0.3086  218 LYS E NZ  
9474  N N   . VAL E 219 ? 0.7460 1.0103 0.5682 -0.0584 -0.0837 0.1821  219 VAL E N   
9475  C CA  . VAL E 219 ? 0.7429 0.9714 0.5572 -0.0655 -0.0809 0.1628  219 VAL E CA  
9476  C C   . VAL E 219 ? 0.7595 0.9854 0.5421 -0.0852 -0.1014 0.1475  219 VAL E C   
9477  O O   . VAL E 219 ? 0.7725 0.9950 0.5246 -0.0896 -0.1130 0.1362  219 VAL E O   
9478  C CB  . VAL E 219 ? 0.7372 0.9211 0.5386 -0.0564 -0.0695 0.1438  219 VAL E CB  
9479  C CG1 . VAL E 219 ? 0.7386 0.8859 0.5258 -0.0646 -0.0691 0.1233  219 VAL E CG1 
9480  C CG2 . VAL E 219 ? 0.7228 0.9083 0.5579 -0.0385 -0.0492 0.1581  219 VAL E CG2 
9481  N N   . ASN E 220 ? 0.7608 0.9887 0.5514 -0.0970 -0.1049 0.1474  220 ASN E N   
9482  C CA  . ASN E 220 ? 0.7789 1.0083 0.5459 -0.1175 -0.1245 0.1360  220 ASN E CA  
9483  C C   . ASN E 220 ? 0.7923 1.0608 0.5505 -0.1247 -0.1416 0.1446  220 ASN E C   
9484  O O   . ASN E 220 ? 0.8120 1.0721 0.5374 -0.1380 -0.1577 0.1277  220 ASN E O   
9485  C CB  . ASN E 220 ? 0.7900 0.9706 0.5193 -0.1233 -0.1287 0.1069  220 ASN E CB  
9486  C CG  . ASN E 220 ? 0.7856 0.9345 0.5187 -0.1261 -0.1201 0.0981  220 ASN E CG  
9487  O OD1 . ASN E 220 ? 0.7714 0.9268 0.5335 -0.1185 -0.1056 0.1106  220 ASN E OD1 
9488  N ND2 . ASN E 220 ? 0.8002 0.9144 0.5035 -0.1367 -0.1283 0.0767  220 ASN E ND2 
9489  N N   . GLY E 221 ? 0.7834 1.0944 0.5708 -0.1155 -0.1378 0.1709  221 GLY E N   
9490  C CA  . GLY E 221 ? 0.7966 1.1518 0.5789 -0.1212 -0.1539 0.1833  221 GLY E CA  
9491  C C   . GLY E 221 ? 0.8066 1.1586 0.5592 -0.1145 -0.1575 0.1762  221 GLY E C   
9492  O O   . GLY E 221 ? 0.8233 1.2076 0.5614 -0.1214 -0.1728 0.1811  221 GLY E O   
9493  N N   . GLN E 222 ? 0.7977 1.1128 0.5413 -0.1013 -0.1434 0.1649  222 GLN E N   
9494  C CA  . GLN E 222 ? 0.8067 1.1165 0.5235 -0.0938 -0.1442 0.1578  222 GLN E CA  
9495  C C   . GLN E 222 ? 0.7866 1.0847 0.5233 -0.0730 -0.1234 0.1674  222 GLN E C   
9496  O O   . GLN E 222 ? 0.7707 1.0398 0.5239 -0.0667 -0.1093 0.1626  222 GLN E O   
9497  C CB  . GLN E 222 ? 0.8242 1.0929 0.4984 -0.1033 -0.1524 0.1251  222 GLN E CB  
9498  C CG  . GLN E 222 ? 0.8493 1.1245 0.5001 -0.1250 -0.1735 0.1121  222 GLN E CG  
9499  C CD  . GLN E 222 ? 0.8693 1.1919 0.5107 -0.1311 -0.1886 0.1238  222 GLN E CD  
9500  O OE1 . GLN E 222 ? 0.8735 1.2130 0.5073 -0.1198 -0.1855 0.1322  222 GLN E OE1 
9501  N NE2 . GLN E 222 ? 0.8839 1.2296 0.5258 -0.1496 -0.2054 0.1249  222 GLN E NE2 
9502  N N   . SER E 223 ? 0.7892 1.1106 0.5239 -0.0629 -0.1216 0.1809  223 SER E N   
9503  C CA  . SER E 223 ? 0.7737 1.0859 0.5276 -0.0440 -0.1024 0.1912  223 SER E CA  
9504  C C   . SER E 223 ? 0.7795 1.0620 0.5017 -0.0397 -0.0999 0.1708  223 SER E C   
9505  O O   . SER E 223 ? 0.7691 1.0404 0.5047 -0.0254 -0.0845 0.1760  223 SER E O   
9506  C CB  . SER E 223 ? 0.7729 1.1322 0.5529 -0.0337 -0.0990 0.2250  223 SER E CB  
9507  O OG  . SER E 223 ? 0.7610 1.1411 0.5811 -0.0319 -0.0941 0.2456  223 SER E OG  
9508  N N   . GLY E 224 ? 0.7969 1.0664 0.4790 -0.0520 -0.1146 0.1474  224 GLY E N   
9509  C CA  . GLY E 224 ? 0.8037 1.0409 0.4555 -0.0487 -0.1123 0.1247  224 GLY E CA  
9510  C C   . GLY E 224 ? 0.7903 0.9799 0.4443 -0.0479 -0.1043 0.1048  224 GLY E C   
9511  O O   . GLY E 224 ? 0.7816 0.9614 0.4498 -0.0543 -0.1047 0.1034  224 GLY E O   
9512  N N   . ARG E 225 ? 0.7891 0.9511 0.4293 -0.0399 -0.0970 0.0903  225 ARG E N   
9513  C CA  . ARG E 225 ? 0.7773 0.8961 0.4192 -0.0378 -0.0896 0.0721  225 ARG E CA  
9514  C C   . ARG E 225 ? 0.7916 0.8799 0.3975 -0.0405 -0.0955 0.0455  225 ARG E C   
9515  O O   . ARG E 225 ? 0.8066 0.9044 0.3911 -0.0380 -0.0985 0.0420  225 ARG E O   
9516  C CB  . ARG E 225 ? 0.7575 0.8701 0.4302 -0.0226 -0.0709 0.0828  225 ARG E CB  
9517  C CG  . ARG E 225 ? 0.7427 0.8779 0.4549 -0.0180 -0.0618 0.1074  225 ARG E CG  
9518  C CD  . ARG E 225 ? 0.7344 0.8537 0.4583 -0.0248 -0.0614 0.1019  225 ARG E CD  
9519  N NE  . ARG E 225 ? 0.7215 0.8606 0.4850 -0.0184 -0.0503 0.1245  225 ARG E NE  
9520  C CZ  . ARG E 225 ? 0.7228 0.8959 0.5012 -0.0227 -0.0554 0.1433  225 ARG E CZ  
9521  N NH1 . ARG E 225 ? 0.7371 0.9298 0.4935 -0.0351 -0.0729 0.1421  225 ARG E NH1 
9522  N NH2 . ARG E 225 ? 0.7113 0.8991 0.5283 -0.0146 -0.0427 0.1635  225 ARG E NH2 
9523  N N   . MET E 226 ? 0.7879 0.8402 0.3877 -0.0449 -0.0964 0.0276  226 MET E N   
9524  C CA  . MET E 226 ? 0.8001 0.8192 0.3710 -0.0455 -0.1002 0.0030  226 MET E CA  
9525  C C   . MET E 226 ? 0.7827 0.7725 0.3676 -0.0364 -0.0886 -0.0037 226 MET E C   
9526  O O   . MET E 226 ? 0.7701 0.7499 0.3728 -0.0381 -0.0847 -0.0009 226 MET E O   
9527  C CB  . MET E 226 ? 0.8178 0.8197 0.3660 -0.0610 -0.1146 -0.0126 226 MET E CB  
9528  C CG  . MET E 226 ? 0.8403 0.8668 0.3686 -0.0722 -0.1286 -0.0121 226 MET E CG  
9529  S SD  . MET E 226 ? 0.8685 0.8873 0.3576 -0.0697 -0.1335 -0.0312 226 MET E SD  
9530  C CE  . MET E 226 ? 0.8958 0.9446 0.3646 -0.0869 -0.1517 -0.0305 226 MET E CE  
9531  N N   . GLU E 227 ? 1.1903 0.8949 0.2427 -0.0315 -0.2931 -0.0509 227 GLU E N   
9532  C CA  . GLU E 227 ? 1.1582 0.8324 0.2477 -0.0246 -0.2782 -0.0527 227 GLU E CA  
9533  C C   . GLU E 227 ? 1.1703 0.7999 0.2421 -0.0331 -0.2806 -0.0777 227 GLU E C   
9534  O O   . GLU E 227 ? 1.1990 0.8090 0.2423 -0.0279 -0.2742 -0.0860 227 GLU E O   
9535  C CB  . GLU E 227 ? 1.1524 0.8279 0.2631 -0.0002 -0.2516 -0.0358 227 GLU E CB  
9536  C CG  . GLU E 227 ? 1.1136 0.7772 0.2771 0.0061  -0.2359 -0.0354 227 GLU E CG  
9537  C CD  . GLU E 227 ? 1.1097 0.7778 0.3017 0.0277  -0.2056 -0.0180 227 GLU E CD  
9538  O OE1 . GLU E 227 ? 1.1367 0.8187 0.3057 0.0409  -0.1961 -0.0004 227 GLU E OE1 
9539  O OE2 . GLU E 227 ? 1.0820 0.7407 0.3202 0.0322  -0.1895 -0.0225 227 GLU E OE2 
9540  N N   . PHE E 228 ? 1.1507 0.7641 0.2381 -0.0440 -0.2884 -0.0883 228 PHE E N   
9541  C CA  . PHE E 228 ? 1.1671 0.7390 0.2344 -0.0509 -0.2907 -0.1097 228 PHE E CA  
9542  C C   . PHE E 228 ? 1.1458 0.6957 0.2403 -0.0355 -0.2771 -0.1150 228 PHE E C   
9543  O O   . PHE E 228 ? 1.1106 0.6751 0.2457 -0.0284 -0.2727 -0.1086 228 PHE E O   
9544  C CB  . PHE E 228 ? 1.1699 0.7359 0.2303 -0.0709 -0.3059 -0.1181 228 PHE E CB  
9545  C CG  . PHE E 228 ? 1.1969 0.7836 0.2300 -0.0895 -0.3195 -0.1212 228 PHE E CG  
9546  C CD1 . PHE E 228 ? 1.2402 0.8054 0.2327 -0.1010 -0.3221 -0.1398 228 PHE E CD1 
9547  C CD2 . PHE E 228 ? 1.1808 0.8117 0.2300 -0.0953 -0.3292 -0.1073 228 PHE E CD2 
9548  C CE1 . PHE E 228 ? 1.2671 0.8576 0.2372 -0.1195 -0.3352 -0.1479 228 PHE E CE1 
9549  C CE2 . PHE E 228 ? 1.2063 0.8648 0.2333 -0.1121 -0.3432 -0.1132 228 PHE E CE2 
9550  C CZ  . PHE E 228 ? 1.2495 0.8896 0.2377 -0.1250 -0.3467 -0.1352 228 PHE E CZ  
9551  N N   . PHE E 229 ? 1.1693 0.6871 0.2418 -0.0304 -0.2703 -0.1286 229 PHE E N   
9552  C CA  . PHE E 229 ? 1.1548 0.6554 0.2505 -0.0146 -0.2578 -0.1369 229 PHE E CA  
9553  C C   . PHE E 229 ? 1.1754 0.6395 0.2471 -0.0169 -0.2619 -0.1534 229 PHE E C   
9554  O O   . PHE E 229 ? 1.2081 0.6524 0.2414 -0.0310 -0.2691 -0.1596 229 PHE E O   
9555  C CB  . PHE E 229 ? 1.1656 0.6628 0.2615 -0.0007 -0.2402 -0.1349 229 PHE E CB  
9556  C CG  . PHE E 229 ? 1.1479 0.6762 0.2717 0.0070  -0.2288 -0.1164 229 PHE E CG  
9557  C CD1 . PHE E 229 ? 1.1641 0.7135 0.2649 0.0024  -0.2338 -0.1013 229 PHE E CD1 
9558  C CD2 . PHE E 229 ? 1.1182 0.6562 0.2922 0.0200  -0.2113 -0.1148 229 PHE E CD2 
9559  C CE1 . PHE E 229 ? 1.1527 0.7290 0.2770 0.0138  -0.2199 -0.0806 229 PHE E CE1 
9560  C CE2 . PHE E 229 ? 1.1070 0.6680 0.3080 0.0279  -0.1953 -0.0966 229 PHE E CE2 
9561  C CZ  . PHE E 229 ? 1.1251 0.7037 0.2996 0.0264  -0.1988 -0.0772 229 PHE E CZ  
9562  N N   . TRP E 230 ? 1.1586 0.6156 0.2542 -0.0021 -0.2556 -0.1614 230 TRP E N   
9563  C CA  . TRP E 230 ? 1.1785 0.6031 0.2534 0.0019  -0.2570 -0.1737 230 TRP E CA  
9564  C C   . TRP E 230 ? 1.1715 0.5913 0.2652 0.0234  -0.2459 -0.1841 230 TRP E C   
9565  O O   . TRP E 230 ? 1.1430 0.5884 0.2765 0.0333  -0.2380 -0.1842 230 TRP E O   
9566  C CB  . TRP E 230 ? 1.1653 0.5940 0.2480 -0.0022 -0.2674 -0.1715 230 TRP E CB  
9567  C CG  . TRP E 230 ? 1.1213 0.5837 0.2518 0.0089  -0.2683 -0.1690 230 TRP E CG  
9568  C CD1 . TRP E 230 ? 1.0909 0.5864 0.2513 0.0024  -0.2718 -0.1582 230 TRP E CD1 
9569  C CD2 . TRP E 230 ? 1.1055 0.5744 0.2596 0.0292  -0.2654 -0.1795 230 TRP E CD2 
9570  N NE1 . TRP E 230 ? 1.0575 0.5764 0.2593 0.0152  -0.2700 -0.1628 230 TRP E NE1 
9571  C CE2 . TRP E 230 ? 1.0655 0.5719 0.2645 0.0318  -0.2674 -0.1771 230 TRP E CE2 
9572  C CE3 . TRP E 230 ? 1.1232 0.5729 0.2650 0.0468  -0.2610 -0.1912 230 TRP E CE3 
9573  C CZ2 . TRP E 230 ? 1.0428 0.5712 0.2752 0.0497  -0.2666 -0.1895 230 TRP E CZ2 
9574  C CZ3 . TRP E 230 ? 1.1001 0.5747 0.2744 0.0671  -0.2612 -0.2013 230 TRP E CZ3 
9575  C CH2 . TRP E 230 ? 1.0602 0.5752 0.2795 0.0676  -0.2647 -0.2021 230 TRP E CH2 
9576  N N   . THR E 231 ? 1.2004 0.5874 0.2667 0.0307  -0.2435 -0.1934 231 THR E N   
9577  C CA  . THR E 231 ? 1.1964 0.5823 0.2792 0.0535  -0.2351 -0.2043 231 THR E CA  
9578  C C   . THR E 231 ? 1.2244 0.5800 0.2787 0.0632  -0.2361 -0.2089 231 THR E C   
9579  O O   . THR E 231 ? 1.2543 0.5799 0.2723 0.0497  -0.2386 -0.2051 231 THR E O   
9580  C CB  . THR E 231 ? 1.2136 0.5872 0.2895 0.0593  -0.2214 -0.2091 231 THR E CB  
9581  O OG1 . THR E 231 ? 1.1998 0.5858 0.3062 0.0812  -0.2133 -0.2205 231 THR E OG1 
9582  C CG2 . THR E 231 ? 1.2643 0.5922 0.2849 0.0523  -0.2179 -0.2116 231 THR E CG2 
9583  N N   . ILE E 232 ? 1.2169 0.5828 0.2897 0.0875  -0.2327 -0.2174 232 ILE E N   
9584  C CA  . ILE E 232 ? 1.2507 0.5865 0.2935 0.1044  -0.2288 -0.2199 232 ILE E CA  
9585  C C   . ILE E 232 ? 1.2782 0.5915 0.3059 0.1160  -0.2157 -0.2277 232 ILE E C   
9586  O O   . ILE E 232 ? 1.2574 0.5981 0.3183 0.1298  -0.2115 -0.2365 232 ILE E O   
9587  C CB  . ILE E 232 ? 1.2290 0.5956 0.2969 0.1286  -0.2349 -0.2234 232 ILE E CB  
9588  C CG1 . ILE E 232 ? 1.2302 0.5914 0.2858 0.1208  -0.2430 -0.2125 232 ILE E CG1 
9589  C CG2 . ILE E 232 ? 1.2587 0.6092 0.3080 0.1580  -0.2267 -0.2286 232 ILE E CG2 
9590  C CD1 . ILE E 232 ? 1.2061 0.5814 0.2752 0.0925  -0.2513 -0.2050 232 ILE E CD1 
9591  N N   . LEU E 233 ? 1.3270 0.5903 0.3069 0.1090  -0.2075 -0.2257 233 LEU E N   
9592  C CA  . LEU E 233 ? 1.3601 0.5950 0.3192 0.1193  -0.1934 -0.2321 233 LEU E CA  
9593  C C   . LEU E 233 ? 1.3853 0.6034 0.3312 0.1483  -0.1858 -0.2334 233 LEU E C   
9594  O O   . LEU E 233 ? 1.4178 0.6016 0.3318 0.1489  -0.1818 -0.2271 233 LEU E O   
9595  C CB  . LEU E 233 ? 1.4032 0.5932 0.3168 0.0955  -0.1871 -0.2318 233 LEU E CB  
9596  C CG  . LEU E 233 ? 1.4401 0.5977 0.3279 0.1014  -0.1716 -0.2387 233 LEU E CG  
9597  C CD1 . LEU E 233 ? 1.4117 0.6012 0.3310 0.1071  -0.1692 -0.2416 233 LEU E CD1 
9598  C CD2 . LEU E 233 ? 1.4860 0.6017 0.3273 0.0759  -0.1670 -0.2418 233 LEU E CD2 
9599  N N   . LYS E 234 ? 1.3729 0.6166 0.3448 0.1736  -0.1820 -0.2413 234 LYS E N   
9600  C CA  . LYS E 234 ? 1.3953 0.6347 0.3582 0.2072  -0.1758 -0.2421 234 LYS E CA  
9601  C C   . LYS E 234 ? 1.4558 0.6344 0.3698 0.2122  -0.1571 -0.2395 234 LYS E C   
9602  O O   . LYS E 234 ? 1.4736 0.6241 0.3699 0.1923  -0.1498 -0.2423 234 LYS E O   
9603  C CB  . LYS E 234 ? 1.3604 0.6560 0.3724 0.2317  -0.1790 -0.2550 234 LYS E CB  
9604  C CG  . LYS E 234 ? 1.3057 0.6608 0.3683 0.2273  -0.1949 -0.2609 234 LYS E CG  
9605  C CD  . LYS E 234 ? 1.2767 0.6914 0.3890 0.2538  -0.1980 -0.2783 234 LYS E CD  
9606  C CE  . LYS E 234 ? 1.2295 0.7003 0.3877 0.2507  -0.2129 -0.2860 234 LYS E CE  
9607  N NZ  . LYS E 234 ? 1.2044 0.7395 0.4121 0.2769  -0.2173 -0.3080 234 LYS E NZ  
9608  N N   . PRO E 235 ? 1.4919 0.6492 0.3821 0.2404  -0.1475 -0.2338 235 PRO E N   
9609  C CA  . PRO E 235 ? 1.5541 0.6477 0.3972 0.2453  -0.1256 -0.2306 235 PRO E CA  
9610  C C   . PRO E 235 ? 1.5601 0.6541 0.4094 0.2530  -0.1165 -0.2401 235 PRO E C   
9611  O O   . PRO E 235 ? 1.5236 0.6696 0.4146 0.2705  -0.1234 -0.2480 235 PRO E O   
9612  C CB  . PRO E 235 ? 1.5845 0.6675 0.4098 0.2830  -0.1161 -0.2204 235 PRO E CB  
9613  C CG  . PRO E 235 ? 1.5421 0.6791 0.3981 0.2930  -0.1349 -0.2178 235 PRO E CG  
9614  C CD  . PRO E 235 ? 1.4800 0.6722 0.3848 0.2723  -0.1543 -0.2300 235 PRO E CD  
9615  N N   . ASN E 236 ? 1.6080 0.6449 0.4178 0.2388  -0.1000 -0.2410 236 ASN E N   
9616  C CA  . ASN E 236 ? 1.6230 0.6505 0.4310 0.2464  -0.0878 -0.2485 236 ASN E CA  
9617  C C   . ASN E 236 ? 1.5794 0.6451 0.4218 0.2279  -0.0979 -0.2567 236 ASN E C   
9618  O O   . ASN E 236 ? 1.5809 0.6523 0.4346 0.2375  -0.0887 -0.2629 236 ASN E O   
9619  C CB  . ASN E 236 ? 1.6278 0.6763 0.4505 0.2900  -0.0805 -0.2482 236 ASN E CB  
9620  C CG  . ASN E 236 ? 1.6859 0.6821 0.4720 0.3049  -0.0557 -0.2475 236 ASN E CG  
9621  O OD1 . ASN E 236 ? 1.7233 0.6691 0.4757 0.2815  -0.0437 -0.2502 236 ASN E OD1 
9622  N ND2 . ASN E 236 ? 1.6981 0.7086 0.4904 0.3455  -0.0477 -0.2447 236 ASN E ND2 
9623  N N   . ASP E 237 ? 1.5445 0.6347 0.4033 0.2028  -0.1141 -0.2552 237 ASP E N   
9624  C CA  . ASP E 237 ? 1.5077 0.6304 0.3963 0.1858  -0.1206 -0.2591 237 ASP E CA  
9625  C C   . ASP E 237 ? 1.5284 0.6222 0.3823 0.1528  -0.1224 -0.2569 237 ASP E C   
9626  O O   . ASP E 237 ? 1.5478 0.6178 0.3748 0.1377  -0.1268 -0.2537 237 ASP E O   
9627  C CB  . ASP E 237 ? 1.4479 0.6319 0.3905 0.1874  -0.1371 -0.2594 237 ASP E CB  
9628  C CG  . ASP E 237 ? 1.4124 0.6297 0.3923 0.1753  -0.1376 -0.2624 237 ASP E CG  
9629  O OD1 . ASP E 237 ? 1.4279 0.6319 0.4031 0.1768  -0.1238 -0.2655 237 ASP E OD1 
9630  O OD2 . ASP E 237 ? 1.3709 0.6261 0.3850 0.1657  -0.1495 -0.2605 237 ASP E OD2 
9631  N N   . ALA E 238 ? 1.5263 0.6249 0.3818 0.1429  -0.1181 -0.2593 238 ALA E N   
9632  C CA  . ALA E 238 ? 1.5483 0.6285 0.3701 0.1153  -0.1206 -0.2589 238 ALA E CA  
9633  C C   . ALA E 238 ? 1.5037 0.6301 0.3569 0.1022  -0.1335 -0.2525 238 ALA E C   
9634  O O   . ALA E 238 ? 1.4658 0.6285 0.3637 0.1140  -0.1316 -0.2506 238 ALA E O   
9635  C CB  . ALA E 238 ? 1.5894 0.6377 0.3794 0.1166  -0.1040 -0.2647 238 ALA E CB  
9636  N N   . ILE E 239 ? 1.5102 0.6356 0.3421 0.0779  -0.1449 -0.2501 239 ILE E N   
9637  C CA  . ILE E 239 ? 1.4783 0.6435 0.3305 0.0658  -0.1550 -0.2420 239 ILE E CA  
9638  C C   . ILE E 239 ? 1.5131 0.6671 0.3276 0.0546  -0.1501 -0.2434 239 ILE E C   
9639  O O   . ILE E 239 ? 1.5597 0.6794 0.3284 0.0423  -0.1485 -0.2531 239 ILE E O   
9640  C CB  . ILE E 239 ? 1.4569 0.6409 0.3172 0.0491  -0.1729 -0.2369 239 ILE E CB  
9641  C CG1 . ILE E 239 ? 1.4210 0.6500 0.3085 0.0419  -0.1811 -0.2260 239 ILE E CG1 
9642  C CG2 . ILE E 239 ? 1.5007 0.6517 0.3146 0.0273  -0.1769 -0.2442 239 ILE E CG2 
9643  C CD1 . ILE E 239 ? 1.3874 0.6433 0.2986 0.0319  -0.1969 -0.2194 239 ILE E CD1 
9644  N N   . ASN E 240 ? 1.4937 0.6768 0.3277 0.0602  -0.1457 -0.2346 240 ASN E N   
9645  C CA  . ASN E 240 ? 1.5276 0.7060 0.3256 0.0560  -0.1397 -0.2335 240 ASN E CA  
9646  C C   . ASN E 240 ? 1.5089 0.7281 0.3140 0.0476  -0.1497 -0.2205 240 ASN E C   
9647  O O   . ASN E 240 ? 1.4670 0.7178 0.3173 0.0561  -0.1474 -0.2080 240 ASN E O   
9648  C CB  . ASN E 240 ? 1.5347 0.7049 0.3421 0.0767  -0.1178 -0.2317 240 ASN E CB  
9649  C CG  . ASN E 240 ? 1.5506 0.6863 0.3560 0.0892  -0.1066 -0.2428 240 ASN E CG  
9650  O OD1 . ASN E 240 ? 1.5943 0.6914 0.3559 0.0830  -0.1050 -0.2534 240 ASN E OD1 
9651  N ND2 . ASN E 240 ? 1.5178 0.6690 0.3721 0.1075  -0.0973 -0.2417 240 ASN E ND2 
9652  N N   . PHE E 241 ? 1.5424 0.7624 0.3037 0.0316  -0.1596 -0.2248 241 PHE E N   
9653  C CA  . PHE E 241 ? 1.5335 0.7956 0.2933 0.0260  -0.1698 -0.2125 241 PHE E CA  
9654  C C   . PHE E 241 ? 1.5717 0.8376 0.2946 0.0354  -0.1597 -0.2090 241 PHE E C   
9655  O O   . PHE E 241 ? 1.6182 0.8549 0.2974 0.0320  -0.1555 -0.2242 241 PHE E O   
9656  C CB  . PHE E 241 ? 1.5430 0.8151 0.2831 0.0008  -0.1916 -0.2218 241 PHE E CB  
9657  C CG  . PHE E 241 ? 1.5041 0.7803 0.2803 -0.0070 -0.2017 -0.2201 241 PHE E CG  
9658  C CD1 . PHE E 241 ? 1.4598 0.7770 0.2741 -0.0058 -0.2100 -0.2037 241 PHE E CD1 
9659  C CD2 . PHE E 241 ? 1.5153 0.7535 0.2859 -0.0134 -0.2008 -0.2335 241 PHE E CD2 
9660  C CE1 . PHE E 241 ? 1.4262 0.7479 0.2719 -0.0120 -0.2190 -0.2024 241 PHE E CE1 
9661  C CE2 . PHE E 241 ? 1.4837 0.7264 0.2842 -0.0173 -0.2089 -0.2303 241 PHE E CE2 
9662  C CZ  . PHE E 241 ? 1.4382 0.7235 0.2761 -0.0171 -0.2189 -0.2155 241 PHE E CZ  
9663  N N   . GLU E 242 ? 1.5551 0.8558 0.2949 0.0490  -0.1537 -0.1884 242 GLU E N   
9664  C CA  . GLU E 242 ? 1.5937 0.9073 0.2946 0.0605  -0.1459 -0.1807 242 GLU E CA  
9665  C C   . GLU E 242 ? 1.5787 0.9436 0.2874 0.0634  -0.1549 -0.1607 242 GLU E C   
9666  O O   . GLU E 242 ? 1.5365 0.9197 0.2936 0.0719  -0.1481 -0.1426 242 GLU E O   
9667  C CB  . GLU E 242 ? 1.6012 0.8952 0.3122 0.0853  -0.1163 -0.1709 242 GLU E CB  
9668  C CG  . GLU E 242 ? 1.6504 0.9504 0.3134 0.1006  -0.1049 -0.1633 242 GLU E CG  
9669  C CD  . GLU E 242 ? 1.6574 0.9368 0.3354 0.1259  -0.0718 -0.1514 242 GLU E CD  
9670  O OE1 . GLU E 242 ? 1.6620 0.9038 0.3460 0.1270  -0.0608 -0.1648 242 GLU E OE1 
9671  O OE2 . GLU E 242 ? 1.6610 0.9614 0.3452 0.1460  -0.0545 -0.1278 242 GLU E OE2 
9672  N N   . SER E 243 ? 1.6149 1.0053 0.2769 0.0570  -0.1697 -0.1653 243 SER E N   
9673  C CA  . SER E 243 ? 1.6059 1.0505 0.2704 0.0621  -0.1798 -0.1462 243 SER E CA  
9674  C C   . SER E 243 ? 1.6592 1.1348 0.2651 0.0686  -0.1872 -0.1483 243 SER E C   
9675  O O   . SER E 243 ? 1.6991 1.1640 0.2620 0.0530  -0.1989 -0.1753 243 SER E O   
9676  C CB  . SER E 243 ? 1.5731 1.0384 0.2613 0.0378  -0.2044 -0.1528 243 SER E CB  
9677  O OG  . SER E 243 ? 1.5614 1.0805 0.2569 0.0445  -0.2130 -0.1325 243 SER E OG  
9678  N N   . ASN E 244 ? 1.6619 1.1773 0.2670 0.0930  -0.1789 -0.1200 244 ASN E N   
9679  C CA  . ASN E 244 ? 1.7107 1.2702 0.2616 0.1053  -0.1876 -0.1174 244 ASN E CA  
9680  C C   . ASN E 244 ? 1.6964 1.3193 0.2543 0.1017  -0.2098 -0.1068 244 ASN E C   
9681  O O   . ASN E 244 ? 1.7303 1.4025 0.2519 0.1203  -0.2147 -0.0957 244 ASN E O   
9682  C CB  . ASN E 244 ? 1.7377 1.2952 0.2726 0.1438  -0.1566 -0.0896 244 ASN E CB  
9683  C CG  . ASN E 244 ? 1.7006 1.2702 0.2856 0.1660  -0.1345 -0.0521 244 ASN E CG  
9684  O OD1 . ASN E 244 ? 1.6485 1.2059 0.2893 0.1527  -0.1345 -0.0503 244 ASN E OD1 
9685  N ND2 . ASN E 244 ? 1.7306 1.3236 0.2952 0.2010  -0.1137 -0.0222 244 ASN E ND2 
9686  N N   . GLY E 245 ? 1.6483 1.2722 0.2516 0.0801  -0.2227 -0.1096 245 GLY E N   
9687  C CA  . GLY E 245 ? 1.6314 1.3136 0.2462 0.0741  -0.2441 -0.1010 245 GLY E CA  
9688  C C   . GLY E 245 ? 1.5729 1.2484 0.2457 0.0570  -0.2498 -0.0963 245 GLY E C   
9689  O O   . GLY E 245 ? 1.5391 1.1744 0.2517 0.0603  -0.2316 -0.0885 245 GLY E O   
9690  N N   . ASN E 246 ? 1.5634 1.2820 0.2406 0.0389  -0.2755 -0.1031 246 ASN E N   
9691  C CA  . ASN E 246 ? 1.5113 1.2377 0.2401 0.0264  -0.2824 -0.0938 246 ASN E CA  
9692  C C   . ASN E 246 ? 1.4815 1.1547 0.2397 0.0021  -0.2831 -0.1132 246 ASN E C   
9693  O O   . ASN E 246 ? 1.4364 1.1033 0.2409 0.0003  -0.2794 -0.1012 246 ASN E O   
9694  C CB  . ASN E 246 ? 1.4827 1.2231 0.2469 0.0555  -0.2606 -0.0546 246 ASN E CB  
9695  C CG  . ASN E 246 ? 1.5143 1.3095 0.2494 0.0843  -0.2575 -0.0301 246 ASN E CG  
9696  O OD1 . ASN E 246 ? 1.5556 1.3479 0.2515 0.1049  -0.2451 -0.0265 246 ASN E OD1 
9697  N ND2 . ASN E 246 ? 1.4973 1.3435 0.2499 0.0885  -0.2675 -0.0117 246 ASN E ND2 
9698  N N   . PHE E 247 ? 1.5106 1.1477 0.2400 -0.0153 -0.2874 -0.1431 247 PHE E N   
9699  C CA  . PHE E 247 ? 1.4925 1.0738 0.2418 -0.0313 -0.2831 -0.1594 247 PHE E CA  
9700  C C   . PHE E 247 ? 1.4925 1.0730 0.2439 -0.0637 -0.3029 -0.1825 247 PHE E C   
9701  O O   . PHE E 247 ? 1.5294 1.1277 0.2487 -0.0812 -0.3170 -0.2043 247 PHE E O   
9702  C CB  . PHE E 247 ? 1.5279 1.0617 0.2457 -0.0262 -0.2687 -0.1748 247 PHE E CB  
9703  C CG  . PHE E 247 ? 1.5179 0.9952 0.2496 -0.0381 -0.2627 -0.1910 247 PHE E CG  
9704  C CD1 . PHE E 247 ? 1.4713 0.9330 0.2501 -0.0309 -0.2543 -0.1785 247 PHE E CD1 
9705  C CD2 . PHE E 247 ? 1.5595 1.0001 0.2560 -0.0541 -0.2635 -0.2189 247 PHE E CD2 
9706  C CE1 . PHE E 247 ? 1.4658 0.8812 0.2542 -0.0368 -0.2490 -0.1919 247 PHE E CE1 
9707  C CE2 . PHE E 247 ? 1.5552 0.9436 0.2620 -0.0603 -0.2550 -0.2304 247 PHE E CE2 
9708  C CZ  . PHE E 247 ? 1.5084 0.8862 0.2600 -0.0501 -0.2486 -0.2159 247 PHE E CZ  
9709  N N   . ILE E 248 ? 1.4535 1.0141 0.2440 -0.0712 -0.3023 -0.1787 248 ILE E N   
9710  C CA  . ILE E 248 ? 1.4546 1.0028 0.2503 -0.0996 -0.3147 -0.1983 248 ILE E CA  
9711  C C   . ILE E 248 ? 1.4656 0.9485 0.2560 -0.1033 -0.3018 -0.2137 248 ILE E C   
9712  O O   . ILE E 248 ? 1.4333 0.8922 0.2528 -0.0913 -0.2918 -0.2029 248 ILE E O   
9713  C CB  . ILE E 248 ? 1.4075 0.9799 0.2473 -0.1034 -0.3224 -0.1821 248 ILE E CB  
9714  C CG1 . ILE E 248 ? 1.3909 1.0249 0.2420 -0.0899 -0.3288 -0.1584 248 ILE E CG1 
9715  C CG2 . ILE E 248 ? 1.4169 0.9845 0.2582 -0.1335 -0.3349 -0.2019 248 ILE E CG2 
9716  C CD1 . ILE E 248 ? 1.4229 1.1072 0.2468 -0.1027 -0.3472 -0.1695 248 ILE E CD1 
9717  N N   . ALA E 249 ? 1.5142 0.9709 0.2672 -0.1186 -0.3011 -0.2399 249 ALA E N   
9718  C CA  . ALA E 249 ? 1.5347 0.9278 0.2754 -0.1183 -0.2855 -0.2534 249 ALA E CA  
9719  C C   . ALA E 249 ? 1.5261 0.8874 0.2855 -0.1334 -0.2844 -0.2602 249 ALA E C   
9720  O O   . ALA E 249 ? 1.5240 0.9060 0.2929 -0.1544 -0.2962 -0.2662 249 ALA E O   
9721  C CB  . ALA E 249 ? 1.5943 0.9681 0.2874 -0.1290 -0.2819 -0.2793 249 ALA E CB  
9722  N N   . PRO E 250 ? 1.5228 0.8359 0.2881 -0.1205 -0.2693 -0.2585 250 PRO E N   
9723  C CA  . PRO E 250 ? 1.5265 0.8029 0.3010 -0.1302 -0.2640 -0.2644 250 PRO E CA  
9724  C C   . PRO E 250 ? 1.5865 0.8201 0.3270 -0.1524 -0.2551 -0.2912 250 PRO E C   
9725  O O   . PRO E 250 ? 1.6224 0.8219 0.3342 -0.1467 -0.2423 -0.3024 250 PRO E O   
9726  C CB  . PRO E 250 ? 1.5059 0.7534 0.2950 -0.1028 -0.2505 -0.2528 250 PRO E CB  
9727  C CG  . PRO E 250 ? 1.5133 0.7622 0.2886 -0.0861 -0.2435 -0.2514 250 PRO E CG  
9728  C CD  . PRO E 250 ? 1.5108 0.8085 0.2802 -0.0929 -0.2559 -0.2478 250 PRO E CD  
9729  N N   . GLU E 251 ? 1.5995 0.8342 0.3453 -0.1781 -0.2595 -0.3024 251 GLU E N   
9730  C CA  . GLU E 251 ? 1.6569 0.8421 0.3791 -0.2004 -0.2448 -0.3284 251 GLU E CA  
9731  C C   . GLU E 251 ? 1.6600 0.7887 0.3893 -0.1871 -0.2251 -0.3193 251 GLU E C   
9732  O O   . GLU E 251 ? 1.6995 0.7738 0.4048 -0.1803 -0.2048 -0.3281 251 GLU E O   
9733  C CB  . GLU E 251 ? 1.6724 0.8845 0.4019 -0.2351 -0.2551 -0.3466 251 GLU E CB  
9734  C CG  . GLU E 251 ? 1.7272 0.9440 0.4265 -0.2609 -0.2560 -0.3808 251 GLU E CG  
9735  C CD  . GLU E 251 ? 1.7838 0.9443 0.4737 -0.2881 -0.2347 -0.4089 251 GLU E CD  
9736  O OE1 . GLU E 251 ? 1.7818 0.9430 0.4961 -0.3075 -0.2332 -0.4122 251 GLU E OE1 
9737  O OE2 . GLU E 251 ? 1.8332 0.9471 0.4923 -0.2902 -0.2169 -0.4277 251 GLU E OE2 
9738  N N   . TYR E 252 ? 1.6201 0.7639 0.3810 -0.1810 -0.2308 -0.3009 252 TYR E N   
9739  C CA  . TYR E 252 ? 1.6207 0.7211 0.3891 -0.1643 -0.2143 -0.2892 252 TYR E CA  
9740  C C   . TYR E 252 ? 1.5654 0.6898 0.3592 -0.1313 -0.2213 -0.2642 252 TYR E C   
9741  O O   . TYR E 252 ? 1.5185 0.6960 0.3361 -0.1280 -0.2393 -0.2530 252 TYR E O   
9742  C CB  . TYR E 252 ? 1.6287 0.7218 0.4120 -0.1849 -0.2111 -0.2909 252 TYR E CB  
9743  C CG  . TYR E 252 ? 1.6862 0.7533 0.4521 -0.2202 -0.2001 -0.3194 252 TYR E CG  
9744  C CD1 . TYR E 252 ? 1.7443 0.7410 0.4883 -0.2231 -0.1705 -0.3313 252 TYR E CD1 
9745  C CD2 . TYR E 252 ? 1.6854 0.8004 0.4584 -0.2501 -0.2179 -0.3357 252 TYR E CD2 
9746  C CE1 . TYR E 252 ? 1.8006 0.7719 0.5328 -0.2582 -0.1572 -0.3614 252 TYR E CE1 
9747  C CE2 . TYR E 252 ? 1.7393 0.8366 0.5008 -0.2847 -0.2082 -0.3674 252 TYR E CE2 
9748  C CZ  . TYR E 252 ? 1.7970 0.8207 0.5394 -0.2903 -0.1770 -0.3815 252 TYR E CZ  
9749  O OH  . TYR E 252 ? 1.8533 0.8578 0.5883 -0.3273 -0.1642 -0.4166 252 TYR E OH  
9750  N N   . ALA E 253 ? 1.5743 0.6604 0.3636 -0.1064 -0.2054 -0.2569 253 ALA E N   
9751  C CA  . ALA E 253 ? 1.5279 0.6361 0.3429 -0.0751 -0.2103 -0.2383 253 ALA E CA  
9752  C C   . ALA E 253 ? 1.5414 0.6165 0.3565 -0.0599 -0.1967 -0.2297 253 ALA E C   
9753  O O   . ALA E 253 ? 1.5932 0.6136 0.3812 -0.0577 -0.1753 -0.2356 253 ALA E O   
9754  C CB  . ALA E 253 ? 1.5253 0.6305 0.3341 -0.0518 -0.2054 -0.2389 253 ALA E CB  
9755  N N   . TYR E 254 ? 1.4987 0.6060 0.3428 -0.0480 -0.2070 -0.2151 254 TYR E N   
9756  C CA  . TYR E 254 ? 1.5104 0.5934 0.3539 -0.0305 -0.1953 -0.2045 254 TYR E CA  
9757  C C   . TYR E 254 ? 1.5173 0.5851 0.3530 0.0082  -0.1846 -0.1992 254 TYR E C   
9758  O O   . TYR E 254 ? 1.4819 0.5845 0.3354 0.0259  -0.1948 -0.1989 254 TYR E O   
9759  C CB  . TYR E 254 ? 1.4632 0.5897 0.3392 -0.0295 -0.2107 -0.1918 254 TYR E CB  
9760  C CG  . TYR E 254 ? 1.4631 0.6003 0.3469 -0.0643 -0.2177 -0.1945 254 TYR E CG  
9761  C CD1 . TYR E 254 ? 1.4992 0.6004 0.3736 -0.0765 -0.2028 -0.1936 254 TYR E CD1 
9762  C CD2 . TYR E 254 ? 1.4292 0.6141 0.3314 -0.0836 -0.2371 -0.1972 254 TYR E CD2 
9763  C CE1 . TYR E 254 ? 1.4988 0.6144 0.3852 -0.1094 -0.2090 -0.1983 254 TYR E CE1 
9764  C CE2 . TYR E 254 ? 1.4293 0.6312 0.3402 -0.1136 -0.2447 -0.2001 254 TYR E CE2 
9765  C CZ  . TYR E 254 ? 1.4628 0.6316 0.3675 -0.1278 -0.2315 -0.2021 254 TYR E CZ  
9766  O OH  . TYR E 254 ? 1.4626 0.6526 0.3807 -0.1588 -0.2388 -0.2073 254 TYR E OH  
9767  N N   . LYS E 255 ? 1.5656 0.5824 0.3764 0.0221  -0.1621 -0.1951 255 LYS E N   
9768  C CA  . LYS E 255 ? 1.5824 0.5822 0.3807 0.0620  -0.1491 -0.1890 255 LYS E CA  
9769  C C   . LYS E 255 ? 1.5674 0.5839 0.3769 0.0911  -0.1500 -0.1730 255 LYS E C   
9770  O O   . LYS E 255 ? 1.5854 0.5816 0.3897 0.0828  -0.1415 -0.1649 255 LYS E O   
9771  C CB  . LYS E 255 ? 1.6548 0.5831 0.4135 0.0617  -0.1192 -0.1934 255 LYS E CB  
9772  C CG  . LYS E 255 ? 1.6744 0.5870 0.4171 0.0932  -0.1078 -0.1940 255 LYS E CG  
9773  C CD  . LYS E 255 ? 1.7409 0.5870 0.4473 0.0802  -0.0814 -0.2045 255 LYS E CD  
9774  C CE  . LYS E 255 ? 1.8046 0.5865 0.4841 0.0923  -0.0484 -0.1946 255 LYS E CE  
9775  N NZ  . LYS E 255 ? 1.8708 0.5877 0.5161 0.0907  -0.0188 -0.2038 255 LYS E NZ  
9776  N N   . ILE E 256 ? 1.5366 0.5919 0.3620 0.1253  -0.1593 -0.1699 256 ILE E N   
9777  C CA  . ILE E 256 ? 1.5160 0.6021 0.3552 0.1546  -0.1652 -0.1580 256 ILE E CA  
9778  C C   . ILE E 256 ? 1.5672 0.6172 0.3751 0.1951  -0.1424 -0.1467 256 ILE E C   
9779  O O   . ILE E 256 ? 1.5648 0.6345 0.3734 0.2291  -0.1430 -0.1484 256 ILE E O   
9780  C CB  . ILE E 256 ? 1.4532 0.6114 0.3328 0.1695  -0.1890 -0.1646 256 ILE E CB  
9781  C CG1 . ILE E 256 ? 1.4156 0.5993 0.3196 0.1378  -0.2034 -0.1766 256 ILE E CG1 
9782  C CG2 . ILE E 256 ? 1.4232 0.6196 0.3233 0.1808  -0.2006 -0.1565 256 ILE E CG2 
9783  C CD1 . ILE E 256 ? 1.3546 0.6053 0.3046 0.1453  -0.2226 -0.1830 256 ILE E CD1 
9784  N N   . VAL E 257 ? 1.6159 0.6137 0.3974 0.1924  -0.1202 -0.1348 257 VAL E N   
9785  C CA  . VAL E 257 ? 1.6759 0.6291 0.4226 0.2316  -0.0918 -0.1204 257 VAL E CA  
9786  C C   . VAL E 257 ? 1.6630 0.6566 0.4138 0.2784  -0.0978 -0.1062 257 VAL E C   
9787  O O   . VAL E 257 ? 1.6842 0.6831 0.4199 0.3227  -0.0898 -0.1003 257 VAL E O   
9788  C CB  . VAL E 257 ? 1.7430 0.6171 0.4596 0.2130  -0.0583 -0.1131 257 VAL E CB  
9789  C CG1 . VAL E 257 ? 1.7654 0.6009 0.4732 0.1735  -0.0503 -0.1313 257 VAL E CG1 
9790  C CG2 . VAL E 257 ? 1.7325 0.6094 0.4621 0.1912  -0.0607 -0.1060 257 VAL E CG2 
9791  N N   . LYS E 258 ? 1.6293 0.6552 0.4003 0.2698  -0.1123 -0.1015 258 LYS E N   
9792  C CA  . LYS E 258 ? 1.6177 0.6856 0.3919 0.3125  -0.1193 -0.0898 258 LYS E CA  
9793  C C   . LYS E 258 ? 1.5423 0.6904 0.3611 0.3057  -0.1542 -0.1027 258 LYS E C   
9794  O O   . LYS E 258 ? 1.5058 0.6659 0.3493 0.2655  -0.1677 -0.1090 258 LYS E O   
9795  C CB  . LYS E 258 ? 1.6587 0.6861 0.4110 0.3181  -0.0976 -0.0687 258 LYS E CB  
9796  C CG  . LYS E 258 ? 1.7296 0.7134 0.4388 0.3676  -0.0651 -0.0476 258 LYS E CG  
9797  C CD  . LYS E 258 ? 1.7404 0.7412 0.4399 0.4030  -0.0609 -0.0275 258 LYS E CD  
9798  C CE  . LYS E 258 ? 1.7534 0.7154 0.4544 0.3699  -0.0473 -0.0177 258 LYS E CE  
9799  N NZ  . LYS E 258 ? 1.7950 0.7441 0.4699 0.4131  -0.0264 0.0088  258 LYS E NZ  
9800  N N   . LYS E 259 ? 1.5224 0.7264 0.3522 0.3461  -0.1670 -0.1075 259 LYS E N   
9801  C CA  . LYS E 259 ? 1.4578 0.7394 0.3308 0.3461  -0.1961 -0.1213 259 LYS E CA  
9802  C C   . LYS E 259 ? 1.4665 0.7784 0.3303 0.3873  -0.1975 -0.1104 259 LYS E C   
9803  O O   . LYS E 259 ? 1.4976 0.8205 0.3397 0.4351  -0.1904 -0.1054 259 LYS E O   
9804  C CB  . LYS E 259 ? 1.4244 0.7570 0.3262 0.3568  -0.2112 -0.1431 259 LYS E CB  
9805  C CG  . LYS E 259 ? 1.4155 0.7236 0.3261 0.3211  -0.2098 -0.1538 259 LYS E CG  
9806  C CD  . LYS E 259 ? 1.3819 0.7424 0.3258 0.3326  -0.2224 -0.1751 259 LYS E CD  
9807  C CE  . LYS E 259 ? 1.3794 0.7115 0.3270 0.3005  -0.2179 -0.1832 259 LYS E CE  
9808  N NZ  . LYS E 259 ? 1.3536 0.7294 0.3326 0.3129  -0.2249 -0.2026 259 LYS E NZ  
9809  N N   . GLY E 260 ? 1.4411 0.7689 0.3202 0.3710  -0.2065 -0.1063 260 GLY E N   
9810  C CA  . GLY E 260 ? 1.4484 0.8073 0.3186 0.4085  -0.2087 -0.0965 260 GLY E CA  
9811  C C   . GLY E 260 ? 1.3915 0.8031 0.3013 0.3889  -0.2311 -0.1067 260 GLY E C   
9812  O O   . GLY E 260 ? 1.3447 0.7726 0.2914 0.3489  -0.2451 -0.1212 260 GLY E O   
9813  N N   . ASP E 261 ? 1.3988 0.8364 0.2995 0.4195  -0.2328 -0.0981 261 ASP E N   
9814  C CA  . ASP E 261 ? 1.3521 0.8340 0.2863 0.4030  -0.2505 -0.1055 261 ASP E CA  
9815  C C   . ASP E 261 ? 1.3524 0.7842 0.2864 0.3591  -0.2410 -0.0900 261 ASP E C   
9816  O O   . ASP E 261 ? 1.4007 0.7771 0.2997 0.3641  -0.2185 -0.0669 261 ASP E O   
9817  C CB  . ASP E 261 ? 1.3663 0.8890 0.2857 0.4506  -0.2536 -0.1004 261 ASP E CB  
9818  C CG  . ASP E 261 ? 1.3513 0.9485 0.2856 0.4893  -0.2711 -0.1247 261 ASP E CG  
9819  O OD1 . ASP E 261 ? 1.3161 0.9408 0.2852 0.4719  -0.2834 -0.1486 261 ASP E OD1 
9820  O OD2 . ASP E 261 ? 1.3764 1.0075 0.2885 0.5380  -0.2719 -0.1206 261 ASP E OD2 
9821  N N   . SER E 262 ? 1.3007 0.7535 0.2757 0.3171  -0.2563 -0.1030 262 SER E N   
9822  C CA  . SER E 262 ? 1.2943 0.7140 0.2762 0.2743  -0.2517 -0.0917 262 SER E CA  
9823  C C   . SER E 262 ? 1.2340 0.7074 0.2630 0.2526  -0.2722 -0.1039 262 SER E C   
9824  O O   . SER E 262 ? 1.2015 0.7318 0.2574 0.2687  -0.2872 -0.1227 262 SER E O   
9825  C CB  . SER E 262 ? 1.3074 0.6797 0.2829 0.2395  -0.2432 -0.0926 262 SER E CB  
9826  O OG  . SER E 262 ? 1.2967 0.6492 0.2841 0.1968  -0.2423 -0.0861 262 SER E OG  
9827  N N   . THR E 263 ? 1.2216 0.6784 0.2625 0.2165  -0.2711 -0.0945 263 THR E N   
9828  C CA  . THR E 263 ? 1.1680 0.6699 0.2526 0.1950  -0.2869 -0.1025 263 THR E CA  
9829  C C   . THR E 263 ? 1.1616 0.6379 0.2550 0.1517  -0.2841 -0.0915 263 THR E C   
9830  O O   . THR E 263 ? 1.1991 0.6290 0.2666 0.1426  -0.2697 -0.0763 263 THR E O   
9831  C CB  . THR E 263 ? 1.1579 0.6967 0.2493 0.2206  -0.2918 -0.1011 263 THR E CB  
9832  O OG1 . THR E 263 ? 1.1047 0.6968 0.2431 0.2081  -0.3071 -0.1173 263 THR E OG1 
9833  C CG2 . THR E 263 ? 1.1818 0.6877 0.2550 0.2140  -0.2797 -0.0777 263 THR E CG2 
9834  N N   . ILE E 264 ? 1.1173 0.6252 0.2483 0.1261  -0.2962 -0.0999 264 ILE E N   
9835  C CA  . ILE E 264 ? 1.1068 0.6050 0.2502 0.0888  -0.2966 -0.0898 264 ILE E CA  
9836  C C   . ILE E 264 ? 1.0835 0.6093 0.2491 0.0882  -0.3006 -0.0819 264 ILE E C   
9837  O O   . ILE E 264 ? 1.0428 0.6120 0.2432 0.0882  -0.3101 -0.0904 264 ILE E O   
9838  C CB  . ILE E 264 ? 1.0780 0.5925 0.2454 0.0638  -0.3045 -0.0989 264 ILE E CB  
9839  C CG1 . ILE E 264 ? 1.1064 0.5895 0.2482 0.0637  -0.2991 -0.1061 264 ILE E CG1 
9840  C CG2 . ILE E 264 ? 1.0676 0.5817 0.2474 0.0296  -0.3065 -0.0879 264 ILE E CG2 
9841  C CD1 . ILE E 264 ? 1.0805 0.5845 0.2437 0.0524  -0.3055 -0.1177 264 ILE E CD1 
9842  N N   . MET E 265 ? 0.7695 0.5860 0.3441 -0.1013 -0.1472 -0.1344 265 MET E N   
9843  C CA  . MET E 265 ? 0.7345 0.5537 0.3476 -0.1136 -0.1577 -0.1258 265 MET E CA  
9844  C C   . MET E 265 ? 0.7510 0.5569 0.3542 -0.1225 -0.1806 -0.1281 265 MET E C   
9845  O O   . MET E 265 ? 0.7863 0.5715 0.3657 -0.1236 -0.1915 -0.1398 265 MET E O   
9846  C CB  . MET E 265 ? 0.7290 0.5331 0.3651 -0.1125 -0.1582 -0.1310 265 MET E CB  
9847  C CG  . MET E 265 ? 0.6845 0.5096 0.3665 -0.1218 -0.1608 -0.1217 265 MET E CG  
9848  S SD  . MET E 265 ? 0.6936 0.4935 0.3856 -0.1257 -0.1559 -0.1262 265 MET E SD  
9849  C CE  . MET E 265 ? 0.6897 0.4946 0.3720 -0.0978 -0.1330 -0.1221 265 MET E CE  
9850  N N   . LYS E 266 ? 0.7341 0.5498 0.3488 -0.1251 -0.1893 -0.1180 266 LYS E N   
9851  C CA  . LYS E 266 ? 0.7565 0.5641 0.3566 -0.1222 -0.2140 -0.1212 266 LYS E CA  
9852  C C   . LYS E 266 ? 0.7294 0.5678 0.3752 -0.1204 -0.2264 -0.1258 266 LYS E C   
9853  O O   . LYS E 266 ? 0.6994 0.5551 0.3721 -0.1162 -0.2230 -0.1175 266 LYS E O   
9854  C CB  . LYS E 266 ? 0.7800 0.5650 0.3394 -0.1198 -0.2191 -0.1086 266 LYS E CB  
9855  C CG  . LYS E 266 ? 0.8274 0.5845 0.3270 -0.1293 -0.2141 -0.1064 266 LYS E CG  
9856  C CD  . LYS E 266 ? 0.8727 0.6052 0.3364 -0.1215 -0.2369 -0.1163 266 LYS E CD  
9857  C CE  . LYS E 266 ? 0.9226 0.6285 0.3249 -0.1336 -0.2302 -0.1147 266 LYS E CE  
9858  N NZ  . LYS E 266 ? 0.9672 0.6492 0.3357 -0.1248 -0.2522 -0.1257 266 LYS E NZ  
9859  N N   . SER E 267 ? 0.7449 0.5963 0.3971 -0.1270 -0.2406 -0.1399 267 SER E N   
9860  C CA  . SER E 267 ? 0.7231 0.6225 0.4188 -0.1349 -0.2507 -0.1468 267 SER E CA  
9861  C C   . SER E 267 ? 0.7521 0.6788 0.4424 -0.1438 -0.2731 -0.1631 267 SER E C   
9862  O O   . SER E 267 ? 0.7890 0.6838 0.4476 -0.1552 -0.2749 -0.1709 267 SER E O   
9863  C CB  . SER E 267 ? 0.7064 0.6010 0.4259 -0.1548 -0.2328 -0.1458 267 SER E CB  
9864  O OG  . SER E 267 ? 0.6932 0.6368 0.4485 -0.1733 -0.2409 -0.1524 267 SER E OG  
9865  N N   . GLU E 268 ? 0.7384 0.7317 0.4585 -0.1370 -0.2905 -0.1697 268 GLU E N   
9866  C CA  . GLU E 268 ? 0.7608 0.8089 0.4849 -0.1479 -0.3129 -0.1874 268 GLU E CA  
9867  C C   . GLU E 268 ? 0.7615 0.8377 0.5087 -0.1956 -0.3071 -0.1957 268 GLU E C   
9868  O O   . GLU E 268 ? 0.7919 0.9010 0.5321 -0.2213 -0.3220 -0.2104 268 GLU E O   
9869  C CB  . GLU E 268 ? 0.7516 0.8776 0.4951 -0.1148 -0.3355 -0.1943 268 GLU E CB  
9870  C CG  . GLU E 268 ? 0.7746 0.8529 0.4747 -0.0671 -0.3454 -0.1856 268 GLU E CG  
9871  C CD  . GLU E 268 ? 0.8249 0.8375 0.4654 -0.0622 -0.3532 -0.1859 268 GLU E CD  
9872  O OE1 . GLU E 268 ? 0.8502 0.8955 0.4838 -0.0665 -0.3714 -0.2011 268 GLU E OE1 
9873  O OE2 . GLU E 268 ? 0.8418 0.7759 0.4409 -0.0575 -0.3408 -0.1713 268 GLU E OE2 
9874  N N   . LEU E 269 ? 0.7384 0.7961 0.5044 -0.2105 -0.2866 -0.1860 269 LEU E N   
9875  C CA  . LEU E 269 ? 0.7542 0.8219 0.5273 -0.2597 -0.2810 -0.1914 269 LEU E CA  
9876  C C   . LEU E 269 ? 0.8192 0.8042 0.5356 -0.2886 -0.2793 -0.1973 269 LEU E C   
9877  O O   . LEU E 269 ? 0.8386 0.7552 0.5183 -0.2648 -0.2744 -0.1942 269 LEU E O   
9878  C CB  . LEU E 269 ? 0.7223 0.7756 0.5183 -0.2626 -0.2602 -0.1784 269 LEU E CB  
9879  C CG  . LEU E 269 ? 0.6721 0.8203 0.5235 -0.2536 -0.2629 -0.1773 269 LEU E CG  
9880  C CD1 . LEU E 269 ? 0.6366 0.7551 0.5050 -0.2401 -0.2423 -0.1613 269 LEU E CD1 
9881  C CD2 . LEU E 269 ? 0.6858 0.9160 0.5569 -0.3032 -0.2710 -0.1902 269 LEU E CD2 
9882  N N   . GLU E 270 ? 0.8621 0.8525 0.5638 -0.3421 -0.2837 -0.2062 270 GLU E N   
9883  C CA  . GLU E 270 ? 0.9471 0.8488 0.5779 -0.3748 -0.2874 -0.2144 270 GLU E CA  
9884  C C   . GLU E 270 ? 0.9945 0.7889 0.5771 -0.3875 -0.2702 -0.2069 270 GLU E C   
9885  O O   . GLU E 270 ? 0.9742 0.7204 0.5538 -0.3437 -0.2546 -0.1967 270 GLU E O   
9886  C CB  . GLU E 270 ? 0.9903 0.9510 0.6116 -0.4309 -0.3082 -0.2311 270 GLU E CB  
9887  C CG  . GLU E 270 ? 0.9603 1.0411 0.6339 -0.4701 -0.3120 -0.2351 270 GLU E CG  
9888  C CD  . GLU E 270 ? 1.0085 1.1628 0.6695 -0.5322 -0.3324 -0.2534 270 GLU E CD  
9889  O OE1 . GLU E 270 ? 1.0760 1.1652 0.6777 -0.5519 -0.3433 -0.2620 270 GLU E OE1 
9890  O OE2 . GLU E 270 ? 0.9810 1.2667 0.6904 -0.5626 -0.3376 -0.2605 270 GLU E OE2 
9891  N N   . TYR E 271 ? 1.0660 0.8231 0.6041 -0.4470 -0.2739 -0.2122 271 TYR E N   
9892  C CA  . TYR E 271 ? 1.1417 0.7700 0.6066 -0.4559 -0.2629 -0.2071 271 TYR E CA  
9893  C C   . TYR E 271 ? 1.1810 0.8131 0.6317 -0.5220 -0.2623 -0.2055 271 TYR E C   
9894  O O   . TYR E 271 ? 1.2336 0.8924 0.6601 -0.5888 -0.2762 -0.2157 271 TYR E O   
9895  C CB  . TYR E 271 ? 1.2510 0.7578 0.6157 -0.4606 -0.2721 -0.2177 271 TYR E CB  
9896  C CG  . TYR E 271 ? 1.3505 0.7054 0.6186 -0.4518 -0.2647 -0.2153 271 TYR E CG  
9897  C CD1 . TYR E 271 ? 1.3209 0.6417 0.5936 -0.3836 -0.2482 -0.2073 271 TYR E CD1 
9898  C CD2 . TYR E 271 ? 1.4867 0.7294 0.6480 -0.5112 -0.2760 -0.2223 271 TYR E CD2 
9899  C CE1 . TYR E 271 ? 1.4197 0.6063 0.5983 -0.3637 -0.2441 -0.2078 271 TYR E CE1 
9900  C CE2 . TYR E 271 ? 1.5986 0.6837 0.6524 -0.4945 -0.2729 -0.2212 271 TYR E CE2 
9901  C CZ  . TYR E 271 ? 1.5628 0.6237 0.6276 -0.4150 -0.2574 -0.2148 271 TYR E CZ  
9902  O OH  . TYR E 271 ? 1.6811 0.5905 0.6339 -0.3874 -0.2569 -0.2162 271 TYR E OH  
9903  N N   . GLY E 272 ? 1.1597 0.7692 0.6220 -0.5074 -0.2463 -0.1930 272 GLY E N   
9904  C CA  . GLY E 272 ? 1.1990 0.8077 0.6440 -0.5697 -0.2434 -0.1893 272 GLY E CA  
9905  C C   . GLY E 272 ? 1.3505 0.7914 0.6643 -0.6123 -0.2469 -0.1905 272 GLY E C   
9906  O O   . GLY E 272 ? 1.4114 0.8371 0.6876 -0.6819 -0.2477 -0.1887 272 GLY E O   
9907  N N   . ASN E 273 ? 1.4224 0.7343 0.6568 -0.5706 -0.2499 -0.1943 273 ASN E N   
9908  C CA  . ASN E 273 ? 1.5846 0.7076 0.6735 -0.5884 -0.2552 -0.1961 273 ASN E CA  
9909  C C   . ASN E 273 ? 1.6026 0.6687 0.6699 -0.5784 -0.2424 -0.1833 273 ASN E C   
9910  O O   . ASN E 273 ? 1.7328 0.6796 0.6928 -0.6318 -0.2481 -0.1817 273 ASN E O   
9911  C CB  . ASN E 273 ? 1.7119 0.7798 0.7101 -0.6853 -0.2736 -0.2061 273 ASN E CB  
9912  C CG  . ASN E 273 ? 1.8996 0.7488 0.7256 -0.6879 -0.2861 -0.2130 273 ASN E CG  
9913  O OD1 . ASN E 273 ? 1.9788 0.7768 0.7402 -0.7126 -0.3021 -0.2255 273 ASN E OD1 
9914  N ND2 . ASN E 273 ? 1.9803 0.6943 0.7236 -0.6572 -0.2806 -0.2058 273 ASN E ND2 
9915  N N   . CYS E 274 ? 1.4793 0.6259 0.6415 -0.5120 -0.2262 -0.1738 274 CYS E N   
9916  C CA  . CYS E 274 ? 1.4764 0.5894 0.6347 -0.4927 -0.2134 -0.1615 274 CYS E CA  
9917  C C   . CYS E 274 ? 1.4752 0.5263 0.6108 -0.3992 -0.2059 -0.1610 274 CYS E C   
9918  O O   . CYS E 274 ? 1.4496 0.5182 0.5979 -0.3531 -0.2073 -0.1687 274 CYS E O   
9919  C CB  . CYS E 274 ? 1.3324 0.6102 0.6240 -0.5017 -0.2011 -0.1516 274 CYS E CB  
9920  S SG  . CYS E 274 ? 1.1940 0.5528 0.5875 -0.4095 -0.1831 -0.1412 274 CYS E SG  
9921  N N   . ASN E 275 ? 1.5085 0.4932 0.6065 -0.3727 -0.1983 -0.1530 275 ASN E N   
9922  C CA  . ASN E 275 ? 1.5056 0.4548 0.5868 -0.2818 -0.1907 -0.1538 275 ASN E CA  
9923  C C   . ASN E 275 ? 1.3772 0.4351 0.5637 -0.2516 -0.1730 -0.1405 275 ASN E C   
9924  O O   . ASN E 275 ? 1.3502 0.4384 0.5688 -0.2955 -0.1685 -0.1301 275 ASN E O   
9925  C CB  . ASN E 275 ? 1.6858 0.4421 0.6057 -0.2620 -0.2014 -0.1593 275 ASN E CB  
9926  C CG  . ASN E 275 ? 1.7012 0.4285 0.5911 -0.1586 -0.1973 -0.1664 275 ASN E CG  
9927  O OD1 . ASN E 275 ? 1.6798 0.4405 0.5815 -0.1151 -0.1975 -0.1771 275 ASN E OD1 
9928  N ND2 . ASN E 275 ? 1.7417 0.4148 0.5907 -0.1184 -0.1937 -0.1614 275 ASN E ND2 
9929  N N   . THR E 276 ? 1.3037 0.4230 0.5395 -0.1806 -0.1630 -0.1412 276 THR E N   
9930  C CA  . THR E 276 ? 1.1888 0.4086 0.5171 -0.1528 -0.1470 -0.1292 276 THR E CA  
9931  C C   . THR E 276 ? 1.1857 0.4118 0.5022 -0.0715 -0.1393 -0.1337 276 THR E C   
9932  O O   . THR E 276 ? 1.2669 0.4284 0.5082 -0.0316 -0.1458 -0.1472 276 THR E O   
9933  C CB  . THR E 276 ? 1.0486 0.4147 0.5001 -0.1763 -0.1410 -0.1226 276 THR E CB  
9934  O OG1 . THR E 276 ? 0.9547 0.4006 0.4814 -0.1570 -0.1274 -0.1105 276 THR E OG1 
9935  C CG2 . THR E 276 ? 1.0143 0.4272 0.4875 -0.1495 -0.1423 -0.1307 276 THR E CG2 
9936  N N   . LYS E 277 ? 1.0974 0.4069 0.4845 -0.0473 -0.1258 -0.1237 277 LYS E N   
9937  C CA  . LYS E 277 ? 1.0737 0.4322 0.4698 0.0226  -0.1164 -0.1281 277 LYS E CA  
9938  C C   . LYS E 277 ? 0.9339 0.4398 0.4432 0.0199  -0.1029 -0.1194 277 LYS E C   
9939  O O   . LYS E 277 ? 0.8989 0.4732 0.4293 0.0639  -0.0929 -0.1213 277 LYS E O   
9940  C CB  . LYS E 277 ? 1.1308 0.4336 0.4769 0.0613  -0.1152 -0.1264 277 LYS E CB  
9941  C CG  . LYS E 277 ? 1.2254 0.4784 0.4847 0.1415  -0.1196 -0.1432 277 LYS E CG  
9942  C CD  . LYS E 277 ? 1.2916 0.4856 0.4933 0.1867  -0.1216 -0.1425 277 LYS E CD  
9943  C CE  . LYS E 277 ? 1.1794 0.5185 0.4733 0.2199  -0.1058 -0.1367 277 LYS E CE  
9944  N NZ  . LYS E 277 ? 1.2463 0.5858 0.4798 0.3110  -0.1080 -0.1512 277 LYS E NZ  
9945  N N   . CYS E 278 ? 0.8660 0.4186 0.4380 -0.0323 -0.1041 -0.1109 278 CYS E N   
9946  C CA  . CYS E 278 ? 0.7589 0.4222 0.4161 -0.0402 -0.0959 -0.1024 278 CYS E CA  
9947  C C   . CYS E 278 ? 0.7357 0.4150 0.4196 -0.0835 -0.1056 -0.1024 278 CYS E C   
9948  O O   . CYS E 278 ? 0.7384 0.4042 0.4324 -0.1215 -0.1118 -0.0992 278 CYS E O   
9949  C CB  . CYS E 278 ? 0.6962 0.4058 0.4062 -0.0462 -0.0871 -0.0887 278 CYS E CB  
9950  S SG  . CYS E 278 ? 0.5906 0.4064 0.3824 -0.0620 -0.0812 -0.0773 278 CYS E SG  
9951  N N   . GLN E 279 ? 0.7179 0.4322 0.4103 -0.0779 -0.1073 -0.1068 279 GLN E N   
9952  C CA  . GLN E 279 ? 0.7080 0.4344 0.4153 -0.1103 -0.1195 -0.1094 279 GLN E CA  
9953  C C   . GLN E 279 ? 0.6383 0.4384 0.3965 -0.1123 -0.1183 -0.1015 279 GLN E C   
9954  O O   . GLN E 279 ? 0.6171 0.4492 0.3790 -0.0923 -0.1087 -0.0980 279 GLN E O   
9955  C CB  . GLN E 279 ? 0.7760 0.4514 0.4253 -0.1048 -0.1280 -0.1233 279 GLN E CB  
9956  C CG  . GLN E 279 ? 0.7749 0.4624 0.4332 -0.1372 -0.1428 -0.1282 279 GLN E CG  
9957  C CD  . GLN E 279 ? 0.8012 0.4675 0.4557 -0.1810 -0.1535 -0.1303 279 GLN E CD  
9958  O OE1 . GLN E 279 ? 0.8787 0.4665 0.4738 -0.1939 -0.1565 -0.1356 279 GLN E OE1 
9959  N NE2 . GLN E 279 ? 0.7478 0.4839 0.4568 -0.2044 -0.1603 -0.1271 279 GLN E NE2 
9960  N N   . THR E 280 ? 0.6144 0.4404 0.4029 -0.1372 -0.1294 -0.0999 280 THR E N   
9961  C CA  . THR E 280 ? 0.5763 0.4478 0.3903 -0.1359 -0.1350 -0.0947 280 THR E CA  
9962  C C   . THR E 280 ? 0.6003 0.4733 0.4038 -0.1485 -0.1528 -0.1046 280 THR E C   
9963  O O   . THR E 280 ? 0.6340 0.4876 0.4239 -0.1677 -0.1604 -0.1141 280 THR E O   
9964  C CB  . THR E 280 ? 0.5290 0.4388 0.3858 -0.1400 -0.1350 -0.0850 280 THR E CB  
9965  O OG1 . THR E 280 ? 0.5284 0.4609 0.4042 -0.1584 -0.1479 -0.0913 280 THR E OG1 
9966  C CG2 . THR E 280 ? 0.5128 0.4182 0.3817 -0.1347 -0.1198 -0.0772 280 THR E CG2 
9967  N N   . PRO E 281 ? 0.5933 0.4847 0.3942 -0.1402 -0.1609 -0.1025 281 PRO E N   
9968  C CA  . PRO E 281 ? 0.6143 0.5160 0.4069 -0.1458 -0.1809 -0.1120 281 PRO E CA  
9969  C C   . PRO E 281 ? 0.6008 0.5496 0.4278 -0.1578 -0.1940 -0.1174 281 PRO E C   
9970  O O   . PRO E 281 ? 0.6219 0.5916 0.4449 -0.1681 -0.2102 -0.1292 281 PRO E O   
9971  C CB  . PRO E 281 ? 0.6162 0.5162 0.3882 -0.1299 -0.1867 -0.1056 281 PRO E CB  
9972  C CG  . PRO E 281 ? 0.5960 0.4909 0.3678 -0.1250 -0.1692 -0.0922 281 PRO E CG  
9973  C CD  . PRO E 281 ? 0.5817 0.4759 0.3713 -0.1276 -0.1521 -0.0922 281 PRO E CD  
9974  N N   . MET E 282 ? 0.5679 0.5429 0.4283 -0.1567 -0.1869 -0.1099 282 MET E N   
9975  C CA  . MET E 282 ? 0.5516 0.5889 0.4482 -0.1670 -0.1960 -0.1155 282 MET E CA  
9976  C C   . MET E 282 ? 0.5678 0.6037 0.4684 -0.2051 -0.1900 -0.1206 282 MET E C   
9977  O O   . MET E 282 ? 0.5706 0.6654 0.4904 -0.2292 -0.1995 -0.1301 282 MET E O   
9978  C CB  . MET E 282 ? 0.5161 0.5770 0.4390 -0.1481 -0.1905 -0.1052 282 MET E CB  
9979  C CG  . MET E 282 ? 0.5217 0.5591 0.4201 -0.1169 -0.1964 -0.0975 282 MET E CG  
9980  S SD  . MET E 282 ? 0.5364 0.6228 0.4333 -0.0838 -0.2229 -0.1063 282 MET E SD  
9981  C CE  . MET E 282 ? 0.4962 0.6304 0.4360 -0.0784 -0.2147 -0.1021 282 MET E CE  
9982  N N   . GLY E 283 ? 0.5870 0.5566 0.4616 -0.2107 -0.1750 -0.1151 283 GLY E N   
9983  C CA  . GLY E 283 ? 0.6267 0.5617 0.4799 -0.2456 -0.1701 -0.1180 283 GLY E CA  
9984  C C   . GLY E 283 ? 0.6438 0.5073 0.4680 -0.2301 -0.1540 -0.1097 283 GLY E C   
9985  O O   . GLY E 283 ? 0.6219 0.4772 0.4472 -0.1961 -0.1460 -0.1037 283 GLY E O   
9986  N N   . ALA E 284 ? 0.6920 0.5055 0.4833 -0.2561 -0.1501 -0.1100 284 ALA E N   
9987  C CA  . ALA E 284 ? 0.7246 0.4642 0.4763 -0.2342 -0.1382 -0.1045 284 ALA E CA  
9988  C C   . ALA E 284 ? 0.6871 0.4490 0.4712 -0.2334 -0.1271 -0.0930 284 ALA E C   
9989  O O   . ALA E 284 ? 0.6564 0.4747 0.4790 -0.2615 -0.1288 -0.0910 284 ALA E O   
9990  C CB  . ALA E 284 ? 0.8315 0.4688 0.4981 -0.2563 -0.1440 -0.1127 284 ALA E CB  
9991  N N   . ILE E 285 ? 0.6913 0.4167 0.4585 -0.1988 -0.1161 -0.0871 285 ILE E N   
9992  C CA  . ILE E 285 ? 0.6581 0.3995 0.4514 -0.1922 -0.1055 -0.0760 285 ILE E CA  
9993  C C   . ILE E 285 ? 0.7375 0.3857 0.4628 -0.1857 -0.1021 -0.0755 285 ILE E C   
9994  O O   . ILE E 285 ? 0.7951 0.3816 0.4635 -0.1532 -0.1031 -0.0819 285 ILE E O   
9995  C CB  . ILE E 285 ? 0.5860 0.3839 0.4245 -0.1550 -0.0964 -0.0683 285 ILE E CB  
9996  C CG1 . ILE E 285 ? 0.5181 0.3925 0.4159 -0.1656 -0.1000 -0.0639 285 ILE E CG1 
9997  C CG2 . ILE E 285 ? 0.5809 0.3667 0.4176 -0.1341 -0.0850 -0.0600 285 ILE E CG2 
9998  C CD1 . ILE E 285 ? 0.4747 0.3848 0.3922 -0.1405 -0.0968 -0.0585 285 ILE E CD1 
9999  N N   . ASN E 286 ? 0.7483 0.3857 0.4729 -0.2136 -0.0992 -0.0688 286 ASN E N   
10000 C CA  . ASN E 286 ? 0.8315 0.3718 0.4838 -0.2082 -0.0973 -0.0662 286 ASN E CA  
10001 C C   . ASN E 286 ? 0.7813 0.3606 0.4757 -0.2083 -0.0869 -0.0539 286 ASN E C   
10002 O O   . ASN E 286 ? 0.7837 0.3766 0.4876 -0.2544 -0.0861 -0.0497 286 ASN E O   
10003 C CB  . ASN E 286 ? 0.9423 0.3919 0.5132 -0.2623 -0.1076 -0.0714 286 ASN E CB  
10004 C CG  . ASN E 286 ? 1.0535 0.3780 0.5272 -0.2606 -0.1086 -0.0678 286 ASN E CG  
10005 O OD1 . ASN E 286 ? 1.0784 0.3572 0.5188 -0.2009 -0.1064 -0.0678 286 ASN E OD1 
10006 N ND2 . ASN E 286 ? 1.1296 0.4005 0.5508 -0.3268 -0.1128 -0.0654 286 ASN E ND2 
10007 N N   . SER E 287 ? 0.7354 0.3429 0.4558 -0.1591 -0.0788 -0.0492 287 SER E N   
10008 C CA  . SER E 287 ? 0.6913 0.3312 0.4469 -0.1544 -0.0696 -0.0379 287 SER E CA  
10009 C C   . SER E 287 ? 0.6937 0.3240 0.4342 -0.0985 -0.0640 -0.0363 287 SER E C   
10010 O O   . SER E 287 ? 0.7100 0.3364 0.4289 -0.0604 -0.0656 -0.0445 287 SER E O   
10011 C CB  . SER E 287 ? 0.5869 0.3356 0.4327 -0.1674 -0.0654 -0.0324 287 SER E CB  
10012 O OG  . SER E 287 ? 0.5285 0.3308 0.4109 -0.1330 -0.0622 -0.0315 287 SER E OG  
10013 N N   . SER E 288 ? 0.6784 0.3149 0.4305 -0.0937 -0.0575 -0.0270 288 SER E N   
10014 C CA  . SER E 288 ? 0.6717 0.3217 0.4195 -0.0422 -0.0525 -0.0255 288 SER E CA  
10015 C C   . SER E 288 ? 0.5638 0.3221 0.3960 -0.0401 -0.0434 -0.0172 288 SER E C   
10016 O O   . SER E 288 ? 0.5459 0.3395 0.3863 -0.0061 -0.0384 -0.0155 288 SER E O   
10017 C CB  . SER E 288 ? 0.7511 0.3148 0.4337 -0.0342 -0.0542 -0.0214 288 SER E CB  
10018 O OG  . SER E 288 ? 0.7531 0.3008 0.4440 -0.0892 -0.0525 -0.0128 288 SER E OG  
10019 N N   . MET E 289 ? 0.5021 0.3110 0.3884 -0.0751 -0.0431 -0.0134 289 MET E N   
10020 C CA  . MET E 289 ? 0.4209 0.3096 0.3679 -0.0758 -0.0379 -0.0059 289 MET E CA  
10021 C C   . MET E 289 ? 0.3999 0.3335 0.3520 -0.0497 -0.0354 -0.0092 289 MET E C   
10022 O O   . MET E 289 ? 0.4286 0.3503 0.3560 -0.0389 -0.0387 -0.0184 289 MET E O   
10023 C CB  . MET E 289 ? 0.3831 0.3059 0.3673 -0.1058 -0.0427 -0.0055 289 MET E CB  
10024 C CG  . MET E 289 ? 0.3944 0.3074 0.3837 -0.1375 -0.0446 -0.0048 289 MET E CG  
10025 S SD  . MET E 289 ? 0.3684 0.3006 0.3810 -0.1398 -0.0362 0.0063  289 MET E SD  
10026 C CE  . MET E 289 ? 0.3515 0.3309 0.3949 -0.1754 -0.0401 0.0029  289 MET E CE  
10027 N N   . PRO E 290 ? 0.3545 0.3437 0.3348 -0.0440 -0.0294 -0.0022 290 PRO E N   
10028 C CA  . PRO E 290 ? 0.3366 0.3841 0.3208 -0.0334 -0.0260 -0.0049 290 PRO E CA  
10029 C C   . PRO E 290 ? 0.3143 0.3799 0.3100 -0.0588 -0.0302 -0.0040 290 PRO E C   
10030 O O   . PRO E 290 ? 0.3150 0.4195 0.3023 -0.0577 -0.0278 -0.0073 290 PRO E O   
10031 C CB  . PRO E 290 ? 0.3060 0.4022 0.3100 -0.0315 -0.0196 0.0033  290 PRO E CB  
10032 C CG  . PRO E 290 ? 0.2892 0.3550 0.3114 -0.0499 -0.0212 0.0123  290 PRO E CG  
10033 C CD  . PRO E 290 ? 0.3277 0.3290 0.3295 -0.0495 -0.0252 0.0078  290 PRO E CD  
10034 N N   . PHE E 291 ? 0.3014 0.3427 0.3108 -0.0797 -0.0371 -0.0005 291 PHE E N   
10035 C CA  . PHE E 291 ? 0.2925 0.3391 0.3022 -0.0965 -0.0449 -0.0001 291 PHE E CA  
10036 C C   . PHE E 291 ? 0.3018 0.3215 0.3134 -0.1041 -0.0547 -0.0065 291 PHE E C   
10037 O O   . PHE E 291 ? 0.3097 0.3116 0.3276 -0.1078 -0.0548 -0.0085 291 PHE E O   
10038 C CB  . PHE E 291 ? 0.2731 0.3297 0.2915 -0.1084 -0.0474 0.0096  291 PHE E CB  
10039 C CG  . PHE E 291 ? 0.2684 0.3562 0.2784 -0.1142 -0.0402 0.0164  291 PHE E CG  
10040 C CD1 . PHE E 291 ? 0.2854 0.3901 0.2691 -0.1296 -0.0406 0.0170  291 PHE E CD1 
10041 C CD2 . PHE E 291 ? 0.2526 0.3568 0.2770 -0.1096 -0.0333 0.0223  291 PHE E CD2 
10042 C CE1 . PHE E 291 ? 0.2864 0.4318 0.2584 -0.1459 -0.0337 0.0227  291 PHE E CE1 
10043 C CE2 . PHE E 291 ? 0.2501 0.3944 0.2664 -0.1201 -0.0276 0.0276  291 PHE E CE2 
10044 C CZ  . PHE E 291 ? 0.2675 0.4362 0.2578 -0.1411 -0.0275 0.0276  291 PHE E CZ  
10045 N N   . HIS E 292 ? 0.3059 0.3256 0.3070 -0.1102 -0.0636 -0.0096 292 HIS E N   
10046 C CA  . HIS E 292 ? 0.3112 0.3235 0.3170 -0.1166 -0.0758 -0.0163 292 HIS E CA  
10047 C C   . HIS E 292 ? 0.3155 0.3282 0.3062 -0.1157 -0.0878 -0.0150 292 HIS E C   
10048 O O   . HIS E 292 ? 0.3236 0.3302 0.2906 -0.1185 -0.0858 -0.0084 292 HIS E O   
10049 C CB  . HIS E 292 ? 0.3399 0.3321 0.3296 -0.1190 -0.0781 -0.0267 292 HIS E CB  
10050 C CG  . HIS E 292 ? 0.3559 0.3444 0.3202 -0.1141 -0.0796 -0.0301 292 HIS E CG  
10051 N ND1 . HIS E 292 ? 0.3720 0.3542 0.3237 -0.1187 -0.0916 -0.0367 292 HIS E ND1 
10052 C CD2 . HIS E 292 ? 0.3605 0.3602 0.3087 -0.1058 -0.0704 -0.0285 292 HIS E CD2 
10053 C CE1 . HIS E 292 ? 0.3879 0.3680 0.3139 -0.1154 -0.0891 -0.0379 292 HIS E CE1 
10054 N NE2 . HIS E 292 ? 0.3803 0.3771 0.3051 -0.1088 -0.0756 -0.0334 292 HIS E NE2 
10055 N N   . ASN E 293 ? 0.3198 0.3395 0.3157 -0.1128 -0.1014 -0.0219 293 ASN E N   
10056 C CA  . ASN E 293 ? 0.3422 0.3494 0.3092 -0.1024 -0.1172 -0.0225 293 ASN E CA  
10057 C C   . ASN E 293 ? 0.3615 0.3754 0.3223 -0.0986 -0.1316 -0.0346 293 ASN E C   
10058 O O   . ASN E 293 ? 0.3833 0.3981 0.3262 -0.0809 -0.1490 -0.0394 293 ASN E O   
10059 C CB  . ASN E 293 ? 0.3390 0.3540 0.3092 -0.0871 -0.1246 -0.0200 293 ASN E CB  
10060 C CG  . ASN E 293 ? 0.3199 0.3867 0.3296 -0.0813 -0.1287 -0.0301 293 ASN E CG  
10061 O OD1 . ASN E 293 ? 0.3069 0.3962 0.3429 -0.0996 -0.1216 -0.0352 293 ASN E OD1 
10062 N ND2 . ASN E 293 ? 0.3286 0.4143 0.3340 -0.0569 -0.1411 -0.0340 293 ASN E ND2 
10063 N N   . ILE E 294 ? 0.3628 0.3772 0.3301 -0.1114 -0.1260 -0.0406 294 ILE E N   
10064 C CA  . ILE E 294 ? 0.3817 0.4064 0.3453 -0.1138 -0.1390 -0.0530 294 ILE E CA  
10065 C C   . ILE E 294 ? 0.4133 0.4084 0.3348 -0.1058 -0.1493 -0.0537 294 ILE E C   
10066 O O   . ILE E 294 ? 0.4345 0.4342 0.3400 -0.0911 -0.1677 -0.0596 294 ILE E O   
10067 C CB  . ILE E 294 ? 0.3901 0.4079 0.3593 -0.1336 -0.1313 -0.0595 294 ILE E CB  
10068 C CG1 . ILE E 294 ? 0.3763 0.4052 0.3699 -0.1474 -0.1210 -0.0570 294 ILE E CG1 
10069 C CG2 . ILE E 294 ? 0.4130 0.4468 0.3775 -0.1429 -0.1461 -0.0729 294 ILE E CG2 
10070 C CD1 . ILE E 294 ? 0.3570 0.4419 0.3822 -0.1502 -0.1277 -0.0601 294 ILE E CD1 
10071 N N   . HIS E 295 ? 0.4225 0.3914 0.3218 -0.1134 -0.1380 -0.0488 295 HIS E N   
10072 C CA  . HIS E 295 ? 0.4581 0.4000 0.3126 -0.1138 -0.1448 -0.0492 295 HIS E CA  
10073 C C   . HIS E 295 ? 0.4608 0.3975 0.2967 -0.1248 -0.1274 -0.0420 295 HIS E C   
10074 O O   . HIS E 295 ? 0.4437 0.3970 0.2997 -0.1245 -0.1131 -0.0444 295 HIS E O   
10075 C CB  . HIS E 295 ? 0.4752 0.4191 0.3277 -0.1149 -0.1538 -0.0623 295 HIS E CB  
10076 C CG  . HIS E 295 ? 0.5162 0.4337 0.3221 -0.1114 -0.1667 -0.0645 295 HIS E CG  
10077 N ND1 . HIS E 295 ? 0.5386 0.4354 0.3088 -0.1209 -0.1575 -0.0606 295 HIS E ND1 
10078 C CD2 . HIS E 295 ? 0.5447 0.4564 0.3296 -0.0985 -0.1886 -0.0711 295 HIS E CD2 
10079 C CE1 . HIS E 295 ? 0.5812 0.4505 0.3069 -0.1185 -0.1725 -0.0629 295 HIS E CE1 
10080 N NE2 . HIS E 295 ? 0.5873 0.4608 0.3194 -0.1019 -0.1926 -0.0694 295 HIS E NE2 
10081 N N   . PRO E 296 ? 0.4922 0.4069 0.2813 -0.1347 -0.1296 -0.0343 296 PRO E N   
10082 C CA  . PRO E 296 ? 0.4960 0.4289 0.2677 -0.1523 -0.1123 -0.0281 296 PRO E CA  
10083 C C   . PRO E 296 ? 0.4973 0.4566 0.2716 -0.1490 -0.1013 -0.0378 296 PRO E C   
10084 O O   . PRO E 296 ? 0.4804 0.4806 0.2696 -0.1461 -0.0848 -0.0388 296 PRO E O   
10085 C CB  . PRO E 296 ? 0.5513 0.4427 0.2549 -0.1728 -0.1215 -0.0192 296 PRO E CB  
10086 C CG  . PRO E 296 ? 0.5831 0.4290 0.2630 -0.1555 -0.1449 -0.0245 296 PRO E CG  
10087 C CD  . PRO E 296 ? 0.5387 0.4087 0.2778 -0.1312 -0.1498 -0.0316 296 PRO E CD  
10088 N N   . LEU E 297 ? 0.5239 0.4612 0.2784 -0.1451 -0.1120 -0.0461 297 LEU E N   
10089 C CA  . LEU E 297 ? 0.5376 0.4898 0.2834 -0.1384 -0.1041 -0.0569 297 LEU E CA  
10090 C C   . LEU E 297 ? 0.5247 0.4741 0.3000 -0.1188 -0.1023 -0.0673 297 LEU E C   
10091 O O   . LEU E 297 ? 0.5334 0.4563 0.3140 -0.1173 -0.1156 -0.0742 297 LEU E O   
10092 C CB  . LEU E 297 ? 0.5784 0.5002 0.2842 -0.1435 -0.1177 -0.0616 297 LEU E CB  
10093 C CG  . LEU E 297 ? 0.6177 0.5172 0.2697 -0.1662 -0.1229 -0.0510 297 LEU E CG  
10094 C CD1 . LEU E 297 ? 0.6630 0.5198 0.2734 -0.1645 -0.1413 -0.0562 297 LEU E CD1 
10095 C CD2 . LEU E 297 ? 0.6283 0.5715 0.2580 -0.1880 -0.1029 -0.0468 297 LEU E CD2 
10096 N N   . THR E 298 ? 0.5146 0.4900 0.3004 -0.1052 -0.0871 -0.0692 298 THR E N   
10097 C CA  . THR E 298 ? 0.5272 0.4780 0.3169 -0.0856 -0.0863 -0.0787 298 THR E CA  
10098 C C   . THR E 298 ? 0.5614 0.5243 0.3202 -0.0591 -0.0767 -0.0903 298 THR E C   
10099 O O   . THR E 298 ? 0.5595 0.5749 0.3083 -0.0575 -0.0665 -0.0902 298 THR E O   
10100 C CB  . THR E 298 ? 0.4999 0.4540 0.3191 -0.0813 -0.0808 -0.0720 298 THR E CB  
10101 O OG1 . THR E 298 ? 0.4894 0.4892 0.3102 -0.0655 -0.0658 -0.0699 298 THR E OG1 
10102 C CG2 . THR E 298 ? 0.4649 0.4238 0.3136 -0.1014 -0.0878 -0.0608 298 THR E CG2 
10103 N N   . ILE E 299 ? 0.6028 0.5155 0.3380 -0.0394 -0.0808 -0.1011 299 ILE E N   
10104 C CA  . ILE E 299 ? 0.6539 0.5621 0.3460 -0.0012 -0.0751 -0.1153 299 ILE E CA  
10105 C C   . ILE E 299 ? 0.6895 0.5473 0.3611 0.0244  -0.0758 -0.1191 299 ILE E C   
10106 O O   . ILE E 299 ? 0.7007 0.4979 0.3719 0.0034  -0.0850 -0.1154 299 ILE E O   
10107 C CB  . ILE E 299 ? 0.7059 0.5707 0.3550 0.0002  -0.0848 -0.1278 299 ILE E CB  
10108 C CG1 . ILE E 299 ? 0.7747 0.6202 0.3659 0.0489  -0.0815 -0.1454 299 ILE E CG1 
10109 C CG2 . ILE E 299 ? 0.7270 0.5191 0.3698 -0.0271 -0.1015 -0.1283 299 ILE E CG2 
10110 C CD1 . ILE E 299 ? 0.7619 0.7043 0.3545 0.0742  -0.0660 -0.1506 299 ILE E CD1 
10111 N N   . GLY E 300 ? 0.7128 0.6013 0.3634 0.0691  -0.0665 -0.1268 300 GLY E N   
10112 C CA  . GLY E 300 ? 0.7681 0.5974 0.3795 0.1049  -0.0692 -0.1322 300 GLY E CA  
10113 C C   . GLY E 300 ? 0.7217 0.6036 0.3731 0.1109  -0.0600 -0.1218 300 GLY E C   
10114 O O   . GLY E 300 ? 0.6523 0.6295 0.3564 0.0940  -0.0495 -0.1131 300 GLY E O   
10115 N N   . GLU E 301 ? 0.7722 0.5825 0.3883 0.1319  -0.0651 -0.1227 301 GLU E N   
10116 C CA  . GLU E 301 ? 0.7396 0.5853 0.3849 0.1413  -0.0584 -0.1136 301 GLU E CA  
10117 C C   . GLU E 301 ? 0.6764 0.5180 0.3777 0.0841  -0.0586 -0.0956 301 GLU E C   
10118 O O   . GLU E 301 ? 0.7095 0.4683 0.3898 0.0634  -0.0665 -0.0918 301 GLU E O   
10119 C CB  . GLU E 301 ? 0.8357 0.5888 0.4050 0.1888  -0.0662 -0.1220 301 GLU E CB  
10120 C CG  . GLU E 301 ? 0.8139 0.5985 0.4031 0.2073  -0.0608 -0.1144 301 GLU E CG  
10121 C CD  . GLU E 301 ? 0.7861 0.6968 0.3965 0.2562  -0.0506 -0.1229 301 GLU E CD  
10122 O OE1 . GLU E 301 ? 0.7820 0.7637 0.3935 0.2731  -0.0460 -0.1344 301 GLU E OE1 
10123 O OE2 . GLU E 301 ? 0.7709 0.7170 0.3956 0.2758  -0.0471 -0.1186 301 GLU E OE2 
10124 N N   . CYS E 302 ? 0.5957 0.5261 0.3595 0.0579  -0.0504 -0.0854 302 CYS E N   
10125 C CA  . CYS E 302 ? 0.5415 0.4725 0.3525 0.0112  -0.0525 -0.0708 302 CYS E CA  
10126 C C   . CYS E 302 ? 0.4845 0.4753 0.3382 0.0052  -0.0438 -0.0587 302 CYS E C   
10127 O O   . CYS E 302 ? 0.4700 0.5305 0.3295 0.0235  -0.0348 -0.0602 302 CYS E O   
10128 C CB  . CYS E 302 ? 0.5167 0.4695 0.3448 -0.0186 -0.0565 -0.0693 302 CYS E CB  
10129 S SG  . CYS E 302 ? 0.5775 0.4605 0.3622 -0.0228 -0.0692 -0.0821 302 CYS E SG  
10130 N N   . PRO E 303 ? 0.4544 0.4255 0.3365 -0.0220 -0.0467 -0.0478 303 PRO E N   
10131 C CA  . PRO E 303 ? 0.4019 0.4242 0.3219 -0.0341 -0.0404 -0.0358 303 PRO E CA  
10132 C C   . PRO E 303 ? 0.3724 0.4393 0.3052 -0.0579 -0.0403 -0.0310 303 PRO E C   
10133 O O   . PRO E 303 ? 0.3879 0.4418 0.3062 -0.0660 -0.0460 -0.0361 303 PRO E O   
10134 C CB  . PRO E 303 ? 0.3896 0.3742 0.3285 -0.0548 -0.0452 -0.0284 303 PRO E CB  
10135 C CG  . PRO E 303 ? 0.4216 0.3574 0.3430 -0.0684 -0.0549 -0.0356 303 PRO E CG  
10136 C CD  . PRO E 303 ? 0.4746 0.3820 0.3508 -0.0441 -0.0557 -0.0475 303 PRO E CD  
10137 N N   . LYS E 304 ? 0.3414 0.4508 0.2909 -0.0717 -0.0351 -0.0212 304 LYS E N   
10138 C CA  . LYS E 304 ? 0.3362 0.4702 0.2759 -0.1001 -0.0362 -0.0154 304 LYS E CA  
10139 C C   . LYS E 304 ? 0.3330 0.4181 0.2722 -0.1185 -0.0490 -0.0094 304 LYS E C   
10140 O O   . LYS E 304 ? 0.3171 0.3802 0.2766 -0.1159 -0.0530 -0.0057 304 LYS E O   
10141 C CB  . LYS E 304 ? 0.3230 0.5134 0.2655 -0.1150 -0.0275 -0.0074 304 LYS E CB  
10142 C CG  . LYS E 304 ? 0.3234 0.5854 0.2707 -0.0898 -0.0157 -0.0155 304 LYS E CG  
10143 C CD  . LYS E 304 ? 0.3473 0.6565 0.2732 -0.0827 -0.0109 -0.0269 304 LYS E CD  
10144 C CE  . LYS E 304 ? 0.3683 0.6914 0.2883 -0.0285 -0.0078 -0.0424 304 LYS E CE  
10145 N NZ  . LYS E 304 ? 0.3888 0.7928 0.2903 -0.0151 -0.0001 -0.0555 304 LYS E NZ  
10146 N N   . TYR E 305 ? 0.3532 0.4247 0.2645 -0.1338 -0.0562 -0.0097 305 TYR E N   
10147 C CA  . TYR E 305 ? 0.3633 0.3898 0.2627 -0.1413 -0.0717 -0.0065 305 TYR E CA  
10148 C C   . TYR E 305 ? 0.3728 0.3850 0.2494 -0.1585 -0.0752 0.0052  305 TYR E C   
10149 O O   . TYR E 305 ? 0.3908 0.4187 0.2375 -0.1823 -0.0690 0.0114  305 TYR E O   
10150 C CB  . TYR E 305 ? 0.3964 0.4013 0.2621 -0.1469 -0.0810 -0.0118 305 TYR E CB  
10151 C CG  . TYR E 305 ? 0.4190 0.3790 0.2631 -0.1453 -0.1002 -0.0104 305 TYR E CG  
10152 C CD1 . TYR E 305 ? 0.4052 0.3620 0.2778 -0.1280 -0.1103 -0.0180 305 TYR E CD1 
10153 C CD2 . TYR E 305 ? 0.4655 0.3866 0.2517 -0.1609 -0.1095 -0.0026 305 TYR E CD2 
10154 C CE1 . TYR E 305 ? 0.4291 0.3615 0.2819 -0.1167 -0.1296 -0.0200 305 TYR E CE1 
10155 C CE2 . TYR E 305 ? 0.5021 0.3736 0.2550 -0.1475 -0.1306 -0.0034 305 TYR E CE2 
10156 C CZ  . TYR E 305 ? 0.4794 0.3650 0.2705 -0.1206 -0.1407 -0.0132 305 TYR E CZ  
10157 O OH  . TYR E 305 ? 0.5172 0.3707 0.2762 -0.0977 -0.1631 -0.0173 305 TYR E OH  
10158 N N   . VAL E 306 ? 0.3675 0.3517 0.2523 -0.1481 -0.0856 0.0073  306 VAL E N   
10159 C CA  . VAL E 306 ? 0.3984 0.3441 0.2426 -0.1572 -0.0951 0.0164  306 VAL E CA  
10160 C C   . VAL E 306 ? 0.4232 0.3291 0.2506 -0.1346 -0.1154 0.0113  306 VAL E C   
10161 O O   . VAL E 306 ? 0.3978 0.3275 0.2643 -0.1164 -0.1186 0.0014  306 VAL E O   
10162 C CB  . VAL E 306 ? 0.3715 0.3345 0.2392 -0.1582 -0.0865 0.0235  306 VAL E CB  
10163 C CG1 . VAL E 306 ? 0.3573 0.3682 0.2313 -0.1787 -0.0695 0.0277  306 VAL E CG1 
10164 C CG2 . VAL E 306 ? 0.3269 0.3131 0.2523 -0.1345 -0.0834 0.0180  306 VAL E CG2 
10165 N N   . LYS E 307 ? 0.4832 0.3284 0.2438 -0.1359 -0.1304 0.0169  307 LYS E N   
10166 C CA  . LYS E 307 ? 0.5226 0.3292 0.2530 -0.1028 -0.1533 0.0101  307 LYS E CA  
10167 C C   . LYS E 307 ? 0.4998 0.3255 0.2613 -0.0742 -0.1569 0.0069  307 LYS E C   
10168 O O   . LYS E 307 ? 0.5316 0.3438 0.2720 -0.0383 -0.1761 -0.0015 307 LYS E O   
10169 C CB  . LYS E 307 ? 0.6222 0.3336 0.2441 -0.1096 -0.1718 0.0166  307 LYS E CB  
10170 C CG  . LYS E 307 ? 0.6622 0.3480 0.2398 -0.1315 -0.1743 0.0170  307 LYS E CG  
10171 C CD  . LYS E 307 ? 0.7816 0.3533 0.2355 -0.1315 -0.1985 0.0221  307 LYS E CD  
10172 C CE  . LYS E 307 ? 0.8350 0.3725 0.2276 -0.1711 -0.1971 0.0274  307 LYS E CE  
10173 N NZ  . LYS E 307 ? 0.9735 0.3773 0.2238 -0.1775 -0.2221 0.0344  307 LYS E NZ  
10174 N N   . SER E 308 ? 0.4496 0.3122 0.2581 -0.0862 -0.1394 0.0125  308 SER E N   
10175 C CA  . SER E 308 ? 0.4311 0.3118 0.2644 -0.0635 -0.1408 0.0107  308 SER E CA  
10176 C C   . SER E 308 ? 0.3950 0.3387 0.2844 -0.0392 -0.1441 -0.0030 308 SER E C   
10177 O O   . SER E 308 ? 0.3644 0.3454 0.2921 -0.0505 -0.1378 -0.0088 308 SER E O   
10178 C CB  . SER E 308 ? 0.3849 0.2940 0.2573 -0.0841 -0.1204 0.0197  308 SER E CB  
10179 O OG  . SER E 308 ? 0.4082 0.2892 0.2414 -0.1155 -0.1141 0.0304  308 SER E OG  
10180 N N   . ASN E 309 ? 0.4064 0.3637 0.2937 -0.0075 -0.1546 -0.0092 309 ASN E N   
10181 C CA  . ASN E 309 ? 0.3677 0.4094 0.3144 0.0074  -0.1539 -0.0222 309 ASN E CA  
10182 C C   . ASN E 309 ? 0.3141 0.3978 0.3158 -0.0129 -0.1330 -0.0167 309 ASN E C   
10183 O O   . ASN E 309 ? 0.2804 0.4306 0.3326 -0.0234 -0.1257 -0.0241 309 ASN E O   
10184 C CB  . ASN E 309 ? 0.4092 0.4634 0.3263 0.0576  -0.1752 -0.0343 309 ASN E CB  
10185 C CG  . ASN E 309 ? 0.4718 0.4889 0.3304 0.0865  -0.1997 -0.0430 309 ASN E CG  
10186 O OD1 . ASN E 309 ? 0.4582 0.5028 0.3374 0.0741  -0.2010 -0.0489 309 ASN E OD1 
10187 N ND2 . ASN E 309 ? 0.5520 0.4965 0.3271 0.1271  -0.2211 -0.0442 309 ASN E ND2 
10188 N N   . ARG E 310 ? 0.3148 0.3570 0.2994 -0.0225 -0.1243 -0.0038 310 ARG E N   
10189 C CA  . ARG E 310 ? 0.2748 0.3476 0.3001 -0.0342 -0.1075 0.0016  310 ARG E CA  
10190 C C   . ARG E 310 ? 0.2684 0.3016 0.2807 -0.0560 -0.0952 0.0162  310 ARG E C   
10191 O O   . ARG E 310 ? 0.3052 0.2870 0.2665 -0.0552 -0.1024 0.0230  310 ARG E O   
10192 C CB  . ARG E 310 ? 0.2876 0.3821 0.3079 -0.0031 -0.1153 -0.0039 310 ARG E CB  
10193 C CG  . ARG E 310 ? 0.2466 0.3991 0.3183 -0.0138 -0.0994 -0.0036 310 ARG E CG  
10194 C CD  . ARG E 310 ? 0.2634 0.4389 0.3244 0.0206  -0.1067 -0.0095 310 ARG E CD  
10195 N NE  . ARG E 310 ? 0.2387 0.4216 0.3211 0.0064  -0.0905 -0.0005 310 ARG E NE  
10196 C CZ  . ARG E 310 ? 0.2045 0.4485 0.3346 -0.0150 -0.0754 -0.0017 310 ARG E CZ  
10197 N NH1 . ARG E 310 ? 0.1921 0.4997 0.3542 -0.0311 -0.0736 -0.0119 310 ARG E NH1 
10198 N NH2 . ARG E 310 ? 0.1910 0.4286 0.3297 -0.0250 -0.0626 0.0074  310 ARG E NH2 
10199 N N   . LEU E 311 ? 0.2312 0.2873 0.2812 -0.0758 -0.0784 0.0201  311 LEU E N   
10200 C CA  . LEU E 311 ? 0.2201 0.2631 0.2674 -0.0895 -0.0665 0.0312  311 LEU E CA  
10201 C C   . LEU E 311 ? 0.1910 0.2596 0.2751 -0.0932 -0.0530 0.0331  311 LEU E C   
10202 O O   . LEU E 311 ? 0.1847 0.2608 0.2851 -0.1014 -0.0459 0.0302  311 LEU E O   
10203 C CB  . LEU E 311 ? 0.2234 0.2598 0.2597 -0.1040 -0.0616 0.0331  311 LEU E CB  
10204 C CG  . LEU E 311 ? 0.2599 0.2659 0.2490 -0.1115 -0.0720 0.0341  311 LEU E CG  
10205 C CD1 . LEU E 311 ? 0.2565 0.2787 0.2450 -0.1256 -0.0637 0.0337  311 LEU E CD1 
10206 C CD2 . LEU E 311 ? 0.2932 0.2641 0.2361 -0.1203 -0.0775 0.0430  311 LEU E CD2 
10207 N N   . VAL E 312 ? 0.1852 0.2559 0.2710 -0.0874 -0.0507 0.0381  312 VAL E N   
10208 C CA  . VAL E 312 ? 0.1660 0.2546 0.2778 -0.0918 -0.0388 0.0410  312 VAL E CA  
10209 C C   . VAL E 312 ? 0.1616 0.2378 0.2639 -0.0923 -0.0330 0.0513  312 VAL E C   
10210 O O   . VAL E 312 ? 0.1740 0.2358 0.2542 -0.0868 -0.0394 0.0546  312 VAL E O   
10211 C CB  . VAL E 312 ? 0.1629 0.2851 0.2915 -0.0843 -0.0409 0.0347  312 VAL E CB  
10212 C CG1 . VAL E 312 ? 0.1530 0.2898 0.3008 -0.0976 -0.0275 0.0386  312 VAL E CG1 
10213 C CG2 . VAL E 312 ? 0.1682 0.3202 0.3065 -0.0841 -0.0489 0.0225  312 VAL E CG2 
10214 N N   . LEU E 313 ? 0.1536 0.2309 0.2641 -0.0969 -0.0228 0.0554  313 LEU E N   
10215 C CA  . LEU E 313 ? 0.1487 0.2273 0.2539 -0.0958 -0.0174 0.0637  313 LEU E CA  
10216 C C   . LEU E 313 ? 0.1439 0.2233 0.2608 -0.0932 -0.0109 0.0672  313 LEU E C   
10217 O O   . LEU E 313 ? 0.1507 0.2256 0.2749 -0.0970 -0.0056 0.0650  313 LEU E O   
10218 C CB  . LEU E 313 ? 0.1511 0.2384 0.2526 -0.0922 -0.0119 0.0638  313 LEU E CB  
10219 C CG  . LEU E 313 ? 0.1549 0.2597 0.2425 -0.0985 -0.0153 0.0621  313 LEU E CG  
10220 C CD1 . LEU E 313 ? 0.1608 0.2872 0.2469 -0.0844 -0.0099 0.0576  313 LEU E CD1 
10221 C CD2 . LEU E 313 ? 0.1587 0.2740 0.2286 -0.1136 -0.0180 0.0689  313 LEU E CD2 
10222 N N   . ALA E 314 ? 0.1417 0.2211 0.2518 -0.0908 -0.0116 0.0729  314 ALA E N   
10223 C CA  . ALA E 314 ? 0.1385 0.2197 0.2561 -0.0884 -0.0042 0.0774  314 ALA E CA  
10224 C C   . ALA E 314 ? 0.1433 0.2195 0.2575 -0.0854 0.0024  0.0818  314 ALA E C   
10225 O O   . ALA E 314 ? 0.1419 0.2302 0.2484 -0.0820 0.0009  0.0834  314 ALA E O   
10226 C CB  . ALA E 314 ? 0.1420 0.2185 0.2454 -0.0845 -0.0082 0.0818  314 ALA E CB  
10227 N N   . THR E 315 ? 0.1588 0.2185 0.2712 -0.0868 0.0089  0.0825  315 THR E N   
10228 C CA  . THR E 315 ? 0.1819 0.2206 0.2750 -0.0755 0.0127  0.0866  315 THR E CA  
10229 C C   . THR E 315 ? 0.1863 0.2189 0.2759 -0.0767 0.0178  0.0938  315 THR E C   
10230 O O   . THR E 315 ? 0.1907 0.2246 0.2703 -0.0629 0.0179  0.0985  315 THR E O   
10231 C CB  . THR E 315 ? 0.2244 0.2202 0.2916 -0.0766 0.0135  0.0827  315 THR E CB  
10232 O OG1 . THR E 315 ? 0.2326 0.2221 0.3042 -0.1030 0.0161  0.0805  315 THR E OG1 
10233 C CG2 . THR E 315 ? 0.2269 0.2273 0.2900 -0.0654 0.0083  0.0755  315 THR E CG2 
10234 N N   . GLY E 316 ? 0.1861 0.2222 0.2843 -0.0928 0.0219  0.0935  316 GLY E N   
10235 C CA  . GLY E 316 ? 0.1910 0.2275 0.2860 -0.0958 0.0279  0.0995  316 GLY E CA  
10236 C C   . GLY E 316 ? 0.1639 0.2281 0.2726 -0.0872 0.0244  0.1004  316 GLY E C   
10237 O O   . GLY E 316 ? 0.1505 0.2220 0.2603 -0.0809 0.0167  0.0990  316 GLY E O   
10238 N N   . LEU E 317 ? 0.1670 0.2408 0.2765 -0.0895 0.0296  0.1025  317 LEU E N   
10239 C CA  . LEU E 317 ? 0.1592 0.2427 0.2660 -0.0779 0.0253  0.1035  317 LEU E CA  
10240 C C   . LEU E 317 ? 0.1592 0.2736 0.2747 -0.0723 0.0246  0.0948  317 LEU E C   
10241 O O   . LEU E 317 ? 0.1583 0.3020 0.2893 -0.0826 0.0293  0.0885  317 LEU E O   
10242 C CB  . LEU E 317 ? 0.1686 0.2391 0.2623 -0.0754 0.0304  0.1122  317 LEU E CB  
10243 C CG  . LEU E 317 ? 0.1888 0.2520 0.2758 -0.0866 0.0418  0.1161  317 LEU E CG  
10244 C CD1 . LEU E 317 ? 0.1876 0.2846 0.2824 -0.0891 0.0477  0.1120  317 LEU E CD1 
10245 C CD2 . LEU E 317 ? 0.2076 0.2410 0.2721 -0.0798 0.0431  0.1254  317 LEU E CD2 
10246 N N   . ARG E 318 ? 0.1691 0.2784 0.2680 -0.0549 0.0171  0.0931  318 ARG E N   
10247 C CA  . ARG E 318 ? 0.1810 0.3198 0.2775 -0.0349 0.0128  0.0820  318 ARG E CA  
10248 C C   . ARG E 318 ? 0.1788 0.3708 0.2965 -0.0422 0.0266  0.0788  318 ARG E C   
10249 O O   . ARG E 318 ? 0.1836 0.3693 0.2956 -0.0486 0.0353  0.0860  318 ARG E O   
10250 C CB  . ARG E 318 ? 0.2113 0.3130 0.2660 -0.0120 0.0011  0.0816  318 ARG E CB  
10251 C CG  . ARG E 318 ? 0.2385 0.3618 0.2752 0.0236  -0.0073 0.0673  318 ARG E CG  
10252 C CD  . ARG E 318 ? 0.2906 0.3503 0.2647 0.0469  -0.0214 0.0675  318 ARG E CD  
10253 N NE  . ARG E 318 ? 0.3262 0.3142 0.2524 0.0418  -0.0380 0.0704  318 ARG E NE  
10254 C CZ  . ARG E 318 ? 0.3769 0.3280 0.2544 0.0699  -0.0561 0.0604  318 ARG E CZ  
10255 N NH1 . ARG E 318 ? 0.3941 0.3845 0.2691 0.1142  -0.0612 0.0445  318 ARG E NH1 
10256 N NH2 . ARG E 318 ? 0.4181 0.2954 0.2432 0.0540  -0.0699 0.0656  318 ARG E NH2 
10257 N N   . ASN E 319 ? 0.1765 0.4259 0.3159 -0.0453 0.0286  0.0676  319 ASN E N   
10258 C CA  . ASN E 319 ? 0.1797 0.4956 0.3376 -0.0647 0.0428  0.0633  319 ASN E CA  
10259 C C   . ASN E 319 ? 0.1919 0.5687 0.3479 -0.0317 0.0415  0.0511  319 ASN E C   
10260 O O   . ASN E 319 ? 0.2037 0.5839 0.3457 0.0094  0.0266  0.0402  319 ASN E O   
10261 C CB  . ASN E 319 ? 0.1749 0.5356 0.3544 -0.0915 0.0455  0.0560  319 ASN E CB  
10262 C CG  . ASN E 319 ? 0.1878 0.6049 0.3751 -0.1333 0.0619  0.0552  319 ASN E CG  
10263 O OD1 . ASN E 319 ? 0.1998 0.6159 0.3759 -0.1429 0.0724  0.0617  319 ASN E OD1 
10264 N ND2 . ASN E 319 ? 0.1925 0.6579 0.3931 -0.1638 0.0640  0.0474  319 ASN E ND2 
10265 N N   . SER E 320 ? 0.2017 0.6228 0.3630 -0.0479 0.0563  0.0521  320 SER E N   
10266 C CA  . SER E 320 ? 0.2180 0.6928 0.3717 -0.0129 0.0569  0.0416  320 SER E CA  
10267 C C   . SER E 320 ? 0.2202 0.8249 0.3996 -0.0030 0.0599  0.0207  320 SER E C   
10268 O O   . SER E 320 ? 0.2121 0.8770 0.4177 -0.0477 0.0702  0.0187  320 SER E O   
10269 C CB  . SER E 320 ? 0.2267 0.6888 0.3705 -0.0350 0.0721  0.0531  320 SER E CB  
10270 O OG  . SER E 320 ? 0.2283 0.5865 0.3512 -0.0436 0.0686  0.0707  320 SER E OG  
10271 N N   . PRO E 321 ? 0.2417 0.8910 0.4065 0.0567  0.0494  0.0038  321 PRO E N   
10272 C CA  . PRO E 321 ? 0.2449 1.0414 0.4334 0.0782  0.0515  -0.0198 321 PRO E CA  
10273 C C   . PRO E 321 ? 0.2471 1.1413 0.4497 0.0573  0.0724  -0.0233 321 PRO E C   
10274 O O   . PRO E 321 ? 0.2393 1.1496 0.4589 -0.0118 0.0914  -0.0114 321 PRO E O   
10275 C CB  . PRO E 321 ? 0.2824 1.0585 0.4295 0.1632  0.0277  -0.0361 321 PRO E CB  
10276 C CG  . PRO E 321 ? 0.3065 0.9470 0.4048 0.1756  0.0219  -0.0205 321 PRO E CG  
10277 C CD  . PRO E 321 ? 0.2744 0.8322 0.3887 0.1105  0.0317  0.0043  321 PRO E CD  
10278 N N   . GLY F 1   ? 0.3187 0.1671 0.2079 0.1344  0.0264  0.0759  1   GLY F N   
10279 C CA  . GLY F 1   ? 0.2802 0.1456 0.2006 0.0998  0.0051  0.0587  1   GLY F CA  
10280 C C   . GLY F 1   ? 0.3206 0.1305 0.1937 0.0768  -0.0020 0.0465  1   GLY F C   
10281 O O   . GLY F 1   ? 0.3747 0.1281 0.1932 0.0810  0.0052  0.0481  1   GLY F O   
10282 N N   . LEU F 2   ? 0.2983 0.1285 0.1899 0.0506  -0.0169 0.0364  2   LEU F N   
10283 C CA  . LEU F 2   ? 0.3380 0.1330 0.1863 0.0198  -0.0263 0.0289  2   LEU F CA  
10284 C C   . LEU F 2   ? 0.3547 0.1362 0.1863 0.0076  -0.0339 0.0269  2   LEU F C   
10285 O O   . LEU F 2   ? 0.4166 0.1440 0.1851 -0.0153 -0.0368 0.0253  2   LEU F O   
10286 C CB  . LEU F 2   ? 0.2993 0.1471 0.1857 -0.0030 -0.0410 0.0229  2   LEU F CB  
10287 C CG  . LEU F 2   ? 0.3074 0.1482 0.1845 -0.0056 -0.0364 0.0229  2   LEU F CG  
10288 C CD1 . LEU F 2   ? 0.2645 0.1685 0.1856 -0.0241 -0.0499 0.0186  2   LEU F CD1 
10289 C CD2 . LEU F 2   ? 0.3927 0.1502 0.1827 -0.0214 -0.0298 0.0235  2   LEU F CD2 
10290 N N   . PHE F 3   ? 0.3086 0.1330 0.1883 0.0197  -0.0378 0.0274  3   PHE F N   
10291 C CA  . PHE F 3   ? 0.3165 0.1394 0.1888 0.0088  -0.0472 0.0254  3   PHE F CA  
10292 C C   . PHE F 3   ? 0.3485 0.1270 0.1900 0.0273  -0.0351 0.0305  3   PHE F C   
10293 O O   . PHE F 3   ? 0.3627 0.1300 0.1899 0.0193  -0.0415 0.0291  3   PHE F O   
10294 C CB  . PHE F 3   ? 0.2596 0.1496 0.1909 0.0098  -0.0601 0.0227  3   PHE F CB  
10295 C CG  . PHE F 3   ? 0.2398 0.1745 0.1919 -0.0058 -0.0706 0.0202  3   PHE F CG  
10296 C CD1 . PHE F 3   ? 0.2576 0.2127 0.1945 -0.0325 -0.0836 0.0214  3   PHE F CD1 
10297 C CD2 . PHE F 3   ? 0.2089 0.1688 0.1917 0.0034  -0.0675 0.0192  3   PHE F CD2 
10298 C CE1 . PHE F 3   ? 0.2412 0.2500 0.1983 -0.0468 -0.0919 0.0232  3   PHE F CE1 
10299 C CE2 . PHE F 3   ? 0.1946 0.1958 0.1935 -0.0086 -0.0750 0.0183  3   PHE F CE2 
10300 C CZ  . PHE F 3   ? 0.2095 0.2390 0.1974 -0.0326 -0.0865 0.0210  3   PHE F CZ  
10301 N N   . GLY F 4   ? 0.3625 0.1214 0.1926 0.0541  -0.0167 0.0386  4   GLY F N   
10302 C CA  . GLY F 4   ? 0.4104 0.1212 0.1957 0.0774  0.0001  0.0472  4   GLY F CA  
10303 C C   . GLY F 4   ? 0.3786 0.1244 0.2006 0.0911  0.0018  0.0530  4   GLY F C   
10304 O O   . GLY F 4   ? 0.4174 0.1302 0.2042 0.1117  0.0167  0.0618  4   GLY F O   
10305 N N   . ALA F 5   ? 0.3188 0.1241 0.2019 0.0808  -0.0119 0.0491  5   ALA F N   
10306 C CA  . ALA F 5   ? 0.2984 0.1274 0.2065 0.0861  -0.0129 0.0536  5   ALA F CA  
10307 C C   . ALA F 5   ? 0.2753 0.1488 0.2155 0.1005  -0.0029 0.0681  5   ALA F C   
10308 O O   . ALA F 5   ? 0.2925 0.1687 0.2223 0.1178  0.0111  0.0820  5   ALA F O   
10309 C CB  . ALA F 5   ? 0.2667 0.1208 0.2041 0.0692  -0.0320 0.0433  5   ALA F CB  
10310 N N   . ILE F 6   ? 0.2407 0.1537 0.2172 0.0921  -0.0102 0.0669  6   ILE F N   
10311 C CA  . ILE F 6   ? 0.2211 0.1855 0.2276 0.0962  -0.0051 0.0825  6   ILE F CA  
10312 C C   . ILE F 6   ? 0.2440 0.2160 0.2350 0.1234  0.0150  0.0992  6   ILE F C   
10313 O O   . ILE F 6   ? 0.2620 0.2061 0.2308 0.1319  0.0197  0.0945  6   ILE F O   
10314 C CB  . ILE F 6   ? 0.1893 0.1824 0.2264 0.0785  -0.0186 0.0764  6   ILE F CB  
10315 C CG1 . ILE F 6   ? 0.1828 0.1646 0.2235 0.0611  -0.0343 0.0649  6   ILE F CG1 
10316 C CG2 . ILE F 6   ? 0.1761 0.2245 0.2375 0.0772  -0.0146 0.0951  6   ILE F CG2 
10317 C CD1 . ILE F 6   ? 0.1685 0.1603 0.2222 0.0482  -0.0461 0.0579  6   ILE F CD1 
10318 N N   . ALA F 7   ? 0.2506 0.2614 0.2482 0.1387  0.0277  0.1208  7   ALA F N   
10319 C CA  . ALA F 7   ? 0.2812 0.3065 0.2588 0.1764  0.0512  0.1423  7   ALA F CA  
10320 C C   . ALA F 7   ? 0.3434 0.2804 0.2525 0.2005  0.0651  0.1346  7   ALA F C   
10321 O O   . ALA F 7   ? 0.3832 0.2980 0.2556 0.2309  0.0823  0.1438  7   ALA F O   
10322 C CB  . ALA F 7   ? 0.2608 0.3331 0.2634 0.1796  0.0511  0.1509  7   ALA F CB  
10323 N N   . GLY F 8   ? 0.3618 0.2426 0.2447 0.1855  0.0574  0.1186  8   GLY F N   
10324 C CA  . GLY F 8   ? 0.4309 0.2171 0.2380 0.1939  0.0649  0.1090  8   GLY F CA  
10325 C C   . GLY F 8   ? 0.4694 0.2199 0.2411 0.2047  0.0734  0.1129  8   GLY F C   
10326 O O   . GLY F 8   ? 0.4993 0.2600 0.2525 0.2412  0.0959  0.1336  8   GLY F O   
10327 N N   . PHE F 9   ? 0.4719 0.1862 0.2331 0.1754  0.0564  0.0954  9   PHE F N   
10328 C CA  . PHE F 9   ? 0.5043 0.1869 0.2356 0.1817  0.0617  0.0978  9   PHE F CA  
10329 C C   . PHE F 9   ? 0.4478 0.2056 0.2439 0.1762  0.0562  0.1057  9   PHE F C   
10330 O O   . PHE F 9   ? 0.4690 0.2215 0.2503 0.1893  0.0664  0.1152  9   PHE F O   
10331 C CB  . PHE F 9   ? 0.5391 0.1534 0.2248 0.1524  0.0456  0.0792  9   PHE F CB  
10332 C CG  . PHE F 9   ? 0.4781 0.1373 0.2195 0.1179  0.0188  0.0655  9   PHE F CG  
10333 C CD1 . PHE F 9   ? 0.4559 0.1357 0.2209 0.1134  0.0118  0.0651  9   PHE F CD1 
10334 C CD2 . PHE F 9   ? 0.4523 0.1293 0.2141 0.0938  0.0023  0.0544  9   PHE F CD2 
10335 C CE1 . PHE F 9   ? 0.4141 0.1269 0.2177 0.0907  -0.0098 0.0544  9   PHE F CE1 
10336 C CE2 . PHE F 9   ? 0.4060 0.1257 0.2117 0.0721  -0.0187 0.0452  9   PHE F CE2 
10337 C CZ  . PHE F 9   ? 0.3899 0.1246 0.2136 0.0732  -0.0242 0.0453  9   PHE F CZ  
10338 N N   . ILE F 10  ? 0.3874 0.2068 0.2455 0.1550  0.0406  0.1021  10  ILE F N   
10339 C CA  . ILE F 10  ? 0.3490 0.2349 0.2557 0.1462  0.0369  0.1135  10  ILE F CA  
10340 C C   . ILE F 10  ? 0.3349 0.2869 0.2690 0.1609  0.0489  0.1350  10  ILE F C   
10341 O O   . ILE F 10  ? 0.3053 0.2855 0.2676 0.1486  0.0396  0.1314  10  ILE F O   
10342 C CB  . ILE F 10  ? 0.3100 0.2087 0.2497 0.1134  0.0125  0.0977  10  ILE F CB  
10343 C CG1 . ILE F 10  ? 0.3252 0.1724 0.2400 0.1036  0.0005  0.0799  10  ILE F CG1 
10344 C CG2 . ILE F 10  ? 0.2920 0.2383 0.2598 0.0981  0.0085  0.1099  10  ILE F CG2 
10345 C CD1 . ILE F 10  ? 0.2986 0.1538 0.2351 0.0835  -0.0199 0.0658  10  ILE F CD1 
10346 N N   . GLU F 11  ? 0.3590 0.3421 0.2843 0.1890  0.0701  0.1597  11  GLU F N   
10347 C CA  . GLU F 11  ? 0.3589 0.4085 0.3000 0.2152  0.0866  0.1857  11  GLU F CA  
10348 C C   . GLU F 11  ? 0.3079 0.4472 0.3090 0.1853  0.0722  0.1962  11  GLU F C   
10349 O O   . GLU F 11  ? 0.2990 0.4831 0.3159 0.1975  0.0773  0.2087  11  GLU F O   
10350 C CB  . GLU F 11  ? 0.3969 0.4771 0.3176 0.2556  0.1139  0.2153  11  GLU F CB  
10351 C CG  . GLU F 11  ? 0.4708 0.4526 0.3124 0.2951  0.1344  0.2102  11  GLU F CG  
10352 C CD  . GLU F 11  ? 0.5200 0.5361 0.3325 0.3538  0.1690  0.2453  11  GLU F CD  
10353 O OE1 . GLU F 11  ? 0.5137 0.5896 0.3466 0.3579  0.1767  0.2657  11  GLU F OE1 
10354 O OE2 . GLU F 11  ? 0.5704 0.5544 0.3357 0.3980  0.1895  0.2543  11  GLU F OE2 
10355 N N   . GLY F 12  ? 0.2854 0.4428 0.3101 0.1454  0.0540  0.1917  12  GLY F N   
10356 C CA  . GLY F 12  ? 0.2558 0.4840 0.3200 0.1084  0.0385  0.2026  12  GLY F CA  
10357 C C   . GLY F 12  ? 0.2510 0.4454 0.3135 0.0627  0.0148  0.1846  12  GLY F C   
10358 O O   . GLY F 12  ? 0.2657 0.4012 0.3048 0.0615  0.0119  0.1693  12  GLY F O   
10359 N N   . GLY F 13  ? 0.2400 0.4662 0.3186 0.0266  -0.0014 0.1876  13  GLY F N   
10360 C CA  . GLY F 13  ? 0.2550 0.4355 0.3142 -0.0145 -0.0224 0.1722  13  GLY F CA  
10361 C C   . GLY F 13  ? 0.2812 0.4864 0.3287 -0.0465 -0.0260 0.1904  13  GLY F C   
10362 O O   . GLY F 13  ? 0.2803 0.5534 0.3437 -0.0369 -0.0119 0.2171  13  GLY F O   
10363 N N   . TRP F 14  ? 0.3132 0.4604 0.3256 -0.0830 -0.0437 0.1773  14  TRP F N   
10364 C CA  . TRP F 14  ? 0.3527 0.5004 0.3377 -0.1210 -0.0498 0.1909  14  TRP F CA  
10365 C C   . TRP F 14  ? 0.3896 0.5428 0.3475 -0.1800 -0.0689 0.2008  14  TRP F C   
10366 O O   . TRP F 14  ? 0.4243 0.4930 0.3372 -0.1965 -0.0831 0.1797  14  TRP F O   
10367 C CB  . TRP F 14  ? 0.3833 0.4336 0.3260 -0.1137 -0.0535 0.1673  14  TRP F CB  
10368 C CG  . TRP F 14  ? 0.3630 0.4030 0.3195 -0.0682 -0.0378 0.1604  14  TRP F CG  
10369 C CD1 . TRP F 14  ? 0.3415 0.4415 0.3276 -0.0395 -0.0187 0.1782  14  TRP F CD1 
10370 C CD2 . TRP F 14  ? 0.3745 0.3355 0.3053 -0.0463 -0.0397 0.1359  14  TRP F CD2 
10371 N NE1 . TRP F 14  ? 0.3442 0.3951 0.3178 -0.0056 -0.0095 0.1641  14  TRP F NE1 
10372 C CE2 . TRP F 14  ? 0.3595 0.3325 0.3042 -0.0120 -0.0236 0.1388  14  TRP F CE2 
10373 C CE3 . TRP F 14  ? 0.4028 0.2856 0.2951 -0.0497 -0.0527 0.1141  14  TRP F CE3 
10374 C CZ2 . TRP F 14  ? 0.3680 0.2817 0.2924 0.0101  -0.0233 0.1204  14  TRP F CZ2 
10375 C CZ3 . TRP F 14  ? 0.4049 0.2420 0.2848 -0.0215 -0.0510 0.0982  14  TRP F CZ3 
10376 C CH2 . TRP F 14  ? 0.3854 0.2403 0.2831 0.0037  -0.0380 0.1013  14  TRP F CH2 
10377 N N   . GLN F 15  ? 0.3903 0.6436 0.3688 -0.2118 -0.0689 0.2353  15  GLN F N   
10378 C CA  . GLN F 15  ? 0.4408 0.7041 0.3826 -0.2827 -0.0895 0.2507  15  GLN F CA  
10379 C C   . GLN F 15  ? 0.5154 0.6701 0.3786 -0.3207 -0.1022 0.2372  15  GLN F C   
10380 O O   . GLN F 15  ? 0.5809 0.6668 0.3791 -0.3691 -0.1210 0.2310  15  GLN F O   
10381 C CB  . GLN F 15  ? 0.4311 0.8399 0.4110 -0.3119 -0.0862 0.2965  15  GLN F CB  
10382 C CG  . GLN F 15  ? 0.3720 0.8959 0.4197 -0.2752 -0.0734 0.3168  15  GLN F CG  
10383 C CD  . GLN F 15  ? 0.3822 0.9457 0.4287 -0.3192 -0.0919 0.3277  15  GLN F CD  
10384 O OE1 . GLN F 15  ? 0.3465 0.9212 0.4219 -0.2855 -0.0875 0.3195  15  GLN F OE1 
10385 N NE2 . GLN F 15  ? 0.4391 1.0204 0.4456 -0.3985 -0.1133 0.3472  15  GLN F NE2 
10386 N N   . GLY F 16  ? 0.5146 0.6447 0.3743 -0.2968 -0.0911 0.2328  16  GLY F N   
10387 C CA  . GLY F 16  ? 0.5881 0.6163 0.3715 -0.3261 -0.1002 0.2221  16  GLY F CA  
10388 C C   . GLY F 16  ? 0.6272 0.5141 0.3505 -0.3042 -0.1066 0.1854  16  GLY F C   
10389 O O   . GLY F 16  ? 0.7046 0.4944 0.3496 -0.3270 -0.1144 0.1772  16  GLY F O   
10390 N N   . MET F 17  ? 0.5806 0.4564 0.3353 -0.2579 -0.1023 0.1653  17  MET F N   
10391 C CA  . MET F 17  ? 0.6169 0.3780 0.3187 -0.2328 -0.1071 0.1354  17  MET F CA  
10392 C C   . MET F 17  ? 0.6529 0.3785 0.3180 -0.2567 -0.1194 0.1305  17  MET F C   
10393 O O   . MET F 17  ? 0.5973 0.3730 0.3137 -0.2370 -0.1168 0.1279  17  MET F O   
10394 C CB  . MET F 17  ? 0.5493 0.3206 0.3034 -0.1676 -0.0949 0.1172  17  MET F CB  
10395 C CG  . MET F 17  ? 0.5869 0.2594 0.2904 -0.1365 -0.0979 0.0921  17  MET F CG  
10396 S SD  . MET F 17  ? 0.5150 0.2139 0.2764 -0.0737 -0.0868 0.0768  17  MET F SD  
10397 C CE  . MET F 17  ? 0.4450 0.2241 0.2748 -0.0673 -0.0833 0.0800  17  MET F CE  
10398 N N   . VAL F 18  ? 0.7564 0.3840 0.3222 -0.2990 -0.1323 0.1289  18  VAL F N   
10399 C CA  . VAL F 18  ? 0.8148 0.3957 0.3246 -0.3338 -0.1455 0.1278  18  VAL F CA  
10400 C C   . VAL F 18  ? 0.8829 0.3304 0.3116 -0.2995 -0.1457 0.1016  18  VAL F C   
10401 O O   . VAL F 18  ? 0.9161 0.3276 0.3103 -0.3086 -0.1521 0.0965  18  VAL F O   
10402 C CB  . VAL F 18  ? 0.9072 0.4680 0.3426 -0.4197 -0.1622 0.1498  18  VAL F CB  
10403 C CG1 . VAL F 18  ? 0.8432 0.5521 0.3593 -0.4499 -0.1602 0.1815  18  VAL F CG1 
10404 C CG2 . VAL F 18  ? 1.0282 0.4450 0.3423 -0.4376 -0.1667 0.1409  18  VAL F CG2 
10405 N N   . ASP F 19  ? 0.9072 0.2856 0.3034 -0.2570 -0.1377 0.0871  19  ASP F N   
10406 C CA  . ASP F 19  ? 0.9883 0.2405 0.2949 -0.2179 -0.1353 0.0674  19  ASP F CA  
10407 C C   . ASP F 19  ? 0.9068 0.2017 0.2825 -0.1451 -0.1237 0.0526  19  ASP F C   
10408 O O   . ASP F 19  ? 0.9588 0.1756 0.2774 -0.0980 -0.1179 0.0397  19  ASP F O   
10409 C CB  . ASP F 19  ? 1.0849 0.2278 0.2964 -0.2135 -0.1338 0.0636  19  ASP F CB  
10410 C CG  . ASP F 19  ? 1.0091 0.2206 0.2943 -0.1878 -0.1254 0.0658  19  ASP F CG  
10411 O OD1 . ASP F 19  ? 0.8911 0.2273 0.2924 -0.1764 -0.1204 0.0710  19  ASP F OD1 
10412 O OD2 . ASP F 19  ? 1.0773 0.2092 0.2948 -0.1786 -0.1233 0.0626  19  ASP F OD2 
10413 N N   . GLY F 20  ? 0.7880 0.2063 0.2792 -0.1355 -0.1197 0.0567  20  GLY F N   
10414 C CA  . GLY F 20  ? 0.7161 0.1790 0.2690 -0.0795 -0.1111 0.0450  20  GLY F CA  
10415 C C   . GLY F 20  ? 0.6069 0.1888 0.2671 -0.0805 -0.1077 0.0513  20  GLY F C   
10416 O O   . GLY F 20  ? 0.5786 0.2201 0.2744 -0.1147 -0.1092 0.0666  20  GLY F O   
10417 N N   . TRP F 21  ? 0.5527 0.1696 0.2588 -0.0412 -0.1021 0.0417  21  TRP F N   
10418 C CA  . TRP F 21  ? 0.4629 0.1744 0.2558 -0.0369 -0.0975 0.0459  21  TRP F CA  
10419 C C   . TRP F 21  ? 0.4101 0.1670 0.2520 -0.0170 -0.0897 0.0470  21  TRP F C   
10420 O O   . TRP F 21  ? 0.3641 0.1822 0.2542 -0.0249 -0.0845 0.0572  21  TRP F O   
10421 C CB  . TRP F 21  ? 0.4383 0.1620 0.2498 -0.0109 -0.0958 0.0360  21  TRP F CB  
10422 C CG  . TRP F 21  ? 0.4473 0.1759 0.2532 -0.0359 -0.1010 0.0398  21  TRP F CG  
10423 C CD1 . TRP F 21  ? 0.4379 0.2068 0.2608 -0.0755 -0.1056 0.0544  21  TRP F CD1 
10424 C CD2 . TRP F 21  ? 0.4676 0.1685 0.2505 -0.0217 -0.1019 0.0312  21  TRP F CD2 
10425 N NE1 . TRP F 21  ? 0.4523 0.2159 0.2621 -0.0903 -0.1112 0.0544  21  TRP F NE1 
10426 C CE2 . TRP F 21  ? 0.4717 0.1882 0.2551 -0.0573 -0.1085 0.0391  21  TRP F CE2 
10427 C CE3 . TRP F 21  ? 0.4849 0.1564 0.2464 0.0194  -0.0971 0.0202  21  TRP F CE3 
10428 C CZ2 . TRP F 21  ? 0.4945 0.1859 0.2537 -0.0544 -0.1107 0.0334  21  TRP F CZ2 
10429 C CZ3 . TRP F 21  ? 0.5074 0.1584 0.2460 0.0260  -0.0973 0.0160  21  TRP F CZ3 
10430 C CH2 . TRP F 21  ? 0.5130 0.1679 0.2487 -0.0114 -0.1042 0.0211  21  TRP F CH2 
10431 N N   . TYR F 22  ? 0.4241 0.1490 0.2470 0.0113  -0.0883 0.0381  22  TYR F N   
10432 C CA  . TYR F 22  ? 0.3879 0.1429 0.2435 0.0273  -0.0829 0.0383  22  TYR F CA  
10433 C C   . TYR F 22  ? 0.4376 0.1402 0.2463 0.0298  -0.0843 0.0381  22  TYR F C   
10434 O O   . TYR F 22  ? 0.4990 0.1374 0.2477 0.0366  -0.0882 0.0335  22  TYR F O   
10435 C CB  . TYR F 22  ? 0.3533 0.1357 0.2365 0.0576  -0.0817 0.0297  22  TYR F CB  
10436 C CG  . TYR F 22  ? 0.3308 0.1376 0.2338 0.0611  -0.0824 0.0262  22  TYR F CG  
10437 C CD1 . TYR F 22  ? 0.2902 0.1392 0.2326 0.0469  -0.0792 0.0307  22  TYR F CD1 
10438 C CD2 . TYR F 22  ? 0.3557 0.1428 0.2335 0.0832  -0.0846 0.0202  22  TYR F CD2 
10439 C CE1 . TYR F 22  ? 0.2723 0.1407 0.2303 0.0494  -0.0799 0.0274  22  TYR F CE1 
10440 C CE2 . TYR F 22  ? 0.3372 0.1473 0.2318 0.0868  -0.0844 0.0177  22  TYR F CE2 
10441 C CZ  . TYR F 22  ? 0.2940 0.1432 0.2296 0.0674  -0.0829 0.0204  22  TYR F CZ  
10442 O OH  . TYR F 22  ? 0.2781 0.1474 0.2282 0.0704  -0.0827 0.0178  22  TYR F OH  
10443 N N   . GLY F 23  ? 0.4206 0.1424 0.2477 0.0275  -0.0799 0.0433  23  GLY F N   
10444 C CA  . GLY F 23  ? 0.4657 0.1399 0.2505 0.0308  -0.0809 0.0431  23  GLY F CA  
10445 C C   . GLY F 23  ? 0.4430 0.1432 0.2518 0.0299  -0.0745 0.0493  23  GLY F C   
10446 O O   . GLY F 23  ? 0.3960 0.1441 0.2488 0.0354  -0.0683 0.0518  23  GLY F O   
10447 N N   . TYR F 24  ? 0.4881 0.1461 0.2569 0.0235  -0.0750 0.0522  24  TYR F N   
10448 C CA  . TYR F 24  ? 0.4797 0.1493 0.2589 0.0264  -0.0686 0.0574  24  TYR F CA  
10449 C C   . TYR F 24  ? 0.5040 0.1761 0.2696 -0.0050 -0.0646 0.0727  24  TYR F C   
10450 O O   . TYR F 24  ? 0.5506 0.1891 0.2758 -0.0325 -0.0709 0.0768  24  TYR F O   
10451 C CB  . TYR F 24  ? 0.5117 0.1363 0.2559 0.0493  -0.0725 0.0492  24  TYR F CB  
10452 C CG  . TYR F 24  ? 0.5092 0.1323 0.2517 0.0786  -0.0786 0.0390  24  TYR F CG  
10453 C CD1 . TYR F 24  ? 0.5521 0.1346 0.2539 0.0879  -0.0829 0.0349  24  TYR F CD1 
10454 C CD2 . TYR F 24  ? 0.4737 0.1356 0.2473 0.0964  -0.0799 0.0357  24  TYR F CD2 
10455 C CE1 . TYR F 24  ? 0.5516 0.1450 0.2526 0.1213  -0.0859 0.0298  24  TYR F CE1 
10456 C CE2 . TYR F 24  ? 0.4703 0.1505 0.2465 0.1205  -0.0860 0.0313  24  TYR F CE2 
10457 C CZ  . TYR F 24  ? 0.5056 0.1577 0.2497 0.1366  -0.0878 0.0293  24  TYR F CZ  
10458 O OH  . TYR F 24  ? 0.5049 0.1861 0.2518 0.1671  -0.0912 0.0289  24  TYR F OH  
10459 N N   . HIS F 25  ? 0.4815 0.1916 0.2738 -0.0023 -0.0539 0.0829  25  HIS F N   
10460 C CA  . HIS F 25  ? 0.5071 0.2278 0.2863 -0.0265 -0.0484 0.1002  25  HIS F CA  
10461 C C   . HIS F 25  ? 0.5168 0.2168 0.2843 -0.0078 -0.0414 0.0989  25  HIS F C   
10462 O O   . HIS F 25  ? 0.4885 0.2069 0.2792 0.0174  -0.0329 0.0968  25  HIS F O   
10463 C CB  . HIS F 25  ? 0.4756 0.2784 0.2976 -0.0382 -0.0379 0.1214  25  HIS F CB  
10464 C CG  . HIS F 25  ? 0.5004 0.3352 0.3137 -0.0648 -0.0319 0.1447  25  HIS F CG  
10465 N ND1 . HIS F 25  ? 0.4960 0.3562 0.3193 -0.0461 -0.0161 0.1564  25  HIS F ND1 
10466 C CD2 . HIS F 25  ? 0.5382 0.3826 0.3274 -0.1119 -0.0397 0.1599  25  HIS F CD2 
10467 C CE1 . HIS F 25  ? 0.5212 0.4176 0.3356 -0.0775 -0.0134 0.1793  25  HIS F CE1 
10468 N NE2 . HIS F 25  ? 0.5477 0.4365 0.3410 -0.1218 -0.0288 0.1823  25  HIS F NE2 
10469 N N   . HIS F 26  ? 0.5673 0.2203 0.2891 -0.0228 -0.0452 0.1005  26  HIS F N   
10470 C CA  . HIS F 26  ? 0.5843 0.2104 0.2877 -0.0074 -0.0400 0.0992  26  HIS F CA  
10471 C C   . HIS F 26  ? 0.6004 0.2561 0.3009 -0.0299 -0.0294 0.1207  26  HIS F C   
10472 O O   . HIS F 26  ? 0.6162 0.2978 0.3124 -0.0659 -0.0315 0.1357  26  HIS F O   
10473 C CB  . HIS F 26  ? 0.6355 0.1823 0.2831 -0.0006 -0.0513 0.0853  26  HIS F CB  
10474 C CG  . HIS F 26  ? 0.7025 0.1990 0.2920 -0.0345 -0.0569 0.0915  26  HIS F CG  
10475 N ND1 . HIS F 26  ? 0.7396 0.1992 0.2941 -0.0516 -0.0663 0.0876  26  HIS F ND1 
10476 C CD2 . HIS F 26  ? 0.7509 0.2187 0.3002 -0.0579 -0.0547 0.1016  26  HIS F CD2 
10477 C CE1 . HIS F 26  ? 0.8145 0.2171 0.3022 -0.0871 -0.0705 0.0948  26  HIS F CE1 
10478 N NE2 . HIS F 26  ? 0.8201 0.2307 0.3066 -0.0929 -0.0639 0.1038  26  HIS F NE2 
10479 N N   . SER F 27  ? 0.6004 0.2561 0.3006 -0.0107 -0.0183 0.1243  27  SER F N   
10480 C CA  . SER F 27  ? 0.6222 0.3043 0.3142 -0.0273 -0.0067 0.1458  27  SER F CA  
10481 C C   . SER F 27  ? 0.6483 0.2806 0.3094 -0.0078 -0.0023 0.1394  27  SER F C   
10482 O O   . SER F 27  ? 0.6320 0.2548 0.3006 0.0246  0.0036  0.1310  27  SER F O   
10483 C CB  . SER F 27  ? 0.5875 0.3603 0.3253 -0.0187 0.0116  0.1690  27  SER F CB  
10484 O OG  . SER F 27  ? 0.5720 0.3402 0.3184 0.0237  0.0254  0.1643  27  SER F OG  
10485 N N   . ASN F 28  ? 0.6975 0.2913 0.3156 -0.0314 -0.0064 0.1438  28  ASN F N   
10486 C CA  . ASN F 28  ? 0.7291 0.2715 0.3121 -0.0165 -0.0035 0.1385  28  ASN F CA  
10487 C C   . ASN F 28  ? 0.7744 0.3189 0.3273 -0.0495 0.0019  0.1580  28  ASN F C   
10488 O O   . ASN F 28  ? 0.7747 0.3774 0.3420 -0.0834 0.0049  0.1787  28  ASN F O   
10489 C CB  . ASN F 28  ? 0.7531 0.2173 0.2989 -0.0012 -0.0200 0.1148  28  ASN F CB  
10490 C CG  . ASN F 28  ? 0.8026 0.2148 0.3013 -0.0271 -0.0332 0.1111  28  ASN F CG  
10491 O OD1 . ASN F 28  ? 0.8309 0.2517 0.3126 -0.0670 -0.0327 0.1256  28  ASN F OD1 
10492 N ND2 . ASN F 28  ? 0.8225 0.1791 0.2920 -0.0044 -0.0449 0.0936  28  ASN F ND2 
10493 N N   . GLU F 29  ? 0.8148 0.3027 0.3258 -0.0426 0.0026  0.1535  29  GLU F N   
10494 C CA  . GLU F 29  ? 0.8631 0.3489 0.3404 -0.0754 0.0081  0.1721  29  GLU F CA  
10495 C C   . GLU F 29  ? 0.9143 0.3730 0.3490 -0.1285 -0.0055 0.1777  29  GLU F C   
10496 O O   . GLU F 29  ? 0.9366 0.4422 0.3666 -0.1719 -0.0012 0.2026  29  GLU F O   
10497 C CB  . GLU F 29  ? 0.9049 0.3172 0.3350 -0.0578 0.0083  0.1622  29  GLU F CB  
10498 C CG  . GLU F 29  ? 0.8781 0.3091 0.3308 -0.0173 0.0235  0.1623  29  GLU F CG  
10499 C CD  . GLU F 29  ? 0.9262 0.2996 0.3308 -0.0110 0.0266  0.1609  29  GLU F CD  
10500 O OE1 . GLU F 29  ? 0.9789 0.2862 0.3311 -0.0298 0.0146  0.1546  29  GLU F OE1 
10501 O OE2 . GLU F 29  ? 0.9202 0.3057 0.3307 0.0146  0.0418  0.1662  29  GLU F OE2 
10502 N N   . GLN F 30  ? 0.9420 0.3237 0.3381 -0.1255 -0.0217 0.1567  30  GLN F N   
10503 C CA  . GLN F 30  ? 1.0152 0.3374 0.3444 -0.1730 -0.0353 0.1585  30  GLN F CA  
10504 C C   . GLN F 30  ? 0.9925 0.3842 0.3534 -0.2118 -0.0389 0.1731  30  GLN F C   
10505 O O   . GLN F 30  ? 1.0577 0.4259 0.3654 -0.2695 -0.0479 0.1854  30  GLN F O   
10506 C CB  . GLN F 30  ? 1.0617 0.2757 0.3316 -0.1450 -0.0476 0.1330  30  GLN F CB  
10507 C CG  . GLN F 30  ? 1.1044 0.2428 0.3256 -0.1136 -0.0469 0.1222  30  GLN F CG  
10508 C CD  . GLN F 30  ? 1.0718 0.1953 0.3116 -0.0534 -0.0507 0.1020  30  GLN F CD  
10509 O OE1 . GLN F 30  ? 1.0021 0.1859 0.3056 -0.0237 -0.0451 0.0995  30  GLN F OE1 
10510 N NE2 . GLN F 30  ? 1.1316 0.1735 0.3079 -0.0355 -0.0599 0.0898  30  GLN F NE2 
10511 N N   . GLY F 31  ? 0.9085 0.3807 0.3480 -0.1834 -0.0331 0.1723  31  GLY F N   
10512 C CA  . GLY F 31  ? 0.8808 0.4302 0.3573 -0.2150 -0.0357 0.1878  31  GLY F CA  
10513 C C   . GLY F 31  ? 0.8073 0.3956 0.3450 -0.1750 -0.0342 0.1751  31  GLY F C   
10514 O O   . GLY F 31  ? 0.7684 0.3469 0.3317 -0.1249 -0.0282 0.1594  31  GLY F O   
10515 N N   . SER F 32  ? 0.7940 0.4262 0.3504 -0.2021 -0.0407 0.1832  32  SER F N   
10516 C CA  . SER F 32  ? 0.7324 0.3962 0.3397 -0.1705 -0.0407 0.1716  32  SER F CA  
10517 C C   . SER F 32  ? 0.7654 0.3920 0.3392 -0.2022 -0.0569 0.1653  32  SER F C   
10518 O O   . SER F 32  ? 0.8349 0.4282 0.3500 -0.2563 -0.0672 0.1757  32  SER F O   
10519 C CB  . SER F 32  ? 0.6664 0.4522 0.3494 -0.1585 -0.0251 0.1938  32  SER F CB  
10520 O OG  . SER F 32  ? 0.6825 0.5443 0.3707 -0.2090 -0.0258 0.2248  32  SER F OG  
10521 N N   . GLY F 33  ? 0.7245 0.3509 0.3272 -0.1714 -0.0594 0.1489  33  GLY F N   
10522 C CA  . GLY F 33  ? 0.7571 0.3456 0.3263 -0.1955 -0.0730 0.1424  33  GLY F CA  
10523 C C   . GLY F 33  ? 0.7055 0.3021 0.3130 -0.1560 -0.0736 0.1249  33  GLY F C   
10524 O O   . GLY F 33  ? 0.6567 0.2651 0.3021 -0.1091 -0.0664 0.1129  33  GLY F O   
10525 N N   . TYR F 34  ? 0.7238 0.3118 0.3151 -0.1802 -0.0832 0.1246  34  TYR F N   
10526 C CA  . TYR F 34  ? 0.6845 0.2767 0.3042 -0.1487 -0.0846 0.1093  34  TYR F CA  
10527 C C   . TYR F 34  ? 0.7526 0.2341 0.2965 -0.1316 -0.0923 0.0896  34  TYR F C   
10528 O O   . TYR F 34  ? 0.8456 0.2429 0.3023 -0.1634 -0.1002 0.0909  34  TYR F O   
10529 C CB  . TYR F 34  ? 0.6646 0.3181 0.3120 -0.1815 -0.0892 0.1225  34  TYR F CB  
10530 C CG  . TYR F 34  ? 0.6017 0.3757 0.3227 -0.1894 -0.0791 0.1465  34  TYR F CG  
10531 C CD1 . TYR F 34  ? 0.5252 0.3624 0.3161 -0.1452 -0.0665 0.1444  34  TYR F CD1 
10532 C CD2 . TYR F 34  ? 0.6286 0.4530 0.3412 -0.2404 -0.0814 0.1740  34  TYR F CD2 
10533 C CE1 . TYR F 34  ? 0.4823 0.4207 0.3274 -0.1420 -0.0537 0.1684  34  TYR F CE1 
10534 C CE2 . TYR F 34  ? 0.5751 0.5217 0.3543 -0.2386 -0.0693 0.2007  34  TYR F CE2 
10535 C CZ  . TYR F 34  ? 0.5047 0.5033 0.3472 -0.1846 -0.0541 0.1975  34  TYR F CZ  
10536 O OH  . TYR F 34  ? 0.4655 0.5763 0.3614 -0.1729 -0.0386 0.2258  34  TYR F OH  
10537 N N   . ALA F 35  ? 0.7156 0.1965 0.2857 -0.0809 -0.0891 0.0736  35  ALA F N   
10538 C CA  . ALA F 35  ? 0.7743 0.1702 0.2808 -0.0516 -0.0930 0.0586  35  ALA F CA  
10539 C C   . ALA F 35  ? 0.7191 0.1591 0.2749 -0.0222 -0.0921 0.0503  35  ALA F C   
10540 O O   . ALA F 35  ? 0.6437 0.1515 0.2693 0.0043  -0.0874 0.0474  35  ALA F O   
10541 C CB  . ALA F 35  ? 0.7969 0.1518 0.2769 -0.0131 -0.0897 0.0514  35  ALA F CB  
10542 N N   . ALA F 36  ? 0.7655 0.1615 0.2772 -0.0306 -0.0968 0.0470  36  ALA F N   
10543 C CA  . ALA F 36  ? 0.7201 0.1551 0.2727 -0.0051 -0.0956 0.0400  36  ALA F CA  
10544 C C   . ALA F 36  ? 0.7261 0.1452 0.2689 0.0528  -0.0916 0.0301  36  ALA F C   
10545 O O   . ALA F 36  ? 0.8075 0.1447 0.2712 0.0749  -0.0906 0.0273  36  ALA F O   
10546 C CB  . ALA F 36  ? 0.7777 0.1631 0.2763 -0.0316 -0.1015 0.0404  36  ALA F CB  
10547 N N   . ASP F 37  ? 0.6470 0.1471 0.2654 0.0768  -0.0890 0.0273  37  ASP F N   
10548 C CA  . ASP F 37  ? 0.6455 0.1583 0.2651 0.1270  -0.0866 0.0227  37  ASP F CA  
10549 C C   . ASP F 37  ? 0.6897 0.1679 0.2685 0.1458  -0.0850 0.0196  37  ASP F C   
10550 O O   . ASP F 37  ? 0.6463 0.1662 0.2659 0.1330  -0.0858 0.0185  37  ASP F O   
10551 C CB  . ASP F 37  ? 0.5535 0.1643 0.2605 0.1338  -0.0864 0.0230  37  ASP F CB  
10552 C CG  . ASP F 37  ? 0.5488 0.1936 0.2622 0.1774  -0.0864 0.0234  37  ASP F CG  
10553 O OD1 . ASP F 37  ? 0.5423 0.2127 0.2636 0.1971  -0.0850 0.0232  37  ASP F OD1 
10554 O OD2 . ASP F 37  ? 0.5532 0.2052 0.2632 0.1916  -0.0878 0.0261  37  ASP F OD2 
10555 N N   . LYS F 38  ? 0.7842 0.1798 0.2749 0.1796  -0.0814 0.0189  38  LYS F N   
10556 C CA  . LYS F 38  ? 0.8535 0.1906 0.2793 0.2028  -0.0770 0.0169  38  LYS F CA  
10557 C C   . LYS F 38  ? 0.7986 0.2195 0.2805 0.2432  -0.0723 0.0182  38  LYS F C   
10558 O O   . LYS F 38  ? 0.7932 0.2189 0.2799 0.2377  -0.0714 0.0160  38  LYS F O   
10559 C CB  . LYS F 38  ? 0.9859 0.2003 0.2862 0.2384  -0.0709 0.0176  38  LYS F CB  
10560 C CG  . LYS F 38  ? 1.0799 0.1778 0.2882 0.1895  -0.0761 0.0162  38  LYS F CG  
10561 C CD  . LYS F 38  ? 1.2363 0.1863 0.2949 0.2271  -0.0683 0.0160  38  LYS F CD  
10562 C CE  . LYS F 38  ? 1.2568 0.1976 0.2979 0.2650  -0.0639 0.0196  38  LYS F CE  
10563 N NZ  . LYS F 38  ? 1.4157 0.2138 0.3055 0.3187  -0.0526 0.0212  38  LYS F NZ  
10564 N N   . GLU F 39  ? 0.7624 0.2526 0.2842 0.2803  -0.0703 0.0236  39  GLU F N   
10565 C CA  . GLU F 39  ? 0.7152 0.2988 0.2885 0.3161  -0.0668 0.0294  39  GLU F CA  
10566 C C   . GLU F 39  ? 0.6260 0.2835 0.2810 0.2793  -0.0714 0.0258  39  GLU F C   
10567 O O   . GLU F 39  ? 0.6288 0.2975 0.2827 0.2924  -0.0673 0.0259  39  GLU F O   
10568 C CB  . GLU F 39  ? 0.6831 0.3468 0.2952 0.3440  -0.0686 0.0389  39  GLU F CB  
10569 C CG  . GLU F 39  ? 0.6161 0.4052 0.3013 0.3586  -0.0698 0.0480  39  GLU F CG  
10570 C CD  . GLU F 39  ? 0.6449 0.4910 0.3166 0.4178  -0.0655 0.0651  39  GLU F CD  
10571 O OE1 . GLU F 39  ? 0.6660 0.5048 0.3203 0.4296  -0.0682 0.0697  39  GLU F OE1 
10572 O OE2 . GLU F 39  ? 0.6496 0.5534 0.3271 0.4551  -0.0586 0.0760  39  GLU F OE2 
10573 N N   . SER F 40  ? 0.5555 0.2568 0.2731 0.2374  -0.0783 0.0232  40  SER F N   
10574 C CA  . SER F 40  ? 0.4813 0.2441 0.2668 0.2064  -0.0811 0.0208  40  SER F CA  
10575 C C   . SER F 40  ? 0.4992 0.2150 0.2634 0.1823  -0.0805 0.0161  40  SER F C   
10576 O O   . SER F 40  ? 0.4624 0.2173 0.2613 0.1756  -0.0800 0.0149  40  SER F O   
10577 C CB  . SER F 40  ? 0.4255 0.2251 0.2617 0.1733  -0.0854 0.0205  40  SER F CB  
10578 O OG  . SER F 40  ? 0.4502 0.1943 0.2604 0.1493  -0.0856 0.0193  40  SER F OG  
10579 N N   . THR F 41  ? 0.5604 0.1929 0.2635 0.1656  -0.0816 0.0147  41  THR F N   
10580 C CA  . THR F 41  ? 0.5903 0.1762 0.2626 0.1340  -0.0841 0.0130  41  THR F CA  
10581 C C   . THR F 41  ? 0.6469 0.1881 0.2646 0.1623  -0.0796 0.0105  41  THR F C   
10582 O O   . THR F 41  ? 0.6287 0.1844 0.2627 0.1466  -0.0808 0.0090  41  THR F O   
10583 C CB  . THR F 41  ? 0.6558 0.1632 0.2652 0.1001  -0.0885 0.0151  41  THR F CB  
10584 O OG1 . THR F 41  ? 0.6003 0.1574 0.2638 0.0750  -0.0906 0.0197  41  THR F OG1 
10585 C CG2 . THR F 41  ? 0.6952 0.1611 0.2675 0.0589  -0.0942 0.0166  41  THR F CG2 
10586 N N   . GLN F 42  ? 0.7212 0.2060 0.2690 0.2082  -0.0729 0.0114  42  GLN F N   
10587 C CA  . GLN F 42  ? 0.7926 0.2246 0.2728 0.2467  -0.0646 0.0111  42  GLN F CA  
10588 C C   . GLN F 42  ? 0.7183 0.2531 0.2728 0.2715  -0.0602 0.0138  42  GLN F C   
10589 O O   . GLN F 42  ? 0.7439 0.2594 0.2736 0.2817  -0.0557 0.0126  42  GLN F O   
10590 C CB  . GLN F 42  ? 0.8947 0.2495 0.2802 0.3027  -0.0547 0.0150  42  GLN F CB  
10591 C CG  . GLN F 42  ? 0.9968 0.2729 0.2865 0.3504  -0.0423 0.0164  42  GLN F CG  
10592 C CD  . GLN F 42  ? 1.0732 0.2392 0.2836 0.3066  -0.0472 0.0090  42  GLN F CD  
10593 O OE1 . GLN F 42  ? 1.0684 0.2424 0.2826 0.3070  -0.0450 0.0074  42  GLN F OE1 
10594 N NE2 . GLN F 42  ? 1.1469 0.2121 0.2831 0.2637  -0.0551 0.0060  42  GLN F NE2 
10595 N N   . LYS F 43  ? 0.6337 0.2735 0.2724 0.2774  -0.0621 0.0183  43  LYS F N   
10596 C CA  . LYS F 43  ? 0.5625 0.3081 0.2736 0.2892  -0.0604 0.0228  43  LYS F CA  
10597 C C   . LYS F 43  ? 0.5061 0.2747 0.2647 0.2450  -0.0654 0.0165  43  LYS F C   
10598 O O   . LYS F 43  ? 0.4872 0.2947 0.2659 0.2554  -0.0617 0.0179  43  LYS F O   
10599 C CB  . LYS F 43  ? 0.4984 0.3393 0.2763 0.2898  -0.0649 0.0294  43  LYS F CB  
10600 C CG  . LYS F 43  ? 0.4874 0.4188 0.2883 0.3324  -0.0600 0.0429  43  LYS F CG  
10601 C CD  . LYS F 43  ? 0.4640 0.4598 0.2943 0.3379  -0.0657 0.0523  43  LYS F CD  
10602 C CE  . LYS F 43  ? 0.4430 0.5579 0.3085 0.3684  -0.0642 0.0708  43  LYS F CE  
10603 N NZ  . LYS F 43  ? 0.3997 0.5922 0.3113 0.3447  -0.0761 0.0786  43  LYS F NZ  
10604 N N   . ALA F 44  ? 0.4817 0.2312 0.2569 0.1988  -0.0727 0.0120  44  ALA F N   
10605 C CA  . ALA F 44  ? 0.4363 0.2067 0.2506 0.1601  -0.0767 0.0091  44  ALA F CA  
10606 C C   . ALA F 44  ? 0.4956 0.1978 0.2512 0.1541  -0.0764 0.0063  44  ALA F C   
10607 O O   . ALA F 44  ? 0.4694 0.1979 0.2492 0.1456  -0.0763 0.0051  44  ALA F O   
10608 C CB  . ALA F 44  ? 0.4054 0.1811 0.2471 0.1206  -0.0821 0.0101  44  ALA F CB  
10609 N N   . ILE F 45  ? 0.5851 0.1909 0.2539 0.1559  -0.0767 0.0054  45  ILE F N   
10610 C CA  . ILE F 45  ? 0.6674 0.1857 0.2554 0.1467  -0.0774 0.0029  45  ILE F CA  
10611 C C   . ILE F 45  ? 0.6885 0.2086 0.2575 0.1931  -0.0671 0.0022  45  ILE F C   
10612 O O   . ILE F 45  ? 0.7037 0.2046 0.2566 0.1798  -0.0681 0.0000  45  ILE F O   
10613 C CB  . ILE F 45  ? 0.7835 0.1789 0.2593 0.1406  -0.0790 0.0026  45  ILE F CB  
10614 C CG1 . ILE F 45  ? 0.7695 0.1648 0.2590 0.0790  -0.0912 0.0061  45  ILE F CG1 
10615 C CG2 . ILE F 45  ? 0.8994 0.1811 0.2625 0.1454  -0.0767 -0.0002 45  ILE F CG2 
10616 C CD1 . ILE F 45  ? 0.8709 0.1619 0.2634 0.0677  -0.0936 0.0072  45  ILE F CD1 
10617 N N   . ASP F 46  ? 0.6899 0.2409 0.2617 0.2476  -0.0571 0.0064  46  ASP F N   
10618 C CA  . ASP F 46  ? 0.7092 0.2810 0.2671 0.2987  -0.0447 0.0106  46  ASP F CA  
10619 C C   . ASP F 46  ? 0.6110 0.2889 0.2632 0.2832  -0.0467 0.0112  46  ASP F C   
10620 O O   . ASP F 46  ? 0.6295 0.2987 0.2642 0.2944  -0.0413 0.0107  46  ASP F O   
10621 C CB  . ASP F 46  ? 0.7281 0.3344 0.2765 0.3605  -0.0340 0.0209  46  ASP F CB  
10622 C CG  . ASP F 46  ? 0.8434 0.3312 0.2810 0.3877  -0.0287 0.0213  46  ASP F CG  
10623 O OD1 . ASP F 46  ? 0.9193 0.2893 0.2777 0.3548  -0.0337 0.0132  46  ASP F OD1 
10624 O OD2 . ASP F 46  ? 0.8645 0.3770 0.2894 0.4396  -0.0202 0.0313  46  ASP F OD2 
10625 N N   . GLY F 47  ? 0.5166 0.2848 0.2588 0.2573  -0.0539 0.0122  47  GLY F N   
10626 C CA  . GLY F 47  ? 0.4347 0.2920 0.2556 0.2386  -0.0560 0.0128  47  GLY F CA  
10627 C C   . GLY F 47  ? 0.4268 0.2557 0.2494 0.2020  -0.0606 0.0063  47  GLY F C   
10628 O O   . GLY F 47  ? 0.4049 0.2687 0.2495 0.2049  -0.0575 0.0065  47  GLY F O   
10629 N N   . VAL F 48  ? 0.4465 0.2190 0.2456 0.1663  -0.0684 0.0027  48  VAL F N   
10630 C CA  . VAL F 48  ? 0.4421 0.1975 0.2422 0.1280  -0.0748 0.0006  48  VAL F CA  
10631 C C   . VAL F 48  ? 0.5253 0.2013 0.2450 0.1379  -0.0723 -0.0020 48  VAL F C   
10632 O O   . VAL F 48  ? 0.5132 0.1993 0.2433 0.1237  -0.0740 -0.0031 48  VAL F O   
10633 C CB  . VAL F 48  ? 0.4403 0.1777 0.2412 0.0846  -0.0843 0.0031  48  VAL F CB  
10634 C CG1 . VAL F 48  ? 0.4561 0.1744 0.2420 0.0450  -0.0924 0.0056  48  VAL F CG1 
10635 C CG2 . VAL F 48  ? 0.3592 0.1737 0.2380 0.0756  -0.0844 0.0063  48  VAL F CG2 
10636 N N   . THR F 49  ? 0.6192 0.2077 0.2496 0.1637  -0.0677 -0.0027 49  THR F N   
10637 C CA  . THR F 49  ? 0.7224 0.2129 0.2532 0.1784  -0.0631 -0.0051 49  THR F CA  
10638 C C   . THR F 49  ? 0.7037 0.2414 0.2561 0.2206  -0.0510 -0.0038 49  THR F C   
10639 O O   . THR F 49  ? 0.7242 0.2375 0.2551 0.2090  -0.0517 -0.0063 49  THR F O   
10640 C CB  . THR F 49  ? 0.8420 0.2189 0.2584 0.2094  -0.0565 -0.0050 49  THR F CB  
10641 O OG1 . THR F 49  ? 0.8653 0.1964 0.2571 0.1634  -0.0687 -0.0054 49  THR F OG1 
10642 C CG2 . THR F 49  ? 0.9702 0.2241 0.2620 0.2272  -0.0498 -0.0074 49  THR F CG2 
10643 N N   . ASN F 50  ? 0.6666 0.2782 0.2613 0.2665  -0.0406 0.0021  50  ASN F N   
10644 C CA  . ASN F 50  ? 0.6426 0.3226 0.2669 0.3053  -0.0287 0.0079  50  ASN F CA  
10645 C C   . ASN F 50  ? 0.5592 0.3088 0.2614 0.2666  -0.0357 0.0048  50  ASN F C   
10646 O O   . ASN F 50  ? 0.5725 0.3233 0.2631 0.2790  -0.0294 0.0052  50  ASN F O   
10647 C CB  . ASN F 50  ? 0.5988 0.3771 0.2745 0.3445  -0.0215 0.0191  50  ASN F CB  
10648 C CG  . ASN F 50  ? 0.6907 0.4109 0.2840 0.4021  -0.0096 0.0263  50  ASN F CG  
10649 O OD1 . ASN F 50  ? 0.7912 0.4285 0.2902 0.4447  0.0035  0.0283  50  ASN F OD1 
10650 N ND2 . ASN F 50  ? 0.6660 0.4230 0.2860 0.4069  -0.0130 0.0309  50  ASN F ND2 
10651 N N   . LYS F 51  ? 0.4814 0.2837 0.2560 0.2233  -0.0471 0.0026  51  LYS F N   
10652 C CA  . LYS F 51  ? 0.4101 0.2695 0.2512 0.1876  -0.0531 0.0006  51  LYS F CA  
10653 C C   . LYS F 51  ? 0.4466 0.2469 0.2495 0.1629  -0.0579 -0.0039 51  LYS F C   
10654 O O   . LYS F 51  ? 0.4214 0.2525 0.2484 0.1591  -0.0560 -0.0043 51  LYS F O   
10655 C CB  . LYS F 51  ? 0.3483 0.2453 0.2459 0.1523  -0.0622 0.0004  51  LYS F CB  
10656 C CG  . LYS F 51  ? 0.2888 0.2284 0.2404 0.1185  -0.0670 -0.0002 51  LYS F CG  
10657 C CD  . LYS F 51  ? 0.2469 0.2129 0.2376 0.0966  -0.0716 0.0017  51  LYS F CD  
10658 C CE  . LYS F 51  ? 0.1903 0.2159 0.2344 0.0852  -0.0701 0.0032  51  LYS F CE  
10659 N NZ  . LYS F 51  ? 0.1679 0.2200 0.2341 0.0834  -0.0703 0.0052  51  LYS F NZ  
10660 N N   . VAL F 52  ? 0.5108 0.2271 0.2508 0.1414  -0.0652 -0.0060 52  VAL F N   
10661 C CA  . VAL F 52  ? 0.5562 0.2155 0.2511 0.1085  -0.0733 -0.0078 52  VAL F CA  
10662 C C   . VAL F 52  ? 0.6306 0.2314 0.2552 0.1416  -0.0634 -0.0104 52  VAL F C   
10663 O O   . VAL F 52  ? 0.6265 0.2305 0.2539 0.1272  -0.0657 -0.0116 52  VAL F O   
10664 C CB  . VAL F 52  ? 0.6212 0.2034 0.2532 0.0702  -0.0853 -0.0065 52  VAL F CB  
10665 C CG1 . VAL F 52  ? 0.6921 0.2043 0.2551 0.0331  -0.0954 -0.0062 52  VAL F CG1 
10666 C CG2 . VAL F 52  ? 0.5449 0.1972 0.2517 0.0365  -0.0939 -0.0009 52  VAL F CG2 
10667 N N   . ASN F 53  ? 0.7029 0.2515 0.2620 0.1906  -0.0509 -0.0098 53  ASN F N   
10668 C CA  . ASN F 53  ? 0.7871 0.2766 0.2684 0.2359  -0.0365 -0.0095 53  ASN F CA  
10669 C C   . ASN F 53  ? 0.7149 0.3098 0.2715 0.2642  -0.0258 -0.0052 53  ASN F C   
10670 O O   . ASN F 53  ? 0.7493 0.3196 0.2725 0.2764  -0.0194 -0.0059 53  ASN F O   
10671 C CB  . ASN F 53  ? 0.8855 0.3006 0.2762 0.2922  -0.0223 -0.0061 53  ASN F CB  
10672 C CG  . ASN F 53  ? 0.9748 0.2719 0.2756 0.2627  -0.0322 -0.0101 53  ASN F CG  
10673 O OD1 . ASN F 53  ? 1.0009 0.2442 0.2722 0.2023  -0.0485 -0.0144 53  ASN F OD1 
10674 N ND2 . ASN F 53  ? 1.0252 0.2868 0.2807 0.3029  -0.0232 -0.0067 53  ASN F ND2 
10675 N N   . SER F 54  ? 0.6225 0.3312 0.2741 0.2705  -0.0248 0.0000  54  SER F N   
10676 C CA  . SER F 54  ? 0.5519 0.3697 0.2783 0.2834  -0.0179 0.0058  54  SER F CA  
10677 C C   . SER F 54  ? 0.5087 0.3424 0.2729 0.2402  -0.0266 0.0001  54  SER F C   
10678 O O   . SER F 54  ? 0.5047 0.3663 0.2758 0.2540  -0.0189 0.0024  54  SER F O   
10679 C CB  . SER F 54  ? 0.4686 0.3933 0.2796 0.2800  -0.0203 0.0123  54  SER F CB  
10680 O OG  . SER F 54  ? 0.5025 0.4469 0.2903 0.3311  -0.0092 0.0229  54  SER F OG  
10681 N N   . ILE F 55  ? 0.4803 0.3012 0.2681 0.1908  -0.0417 -0.0051 55  ILE F N   
10682 C CA  . ILE F 55  ? 0.4455 0.2809 0.2646 0.1517  -0.0504 -0.0079 55  ILE F CA  
10683 C C   . ILE F 55  ? 0.5243 0.2786 0.2680 0.1497  -0.0508 -0.0111 55  ILE F C   
10684 O O   . ILE F 55  ? 0.5102 0.2857 0.2676 0.1491  -0.0479 -0.0116 55  ILE F O   
10685 C CB  . ILE F 55  ? 0.4073 0.2513 0.2600 0.1071  -0.0644 -0.0078 55  ILE F CB  
10686 C CG1 . ILE F 55  ? 0.3303 0.2544 0.2582 0.1061  -0.0630 -0.0051 55  ILE F CG1 
10687 C CG2 . ILE F 55  ? 0.3936 0.2399 0.2574 0.0718  -0.0733 -0.0070 55  ILE F CG2 
10688 C CD1 . ILE F 55  ? 0.3010 0.2336 0.2556 0.0751  -0.0721 -0.0027 55  ILE F CD1 
10689 N N   . ILE F 56  ? 0.6175 0.2715 0.2730 0.1455  -0.0548 -0.0132 56  ILE F N   
10690 C CA  . ILE F 56  ? 0.7173 0.2715 0.2770 0.1397  -0.0562 -0.0163 56  ILE F CA  
10691 C C   . ILE F 56  ? 0.7511 0.3024 0.2839 0.1914  -0.0377 -0.0158 56  ILE F C   
10692 O O   . ILE F 56  ? 0.7647 0.3022 0.2831 0.1811  -0.0385 -0.0175 56  ILE F O   
10693 C CB  . ILE F 56  ? 0.8355 0.2638 0.2802 0.1338  -0.0603 -0.0179 56  ILE F CB  
10694 C CG1 . ILE F 56  ? 0.8174 0.2467 0.2783 0.0691  -0.0814 -0.0155 56  ILE F CG1 
10695 C CG2 . ILE F 56  ? 0.9661 0.2682 0.2832 0.1416  -0.0566 -0.0211 56  ILE F CG2 
10696 C CD1 . ILE F 56  ? 0.9222 0.2424 0.2820 0.0566  -0.0866 -0.0158 56  ILE F CD1 
10697 N N   . ASP F 57  ? 0.7663 0.3387 0.2936 0.2479  -0.0207 -0.0109 57  ASP F N   
10698 C CA  . ASP F 57  ? 0.8124 0.3863 0.3039 0.3067  0.0002  -0.0054 57  ASP F CA  
10699 C C   . ASP F 57  ? 0.7240 0.4113 0.3061 0.3047  0.0041  -0.0017 57  ASP F C   
10700 O O   . ASP F 57  ? 0.7628 0.4344 0.3103 0.3292  0.0156  0.0002  57  ASP F O   
10701 C CB  . ASP F 57  ? 0.8483 0.4346 0.3146 0.3711  0.0179  0.0041  57  ASP F CB  
10702 C CG  . ASP F 57  ? 0.9927 0.4267 0.3190 0.3966  0.0235  0.0017  57  ASP F CG  
10703 O OD1 . ASP F 57  ? 1.1012 0.4210 0.3207 0.4050  0.0287  -0.0021 57  ASP F OD1 
10704 O OD2 . ASP F 57  ? 1.0078 0.4271 0.3213 0.4070  0.0227  0.0036  57  ASP F OD2 
10705 N N   . LYS F 58  ? 0.6167 0.4092 0.3049 0.2750  -0.0045 -0.0003 58  LYS F N   
10706 C CA  . LYS F 58  ? 0.5432 0.4308 0.3069 0.2640  -0.0026 0.0028  58  LYS F CA  
10707 C C   . LYS F 58  ? 0.5504 0.3995 0.3036 0.2290  -0.0111 -0.0045 58  LYS F C   
10708 O O   . LYS F 58  ? 0.5334 0.4211 0.3058 0.2351  -0.0042 -0.0021 58  LYS F O   
10709 C CB  . LYS F 58  ? 0.4460 0.4310 0.3038 0.2363  -0.0106 0.0055  58  LYS F CB  
10710 C CG  . LYS F 58  ? 0.4127 0.5008 0.3138 0.2651  0.0004  0.0188  58  LYS F CG  
10711 C CD  . LYS F 58  ? 0.4801 0.5554 0.3257 0.3273  0.0164  0.0290  58  LYS F CD  
10712 C CE  . LYS F 58  ? 0.4457 0.6482 0.3395 0.3550  0.0274  0.0481  58  LYS F CE  
10713 N NZ  . LYS F 58  ? 0.5203 0.7189 0.3550 0.4280  0.0475  0.0627  58  LYS F NZ  
10714 N N   . MET F 59  ? 0.5808 0.3592 0.3018 0.1915  -0.0264 -0.0112 59  MET F N   
10715 C CA  . MET F 59  ? 0.5931 0.3393 0.3002 0.1555  -0.0370 -0.0152 59  MET F CA  
10716 C C   . MET F 59  ? 0.7084 0.3460 0.3056 0.1712  -0.0323 -0.0180 59  MET F C   
10717 O O   . MET F 59  ? 0.7234 0.3398 0.3033 0.1522  -0.0369 -0.0200 59  MET F O   
10718 C CB  . MET F 59  ? 0.5700 0.3097 0.2964 0.1043  -0.0566 -0.0157 59  MET F CB  
10719 C CG  . MET F 59  ? 0.4762 0.3047 0.2942 0.0927  -0.0594 -0.0126 59  MET F CG  
10720 S SD  . MET F 59  ? 0.3956 0.3148 0.2935 0.0892  -0.0544 -0.0107 59  MET F SD  
10721 C CE  . MET F 59  ? 0.4034 0.3015 0.2900 0.0547  -0.0662 -0.0098 59  MET F CE  
10722 N N   . ASN F 60  ? 0.7992 0.3616 0.3142 0.2079  -0.0222 -0.0177 60  ASN F N   
10723 C CA  . ASN F 60  ? 0.9385 0.3691 0.3207 0.2283  -0.0153 -0.0203 60  ASN F CA  
10724 C C   . ASN F 60  ? 0.9623 0.3929 0.3250 0.2541  -0.0022 -0.0193 60  ASN F C   
10725 O O   . ASN F 60  ? 1.0509 0.3809 0.3241 0.2376  -0.0070 -0.0238 60  ASN F O   
10726 C CB  . ASN F 60  ? 1.0318 0.3895 0.3286 0.2810  -0.0001 -0.0175 60  ASN F CB  
10727 C CG  . ASN F 60  ? 1.1606 0.4212 0.3372 0.3404  0.0220  -0.0152 60  ASN F CG  
10728 O OD1 . ASN F 60  ? 1.1357 0.4669 0.3445 0.3909  0.0418  -0.0073 60  ASN F OD1 
10729 N ND2 . ASN F 60  ? 1.3096 0.4049 0.3387 0.3351  0.0196  -0.0202 60  ASN F ND2 
10730 N N   . THR F 61  ? 0.8915 0.4326 0.3314 0.2902  0.0134  -0.0124 61  THR F N   
10731 C CA  . THR F 61  ? 0.8949 0.4570 0.3352 0.3060  0.0242  -0.0103 61  THR F CA  
10732 C C   . THR F 61  ? 0.7774 0.4375 0.3273 0.2569  0.0102  -0.0122 61  THR F C   
10733 O O   . THR F 61  ? 0.6825 0.4508 0.3277 0.2517  0.0101  -0.0077 61  THR F O   
10734 C CB  . THR F 61  ? 0.9059 0.5296 0.3490 0.3780  0.0524  0.0026  61  THR F CB  
10735 O OG1 . THR F 61  ? 0.7871 0.5627 0.3538 0.3705  0.0525  0.0107  61  THR F OG1 
10736 C CG2 . THR F 61  ? 1.0029 0.5603 0.3584 0.4373  0.0687  0.0088  61  THR F CG2 
10737 N N   . GLN F 62  ? 0.7949 0.4093 0.3208 0.2201  -0.0017 -0.0180 62  GLN F N   
10738 C CA  . GLN F 62  ? 0.7011 0.3922 0.3139 0.1780  -0.0140 -0.0187 62  GLN F CA  
10739 C C   . GLN F 62  ? 0.7452 0.3824 0.3102 0.1603  -0.0190 -0.0219 62  GLN F C   
10740 O O   . GLN F 62  ? 0.8547 0.3846 0.3143 0.1704  -0.0169 -0.0248 62  GLN F O   
10741 C CB  . GLN F 62  ? 0.6486 0.3621 0.3096 0.1322  -0.0341 -0.0197 62  GLN F CB  
10742 C CG  . GLN F 62  ? 0.6697 0.3418 0.3075 0.0814  -0.0551 -0.0206 62  GLN F CG  
10743 C CD  . GLN F 62  ? 0.6133 0.3304 0.3073 0.0452  -0.0708 -0.0165 62  GLN F CD  
10744 O OE1 . GLN F 62  ? 0.5844 0.3288 0.3090 0.0566  -0.0673 -0.0160 62  GLN F OE1 
10745 N NE2 . GLN F 62  ? 0.6004 0.3310 0.3076 0.0039  -0.0874 -0.0114 62  GLN F NE2 
10746 N N   . PHE F 63  ? 0.6704 0.3730 0.3028 0.1341  -0.0253 -0.0212 63  PHE F N   
10747 C CA  . PHE F 63  ? 0.7015 0.3688 0.2990 0.1205  -0.0287 -0.0230 63  PHE F CA  
10748 C C   . PHE F 63  ? 0.7857 0.3507 0.2961 0.0857  -0.0471 -0.0255 63  PHE F C   
10749 O O   . PHE F 63  ? 0.7808 0.3403 0.2970 0.0502  -0.0646 -0.0236 63  PHE F O   
10750 C CB  . PHE F 63  ? 0.6123 0.3623 0.2940 0.0942  -0.0352 -0.0207 63  PHE F CB  
10751 C CG  . PHE F 63  ? 0.6406 0.3644 0.2924 0.0852  -0.0367 -0.0216 63  PHE F CG  
10752 C CD1 . PHE F 63  ? 0.6668 0.3874 0.2953 0.1197  -0.0176 -0.0219 63  PHE F CD1 
10753 C CD2 . PHE F 63  ? 0.6444 0.3524 0.2897 0.0432  -0.0570 -0.0198 63  PHE F CD2 
10754 C CE1 . PHE F 63  ? 0.6967 0.3884 0.2937 0.1118  -0.0186 -0.0232 63  PHE F CE1 
10755 C CE2 . PHE F 63  ? 0.6738 0.3575 0.2889 0.0343  -0.0595 -0.0200 63  PHE F CE2 
10756 C CZ  . PHE F 63  ? 0.7003 0.3699 0.2896 0.0682  -0.0402 -0.0231 63  PHE F CZ  
10757 N N   . GLU F 64  ? 0.8696 0.3542 0.2942 0.0938  -0.0429 -0.0281 64  GLU F N   
10758 C CA  . GLU F 64  ? 0.9632 0.3451 0.2921 0.0520  -0.0623 -0.0294 64  GLU F CA  
10759 C C   . GLU F 64  ? 0.9597 0.3474 0.2879 0.0313  -0.0690 -0.0286 64  GLU F C   
10760 O O   . GLU F 64  ? 0.9672 0.3569 0.2886 0.0678  -0.0504 -0.0308 64  GLU F O   
10761 C CB  . GLU F 64  ? 1.1079 0.3502 0.2965 0.0812  -0.0511 -0.0338 64  GLU F CB  
10762 C CG  . GLU F 64  ? 1.1335 0.3475 0.2992 0.1014  -0.0456 -0.0340 64  GLU F CG  
10763 C CD  . GLU F 64  ? 1.2950 0.3559 0.3044 0.1394  -0.0308 -0.0373 64  GLU F CD  
10764 O OE1 . GLU F 64  ? 1.4031 0.3583 0.3048 0.1331  -0.0314 -0.0400 64  GLU F OE1 
10765 O OE2 . GLU F 64  ? 1.3217 0.3619 0.3081 0.1780  -0.0177 -0.0364 64  GLU F OE2 
10766 N N   . ALA F 65  ? 0.9504 0.3469 0.2847 -0.0264 -0.0951 -0.0230 65  ALA F N   
10767 C CA  . ALA F 65  ? 0.9506 0.3546 0.2815 -0.0496 -0.1044 -0.0202 65  ALA F CA  
10768 C C   . ALA F 65  ? 1.0900 0.3576 0.2812 -0.0540 -0.1054 -0.0250 65  ALA F C   
10769 O O   . ALA F 65  ? 1.1974 0.3571 0.2840 -0.0645 -0.1102 -0.0274 65  ALA F O   
10770 C CB  . ALA F 65  ? 0.9026 0.3726 0.2839 -0.1064 -0.1317 -0.0079 65  ALA F CB  
10771 N N   . VAL F 66  ? 1.0965 0.3595 0.2767 -0.0450 -0.0997 -0.0264 66  VAL F N   
10772 C CA  . VAL F 66  ? 1.2335 0.3642 0.2765 -0.0528 -0.1018 -0.0303 66  VAL F CA  
10773 C C   . VAL F 66  ? 1.2162 0.3769 0.2738 -0.0948 -0.1208 -0.0245 66  VAL F C   
10774 O O   . VAL F 66  ? 1.1044 0.3779 0.2713 -0.0876 -0.1178 -0.0207 66  VAL F O   
10775 C CB  . VAL F 66  ? 1.2895 0.3628 0.2770 0.0188  -0.0675 -0.0378 66  VAL F CB  
10776 C CG1 . VAL F 66  ? 1.4574 0.3688 0.2794 0.0148  -0.0677 -0.0419 66  VAL F CG1 
10777 C CG2 . VAL F 66  ? 1.2875 0.3612 0.2798 0.0689  -0.0467 -0.0395 66  VAL F CG2 
10778 N N   . GLY F 67  ? 1.3358 0.3893 0.2741 -0.1406 -0.1408 -0.0227 67  GLY F N   
10779 C CA  . GLY F 67  ? 1.3359 0.4115 0.2733 -0.1865 -0.1625 -0.0147 67  GLY F CA  
10780 C C   . GLY F 67  ? 1.3605 0.4003 0.2674 -0.1474 -0.1427 -0.0222 67  GLY F C   
10781 O O   . GLY F 67  ? 1.4761 0.3912 0.2675 -0.1154 -0.1252 -0.0314 67  GLY F O   
10782 N N   . ARG F 68  ? 1.2580 0.4038 0.2622 -0.1467 -0.1438 -0.0171 68  ARG F N   
10783 C CA  . ARG F 68  ? 1.2678 0.3965 0.2566 -0.1139 -0.1261 -0.0226 68  ARG F CA  
10784 C C   . ARG F 68  ? 1.2336 0.4186 0.2558 -0.1559 -0.1485 -0.0124 68  ARG F C   
10785 O O   . ARG F 68  ? 1.1321 0.4329 0.2570 -0.1755 -0.1617 -0.0013 68  ARG F O   
10786 C CB  . ARG F 68  ? 1.1681 0.3792 0.2527 -0.0505 -0.0936 -0.0276 68  ARG F CB  
10787 C CG  . ARG F 68  ? 1.2269 0.3717 0.2540 0.0043  -0.0656 -0.0354 68  ARG F CG  
10788 C CD  . ARG F 68  ? 1.1361 0.3743 0.2532 0.0607  -0.0352 -0.0359 68  ARG F CD  
10789 N NE  . ARG F 68  ? 1.0075 0.3669 0.2511 0.0526  -0.0393 -0.0320 68  ARG F NE  
10790 C CZ  . ARG F 68  ? 0.9803 0.3612 0.2521 0.0609  -0.0377 -0.0318 68  ARG F CZ  
10791 N NH1 . ARG F 68  ? 1.0706 0.3620 0.2554 0.0791  -0.0319 -0.0350 68  ARG F NH1 
10792 N NH2 . ARG F 68  ? 0.8694 0.3554 0.2503 0.0518  -0.0415 -0.0282 68  ARG F NH2 
10793 N N   . GLU F 69  ? 1.3251 0.4251 0.2539 -0.1654 -0.1515 -0.0149 69  GLU F N   
10794 C CA  . GLU F 69  ? 1.3202 0.4553 0.2551 -0.2105 -0.1762 -0.0037 69  GLU F CA  
10795 C C   . GLU F 69  ? 1.2666 0.4414 0.2475 -0.1714 -0.1562 -0.0077 69  GLU F C   
10796 O O   . GLU F 69  ? 1.3009 0.4192 0.2436 -0.1227 -0.1276 -0.0194 69  GLU F O   
10797 C CB  . GLU F 69  ? 1.4806 0.4804 0.2613 -0.2613 -0.1988 -0.0024 69  GLU F CB  
10798 C CG  . GLU F 69  ? 1.5591 0.5004 0.2686 -0.3132 -0.2222 0.0028  69  GLU F CG  
10799 C CD  . GLU F 69  ? 1.5290 0.5631 0.2794 -0.3890 -0.2625 0.0255  69  GLU F CD  
10800 O OE1 . GLU F 69  ? 1.3914 0.5802 0.2824 -0.3797 -0.2640 0.0372  69  GLU F OE1 
10801 O OE2 . GLU F 69  ? 1.6528 0.6043 0.2875 -0.4578 -0.2921 0.0338  69  GLU F OE2 
10802 N N   . PHE F 70  ? 1.1885 0.4614 0.2459 -0.1914 -0.1706 0.0043  70  PHE F N   
10803 C CA  . PHE F 70  ? 1.1417 0.4516 0.2395 -0.1612 -0.1544 0.0021  70  PHE F CA  
10804 C C   . PHE F 70  ? 1.1583 0.4909 0.2427 -0.2031 -0.1810 0.0160  70  PHE F C   
10805 O O   . PHE F 70  ? 1.1403 0.5331 0.2499 -0.2462 -0.2092 0.0332  70  PHE F O   
10806 C CB  . PHE F 70  ? 1.0112 0.4345 0.2355 -0.1264 -0.1364 0.0029  70  PHE F CB  
10807 C CG  . PHE F 70  ? 0.9810 0.4063 0.2324 -0.0929 -0.1153 -0.0063 70  PHE F CG  
10808 C CD1 . PHE F 70  ? 0.9493 0.4074 0.2343 -0.1088 -0.1267 -0.0016 70  PHE F CD1 
10809 C CD2 . PHE F 70  ? 0.9848 0.3881 0.2290 -0.0454 -0.0840 -0.0170 70  PHE F CD2 
10810 C CE1 . PHE F 70  ? 0.9231 0.3846 0.2320 -0.0778 -0.1080 -0.0094 70  PHE F CE1 
10811 C CE2 . PHE F 70  ? 0.9577 0.3757 0.2287 -0.0142 -0.0655 -0.0220 70  PHE F CE2 
10812 C CZ  . PHE F 70  ? 0.9273 0.3705 0.2295 -0.0304 -0.0779 -0.0191 70  PHE F CZ  
10813 N N   . ASN F 71  ? 1.1921 0.4851 0.2381 -0.1892 -0.1718 0.0110  71  ASN F N   
10814 C CA  . ASN F 71  ? 1.2136 0.5263 0.2419 -0.2263 -0.1964 0.0247  71  ASN F CA  
10815 C C   . ASN F 71  ? 1.0991 0.5416 0.2419 -0.2120 -0.1958 0.0377  71  ASN F C   
10816 O O   . ASN F 71  ? 1.0095 0.5195 0.2384 -0.1813 -0.1795 0.0361  71  ASN F O   
10817 C CB  . ASN F 71  ? 1.3127 0.5180 0.2390 -0.2204 -0.1887 0.0148  71  ASN F CB  
10818 C CG  . ASN F 71  ? 1.2634 0.4850 0.2318 -0.1634 -0.1540 0.0041  71  ASN F CG  
10819 O OD1 . ASN F 71  ? 1.1730 0.4881 0.2306 -0.1500 -0.1495 0.0105  71  ASN F OD1 
10820 N ND2 . ASN F 71  ? 1.3331 0.4609 0.2285 -0.1295 -0.1285 -0.0101 71  ASN F ND2 
10821 N N   . ASN F 72  ? 1.1125 0.5819 0.2458 -0.2333 -0.2134 0.0513  72  ASN F N   
10822 C CA  . ASN F 72  ? 1.0271 0.6131 0.2492 -0.2220 -0.2170 0.0690  72  ASN F CA  
10823 C C   . ASN F 72  ? 0.9661 0.5689 0.2394 -0.1689 -0.1848 0.0583  72  ASN F C   
10824 O O   . ASN F 72  ? 0.8972 0.5816 0.2411 -0.1489 -0.1802 0.0697  72  ASN F O   
10825 C CB  . ASN F 72  ? 1.0726 0.6837 0.2597 -0.2615 -0.2473 0.0901  72  ASN F CB  
10826 C CG  . ASN F 72  ? 1.0000 0.7453 0.2702 -0.2552 -0.2580 0.1175  72  ASN F CG  
10827 O OD1 . ASN F 72  ? 0.9429 0.7627 0.2753 -0.2504 -0.2594 0.1283  72  ASN F OD1 
10828 N ND2 . ASN F 72  ? 1.0080 0.7834 0.2747 -0.2509 -0.2640 0.1304  72  ASN F ND2 
10829 N N   . LEU F 73  ? 1.0010 0.5243 0.2303 -0.1467 -0.1620 0.0387  73  LEU F N   
10830 C CA  . LEU F 73  ? 0.9525 0.4898 0.2228 -0.1045 -0.1313 0.0291  73  LEU F CA  
10831 C C   . LEU F 73  ? 0.9292 0.4497 0.2173 -0.0772 -0.1055 0.0138  73  LEU F C   
10832 O O   . LEU F 73  ? 0.9292 0.4299 0.2132 -0.0495 -0.0795 0.0035  73  LEU F O   
10833 C CB  . LEU F 73  ? 1.0067 0.4894 0.2206 -0.0990 -0.1240 0.0241  73  LEU F CB  
10834 C CG  . LEU F 73  ? 1.0189 0.5323 0.2259 -0.1185 -0.1460 0.0409  73  LEU F CG  
10835 C CD1 . LEU F 73  ? 1.0960 0.5336 0.2242 -0.1231 -0.1445 0.0347  73  LEU F CD1 
10836 C CD2 . LEU F 73  ? 0.9473 0.5365 0.2259 -0.0933 -0.1360 0.0503  73  LEU F CD2 
10837 N N   . GLU F 74  ? 0.9100 0.4469 0.2184 -0.0866 -0.1137 0.0150  74  GLU F N   
10838 C CA  . GLU F 74  ? 0.8766 0.4179 0.2148 -0.0614 -0.0926 0.0046  74  GLU F CA  
10839 C C   . GLU F 74  ? 0.8043 0.4201 0.2166 -0.0665 -0.1005 0.0129  74  GLU F C   
10840 O O   . GLU F 74  ? 0.7943 0.4081 0.2163 -0.0649 -0.0989 0.0088  74  GLU F O   
10841 C CB  . GLU F 74  ? 0.9534 0.4106 0.2151 -0.0629 -0.0917 -0.0042 74  GLU F CB  
10842 C CG  . GLU F 74  ? 1.0322 0.4084 0.2137 -0.0449 -0.0760 -0.0128 74  GLU F CG  
10843 C CD  . GLU F 74  ? 1.1184 0.4024 0.2149 -0.0324 -0.0679 -0.0211 74  GLU F CD  
10844 O OE1 . GLU F 74  ? 1.1762 0.4083 0.2171 -0.0657 -0.0909 -0.0190 74  GLU F OE1 
10845 O OE2 . GLU F 74  ? 1.1348 0.3994 0.2152 0.0110  -0.0379 -0.0276 74  GLU F OE2 
10846 N N   . ARG F 75  ? 0.7609 0.4383 0.2191 -0.0683 -0.1075 0.0255  75  ARG F N   
10847 C CA  . ARG F 75  ? 0.7040 0.4514 0.2230 -0.0698 -0.1154 0.0373  75  ARG F CA  
10848 C C   . ARG F 75  ? 0.6495 0.4183 0.2179 -0.0446 -0.0929 0.0288  75  ARG F C   
10849 O O   . ARG F 75  ? 0.6146 0.4174 0.2193 -0.0458 -0.0966 0.0325  75  ARG F O   
10850 C CB  . ARG F 75  ? 0.6885 0.4906 0.2293 -0.0687 -0.1253 0.0563  75  ARG F CB  
10851 C CG  . ARG F 75  ? 0.7330 0.5460 0.2391 -0.1013 -0.1545 0.0727  75  ARG F CG  
10852 C CD  . ARG F 75  ? 0.7162 0.5929 0.2498 -0.1240 -0.1761 0.0912  75  ARG F CD  
10853 N NE  . ARG F 75  ? 0.7741 0.6525 0.2606 -0.1702 -0.2072 0.1060  75  ARG F NE  
10854 C CZ  . ARG F 75  ? 0.8360 0.6493 0.2612 -0.2081 -0.2215 0.0981  75  ARG F CZ  
10855 N NH1 . ARG F 75  ? 0.8457 0.5900 0.2523 -0.1973 -0.2055 0.0760  75  ARG F NH1 
10856 N NH2 . ARG F 75  ? 0.8983 0.7124 0.2718 -0.2581 -0.2523 0.1143  75  ARG F NH2 
10857 N N   . ARG F 76  ? 0.6459 0.3979 0.2130 -0.0257 -0.0706 0.0190  76  ARG F N   
10858 C CA  . ARG F 76  ? 0.6039 0.3775 0.2101 -0.0100 -0.0507 0.0126  76  ARG F CA  
10859 C C   . ARG F 76  ? 0.5994 0.3661 0.2099 -0.0072 -0.0467 0.0044  76  ARG F C   
10860 O O   . ARG F 76  ? 0.5596 0.3582 0.2097 -0.0051 -0.0456 0.0054  76  ARG F O   
10861 C CB  . ARG F 76  ? 0.6127 0.3733 0.2078 0.0004  -0.0296 0.0065  76  ARG F CB  
10862 C CG  . ARG F 76  ? 0.6165 0.3797 0.2073 0.0018  -0.0283 0.0139  76  ARG F CG  
10863 C CD  . ARG F 76  ? 0.6378 0.3806 0.2061 0.0049  -0.0091 0.0078  76  ARG F CD  
10864 N NE  . ARG F 76  ? 0.6782 0.3879 0.2068 0.0058  -0.0093 0.0030  76  ARG F NE  
10865 C CZ  . ARG F 76  ? 0.7001 0.3971 0.2076 0.0124  0.0089  -0.0021 76  ARG F CZ  
10866 N NH1 . ARG F 76  ? 0.6832 0.4064 0.2091 0.0118  0.0272  -0.0020 76  ARG F NH1 
10867 N NH2 . ARG F 76  ? 0.7473 0.4045 0.2087 0.0177  0.0089  -0.0056 76  ARG F NH2 
10868 N N   . ILE F 77  ? 0.6482 0.3673 0.2106 -0.0035 -0.0431 -0.0028 77  ILE F N   
10869 C CA  . ILE F 77  ? 0.6607 0.3621 0.2121 0.0067  -0.0369 -0.0092 77  ILE F CA  
10870 C C   . ILE F 77  ? 0.6694 0.3607 0.2139 -0.0130 -0.0586 -0.0057 77  ILE F C   
10871 O O   . ILE F 77  ? 0.6565 0.3528 0.2144 -0.0060 -0.0551 -0.0087 77  ILE F O   
10872 C CB  . ILE F 77  ? 0.7275 0.3705 0.2139 0.0260  -0.0224 -0.0160 77  ILE F CB  
10873 C CG1 . ILE F 77  ? 0.8034 0.3749 0.2144 0.0085  -0.0388 -0.0160 77  ILE F CG1 
10874 C CG2 . ILE F 77  ? 0.7125 0.3846 0.2149 0.0455  0.0014  -0.0164 77  ILE F CG2 
10875 C CD1 . ILE F 77  ? 0.8910 0.3819 0.2169 0.0310  -0.0247 -0.0226 77  ILE F CD1 
10876 N N   . GLU F 78  ? 0.6936 0.3764 0.2165 -0.0400 -0.0816 0.0026  78  GLU F N   
10877 C CA  . GLU F 78  ? 0.6982 0.3909 0.2211 -0.0672 -0.1047 0.0110  78  GLU F CA  
10878 C C   . GLU F 78  ? 0.6214 0.3880 0.2214 -0.0605 -0.1028 0.0174  78  GLU F C   
10879 O O   . GLU F 78  ? 0.6115 0.3859 0.2231 -0.0677 -0.1088 0.0183  78  GLU F O   
10880 C CB  . GLU F 78  ? 0.7328 0.4288 0.2272 -0.1008 -0.1305 0.0247  78  GLU F CB  
10881 C CG  . GLU F 78  ? 0.7405 0.4635 0.2355 -0.1372 -0.1569 0.0388  78  GLU F CG  
10882 C CD  . GLU F 78  ? 0.7948 0.5169 0.2444 -0.1789 -0.1850 0.0544  78  GLU F CD  
10883 O OE1 . GLU F 78  ? 0.7735 0.5435 0.2473 -0.1742 -0.1880 0.0657  78  GLU F OE1 
10884 O OE2 . GLU F 78  ? 0.8666 0.5375 0.2496 -0.2187 -0.2049 0.0567  78  GLU F OE2 
10885 N N   . ASN F 79  ? 0.5775 0.3886 0.2201 -0.0461 -0.0937 0.0221  79  ASN F N   
10886 C CA  . ASN F 79  ? 0.5204 0.3873 0.2210 -0.0361 -0.0896 0.0288  79  ASN F CA  
10887 C C   . ASN F 79  ? 0.4915 0.3576 0.2163 -0.0200 -0.0712 0.0169  79  ASN F C   
10888 O O   . ASN F 79  ? 0.4590 0.3536 0.2172 -0.0188 -0.0725 0.0196  79  ASN F O   
10889 C CB  . ASN F 79  ? 0.5063 0.3985 0.2218 -0.0231 -0.0834 0.0373  79  ASN F CB  
10890 C CG  . ASN F 79  ? 0.4674 0.4006 0.2237 -0.0084 -0.0774 0.0456  79  ASN F CG  
10891 O OD1 . ASN F 79  ? 0.4560 0.4323 0.2312 -0.0107 -0.0899 0.0615  79  ASN F OD1 
10892 N ND2 . ASN F 79  ? 0.4543 0.3748 0.2188 0.0049  -0.0581 0.0368  79  ASN F ND2 
10893 N N   . LEU F 80  ? 0.5052 0.3460 0.2130 -0.0077 -0.0541 0.0061  80  LEU F N   
10894 C CA  . LEU F 80  ? 0.4848 0.3358 0.2116 0.0061  -0.0374 -0.0016 80  LEU F CA  
10895 C C   . LEU F 80  ? 0.4972 0.3315 0.2130 0.0058  -0.0442 -0.0046 80  LEU F C   
10896 O O   . LEU F 80  ? 0.4644 0.3249 0.2131 0.0099  -0.0413 -0.0051 80  LEU F O   
10897 C CB  . LEU F 80  ? 0.5088 0.3454 0.2121 0.0196  -0.0191 -0.0074 80  LEU F CB  
10898 C CG  . LEU F 80  ? 0.4893 0.3595 0.2147 0.0339  0.0005  -0.0097 80  LEU F CG  
10899 C CD1 . LEU F 80  ? 0.5155 0.3849 0.2178 0.0442  0.0173  -0.0098 80  LEU F CD1 
10900 C CD2 . LEU F 80  ? 0.4976 0.3632 0.2178 0.0489  0.0027  -0.0123 80  LEU F CD2 
10901 N N   . ASN F 81  ? 0.5548 0.3362 0.2145 -0.0010 -0.0535 -0.0064 81  ASN F N   
10902 C CA  . ASN F 81  ? 0.5905 0.3334 0.2166 -0.0050 -0.0611 -0.0090 81  ASN F CA  
10903 C C   . ASN F 81  ? 0.5567 0.3342 0.2187 -0.0253 -0.0779 -0.0015 81  ASN F C   
10904 O O   . ASN F 81  ? 0.5496 0.3257 0.2190 -0.0197 -0.0757 -0.0044 81  ASN F O   
10905 C CB  . ASN F 81  ? 0.6770 0.3414 0.2181 -0.0188 -0.0721 -0.0105 81  ASN F CB  
10906 C CG  . ASN F 81  ? 0.7373 0.3389 0.2203 -0.0256 -0.0794 -0.0136 81  ASN F CG  
10907 O OD1 . ASN F 81  ? 0.7457 0.3317 0.2204 0.0033  -0.0628 -0.0195 81  ASN F OD1 
10908 N ND2 . ASN F 81  ? 0.7859 0.3523 0.2234 -0.0658 -0.1046 -0.0075 81  ASN F ND2 
10909 N N   . LYS F 82  ? 0.5389 0.3520 0.2219 -0.0456 -0.0936 0.0101  82  LYS F N   
10910 C CA  . LYS F 82  ? 0.5096 0.3683 0.2271 -0.0624 -0.1085 0.0220  82  LYS F CA  
10911 C C   . LYS F 82  ? 0.4487 0.3502 0.2244 -0.0419 -0.0945 0.0201  82  LYS F C   
10912 O O   . LYS F 82  ? 0.4365 0.3460 0.2256 -0.0456 -0.0981 0.0204  82  LYS F O   
10913 C CB  . LYS F 82  ? 0.5019 0.4083 0.2340 -0.0785 -0.1242 0.0402  82  LYS F CB  
10914 C CG  . LYS F 82  ? 0.4680 0.4403 0.2422 -0.0885 -0.1359 0.0573  82  LYS F CG  
10915 C CD  . LYS F 82  ? 0.4764 0.5052 0.2541 -0.1078 -0.1552 0.0816  82  LYS F CD  
10916 C CE  . LYS F 82  ? 0.4386 0.5215 0.2562 -0.0757 -0.1434 0.0935  82  LYS F CE  
10917 N NZ  . LYS F 82  ? 0.4537 0.5944 0.2688 -0.0872 -0.1603 0.1191  82  LYS F NZ  
10918 N N   . LYS F 83  ? 0.9226 0.7348 0.1797 -0.0069 -0.0344 0.0993  83  LYS F N   
10919 C CA  . LYS F 83  ? 0.8964 0.6763 0.1803 0.0125  -0.0122 0.0997  83  LYS F CA  
10920 C C   . LYS F 83  ? 0.8487 0.6111 0.1713 -0.0099 0.0027  0.0671  83  LYS F C   
10921 O O   . LYS F 83  ? 0.8045 0.5730 0.1711 -0.0016 0.0072  0.0648  83  LYS F O   
10922 C CB  . LYS F 83  ? 0.9589 0.6719 0.1852 0.0300  0.0123  0.1139  83  LYS F CB  
10923 C CG  . LYS F 83  ? 1.0017 0.7168 0.1999 0.0755  0.0068  0.1523  83  LYS F CG  
10924 C CD  . LYS F 83  ? 0.9904 0.7992 0.2086 0.0903  -0.0278 0.1744  83  LYS F CD  
10925 C CE  . LYS F 83  ? 1.0326 0.8573 0.2278 0.1477  -0.0304 0.2159  83  LYS F CE  
10926 N NZ  . LYS F 83  ? 1.1154 0.9210 0.2371 0.1683  -0.0318 0.2403  83  LYS F NZ  
10927 N N   . MET F 84  ? 0.8626 0.6060 0.1658 -0.0345 0.0112  0.0432  84  MET F N   
10928 C CA  . MET F 84  ? 0.8255 0.5623 0.1619 -0.0477 0.0257  0.0147  84  MET F CA  
10929 C C   . MET F 84  ? 0.7805 0.5508 0.1607 -0.0512 0.0052  0.0076  84  MET F C   
10930 O O   . MET F 84  ? 0.7340 0.5107 0.1599 -0.0457 0.0117  0.0003  84  MET F O   
10931 C CB  . MET F 84  ? 0.8621 0.5762 0.1611 -0.0647 0.0394  -0.0067 84  MET F CB  
10932 C CG  . MET F 84  ? 0.8359 0.5481 0.1628 -0.0676 0.0633  -0.0310 84  MET F CG  
10933 S SD  . MET F 84  ? 0.8662 0.5651 0.1659 -0.0743 0.0661  -0.0587 84  MET F SD  
10934 C CE  . MET F 84  ? 0.8401 0.5485 0.1649 -0.0768 0.0352  -0.0591 84  MET F CE  
10935 N N   . GLU F 85  ? 0.8010 0.5917 0.1616 -0.0647 -0.0198 0.0104  85  GLU F N   
10936 C CA  . GLU F 85  ? 0.7754 0.5903 0.1626 -0.0781 -0.0396 0.0033  85  GLU F CA  
10937 C C   . GLU F 85  ? 0.7252 0.5858 0.1653 -0.0613 -0.0503 0.0235  85  GLU F C   
10938 O O   . GLU F 85  ? 0.6841 0.5486 0.1642 -0.0617 -0.0493 0.0139  85  GLU F O   
10939 C CB  . GLU F 85  ? 0.8244 0.6508 0.1662 -0.1074 -0.0650 0.0034  85  GLU F CB  
10940 C CG  . GLU F 85  ? 0.8871 0.6590 0.1647 -0.1233 -0.0535 -0.0175 85  GLU F CG  
10941 C CD  . GLU F 85  ? 0.9336 0.6715 0.1681 -0.1552 -0.0646 -0.0389 85  GLU F CD  
10942 O OE1 . GLU F 85  ? 0.9775 0.7335 0.1724 -0.1867 -0.0909 -0.0315 85  GLU F OE1 
10943 O OE2 . GLU F 85  ? 0.9374 0.6274 0.1693 -0.1491 -0.0462 -0.0626 85  GLU F OE2 
10944 N N   . ASP F 86  ? 0.7349 0.6280 0.1704 -0.0419 -0.0586 0.0527  86  ASP F N   
10945 C CA  . ASP F 86  ? 0.6988 0.6340 0.1765 -0.0161 -0.0642 0.0751  86  ASP F CA  
10946 C C   . ASP F 86  ? 0.6674 0.5629 0.1723 0.0016  -0.0389 0.0678  86  ASP F C   
10947 O O   . ASP F 86  ? 0.6262 0.5450 0.1741 0.0103  -0.0419 0.0710  86  ASP F O   
10948 C CB  . ASP F 86  ? 0.7336 0.7020 0.1875 0.0138  -0.0718 0.1102  86  ASP F CB  
10949 C CG  . ASP F 86  ? 0.7376 0.7969 0.1986 0.0039  -0.1048 0.1298  86  ASP F CG  
10950 O OD1 . ASP F 86  ? 0.6989 0.8068 0.2021 -0.0104 -0.1189 0.1277  86  ASP F OD1 
10951 O OD2 . ASP F 86  ? 0.7828 0.8698 0.2055 0.0078  -0.1170 0.1484  86  ASP F OD2 
10952 N N   . GLY F 87  ? 0.6920 0.5310 0.1679 0.0029  -0.0143 0.0589  87  GLY F N   
10953 C CA  . GLY F 87  ? 0.6756 0.4772 0.1659 0.0096  0.0099  0.0519  87  GLY F CA  
10954 C C   . GLY F 87  ? 0.6218 0.4348 0.1609 -0.0040 0.0117  0.0289  87  GLY F C   
10955 O O   . GLY F 87  ? 0.5920 0.4045 0.1615 0.0045  0.0180  0.0304  87  GLY F O   
10956 N N   . PHE F 88  ? 0.6191 0.4361 0.1575 -0.0228 0.0070  0.0084  88  PHE F N   
10957 C CA  . PHE F 88  ? 0.5818 0.4042 0.1559 -0.0296 0.0086  -0.0119 88  PHE F CA  
10958 C C   . PHE F 88  ? 0.5501 0.4035 0.1578 -0.0292 -0.0130 -0.0050 88  PHE F C   
10959 O O   . PHE F 88  ? 0.5130 0.3705 0.1573 -0.0262 -0.0096 -0.0128 88  PHE F O   
10960 C CB  . PHE F 88  ? 0.6091 0.4128 0.1558 -0.0419 0.0126  -0.0340 88  PHE F CB  
10961 C CG  . PHE F 88  ? 0.6254 0.4137 0.1568 -0.0412 0.0398  -0.0460 88  PHE F CG  
10962 C CD1 . PHE F 88  ? 0.5940 0.3950 0.1589 -0.0371 0.0584  -0.0525 88  PHE F CD1 
10963 C CD2 . PHE F 88  ? 0.6749 0.4443 0.1573 -0.0480 0.0466  -0.0501 88  PHE F CD2 
10964 C CE1 . PHE F 88  ? 0.6102 0.4156 0.1635 -0.0420 0.0831  -0.0617 88  PHE F CE1 
10965 C CE2 . PHE F 88  ? 0.6913 0.4575 0.1609 -0.0494 0.0731  -0.0600 88  PHE F CE2 
10966 C CZ  . PHE F 88  ? 0.6581 0.4476 0.1649 -0.0475 0.0913  -0.0652 88  PHE F CZ  
10967 N N   . LEU F 89  ? 0.5668 0.4495 0.1618 -0.0344 -0.0354 0.0106  89  LEU F N   
10968 C CA  . LEU F 89  ? 0.5403 0.4673 0.1670 -0.0383 -0.0558 0.0210  89  LEU F CA  
10969 C C   . LEU F 89  ? 0.5043 0.4506 0.1694 -0.0119 -0.0489 0.0373  89  LEU F C   
10970 O O   . LEU F 89  ? 0.4697 0.4358 0.1704 -0.0134 -0.0545 0.0361  89  LEU F O   
10971 C CB  . LEU F 89  ? 0.5688 0.5445 0.1747 -0.0521 -0.0814 0.0388  89  LEU F CB  
10972 C CG  . LEU F 89  ? 0.6176 0.5705 0.1748 -0.0875 -0.0925 0.0224  89  LEU F CG  
10973 C CD1 . LEU F 89  ? 0.6479 0.6634 0.1839 -0.1057 -0.1197 0.0439  89  LEU F CD1 
10974 C CD2 . LEU F 89  ? 0.6197 0.5378 0.1745 -0.1107 -0.0943 -0.0009 89  LEU F CD2 
10975 N N   . ASP F 90  ? 0.5238 0.4546 0.1716 0.0121  -0.0352 0.0525  90  ASP F N   
10976 C CA  . ASP F 90  ? 0.5115 0.4380 0.1760 0.0396  -0.0236 0.0669  90  ASP F CA  
10977 C C   . ASP F 90  ? 0.4839 0.3742 0.1695 0.0320  -0.0060 0.0467  90  ASP F C   
10978 O O   . ASP F 90  ? 0.4571 0.3560 0.1714 0.0420  -0.0043 0.0506  90  ASP F O   
10979 C CB  . ASP F 90  ? 0.5637 0.4570 0.1821 0.0667  -0.0096 0.0871  90  ASP F CB  
10980 C CG  . ASP F 90  ? 0.5925 0.5358 0.1929 0.0848  -0.0276 0.1139  90  ASP F CG  
10981 O OD1 . ASP F 90  ? 0.5660 0.5822 0.1972 0.0746  -0.0516 0.1197  90  ASP F OD1 
10982 O OD2 . ASP F 90  ? 0.6476 0.5593 0.1988 0.1069  -0.0179 0.1302  90  ASP F OD2 
10983 N N   . VAL F 91  ? 0.4929 0.3511 0.1641 0.0146  0.0072  0.0265  91  VAL F N   
10984 C CA  . VAL F 91  ? 0.4679 0.3111 0.1610 0.0051  0.0224  0.0083  91  VAL F CA  
10985 C C   . VAL F 91  ? 0.4249 0.2953 0.1599 0.0000  0.0097  -0.0028 91  VAL F C   
10986 O O   . VAL F 91  ? 0.3965 0.2705 0.1600 0.0033  0.0138  -0.0047 91  VAL F O   
10987 C CB  . VAL F 91  ? 0.4881 0.3132 0.1598 -0.0105 0.0391  -0.0086 91  VAL F CB  
10988 C CG1 . VAL F 91  ? 0.4570 0.2951 0.1603 -0.0192 0.0503  -0.0265 91  VAL F CG1 
10989 C CG2 . VAL F 91  ? 0.5371 0.3238 0.1621 -0.0118 0.0565  0.0017  91  VAL F CG2 
10990 N N   . TRP F 92  ? 0.4311 0.3118 0.1601 -0.0100 -0.0051 -0.0102 92  TRP F N   
10991 C CA  . TRP F 92  ? 0.4100 0.2983 0.1613 -0.0171 -0.0158 -0.0209 92  TRP F CA  
10992 C C   . TRP F 92  ? 0.3866 0.3076 0.1637 -0.0161 -0.0324 -0.0052 92  TRP F C   
10993 O O   . TRP F 92  ? 0.3614 0.2859 0.1643 -0.0178 -0.0352 -0.0106 92  TRP F O   
10994 C CB  . TRP F 92  ? 0.4471 0.3144 0.1637 -0.0315 -0.0230 -0.0354 92  TRP F CB  
10995 C CG  . TRP F 92  ? 0.4636 0.3061 0.1653 -0.0248 -0.0027 -0.0537 92  TRP F CG  
10996 C CD1 . TRP F 92  ? 0.5011 0.3278 0.1663 -0.0266 0.0072  -0.0594 92  TRP F CD1 
10997 C CD2 . TRP F 92  ? 0.4445 0.2875 0.1692 -0.0126 0.0109  -0.0664 92  TRP F CD2 
10998 N NE1 . TRP F 92  ? 0.5052 0.3277 0.1711 -0.0156 0.0276  -0.0748 92  TRP F NE1 
10999 C CE2 . TRP F 92  ? 0.4705 0.3072 0.1739 -0.0056 0.0296  -0.0785 92  TRP F CE2 
11000 C CE3 . TRP F 92  ? 0.4101 0.2648 0.1708 -0.0056 0.0092  -0.0674 92  TRP F CE3 
11001 C CZ2 . TRP F 92  ? 0.4616 0.3151 0.1820 0.0106  0.0463  -0.0897 92  TRP F CZ2 
11002 C CZ3 . TRP F 92  ? 0.4025 0.2664 0.1773 0.0092  0.0242  -0.0790 92  TRP F CZ3 
11003 C CH2 . TRP F 92  ? 0.4275 0.2964 0.1839 0.0185  0.0424  -0.0892 92  TRP F CH2 
11004 N N   . THR F 93  ? 0.3976 0.3488 0.1673 -0.0108 -0.0426 0.0159  93  THR F N   
11005 C CA  . THR F 93  ? 0.3762 0.3757 0.1736 -0.0036 -0.0549 0.0351  93  THR F CA  
11006 C C   . THR F 93  ? 0.3511 0.3384 0.1726 0.0187  -0.0385 0.0390  93  THR F C   
11007 O O   . THR F 93  ? 0.3236 0.3307 0.1749 0.0185  -0.0429 0.0405  93  THR F O   
11008 C CB  . THR F 93  ? 0.3981 0.4464 0.1824 0.0077  -0.0663 0.0616  93  THR F CB  
11009 O OG1 . THR F 93  ? 0.4265 0.4895 0.1840 -0.0208 -0.0841 0.0578  93  THR F OG1 
11010 C CG2 . THR F 93  ? 0.3765 0.4915 0.1933 0.0206  -0.0763 0.0838  93  THR F CG2 
11011 N N   . TYR F 94  ? 0.3702 0.3189 0.1703 0.0336  -0.0190 0.0402  94  TYR F N   
11012 C CA  . TYR F 94  ? 0.3660 0.2866 0.1704 0.0480  -0.0013 0.0422  94  TYR F CA  
11013 C C   . TYR F 94  ? 0.3305 0.2442 0.1644 0.0321  0.0019  0.0219  94  TYR F C   
11014 O O   . TYR F 94  ? 0.3110 0.2287 0.1651 0.0387  0.0041  0.0250  94  TYR F O   
11015 C CB  . TYR F 94  ? 0.4124 0.2788 0.1708 0.0540  0.0195  0.0441  94  TYR F CB  
11016 C CG  . TYR F 94  ? 0.4254 0.2451 0.1710 0.0531  0.0401  0.0395  94  TYR F CG  
11017 C CD1 . TYR F 94  ? 0.4111 0.2199 0.1657 0.0261  0.0493  0.0182  94  TYR F CD1 
11018 C CD2 . TYR F 94  ? 0.4616 0.2491 0.1791 0.0795  0.0514  0.0573  94  TYR F CD2 
11019 C CE1 . TYR F 94  ? 0.4293 0.2014 0.1671 0.0158  0.0662  0.0141  94  TYR F CE1 
11020 C CE2 . TYR F 94  ? 0.4889 0.2203 0.1800 0.0720  0.0708  0.0515  94  TYR F CE2 
11021 C CZ  . TYR F 94  ? 0.4712 0.1973 0.1731 0.0354  0.0768  0.0295  94  TYR F CZ  
11022 O OH  . TYR F 94  ? 0.5037 0.1803 0.1749 0.0188  0.0942  0.0238  94  TYR F OH  
11023 N N   . ASN F 95  ? 0.3275 0.2331 0.1604 0.0152  0.0031  0.0027  95  ASN F N   
11024 C CA  . ASN F 95  ? 0.3012 0.2080 0.1587 0.0069  0.0062  -0.0143 95  ASN F CA  
11025 C C   . ASN F 95  ? 0.2758 0.2018 0.1602 0.0062  -0.0091 -0.0136 95  ASN F C   
11026 O O   . ASN F 95  ? 0.2529 0.1816 0.1599 0.0080  -0.0061 -0.0166 95  ASN F O   
11027 C CB  . ASN F 95  ? 0.3133 0.2149 0.1591 -0.0007 0.0104  -0.0315 95  ASN F CB  
11028 C CG  . ASN F 95  ? 0.3344 0.2256 0.1596 -0.0060 0.0294  -0.0352 95  ASN F CG  
11029 O OD1 . ASN F 95  ? 0.3463 0.2223 0.1602 -0.0086 0.0402  -0.0270 95  ASN F OD1 
11030 N ND2 . ASN F 95  ? 0.3502 0.2440 0.1620 -0.0089 0.0354  -0.0475 95  ASN F ND2 
11031 N N   . ALA F 96  ? 0.2868 0.2253 0.1626 -0.0013 -0.0258 -0.0094 96  ALA F N   
11032 C CA  . ALA F 96  ? 0.2761 0.2300 0.1658 -0.0115 -0.0414 -0.0078 96  ALA F CA  
11033 C C   . ALA F 96  ? 0.2508 0.2364 0.1680 -0.0014 -0.0427 0.0091  96  ALA F C   
11034 O O   . ALA F 96  ? 0.2310 0.2178 0.1684 -0.0031 -0.0438 0.0062  96  ALA F O   
11035 C CB  . ALA F 96  ? 0.3071 0.2702 0.1706 -0.0320 -0.0589 -0.0049 96  ALA F CB  
11036 N N   . GLU F 97  ? 0.2584 0.2679 0.1715 0.0135  -0.0412 0.0281  97  GLU F N   
11037 C CA  . GLU F 97  ? 0.2458 0.2884 0.1783 0.0319  -0.0398 0.0472  97  GLU F CA  
11038 C C   . GLU F 97  ? 0.2366 0.2428 0.1739 0.0457  -0.0212 0.0421  97  GLU F C   
11039 O O   . GLU F 97  ? 0.2204 0.2422 0.1773 0.0519  -0.0207 0.0479  97  GLU F O   
11040 C CB  . GLU F 97  ? 0.2698 0.3452 0.1880 0.0555  -0.0397 0.0715  97  GLU F CB  
11041 C CG  . GLU F 97  ? 0.2788 0.4122 0.1954 0.0373  -0.0619 0.0810  97  GLU F CG  
11042 C CD  . GLU F 97  ? 0.3019 0.4879 0.2089 0.0665  -0.0638 0.1098  97  GLU F CD  
11043 O OE1 . GLU F 97  ? 0.3199 0.4837 0.2138 0.1068  -0.0452 0.1229  97  GLU F OE1 
11044 O OE2 . GLU F 97  ? 0.3117 0.5593 0.2172 0.0492  -0.0836 0.1204  97  GLU F OE2 
11045 N N   . LEU F 98  ? 0.2524 0.2121 0.1678 0.0457  -0.0060 0.0313  98  LEU F N   
11046 C CA  . LEU F 98  ? 0.2553 0.1787 0.1648 0.0476  0.0109  0.0250  98  LEU F CA  
11047 C C   . LEU F 98  ? 0.2211 0.1530 0.1602 0.0318  0.0056  0.0094  98  LEU F C   
11048 O O   . LEU F 98  ? 0.2118 0.1393 0.1601 0.0345  0.0102  0.0105  98  LEU F O   
11049 C CB  . LEU F 98  ? 0.2887 0.1684 0.1623 0.0402  0.0273  0.0175  98  LEU F CB  
11050 C CG  . LEU F 98  ? 0.3118 0.1483 0.1627 0.0331  0.0458  0.0128  98  LEU F CG  
11051 C CD1 . LEU F 98  ? 0.3536 0.1540 0.1703 0.0595  0.0575  0.0311  98  LEU F CD1 
11052 C CD2 . LEU F 98  ? 0.3447 0.1503 0.1619 0.0111  0.0598  0.0026  98  LEU F CD2 
11053 N N   . LEU F 99  ? 0.2108 0.1503 0.1576 0.0189  -0.0026 -0.0041 99  LEU F N   
11054 C CA  . LEU F 99  ? 0.1904 0.1343 0.1570 0.0121  -0.0067 -0.0168 99  LEU F CA  
11055 C C   . LEU F 99  ? 0.1738 0.1322 0.1588 0.0122  -0.0182 -0.0095 99  LEU F C   
11056 O O   . LEU F 99  ? 0.1591 0.1168 0.1583 0.0123  -0.0164 -0.0128 99  LEU F O   
11057 C CB  . LEU F 99  ? 0.2012 0.1408 0.1591 0.0079  -0.0116 -0.0298 99  LEU F CB  
11058 C CG  . LEU F 99  ? 0.1953 0.1344 0.1633 0.0115  -0.0125 -0.0414 99  LEU F CG  
11059 C CD1 . LEU F 99  ? 0.1809 0.1381 0.1641 0.0123  0.0000  -0.0458 99  LEU F CD1 
11060 C CD2 . LEU F 99  ? 0.2245 0.1467 0.1687 0.0166  -0.0133 -0.0525 99  LEU F CD2 
11061 N N   . VAL F 100 ? 0.1789 0.1566 0.1619 0.0088  -0.0305 0.0011  100 VAL F N   
11062 C CA  . VAL F 100 ? 0.1675 0.1699 0.1662 0.0030  -0.0409 0.0104  100 VAL F CA  
11063 C C   . VAL F 100 ? 0.1542 0.1668 0.1667 0.0198  -0.0299 0.0216  100 VAL F C   
11064 O O   . VAL F 100 ? 0.1408 0.1531 0.1667 0.0171  -0.0303 0.0197  100 VAL F O   
11065 C CB  . VAL F 100 ? 0.1812 0.2203 0.1735 -0.0103 -0.0563 0.0227  100 VAL F CB  
11066 C CG1 . VAL F 100 ? 0.1702 0.2557 0.1821 -0.0170 -0.0642 0.0377  100 VAL F CG1 
11067 C CG2 . VAL F 100 ? 0.2090 0.2193 0.1738 -0.0339 -0.0673 0.0088  100 VAL F CG2 
11068 N N   . LEU F 101 ? 0.1683 0.1809 0.1683 0.0392  -0.0187 0.0333  101 LEU F N   
11069 C CA  . LEU F 101 ? 0.1775 0.1795 0.1714 0.0606  -0.0032 0.0436  101 LEU F CA  
11070 C C   . LEU F 101 ? 0.1749 0.1364 0.1645 0.0525  0.0072  0.0291  101 LEU F C   
11071 O O   . LEU F 101 ? 0.1708 0.1323 0.1663 0.0574  0.0114  0.0325  101 LEU F O   
11072 C CB  . LEU F 101 ? 0.2168 0.1967 0.1764 0.0853  0.0110  0.0558  101 LEU F CB  
11073 C CG  . LEU F 101 ? 0.2357 0.2557 0.1912 0.1189  0.0136  0.0824  101 LEU F CG  
11074 C CD1 . LEU F 101 ? 0.2060 0.3112 0.1987 0.1080  -0.0080 0.0932  101 LEU F CD1 
11075 C CD2 . LEU F 101 ? 0.2814 0.2734 0.1959 0.1414  0.0238  0.0926  101 LEU F CD2 
11076 N N   . MET F 102 ? 0.1799 0.1147 0.1579 0.0387  0.0115  0.0140  102 MET F N   
11077 C CA  . MET F 102 ? 0.1818 0.0937 0.1541 0.0255  0.0203  0.0016  102 MET F CA  
11078 C C   . MET F 102 ? 0.1497 0.0852 0.1527 0.0170  0.0082  -0.0060 102 MET F C   
11079 O O   . MET F 102 ? 0.1483 0.0773 0.1522 0.0130  0.0121  -0.0078 102 MET F O   
11080 C CB  . MET F 102 ? 0.1963 0.0950 0.1519 0.0101  0.0274  -0.0100 102 MET F CB  
11081 C CG  . MET F 102 ? 0.2446 0.1006 0.1543 0.0133  0.0434  -0.0035 102 MET F CG  
11082 S SD  . MET F 102 ? 0.2713 0.1121 0.1540 -0.0168 0.0555  -0.0174 102 MET F SD  
11083 C CE  . MET F 102 ? 0.2300 0.1248 0.1526 -0.0152 0.0406  -0.0263 102 MET F CE  
11084 N N   . GLU F 103 ? 0.1349 0.0891 0.1533 0.0146  -0.0056 -0.0100 103 GLU F N   
11085 C CA  . GLU F 103 ? 0.1215 0.0831 0.1549 0.0108  -0.0157 -0.0164 103 GLU F CA  
11086 C C   . GLU F 103 ? 0.1150 0.0849 0.1580 0.0101  -0.0235 -0.0063 103 GLU F C   
11087 O O   . GLU F 103 ? 0.1096 0.0770 0.1591 0.0076  -0.0273 -0.0091 103 GLU F O   
11088 C CB  . GLU F 103 ? 0.1303 0.0881 0.1576 0.0107  -0.0235 -0.0253 103 GLU F CB  
11089 C CG  . GLU F 103 ? 0.1348 0.0986 0.1583 0.0135  -0.0144 -0.0359 103 GLU F CG  
11090 C CD  . GLU F 103 ? 0.1247 0.1090 0.1607 0.0138  -0.0099 -0.0412 103 GLU F CD  
11091 O OE1 . GLU F 103 ? 0.1170 0.1014 0.1615 0.0156  -0.0157 -0.0386 103 GLU F OE1 
11092 O OE2 . GLU F 103 ? 0.1272 0.1342 0.1634 0.0095  -0.0010 -0.0470 103 GLU F OE2 
11093 N N   . ASN F 104 ? 0.1183 0.1056 0.1617 0.0126  -0.0256 0.0068  104 ASN F N   
11094 C CA  . ASN F 104 ? 0.1129 0.1246 0.1677 0.0118  -0.0293 0.0195  104 ASN F CA  
11095 C C   . ASN F 104 ? 0.1121 0.1133 0.1673 0.0224  -0.0162 0.0217  104 ASN F C   
11096 O O   . ASN F 104 ? 0.1053 0.1124 0.1687 0.0175  -0.0191 0.0237  104 ASN F O   
11097 C CB  . ASN F 104 ? 0.1177 0.1709 0.1755 0.0182  -0.0312 0.0372  104 ASN F CB  
11098 C CG  . ASN F 104 ? 0.1251 0.2000 0.1801 -0.0046 -0.0488 0.0383  104 ASN F CG  
11099 O OD1 . ASN F 104 ? 0.1347 0.1811 0.1782 -0.0241 -0.0581 0.0263  104 ASN F OD1 
11100 N ND2 . ASN F 104 ? 0.1307 0.2535 0.1880 -0.0017 -0.0528 0.0538  104 ASN F ND2 
11101 N N   . GLU F 105 ? 0.1296 0.1066 0.1662 0.0343  -0.0008 0.0213  105 GLU F N   
11102 C CA  . GLU F 105 ? 0.1476 0.0974 0.1669 0.0404  0.0140  0.0216  105 GLU F CA  
11103 C C   . GLU F 105 ? 0.1369 0.0764 0.1613 0.0223  0.0097  0.0076  105 GLU F C   
11104 O O   . GLU F 105 ? 0.1408 0.0733 0.1616 0.0211  0.0133  0.0086  105 GLU F O   
11105 C CB  . GLU F 105 ? 0.1896 0.0954 0.1686 0.0498  0.0325  0.0222  105 GLU F CB  
11106 C CG  . GLU F 105 ? 0.2313 0.0932 0.1730 0.0589  0.0514  0.0254  105 GLU F CG  
11107 C CD  . GLU F 105 ? 0.2949 0.1019 0.1807 0.0797  0.0726  0.0335  105 GLU F CD  
11108 O OE1 . GLU F 105 ? 0.3169 0.0940 0.1786 0.0661  0.0763  0.0260  105 GLU F OE1 
11109 O OE2 . GLU F 105 ? 0.3318 0.1235 0.1924 0.1123  0.0874  0.0485  105 GLU F OE2 
11110 N N   . ARG F 106 ? 0.1272 0.0709 0.1582 0.0113  0.0027  -0.0041 106 ARG F N   
11111 C CA  . ARG F 106 ? 0.1186 0.0697 0.1571 0.0004  -0.0024 -0.0142 106 ARG F CA  
11112 C C   . ARG F 106 ? 0.1028 0.0651 0.1576 0.0031  -0.0158 -0.0117 106 ARG F C   
11113 O O   . ARG F 106 ? 0.1016 0.0663 0.1579 -0.0003 -0.0183 -0.0139 106 ARG F O   
11114 C CB  . ARG F 106 ? 0.1182 0.0838 0.1597 -0.0044 -0.0041 -0.0245 106 ARG F CB  
11115 C CG  . ARG F 106 ? 0.1421 0.0959 0.1605 -0.0178 0.0098  -0.0287 106 ARG F CG  
11116 C CD  . ARG F 106 ? 0.1401 0.1306 0.1661 -0.0303 0.0090  -0.0385 106 ARG F CD  
11117 N NE  . ARG F 106 ? 0.1513 0.1565 0.1697 -0.0515 0.0115  -0.0420 106 ARG F NE  
11118 C CZ  . ARG F 106 ? 0.1413 0.2030 0.1782 -0.0569 0.0050  -0.0461 106 ARG F CZ  
11119 N NH1 . ARG F 106 ? 0.1237 0.2254 0.1850 -0.0353 -0.0019 -0.0473 106 ARG F NH1 
11120 N NH2 . ARG F 106 ? 0.1566 0.2363 0.1823 -0.0824 0.0060  -0.0480 106 ARG F NH2 
11121 N N   . THR F 107 ? 0.0985 0.0645 0.1582 0.0055  -0.0247 -0.0066 107 THR F N   
11122 C CA  . THR F 107 ? 0.1008 0.0633 0.1611 0.0010  -0.0363 -0.0038 107 THR F CA  
11123 C C   . THR F 107 ? 0.0963 0.0656 0.1607 -0.0019 -0.0334 0.0053  107 THR F C   
11124 O O   . THR F 107 ? 0.1013 0.0617 0.1623 -0.0056 -0.0387 0.0048  107 THR F O   
11125 C CB  . THR F 107 ? 0.1139 0.0740 0.1657 -0.0075 -0.0460 -0.0004 107 THR F CB  
11126 O OG1 . THR F 107 ? 0.1257 0.0702 0.1657 -0.0028 -0.0477 -0.0103 107 THR F OG1 
11127 C CG2 . THR F 107 ? 0.1357 0.0780 0.1725 -0.0206 -0.0563 0.0024  107 THR F CG2 
11128 N N   . LEU F 108 ? 0.0927 0.0765 0.1599 0.0038  -0.0234 0.0150  108 LEU F N   
11129 C CA  . LEU F 108 ? 0.0943 0.0879 0.1624 0.0064  -0.0168 0.0247  108 LEU F CA  
11130 C C   . LEU F 108 ? 0.1009 0.0692 0.1563 0.0069  -0.0086 0.0175  108 LEU F C   
11131 O O   . LEU F 108 ? 0.1033 0.0709 0.1572 0.0028  -0.0093 0.0203  108 LEU F O   
11132 C CB  . LEU F 108 ? 0.1006 0.1188 0.1691 0.0232  -0.0047 0.0392  108 LEU F CB  
11133 C CG  . LEU F 108 ? 0.0947 0.1563 0.1766 0.0199  -0.0141 0.0497  108 LEU F CG  
11134 C CD1 . LEU F 108 ? 0.1046 0.2031 0.1871 0.0466  -0.0004 0.0681  108 LEU F CD1 
11135 C CD2 . LEU F 108 ? 0.0926 0.1776 0.1827 -0.0066 -0.0299 0.0532  108 LEU F CD2 
11136 N N   . ASP F 109 ? 0.1088 0.0573 0.1505 0.0070  -0.0010 0.0085  109 ASP F N   
11137 C CA  . ASP F 109 ? 0.1231 0.0524 0.1465 -0.0029 0.0045  0.0005  109 ASP F CA  
11138 C C   . ASP F 109 ? 0.1081 0.0545 0.1452 -0.0115 -0.0107 -0.0059 109 ASP F C   
11139 O O   . ASP F 109 ? 0.1170 0.0612 0.1445 -0.0197 -0.0110 -0.0080 109 ASP F O   
11140 C CB  . ASP F 109 ? 0.1475 0.0529 0.1447 -0.0102 0.0165  -0.0068 109 ASP F CB  
11141 C CG  . ASP F 109 ? 0.1848 0.0528 0.1483 0.0045  0.0361  0.0011  109 ASP F CG  
11142 O OD1 . ASP F 109 ? 0.1982 0.0585 0.1526 0.0194  0.0446  0.0105  109 ASP F OD1 
11143 O OD2 . ASP F 109 ? 0.2077 0.0528 0.1491 0.0044  0.0448  -0.0009 109 ASP F OD2 
11144 N N   . PHE F 110 ? 0.0937 0.0538 0.1462 -0.0066 -0.0223 -0.0081 110 PHE F N   
11145 C CA  . PHE F 110 ? 0.0929 0.0626 0.1497 -0.0024 -0.0348 -0.0110 110 PHE F CA  
11146 C C   . PHE F 110 ? 0.1008 0.0573 0.1519 -0.0031 -0.0407 -0.0036 110 PHE F C   
11147 O O   . PHE F 110 ? 0.1084 0.0688 0.1540 -0.0024 -0.0454 -0.0036 110 PHE F O   
11148 C CB  . PHE F 110 ? 0.0950 0.0630 0.1540 0.0083  -0.0414 -0.0139 110 PHE F CB  
11149 C CG  . PHE F 110 ? 0.1126 0.0773 0.1629 0.0238  -0.0508 -0.0149 110 PHE F CG  
11150 C CD1 . PHE F 110 ? 0.1120 0.1112 0.1680 0.0328  -0.0522 -0.0172 110 PHE F CD1 
11151 C CD2 . PHE F 110 ? 0.1410 0.0669 0.1694 0.0300  -0.0576 -0.0124 110 PHE F CD2 
11152 C CE1 . PHE F 110 ? 0.1369 0.1357 0.1805 0.0583  -0.0594 -0.0148 110 PHE F CE1 
11153 C CE2 . PHE F 110 ? 0.1767 0.0812 0.1810 0.0518  -0.0631 -0.0121 110 PHE F CE2 
11154 C CZ  . PHE F 110 ? 0.1734 0.1163 0.1871 0.0716  -0.0635 -0.0122 110 PHE F CZ  
11155 N N   . HIS F 111 ? 0.1016 0.0494 0.1526 -0.0069 -0.0405 0.0039  111 HIS F N   
11156 C CA  . HIS F 111 ? 0.1129 0.0523 0.1560 -0.0142 -0.0440 0.0123  111 HIS F CA  
11157 C C   . HIS F 111 ? 0.1122 0.0554 0.1522 -0.0162 -0.0348 0.0145  111 HIS F C   
11158 O O   . HIS F 111 ? 0.1244 0.0589 0.1540 -0.0199 -0.0392 0.0173  111 HIS F O   
11159 C CB  . HIS F 111 ? 0.1144 0.0647 0.1610 -0.0245 -0.0440 0.0217  111 HIS F CB  
11160 C CG  . HIS F 111 ? 0.1335 0.0658 0.1666 -0.0327 -0.0552 0.0198  111 HIS F CG  
11161 N ND1 . HIS F 111 ? 0.1707 0.0609 0.1732 -0.0375 -0.0646 0.0181  111 HIS F ND1 
11162 C CD2 . HIS F 111 ? 0.1326 0.0737 0.1678 -0.0372 -0.0573 0.0194  111 HIS F CD2 
11163 C CE1 . HIS F 111 ? 0.1979 0.0635 0.1785 -0.0459 -0.0707 0.0154  111 HIS F CE1 
11164 N NE2 . HIS F 111 ? 0.1713 0.0721 0.1745 -0.0480 -0.0675 0.0158  111 HIS F NE2 
11165 N N   . ASP F 112 ? 0.1084 0.0550 0.1477 -0.0130 -0.0208 0.0135  112 ASP F N   
11166 C CA  . ASP F 112 ? 0.1247 0.0586 0.1453 -0.0149 -0.0084 0.0138  112 ASP F CA  
11167 C C   . ASP F 112 ? 0.1328 0.0631 0.1424 -0.0253 -0.0152 0.0051  112 ASP F C   
11168 O O   . ASP F 112 ? 0.1474 0.0704 0.1423 -0.0314 -0.0147 0.0066  112 ASP F O   
11169 C CB  . ASP F 112 ? 0.1402 0.0583 0.1443 -0.0066 0.0101  0.0136  112 ASP F CB  
11170 C CG  . ASP F 112 ? 0.1760 0.0648 0.1456 -0.0035 0.0281  0.0157  112 ASP F CG  
11171 O OD1 . ASP F 112 ? 0.1800 0.0714 0.1467 -0.0078 0.0263  0.0189  112 ASP F OD1 
11172 O OD2 . ASP F 112 ? 0.2101 0.0641 0.1466 0.0041  0.0459  0.0142  112 ASP F OD2 
11173 N N   . SER F 113 ? 0.1246 0.0691 0.1416 -0.0273 -0.0217 -0.0027 113 SER F N   
11174 C CA  . SER F 113 ? 0.1297 0.0964 0.1432 -0.0362 -0.0303 -0.0083 113 SER F CA  
11175 C C   . SER F 113 ? 0.1315 0.1077 0.1489 -0.0261 -0.0448 -0.0025 113 SER F C   
11176 O O   . SER F 113 ? 0.1443 0.1330 0.1503 -0.0336 -0.0495 -0.0019 113 SER F O   
11177 C CB  . SER F 113 ? 0.1187 0.1150 0.1454 -0.0357 -0.0336 -0.0148 113 SER F CB  
11178 O OG  . SER F 113 ? 0.1201 0.1617 0.1520 -0.0377 -0.0444 -0.0162 113 SER F OG  
11179 N N   . ASN F 114 ? 0.1290 0.0932 0.1535 -0.0110 -0.0517 0.0022  114 ASN F N   
11180 C CA  . ASN F 114 ? 0.1495 0.1022 0.1618 0.0012  -0.0635 0.0086  114 ASN F CA  
11181 C C   . ASN F 114 ? 0.1648 0.0980 0.1610 -0.0089 -0.0625 0.0155  114 ASN F C   
11182 O O   . ASN F 114 ? 0.1857 0.1167 0.1664 -0.0025 -0.0711 0.0202  114 ASN F O   
11183 C CB  . ASN F 114 ? 0.1640 0.0858 0.1680 0.0123  -0.0680 0.0108  114 ASN F CB  
11184 C CG  . ASN F 114 ? 0.1605 0.0970 0.1721 0.0294  -0.0694 0.0046  114 ASN F CG  
11185 O OD1 . ASN F 114 ? 0.1534 0.1312 0.1754 0.0400  -0.0711 0.0018  114 ASN F OD1 
11186 N ND2 . ASN F 114 ? 0.1696 0.0783 0.1737 0.0300  -0.0688 0.0032  114 ASN F ND2 
11187 N N   . VAL F 115 ? 0.1584 0.0818 0.1567 -0.0213 -0.0512 0.0178  115 VAL F N   
11188 C CA  . VAL F 115 ? 0.1735 0.0852 0.1574 -0.0307 -0.0461 0.0247  115 VAL F CA  
11189 C C   . VAL F 115 ? 0.1841 0.1014 0.1539 -0.0375 -0.0427 0.0205  115 VAL F C   
11190 O O   . VAL F 115 ? 0.2038 0.1137 0.1558 -0.0414 -0.0470 0.0250  115 VAL F O   
11191 C CB  . VAL F 115 ? 0.1653 0.0819 0.1571 -0.0354 -0.0314 0.0301  115 VAL F CB  
11192 C CG1 . VAL F 115 ? 0.1826 0.0954 0.1588 -0.0416 -0.0216 0.0371  115 VAL F CG1 
11193 C CG2 . VAL F 115 ? 0.1628 0.0826 0.1636 -0.0395 -0.0372 0.0362  115 VAL F CG2 
11194 N N   . LYS F 116 ? 0.1798 0.1053 0.1499 -0.0430 -0.0347 0.0118  116 LYS F N   
11195 C CA  . LYS F 116 ? 0.2035 0.1265 0.1475 -0.0598 -0.0301 0.0058  116 LYS F CA  
11196 C C   . LYS F 116 ? 0.2080 0.1656 0.1521 -0.0635 -0.0480 0.0056  116 LYS F C   
11197 O O   . LYS F 116 ? 0.2319 0.1903 0.1524 -0.0769 -0.0506 0.0062  116 LYS F O   
11198 C CB  . LYS F 116 ? 0.2124 0.1257 0.1444 -0.0708 -0.0172 -0.0034 116 LYS F CB  
11199 C CG  . LYS F 116 ? 0.2595 0.1286 0.1427 -0.0862 0.0012  -0.0077 116 LYS F CG  
11200 C CD  . LYS F 116 ? 0.2932 0.1650 0.1428 -0.1194 -0.0018 -0.0177 116 LYS F CD  
11201 C CE  . LYS F 116 ? 0.3584 0.1660 0.1422 -0.1360 0.0179  -0.0223 116 LYS F CE  
11202 N NZ  . LYS F 116 ? 0.4110 0.1940 0.1434 -0.1751 0.0239  -0.0346 116 LYS F NZ  
11203 N N   . ASN F 117 ? 0.1901 0.1801 0.1581 -0.0488 -0.0598 0.0060  117 ASN F N   
11204 C CA  . ASN F 117 ? 0.1968 0.2347 0.1678 -0.0410 -0.0762 0.0097  117 ASN F CA  
11205 C C   . ASN F 117 ? 0.2180 0.2381 0.1744 -0.0239 -0.0860 0.0210  117 ASN F C   
11206 O O   . ASN F 117 ? 0.2356 0.2874 0.1808 -0.0231 -0.0970 0.0263  117 ASN F O   
11207 C CB  . ASN F 117 ? 0.1797 0.2561 0.1756 -0.0205 -0.0821 0.0089  117 ASN F CB  
11208 C CG  . ASN F 117 ? 0.1663 0.2689 0.1716 -0.0427 -0.0738 -0.0014 117 ASN F CG  
11209 O OD1 . ASN F 117 ? 0.1806 0.2784 0.1657 -0.0759 -0.0664 -0.0078 117 ASN F OD1 
11210 N ND2 . ASN F 117 ? 0.1496 0.2700 0.1758 -0.0261 -0.0734 -0.0034 117 ASN F ND2 
11211 N N   . LEU F 118 ? 0.2228 0.1939 0.1748 -0.0139 -0.0822 0.0256  118 LEU F N   
11212 C CA  . LEU F 118 ? 0.2552 0.1925 0.1817 -0.0049 -0.0885 0.0364  118 LEU F CA  
11213 C C   . LEU F 118 ? 0.2685 0.1965 0.1763 -0.0267 -0.0830 0.0379  118 LEU F C   
11214 O O   . LEU F 118 ? 0.2973 0.2208 0.1817 -0.0227 -0.0917 0.0459  118 LEU F O   
11215 C CB  . LEU F 118 ? 0.2648 0.1528 0.1843 -0.0021 -0.0846 0.0401  118 LEU F CB  
11216 C CG  . LEU F 118 ? 0.3111 0.1492 0.1926 -0.0017 -0.0887 0.0513  118 LEU F CG  
11217 C CD1 . LEU F 118 ? 0.3530 0.1824 0.2057 0.0277  -0.1020 0.0593  118 LEU F CD1 
11218 C CD2 . LEU F 118 ? 0.3270 0.1222 0.1970 -0.0104 -0.0854 0.0532  118 LEU F CD2 
11219 N N   . TYR F 119 ? 0.2561 0.1767 0.1677 -0.0457 -0.0671 0.0310  119 TYR F N   
11220 C CA  . TYR F 119 ? 0.2781 0.1826 0.1639 -0.0630 -0.0573 0.0311  119 TYR F CA  
11221 C C   . TYR F 119 ? 0.2971 0.2273 0.1640 -0.0771 -0.0656 0.0269  119 TYR F C   
11222 O O   . TYR F 119 ? 0.3251 0.2479 0.1651 -0.0849 -0.0689 0.0314  119 TYR F O   
11223 C CB  . TYR F 119 ? 0.2739 0.1597 0.1583 -0.0706 -0.0350 0.0257  119 TYR F CB  
11224 C CG  . TYR F 119 ? 0.3094 0.1700 0.1559 -0.0837 -0.0203 0.0242  119 TYR F CG  
11225 C CD1 . TYR F 119 ? 0.3248 0.1708 0.1593 -0.0818 -0.0130 0.0336  119 TYR F CD1 
11226 C CD2 . TYR F 119 ? 0.3378 0.1845 0.1520 -0.1015 -0.0123 0.0133  119 TYR F CD2 
11227 C CE1 . TYR F 119 ? 0.3635 0.1838 0.1585 -0.0903 0.0029  0.0322  119 TYR F CE1 
11228 C CE2 . TYR F 119 ? 0.3857 0.1944 0.1511 -0.1134 0.0034  0.0108  119 TYR F CE2 
11229 C CZ  . TYR F 119 ? 0.3964 0.1931 0.1542 -0.1042 0.0115  0.0203  119 TYR F CZ  
11230 O OH  . TYR F 119 ? 0.4495 0.2065 0.1547 -0.1123 0.0296  0.0178  119 TYR F OH  
11231 N N   . ASP F 120 ? 0.2861 0.2512 0.1646 -0.0847 -0.0691 0.0188  120 ASP F N   
11232 C CA  . ASP F 120 ? 0.3071 0.3132 0.1677 -0.1073 -0.0789 0.0154  120 ASP F CA  
11233 C C   . ASP F 120 ? 0.3130 0.3667 0.1795 -0.0879 -0.1012 0.0278  120 ASP F C   
11234 O O   . ASP F 120 ? 0.3402 0.4183 0.1827 -0.1038 -0.1104 0.0308  120 ASP F O   
11235 C CB  . ASP F 120 ? 0.2972 0.3382 0.1683 -0.1251 -0.0773 0.0053  120 ASP F CB  
11236 C CG  . ASP F 120 ? 0.3206 0.3039 0.1598 -0.1504 -0.0543 -0.0067 120 ASP F CG  
11237 O OD1 . ASP F 120 ? 0.3592 0.2904 0.1555 -0.1638 -0.0414 -0.0092 120 ASP F OD1 
11238 O OD2 . ASP F 120 ? 0.3088 0.2943 0.1590 -0.1541 -0.0476 -0.0132 120 ASP F OD2 
11239 N N   . LYS F 121 ? 0.2980 0.3590 0.1884 -0.0515 -0.1088 0.0358  121 LYS F N   
11240 C CA  . LYS F 121 ? 0.3185 0.4090 0.2040 -0.0194 -0.1266 0.0505  121 LYS F CA  
11241 C C   . LYS F 121 ? 0.3547 0.4080 0.2044 -0.0220 -0.1298 0.0595  121 LYS F C   
11242 O O   . LYS F 121 ? 0.3798 0.4742 0.2140 -0.0164 -0.1443 0.0690  121 LYS F O   
11243 C CB  . LYS F 121 ? 0.3177 0.3795 0.2126 0.0203  -0.1269 0.0561  121 LYS F CB  
11244 C CG  . LYS F 121 ? 0.3542 0.4339 0.2332 0.0662  -0.1413 0.0721  121 LYS F CG  
11245 C CD  . LYS F 121 ? 0.3671 0.4015 0.2422 0.1018  -0.1371 0.0738  121 LYS F CD  
11246 C CE  . LYS F 121 ? 0.4160 0.4656 0.2674 0.1592  -0.1471 0.0899  121 LYS F CE  
11247 N NZ  . LYS F 121 ? 0.4852 0.4468 0.2769 0.1798  -0.1493 0.1031  121 LYS F NZ  
11248 N N   . VAL F 122 ? 0.3596 0.3429 0.1962 -0.0310 -0.1160 0.0578  122 VAL F N   
11249 C CA  . VAL F 122 ? 0.3949 0.3386 0.1962 -0.0380 -0.1151 0.0657  122 VAL F CA  
11250 C C   . VAL F 122 ? 0.4089 0.3705 0.1898 -0.0708 -0.1124 0.0593  122 VAL F C   
11251 O O   . VAL F 122 ? 0.4422 0.4106 0.1940 -0.0734 -0.1225 0.0675  122 VAL F O   
11252 C CB  . VAL F 122 ? 0.3944 0.2763 0.1911 -0.0445 -0.0989 0.0661  122 VAL F CB  
11253 C CG1 . VAL F 122 ? 0.4306 0.2783 0.1907 -0.0579 -0.0943 0.0736  122 VAL F CG1 
11254 C CG2 . VAL F 122 ? 0.4018 0.2538 0.2006 -0.0208 -0.1034 0.0726  122 VAL F CG2 
11255 N N   . ARG F 123 ? 0.3947 0.3555 0.1812 -0.0959 -0.0981 0.0449  123 ARG F N   
11256 C CA  . ARG F 123 ? 0.4263 0.3831 0.1762 -0.1315 -0.0917 0.0361  123 ARG F CA  
11257 C C   . ARG F 123 ? 0.4461 0.4702 0.1854 -0.1444 -0.1140 0.0398  123 ARG F C   
11258 O O   . ARG F 123 ? 0.4855 0.5064 0.1851 -0.1656 -0.1179 0.0413  123 ARG F O   
11259 C CB  . ARG F 123 ? 0.4216 0.3588 0.1688 -0.1520 -0.0731 0.0206  123 ARG F CB  
11260 C CG  . ARG F 123 ? 0.4757 0.3729 0.1637 -0.1887 -0.0585 0.0097  123 ARG F CG  
11261 C CD  . ARG F 123 ? 0.4890 0.3512 0.1599 -0.2051 -0.0388 -0.0043 123 ARG F CD  
11262 N NE  . ARG F 123 ? 0.4608 0.3792 0.1635 -0.2132 -0.0518 -0.0079 123 ARG F NE  
11263 C CZ  . ARG F 123 ? 0.4784 0.4541 0.1692 -0.2470 -0.0681 -0.0112 123 ARG F CZ  
11264 N NH1 . ARG F 123 ? 0.5262 0.5090 0.1713 -0.2790 -0.0761 -0.0118 123 ARG F NH1 
11265 N NH2 . ARG F 123 ? 0.4500 0.4849 0.1746 -0.2512 -0.0771 -0.0129 123 ARG F NH2 
11266 N N   . LEU F 124 ? 0.4216 0.5143 0.1959 -0.1311 -0.1283 0.0426  124 LEU F N   
11267 C CA  . LEU F 124 ? 0.4357 0.6219 0.2096 -0.1409 -0.1505 0.0490  124 LEU F CA  
11268 C C   . LEU F 124 ? 0.4607 0.6717 0.2234 -0.1097 -0.1692 0.0687  124 LEU F C   
11269 O O   . LEU F 124 ? 0.4853 0.7677 0.2333 -0.1245 -0.1867 0.0758  124 LEU F O   
11270 C CB  . LEU F 124 ? 0.4014 0.6646 0.2195 -0.1281 -0.1578 0.0491  124 LEU F CB  
11271 C CG  . LEU F 124 ? 0.3919 0.6458 0.2106 -0.1689 -0.1429 0.0307  124 LEU F CG  
11272 C CD1 . LEU F 124 ? 0.3523 0.6606 0.2186 -0.1466 -0.1448 0.0311  124 LEU F CD1 
11273 C CD2 . LEU F 124 ? 0.4333 0.7244 0.2120 -0.2306 -0.1475 0.0225  124 LEU F CD2 
11274 N N   . GLN F 125 ? 0.4638 0.6152 0.2267 -0.0694 -0.1656 0.0784  125 GLN F N   
11275 C CA  . GLN F 125 ? 0.5039 0.6497 0.2400 -0.0385 -0.1793 0.0977  125 GLN F CA  
11276 C C   . GLN F 125 ? 0.5395 0.6415 0.2313 -0.0698 -0.1751 0.0966  125 GLN F C   
11277 O O   . GLN F 125 ? 0.5736 0.7164 0.2395 -0.0732 -0.1912 0.1071  125 GLN F O   
11278 C CB  . GLN F 125 ? 0.5139 0.5878 0.2465 0.0045  -0.1738 0.1069  125 GLN F CB  
11279 C CG  . GLN F 125 ? 0.5072 0.6175 0.2638 0.0513  -0.1812 0.1144  125 GLN F CG  
11280 C CD  . GLN F 125 ? 0.5358 0.5524 0.2703 0.0846  -0.1734 0.1207  125 GLN F CD  
11281 O OE1 . GLN F 125 ? 0.5956 0.5610 0.2833 0.1101  -0.1783 0.1363  125 GLN F OE1 
11282 N NE2 . GLN F 125 ? 0.5042 0.4923 0.2635 0.0809  -0.1611 0.1090  125 GLN F NE2 
11283 N N   . LEU F 126 ? 0.5351 0.5594 0.2174 -0.0899 -0.1527 0.0853  126 LEU F N   
11284 C CA  . LEU F 126 ? 0.5727 0.5464 0.2107 -0.1135 -0.1433 0.0847  126 LEU F CA  
11285 C C   . LEU F 126 ? 0.6003 0.6038 0.2073 -0.1568 -0.1459 0.0748  126 LEU F C   
11286 O O   . LEU F 126 ? 0.6431 0.6376 0.2078 -0.1701 -0.1511 0.0804  126 LEU F O   
11287 C CB  . LEU F 126 ? 0.5605 0.4619 0.1998 -0.1203 -0.1161 0.0766  126 LEU F CB  
11288 C CG  . LEU F 126 ? 0.5462 0.4111 0.2046 -0.0918 -0.1123 0.0855  126 LEU F CG  
11289 C CD1 . LEU F 126 ? 0.5416 0.3582 0.1975 -0.1055 -0.0868 0.0811  126 LEU F CD1 
11290 C CD2 . LEU F 126 ? 0.5882 0.4355 0.2175 -0.0677 -0.1280 0.1045  126 LEU F CD2 
11291 N N   . ARG F 127 ? 0.5863 0.6192 0.2058 -0.1829 -0.1420 0.0601  127 ARG F N   
11292 C CA  . ARG F 127 ? 0.6293 0.6800 0.2049 -0.2350 -0.1436 0.0487  127 ARG F CA  
11293 C C   . ARG F 127 ? 0.6813 0.6438 0.1960 -0.2578 -0.1222 0.0408  127 ARG F C   
11294 O O   . ARG F 127 ? 0.6730 0.5658 0.1889 -0.2443 -0.0966 0.0355  127 ARG F O   
11295 C CB  . ARG F 127 ? 0.6449 0.8001 0.2199 -0.2413 -0.1756 0.0618  127 ARG F CB  
11296 C CG  . ARG F 127 ? 0.6097 0.8640 0.2315 -0.2398 -0.1898 0.0626  127 ARG F CG  
11297 C CD  . ARG F 127 ? 0.5980 0.9591 0.2531 -0.1960 -0.2179 0.0864  127 ARG F CD  
11298 N NE  . ARG F 127 ? 0.6402 1.0763 0.2663 -0.2079 -0.2421 0.1011  127 ARG F NE  
11299 C CZ  . ARG F 127 ? 0.6823 1.1554 0.2662 -0.2717 -0.2501 0.0934  127 ARG F CZ  
11300 N NH1 . ARG F 127 ? 0.7013 1.1300 0.2540 -0.3346 -0.2338 0.0696  127 ARG F NH1 
11301 N NH2 . ARG F 127 ? 0.7175 1.2694 0.2807 -0.2733 -0.2751 0.1110  127 ARG F NH2 
11302 N N   . ASP F 128 ? 0.7382 0.7082 0.1990 -0.2897 -0.1314 0.0413  128 ASP F N   
11303 C CA  . ASP F 128 ? 0.7976 0.6804 0.1921 -0.3104 -0.1086 0.0329  128 ASP F CA  
11304 C C   . ASP F 128 ? 0.8038 0.6604 0.1935 -0.2809 -0.1083 0.0487  128 ASP F C   
11305 O O   . ASP F 128 ? 0.8576 0.6592 0.1896 -0.2979 -0.0938 0.0453  128 ASP F O   
11306 C CB  . ASP F 128 ? 0.8720 0.7585 0.1934 -0.3696 -0.1148 0.0220  128 ASP F CB  
11307 C CG  . ASP F 128 ? 0.8844 0.8619 0.2044 -0.3778 -0.1506 0.0380  128 ASP F CG  
11308 O OD1 . ASP F 128 ? 0.8339 0.8852 0.2150 -0.3359 -0.1722 0.0564  128 ASP F OD1 
11309 O OD2 . ASP F 128 ? 0.9540 0.9265 0.2055 -0.4238 -0.1563 0.0331  128 ASP F OD2 
11310 N N   . ASN F 129 ? 0.7603 0.6472 0.2008 -0.2385 -0.1221 0.0657  129 ASN F N   
11311 C CA  . ASN F 129 ? 0.7745 0.6250 0.2042 -0.2137 -0.1202 0.0814  129 ASN F CA  
11312 C C   . ASN F 129 ? 0.7561 0.5435 0.1988 -0.2002 -0.0907 0.0790  129 ASN F C   
11313 O O   . ASN F 129 ? 0.7726 0.5289 0.2028 -0.1880 -0.0864 0.0916  129 ASN F O   
11314 C CB  . ASN F 129 ? 0.7617 0.6567 0.2188 -0.1750 -0.1472 0.1023  129 ASN F CB  
11315 C CG  . ASN F 129 ? 0.7995 0.7590 0.2302 -0.1793 -0.1761 0.1143  129 ASN F CG  
11316 O OD1 . ASN F 129 ? 0.8255 0.8160 0.2279 -0.2199 -0.1810 0.1046  129 ASN F OD1 
11317 N ND2 . ASN F 129 ? 0.8137 0.7913 0.2458 -0.1375 -0.1951 0.1367  129 ASN F ND2 
11318 N N   . ALA F 130 ? 0.7279 0.5010 0.1921 -0.2037 -0.0706 0.0647  130 ALA F N   
11319 C CA  . ALA F 130 ? 0.7116 0.4443 0.1899 -0.1907 -0.0419 0.0639  130 ALA F CA  
11320 C C   . ALA F 130 ? 0.7231 0.4252 0.1840 -0.2014 -0.0145 0.0468  130 ALA F C   
11321 O O   . ALA F 130 ? 0.7345 0.4428 0.1814 -0.2203 -0.0198 0.0344  130 ALA F O   
11322 C CB  . ALA F 130 ? 0.6579 0.4096 0.1944 -0.1647 -0.0489 0.0720  130 ALA F CB  
11323 N N   . LYS F 131 ? 0.7292 0.3993 0.1855 -0.1887 0.0155  0.0477  131 LYS F N   
11324 C CA  . LYS F 131 ? 0.7515 0.3837 0.1845 -0.1851 0.0463  0.0349  131 LYS F CA  
11325 C C   . LYS F 131 ? 0.6934 0.3488 0.1845 -0.1647 0.0490  0.0341  131 LYS F C   
11326 O O   . LYS F 131 ? 0.6478 0.3337 0.1890 -0.1459 0.0483  0.0458  131 LYS F O   
11327 C CB  . LYS F 131 ? 0.7910 0.3907 0.1916 -0.1709 0.0805  0.0395  131 LYS F CB  
11328 C CG  . LYS F 131 ? 0.8605 0.4251 0.1922 -0.1898 0.0852  0.0387  131 LYS F CG  
11329 C CD  . LYS F 131 ? 0.8890 0.4402 0.2028 -0.1697 0.1192  0.0475  131 LYS F CD  
11330 C CE  . LYS F 131 ? 0.9813 0.4720 0.2042 -0.1827 0.1392  0.0403  131 LYS F CE  
11331 N NZ  . LYS F 131 ? 1.0523 0.4699 0.2045 -0.1837 0.1638  0.0219  131 LYS F NZ  
11332 N N   . GLU F 132 ? 0.7024 0.3408 0.1803 -0.1731 0.0521  0.0205  132 GLU F N   
11333 C CA  . GLU F 132 ? 0.6585 0.3096 0.1806 -0.1532 0.0588  0.0191  132 GLU F CA  
11334 C C   . GLU F 132 ? 0.6854 0.3024 0.1880 -0.1253 0.0966  0.0214  132 GLU F C   
11335 O O   . GLU F 132 ? 0.7529 0.3063 0.1896 -0.1254 0.1214  0.0111  132 GLU F O   
11336 C CB  . GLU F 132 ? 0.6696 0.3112 0.1759 -0.1749 0.0506  0.0046  132 GLU F CB  
11337 C CG  . GLU F 132 ? 0.6183 0.2814 0.1760 -0.1567 0.0509  0.0042  132 GLU F CG  
11338 C CD  . GLU F 132 ? 0.6235 0.2921 0.1725 -0.1834 0.0384  -0.0080 132 GLU F CD  
11339 O OE1 . GLU F 132 ? 0.6856 0.3237 0.1717 -0.2195 0.0386  -0.0188 132 GLU F OE1 
11340 O OE2 . GLU F 132 ? 0.5705 0.2760 0.1723 -0.1722 0.0287  -0.0067 132 GLU F OE2 
11341 N N   . LEU F 133 ? 0.6420 0.3017 0.1951 -0.1015 0.1018  0.0361  133 LEU F N   
11342 C CA  . LEU F 133 ? 0.6637 0.3195 0.2071 -0.0697 0.1371  0.0440  133 LEU F CA  
11343 C C   . LEU F 133 ? 0.6716 0.3087 0.2118 -0.0433 0.1569  0.0399  133 LEU F C   
11344 O O   . LEU F 133 ? 0.7244 0.3312 0.2235 -0.0125 0.1915  0.0429  133 LEU F O   
11345 C CB  . LEU F 133 ? 0.6155 0.3401 0.2160 -0.0610 0.1342  0.0627  133 LEU F CB  
11346 C CG  . LEU F 133 ? 0.6448 0.3744 0.2217 -0.0702 0.1412  0.0721  133 LEU F CG  
11347 C CD1 . LEU F 133 ? 0.6832 0.3665 0.2107 -0.0978 0.1252  0.0626  133 LEU F CD1 
11348 C CD2 . LEU F 133 ? 0.5988 0.3903 0.2288 -0.0803 0.1269  0.0885  133 LEU F CD2 
11349 N N   . GLY F 134 ? 0.6263 0.2796 0.2048 -0.0508 0.1367  0.0346  134 GLY F N   
11350 C CA  . GLY F 134 ? 0.6366 0.2679 0.2088 -0.0284 0.1527  0.0310  134 GLY F CA  
11351 C C   . GLY F 134 ? 0.5712 0.2717 0.2161 -0.0035 0.1498  0.0446  134 GLY F C   
11352 O O   . GLY F 134 ? 0.5757 0.2654 0.2202 0.0181  0.1613  0.0441  134 GLY F O   
11353 N N   . ASN F 135 ? 0.5191 0.2858 0.2189 -0.0105 0.1338  0.0568  135 ASN F N   
11354 C CA  . ASN F 135 ? 0.4667 0.3041 0.2282 0.0039  0.1307  0.0709  135 ASN F CA  
11355 C C   . ASN F 135 ? 0.4072 0.2765 0.2180 -0.0220 0.0965  0.0706  135 ASN F C   
11356 O O   . ASN F 135 ? 0.3715 0.2951 0.2252 -0.0222 0.0902  0.0818  135 ASN F O   
11357 C CB  . ASN F 135 ? 0.4773 0.3674 0.2478 0.0174  0.1493  0.0890  135 ASN F CB  
11358 C CG  . ASN F 135 ? 0.4885 0.3761 0.2470 -0.0110 0.1392  0.0910  135 ASN F CG  
11359 O OD1 . ASN F 135 ? 0.4806 0.3379 0.2339 -0.0382 0.1139  0.0817  135 ASN F OD1 
11360 N ND2 . ASN F 135 ? 0.5130 0.4364 0.2646 -0.0019 0.1600  0.1047  135 ASN F ND2 
11361 N N   . GLY F 136 ? 0.4045 0.2408 0.2028 -0.0433 0.0753  0.0586  136 GLY F N   
11362 C CA  . GLY F 136 ? 0.3668 0.2207 0.1968 -0.0597 0.0457  0.0590  136 GLY F CA  
11363 C C   . GLY F 136 ? 0.3822 0.2287 0.1959 -0.0767 0.0331  0.0646  136 GLY F C   
11364 O O   . GLY F 136 ? 0.3714 0.2156 0.1937 -0.0851 0.0101  0.0656  136 GLY F O   
11365 N N   . CYS F 137 ? 0.4155 0.2527 0.1987 -0.0781 0.0500  0.0691  137 CYS F N   
11366 C CA  . CYS F 137 ? 0.4383 0.2666 0.2004 -0.0945 0.0411  0.0765  137 CYS F CA  
11367 C C   . CYS F 137 ? 0.4749 0.2671 0.1926 -0.1027 0.0367  0.0681  137 CYS F C   
11368 O O   . CYS F 137 ? 0.4997 0.2682 0.1882 -0.0996 0.0515  0.0579  137 CYS F O   
11369 C CB  . CYS F 137 ? 0.4531 0.3078 0.2123 -0.0955 0.0621  0.0903  137 CYS F CB  
11370 S SG  . CYS F 137 ? 0.4170 0.3354 0.2259 -0.0979 0.0643  0.1040  137 CYS F SG  
11371 N N   . PHE F 138 ? 0.4887 0.2721 0.1931 -0.1145 0.0162  0.0734  138 PHE F N   
11372 C CA  . PHE F 138 ? 0.5266 0.2882 0.1885 -0.1250 0.0081  0.0696  138 PHE F CA  
11373 C C   . PHE F 138 ? 0.5631 0.3118 0.1960 -0.1342 0.0122  0.0818  138 PHE F C   
11374 O O   . PHE F 138 ? 0.5630 0.3119 0.2034 -0.1371 0.0017  0.0935  138 PHE F O   
11375 C CB  . PHE F 138 ? 0.5160 0.2882 0.1858 -0.1242 -0.0218 0.0684  138 PHE F CB  
11376 C CG  . PHE F 138 ? 0.4859 0.2774 0.1803 -0.1205 -0.0263 0.0563  138 PHE F CG  
11377 C CD1 . PHE F 138 ? 0.5070 0.2950 0.1740 -0.1361 -0.0234 0.0440  138 PHE F CD1 
11378 C CD2 . PHE F 138 ? 0.4447 0.2535 0.1819 -0.1066 -0.0325 0.0569  138 PHE F CD2 
11379 C CE1 . PHE F 138 ? 0.4873 0.2918 0.1708 -0.1395 -0.0266 0.0334  138 PHE F CE1 
11380 C CE2 . PHE F 138 ? 0.4198 0.2473 0.1777 -0.1047 -0.0354 0.0463  138 PHE F CE2 
11381 C CZ  . PHE F 138 ? 0.4405 0.2675 0.1725 -0.1219 -0.0323 0.0349  138 PHE F CZ  
11382 N N   . GLU F 139 ? 0.6055 0.3343 0.1959 -0.1409 0.0288  0.0786  139 GLU F N   
11383 C CA  . GLU F 139 ? 0.6452 0.3624 0.2033 -0.1506 0.0367  0.0897  139 GLU F CA  
11384 C C   . GLU F 139 ? 0.6862 0.3806 0.1999 -0.1632 0.0173  0.0894  139 GLU F C   
11385 O O   . GLU F 139 ? 0.7107 0.3916 0.1929 -0.1709 0.0183  0.0776  139 GLU F O   
11386 C CB  . GLU F 139 ? 0.6716 0.3846 0.2081 -0.1439 0.0728  0.0879  139 GLU F CB  
11387 C CG  . GLU F 139 ? 0.7066 0.4223 0.2182 -0.1525 0.0875  0.1011  139 GLU F CG  
11388 C CD  . GLU F 139 ? 0.7480 0.4534 0.2240 -0.1389 0.1247  0.0977  139 GLU F CD  
11389 O OE1 . GLU F 139 ? 0.7323 0.4705 0.2342 -0.1165 0.1492  0.1014  139 GLU F OE1 
11390 O OE2 . GLU F 139 ? 0.8035 0.4668 0.2203 -0.1477 0.1301  0.0920  139 GLU F OE2 
11391 N N   . PHE F 140 ? 0.7041 0.3912 0.2074 -0.1672 0.0000  0.1032  140 PHE F N   
11392 C CA  . PHE F 140 ? 0.7415 0.4170 0.2075 -0.1714 -0.0238 0.1073  140 PHE F CA  
11393 C C   . PHE F 140 ? 0.7981 0.4510 0.2077 -0.1876 -0.0123 0.1076  140 PHE F C   
11394 O O   . PHE F 140 ? 0.8182 0.4578 0.2127 -0.1937 0.0110  0.1128  140 PHE F O   
11395 C CB  . PHE F 140 ? 0.7564 0.4161 0.2171 -0.1628 -0.0438 0.1241  140 PHE F CB  
11396 C CG  . PHE F 140 ? 0.7184 0.3901 0.2195 -0.1444 -0.0578 0.1237  140 PHE F CG  
11397 C CD1 . PHE F 140 ? 0.6916 0.3615 0.2235 -0.1462 -0.0462 0.1243  140 PHE F CD1 
11398 C CD2 . PHE F 140 ? 0.7132 0.4056 0.2201 -0.1253 -0.0823 0.1236  140 PHE F CD2 
11399 C CE1 . PHE F 140 ? 0.6646 0.3384 0.2262 -0.1305 -0.0582 0.1229  140 PHE F CE1 
11400 C CE2 . PHE F 140 ? 0.6844 0.3866 0.2245 -0.1045 -0.0925 0.1233  140 PHE F CE2 
11401 C CZ  . PHE F 140 ? 0.6621 0.3478 0.2266 -0.1076 -0.0802 0.1219  140 PHE F CZ  
11402 N N   . TYR F 141 ? 0.8281 0.4835 0.2050 -0.1963 -0.0290 0.1029  141 TYR F N   
11403 C CA  . TYR F 141 ? 0.8917 0.5217 0.2057 -0.2144 -0.0226 0.1038  141 TYR F CA  
11404 C C   . TYR F 141 ? 0.9281 0.5426 0.2154 -0.2121 -0.0360 0.1237  141 TYR F C   
11405 O O   . TYR F 141 ? 0.9751 0.5620 0.2182 -0.2246 -0.0213 0.1288  141 TYR F O   
11406 C CB  . TYR F 141 ? 0.9180 0.5610 0.1997 -0.2326 -0.0386 0.0927  141 TYR F CB  
11407 C CG  . TYR F 141 ? 0.9123 0.5466 0.1933 -0.2437 -0.0208 0.0720  141 TYR F CG  
11408 C CD1 . TYR F 141 ? 0.9425 0.5298 0.1925 -0.2450 0.0165  0.0624  141 TYR F CD1 
11409 C CD2 . TYR F 141 ? 0.8859 0.5566 0.1911 -0.2503 -0.0391 0.0634  141 TYR F CD2 
11410 C CE1 . TYR F 141 ? 0.9559 0.5167 0.1894 -0.2505 0.0355  0.0447  141 TYR F CE1 
11411 C CE2 . TYR F 141 ? 0.8948 0.5437 0.1868 -0.2644 -0.0215 0.0447  141 TYR F CE2 
11412 C CZ  . TYR F 141 ? 0.9344 0.5203 0.1859 -0.2633 0.0159  0.0354  141 TYR F CZ  
11413 O OH  . TYR F 141 ? 0.9609 0.5076 0.1842 -0.2728 0.0358  0.0180  141 TYR F OH  
11414 N N   . HIS F 142 ? 0.9168 0.5431 0.2237 -0.1938 -0.0622 0.1355  142 HIS F N   
11415 C CA  . HIS F 142 ? 0.9640 0.5583 0.2359 -0.1859 -0.0745 0.1562  142 HIS F CA  
11416 C C   . HIS F 142 ? 0.9553 0.5211 0.2446 -0.1848 -0.0612 0.1637  142 HIS F C   
11417 O O   . HIS F 142 ? 0.9030 0.4883 0.2426 -0.1821 -0.0512 0.1546  142 HIS F O   
11418 C CB  . HIS F 142 ? 0.9766 0.5911 0.2440 -0.1595 -0.1086 0.1673  142 HIS F CB  
11419 C CG  . HIS F 142 ? 0.9240 0.5692 0.2466 -0.1366 -0.1181 0.1625  142 HIS F CG  
11420 N ND1 . HIS F 142 ? 0.9314 0.5442 0.2588 -0.1124 -0.1232 0.1735  142 HIS F ND1 
11421 C CD2 . HIS F 142 ? 0.8723 0.5712 0.2399 -0.1368 -0.1218 0.1473  142 HIS F CD2 
11422 C CE1 . HIS F 142 ? 0.8809 0.5309 0.2581 -0.0951 -0.1297 0.1654  142 HIS F CE1 
11423 N NE2 . HIS F 142 ? 0.8413 0.5474 0.2465 -0.1100 -0.1292 0.1500  142 HIS F NE2 
11424 N N   . LYS F 143 ? 1.0145 0.5330 0.2561 -0.1911 -0.0616 0.1808  143 LYS F N   
11425 C CA  . LYS F 143 ? 1.0264 0.5105 0.2679 -0.1994 -0.0531 0.1899  143 LYS F CA  
11426 C C   . LYS F 143 ? 1.0213 0.4896 0.2748 -0.1709 -0.0746 0.1934  143 LYS F C   
11427 O O   . LYS F 143 ? 1.0533 0.5106 0.2796 -0.1426 -0.0973 0.2018  143 LYS F O   
11428 C CB  . LYS F 143 ? 1.1094 0.5353 0.2801 -0.2187 -0.0488 0.2079  143 LYS F CB  
11429 C CG  . LYS F 143 ? 1.1325 0.5288 0.2937 -0.2476 -0.0330 0.2160  143 LYS F CG  
11430 C CD  . LYS F 143 ? 1.2289 0.5593 0.3075 -0.2713 -0.0298 0.2346  143 LYS F CD  
11431 C CE  . LYS F 143 ? 1.2780 0.5585 0.3254 -0.3042 -0.0222 0.2453  143 LYS F CE  
11432 N NZ  . LYS F 143 ? 1.3164 0.5277 0.3349 -0.2815 -0.0422 0.2499  143 LYS F NZ  
11433 N N   . CYS F 144 ? 0.9854 0.4576 0.2773 -0.1755 -0.0667 0.1880  144 CYS F N   
11434 C CA  . CYS F 144 ? 0.9793 0.4359 0.2835 -0.1477 -0.0829 0.1883  144 CYS F CA  
11435 C C   . CYS F 144 ? 1.0305 0.4185 0.2983 -0.1647 -0.0777 0.1977  144 CYS F C   
11436 O O   . CYS F 144 ? 0.9954 0.4039 0.2981 -0.1899 -0.0637 0.1912  144 CYS F O   
11437 C CB  . CYS F 144 ? 0.8908 0.4146 0.2719 -0.1389 -0.0804 0.1701  144 CYS F CB  
11438 S SG  . CYS F 144 ? 0.8748 0.3970 0.2786 -0.1003 -0.0992 0.1681  144 CYS F SG  
11439 N N   . ASP F 145 ? 1.1243 0.4280 0.3135 -0.1519 -0.0887 0.2139  145 ASP F N   
11440 C CA  . ASP F 145 ? 1.2035 0.4156 0.3306 -0.1739 -0.0837 0.2233  145 ASP F CA  
11441 C C   . ASP F 145 ? 1.1899 0.3850 0.3350 -0.1532 -0.0899 0.2162  145 ASP F C   
11442 O O   . ASP F 145 ? 1.1094 0.3737 0.3235 -0.1233 -0.0967 0.2042  145 ASP F O   
11443 C CB  . ASP F 145 ? 1.3295 0.4360 0.3478 -0.1639 -0.0911 0.2438  145 ASP F CB  
11444 C CG  . ASP F 145 ? 1.3631 0.4484 0.3549 -0.0963 -0.1122 0.2523  145 ASP F CG  
11445 O OD1 . ASP F 145 ? 1.2913 0.4428 0.3479 -0.0616 -0.1215 0.2420  145 ASP F OD1 
11446 O OD2 . ASP F 145 ? 1.4668 0.4734 0.3702 -0.0765 -0.1190 0.2710  145 ASP F OD2 
11447 N N   . ASN F 146 ? 1.2771 0.3751 0.3525 -0.1733 -0.0864 0.2231  146 ASN F N   
11448 C CA  . ASN F 146 ? 1.2783 0.3476 0.3581 -0.1600 -0.0896 0.2156  146 ASN F CA  
11449 C C   . ASN F 146 ? 1.2994 0.3451 0.3650 -0.0876 -0.1051 0.2181  146 ASN F C   
11450 O O   . ASN F 146 ? 1.2602 0.3260 0.3631 -0.0657 -0.1079 0.2080  146 ASN F O   
11451 C CB  . ASN F 146 ? 1.3889 0.3449 0.3775 -0.2070 -0.0814 0.2222  146 ASN F CB  
11452 C CG  . ASN F 146 ? 1.3571 0.3669 0.3748 -0.2819 -0.0661 0.2199  146 ASN F CG  
11453 O OD1 . ASN F 146 ? 1.2408 0.3740 0.3582 -0.2901 -0.0597 0.2104  146 ASN F OD1 
11454 N ND2 . ASN F 146 ? 1.4700 0.3873 0.3942 -0.3366 -0.0588 0.2301  146 ASN F ND2 
11455 N N   . GLU F 147 ? 1.3634 0.3751 0.3755 -0.0485 -0.1148 0.2332  147 GLU F N   
11456 C CA  . GLU F 147 ? 1.3767 0.3989 0.3856 0.0267  -0.1298 0.2394  147 GLU F CA  
11457 C C   . GLU F 147 ? 1.2433 0.4165 0.3660 0.0415  -0.1382 0.2269  147 GLU F C   
11458 O O   . GLU F 147 ? 1.2011 0.4245 0.3667 0.0817  -0.1456 0.2215  147 GLU F O   
11459 C CB  . GLU F 147 ? 1.4915 0.4410 0.4055 0.0669  -0.1381 0.2629  147 GLU F CB  
11460 C CG  . GLU F 147 ? 1.6522 0.4282 0.4300 0.0545  -0.1286 0.2769  147 GLU F CG  
11461 C CD  . GLU F 147 ? 1.6848 0.4247 0.4264 -0.0172 -0.1179 0.2803  147 GLU F CD  
11462 O OE1 . GLU F 147 ? 1.7356 0.4578 0.4316 -0.0073 -0.1224 0.2957  147 GLU F OE1 
11463 O OE2 . GLU F 147 ? 1.6616 0.3988 0.4207 -0.0834 -0.1048 0.2688  147 GLU F OE2 
11464 N N   . CYS F 148 ? 1.1884 0.4273 0.3505 0.0066  -0.1355 0.2225  148 CYS F N   
11465 C CA  . CYS F 148 ? 1.0779 0.4413 0.3319 0.0053  -0.1396 0.2083  148 CYS F CA  
11466 C C   . CYS F 148 ? 0.9950 0.4044 0.3225 -0.0092 -0.1311 0.1892  148 CYS F C   
11467 O O   . CYS F 148 ? 0.9322 0.4168 0.3171 0.0127  -0.1385 0.1801  148 CYS F O   
11468 C CB  . CYS F 148 ? 1.0551 0.4509 0.3173 -0.0352 -0.1318 0.2058  148 CYS F CB  
11469 S SG  . CYS F 148 ? 0.9400 0.4552 0.2928 -0.0520 -0.1286 0.1846  148 CYS F SG  
11470 N N   . MET F 149 ? 1.0009 0.3702 0.3241 -0.0488 -0.1159 0.1845  149 MET F N   
11471 C CA  . MET F 149 ? 0.9324 0.3401 0.3173 -0.0619 -0.1083 0.1691  149 MET F CA  
11472 C C   . MET F 149 ? 0.9551 0.3363 0.3322 -0.0210 -0.1176 0.1684  149 MET F C   
11473 O O   . MET F 149 ? 0.8839 0.3266 0.3240 -0.0097 -0.1186 0.1559  149 MET F O   
11474 C CB  . MET F 149 ? 0.9464 0.3220 0.3186 -0.1131 -0.0926 0.1689  149 MET F CB  
11475 C CG  . MET F 149 ? 0.9196 0.3382 0.3093 -0.1510 -0.0783 0.1694  149 MET F CG  
11476 S SD  . MET F 149 ? 0.8063 0.3359 0.2863 -0.1447 -0.0703 0.1531  149 MET F SD  
11477 C CE  . MET F 149 ? 0.8067 0.3634 0.2859 -0.1863 -0.0466 0.1573  149 MET F CE  
11478 N N   . GLU F 150 ? 1.0673 0.3497 0.3586 0.0028  -0.1224 0.1824  150 GLU F N   
11479 C CA  . GLU F 150 ? 1.1135 0.3539 0.3787 0.0498  -0.1277 0.1838  150 GLU F CA  
11480 C C   . GLU F 150 ? 1.0710 0.4011 0.3839 0.1060  -0.1408 0.1847  150 GLU F C   
11481 O O   . GLU F 150 ? 1.0472 0.4026 0.3886 0.1354  -0.1422 0.1782  150 GLU F O   
11482 C CB  . GLU F 150 ? 1.2646 0.3588 0.4054 0.0672  -0.1264 0.2006  150 GLU F CB  
11483 C CG  . GLU F 150 ? 1.3375 0.3651 0.4268 0.1268  -0.1282 0.2047  150 GLU F CG  
11484 C CD  . GLU F 150 ? 1.2968 0.3290 0.4218 0.1097  -0.1215 0.1874  150 GLU F CD  
11485 O OE1 . GLU F 150 ? 1.2507 0.2988 0.4090 0.0451  -0.1142 0.1760  150 GLU F OE1 
11486 O OE2 . GLU F 150 ? 1.3157 0.3411 0.4344 0.1635  -0.1230 0.1867  150 GLU F OE2 
11487 N N   . SER F 151 ? 1.0671 0.4520 0.3875 0.1168  -0.1504 0.1931  151 SER F N   
11488 C CA  . SER F 151 ? 1.0300 0.5197 0.3955 0.1601  -0.1648 0.1959  151 SER F CA  
11489 C C   . SER F 151 ? 0.9200 0.5151 0.3818 0.1360  -0.1628 0.1753  151 SER F C   
11490 O O   . SER F 151 ? 0.8872 0.5596 0.3885 0.1679  -0.1710 0.1740  151 SER F O   
11491 C CB  . SER F 151 ? 1.0490 0.5778 0.3970 0.1645  -0.1766 0.2090  151 SER F CB  
11492 O OG  . SER F 151 ? 0.9856 0.5587 0.3738 0.1077  -0.1713 0.1963  151 SER F OG  
11493 N N   . VAL F 152 ? 0.8739 0.4718 0.3680 0.0812  -0.1506 0.1610  152 VAL F N   
11494 C CA  . VAL F 152 ? 0.7842 0.4586 0.3543 0.0576  -0.1449 0.1421  152 VAL F CA  
11495 C C   . VAL F 152 ? 0.7753 0.4351 0.3653 0.0720  -0.1404 0.1346  152 VAL F C   
11496 O O   . VAL F 152 ? 0.7215 0.4504 0.3618 0.0829  -0.1431 0.1256  152 VAL F O   
11497 C CB  . VAL F 152 ? 0.7465 0.4195 0.3350 0.0061  -0.1294 0.1320  152 VAL F CB  
11498 C CG1 . VAL F 152 ? 0.6661 0.4025 0.3187 -0.0109 -0.1214 0.1142  152 VAL F CG1 
11499 C CG2 . VAL F 152 ? 0.7700 0.4502 0.3314 -0.0085 -0.1317 0.1384  152 VAL F CG2 
11500 N N   . ARG F 153 ? 0.8395 0.4075 0.3836 0.0671  -0.1333 0.1383  153 ARG F N   
11501 C CA  . ARG F 153 ? 0.8516 0.3906 0.3985 0.0794  -0.1294 0.1317  153 ARG F CA  
11502 C C   . ARG F 153 ? 0.9108 0.4455 0.4320 0.1426  -0.1382 0.1404  153 ARG F C   
11503 O O   . ARG F 153 ? 0.8780 0.4475 0.4329 0.1625  -0.1374 0.1324  153 ARG F O   
11504 C CB  . ARG F 153 ? 0.9128 0.3491 0.4024 0.0489  -0.1202 0.1338  153 ARG F CB  
11505 C CG  . ARG F 153 ? 0.8698 0.3249 0.3856 -0.0096 -0.1098 0.1288  153 ARG F CG  
11506 C CD  . ARG F 153 ? 0.9327 0.3050 0.3943 -0.0475 -0.1024 0.1315  153 ARG F CD  
11507 N NE  . ARG F 153 ? 0.9579 0.3157 0.3943 -0.0907 -0.0956 0.1396  153 ARG F NE  
11508 C CZ  . ARG F 153 ? 1.0577 0.3274 0.4087 -0.0978 -0.0965 0.1529  153 ARG F CZ  
11509 N NH1 . ARG F 153 ? 1.1518 0.3275 0.4250 -0.0596 -0.1032 0.1610  153 ARG F NH1 
11510 N NH2 . ARG F 153 ? 1.0723 0.3447 0.4093 -0.1411 -0.0886 0.1596  153 ARG F NH2 
11511 N N   . ASN F 154 ? 1.0127 0.5051 0.4704 0.1774  -0.1453 0.1582  154 ASN F N   
11512 C CA  . ASN F 154 ? 1.0777 0.5859 0.5100 0.2495  -0.1535 0.1720  154 ASN F CA  
11513 C C   . ASN F 154 ? 0.9802 0.6332 0.4970 0.2676  -0.1615 0.1664  154 ASN F C   
11514 O O   . ASN F 154 ? 0.9907 0.6692 0.5127 0.3154  -0.1613 0.1688  154 ASN F O   
11515 C CB  . ASN F 154 ? 1.1792 0.6630 0.5506 0.2798  -0.1627 0.1938  154 ASN F CB  
11516 C CG  . ASN F 154 ? 1.3573 0.6841 0.6103 0.3097  -0.1560 0.2087  154 ASN F CG  
11517 O OD1 . ASN F 154 ? 1.4135 0.6448 0.6236 0.3062  -0.1447 0.2020  154 ASN F OD1 
11518 N ND2 . ASN F 154 ? 1.4827 0.7748 0.6724 0.3375  -0.1628 0.2294  154 ASN F ND2 
11519 N N   . GLY F 155 ? 0.8922 0.6349 0.4667 0.2267  -0.1668 0.1590  155 GLY F N   
11520 C CA  . GLY F 155 ? 0.8203 0.7010 0.4565 0.2342  -0.1774 0.1575  155 GLY F CA  
11521 C C   . GLY F 155 ? 0.8480 0.7827 0.4620 0.2580  -0.1933 0.1766  155 GLY F C   
11522 O O   . GLY F 155 ? 0.8109 0.8702 0.4661 0.2631  -0.2053 0.1796  155 GLY F O   
11523 N N   . THR F 156 ? 0.9169 0.7605 0.4623 0.2671  -0.1937 0.1900  156 THR F N   
11524 C CA  . THR F 156 ? 0.9692 0.8439 0.4761 0.3028  -0.2089 0.2130  156 THR F CA  
11525 C C   . THR F 156 ? 0.9578 0.8302 0.4556 0.2506  -0.2127 0.2112  156 THR F C   
11526 O O   . THR F 156 ? 1.0221 0.8794 0.4687 0.2725  -0.2225 0.2305  156 THR F O   
11527 C CB  . THR F 156 ? 1.0895 0.8433 0.5025 0.3645  -0.2052 0.2338  156 THR F CB  
11528 O OG1 . THR F 156 ? 1.1101 0.8408 0.5184 0.4109  -0.1968 0.2327  156 THR F OG1 
11529 C CG2 . THR F 156 ? 1.1583 0.9541 0.5290 0.4203  -0.2212 0.2623  156 THR F CG2 
11530 N N   . TYR F 157 ? 0.8837 0.7682 0.4250 0.1858  -0.2037 0.1893  157 TYR F N   
11531 C CA  . TYR F 157 ? 0.8792 0.7544 0.4065 0.1378  -0.2029 0.1860  157 TYR F CA  
11532 C C   . TYR F 157 ? 0.8872 0.8626 0.4150 0.1429  -0.2230 0.1971  157 TYR F C   
11533 O O   . TYR F 157 ? 0.8351 0.9174 0.4109 0.1266  -0.2308 0.1889  157 TYR F O   
11534 C CB  . TYR F 157 ? 0.8064 0.6871 0.3781 0.0784  -0.1874 0.1614  157 TYR F CB  
11535 C CG  . TYR F 157 ? 0.8092 0.6804 0.3613 0.0338  -0.1830 0.1572  157 TYR F CG  
11536 C CD1 . TYR F 157 ? 0.8523 0.6363 0.3584 0.0210  -0.1726 0.1631  157 TYR F CD1 
11537 C CD2 . TYR F 157 ? 0.7792 0.7248 0.3504 0.0013  -0.1879 0.1472  157 TYR F CD2 
11538 C CE1 . TYR F 157 ? 0.8605 0.6368 0.3459 -0.0160 -0.1660 0.1596  157 TYR F CE1 
11539 C CE2 . TYR F 157 ? 0.7963 0.7216 0.3379 -0.0375 -0.1813 0.1424  157 TYR F CE2 
11540 C CZ  . TYR F 157 ? 0.8339 0.6771 0.3355 -0.0426 -0.1698 0.1488  157 TYR F CZ  
11541 O OH  . TYR F 157 ? 0.8544 0.6791 0.3246 -0.0777 -0.1609 0.1444  157 TYR F OH  
11542 N N   . ASP F 158 ? 0.9597 0.9008 0.4289 0.1613  -0.2316 0.2165  158 ASP F N   
11543 C CA  . ASP F 158 ? 0.9808 1.0207 0.4428 0.1712  -0.2536 0.2315  158 ASP F CA  
11544 C C   . ASP F 158 ? 0.9519 1.0250 0.4229 0.1014  -0.2534 0.2160  158 ASP F C   
11545 O O   . ASP F 158 ? 0.9945 1.0112 0.4182 0.0812  -0.2512 0.2202  158 ASP F O   
11546 C CB  . ASP F 158 ? 1.0785 1.0636 0.4656 0.2227  -0.2629 0.2604  158 ASP F CB  
11547 C CG  . ASP F 158 ? 1.1021 1.2128 0.4874 0.2564  -0.2888 0.2827  158 ASP F CG  
11548 O OD1 . ASP F 158 ? 1.0775 1.2967 0.5049 0.2930  -0.2987 0.2893  158 ASP F OD1 
11549 O OD2 . ASP F 158 ? 1.1466 1.2563 0.4889 0.2459  -0.2993 0.2949  158 ASP F OD2 
11550 N N   . TYR F 159 ? 0.8913 1.0486 0.4141 0.0643  -0.2540 0.1980  159 TYR F N   
11551 C CA  . TYR F 159 ? 0.8755 1.0519 0.3949 -0.0037 -0.2506 0.1803  159 TYR F CA  
11552 C C   . TYR F 159 ? 0.9315 1.1440 0.4040 -0.0151 -0.2688 0.1946  159 TYR F C   
11553 O O   . TYR F 159 ? 0.9585 1.1050 0.3913 -0.0513 -0.2584 0.1873  159 TYR F O   
11554 C CB  . TYR F 159 ? 0.8204 1.0836 0.3880 -0.0383 -0.2514 0.1625  159 TYR F CB  
11555 C CG  . TYR F 159 ? 0.8267 1.1095 0.3719 -0.1089 -0.2500 0.1457  159 TYR F CG  
11556 C CD1 . TYR F 159 ? 0.8558 1.2391 0.3822 -0.1321 -0.2739 0.1547  159 TYR F CD1 
11557 C CD2 . TYR F 159 ? 0.8139 1.0132 0.3485 -0.1514 -0.2239 0.1219  159 TYR F CD2 
11558 C CE1 . TYR F 159 ? 0.8798 1.2656 0.3694 -0.2032 -0.2717 0.1377  159 TYR F CE1 
11559 C CE2 . TYR F 159 ? 0.8409 1.0362 0.3367 -0.2128 -0.2189 0.1059  159 TYR F CE2 
11560 C CZ  . TYR F 159 ? 0.8782 1.1602 0.3477 -0.2423 -0.2428 0.1125  159 TYR F CZ  
11561 O OH  . TYR F 159 ? 0.9231 1.1881 0.3387 -0.3100 -0.2373 0.0952  159 TYR F OH  
11562 N N   . PRO F 160 ? 0.9546 1.2768 0.4300 0.0185  -0.2953 0.2165  160 PRO F N   
11563 C CA  . PRO F 160 ? 1.0099 1.3791 0.4401 0.0091  -0.3158 0.2328  160 PRO F CA  
11564 C C   . PRO F 160 ? 1.0763 1.3332 0.4416 0.0259  -0.3104 0.2457  160 PRO F C   
11565 O O   . PRO F 160 ? 1.1186 1.3877 0.4412 -0.0029 -0.3204 0.2504  160 PRO F O   
11566 C CB  . PRO F 160 ? 1.0206 1.5271 0.4717 0.0655  -0.3425 0.2602  160 PRO F CB  
11567 C CG  . PRO F 160 ? 0.9565 1.5260 0.4727 0.0673  -0.3371 0.2479  160 PRO F CG  
11568 C CD  . PRO F 160 ? 0.9276 1.3553 0.4509 0.0626  -0.3075 0.2270  160 PRO F CD  
11569 N N   . GLN F 161 ? 1.0966 1.2450 0.4475 0.0676  -0.2952 0.2516  161 GLN F N   
11570 C CA  . GLN F 161 ? 1.1685 1.2018 0.4512 0.0771  -0.2877 0.2639  161 GLN F CA  
11571 C C   . GLN F 161 ? 1.1572 1.1154 0.4259 0.0119  -0.2651 0.2415  161 GLN F C   
11572 O O   . GLN F 161 ? 1.2067 1.1287 0.4224 -0.0073 -0.2655 0.2478  161 GLN F O   
11573 C CB  . GLN F 161 ? 1.2065 1.1380 0.4655 0.1315  -0.2768 0.2760  161 GLN F CB  
11574 C CG  . GLN F 161 ? 1.2857 1.0849 0.4669 0.1316  -0.2659 0.2875  161 GLN F CG  
11575 C CD  . GLN F 161 ? 1.3341 1.0178 0.4804 0.1702  -0.2526 0.2954  161 GLN F CD  
11576 O OE1 . GLN F 161 ? 1.2876 0.9676 0.4769 0.1755  -0.2429 0.2824  161 GLN F OE1 
11577 N NE2 . GLN F 161 ? 1.4376 1.0181 0.4962 0.1934  -0.2514 0.3166  161 GLN F NE2 
11578 N N   . TYR F 162 ? 1.0966 1.0338 0.4102 -0.0169 -0.2444 0.2171  162 TYR F N   
11579 C CA  . TYR F 162 ? 1.0872 0.9579 0.3906 -0.0674 -0.2186 0.1974  162 TYR F CA  
11580 C C   . TYR F 162 ? 1.0731 0.9944 0.3789 -0.1201 -0.2172 0.1779  162 TYR F C   
11581 O O   . TYR F 162 ? 1.0684 0.9387 0.3647 -0.1565 -0.1924 0.1599  162 TYR F O   
11582 C CB  . TYR F 162 ? 1.0400 0.8584 0.3824 -0.0668 -0.1953 0.1840  162 TYR F CB  
11583 C CG  . TYR F 162 ? 1.0723 0.8215 0.3967 -0.0270 -0.1938 0.2002  162 TYR F CG  
11584 C CD1 . TYR F 162 ? 1.1307 0.7909 0.3995 -0.0335 -0.1830 0.2108  162 TYR F CD1 
11585 C CD2 . TYR F 162 ? 1.0557 0.8212 0.4088 0.0137  -0.2014 0.2045  162 TYR F CD2 
11586 C CE1 . TYR F 162 ? 1.1798 0.7609 0.4150 -0.0060 -0.1805 0.2247  162 TYR F CE1 
11587 C CE2 . TYR F 162 ? 1.1045 0.7873 0.4232 0.0472  -0.1979 0.2178  162 TYR F CE2 
11588 C CZ  . TYR F 162 ? 1.1708 0.7572 0.4268 0.0344  -0.1878 0.2276  162 TYR F CZ  
11589 O OH  . TYR F 162 ? 1.2383 0.7279 0.4439 0.0593  -0.1834 0.2401  162 TYR F OH  
11590 N N   . SER F 163 ? 1.0792 1.1004 0.3908 -0.1242 -0.2425 0.1826  163 SER F N   
11591 C CA  . SER F 163 ? 1.0882 1.1525 0.3828 -0.1827 -0.2444 0.1654  163 SER F CA  
11592 C C   . SER F 163 ? 1.1548 1.2279 0.3855 -0.2001 -0.2592 0.1773  163 SER F C   
11593 O O   . SER F 163 ? 1.1807 1.3050 0.3844 -0.2477 -0.2697 0.1689  163 SER F O   
11594 C CB  . SER F 163 ? 1.0547 1.2349 0.3928 -0.1903 -0.2634 0.1624  163 SER F CB  
11595 O OG  . SER F 163 ? 1.0723 1.2787 0.3855 -0.2577 -0.2620 0.1422  163 SER F OG  
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   
;NAG B1154 HAS THE WRONG CHIRALITY AT ATOM C1 NAG D1154 HAS THE WRONG CHIRALITY AT ATOM C1 NAG F1154 HAS THE WRONG CHIRALITY AT ATOM C1
;
# 
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   ASP 1   1   1   ASP ASP A . n 
A 1 2   GLN 2   2   2   GLN GLN A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   CYS 4   4   4   CYS CYS A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  HIS 37  37  37  HIS HIS A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  CYS 42  42  42  CYS CYS A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  CYS 55  55  55  CYS CYS A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  MET 66  66  66  MET MET A . n 
A 1 67  CYS 67  67  67  CYS CYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 PHE 111 111 111 PHE PHE A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 TRP 122 122 122 TRP TRP A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 HIS 125 125 125 HIS HIS A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 CYS 135 135 135 CYS CYS A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 TRP 149 149 149 TRP TRP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 LYS 152 152 152 LYS LYS 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 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ILE 178 178 178 ILE ILE A . n 
A 1 179 HIS 179 179 179 HIS HIS A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 GLN 222 222 222 GLN GLN A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 MET 226 226 226 MET MET A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 TRP 230 230 230 TRP TRP A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 ASN 236 236 236 ASN ASN A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 ASN 240 240 240 ASN ASN A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 TYR 252 252 252 TYR TYR A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 LYS 255 255 255 LYS LYS A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 TYR 271 271 271 TYR TYR A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 CYS 274 274 274 CYS CYS A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 CYS 278 278 278 CYS CYS A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 MET 282 282 282 MET MET A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 MET 289 289 289 MET MET A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 THR 298 298 298 THR THR A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 CYS 302 302 302 CYS CYS A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 ASN 309 309 309 ASN ASN A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 ARG 318 318 318 ARG ARG A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 PRO 321 321 321 PRO PRO A . n 
A 1 322 GLN 322 322 ?   ?   ?   A . n 
A 1 323 ARG 323 323 ?   ?   ?   A . n 
A 1 324 GLU 324 324 ?   ?   ?   A . n 
A 1 325 THR 325 325 ?   ?   ?   A . n 
A 1 326 ARG 326 326 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASP 19  19  19  ASP ASP B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  HIS 25  25  25  HIS HIS B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  SER 27  27  27  SER SER B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  SER 32  32  32  SER SER B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  LYS 38  38  38  LYS LYS B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  ASN 50  50  50  ASN ASN B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  ASP 57  57  57  ASP ASP B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  MET 59  59  59  MET MET B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  GLU 64  64  64  GLU GLU B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  ARG 68  68  68  ARG ARG B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  MET 84  84  84  MET MET B . n 
B 2 85  GLU 85  85  85  GLU GLU B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  GLY 87  87  87  GLY GLY B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 MET 102 102 102 MET MET B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 ARG 106 106 106 ARG ARG B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASN 117 117 117 ASN ASN B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 ASP 120 120 120 ASP ASP B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 ARG 123 123 123 ARG ARG B . n 
B 2 124 LEU 124 124 124 LEU LEU B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 ARG 127 127 127 ARG ARG B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 TYR 141 141 141 TYR TYR B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ASN 146 146 146 ASN ASN B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 ARG 153 153 153 ARG ARG B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 GLY 155 155 155 GLY GLY B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 GLN 161 161 161 GLN GLN B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 GLU 164 164 ?   ?   ?   B . n 
B 2 165 GLU 165 165 ?   ?   ?   B . n 
B 2 166 ALA 166 166 ?   ?   ?   B . n 
C 1 1   ASP 1   1   1   ASP ASP C . n 
C 1 2   GLN 2   2   2   GLN GLN C . n 
C 1 3   ILE 3   3   3   ILE ILE C . n 
C 1 4   CYS 4   4   4   CYS CYS C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   GLY 6   6   6   GLY GLY C . n 
C 1 7   TYR 7   7   7   TYR TYR C . n 
C 1 8   HIS 8   8   8   HIS HIS C . n 
C 1 9   ALA 9   9   9   ALA ALA C . n 
C 1 10  ASN 10  10  10  ASN ASN C . n 
C 1 11  ASN 11  11  11  ASN ASN C . n 
C 1 12  SER 12  12  12  SER SER C . n 
C 1 13  THR 13  13  13  THR THR C . n 
C 1 14  GLU 14  14  14  GLU GLU C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  VAL 16  16  16  VAL VAL C . n 
C 1 17  ASP 17  17  17  ASP ASP C . n 
C 1 18  THR 18  18  18  THR THR C . n 
C 1 19  ILE 19  19  19  ILE ILE C . n 
C 1 20  MET 20  20  20  MET MET C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  LYS 22  22  22  LYS LYS C . n 
C 1 23  ASN 23  23  23  ASN ASN C . n 
C 1 24  VAL 24  24  24  VAL VAL C . n 
C 1 25  THR 25  25  25  THR THR C . n 
C 1 26  VAL 26  26  26  VAL VAL C . n 
C 1 27  THR 27  27  27  THR THR C . n 
C 1 28  HIS 28  28  28  HIS HIS C . n 
C 1 29  ALA 29  29  29  ALA ALA C . n 
C 1 30  GLN 30  30  30  GLN GLN C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  ILE 32  32  32  ILE ILE C . n 
C 1 33  LEU 33  33  33  LEU LEU C . n 
C 1 34  GLU 34  34  34  GLU GLU C . n 
C 1 35  LYS 35  35  35  LYS LYS C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  HIS 37  37  37  HIS HIS C . n 
C 1 38  ASN 38  38  38  ASN ASN C . n 
C 1 39  GLY 39  39  39  GLY GLY C . n 
C 1 40  LYS 40  40  40  LYS LYS C . n 
C 1 41  LEU 41  41  41  LEU LEU C . n 
C 1 42  CYS 42  42  42  CYS CYS C . n 
C 1 43  ASP 43  43  43  ASP ASP C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  ASP 45  45  45  ASP ASP C . n 
C 1 46  GLY 46  46  46  GLY GLY C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  LYS 48  48  48  LYS LYS C . n 
C 1 49  PRO 49  49  49  PRO PRO C . n 
C 1 50  LEU 50  50  50  LEU LEU C . n 
C 1 51  ILE 51  51  51  ILE ILE C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  ARG 53  53  53  ARG ARG C . n 
C 1 54  ASP 54  54  54  ASP ASP C . n 
C 1 55  CYS 55  55  55  CYS CYS C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  VAL 57  57  57  VAL VAL C . n 
C 1 58  ALA 58  58  58  ALA ALA C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  TRP 60  60  60  TRP TRP C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  PRO 65  65  65  PRO PRO C . n 
C 1 66  MET 66  66  66  MET MET C . n 
C 1 67  CYS 67  67  67  CYS CYS C . n 
C 1 68  ASP 68  68  68  ASP ASP C . n 
C 1 69  GLU 69  69  69  GLU GLU C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  ILE 71  71  71  ILE ILE C . n 
C 1 72  ASN 72  72  72  ASN ASN C . n 
C 1 73  VAL 73  73  73  VAL VAL C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  GLU 75  75  75  GLU GLU C . n 
C 1 76  TRP 76  76  76  TRP TRP C . n 
C 1 77  SER 77  77  77  SER SER C . n 
C 1 78  TYR 78  78  78  TYR TYR C . n 
C 1 79  ILE 79  79  79  ILE ILE C . n 
C 1 80  VAL 80  80  80  VAL VAL C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  LYS 82  82  82  LYS LYS C . n 
C 1 83  ALA 83  83  83  ALA ALA C . n 
C 1 84  ASN 84  84  84  ASN ASN C . n 
C 1 85  PRO 85  85  85  PRO PRO C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  ASN 87  87  87  ASN ASN C . n 
C 1 88  ASP 88  88  88  ASP ASP C . n 
C 1 89  LEU 89  89  89  LEU LEU C . n 
C 1 90  CYS 90  90  90  CYS CYS C . n 
C 1 91  TYR 91  91  91  TYR TYR C . n 
C 1 92  PRO 92  92  92  PRO PRO C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  ASP 94  94  94  ASP ASP C . n 
C 1 95  PHE 95  95  95  PHE PHE C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  TYR 98  98  98  TYR TYR C . n 
C 1 99  GLU 99  99  99  GLU GLU C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 LEU 101 101 101 LEU LEU C . n 
C 1 102 LYS 102 102 102 LYS LYS C . n 
C 1 103 HIS 103 103 103 HIS HIS C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 LEU 105 105 105 LEU LEU C . n 
C 1 106 SER 106 106 106 SER SER C . n 
C 1 107 ARG 107 107 107 ARG ARG C . n 
C 1 108 ILE 108 108 108 ILE ILE C . n 
C 1 109 ASN 109 109 109 ASN ASN C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 PHE 111 111 111 PHE PHE C . n 
C 1 112 GLU 112 112 112 GLU GLU C . n 
C 1 113 LYS 113 113 113 LYS LYS C . n 
C 1 114 ILE 114 114 114 ILE ILE C . n 
C 1 115 GLN 115 115 115 GLN GLN C . n 
C 1 116 ILE 116 116 116 ILE ILE C . n 
C 1 117 ILE 117 117 117 ILE ILE C . n 
C 1 118 PRO 118 118 118 PRO PRO C . n 
C 1 119 LYS 119 119 119 LYS LYS C . n 
C 1 120 SER 120 120 120 SER SER C . n 
C 1 121 SER 121 121 121 SER SER C . n 
C 1 122 TRP 122 122 122 TRP TRP C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 HIS 125 125 125 HIS HIS C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 SER 128 128 128 SER SER C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 VAL 131 131 131 VAL VAL C . n 
C 1 132 SER 132 132 132 SER SER C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ALA 134 134 134 ALA ALA C . n 
C 1 135 CYS 135 135 135 CYS CYS C . n 
C 1 136 PRO 136 136 136 PRO PRO C . n 
C 1 137 TYR 137 137 137 TYR TYR C . n 
C 1 138 GLN 138 138 138 GLN GLN C . n 
C 1 139 GLY 139 139 139 GLY GLY C . n 
C 1 140 LYS 140 140 140 LYS LYS C . n 
C 1 141 SER 141 141 141 SER SER C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 PHE 143 143 143 PHE PHE C . n 
C 1 144 PHE 144 144 144 PHE PHE C . n 
C 1 145 ARG 145 145 145 ARG ARG C . n 
C 1 146 ASN 146 146 146 ASN ASN C . n 
C 1 147 VAL 147 147 147 VAL VAL C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 TRP 149 149 149 TRP TRP C . n 
C 1 150 LEU 150 150 150 LEU LEU C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 LYS 152 152 152 LYS LYS C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 ASN 154 154 154 ASN ASN C . n 
C 1 155 SER 155 155 155 SER SER C . n 
C 1 156 THR 156 156 156 THR THR C . n 
C 1 157 TYR 157 157 157 TYR TYR C . n 
C 1 158 PRO 158 158 158 PRO PRO C . n 
C 1 159 THR 159 159 159 THR THR C . n 
C 1 160 ILE 160 160 160 ILE ILE C . n 
C 1 161 LYS 161 161 161 LYS LYS C . n 
C 1 162 ARG 162 162 162 ARG ARG C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 ASN 165 165 165 ASN ASN C . n 
C 1 166 ASN 166 166 166 ASN ASN C . n 
C 1 167 THR 167 167 167 THR THR C . n 
C 1 168 ASN 168 168 168 ASN ASN C . n 
C 1 169 GLN 169 169 169 GLN GLN C . n 
C 1 170 GLU 170 170 170 GLU GLU C . n 
C 1 171 ASP 171 171 171 ASP ASP C . n 
C 1 172 LEU 172 172 172 LEU LEU C . n 
C 1 173 LEU 173 173 173 LEU LEU C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 LEU 175 175 175 LEU LEU C . n 
C 1 176 TRP 176 176 176 TRP TRP C . n 
C 1 177 GLY 177 177 177 GLY GLY C . n 
C 1 178 ILE 178 178 178 ILE ILE C . n 
C 1 179 HIS 179 179 179 HIS HIS C . n 
C 1 180 HIS 180 180 180 HIS HIS C . n 
C 1 181 PRO 181 181 181 PRO PRO C . n 
C 1 182 ASN 182 182 182 ASN ASN C . n 
C 1 183 ASP 183 183 183 ASP ASP C . n 
C 1 184 ALA 184 184 184 ALA ALA C . n 
C 1 185 ALA 185 185 185 ALA ALA C . n 
C 1 186 GLU 186 186 186 GLU GLU C . n 
C 1 187 GLN 187 187 187 GLN GLN C . n 
C 1 188 THR 188 188 188 THR THR C . n 
C 1 189 LYS 189 189 189 LYS LYS C . n 
C 1 190 LEU 190 190 190 LEU LEU C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 GLN 192 192 192 GLN GLN C . n 
C 1 193 ASN 193 193 193 ASN ASN C . n 
C 1 194 PRO 194 194 194 PRO PRO C . n 
C 1 195 THR 195 195 195 THR THR C . n 
C 1 196 THR 196 196 196 THR THR C . n 
C 1 197 TYR 197 197 197 TYR TYR C . n 
C 1 198 ILE 198 198 198 ILE ILE C . n 
C 1 199 SER 199 199 199 SER SER C . n 
C 1 200 VAL 200 200 200 VAL VAL C . n 
C 1 201 GLY 201 201 201 GLY GLY C . n 
C 1 202 THR 202 202 202 THR THR C . n 
C 1 203 SER 203 203 203 SER SER C . n 
C 1 204 THR 204 204 204 THR THR C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 ASN 206 206 206 ASN ASN C . n 
C 1 207 GLN 207 207 207 GLN GLN C . n 
C 1 208 ARG 208 208 208 ARG ARG C . n 
C 1 209 LEU 209 209 209 LEU LEU C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PRO 211 211 211 PRO PRO C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ILE 213 213 213 ILE ILE C . n 
C 1 214 ALA 214 214 214 ALA ALA C . n 
C 1 215 THR 215 215 215 THR THR C . n 
C 1 216 ARG 216 216 216 ARG ARG C . n 
C 1 217 SER 217 217 217 SER SER C . n 
C 1 218 LYS 218 218 218 LYS LYS C . n 
C 1 219 VAL 219 219 219 VAL VAL C . n 
C 1 220 ASN 220 220 220 ASN ASN C . n 
C 1 221 GLY 221 221 221 GLY GLY C . n 
C 1 222 GLN 222 222 222 GLN GLN C . n 
C 1 223 SER 223 223 223 SER SER C . n 
C 1 224 GLY 224 224 224 GLY GLY C . n 
C 1 225 ARG 225 225 225 ARG ARG C . n 
C 1 226 MET 226 226 226 MET MET C . n 
C 1 227 GLU 227 227 227 GLU GLU C . n 
C 1 228 PHE 228 228 228 PHE PHE C . n 
C 1 229 PHE 229 229 229 PHE PHE C . n 
C 1 230 TRP 230 230 230 TRP TRP C . n 
C 1 231 THR 231 231 231 THR THR C . n 
C 1 232 ILE 232 232 232 ILE ILE C . n 
C 1 233 LEU 233 233 233 LEU LEU C . n 
C 1 234 LYS 234 234 234 LYS LYS C . n 
C 1 235 PRO 235 235 235 PRO PRO C . n 
C 1 236 ASN 236 236 236 ASN ASN C . n 
C 1 237 ASP 237 237 237 ASP ASP C . n 
C 1 238 ALA 238 238 238 ALA ALA C . n 
C 1 239 ILE 239 239 239 ILE ILE C . n 
C 1 240 ASN 240 240 240 ASN ASN C . n 
C 1 241 PHE 241 241 241 PHE PHE C . n 
C 1 242 GLU 242 242 242 GLU GLU C . n 
C 1 243 SER 243 243 243 SER SER C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 GLY 245 245 245 GLY GLY C . n 
C 1 246 ASN 246 246 246 ASN ASN C . n 
C 1 247 PHE 247 247 247 PHE PHE C . n 
C 1 248 ILE 248 248 248 ILE ILE C . n 
C 1 249 ALA 249 249 249 ALA ALA C . n 
C 1 250 PRO 250 250 250 PRO PRO C . n 
C 1 251 GLU 251 251 251 GLU GLU C . n 
C 1 252 TYR 252 252 252 TYR TYR C . n 
C 1 253 ALA 253 253 253 ALA ALA C . n 
C 1 254 TYR 254 254 254 TYR TYR C . n 
C 1 255 LYS 255 255 255 LYS LYS C . n 
C 1 256 ILE 256 256 256 ILE ILE C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 LYS 258 258 258 LYS LYS C . n 
C 1 259 LYS 259 259 259 LYS LYS C . n 
C 1 260 GLY 260 260 260 GLY GLY C . n 
C 1 261 ASP 261 261 261 ASP ASP C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 THR 263 263 263 THR THR C . n 
C 1 264 ILE 264 264 264 ILE ILE C . n 
C 1 265 MET 265 265 265 MET MET C . n 
C 1 266 LYS 266 266 266 LYS LYS C . n 
C 1 267 SER 267 267 267 SER SER C . n 
C 1 268 GLU 268 268 268 GLU GLU C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 GLU 270 270 270 GLU GLU C . n 
C 1 271 TYR 271 271 271 TYR TYR C . n 
C 1 272 GLY 272 272 272 GLY GLY C . n 
C 1 273 ASN 273 273 273 ASN ASN C . n 
C 1 274 CYS 274 274 274 CYS CYS C . n 
C 1 275 ASN 275 275 275 ASN ASN C . n 
C 1 276 THR 276 276 276 THR THR C . n 
C 1 277 LYS 277 277 277 LYS LYS C . n 
C 1 278 CYS 278 278 278 CYS CYS C . n 
C 1 279 GLN 279 279 279 GLN GLN C . n 
C 1 280 THR 280 280 280 THR THR C . n 
C 1 281 PRO 281 281 281 PRO PRO C . n 
C 1 282 MET 282 282 282 MET MET C . n 
C 1 283 GLY 283 283 283 GLY GLY C . n 
C 1 284 ALA 284 284 284 ALA ALA C . n 
C 1 285 ILE 285 285 285 ILE ILE C . n 
C 1 286 ASN 286 286 286 ASN ASN C . n 
C 1 287 SER 287 287 287 SER SER C . n 
C 1 288 SER 288 288 288 SER SER C . n 
C 1 289 MET 289 289 289 MET MET C . n 
C 1 290 PRO 290 290 290 PRO PRO C . n 
C 1 291 PHE 291 291 291 PHE PHE C . n 
C 1 292 HIS 292 292 292 HIS HIS C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 ILE 294 294 294 ILE ILE C . n 
C 1 295 HIS 295 295 295 HIS HIS C . n 
C 1 296 PRO 296 296 296 PRO PRO C . n 
C 1 297 LEU 297 297 297 LEU LEU C . n 
C 1 298 THR 298 298 298 THR THR C . n 
C 1 299 ILE 299 299 299 ILE ILE C . n 
C 1 300 GLY 300 300 300 GLY GLY C . n 
C 1 301 GLU 301 301 301 GLU GLU C . n 
C 1 302 CYS 302 302 302 CYS CYS C . n 
C 1 303 PRO 303 303 303 PRO PRO C . n 
C 1 304 LYS 304 304 304 LYS LYS C . n 
C 1 305 TYR 305 305 305 TYR TYR C . n 
C 1 306 VAL 306 306 306 VAL VAL C . n 
C 1 307 LYS 307 307 307 LYS LYS C . n 
C 1 308 SER 308 308 308 SER SER C . n 
C 1 309 ASN 309 309 309 ASN ASN C . n 
C 1 310 ARG 310 310 310 ARG ARG C . n 
C 1 311 LEU 311 311 311 LEU LEU C . n 
C 1 312 VAL 312 312 312 VAL VAL C . n 
C 1 313 LEU 313 313 313 LEU LEU C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 THR 315 315 315 THR THR C . n 
C 1 316 GLY 316 316 316 GLY GLY C . n 
C 1 317 LEU 317 317 317 LEU LEU C . n 
C 1 318 ARG 318 318 318 ARG ARG C . n 
C 1 319 ASN 319 319 319 ASN ASN C . n 
C 1 320 SER 320 320 320 SER SER C . n 
C 1 321 PRO 321 321 321 PRO PRO C . n 
C 1 322 GLN 322 322 ?   ?   ?   C . n 
C 1 323 ARG 323 323 ?   ?   ?   C . n 
C 1 324 GLU 324 324 ?   ?   ?   C . n 
C 1 325 THR 325 325 ?   ?   ?   C . n 
C 1 326 ARG 326 326 ?   ?   ?   C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  GLY 12  12  12  GLY GLY D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  MET 17  17  17  MET MET D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASP 19  19  19  ASP ASP D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  TYR 24  24  24  TYR TYR D . n 
D 2 25  HIS 25  25  25  HIS HIS D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  SER 27  27  27  SER SER D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  GLU 29  29  29  GLU GLU D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  SER 32  32  32  SER SER D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  TYR 34  34  34  TYR TYR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  LYS 38  38  38  LYS LYS D . n 
D 2 39  GLU 39  39  39  GLU GLU D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  THR 41  41  41  THR THR D . n 
D 2 42  GLN 42  42  42  GLN GLN D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLY 47  47  47  GLY GLY D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  ASN 50  50  50  ASN ASN D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  SER 54  54  54  SER SER D . n 
D 2 55  ILE 55  55  55  ILE ILE D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  ASP 57  57  57  ASP ASP D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  MET 59  59  59  MET MET D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  GLU 64  64  64  GLU GLU D . n 
D 2 65  ALA 65  65  65  ALA ALA D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  GLY 67  67  67  GLY GLY D . n 
D 2 68  ARG 68  68  68  ARG ARG D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  ASN 71  71  71  ASN ASN D . n 
D 2 72  ASN 72  72  72  ASN ASN D . n 
D 2 73  LEU 73  73  73  LEU LEU D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  ARG 75  75  75  ARG ARG D . n 
D 2 76  ARG 76  76  76  ARG ARG D . n 
D 2 77  ILE 77  77  77  ILE ILE D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ASN 81  81  81  ASN ASN D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  LYS 83  83  83  LYS LYS D . n 
D 2 84  MET 84  84  84  MET MET D . n 
D 2 85  GLU 85  85  85  GLU GLU D . n 
D 2 86  ASP 86  86  86  ASP ASP D . n 
D 2 87  GLY 87  87  87  GLY GLY D . n 
D 2 88  PHE 88  88  88  PHE PHE D . n 
D 2 89  LEU 89  89  89  LEU LEU D . n 
D 2 90  ASP 90  90  90  ASP ASP D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  TRP 92  92  92  TRP TRP D . n 
D 2 93  THR 93  93  93  THR THR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  ASN 95  95  95  ASN ASN D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  GLU 97  97  97  GLU GLU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 LEU 101 101 101 LEU LEU D . n 
D 2 102 MET 102 102 102 MET MET D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 ASN 104 104 104 ASN ASN D . n 
D 2 105 GLU 105 105 105 GLU GLU D . n 
D 2 106 ARG 106 106 106 ARG ARG D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 ASP 109 109 109 ASP ASP D . n 
D 2 110 PHE 110 110 110 PHE PHE D . n 
D 2 111 HIS 111 111 111 HIS HIS D . n 
D 2 112 ASP 112 112 112 ASP ASP D . n 
D 2 113 SER 113 113 113 SER SER D . n 
D 2 114 ASN 114 114 114 ASN ASN D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 LYS 116 116 116 LYS LYS D . n 
D 2 117 ASN 117 117 117 ASN ASN D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 TYR 119 119 119 TYR TYR D . n 
D 2 120 ASP 120 120 120 ASP ASP D . n 
D 2 121 LYS 121 121 121 LYS LYS D . n 
D 2 122 VAL 122 122 122 VAL VAL D . n 
D 2 123 ARG 123 123 123 ARG ARG D . n 
D 2 124 LEU 124 124 124 LEU LEU D . n 
D 2 125 GLN 125 125 125 GLN GLN D . n 
D 2 126 LEU 126 126 126 LEU LEU D . n 
D 2 127 ARG 127 127 127 ARG ARG D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 ALA 130 130 130 ALA ALA D . n 
D 2 131 LYS 131 131 131 LYS LYS D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 LEU 133 133 133 LEU LEU D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 ASN 135 135 135 ASN ASN D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 PHE 140 140 140 PHE PHE D . n 
D 2 141 TYR 141 141 141 TYR TYR D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASN 146 146 146 ASN ASN D . n 
D 2 147 GLU 147 147 147 GLU GLU D . n 
D 2 148 CYS 148 148 148 CYS CYS D . n 
D 2 149 MET 149 149 149 MET MET D . n 
D 2 150 GLU 150 150 150 GLU GLU D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 VAL 152 152 152 VAL VAL D . n 
D 2 153 ARG 153 153 153 ARG ARG D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 GLN 161 161 161 GLN GLN D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 SER 163 163 163 SER SER D . n 
D 2 164 GLU 164 164 ?   ?   ?   D . n 
D 2 165 GLU 165 165 ?   ?   ?   D . n 
D 2 166 ALA 166 166 ?   ?   ?   D . n 
E 1 1   ASP 1   1   1   ASP ASP E . n 
E 1 2   GLN 2   2   2   GLN GLN E . n 
E 1 3   ILE 3   3   3   ILE ILE E . n 
E 1 4   CYS 4   4   4   CYS CYS E . n 
E 1 5   ILE 5   5   5   ILE ILE E . n 
E 1 6   GLY 6   6   6   GLY GLY E . n 
E 1 7   TYR 7   7   7   TYR TYR E . n 
E 1 8   HIS 8   8   8   HIS HIS E . n 
E 1 9   ALA 9   9   9   ALA ALA E . n 
E 1 10  ASN 10  10  10  ASN ASN E . n 
E 1 11  ASN 11  11  11  ASN ASN E . n 
E 1 12  SER 12  12  12  SER SER E . n 
E 1 13  THR 13  13  13  THR THR E . n 
E 1 14  GLU 14  14  14  GLU GLU E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  VAL 16  16  16  VAL VAL E . n 
E 1 17  ASP 17  17  17  ASP ASP E . n 
E 1 18  THR 18  18  18  THR THR E . n 
E 1 19  ILE 19  19  19  ILE ILE E . n 
E 1 20  MET 20  20  20  MET MET E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  LYS 22  22  22  LYS LYS E . n 
E 1 23  ASN 23  23  23  ASN ASN E . n 
E 1 24  VAL 24  24  24  VAL VAL E . n 
E 1 25  THR 25  25  25  THR THR E . n 
E 1 26  VAL 26  26  26  VAL VAL E . n 
E 1 27  THR 27  27  27  THR THR E . n 
E 1 28  HIS 28  28  28  HIS HIS E . n 
E 1 29  ALA 29  29  29  ALA ALA E . n 
E 1 30  GLN 30  30  30  GLN GLN E . n 
E 1 31  ASP 31  31  31  ASP ASP E . n 
E 1 32  ILE 32  32  32  ILE ILE E . n 
E 1 33  LEU 33  33  33  LEU LEU E . n 
E 1 34  GLU 34  34  34  GLU GLU E . n 
E 1 35  LYS 35  35  35  LYS LYS E . n 
E 1 36  THR 36  36  36  THR THR E . n 
E 1 37  HIS 37  37  37  HIS HIS E . n 
E 1 38  ASN 38  38  38  ASN ASN E . n 
E 1 39  GLY 39  39  39  GLY GLY E . n 
E 1 40  LYS 40  40  40  LYS LYS E . n 
E 1 41  LEU 41  41  41  LEU LEU E . n 
E 1 42  CYS 42  42  42  CYS CYS E . n 
E 1 43  ASP 43  43  43  ASP ASP E . n 
E 1 44  LEU 44  44  44  LEU LEU E . n 
E 1 45  ASP 45  45  45  ASP ASP E . n 
E 1 46  GLY 46  46  46  GLY GLY E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  LYS 48  48  48  LYS LYS E . n 
E 1 49  PRO 49  49  49  PRO PRO E . n 
E 1 50  LEU 50  50  50  LEU LEU E . n 
E 1 51  ILE 51  51  51  ILE ILE E . n 
E 1 52  LEU 52  52  52  LEU LEU E . n 
E 1 53  ARG 53  53  53  ARG ARG E . n 
E 1 54  ASP 54  54  54  ASP ASP E . n 
E 1 55  CYS 55  55  55  CYS CYS E . n 
E 1 56  SER 56  56  56  SER SER E . n 
E 1 57  VAL 57  57  57  VAL VAL E . n 
E 1 58  ALA 58  58  58  ALA ALA E . n 
E 1 59  GLY 59  59  59  GLY GLY E . n 
E 1 60  TRP 60  60  60  TRP TRP E . n 
E 1 61  LEU 61  61  61  LEU LEU E . n 
E 1 62  LEU 62  62  62  LEU LEU E . n 
E 1 63  GLY 63  63  63  GLY GLY E . n 
E 1 64  ASN 64  64  64  ASN ASN E . n 
E 1 65  PRO 65  65  65  PRO PRO E . n 
E 1 66  MET 66  66  66  MET MET E . n 
E 1 67  CYS 67  67  67  CYS CYS E . n 
E 1 68  ASP 68  68  68  ASP ASP E . n 
E 1 69  GLU 69  69  69  GLU GLU E . n 
E 1 70  PHE 70  70  70  PHE PHE E . n 
E 1 71  ILE 71  71  71  ILE ILE E . n 
E 1 72  ASN 72  72  72  ASN ASN E . n 
E 1 73  VAL 73  73  73  VAL VAL E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  GLU 75  75  75  GLU GLU E . n 
E 1 76  TRP 76  76  76  TRP TRP E . n 
E 1 77  SER 77  77  77  SER SER E . n 
E 1 78  TYR 78  78  78  TYR TYR E . n 
E 1 79  ILE 79  79  79  ILE ILE E . n 
E 1 80  VAL 80  80  80  VAL VAL E . n 
E 1 81  GLU 81  81  81  GLU GLU E . n 
E 1 82  LYS 82  82  82  LYS LYS E . n 
E 1 83  ALA 83  83  83  ALA ALA E . n 
E 1 84  ASN 84  84  84  ASN ASN E . n 
E 1 85  PRO 85  85  85  PRO PRO E . n 
E 1 86  VAL 86  86  86  VAL VAL E . n 
E 1 87  ASN 87  87  87  ASN ASN E . n 
E 1 88  ASP 88  88  88  ASP ASP E . n 
E 1 89  LEU 89  89  89  LEU LEU E . n 
E 1 90  CYS 90  90  90  CYS CYS E . n 
E 1 91  TYR 91  91  91  TYR TYR E . n 
E 1 92  PRO 92  92  92  PRO PRO E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  ASP 94  94  94  ASP ASP E . n 
E 1 95  PHE 95  95  95  PHE PHE E . n 
E 1 96  ASN 96  96  96  ASN ASN E . n 
E 1 97  ASP 97  97  97  ASP ASP E . n 
E 1 98  TYR 98  98  98  TYR TYR E . n 
E 1 99  GLU 99  99  99  GLU GLU E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 LEU 101 101 101 LEU LEU E . n 
E 1 102 LYS 102 102 102 LYS LYS E . n 
E 1 103 HIS 103 103 103 HIS HIS E . n 
E 1 104 LEU 104 104 104 LEU LEU E . n 
E 1 105 LEU 105 105 105 LEU LEU E . n 
E 1 106 SER 106 106 106 SER SER E . n 
E 1 107 ARG 107 107 107 ARG ARG E . n 
E 1 108 ILE 108 108 108 ILE ILE E . n 
E 1 109 ASN 109 109 109 ASN ASN E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 PHE 111 111 111 PHE PHE E . n 
E 1 112 GLU 112 112 112 GLU GLU E . n 
E 1 113 LYS 113 113 113 LYS LYS E . n 
E 1 114 ILE 114 114 114 ILE ILE E . n 
E 1 115 GLN 115 115 115 GLN GLN E . n 
E 1 116 ILE 116 116 116 ILE ILE E . n 
E 1 117 ILE 117 117 117 ILE ILE E . n 
E 1 118 PRO 118 118 118 PRO PRO E . n 
E 1 119 LYS 119 119 119 LYS LYS E . n 
E 1 120 SER 120 120 120 SER SER E . n 
E 1 121 SER 121 121 121 SER SER E . n 
E 1 122 TRP 122 122 122 TRP TRP E . n 
E 1 123 SER 123 123 123 SER SER E . n 
E 1 124 SER 124 124 124 SER SER E . n 
E 1 125 HIS 125 125 125 HIS HIS E . n 
E 1 126 GLU 126 126 126 GLU GLU E . n 
E 1 127 ALA 127 127 127 ALA ALA E . n 
E 1 128 SER 128 128 128 SER SER E . n 
E 1 129 LEU 129 129 129 LEU LEU E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 VAL 131 131 131 VAL VAL E . n 
E 1 132 SER 132 132 132 SER SER E . n 
E 1 133 SER 133 133 133 SER SER E . n 
E 1 134 ALA 134 134 134 ALA ALA E . n 
E 1 135 CYS 135 135 135 CYS CYS E . n 
E 1 136 PRO 136 136 136 PRO PRO E . n 
E 1 137 TYR 137 137 137 TYR TYR E . n 
E 1 138 GLN 138 138 138 GLN GLN E . n 
E 1 139 GLY 139 139 139 GLY GLY E . n 
E 1 140 LYS 140 140 140 LYS LYS E . n 
E 1 141 SER 141 141 141 SER SER E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 PHE 143 143 143 PHE PHE E . n 
E 1 144 PHE 144 144 144 PHE PHE E . n 
E 1 145 ARG 145 145 145 ARG ARG E . n 
E 1 146 ASN 146 146 146 ASN ASN E . n 
E 1 147 VAL 147 147 147 VAL VAL E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 TRP 149 149 149 TRP TRP E . n 
E 1 150 LEU 150 150 150 LEU LEU E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 LYS 152 152 152 LYS LYS 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 SER 155 155 155 SER SER E . n 
E 1 156 THR 156 156 156 THR THR E . n 
E 1 157 TYR 157 157 157 TYR TYR E . n 
E 1 158 PRO 158 158 158 PRO PRO E . n 
E 1 159 THR 159 159 159 THR THR E . n 
E 1 160 ILE 160 160 160 ILE ILE E . n 
E 1 161 LYS 161 161 161 LYS LYS E . n 
E 1 162 ARG 162 162 162 ARG ARG E . n 
E 1 163 SER 163 163 163 SER SER E . n 
E 1 164 TYR 164 164 164 TYR TYR E . n 
E 1 165 ASN 165 165 165 ASN ASN E . n 
E 1 166 ASN 166 166 166 ASN ASN E . n 
E 1 167 THR 167 167 167 THR THR E . n 
E 1 168 ASN 168 168 168 ASN ASN E . n 
E 1 169 GLN 169 169 169 GLN GLN E . n 
E 1 170 GLU 170 170 170 GLU GLU E . n 
E 1 171 ASP 171 171 171 ASP ASP E . n 
E 1 172 LEU 172 172 172 LEU LEU E . n 
E 1 173 LEU 173 173 173 LEU LEU E . n 
E 1 174 VAL 174 174 174 VAL VAL E . n 
E 1 175 LEU 175 175 175 LEU LEU E . n 
E 1 176 TRP 176 176 176 TRP TRP E . n 
E 1 177 GLY 177 177 177 GLY GLY E . n 
E 1 178 ILE 178 178 178 ILE ILE E . n 
E 1 179 HIS 179 179 179 HIS HIS E . n 
E 1 180 HIS 180 180 180 HIS HIS E . n 
E 1 181 PRO 181 181 181 PRO PRO E . n 
E 1 182 ASN 182 182 182 ASN ASN E . n 
E 1 183 ASP 183 183 183 ASP ASP E . n 
E 1 184 ALA 184 184 184 ALA ALA E . n 
E 1 185 ALA 185 185 185 ALA ALA E . n 
E 1 186 GLU 186 186 186 GLU GLU E . n 
E 1 187 GLN 187 187 187 GLN GLN E . n 
E 1 188 THR 188 188 188 THR THR E . n 
E 1 189 LYS 189 189 189 LYS LYS E . n 
E 1 190 LEU 190 190 190 LEU LEU E . n 
E 1 191 TYR 191 191 191 TYR TYR E . n 
E 1 192 GLN 192 192 192 GLN GLN E . n 
E 1 193 ASN 193 193 193 ASN ASN E . n 
E 1 194 PRO 194 194 194 PRO PRO E . n 
E 1 195 THR 195 195 195 THR THR E . n 
E 1 196 THR 196 196 196 THR THR E . n 
E 1 197 TYR 197 197 197 TYR TYR E . n 
E 1 198 ILE 198 198 198 ILE ILE E . n 
E 1 199 SER 199 199 199 SER SER E . n 
E 1 200 VAL 200 200 200 VAL VAL E . n 
E 1 201 GLY 201 201 201 GLY GLY E . n 
E 1 202 THR 202 202 202 THR THR E . n 
E 1 203 SER 203 203 203 SER SER E . n 
E 1 204 THR 204 204 204 THR THR E . n 
E 1 205 LEU 205 205 205 LEU LEU E . n 
E 1 206 ASN 206 206 206 ASN ASN E . n 
E 1 207 GLN 207 207 207 GLN GLN E . n 
E 1 208 ARG 208 208 208 ARG ARG E . n 
E 1 209 LEU 209 209 209 LEU LEU E . n 
E 1 210 VAL 210 210 210 VAL VAL E . n 
E 1 211 PRO 211 211 211 PRO PRO E . n 
E 1 212 ARG 212 212 212 ARG ARG E . n 
E 1 213 ILE 213 213 213 ILE ILE E . n 
E 1 214 ALA 214 214 214 ALA ALA E . n 
E 1 215 THR 215 215 215 THR THR E . n 
E 1 216 ARG 216 216 216 ARG ARG E . n 
E 1 217 SER 217 217 217 SER SER E . n 
E 1 218 LYS 218 218 218 LYS LYS E . n 
E 1 219 VAL 219 219 219 VAL VAL E . n 
E 1 220 ASN 220 220 220 ASN ASN E . n 
E 1 221 GLY 221 221 221 GLY GLY E . n 
E 1 222 GLN 222 222 222 GLN GLN E . n 
E 1 223 SER 223 223 223 SER SER E . n 
E 1 224 GLY 224 224 224 GLY GLY E . n 
E 1 225 ARG 225 225 225 ARG ARG E . n 
E 1 226 MET 226 226 226 MET MET E . n 
E 1 227 GLU 227 227 227 GLU GLU E . n 
E 1 228 PHE 228 228 228 PHE PHE E . n 
E 1 229 PHE 229 229 229 PHE PHE E . n 
E 1 230 TRP 230 230 230 TRP TRP E . n 
E 1 231 THR 231 231 231 THR THR E . n 
E 1 232 ILE 232 232 232 ILE ILE E . n 
E 1 233 LEU 233 233 233 LEU LEU E . n 
E 1 234 LYS 234 234 234 LYS LYS E . n 
E 1 235 PRO 235 235 235 PRO PRO E . n 
E 1 236 ASN 236 236 236 ASN ASN E . n 
E 1 237 ASP 237 237 237 ASP ASP E . n 
E 1 238 ALA 238 238 238 ALA ALA E . n 
E 1 239 ILE 239 239 239 ILE ILE E . n 
E 1 240 ASN 240 240 240 ASN ASN E . n 
E 1 241 PHE 241 241 241 PHE PHE E . n 
E 1 242 GLU 242 242 242 GLU GLU E . n 
E 1 243 SER 243 243 243 SER SER E . n 
E 1 244 ASN 244 244 244 ASN ASN E . n 
E 1 245 GLY 245 245 245 GLY GLY E . n 
E 1 246 ASN 246 246 246 ASN ASN E . n 
E 1 247 PHE 247 247 247 PHE PHE E . n 
E 1 248 ILE 248 248 248 ILE ILE E . n 
E 1 249 ALA 249 249 249 ALA ALA E . n 
E 1 250 PRO 250 250 250 PRO PRO E . n 
E 1 251 GLU 251 251 251 GLU GLU E . n 
E 1 252 TYR 252 252 252 TYR TYR E . n 
E 1 253 ALA 253 253 253 ALA ALA E . n 
E 1 254 TYR 254 254 254 TYR TYR E . n 
E 1 255 LYS 255 255 255 LYS LYS E . n 
E 1 256 ILE 256 256 256 ILE ILE E . n 
E 1 257 VAL 257 257 257 VAL VAL E . n 
E 1 258 LYS 258 258 258 LYS LYS E . n 
E 1 259 LYS 259 259 259 LYS LYS E . n 
E 1 260 GLY 260 260 260 GLY GLY E . n 
E 1 261 ASP 261 261 261 ASP ASP E . n 
E 1 262 SER 262 262 262 SER SER E . n 
E 1 263 THR 263 263 263 THR THR E . n 
E 1 264 ILE 264 264 264 ILE ILE E . n 
E 1 265 MET 265 265 265 MET MET E . n 
E 1 266 LYS 266 266 266 LYS LYS E . n 
E 1 267 SER 267 267 267 SER SER E . n 
E 1 268 GLU 268 268 268 GLU GLU E . n 
E 1 269 LEU 269 269 269 LEU LEU E . n 
E 1 270 GLU 270 270 270 GLU GLU E . n 
E 1 271 TYR 271 271 271 TYR TYR E . n 
E 1 272 GLY 272 272 272 GLY GLY E . n 
E 1 273 ASN 273 273 273 ASN ASN E . n 
E 1 274 CYS 274 274 274 CYS CYS E . n 
E 1 275 ASN 275 275 275 ASN ASN E . n 
E 1 276 THR 276 276 276 THR THR E . n 
E 1 277 LYS 277 277 277 LYS LYS E . n 
E 1 278 CYS 278 278 278 CYS CYS E . n 
E 1 279 GLN 279 279 279 GLN GLN E . n 
E 1 280 THR 280 280 280 THR THR E . n 
E 1 281 PRO 281 281 281 PRO PRO E . n 
E 1 282 MET 282 282 282 MET MET E . n 
E 1 283 GLY 283 283 283 GLY GLY E . n 
E 1 284 ALA 284 284 284 ALA ALA E . n 
E 1 285 ILE 285 285 285 ILE ILE E . n 
E 1 286 ASN 286 286 286 ASN ASN E . n 
E 1 287 SER 287 287 287 SER SER E . n 
E 1 288 SER 288 288 288 SER SER E . n 
E 1 289 MET 289 289 289 MET MET E . n 
E 1 290 PRO 290 290 290 PRO PRO E . n 
E 1 291 PHE 291 291 291 PHE PHE E . n 
E 1 292 HIS 292 292 292 HIS HIS E . n 
E 1 293 ASN 293 293 293 ASN ASN E . n 
E 1 294 ILE 294 294 294 ILE ILE E . n 
E 1 295 HIS 295 295 295 HIS HIS E . n 
E 1 296 PRO 296 296 296 PRO PRO E . n 
E 1 297 LEU 297 297 297 LEU LEU E . n 
E 1 298 THR 298 298 298 THR THR E . n 
E 1 299 ILE 299 299 299 ILE ILE E . n 
E 1 300 GLY 300 300 300 GLY GLY E . n 
E 1 301 GLU 301 301 301 GLU GLU E . n 
E 1 302 CYS 302 302 302 CYS CYS E . n 
E 1 303 PRO 303 303 303 PRO PRO E . n 
E 1 304 LYS 304 304 304 LYS LYS E . n 
E 1 305 TYR 305 305 305 TYR TYR E . n 
E 1 306 VAL 306 306 306 VAL VAL E . n 
E 1 307 LYS 307 307 307 LYS LYS E . n 
E 1 308 SER 308 308 308 SER SER E . n 
E 1 309 ASN 309 309 309 ASN ASN E . n 
E 1 310 ARG 310 310 310 ARG ARG E . n 
E 1 311 LEU 311 311 311 LEU LEU E . n 
E 1 312 VAL 312 312 312 VAL VAL E . n 
E 1 313 LEU 313 313 313 LEU LEU E . n 
E 1 314 ALA 314 314 314 ALA ALA E . n 
E 1 315 THR 315 315 315 THR THR E . n 
E 1 316 GLY 316 316 316 GLY GLY E . n 
E 1 317 LEU 317 317 317 LEU LEU E . n 
E 1 318 ARG 318 318 318 ARG ARG E . n 
E 1 319 ASN 319 319 319 ASN ASN E . n 
E 1 320 SER 320 320 320 SER SER E . n 
E 1 321 PRO 321 321 321 PRO PRO E . n 
E 1 322 GLN 322 322 ?   ?   ?   E . n 
E 1 323 ARG 323 323 ?   ?   ?   E . n 
E 1 324 GLU 324 324 ?   ?   ?   E . n 
E 1 325 THR 325 325 ?   ?   ?   E . n 
E 1 326 ARG 326 326 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLN 15  15  15  GLN GLN F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  SER 27  27  27  SER SER F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  GLU 29  29  29  GLU GLU F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  LYS 43  43  43  LYS LYS F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLY 47  47  47  GLY GLY F . n 
F 2 48  VAL 48  48  48  VAL VAL F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  ILE 55  55  55  ILE ILE F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  ASP 57  57  57  ASP ASP F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  ARG 68  68  68  ARG ARG F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  ASN 72  72  72  ASN ASN F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  ARG 75  75  75  ARG ARG F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  MET 84  84  84  MET MET F . n 
F 2 85  GLU 85  85  85  GLU GLU F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  VAL 91  91  91  VAL VAL F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 ARG 106 106 106 ARG ARG F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 PHE 110 110 110 PHE PHE F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 ASP 120 120 120 ASP ASP F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 LEU 124 124 124 LEU LEU F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 LEU 133 133 133 LEU LEU F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASN 146 146 146 ASN ASN F . n 
F 2 147 GLU 147 147 147 GLU GLU F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 ARG 153 153 153 ARG ARG F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 GLN 161 161 161 GLN GLN F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 SER 163 163 163 SER SER F . n 
F 2 164 GLU 164 164 ?   ?   ?   F . n 
F 2 165 GLU 165 165 ?   ?   ?   F . n 
F 2 166 ALA 166 166 ?   ?   ?   F . 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 
G  3 NAG 1  1023 1023 NAG NAG A . 
H  3 NAG 1  1165 1165 NAG NAG A . 
I  4 SIA 1  1322 1322 SIA SIA A . 
J  5 GLA 2  1323 1323 GLA GLA A . 
K  6 NGS 3  1324 1324 NGS NGS A . 
L  7 FUC 4  1325 1325 FUC FUC A . 
M  3 NAG 1  1154 1154 NAG NAG B . 
N  8 EPE 1  1164 1164 EPE EPE B . 
O  3 NAG 1  1023 1023 NAG NAG C . 
P  3 NAG 1  1165 1165 NAG NAG C . 
Q  4 SIA 1  1322 1322 SIA SIA C . 
R  5 GLA 2  1323 1323 GLA GLA C . 
S  6 NGS 3  1324 1324 NGS NGS C . 
T  7 FUC 4  1325 1325 FUC FUC C . 
U  3 NAG 1  1154 1154 NAG NAG D . 
V  8 EPE 1  1164 1164 EPE EPE D . 
W  3 NAG 1  1023 1023 NAG NAG E . 
X  3 NAG 1  1165 1165 NAG NAG E . 
Y  4 SIA 1  1322 1322 SIA SIA E . 
Z  5 GLA 2  1323 1323 GLA GLA E . 
AA 6 NGS 3  1324 1324 NGS NGS E . 
BA 7 FUC 4  1325 1325 FUC FUC E . 
CA 3 NAG 1  1154 1154 NAG NAG F . 
DA 8 EPE 1  1164 1164 EPE EPE F . 
EA 9 HOH 1  2001 2001 HOH HOH A . 
EA 9 HOH 2  2002 2002 HOH HOH A . 
EA 9 HOH 3  2003 2003 HOH HOH A . 
EA 9 HOH 4  2004 2004 HOH HOH A . 
EA 9 HOH 5  2005 2005 HOH HOH A . 
EA 9 HOH 6  2006 2006 HOH HOH A . 
EA 9 HOH 7  2007 2007 HOH HOH A . 
EA 9 HOH 8  2008 2008 HOH HOH A . 
EA 9 HOH 9  2009 2009 HOH HOH A . 
EA 9 HOH 10 2010 2010 HOH HOH A . 
EA 9 HOH 11 2011 2011 HOH HOH A . 
EA 9 HOH 12 2012 2012 HOH HOH A . 
EA 9 HOH 13 2013 2013 HOH HOH A . 
EA 9 HOH 14 2014 2014 HOH HOH A . 
EA 9 HOH 15 2015 2015 HOH HOH A . 
EA 9 HOH 16 2016 2016 HOH HOH A . 
EA 9 HOH 17 2017 2017 HOH HOH A . 
EA 9 HOH 18 2018 2018 HOH HOH A . 
EA 9 HOH 19 2019 2019 HOH HOH A . 
EA 9 HOH 20 2020 2020 HOH HOH A . 
EA 9 HOH 21 2021 2021 HOH HOH A . 
EA 9 HOH 22 2022 2022 HOH HOH A . 
EA 9 HOH 23 2023 2023 HOH HOH A . 
EA 9 HOH 24 2024 2024 HOH HOH A . 
EA 9 HOH 25 2025 2025 HOH HOH A . 
EA 9 HOH 26 2026 2026 HOH HOH A . 
EA 9 HOH 27 2027 2027 HOH HOH A . 
EA 9 HOH 28 2028 2028 HOH HOH A . 
EA 9 HOH 29 2029 2029 HOH HOH A . 
EA 9 HOH 30 2030 2030 HOH HOH A . 
EA 9 HOH 31 2031 2031 HOH HOH A . 
EA 9 HOH 32 2032 2032 HOH HOH A . 
EA 9 HOH 33 2033 2033 HOH HOH A . 
EA 9 HOH 34 2034 2034 HOH HOH A . 
EA 9 HOH 35 2035 2035 HOH HOH A . 
EA 9 HOH 36 2036 2036 HOH HOH A . 
EA 9 HOH 37 2037 2037 HOH HOH A . 
EA 9 HOH 38 2038 2038 HOH HOH A . 
EA 9 HOH 39 2039 2039 HOH HOH A . 
EA 9 HOH 40 2040 2040 HOH HOH A . 
EA 9 HOH 41 2041 2041 HOH HOH A . 
EA 9 HOH 42 2042 2042 HOH HOH A . 
EA 9 HOH 43 2043 2043 HOH HOH A . 
EA 9 HOH 44 2044 2044 HOH HOH A . 
EA 9 HOH 45 2045 2045 HOH HOH A . 
EA 9 HOH 46 2046 2046 HOH HOH A . 
EA 9 HOH 47 2047 2047 HOH HOH A . 
EA 9 HOH 48 2048 2048 HOH HOH A . 
EA 9 HOH 49 2049 2049 HOH HOH A . 
EA 9 HOH 50 2050 2050 HOH HOH A . 
EA 9 HOH 51 2051 2051 HOH HOH A . 
EA 9 HOH 52 2052 2052 HOH HOH A . 
EA 9 HOH 53 2053 2053 HOH HOH A . 
EA 9 HOH 54 2054 2054 HOH HOH A . 
EA 9 HOH 55 2055 2055 HOH HOH A . 
EA 9 HOH 56 2056 2056 HOH HOH A . 
EA 9 HOH 57 2057 2057 HOH HOH A . 
EA 9 HOH 58 2058 2058 HOH HOH A . 
EA 9 HOH 59 2059 2059 HOH HOH A . 
EA 9 HOH 60 2060 2060 HOH HOH A . 
FA 9 HOH 1  2001 2001 HOH HOH B . 
FA 9 HOH 2  2002 2002 HOH HOH B . 
FA 9 HOH 3  2003 2003 HOH HOH B . 
FA 9 HOH 4  2004 2004 HOH HOH B . 
FA 9 HOH 5  2005 2005 HOH HOH B . 
FA 9 HOH 6  2006 2006 HOH HOH B . 
FA 9 HOH 7  2007 2007 HOH HOH B . 
FA 9 HOH 8  2008 2008 HOH HOH B . 
FA 9 HOH 9  2009 2009 HOH HOH B . 
FA 9 HOH 10 2010 2010 HOH HOH B . 
FA 9 HOH 11 2011 2011 HOH HOH B . 
FA 9 HOH 12 2012 2012 HOH HOH B . 
FA 9 HOH 13 2013 2013 HOH HOH B . 
FA 9 HOH 14 2014 2014 HOH HOH B . 
FA 9 HOH 15 2015 2015 HOH HOH B . 
FA 9 HOH 16 2016 2016 HOH HOH B . 
FA 9 HOH 17 2017 2017 HOH HOH B . 
FA 9 HOH 18 2018 2018 HOH HOH B . 
FA 9 HOH 19 2019 2019 HOH HOH B . 
FA 9 HOH 20 2020 2020 HOH HOH B . 
FA 9 HOH 21 2021 2021 HOH HOH B . 
FA 9 HOH 22 2022 2022 HOH HOH B . 
FA 9 HOH 23 2023 2023 HOH HOH B . 
FA 9 HOH 24 2024 2024 HOH HOH B . 
FA 9 HOH 25 2025 2025 HOH HOH B . 
FA 9 HOH 26 2026 2026 HOH HOH B . 
FA 9 HOH 27 2027 2027 HOH HOH B . 
FA 9 HOH 28 2028 2028 HOH HOH B . 
FA 9 HOH 29 2029 2029 HOH HOH B . 
FA 9 HOH 30 2030 2030 HOH HOH B . 
FA 9 HOH 31 2031 2031 HOH HOH B . 
FA 9 HOH 32 2032 2032 HOH HOH B . 
FA 9 HOH 33 2033 2033 HOH HOH B . 
FA 9 HOH 34 2034 2034 HOH HOH B . 
FA 9 HOH 35 2035 2035 HOH HOH B . 
FA 9 HOH 36 2036 2036 HOH HOH B . 
FA 9 HOH 37 2037 2037 HOH HOH B . 
GA 9 HOH 1  2001 2001 HOH HOH C . 
GA 9 HOH 2  2002 2002 HOH HOH C . 
GA 9 HOH 3  2003 2003 HOH HOH C . 
GA 9 HOH 4  2004 2004 HOH HOH C . 
GA 9 HOH 5  2005 2005 HOH HOH C . 
GA 9 HOH 6  2006 2006 HOH HOH C . 
GA 9 HOH 7  2007 2007 HOH HOH C . 
GA 9 HOH 8  2008 2008 HOH HOH C . 
GA 9 HOH 9  2009 2009 HOH HOH C . 
GA 9 HOH 10 2010 2010 HOH HOH C . 
GA 9 HOH 11 2011 2011 HOH HOH C . 
GA 9 HOH 12 2012 2012 HOH HOH C . 
GA 9 HOH 13 2013 2013 HOH HOH C . 
GA 9 HOH 14 2014 2014 HOH HOH C . 
GA 9 HOH 15 2015 2015 HOH HOH C . 
GA 9 HOH 16 2016 2016 HOH HOH C . 
GA 9 HOH 17 2017 2017 HOH HOH C . 
GA 9 HOH 18 2018 2018 HOH HOH C . 
GA 9 HOH 19 2019 2019 HOH HOH C . 
GA 9 HOH 20 2020 2020 HOH HOH C . 
GA 9 HOH 21 2021 2021 HOH HOH C . 
GA 9 HOH 22 2022 2022 HOH HOH C . 
GA 9 HOH 23 2023 2023 HOH HOH C . 
GA 9 HOH 24 2024 2024 HOH HOH C . 
GA 9 HOH 25 2025 2025 HOH HOH C . 
GA 9 HOH 26 2026 2026 HOH HOH C . 
GA 9 HOH 27 2027 2027 HOH HOH C . 
GA 9 HOH 28 2028 2028 HOH HOH C . 
GA 9 HOH 29 2029 2029 HOH HOH C . 
GA 9 HOH 30 2030 2030 HOH HOH C . 
GA 9 HOH 31 2031 2031 HOH HOH C . 
GA 9 HOH 32 2032 2032 HOH HOH C . 
GA 9 HOH 33 2033 2033 HOH HOH C . 
GA 9 HOH 34 2034 2034 HOH HOH C . 
GA 9 HOH 35 2035 2035 HOH HOH C . 
GA 9 HOH 36 2036 2036 HOH HOH C . 
GA 9 HOH 37 2037 2037 HOH HOH C . 
GA 9 HOH 38 2038 2038 HOH HOH C . 
GA 9 HOH 39 2039 2039 HOH HOH C . 
GA 9 HOH 40 2040 2040 HOH HOH C . 
GA 9 HOH 41 2041 2041 HOH HOH C . 
GA 9 HOH 42 2042 2042 HOH HOH C . 
GA 9 HOH 43 2043 2043 HOH HOH C . 
GA 9 HOH 44 2044 2044 HOH HOH C . 
GA 9 HOH 45 2045 2045 HOH HOH C . 
GA 9 HOH 46 2046 2046 HOH HOH C . 
GA 9 HOH 47 2047 2047 HOH HOH C . 
GA 9 HOH 48 2048 2048 HOH HOH C . 
GA 9 HOH 49 2049 2049 HOH HOH C . 
GA 9 HOH 50 2050 2050 HOH HOH C . 
GA 9 HOH 51 2051 2051 HOH HOH C . 
GA 9 HOH 52 2052 2052 HOH HOH C . 
HA 9 HOH 1  2001 2001 HOH HOH D . 
HA 9 HOH 2  2002 2002 HOH HOH D . 
HA 9 HOH 3  2003 2003 HOH HOH D . 
HA 9 HOH 4  2004 2004 HOH HOH D . 
HA 9 HOH 5  2005 2005 HOH HOH D . 
HA 9 HOH 6  2006 2006 HOH HOH D . 
HA 9 HOH 7  2007 2007 HOH HOH D . 
HA 9 HOH 8  2008 2008 HOH HOH D . 
HA 9 HOH 9  2009 2009 HOH HOH D . 
HA 9 HOH 10 2010 2010 HOH HOH D . 
HA 9 HOH 11 2011 2011 HOH HOH D . 
HA 9 HOH 12 2012 2012 HOH HOH D . 
HA 9 HOH 13 2013 2013 HOH HOH D . 
HA 9 HOH 14 2014 2014 HOH HOH D . 
HA 9 HOH 15 2015 2015 HOH HOH D . 
HA 9 HOH 16 2016 2016 HOH HOH D . 
HA 9 HOH 17 2017 2017 HOH HOH D . 
HA 9 HOH 18 2018 2018 HOH HOH D . 
HA 9 HOH 19 2019 2019 HOH HOH D . 
HA 9 HOH 20 2020 2020 HOH HOH D . 
HA 9 HOH 21 2021 2021 HOH HOH D . 
HA 9 HOH 22 2022 2022 HOH HOH D . 
HA 9 HOH 23 2023 2023 HOH HOH D . 
HA 9 HOH 24 2024 2024 HOH HOH D . 
HA 9 HOH 25 2025 2025 HOH HOH D . 
HA 9 HOH 26 2026 2026 HOH HOH D . 
HA 9 HOH 27 2027 2027 HOH HOH D . 
HA 9 HOH 28 2028 2028 HOH HOH D . 
HA 9 HOH 29 2029 2029 HOH HOH D . 
HA 9 HOH 30 2030 2030 HOH HOH D . 
HA 9 HOH 31 2031 2031 HOH HOH D . 
HA 9 HOH 32 2032 2032 HOH HOH D . 
HA 9 HOH 33 2033 2033 HOH HOH D . 
HA 9 HOH 34 2034 2034 HOH HOH D . 
HA 9 HOH 35 2035 2035 HOH HOH D . 
HA 9 HOH 36 2036 2036 HOH HOH D . 
HA 9 HOH 37 2037 2037 HOH HOH D . 
HA 9 HOH 38 2038 2038 HOH HOH D . 
IA 9 HOH 1  2001 2001 HOH HOH E . 
IA 9 HOH 2  2002 2002 HOH HOH E . 
IA 9 HOH 3  2003 2003 HOH HOH E . 
IA 9 HOH 4  2004 2004 HOH HOH E . 
IA 9 HOH 5  2005 2005 HOH HOH E . 
IA 9 HOH 6  2006 2006 HOH HOH E . 
IA 9 HOH 7  2007 2007 HOH HOH E . 
IA 9 HOH 8  2008 2008 HOH HOH E . 
IA 9 HOH 9  2009 2009 HOH HOH E . 
IA 9 HOH 10 2010 2010 HOH HOH E . 
IA 9 HOH 11 2011 2011 HOH HOH E . 
IA 9 HOH 12 2012 2012 HOH HOH E . 
IA 9 HOH 13 2013 2013 HOH HOH E . 
IA 9 HOH 14 2014 2014 HOH HOH E . 
IA 9 HOH 15 2015 2015 HOH HOH E . 
IA 9 HOH 16 2016 2016 HOH HOH E . 
IA 9 HOH 17 2017 2017 HOH HOH E . 
IA 9 HOH 18 2018 2018 HOH HOH E . 
IA 9 HOH 19 2019 2019 HOH HOH E . 
IA 9 HOH 20 2020 2020 HOH HOH E . 
IA 9 HOH 21 2021 2021 HOH HOH E . 
IA 9 HOH 22 2022 2022 HOH HOH E . 
IA 9 HOH 23 2023 2023 HOH HOH E . 
IA 9 HOH 24 2024 2024 HOH HOH E . 
IA 9 HOH 25 2025 2025 HOH HOH E . 
IA 9 HOH 26 2026 2026 HOH HOH E . 
IA 9 HOH 27 2027 2027 HOH HOH E . 
IA 9 HOH 28 2028 2028 HOH HOH E . 
IA 9 HOH 29 2029 2029 HOH HOH E . 
IA 9 HOH 30 2030 2030 HOH HOH E . 
IA 9 HOH 31 2031 2031 HOH HOH E . 
IA 9 HOH 32 2032 2032 HOH HOH E . 
IA 9 HOH 33 2033 2033 HOH HOH E . 
IA 9 HOH 34 2034 2034 HOH HOH E . 
IA 9 HOH 35 2035 2035 HOH HOH E . 
IA 9 HOH 36 2036 2036 HOH HOH E . 
IA 9 HOH 37 2037 2037 HOH HOH E . 
IA 9 HOH 38 2038 2038 HOH HOH E . 
IA 9 HOH 39 2039 2039 HOH HOH E . 
IA 9 HOH 40 2040 2040 HOH HOH E . 
IA 9 HOH 41 2041 2041 HOH HOH E . 
IA 9 HOH 42 2042 2042 HOH HOH E . 
IA 9 HOH 43 2043 2043 HOH HOH E . 
IA 9 HOH 44 2044 2044 HOH HOH E . 
IA 9 HOH 45 2045 2045 HOH HOH E . 
IA 9 HOH 46 2046 2046 HOH HOH E . 
IA 9 HOH 47 2047 2047 HOH HOH E . 
IA 9 HOH 48 2048 2048 HOH HOH E . 
IA 9 HOH 49 2049 2049 HOH HOH E . 
JA 9 HOH 1  2001 2001 HOH HOH F . 
JA 9 HOH 2  2002 2002 HOH HOH F . 
JA 9 HOH 3  2003 2003 HOH HOH F . 
JA 9 HOH 4  2004 2004 HOH HOH F . 
JA 9 HOH 5  2005 2005 HOH HOH F . 
JA 9 HOH 6  2006 2006 HOH HOH F . 
JA 9 HOH 7  2007 2007 HOH HOH F . 
JA 9 HOH 8  2008 2008 HOH HOH F . 
JA 9 HOH 9  2009 2009 HOH HOH F . 
JA 9 HOH 10 2010 2010 HOH HOH F . 
JA 9 HOH 11 2011 2011 HOH HOH F . 
JA 9 HOH 12 2012 2012 HOH HOH F . 
JA 9 HOH 13 2013 2013 HOH HOH F . 
JA 9 HOH 14 2014 2014 HOH HOH F . 
JA 9 HOH 15 2015 2015 HOH HOH F . 
JA 9 HOH 16 2016 2016 HOH HOH F . 
JA 9 HOH 17 2017 2017 HOH HOH F . 
JA 9 HOH 18 2018 2018 HOH HOH F . 
JA 9 HOH 19 2019 2019 HOH HOH F . 
JA 9 HOH 20 2020 2020 HOH HOH F . 
JA 9 HOH 21 2021 2021 HOH HOH F . 
JA 9 HOH 22 2022 2022 HOH HOH F . 
JA 9 HOH 23 2023 2023 HOH HOH F . 
JA 9 HOH 24 2024 2024 HOH HOH F . 
JA 9 HOH 25 2025 2025 HOH HOH F . 
JA 9 HOH 26 2026 2026 HOH HOH F . 
JA 9 HOH 27 2027 2027 HOH HOH F . 
JA 9 HOH 28 2030 2030 HOH HOH F . 
JA 9 HOH 29 2031 2031 HOH HOH F . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 23  A ASN 23  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' 
4 C ASN 23  C ASN 23  ? ASN 'GLYCOSYLATION SITE' 
5 C ASN 165 C ASN 165 ? ASN 'GLYCOSYLATION SITE' 
6 D ASN 154 D ASN 154 ? ASN 'GLYCOSYLATION SITE' 
7 E ASN 23  E ASN 23  ? ASN 'GLYCOSYLATION SITE' 
8 E ASN 165 E ASN 165 ? ASN 'GLYCOSYLATION SITE' 
9 F ASN 154 F ASN 154 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 34760 ? 
1 MORE         -73.0 ? 
1 'SSA (A^2)'  60720 ? 
# 
_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 2013-09-25 
2 'Structure model' 1 1 2013-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               '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 6.3291  57.1668 52.2900 0.2079 0.5976 0.2743 0.0087  0.0803  -0.0965 0.8433 0.2905 8.4946  
-0.0643 -1.5773 -0.4269 -0.0407 -0.1576 -0.0400 0.2322  0.0085  0.1735  -0.3729 -1.3015 0.0322  
'X-RAY DIFFRACTION' 2  ? refined 8.3500  47.2504 81.2297 0.3553 0.6778 0.2911 -0.0665 0.1775  -0.0393 4.8703 1.5295 3.5095  0.1418 
-1.3126 -0.9893 -0.4096 -0.3085 -0.2775 0.3167  0.0808  0.2565  0.1677  -0.9783 0.3287  
'X-RAY DIFFRACTION' 3  ? refined 10.4208 49.8007 93.0866 0.6460 0.9074 0.2397 -0.0675 0.1731  -0.0683 1.5707 3.0139 2.4801  
-0.4707 0.4946  -0.5734 -0.2907 -0.4922 0.0228  0.7588  0.1063  0.1211  -0.0297 -0.7371 0.1845  
'X-RAY DIFFRACTION' 4  ? refined 8.9517  56.0711 48.5969 0.1210 0.4123 0.3424 0.0560  0.0809  -0.0590 0.6962 0.3793 13.1346 0.2094 
-1.3326 -0.0068 0.1233  -0.2384 0.0813  0.1324  -0.0897 0.3405  -0.0082 -0.7394 -0.0336 
'X-RAY DIFFRACTION' 5  ? refined 17.7238 53.3488 34.1109 0.1233 0.1696 0.1790 -0.0399 0.0531  -0.0866 1.2998 0.3288 10.2986 0.3854 
2.4918  0.6259  -0.0789 -0.3608 0.0476  0.0974  -0.1812 0.1215  0.3093  -1.0683 0.2601  
'X-RAY DIFFRACTION' 6  ? refined 17.0572 49.1275 1.6788  0.1757 0.2695 0.1378 -0.0145 -0.0050 -0.1038 4.5488 2.3942 11.0618 
-0.0399 0.8259  -0.0875 -0.1001 1.1055  -0.4110 -0.4705 -0.0530 0.2056  0.9338  0.2175  0.1532  
'X-RAY DIFFRACTION' 7  ? refined 35.7852 30.1135 56.0910 0.4922 0.3422 0.2737 0.1150  0.0409  0.1394  0.2464 0.7108 6.3309  
-0.0896 0.6560  -0.2438 0.0594  -0.1884 -0.1478 0.2338  -0.0486 -0.1139 1.4660  0.2916  -0.0107 
'X-RAY DIFFRACTION' 8  ? refined 40.0291 34.9124 92.8111 0.7672 0.7831 0.2579 0.0946  -0.0373 0.1878  1.8198 2.2108 2.0457  0.2986 
0.0713  1.0367  0.1604  -0.5930 -0.1458 0.8272  -0.3539 -0.0688 0.6624  0.2985  0.1936  
'X-RAY DIFFRACTION' 9  ? refined 47.6701 38.8361 83.7750 0.7276 1.0869 0.2989 0.3541  -0.0761 0.2931  2.6759 0.6317 3.6834  1.0317 
2.6696  1.3310  -0.0261 -0.0692 -0.0060 0.3432  0.0058  -0.1786 0.6895  0.8288  0.0203  
'X-RAY DIFFRACTION' 10 ? refined 35.0376 31.2595 47.4399 0.3181 0.1401 0.3064 0.0468  0.0039  0.1094  1.0779 1.0398 13.2052 
-0.5038 0.1228  -2.0212 -0.1271 -0.3714 -0.3225 0.2270  0.1114  -0.1406 0.4601  0.3499  0.0158  
'X-RAY DIFFRACTION' 11 ? refined 33.5170 40.5174 34.1038 0.0985 0.2061 0.1678 0.0439  0.0411  0.0803  0.8308 0.7449 10.1944 
-0.5374 -1.7066 1.6914  -0.2637 -0.2068 -0.1490 0.2428  -0.0523 0.0053  0.7810  0.8014  0.3160  
'X-RAY DIFFRACTION' 12 ? refined 37.5188 42.0384 1.6598  0.2504 0.2185 0.1428 0.0902  0.0992  0.0562  2.4859 4.0521 10.8940 
-0.8337 0.2043  0.7577  0.2581  0.6271  0.0524  -0.9732 -0.4297 -0.4819 -0.5712 0.7167  0.1716  
'X-RAY DIFFRACTION' 13 ? refined 44.6140 67.7678 56.0888 0.4397 0.2968 0.2719 -0.1211 -0.1446 -0.0308 0.5531 0.3507 7.4480  0.2062 
-0.1716 0.7528  0.0242  -0.2899 0.1627  0.1291  -0.0084 -0.0889 -0.9986 1.0309  -0.0157 
'X-RAY DIFFRACTION' 14 ? refined 38.7279 69.1795 93.3782 0.8875 0.7730 0.2609 -0.0598 -0.1393 -0.1321 2.4015 1.5156 1.4271  
-0.0035 -0.4161 -0.4854 -0.1337 -0.9188 0.0750  0.4173  -0.1245 -0.0824 -0.6150 0.3705  0.2581  
'X-RAY DIFFRACTION' 15 ? refined 31.3380 72.2214 83.9392 1.2703 0.5306 0.2035 -0.0001 -0.2382 -0.2068 3.3647 1.8632 2.4337  
-1.5169 -2.5740 0.7136  0.2907  -0.2941 0.2028  0.4040  -0.2273 0.0934  -0.9839 0.1652  -0.0634 
'X-RAY DIFFRACTION' 16 ? refined 43.9970 66.5408 47.4372 0.2788 0.2620 0.2684 -0.1309 -0.0851 -0.0348 0.8538 1.4736 12.6075 0.0759 
1.5695  1.3324  0.0365  -0.2217 0.3000  0.4140  0.0892  -0.3014 -0.6186 0.2850  -0.1257 
'X-RAY DIFFRACTION' 17 ? refined 37.0543 62.5438 31.0837 0.2467 0.1368 0.1797 -0.0019 -0.0967 0.0137  0.1540 1.9380 10.5355 0.0941 
-0.5310 -2.8664 0.0004  -0.1029 0.0649  0.3785  -0.2128 -0.0861 -1.4761 0.2408  0.2124  
'X-RAY DIFFRACTION' 18 ? refined 34.0214 60.7207 13.4726 0.1158 0.0483 0.1152 -0.0200 -0.0526 0.0147  1.3539 2.1690 11.4835 0.5594 
-1.4230 -1.4877 -0.2548 0.2327  0.1543  -0.3286 0.0118  0.0279  -0.2677 -0.4142 0.2430  
# 
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 1   ? ? A 90  ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 91  ? ? A 122 ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 123 ? ? A 259 ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 260 ? ? A 321 ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  B 1   ? ? B 104 ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  B 105 ? ? B 163 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  C 1   ? ? C 104 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  C 105 ? ? C 233 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  C 234 ? ? C 264 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 C 265 ? ? C 321 ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 D 1   ? ? D 104 ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 D 105 ? ? D 163 ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 E 1   ? ? E 104 ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 E 105 ? ? E 226 ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 E 227 ? ? E 264 ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 E 265 ? ? E 321 ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 F 1   ? ? F 82  ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 F 83  ? ? F 163 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.7.0032 ? 1 
MOSFLM 'data reduction' .        ? 2 
SCALA  'data scaling'   .        ? 3 
PHASER phasing          .        ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 121  ? ? NH2 A ARG 162  ? ? 2.00 
2 1 O   B HOH 2026 ? ? O   D HOH 2026 ? ? 2.01 
3 1 NH1 B ARG 68   ? ? OD1 B ASN 81   ? ? 2.03 
4 1 O   A ASN 87   ? ? O   A HOH 2027 ? ? 2.10 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             E 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              162 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             E 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              162 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             E 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              162 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.32 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.02 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 53  ? ? 57.29   -114.90 
2  1 ASP A 88  ? ? -104.58 -114.23 
3  1 GLN A 192 ? ? 63.13   -60.86  
4  1 GLU A 270 ? ? -99.74  -114.46 
5  1 ALA B 5   ? ? -90.86  -62.99  
6  1 ARG B 127 ? ? 54.48   -133.18 
7  1 ARG C 53  ? ? 57.37   -114.97 
8  1 ASP C 88  ? ? -104.67 -114.24 
9  1 GLN C 192 ? ? 63.16   -60.95  
10 1 GLU C 270 ? ? -99.74  -114.62 
11 1 ALA D 5   ? ? -90.95  -62.79  
12 1 ARG D 127 ? ? 54.41   -133.15 
13 1 ARG E 53  ? ? 57.42   -115.00 
14 1 ASP E 88  ? ? -104.54 -114.24 
15 1 GLN E 192 ? ? 63.20   -60.75  
16 1 GLU E 270 ? ? -99.64  -114.53 
17 1 ALA F 5   ? ? -90.90  -62.88  
18 1 ARG F 127 ? ? 54.57   -133.12 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C1 ? B NAG 1154 ? 'WRONG HAND' . 
2 1 C1 ? D NAG 1154 ? 'WRONG HAND' . 
3 1 C1 ? F NAG 1154 ? 'WRONG HAND' . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 2051 ? 6.77 . 
2 1 O ? F HOH 2030 ? 6.36 . 
3 1 O ? F HOH 2031 ? 6.40 . 
# 
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 GLN 322 ? A GLN 322 
2  1 Y 1 A ARG 323 ? A ARG 323 
3  1 Y 1 A GLU 324 ? A GLU 324 
4  1 Y 1 A THR 325 ? A THR 325 
5  1 Y 1 A ARG 326 ? A ARG 326 
6  1 Y 1 B GLU 164 ? B GLU 164 
7  1 Y 1 B GLU 165 ? B GLU 165 
8  1 Y 1 B ALA 166 ? B ALA 166 
9  1 Y 1 C GLN 322 ? C GLN 322 
10 1 Y 1 C ARG 323 ? C ARG 323 
11 1 Y 1 C GLU 324 ? C GLU 324 
12 1 Y 1 C THR 325 ? C THR 325 
13 1 Y 1 C ARG 326 ? C ARG 326 
14 1 Y 1 D GLU 164 ? D GLU 164 
15 1 Y 1 D GLU 165 ? D GLU 165 
16 1 Y 1 D ALA 166 ? D ALA 166 
17 1 Y 1 E GLN 322 ? E GLN 322 
18 1 Y 1 E ARG 323 ? E ARG 323 
19 1 Y 1 E GLU 324 ? E GLU 324 
20 1 Y 1 E THR 325 ? E THR 325 
21 1 Y 1 E ARG 326 ? E ARG 326 
22 1 Y 1 F GLU 164 ? F GLU 164 
23 1 Y 1 F GLU 165 ? F GLU 165 
24 1 Y 1 F ALA 166 ? F ALA 166 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE                                   NAG 
4 'O-SIALIC ACID'                                          SIA 
5 'ALPHA D-GALACTOSE'                                      GLA 
6 '2-(acetylamino)-2-deoxy-6-O-sulfo-beta-D-glucopyranose' NGS 
7 ALPHA-L-FUCOSE                                           FUC 
8 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'    EPE 
9 water                                                    HOH 
# 
