data_3ZNM
# 
_entry.id   3ZNM 
# 
_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   3ZNM         
PDBE  EBI-55837    
WWPDB D_1290055837 
# 
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 3ZNL unspecified 'H5 HAEMAGGLUTININ IN COMPLEX WITH 6-O-SULFO-SIALYL- LEWIS X (SULFATED LEWIS X)'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3ZNM 
_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           3ZNM 
_cell.length_a           175.560 
_cell.length_b           101.360 
_cell.length_c           161.200 
_cell.angle_alpha        90.00 
_cell.angle_beta         111.29 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         3ZNM 
_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 17-342'  ? 
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   12  ? ? ? ? 
4 non-polymer man 'O-SIALIC ACID'                                       309.270   3   ? ? ? ? 
5 non-polymer man 'ALPHA D-GALACTOSE'                                   180.156   3   ? ? ? ? 
6 non-polymer man ALPHA-L-FUCOSE                                        164.156   3   ? ? ? ? 
7 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   3   ? ? ? ? 
8 water       nat water                                                 18.015    303 ? ? ? ? 
# 
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 ? ? 'VIETNAM/1194/2004 (H5N1)' ? ? ? ? 'VN/1194/04/NIBRG14 VACCINE STRAIN' ? ? ? ? ? ? 
? ? 'THE NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL (NIBSC)' 
2 1 sample ? ? ? 'INFLUENZA A VIRUS' 644788 ? ? 'VIETNAM/1194/2004 (H5N1)' ? ? ? ? '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 3ZNM A 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
2 2 3ZNM B 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 
3 1 3ZNM C 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
4 2 3ZNM D 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 
5 1 3ZNM E 1 ? 326 ? Q6DQ34 17  ? 342 ? 1 326 
6 2 3ZNM 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 3ZNM THR A 325 ? UNP Q6DQ34 ARG 341 conflict 325 1 
3 3ZNM THR C 325 ? UNP Q6DQ34 ARG 341 conflict 325 2 
5 3ZNM 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 
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          3ZNM 
_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                     3ZNM 
_reflns.observed_criterion_sigma_I   3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             150.76 
_reflns.d_resolution_high            2.40 
_reflns.number_obs                   77719 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         75.6 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.20 
_reflns.B_iso_Wilson_estimate        53.2 
_reflns.pdbx_redundancy              3.3 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3ZNM 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     73837 
_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                             37.15 
_refine.ls_d_res_high                            2.40 
_refine.ls_percent_reflns_obs                    75.64 
_refine.ls_R_factor_obs                          0.23870 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23777 
_refine.ls_R_factor_R_free                       0.25632 
_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                  3882 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.891 
_refine.B_iso_mean                               47.100 
_refine.aniso_B[1][1]                            -0.11 
_refine.aniso_B[2][2]                            -0.65 
_refine.aniso_B[3][3]                            0.52 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.21 
_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. U VALUES WITH TLS ADDED. 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                       0.447 
_refine.pdbx_overall_ESU_R_Free                  0.280 
_refine.overall_SU_ML                            0.212 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             18.031 
_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         339 
_refine_hist.number_atoms_solvent             303 
_refine_hist.number_atoms_total               12237 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        37.15 
# 
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  ? 12237 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 11232 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          0.997  1.970  ? 16614 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.720  3.003  ? 25851 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.225  5.000  ? 1446  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.912 25.174 ? 603   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.569 15.000 ? 2034  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.025 15.000 ? 51    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.055  0.200  ? 1809  '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                  0.154  0.551  ? 5802  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.154  0.551  ? 5801  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.287  0.826  ? 7242  'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.594  0.819  ? 6435  '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                       2.403 
_refine_ls_shell.d_res_low                        2.466 
_refine_ls_shell.number_reflns_R_work             361 
_refine_ls_shell.R_factor_R_work                  0.382 
_refine_ls_shell.percent_reflns_obs               4.98 
_refine_ls_shell.R_factor_R_free                  0.546 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             18 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  3ZNM 
_struct.title                     'H5 Haemagglutinin in Complex with Sialyl-Lewis X' 
_struct.pdbx_descriptor           HAEMAGGLUTININ 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3ZNM 
_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, 3SLN, 3'SLN, SULFATED LEWIS X
;
# 
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 3 ? 
L  N N 6 ? 
M  N N 3 ? 
N  N N 7 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 3 ? 
T  N N 6 ? 
U  N N 3 ? 
V  N N 7 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA N N 3 ? 
BA N N 6 ? 
CA N N 3 ? 
DA N N 7 ? 
EA N N 8 ? 
FA N N 8 ? 
GA N N 8 ? 
HA N N 8 ? 
IA N N 8 ? 
JA N N 8 ? 
# 
_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  ? SER A 106 ? ASP A 97  SER A 106 1 ? 10 
HELX_P HELX_P4  4  ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 
HELX_P HELX_P5  5  ASP B 37  ? THR B 61  ? ASP B 37  THR B 61  1 ? 25 
HELX_P HELX_P6  6  GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P7  7  ASP B 145 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 
HELX_P HELX_P8  8  ASP B 158 ? SER B 163 ? ASP B 158 SER B 163 1 ? 6  
HELX_P HELX_P9  9  SER C 56  ? GLY C 63  ? SER C 56  GLY C 63  1 ? 8  
HELX_P HELX_P10 10 ASN C 64  ? ILE C 71  ? ASN C 64  ILE C 71  5 ? 8  
HELX_P HELX_P11 11 ASP C 97  ? SER C 106 ? ASP C 97  SER C 106 1 ? 10 
HELX_P HELX_P12 12 ASP C 183 ? GLN C 192 ? ASP C 183 GLN C 192 1 ? 10 
HELX_P HELX_P13 13 ASP D 37  ? THR D 61  ? ASP D 37  THR D 61  1 ? 25 
HELX_P HELX_P14 14 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P15 15 ASP D 145 ? GLY D 155 ? ASP D 145 GLY D 155 1 ? 11 
HELX_P HELX_P16 16 ASP D 158 ? SER D 163 ? ASP D 158 SER D 163 1 ? 6  
HELX_P HELX_P17 17 SER E 56  ? GLY E 63  ? SER E 56  GLY E 63  1 ? 8  
HELX_P HELX_P18 18 ASN E 64  ? ILE E 71  ? ASN E 64  ILE E 71  5 ? 8  
HELX_P HELX_P19 19 ASP E 97  ? SER E 106 ? ASP E 97  SER E 106 1 ? 10 
HELX_P HELX_P20 20 ASP E 183 ? GLN E 192 ? ASP E 183 GLN E 192 1 ? 10 
HELX_P HELX_P21 21 ASP F 37  ? THR F 61  ? ASP F 37  THR F 61  1 ? 25 
HELX_P HELX_P22 22 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P23 23 ASP F 145 ? GLY F 155 ? ASP F 145 GLY F 155 1 ? 11 
HELX_P HELX_P24 24 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 ? ? ? ? ? ? ? 2.060 ? 
disulf2  disulf ? ? A  CYS 42  SG  ? ? ? 1_555 A  CYS 274 SG ? ? A CYS 42   A CYS 274  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf3  disulf ? ? A  CYS 55  SG  ? ? ? 1_555 A  CYS 67  SG ? ? A CYS 55   A CYS 67   1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf4  disulf ? ? A  CYS 90  SG  ? ? ? 1_555 A  CYS 135 SG ? ? A CYS 90   A CYS 135  1_555 ? ? ? ? ? ? ? 2.051 ? 
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 ? ? ? ? ? ? ? 2.036 ? 
disulf7  disulf ? ? C  CYS 4   SG  ? ? ? 1_555 D  CYS 137 SG ? ? C CYS 4    D CYS 137  1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf8  disulf ? ? C  CYS 42  SG  ? ? ? 1_555 C  CYS 274 SG ? ? C CYS 42   C CYS 274  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf9  disulf ? ? C  CYS 55  SG  ? ? ? 1_555 C  CYS 67  SG ? ? C CYS 55   C CYS 67   1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf10 disulf ? ? C  CYS 90  SG  ? ? ? 1_555 C  CYS 135 SG ? ? C CYS 90   C CYS 135  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf11 disulf ? ? C  CYS 278 SG  ? ? ? 1_555 C  CYS 302 SG ? ? C CYS 278  C CYS 302  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf12 disulf ? ? D  CYS 144 SG  ? ? ? 1_555 D  CYS 148 SG ? ? D CYS 144  D CYS 148  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf13 disulf ? ? E  CYS 4   SG  ? ? ? 1_555 F  CYS 137 SG ? ? E CYS 4    F CYS 137  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf14 disulf ? ? E  CYS 42  SG  ? ? ? 1_555 E  CYS 274 SG ? ? E CYS 42   E CYS 274  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf15 disulf ? ? E  CYS 55  SG  ? ? ? 1_555 E  CYS 67  SG ? ? E CYS 55   E CYS 67   1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf16 disulf ? ? E  CYS 90  SG  ? ? ? 1_555 E  CYS 135 SG ? ? E CYS 90   E CYS 135  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf17 disulf ? ? E  CYS 278 SG  ? ? ? 1_555 E  CYS 302 SG ? ? E CYS 278  E CYS 302  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf18 disulf ? ? F  CYS 144 SG  ? ? ? 1_555 F  CYS 148 SG ? ? F CYS 144  F CYS 148  1_555 ? ? ? ? ? ? ? 2.036 ? 
covale1  covale ? ? A  ASN 23  ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 23   A NAG 1322 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale2  covale ? ? A  ASN 165 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? A ASN 165  A NAG 1323 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale3  covale ? ? I  SIA .   C2  ? ? ? 1_555 J  GLA .   O3 ? ? A SIA 1324 A GLA 1325 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale4  covale ? ? J  GLA .   C1  ? ? ? 1_555 K  NAG .   O4 ? ? A GLA 1325 A NAG 1326 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale5  covale ? ? K  NAG .   O3  ? ? ? 1_555 L  FUC .   C1 ? ? A NAG 1326 A FUC 1327 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale6  covale ? ? B  ASN 154 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? B ASN 154  B NAG 1164 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale7  covale ? ? C  ASN 23  ND2 ? ? ? 1_555 O  NAG .   C1 ? ? C ASN 23   C NAG 1322 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale8  covale ? ? C  ASN 165 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? C ASN 165  C NAG 1323 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale9  covale ? ? Q  SIA .   C2  ? ? ? 1_555 R  GLA .   O3 ? ? C SIA 1324 C GLA 1325 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale10 covale ? ? R  GLA .   C1  ? ? ? 1_555 S  NAG .   O4 ? ? C GLA 1325 C NAG 1326 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale11 covale ? ? S  NAG .   O3  ? ? ? 1_555 T  FUC .   C1 ? ? C NAG 1326 C FUC 1327 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale12 covale ? ? D  ASN 154 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? D ASN 154  D NAG 1164 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale13 covale ? ? E  ASN 23  ND2 ? ? ? 1_555 W  NAG .   C1 ? ? E ASN 23   E NAG 1322 1_555 ? ? ? ? ? ? ? 1.460 ? 
covale14 covale ? ? E  ASN 165 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? E ASN 165  E NAG 1323 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale15 covale ? ? Y  SIA .   C2  ? ? ? 1_555 Z  GLA .   O3 ? ? E SIA 1324 E GLA 1325 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale16 covale ? ? Z  GLA .   C1  ? ? ? 1_555 AA NAG .   O4 ? ? E GLA 1325 E NAG 1326 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale17 covale ? ? AA NAG .   O3  ? ? ? 1_555 BA FUC .   C1 ? ? E NAG 1326 E FUC 1327 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale18 covale ? ? F  ASN 154 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? F ASN 154  F NAG 1164 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 1165'                           
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE EPE B 1165'                           
AC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE EPE D 1165'                           
AC4 Software ? ? ? ? 12 'BINDING SITE FOR LINKED RESIDUES A 1324 A 1325 A 1326 A 1327'  
AC5 Software ? ? ? ? 12 'BINDING SITE FOR LINKED RESIDUES C 1324 C 1325 C 1326 C 1327'  
AC6 Software ? ? ? ? 12 'BINDING SITE FOR LINKED RESIDUES E 1324 E 1325 E 1326 E 1327'  
AC7 Software ? ? ? ? 1  'Binding site for Mono-Saccharide NAG A1322 bound to ASN A 23'  
AC8 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG A1323 bound to ASN A 165' 
AC9 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG B1164 bound to ASN B 154' 
BC1 Software ? ? ? ? 1  'Binding site for Mono-Saccharide NAG C1322 bound to ASN C 23'  
BC2 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG C1323 bound to ASN C 165' 
BC3 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG D1164 bound to ASN D 154' 
BC4 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG E1322 bound to ASN E 23'  
BC5 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG E1323 bound to ASN E 165' 
BC6 Software ? ? ? ? 3  'Binding site for Mono-Saccharide NAG F1164 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  CYS A  4   ? CYS A 4    . ? 1_555 ? 
6  AC2 4  TRP B  14  ? TRP B 14   . ? 1_555 ? 
7  AC2 4  HIS B  25  ? HIS B 25   . ? 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 12 TYR A  91  ? TYR A 91   . ? 1_555 ? 
13 AC4 12 LEU A  129 ? LEU A 129  . ? 1_555 ? 
14 AC4 12 VAL A  131 ? VAL A 131  . ? 1_555 ? 
15 AC4 12 SER A  132 ? SER A 132  . ? 1_555 ? 
16 AC4 12 SER A  133 ? SER A 133  . ? 1_555 ? 
17 AC4 12 HIS A  179 ? HIS A 179  . ? 1_555 ? 
18 AC4 12 ASN A  182 ? ASN A 182  . ? 1_555 ? 
19 AC4 12 GLU A  186 ? GLU A 186  . ? 1_555 ? 
20 AC4 12 LEU A  190 ? LEU A 190  . ? 1_555 ? 
21 AC4 12 LYS A  218 ? LYS A 218  . ? 1_555 ? 
22 AC4 12 GLN A  222 ? GLN A 222  . ? 1_555 ? 
23 AC4 12 HOH EA .   ? HOH A 2030 . ? 1_555 ? 
24 AC5 12 TYR C  91  ? TYR C 91   . ? 1_555 ? 
25 AC5 12 LEU C  129 ? LEU C 129  . ? 1_555 ? 
26 AC5 12 VAL C  131 ? VAL C 131  . ? 1_555 ? 
27 AC5 12 SER C  132 ? SER C 132  . ? 1_555 ? 
28 AC5 12 SER C  133 ? SER C 133  . ? 1_555 ? 
29 AC5 12 HIS C  179 ? HIS C 179  . ? 1_555 ? 
30 AC5 12 ASN C  182 ? ASN C 182  . ? 1_555 ? 
31 AC5 12 GLU C  186 ? GLU C 186  . ? 1_555 ? 
32 AC5 12 LEU C  190 ? LEU C 190  . ? 1_555 ? 
33 AC5 12 LYS C  218 ? LYS C 218  . ? 1_555 ? 
34 AC5 12 GLN C  222 ? GLN C 222  . ? 1_555 ? 
35 AC5 12 HOH GA .   ? HOH C 2028 . ? 1_555 ? 
36 AC6 12 TYR E  91  ? TYR E 91   . ? 1_555 ? 
37 AC6 12 LEU E  129 ? LEU E 129  . ? 1_555 ? 
38 AC6 12 VAL E  131 ? VAL E 131  . ? 1_555 ? 
39 AC6 12 SER E  132 ? SER E 132  . ? 1_555 ? 
40 AC6 12 SER E  133 ? SER E 133  . ? 1_555 ? 
41 AC6 12 HIS E  179 ? HIS E 179  . ? 1_555 ? 
42 AC6 12 ASN E  182 ? ASN E 182  . ? 1_555 ? 
43 AC6 12 GLU E  186 ? GLU E 186  . ? 1_555 ? 
44 AC6 12 LEU E  190 ? LEU E 190  . ? 1_555 ? 
45 AC6 12 LYS E  218 ? LYS E 218  . ? 1_555 ? 
46 AC6 12 GLN E  222 ? GLN E 222  . ? 1_555 ? 
47 AC6 12 HOH IA .   ? HOH E 2028 . ? 1_555 ? 
48 AC7 1  ASN A  23  ? ASN A 23   . ? 1_555 ? 
49 AC8 2  ASN A  165 ? ASN A 165  . ? 1_555 ? 
50 AC8 2  ASN A  236 ? ASN A 236  . ? 1_555 ? 
51 AC9 3  GLU B  147 ? GLU B 147  . ? 1_555 ? 
52 AC9 3  GLU B  150 ? GLU B 150  . ? 1_555 ? 
53 AC9 3  ASN B  154 ? ASN B 154  . ? 1_555 ? 
54 BC1 1  ASN C  23  ? ASN C 23   . ? 1_555 ? 
55 BC2 2  ASN C  165 ? ASN C 165  . ? 1_555 ? 
56 BC2 2  ASN C  236 ? ASN C 236  . ? 1_555 ? 
57 BC3 3  GLU D  147 ? GLU D 147  . ? 1_555 ? 
58 BC3 3  GLU D  150 ? GLU D 150  . ? 1_555 ? 
59 BC3 3  ASN D  154 ? ASN D 154  . ? 1_555 ? 
60 BC4 2  LYS E  22  ? LYS E 22   . ? 1_555 ? 
61 BC4 2  ASN E  23  ? ASN E 23   . ? 1_555 ? 
62 BC5 2  ASN E  165 ? ASN E 165  . ? 1_555 ? 
63 BC5 2  ASN E  236 ? ASN E 236  . ? 1_555 ? 
64 BC6 3  GLU F  147 ? GLU F 147  . ? 1_555 ? 
65 BC6 3  GLU F  150 ? GLU F 150  . ? 1_555 ? 
66 BC6 3  ASN F  154 ? ASN F 154  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3ZNM 
_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                    3ZNM 
_atom_sites.fract_transf_matrix[1][1]   0.005696 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002220 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009866 
_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]   0.006658 
_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   ? 34.452  32.809 -8.486  1.00 34.33  ? 1    ASP A N   1 
ATOM   2     C CA  . ASP A  1 1   ? 35.393  32.821 -7.328  1.00 35.04  ? 1    ASP A CA  1 
ATOM   3     C C   . ASP A  1 1   ? 34.996  33.900 -6.323  1.00 32.83  ? 1    ASP A C   1 
ATOM   4     O O   . ASP A  1 1   ? 34.560  34.982 -6.711  1.00 31.19  ? 1    ASP A O   1 
ATOM   5     C CB  . ASP A  1 1   ? 36.833  33.039 -7.805  1.00 36.90  ? 1    ASP A CB  1 
ATOM   6     C CG  . ASP A  1 1   ? 37.279  31.995 -8.818  1.00 39.40  ? 1    ASP A CG  1 
ATOM   7     O OD1 . ASP A  1 1   ? 36.461  31.126 -9.190  1.00 39.62  ? 1    ASP A OD1 1 
ATOM   8     O OD2 . ASP A  1 1   ? 38.451  32.045 -9.249  1.00 41.44  ? 1    ASP A OD2 1 
ATOM   9     N N   . GLN A  1 2   ? 35.140  33.592 -5.034  1.00 32.95  ? 2    GLN A N   1 
ATOM   10    C CA  . GLN A  1 2   ? 34.758  34.523 -3.973  1.00 31.09  ? 2    GLN A CA  1 
ATOM   11    C C   . GLN A  1 2   ? 35.618  34.404 -2.722  1.00 31.85  ? 2    GLN A C   1 
ATOM   12    O O   . GLN A  1 2   ? 36.173  33.345 -2.433  1.00 33.68  ? 2    GLN A O   1 
ATOM   13    C CB  . GLN A  1 2   ? 33.287  34.323 -3.587  1.00 29.66  ? 2    GLN A CB  1 
ATOM   14    C CG  . GLN A  1 2   ? 32.960  32.942 -3.039  1.00 30.88  ? 2    GLN A CG  1 
ATOM   15    C CD  . GLN A  1 2   ? 31.572  32.862 -2.432  1.00 29.66  ? 2    GLN A CD  1 
ATOM   16    O OE1 . GLN A  1 2   ? 31.367  32.182 -1.426  1.00 30.18  ? 2    GLN A OE1 1 
ATOM   17    N NE2 . GLN A  1 2   ? 30.611  33.554 -3.037  1.00 28.25  ? 2    GLN A NE2 1 
ATOM   18    N N   . ILE A  1 3   ? 35.712  35.508 -1.988  1.00 30.59  ? 3    ILE A N   1 
ATOM   19    C CA  . ILE A  1 3   ? 36.310  35.515 -0.659  1.00 30.96  ? 3    ILE A CA  1 
ATOM   20    C C   . ILE A  1 3   ? 35.283  36.048 0.339   1.00 28.96  ? 3    ILE A C   1 
ATOM   21    O O   . ILE A  1 3   ? 34.580  37.013 0.055   1.00 27.42  ? 3    ILE A O   1 
ATOM   22    C CB  . ILE A  1 3   ? 37.619  36.339 -0.612  1.00 31.98  ? 3    ILE A CB  1 
ATOM   23    C CG1 . ILE A  1 3   ? 38.352  36.097 0.715   1.00 32.89  ? 3    ILE A CG1 1 
ATOM   24    C CG2 . ILE A  1 3   ? 37.355  37.825 -0.817  1.00 30.49  ? 3    ILE A CG2 1 
ATOM   25    C CD1 . ILE A  1 3   ? 39.829  36.412 0.659   1.00 34.98  ? 3    ILE A CD1 1 
ATOM   26    N N   . CYS A  1 4   ? 35.186  35.394 1.493   1.00 29.23  ? 4    CYS A N   1 
ATOM   27    C CA  . CYS A  1 4   ? 34.201  35.753 2.508   1.00 27.66  ? 4    CYS A CA  1 
ATOM   28    C C   . CYS A  1 4   ? 34.887  36.156 3.792   1.00 27.62  ? 4    CYS A C   1 
ATOM   29    O O   . CYS A  1 4   ? 35.992  35.705 4.072   1.00 29.19  ? 4    CYS A O   1 
ATOM   30    C CB  . CYS A  1 4   ? 33.265  34.579 2.789   1.00 28.03  ? 4    CYS A CB  1 
ATOM   31    S SG  . CYS A  1 4   ? 32.449  33.912 1.323   1.00 28.55  ? 4    CYS A SG  1 
ATOM   32    N N   . ILE A  1 5   ? 34.227  37.012 4.564   1.00 25.97  ? 5    ILE A N   1 
ATOM   33    C CA  . ILE A  1 5   ? 34.676  37.332 5.906   1.00 25.85  ? 5    ILE A CA  1 
ATOM   34    C C   . ILE A  1 5   ? 33.708  36.671 6.872   1.00 25.24  ? 5    ILE A C   1 
ATOM   35    O O   . ILE A  1 5   ? 32.495  36.700 6.667   1.00 24.26  ? 5    ILE A O   1 
ATOM   36    C CB  . ILE A  1 5   ? 34.725  38.849 6.146   1.00 24.90  ? 5    ILE A CB  1 
ATOM   37    C CG1 . ILE A  1 5   ? 35.569  39.530 5.068   1.00 25.61  ? 5    ILE A CG1 1 
ATOM   38    C CG2 . ILE A  1 5   ? 35.270  39.166 7.534   1.00 25.09  ? 5    ILE A CG2 1 
ATOM   39    C CD1 . ILE A  1 5   ? 37.048  39.257 5.177   1.00 27.50  ? 5    ILE A CD1 1 
ATOM   40    N N   . GLY A  1 6   ? 34.254  36.058 7.915   1.00 26.03  ? 6    GLY A N   1 
ATOM   41    C CA  . GLY A  1 6   ? 33.448  35.322 8.878   1.00 25.82  ? 6    GLY A CA  1 
ATOM   42    C C   . GLY A  1 6   ? 34.132  35.177 10.213  1.00 26.32  ? 6    GLY A C   1 
ATOM   43    O O   . GLY A  1 6   ? 35.250  35.651 10.410  1.00 26.91  ? 6    GLY A O   1 
ATOM   44    N N   . TYR A  1 7   ? 33.454  34.503 11.128  1.00 26.29  ? 7    TYR A N   1 
ATOM   45    C CA  . TYR A  1 7   ? 33.903  34.423 12.509  1.00 26.59  ? 7    TYR A CA  1 
ATOM   46    C C   . TYR A  1 7   ? 33.768  33.010 13.057  1.00 27.97  ? 7    TYR A C   1 
ATOM   47    O O   . TYR A  1 7   ? 33.050  32.181 12.509  1.00 28.45  ? 7    TYR A O   1 
ATOM   48    C CB  . TYR A  1 7   ? 33.135  35.432 13.383  1.00 24.98  ? 7    TYR A CB  1 
ATOM   49    C CG  . TYR A  1 7   ? 31.625  35.312 13.319  1.00 24.12  ? 7    TYR A CG  1 
ATOM   50    C CD1 . TYR A  1 7   ? 30.896  35.927 12.310  1.00 23.25  ? 7    TYR A CD1 1 
ATOM   51    C CD2 . TYR A  1 7   ? 30.930  34.592 14.276  1.00 24.43  ? 7    TYR A CD2 1 
ATOM   52    C CE1 . TYR A  1 7   ? 29.517  35.817 12.251  1.00 22.81  ? 7    TYR A CE1 1 
ATOM   53    C CE2 . TYR A  1 7   ? 29.552  34.475 14.224  1.00 24.05  ? 7    TYR A CE2 1 
ATOM   54    C CZ  . TYR A  1 7   ? 28.853  35.088 13.212  1.00 23.29  ? 7    TYR A CZ  1 
ATOM   55    O OH  . TYR A  1 7   ? 27.484  34.957 13.168  1.00 23.25  ? 7    TYR A OH  1 
ATOM   56    N N   . HIS A  1 8   ? 34.477  32.765 14.151  1.00 28.81  ? 8    HIS A N   1 
ATOM   57    C CA  . HIS A  1 8   ? 34.577  31.451 14.780  1.00 30.51  ? 8    HIS A CA  1 
ATOM   58    C C   . HIS A  1 8   ? 33.250  30.983 15.369  1.00 30.16  ? 8    HIS A C   1 
ATOM   59    O O   . HIS A  1 8   ? 32.506  31.770 15.943  1.00 28.63  ? 8    HIS A O   1 
ATOM   60    C CB  . HIS A  1 8   ? 35.628  31.527 15.893  1.00 31.23  ? 8    HIS A CB  1 
ATOM   61    C CG  . HIS A  1 8   ? 35.920  30.218 16.558  1.00 33.22  ? 8    HIS A CG  1 
ATOM   62    N ND1 . HIS A  1 8   ? 36.530  29.170 15.904  1.00 35.47  ? 8    HIS A ND1 1 
ATOM   63    C CD2 . HIS A  1 8   ? 35.717  29.800 17.830  1.00 33.51  ? 8    HIS A CD2 1 
ATOM   64    C CE1 . HIS A  1 8   ? 36.675  28.156 16.738  1.00 37.14  ? 8    HIS A CE1 1 
ATOM   65    N NE2 . HIS A  1 8   ? 36.189  28.512 17.914  1.00 35.93  ? 8    HIS A NE2 1 
ATOM   66    N N   . ALA A  1 9   ? 32.959  29.696 15.208  1.00 31.92  ? 9    ALA A N   1 
ATOM   67    C CA  . ALA A  1 9   ? 31.909  29.031 15.979  1.00 32.38  ? 9    ALA A CA  1 
ATOM   68    C C   . ALA A  1 9   ? 32.500  27.753 16.550  1.00 34.87  ? 9    ALA A C   1 
ATOM   69    O O   . ALA A  1 9   ? 33.587  27.346 16.151  1.00 36.32  ? 9    ALA A O   1 
ATOM   70    C CB  . ALA A  1 9   ? 30.704  28.729 15.110  1.00 32.37  ? 9    ALA A CB  1 
ATOM   71    N N   . ASN A  1 10  ? 31.806  27.137 17.499  1.00 35.68  ? 10   ASN A N   1 
ATOM   72    C CA  . ASN A  1 10  ? 32.260  25.871 18.078  1.00 38.36  ? 10   ASN A CA  1 
ATOM   73    C C   . ASN A  1 10  ? 31.135  25.140 18.812  1.00 39.44  ? 10   ASN A C   1 
ATOM   74    O O   . ASN A  1 10  ? 29.981  25.559 18.746  1.00 38.32  ? 10   ASN A O   1 
ATOM   75    C CB  . ASN A  1 10  ? 33.488  26.088 18.984  1.00 38.57  ? 10   ASN A CB  1 
ATOM   76    C CG  . ASN A  1 10  ? 33.173  26.875 20.243  1.00 36.85  ? 10   ASN A CG  1 
ATOM   77    O OD1 . ASN A  1 10  ? 32.015  27.137 20.568  1.00 35.78  ? 10   ASN A OD1 1 
ATOM   78    N ND2 . ASN A  1 10  ? 34.215  27.254 20.962  1.00 36.81  ? 10   ASN A ND2 1 
ATOM   79    N N   . ASN A  1 11  ? 31.477  24.056 19.506  1.00 42.02  ? 11   ASN A N   1 
ATOM   80    C CA  . ASN A  1 11  ? 30.490  23.219 20.200  1.00 43.66  ? 11   ASN A CA  1 
ATOM   81    C C   . ASN A  1 11  ? 30.214  23.641 21.654  1.00 42.69  ? 11   ASN A C   1 
ATOM   82    O O   . ASN A  1 11  ? 29.566  22.905 22.402  1.00 44.18  ? 11   ASN A O   1 
ATOM   83    C CB  . ASN A  1 11  ? 30.912  21.735 20.130  1.00 47.31  ? 11   ASN A CB  1 
ATOM   84    C CG  . ASN A  1 11  ? 32.224  21.450 20.853  1.00 48.49  ? 11   ASN A CG  1 
ATOM   85    O OD1 . ASN A  1 11  ? 32.760  22.308 21.562  1.00 46.73  ? 11   ASN A OD1 1 
ATOM   86    N ND2 . ASN A  1 11  ? 32.748  20.233 20.676  1.00 51.77  ? 11   ASN A ND2 1 
ATOM   87    N N   . SER A  1 12  ? 30.697  24.822 22.042  1.00 40.40  ? 12   SER A N   1 
ATOM   88    C CA  . SER A  1 12  ? 30.521  25.343 23.400  1.00 39.39  ? 12   SER A CA  1 
ATOM   89    C C   . SER A  1 12  ? 29.056  25.629 23.712  1.00 38.72  ? 12   SER A C   1 
ATOM   90    O O   . SER A  1 12  ? 28.315  26.110 22.854  1.00 37.82  ? 12   SER A O   1 
ATOM   91    C CB  . SER A  1 12  ? 31.338  26.627 23.593  1.00 37.20  ? 12   SER A CB  1 
ATOM   92    O OG  . SER A  1 12  ? 31.152  27.179 24.886  1.00 36.21  ? 12   SER A OG  1 
ATOM   93    N N   . THR A  1 13  ? 28.654  25.318 24.945  1.00 39.47  ? 13   THR A N   1 
ATOM   94    C CA  . THR A  1 13  ? 27.316  25.628 25.449  1.00 39.09  ? 13   THR A CA  1 
ATOM   95    C C   . THR A  1 13  ? 27.359  26.630 26.604  1.00 37.43  ? 13   THR A C   1 
ATOM   96    O O   . THR A  1 13  ? 26.330  26.906 27.219  1.00 37.33  ? 13   THR A O   1 
ATOM   97    C CB  . THR A  1 13  ? 26.586  24.354 25.931  1.00 41.81  ? 13   THR A CB  1 
ATOM   98    O OG1 . THR A  1 13  ? 27.425  23.632 26.844  1.00 43.23  ? 13   THR A OG1 1 
ATOM   99    C CG2 . THR A  1 13  ? 26.220  23.462 24.751  1.00 43.65  ? 13   THR A CG2 1 
ATOM   100   N N   . GLU A  1 14  ? 28.538  27.174 26.898  1.00 36.43  ? 14   GLU A N   1 
ATOM   101   C CA  . GLU A  1 14  ? 28.672  28.176 27.956  1.00 34.94  ? 14   GLU A CA  1 
ATOM   102   C C   . GLU A  1 14  ? 27.875  29.435 27.630  1.00 32.97  ? 14   GLU A C   1 
ATOM   103   O O   . GLU A  1 14  ? 27.926  29.933 26.510  1.00 32.11  ? 14   GLU A O   1 
ATOM   104   C CB  . GLU A  1 14  ? 30.137  28.547 28.178  1.00 34.55  ? 14   GLU A CB  1 
ATOM   105   C CG  . GLU A  1 14  ? 30.980  27.413 28.747  1.00 36.68  ? 14   GLU A CG  1 
ATOM   106   C CD  . GLU A  1 14  ? 31.838  27.851 29.924  1.00 36.44  ? 14   GLU A CD  1 
ATOM   107   O OE1 . GLU A  1 14  ? 31.265  28.343 30.931  1.00 35.70  ? 14   GLU A OE1 1 
ATOM   108   O OE2 . GLU A  1 14  ? 33.084  27.711 29.841  1.00 37.23  ? 14   GLU A OE2 1 
ATOM   109   N N   . GLN A  1 15  ? 27.142  29.936 28.619  1.00 32.48  ? 15   GLN A N   1 
ATOM   110   C CA  . GLN A  1 15  ? 26.290  31.103 28.450  1.00 31.08  ? 15   GLN A CA  1 
ATOM   111   C C   . GLN A  1 15  ? 26.725  32.224 29.380  1.00 29.67  ? 15   GLN A C   1 
ATOM   112   O O   . GLN A  1 15  ? 27.282  31.974 30.448  1.00 29.98  ? 15   GLN A O   1 
ATOM   113   C CB  . GLN A  1 15  ? 24.840  30.745 28.749  1.00 32.28  ? 15   GLN A CB  1 
ATOM   114   C CG  . GLN A  1 15  ? 24.331  29.530 27.995  1.00 34.14  ? 15   GLN A CG  1 
ATOM   115   C CD  . GLN A  1 15  ? 22.862  29.257 28.248  1.00 35.60  ? 15   GLN A CD  1 
ATOM   116   O OE1 . GLN A  1 15  ? 22.106  28.968 27.323  1.00 36.47  ? 15   GLN A OE1 1 
ATOM   117   N NE2 . GLN A  1 15  ? 22.451  29.344 29.507  1.00 36.14  ? 15   GLN A NE2 1 
ATOM   118   N N   . VAL A  1 16  ? 26.464  33.459 28.967  1.00 28.24  ? 16   VAL A N   1 
ATOM   119   C CA  . VAL A  1 16  ? 26.719  34.626 29.803  1.00 27.21  ? 16   VAL A CA  1 
ATOM   120   C C   . VAL A  1 16  ? 25.506  35.532 29.765  1.00 26.91  ? 16   VAL A C   1 
ATOM   121   O O   . VAL A  1 16  ? 24.722  35.476 28.821  1.00 27.08  ? 16   VAL A O   1 
ATOM   122   C CB  . VAL A  1 16  ? 27.963  35.415 29.345  1.00 26.16  ? 16   VAL A CB  1 
ATOM   123   C CG1 . VAL A  1 16  ? 29.189  34.518 29.350  1.00 26.78  ? 16   VAL A CG1 1 
ATOM   124   C CG2 . VAL A  1 16  ? 27.750  36.033 27.969  1.00 25.45  ? 16   VAL A CG2 1 
ATOM   125   N N   . ASP A  1 17  ? 25.352  36.358 30.796  1.00 26.68  ? 17   ASP A N   1 
ATOM   126   C CA  . ASP A  1 17  ? 24.288  37.354 30.834  1.00 26.66  ? 17   ASP A CA  1 
ATOM   127   C C   . ASP A  1 17  ? 24.823  38.727 30.449  1.00 25.61  ? 17   ASP A C   1 
ATOM   128   O O   . ASP A  1 17  ? 25.999  39.035 30.656  1.00 24.97  ? 17   ASP A O   1 
ATOM   129   C CB  . ASP A  1 17  ? 23.663  37.428 32.227  1.00 27.48  ? 17   ASP A CB  1 
ATOM   130   C CG  . ASP A  1 17  ? 22.857  36.191 32.581  1.00 28.93  ? 17   ASP A CG  1 
ATOM   131   O OD1 . ASP A  1 17  ? 22.249  35.575 31.681  1.00 29.60  ? 17   ASP A OD1 1 
ATOM   132   O OD2 . ASP A  1 17  ? 22.819  35.843 33.781  1.00 29.64  ? 17   ASP A OD2 1 
ATOM   133   N N   . THR A  1 18  ? 23.937  39.528 29.863  1.00 25.71  ? 18   THR A N   1 
ATOM   134   C CA  . THR A  1 18  ? 24.177  40.940 29.583  1.00 25.22  ? 18   THR A CA  1 
ATOM   135   C C   . THR A  1 18  ? 22.962  41.708 30.084  1.00 26.24  ? 18   THR A C   1 
ATOM   136   O O   . THR A  1 18  ? 22.015  41.111 30.588  1.00 27.24  ? 18   THR A O   1 
ATOM   137   C CB  . THR A  1 18  ? 24.363  41.206 28.072  1.00 24.56  ? 18   THR A CB  1 
ATOM   138   O OG1 . THR A  1 18  ? 23.140  40.949 27.377  1.00 25.08  ? 18   THR A OG1 1 
ATOM   139   C CG2 . THR A  1 18  ? 25.457  40.332 27.498  1.00 23.99  ? 18   THR A CG2 1 
ATOM   140   N N   . ILE A  1 19  ? 22.976  43.025 29.939  1.00 26.39  ? 19   ILE A N   1 
ATOM   141   C CA  . ILE A  1 19  ? 21.854  43.850 30.385  1.00 27.71  ? 19   ILE A CA  1 
ATOM   142   C C   . ILE A  1 19  ? 20.585  43.545 29.577  1.00 28.69  ? 19   ILE A C   1 
ATOM   143   O O   . ILE A  1 19  ? 19.503  43.372 30.143  1.00 30.02  ? 19   ILE A O   1 
ATOM   144   C CB  . ILE A  1 19  ? 22.188  45.355 30.264  1.00 27.81  ? 19   ILE A CB  1 
ATOM   145   C CG1 . ILE A  1 19  ? 23.372  45.732 31.169  1.00 27.44  ? 19   ILE A CG1 1 
ATOM   146   C CG2 . ILE A  1 19  ? 20.979  46.214 30.607  1.00 29.37  ? 19   ILE A CG2 1 
ATOM   147   C CD1 . ILE A  1 19  ? 23.053  45.770 32.649  1.00 28.27  ? 19   ILE A CD1 1 
ATOM   148   N N   . MET A  1 20  ? 20.731  43.478 28.257  1.00 28.28  ? 20   MET A N   1 
ATOM   149   C CA  . MET A  1 20  ? 19.588  43.323 27.359  1.00 29.29  ? 20   MET A CA  1 
ATOM   150   C C   . MET A  1 20  ? 19.195  41.880 27.078  1.00 29.90  ? 20   MET A C   1 
ATOM   151   O O   . MET A  1 20  ? 18.100  41.626 26.572  1.00 30.98  ? 20   MET A O   1 
ATOM   152   C CB  . MET A  1 20  ? 19.888  43.987 26.024  1.00 28.50  ? 20   MET A CB  1 
ATOM   153   C CG  . MET A  1 20  ? 20.010  45.490 26.097  1.00 28.75  ? 20   MET A CG  1 
ATOM   154   S SD  . MET A  1 20  ? 20.030  46.168 24.439  1.00 28.35  ? 20   MET A SD  1 
ATOM   155   C CE  . MET A  1 20  ? 20.141  47.908 24.812  1.00 29.28  ? 20   MET A CE  1 
ATOM   156   N N   . GLU A  1 21  ? 20.088  40.941 27.366  1.00 29.61  ? 21   GLU A N   1 
ATOM   157   C CA  . GLU A  1 21  ? 19.834  39.549 27.039  1.00 30.52  ? 21   GLU A CA  1 
ATOM   158   C C   . GLU A  1 21  ? 20.510  38.617 28.032  1.00 31.01  ? 21   GLU A C   1 
ATOM   159   O O   . GLU A  1 21  ? 21.665  38.823 28.417  1.00 30.01  ? 21   GLU A O   1 
ATOM   160   C CB  . GLU A  1 21  ? 20.316  39.250 25.623  1.00 29.67  ? 21   GLU A CB  1 
ATOM   161   C CG  . GLU A  1 21  ? 19.629  38.058 24.978  1.00 30.71  ? 21   GLU A CG  1 
ATOM   162   C CD  . GLU A  1 21  ? 20.107  37.795 23.557  1.00 30.00  ? 21   GLU A CD  1 
ATOM   163   O OE1 . GLU A  1 21  ? 20.771  38.681 22.964  1.00 28.82  ? 21   GLU A OE1 1 
ATOM   164   O OE2 . GLU A  1 21  ? 19.819  36.695 23.031  1.00 30.80  ? 21   GLU A OE2 1 
ATOM   165   N N   . LYS A  1 22  ? 19.775  37.587 28.438  1.00 33.04  ? 22   LYS A N   1 
ATOM   166   C CA  . LYS A  1 22  ? 20.280  36.593 29.368  1.00 33.99  ? 22   LYS A CA  1 
ATOM   167   C C   . LYS A  1 22  ? 20.509  35.279 28.647  1.00 35.11  ? 22   LYS A C   1 
ATOM   168   O O   . LYS A  1 22  ? 19.889  35.016 27.627  1.00 35.63  ? 22   LYS A O   1 
ATOM   169   C CB  . LYS A  1 22  ? 19.294  36.400 30.521  1.00 35.59  ? 22   LYS A CB  1 
ATOM   170   C CG  . LYS A  1 22  ? 19.575  37.274 31.738  1.00 35.19  ? 22   LYS A CG  1 
ATOM   171   C CD  . LYS A  1 22  ? 18.522  38.330 32.028  1.00 36.11  ? 22   LYS A CD  1 
ATOM   172   C CE  . LYS A  1 22  ? 18.986  39.766 31.723  1.00 34.91  ? 22   LYS A CE  1 
ATOM   173   N NZ  . LYS A  1 22  ? 19.916  40.350 32.751  1.00 34.10  ? 22   LYS A NZ  1 
ATOM   174   N N   . ASN A  1 23  ? 21.414  34.466 29.183  1.00 36.14  ? 23   ASN A N   1 
ATOM   175   C CA  . ASN A  1 23  ? 21.701  33.139 28.641  1.00 37.86  ? 23   ASN A CA  1 
ATOM   176   C C   . ASN A  1 23  ? 22.155  33.171 27.178  1.00 35.80  ? 23   ASN A C   1 
ATOM   177   O O   . ASN A  1 23  ? 21.695  32.384 26.353  1.00 36.67  ? 23   ASN A O   1 
ATOM   178   C CB  . ASN A  1 23  ? 20.489  32.208 28.833  1.00 42.10  ? 23   ASN A CB  1 
ATOM   179   C CG  . ASN A  1 23  ? 20.182  31.943 30.296  1.00 46.10  ? 23   ASN A CG  1 
ATOM   180   O OD1 . ASN A  1 23  ? 21.053  32.094 31.159  1.00 45.65  ? 23   ASN A OD1 1 
ATOM   181   N ND2 . ASN A  1 23  ? 18.941  31.539 30.585  1.00 52.15  ? 23   ASN A ND2 1 
ATOM   182   N N   . VAL A  1 24  ? 23.073  34.084 26.878  1.00 32.98  ? 24   VAL A N   1 
ATOM   183   C CA  . VAL A  1 24  ? 23.684  34.187 25.552  1.00 31.39  ? 24   VAL A CA  1 
ATOM   184   C C   . VAL A  1 24  ? 24.817  33.167 25.429  1.00 31.14  ? 24   VAL A C   1 
ATOM   185   O O   . VAL A  1 24  ? 25.798  33.239 26.166  1.00 30.72  ? 24   VAL A O   1 
ATOM   186   C CB  . VAL A  1 24  ? 24.255  35.605 25.310  1.00 29.75  ? 24   VAL A CB  1 
ATOM   187   C CG1 . VAL A  1 24  ? 24.996  35.675 23.983  1.00 29.03  ? 24   VAL A CG1 1 
ATOM   188   C CG2 . VAL A  1 24  ? 23.143  36.646 25.362  1.00 29.66  ? 24   VAL A CG2 1 
ATOM   189   N N   . THR A  1 25  ? 24.689  32.227 24.495  1.00 31.36  ? 25   THR A N   1 
ATOM   190   C CA  . THR A  1 25  ? 25.715  31.203 24.296  1.00 31.68  ? 25   THR A CA  1 
ATOM   191   C C   . THR A  1 25  ? 26.945  31.806 23.628  1.00 30.13  ? 25   THR A C   1 
ATOM   192   O O   . THR A  1 25  ? 26.830  32.459 22.588  1.00 29.19  ? 25   THR A O   1 
ATOM   193   C CB  . THR A  1 25  ? 25.213  30.040 23.419  1.00 33.25  ? 25   THR A CB  1 
ATOM   194   O OG1 . THR A  1 25  ? 23.894  29.660 23.823  1.00 34.48  ? 25   THR A OG1 1 
ATOM   195   C CG2 . THR A  1 25  ? 26.136  28.842 23.545  1.00 34.72  ? 25   THR A CG2 1 
ATOM   196   N N   . VAL A  1 26  ? 28.114  31.568 24.217  1.00 29.91  ? 26   VAL A N   1 
ATOM   197   C CA  . VAL A  1 26  ? 29.370  32.119 23.709  1.00 28.92  ? 26   VAL A CA  1 
ATOM   198   C C   . VAL A  1 26  ? 30.388  31.021 23.461  1.00 30.20  ? 26   VAL A C   1 
ATOM   199   O O   . VAL A  1 26  ? 30.307  29.945 24.048  1.00 31.68  ? 26   VAL A O   1 
ATOM   200   C CB  . VAL A  1 26  ? 29.976  33.169 24.663  1.00 27.87  ? 26   VAL A CB  1 
ATOM   201   C CG1 . VAL A  1 26  ? 29.096  34.403 24.714  1.00 26.54  ? 26   VAL A CG1 1 
ATOM   202   C CG2 . VAL A  1 26  ? 30.190  32.596 26.059  1.00 28.67  ? 26   VAL A CG2 1 
ATOM   203   N N   . THR A  1 27  ? 31.352  31.312 22.594  1.00 29.83  ? 27   THR A N   1 
ATOM   204   C CA  . THR A  1 27  ? 32.369  30.340 22.209  1.00 31.37  ? 27   THR A CA  1 
ATOM   205   C C   . THR A  1 27  ? 33.361  30.103 23.339  1.00 32.13  ? 27   THR A C   1 
ATOM   206   O O   . THR A  1 27  ? 33.839  28.986 23.525  1.00 34.11  ? 27   THR A O   1 
ATOM   207   C CB  . THR A  1 27  ? 33.145  30.778 20.948  1.00 31.12  ? 27   THR A CB  1 
ATOM   208   O OG1 . THR A  1 27  ? 33.871  31.984 21.210  1.00 30.01  ? 27   THR A OG1 1 
ATOM   209   C CG2 . THR A  1 27  ? 32.196  30.996 19.784  1.00 30.32  ? 27   THR A CG2 1 
ATOM   210   N N   . HIS A  1 28  ? 33.677  31.161 24.078  1.00 30.79  ? 28   HIS A N   1 
ATOM   211   C CA  . HIS A  1 28  ? 34.586  31.070 25.214  1.00 31.42  ? 28   HIS A CA  1 
ATOM   212   C C   . HIS A  1 28  ? 34.095  31.955 26.337  1.00 30.04  ? 28   HIS A C   1 
ATOM   213   O O   . HIS A  1 28  ? 33.501  33.005 26.096  1.00 28.54  ? 28   HIS A O   1 
ATOM   214   C CB  . HIS A  1 28  ? 35.995  31.495 24.810  1.00 31.93  ? 28   HIS A CB  1 
ATOM   215   C CG  . HIS A  1 28  ? 36.532  30.741 23.636  1.00 33.35  ? 28   HIS A CG  1 
ATOM   216   N ND1 . HIS A  1 28  ? 36.181  31.043 22.339  1.00 32.64  ? 28   HIS A ND1 1 
ATOM   217   C CD2 . HIS A  1 28  ? 37.380  29.689 23.563  1.00 35.60  ? 28   HIS A CD2 1 
ATOM   218   C CE1 . HIS A  1 28  ? 36.794  30.213 21.517  1.00 34.36  ? 28   HIS A CE1 1 
ATOM   219   N NE2 . HIS A  1 28  ? 37.528  29.382 22.234  1.00 36.25  ? 28   HIS A NE2 1 
ATOM   220   N N   . ALA A  1 29  ? 34.358  31.527 27.563  1.00 30.76  ? 29   ALA A N   1 
ATOM   221   C CA  . ALA A  1 29  ? 33.948  32.262 28.749  1.00 29.75  ? 29   ALA A CA  1 
ATOM   222   C C   . ALA A  1 29  ? 34.944  32.003 29.864  1.00 30.75  ? 29   ALA A C   1 
ATOM   223   O O   . ALA A  1 29  ? 35.820  31.151 29.735  1.00 32.38  ? 29   ALA A O   1 
ATOM   224   C CB  . ALA A  1 29  ? 32.553  31.840 29.174  1.00 29.60  ? 29   ALA A CB  1 
ATOM   225   N N   . GLN A  1 30  ? 34.821  32.752 30.950  1.00 29.99  ? 30   GLN A N   1 
ATOM   226   C CA  . GLN A  1 30  ? 35.682  32.554 32.106  1.00 30.92  ? 30   GLN A CA  1 
ATOM   227   C C   . GLN A  1 30  ? 34.905  32.749 33.399  1.00 30.30  ? 30   GLN A C   1 
ATOM   228   O O   . GLN A  1 30  ? 34.497  33.863 33.729  1.00 29.03  ? 30   GLN A O   1 
ATOM   229   C CB  . GLN A  1 30  ? 36.883  33.502 32.067  1.00 30.96  ? 30   GLN A CB  1 
ATOM   230   C CG  . GLN A  1 30  ? 37.896  33.222 33.170  1.00 32.28  ? 30   GLN A CG  1 
ATOM   231   C CD  . GLN A  1 30  ? 39.223  33.932 32.971  1.00 33.01  ? 30   GLN A CD  1 
ATOM   232   O OE1 . GLN A  1 30  ? 39.602  34.276 31.852  1.00 33.13  ? 30   GLN A OE1 1 
ATOM   233   N NE2 . GLN A  1 30  ? 39.943  34.148 34.065  1.00 33.74  ? 30   GLN A NE2 1 
ATOM   234   N N   . ASP A  1 31  ? 34.699  31.653 34.122  1.00 31.40  ? 31   ASP A N   1 
ATOM   235   C CA  . ASP A  1 31  ? 34.110  31.713 35.450  1.00 31.19  ? 31   ASP A CA  1 
ATOM   236   C C   . ASP A  1 31  ? 35.128  32.345 36.395  1.00 31.14  ? 31   ASP A C   1 
ATOM   237   O O   . ASP A  1 31  ? 36.306  31.979 36.387  1.00 32.25  ? 31   ASP A O   1 
ATOM   238   C CB  . ASP A  1 31  ? 33.725  30.314 35.937  1.00 32.79  ? 31   ASP A CB  1 
ATOM   239   C CG  . ASP A  1 31  ? 32.757  30.343 37.108  1.00 32.64  ? 31   ASP A CG  1 
ATOM   240   O OD1 . ASP A  1 31  ? 32.623  31.398 37.767  1.00 31.48  ? 31   ASP A OD1 1 
ATOM   241   O OD2 . ASP A  1 31  ? 32.124  29.299 37.369  1.00 33.95  ? 31   ASP A OD2 1 
ATOM   242   N N   . ILE A  1 32  ? 34.666  33.308 37.188  1.00 30.03  ? 32   ILE A N   1 
ATOM   243   C CA  . ILE A  1 32  ? 35.522  34.016 38.142  1.00 30.04  ? 32   ILE A CA  1 
ATOM   244   C C   . ILE A  1 32  ? 35.052  33.852 39.595  1.00 30.20  ? 32   ILE A C   1 
ATOM   245   O O   . ILE A  1 32  ? 35.618  34.456 40.503  1.00 30.23  ? 32   ILE A O   1 
ATOM   246   C CB  . ILE A  1 32  ? 35.621  35.517 37.788  1.00 28.90  ? 32   ILE A CB  1 
ATOM   247   C CG1 . ILE A  1 32  ? 34.233  36.141 37.639  1.00 27.71  ? 32   ILE A CG1 1 
ATOM   248   C CG2 . ILE A  1 32  ? 36.414  35.700 36.506  1.00 29.07  ? 32   ILE A CG2 1 
ATOM   249   C CD1 . ILE A  1 32  ? 34.242  37.649 37.721  1.00 26.97  ? 32   ILE A CD1 1 
ATOM   250   N N   . LEU A  1 33  ? 34.032  33.024 39.806  1.00 30.49  ? 33   LEU A N   1 
ATOM   251   C CA  . LEU A  1 33  ? 33.475  32.790 41.131  1.00 30.83  ? 33   LEU A CA  1 
ATOM   252   C C   . LEU A  1 33  ? 33.804  31.385 41.625  1.00 32.54  ? 33   LEU A C   1 
ATOM   253   O O   . LEU A  1 33  ? 33.382  30.395 41.022  1.00 33.42  ? 33   LEU A O   1 
ATOM   254   C CB  . LEU A  1 33  ? 31.957  32.961 41.088  1.00 30.30  ? 33   LEU A CB  1 
ATOM   255   C CG  . LEU A  1 33  ? 31.210  32.861 42.417  1.00 30.70  ? 33   LEU A CG  1 
ATOM   256   C CD1 . LEU A  1 33  ? 31.574  34.030 43.314  1.00 29.98  ? 33   LEU A CD1 1 
ATOM   257   C CD2 . LEU A  1 33  ? 29.710  32.818 42.178  1.00 30.75  ? 33   LEU A CD2 1 
ATOM   258   N N   . GLU A  1 34  ? 34.543  31.297 42.728  1.00 33.23  ? 34   GLU A N   1 
ATOM   259   C CA  . GLU A  1 34  ? 34.788  30.013 43.378  1.00 35.03  ? 34   GLU A CA  1 
ATOM   260   C C   . GLU A  1 34  ? 33.562  29.587 44.185  1.00 35.36  ? 34   GLU A C   1 
ATOM   261   O O   . GLU A  1 34  ? 33.166  30.266 45.129  1.00 34.67  ? 34   GLU A O   1 
ATOM   262   C CB  . GLU A  1 34  ? 36.017  30.080 44.286  1.00 35.78  ? 34   GLU A CB  1 
ATOM   263   C CG  . GLU A  1 34  ? 36.349  28.759 44.962  1.00 37.85  ? 34   GLU A CG  1 
ATOM   264   C CD  . GLU A  1 34  ? 36.327  27.596 43.990  1.00 39.32  ? 34   GLU A CD  1 
ATOM   265   O OE1 . GLU A  1 34  ? 37.166  27.570 43.065  1.00 39.76  ? 34   GLU A OE1 1 
ATOM   266   O OE2 . GLU A  1 34  ? 35.444  26.726 44.133  1.00 40.26  ? 34   GLU A OE2 1 
ATOM   267   N N   . LYS A  1 35  ? 32.976  28.452 43.815  1.00 36.69  ? 35   LYS A N   1 
ATOM   268   C CA  . LYS A  1 35  ? 31.719  27.988 44.416  1.00 37.39  ? 35   LYS A CA  1 
ATOM   269   C C   . LYS A  1 35  ? 31.889  26.844 45.427  1.00 39.47  ? 35   LYS A C   1 
ATOM   270   O O   . LYS A  1 35  ? 30.953  26.550 46.175  1.00 40.18  ? 35   LYS A O   1 
ATOM   271   C CB  . LYS A  1 35  ? 30.729  27.572 43.316  1.00 37.70  ? 35   LYS A CB  1 
ATOM   272   C CG  . LYS A  1 35  ? 29.872  28.712 42.781  1.00 35.95  ? 35   LYS A CG  1 
ATOM   273   C CD  . LYS A  1 35  ? 29.062  28.293 41.561  1.00 36.34  ? 35   LYS A CD  1 
ATOM   274   C CE  . LYS A  1 35  ? 29.656  28.806 40.254  1.00 35.14  ? 35   LYS A CE  1 
ATOM   275   N NZ  . LYS A  1 35  ? 31.088  28.450 40.032  1.00 35.53  ? 35   LYS A NZ  1 
ATOM   276   N N   . THR A  1 36  ? 33.072  26.225 45.471  1.00 40.68  ? 36   THR A N   1 
ATOM   277   C CA  . THR A  1 36  ? 33.285  25.022 46.286  1.00 43.05  ? 36   THR A CA  1 
ATOM   278   C C   . THR A  1 36  ? 34.281  25.197 47.433  1.00 43.34  ? 36   THR A C   1 
ATOM   279   O O   . THR A  1 36  ? 35.125  26.094 47.416  1.00 42.12  ? 36   THR A O   1 
ATOM   280   C CB  . THR A  1 36  ? 33.768  23.836 45.425  1.00 45.15  ? 36   THR A CB  1 
ATOM   281   O OG1 . THR A  1 36  ? 35.053  24.132 44.863  1.00 44.90  ? 36   THR A OG1 1 
ATOM   282   C CG2 . THR A  1 36  ? 32.775  23.537 44.311  1.00 45.26  ? 36   THR A CG2 1 
ATOM   283   N N   . HIS A  1 37  ? 34.151  24.316 48.425  1.00 45.20  ? 37   HIS A N   1 
ATOM   284   C CA  . HIS A  1 37  ? 35.085  24.197 49.549  1.00 46.05  ? 37   HIS A CA  1 
ATOM   285   C C   . HIS A  1 37  ? 35.164  22.712 49.925  1.00 49.10  ? 37   HIS A C   1 
ATOM   286   O O   . HIS A  1 37  ? 34.308  21.928 49.508  1.00 50.36  ? 37   HIS A O   1 
ATOM   287   C CB  . HIS A  1 37  ? 34.604  25.031 50.742  1.00 44.72  ? 37   HIS A CB  1 
ATOM   288   C CG  . HIS A  1 37  ? 33.240  24.655 51.234  1.00 45.27  ? 37   HIS A CG  1 
ATOM   289   N ND1 . HIS A  1 37  ? 33.043  23.874 52.351  1.00 47.04  ? 37   HIS A ND1 1 
ATOM   290   C CD2 . HIS A  1 37  ? 32.006  24.940 50.752  1.00 44.54  ? 37   HIS A CD2 1 
ATOM   291   C CE1 . HIS A  1 37  ? 31.747  23.700 52.544  1.00 47.44  ? 37   HIS A CE1 1 
ATOM   292   N NE2 . HIS A  1 37  ? 31.096  24.337 51.586  1.00 45.99  ? 37   HIS A NE2 1 
ATOM   293   N N   . ASN A  1 38  ? 36.177  22.321 50.698  1.00 50.56  ? 38   ASN A N   1 
ATOM   294   C CA  . ASN A  1 38  ? 36.346  20.903 51.071  1.00 53.80  ? 38   ASN A CA  1 
ATOM   295   C C   . ASN A  1 38  ? 35.425  20.431 52.211  1.00 54.82  ? 38   ASN A C   1 
ATOM   296   O O   . ASN A  1 38  ? 35.197  19.231 52.371  1.00 57.60  ? 38   ASN A O   1 
ATOM   297   C CB  . ASN A  1 38  ? 37.819  20.565 51.378  1.00 55.43  ? 38   ASN A CB  1 
ATOM   298   C CG  . ASN A  1 38  ? 38.372  21.312 52.580  1.00 54.39  ? 38   ASN A CG  1 
ATOM   299   O OD1 . ASN A  1 38  ? 37.635  21.930 53.347  1.00 52.79  ? 38   ASN A OD1 1 
ATOM   300   N ND2 . ASN A  1 38  ? 39.687  21.252 52.749  1.00 55.55  ? 38   ASN A ND2 1 
ATOM   301   N N   . GLY A  1 39  ? 34.916  21.376 53.000  1.00 52.85  ? 39   GLY A N   1 
ATOM   302   C CA  . GLY A  1 39  ? 33.940  21.083 54.060  1.00 53.63  ? 39   GLY A CA  1 
ATOM   303   C C   . GLY A  1 39  ? 34.573  20.840 55.417  1.00 54.75  ? 39   GLY A C   1 
ATOM   304   O O   . GLY A  1 39  ? 33.912  20.349 56.339  1.00 56.03  ? 39   GLY A O   1 
ATOM   305   N N   . LYS A  1 40  ? 35.850  21.204 55.543  1.00 54.41  ? 40   LYS A N   1 
ATOM   306   C CA  . LYS A  1 40  ? 36.651  20.857 56.712  1.00 55.87  ? 40   LYS A CA  1 
ATOM   307   C C   . LYS A  1 40  ? 37.355  22.065 57.318  1.00 53.88  ? 40   LYS A C   1 
ATOM   308   O O   . LYS A  1 40  ? 37.657  23.034 56.628  1.00 51.92  ? 40   LYS A O   1 
ATOM   309   C CB  . LYS A  1 40  ? 37.697  19.813 56.319  1.00 58.60  ? 40   LYS A CB  1 
ATOM   310   C CG  . LYS A  1 40  ? 37.133  18.417 56.121  1.00 61.59  ? 40   LYS A CG  1 
ATOM   311   C CD  . LYS A  1 40  ? 37.897  17.655 55.053  1.00 63.65  ? 40   LYS A CD  1 
ATOM   312   C CE  . LYS A  1 40  ? 37.433  16.211 54.965  1.00 67.19  ? 40   LYS A CE  1 
ATOM   313   N NZ  . LYS A  1 40  ? 38.046  15.498 53.810  1.00 69.27  ? 40   LYS A NZ  1 
ATOM   314   N N   . LEU A  1 41  ? 37.615  21.983 58.619  1.00 54.65  ? 41   LEU A N   1 
ATOM   315   C CA  . LEU A  1 41  ? 38.447  22.957 59.317  1.00 53.43  ? 41   LEU A CA  1 
ATOM   316   C C   . LEU A  1 41  ? 39.896  22.476 59.220  1.00 55.33  ? 41   LEU A C   1 
ATOM   317   O O   . LEU A  1 41  ? 40.210  21.347 59.611  1.00 57.96  ? 41   LEU A O   1 
ATOM   318   C CB  . LEU A  1 41  ? 37.995  23.089 60.775  1.00 53.43  ? 41   LEU A CB  1 
ATOM   319   C CG  . LEU A  1 41  ? 36.682  23.847 61.075  1.00 51.58  ? 41   LEU A CG  1 
ATOM   320   C CD1 . LEU A  1 41  ? 36.951  25.128 61.854  1.00 49.76  ? 41   LEU A CD1 1 
ATOM   321   C CD2 . LEU A  1 41  ? 35.838  24.164 59.839  1.00 50.27  ? 41   LEU A CD2 1 
ATOM   322   N N   . CYS A  1 42  ? 40.767  23.335 58.692  1.00 54.26  ? 42   CYS A N   1 
ATOM   323   C CA  . CYS A  1 42  ? 42.113  22.931 58.286  1.00 56.23  ? 42   CYS A CA  1 
ATOM   324   C C   . CYS A  1 42  ? 43.206  23.762 58.933  1.00 56.02  ? 42   CYS A C   1 
ATOM   325   O O   . CYS A  1 42  ? 42.959  24.854 59.439  1.00 53.96  ? 42   CYS A O   1 
ATOM   326   C CB  . CYS A  1 42  ? 42.273  23.057 56.759  1.00 55.80  ? 42   CYS A CB  1 
ATOM   327   S SG  . CYS A  1 42  ? 41.284  21.967 55.687  1.00 56.73  ? 42   CYS A SG  1 
ATOM   328   N N   . ASP A  1 43  ? 44.425  23.233 58.890  1.00 58.49  ? 43   ASP A N   1 
ATOM   329   C CA  . ASP A  1 43  ? 45.615  23.997 59.247  1.00 58.80  ? 43   ASP A CA  1 
ATOM   330   C C   . ASP A  1 43  ? 45.787  25.129 58.247  1.00 56.90  ? 43   ASP A C   1 
ATOM   331   O O   . ASP A  1 43  ? 45.629  24.921 57.044  1.00 56.77  ? 43   ASP A O   1 
ATOM   332   C CB  . ASP A  1 43  ? 46.865  23.107 59.222  1.00 62.31  ? 43   ASP A CB  1 
ATOM   333   C CG  . ASP A  1 43  ? 46.868  22.054 60.320  1.00 64.56  ? 43   ASP A CG  1 
ATOM   334   O OD1 . ASP A  1 43  ? 45.945  22.047 61.160  1.00 63.36  ? 43   ASP A OD1 1 
ATOM   335   O OD2 . ASP A  1 43  ? 47.800  21.223 60.343  1.00 67.77  ? 43   ASP A OD2 1 
ATOM   336   N N   . LEU A  1 44  ? 46.105  26.322 58.743  1.00 55.63  ? 44   LEU A N   1 
ATOM   337   C CA  . LEU A  1 44  ? 46.361  27.473 57.877  1.00 54.21  ? 44   LEU A CA  1 
ATOM   338   C C   . LEU A  1 44  ? 47.861  27.675 57.713  1.00 56.42  ? 44   LEU A C   1 
ATOM   339   O O   . LEU A  1 44  ? 48.564  27.923 58.691  1.00 57.55  ? 44   LEU A O   1 
ATOM   340   C CB  . LEU A  1 44  ? 45.730  28.742 58.455  1.00 51.70  ? 44   LEU A CB  1 
ATOM   341   C CG  . LEU A  1 44  ? 45.695  29.954 57.516  1.00 49.98  ? 44   LEU A CG  1 
ATOM   342   C CD1 . LEU A  1 44  ? 44.556  29.820 56.514  1.00 48.28  ? 44   LEU A CD1 1 
ATOM   343   C CD2 . LEU A  1 44  ? 45.558  31.253 58.297  1.00 48.61  ? 44   LEU A CD2 1 
ATOM   344   N N   . ASP A  1 45  ? 48.344  27.568 56.477  1.00 57.23  ? 45   ASP A N   1 
ATOM   345   C CA  . ASP A  1 45  ? 49.768  27.721 56.174  1.00 59.68  ? 45   ASP A CA  1 
ATOM   346   C C   . ASP A  1 45  ? 50.613  26.719 56.974  1.00 62.85  ? 45   ASP A C   1 
ATOM   347   O O   . ASP A  1 45  ? 51.739  27.021 57.379  1.00 64.84  ? 45   ASP A O   1 
ATOM   348   C CB  . ASP A  1 45  ? 50.216  29.162 56.466  1.00 58.83  ? 45   ASP A CB  1 
ATOM   349   C CG  . ASP A  1 45  ? 51.427  29.577 55.651  1.00 60.78  ? 45   ASP A CG  1 
ATOM   350   O OD1 . ASP A  1 45  ? 51.274  29.781 54.429  1.00 60.10  ? 45   ASP A OD1 1 
ATOM   351   O OD2 . ASP A  1 45  ? 52.527  29.710 56.232  1.00 63.16  ? 45   ASP A OD2 1 
ATOM   352   N N   . GLY A  1 46  ? 50.051  25.532 57.209  1.00 63.52  ? 46   GLY A N   1 
ATOM   353   C CA  . GLY A  1 46  ? 50.693  24.504 58.033  1.00 66.57  ? 46   GLY A CA  1 
ATOM   354   C C   . GLY A  1 46  ? 50.462  24.657 59.528  1.00 65.99  ? 46   GLY A C   1 
ATOM   355   O O   . GLY A  1 46  ? 50.623  23.693 60.278  1.00 68.09  ? 46   GLY A O   1 
ATOM   356   N N   . VAL A  1 47  ? 50.077  25.860 59.961  1.00 63.26  ? 47   VAL A N   1 
ATOM   357   C CA  . VAL A  1 47  ? 49.935  26.187 61.384  1.00 62.68  ? 47   VAL A CA  1 
ATOM   358   C C   . VAL A  1 47  ? 48.533  25.825 61.872  1.00 60.75  ? 47   VAL A C   1 
ATOM   359   O O   . VAL A  1 47  ? 47.543  26.376 61.394  1.00 58.14  ? 47   VAL A O   1 
ATOM   360   C CB  . VAL A  1 47  ? 50.195  27.687 61.643  1.00 61.06  ? 47   VAL A CB  1 
ATOM   361   C CG1 . VAL A  1 47  ? 50.067  28.006 63.126  1.00 60.72  ? 47   VAL A CG1 1 
ATOM   362   C CG2 . VAL A  1 47  ? 51.570  28.090 61.130  1.00 63.20  ? 47   VAL A CG2 1 
ATOM   363   N N   . LYS A  1 48  ? 48.464  24.917 62.842  1.00 62.27  ? 48   LYS A N   1 
ATOM   364   C CA  . LYS A  1 48  ? 47.195  24.351 63.303  1.00 61.23  ? 48   LYS A CA  1 
ATOM   365   C C   . LYS A  1 48  ? 46.337  25.381 64.046  1.00 58.39  ? 48   LYS A C   1 
ATOM   366   O O   . LYS A  1 48  ? 46.867  26.177 64.828  1.00 58.15  ? 48   LYS A O   1 
ATOM   367   C CB  . LYS A  1 48  ? 47.455  23.154 64.230  1.00 64.01  ? 48   LYS A CB  1 
ATOM   368   C CG  . LYS A  1 48  ? 46.326  22.138 64.268  1.00 64.27  ? 48   LYS A CG  1 
ATOM   369   C CD  . LYS A  1 48  ? 46.164  21.508 65.638  1.00 65.67  ? 48   LYS A CD  1 
ATOM   370   C CE  . LYS A  1 48  ? 45.077  20.469 65.612  1.00 66.39  ? 48   LYS A CE  1 
ATOM   371   N NZ  . LYS A  1 48  ? 44.399  20.323 66.923  1.00 66.26  ? 48   LYS A NZ  1 
ATOM   372   N N   . PRO A  1 49  ? 45.009  25.373 63.805  1.00 56.47  ? 49   PRO A N   1 
ATOM   373   C CA  . PRO A  1 49  ? 44.138  26.218 64.622  1.00 54.30  ? 49   PRO A CA  1 
ATOM   374   C C   . PRO A  1 49  ? 43.978  25.693 66.043  1.00 55.35  ? 49   PRO A C   1 
ATOM   375   O O   . PRO A  1 49  ? 44.072  24.486 66.271  1.00 57.48  ? 49   PRO A O   1 
ATOM   376   C CB  . PRO A  1 49  ? 42.789  26.129 63.905  1.00 52.70  ? 49   PRO A CB  1 
ATOM   377   C CG  . PRO A  1 49  ? 42.829  24.818 63.200  1.00 54.62  ? 49   PRO A CG  1 
ATOM   378   C CD  . PRO A  1 49  ? 44.250  24.704 62.731  1.00 56.29  ? 49   PRO A CD  1 
ATOM   379   N N   . LEU A  1 50  ? 43.731  26.605 66.978  1.00 54.00  ? 50   LEU A N   1 
ATOM   380   C CA  . LEU A  1 50  ? 43.333  26.237 68.327  1.00 54.58  ? 50   LEU A CA  1 
ATOM   381   C C   . LEU A  1 50  ? 41.849  25.906 68.301  1.00 53.65  ? 50   LEU A C   1 
ATOM   382   O O   . LEU A  1 50  ? 41.014  26.805 68.205  1.00 51.62  ? 50   LEU A O   1 
ATOM   383   C CB  . LEU A  1 50  ? 43.612  27.384 69.305  1.00 53.64  ? 50   LEU A CB  1 
ATOM   384   C CG  . LEU A  1 50  ? 42.983  27.318 70.702  1.00 53.65  ? 50   LEU A CG  1 
ATOM   385   C CD1 . LEU A  1 50  ? 43.242  25.979 71.375  1.00 56.06  ? 50   LEU A CD1 1 
ATOM   386   C CD2 . LEU A  1 50  ? 43.512  28.456 71.563  1.00 53.11  ? 50   LEU A CD2 1 
ATOM   387   N N   . ILE A  1 51  ? 41.524  24.618 68.363  1.00 55.42  ? 51   ILE A N   1 
ATOM   388   C CA  . ILE A  1 51  ? 40.132  24.181 68.377  1.00 55.14  ? 51   ILE A CA  1 
ATOM   389   C C   . ILE A  1 51  ? 39.731  23.883 69.812  1.00 56.03  ? 51   ILE A C   1 
ATOM   390   O O   . ILE A  1 51  ? 40.177  22.898 70.399  1.00 58.32  ? 51   ILE A O   1 
ATOM   391   C CB  . ILE A  1 51  ? 39.903  22.942 67.486  1.00 56.83  ? 51   ILE A CB  1 
ATOM   392   C CG1 . ILE A  1 51  ? 40.537  23.174 66.111  1.00 56.32  ? 51   ILE A CG1 1 
ATOM   393   C CG2 . ILE A  1 51  ? 38.411  22.642 67.365  1.00 56.52  ? 51   ILE A CG2 1 
ATOM   394   C CD1 . ILE A  1 51  ? 40.048  22.249 65.018  1.00 57.33  ? 51   ILE A CD1 1 
ATOM   395   N N   . LEU A  1 52  ? 38.878  24.739 70.369  1.00 54.39  ? 52   LEU A N   1 
ATOM   396   C CA  . LEU A  1 52  ? 38.464  24.623 71.765  1.00 55.06  ? 52   LEU A CA  1 
ATOM   397   C C   . LEU A  1 52  ? 37.453  23.494 71.991  1.00 56.76  ? 52   LEU A C   1 
ATOM   398   O O   . LEU A  1 52  ? 37.177  23.125 73.135  1.00 57.92  ? 52   LEU A O   1 
ATOM   399   C CB  . LEU A  1 52  ? 37.892  25.955 72.256  1.00 53.00  ? 52   LEU A CB  1 
ATOM   400   C CG  . LEU A  1 52  ? 38.824  27.166 72.128  1.00 51.58  ? 52   LEU A CG  1 
ATOM   401   C CD1 . LEU A  1 52  ? 38.099  28.446 72.513  1.00 49.86  ? 52   LEU A CD1 1 
ATOM   402   C CD2 . LEU A  1 52  ? 40.075  26.994 72.979  1.00 52.88  ? 52   LEU A CD2 1 
ATOM   403   N N   . ARG A  1 53  ? 36.913  22.951 70.901  1.00 57.09  ? 53   ARG A N   1 
ATOM   404   C CA  . ARG A  1 53  ? 35.934  21.869 70.946  1.00 59.02  ? 53   ARG A CA  1 
ATOM   405   C C   . ARG A  1 53  ? 34.678  22.348 71.696  1.00 58.43  ? 53   ARG A C   1 
ATOM   406   O O   . ARG A  1 53  ? 33.984  23.238 71.199  1.00 56.59  ? 53   ARG A O   1 
ATOM   407   C CB  . ARG A  1 53  ? 36.558  20.583 71.523  1.00 62.04  ? 53   ARG A CB  1 
ATOM   408   C CG  . ARG A  1 53  ? 35.732  19.325 71.271  1.00 64.57  ? 53   ARG A CG  1 
ATOM   409   C CD  . ARG A  1 53  ? 36.324  18.082 71.932  1.00 67.85  ? 53   ARG A CD  1 
ATOM   410   N NE  . ARG A  1 53  ? 37.110  17.269 70.996  1.00 69.58  ? 53   ARG A NE  1 
ATOM   411   C CZ  . ARG A  1 53  ? 38.438  17.307 70.849  1.00 69.88  ? 53   ARG A CZ  1 
ATOM   412   N NH1 . ARG A  1 53  ? 39.197  18.123 71.576  1.00 68.56  ? 53   ARG A NH1 1 
ATOM   413   N NH2 . ARG A  1 53  ? 39.018  16.508 69.958  1.00 71.80  ? 53   ARG A NH2 1 
ATOM   414   N N   . ASP A  1 54  ? 34.387  21.789 72.872  1.00 60.15  ? 54   ASP A N   1 
ATOM   415   C CA  . ASP A  1 54  ? 33.221  22.204 73.657  1.00 59.97  ? 54   ASP A CA  1 
ATOM   416   C C   . ASP A  1 54  ? 33.559  23.239 74.737  1.00 58.60  ? 54   ASP A C   1 
ATOM   417   O O   . ASP A  1 54  ? 32.659  23.732 75.417  1.00 58.39  ? 54   ASP A O   1 
ATOM   418   C CB  . ASP A  1 54  ? 32.551  20.981 74.292  1.00 62.93  ? 54   ASP A CB  1 
ATOM   419   C CG  . ASP A  1 54  ? 31.875  20.088 73.265  1.00 64.47  ? 54   ASP A CG  1 
ATOM   420   O OD1 . ASP A  1 54  ? 31.009  20.586 72.514  1.00 63.34  ? 54   ASP A OD1 1 
ATOM   421   O OD2 . ASP A  1 54  ? 32.202  18.884 73.216  1.00 67.01  ? 54   ASP A OD2 1 
ATOM   422   N N   . CYS A  1 55  ? 34.843  23.562 74.898  1.00 57.93  ? 55   CYS A N   1 
ATOM   423   C CA  . CYS A  1 55  ? 35.258  24.623 75.824  1.00 56.67  ? 55   CYS A CA  1 
ATOM   424   C C   . CYS A  1 55  ? 35.087  26.004 75.182  1.00 54.11  ? 55   CYS A C   1 
ATOM   425   O O   . CYS A  1 55  ? 35.201  26.152 73.966  1.00 53.18  ? 55   CYS A O   1 
ATOM   426   C CB  . CYS A  1 55  ? 36.713  24.431 76.279  1.00 57.35  ? 55   CYS A CB  1 
ATOM   427   S SG  . CYS A  1 55  ? 36.956  23.101 77.481  1.00 60.40  ? 55   CYS A SG  1 
ATOM   428   N N   . SER A  1 56  ? 34.803  27.004 76.011  1.00 53.15  ? 56   SER A N   1 
ATOM   429   C CA  . SER A  1 56  ? 34.739  28.394 75.567  1.00 51.07  ? 56   SER A CA  1 
ATOM   430   C C   . SER A  1 56  ? 36.082  29.076 75.821  1.00 50.38  ? 56   SER A C   1 
ATOM   431   O O   . SER A  1 56  ? 37.001  28.474 76.378  1.00 51.51  ? 56   SER A O   1 
ATOM   432   C CB  . SER A  1 56  ? 33.633  29.145 76.310  1.00 50.85  ? 56   SER A CB  1 
ATOM   433   O OG  . SER A  1 56  ? 34.066  29.550 77.598  1.00 51.18  ? 56   SER A OG  1 
ATOM   434   N N   . VAL A  1 57  ? 36.185  30.338 75.420  1.00 48.77  ? 57   VAL A N   1 
ATOM   435   C CA  . VAL A  1 57  ? 37.404  31.117 75.634  1.00 48.33  ? 57   VAL A CA  1 
ATOM   436   C C   . VAL A  1 57  ? 37.594  31.367 77.129  1.00 49.03  ? 57   VAL A C   1 
ATOM   437   O O   . VAL A  1 57  ? 38.715  31.314 77.637  1.00 49.69  ? 57   VAL A O   1 
ATOM   438   C CB  . VAL A  1 57  ? 37.362  32.458 74.867  1.00 46.79  ? 57   VAL A CB  1 
ATOM   439   C CG1 . VAL A  1 57  ? 38.578  33.313 75.190  1.00 46.78  ? 57   VAL A CG1 1 
ATOM   440   C CG2 . VAL A  1 57  ? 37.280  32.208 73.366  1.00 46.07  ? 57   VAL A CG2 1 
ATOM   441   N N   . ALA A  1 58  ? 36.490  31.637 77.823  1.00 49.02  ? 58   ALA A N   1 
ATOM   442   C CA  . ALA A  1 58  ? 36.503  31.813 79.276  1.00 49.80  ? 58   ALA A CA  1 
ATOM   443   C C   . ALA A  1 58  ? 36.948  30.532 79.986  1.00 51.34  ? 58   ALA A C   1 
ATOM   444   O O   . ALA A  1 58  ? 37.836  30.567 80.841  1.00 51.99  ? 58   ALA A O   1 
ATOM   445   C CB  . ALA A  1 58  ? 35.126  32.235 79.766  1.00 49.83  ? 58   ALA A CB  1 
ATOM   446   N N   . GLY A  1 59  ? 36.332  29.408 79.619  1.00 52.12  ? 59   GLY A N   1 
ATOM   447   C CA  . GLY A  1 59  ? 36.684  28.105 80.178  1.00 53.92  ? 59   GLY A CA  1 
ATOM   448   C C   . GLY A  1 59  ? 38.162  27.793 80.024  1.00 54.43  ? 59   GLY A C   1 
ATOM   449   O O   . GLY A  1 59  ? 38.806  27.324 80.965  1.00 55.80  ? 59   GLY A O   1 
ATOM   450   N N   . TRP A  1 60  ? 38.698  28.060 78.838  1.00 53.53  ? 60   TRP A N   1 
ATOM   451   C CA  . TRP A  1 60  ? 40.118  27.862 78.565  1.00 54.19  ? 60   TRP A CA  1 
ATOM   452   C C   . TRP A  1 60  ? 40.987  28.788 79.422  1.00 54.09  ? 60   TRP A C   1 
ATOM   453   O O   . TRP A  1 60  ? 41.898  28.326 80.113  1.00 55.58  ? 60   TRP A O   1 
ATOM   454   C CB  . TRP A  1 60  ? 40.401  28.058 77.065  1.00 53.26  ? 60   TRP A CB  1 
ATOM   455   C CG  . TRP A  1 60  ? 41.836  28.345 76.706  1.00 53.65  ? 60   TRP A CG  1 
ATOM   456   C CD1 . TRP A  1 60  ? 42.948  27.758 77.227  1.00 55.50  ? 60   TRP A CD1 1 
ATOM   457   C CD2 . TRP A  1 60  ? 42.300  29.277 75.723  1.00 52.46  ? 60   TRP A CD2 1 
ATOM   458   N NE1 . TRP A  1 60  ? 44.079  28.277 76.645  1.00 55.63  ? 60   TRP A NE1 1 
ATOM   459   C CE2 . TRP A  1 60  ? 43.709  29.211 75.715  1.00 53.77  ? 60   TRP A CE2 1 
ATOM   460   C CE3 . TRP A  1 60  ? 41.661  30.166 74.849  1.00 50.61  ? 60   TRP A CE3 1 
ATOM   461   C CZ2 . TRP A  1 60  ? 44.492  30.000 74.867  1.00 53.36  ? 60   TRP A CZ2 1 
ATOM   462   C CZ3 . TRP A  1 60  ? 42.440  30.952 74.007  1.00 50.07  ? 60   TRP A CZ3 1 
ATOM   463   C CH2 . TRP A  1 60  ? 43.839  30.862 74.022  1.00 51.46  ? 60   TRP A CH2 1 
ATOM   464   N N   . LEU A  1 61  ? 40.694  30.085 79.385  1.00 52.58  ? 61   LEU A N   1 
ATOM   465   C CA  . LEU A  1 61  ? 41.544  31.082 80.045  1.00 52.60  ? 61   LEU A CA  1 
ATOM   466   C C   . LEU A  1 61  ? 41.499  31.013 81.574  1.00 53.56  ? 61   LEU A C   1 
ATOM   467   O O   . LEU A  1 61  ? 42.531  31.160 82.231  1.00 54.52  ? 61   LEU A O   1 
ATOM   468   C CB  . LEU A  1 61  ? 41.194  32.497 79.570  1.00 51.03  ? 61   LEU A CB  1 
ATOM   469   C CG  . LEU A  1 61  ? 41.575  32.844 78.125  1.00 50.20  ? 61   LEU A CG  1 
ATOM   470   C CD1 . LEU A  1 61  ? 41.283  34.312 77.857  1.00 49.02  ? 61   LEU A CD1 1 
ATOM   471   C CD2 . LEU A  1 61  ? 43.037  32.532 77.833  1.00 51.37  ? 61   LEU A CD2 1 
ATOM   472   N N   . LEU A  1 62  ? 40.315  30.789 82.137  1.00 53.47  ? 62   LEU A N   1 
ATOM   473   C CA  . LEU A  1 62  ? 40.185  30.611 83.589  1.00 54.50  ? 62   LEU A CA  1 
ATOM   474   C C   . LEU A  1 62  ? 40.723  29.261 84.059  1.00 56.35  ? 62   LEU A C   1 
ATOM   475   O O   . LEU A  1 62  ? 41.040  29.100 85.231  1.00 57.41  ? 62   LEU A O   1 
ATOM   476   C CB  . LEU A  1 62  ? 38.730  30.774 84.029  1.00 54.12  ? 62   LEU A CB  1 
ATOM   477   C CG  . LEU A  1 62  ? 38.203  32.202 83.917  1.00 52.83  ? 62   LEU A CG  1 
ATOM   478   C CD1 . LEU A  1 62  ? 36.690  32.220 84.052  1.00 52.74  ? 62   LEU A CD1 1 
ATOM   479   C CD2 . LEU A  1 62  ? 38.849  33.107 84.956  1.00 53.15  ? 62   LEU A CD2 1 
ATOM   480   N N   . GLY A  1 63  ? 40.839  28.302 83.144  1.00 56.92  ? 63   GLY A N   1 
ATOM   481   C CA  . GLY A  1 63  ? 41.371  26.985 83.473  1.00 59.03  ? 63   GLY A CA  1 
ATOM   482   C C   . GLY A  1 63  ? 40.311  26.077 84.063  1.00 60.10  ? 63   GLY A C   1 
ATOM   483   O O   . GLY A  1 63  ? 40.534  25.432 85.084  1.00 61.73  ? 63   GLY A O   1 
ATOM   484   N N   . ASN A  1 64  ? 39.150  26.035 83.418  1.00 59.38  ? 64   ASN A N   1 
ATOM   485   C CA  . ASN A  1 64  ? 38.087  25.107 83.787  1.00 60.73  ? 64   ASN A CA  1 
ATOM   486   C C   . ASN A  1 64  ? 38.611  23.665 83.667  1.00 63.08  ? 64   ASN A C   1 
ATOM   487   O O   . ASN A  1 64  ? 39.262  23.330 82.676  1.00 63.23  ? 64   ASN A O   1 
ATOM   488   C CB  . ASN A  1 64  ? 36.857  25.374 82.895  1.00 59.62  ? 64   ASN A CB  1 
ATOM   489   C CG  . ASN A  1 64  ? 35.799  24.278 82.962  1.00 61.35  ? 64   ASN A CG  1 
ATOM   490   O OD1 . ASN A  1 64  ? 36.106  23.095 83.073  1.00 63.39  ? 64   ASN A OD1 1 
ATOM   491   N ND2 . ASN A  1 64  ? 34.535  24.676 82.850  1.00 60.83  ? 64   ASN A ND2 1 
ATOM   492   N N   . PRO A  1 65  ? 38.346  22.813 84.683  1.00 65.17  ? 65   PRO A N   1 
ATOM   493   C CA  . PRO A  1 65  ? 38.891  21.439 84.732  1.00 67.87  ? 65   PRO A CA  1 
ATOM   494   C C   . PRO A  1 65  ? 38.578  20.541 83.521  1.00 68.88  ? 65   PRO A C   1 
ATOM   495   O O   . PRO A  1 65  ? 39.313  19.587 83.263  1.00 70.92  ? 65   PRO A O   1 
ATOM   496   C CB  . PRO A  1 65  ? 38.267  20.846 86.005  1.00 69.65  ? 65   PRO A CB  1 
ATOM   497   C CG  . PRO A  1 65  ? 37.162  21.765 86.394  1.00 68.04  ? 65   PRO A CG  1 
ATOM   498   C CD  . PRO A  1 65  ? 37.540  23.118 85.879  1.00 65.31  ? 65   PRO A CD  1 
ATOM   499   N N   . MET A  1 66  ? 37.500  20.840 82.798  1.00 67.73  ? 66   MET A N   1 
ATOM   500   C CA  . MET A  1 66  ? 37.153  20.115 81.570  1.00 68.48  ? 66   MET A CA  1 
ATOM   501   C C   . MET A  1 66  ? 38.051  20.528 80.402  1.00 67.14  ? 66   MET A C   1 
ATOM   502   O O   . MET A  1 66  ? 38.146  19.818 79.399  1.00 68.08  ? 66   MET A O   1 
ATOM   503   C CB  . MET A  1 66  ? 35.697  20.389 81.180  1.00 67.68  ? 66   MET A CB  1 
ATOM   504   C CG  . MET A  1 66  ? 34.667  20.084 82.255  1.00 69.12  ? 66   MET A CG  1 
ATOM   505   S SD  . MET A  1 66  ? 34.657  18.349 82.735  1.00 73.23  ? 66   MET A SD  1 
ATOM   506   C CE  . MET A  1 66  ? 32.971  18.176 83.315  1.00 74.52  ? 66   MET A CE  1 
ATOM   507   N N   . CYS A  1 67  ? 38.695  21.683 80.537  1.00 65.14  ? 67   CYS A N   1 
ATOM   508   C CA  . CYS A  1 67  ? 39.548  22.236 79.494  1.00 63.85  ? 67   CYS A CA  1 
ATOM   509   C C   . CYS A  1 67  ? 41.027  21.981 79.790  1.00 65.27  ? 67   CYS A C   1 
ATOM   510   O O   . CYS A  1 67  ? 41.887  22.812 79.487  1.00 64.16  ? 67   CYS A O   1 
ATOM   511   C CB  . CYS A  1 67  ? 39.258  23.730 79.370  1.00 61.02  ? 67   CYS A CB  1 
ATOM   512   S SG  . CYS A  1 67  ? 37.486  24.065 79.212  1.00 59.87  ? 67   CYS A SG  1 
ATOM   513   N N   . ASP A  1 68  ? 41.309  20.817 80.377  1.00 68.04  ? 68   ASP A N   1 
ATOM   514   C CA  . ASP A  1 68  ? 42.678  20.369 80.639  1.00 70.04  ? 68   ASP A CA  1 
ATOM   515   C C   . ASP A  1 68  ? 43.468  20.158 79.350  1.00 70.54  ? 68   ASP A C   1 
ATOM   516   O O   . ASP A  1 68  ? 44.695  20.179 79.364  1.00 71.69  ? 68   ASP A O   1 
ATOM   517   C CB  . ASP A  1 68  ? 42.677  19.061 81.447  1.00 73.19  ? 68   ASP A CB  1 
ATOM   518   C CG  . ASP A  1 68  ? 42.429  19.282 82.932  1.00 73.27  ? 68   ASP A CG  1 
ATOM   519   O OD1 . ASP A  1 68  ? 42.195  20.434 83.349  1.00 70.93  ? 68   ASP A OD1 1 
ATOM   520   O OD2 . ASP A  1 68  ? 42.473  18.293 83.694  1.00 75.88  ? 68   ASP A OD2 1 
ATOM   521   N N   . GLU A  1 69  ? 42.769  19.938 78.242  1.00 69.95  ? 69   GLU A N   1 
ATOM   522   C CA  . GLU A  1 69  ? 43.418  19.858 76.939  1.00 70.13  ? 69   GLU A CA  1 
ATOM   523   C C   . GLU A  1 69  ? 44.182  21.146 76.617  1.00 68.12  ? 69   GLU A C   1 
ATOM   524   O O   . GLU A  1 69  ? 45.227  21.103 75.966  1.00 69.03  ? 69   GLU A O   1 
ATOM   525   C CB  . GLU A  1 69  ? 42.380  19.580 75.850  1.00 69.37  ? 69   GLU A CB  1 
ATOM   526   C CG  . GLU A  1 69  ? 42.970  19.381 74.461  1.00 69.72  ? 69   GLU A CG  1 
ATOM   527   C CD  . GLU A  1 69  ? 41.923  19.057 73.410  1.00 69.15  ? 69   GLU A CD  1 
ATOM   528   O OE1 . GLU A  1 69  ? 40.762  18.765 73.775  1.00 69.14  ? 69   GLU A OE1 1 
ATOM   529   O OE2 . GLU A  1 69  ? 42.268  19.092 72.209  1.00 68.87  ? 69   GLU A OE2 1 
ATOM   530   N N   . PHE A  1 70  ? 43.668  22.277 77.102  1.00 65.74  ? 70   PHE A N   1 
ATOM   531   C CA  . PHE A  1 70  ? 44.156  23.598 76.705  1.00 63.73  ? 70   PHE A CA  1 
ATOM   532   C C   . PHE A  1 70  ? 45.012  24.317 77.764  1.00 63.99  ? 70   PHE A C   1 
ATOM   533   O O   . PHE A  1 70  ? 45.066  25.547 77.793  1.00 62.13  ? 70   PHE A O   1 
ATOM   534   C CB  . PHE A  1 70  ? 42.959  24.459 76.276  1.00 60.97  ? 70   PHE A CB  1 
ATOM   535   C CG  . PHE A  1 70  ? 42.007  23.741 75.354  1.00 60.91  ? 70   PHE A CG  1 
ATOM   536   C CD1 . PHE A  1 70  ? 42.406  23.376 74.076  1.00 61.26  ? 70   PHE A CD1 1 
ATOM   537   C CD2 . PHE A  1 70  ? 40.727  23.398 75.773  1.00 60.81  ? 70   PHE A CD2 1 
ATOM   538   C CE1 . PHE A  1 70  ? 41.542  22.703 73.229  1.00 61.40  ? 70   PHE A CE1 1 
ATOM   539   C CE2 . PHE A  1 70  ? 39.858  22.725 74.930  1.00 61.09  ? 70   PHE A CE2 1 
ATOM   540   C CZ  . PHE A  1 70  ? 40.267  22.375 73.656  1.00 61.34  ? 70   PHE A CZ  1 
ATOM   541   N N   . ILE A  1 71  ? 45.686  23.549 78.620  1.00 66.53  ? 71   ILE A N   1 
ATOM   542   C CA  . ILE A  1 71  ? 46.756  24.089 79.480  1.00 67.40  ? 71   ILE A CA  1 
ATOM   543   C C   . ILE A  1 71  ? 48.064  24.097 78.679  1.00 68.91  ? 71   ILE A C   1 
ATOM   544   O O   . ILE A  1 71  ? 48.420  23.092 78.056  1.00 70.98  ? 71   ILE A O   1 
ATOM   545   C CB  . ILE A  1 71  ? 46.916  23.302 80.815  1.00 69.52  ? 71   ILE A CB  1 
ATOM   546   C CG1 . ILE A  1 71  ? 48.260  23.611 81.496  1.00 71.09  ? 71   ILE A CG1 1 
ATOM   547   C CG2 . ILE A  1 71  ? 46.808  21.794 80.606  1.00 71.98  ? 71   ILE A CG2 1 
ATOM   548   C CD1 . ILE A  1 71  ? 48.312  23.231 82.963  1.00 72.44  ? 71   ILE A CD1 1 
ATOM   549   N N   . ASN A  1 72  ? 48.768  25.232 78.691  1.00 68.25  ? 72   ASN A N   1 
ATOM   550   C CA  . ASN A  1 72  ? 49.997  25.423 77.901  1.00 69.64  ? 72   ASN A CA  1 
ATOM   551   C C   . ASN A  1 72  ? 49.832  25.096 76.410  1.00 69.34  ? 72   ASN A C   1 
ATOM   552   O O   . ASN A  1 72  ? 50.576  24.286 75.856  1.00 71.74  ? 72   ASN A O   1 
ATOM   553   C CB  . ASN A  1 72  ? 51.161  24.613 78.500  1.00 73.12  ? 72   ASN A CB  1 
ATOM   554   C CG  . ASN A  1 72  ? 51.615  25.148 79.846  1.00 73.66  ? 72   ASN A CG  1 
ATOM   555   O OD1 . ASN A  1 72  ? 51.096  26.153 80.337  1.00 71.53  ? 72   ASN A OD1 1 
ATOM   556   N ND2 . ASN A  1 72  ? 52.593  24.477 80.451  1.00 76.75  ? 72   ASN A ND2 1 
ATOM   557   N N   . VAL A  1 73  ? 48.855  25.728 75.765  1.00 66.53  ? 73   VAL A N   1 
ATOM   558   C CA  . VAL A  1 73  ? 48.586  25.480 74.340  1.00 65.92  ? 73   VAL A CA  1 
ATOM   559   C C   . VAL A  1 73  ? 49.723  25.953 73.430  1.00 66.64  ? 73   VAL A C   1 
ATOM   560   O O   . VAL A  1 73  ? 50.385  26.949 73.731  1.00 66.54  ? 73   VAL A O   1 
ATOM   561   C CB  . VAL A  1 73  ? 47.271  26.140 73.854  1.00 62.80  ? 73   VAL A CB  1 
ATOM   562   C CG1 . VAL A  1 73  ? 46.066  25.412 74.425  1.00 62.49  ? 73   VAL A CG1 1 
ATOM   563   C CG2 . VAL A  1 73  ? 47.225  27.628 74.194  1.00 60.88  ? 73   VAL A CG2 1 
ATOM   564   N N   . PRO A  1 74  ? 49.946  25.244 72.307  1.00 67.57  ? 74   PRO A N   1 
ATOM   565   C CA  . PRO A  1 74  ? 50.897  25.723 71.312  1.00 68.14  ? 74   PRO A CA  1 
ATOM   566   C C   . PRO A  1 74  ? 50.298  26.882 70.521  1.00 65.03  ? 74   PRO A C   1 
ATOM   567   O O   . PRO A  1 74  ? 49.083  27.110 70.578  1.00 62.61  ? 74   PRO A O   1 
ATOM   568   C CB  . PRO A  1 74  ? 51.102  24.505 70.411  1.00 70.20  ? 74   PRO A CB  1 
ATOM   569   C CG  . PRO A  1 74  ? 49.810  23.771 70.484  1.00 69.12  ? 74   PRO A CG  1 
ATOM   570   C CD  . PRO A  1 74  ? 49.253  24.019 71.861  1.00 68.20  ? 74   PRO A CD  1 
ATOM   571   N N   . GLU A  1 75  ? 51.138  27.605 69.787  1.00 65.28  ? 75   GLU A N   1 
ATOM   572   C CA  . GLU A  1 75  ? 50.667  28.755 69.024  1.00 62.65  ? 75   GLU A CA  1 
ATOM   573   C C   . GLU A  1 75  ? 49.679  28.319 67.943  1.00 60.94  ? 75   GLU A C   1 
ATOM   574   O O   . GLU A  1 75  ? 49.763  27.206 67.418  1.00 62.33  ? 75   GLU A O   1 
ATOM   575   C CB  . GLU A  1 75  ? 51.831  29.543 68.418  1.00 63.87  ? 75   GLU A CB  1 
ATOM   576   C CG  . GLU A  1 75  ? 52.354  29.017 67.094  1.00 65.21  ? 75   GLU A CG  1 
ATOM   577   C CD  . GLU A  1 75  ? 53.418  29.920 66.510  1.00 66.40  ? 75   GLU A CD  1 
ATOM   578   O OE1 . GLU A  1 75  ? 54.494  30.066 67.134  1.00 68.89  ? 75   GLU A OE1 1 
ATOM   579   O OE2 . GLU A  1 75  ? 53.174  30.488 65.426  1.00 65.03  ? 75   GLU A OE2 1 
ATOM   580   N N   . TRP A  1 76  ? 48.750  29.214 67.624  1.00 58.08  ? 76   TRP A N   1 
ATOM   581   C CA  . TRP A  1 76  ? 47.647  28.912 66.720  1.00 56.27  ? 76   TRP A CA  1 
ATOM   582   C C   . TRP A  1 76  ? 47.610  29.918 65.578  1.00 54.68  ? 76   TRP A C   1 
ATOM   583   O O   . TRP A  1 76  ? 47.991  31.076 65.748  1.00 54.19  ? 76   TRP A O   1 
ATOM   584   C CB  . TRP A  1 76  ? 46.317  28.945 67.481  1.00 54.51  ? 76   TRP A CB  1 
ATOM   585   C CG  . TRP A  1 76  ? 46.046  30.266 68.155  1.00 52.95  ? 76   TRP A CG  1 
ATOM   586   C CD1 . TRP A  1 76  ? 45.412  31.351 67.615  1.00 50.88  ? 76   TRP A CD1 1 
ATOM   587   C CD2 . TRP A  1 76  ? 46.420  30.645 69.487  1.00 53.59  ? 76   TRP A CD2 1 
ATOM   588   N NE1 . TRP A  1 76  ? 45.366  32.378 68.529  1.00 50.33  ? 76   TRP A NE1 1 
ATOM   589   C CE2 . TRP A  1 76  ? 45.976  31.971 69.686  1.00 51.90  ? 76   TRP A CE2 1 
ATOM   590   C CE3 . TRP A  1 76  ? 47.088  29.992 70.530  1.00 55.56  ? 76   TRP A CE3 1 
ATOM   591   C CZ2 . TRP A  1 76  ? 46.173  32.654 70.888  1.00 52.13  ? 76   TRP A CZ2 1 
ATOM   592   C CZ3 . TRP A  1 76  ? 47.285  30.671 71.724  1.00 55.64  ? 76   TRP A CZ3 1 
ATOM   593   C CH2 . TRP A  1 76  ? 46.830  31.989 71.893  1.00 53.93  ? 76   TRP A CH2 1 
ATOM   594   N N   . SER A  1 77  ? 47.154  29.465 64.414  1.00 54.03  ? 77   SER A N   1 
ATOM   595   C CA  . SER A  1 77  ? 46.908  30.349 63.276  1.00 52.29  ? 77   SER A CA  1 
ATOM   596   C C   . SER A  1 77  ? 45.620  31.132 63.510  1.00 49.65  ? 77   SER A C   1 
ATOM   597   O O   . SER A  1 77  ? 45.563  32.344 63.295  1.00 48.43  ? 77   SER A O   1 
ATOM   598   C CB  . SER A  1 77  ? 46.794  29.532 61.992  1.00 52.63  ? 77   SER A CB  1 
ATOM   599   O OG  . SER A  1 77  ? 46.016  28.366 62.204  1.00 52.94  ? 77   SER A OG  1 
ATOM   600   N N   . TYR A  1 78  ? 44.588  30.418 63.952  1.00 49.06  ? 78   TYR A N   1 
ATOM   601   C CA  . TYR A  1 78  ? 43.310  31.020 64.321  1.00 47.03  ? 78   TYR A CA  1 
ATOM   602   C C   . TYR A  1 78  ? 42.628  30.151 65.380  1.00 47.55  ? 78   TYR A C   1 
ATOM   603   O O   . TYR A  1 78  ? 43.065  29.031 65.637  1.00 49.32  ? 78   TYR A O   1 
ATOM   604   C CB  . TYR A  1 78  ? 42.418  31.186 63.083  1.00 45.43  ? 78   TYR A CB  1 
ATOM   605   C CG  . TYR A  1 78  ? 42.072  29.889 62.374  1.00 46.12  ? 78   TYR A CG  1 
ATOM   606   C CD1 . TYR A  1 78  ? 42.975  29.281 61.498  1.00 47.44  ? 78   TYR A CD1 1 
ATOM   607   C CD2 . TYR A  1 78  ? 40.840  29.272 62.576  1.00 45.76  ? 78   TYR A CD2 1 
ATOM   608   C CE1 . TYR A  1 78  ? 42.659  28.094 60.849  1.00 48.35  ? 78   TYR A CE1 1 
ATOM   609   C CE2 . TYR A  1 78  ? 40.518  28.086 61.935  1.00 46.72  ? 78   TYR A CE2 1 
ATOM   610   C CZ  . TYR A  1 78  ? 41.430  27.500 61.071  1.00 47.99  ? 78   TYR A CZ  1 
ATOM   611   O OH  . TYR A  1 78  ? 41.104  26.322 60.440  1.00 49.19  ? 78   TYR A OH  1 
ATOM   612   N N   . ILE A  1 79  ? 41.565  30.671 65.988  1.00 46.25  ? 79   ILE A N   1 
ATOM   613   C CA  . ILE A  1 79  ? 40.837  29.957 67.039  1.00 46.83  ? 79   ILE A CA  1 
ATOM   614   C C   . ILE A  1 79  ? 39.454  29.543 66.548  1.00 46.13  ? 79   ILE A C   1 
ATOM   615   O O   . ILE A  1 79  ? 38.818  30.274 65.791  1.00 44.64  ? 79   ILE A O   1 
ATOM   616   C CB  . ILE A  1 79  ? 40.697  30.825 68.307  1.00 46.40  ? 79   ILE A CB  1 
ATOM   617   C CG1 . ILE A  1 79  ? 42.080  31.129 68.891  1.00 47.50  ? 79   ILE A CG1 1 
ATOM   618   C CG2 . ILE A  1 79  ? 39.836  30.123 69.351  1.00 47.00  ? 79   ILE A CG2 1 
ATOM   619   C CD1 . ILE A  1 79  ? 42.101  32.276 69.878  1.00 47.00  ? 79   ILE A CD1 1 
ATOM   620   N N   . VAL A  1 80  ? 38.995  28.371 66.981  1.00 47.46  ? 80   VAL A N   1 
ATOM   621   C CA  . VAL A  1 80  ? 37.667  27.875 66.621  1.00 47.33  ? 80   VAL A CA  1 
ATOM   622   C C   . VAL A  1 80  ? 36.846  27.595 67.878  1.00 48.04  ? 80   VAL A C   1 
ATOM   623   O O   . VAL A  1 80  ? 37.244  26.799 68.731  1.00 49.68  ? 80   VAL A O   1 
ATOM   624   C CB  . VAL A  1 80  ? 37.743  26.598 65.759  1.00 48.73  ? 80   VAL A CB  1 
ATOM   625   C CG1 . VAL A  1 80  ? 36.349  26.157 65.323  1.00 48.70  ? 80   VAL A CG1 1 
ATOM   626   C CG2 . VAL A  1 80  ? 38.623  26.835 64.543  1.00 48.29  ? 80   VAL A CG2 1 
ATOM   627   N N   . GLU A  1 81  ? 35.692  28.250 67.966  1.00 47.03  ? 81   GLU A N   1 
ATOM   628   C CA  . GLU A  1 81  ? 34.797  28.139 69.107  1.00 47.73  ? 81   GLU A CA  1 
ATOM   629   C C   . GLU A  1 81  ? 33.388  27.860 68.602  1.00 47.94  ? 81   GLU A C   1 
ATOM   630   O O   . GLU A  1 81  ? 32.971  28.414 67.591  1.00 46.77  ? 81   GLU A O   1 
ATOM   631   C CB  . GLU A  1 81  ? 34.818  29.445 69.905  1.00 46.62  ? 81   GLU A CB  1 
ATOM   632   C CG  . GLU A  1 81  ? 34.044  29.408 71.215  1.00 47.43  ? 81   GLU A CG  1 
ATOM   633   C CD  . GLU A  1 81  ? 33.974  30.761 71.905  1.00 46.47  ? 81   GLU A CD  1 
ATOM   634   O OE1 . GLU A  1 81  ? 33.772  31.783 71.208  1.00 45.15  ? 81   GLU A OE1 1 
ATOM   635   O OE2 . GLU A  1 81  ? 34.115  30.801 73.149  1.00 47.17  ? 81   GLU A OE2 1 
ATOM   636   N N   . LYS A  1 82  ? 32.653  27.009 69.308  1.00 49.67  ? 82   LYS A N   1 
ATOM   637   C CA  . LYS A  1 82  ? 31.265  26.720 68.949  1.00 50.35  ? 82   LYS A CA  1 
ATOM   638   C C   . LYS A  1 82  ? 30.337  27.892 69.284  1.00 49.42  ? 82   LYS A C   1 
ATOM   639   O O   . LYS A  1 82  ? 30.725  28.834 69.980  1.00 48.48  ? 82   LYS A O   1 
ATOM   640   C CB  . LYS A  1 82  ? 30.783  25.444 69.648  1.00 52.86  ? 82   LYS A CB  1 
ATOM   641   C CG  . LYS A  1 82  ? 31.255  24.169 68.972  1.00 54.36  ? 82   LYS A CG  1 
ATOM   642   C CD  . LYS A  1 82  ? 30.753  22.929 69.693  1.00 57.18  ? 82   LYS A CD  1 
ATOM   643   C CE  . LYS A  1 82  ? 30.892  21.685 68.829  1.00 59.04  ? 82   LYS A CE  1 
ATOM   644   N NZ  . LYS A  1 82  ? 32.305  21.234 68.706  1.00 59.40  ? 82   LYS A NZ  1 
ATOM   645   N N   . ALA A  1 83  ? 29.113  27.825 68.771  1.00 49.98  ? 83   ALA A N   1 
ATOM   646   C CA  . ALA A  1 83  ? 28.107  28.852 69.031  1.00 49.62  ? 83   ALA A CA  1 
ATOM   647   C C   . ALA A  1 83  ? 27.646  28.836 70.492  1.00 51.04  ? 83   ALA A C   1 
ATOM   648   O O   . ALA A  1 83  ? 27.450  29.895 71.092  1.00 50.46  ? 83   ALA A O   1 
ATOM   649   C CB  . ALA A  1 83  ? 26.918  28.679 68.095  1.00 50.18  ? 83   ALA A CB  1 
ATOM   650   N N   . ASN A  1 84  ? 27.485  27.638 71.060  1.00 53.13  ? 84   ASN A N   1 
ATOM   651   C CA  . ASN A  1 84  ? 27.035  27.487 72.446  1.00 54.73  ? 84   ASN A CA  1 
ATOM   652   C C   . ASN A  1 84  ? 27.831  26.420 73.212  1.00 56.05  ? 84   ASN A C   1 
ATOM   653   O O   . ASN A  1 84  ? 27.276  25.388 73.601  1.00 58.35  ? 84   ASN A O   1 
ATOM   654   C CB  . ASN A  1 84  ? 25.537  27.151 72.474  1.00 56.75  ? 84   ASN A CB  1 
ATOM   655   C CG  . ASN A  1 84  ? 24.691  28.189 71.749  1.00 55.88  ? 84   ASN A CG  1 
ATOM   656   O OD1 . ASN A  1 84  ? 24.661  29.361 72.135  1.00 54.83  ? 84   ASN A OD1 1 
ATOM   657   N ND2 . ASN A  1 84  ? 24.002  27.765 70.687  1.00 56.52  ? 84   ASN A ND2 1 
ATOM   658   N N   . PRO A  1 85  ? 29.134  26.673 73.449  1.00 54.88  ? 85   PRO A N   1 
ATOM   659   C CA  . PRO A  1 85  ? 29.973  25.686 74.137  1.00 56.24  ? 85   PRO A CA  1 
ATOM   660   C C   . PRO A  1 85  ? 29.481  25.384 75.549  1.00 57.99  ? 85   PRO A C   1 
ATOM   661   O O   . PRO A  1 85  ? 29.220  26.311 76.318  1.00 57.35  ? 85   PRO A O   1 
ATOM   662   C CB  . PRO A  1 85  ? 31.356  26.358 74.181  1.00 54.53  ? 85   PRO A CB  1 
ATOM   663   C CG  . PRO A  1 85  ? 31.311  27.428 73.147  1.00 52.42  ? 85   PRO A CG  1 
ATOM   664   C CD  . PRO A  1 85  ? 29.889  27.896 73.128  1.00 52.54  ? 85   PRO A CD  1 
ATOM   665   N N   . VAL A  1 86  ? 29.360  24.098 75.879  1.00 60.39  ? 86   VAL A N   1 
ATOM   666   C CA  . VAL A  1 86  ? 28.848  23.678 77.191  1.00 62.39  ? 86   VAL A CA  1 
ATOM   667   C C   . VAL A  1 86  ? 29.822  23.962 78.342  1.00 61.96  ? 86   VAL A C   1 
ATOM   668   O O   . VAL A  1 86  ? 29.392  24.325 79.439  1.00 62.53  ? 86   VAL A O   1 
ATOM   669   C CB  . VAL A  1 86  ? 28.445  22.179 77.221  1.00 65.44  ? 86   VAL A CB  1 
ATOM   670   C CG1 . VAL A  1 86  ? 27.355  21.898 76.195  1.00 66.24  ? 86   VAL A CG1 1 
ATOM   671   C CG2 . VAL A  1 86  ? 29.647  21.262 77.006  1.00 66.14  ? 86   VAL A CG2 1 
ATOM   672   N N   . ASN A  1 87  ? 31.121  23.790 78.092  1.00 61.20  ? 87   ASN A N   1 
ATOM   673   C CA  . ASN A  1 87  ? 32.149  24.007 79.116  1.00 60.95  ? 87   ASN A CA  1 
ATOM   674   C C   . ASN A  1 87  ? 32.588  25.467 79.165  1.00 58.46  ? 87   ASN A C   1 
ATOM   675   O O   . ASN A  1 87  ? 33.695  25.814 78.744  1.00 57.33  ? 87   ASN A O   1 
ATOM   676   C CB  . ASN A  1 87  ? 33.366  23.103 78.874  1.00 61.90  ? 87   ASN A CB  1 
ATOM   677   C CG  . ASN A  1 87  ? 33.092  21.644 79.194  1.00 64.89  ? 87   ASN A CG  1 
ATOM   678   O OD1 . ASN A  1 87  ? 32.240  21.321 80.024  1.00 66.40  ? 87   ASN A OD1 1 
ATOM   679   N ND2 . ASN A  1 87  ? 33.831  20.750 78.543  1.00 66.04  ? 87   ASN A ND2 1 
ATOM   680   N N   . ASP A  1 88  ? 31.704  26.315 79.682  1.00 57.92  ? 88   ASP A N   1 
ATOM   681   C CA  . ASP A  1 88  ? 31.980  27.737 79.831  1.00 55.97  ? 88   ASP A CA  1 
ATOM   682   C C   . ASP A  1 88  ? 32.331  27.997 81.307  1.00 56.51  ? 88   ASP A C   1 
ATOM   683   O O   . ASP A  1 88  ? 33.300  27.426 81.819  1.00 57.17  ? 88   ASP A O   1 
ATOM   684   C CB  . ASP A  1 88  ? 30.774  28.551 79.330  1.00 55.27  ? 88   ASP A CB  1 
ATOM   685   C CG  . ASP A  1 88  ? 31.074  30.042 79.189  1.00 53.42  ? 88   ASP A CG  1 
ATOM   686   O OD1 . ASP A  1 88  ? 32.249  30.447 79.297  1.00 52.52  ? 88   ASP A OD1 1 
ATOM   687   O OD2 . ASP A  1 88  ? 30.120  30.817 78.970  1.00 53.13  ? 88   ASP A OD2 1 
ATOM   688   N N   . LEU A  1 89  ? 31.554  28.834 81.990  1.00 56.41  ? 89   LEU A N   1 
ATOM   689   C CA  . LEU A  1 89  ? 31.750  29.093 83.411  1.00 57.07  ? 89   LEU A CA  1 
ATOM   690   C C   . LEU A  1 89  ? 31.047  27.995 84.203  1.00 59.29  ? 89   LEU A C   1 
ATOM   691   O O   . LEU A  1 89  ? 29.826  28.031 84.371  1.00 60.24  ? 89   LEU A O   1 
ATOM   692   C CB  . LEU A  1 89  ? 31.199  30.481 83.786  1.00 56.32  ? 89   LEU A CB  1 
ATOM   693   C CG  . LEU A  1 89  ? 32.145  31.696 83.766  1.00 54.77  ? 89   LEU A CG  1 
ATOM   694   C CD1 . LEU A  1 89  ? 33.356  31.517 82.860  1.00 53.69  ? 89   LEU A CD1 1 
ATOM   695   C CD2 . LEU A  1 89  ? 31.377  32.956 83.389  1.00 54.03  ? 89   LEU A CD2 1 
ATOM   696   N N   . CYS A  1 90  ? 31.826  27.020 84.672  1.00 60.38  ? 90   CYS A N   1 
ATOM   697   C CA  . CYS A  1 90  ? 31.287  25.895 85.437  1.00 62.78  ? 90   CYS A CA  1 
ATOM   698   C C   . CYS A  1 90  ? 30.591  26.391 86.702  1.00 63.55  ? 90   CYS A C   1 
ATOM   699   O O   . CYS A  1 90  ? 29.432  26.058 86.947  1.00 65.12  ? 90   CYS A O   1 
ATOM   700   C CB  . CYS A  1 90  ? 32.384  24.875 85.775  1.00 63.91  ? 90   CYS A CB  1 
ATOM   701   S SG  . CYS A  1 90  ? 33.922  25.550 86.450  1.00 62.79  ? 90   CYS A SG  1 
ATOM   702   N N   . TYR A  1 91  ? 31.297  27.196 87.490  1.00 60.29  ? 91   TYR A N   1 
ATOM   703   C CA  . TYR A  1 91  ? 30.679  27.928 88.589  1.00 61.20  ? 91   TYR A CA  1 
ATOM   704   C C   . TYR A  1 91  ? 30.029  29.184 88.001  1.00 58.82  ? 91   TYR A C   1 
ATOM   705   O O   . TYR A  1 91  ? 30.707  29.959 87.320  1.00 55.78  ? 91   TYR A O   1 
ATOM   706   C CB  . TYR A  1 91  ? 31.720  28.312 89.643  1.00 61.11  ? 91   TYR A CB  1 
ATOM   707   C CG  . TYR A  1 91  ? 31.117  28.725 90.970  1.00 63.29  ? 91   TYR A CG  1 
ATOM   708   C CD1 . TYR A  1 91  ? 30.669  30.028 91.180  1.00 62.03  ? 91   TYR A CD1 1 
ATOM   709   C CD2 . TYR A  1 91  ? 30.986  27.810 92.013  1.00 66.95  ? 91   TYR A CD2 1 
ATOM   710   C CE1 . TYR A  1 91  ? 30.112  30.408 92.392  1.00 64.43  ? 91   TYR A CE1 1 
ATOM   711   C CE2 . TYR A  1 91  ? 30.432  28.182 93.229  1.00 69.34  ? 91   TYR A CE2 1 
ATOM   712   C CZ  . TYR A  1 91  ? 29.997  29.481 93.413  1.00 68.09  ? 91   TYR A CZ  1 
ATOM   713   O OH  . TYR A  1 91  ? 29.445  29.853 94.618  1.00 70.84  ? 91   TYR A OH  1 
ATOM   714   N N   . PRO A  1 92  ? 28.723  29.402 88.265  1.00 60.52  ? 92   PRO A N   1 
ATOM   715   C CA  . PRO A  1 92  ? 28.004  30.492 87.589  1.00 58.65  ? 92   PRO A CA  1 
ATOM   716   C C   . PRO A  1 92  ? 28.582  31.871 87.877  1.00 56.26  ? 92   PRO A C   1 
ATOM   717   O O   . PRO A  1 92  ? 29.178  32.088 88.936  1.00 56.94  ? 92   PRO A O   1 
ATOM   718   C CB  . PRO A  1 92  ? 26.581  30.404 88.162  1.00 61.88  ? 92   PRO A CB  1 
ATOM   719   C CG  . PRO A  1 92  ? 26.513  29.118 88.899  1.00 65.44  ? 92   PRO A CG  1 
ATOM   720   C CD  . PRO A  1 92  ? 27.904  28.791 89.325  1.00 64.53  ? 92   PRO A CD  1 
ATOM   721   N N   . GLY A  1 93  ? 28.395  32.793 86.939  1.00 53.80  ? 93   GLY A N   1 
ATOM   722   C CA  . GLY A  1 93  ? 28.878  34.154 87.107  1.00 51.77  ? 93   GLY A CA  1 
ATOM   723   C C   . GLY A  1 93  ? 28.936  34.952 85.822  1.00 48.94  ? 93   GLY A C   1 
ATOM   724   O O   . GLY A  1 93  ? 28.250  34.640 84.845  1.00 48.74  ? 93   GLY A O   1 
ATOM   725   N N   . ASP A  1 94  ? 29.757  35.998 85.842  1.00 47.06  ? 94   ASP A N   1 
ATOM   726   C CA  . ASP A  1 94  ? 29.997  36.838 84.679  1.00 44.50  ? 94   ASP A CA  1 
ATOM   727   C C   . ASP A  1 94  ? 31.487  36.943 84.438  1.00 42.92  ? 94   ASP A C   1 
ATOM   728   O O   . ASP A  1 94  ? 32.298  36.712 85.343  1.00 43.74  ? 94   ASP A O   1 
ATOM   729   C CB  . ASP A  1 94  ? 29.438  38.243 84.899  1.00 44.21  ? 94   ASP A CB  1 
ATOM   730   C CG  . ASP A  1 94  ? 27.938  38.250 85.101  1.00 46.16  ? 94   ASP A CG  1 
ATOM   731   O OD1 . ASP A  1 94  ? 27.204  37.902 84.148  1.00 46.08  ? 94   ASP A OD1 1 
ATOM   732   O OD2 . ASP A  1 94  ? 27.492  38.617 86.211  1.00 48.14  ? 94   ASP A OD2 1 
ATOM   733   N N   . PHE A  1 95  ? 31.834  37.286 83.204  1.00 40.98  ? 95   PHE A N   1 
ATOM   734   C CA  . PHE A  1 95  ? 33.201  37.594 82.831  1.00 39.66  ? 95   PHE A CA  1 
ATOM   735   C C   . PHE A  1 95  ? 33.192  39.052 82.384  1.00 38.20  ? 95   PHE A C   1 
ATOM   736   O O   . PHE A  1 95  ? 32.513  39.412 81.417  1.00 37.31  ? 95   PHE A O   1 
ATOM   737   C CB  . PHE A  1 95  ? 33.659  36.662 81.708  1.00 39.21  ? 95   PHE A CB  1 
ATOM   738   C CG  . PHE A  1 95  ? 35.149  36.483 81.631  1.00 39.02  ? 95   PHE A CG  1 
ATOM   739   C CD1 . PHE A  1 95  ? 35.985  37.558 81.359  1.00 37.93  ? 95   PHE A CD1 1 
ATOM   740   C CD2 . PHE A  1 95  ? 35.715  35.232 81.823  1.00 40.32  ? 95   PHE A CD2 1 
ATOM   741   C CE1 . PHE A  1 95  ? 37.355  37.388 81.282  1.00 38.24  ? 95   PHE A CE1 1 
ATOM   742   C CE2 . PHE A  1 95  ? 37.084  35.056 81.745  1.00 40.55  ? 95   PHE A CE2 1 
ATOM   743   C CZ  . PHE A  1 95  ? 37.907  36.135 81.478  1.00 39.55  ? 95   PHE A CZ  1 
ATOM   744   N N   . ASN A  1 96  ? 33.929  39.888 83.105  1.00 38.22  ? 96   ASN A N   1 
ATOM   745   C CA  . ASN A  1 96  ? 33.909  41.323 82.869  1.00 37.36  ? 96   ASN A CA  1 
ATOM   746   C C   . ASN A  1 96  ? 34.705  41.702 81.624  1.00 35.90  ? 96   ASN A C   1 
ATOM   747   O O   . ASN A  1 96  ? 35.846  41.259 81.457  1.00 35.95  ? 96   ASN A O   1 
ATOM   748   C CB  . ASN A  1 96  ? 34.465  42.059 84.086  1.00 38.39  ? 96   ASN A CB  1 
ATOM   749   C CG  . ASN A  1 96  ? 34.084  43.524 84.099  1.00 38.26  ? 96   ASN A CG  1 
ATOM   750   O OD1 . ASN A  1 96  ? 32.904  43.867 84.239  1.00 38.74  ? 96   ASN A OD1 1 
ATOM   751   N ND2 . ASN A  1 96  ? 35.076  44.401 83.955  1.00 37.95  ? 96   ASN A ND2 1 
ATOM   752   N N   . ASP A  1 97  ? 34.102  42.535 80.772  1.00 34.94  ? 97   ASP A N   1 
ATOM   753   C CA  . ASP A  1 97  ? 34.681  42.937 79.482  1.00 33.80  ? 97   ASP A CA  1 
ATOM   754   C C   . ASP A  1 97  ? 35.193  41.729 78.698  1.00 33.55  ? 97   ASP A C   1 
ATOM   755   O O   . ASP A  1 97  ? 36.324  41.721 78.197  1.00 33.54  ? 97   ASP A O   1 
ATOM   756   C CB  . ASP A  1 97  ? 35.791  43.982 79.680  1.00 34.01  ? 97   ASP A CB  1 
ATOM   757   C CG  . ASP A  1 97  ? 35.250  45.360 80.047  1.00 34.25  ? 97   ASP A CG  1 
ATOM   758   O OD1 . ASP A  1 97  ? 34.056  45.628 79.822  1.00 34.09  ? 97   ASP A OD1 1 
ATOM   759   O OD2 . ASP A  1 97  ? 36.031  46.186 80.558  1.00 34.96  ? 97   ASP A OD2 1 
ATOM   760   N N   . TYR A  1 98  ? 34.344  40.711 78.610  1.00 33.71  ? 98   TYR A N   1 
ATOM   761   C CA  . TYR A  1 98  ? 34.678  39.443 77.962  1.00 33.93  ? 98   TYR A CA  1 
ATOM   762   C C   . TYR A  1 98  ? 34.873  39.623 76.457  1.00 33.15  ? 98   TYR A C   1 
ATOM   763   O O   . TYR A  1 98  ? 35.779  39.032 75.862  1.00 33.48  ? 98   TYR A O   1 
ATOM   764   C CB  . TYR A  1 98  ? 33.553  38.444 78.243  1.00 34.78  ? 98   TYR A CB  1 
ATOM   765   C CG  . TYR A  1 98  ? 33.753  37.033 77.728  1.00 35.58  ? 98   TYR A CG  1 
ATOM   766   C CD1 . TYR A  1 98  ? 34.965  36.362 77.890  1.00 36.18  ? 98   TYR A CD1 1 
ATOM   767   C CD2 . TYR A  1 98  ? 32.701  36.347 77.116  1.00 36.12  ? 98   TYR A CD2 1 
ATOM   768   C CE1 . TYR A  1 98  ? 35.130  35.062 77.429  1.00 37.27  ? 98   TYR A CE1 1 
ATOM   769   C CE2 . TYR A  1 98  ? 32.857  35.051 76.657  1.00 37.22  ? 98   TYR A CE2 1 
ATOM   770   C CZ  . TYR A  1 98  ? 34.070  34.412 76.815  1.00 37.79  ? 98   TYR A CZ  1 
ATOM   771   O OH  . TYR A  1 98  ? 34.216  33.126 76.353  1.00 39.22  ? 98   TYR A OH  1 
ATOM   772   N N   . GLU A  1 99  ? 34.027  40.459 75.859  1.00 32.37  ? 99   GLU A N   1 
ATOM   773   C CA  . GLU A  1 99  ? 34.051  40.697 74.420  1.00 31.84  ? 99   GLU A CA  1 
ATOM   774   C C   . GLU A  1 99  ? 35.273  41.524 74.021  1.00 31.61  ? 99   GLU A C   1 
ATOM   775   O O   . GLU A  1 99  ? 35.873  41.295 72.970  1.00 31.81  ? 99   GLU A O   1 
ATOM   776   C CB  . GLU A  1 99  ? 32.767  41.400 73.966  1.00 31.41  ? 99   GLU A CB  1 
ATOM   777   C CG  . GLU A  1 99  ? 31.515  40.531 74.015  1.00 32.08  ? 99   GLU A CG  1 
ATOM   778   C CD  . GLU A  1 99  ? 30.990  40.299 75.424  1.00 32.83  ? 99   GLU A CD  1 
ATOM   779   O OE1 . GLU A  1 99  ? 31.077  41.223 76.269  1.00 32.68  ? 99   GLU A OE1 1 
ATOM   780   O OE2 . GLU A  1 99  ? 30.482  39.190 75.683  1.00 33.87  ? 99   GLU A OE2 1 
ATOM   781   N N   . GLU A  1 100 ? 35.632  42.488 74.865  1.00 31.53  ? 100  GLU A N   1 
ATOM   782   C CA  . GLU A  1 100 ? 36.848  43.271 74.662  1.00 31.83  ? 100  GLU A CA  1 
ATOM   783   C C   . GLU A  1 100 ? 38.103  42.402 74.787  1.00 32.76  ? 100  GLU A C   1 
ATOM   784   O O   . GLU A  1 100 ? 39.094  42.636 74.095  1.00 33.42  ? 100  GLU A O   1 
ATOM   785   C CB  . GLU A  1 100 ? 36.908  44.437 75.651  1.00 31.95  ? 100  GLU A CB  1 
ATOM   786   C CG  . GLU A  1 100 ? 35.980  45.586 75.298  1.00 31.47  ? 100  GLU A CG  1 
ATOM   787   C CD  . GLU A  1 100 ? 36.442  46.354 74.073  1.00 31.54  ? 100  GLU A CD  1 
ATOM   788   O OE1 . GLU A  1 100 ? 37.639  46.697 73.997  1.00 32.35  ? 100  GLU A OE1 1 
ATOM   789   O OE2 . GLU A  1 100 ? 35.607  46.625 73.184  1.00 31.07  ? 100  GLU A OE2 1 
ATOM   790   N N   . LEU A  1 101 ? 38.058  41.405 75.667  1.00 33.14  ? 101  LEU A N   1 
ATOM   791   C CA  . LEU A  1 101 ? 39.172  40.469 75.814  1.00 34.30  ? 101  LEU A CA  1 
ATOM   792   C C   . LEU A  1 101 ? 39.253  39.554 74.600  1.00 34.67  ? 101  LEU A C   1 
ATOM   793   O O   . LEU A  1 101 ? 40.336  39.324 74.061  1.00 35.75  ? 101  LEU A O   1 
ATOM   794   C CB  . LEU A  1 101 ? 39.027  39.633 77.093  1.00 34.86  ? 101  LEU A CB  1 
ATOM   795   C CG  . LEU A  1 101 ? 40.166  38.657 77.411  1.00 36.34  ? 101  LEU A CG  1 
ATOM   796   C CD1 . LEU A  1 101 ? 41.525  39.341 77.343  1.00 37.22  ? 101  LEU A CD1 1 
ATOM   797   C CD2 . LEU A  1 101 ? 39.952  38.039 78.783  1.00 37.02  ? 101  LEU A CD2 1 
ATOM   798   N N   . LYS A  1 102 ? 38.103  39.028 74.188  1.00 34.13  ? 102  LYS A N   1 
ATOM   799   C CA  . LYS A  1 102 ? 38.008  38.224 72.970  1.00 34.67  ? 102  LYS A CA  1 
ATOM   800   C C   . LYS A  1 102 ? 38.512  38.988 71.746  1.00 34.71  ? 102  LYS A C   1 
ATOM   801   O O   . LYS A  1 102 ? 39.127  38.409 70.852  1.00 35.89  ? 102  LYS A O   1 
ATOM   802   C CB  . LYS A  1 102 ? 36.567  37.777 72.736  1.00 34.24  ? 102  LYS A CB  1 
ATOM   803   C CG  . LYS A  1 102 ? 36.214  36.445 73.372  1.00 35.25  ? 102  LYS A CG  1 
ATOM   804   C CD  . LYS A  1 102 ? 34.712  36.207 73.312  1.00 35.14  ? 102  LYS A CD  1 
ATOM   805   C CE  . LYS A  1 102 ? 34.374  34.768 72.948  1.00 36.67  ? 102  LYS A CE  1 
ATOM   806   N NZ  . LYS A  1 102 ? 32.952  34.655 72.521  1.00 36.86  ? 102  LYS A NZ  1 
ATOM   807   N N   . HIS A  1 103 ? 38.244  40.288 71.707  1.00 33.77  ? 103  HIS A N   1 
ATOM   808   C CA  . HIS A  1 103 ? 38.747  41.123 70.630  1.00 34.10  ? 103  HIS A CA  1 
ATOM   809   C C   . HIS A  1 103 ? 40.269  41.204 70.678  1.00 35.64  ? 103  HIS A C   1 
ATOM   810   O O   . HIS A  1 103 ? 40.925  41.219 69.644  1.00 36.85  ? 103  HIS A O   1 
ATOM   811   C CB  . HIS A  1 103 ? 38.142  42.528 70.697  1.00 33.05  ? 103  HIS A CB  1 
ATOM   812   C CG  . HIS A  1 103 ? 38.651  43.445 69.630  1.00 33.63  ? 103  HIS A CG  1 
ATOM   813   N ND1 . HIS A  1 103 ? 38.173  43.420 68.338  1.00 33.74  ? 103  HIS A ND1 1 
ATOM   814   C CD2 . HIS A  1 103 ? 39.616  44.393 69.657  1.00 34.49  ? 103  HIS A CD2 1 
ATOM   815   C CE1 . HIS A  1 103 ? 38.812  44.323 67.618  1.00 34.63  ? 103  HIS A CE1 1 
ATOM   816   N NE2 . HIS A  1 103 ? 39.694  44.926 68.394  1.00 35.15  ? 103  HIS A NE2 1 
ATOM   817   N N   . LEU A  1 104 ? 40.819  41.255 71.886  1.00 35.96  ? 104  LEU A N   1 
ATOM   818   C CA  . LEU A  1 104 ? 42.269  41.298 72.083  1.00 37.80  ? 104  LEU A CA  1 
ATOM   819   C C   . LEU A  1 104 ? 42.943  40.048 71.506  1.00 39.49  ? 104  LEU A C   1 
ATOM   820   O O   . LEU A  1 104 ? 44.047  40.125 70.970  1.00 41.37  ? 104  LEU A O   1 
ATOM   821   C CB  . LEU A  1 104 ? 42.596  41.434 73.580  1.00 37.88  ? 104  LEU A CB  1 
ATOM   822   C CG  . LEU A  1 104 ? 43.573  42.534 74.004  1.00 39.00  ? 104  LEU A CG  1 
ATOM   823   C CD1 . LEU A  1 104 ? 43.057  43.910 73.609  1.00 38.21  ? 104  LEU A CD1 1 
ATOM   824   C CD2 . LEU A  1 104 ? 43.786  42.467 75.507  1.00 39.22  ? 104  LEU A CD2 1 
ATOM   825   N N   . LEU A  1 105 ? 42.259  38.910 71.615  1.00 39.21  ? 105  LEU A N   1 
ATOM   826   C CA  . LEU A  1 105 ? 42.741  37.630 71.081  1.00 41.02  ? 105  LEU A CA  1 
ATOM   827   C C   . LEU A  1 105 ? 42.877  37.589 69.566  1.00 42.13  ? 105  LEU A C   1 
ATOM   828   O O   . LEU A  1 105 ? 43.620  36.759 69.041  1.00 44.28  ? 105  LEU A O   1 
ATOM   829   C CB  . LEU A  1 105 ? 41.809  36.491 71.495  1.00 40.53  ? 105  LEU A CB  1 
ATOM   830   C CG  . LEU A  1 105 ? 41.979  35.904 72.887  1.00 40.80  ? 105  LEU A CG  1 
ATOM   831   C CD1 . LEU A  1 105 ? 40.854  34.914 73.145  1.00 40.47  ? 105  LEU A CD1 1 
ATOM   832   C CD2 . LEU A  1 105 ? 43.336  35.228 73.017  1.00 43.16  ? 105  LEU A CD2 1 
ATOM   833   N N   . SER A  1 106 ? 42.145  38.451 68.862  1.00 41.01  ? 106  SER A N   1 
ATOM   834   C CA  . SER A  1 106 ? 42.281  38.550 67.410  1.00 42.27  ? 106  SER A CA  1 
ATOM   835   C C   . SER A  1 106 ? 43.660  39.089 67.005  1.00 44.44  ? 106  SER A C   1 
ATOM   836   O O   . SER A  1 106 ? 44.088  38.899 65.867  1.00 46.39  ? 106  SER A O   1 
ATOM   837   C CB  . SER A  1 106 ? 41.163  39.415 66.804  1.00 40.69  ? 106  SER A CB  1 
ATOM   838   O OG  . SER A  1 106 ? 41.305  40.786 67.139  1.00 39.95  ? 106  SER A OG  1 
ATOM   839   N N   . ARG A  1 107 ? 44.342  39.764 67.933  1.00 44.50  ? 107  ARG A N   1 
ATOM   840   C CA  . ARG A  1 107 ? 45.721  40.235 67.721  1.00 47.04  ? 107  ARG A CA  1 
ATOM   841   C C   . ARG A  1 107 ? 46.782  39.303 68.321  1.00 49.01  ? 107  ARG A C   1 
ATOM   842   O O   . ARG A  1 107 ? 47.962  39.653 68.335  1.00 51.40  ? 107  ARG A O   1 
ATOM   843   C CB  . ARG A  1 107 ? 45.914  41.640 68.321  1.00 46.55  ? 107  ARG A CB  1 
ATOM   844   C CG  . ARG A  1 107 ? 45.498  42.804 67.428  1.00 46.29  ? 107  ARG A CG  1 
ATOM   845   C CD  . ARG A  1 107 ? 46.363  44.040 67.694  1.00 47.85  ? 107  ARG A CD  1 
ATOM   846   N NE  . ARG A  1 107 ? 45.620  45.300 67.549  1.00 46.57  ? 107  ARG A NE  1 
ATOM   847   C CZ  . ARG A  1 107 ? 45.738  46.179 66.546  1.00 47.87  ? 107  ARG A CZ  1 
ATOM   848   N NH1 . ARG A  1 107 ? 46.585  45.983 65.532  1.00 50.69  ? 107  ARG A NH1 1 
ATOM   849   N NH2 . ARG A  1 107 ? 44.992  47.282 66.560  1.00 46.65  ? 107  ARG A NH2 1 
ATOM   850   N N   . ILE A  1 108 ? 46.375  38.130 68.807  1.00 48.34  ? 108  ILE A N   1 
ATOM   851   C CA  . ILE A  1 108 ? 47.282  37.245 69.548  1.00 50.14  ? 108  ILE A CA  1 
ATOM   852   C C   . ILE A  1 108 ? 47.376  35.846 68.925  1.00 51.87  ? 108  ILE A C   1 
ATOM   853   O O   . ILE A  1 108 ? 46.359  35.205 68.650  1.00 50.61  ? 108  ILE A O   1 
ATOM   854   C CB  . ILE A  1 108 ? 46.867  37.136 71.037  1.00 48.34  ? 108  ILE A CB  1 
ATOM   855   C CG1 . ILE A  1 108 ? 46.974  38.511 71.710  1.00 47.30  ? 108  ILE A CG1 1 
ATOM   856   C CG2 . ILE A  1 108 ? 47.747  36.132 71.775  1.00 50.44  ? 108  ILE A CG2 1 
ATOM   857   C CD1 . ILE A  1 108 ? 46.367  38.581 73.095  1.00 45.47  ? 108  ILE A CD1 1 
ATOM   858   N N   . ASN A  1 109 ? 48.612  35.385 68.726  1.00 55.10  ? 109  ASN A N   1 
ATOM   859   C CA  . ASN A  1 109 ? 48.891  34.063 68.161  1.00 57.51  ? 109  ASN A CA  1 
ATOM   860   C C   . ASN A  1 109 ? 49.416  33.043 69.170  1.00 58.86  ? 109  ASN A C   1 
ATOM   861   O O   . ASN A  1 109 ? 49.270  31.836 68.950  1.00 60.18  ? 109  ASN A O   1 
ATOM   862   C CB  . ASN A  1 109 ? 49.888  34.176 67.003  1.00 61.02  ? 109  ASN A CB  1 
ATOM   863   C CG  . ASN A  1 109 ? 49.205  34.314 65.661  1.00 60.75  ? 109  ASN A CG  1 
ATOM   864   O OD1 . ASN A  1 109 ? 49.240  33.401 64.839  1.00 62.92  ? 109  ASN A OD1 1 
ATOM   865   N ND2 . ASN A  1 109 ? 48.570  35.450 65.435  1.00 58.35  ? 109  ASN A ND2 1 
ATOM   866   N N   . HIS A  1 110 ? 50.038  33.506 70.255  1.00 58.84  ? 110  HIS A N   1 
ATOM   867   C CA  . HIS A  1 110 ? 50.533  32.583 71.276  1.00 60.23  ? 110  HIS A CA  1 
ATOM   868   C C   . HIS A  1 110 ? 50.574  33.149 72.693  1.00 58.71  ? 110  HIS A C   1 
ATOM   869   O O   . HIS A  1 110 ? 51.053  34.262 72.930  1.00 58.58  ? 110  HIS A O   1 
ATOM   870   C CB  . HIS A  1 110 ? 51.925  32.064 70.901  1.00 64.65  ? 110  HIS A CB  1 
ATOM   871   C CG  . HIS A  1 110 ? 52.325  30.823 71.640  1.00 66.65  ? 110  HIS A CG  1 
ATOM   872   N ND1 . HIS A  1 110 ? 53.628  30.556 72.000  1.00 70.28  ? 110  HIS A ND1 1 
ATOM   873   C CD2 . HIS A  1 110 ? 51.587  29.784 72.101  1.00 65.83  ? 110  HIS A CD2 1 
ATOM   874   C CE1 . HIS A  1 110 ? 53.678  29.401 72.639  1.00 71.52  ? 110  HIS A CE1 1 
ATOM   875   N NE2 . HIS A  1 110 ? 52.453  28.912 72.713  1.00 68.89  ? 110  HIS A NE2 1 
ATOM   876   N N   . PHE A  1 111 ? 50.071  32.346 73.625  1.00 57.90  ? 111  PHE A N   1 
ATOM   877   C CA  . PHE A  1 111 ? 50.205  32.604 75.051  1.00 57.28  ? 111  PHE A CA  1 
ATOM   878   C C   . PHE A  1 111 ? 51.224  31.632 75.630  1.00 60.56  ? 111  PHE A C   1 
ATOM   879   O O   . PHE A  1 111 ? 51.294  30.481 75.199  1.00 62.34  ? 111  PHE A O   1 
ATOM   880   C CB  . PHE A  1 111 ? 48.871  32.385 75.779  1.00 54.42  ? 111  PHE A CB  1 
ATOM   881   C CG  . PHE A  1 111 ? 47.937  33.566 75.750  1.00 51.25  ? 111  PHE A CG  1 
ATOM   882   C CD1 . PHE A  1 111 ? 48.399  34.862 75.966  1.00 50.86  ? 111  PHE A CD1 1 
ATOM   883   C CD2 . PHE A  1 111 ? 46.577  33.374 75.555  1.00 48.99  ? 111  PHE A CD2 1 
ATOM   884   C CE1 . PHE A  1 111 ? 47.528  35.936 75.957  1.00 48.24  ? 111  PHE A CE1 1 
ATOM   885   C CE2 . PHE A  1 111 ? 45.706  34.445 75.548  1.00 46.42  ? 111  PHE A CE2 1 
ATOM   886   C CZ  . PHE A  1 111 ? 46.181  35.728 75.750  1.00 46.01  ? 111  PHE A CZ  1 
ATOM   887   N N   . GLU A  1 112 ? 52.010  32.103 76.598  1.00 61.60  ? 112  GLU A N   1 
ATOM   888   C CA  . GLU A  1 112 ? 52.816  31.222 77.448  1.00 64.43  ? 112  GLU A CA  1 
ATOM   889   C C   . GLU A  1 112 ? 52.395  31.421 78.901  1.00 62.91  ? 112  GLU A C   1 
ATOM   890   O O   . GLU A  1 112 ? 52.419  32.533 79.413  1.00 61.69  ? 112  GLU A O   1 
ATOM   891   C CB  . GLU A  1 112 ? 54.313  31.502 77.296  1.00 68.11  ? 112  GLU A CB  1 
ATOM   892   C CG  . GLU A  1 112 ? 55.187  30.383 77.845  1.00 71.75  ? 112  GLU A CG  1 
ATOM   893   C CD  . GLU A  1 112 ? 56.648  30.773 77.963  1.00 75.57  ? 112  GLU A CD  1 
ATOM   894   O OE1 . GLU A  1 112 ? 57.158  31.457 77.049  1.00 76.72  ? 112  GLU A OE1 1 
ATOM   895   O OE2 . GLU A  1 112 ? 57.290  30.385 78.966  1.00 77.73  ? 112  GLU A OE2 1 
ATOM   896   N N   . LYS A  1 113 ? 52.008  30.339 79.562  1.00 63.30  ? 113  LYS A N   1 
ATOM   897   C CA  . LYS A  1 113 ? 51.521  30.421 80.934  1.00 62.19  ? 113  LYS A CA  1 
ATOM   898   C C   . LYS A  1 113 ? 52.679  30.480 81.932  1.00 64.90  ? 113  LYS A C   1 
ATOM   899   O O   . LYS A  1 113 ? 53.672  29.766 81.777  1.00 68.18  ? 113  LYS A O   1 
ATOM   900   C CB  . LYS A  1 113 ? 50.634  29.216 81.227  1.00 62.01  ? 113  LYS A CB  1 
ATOM   901   C CG  . LYS A  1 113 ? 49.805  29.337 82.492  1.00 60.57  ? 113  LYS A CG  1 
ATOM   902   C CD  . LYS A  1 113 ? 48.379  28.858 82.266  1.00 58.66  ? 113  LYS A CD  1 
ATOM   903   C CE  . LYS A  1 113 ? 48.294  27.376 81.925  1.00 60.75  ? 113  LYS A CE  1 
ATOM   904   N NZ  . LYS A  1 113 ? 46.886  26.978 81.637  1.00 59.15  ? 113  LYS A NZ  1 
ATOM   905   N N   . ILE A  1 114 ? 52.557  31.344 82.939  1.00 63.81  ? 114  ILE A N   1 
ATOM   906   C CA  . ILE A  1 114 ? 53.540  31.417 84.024  1.00 66.42  ? 114  ILE A CA  1 
ATOM   907   C C   . ILE A  1 114 ? 52.867  31.628 85.378  1.00 65.23  ? 114  ILE A C   1 
ATOM   908   O O   . ILE A  1 114 ? 51.785  32.216 85.463  1.00 62.28  ? 114  ILE A O   1 
ATOM   909   C CB  . ILE A  1 114 ? 54.579  32.543 83.817  1.00 67.78  ? 114  ILE A CB  1 
ATOM   910   C CG1 . ILE A  1 114 ? 53.888  33.894 83.588  1.00 64.73  ? 114  ILE A CG1 1 
ATOM   911   C CG2 . ILE A  1 114 ? 55.518  32.203 82.666  1.00 70.31  ? 114  ILE A CG2 1 
ATOM   912   C CD1 . ILE A  1 114 ? 54.743  35.075 83.994  1.00 66.21  ? 114  ILE A CD1 1 
ATOM   913   N N   . GLN A  1 115 ? 53.529  31.147 86.428  1.00 67.87  ? 115  GLN A N   1 
ATOM   914   C CA  . GLN A  1 115 ? 53.049  31.301 87.796  1.00 67.54  ? 115  GLN A CA  1 
ATOM   915   C C   . GLN A  1 115 ? 53.535  32.632 88.367  1.00 67.75  ? 115  GLN A C   1 
ATOM   916   O O   . GLN A  1 115 ? 54.737  32.902 88.380  1.00 70.37  ? 115  GLN A O   1 
ATOM   917   C CB  . GLN A  1 115 ? 53.546  30.139 88.659  1.00 70.64  ? 115  GLN A CB  1 
ATOM   918   C CG  . GLN A  1 115 ? 53.230  30.261 90.142  1.00 71.14  ? 115  GLN A CG  1 
ATOM   919   C CD  . GLN A  1 115 ? 53.648  29.030 90.925  1.00 74.33  ? 115  GLN A CD  1 
ATOM   920   O OE1 . GLN A  1 115 ? 52.944  28.020 90.937  1.00 74.23  ? 115  GLN A OE1 1 
ATOM   921   N NE2 . GLN A  1 115 ? 54.795  29.109 91.589  1.00 77.47  ? 115  GLN A NE2 1 
ATOM   922   N N   . ILE A  1 116 ? 52.596  33.452 88.837  1.00 65.36  ? 116  ILE A N   1 
ATOM   923   C CA  . ILE A  1 116 ? 52.925  34.729 89.490  1.00 65.73  ? 116  ILE A CA  1 
ATOM   924   C C   . ILE A  1 116 ? 52.738  34.649 91.014  1.00 67.00  ? 116  ILE A C   1 
ATOM   925   O O   . ILE A  1 116 ? 53.582  35.132 91.774  1.00 69.40  ? 116  ILE A O   1 
ATOM   926   C CB  . ILE A  1 116 ? 52.133  35.931 88.903  1.00 62.69  ? 116  ILE A CB  1 
ATOM   927   C CG1 . ILE A  1 116 ? 50.675  35.563 88.607  1.00 59.66  ? 116  ILE A CG1 1 
ATOM   928   C CG2 . ILE A  1 116 ? 52.801  36.438 87.630  1.00 62.76  ? 116  ILE A CG2 1 
ATOM   929   C CD1 . ILE A  1 116 ? 49.732  36.741 88.678  1.00 57.29  ? 116  ILE A CD1 1 
ATOM   930   N N   . ILE A  1 117 ? 51.642  34.032 91.453  1.00 65.76  ? 117  ILE A N   1 
ATOM   931   C CA  . ILE A  1 117 ? 51.416  33.730 92.869  1.00 67.39  ? 117  ILE A CA  1 
ATOM   932   C C   . ILE A  1 117 ? 51.422  32.206 93.035  1.00 68.97  ? 117  ILE A C   1 
ATOM   933   O O   . ILE A  1 117 ? 50.570  31.525 92.460  1.00 67.40  ? 117  ILE A O   1 
ATOM   934   C CB  . ILE A  1 117 ? 50.073  34.325 93.370  1.00 65.27  ? 117  ILE A CB  1 
ATOM   935   C CG1 . ILE A  1 117 ? 50.266  35.759 93.884  1.00 65.40  ? 117  ILE A CG1 1 
ATOM   936   C CG2 . ILE A  1 117 ? 49.435  33.467 94.466  1.00 66.59  ? 117  ILE A CG2 1 
ATOM   937   C CD1 . ILE A  1 117 ? 50.321  36.807 92.795  1.00 63.35  ? 117  ILE A CD1 1 
ATOM   938   N N   . PRO A  1 118 ? 52.391  31.662 93.801  1.00 72.38  ? 118  PRO A N   1 
ATOM   939   C CA  . PRO A  1 118 ? 52.326  30.223 94.082  1.00 74.21  ? 118  PRO A CA  1 
ATOM   940   C C   . PRO A  1 118 ? 51.202  29.873 95.062  1.00 74.08  ? 118  PRO A C   1 
ATOM   941   O O   . PRO A  1 118 ? 50.925  30.635 95.987  1.00 74.21  ? 118  PRO A O   1 
ATOM   942   C CB  . PRO A  1 118 ? 53.709  29.902 94.680  1.00 78.14  ? 118  PRO A CB  1 
ATOM   943   C CG  . PRO A  1 118 ? 54.579  31.071 94.354  1.00 78.26  ? 118  PRO A CG  1 
ATOM   944   C CD  . PRO A  1 118 ? 53.670  32.257 94.234  1.00 75.00  ? 118  PRO A CD  1 
ATOM   945   N N   . LYS A  1 119 ? 50.564  28.726 94.847  1.00 74.19  ? 119  LYS A N   1 
ATOM   946   C CA  . LYS A  1 119 ? 49.448  28.286 95.686  1.00 74.49  ? 119  LYS A CA  1 
ATOM   947   C C   . LYS A  1 119 ? 49.920  27.954 97.104  1.00 78.04  ? 119  LYS A C   1 
ATOM   948   O O   . LYS A  1 119 ? 49.223  28.228 98.083  1.00 78.51  ? 119  LYS A O   1 
ATOM   949   C CB  . LYS A  1 119 ? 48.773  27.067 95.057  1.00 74.38  ? 119  LYS A CB  1 
ATOM   950   C CG  . LYS A  1 119 ? 47.362  26.804 95.546  1.00 73.94  ? 119  LYS A CG  1 
ATOM   951   C CD  . LYS A  1 119 ? 46.725  25.683 94.741  1.00 73.85  ? 119  LYS A CD  1 
ATOM   952   C CE  . LYS A  1 119 ? 45.492  25.118 95.426  1.00 74.92  ? 119  LYS A CE  1 
ATOM   953   N NZ  . LYS A  1 119 ? 45.076  23.824 94.815  1.00 76.04  ? 119  LYS A NZ  1 
ATOM   954   N N   . SER A  1 120 ? 51.109  27.360 97.199  1.00 80.84  ? 120  SER A N   1 
ATOM   955   C CA  . SER A  1 120 ? 51.748  27.066 98.484  1.00 84.55  ? 120  SER A CA  1 
ATOM   956   C C   . SER A  1 120 ? 52.034  28.333 99.289  1.00 84.77  ? 120  SER A C   1 
ATOM   957   O O   . SER A  1 120 ? 52.020  28.308 100.514 1.00 87.18  ? 120  SER A O   1 
ATOM   958   C CB  . SER A  1 120 ? 53.063  26.323 98.250  1.00 87.47  ? 120  SER A CB  1 
ATOM   959   O OG  . SER A  1 120 ? 53.946  27.099 97.454  1.00 86.61  ? 120  SER A OG  1 
ATOM   960   N N   . SER A  1 121 ? 52.283  29.435 98.584  1.00 82.56  ? 121  SER A N   1 
ATOM   961   C CA  . SER A  1 121 ? 52.659  30.712 99.190  1.00 82.95  ? 121  SER A CA  1 
ATOM   962   C C   . SER A  1 121 ? 51.616  31.303 100.165 1.00 82.54  ? 121  SER A C   1 
ATOM   963   O O   . SER A  1 121 ? 51.959  32.159 100.982 1.00 83.97  ? 121  SER A O   1 
ATOM   964   C CB  . SER A  1 121 ? 53.038  31.717 98.078  1.00 80.62  ? 121  SER A CB  1 
ATOM   965   O OG  . SER A  1 121 ? 52.231  32.868 98.123  1.00 78.24  ? 121  SER A OG  1 
ATOM   966   N N   . TRP A  1 122 ? 50.368  30.839 100.101 1.00 81.06  ? 122  TRP A N   1 
ATOM   967   C CA  . TRP A  1 122 ? 49.314  31.320 100.997 1.00 81.11  ? 122  TRP A CA  1 
ATOM   968   C C   . TRP A  1 122 ? 49.421  30.644 102.357 1.00 85.05  ? 122  TRP A C   1 
ATOM   969   O O   . TRP A  1 122 ? 48.634  29.756 102.686 1.00 85.95  ? 122  TRP A O   1 
ATOM   970   C CB  . TRP A  1 122 ? 47.935  31.076 100.381 1.00 78.44  ? 122  TRP A CB  1 
ATOM   971   C CG  . TRP A  1 122 ? 47.739  31.823 99.107  1.00 74.76  ? 122  TRP A CG  1 
ATOM   972   C CD1 . TRP A  1 122 ? 47.716  31.305 97.846  1.00 72.76  ? 122  TRP A CD1 1 
ATOM   973   C CD2 . TRP A  1 122 ? 47.562  33.236 98.966  1.00 72.97  ? 122  TRP A CD2 1 
ATOM   974   N NE1 . TRP A  1 122 ? 47.521  32.308 96.926  1.00 69.78  ? 122  TRP A NE1 1 
ATOM   975   C CE2 . TRP A  1 122 ? 47.426  33.505 97.587  1.00 69.84  ? 122  TRP A CE2 1 
ATOM   976   C CE3 . TRP A  1 122 ? 47.499  34.302 99.873  1.00 73.99  ? 122  TRP A CE3 1 
ATOM   977   C CZ2 . TRP A  1 122 ? 47.228  34.799 97.092  1.00 67.67  ? 122  TRP A CZ2 1 
ATOM   978   C CZ3 . TRP A  1 122 ? 47.305  35.586 99.382  1.00 71.89  ? 122  TRP A CZ3 1 
ATOM   979   C CH2 . TRP A  1 122 ? 47.171  35.824 98.002  1.00 68.75  ? 122  TRP A CH2 1 
ATOM   980   N N   . SER A  1 123 ? 50.402  31.085 103.143 1.00 80.33  ? 123  SER A N   1 
ATOM   981   C CA  . SER A  1 123 ? 50.714  30.476 104.439 1.00 83.85  ? 123  SER A CA  1 
ATOM   982   C C   . SER A  1 123 ? 49.763  30.930 105.547 1.00 84.62  ? 123  SER A C   1 
ATOM   983   O O   . SER A  1 123 ? 49.548  30.202 106.515 1.00 87.41  ? 123  SER A O   1 
ATOM   984   C CB  . SER A  1 123 ? 52.156  30.801 104.838 1.00 85.52  ? 123  SER A CB  1 
ATOM   985   O OG  . SER A  1 123 ? 52.354  32.199 104.941 1.00 84.05  ? 123  SER A OG  1 
ATOM   986   N N   . SER A  1 124 ? 49.206  32.131 105.401 1.00 82.42  ? 124  SER A N   1 
ATOM   987   C CA  . SER A  1 124 ? 48.291  32.704 106.392 1.00 83.07  ? 124  SER A CA  1 
ATOM   988   C C   . SER A  1 124 ? 46.808  32.425 106.080 1.00 81.90  ? 124  SER A C   1 
ATOM   989   O O   . SER A  1 124 ? 45.933  32.741 106.887 1.00 82.69  ? 124  SER A O   1 
ATOM   990   C CB  . SER A  1 124 ? 48.534  34.213 106.491 1.00 81.68  ? 124  SER A CB  1 
ATOM   991   O OG  . SER A  1 124 ? 47.721  34.803 107.488 1.00 82.56  ? 124  SER A OG  1 
ATOM   992   N N   . HIS A  1 125 ? 46.535  31.834 104.916 1.00 80.25  ? 125  HIS A N   1 
ATOM   993   C CA  . HIS A  1 125 ? 45.167  31.508 104.497 1.00 79.15  ? 125  HIS A CA  1 
ATOM   994   C C   . HIS A  1 125 ? 45.067  30.056 104.045 1.00 80.21  ? 125  HIS A C   1 
ATOM   995   O O   . HIS A  1 125 ? 46.083  29.402 103.801 1.00 81.30  ? 125  HIS A O   1 
ATOM   996   C CB  . HIS A  1 125 ? 44.732  32.423 103.351 1.00 75.59  ? 125  HIS A CB  1 
ATOM   997   C CG  . HIS A  1 125 ? 44.587  33.859 103.746 1.00 74.63  ? 125  HIS A CG  1 
ATOM   998   N ND1 . HIS A  1 125 ? 45.657  34.725 103.803 1.00 74.35  ? 125  HIS A ND1 1 
ATOM   999   C CD2 . HIS A  1 125 ? 43.498  34.581 104.100 1.00 74.08  ? 125  HIS A CD2 1 
ATOM   1000  C CE1 . HIS A  1 125 ? 45.234  35.919 104.181 1.00 73.67  ? 125  HIS A CE1 1 
ATOM   1001  N NE2 . HIS A  1 125 ? 43.927  35.858 104.365 1.00 73.50  ? 125  HIS A NE2 1 
ATOM   1002  N N   . GLU A  1 126 ? 43.840  29.551 103.954 1.00 80.23  ? 126  GLU A N   1 
ATOM   1003  C CA  . GLU A  1 126 ? 43.594  28.209 103.436 1.00 81.07  ? 126  GLU A CA  1 
ATOM   1004  C C   . GLU A  1 126 ? 43.307  28.312 101.941 1.00 78.05  ? 126  GLU A C   1 
ATOM   1005  O O   . GLU A  1 126 ? 42.454  29.099 101.525 1.00 75.92  ? 126  GLU A O   1 
ATOM   1006  C CB  . GLU A  1 126 ? 42.420  27.563 104.171 1.00 82.99  ? 126  GLU A CB  1 
ATOM   1007  C CG  . GLU A  1 126 ? 42.168  26.107 103.811 1.00 84.39  ? 126  GLU A CG  1 
ATOM   1008  C CD  . GLU A  1 126 ? 43.331  25.193 104.167 1.00 87.10  ? 126  GLU A CD  1 
ATOM   1009  O OE1 . GLU A  1 126 ? 43.677  25.093 105.367 1.00 89.92  ? 126  GLU A OE1 1 
ATOM   1010  O OE2 . GLU A  1 126 ? 43.889  24.564 103.240 1.00 86.57  ? 126  GLU A OE2 1 
ATOM   1011  N N   . ALA A  1 127 ? 44.024  27.524 101.140 1.00 78.09  ? 127  ALA A N   1 
ATOM   1012  C CA  . ALA A  1 127 ? 43.968  27.633 99.674  1.00 75.34  ? 127  ALA A CA  1 
ATOM   1013  C C   . ALA A  1 127 ? 43.520  26.361 98.944  1.00 75.77  ? 127  ALA A C   1 
ATOM   1014  O O   . ALA A  1 127 ? 43.187  26.421 97.757  1.00 73.59  ? 127  ALA A O   1 
ATOM   1015  C CB  . ALA A  1 127 ? 45.326  28.075 99.146  1.00 74.65  ? 127  ALA A CB  1 
ATOM   1016  N N   . SER A  1 128 ? 43.500  25.226 99.641  1.00 78.69  ? 128  SER A N   1 
ATOM   1017  C CA  . SER A  1 128 ? 43.257  23.923 99.008  1.00 79.59  ? 128  SER A CA  1 
ATOM   1018  C C   . SER A  1 128 ? 41.815  23.425 99.132  1.00 79.92  ? 128  SER A C   1 
ATOM   1019  O O   . SER A  1 128 ? 41.472  22.382 98.573  1.00 80.58  ? 128  SER A O   1 
ATOM   1020  C CB  . SER A  1 128 ? 44.216  22.876 99.585  1.00 82.94  ? 128  SER A CB  1 
ATOM   1021  O OG  . SER A  1 128 ? 45.535  23.101 99.123  1.00 82.64  ? 128  SER A OG  1 
ATOM   1022  N N   . LEU A  1 129 ? 40.978  24.165 99.856  1.00 79.65  ? 129  LEU A N   1 
ATOM   1023  C CA  . LEU A  1 129 ? 39.583  23.776 100.063 1.00 80.20  ? 129  LEU A CA  1 
ATOM   1024  C C   . LEU A  1 129 ? 38.616  24.641 99.250  1.00 77.13  ? 129  LEU A C   1 
ATOM   1025  O O   . LEU A  1 129 ? 37.400  24.519 99.396  1.00 77.45  ? 129  LEU A O   1 
ATOM   1026  C CB  . LEU A  1 129 ? 39.228  23.842 101.553 1.00 82.79  ? 129  LEU A CB  1 
ATOM   1027  C CG  . LEU A  1 129 ? 39.754  22.704 102.433 1.00 86.59  ? 129  LEU A CG  1 
ATOM   1028  C CD1 . LEU A  1 129 ? 41.236  22.855 102.729 1.00 87.39  ? 129  LEU A CD1 1 
ATOM   1029  C CD2 . LEU A  1 129 ? 38.968  22.661 103.733 1.00 89.17  ? 129  LEU A CD2 1 
ATOM   1030  N N   . GLY A  1 130 ? 39.156  25.500 98.389  1.00 74.46  ? 130  GLY A N   1 
ATOM   1031  C CA  . GLY A  1 130 ? 38.343  26.383 97.557  1.00 71.58  ? 130  GLY A CA  1 
ATOM   1032  C C   . GLY A  1 130 ? 37.842  25.727 96.282  1.00 70.35  ? 130  GLY A C   1 
ATOM   1033  O O   . GLY A  1 130 ? 38.258  26.096 95.176  1.00 68.20  ? 130  GLY A O   1 
ATOM   1034  N N   . VAL A  1 131 ? 36.937  24.761 96.440  1.00 71.83  ? 131  VAL A N   1 
ATOM   1035  C CA  . VAL A  1 131 ? 36.376  24.006 95.315  1.00 71.10  ? 131  VAL A CA  1 
ATOM   1036  C C   . VAL A  1 131 ? 34.847  24.013 95.359  1.00 71.04  ? 131  VAL A C   1 
ATOM   1037  O O   . VAL A  1 131 ? 34.246  24.544 96.292  1.00 71.85  ? 131  VAL A O   1 
ATOM   1038  C CB  . VAL A  1 131 ? 36.886  22.544 95.300  1.00 73.45  ? 131  VAL A CB  1 
ATOM   1039  C CG1 . VAL A  1 131 ? 38.407  22.506 95.387  1.00 73.99  ? 131  VAL A CG1 1 
ATOM   1040  C CG2 . VAL A  1 131 ? 36.261  21.726 96.428  1.00 76.51  ? 131  VAL A CG2 1 
ATOM   1041  N N   . SER A  1 132 ? 34.229  23.423 94.339  1.00 70.34  ? 132  SER A N   1 
ATOM   1042  C CA  . SER A  1 132 ? 32.772  23.357 94.241  1.00 70.32  ? 132  SER A CA  1 
ATOM   1043  C C   . SER A  1 132 ? 32.328  22.181 93.379  1.00 70.78  ? 132  SER A C   1 
ATOM   1044  O O   . SER A  1 132 ? 33.067  21.722 92.505  1.00 70.17  ? 132  SER A O   1 
ATOM   1045  C CB  . SER A  1 132 ? 32.220  24.660 93.652  1.00 67.67  ? 132  SER A CB  1 
ATOM   1046  O OG  . SER A  1 132 ? 30.864  24.519 93.262  1.00 67.59  ? 132  SER A OG  1 
ATOM   1047  N N   . SER A  1 133 ? 31.107  21.711 93.628  1.00 71.96  ? 133  SER A N   1 
ATOM   1048  C CA  . SER A  1 133 ? 30.509  20.630 92.849  1.00 72.53  ? 133  SER A CA  1 
ATOM   1049  C C   . SER A  1 133 ? 30.119  21.089 91.438  1.00 69.66  ? 133  SER A C   1 
ATOM   1050  O O   . SER A  1 133 ? 29.888  20.258 90.558  1.00 69.82  ? 133  SER A O   1 
ATOM   1051  C CB  . SER A  1 133 ? 29.282  20.071 93.573  1.00 74.88  ? 133  SER A CB  1 
ATOM   1052  O OG  . SER A  1 133 ? 28.285  21.066 93.721  1.00 73.81  ? 133  SER A OG  1 
ATOM   1053  N N   . ALA A  1 134 ? 30.042  22.404 91.233  1.00 67.17  ? 134  ALA A N   1 
ATOM   1054  C CA  . ALA A  1 134 ? 29.742  22.979 89.919  1.00 64.50  ? 134  ALA A CA  1 
ATOM   1055  C C   . ALA A  1 134 ? 30.885  22.778 88.917  1.00 63.22  ? 134  ALA A C   1 
ATOM   1056  O O   . ALA A  1 134 ? 30.637  22.647 87.721  1.00 62.04  ? 134  ALA A O   1 
ATOM   1057  C CB  . ALA A  1 134 ? 29.411  24.457 90.054  1.00 62.67  ? 134  ALA A CB  1 
ATOM   1058  N N   . CYS A  1 135 ? 32.125  22.759 89.408  1.00 63.58  ? 135  CYS A N   1 
ATOM   1059  C CA  . CYS A  1 135 ? 33.297  22.434 88.588  1.00 63.00  ? 135  CYS A CA  1 
ATOM   1060  C C   . CYS A  1 135 ? 33.893  21.079 89.007  1.00 65.53  ? 135  CYS A C   1 
ATOM   1061  O O   . CYS A  1 135 ? 34.852  21.038 89.777  1.00 66.59  ? 135  CYS A O   1 
ATOM   1062  C CB  . CYS A  1 135 ? 34.364  23.531 88.720  1.00 61.60  ? 135  CYS A CB  1 
ATOM   1063  S SG  . CYS A  1 135 ? 33.765  25.217 88.468  1.00 58.98  ? 135  CYS A SG  1 
ATOM   1064  N N   . PRO A  1 136 ? 33.320  19.964 88.510  1.00 66.62  ? 136  PRO A N   1 
ATOM   1065  C CA  . PRO A  1 136 ? 33.833  18.632 88.843  1.00 69.31  ? 136  PRO A CA  1 
ATOM   1066  C C   . PRO A  1 136 ? 34.983  18.155 87.949  1.00 69.26  ? 136  PRO A C   1 
ATOM   1067  O O   . PRO A  1 136 ? 34.971  18.404 86.741  1.00 67.50  ? 136  PRO A O   1 
ATOM   1068  C CB  . PRO A  1 136 ? 32.611  17.739 88.636  1.00 70.59  ? 136  PRO A CB  1 
ATOM   1069  C CG  . PRO A  1 136 ? 31.861  18.410 87.542  1.00 68.09  ? 136  PRO A CG  1 
ATOM   1070  C CD  . PRO A  1 136 ? 32.040  19.881 87.781  1.00 65.87  ? 136  PRO A CD  1 
ATOM   1071  N N   . TYR A  1 137 ? 35.957  17.471 88.553  1.00 71.38  ? 137  TYR A N   1 
ATOM   1072  C CA  . TYR A  1 137 ? 37.067  16.842 87.829  1.00 72.06  ? 137  TYR A CA  1 
ATOM   1073  C C   . TYR A  1 137 ? 37.309  15.429 88.365  1.00 75.50  ? 137  TYR A C   1 
ATOM   1074  O O   . TYR A  1 137 ? 37.603  15.257 89.548  1.00 77.40  ? 137  TYR A O   1 
ATOM   1075  C CB  . TYR A  1 137 ? 38.342  17.677 87.975  1.00 71.15  ? 137  TYR A CB  1 
ATOM   1076  C CG  . TYR A  1 137 ? 39.590  17.032 87.392  1.00 72.39  ? 137  TYR A CG  1 
ATOM   1077  C CD1 . TYR A  1 137 ? 39.741  16.873 86.012  1.00 71.42  ? 137  TYR A CD1 1 
ATOM   1078  C CD2 . TYR A  1 137 ? 40.627  16.595 88.220  1.00 74.71  ? 137  TYR A CD2 1 
ATOM   1079  C CE1 . TYR A  1 137 ? 40.881  16.289 85.477  1.00 72.78  ? 137  TYR A CE1 1 
ATOM   1080  C CE2 . TYR A  1 137 ? 41.771  16.015 87.692  1.00 76.07  ? 137  TYR A CE2 1 
ATOM   1081  C CZ  . TYR A  1 137 ? 41.894  15.863 86.322  1.00 75.11  ? 137  TYR A CZ  1 
ATOM   1082  O OH  . TYR A  1 137 ? 43.029  15.285 85.801  1.00 76.70  ? 137  TYR A OH  1 
ATOM   1083  N N   . GLN A  1 138 ? 37.188  14.433 87.488  1.00 76.45  ? 138  GLN A N   1 
ATOM   1084  C CA  . GLN A  1 138 ? 37.342  13.015 87.850  1.00 79.93  ? 138  GLN A CA  1 
ATOM   1085  C C   . GLN A  1 138 ? 36.419  12.590 88.998  1.00 81.86  ? 138  GLN A C   1 
ATOM   1086  O O   . GLN A  1 138 ? 36.829  11.857 89.903  1.00 84.83  ? 138  GLN A O   1 
ATOM   1087  C CB  . GLN A  1 138 ? 38.801  12.688 88.191  1.00 81.74  ? 138  GLN A CB  1 
ATOM   1088  C CG  . GLN A  1 138 ? 39.798  13.223 87.176  1.00 79.98  ? 138  GLN A CG  1 
ATOM   1089  C CD  . GLN A  1 138 ? 41.020  12.336 87.008  1.00 82.57  ? 138  GLN A CD  1 
ATOM   1090  O OE1 . GLN A  1 138 ? 41.564  11.818 87.982  1.00 85.20  ? 138  GLN A OE1 1 
ATOM   1091  N NE2 . GLN A  1 138 ? 41.461  12.166 85.765  1.00 82.03  ? 138  GLN A NE2 1 
ATOM   1092  N N   . GLY A  1 139 ? 35.175  13.065 88.954  1.00 80.35  ? 139  GLY A N   1 
ATOM   1093  C CA  . GLY A  1 139 ? 34.159  12.704 89.945  1.00 82.18  ? 139  GLY A CA  1 
ATOM   1094  C C   . GLY A  1 139 ? 34.264  13.434 91.274  1.00 82.43  ? 139  GLY A C   1 
ATOM   1095  O O   . GLY A  1 139 ? 33.470  13.185 92.180  1.00 84.19  ? 139  GLY A O   1 
ATOM   1096  N N   . LYS A  1 140 ? 35.231  14.344 91.382  1.00 80.79  ? 140  LYS A N   1 
ATOM   1097  C CA  . LYS A  1 140 ? 35.492  15.083 92.613  1.00 81.06  ? 140  LYS A CA  1 
ATOM   1098  C C   . LYS A  1 140 ? 35.373  16.580 92.352  1.00 77.61  ? 140  LYS A C   1 
ATOM   1099  O O   . LYS A  1 140 ? 35.570  17.036 91.226  1.00 75.17  ? 140  LYS A O   1 
ATOM   1100  C CB  . LYS A  1 140 ? 36.889  14.742 93.138  1.00 82.91  ? 140  LYS A CB  1 
ATOM   1101  C CG  . LYS A  1 140 ? 36.984  13.346 93.733  1.00 86.91  ? 140  LYS A CG  1 
ATOM   1102  C CD  . LYS A  1 140 ? 38.259  12.621 93.322  1.00 88.38  ? 140  LYS A CD  1 
ATOM   1103  C CE  . LYS A  1 140 ? 38.225  11.151 93.720  1.00 92.44  ? 140  LYS A CE  1 
ATOM   1104  N NZ  . LYS A  1 140 ? 38.595  10.930 95.145  1.00 95.46  ? 140  LYS A NZ  1 
ATOM   1105  N N   . SER A  1 141 ? 35.049  17.334 93.399  1.00 77.64  ? 141  SER A N   1 
ATOM   1106  C CA  . SER A  1 141 ? 34.871  18.782 93.293  1.00 74.73  ? 141  SER A CA  1 
ATOM   1107  C C   . SER A  1 141 ? 36.204  19.483 93.031  1.00 73.26  ? 141  SER A C   1 
ATOM   1108  O O   . SER A  1 141 ? 37.202  19.202 93.694  1.00 74.98  ? 141  SER A O   1 
ATOM   1109  C CB  . SER A  1 141 ? 34.229  19.338 94.567  1.00 75.65  ? 141  SER A CB  1 
ATOM   1110  O OG  . SER A  1 141 ? 32.909  18.847 94.729  1.00 76.86  ? 141  SER A OG  1 
ATOM   1111  N N   . SER A  1 142 ? 36.204  20.395 92.062  1.00 70.25  ? 142  SER A N   1 
ATOM   1112  C CA  . SER A  1 142 ? 37.414  21.096 91.638  1.00 68.76  ? 142  SER A CA  1 
ATOM   1113  C C   . SER A  1 142 ? 37.090  22.572 91.411  1.00 65.96  ? 142  SER A C   1 
ATOM   1114  O O   . SER A  1 142 ? 36.034  23.051 91.833  1.00 65.53  ? 142  SER A O   1 
ATOM   1115  C CB  . SER A  1 142 ? 37.962  20.451 90.359  1.00 68.42  ? 142  SER A CB  1 
ATOM   1116  O OG  . SER A  1 142 ? 39.224  20.985 89.999  1.00 67.57  ? 142  SER A OG  1 
ATOM   1117  N N   . PHE A  1 143 ? 38.001  23.294 90.762  1.00 64.27  ? 143  PHE A N   1 
ATOM   1118  C CA  . PHE A  1 143 ? 37.782  24.704 90.436  1.00 61.72  ? 143  PHE A CA  1 
ATOM   1119  C C   . PHE A  1 143 ? 38.646  25.125 89.246  1.00 60.09  ? 143  PHE A C   1 
ATOM   1120  O O   . PHE A  1 143 ? 39.514  24.370 88.803  1.00 61.06  ? 143  PHE A O   1 
ATOM   1121  C CB  . PHE A  1 143 ? 38.093  25.580 91.660  1.00 62.04  ? 143  PHE A CB  1 
ATOM   1122  C CG  . PHE A  1 143 ? 37.429  26.932 91.632  1.00 60.01  ? 143  PHE A CG  1 
ATOM   1123  C CD1 . PHE A  1 143 ? 36.043  27.038 91.606  1.00 59.59  ? 143  PHE A CD1 1 
ATOM   1124  C CD2 . PHE A  1 143 ? 38.187  28.099 91.642  1.00 58.75  ? 143  PHE A CD2 1 
ATOM   1125  C CE1 . PHE A  1 143 ? 35.425  28.280 91.584  1.00 57.99  ? 143  PHE A CE1 1 
ATOM   1126  C CE2 . PHE A  1 143 ? 37.574  29.343 91.622  1.00 57.12  ? 143  PHE A CE2 1 
ATOM   1127  C CZ  . PHE A  1 143 ? 36.191  29.434 91.593  1.00 56.75  ? 143  PHE A CZ  1 
ATOM   1128  N N   . PHE A  1 144 ? 38.390  26.323 88.724  1.00 57.84  ? 144  PHE A N   1 
ATOM   1129  C CA  . PHE A  1 144 ? 39.242  26.925 87.701  1.00 56.41  ? 144  PHE A CA  1 
ATOM   1130  C C   . PHE A  1 144 ? 40.705  26.841 88.148  1.00 57.63  ? 144  PHE A C   1 
ATOM   1131  O O   . PHE A  1 144 ? 41.080  27.434 89.155  1.00 58.05  ? 144  PHE A O   1 
ATOM   1132  C CB  . PHE A  1 144 ? 38.874  28.397 87.468  1.00 54.28  ? 144  PHE A CB  1 
ATOM   1133  C CG  . PHE A  1 144 ? 37.421  28.634 87.141  1.00 53.25  ? 144  PHE A CG  1 
ATOM   1134  C CD1 . PHE A  1 144 ? 36.905  28.306 85.892  1.00 52.41  ? 144  PHE A CD1 1 
ATOM   1135  C CD2 . PHE A  1 144 ? 36.571  29.210 88.081  1.00 53.28  ? 144  PHE A CD2 1 
ATOM   1136  C CE1 . PHE A  1 144 ? 35.570  28.537 85.596  1.00 51.62  ? 144  PHE A CE1 1 
ATOM   1137  C CE2 . PHE A  1 144 ? 35.237  29.441 87.790  1.00 52.54  ? 144  PHE A CE2 1 
ATOM   1138  C CZ  . PHE A  1 144 ? 34.735  29.106 86.547  1.00 51.70  ? 144  PHE A CZ  1 
ATOM   1139  N N   . ARG A  1 145 ? 41.523  26.106 87.399  1.00 58.38  ? 145  ARG A N   1 
ATOM   1140  C CA  . ARG A  1 145 ? 42.905  25.814 87.799  1.00 60.02  ? 145  ARG A CA  1 
ATOM   1141  C C   . ARG A  1 145 ? 43.835  27.024 87.880  1.00 59.17  ? 145  ARG A C   1 
ATOM   1142  O O   . ARG A  1 145 ? 44.845  26.979 88.581  1.00 60.62  ? 145  ARG A O   1 
ATOM   1143  C CB  . ARG A  1 145 ? 43.531  24.804 86.839  1.00 61.05  ? 145  ARG A CB  1 
ATOM   1144  C CG  . ARG A  1 145 ? 42.790  23.487 86.743  1.00 62.37  ? 145  ARG A CG  1 
ATOM   1145  C CD  . ARG A  1 145 ? 43.701  22.407 86.196  1.00 64.28  ? 145  ARG A CD  1 
ATOM   1146  N NE  . ARG A  1 145 ? 42.964  21.183 85.910  1.00 65.49  ? 145  ARG A NE  1 
ATOM   1147  C CZ  . ARG A  1 145 ? 42.582  20.295 86.826  1.00 67.51  ? 145  ARG A CZ  1 
ATOM   1148  N NH1 . ARG A  1 145 ? 42.849  20.474 88.120  1.00 68.62  ? 145  ARG A NH1 1 
ATOM   1149  N NH2 . ARG A  1 145 ? 41.917  19.216 86.445  1.00 68.61  ? 145  ARG A NH2 1 
ATOM   1150  N N   . ASN A  1 146 ? 43.516  28.090 87.154  1.00 57.07  ? 146  ASN A N   1 
ATOM   1151  C CA  . ASN A  1 146 ? 44.409  29.249 87.068  1.00 56.32  ? 146  ASN A CA  1 
ATOM   1152  C C   . ASN A  1 146 ? 44.258  30.246 88.213  1.00 56.05  ? 146  ASN A C   1 
ATOM   1153  O O   . ASN A  1 146 ? 45.132  31.092 88.413  1.00 55.96  ? 146  ASN A O   1 
ATOM   1154  C CB  . ASN A  1 146 ? 44.237  29.954 85.718  1.00 54.46  ? 146  ASN A CB  1 
ATOM   1155  C CG  . ASN A  1 146 ? 44.818  29.150 84.570  1.00 55.08  ? 146  ASN A CG  1 
ATOM   1156  O OD1 . ASN A  1 146 ? 45.938  28.648 84.663  1.00 56.69  ? 146  ASN A OD1 1 
ATOM   1157  N ND2 . ASN A  1 146 ? 44.062  29.018 83.486  1.00 54.03  ? 146  ASN A ND2 1 
ATOM   1158  N N   . VAL A  1 147 ? 43.163  30.142 88.965  1.00 56.13  ? 147  VAL A N   1 
ATOM   1159  C CA  . VAL A  1 147 ? 42.935  31.023 90.113  1.00 56.18  ? 147  VAL A CA  1 
ATOM   1160  C C   . VAL A  1 147 ? 42.596  30.239 91.383  1.00 58.18  ? 147  VAL A C   1 
ATOM   1161  O O   . VAL A  1 147 ? 42.002  29.162 91.319  1.00 59.04  ? 147  VAL A O   1 
ATOM   1162  C CB  . VAL A  1 147 ? 41.833  32.064 89.828  1.00 54.26  ? 147  VAL A CB  1 
ATOM   1163  C CG1 . VAL A  1 147 ? 42.318  33.094 88.817  1.00 52.65  ? 147  VAL A CG1 1 
ATOM   1164  C CG2 . VAL A  1 147 ? 40.548  31.398 89.344  1.00 53.85  ? 147  VAL A CG2 1 
ATOM   1165  N N   . VAL A  1 148 ? 42.975  30.797 92.531  1.00 59.10  ? 148  VAL A N   1 
ATOM   1166  C CA  . VAL A  1 148 ? 42.817  30.133 93.827  1.00 61.36  ? 148  VAL A CA  1 
ATOM   1167  C C   . VAL A  1 148 ? 41.656  30.747 94.614  1.00 61.16  ? 148  VAL A C   1 
ATOM   1168  O O   . VAL A  1 148 ? 41.653  31.947 94.889  1.00 60.23  ? 148  VAL A O   1 
ATOM   1169  C CB  . VAL A  1 148 ? 44.104  30.255 94.676  1.00 63.02  ? 148  VAL A CB  1 
ATOM   1170  C CG1 . VAL A  1 148 ? 44.059  29.302 95.863  1.00 65.76  ? 148  VAL A CG1 1 
ATOM   1171  C CG2 . VAL A  1 148 ? 45.340  29.984 93.831  1.00 63.08  ? 148  VAL A CG2 1 
ATOM   1172  N N   . TRP A  1 149 ? 40.676  29.920 94.972  1.00 62.26  ? 149  TRP A N   1 
ATOM   1173  C CA  . TRP A  1 149 ? 39.583  30.348 95.842  1.00 62.72  ? 149  TRP A CA  1 
ATOM   1174  C C   . TRP A  1 149 ? 40.055  30.275 97.304  1.00 65.10  ? 149  TRP A C   1 
ATOM   1175  O O   . TRP A  1 149 ? 40.145  29.192 97.888  1.00 67.35  ? 149  TRP A O   1 
ATOM   1176  C CB  . TRP A  1 149 ? 38.348  29.466 95.619  1.00 63.19  ? 149  TRP A CB  1 
ATOM   1177  C CG  . TRP A  1 149 ? 37.075  29.963 96.268  1.00 63.47  ? 149  TRP A CG  1 
ATOM   1178  C CD1 . TRP A  1 149 ? 36.938  31.017 97.129  1.00 63.64  ? 149  TRP A CD1 1 
ATOM   1179  C CD2 . TRP A  1 149 ? 35.765  29.398 96.120  1.00 63.88  ? 149  TRP A CD2 1 
ATOM   1180  N NE1 . TRP A  1 149 ? 35.625  31.152 97.508  1.00 64.10  ? 149  TRP A NE1 1 
ATOM   1181  C CE2 . TRP A  1 149 ? 34.884  30.170 96.907  1.00 64.27  ? 149  TRP A CE2 1 
ATOM   1182  C CE3 . TRP A  1 149 ? 35.249  28.320 95.392  1.00 64.12  ? 149  TRP A CE3 1 
ATOM   1183  C CZ2 . TRP A  1 149 ? 33.516  29.899 96.986  1.00 64.92  ? 149  TRP A CZ2 1 
ATOM   1184  C CZ3 . TRP A  1 149 ? 33.888  28.050 95.473  1.00 64.69  ? 149  TRP A CZ3 1 
ATOM   1185  C CH2 . TRP A  1 149 ? 33.039  28.837 96.264  1.00 65.15  ? 149  TRP A CH2 1 
ATOM   1186  N N   . LEU A  1 150 ? 40.364  31.435 97.882  1.00 64.76  ? 150  LEU A N   1 
ATOM   1187  C CA  . LEU A  1 150 ? 40.924  31.505 99.232  1.00 67.00  ? 150  LEU A CA  1 
ATOM   1188  C C   . LEU A  1 150 ? 39.833  31.588 100.293 1.00 68.42  ? 150  LEU A C   1 
ATOM   1189  O O   . LEU A  1 150 ? 38.827  32.276 100.107 1.00 67.17  ? 150  LEU A O   1 
ATOM   1190  C CB  . LEU A  1 150 ? 41.860  32.712 99.369  1.00 66.22  ? 150  LEU A CB  1 
ATOM   1191  C CG  . LEU A  1 150 ? 43.172  32.678 98.581  1.00 65.54  ? 150  LEU A CG  1 
ATOM   1192  C CD1 . LEU A  1 150 ? 43.916  33.992 98.770  1.00 64.85  ? 150  LEU A CD1 1 
ATOM   1193  C CD2 . LEU A  1 150 ? 44.047  31.502 98.994  1.00 67.90  ? 150  LEU A CD2 1 
ATOM   1194  N N   . ILE A  1 151 ? 40.052  30.881 101.403 1.00 71.26  ? 151  ILE A N   1 
ATOM   1195  C CA  . ILE A  1 151 ? 39.146  30.909 102.556 1.00 73.21  ? 151  ILE A CA  1 
ATOM   1196  C C   . ILE A  1 151 ? 39.926  31.058 103.866 1.00 75.68  ? 151  ILE A C   1 
ATOM   1197  O O   . ILE A  1 151 ? 41.149  30.896 103.903 1.00 76.20  ? 151  ILE A O   1 
ATOM   1198  C CB  . ILE A  1 151 ? 38.252  29.647 102.614 1.00 74.80  ? 151  ILE A CB  1 
ATOM   1199  C CG1 . ILE A  1 151 ? 39.086  28.396 102.928 1.00 77.19  ? 151  ILE A CG1 1 
ATOM   1200  C CG2 . ILE A  1 151 ? 37.484  29.486 101.308 1.00 72.44  ? 151  ILE A CG2 1 
ATOM   1201  C CD1 . ILE A  1 151 ? 38.312  27.095 102.877 1.00 78.81  ? 151  ILE A CD1 1 
ATOM   1202  N N   . LYS A  1 152 ? 39.197  31.366 104.934 1.00 77.37  ? 152  LYS A N   1 
ATOM   1203  C CA  . LYS A  1 152 ? 39.777  31.583 106.267 1.00 79.97  ? 152  LYS A CA  1 
ATOM   1204  C C   . LYS A  1 152 ? 40.507  30.349 106.815 1.00 82.82  ? 152  LYS A C   1 
ATOM   1205  O O   . LYS A  1 152 ? 40.109  29.216 106.540 1.00 83.64  ? 152  LYS A O   1 
ATOM   1206  C CB  . LYS A  1 152 ? 38.670  31.996 107.244 1.00 81.53  ? 152  LYS A CB  1 
ATOM   1207  C CG  . LYS A  1 152 ? 37.675  30.887 107.553 1.00 83.57  ? 152  LYS A CG  1 
ATOM   1208  C CD  . LYS A  1 152 ? 36.400  31.419 108.183 1.00 84.49  ? 152  LYS A CD  1 
ATOM   1209  C CE  . LYS A  1 152 ? 35.615  30.298 108.850 1.00 87.60  ? 152  LYS A CE  1 
ATOM   1210  N NZ  . LYS A  1 152 ? 34.521  30.822 109.710 1.00 89.31  ? 152  LYS A NZ  1 
ATOM   1211  N N   . LYS A  1 153 ? 41.568  30.582 107.592 1.00 84.47  ? 153  LYS A N   1 
ATOM   1212  C CA  . LYS A  1 153 ? 42.293  29.505 108.286 1.00 87.70  ? 153  LYS A CA  1 
ATOM   1213  C C   . LYS A  1 153 ? 42.076  29.610 109.798 1.00 91.05  ? 153  LYS A C   1 
ATOM   1214  O O   . LYS A  1 153 ? 42.332  30.656 110.395 1.00 91.10  ? 153  LYS A O   1 
ATOM   1215  C CB  . LYS A  1 153 ? 43.798  29.547 107.971 1.00 87.44  ? 153  LYS A CB  1 
ATOM   1216  C CG  . LYS A  1 153 ? 44.490  28.189 108.139 1.00 90.09  ? 153  LYS A CG  1 
ATOM   1217  C CD  . LYS A  1 153 ? 45.957  28.245 108.589 1.00 91.76  ? 153  LYS A CD  1 
ATOM   1218  C CE  . LYS A  1 153 ? 46.926  27.884 107.466 1.00 90.38  ? 153  LYS A CE  1 
ATOM   1219  N NZ  . LYS A  1 153 ? 47.073  28.878 106.372 1.00 86.64  ? 153  LYS A NZ  1 
ATOM   1220  N N   . ASN A  1 154 ? 41.613  28.515 110.402 1.00 94.02  ? 154  ASN A N   1 
ATOM   1221  C CA  . ASN A  1 154 ? 41.270  28.459 111.832 1.00 97.66  ? 154  ASN A CA  1 
ATOM   1222  C C   . ASN A  1 154 ? 40.311  29.578 112.257 1.00 97.01  ? 154  ASN A C   1 
ATOM   1223  O O   . ASN A  1 154 ? 40.484  30.200 113.309 1.00 98.91  ? 154  ASN A O   1 
ATOM   1224  C CB  . ASN A  1 154 ? 42.536  28.456 112.706 1.00 100.19 ? 154  ASN A CB  1 
ATOM   1225  C CG  . ASN A  1 154 ? 42.287  27.892 114.099 1.00 104.74 ? 154  ASN A CG  1 
ATOM   1226  O OD1 . ASN A  1 154 ? 41.404  27.055 114.293 1.00 106.47 ? 154  ASN A OD1 1 
ATOM   1227  N ND2 . ASN A  1 154 ? 43.070  28.345 115.076 1.00 106.90 ? 154  ASN A ND2 1 
ATOM   1228  N N   . SER A  1 155 ? 39.305  29.823 111.417 1.00 94.47  ? 155  SER A N   1 
ATOM   1229  C CA  . SER A  1 155 ? 38.244  30.788 111.702 1.00 93.94  ? 155  SER A CA  1 
ATOM   1230  C C   . SER A  1 155 ? 38.746  32.239 111.748 1.00 92.22  ? 155  SER A C   1 
ATOM   1231  O O   . SER A  1 155 ? 38.274  33.033 112.558 1.00 93.40  ? 155  SER A O   1 
ATOM   1232  C CB  . SER A  1 155 ? 37.533  30.412 113.014 1.00 97.95  ? 155  SER A CB  1 
ATOM   1233  O OG  . SER A  1 155 ? 36.213  30.924 113.054 1.00 97.61  ? 155  SER A OG  1 
ATOM   1234  N N   . THR A  1 156 ? 39.710  32.577 110.891 1.00 89.68  ? 156  THR A N   1 
ATOM   1235  C CA  . THR A  1 156 ? 40.209  33.956 110.776 1.00 87.86  ? 156  THR A CA  1 
ATOM   1236  C C   . THR A  1 156 ? 40.657  34.224 109.341 1.00 84.22  ? 156  THR A C   1 
ATOM   1237  O O   . THR A  1 156 ? 41.436  33.449 108.786 1.00 83.92  ? 156  THR A O   1 
ATOM   1238  C CB  . THR A  1 156 ? 41.417  34.248 111.707 1.00 89.92  ? 156  THR A CB  1 
ATOM   1239  O OG1 . THR A  1 156 ? 42.637  33.846 111.069 1.00 89.02  ? 156  THR A OG1 1 
ATOM   1240  C CG2 . THR A  1 156 ? 41.298  33.543 113.065 1.00 94.15  ? 156  THR A CG2 1 
ATOM   1241  N N   . TYR A  1 157 ? 40.165  35.310 108.745 1.00 81.75  ? 157  TYR A N   1 
ATOM   1242  C CA  . TYR A  1 157 ? 40.600  35.733 107.410 1.00 78.44  ? 157  TYR A CA  1 
ATOM   1243  C C   . TYR A  1 157 ? 41.383  37.045 107.527 1.00 77.68  ? 157  TYR A C   1 
ATOM   1244  O O   . TYR A  1 157 ? 40.796  38.131 107.474 1.00 76.59  ? 157  TYR A O   1 
ATOM   1245  C CB  . TYR A  1 157 ? 39.402  35.901 106.468 1.00 76.17  ? 157  TYR A CB  1 
ATOM   1246  C CG  . TYR A  1 157 ? 39.764  35.930 104.988 1.00 73.11  ? 157  TYR A CG  1 
ATOM   1247  C CD1 . TYR A  1 157 ? 40.350  37.055 104.406 1.00 71.07  ? 157  TYR A CD1 1 
ATOM   1248  C CD2 . TYR A  1 157 ? 39.514  34.831 104.170 1.00 72.46  ? 157  TYR A CD2 1 
ATOM   1249  C CE1 . TYR A  1 157 ? 40.674  37.082 103.058 1.00 68.55  ? 157  TYR A CE1 1 
ATOM   1250  C CE2 . TYR A  1 157 ? 39.834  34.851 102.822 1.00 69.90  ? 157  TYR A CE2 1 
ATOM   1251  C CZ  . TYR A  1 157 ? 40.415  35.978 102.268 1.00 67.97  ? 157  TYR A CZ  1 
ATOM   1252  O OH  . TYR A  1 157 ? 40.735  35.998 100.924 1.00 65.67  ? 157  TYR A OH  1 
ATOM   1253  N N   . PRO A  1 158 ? 42.713  36.950 107.710 1.00 78.49  ? 158  PRO A N   1 
ATOM   1254  C CA  . PRO A  1 158 ? 43.528  38.164 107.780 1.00 77.88  ? 158  PRO A CA  1 
ATOM   1255  C C   . PRO A  1 158 ? 43.620  38.873 106.432 1.00 74.65  ? 158  PRO A C   1 
ATOM   1256  O O   . PRO A  1 158 ? 43.485  38.240 105.384 1.00 73.00  ? 158  PRO A O   1 
ATOM   1257  C CB  . PRO A  1 158 ? 44.905  37.654 108.228 1.00 79.69  ? 158  PRO A CB  1 
ATOM   1258  C CG  . PRO A  1 158 ? 44.922  36.205 107.893 1.00 80.30  ? 158  PRO A CG  1 
ATOM   1259  C CD  . PRO A  1 158 ? 43.504  35.730 107.960 1.00 80.39  ? 158  PRO A CD  1 
ATOM   1260  N N   . THR A  1 159 ? 43.841  40.182 106.473 1.00 74.01  ? 159  THR A N   1 
ATOM   1261  C CA  . THR A  1 159 ? 43.925  40.988 105.262 1.00 71.27  ? 159  THR A CA  1 
ATOM   1262  C C   . THR A  1 159 ? 45.084  40.505 104.393 1.00 70.50  ? 159  THR A C   1 
ATOM   1263  O O   . THR A  1 159 ? 46.176  40.220 104.896 1.00 72.07  ? 159  THR A O   1 
ATOM   1264  C CB  . THR A  1 159 ? 44.110  42.487 105.585 1.00 71.12  ? 159  THR A CB  1 
ATOM   1265  O OG1 . THR A  1 159 ? 43.105  42.908 106.515 1.00 72.45  ? 159  THR A OG1 1 
ATOM   1266  C CG2 . THR A  1 159 ? 44.005  43.337 104.325 1.00 68.37  ? 159  THR A CG2 1 
ATOM   1267  N N   . ILE A  1 160 ? 44.821  40.405 103.091 1.00 68.31  ? 160  ILE A N   1 
ATOM   1268  C CA  . ILE A  1 160 ? 45.813  39.982 102.106 1.00 67.49  ? 160  ILE A CA  1 
ATOM   1269  C C   . ILE A  1 160 ? 46.421  41.214 101.455 1.00 66.20  ? 160  ILE A C   1 
ATOM   1270  O O   . ILE A  1 160 ? 45.693  42.088 101.001 1.00 64.69  ? 160  ILE A O   1 
ATOM   1271  C CB  . ILE A  1 160 ? 45.172  39.110 101.004 1.00 65.90  ? 160  ILE A CB  1 
ATOM   1272  C CG1 . ILE A  1 160 ? 44.655  37.798 101.601 1.00 67.54  ? 160  ILE A CG1 1 
ATOM   1273  C CG2 . ILE A  1 160 ? 46.174  38.833 99.888  1.00 64.87  ? 160  ILE A CG2 1 
ATOM   1274  C CD1 . ILE A  1 160 ? 43.689  37.043 100.715 1.00 66.23  ? 160  ILE A CD1 1 
ATOM   1275  N N   . LYS A  1 161 ? 47.749  41.288 101.423 1.00 67.11  ? 161  LYS A N   1 
ATOM   1276  C CA  . LYS A  1 161 ? 48.451  42.331 100.674 1.00 66.08  ? 161  LYS A CA  1 
ATOM   1277  C C   . LYS A  1 161 ? 49.509  41.674 99.800  1.00 66.13  ? 161  LYS A C   1 
ATOM   1278  O O   . LYS A  1 161 ? 50.543  41.232 100.298 1.00 67.93  ? 161  LYS A O   1 
ATOM   1279  C CB  . LYS A  1 161 ? 49.092  43.358 101.612 1.00 67.45  ? 161  LYS A CB  1 
ATOM   1280  C CG  . LYS A  1 161 ? 48.093  44.113 102.474 1.00 67.83  ? 161  LYS A CG  1 
ATOM   1281  C CD  . LYS A  1 161 ? 48.730  45.302 103.177 1.00 68.94  ? 161  LYS A CD  1 
ATOM   1282  C CE  . LYS A  1 161 ? 47.713  46.042 104.036 1.00 69.55  ? 161  LYS A CE  1 
ATOM   1283  N NZ  . LYS A  1 161 ? 48.353  46.956 105.029 1.00 71.37  ? 161  LYS A NZ  1 
ATOM   1284  N N   . ARG A  1 162 ? 49.242  41.605 98.499  1.00 64.48  ? 162  ARG A N   1 
ATOM   1285  C CA  . ARG A  1 162 ? 50.139  40.929 97.565  1.00 64.62  ? 162  ARG A CA  1 
ATOM   1286  C C   . ARG A  1 162 ? 50.445  41.802 96.350  1.00 63.35  ? 162  ARG A C   1 
ATOM   1287  O O   . ARG A  1 162 ? 49.563  42.465 95.802  1.00 61.68  ? 162  ARG A O   1 
ATOM   1288  C CB  . ARG A  1 162 ? 49.561  39.575 97.129  1.00 64.30  ? 162  ARG A CB  1 
ATOM   1289  C CG  . ARG A  1 162 ? 49.717  38.446 98.127  1.00 66.44  ? 162  ARG A CG  1 
ATOM   1290  C CD  . ARG A  1 162 ? 51.170  38.198 98.547  1.00 68.45  ? 162  ARG A CD  1 
ATOM   1291  N NE  . ARG A  1 162 ? 51.594  36.844 98.212  1.00 69.46  ? 162  ARG A NE  1 
ATOM   1292  C CZ  . ARG A  1 162 ? 51.214  35.767 98.889  1.00 70.93  ? 162  ARG A CZ  1 
ATOM   1293  N NH1 . ARG A  1 162 ? 50.401  35.871 99.936  1.00 71.58  ? 162  ARG A NH1 1 
ATOM   1294  N NH2 . ARG A  1 162 ? 51.642  34.576 98.515  1.00 71.97  ? 162  ARG A NH2 1 
ATOM   1295  N N   . SER A  1 163 ? 51.714  41.796 95.951  1.00 64.58  ? 163  SER A N   1 
ATOM   1296  C CA  . SER A  1 163 ? 52.195  42.588 94.834  1.00 63.95  ? 163  SER A CA  1 
ATOM   1297  C C   . SER A  1 163 ? 53.042  41.717 93.913  1.00 64.92  ? 163  SER A C   1 
ATOM   1298  O O   . SER A  1 163 ? 53.858  40.927 94.387  1.00 66.70  ? 163  SER A O   1 
ATOM   1299  C CB  . SER A  1 163 ? 53.025  43.765 95.352  1.00 64.83  ? 163  SER A CB  1 
ATOM   1300  O OG  . SER A  1 163 ? 53.514  44.559 94.285  1.00 64.09  ? 163  SER A OG  1 
ATOM   1301  N N   . TYR A  1 164 ? 52.841  41.852 92.602  1.00 64.22  ? 164  TYR A N   1 
ATOM   1302  C CA  . TYR A  1 164 ? 53.704  41.193 91.621  1.00 65.41  ? 164  TYR A CA  1 
ATOM   1303  C C   . TYR A  1 164 ? 54.302  42.191 90.636  1.00 65.85  ? 164  TYR A C   1 
ATOM   1304  O O   . TYR A  1 164 ? 53.577  42.977 90.033  1.00 64.21  ? 164  TYR A O   1 
ATOM   1305  C CB  . TYR A  1 164 ? 52.956  40.117 90.834  1.00 64.37  ? 164  TYR A CB  1 
ATOM   1306  C CG  . TYR A  1 164 ? 53.769  39.651 89.649  1.00 64.71  ? 164  TYR A CG  1 
ATOM   1307  C CD1 . TYR A  1 164 ? 54.805  38.733 89.809  1.00 66.68  ? 164  TYR A CD1 1 
ATOM   1308  C CD2 . TYR A  1 164 ? 53.543  40.172 88.377  1.00 63.36  ? 164  TYR A CD2 1 
ATOM   1309  C CE1 . TYR A  1 164 ? 55.573  38.323 88.728  1.00 67.28  ? 164  TYR A CE1 1 
ATOM   1310  C CE2 . TYR A  1 164 ? 54.303  39.769 87.290  1.00 63.94  ? 164  TYR A CE2 1 
ATOM   1311  C CZ  . TYR A  1 164 ? 55.316  38.844 87.468  1.00 65.90  ? 164  TYR A CZ  1 
ATOM   1312  O OH  . TYR A  1 164 ? 56.071  38.442 86.392  1.00 66.70  ? 164  TYR A OH  1 
ATOM   1313  N N   . ASN A  1 165 ? 55.621  42.117 90.454  1.00 68.68  ? 165  ASN A N   1 
ATOM   1314  C CA  . ASN A  1 165 ? 56.345  42.964 89.508  1.00 69.95  ? 165  ASN A CA  1 
ATOM   1315  C C   . ASN A  1 165 ? 56.606  42.221 88.197  1.00 68.94  ? 165  ASN A C   1 
ATOM   1316  O O   . ASN A  1 165 ? 57.236  41.164 88.195  1.00 70.29  ? 165  ASN A O   1 
ATOM   1317  C CB  . ASN A  1 165 ? 57.678  43.395 90.124  1.00 74.11  ? 165  ASN A CB  1 
ATOM   1318  C CG  . ASN A  1 165 ? 58.312  44.568 89.401  1.00 77.07  ? 165  ASN A CG  1 
ATOM   1319  O OD1 . ASN A  1 165 ? 57.930  44.915 88.283  1.00 75.79  ? 165  ASN A OD1 1 
ATOM   1320  N ND2 . ASN A  1 165 ? 59.295  45.185 90.044  1.00 82.37  ? 165  ASN A ND2 1 
ATOM   1321  N N   . ASN A  1 166 ? 56.136  42.786 87.086  1.00 66.54  ? 166  ASN A N   1 
ATOM   1322  C CA  . ASN A  1 166 ? 56.321  42.173 85.769  1.00 65.75  ? 166  ASN A CA  1 
ATOM   1323  C C   . ASN A  1 166 ? 57.735  42.393 85.228  1.00 66.99  ? 166  ASN A C   1 
ATOM   1324  O O   . ASN A  1 166 ? 58.009  43.388 84.554  1.00 66.84  ? 166  ASN A O   1 
ATOM   1325  C CB  . ASN A  1 166 ? 55.283  42.708 84.775  1.00 63.74  ? 166  ASN A CB  1 
ATOM   1326  C CG  . ASN A  1 166 ? 55.228  41.895 83.493  1.00 63.59  ? 166  ASN A CG  1 
ATOM   1327  O OD1 . ASN A  1 166 ? 55.628  40.730 83.464  1.00 64.56  ? 166  ASN A OD1 1 
ATOM   1328  N ND2 . ASN A  1 166 ? 54.718  42.503 82.427  1.00 62.48  ? 166  ASN A ND2 1 
ATOM   1329  N N   . THR A  1 167 ? 58.623  41.449 85.531  1.00 68.13  ? 167  THR A N   1 
ATOM   1330  C CA  . THR A  1 167 ? 60.023  41.511 85.097  1.00 69.83  ? 167  THR A CA  1 
ATOM   1331  C C   . THR A  1 167 ? 60.245  40.949 83.685  1.00 69.74  ? 167  THR A C   1 
ATOM   1332  O O   . THR A  1 167 ? 61.338  41.091 83.129  1.00 71.59  ? 167  THR A O   1 
ATOM   1333  C CB  . THR A  1 167 ? 60.943  40.748 86.071  1.00 71.99  ? 167  THR A CB  1 
ATOM   1334  O OG1 . THR A  1 167 ? 60.503  39.387 86.180  1.00 71.98  ? 167  THR A OG1 1 
ATOM   1335  C CG2 . THR A  1 167 ? 60.927  41.402 87.443  1.00 72.07  ? 167  THR A CG2 1 
ATOM   1336  N N   . ASN A  1 168 ? 59.223  40.309 83.116  1.00 67.64  ? 168  ASN A N   1 
ATOM   1337  C CA  . ASN A  1 168 ? 59.291  39.822 81.734  1.00 67.50  ? 168  ASN A CA  1 
ATOM   1338  C C   . ASN A  1 168 ? 59.207  41.024 80.815  1.00 66.43  ? 168  ASN A C   1 
ATOM   1339  O O   . ASN A  1 168 ? 58.533  41.998 81.147  1.00 64.89  ? 168  ASN A O   1 
ATOM   1340  C CB  . ASN A  1 168 ? 58.137  38.867 81.385  1.00 66.00  ? 168  ASN A CB  1 
ATOM   1341  C CG  . ASN A  1 168 ? 57.707  37.997 82.548  1.00 65.89  ? 168  ASN A CG  1 
ATOM   1342  O OD1 . ASN A  1 168 ? 58.137  36.850 82.667  1.00 67.40  ? 168  ASN A OD1 1 
ATOM   1343  N ND2 . ASN A  1 168 ? 56.844  38.534 83.406  1.00 64.33  ? 168  ASN A ND2 1 
ATOM   1344  N N   . GLN A  1 169 ? 59.874  40.968 79.665  1.00 67.32  ? 169  GLN A N   1 
ATOM   1345  C CA  . GLN A  1 169 ? 59.729  42.035 78.674  1.00 66.56  ? 169  GLN A CA  1 
ATOM   1346  C C   . GLN A  1 169 ? 58.555  41.722 77.729  1.00 64.56  ? 169  GLN A C   1 
ATOM   1347  O O   . GLN A  1 169 ? 58.708  41.619 76.511  1.00 65.24  ? 169  GLN A O   1 
ATOM   1348  C CB  . GLN A  1 169 ? 61.045  42.321 77.936  1.00 69.05  ? 169  GLN A CB  1 
ATOM   1349  C CG  . GLN A  1 169 ? 61.650  41.177 77.133  1.00 70.87  ? 169  GLN A CG  1 
ATOM   1350  C CD  . GLN A  1 169 ? 62.531  41.679 75.996  1.00 72.91  ? 169  GLN A CD  1 
ATOM   1351  O OE1 . GLN A  1 169 ? 63.536  41.059 75.647  1.00 75.36  ? 169  GLN A OE1 1 
ATOM   1352  N NE2 . GLN A  1 169 ? 62.156  42.814 75.416  1.00 72.09  ? 169  GLN A NE2 1 
ATOM   1353  N N   . GLU A  1 170 ? 57.378  41.571 78.333  1.00 62.16  ? 170  GLU A N   1 
ATOM   1354  C CA  . GLU A  1 170 ? 56.140  41.257 77.630  1.00 60.19  ? 170  GLU A CA  1 
ATOM   1355  C C   . GLU A  1 170 ? 54.966  41.880 78.382  1.00 57.86  ? 170  GLU A C   1 
ATOM   1356  O O   . GLU A  1 170 ? 55.056  42.141 79.584  1.00 57.71  ? 170  GLU A O   1 
ATOM   1357  C CB  . GLU A  1 170 ? 55.917  39.740 77.546  1.00 60.37  ? 170  GLU A CB  1 
ATOM   1358  C CG  . GLU A  1 170 ? 56.756  39.007 76.505  1.00 62.31  ? 170  GLU A CG  1 
ATOM   1359  C CD  . GLU A  1 170 ? 57.974  38.297 77.080  1.00 64.56  ? 170  GLU A CD  1 
ATOM   1360  O OE1 . GLU A  1 170 ? 58.449  38.672 78.174  1.00 64.95  ? 170  GLU A OE1 1 
ATOM   1361  O OE2 . GLU A  1 170 ? 58.464  37.351 76.428  1.00 66.10  ? 170  GLU A OE2 1 
ATOM   1362  N N   . ASP A  1 171 ? 53.874  42.132 77.663  1.00 56.16  ? 171  ASP A N   1 
ATOM   1363  C CA  . ASP A  1 171 ? 52.587  42.407 78.291  1.00 54.08  ? 171  ASP A CA  1 
ATOM   1364  C C   . ASP A  1 171 ? 52.137  41.103 78.949  1.00 53.57  ? 171  ASP A C   1 
ATOM   1365  O O   . ASP A  1 171 ? 52.457  40.014 78.460  1.00 54.37  ? 171  ASP A O   1 
ATOM   1366  C CB  . ASP A  1 171 ? 51.538  42.864 77.260  1.00 52.87  ? 171  ASP A CB  1 
ATOM   1367  C CG  . ASP A  1 171 ? 51.823  44.252 76.677  1.00 53.25  ? 171  ASP A CG  1 
ATOM   1368  O OD1 . ASP A  1 171 ? 52.514  45.075 77.316  1.00 53.93  ? 171  ASP A OD1 1 
ATOM   1369  O OD2 . ASP A  1 171 ? 51.328  44.524 75.564  1.00 53.00  ? 171  ASP A OD2 1 
ATOM   1370  N N   . LEU A  1 172 ? 51.407  41.217 80.055  1.00 52.39  ? 172  LEU A N   1 
ATOM   1371  C CA  . LEU A  1 172 ? 50.949  40.047 80.794  1.00 52.13  ? 172  LEU A CA  1 
ATOM   1372  C C   . LEU A  1 172 ? 49.452  40.113 81.063  1.00 50.33  ? 172  LEU A C   1 
ATOM   1373  O O   . LEU A  1 172 ? 48.960  41.090 81.627  1.00 49.53  ? 172  LEU A O   1 
ATOM   1374  C CB  . LEU A  1 172 ? 51.700  39.937 82.119  1.00 53.22  ? 172  LEU A CB  1 
ATOM   1375  C CG  . LEU A  1 172 ? 51.519  38.596 82.840  1.00 53.78  ? 172  LEU A CG  1 
ATOM   1376  C CD1 . LEU A  1 172 ? 52.498  37.564 82.295  1.00 55.46  ? 172  LEU A CD1 1 
ATOM   1377  C CD2 . LEU A  1 172 ? 51.694  38.754 84.343  1.00 54.33  ? 172  LEU A CD2 1 
ATOM   1378  N N   . LEU A  1 173 ? 48.738  39.062 80.665  1.00 49.82  ? 173  LEU A N   1 
ATOM   1379  C CA  . LEU A  1 173 ? 47.313  38.945 80.948  1.00 48.41  ? 173  LEU A CA  1 
ATOM   1380  C C   . LEU A  1 173 ? 47.097  38.337 82.330  1.00 48.71  ? 173  LEU A C   1 
ATOM   1381  O O   . LEU A  1 173 ? 47.328  37.144 82.533  1.00 49.60  ? 173  LEU A O   1 
ATOM   1382  C CB  . LEU A  1 173 ? 46.616  38.078 79.900  1.00 47.99  ? 173  LEU A CB  1 
ATOM   1383  C CG  . LEU A  1 173 ? 45.138  37.766 80.178  1.00 46.88  ? 173  LEU A CG  1 
ATOM   1384  C CD1 . LEU A  1 173 ? 44.282  39.024 80.125  1.00 45.66  ? 173  LEU A CD1 1 
ATOM   1385  C CD2 . LEU A  1 173 ? 44.625  36.728 79.195  1.00 46.85  ? 173  LEU A CD2 1 
ATOM   1386  N N   . VAL A  1 174 ? 46.635  39.164 83.263  1.00 48.13  ? 174  VAL A N   1 
ATOM   1387  C CA  . VAL A  1 174 ? 46.338  38.729 84.621  1.00 48.53  ? 174  VAL A CA  1 
ATOM   1388  C C   . VAL A  1 174 ? 44.827  38.579 84.781  1.00 47.47  ? 174  VAL A C   1 
ATOM   1389  O O   . VAL A  1 174 ? 44.067  39.476 84.409  1.00 46.39  ? 174  VAL A O   1 
ATOM   1390  C CB  . VAL A  1 174 ? 46.855  39.745 85.662  1.00 48.96  ? 174  VAL A CB  1 
ATOM   1391  C CG1 . VAL A  1 174 ? 46.755  39.167 87.068  1.00 49.90  ? 174  VAL A CG1 1 
ATOM   1392  C CG2 . VAL A  1 174 ? 48.289  40.150 85.355  1.00 49.90  ? 174  VAL A CG2 1 
ATOM   1393  N N   . LEU A  1 175 ? 44.405  37.445 85.336  1.00 48.00  ? 175  LEU A N   1 
ATOM   1394  C CA  . LEU A  1 175 ? 42.999  37.180 85.629  1.00 47.38  ? 175  LEU A CA  1 
ATOM   1395  C C   . LEU A  1 175 ? 42.804  37.000 87.129  1.00 48.31  ? 175  LEU A C   1 
ATOM   1396  O O   . LEU A  1 175 ? 43.626  36.375 87.791  1.00 49.64  ? 175  LEU A O   1 
ATOM   1397  C CB  . LEU A  1 175 ? 42.542  35.904 84.927  1.00 47.47  ? 175  LEU A CB  1 
ATOM   1398  C CG  . LEU A  1 175 ? 42.730  35.827 83.413  1.00 46.89  ? 175  LEU A CG  1 
ATOM   1399  C CD1 . LEU A  1 175 ? 42.401  34.427 82.915  1.00 47.40  ? 175  LEU A CD1 1 
ATOM   1400  C CD2 . LEU A  1 175 ? 41.872  36.867 82.716  1.00 45.49  ? 175  LEU A CD2 1 
ATOM   1401  N N   . TRP A  1 176 ? 41.711  37.544 87.655  1.00 47.80  ? 176  TRP A N   1 
ATOM   1402  C CA  . TRP A  1 176 ? 41.310  37.301 89.040  1.00 48.83  ? 176  TRP A CA  1 
ATOM   1403  C C   . TRP A  1 176 ? 39.790  37.372 89.168  1.00 48.36  ? 176  TRP A C   1 
ATOM   1404  O O   . TRP A  1 176 ? 39.089  37.649 88.194  1.00 47.18  ? 176  TRP A O   1 
ATOM   1405  C CB  . TRP A  1 176 ? 41.988  38.297 89.988  1.00 49.37  ? 176  TRP A CB  1 
ATOM   1406  C CG  . TRP A  1 176 ? 41.529  39.713 89.831  1.00 48.33  ? 176  TRP A CG  1 
ATOM   1407  C CD1 . TRP A  1 176 ? 40.594  40.364 90.585  1.00 48.39  ? 176  TRP A CD1 1 
ATOM   1408  C CD2 . TRP A  1 176 ? 41.991  40.658 88.862  1.00 47.35  ? 176  TRP A CD2 1 
ATOM   1409  N NE1 . TRP A  1 176 ? 40.444  41.654 90.144  1.00 47.51  ? 176  TRP A NE1 1 
ATOM   1410  C CE2 . TRP A  1 176 ? 41.291  41.861 89.085  1.00 46.86  ? 176  TRP A CE2 1 
ATOM   1411  C CE3 . TRP A  1 176 ? 42.929  40.603 87.823  1.00 47.05  ? 176  TRP A CE3 1 
ATOM   1412  C CZ2 . TRP A  1 176 ? 41.497  43.002 88.305  1.00 46.09  ? 176  TRP A CZ2 1 
ATOM   1413  C CZ3 . TRP A  1 176 ? 43.134  41.735 87.052  1.00 46.30  ? 176  TRP A CZ3 1 
ATOM   1414  C CH2 . TRP A  1 176 ? 42.422  42.919 87.298  1.00 45.83  ? 176  TRP A CH2 1 
ATOM   1415  N N   . GLY A  1 177 ? 39.284  37.118 90.369  1.00 49.49  ? 177  GLY A N   1 
ATOM   1416  C CA  . GLY A  1 177 ? 37.843  37.097 90.592  1.00 49.43  ? 177  GLY A CA  1 
ATOM   1417  C C   . GLY A  1 177 ? 37.411  37.523 91.979  1.00 50.60  ? 177  GLY A C   1 
ATOM   1418  O O   . GLY A  1 177 ? 38.222  37.611 92.905  1.00 51.71  ? 177  GLY A O   1 
ATOM   1419  N N   . ILE A  1 178 ? 36.116  37.790 92.102  1.00 50.53  ? 178  ILE A N   1 
ATOM   1420  C CA  . ILE A  1 178 ? 35.470  38.056 93.381  1.00 51.92  ? 178  ILE A CA  1 
ATOM   1421  C C   . ILE A  1 178 ? 34.318  37.062 93.517  1.00 52.77  ? 178  ILE A C   1 
ATOM   1422  O O   . ILE A  1 178 ? 33.671  36.722 92.524  1.00 51.83  ? 178  ILE A O   1 
ATOM   1423  C CB  . ILE A  1 178 ? 34.946  39.515 93.469  1.00 51.38  ? 178  ILE A CB  1 
ATOM   1424  C CG1 . ILE A  1 178 ? 34.636  39.891 94.933  1.00 53.12  ? 178  ILE A CG1 1 
ATOM   1425  C CG2 . ILE A  1 178 ? 33.768  39.731 92.519  1.00 50.32  ? 178  ILE A CG2 1 
ATOM   1426  C CD1 . ILE A  1 178 ? 33.458  40.821 95.151  1.00 53.30  ? 178  ILE A CD1 1 
ATOM   1427  N N   . HIS A  1 179 ? 34.068  36.592 94.735  1.00 54.73  ? 179  HIS A N   1 
ATOM   1428  C CA  . HIS A  1 179 ? 32.941  35.698 94.992  1.00 55.91  ? 179  HIS A CA  1 
ATOM   1429  C C   . HIS A  1 179 ? 31.770  36.437 95.636  1.00 56.70  ? 179  HIS A C   1 
ATOM   1430  O O   . HIS A  1 179 ? 31.945  37.188 96.600  1.00 57.63  ? 179  HIS A O   1 
ATOM   1431  C CB  . HIS A  1 179 ? 33.357  34.534 95.889  1.00 57.98  ? 179  HIS A CB  1 
ATOM   1432  C CG  . HIS A  1 179 ? 32.214  33.658 96.297  1.00 59.58  ? 179  HIS A CG  1 
ATOM   1433  N ND1 . HIS A  1 179 ? 31.857  33.466 97.615  1.00 61.95  ? 179  HIS A ND1 1 
ATOM   1434  C CD2 . HIS A  1 179 ? 31.328  32.948 95.560  1.00 59.32  ? 179  HIS A CD2 1 
ATOM   1435  C CE1 . HIS A  1 179 ? 30.813  32.658 97.673  1.00 63.12  ? 179  HIS A CE1 1 
ATOM   1436  N NE2 . HIS A  1 179 ? 30.472  32.330 96.440  1.00 61.54  ? 179  HIS A NE2 1 
ATOM   1437  N N   . HIS A  1 180 ? 30.576  36.202 95.097  1.00 56.53  ? 180  HIS A N   1 
ATOM   1438  C CA  . HIS A  1 180 ? 29.343  36.764 95.631  1.00 57.54  ? 180  HIS A CA  1 
ATOM   1439  C C   . HIS A  1 180 ? 28.582  35.654 96.358  1.00 59.75  ? 180  HIS A C   1 
ATOM   1440  O O   . HIS A  1 180 ? 28.083  34.726 95.717  1.00 59.66  ? 180  HIS A O   1 
ATOM   1441  C CB  . HIS A  1 180 ? 28.490  37.329 94.497  1.00 56.04  ? 180  HIS A CB  1 
ATOM   1442  C CG  . HIS A  1 180 ? 29.166  38.412 93.712  1.00 54.11  ? 180  HIS A CG  1 
ATOM   1443  N ND1 . HIS A  1 180 ? 28.777  39.731 93.783  1.00 53.90  ? 180  HIS A ND1 1 
ATOM   1444  C CD2 . HIS A  1 180 ? 30.197  38.373 92.834  1.00 52.52  ? 180  HIS A CD2 1 
ATOM   1445  C CE1 . HIS A  1 180 ? 29.539  40.459 92.988  1.00 52.25  ? 180  HIS A CE1 1 
ATOM   1446  N NE2 . HIS A  1 180 ? 30.410  39.659 92.400  1.00 51.39  ? 180  HIS A NE2 1 
ATOM   1447  N N   . PRO A  1 181 ? 28.502  35.736 97.701  1.00 61.91  ? 181  PRO A N   1 
ATOM   1448  C CA  . PRO A  1 181 ? 27.843  34.693 98.485  1.00 64.38  ? 181  PRO A CA  1 
ATOM   1449  C C   . PRO A  1 181 ? 26.321  34.835 98.493  1.00 65.31  ? 181  PRO A C   1 
ATOM   1450  O O   . PRO A  1 181 ? 25.794  35.897 98.157  1.00 64.39  ? 181  PRO A O   1 
ATOM   1451  C CB  . PRO A  1 181 ? 28.410  34.912 99.888  1.00 66.38  ? 181  PRO A CB  1 
ATOM   1452  C CG  . PRO A  1 181 ? 28.660  36.380 99.954  1.00 65.31  ? 181  PRO A CG  1 
ATOM   1453  C CD  . PRO A  1 181 ? 29.019  36.820 98.559  1.00 62.36  ? 181  PRO A CD  1 
ATOM   1454  N N   . ASN A  1 182 ? 25.634  33.768 98.885  1.00 67.34  ? 182  ASN A N   1 
ATOM   1455  C CA  . ASN A  1 182 ? 24.168  33.738 98.901  1.00 68.59  ? 182  ASN A CA  1 
ATOM   1456  C C   . ASN A  1 182 ? 23.530  34.634 99.963  1.00 70.48  ? 182  ASN A C   1 
ATOM   1457  O O   . ASN A  1 182 ? 22.575  35.358 99.670  1.00 70.33  ? 182  ASN A O   1 
ATOM   1458  C CB  . ASN A  1 182 ? 23.679  32.299 99.085  1.00 70.55  ? 182  ASN A CB  1 
ATOM   1459  C CG  . ASN A  1 182 ? 23.878  31.463 97.841  1.00 68.84  ? 182  ASN A CG  1 
ATOM   1460  O OD1 . ASN A  1 182 ? 23.168  31.641 96.859  1.00 67.56  ? 182  ASN A OD1 1 
ATOM   1461  N ND2 . ASN A  1 182 ? 24.849  30.556 97.870  1.00 68.97  ? 182  ASN A ND2 1 
ATOM   1462  N N   . ASP A  1 183 ? 24.058  34.573 101.186 1.00 72.43  ? 183  ASP A N   1 
ATOM   1463  C CA  . ASP A  1 183 ? 23.518  35.339 102.318 1.00 74.69  ? 183  ASP A CA  1 
ATOM   1464  C C   . ASP A  1 183 ? 24.606  35.734 103.325 1.00 75.49  ? 183  ASP A C   1 
ATOM   1465  O O   . ASP A  1 183 ? 25.757  35.308 103.207 1.00 74.52  ? 183  ASP A O   1 
ATOM   1466  C CB  . ASP A  1 183 ? 22.397  34.546 103.012 1.00 77.88  ? 183  ASP A CB  1 
ATOM   1467  C CG  . ASP A  1 183 ? 22.804  33.117 103.358 1.00 79.37  ? 183  ASP A CG  1 
ATOM   1468  O OD1 . ASP A  1 183 ? 23.928  32.904 103.862 1.00 79.56  ? 183  ASP A OD1 1 
ATOM   1469  O OD2 . ASP A  1 183 ? 21.987  32.200 103.133 1.00 80.54  ? 183  ASP A OD2 1 
ATOM   1470  N N   . ALA A  1 184 ? 24.226  36.548 104.309 1.00 77.42  ? 184  ALA A N   1 
ATOM   1471  C CA  . ALA A  1 184 ? 25.153  37.032 105.342 1.00 78.52  ? 184  ALA A CA  1 
ATOM   1472  C C   . ALA A  1 184 ? 25.780  35.901 106.165 1.00 80.63  ? 184  ALA A C   1 
ATOM   1473  O O   . ALA A  1 184 ? 26.916  36.024 106.626 1.00 80.62  ? 184  ALA A O   1 
ATOM   1474  C CB  . ALA A  1 184 ? 24.447  38.020 106.262 1.00 80.66  ? 184  ALA A CB  1 
ATOM   1475  N N   . ALA A  1 185 ? 25.035  34.811 106.344 1.00 82.61  ? 185  ALA A N   1 
ATOM   1476  C CA  . ALA A  1 185 ? 25.528  33.634 107.062 1.00 84.92  ? 185  ALA A CA  1 
ATOM   1477  C C   . ALA A  1 185 ? 26.639  32.913 106.295 1.00 82.87  ? 185  ALA A C   1 
ATOM   1478  O O   . ALA A  1 185 ? 27.597  32.420 106.894 1.00 84.03  ? 185  ALA A O   1 
ATOM   1479  C CB  . ALA A  1 185 ? 24.381  32.676 107.350 1.00 87.59  ? 185  ALA A CB  1 
ATOM   1480  N N   . GLU A  1 186 ? 26.507  32.853 104.972 1.00 80.05  ? 186  GLU A N   1 
ATOM   1481  C CA  . GLU A  1 186 ? 27.523  32.226 104.125 1.00 78.07  ? 186  GLU A CA  1 
ATOM   1482  C C   . GLU A  1 186 ? 28.784  33.085 104.014 1.00 76.17  ? 186  GLU A C   1 
ATOM   1483  O O   . GLU A  1 186 ? 29.896  32.554 103.954 1.00 75.90  ? 186  GLU A O   1 
ATOM   1484  C CB  . GLU A  1 186 ? 26.959  31.936 102.733 1.00 75.83  ? 186  GLU A CB  1 
ATOM   1485  C CG  . GLU A  1 186 ? 27.913  31.157 101.840 1.00 74.17  ? 186  GLU A CG  1 
ATOM   1486  C CD  . GLU A  1 186 ? 27.210  30.456 100.696 1.00 73.13  ? 186  GLU A CD  1 
ATOM   1487  O OE1 . GLU A  1 186 ? 26.820  31.144 99.728  1.00 70.79  ? 186  GLU A OE1 1 
ATOM   1488  O OE2 . GLU A  1 186 ? 27.056  29.216 100.760 1.00 74.71  ? 186  GLU A OE2 1 
ATOM   1489  N N   . GLN A  1 187 ? 28.606  34.405 103.979 1.00 75.03  ? 187  GLN A N   1 
ATOM   1490  C CA  . GLN A  1 187 ? 29.731  35.345 103.984 1.00 73.59  ? 187  GLN A CA  1 
ATOM   1491  C C   . GLN A  1 187 ? 30.634  35.095 105.192 1.00 75.91  ? 187  GLN A C   1 
ATOM   1492  O O   . GLN A  1 187 ? 31.854  34.976 105.053 1.00 75.11  ? 187  GLN A O   1 
ATOM   1493  C CB  . GLN A  1 187 ? 29.221  36.796 103.986 1.00 72.80  ? 187  GLN A CB  1 
ATOM   1494  C CG  . GLN A  1 187 ? 30.283  37.864 104.240 1.00 71.96  ? 187  GLN A CG  1 
ATOM   1495  C CD  . GLN A  1 187 ? 31.423  37.825 103.232 1.00 69.33  ? 187  GLN A CD  1 
ATOM   1496  O OE1 . GLN A  1 187 ? 31.195  37.757 102.026 1.00 67.12  ? 187  GLN A OE1 1 
ATOM   1497  N NE2 . GLN A  1 187 ? 32.657  37.876 103.725 1.00 69.73  ? 187  GLN A NE2 1 
ATOM   1498  N N   . THR A  1 188 ? 30.023  35.010 106.371 1.00 78.99  ? 188  THR A N   1 
ATOM   1499  C CA  . THR A  1 188 ? 30.761  34.759 107.604 1.00 81.67  ? 188  THR A CA  1 
ATOM   1500  C C   . THR A  1 188 ? 31.341  33.339 107.635 1.00 82.82  ? 188  THR A C   1 
ATOM   1501  O O   . THR A  1 188 ? 32.472  33.133 108.076 1.00 83.55  ? 188  THR A O   1 
ATOM   1502  C CB  . THR A  1 188 ? 29.877  34.970 108.849 1.00 85.01  ? 188  THR A CB  1 
ATOM   1503  O OG1 . THR A  1 188 ? 28.715  34.135 108.762 1.00 86.36  ? 188  THR A OG1 1 
ATOM   1504  C CG2 . THR A  1 188 ? 29.447  36.433 108.975 1.00 84.36  ? 188  THR A CG2 1 
ATOM   1505  N N   . LYS A  1 189 ? 30.569  32.364 107.163 1.00 83.16  ? 189  LYS A N   1 
ATOM   1506  C CA  . LYS A  1 189 ? 31.027  30.974 107.124 1.00 84.42  ? 189  LYS A CA  1 
ATOM   1507  C C   . LYS A  1 189 ? 32.324  30.808 106.326 1.00 82.24  ? 189  LYS A C   1 
ATOM   1508  O O   . LYS A  1 189 ? 33.211  30.059 106.729 1.00 83.75  ? 189  LYS A O   1 
ATOM   1509  C CB  . LYS A  1 189 ? 29.938  30.066 106.541 1.00 84.67  ? 189  LYS A CB  1 
ATOM   1510  C CG  . LYS A  1 189 ? 30.391  28.633 106.292 1.00 85.64  ? 189  LYS A CG  1 
ATOM   1511  C CD  . LYS A  1 189 ? 29.211  27.681 106.172 1.00 87.25  ? 189  LYS A CD  1 
ATOM   1512  C CE  . LYS A  1 189 ? 29.660  26.254 105.885 1.00 88.33  ? 189  LYS A CE  1 
ATOM   1513  N NZ  . LYS A  1 189 ? 29.698  25.958 104.424 1.00 85.36  ? 189  LYS A NZ  1 
ATOM   1514  N N   . LEU A  1 190 ? 32.422  31.511 105.201 1.00 78.96  ? 190  LEU A N   1 
ATOM   1515  C CA  . LEU A  1 190 ? 33.574  31.395 104.303 1.00 76.84  ? 190  LEU A CA  1 
ATOM   1516  C C   . LEU A  1 190 ? 34.744  32.286 104.711 1.00 76.38  ? 190  LEU A C   1 
ATOM   1517  O O   . LEU A  1 190 ? 35.887  31.829 104.777 1.00 76.81  ? 190  LEU A O   1 
ATOM   1518  C CB  . LEU A  1 190 ? 33.157  31.745 102.874 1.00 73.74  ? 190  LEU A CB  1 
ATOM   1519  C CG  . LEU A  1 190 ? 32.492  30.610 102.094 1.00 73.74  ? 190  LEU A CG  1 
ATOM   1520  C CD1 . LEU A  1 190 ? 31.465  31.142 101.107 1.00 71.61  ? 190  LEU A CD1 1 
ATOM   1521  C CD2 . LEU A  1 190 ? 33.546  29.780 101.380 1.00 73.11  ? 190  LEU A CD2 1 
ATOM   1522  N N   . TYR A  1 191 ? 34.448  33.560 104.960 1.00 75.59  ? 191  TYR A N   1 
ATOM   1523  C CA  . TYR A  1 191 ? 35.478  34.578 105.192 1.00 74.82  ? 191  TYR A CA  1 
ATOM   1524  C C   . TYR A  1 191 ? 35.370  35.278 106.554 1.00 77.09  ? 191  TYR A C   1 
ATOM   1525  O O   . TYR A  1 191 ? 36.270  36.026 106.937 1.00 77.08  ? 191  TYR A O   1 
ATOM   1526  C CB  . TYR A  1 191 ? 35.415  35.619 104.072 1.00 71.59  ? 191  TYR A CB  1 
ATOM   1527  C CG  . TYR A  1 191 ? 35.084  35.023 102.717 1.00 69.48  ? 191  TYR A CG  1 
ATOM   1528  C CD1 . TYR A  1 191 ? 36.060  34.379 101.961 1.00 68.46  ? 191  TYR A CD1 1 
ATOM   1529  C CD2 . TYR A  1 191 ? 33.788  35.081 102.205 1.00 68.73  ? 191  TYR A CD2 1 
ATOM   1530  C CE1 . TYR A  1 191 ? 35.761  33.827 100.725 1.00 66.72  ? 191  TYR A CE1 1 
ATOM   1531  C CE2 . TYR A  1 191 ? 33.481  34.528 100.973 1.00 66.96  ? 191  TYR A CE2 1 
ATOM   1532  C CZ  . TYR A  1 191 ? 34.471  33.903 100.238 1.00 65.96  ? 191  TYR A CZ  1 
ATOM   1533  O OH  . TYR A  1 191 ? 34.176  33.351 99.018  1.00 64.38  ? 191  TYR A OH  1 
ATOM   1534  N N   . GLN A  1 192 ? 34.267  35.045 107.264 1.00 79.14  ? 192  GLN A N   1 
ATOM   1535  C CA  . GLN A  1 192 ? 34.024  35.590 108.606 1.00 81.79  ? 192  GLN A CA  1 
ATOM   1536  C C   . GLN A  1 192 ? 33.732  37.086 108.645 1.00 80.69  ? 192  GLN A C   1 
ATOM   1537  O O   . GLN A  1 192 ? 32.739  37.507 109.241 1.00 82.22  ? 192  GLN A O   1 
ATOM   1538  C CB  . GLN A  1 192 ? 35.162  35.246 109.565 1.00 84.02  ? 192  GLN A CB  1 
ATOM   1539  C CG  . GLN A  1 192 ? 34.682  35.101 110.998 1.00 87.85  ? 192  GLN A CG  1 
ATOM   1540  C CD  . GLN A  1 192 ? 35.732  34.511 111.901 1.00 90.43  ? 192  GLN A CD  1 
ATOM   1541  O OE1 . GLN A  1 192 ? 35.542  33.436 112.464 1.00 93.12  ? 192  GLN A OE1 1 
ATOM   1542  N NE2 . GLN A  1 192 ? 36.856  35.205 112.036 1.00 89.80  ? 192  GLN A NE2 1 
ATOM   1543  N N   . ASN A  1 193 ? 34.595  37.887 108.027 1.00 78.30  ? 193  ASN A N   1 
ATOM   1544  C CA  . ASN A  1 193 ? 34.423  39.339 108.012 1.00 77.30  ? 193  ASN A CA  1 
ATOM   1545  C C   . ASN A  1 193 ? 33.128  39.703 107.279 1.00 75.93  ? 193  ASN A C   1 
ATOM   1546  O O   . ASN A  1 193 ? 32.942  39.305 106.127 1.00 73.71  ? 193  ASN A O   1 
ATOM   1547  C CB  . ASN A  1 193 ? 35.624  40.026 107.347 1.00 75.02  ? 193  ASN A CB  1 
ATOM   1548  C CG  . ASN A  1 193 ? 36.960  39.526 107.881 1.00 76.20  ? 193  ASN A CG  1 
ATOM   1549  O OD1 . ASN A  1 193 ? 37.028  38.488 108.536 1.00 78.39  ? 193  ASN A OD1 1 
ATOM   1550  N ND2 . ASN A  1 193 ? 38.029  40.260 107.596 1.00 74.95  ? 193  ASN A ND2 1 
ATOM   1551  N N   . PRO A  1 194 ? 32.225  40.449 107.946 1.00 77.41  ? 194  PRO A N   1 
ATOM   1552  C CA  . PRO A  1 194 ? 30.910  40.725 107.358 1.00 76.66  ? 194  PRO A CA  1 
ATOM   1553  C C   . PRO A  1 194 ? 30.989  41.622 106.126 1.00 73.48  ? 194  PRO A C   1 
ATOM   1554  O O   . PRO A  1 194 ? 30.326  41.352 105.124 1.00 71.87  ? 194  PRO A O   1 
ATOM   1555  C CB  . PRO A  1 194 ? 30.156  41.428 108.492 1.00 79.41  ? 194  PRO A CB  1 
ATOM   1556  C CG  . PRO A  1 194 ? 31.215  42.051 109.333 1.00 80.41  ? 194  PRO A CG  1 
ATOM   1557  C CD  . PRO A  1 194 ? 32.425  41.167 109.219 1.00 79.86  ? 194  PRO A CD  1 
ATOM   1558  N N   . THR A  1 195 ? 31.804  42.671 106.210 1.00 72.76  ? 195  THR A N   1 
ATOM   1559  C CA  . THR A  1 195 ? 31.984  43.620 105.121 1.00 70.08  ? 195  THR A CA  1 
ATOM   1560  C C   . THR A  1 195 ? 33.394  43.444 104.568 1.00 68.34  ? 195  THR A C   1 
ATOM   1561  O O   . THR A  1 195 ? 34.373  43.572 105.306 1.00 69.37  ? 195  THR A O   1 
ATOM   1562  C CB  . THR A  1 195 ? 31.790  45.068 105.617 1.00 70.86  ? 195  THR A CB  1 
ATOM   1563  O OG1 . THR A  1 195 ? 30.644  45.132 106.474 1.00 73.33  ? 195  THR A OG1 1 
ATOM   1564  C CG2 . THR A  1 195 ? 31.597  46.025 104.448 1.00 68.50  ? 195  THR A CG2 1 
ATOM   1565  N N   . THR A  1 196 ? 33.493  43.133 103.276 1.00 65.90  ? 196  THR A N   1 
ATOM   1566  C CA  . THR A  1 196 ? 34.782  42.835 102.650 1.00 64.38  ? 196  THR A CA  1 
ATOM   1567  C C   . THR A  1 196 ? 34.963  43.583 101.336 1.00 61.79  ? 196  THR A C   1 
ATOM   1568  O O   . THR A  1 196 ? 34.002  44.092 100.760 1.00 60.98  ? 196  THR A O   1 
ATOM   1569  C CB  . THR A  1 196 ? 34.942  41.327 102.384 1.00 64.41  ? 196  THR A CB  1 
ATOM   1570  O OG1 . THR A  1 196 ? 33.867  40.868 101.557 1.00 63.43  ? 196  THR A OG1 1 
ATOM   1571  C CG2 . THR A  1 196 ? 34.947  40.548 103.693 1.00 67.22  ? 196  THR A CG2 1 
ATOM   1572  N N   . TYR A  1 197 ? 36.211  43.641 100.876 1.00 60.71  ? 197  TYR A N   1 
ATOM   1573  C CA  . TYR A  1 197 ? 36.557  44.334 99.642  1.00 58.50  ? 197  TYR A CA  1 
ATOM   1574  C C   . TYR A  1 197 ? 37.737  43.669 98.947  1.00 57.48  ? 197  TYR A C   1 
ATOM   1575  O O   . TYR A  1 197 ? 38.422  42.828 99.531  1.00 58.59  ? 197  TYR A O   1 
ATOM   1576  C CB  . TYR A  1 197 ? 36.921  45.790 99.940  1.00 58.68  ? 197  TYR A CB  1 
ATOM   1577  C CG  . TYR A  1 197 ? 38.200  45.931 100.734 1.00 59.78  ? 197  TYR A CG  1 
ATOM   1578  C CD1 . TYR A  1 197 ? 38.182  45.897 102.125 1.00 62.08  ? 197  TYR A CD1 1 
ATOM   1579  C CD2 . TYR A  1 197 ? 39.429  46.088 100.094 1.00 58.74  ? 197  TYR A CD2 1 
ATOM   1580  C CE1 . TYR A  1 197 ? 39.350  46.018 102.859 1.00 63.25  ? 197  TYR A CE1 1 
ATOM   1581  C CE2 . TYR A  1 197 ? 40.602  46.212 100.818 1.00 59.92  ? 197  TYR A CE2 1 
ATOM   1582  C CZ  . TYR A  1 197 ? 40.557  46.176 102.201 1.00 62.15  ? 197  TYR A CZ  1 
ATOM   1583  O OH  . TYR A  1 197 ? 41.716  46.297 102.929 1.00 63.47  ? 197  TYR A OH  1 
ATOM   1584  N N   . ILE A  1 198 ? 37.962  44.063 97.695  1.00 55.57  ? 198  ILE A N   1 
ATOM   1585  C CA  . ILE A  1 198 ? 39.163  43.692 96.950  1.00 54.66  ? 198  ILE A CA  1 
ATOM   1586  C C   . ILE A  1 198 ? 39.644  44.904 96.166  1.00 53.46  ? 198  ILE A C   1 
ATOM   1587  O O   . ILE A  1 198 ? 38.960  45.361 95.248  1.00 52.21  ? 198  ILE A O   1 
ATOM   1588  C CB  . ILE A  1 198 ? 38.908  42.544 95.954  1.00 53.63  ? 198  ILE A CB  1 
ATOM   1589  C CG1 . ILE A  1 198 ? 38.128  41.416 96.632  1.00 54.85  ? 198  ILE A CG1 1 
ATOM   1590  C CG2 . ILE A  1 198 ? 40.231  42.041 95.379  1.00 53.26  ? 198  ILE A CG2 1 
ATOM   1591  C CD1 . ILE A  1 198 ? 37.966  40.186 95.775  1.00 54.19  ? 198  ILE A CD1 1 
ATOM   1592  N N   . SER A  1 199 ? 40.816  45.419 96.525  1.00 54.02  ? 199  SER A N   1 
ATOM   1593  C CA  . SER A  1 199 ? 41.403  46.544 95.810  1.00 53.19  ? 199  SER A CA  1 
ATOM   1594  C C   . SER A  1 199 ? 42.555  46.060 94.937  1.00 52.54  ? 199  SER A C   1 
ATOM   1595  O O   . SER A  1 199 ? 43.442  45.352 95.409  1.00 53.45  ? 199  SER A O   1 
ATOM   1596  C CB  . SER A  1 199 ? 41.873  47.625 96.785  1.00 54.46  ? 199  SER A CB  1 
ATOM   1597  O OG  . SER A  1 199 ? 42.770  47.102 97.742  1.00 55.91  ? 199  SER A OG  1 
ATOM   1598  N N   . VAL A  1 200 ? 42.517  46.436 93.660  1.00 51.17  ? 200  VAL A N   1 
ATOM   1599  C CA  . VAL A  1 200 ? 43.543  46.053 92.692  1.00 50.64  ? 200  VAL A CA  1 
ATOM   1600  C C   . VAL A  1 200 ? 44.117  47.312 92.051  1.00 50.31  ? 200  VAL A C   1 
ATOM   1601  O O   . VAL A  1 200 ? 43.369  48.168 91.574  1.00 49.63  ? 200  VAL A O   1 
ATOM   1602  C CB  . VAL A  1 200 ? 42.977  45.141 91.584  1.00 49.46  ? 200  VAL A CB  1 
ATOM   1603  C CG1 . VAL A  1 200 ? 44.108  44.428 90.853  1.00 49.45  ? 200  VAL A CG1 1 
ATOM   1604  C CG2 . VAL A  1 200 ? 41.999  44.129 92.167  1.00 49.76  ? 200  VAL A CG2 1 
ATOM   1605  N N   . GLY A  1 201 ? 45.442  47.418 92.040  1.00 50.99  ? 201  GLY A N   1 
ATOM   1606  C CA  . GLY A  1 201 ? 46.114  48.598 91.514  1.00 51.04  ? 201  GLY A CA  1 
ATOM   1607  C C   . GLY A  1 201 ? 47.227  48.246 90.551  1.00 51.02  ? 201  GLY A C   1 
ATOM   1608  O O   . GLY A  1 201 ? 47.915  47.240 90.726  1.00 51.62  ? 201  GLY A O   1 
ATOM   1609  N N   . THR A  1 202 ? 47.373  49.063 89.510  1.00 50.54  ? 202  THR A N   1 
ATOM   1610  C CA  . THR A  1 202 ? 48.548  49.044 88.639  1.00 50.92  ? 202  THR A CA  1 
ATOM   1611  C C   . THR A  1 202 ? 48.915  50.503 88.395  1.00 51.39  ? 202  THR A C   1 
ATOM   1612  O O   . THR A  1 202 ? 48.463  51.386 89.132  1.00 51.74  ? 202  THR A O   1 
ATOM   1613  C CB  . THR A  1 202 ? 48.284  48.314 87.297  1.00 49.94  ? 202  THR A CB  1 
ATOM   1614  O OG1 . THR A  1 202 ? 47.473  49.129 86.439  1.00 49.06  ? 202  THR A OG1 1 
ATOM   1615  C CG2 . THR A  1 202 ? 47.598  46.972 87.526  1.00 49.40  ? 202  THR A CG2 1 
ATOM   1616  N N   . SER A  1 203 ? 49.730  50.767 87.378  1.00 51.67  ? 203  SER A N   1 
ATOM   1617  C CA  . SER A  1 203 ? 49.982  52.142 86.958  1.00 52.15  ? 203  SER A CA  1 
ATOM   1618  C C   . SER A  1 203 ? 48.694  52.785 86.455  1.00 51.13  ? 203  SER A C   1 
ATOM   1619  O O   . SER A  1 203 ? 48.481  53.981 86.649  1.00 51.61  ? 203  SER A O   1 
ATOM   1620  C CB  . SER A  1 203 ? 51.053  52.189 85.869  1.00 52.84  ? 203  SER A CB  1 
ATOM   1621  O OG  . SER A  1 203 ? 50.707  51.348 84.786  1.00 51.96  ? 203  SER A OG  1 
ATOM   1622  N N   . THR A  1 204 ? 47.837  51.984 85.825  1.00 49.90  ? 204  THR A N   1 
ATOM   1623  C CA  . THR A  1 204 ? 46.581  52.476 85.265  1.00 49.03  ? 204  THR A CA  1 
ATOM   1624  C C   . THR A  1 204 ? 45.369  52.056 86.090  1.00 48.34  ? 204  THR A C   1 
ATOM   1625  O O   . THR A  1 204 ? 44.469  52.862 86.321  1.00 48.33  ? 204  THR A O   1 
ATOM   1626  C CB  . THR A  1 204 ? 46.386  51.989 83.813  1.00 48.32  ? 204  THR A CB  1 
ATOM   1627  O OG1 . THR A  1 204 ? 46.324  50.558 83.783  1.00 47.69  ? 204  THR A OG1 1 
ATOM   1628  C CG2 . THR A  1 204 ? 47.532  52.464 82.931  1.00 49.24  ? 204  THR A CG2 1 
ATOM   1629  N N   . LEU A  1 205 ? 45.342  50.802 86.532  1.00 48.01  ? 205  LEU A N   1 
ATOM   1630  C CA  . LEU A  1 205 ? 44.161  50.260 87.201  1.00 47.50  ? 205  LEU A CA  1 
ATOM   1631  C C   . LEU A  1 205 ? 43.963  50.842 88.608  1.00 48.35  ? 205  LEU A C   1 
ATOM   1632  O O   . LEU A  1 205 ? 44.912  50.945 89.389  1.00 49.38  ? 205  LEU A O   1 
ATOM   1633  C CB  . LEU A  1 205 ? 44.238  48.730 87.268  1.00 47.18  ? 205  LEU A CB  1 
ATOM   1634  C CG  . LEU A  1 205 ? 42.949  47.979 87.631  1.00 46.62  ? 205  LEU A CG  1 
ATOM   1635  C CD1 . LEU A  1 205 ? 41.802  48.362 86.702  1.00 45.72  ? 205  LEU A CD1 1 
ATOM   1636  C CD2 . LEU A  1 205 ? 43.182  46.474 87.605  1.00 46.56  ? 205  LEU A CD2 1 
ATOM   1637  N N   . ASN A  1 206 ? 42.723  51.233 88.904  1.00 48.14  ? 206  ASN A N   1 
ATOM   1638  C CA  . ASN A  1 206 ? 42.325  51.703 90.232  1.00 49.04  ? 206  ASN A CA  1 
ATOM   1639  C C   . ASN A  1 206 ? 40.964  51.121 90.592  1.00 48.72  ? 206  ASN A C   1 
ATOM   1640  O O   . ASN A  1 206 ? 39.936  51.797 90.516  1.00 48.71  ? 206  ASN A O   1 
ATOM   1641  C CB  . ASN A  1 206 ? 42.284  53.232 90.282  1.00 49.72  ? 206  ASN A CB  1 
ATOM   1642  C CG  . ASN A  1 206 ? 41.992  53.765 91.676  1.00 50.93  ? 206  ASN A CG  1 
ATOM   1643  O OD1 . ASN A  1 206 ? 42.213  53.083 92.677  1.00 51.48  ? 206  ASN A OD1 1 
ATOM   1644  N ND2 . ASN A  1 206 ? 41.497  54.994 91.746  1.00 51.56  ? 206  ASN A ND2 1 
ATOM   1645  N N   . GLN A  1 207 ? 40.978  49.858 90.997  1.00 48.66  ? 207  GLN A N   1 
ATOM   1646  C CA  . GLN A  1 207 ? 39.763  49.087 91.200  1.00 48.43  ? 207  GLN A CA  1 
ATOM   1647  C C   . GLN A  1 207 ? 39.527  48.791 92.680  1.00 49.68  ? 207  GLN A C   1 
ATOM   1648  O O   . GLN A  1 207 ? 40.474  48.620 93.444  1.00 50.54  ? 207  GLN A O   1 
ATOM   1649  C CB  . GLN A  1 207 ? 39.874  47.784 90.407  1.00 47.57  ? 207  GLN A CB  1 
ATOM   1650  C CG  . GLN A  1 207 ? 38.737  46.799 90.605  1.00 47.47  ? 207  GLN A CG  1 
ATOM   1651  C CD  . GLN A  1 207 ? 38.859  45.602 89.684  1.00 46.70  ? 207  GLN A CD  1 
ATOM   1652  O OE1 . GLN A  1 207 ? 39.123  44.487 90.134  1.00 47.17  ? 207  GLN A OE1 1 
ATOM   1653  N NE2 . GLN A  1 207 ? 38.689  45.831 88.380  1.00 45.69  ? 207  GLN A NE2 1 
ATOM   1654  N N   . ARG A  1 208 ? 38.256  48.746 93.073  1.00 49.98  ? 208  ARG A N   1 
ATOM   1655  C CA  . ARG A  1 208 ? 37.864  48.278 94.398  1.00 51.33  ? 208  ARG A CA  1 
ATOM   1656  C C   . ARG A  1 208 ? 36.511  47.574 94.317  1.00 51.24  ? 208  ARG A C   1 
ATOM   1657  O O   . ARG A  1 208 ? 35.483  48.214 94.092  1.00 51.21  ? 208  ARG A O   1 
ATOM   1658  C CB  . ARG A  1 208 ? 37.803  49.429 95.403  1.00 52.68  ? 208  ARG A CB  1 
ATOM   1659  C CG  . ARG A  1 208 ? 37.933  48.963 96.845  1.00 54.38  ? 208  ARG A CG  1 
ATOM   1660  C CD  . ARG A  1 208 ? 37.409  49.993 97.831  1.00 55.91  ? 208  ARG A CD  1 
ATOM   1661  N NE  . ARG A  1 208 ? 37.636  49.578 99.214  1.00 57.75  ? 208  ARG A NE  1 
ATOM   1662  C CZ  . ARG A  1 208 ? 38.804  49.660 99.854  1.00 58.62  ? 208  ARG A CZ  1 
ATOM   1663  N NH1 . ARG A  1 208 ? 39.885  50.141 99.247  1.00 57.82  ? 208  ARG A NH1 1 
ATOM   1664  N NH2 . ARG A  1 208 ? 38.894  49.251 101.118 1.00 60.48  ? 208  ARG A NH2 1 
ATOM   1665  N N   . LEU A  1 209 ? 36.522  46.256 94.500  1.00 51.40  ? 209  LEU A N   1 
ATOM   1666  C CA  . LEU A  1 209 ? 35.325  45.433 94.361  1.00 51.40  ? 209  LEU A CA  1 
ATOM   1667  C C   . LEU A  1 209 ? 34.753  45.090 95.727  1.00 53.25  ? 209  LEU A C   1 
ATOM   1668  O O   . LEU A  1 209 ? 35.503  44.823 96.661  1.00 54.36  ? 209  LEU A O   1 
ATOM   1669  C CB  . LEU A  1 209 ? 35.660  44.137 93.623  1.00 50.58  ? 209  LEU A CB  1 
ATOM   1670  C CG  . LEU A  1 209 ? 36.356  44.275 92.266  1.00 49.02  ? 209  LEU A CG  1 
ATOM   1671  C CD1 . LEU A  1 209 ? 36.754  42.903 91.741  1.00 48.67  ? 209  LEU A CD1 1 
ATOM   1672  C CD2 . LEU A  1 209 ? 35.466  45.006 91.271  1.00 48.04  ? 209  LEU A CD2 1 
ATOM   1673  N N   . VAL A  1 210 ? 33.426  45.106 95.833  1.00 53.78  ? 210  VAL A N   1 
ATOM   1674  C CA  . VAL A  1 210 ? 32.730  44.661 97.041  1.00 55.76  ? 210  VAL A CA  1 
ATOM   1675  C C   . VAL A  1 210 ? 31.699  43.587 96.664  1.00 55.80  ? 210  VAL A C   1 
ATOM   1676  O O   . VAL A  1 210 ? 31.043  43.702 95.623  1.00 54.61  ? 210  VAL A O   1 
ATOM   1677  C CB  . VAL A  1 210 ? 32.054  45.834 97.797  1.00 57.06  ? 210  VAL A CB  1 
ATOM   1678  C CG1 . VAL A  1 210 ? 33.071  46.927 98.094  1.00 57.08  ? 210  VAL A CG1 1 
ATOM   1679  C CG2 . VAL A  1 210 ? 30.872  46.402 97.020  1.00 56.50  ? 210  VAL A CG2 1 
ATOM   1680  N N   . PRO A  1 211 ? 31.565  42.530 97.494  1.00 57.33  ? 211  PRO A N   1 
ATOM   1681  C CA  . PRO A  1 211 ? 30.568  41.497 97.189  1.00 57.63  ? 211  PRO A CA  1 
ATOM   1682  C C   . PRO A  1 211 ? 29.129  41.999 97.289  1.00 58.45  ? 211  PRO A C   1 
ATOM   1683  O O   . PRO A  1 211 ? 28.744  42.598 98.295  1.00 60.15  ? 211  PRO A O   1 
ATOM   1684  C CB  . PRO A  1 211 ? 30.822  40.422 98.256  1.00 59.53  ? 211  PRO A CB  1 
ATOM   1685  C CG  . PRO A  1 211 ? 32.202  40.671 98.743  1.00 59.61  ? 211  PRO A CG  1 
ATOM   1686  C CD  . PRO A  1 211 ? 32.414  42.150 98.638  1.00 58.85  ? 211  PRO A CD  1 
ATOM   1687  N N   . ARG A  1 212 ? 28.361  41.767 96.231  1.00 57.42  ? 212  ARG A N   1 
ATOM   1688  C CA  . ARG A  1 212 ? 26.932  42.062 96.207  1.00 58.33  ? 212  ARG A CA  1 
ATOM   1689  C C   . ARG A  1 212 ? 26.152  40.801 96.576  1.00 59.82  ? 212  ARG A C   1 
ATOM   1690  O O   . ARG A  1 212 ? 26.251  39.782 95.893  1.00 59.01  ? 212  ARG A O   1 
ATOM   1691  C CB  . ARG A  1 212 ? 26.508  42.556 94.819  1.00 56.54  ? 212  ARG A CB  1 
ATOM   1692  C CG  . ARG A  1 212 ? 27.370  43.686 94.272  1.00 55.07  ? 212  ARG A CG  1 
ATOM   1693  C CD  . ARG A  1 212 ? 26.755  44.322 93.035  1.00 53.90  ? 212  ARG A CD  1 
ATOM   1694  N NE  . ARG A  1 212 ? 26.556  43.357 91.953  1.00 52.76  ? 212  ARG A NE  1 
ATOM   1695  C CZ  . ARG A  1 212 ? 27.515  42.898 91.146  1.00 51.23  ? 212  ARG A CZ  1 
ATOM   1696  N NH1 . ARG A  1 212 ? 28.776  43.300 91.276  1.00 50.61  ? 212  ARG A NH1 1 
ATOM   1697  N NH2 . ARG A  1 212 ? 27.209  42.020 90.197  1.00 50.49  ? 212  ARG A NH2 1 
ATOM   1698  N N   . ILE A  1 213 ? 25.385  40.874 97.661  1.00 62.20  ? 213  ILE A N   1 
ATOM   1699  C CA  . ILE A  1 213 ? 24.591  39.739 98.129  1.00 64.08  ? 213  ILE A CA  1 
ATOM   1700  C C   . ILE A  1 213 ? 23.177  39.804 97.545  1.00 64.45  ? 213  ILE A C   1 
ATOM   1701  O O   . ILE A  1 213 ? 22.557  40.870 97.502  1.00 64.68  ? 213  ILE A O   1 
ATOM   1702  C CB  . ILE A  1 213 ? 24.546  39.680 99.677  1.00 66.85  ? 213  ILE A CB  1 
ATOM   1703  C CG1 . ILE A  1 213 ? 25.956  39.435 100.229 1.00 66.71  ? 213  ILE A CG1 1 
ATOM   1704  C CG2 . ILE A  1 213 ? 23.603  38.579 100.159 1.00 69.09  ? 213  ILE A CG2 1 
ATOM   1705  C CD1 . ILE A  1 213 ? 26.096  39.665 101.719 1.00 69.30  ? 213  ILE A CD1 1 
ATOM   1706  N N   . ALA A  1 214 ? 22.684  38.655 97.087  1.00 64.68  ? 214  ALA A N   1 
ATOM   1707  C CA  . ALA A  1 214 ? 21.325  38.535 96.563  1.00 65.34  ? 214  ALA A CA  1 
ATOM   1708  C C   . ALA A  1 214 ? 20.902  37.069 96.526  1.00 66.41  ? 214  ALA A C   1 
ATOM   1709  O O   . ALA A  1 214 ? 21.746  36.171 96.458  1.00 65.86  ? 214  ALA A O   1 
ATOM   1710  C CB  . ALA A  1 214 ? 21.237  39.143 95.170  1.00 63.01  ? 214  ALA A CB  1 
ATOM   1711  N N   . THR A  1 215 ? 19.593  36.836 96.584  1.00 68.18  ? 215  THR A N   1 
ATOM   1712  C CA  . THR A  1 215 ? 19.040  35.493 96.440  1.00 69.31  ? 215  THR A CA  1 
ATOM   1713  C C   . THR A  1 215 ? 18.910  35.211 94.950  1.00 67.18  ? 215  THR A C   1 
ATOM   1714  O O   . THR A  1 215 ? 18.216  35.935 94.235  1.00 66.48  ? 215  THR A O   1 
ATOM   1715  C CB  . THR A  1 215 ? 17.661  35.358 97.118  1.00 72.30  ? 215  THR A CB  1 
ATOM   1716  O OG1 . THR A  1 215 ? 17.695  35.981 98.408  1.00 74.27  ? 215  THR A OG1 1 
ATOM   1717  C CG2 . THR A  1 215 ? 17.276  33.889 97.274  1.00 74.00  ? 215  THR A CG2 1 
ATOM   1718  N N   . ARG A  1 216 ? 19.583  34.167 94.482  1.00 66.32  ? 216  ARG A N   1 
ATOM   1719  C CA  . ARG A  1 216 ? 19.672  33.898 93.054  1.00 64.23  ? 216  ARG A CA  1 
ATOM   1720  C C   . ARG A  1 216 ? 19.223  32.483 92.730  1.00 65.27  ? 216  ARG A C   1 
ATOM   1721  O O   . ARG A  1 216 ? 19.275  31.592 93.580  1.00 67.17  ? 216  ARG A O   1 
ATOM   1722  C CB  . ARG A  1 216 ? 21.108  34.112 92.577  1.00 61.87  ? 216  ARG A CB  1 
ATOM   1723  C CG  . ARG A  1 216 ? 21.619  35.529 92.787  1.00 60.83  ? 216  ARG A CG  1 
ATOM   1724  C CD  . ARG A  1 216 ? 23.110  35.627 92.513  1.00 59.01  ? 216  ARG A CD  1 
ATOM   1725  N NE  . ARG A  1 216 ? 23.920  35.252 93.676  1.00 60.19  ? 216  ARG A NE  1 
ATOM   1726  C CZ  . ARG A  1 216 ? 24.422  36.100 94.578  1.00 60.61  ? 216  ARG A CZ  1 
ATOM   1727  N NH1 . ARG A  1 216 ? 24.213  37.411 94.491  1.00 59.97  ? 216  ARG A NH1 1 
ATOM   1728  N NH2 . ARG A  1 216 ? 25.146  35.630 95.588  1.00 61.85  ? 216  ARG A NH2 1 
ATOM   1729  N N   . SER A  1 217 ? 18.785  32.290 91.490  1.00 64.20  ? 217  SER A N   1 
ATOM   1730  C CA  . SER A  1 217 ? 18.388  30.976 91.005  1.00 65.04  ? 217  SER A CA  1 
ATOM   1731  C C   . SER A  1 217 ? 19.613  30.072 90.906  1.00 64.46  ? 217  SER A C   1 
ATOM   1732  O O   . SER A  1 217 ? 20.725  30.545 90.668  1.00 62.64  ? 217  SER A O   1 
ATOM   1733  C CB  . SER A  1 217 ? 17.712  31.094 89.638  1.00 63.82  ? 217  SER A CB  1 
ATOM   1734  O OG  . SER A  1 217 ? 16.727  32.112 89.645  1.00 64.25  ? 217  SER A OG  1 
ATOM   1735  N N   . LYS A  1 218 ? 19.405  28.775 91.107  1.00 66.32  ? 218  LYS A N   1 
ATOM   1736  C CA  . LYS A  1 218 ? 20.486  27.801 90.988  1.00 66.19  ? 218  LYS A CA  1 
ATOM   1737  C C   . LYS A  1 218 ? 20.883  27.637 89.532  1.00 63.90  ? 218  LYS A C   1 
ATOM   1738  O O   . LYS A  1 218 ? 20.051  27.318 88.684  1.00 63.91  ? 218  LYS A O   1 
ATOM   1739  C CB  . LYS A  1 218 ? 20.083  26.440 91.567  1.00 69.12  ? 218  LYS A CB  1 
ATOM   1740  C CG  . LYS A  1 218 ? 20.488  26.244 93.017  1.00 71.41  ? 218  LYS A CG  1 
ATOM   1741  C CD  . LYS A  1 218 ? 19.568  25.266 93.729  1.00 74.90  ? 218  LYS A CD  1 
ATOM   1742  C CE  . LYS A  1 218 ? 19.943  25.118 95.195  1.00 77.51  ? 218  LYS A CE  1 
ATOM   1743  N NZ  . LYS A  1 218 ? 18.740  25.207 96.066  1.00 80.43  ? 218  LYS A NZ  1 
ATOM   1744  N N   . VAL A  1 219 ? 22.156  27.885 89.255  1.00 62.09  ? 219  VAL A N   1 
ATOM   1745  C CA  . VAL A  1 219 ? 22.750  27.586 87.966  1.00 60.25  ? 219  VAL A CA  1 
ATOM   1746  C C   . VAL A  1 219 ? 23.875  26.600 88.254  1.00 60.81  ? 219  VAL A C   1 
ATOM   1747  O O   . VAL A  1 219 ? 24.706  26.846 89.124  1.00 61.05  ? 219  VAL A O   1 
ATOM   1748  C CB  . VAL A  1 219 ? 23.274  28.871 87.296  1.00 57.84  ? 219  VAL A CB  1 
ATOM   1749  C CG1 . VAL A  1 219 ? 24.057  28.550 86.029  1.00 56.28  ? 219  VAL A CG1 1 
ATOM   1750  C CG2 . VAL A  1 219 ? 22.114  29.812 86.989  1.00 57.52  ? 219  VAL A CG2 1 
ATOM   1751  N N   . ASN A  1 220 ? 23.881  25.469 87.551  1.00 61.22  ? 220  ASN A N   1 
ATOM   1752  C CA  . ASN A  1 220 ? 24.813  24.371 87.842  1.00 62.32  ? 220  ASN A CA  1 
ATOM   1753  C C   . ASN A  1 220 ? 24.814  23.963 89.323  1.00 64.64  ? 220  ASN A C   1 
ATOM   1754  O O   . ASN A  1 220 ? 25.864  23.667 89.896  1.00 65.22  ? 220  ASN A O   1 
ATOM   1755  C CB  . ASN A  1 220 ? 26.236  24.727 87.384  1.00 60.63  ? 220  ASN A CB  1 
ATOM   1756  C CG  . ASN A  1 220 ? 26.419  24.602 85.883  1.00 59.12  ? 220  ASN A CG  1 
ATOM   1757  O OD1 . ASN A  1 220 ? 25.458  24.679 85.113  1.00 58.69  ? 220  ASN A OD1 1 
ATOM   1758  N ND2 . ASN A  1 220 ? 27.665  24.413 85.457  1.00 58.47  ? 220  ASN A ND2 1 
ATOM   1759  N N   . GLY A  1 221 ? 23.631  23.957 89.933  1.00 66.16  ? 221  GLY A N   1 
ATOM   1760  C CA  . GLY A  1 221 ? 23.468  23.534 91.324  1.00 68.73  ? 221  GLY A CA  1 
ATOM   1761  C C   . GLY A  1 221 ? 23.986  24.507 92.370  1.00 68.59  ? 221  GLY A C   1 
ATOM   1762  O O   . GLY A  1 221 ? 24.107  24.148 93.540  1.00 70.78  ? 221  GLY A O   1 
ATOM   1763  N N   . GLN A  1 222 ? 24.287  25.739 91.960  1.00 66.18  ? 222  GLN A N   1 
ATOM   1764  C CA  . GLN A  1 222 ? 24.820  26.754 92.867  1.00 65.93  ? 222  GLN A CA  1 
ATOM   1765  C C   . GLN A  1 222 ? 24.143  28.098 92.630  1.00 64.40  ? 222  GLN A C   1 
ATOM   1766  O O   . GLN A  1 222 ? 23.946  28.505 91.485  1.00 62.47  ? 222  GLN A O   1 
ATOM   1767  C CB  . GLN A  1 222 ? 26.335  26.898 92.682  1.00 64.65  ? 222  GLN A CB  1 
ATOM   1768  C CG  . GLN A  1 222 ? 27.135  25.637 92.998  1.00 66.35  ? 222  GLN A CG  1 
ATOM   1769  C CD  . GLN A  1 222 ? 26.953  25.157 94.432  1.00 69.41  ? 222  GLN A CD  1 
ATOM   1770  O OE1 . GLN A  1 222 ? 26.840  25.959 95.357  1.00 69.95  ? 222  GLN A OE1 1 
ATOM   1771  N NE2 . GLN A  1 222 ? 26.929  23.841 94.621  1.00 71.62  ? 222  GLN A NE2 1 
ATOM   1772  N N   . SER A  1 223 ? 23.781  28.774 93.719  1.00 65.47  ? 223  SER A N   1 
ATOM   1773  C CA  . SER A  1 223 ? 23.174  30.106 93.655  1.00 64.42  ? 223  SER A CA  1 
ATOM   1774  C C   . SER A  1 223 ? 24.198  31.218 93.925  1.00 62.91  ? 223  SER A C   1 
ATOM   1775  O O   . SER A  1 223 ? 23.890  32.401 93.770  1.00 61.90  ? 223  SER A O   1 
ATOM   1776  C CB  . SER A  1 223 ? 21.996  30.202 94.632  1.00 66.89  ? 223  SER A CB  1 
ATOM   1777  O OG  . SER A  1 223 ? 20.865  29.510 94.136  1.00 67.83  ? 223  SER A OG  1 
ATOM   1778  N N   . GLY A  1 224 ? 25.409  30.834 94.328  1.00 62.90  ? 224  GLY A N   1 
ATOM   1779  C CA  . GLY A  1 224 ? 26.519  31.776 94.468  1.00 61.46  ? 224  GLY A CA  1 
ATOM   1780  C C   . GLY A  1 224 ? 27.091  32.144 93.112  1.00 58.74  ? 224  GLY A C   1 
ATOM   1781  O O   . GLY A  1 224 ? 26.962  31.380 92.150  1.00 58.12  ? 224  GLY A O   1 
ATOM   1782  N N   . ARG A  1 225 ? 27.728  33.311 93.036  1.00 57.27  ? 225  ARG A N   1 
ATOM   1783  C CA  . ARG A  1 225 ? 28.259  33.828 91.771  1.00 54.87  ? 225  ARG A CA  1 
ATOM   1784  C C   . ARG A  1 225 ? 29.737  34.206 91.866  1.00 54.03  ? 225  ARG A C   1 
ATOM   1785  O O   . ARG A  1 225 ? 30.213  34.636 92.916  1.00 54.91  ? 225  ARG A O   1 
ATOM   1786  C CB  . ARG A  1 225 ? 27.443  35.040 91.308  1.00 53.89  ? 225  ARG A CB  1 
ATOM   1787  C CG  . ARG A  1 225 ? 25.993  34.730 90.965  1.00 54.51  ? 225  ARG A CG  1 
ATOM   1788  C CD  . ARG A  1 225 ? 25.869  33.959 89.660  1.00 53.50  ? 225  ARG A CD  1 
ATOM   1789  N NE  . ARG A  1 225 ? 24.474  33.667 89.318  1.00 54.21  ? 225  ARG A NE  1 
ATOM   1790  C CZ  . ARG A  1 225 ? 23.780  32.607 89.737  1.00 55.93  ? 225  ARG A CZ  1 
ATOM   1791  N NH1 . ARG A  1 225 ? 24.325  31.696 90.542  1.00 57.23  ? 225  ARG A NH1 1 
ATOM   1792  N NH2 . ARG A  1 225 ? 22.518  32.456 89.349  1.00 56.56  ? 225  ARG A NH2 1 
ATOM   1793  N N   . MET A  1 226 ? 30.450  34.030 90.757  1.00 52.49  ? 226  MET A N   1 
ATOM   1794  C CA  . MET A  1 226 ? 31.843  34.444 90.641  1.00 51.64  ? 226  MET A CA  1 
ATOM   1795  C C   . MET A  1 226 ? 31.951  35.427 89.488  1.00 49.66  ? 226  MET A C   1 
ATOM   1796  O O   . MET A  1 226 ? 31.572  35.108 88.366  1.00 48.83  ? 226  MET A O   1 
ATOM   1797  C CB  . MET A  1 226 ? 32.741  33.238 90.366  1.00 52.07  ? 226  MET A CB  1 
ATOM   1798  C CG  . MET A  1 226 ? 32.953  32.331 91.567  1.00 54.20  ? 226  MET A CG  1 
ATOM   1799  S SD  . MET A  1 226 ? 34.200  32.941 92.718  1.00 54.98  ? 226  MET A SD  1 
ATOM   1800  C CE  . MET A  1 226 ? 34.267  31.573 93.870  1.00 57.74  ? 226  MET A CE  1 
ATOM   1801  N N   . GLU A  1 227 ? 32.466  36.618 89.766  1.00 49.07  ? 227  GLU A N   1 
ATOM   1802  C CA  . GLU A  1 227 ? 32.625  37.645 88.749  1.00 47.45  ? 227  GLU A CA  1 
ATOM   1803  C C   . GLU A  1 227 ? 34.107  37.825 88.470  1.00 46.86  ? 227  GLU A C   1 
ATOM   1804  O O   . GLU A  1 227 ? 34.875  38.149 89.376  1.00 47.50  ? 227  GLU A O   1 
ATOM   1805  C CB  . GLU A  1 227 ? 31.998  38.952 89.223  1.00 47.49  ? 227  GLU A CB  1 
ATOM   1806  C CG  . GLU A  1 227 ? 31.803  39.980 88.122  1.00 46.19  ? 227  GLU A CG  1 
ATOM   1807  C CD  . GLU A  1 227 ? 30.981  41.175 88.570  1.00 46.55  ? 227  GLU A CD  1 
ATOM   1808  O OE1 . GLU A  1 227 ? 30.615  41.250 89.765  1.00 47.79  ? 227  GLU A OE1 1 
ATOM   1809  O OE2 . GLU A  1 227 ? 30.694  42.041 87.717  1.00 45.78  ? 227  GLU A OE2 1 
ATOM   1810  N N   . PHE A  1 228 ? 34.506  37.604 87.218  1.00 45.81  ? 228  PHE A N   1 
ATOM   1811  C CA  . PHE A  1 228 ? 35.921  37.575 86.852  1.00 45.52  ? 228  PHE A CA  1 
ATOM   1812  C C   . PHE A  1 228 ? 36.359  38.834 86.113  1.00 44.45  ? 228  PHE A C   1 
ATOM   1813  O O   . PHE A  1 228 ? 35.653  39.333 85.237  1.00 43.64  ? 228  PHE A O   1 
ATOM   1814  C CB  . PHE A  1 228 ? 36.221  36.324 86.029  1.00 45.57  ? 228  PHE A CB  1 
ATOM   1815  C CG  . PHE A  1 228 ? 36.098  35.054 86.818  1.00 46.91  ? 228  PHE A CG  1 
ATOM   1816  C CD1 . PHE A  1 228 ? 37.151  34.612 87.607  1.00 48.00  ? 228  PHE A CD1 1 
ATOM   1817  C CD2 . PHE A  1 228 ? 34.921  34.317 86.802  1.00 47.28  ? 228  PHE A CD2 1 
ATOM   1818  C CE1 . PHE A  1 228 ? 37.042  33.449 88.351  1.00 49.50  ? 228  PHE A CE1 1 
ATOM   1819  C CE2 . PHE A  1 228 ? 34.805  33.152 87.544  1.00 48.76  ? 228  PHE A CE2 1 
ATOM   1820  C CZ  . PHE A  1 228 ? 35.867  32.718 88.320  1.00 49.89  ? 228  PHE A CZ  1 
ATOM   1821  N N   . PHE A  1 229 ? 37.529  39.338 86.495  1.00 44.66  ? 229  PHE A N   1 
ATOM   1822  C CA  . PHE A  1 229 ? 38.090  40.563 85.936  1.00 43.98  ? 229  PHE A CA  1 
ATOM   1823  C C   . PHE A  1 229 ? 39.492  40.305 85.402  1.00 44.11  ? 229  PHE A C   1 
ATOM   1824  O O   . PHE A  1 229 ? 40.142  39.319 85.770  1.00 44.86  ? 229  PHE A O   1 
ATOM   1825  C CB  . PHE A  1 229 ? 38.144  41.657 87.001  1.00 44.40  ? 229  PHE A CB  1 
ATOM   1826  C CG  . PHE A  1 229 ? 36.794  42.084 87.494  1.00 44.48  ? 229  PHE A CG  1 
ATOM   1827  C CD1 . PHE A  1 229 ? 36.112  41.322 88.437  1.00 45.33  ? 229  PHE A CD1 1 
ATOM   1828  C CD2 . PHE A  1 229 ? 36.199  43.245 87.017  1.00 43.94  ? 229  PHE A CD2 1 
ATOM   1829  C CE1 . PHE A  1 229 ? 34.864  41.709 88.893  1.00 45.65  ? 229  PHE A CE1 1 
ATOM   1830  C CE2 . PHE A  1 229 ? 34.952  43.639 87.472  1.00 44.25  ? 229  PHE A CE2 1 
ATOM   1831  C CZ  . PHE A  1 229 ? 34.283  42.869 88.411  1.00 45.10  ? 229  PHE A CZ  1 
ATOM   1832  N N   . TRP A  1 230 ? 39.950  41.198 84.529  1.00 43.55  ? 230  TRP A N   1 
ATOM   1833  C CA  . TRP A  1 230 ? 41.258  41.053 83.912  1.00 43.82  ? 230  TRP A CA  1 
ATOM   1834  C C   . TRP A  1 230 ? 41.929  42.390 83.649  1.00 43.76  ? 230  TRP A C   1 
ATOM   1835  O O   . TRP A  1 230 ? 41.298  43.442 83.702  1.00 43.34  ? 230  TRP A O   1 
ATOM   1836  C CB  . TRP A  1 230 ? 41.133  40.270 82.606  1.00 43.47  ? 230  TRP A CB  1 
ATOM   1837  C CG  . TRP A  1 230 ? 40.254  40.918 81.580  1.00 42.60  ? 230  TRP A CG  1 
ATOM   1838  C CD1 . TRP A  1 230 ? 38.904  40.766 81.447  1.00 42.09  ? 230  TRP A CD1 1 
ATOM   1839  C CD2 . TRP A  1 230 ? 40.662  41.810 80.536  1.00 42.36  ? 230  TRP A CD2 1 
ATOM   1840  N NE1 . TRP A  1 230 ? 38.443  41.509 80.389  1.00 41.54  ? 230  TRP A NE1 1 
ATOM   1841  C CE2 . TRP A  1 230 ? 39.501  42.161 79.812  1.00 41.72  ? 230  TRP A CE2 1 
ATOM   1842  C CE3 . TRP A  1 230 ? 41.893  42.349 80.143  1.00 42.84  ? 230  TRP A CE3 1 
ATOM   1843  C CZ2 . TRP A  1 230 ? 39.536  43.025 78.712  1.00 41.57  ? 230  TRP A CZ2 1 
ATOM   1844  C CZ3 . TRP A  1 230 ? 41.927  43.210 79.050  1.00 42.70  ? 230  TRP A CZ3 1 
ATOM   1845  C CH2 . TRP A  1 230 ? 40.755  43.540 78.349  1.00 42.08  ? 230  TRP A CH2 1 
ATOM   1846  N N   . THR A  1 231 ? 43.227  42.328 83.384  1.00 44.39  ? 231  THR A N   1 
ATOM   1847  C CA  . THR A  1 231 ? 43.986  43.484 82.936  1.00 44.57  ? 231  THR A CA  1 
ATOM   1848  C C   . THR A  1 231 ? 45.184  43.015 82.125  1.00 45.28  ? 231  THR A C   1 
ATOM   1849  O O   . THR A  1 231 ? 45.544  41.838 82.159  1.00 45.77  ? 231  THR A O   1 
ATOM   1850  C CB  . THR A  1 231 ? 44.474  44.340 84.121  1.00 45.16  ? 231  THR A CB  1 
ATOM   1851  O OG1 . THR A  1 231 ? 45.000  45.579 83.634  1.00 45.31  ? 231  THR A OG1 1 
ATOM   1852  C CG2 . THR A  1 231 ? 45.554  43.612 84.926  1.00 46.25  ? 231  THR A CG2 1 
ATOM   1853  N N   . ILE A  1 232 ? 45.784  43.938 81.384  1.00 45.57  ? 232  ILE A N   1 
ATOM   1854  C CA  . ILE A  1 232 ? 47.069  43.695 80.743  1.00 46.63  ? 232  ILE A CA  1 
ATOM   1855  C C   . ILE A  1 232 ? 48.101  44.447 81.562  1.00 47.64  ? 232  ILE A C   1 
ATOM   1856  O O   . ILE A  1 232 ? 48.062  45.672 81.650  1.00 47.58  ? 232  ILE A O   1 
ATOM   1857  C CB  . ILE A  1 232 ? 47.078  44.124 79.255  1.00 46.58  ? 232  ILE A CB  1 
ATOM   1858  C CG1 . ILE A  1 232 ? 46.780  42.925 78.350  1.00 46.44  ? 232  ILE A CG1 1 
ATOM   1859  C CG2 . ILE A  1 232 ? 48.433  44.686 78.834  1.00 47.86  ? 232  ILE A CG2 1 
ATOM   1860  C CD1 . ILE A  1 232 ? 45.520  42.165 78.694  1.00 45.45  ? 232  ILE A CD1 1 
ATOM   1861  N N   . LEU A  1 233 ? 49.005  43.698 82.183  1.00 48.75  ? 233  LEU A N   1 
ATOM   1862  C CA  . LEU A  1 233 ? 50.063  44.278 82.994  1.00 49.96  ? 233  LEU A CA  1 
ATOM   1863  C C   . LEU A  1 233 ? 51.293  44.489 82.117  1.00 51.25  ? 233  LEU A C   1 
ATOM   1864  O O   . LEU A  1 233 ? 51.894  43.529 81.633  1.00 52.04  ? 233  LEU A O   1 
ATOM   1865  C CB  . LEU A  1 233 ? 50.379  43.359 84.176  1.00 50.69  ? 233  LEU A CB  1 
ATOM   1866  C CG  . LEU A  1 233 ? 51.377  43.861 85.222  1.00 51.97  ? 233  LEU A CG  1 
ATOM   1867  C CD1 . LEU A  1 233 ? 50.894  45.143 85.889  1.00 51.48  ? 233  LEU A CD1 1 
ATOM   1868  C CD2 . LEU A  1 233 ? 51.615  42.770 86.255  1.00 52.86  ? 233  LEU A CD2 1 
ATOM   1869  N N   . LYS A  1 234 ? 51.654  45.751 81.908  1.00 51.69  ? 234  LYS A N   1 
ATOM   1870  C CA  . LYS A  1 234 ? 52.787  46.101 81.053  1.00 53.14  ? 234  LYS A CA  1 
ATOM   1871  C C   . LYS A  1 234 ? 54.116  45.761 81.728  1.00 54.95  ? 234  LYS A C   1 
ATOM   1872  O O   . LYS A  1 234 ? 54.157  45.566 82.946  1.00 55.08  ? 234  LYS A O   1 
ATOM   1873  C CB  . LYS A  1 234 ? 52.728  47.587 80.685  1.00 53.18  ? 234  LYS A CB  1 
ATOM   1874  C CG  . LYS A  1 234 ? 51.650  47.902 79.660  1.00 52.05  ? 234  LYS A CG  1 
ATOM   1875  C CD  . LYS A  1 234 ? 51.459  49.397 79.473  1.00 52.19  ? 234  LYS A CD  1 
ATOM   1876  C CE  . LYS A  1 234 ? 50.648  49.683 78.219  1.00 51.64  ? 234  LYS A CE  1 
ATOM   1877  N NZ  . LYS A  1 234 ? 50.433  51.140 78.005  1.00 52.01  ? 234  LYS A NZ  1 
ATOM   1878  N N   . PRO A  1 235 ? 55.209  45.674 80.942  1.00 56.60  ? 235  PRO A N   1 
ATOM   1879  C CA  . PRO A  1 235 ? 56.493  45.303 81.536  1.00 58.54  ? 235  PRO A CA  1 
ATOM   1880  C C   . PRO A  1 235 ? 57.002  46.356 82.513  1.00 59.32  ? 235  PRO A C   1 
ATOM   1881  O O   . PRO A  1 235 ? 56.742  47.547 82.323  1.00 58.94  ? 235  PRO A O   1 
ATOM   1882  C CB  . PRO A  1 235 ? 57.439  45.198 80.328  1.00 60.07  ? 235  PRO A CB  1 
ATOM   1883  C CG  . PRO A  1 235 ? 56.575  45.224 79.118  1.00 58.91  ? 235  PRO A CG  1 
ATOM   1884  C CD  . PRO A  1 235 ? 55.341  45.973 79.505  1.00 56.96  ? 235  PRO A CD  1 
ATOM   1885  N N   . ASN A  1 236 ? 57.705  45.909 83.552  1.00 60.59  ? 236  ASN A N   1 
ATOM   1886  C CA  . ASN A  1 236 ? 58.306  46.802 84.544  1.00 61.67  ? 236  ASN A CA  1 
ATOM   1887  C C   . ASN A  1 236 ? 57.261  47.454 85.461  1.00 60.22  ? 236  ASN A C   1 
ATOM   1888  O O   . ASN A  1 236 ? 57.591  48.342 86.248  1.00 60.96  ? 236  ASN A O   1 
ATOM   1889  C CB  . ASN A  1 236 ? 59.158  47.882 83.844  1.00 63.04  ? 236  ASN A CB  1 
ATOM   1890  C CG  . ASN A  1 236 ? 60.564  47.999 84.411  1.00 65.51  ? 236  ASN A CG  1 
ATOM   1891  O OD1 . ASN A  1 236 ? 60.841  47.589 85.537  1.00 66.37  ? 236  ASN A OD1 1 
ATOM   1892  N ND2 . ASN A  1 236 ? 61.467  48.562 83.616  1.00 67.09  ? 236  ASN A ND2 1 
ATOM   1893  N N   . ASP A  1 237 ? 56.010  47.002 85.360  1.00 58.39  ? 237  ASP A N   1 
ATOM   1894  C CA  . ASP A  1 237 ? 54.908  47.524 86.166  1.00 57.07  ? 237  ASP A CA  1 
ATOM   1895  C C   . ASP A  1 237 ? 54.431  46.424 87.106  1.00 56.78  ? 237  ASP A C   1 
ATOM   1896  O O   . ASP A  1 237 ? 54.537  45.234 86.791  1.00 56.91  ? 237  ASP A O   1 
ATOM   1897  C CB  . ASP A  1 237 ? 53.756  47.990 85.264  1.00 55.40  ? 237  ASP A CB  1 
ATOM   1898  C CG  . ASP A  1 237 ? 52.659  48.732 86.030  1.00 54.39  ? 237  ASP A CG  1 
ATOM   1899  O OD1 . ASP A  1 237 ? 52.969  49.401 87.043  1.00 55.14  ? 237  ASP A OD1 1 
ATOM   1900  O OD2 . ASP A  1 237 ? 51.482  48.654 85.610  1.00 52.96  ? 237  ASP A OD2 1 
ATOM   1901  N N   . ALA A  1 238 ? 53.904  46.830 88.258  1.00 56.56  ? 238  ALA A N   1 
ATOM   1902  C CA  . ALA A  1 238 ? 53.480  45.895 89.289  1.00 56.64  ? 238  ALA A CA  1 
ATOM   1903  C C   . ALA A  1 238 ? 51.971  45.946 89.501  1.00 55.05  ? 238  ALA A C   1 
ATOM   1904  O O   . ALA A  1 238 ? 51.350  47.001 89.345  1.00 54.26  ? 238  ALA A O   1 
ATOM   1905  C CB  . ALA A  1 238 ? 54.203  46.200 90.592  1.00 58.22  ? 238  ALA A CB  1 
ATOM   1906  N N   . ILE A  1 239 ? 51.389  44.799 89.852  1.00 54.78  ? 239  ILE A N   1 
ATOM   1907  C CA  . ILE A  1 239 ? 49.980  44.733 90.251  1.00 53.65  ? 239  ILE A CA  1 
ATOM   1908  C C   . ILE A  1 239 ? 49.878  44.499 91.765  1.00 54.72  ? 239  ILE A C   1 
ATOM   1909  O O   . ILE A  1 239 ? 50.613  43.682 92.321  1.00 56.06  ? 239  ILE A O   1 
ATOM   1910  C CB  . ILE A  1 239 ? 49.193  43.659 89.456  1.00 52.61  ? 239  ILE A CB  1 
ATOM   1911  C CG1 . ILE A  1 239 ? 47.691  43.786 89.734  1.00 51.51  ? 239  ILE A CG1 1 
ATOM   1912  C CG2 . ILE A  1 239 ? 49.678  42.246 89.768  1.00 53.66  ? 239  ILE A CG2 1 
ATOM   1913  C CD1 . ILE A  1 239 ? 46.818  43.192 88.649  1.00 50.25  ? 239  ILE A CD1 1 
ATOM   1914  N N   . ASN A  1 240 ? 48.976  45.232 92.420  1.00 54.31  ? 240  ASN A N   1 
ATOM   1915  C CA  . ASN A  1 240 ? 48.824  45.179 93.876  1.00 55.49  ? 240  ASN A CA  1 
ATOM   1916  C C   . ASN A  1 240 ? 47.422  44.753 94.290  1.00 54.92  ? 240  ASN A C   1 
ATOM   1917  O O   . ASN A  1 240 ? 46.444  45.406 93.933  1.00 53.80  ? 240  ASN A O   1 
ATOM   1918  C CB  . ASN A  1 240 ? 49.115  46.546 94.489  1.00 56.12  ? 240  ASN A CB  1 
ATOM   1919  C CG  . ASN A  1 240 ? 50.527  47.027 94.212  1.00 56.99  ? 240  ASN A CG  1 
ATOM   1920  O OD1 . ASN A  1 240 ? 51.495  46.301 94.431  1.00 58.18  ? 240  ASN A OD1 1 
ATOM   1921  N ND2 . ASN A  1 240 ? 50.650  48.265 93.736  1.00 56.62  ? 240  ASN A ND2 1 
ATOM   1922  N N   . PHE A  1 241 ? 47.337  43.671 95.061  1.00 55.90  ? 241  PHE A N   1 
ATOM   1923  C CA  . PHE A  1 241 ? 46.067  43.174 95.582  1.00 55.79  ? 241  PHE A CA  1 
ATOM   1924  C C   . PHE A  1 241 ? 45.966  43.405 97.085  1.00 57.42  ? 241  PHE A C   1 
ATOM   1925  O O   . PHE A  1 241 ? 46.922  43.159 97.817  1.00 59.00  ? 241  PHE A O   1 
ATOM   1926  C CB  . PHE A  1 241 ? 45.931  41.680 95.295  1.00 55.93  ? 241  PHE A CB  1 
ATOM   1927  C CG  . PHE A  1 241 ? 45.731  41.362 93.847  1.00 54.36  ? 241  PHE A CG  1 
ATOM   1928  C CD1 . PHE A  1 241 ? 44.464  41.409 93.286  1.00 53.04  ? 241  PHE A CD1 1 
ATOM   1929  C CD2 . PHE A  1 241 ? 46.809  41.020 93.040  1.00 54.39  ? 241  PHE A CD2 1 
ATOM   1930  C CE1 . PHE A  1 241 ? 44.270  41.118 91.947  1.00 51.73  ? 241  PHE A CE1 1 
ATOM   1931  C CE2 . PHE A  1 241 ? 46.623  40.726 91.700  1.00 53.13  ? 241  PHE A CE2 1 
ATOM   1932  C CZ  . PHE A  1 241 ? 45.351  40.776 91.151  1.00 51.78  ? 241  PHE A CZ  1 
ATOM   1933  N N   . GLU A  1 242 ? 44.808  43.884 97.535  1.00 57.21  ? 242  GLU A N   1 
ATOM   1934  C CA  . GLU A  1 242 ? 44.483  43.925 98.959  1.00 58.94  ? 242  GLU A CA  1 
ATOM   1935  C C   . GLU A  1 242 ? 43.035  43.481 99.163  1.00 58.79  ? 242  GLU A C   1 
ATOM   1936  O O   . GLU A  1 242 ? 42.124  44.027 98.536  1.00 57.47  ? 242  GLU A O   1 
ATOM   1937  C CB  . GLU A  1 242 ? 44.706  45.326 99.541  1.00 59.49  ? 242  GLU A CB  1 
ATOM   1938  C CG  . GLU A  1 242 ? 44.503  45.422 101.050 1.00 61.62  ? 242  GLU A CG  1 
ATOM   1939  C CD  . GLU A  1 242 ? 44.641  46.841 101.576 1.00 62.21  ? 242  GLU A CD  1 
ATOM   1940  O OE1 . GLU A  1 242 ? 45.686  47.480 101.331 1.00 62.17  ? 242  GLU A OE1 1 
ATOM   1941  O OE2 . GLU A  1 242 ? 43.705  47.321 102.247 1.00 62.90  ? 242  GLU A OE2 1 
ATOM   1942  N N   . SER A  1 243 ? 42.827  42.489 100.029 1.00 60.30  ? 243  SER A N   1 
ATOM   1943  C CA  . SER A  1 243 ? 41.480  41.999 100.323 1.00 60.57  ? 243  SER A CA  1 
ATOM   1944  C C   . SER A  1 243 ? 41.364  41.366 101.708 1.00 63.06  ? 243  SER A C   1 
ATOM   1945  O O   . SER A  1 243 ? 42.273  40.665 102.160 1.00 64.39  ? 243  SER A O   1 
ATOM   1946  C CB  . SER A  1 243 ? 41.043  40.980 99.270  1.00 59.29  ? 243  SER A CB  1 
ATOM   1947  O OG  . SER A  1 243 ? 39.755  40.467 99.564  1.00 59.77  ? 243  SER A OG  1 
ATOM   1948  N N   . ASN A  1 244 ? 40.228  41.614 102.360 1.00 63.85  ? 244  ASN A N   1 
ATOM   1949  C CA  . ASN A  1 244 ? 39.878  40.971 103.633 1.00 66.40  ? 244  ASN A CA  1 
ATOM   1950  C C   . ASN A  1 244 ? 38.782  39.907 103.467 1.00 66.61  ? 244  ASN A C   1 
ATOM   1951  O O   . ASN A  1 244 ? 38.253  39.398 104.457 1.00 68.81  ? 244  ASN A O   1 
ATOM   1952  C CB  . ASN A  1 244 ? 39.440  42.020 104.665 1.00 67.79  ? 244  ASN A CB  1 
ATOM   1953  C CG  . ASN A  1 244 ? 38.253  42.846 104.195 1.00 66.60  ? 244  ASN A CG  1 
ATOM   1954  O OD1 . ASN A  1 244 ? 38.049  43.026 102.993 1.00 64.34  ? 244  ASN A OD1 1 
ATOM   1955  N ND2 . ASN A  1 244 ? 37.469  43.355 105.138 1.00 68.30  ? 244  ASN A ND2 1 
ATOM   1956  N N   . GLY A  1 245 ? 38.442  39.580 102.219 1.00 64.51  ? 245  GLY A N   1 
ATOM   1957  C CA  . GLY A  1 245 ? 37.483  38.513 101.939 1.00 64.66  ? 245  GLY A CA  1 
ATOM   1958  C C   . GLY A  1 245 ? 37.019  38.415 100.494 1.00 62.21  ? 245  GLY A C   1 
ATOM   1959  O O   . GLY A  1 245 ? 37.119  39.375 99.727  1.00 60.37  ? 245  GLY A O   1 
ATOM   1960  N N   . ASN A  1 246 ? 36.513  37.233 100.143 1.00 62.40  ? 246  ASN A N   1 
ATOM   1961  C CA  . ASN A  1 246 ? 35.871  36.951 98.847  1.00 60.49  ? 246  ASN A CA  1 
ATOM   1962  C C   . ASN A  1 246 ? 36.794  37.033 97.622  1.00 58.43  ? 246  ASN A C   1 
ATOM   1963  O O   . ASN A  1 246 ? 36.322  37.211 96.500  1.00 56.65  ? 246  ASN A O   1 
ATOM   1964  C CB  . ASN A  1 246 ? 34.635  37.843 98.647  1.00 59.76  ? 246  ASN A CB  1 
ATOM   1965  C CG  . ASN A  1 246 ? 33.688  37.815 99.839  1.00 61.99  ? 246  ASN A CG  1 
ATOM   1966  O OD1 . ASN A  1 246 ? 33.992  38.368 100.896 1.00 63.40  ? 246  ASN A OD1 1 
ATOM   1967  N ND2 . ASN A  1 246 ? 32.529  37.182 99.671  1.00 62.45  ? 246  ASN A ND2 1 
ATOM   1968  N N   . PHE A  1 247 ? 38.097  36.859 97.840  1.00 58.90  ? 247  PHE A N   1 
ATOM   1969  C CA  . PHE A  1 247 ? 39.104  37.061 96.793  1.00 57.30  ? 247  PHE A CA  1 
ATOM   1970  C C   . PHE A  1 247 ? 39.482  35.766 96.087  1.00 57.30  ? 247  PHE A C   1 
ATOM   1971  O O   . PHE A  1 247 ? 39.816  34.771 96.727  1.00 59.07  ? 247  PHE A O   1 
ATOM   1972  C CB  . PHE A  1 247 ? 40.350  37.715 97.401  1.00 57.96  ? 247  PHE A CB  1 
ATOM   1973  C CG  . PHE A  1 247 ? 41.466  37.974 96.417  1.00 56.72  ? 247  PHE A CG  1 
ATOM   1974  C CD1 . PHE A  1 247 ? 41.234  38.656 95.229  1.00 54.67  ? 247  PHE A CD1 1 
ATOM   1975  C CD2 . PHE A  1 247 ? 42.763  37.570 96.706  1.00 57.84  ? 247  PHE A CD2 1 
ATOM   1976  C CE1 . PHE A  1 247 ? 42.265  38.905 94.340  1.00 53.81  ? 247  PHE A CE1 1 
ATOM   1977  C CE2 . PHE A  1 247 ? 43.798  37.820 95.820  1.00 56.96  ? 247  PHE A CE2 1 
ATOM   1978  C CZ  . PHE A  1 247 ? 43.549  38.489 94.637  1.00 54.96  ? 247  PHE A CZ  1 
ATOM   1979  N N   . ILE A  1 248 ? 39.412  35.793 94.757  1.00 55.49  ? 248  ILE A N   1 
ATOM   1980  C CA  . ILE A  1 248 ? 39.883  34.690 93.931  1.00 55.41  ? 248  ILE A CA  1 
ATOM   1981  C C   . ILE A  1 248 ? 41.235  35.110 93.365  1.00 54.82  ? 248  ILE A C   1 
ATOM   1982  O O   . ILE A  1 248 ? 41.312  35.887 92.414  1.00 53.17  ? 248  ILE A O   1 
ATOM   1983  C CB  . ILE A  1 248 ? 38.894  34.341 92.799  1.00 54.06  ? 248  ILE A CB  1 
ATOM   1984  C CG1 . ILE A  1 248 ? 37.446  34.346 93.303  1.00 54.42  ? 248  ILE A CG1 1 
ATOM   1985  C CG2 . ILE A  1 248 ? 39.230  32.984 92.203  1.00 54.61  ? 248  ILE A CG2 1 
ATOM   1986  C CD1 . ILE A  1 248 ? 37.181  33.466 94.509  1.00 56.69  ? 248  ILE A CD1 1 
ATOM   1987  N N   . ALA A  1 249 ? 42.300  34.603 93.976  1.00 56.41  ? 249  ALA A N   1 
ATOM   1988  C CA  . ALA A  1 249 ? 43.654  35.039 93.659  1.00 56.35  ? 249  ALA A CA  1 
ATOM   1989  C C   . ALA A  1 249 ? 44.167  34.401 92.374  1.00 55.74  ? 249  ALA A C   1 
ATOM   1990  O O   . ALA A  1 249 ? 43.801  33.274 92.053  1.00 56.18  ? 249  ALA A O   1 
ATOM   1991  C CB  . ALA A  1 249 ? 44.591  34.711 94.812  1.00 58.54  ? 249  ALA A CB  1 
ATOM   1992  N N   . PRO A  1 250 ? 45.018  35.126 91.630  1.00 54.93  ? 250  PRO A N   1 
ATOM   1993  C CA  . PRO A  1 250 ? 45.661  34.539 90.459  1.00 54.76  ? 250  PRO A CA  1 
ATOM   1994  C C   . PRO A  1 250 ? 46.822  33.617 90.820  1.00 56.84  ? 250  PRO A C   1 
ATOM   1995  O O   . PRO A  1 250 ? 47.789  34.066 91.421  1.00 57.81  ? 250  PRO A O   1 
ATOM   1996  C CB  . PRO A  1 250 ? 46.182  35.759 89.693  1.00 53.50  ? 250  PRO A CB  1 
ATOM   1997  C CG  . PRO A  1 250 ? 46.350  36.822 90.716  1.00 53.73  ? 250  PRO A CG  1 
ATOM   1998  C CD  . PRO A  1 250 ? 45.304  36.568 91.759  1.00 54.15  ? 250  PRO A CD  1 
ATOM   1999  N N   . GLU A  1 251 ? 46.718  32.340 90.460  1.00 57.68  ? 251  GLU A N   1 
ATOM   2000  C CA  . GLU A  1 251 ? 47.869  31.436 90.493  1.00 59.68  ? 251  GLU A CA  1 
ATOM   2001  C C   . GLU A  1 251 ? 48.726  31.693 89.257  1.00 59.16  ? 251  GLU A C   1 
ATOM   2002  O O   . GLU A  1 251 ? 49.912  32.023 89.365  1.00 60.11  ? 251  GLU A O   1 
ATOM   2003  C CB  . GLU A  1 251 ? 47.422  29.965 90.537  1.00 60.99  ? 251  GLU A CB  1 
ATOM   2004  C CG  . GLU A  1 251 ? 47.795  29.216 91.808  1.00 63.52  ? 251  GLU A CG  1 
ATOM   2005  C CD  . GLU A  1 251 ? 48.979  28.284 91.619  1.00 65.67  ? 251  GLU A CD  1 
ATOM   2006  O OE1 . GLU A  1 251 ? 48.842  27.307 90.857  1.00 66.10  ? 251  GLU A OE1 1 
ATOM   2007  O OE2 . GLU A  1 251 ? 50.041  28.513 92.238  1.00 67.13  ? 251  GLU A OE2 1 
ATOM   2008  N N   . TYR A  1 252 ? 48.100  31.558 88.087  1.00 57.81  ? 252  TYR A N   1 
ATOM   2009  C CA  . TYR A  1 252 ? 48.776  31.716 86.799  1.00 57.44  ? 252  TYR A CA  1 
ATOM   2010  C C   . TYR A  1 252 ? 48.262  32.923 86.010  1.00 55.30  ? 252  TYR A C   1 
ATOM   2011  O O   . TYR A  1 252 ? 47.077  33.270 86.064  1.00 53.91  ? 252  TYR A O   1 
ATOM   2012  C CB  . TYR A  1 252 ? 48.599  30.456 85.953  1.00 58.06  ? 252  TYR A CB  1 
ATOM   2013  C CG  . TYR A  1 252 ? 49.205  29.218 86.567  1.00 60.51  ? 252  TYR A CG  1 
ATOM   2014  C CD1 . TYR A  1 252 ? 50.561  28.938 86.420  1.00 62.30  ? 252  TYR A CD1 1 
ATOM   2015  C CD2 . TYR A  1 252 ? 48.427  28.328 87.301  1.00 61.28  ? 252  TYR A CD2 1 
ATOM   2016  C CE1 . TYR A  1 252 ? 51.125  27.804 86.986  1.00 64.79  ? 252  TYR A CE1 1 
ATOM   2017  C CE2 . TYR A  1 252 ? 48.978  27.192 87.869  1.00 63.76  ? 252  TYR A CE2 1 
ATOM   2018  C CZ  . TYR A  1 252 ? 50.330  26.934 87.711  1.00 65.52  ? 252  TYR A CZ  1 
ATOM   2019  O OH  . TYR A  1 252 ? 50.885  25.805 88.272  1.00 68.21  ? 252  TYR A OH  1 
ATOM   2020  N N   . ALA A  1 253 ? 49.177  33.552 85.277  1.00 55.30  ? 253  ALA A N   1 
ATOM   2021  C CA  . ALA A  1 253 ? 48.851  34.637 84.359  1.00 53.64  ? 253  ALA A CA  1 
ATOM   2022  C C   . ALA A  1 253 ? 49.491  34.335 83.007  1.00 54.05  ? 253  ALA A C   1 
ATOM   2023  O O   . ALA A  1 253 ? 50.643  33.894 82.943  1.00 55.72  ? 253  ALA A O   1 
ATOM   2024  C CB  . ALA A  1 253 ? 49.360  35.962 84.906  1.00 53.43  ? 253  ALA A CB  1 
ATOM   2025  N N   . TYR A  1 254 ? 48.744  34.566 81.932  1.00 52.74  ? 254  TYR A N   1 
ATOM   2026  C CA  . TYR A  1 254 ? 49.220  34.262 80.585  1.00 53.19  ? 254  TYR A CA  1 
ATOM   2027  C C   . TYR A  1 254 ? 50.179  35.330 80.071  1.00 53.47  ? 254  TYR A C   1 
ATOM   2028  O O   . TYR A  1 254 ? 49.999  36.520 80.320  1.00 52.54  ? 254  TYR A O   1 
ATOM   2029  C CB  . TYR A  1 254 ? 48.043  34.108 79.623  1.00 51.88  ? 254  TYR A CB  1 
ATOM   2030  C CG  . TYR A  1 254 ? 47.244  32.845 79.842  1.00 52.06  ? 254  TYR A CG  1 
ATOM   2031  C CD1 . TYR A  1 254 ? 47.610  31.654 79.224  1.00 53.39  ? 254  TYR A CD1 1 
ATOM   2032  C CD2 . TYR A  1 254 ? 46.127  32.839 80.666  1.00 51.14  ? 254  TYR A CD2 1 
ATOM   2033  C CE1 . TYR A  1 254 ? 46.883  30.491 79.415  1.00 53.76  ? 254  TYR A CE1 1 
ATOM   2034  C CE2 . TYR A  1 254 ? 45.395  31.682 80.866  1.00 51.53  ? 254  TYR A CE2 1 
ATOM   2035  C CZ  . TYR A  1 254 ? 45.776  30.508 80.239  1.00 52.83  ? 254  TYR A CZ  1 
ATOM   2036  O OH  . TYR A  1 254 ? 45.054  29.348 80.435  1.00 53.41  ? 254  TYR A OH  1 
ATOM   2037  N N   . LYS A  1 255 ? 51.192  34.884 79.339  1.00 54.99  ? 255  LYS A N   1 
ATOM   2038  C CA  . LYS A  1 255 ? 52.229  35.755 78.796  1.00 55.74  ? 255  LYS A CA  1 
ATOM   2039  C C   . LYS A  1 255 ? 52.016  35.827 77.291  1.00 55.50  ? 255  LYS A C   1 
ATOM   2040  O O   . LYS A  1 255 ? 51.856  34.796 76.640  1.00 56.04  ? 255  LYS A O   1 
ATOM   2041  C CB  . LYS A  1 255 ? 53.605  35.161 79.111  1.00 58.07  ? 255  LYS A CB  1 
ATOM   2042  C CG  . LYS A  1 255 ? 54.683  36.156 79.515  1.00 58.97  ? 255  LYS A CG  1 
ATOM   2043  C CD  . LYS A  1 255 ? 55.795  35.473 80.324  1.00 61.17  ? 255  LYS A CD  1 
ATOM   2044  C CE  . LYS A  1 255 ? 57.133  35.353 79.598  1.00 63.45  ? 255  LYS A CE  1 
ATOM   2045  N NZ  . LYS A  1 255 ? 58.221  34.995 80.559  1.00 65.58  ? 255  LYS A NZ  1 
ATOM   2046  N N   . ILE A  1 256 ? 52.022  37.039 76.742  1.00 54.85  ? 256  ILE A N   1 
ATOM   2047  C CA  . ILE A  1 256 ? 51.726  37.240 75.323  1.00 54.67  ? 256  ILE A CA  1 
ATOM   2048  C C   . ILE A  1 256 ? 53.040  37.314 74.548  1.00 56.71  ? 256  ILE A C   1 
ATOM   2049  O O   . ILE A  1 256 ? 53.617  38.386 74.379  1.00 57.10  ? 256  ILE A O   1 
ATOM   2050  C CB  . ILE A  1 256 ? 50.886  38.517 75.068  1.00 53.06  ? 256  ILE A CB  1 
ATOM   2051  C CG1 . ILE A  1 256 ? 49.956  38.818 76.252  1.00 51.48  ? 256  ILE A CG1 1 
ATOM   2052  C CG2 . ILE A  1 256 ? 50.099  38.366 73.772  1.00 52.59  ? 256  ILE A CG2 1 
ATOM   2053  C CD1 . ILE A  1 256 ? 48.991  39.961 76.016  1.00 50.02  ? 256  ILE A CD1 1 
ATOM   2054  N N   . VAL A  1 257 ? 53.519  36.162 74.091  1.00 58.22  ? 257  VAL A N   1 
ATOM   2055  C CA  . VAL A  1 257 ? 54.818  36.098 73.415  1.00 60.56  ? 257  VAL A CA  1 
ATOM   2056  C C   . VAL A  1 257 ? 54.736  36.543 71.948  1.00 60.94  ? 257  VAL A C   1 
ATOM   2057  O O   . VAL A  1 257 ? 55.649  37.216 71.451  1.00 62.39  ? 257  VAL A O   1 
ATOM   2058  C CB  . VAL A  1 257 ? 55.486  34.702 73.535  1.00 62.49  ? 257  VAL A CB  1 
ATOM   2059  C CG1 . VAL A  1 257 ? 55.861  34.420 74.983  1.00 62.76  ? 257  VAL A CG1 1 
ATOM   2060  C CG2 . VAL A  1 257 ? 54.601  33.590 72.985  1.00 62.10  ? 257  VAL A CG2 1 
ATOM   2061  N N   . LYS A  1 258 ? 53.651  36.173 71.264  1.00 59.82  ? 258  LYS A N   1 
ATOM   2062  C CA  . LYS A  1 258 ? 53.452  36.545 69.858  1.00 60.22  ? 258  LYS A CA  1 
ATOM   2063  C C   . LYS A  1 258 ? 52.160  37.318 69.620  1.00 58.08  ? 258  LYS A C   1 
ATOM   2064  O O   . LYS A  1 258 ? 51.083  36.883 70.031  1.00 56.46  ? 258  LYS A O   1 
ATOM   2065  C CB  . LYS A  1 258 ? 53.473  35.307 68.950  1.00 61.57  ? 258  LYS A CB  1 
ATOM   2066  C CG  . LYS A  1 258 ? 54.708  35.215 68.065  1.00 64.34  ? 258  LYS A CG  1 
ATOM   2067  C CD  . LYS A  1 258 ? 54.357  34.864 66.624  1.00 65.21  ? 258  LYS A CD  1 
ATOM   2068  C CE  . LYS A  1 258 ? 53.888  33.426 66.470  1.00 65.46  ? 258  LYS A CE  1 
ATOM   2069  N NZ  . LYS A  1 258 ? 54.186  32.924 65.098  1.00 67.60  ? 258  LYS A NZ  1 
ATOM   2070  N N   . LYS A  1 259 ? 52.288  38.459 68.944  1.00 58.32  ? 259  LYS A N   1 
ATOM   2071  C CA  . LYS A  1 259 ? 51.146  39.236 68.469  1.00 56.82  ? 259  LYS A CA  1 
ATOM   2072  C C   . LYS A  1 259 ? 51.108  39.182 66.946  1.00 58.06  ? 259  LYS A C   1 
ATOM   2073  O O   . LYS A  1 259 ? 52.017  39.685 66.281  1.00 59.87  ? 259  LYS A O   1 
ATOM   2074  C CB  . LYS A  1 259 ? 51.258  40.692 68.920  1.00 56.30  ? 259  LYS A CB  1 
ATOM   2075  C CG  . LYS A  1 259 ? 51.009  40.906 70.402  1.00 54.86  ? 259  LYS A CG  1 
ATOM   2076  C CD  . LYS A  1 259 ? 51.309  42.339 70.817  1.00 54.80  ? 259  LYS A CD  1 
ATOM   2077  C CE  . LYS A  1 259 ? 51.101  42.529 72.312  1.00 53.59  ? 259  LYS A CE  1 
ATOM   2078  N NZ  . LYS A  1 259 ? 51.540  43.871 72.786  1.00 53.82  ? 259  LYS A NZ  1 
ATOM   2079  N N   . GLY A  1 260 ? 50.065  38.565 66.397  1.00 69.62  ? 260  GLY A N   1 
ATOM   2080  C CA  . GLY A  1 260 ? 49.907  38.465 64.947  1.00 68.13  ? 260  GLY A CA  1 
ATOM   2081  C C   . GLY A  1 260 ? 48.458  38.524 64.507  1.00 63.71  ? 260  GLY A C   1 
ATOM   2082  O O   . GLY A  1 260 ? 47.562  38.768 65.314  1.00 62.06  ? 260  GLY A O   1 
ATOM   2083  N N   . ASP A  1 261 ? 48.233  38.298 63.218  1.00 62.12  ? 261  ASP A N   1 
ATOM   2084  C CA  . ASP A  1 261 ? 46.880  38.228 62.687  1.00 58.26  ? 261  ASP A CA  1 
ATOM   2085  C C   . ASP A  1 261 ? 46.246  36.902 63.073  1.00 56.22  ? 261  ASP A C   1 
ATOM   2086  O O   . ASP A  1 261 ? 46.785  35.835 62.780  1.00 56.97  ? 261  ASP A O   1 
ATOM   2087  C CB  . ASP A  1 261 ? 46.871  38.397 61.162  1.00 57.45  ? 261  ASP A CB  1 
ATOM   2088  C CG  . ASP A  1 261 ? 47.041  39.843 60.733  1.00 58.86  ? 261  ASP A CG  1 
ATOM   2089  O OD1 . ASP A  1 261 ? 46.931  40.740 61.601  1.00 60.10  ? 261  ASP A OD1 1 
ATOM   2090  O OD2 . ASP A  1 261 ? 47.278  40.083 59.528  1.00 58.99  ? 261  ASP A OD2 1 
ATOM   2091  N N   . SER A  1 262 ? 45.103  36.985 63.740  1.00 54.13  ? 262  SER A N   1 
ATOM   2092  C CA  . SER A  1 262 ? 44.353  35.813 64.162  1.00 52.48  ? 262  SER A CA  1 
ATOM   2093  C C   . SER A  1 262 ? 42.871  36.170 64.169  1.00 49.92  ? 262  SER A C   1 
ATOM   2094  O O   . SER A  1 262 ? 42.504  37.325 63.933  1.00 49.67  ? 262  SER A O   1 
ATOM   2095  C CB  . SER A  1 262 ? 44.814  35.365 65.554  1.00 54.17  ? 262  SER A CB  1 
ATOM   2096  O OG  . SER A  1 262 ? 44.006  34.319 66.067  1.00 52.84  ? 262  SER A OG  1 
ATOM   2097  N N   . THR A  1 263 ? 42.021  35.182 64.426  1.00 48.54  ? 263  THR A N   1 
ATOM   2098  C CA  . THR A  1 263 ? 40.584  35.415 64.482  1.00 46.64  ? 263  THR A CA  1 
ATOM   2099  C C   . THR A  1 263 ? 39.893  34.312 65.275  1.00 46.34  ? 263  THR A C   1 
ATOM   2100  O O   . THR A  1 263 ? 40.332  33.161 65.260  1.00 47.02  ? 263  THR A O   1 
ATOM   2101  C CB  . THR A  1 263 ? 39.974  35.517 63.063  1.00 45.02  ? 263  THR A CB  1 
ATOM   2102  O OG1 . THR A  1 263 ? 38.736  36.228 63.121  1.00 43.96  ? 263  THR A OG1 1 
ATOM   2103  C CG2 . THR A  1 263 ? 39.736  34.144 62.440  1.00 44.38  ? 263  THR A CG2 1 
ATOM   2104  N N   . ILE A  1 264 ? 38.821  34.675 65.973  1.00 45.78  ? 264  ILE A N   1 
ATOM   2105  C CA  . ILE A  1 264 ? 37.983  33.693 66.643  1.00 45.69  ? 264  ILE A CA  1 
ATOM   2106  C C   . ILE A  1 264 ? 36.828  33.350 65.710  1.00 44.45  ? 264  ILE A C   1 
ATOM   2107  O O   . ILE A  1 264 ? 35.907  34.143 65.512  1.00 43.77  ? 264  ILE A O   1 
ATOM   2108  C CB  . ILE A  1 264 ? 37.470  34.188 68.005  1.00 46.29  ? 264  ILE A CB  1 
ATOM   2109  C CG1 . ILE A  1 264 ? 38.656  34.506 68.917  1.00 47.83  ? 264  ILE A CG1 1 
ATOM   2110  C CG2 . ILE A  1 264 ? 36.590  33.124 68.654  1.00 46.47  ? 264  ILE A CG2 1 
ATOM   2111  C CD1 . ILE A  1 264 ? 38.303  35.360 70.112  1.00 48.59  ? 264  ILE A CD1 1 
ATOM   2112  N N   . MET A  1 265 ? 36.911  32.153 65.140  1.00 44.59  ? 265  MET A N   1 
ATOM   2113  C CA  . MET A  1 265 ? 35.964  31.661 64.157  1.00 43.87  ? 265  MET A CA  1 
ATOM   2114  C C   . MET A  1 265 ? 34.866  30.871 64.864  1.00 44.65  ? 265  MET A C   1 
ATOM   2115  O O   . MET A  1 265 ? 35.146  30.059 65.744  1.00 45.89  ? 265  MET A O   1 
ATOM   2116  C CB  . MET A  1 265 ? 36.715  30.761 63.181  1.00 44.22  ? 265  MET A CB  1 
ATOM   2117  C CG  . MET A  1 265 ? 35.961  30.375 61.927  1.00 43.56  ? 265  MET A CG  1 
ATOM   2118  S SD  . MET A  1 265 ? 37.045  29.452 60.821  1.00 44.39  ? 265  MET A SD  1 
ATOM   2119  C CE  . MET A  1 265 ? 38.154  30.740 60.241  1.00 43.52  ? 265  MET A CE  1 
ATOM   2120  N N   . LYS A  1 266 ? 33.617  31.129 64.489  1.00 44.29  ? 266  LYS A N   1 
ATOM   2121  C CA  . LYS A  1 266 ? 32.478  30.440 65.077  1.00 45.55  ? 266  LYS A CA  1 
ATOM   2122  C C   . LYS A  1 266 ? 32.053  29.301 64.168  1.00 46.33  ? 266  LYS A C   1 
ATOM   2123  O O   . LYS A  1 266 ? 31.607  29.532 63.042  1.00 45.63  ? 266  LYS A O   1 
ATOM   2124  C CB  . LYS A  1 266 ? 31.315  31.409 65.299  1.00 45.50  ? 266  LYS A CB  1 
ATOM   2125  C CG  . LYS A  1 266 ? 31.506  32.354 66.479  1.00 45.66  ? 266  LYS A CG  1 
ATOM   2126  C CD  . LYS A  1 266 ? 31.451  31.606 67.801  1.00 47.04  ? 266  LYS A CD  1 
ATOM   2127  C CE  . LYS A  1 266 ? 31.263  32.546 68.976  1.00 47.56  ? 266  LYS A CE  1 
ATOM   2128  N NZ  . LYS A  1 266 ? 31.023  31.796 70.245  1.00 49.03  ? 266  LYS A NZ  1 
ATOM   2129  N N   . SER A  1 267 ? 32.200  28.072 64.657  1.00 48.12  ? 267  SER A N   1 
ATOM   2130  C CA  . SER A  1 267 ? 31.904  26.887 63.860  1.00 49.60  ? 267  SER A CA  1 
ATOM   2131  C C   . SER A  1 267 ? 31.632  25.663 64.732  1.00 52.35  ? 267  SER A C   1 
ATOM   2132  O O   . SER A  1 267 ? 32.259  25.478 65.781  1.00 52.97  ? 267  SER A O   1 
ATOM   2133  C CB  . SER A  1 267 ? 33.070  26.595 62.913  1.00 49.15  ? 267  SER A CB  1 
ATOM   2134  O OG  . SER A  1 267 ? 32.821  25.438 62.130  1.00 50.92  ? 267  SER A OG  1 
ATOM   2135  N N   . GLU A  1 268 ? 30.698  24.830 64.280  1.00 54.35  ? 268  GLU A N   1 
ATOM   2136  C CA  . GLU A  1 268 ? 30.382  23.569 64.950  1.00 57.65  ? 268  GLU A CA  1 
ATOM   2137  C C   . GLU A  1 268 ? 31.276  22.442 64.437  1.00 59.42  ? 268  GLU A C   1 
ATOM   2138  O O   . GLU A  1 268 ? 31.290  21.353 65.011  1.00 62.48  ? 268  GLU A O   1 
ATOM   2139  C CB  . GLU A  1 268 ? 28.910  23.189 64.737  1.00 59.80  ? 268  GLU A CB  1 
ATOM   2140  C CG  . GLU A  1 268 ? 27.907  24.293 65.052  1.00 58.72  ? 268  GLU A CG  1 
ATOM   2141  C CD  . GLU A  1 268 ? 28.027  24.817 66.471  1.00 58.32  ? 268  GLU A CD  1 
ATOM   2142  O OE1 . GLU A  1 268 ? 27.996  23.997 67.415  1.00 60.58  ? 268  GLU A OE1 1 
ATOM   2143  O OE2 . GLU A  1 268 ? 28.147  26.053 66.633  1.00 55.98  ? 268  GLU A OE2 1 
ATOM   2144  N N   . LEU A  1 269 ? 32.017  22.704 63.361  1.00 57.89  ? 269  LEU A N   1 
ATOM   2145  C CA  . LEU A  1 269 ? 32.877  21.692 62.745  1.00 59.86  ? 269  LEU A CA  1 
ATOM   2146  C C   . LEU A  1 269 ? 34.094  21.383 63.608  1.00 60.84  ? 269  LEU A C   1 
ATOM   2147  O O   . LEU A  1 269 ? 34.510  22.198 64.433  1.00 59.06  ? 269  LEU A O   1 
ATOM   2148  C CB  . LEU A  1 269 ? 33.328  22.136 61.350  1.00 57.99  ? 269  LEU A CB  1 
ATOM   2149  C CG  . LEU A  1 269 ? 32.240  22.127 60.271  1.00 57.92  ? 269  LEU A CG  1 
ATOM   2150  C CD1 . LEU A  1 269 ? 32.689  22.904 59.046  1.00 55.32  ? 269  LEU A CD1 1 
ATOM   2151  C CD2 . LEU A  1 269 ? 31.866  20.706 59.884  1.00 61.84  ? 269  LEU A CD2 1 
ATOM   2152  N N   . GLU A  1 270 ? 34.659  20.197 63.394  1.00 64.10  ? 270  GLU A N   1 
ATOM   2153  C CA  . GLU A  1 270 ? 35.787  19.712 64.196  1.00 66.02  ? 270  GLU A CA  1 
ATOM   2154  C C   . GLU A  1 270 ? 37.108  19.928 63.430  1.00 65.53  ? 270  GLU A C   1 
ATOM   2155  O O   . GLU A  1 270 ? 37.483  21.078 63.198  1.00 62.40  ? 270  GLU A O   1 
ATOM   2156  C CB  . GLU A  1 270 ? 35.563  18.257 64.686  1.00 70.74  ? 270  GLU A CB  1 
ATOM   2157  C CG  . GLU A  1 270 ? 34.778  17.347 63.742  1.00 73.42  ? 270  GLU A CG  1 
ATOM   2158  C CD  . GLU A  1 270 ? 34.611  15.926 64.265  1.00 78.72  ? 270  GLU A CD  1 
ATOM   2159  O OE1 . GLU A  1 270 ? 35.102  15.614 65.373  1.00 80.27  ? 270  GLU A OE1 1 
ATOM   2160  O OE2 . GLU A  1 270 ? 33.977  15.110 63.560  1.00 81.67  ? 270  GLU A OE2 1 
ATOM   2161  N N   . TYR A  1 271 ? 37.797  18.862 63.025  1.00 69.00  ? 271  TYR A N   1 
ATOM   2162  C CA  . TYR A  1 271 ? 39.131  18.987 62.436  1.00 69.36  ? 271  TYR A CA  1 
ATOM   2163  C C   . TYR A  1 271 ? 39.312  17.999 61.281  1.00 72.36  ? 271  TYR A C   1 
ATOM   2164  O O   . TYR A  1 271 ? 39.163  16.789 61.460  1.00 76.45  ? 271  TYR A O   1 
ATOM   2165  C CB  . TYR A  1 271 ? 40.190  18.746 63.516  1.00 71.47  ? 271  TYR A CB  1 
ATOM   2166  C CG  . TYR A  1 271 ? 41.616  18.983 63.068  1.00 72.28  ? 271  TYR A CG  1 
ATOM   2167  C CD1 . TYR A  1 271 ? 42.037  20.243 62.652  1.00 68.96  ? 271  TYR A CD1 1 
ATOM   2168  C CD2 . TYR A  1 271 ? 42.551  17.948 63.077  1.00 76.91  ? 271  TYR A CD2 1 
ATOM   2169  C CE1 . TYR A  1 271 ? 43.343  20.464 62.247  1.00 70.21  ? 271  TYR A CE1 1 
ATOM   2170  C CE2 . TYR A  1 271 ? 43.858  18.160 62.676  1.00 78.23  ? 271  TYR A CE2 1 
ATOM   2171  C CZ  . TYR A  1 271 ? 44.250  19.419 62.261  1.00 74.87  ? 271  TYR A CZ  1 
ATOM   2172  O OH  . TYR A  1 271 ? 45.551  19.621 61.863  1.00 76.72  ? 271  TYR A OH  1 
ATOM   2173  N N   . GLY A  1 272 ? 39.632  18.523 60.099  1.00 70.61  ? 272  GLY A N   1 
ATOM   2174  C CA  . GLY A  1 272 ? 39.800  17.695 58.903  1.00 73.25  ? 272  GLY A CA  1 
ATOM   2175  C C   . GLY A  1 272 ? 41.177  17.072 58.734  1.00 76.95  ? 272  GLY A C   1 
ATOM   2176  O O   . GLY A  1 272 ? 41.357  16.181 57.898  1.00 80.29  ? 272  GLY A O   1 
ATOM   2177  N N   . ASN A  1 273 ? 42.147  17.537 59.522  1.00 76.79  ? 273  ASN A N   1 
ATOM   2178  C CA  . ASN A  1 273 ? 43.547  17.105 59.406  1.00 80.47  ? 273  ASN A CA  1 
ATOM   2179  C C   . ASN A  1 273 ? 44.117  17.398 58.013  1.00 80.19  ? 273  ASN A C   1 
ATOM   2180  O O   . ASN A  1 273 ? 44.897  16.623 57.456  1.00 84.36  ? 273  ASN A O   1 
ATOM   2181  C CB  . ASN A  1 273 ? 43.692  15.625 59.785  1.00 86.21  ? 273  ASN A CB  1 
ATOM   2182  C CG  . ASN A  1 273 ? 44.985  15.340 60.527  1.00 89.82  ? 273  ASN A CG  1 
ATOM   2183  O OD1 . ASN A  1 273 ? 44.971  14.786 61.626  1.00 92.13  ? 273  ASN A OD1 1 
ATOM   2184  N ND2 . ASN A  1 273 ? 46.109  15.735 59.937  1.00 90.56  ? 273  ASN A ND2 1 
ATOM   2185  N N   . CYS A  1 274 ? 43.720  18.550 57.484  1.00 75.47  ? 274  CYS A N   1 
ATOM   2186  C CA  . CYS A  1 274 ? 44.094  19.013 56.155  1.00 74.40  ? 274  CYS A CA  1 
ATOM   2187  C C   . CYS A  1 274 ? 44.944  20.275 56.297  1.00 72.18  ? 274  CYS A C   1 
ATOM   2188  O O   . CYS A  1 274 ? 45.204  20.734 57.412  1.00 71.60  ? 274  CYS A O   1 
ATOM   2189  C CB  . CYS A  1 274 ? 42.822  19.329 55.354  1.00 71.05  ? 274  CYS A CB  1 
ATOM   2190  S SG  . CYS A  1 274 ? 41.529  20.067 56.382  1.00 67.04  ? 274  CYS A SG  1 
ATOM   2191  N N   . ASN A  1 275 ? 45.374  20.826 55.167  1.00 71.24  ? 275  ASN A N   1 
ATOM   2192  C CA  . ASN A  1 275 ? 46.091  22.096 55.137  1.00 69.31  ? 275  ASN A CA  1 
ATOM   2193  C C   . ASN A  1 275 ? 45.472  23.022 54.091  1.00 65.39  ? 275  ASN A C   1 
ATOM   2194  O O   . ASN A  1 275 ? 44.954  22.556 53.075  1.00 65.29  ? 275  ASN A O   1 
ATOM   2195  C CB  . ASN A  1 275 ? 47.571  21.857 54.829  1.00 73.45  ? 275  ASN A CB  1 
ATOM   2196  C CG  . ASN A  1 275 ? 48.407  23.119 54.952  1.00 72.48  ? 275  ASN A CG  1 
ATOM   2197  O OD1 . ASN A  1 275 ? 48.380  23.792 55.978  1.00 71.05  ? 275  ASN A OD1 1 
ATOM   2198  N ND2 . ASN A  1 275 ? 49.155  23.445 53.906  1.00 73.62  ? 275  ASN A ND2 1 
ATOM   2199  N N   . THR A  1 276 ? 45.515  24.328 54.343  1.00 62.49  ? 276  THR A N   1 
ATOM   2200  C CA  . THR A  1 276 ? 44.980  25.304 53.392  1.00 59.06  ? 276  THR A CA  1 
ATOM   2201  C C   . THR A  1 276 ? 45.695  26.647 53.484  1.00 58.10  ? 276  THR A C   1 
ATOM   2202  O O   . THR A  1 276 ? 46.511  26.871 54.375  1.00 59.84  ? 276  THR A O   1 
ATOM   2203  C CB  . THR A  1 276 ? 43.460  25.509 53.592  1.00 55.73  ? 276  THR A CB  1 
ATOM   2204  O OG1 . THR A  1 276 ? 42.926  26.271 52.503  1.00 53.07  ? 276  THR A OG1 1 
ATOM   2205  C CG2 . THR A  1 276 ? 43.152  26.224 54.914  1.00 54.18  ? 276  THR A CG2 1 
ATOM   2206  N N   . LYS A  1 277 ? 45.387  27.528 52.538  1.00 55.72  ? 277  LYS A N   1 
ATOM   2207  C CA  . LYS A  1 277 ? 45.880  28.909 52.551  1.00 54.82  ? 277  LYS A CA  1 
ATOM   2208  C C   . LYS A  1 277 ? 44.745  29.925 52.733  1.00 51.11  ? 277  LYS A C   1 
ATOM   2209  O O   . LYS A  1 277 ? 44.993  31.126 52.841  1.00 50.45  ? 277  LYS A O   1 
ATOM   2210  C CB  . LYS A  1 277 ? 46.657  29.208 51.265  1.00 55.99  ? 277  LYS A CB  1 
ATOM   2211  C CG  . LYS A  1 277 ? 48.156  28.946 51.334  1.00 60.29  ? 277  LYS A CG  1 
ATOM   2212  C CD  . LYS A  1 277 ? 48.923  29.842 50.362  1.00 61.16  ? 277  LYS A CD  1 
ATOM   2213  C CE  . LYS A  1 277 ? 48.817  31.334 50.679  1.00 59.44  ? 277  LYS A CE  1 
ATOM   2214  N NZ  . LYS A  1 277 ? 49.961  32.096 50.100  1.00 62.14  ? 277  LYS A NZ  1 
ATOM   2215  N N   . CYS A  1 278 ? 43.508  29.435 52.763  1.00 49.23  ? 278  CYS A N   1 
ATOM   2216  C CA  . CYS A  1 278 ? 42.331  30.270 52.956  1.00 46.27  ? 278  CYS A CA  1 
ATOM   2217  C C   . CYS A  1 278 ? 41.279  29.443 53.675  1.00 45.86  ? 278  CYS A C   1 
ATOM   2218  O O   . CYS A  1 278 ? 40.872  28.390 53.177  1.00 46.56  ? 278  CYS A O   1 
ATOM   2219  C CB  . CYS A  1 278 ? 41.781  30.731 51.608  1.00 44.48  ? 278  CYS A CB  1 
ATOM   2220  S SG  . CYS A  1 278 ? 40.225  31.651 51.713  1.00 41.53  ? 278  CYS A SG  1 
ATOM   2221  N N   . GLN A  1 279 ? 40.838  29.914 54.839  1.00 45.10  ? 279  GLN A N   1 
ATOM   2222  C CA  . GLN A  1 279 ? 39.917  29.143 55.668  1.00 45.17  ? 279  GLN A CA  1 
ATOM   2223  C C   . GLN A  1 279 ? 38.620  29.890 55.936  1.00 43.09  ? 279  GLN A C   1 
ATOM   2224  O O   . GLN A  1 279 ? 38.628  31.098 56.158  1.00 41.97  ? 279  GLN A O   1 
ATOM   2225  C CB  . GLN A  1 279 ? 40.584  28.788 56.997  1.00 46.90  ? 279  GLN A CB  1 
ATOM   2226  C CG  . GLN A  1 279 ? 39.750  27.881 57.890  1.00 47.52  ? 279  GLN A CG  1 
ATOM   2227  C CD  . GLN A  1 279 ? 39.673  26.460 57.372  1.00 49.52  ? 279  GLN A CD  1 
ATOM   2228  O OE1 . GLN A  1 279 ? 40.698  25.820 57.155  1.00 51.79  ? 279  GLN A OE1 1 
ATOM   2229  N NE2 . GLN A  1 279 ? 38.459  25.955 57.178  1.00 49.23  ? 279  GLN A NE2 1 
ATOM   2230  N N   . THR A  1 280 ? 37.513  29.149 55.917  1.00 43.14  ? 280  THR A N   1 
ATOM   2231  C CA  . THR A  1 280 ? 36.206  29.661 56.313  1.00 42.02  ? 280  THR A CA  1 
ATOM   2232  C C   . THR A  1 280 ? 35.600  28.763 57.402  1.00 43.46  ? 280  THR A C   1 
ATOM   2233  O O   . THR A  1 280 ? 36.042  27.623 57.587  1.00 45.28  ? 280  THR A O   1 
ATOM   2234  C CB  . THR A  1 280 ? 35.227  29.731 55.115  1.00 41.10  ? 280  THR A CB  1 
ATOM   2235  O OG1 . THR A  1 280 ? 34.560  28.473 54.940  1.00 42.55  ? 280  THR A OG1 1 
ATOM   2236  C CG2 . THR A  1 280 ? 35.957  30.102 53.828  1.00 40.38  ? 280  THR A CG2 1 
ATOM   2237  N N   . PRO A  1 281 ? 34.587  29.276 58.128  1.00 43.02  ? 281  PRO A N   1 
ATOM   2238  C CA  . PRO A  1 281 ? 33.818  28.456 59.087  1.00 44.58  ? 281  PRO A CA  1 
ATOM   2239  C C   . PRO A  1 281 ? 33.039  27.289 58.451  1.00 46.23  ? 281  PRO A C   1 
ATOM   2240  O O   . PRO A  1 281 ? 32.648  26.357 59.162  1.00 48.24  ? 281  PRO A O   1 
ATOM   2241  C CB  . PRO A  1 281 ? 32.839  29.449 59.728  1.00 43.78  ? 281  PRO A CB  1 
ATOM   2242  C CG  . PRO A  1 281 ? 33.226  30.809 59.271  1.00 42.04  ? 281  PRO A CG  1 
ATOM   2243  C CD  . PRO A  1 281 ? 34.324  30.720 58.263  1.00 41.51  ? 281  PRO A CD  1 
ATOM   2244  N N   . MET A  1 282 ? 32.813  27.356 57.136  1.00 45.71  ? 282  MET A N   1 
ATOM   2245  C CA  . MET A  1 282 ? 32.163  26.283 56.369  1.00 47.54  ? 282  MET A CA  1 
ATOM   2246  C C   . MET A  1 282 ? 33.173  25.223 55.932  1.00 49.11  ? 282  MET A C   1 
ATOM   2247  O O   . MET A  1 282 ? 32.828  24.053 55.757  1.00 51.64  ? 282  MET A O   1 
ATOM   2248  C CB  . MET A  1 282 ? 31.521  26.860 55.105  1.00 46.39  ? 282  MET A CB  1 
ATOM   2249  C CG  . MET A  1 282 ? 30.561  28.015 55.342  1.00 45.24  ? 282  MET A CG  1 
ATOM   2250  S SD  . MET A  1 282 ? 28.864  27.446 55.531  1.00 47.82  ? 282  MET A SD  1 
ATOM   2251  C CE  . MET A  1 282 ? 28.471  27.089 53.818  1.00 48.09  ? 282  MET A CE  1 
ATOM   2252  N N   . GLY A  1 283 ? 34.415  25.655 55.728  1.00 48.04  ? 283  GLY A N   1 
ATOM   2253  C CA  . GLY A  1 283 ? 35.468  24.797 55.201  1.00 49.76  ? 283  GLY A CA  1 
ATOM   2254  C C   . GLY A  1 283 ? 36.579  25.619 54.571  1.00 48.25  ? 283  GLY A C   1 
ATOM   2255  O O   . GLY A  1 283 ? 36.535  26.851 54.587  1.00 45.96  ? 283  GLY A O   1 
ATOM   2256  N N   . ALA A  1 284 ? 37.571  24.940 54.004  1.00 50.01  ? 284  ALA A N   1 
ATOM   2257  C CA  . ALA A  1 284 ? 38.737  25.606 53.425  1.00 49.36  ? 284  ALA A CA  1 
ATOM   2258  C C   . ALA A  1 284 ? 38.574  25.836 51.921  1.00 48.35  ? 284  ALA A C   1 
ATOM   2259  O O   . ALA A  1 284 ? 37.770  25.168 51.261  1.00 48.88  ? 284  ALA A O   1 
ATOM   2260  C CB  . ALA A  1 284 ? 39.988  24.791 53.698  1.00 52.39  ? 284  ALA A CB  1 
ATOM   2261  N N   . ILE A  1 285 ? 39.354  26.780 51.393  1.00 47.17  ? 285  ILE A N   1 
ATOM   2262  C CA  . ILE A  1 285 ? 39.292  27.167 49.980  1.00 46.05  ? 285  ILE A CA  1 
ATOM   2263  C C   . ILE A  1 285 ? 40.648  26.981 49.288  1.00 47.81  ? 285  ILE A C   1 
ATOM   2264  O O   . ILE A  1 285 ? 41.692  27.375 49.814  1.00 48.70  ? 285  ILE A O   1 
ATOM   2265  C CB  . ILE A  1 285 ? 38.792  28.628 49.823  1.00 43.14  ? 285  ILE A CB  1 
ATOM   2266  C CG1 . ILE A  1 285 ? 37.263  28.653 49.724  1.00 41.81  ? 285  ILE A CG1 1 
ATOM   2267  C CG2 . ILE A  1 285 ? 39.383  29.302 48.589  1.00 42.46  ? 285  ILE A CG2 1 
ATOM   2268  C CD1 . ILE A  1 285 ? 36.639  29.981 50.093  1.00 39.74  ? 285  ILE A CD1 1 
ATOM   2269  N N   . ASN A  1 286 ? 40.603  26.374 48.104  1.00 48.65  ? 286  ASN A N   1 
ATOM   2270  C CA  . ASN A  1 286 ? 41.768  26.212 47.245  1.00 50.47  ? 286  ASN A CA  1 
ATOM   2271  C C   . ASN A  1 286 ? 41.382  26.558 45.811  1.00 48.98  ? 286  ASN A C   1 
ATOM   2272  O O   . ASN A  1 286 ? 40.903  25.706 45.061  1.00 49.93  ? 286  ASN A O   1 
ATOM   2273  C CB  . ASN A  1 286 ? 42.297  24.774 47.320  1.00 54.37  ? 286  ASN A CB  1 
ATOM   2274  C CG  . ASN A  1 286 ? 43.490  24.537 46.406  1.00 56.92  ? 286  ASN A CG  1 
ATOM   2275  O OD1 . ASN A  1 286 ? 44.278  25.450 46.148  1.00 56.43  ? 286  ASN A OD1 1 
ATOM   2276  N ND2 . ASN A  1 286 ? 43.630  23.307 45.912  1.00 60.14  ? 286  ASN A ND2 1 
ATOM   2277  N N   . SER A  1 287 ? 41.566  27.821 45.439  1.00 46.88  ? 287  SER A N   1 
ATOM   2278  C CA  . SER A  1 287 ? 41.271  28.247 44.079  1.00 45.50  ? 287  SER A CA  1 
ATOM   2279  C C   . SER A  1 287 ? 42.041  29.494 43.670  1.00 44.71  ? 287  SER A C   1 
ATOM   2280  O O   . SER A  1 287 ? 42.529  30.251 44.507  1.00 44.67  ? 287  SER A O   1 
ATOM   2281  C CB  . SER A  1 287 ? 39.766  28.484 43.904  1.00 43.08  ? 287  SER A CB  1 
ATOM   2282  O OG  . SER A  1 287 ? 39.377  29.759 44.380  1.00 40.84  ? 287  SER A OG  1 
ATOM   2283  N N   . SER A  1 288 ? 42.128  29.690 42.360  1.00 44.36  ? 288  SER A N   1 
ATOM   2284  C CA  . SER A  1 288 ? 42.783  30.852 41.773  1.00 43.91  ? 288  SER A CA  1 
ATOM   2285  C C   . SER A  1 288 ? 41.764  31.916 41.352  1.00 40.89  ? 288  SER A C   1 
ATOM   2286  O O   . SER A  1 288 ? 42.133  32.948 40.794  1.00 40.52  ? 288  SER A O   1 
ATOM   2287  C CB  . SER A  1 288 ? 43.630  30.407 40.574  1.00 45.94  ? 288  SER A CB  1 
ATOM   2288  O OG  . SER A  1 288 ? 43.043  29.287 39.924  1.00 46.34  ? 288  SER A OG  1 
ATOM   2289  N N   . MET A  1 289 ? 40.487  31.674 41.643  1.00 39.17  ? 289  MET A N   1 
ATOM   2290  C CA  . MET A  1 289 ? 39.423  32.609 41.285  1.00 36.82  ? 289  MET A CA  1 
ATOM   2291  C C   . MET A  1 289 ? 39.604  33.926 42.036  1.00 36.21  ? 289  MET A C   1 
ATOM   2292  O O   . MET A  1 289 ? 40.122  33.934 43.149  1.00 37.12  ? 289  MET A O   1 
ATOM   2293  C CB  . MET A  1 289 ? 38.050  32.043 41.651  1.00 35.96  ? 289  MET A CB  1 
ATOM   2294  C CG  . MET A  1 289 ? 37.688  30.721 41.001  1.00 36.97  ? 289  MET A CG  1 
ATOM   2295  S SD  . MET A  1 289 ? 37.468  30.859 39.224  1.00 36.37  ? 289  MET A SD  1 
ATOM   2296  C CE  . MET A  1 289 ? 36.226  29.584 38.984  1.00 37.22  ? 289  MET A CE  1 
ATOM   2297  N N   . PRO A  1 290 ? 39.176  35.046 41.430  1.00 34.98  ? 290  PRO A N   1 
ATOM   2298  C CA  . PRO A  1 290 ? 39.195  36.322 42.147  1.00 34.84  ? 290  PRO A CA  1 
ATOM   2299  C C   . PRO A  1 290 ? 38.089  36.444 43.197  1.00 33.94  ? 290  PRO A C   1 
ATOM   2300  O O   . PRO A  1 290 ? 38.199  37.272 44.098  1.00 34.35  ? 290  PRO A O   1 
ATOM   2301  C CB  . PRO A  1 290 ? 38.978  37.346 41.034  1.00 34.28  ? 290  PRO A CB  1 
ATOM   2302  C CG  . PRO A  1 290 ? 38.203  36.604 40.008  1.00 33.21  ? 290  PRO A CG  1 
ATOM   2303  C CD  . PRO A  1 290 ? 38.755  35.213 40.028  1.00 34.10  ? 290  PRO A CD  1 
ATOM   2304  N N   . PHE A  1 291 ? 37.039  35.633 43.066  1.00 33.11  ? 291  PHE A N   1 
ATOM   2305  C CA  . PHE A  1 291 ? 35.866  35.703 43.934  1.00 32.61  ? 291  PHE A CA  1 
ATOM   2306  C C   . PHE A  1 291 ? 35.471  34.345 44.478  1.00 32.96  ? 291  PHE A C   1 
ATOM   2307  O O   . PHE A  1 291 ? 35.833  33.314 43.918  1.00 33.54  ? 291  PHE A O   1 
ATOM   2308  C CB  . PHE A  1 291 ? 34.658  36.210 43.153  1.00 31.88  ? 291  PHE A CB  1 
ATOM   2309  C CG  . PHE A  1 291 ? 34.719  37.657 42.792  1.00 31.86  ? 291  PHE A CG  1 
ATOM   2310  C CD1 . PHE A  1 291 ? 34.499  38.625 43.756  1.00 32.44  ? 291  PHE A CD1 1 
ATOM   2311  C CD2 . PHE A  1 291 ? 34.958  38.051 41.484  1.00 31.61  ? 291  PHE A CD2 1 
ATOM   2312  C CE1 . PHE A  1 291 ? 34.533  39.965 43.432  1.00 33.02  ? 291  PHE A CE1 1 
ATOM   2313  C CE2 . PHE A  1 291 ? 34.993  39.393 41.151  1.00 32.01  ? 291  PHE A CE2 1 
ATOM   2314  C CZ  . PHE A  1 291 ? 34.781  40.348 42.129  1.00 32.86  ? 291  PHE A CZ  1 
ATOM   2315  N N   . HIS A  1 292 ? 34.689  34.366 45.553  1.00 32.93  ? 292  HIS A N   1 
ATOM   2316  C CA  . HIS A  1 292 ? 34.018  33.176 46.062  1.00 33.56  ? 292  HIS A CA  1 
ATOM   2317  C C   . HIS A  1 292 ? 32.704  33.581 46.727  1.00 33.51  ? 292  HIS A C   1 
ATOM   2318  O O   . HIS A  1 292 ? 32.462  34.766 46.943  1.00 33.07  ? 292  HIS A O   1 
ATOM   2319  C CB  . HIS A  1 292 ? 34.917  32.442 47.060  1.00 34.59  ? 292  HIS A CB  1 
ATOM   2320  C CG  . HIS A  1 292 ? 35.041  33.133 48.380  1.00 34.56  ? 292  HIS A CG  1 
ATOM   2321  N ND1 . HIS A  1 292 ? 34.367  32.712 49.503  1.00 35.10  ? 292  HIS A ND1 1 
ATOM   2322  C CD2 . HIS A  1 292 ? 35.741  34.228 48.750  1.00 34.37  ? 292  HIS A CD2 1 
ATOM   2323  C CE1 . HIS A  1 292 ? 34.655  33.511 50.513  1.00 35.06  ? 292  HIS A CE1 1 
ATOM   2324  N NE2 . HIS A  1 292 ? 35.489  34.440 50.083  1.00 34.71  ? 292  HIS A NE2 1 
ATOM   2325  N N   . ASN A  1 293 ? 31.862  32.602 47.050  1.00 34.45  ? 293  ASN A N   1 
ATOM   2326  C CA  . ASN A  1 293 ? 30.570  32.868 47.693  1.00 35.04  ? 293  ASN A CA  1 
ATOM   2327  C C   . ASN A  1 293 ? 30.270  31.931 48.869  1.00 36.44  ? 293  ASN A C   1 
ATOM   2328  O O   . ASN A  1 293 ? 29.110  31.685 49.202  1.00 37.74  ? 293  ASN A O   1 
ATOM   2329  C CB  . ASN A  1 293 ? 29.448  32.779 46.656  1.00 35.45  ? 293  ASN A CB  1 
ATOM   2330  C CG  . ASN A  1 293 ? 29.234  31.368 46.144  1.00 36.71  ? 293  ASN A CG  1 
ATOM   2331  O OD1 . ASN A  1 293 ? 30.119  30.519 46.238  1.00 37.06  ? 293  ASN A OD1 1 
ATOM   2332  N ND2 . ASN A  1 293 ? 28.055  31.112 45.600  1.00 37.91  ? 293  ASN A ND2 1 
ATOM   2333  N N   . ILE A  1 294 ? 31.324  31.427 49.500  1.00 36.57  ? 294  ILE A N   1 
ATOM   2334  C CA  . ILE A  1 294 ? 31.203  30.437 50.570  1.00 38.09  ? 294  ILE A CA  1 
ATOM   2335  C C   . ILE A  1 294 ? 30.745  31.074 51.883  1.00 38.18  ? 294  ILE A C   1 
ATOM   2336  O O   . ILE A  1 294 ? 29.708  30.697 52.434  1.00 39.55  ? 294  ILE A O   1 
ATOM   2337  C CB  . ILE A  1 294 ? 32.542  29.691 50.802  1.00 38.58  ? 294  ILE A CB  1 
ATOM   2338  C CG1 . ILE A  1 294 ? 33.060  29.061 49.499  1.00 38.89  ? 294  ILE A CG1 1 
ATOM   2339  C CG2 . ILE A  1 294 ? 32.387  28.620 51.873  1.00 40.50  ? 294  ILE A CG2 1 
ATOM   2340  C CD1 . ILE A  1 294 ? 32.028  28.266 48.727  1.00 40.08  ? 294  ILE A CD1 1 
ATOM   2341  N N   . HIS A  1 295 ? 31.526  32.030 52.379  1.00 37.13  ? 295  HIS A N   1 
ATOM   2342  C CA  . HIS A  1 295 ? 31.268  32.649 53.676  1.00 37.40  ? 295  HIS A CA  1 
ATOM   2343  C C   . HIS A  1 295 ? 32.057  33.966 53.801  1.00 36.43  ? 295  HIS A C   1 
ATOM   2344  O O   . HIS A  1 295 ? 33.223  34.011 53.414  1.00 35.96  ? 295  HIS A O   1 
ATOM   2345  C CB  . HIS A  1 295 ? 31.675  31.673 54.788  1.00 38.49  ? 295  HIS A CB  1 
ATOM   2346  C CG  . HIS A  1 295 ? 31.037  31.955 56.110  1.00 39.25  ? 295  HIS A CG  1 
ATOM   2347  N ND1 . HIS A  1 295 ? 31.457  32.976 56.931  1.00 38.82  ? 295  HIS A ND1 1 
ATOM   2348  C CD2 . HIS A  1 295 ? 30.020  31.342 56.762  1.00 40.76  ? 295  HIS A CD2 1 
ATOM   2349  C CE1 . HIS A  1 295 ? 30.718  32.993 58.027  1.00 39.84  ? 295  HIS A CE1 1 
ATOM   2350  N NE2 . HIS A  1 295 ? 29.841  32.009 57.951  1.00 41.02  ? 295  HIS A NE2 1 
ATOM   2351  N N   . PRO A  1 296 ? 31.432  35.036 54.341  1.00 36.64  ? 296  PRO A N   1 
ATOM   2352  C CA  . PRO A  1 296 ? 32.110  36.343 54.450  1.00 36.38  ? 296  PRO A CA  1 
ATOM   2353  C C   . PRO A  1 296 ? 33.362  36.352 55.333  1.00 36.64  ? 296  PRO A C   1 
ATOM   2354  O O   . PRO A  1 296 ? 34.385  36.915 54.953  1.00 36.53  ? 296  PRO A O   1 
ATOM   2355  C CB  . PRO A  1 296 ? 31.034  37.257 55.057  1.00 37.33  ? 296  PRO A CB  1 
ATOM   2356  C CG  . PRO A  1 296 ? 30.029  36.343 55.662  1.00 38.15  ? 296  PRO A CG  1 
ATOM   2357  C CD  . PRO A  1 296 ? 30.036  35.110 54.811  1.00 37.69  ? 296  PRO A CD  1 
ATOM   2358  N N   . LEU A  1 297 ? 33.268  35.742 56.507  1.00 37.30  ? 297  LEU A N   1 
ATOM   2359  C CA  . LEU A  1 297 ? 34.372  35.719 57.469  1.00 37.86  ? 297  LEU A CA  1 
ATOM   2360  C C   . LEU A  1 297 ? 35.425  34.674 57.105  1.00 37.94  ? 297  LEU A C   1 
ATOM   2361  O O   . LEU A  1 297 ? 35.243  33.483 57.355  1.00 38.37  ? 297  LEU A O   1 
ATOM   2362  C CB  . LEU A  1 297 ? 33.840  35.453 58.882  1.00 38.68  ? 297  LEU A CB  1 
ATOM   2363  C CG  . LEU A  1 297 ? 32.730  36.390 59.373  1.00 39.24  ? 297  LEU A CG  1 
ATOM   2364  C CD1 . LEU A  1 297 ? 32.077  35.841 60.634  1.00 40.17  ? 297  LEU A CD1 1 
ATOM   2365  C CD2 . LEU A  1 297 ? 33.267  37.795 59.608  1.00 39.78  ? 297  LEU A CD2 1 
ATOM   2366  N N   . THR A  1 298 ? 36.526  35.127 56.513  1.00 38.01  ? 298  THR A N   1 
ATOM   2367  C CA  . THR A  1 298 ? 37.635  34.239 56.168  1.00 38.67  ? 298  THR A CA  1 
ATOM   2368  C C   . THR A  1 298 ? 38.939  34.729 56.787  1.00 40.00  ? 298  THR A C   1 
ATOM   2369  O O   . THR A  1 298 ? 39.034  35.863 57.258  1.00 40.28  ? 298  THR A O   1 
ATOM   2370  C CB  . THR A  1 298 ? 37.811  34.097 54.637  1.00 38.09  ? 298  THR A CB  1 
ATOM   2371  O OG1 . THR A  1 298 ? 38.408  35.280 54.091  1.00 38.08  ? 298  THR A OG1 1 
ATOM   2372  C CG2 . THR A  1 298 ? 36.474  33.850 53.964  1.00 37.00  ? 298  THR A CG2 1 
ATOM   2373  N N   . ILE A  1 299 ? 39.931  33.848 56.786  1.00 41.29  ? 299  ILE A N   1 
ATOM   2374  C CA  . ILE A  1 299 ? 41.263  34.158 57.292  1.00 43.20  ? 299  ILE A CA  1 
ATOM   2375  C C   . ILE A  1 299 ? 42.266  33.636 56.266  1.00 44.43  ? 299  ILE A C   1 
ATOM   2376  O O   . ILE A  1 299 ? 42.087  32.547 55.711  1.00 44.40  ? 299  ILE A O   1 
ATOM   2377  C CB  . ILE A  1 299 ? 41.496  33.550 58.710  1.00 44.41  ? 299  ILE A CB  1 
ATOM   2378  C CG1 . ILE A  1 299 ? 42.955  33.711 59.186  1.00 46.88  ? 299  ILE A CG1 1 
ATOM   2379  C CG2 . ILE A  1 299 ? 41.091  32.082 58.761  1.00 44.57  ? 299  ILE A CG2 1 
ATOM   2380  C CD1 . ILE A  1 299 ? 43.227  34.994 59.943  1.00 47.57  ? 299  ILE A CD1 1 
ATOM   2381  N N   . GLY A  1 300 ? 43.299  34.433 56.003  1.00 45.92  ? 300  GLY A N   1 
ATOM   2382  C CA  . GLY A  1 300 ? 44.373  34.045 55.095  1.00 47.74  ? 300  GLY A CA  1 
ATOM   2383  C C   . GLY A  1 300 ? 44.285  34.743 53.755  1.00 46.93  ? 300  GLY A C   1 
ATOM   2384  O O   . GLY A  1 300 ? 43.571  35.738 53.605  1.00 45.42  ? 300  GLY A O   1 
ATOM   2385  N N   . GLU A  1 301 ? 45.017  34.212 52.779  1.00 48.28  ? 301  GLU A N   1 
ATOM   2386  C CA  . GLU A  1 301 ? 45.037  34.761 51.426  1.00 47.76  ? 301  GLU A CA  1 
ATOM   2387  C C   . GLU A  1 301 ? 43.836  34.221 50.660  1.00 45.16  ? 301  GLU A C   1 
ATOM   2388  O O   . GLU A  1 301 ? 43.861  33.098 50.157  1.00 45.54  ? 301  GLU A O   1 
ATOM   2389  C CB  . GLU A  1 301 ? 46.342  34.386 50.720  1.00 50.66  ? 301  GLU A CB  1 
ATOM   2390  C CG  . GLU A  1 301 ? 46.582  35.113 49.403  1.00 50.71  ? 301  GLU A CG  1 
ATOM   2391  C CD  . GLU A  1 301 ? 46.959  36.581 49.578  1.00 51.75  ? 301  GLU A CD  1 
ATOM   2392  O OE1 . GLU A  1 301 ? 47.075  37.055 50.734  1.00 52.58  ? 301  GLU A OE1 1 
ATOM   2393  O OE2 . GLU A  1 301 ? 47.147  37.264 48.545  1.00 52.06  ? 301  GLU A OE2 1 
ATOM   2394  N N   . CYS A  1 302 ? 42.785  35.032 50.580  1.00 42.99  ? 302  CYS A N   1 
ATOM   2395  C CA  . CYS A  1 302 ? 41.506  34.587 50.044  1.00 40.81  ? 302  CYS A CA  1 
ATOM   2396  C C   . CYS A  1 302 ? 41.019  35.448 48.884  1.00 39.42  ? 302  CYS A C   1 
ATOM   2397  O O   . CYS A  1 302 ? 41.371  36.626 48.787  1.00 39.86  ? 302  CYS A O   1 
ATOM   2398  C CB  . CYS A  1 302 ? 40.450  34.615 51.149  1.00 39.79  ? 302  CYS A CB  1 
ATOM   2399  S SG  . CYS A  1 302 ? 40.766  33.459 52.496  1.00 41.25  ? 302  CYS A SG  1 
ATOM   2400  N N   . PRO A  1 303 ? 40.190  34.859 48.004  1.00 38.03  ? 303  PRO A N   1 
ATOM   2401  C CA  . PRO A  1 303 ? 39.454  35.673 47.042  1.00 36.61  ? 303  PRO A CA  1 
ATOM   2402  C C   . PRO A  1 303 ? 38.382  36.493 47.763  1.00 35.67  ? 303  PRO A C   1 
ATOM   2403  O O   . PRO A  1 303 ? 38.109  36.244 48.940  1.00 35.89  ? 303  PRO A O   1 
ATOM   2404  C CB  . PRO A  1 303 ? 38.827  34.642 46.098  1.00 35.86  ? 303  PRO A CB  1 
ATOM   2405  C CG  . PRO A  1 303 ? 38.813  33.358 46.847  1.00 36.70  ? 303  PRO A CG  1 
ATOM   2406  C CD  . PRO A  1 303 ? 39.926  33.417 47.846  1.00 38.24  ? 303  PRO A CD  1 
ATOM   2407  N N   . LYS A  1 304 ? 37.785  37.459 47.074  1.00 34.92  ? 304  LYS A N   1 
ATOM   2408  C CA  . LYS A  1 304 ? 36.804  38.340 47.703  1.00 34.66  ? 304  LYS A CA  1 
ATOM   2409  C C   . LYS A  1 304 ? 35.440  37.672 47.756  1.00 33.61  ? 304  LYS A C   1 
ATOM   2410  O O   . LYS A  1 304 ? 35.033  36.990 46.814  1.00 32.98  ? 304  LYS A O   1 
ATOM   2411  C CB  . LYS A  1 304 ? 36.711  39.669 46.953  1.00 35.03  ? 304  LYS A CB  1 
ATOM   2412  C CG  . LYS A  1 304 ? 38.037  40.414 46.855  1.00 36.62  ? 304  LYS A CG  1 
ATOM   2413  C CD  . LYS A  1 304 ? 38.466  41.009 48.194  1.00 38.20  ? 304  LYS A CD  1 
ATOM   2414  C CE  . LYS A  1 304 ? 39.958  40.829 48.454  1.00 39.89  ? 304  LYS A CE  1 
ATOM   2415  N NZ  . LYS A  1 304 ? 40.526  41.950 49.259  1.00 42.21  ? 304  LYS A NZ  1 
ATOM   2416  N N   . TYR A  1 305 ? 34.736  37.867 48.864  1.00 33.76  ? 305  TYR A N   1 
ATOM   2417  C CA  . TYR A  1 305 ? 33.426  37.265 49.038  1.00 33.42  ? 305  TYR A CA  1 
ATOM   2418  C C   . TYR A  1 305 ? 32.347  38.115 48.380  1.00 33.35  ? 305  TYR A C   1 
ATOM   2419  O O   . TYR A  1 305 ? 32.322  39.340 48.539  1.00 33.97  ? 305  TYR A O   1 
ATOM   2420  C CB  . TYR A  1 305 ? 33.096  37.076 50.519  1.00 34.08  ? 305  TYR A CB  1 
ATOM   2421  C CG  . TYR A  1 305 ? 31.691  36.568 50.740  1.00 34.41  ? 305  TYR A CG  1 
ATOM   2422  C CD1 . TYR A  1 305 ? 31.376  35.230 50.536  1.00 34.52  ? 305  TYR A CD1 1 
ATOM   2423  C CD2 . TYR A  1 305 ? 30.673  37.429 51.127  1.00 35.18  ? 305  TYR A CD2 1 
ATOM   2424  C CE1 . TYR A  1 305 ? 30.088  34.762 50.728  1.00 35.44  ? 305  TYR A CE1 1 
ATOM   2425  C CE2 . TYR A  1 305 ? 29.381  36.971 51.320  1.00 36.07  ? 305  TYR A CE2 1 
ATOM   2426  C CZ  . TYR A  1 305 ? 29.094  35.637 51.119  1.00 36.20  ? 305  TYR A CZ  1 
ATOM   2427  O OH  . TYR A  1 305 ? 27.818  35.170 51.311  1.00 37.64  ? 305  TYR A OH  1 
ATOM   2428  N N   . VAL A  1 306 ? 31.459  37.453 47.642  1.00 32.99  ? 306  VAL A N   1 
ATOM   2429  C CA  . VAL A  1 306 ? 30.259  38.088 47.105  1.00 33.40  ? 306  VAL A CA  1 
ATOM   2430  C C   . VAL A  1 306 ? 29.071  37.158 47.315  1.00 34.10  ? 306  VAL A C   1 
ATOM   2431  O O   . VAL A  1 306 ? 29.243  35.956 47.472  1.00 34.06  ? 306  VAL A O   1 
ATOM   2432  C CB  . VAL A  1 306 ? 30.400  38.442 45.604  1.00 32.73  ? 306  VAL A CB  1 
ATOM   2433  C CG1 . VAL A  1 306 ? 31.305  39.651 45.422  1.00 32.76  ? 306  VAL A CG1 1 
ATOM   2434  C CG2 . VAL A  1 306 ? 30.923  37.257 44.802  1.00 31.89  ? 306  VAL A CG2 1 
ATOM   2435  N N   . LYS A  1 307 ? 27.870  37.726 47.315  1.00 35.27  ? 307  LYS A N   1 
ATOM   2436  C CA  . LYS A  1 307 ? 26.638  36.955 47.484  1.00 36.67  ? 307  LYS A CA  1 
ATOM   2437  C C   . LYS A  1 307 ? 26.106  36.332 46.184  1.00 36.74  ? 307  LYS A C   1 
ATOM   2438  O O   . LYS A  1 307 ? 25.014  35.768 46.176  1.00 38.47  ? 307  LYS A O   1 
ATOM   2439  C CB  . LYS A  1 307 ? 25.541  37.841 48.086  1.00 38.64  ? 307  LYS A CB  1 
ATOM   2440  C CG  . LYS A  1 307 ? 25.723  38.181 49.553  1.00 39.26  ? 307  LYS A CG  1 
ATOM   2441  C CD  . LYS A  1 307 ? 24.443  38.786 50.105  1.00 41.87  ? 307  LYS A CD  1 
ATOM   2442  C CE  . LYS A  1 307 ? 24.673  39.508 51.422  1.00 42.67  ? 307  LYS A CE  1 
ATOM   2443  N NZ  . LYS A  1 307 ? 23.412  40.102 51.960  1.00 45.70  ? 307  LYS A NZ  1 
ATOM   2444  N N   . SER A  1 308 ? 26.859  36.428 45.091  1.00 35.22  ? 308  SER A N   1 
ATOM   2445  C CA  . SER A  1 308 ? 26.393  35.926 43.799  1.00 35.31  ? 308  SER A CA  1 
ATOM   2446  C C   . SER A  1 308 ? 26.375  34.402 43.762  1.00 35.88  ? 308  SER A C   1 
ATOM   2447  O O   . SER A  1 308 ? 27.174  33.742 44.432  1.00 35.50  ? 308  SER A O   1 
ATOM   2448  C CB  . SER A  1 308 ? 27.282  36.440 42.662  1.00 33.67  ? 308  SER A CB  1 
ATOM   2449  O OG  . SER A  1 308 ? 27.675  37.781 42.879  1.00 33.31  ? 308  SER A OG  1 
ATOM   2450  N N   . ASN A  1 309 ? 25.447  33.857 42.980  1.00 37.20  ? 309  ASN A N   1 
ATOM   2451  C CA  . ASN A  1 309 ? 25.445  32.438 42.640  1.00 38.20  ? 309  ASN A CA  1 
ATOM   2452  C C   . ASN A  1 309 ? 26.273  32.171 41.391  1.00 36.86  ? 309  ASN A C   1 
ATOM   2453  O O   . ASN A  1 309 ? 26.720  31.043 41.172  1.00 37.49  ? 309  ASN A O   1 
ATOM   2454  C CB  . ASN A  1 309 ? 24.016  31.938 42.413  1.00 40.98  ? 309  ASN A CB  1 
ATOM   2455  C CG  . ASN A  1 309 ? 23.235  31.790 43.708  1.00 43.05  ? 309  ASN A CG  1 
ATOM   2456  O OD1 . ASN A  1 309 ? 23.731  31.222 44.687  1.00 43.08  ? 309  ASN A OD1 1 
ATOM   2457  N ND2 . ASN A  1 309 ? 21.999  32.290 43.720  1.00 45.10  ? 309  ASN A ND2 1 
ATOM   2458  N N   . ARG A  1 310 ? 26.477  33.204 40.575  1.00 35.37  ? 310  ARG A N   1 
ATOM   2459  C CA  . ARG A  1 310 ? 27.105  33.035 39.267  1.00 34.34  ? 310  ARG A CA  1 
ATOM   2460  C C   . ARG A  1 310 ? 27.796  34.314 38.775  1.00 32.44  ? 310  ARG A C   1 
ATOM   2461  O O   . ARG A  1 310 ? 27.166  35.369 38.689  1.00 32.51  ? 310  ARG A O   1 
ATOM   2462  C CB  . ARG A  1 310 ? 26.039  32.602 38.256  1.00 35.85  ? 310  ARG A CB  1 
ATOM   2463  C CG  . ARG A  1 310 ? 26.586  32.029 36.960  1.00 35.47  ? 310  ARG A CG  1 
ATOM   2464  C CD  . ARG A  1 310 ? 25.470  31.699 35.982  1.00 37.18  ? 310  ARG A CD  1 
ATOM   2465  N NE  . ARG A  1 310 ? 25.940  31.788 34.598  1.00 36.20  ? 310  ARG A NE  1 
ATOM   2466  C CZ  . ARG A  1 310 ? 26.552  30.811 33.927  1.00 36.61  ? 310  ARG A CZ  1 
ATOM   2467  N NH1 . ARG A  1 310 ? 26.784  29.623 34.486  1.00 38.21  ? 310  ARG A NH1 1 
ATOM   2468  N NH2 . ARG A  1 310 ? 26.935  31.022 32.673  1.00 35.73  ? 310  ARG A NH2 1 
ATOM   2469  N N   . LEU A  1 311 ? 29.090  34.208 38.466  1.00 31.20  ? 311  LEU A N   1 
ATOM   2470  C CA  . LEU A  1 311 ? 29.836  35.286 37.805  1.00 29.88  ? 311  LEU A CA  1 
ATOM   2471  C C   . LEU A  1 311 ? 30.676  34.728 36.655  1.00 29.41  ? 311  LEU A C   1 
ATOM   2472  O O   . LEU A  1 311 ? 31.733  34.140 36.879  1.00 29.47  ? 311  LEU A O   1 
ATOM   2473  C CB  . LEU A  1 311 ? 30.746  36.020 38.792  1.00 29.40  ? 311  LEU A CB  1 
ATOM   2474  C CG  . LEU A  1 311 ? 30.099  36.856 39.901  1.00 29.90  ? 311  LEU A CG  1 
ATOM   2475  C CD1 . LEU A  1 311 ? 31.181  37.389 40.824  1.00 29.68  ? 311  LEU A CD1 1 
ATOM   2476  C CD2 . LEU A  1 311 ? 29.272  37.999 39.338  1.00 30.25  ? 311  LEU A CD2 1 
ATOM   2477  N N   . VAL A  1 312 ? 30.199  34.917 35.428  1.00 29.23  ? 312  VAL A N   1 
ATOM   2478  C CA  . VAL A  1 312 ? 30.880  34.419 34.241  1.00 28.97  ? 312  VAL A CA  1 
ATOM   2479  C C   . VAL A  1 312 ? 31.123  35.559 33.261  1.00 28.04  ? 312  VAL A C   1 
ATOM   2480  O O   . VAL A  1 312 ? 30.189  36.258 32.870  1.00 28.06  ? 312  VAL A O   1 
ATOM   2481  C CB  . VAL A  1 312 ? 30.053  33.323 33.540  1.00 30.11  ? 312  VAL A CB  1 
ATOM   2482  C CG1 . VAL A  1 312 ? 30.824  32.734 32.364  1.00 30.18  ? 312  VAL A CG1 1 
ATOM   2483  C CG2 . VAL A  1 312 ? 29.676  32.230 34.531  1.00 31.57  ? 312  VAL A CG2 1 
ATOM   2484  N N   . LEU A  1 313 ? 32.384  35.735 32.872  1.00 27.62  ? 313  LEU A N   1 
ATOM   2485  C CA  . LEU A  1 313 ? 32.775  36.746 31.894  1.00 27.10  ? 313  LEU A CA  1 
ATOM   2486  C C   . LEU A  1 313 ? 32.873  36.142 30.504  1.00 27.12  ? 313  LEU A C   1 
ATOM   2487  O O   . LEU A  1 313 ? 33.495  35.096 30.326  1.00 27.67  ? 313  LEU A O   1 
ATOM   2488  C CB  . LEU A  1 313 ? 34.136  37.342 32.248  1.00 27.23  ? 313  LEU A CB  1 
ATOM   2489  C CG  . LEU A  1 313 ? 34.148  38.404 33.338  1.00 27.43  ? 313  LEU A CG  1 
ATOM   2490  C CD1 . LEU A  1 313 ? 35.570  38.665 33.808  1.00 28.13  ? 313  LEU A CD1 1 
ATOM   2491  C CD2 . LEU A  1 313 ? 33.498  39.686 32.838  1.00 27.49  ? 313  LEU A CD2 1 
ATOM   2492  N N   . ALA A  1 314 ? 32.275  36.811 29.521  1.00 26.80  ? 314  ALA A N   1 
ATOM   2493  C CA  . ALA A  1 314 ? 32.468  36.441 28.124  1.00 26.80  ? 314  ALA A CA  1 
ATOM   2494  C C   . ALA A  1 314 ? 33.890  36.793 27.729  1.00 26.84  ? 314  ALA A C   1 
ATOM   2495  O O   . ALA A  1 314 ? 34.345  37.907 27.978  1.00 26.80  ? 314  ALA A O   1 
ATOM   2496  C CB  . ALA A  1 314 ? 31.485  37.175 27.225  1.00 26.60  ? 314  ALA A CB  1 
ATOM   2497  N N   . THR A  1 315 ? 34.593  35.825 27.155  1.00 27.46  ? 315  THR A N   1 
ATOM   2498  C CA  . THR A  1 315 ? 35.879  36.071 26.513  1.00 28.02  ? 315  THR A CA  1 
ATOM   2499  C C   . THR A  1 315 ? 35.713  35.978 25.004  1.00 27.98  ? 315  THR A C   1 
ATOM   2500  O O   . THR A  1 315 ? 36.198  36.827 24.269  1.00 27.95  ? 315  THR A O   1 
ATOM   2501  C CB  . THR A  1 315 ? 36.963  35.076 26.975  1.00 29.37  ? 315  THR A CB  1 
ATOM   2502  O OG1 . THR A  1 315 ? 36.433  33.745 26.992  1.00 29.98  ? 315  THR A OG1 1 
ATOM   2503  C CG2 . THR A  1 315 ? 37.457  35.436 28.366  1.00 29.61  ? 315  THR A CG2 1 
ATOM   2504  N N   . GLY A  1 316 ? 35.016  34.945 24.552  1.00 28.28  ? 316  GLY A N   1 
ATOM   2505  C CA  . GLY A  1 316 ? 34.767  34.744 23.141  1.00 28.43  ? 316  GLY A CA  1 
ATOM   2506  C C   . GLY A  1 316 ? 33.560  35.515 22.660  1.00 27.54  ? 316  GLY A C   1 
ATOM   2507  O O   . GLY A  1 316 ? 33.053  36.406 23.343  1.00 26.93  ? 316  GLY A O   1 
ATOM   2508  N N   . LEU A  1 317 ? 33.093  35.152 21.475  1.00 27.85  ? 317  LEU A N   1 
ATOM   2509  C CA  . LEU A  1 317 ? 32.002  35.859 20.821  1.00 27.43  ? 317  LEU A CA  1 
ATOM   2510  C C   . LEU A  1 317 ? 30.742  35.007 20.819  1.00 28.35  ? 317  LEU A C   1 
ATOM   2511  O O   . LEU A  1 317 ? 30.767  33.845 21.217  1.00 29.36  ? 317  LEU A O   1 
ATOM   2512  C CB  . LEU A  1 317 ? 32.407  36.274 19.398  1.00 27.27  ? 317  LEU A CB  1 
ATOM   2513  C CG  . LEU A  1 317 ? 33.033  35.234 18.462  1.00 28.12  ? 317  LEU A CG  1 
ATOM   2514  C CD1 . LEU A  1 317 ? 31.957  34.388 17.811  1.00 28.89  ? 317  LEU A CD1 1 
ATOM   2515  C CD2 . LEU A  1 317 ? 33.899  35.902 17.407  1.00 28.00  ? 317  LEU A CD2 1 
ATOM   2516  N N   . ARG A  1 318 ? 29.640  35.605 20.384  1.00 28.51  ? 318  ARG A N   1 
ATOM   2517  C CA  . ARG A  1 318 ? 28.352  34.930 20.346  1.00 29.96  ? 318  ARG A CA  1 
ATOM   2518  C C   . ARG A  1 318 ? 28.429  33.700 19.454  1.00 31.32  ? 318  ARG A C   1 
ATOM   2519  O O   . ARG A  1 318 ? 28.763  33.799 18.274  1.00 31.14  ? 318  ARG A O   1 
ATOM   2520  C CB  . ARG A  1 318 ? 27.278  35.887 19.838  1.00 30.15  ? 318  ARG A CB  1 
ATOM   2521  C CG  . ARG A  1 318 ? 25.886  35.288 19.724  1.00 32.08  ? 318  ARG A CG  1 
ATOM   2522  C CD  . ARG A  1 318 ? 24.918  36.298 19.126  1.00 32.64  ? 318  ARG A CD  1 
ATOM   2523  N NE  . ARG A  1 318 ? 24.554  37.347 20.080  1.00 32.62  ? 318  ARG A NE  1 
ATOM   2524  C CZ  . ARG A  1 318 ? 23.455  37.347 20.832  1.00 34.36  ? 318  ARG A CZ  1 
ATOM   2525  N NH1 . ARG A  1 318 ? 22.577  36.348 20.763  1.00 36.39  ? 318  ARG A NH1 1 
ATOM   2526  N NH2 . ARG A  1 318 ? 23.229  38.357 21.666  1.00 34.50  ? 318  ARG A NH2 1 
ATOM   2527  N N   . ASN A  1 319 ? 28.115  32.546 20.031  1.00 33.11  ? 319  ASN A N   1 
ATOM   2528  C CA  . ASN A  1 319 ? 28.240  31.272 19.344  1.00 35.11  ? 319  ASN A CA  1 
ATOM   2529  C C   . ASN A  1 319 ? 26.963  30.934 18.583  1.00 37.16  ? 319  ASN A C   1 
ATOM   2530  O O   . ASN A  1 319 ? 25.857  31.136 19.082  1.00 38.03  ? 319  ASN A O   1 
ATOM   2531  C CB  . ASN A  1 319 ? 28.570  30.176 20.352  1.00 36.53  ? 319  ASN A CB  1 
ATOM   2532  C CG  . ASN A  1 319 ? 29.002  28.883 19.697  1.00 38.78  ? 319  ASN A CG  1 
ATOM   2533  O OD1 . ASN A  1 319 ? 29.183  28.811 18.485  1.00 39.03  ? 319  ASN A OD1 1 
ATOM   2534  N ND2 . ASN A  1 319 ? 29.175  27.848 20.505  1.00 40.71  ? 319  ASN A ND2 1 
ATOM   2535  N N   . SER A  1 320 ? 27.132  30.409 17.373  1.00 38.39  ? 320  SER A N   1 
ATOM   2536  C CA  . SER A  1 320 ? 26.021  30.180 16.447  1.00 40.41  ? 320  SER A CA  1 
ATOM   2537  C C   . SER A  1 320 ? 25.266  28.870 16.726  1.00 44.11  ? 320  SER A C   1 
ATOM   2538  O O   . SER A  1 320 ? 25.848  27.918 17.244  1.00 45.39  ? 320  SER A O   1 
ATOM   2539  C CB  . SER A  1 320 ? 26.545  30.178 15.007  1.00 40.12  ? 320  SER A CB  1 
ATOM   2540  O OG  . SER A  1 320 ? 27.209  31.400 14.721  1.00 37.38  ? 320  SER A OG  1 
ATOM   2541  N N   . PRO A  1 321 ? 23.959  28.827 16.390  1.00 46.38  ? 321  PRO A N   1 
ATOM   2542  C CA  . PRO A  1 321 ? 23.155  27.607 16.475  1.00 50.52  ? 321  PRO A CA  1 
ATOM   2543  C C   . PRO A  1 321 ? 23.170  26.812 15.170  1.00 52.82  ? 321  PRO A C   1 
ATOM   2544  O O   . PRO A  1 321 ? 24.097  26.040 14.925  1.00 53.52  ? 321  PRO A O   1 
ATOM   2545  C CB  . PRO A  1 321 ? 21.750  28.148 16.739  1.00 51.87  ? 321  PRO A CB  1 
ATOM   2546  C CG  . PRO A  1 321 ? 21.724  29.442 15.994  1.00 49.27  ? 321  PRO A CG  1 
ATOM   2547  C CD  . PRO A  1 321 ? 23.121  30.004 16.080  1.00 45.50  ? 321  PRO A CD  1 
ATOM   2548  N N   . GLY B  2 1   ? 23.563  42.431 17.111  1.00 21.75  ? 1    GLY B N   1 
ATOM   2549  C CA  . GLY B  2 1   ? 24.625  43.243 17.772  1.00 20.54  ? 1    GLY B CA  1 
ATOM   2550  C C   . GLY B  2 1   ? 24.715  44.645 17.208  1.00 20.86  ? 1    GLY B C   1 
ATOM   2551  O O   . GLY B  2 1   ? 24.188  44.930 16.132  1.00 21.81  ? 1    GLY B O   1 
ATOM   2552  N N   . LEU B  2 2   ? 25.407  45.515 17.933  1.00 20.36  ? 2    LEU B N   1 
ATOM   2553  C CA  . LEU B  2 2   ? 25.470  46.931 17.588  1.00 21.15  ? 2    LEU B CA  1 
ATOM   2554  C C   . LEU B  2 2   ? 26.063  47.205 16.210  1.00 21.40  ? 2    LEU B C   1 
ATOM   2555  O O   . LEU B  2 2   ? 25.652  48.147 15.535  1.00 22.71  ? 2    LEU B O   1 
ATOM   2556  C CB  . LEU B  2 2   ? 26.269  47.702 18.640  1.00 20.74  ? 2    LEU B CB  1 
ATOM   2557  C CG  . LEU B  2 2   ? 25.567  48.010 19.957  1.00 20.99  ? 2    LEU B CG  1 
ATOM   2558  C CD1 . LEU B  2 2   ? 26.510  48.770 20.872  1.00 20.71  ? 2    LEU B CD1 1 
ATOM   2559  C CD2 . LEU B  2 2   ? 24.292  48.802 19.734  1.00 22.68  ? 2    LEU B CD2 1 
ATOM   2560  N N   . PHE B  2 3   ? 27.017  46.379 15.793  1.00 20.41  ? 3    PHE B N   1 
ATOM   2561  C CA  . PHE B  2 3   ? 27.763  46.638 14.563  1.00 20.60  ? 3    PHE B CA  1 
ATOM   2562  C C   . PHE B  2 3   ? 27.243  45.867 13.361  1.00 20.89  ? 3    PHE B C   1 
ATOM   2563  O O   . PHE B  2 3   ? 27.712  46.062 12.248  1.00 21.16  ? 3    PHE B O   1 
ATOM   2564  C CB  . PHE B  2 3   ? 29.255  46.441 14.824  1.00 19.78  ? 3    PHE B CB  1 
ATOM   2565  C CG  . PHE B  2 3   ? 29.783  47.427 15.818  1.00 20.03  ? 3    PHE B CG  1 
ATOM   2566  C CD1 . PHE B  2 3   ? 30.182  48.690 15.411  1.00 21.18  ? 3    PHE B CD1 1 
ATOM   2567  C CD2 . PHE B  2 3   ? 29.773  47.135 17.174  1.00 19.42  ? 3    PHE B CD2 1 
ATOM   2568  C CE1 . PHE B  2 3   ? 30.614  49.623 16.331  1.00 21.79  ? 3    PHE B CE1 1 
ATOM   2569  C CE2 . PHE B  2 3   ? 30.199  48.065 18.100  1.00 19.81  ? 3    PHE B CE2 1 
ATOM   2570  C CZ  . PHE B  2 3   ? 30.621  49.311 17.677  1.00 21.04  ? 3    PHE B CZ  1 
ATOM   2571  N N   . GLY B  2 4   ? 26.264  44.999 13.601  1.00 21.08  ? 4    GLY B N   1 
ATOM   2572  C CA  . GLY B  2 4   ? 25.449  44.428 12.541  1.00 21.96  ? 4    GLY B CA  1 
ATOM   2573  C C   . GLY B  2 4   ? 26.072  43.313 11.732  1.00 21.42  ? 4    GLY B C   1 
ATOM   2574  O O   . GLY B  2 4   ? 25.489  42.886 10.743  1.00 22.23  ? 4    GLY B O   1 
ATOM   2575  N N   . ALA B  2 5   ? 27.242  42.831 12.147  1.00 20.39  ? 5    ALA B N   1 
ATOM   2576  C CA  . ALA B  2 5   ? 27.966  41.803 11.399  1.00 20.11  ? 5    ALA B CA  1 
ATOM   2577  C C   . ALA B  2 5   ? 27.659  40.419 11.940  1.00 20.29  ? 5    ALA B C   1 
ATOM   2578  O O   . ALA B  2 5   ? 27.090  39.592 11.239  1.00 21.02  ? 5    ALA B O   1 
ATOM   2579  C CB  . ALA B  2 5   ? 29.460  42.074 11.439  1.00 19.42  ? 5    ALA B CB  1 
ATOM   2580  N N   . ILE B  2 6   ? 28.028  40.182 13.194  1.00 19.92  ? 6    ILE B N   1 
ATOM   2581  C CA  . ILE B  2 6   ? 27.795  38.897 13.855  1.00 20.44  ? 6    ILE B CA  1 
ATOM   2582  C C   . ILE B  2 6   ? 26.300  38.661 14.035  1.00 21.61  ? 6    ILE B C   1 
ATOM   2583  O O   . ILE B  2 6   ? 25.604  39.492 14.613  1.00 21.75  ? 6    ILE B O   1 
ATOM   2584  C CB  . ILE B  2 6   ? 28.505  38.829 15.225  1.00 19.92  ? 6    ILE B CB  1 
ATOM   2585  C CG1 . ILE B  2 6   ? 30.018  38.755 15.017  1.00 19.48  ? 6    ILE B CG1 1 
ATOM   2586  C CG2 . ILE B  2 6   ? 28.023  37.630 16.032  1.00 20.77  ? 6    ILE B CG2 1 
ATOM   2587  C CD1 . ILE B  2 6   ? 30.832  38.816 16.290  1.00 19.24  ? 6    ILE B CD1 1 
ATOM   2588  N N   . ALA B  2 7   ? 25.815  37.527 13.533  1.00 22.84  ? 7    ALA B N   1 
ATOM   2589  C CA  . ALA B  2 7   ? 24.384  37.218 13.516  1.00 24.50  ? 7    ALA B CA  1 
ATOM   2590  C C   . ALA B  2 7   ? 23.593  38.342 12.859  1.00 24.93  ? 7    ALA B C   1 
ATOM   2591  O O   . ALA B  2 7   ? 22.471  38.629 13.251  1.00 26.08  ? 7    ALA B O   1 
ATOM   2592  C CB  . ALA B  2 7   ? 23.877  36.964 14.930  1.00 24.97  ? 7    ALA B CB  1 
ATOM   2593  N N   . GLY B  2 8   ? 24.194  38.974 11.856  1.00 24.30  ? 8    GLY B N   1 
ATOM   2594  C CA  . GLY B  2 8   ? 23.604  40.129 11.194  1.00 24.91  ? 8    GLY B CA  1 
ATOM   2595  C C   . GLY B  2 8   ? 23.601  39.893 9.705   1.00 25.58  ? 8    GLY B C   1 
ATOM   2596  O O   . GLY B  2 8   ? 22.830  39.072 9.218   1.00 27.04  ? 8    GLY B O   1 
ATOM   2597  N N   . PHE B  2 9   ? 24.468  40.595 8.980   1.00 24.82  ? 9    PHE B N   1 
ATOM   2598  C CA  . PHE B  2 9   ? 24.622  40.341 7.553   1.00 25.32  ? 9    PHE B CA  1 
ATOM   2599  C C   . PHE B  2 9   ? 25.509  39.112 7.320   1.00 24.78  ? 9    PHE B C   1 
ATOM   2600  O O   . PHE B  2 9   ? 25.493  38.542 6.234   1.00 25.46  ? 9    PHE B O   1 
ATOM   2601  C CB  . PHE B  2 9   ? 25.101  41.589 6.780   1.00 25.10  ? 9    PHE B CB  1 
ATOM   2602  C CG  . PHE B  2 9   ? 26.557  41.928 6.963   1.00 23.63  ? 9    PHE B CG  1 
ATOM   2603  C CD1 . PHE B  2 9   ? 27.518  41.409 6.105   1.00 23.13  ? 9    PHE B CD1 1 
ATOM   2604  C CD2 . PHE B  2 9   ? 26.959  42.811 7.953   1.00 23.07  ? 9    PHE B CD2 1 
ATOM   2605  C CE1 . PHE B  2 9   ? 28.854  41.738 6.258   1.00 22.24  ? 9    PHE B CE1 1 
ATOM   2606  C CE2 . PHE B  2 9   ? 28.294  43.142 8.112   1.00 22.19  ? 9    PHE B CE2 1 
ATOM   2607  C CZ  . PHE B  2 9   ? 29.242  42.604 7.264   1.00 21.85  ? 9    PHE B CZ  1 
ATOM   2608  N N   . ILE B  2 10  ? 26.260  38.709 8.346   1.00 23.95  ? 10   ILE B N   1 
ATOM   2609  C CA  . ILE B  2 10  ? 26.923  37.404 8.374   1.00 24.03  ? 10   ILE B CA  1 
ATOM   2610  C C   . ILE B  2 10  ? 26.130  36.495 9.312   1.00 25.12  ? 10   ILE B C   1 
ATOM   2611  O O   . ILE B  2 10  ? 26.326  36.513 10.525  1.00 24.67  ? 10   ILE B O   1 
ATOM   2612  C CB  . ILE B  2 10  ? 28.384  37.513 8.841   1.00 22.82  ? 10   ILE B CB  1 
ATOM   2613  C CG1 . ILE B  2 10  ? 29.132  38.554 8.001   1.00 22.16  ? 10   ILE B CG1 1 
ATOM   2614  C CG2 . ILE B  2 10  ? 29.077  36.162 8.738   1.00 23.29  ? 10   ILE B CG2 1 
ATOM   2615  C CD1 . ILE B  2 10  ? 30.492  38.926 8.548   1.00 21.38  ? 10   ILE B CD1 1 
ATOM   2616  N N   . GLU B  2 11  ? 25.232  35.704 8.734   1.00 26.85  ? 11   GLU B N   1 
ATOM   2617  C CA  . GLU B  2 11  ? 24.239  34.944 9.504   1.00 28.54  ? 11   GLU B CA  1 
ATOM   2618  C C   . GLU B  2 11  ? 24.792  34.066 10.620  1.00 28.58  ? 11   GLU B C   1 
ATOM   2619  O O   . GLU B  2 11  ? 24.149  33.912 11.658  1.00 29.32  ? 11   GLU B O   1 
ATOM   2620  C CB  . GLU B  2 11  ? 23.435  34.037 8.578   1.00 30.76  ? 11   GLU B CB  1 
ATOM   2621  C CG  . GLU B  2 11  ? 22.296  34.704 7.833   1.00 31.96  ? 11   GLU B CG  1 
ATOM   2622  C CD  . GLU B  2 11  ? 21.430  33.668 7.134   1.00 34.65  ? 11   GLU B CD  1 
ATOM   2623  O OE1 . GLU B  2 11  ? 21.981  32.898 6.306   1.00 34.91  ? 11   GLU B OE1 1 
ATOM   2624  O OE2 . GLU B  2 11  ? 20.212  33.606 7.430   1.00 36.76  ? 11   GLU B OE2 1 
ATOM   2625  N N   . GLY B  2 12  ? 25.956  33.463 10.391  1.00 28.12  ? 12   GLY B N   1 
ATOM   2626  C CA  . GLY B  2 12  ? 26.515  32.500 11.336  1.00 28.73  ? 12   GLY B CA  1 
ATOM   2627  C C   . GLY B  2 12  ? 28.024  32.377 11.293  1.00 27.79  ? 12   GLY B C   1 
ATOM   2628  O O   . GLY B  2 12  ? 28.675  32.817 10.342  1.00 26.89  ? 12   GLY B O   1 
ATOM   2629  N N   . GLY B  2 13  ? 28.572  31.780 12.346  1.00 28.30  ? 13   GLY B N   1 
ATOM   2630  C CA  . GLY B  2 13  ? 30.006  31.545 12.461  1.00 28.04  ? 13   GLY B CA  1 
ATOM   2631  C C   . GLY B  2 13  ? 30.448  30.296 11.718  1.00 29.83  ? 13   GLY B C   1 
ATOM   2632  O O   . GLY B  2 13  ? 29.634  29.583 11.128  1.00 31.33  ? 13   GLY B O   1 
ATOM   2633  N N   . TRP B  2 14  ? 31.750  30.030 11.766  1.00 30.00  ? 14   TRP B N   1 
ATOM   2634  C CA  . TRP B  2 14  ? 32.349  28.917 11.055  1.00 31.79  ? 14   TRP B CA  1 
ATOM   2635  C C   . TRP B  2 14  ? 32.975  27.915 12.014  1.00 33.83  ? 14   TRP B C   1 
ATOM   2636  O O   . TRP B  2 14  ? 34.030  28.173 12.597  1.00 33.57  ? 14   TRP B O   1 
ATOM   2637  C CB  . TRP B  2 14  ? 33.419  29.429 10.090  1.00 30.80  ? 14   TRP B CB  1 
ATOM   2638  C CG  . TRP B  2 14  ? 32.887  30.242 8.952   1.00 29.35  ? 14   TRP B CG  1 
ATOM   2639  C CD1 . TRP B  2 14  ? 31.642  30.169 8.402   1.00 29.57  ? 14   TRP B CD1 1 
ATOM   2640  C CD2 . TRP B  2 14  ? 33.601  31.224 8.194   1.00 27.90  ? 14   TRP B CD2 1 
ATOM   2641  N NE1 . TRP B  2 14  ? 31.532  31.055 7.362   1.00 28.28  ? 14   TRP B NE1 1 
ATOM   2642  C CE2 . TRP B  2 14  ? 32.721  31.715 7.211   1.00 27.22  ? 14   TRP B CE2 1 
ATOM   2643  C CE3 . TRP B  2 14  ? 34.900  31.738 8.254   1.00 27.45  ? 14   TRP B CE3 1 
ATOM   2644  C CZ2 . TRP B  2 14  ? 33.094  32.696 6.295   1.00 26.05  ? 14   TRP B CZ2 1 
ATOM   2645  C CZ3 . TRP B  2 14  ? 35.268  32.716 7.347   1.00 26.33  ? 14   TRP B CZ3 1 
ATOM   2646  C CH2 . TRP B  2 14  ? 34.368  33.183 6.378   1.00 25.60  ? 14   TRP B CH2 1 
ATOM   2647  N N   . GLN B  2 15  ? 32.325  26.760 12.148  1.00 36.24  ? 15   GLN B N   1 
ATOM   2648  C CA  . GLN B  2 15  ? 32.908  25.602 12.836  1.00 39.02  ? 15   GLN B CA  1 
ATOM   2649  C C   . GLN B  2 15  ? 34.251  25.218 12.206  1.00 39.91  ? 15   GLN B C   1 
ATOM   2650  O O   . GLN B  2 15  ? 35.143  24.719 12.890  1.00 41.61  ? 15   GLN B O   1 
ATOM   2651  C CB  . GLN B  2 15  ? 31.970  24.394 12.753  1.00 41.99  ? 15   GLN B CB  1 
ATOM   2652  C CG  . GLN B  2 15  ? 30.604  24.561 13.410  1.00 42.00  ? 15   GLN B CG  1 
ATOM   2653  C CD  . GLN B  2 15  ? 30.587  24.198 14.886  1.00 43.39  ? 15   GLN B CD  1 
ATOM   2654  O OE1 . GLN B  2 15  ? 30.004  24.915 15.700  1.00 42.00  ? 15   GLN B OE1 1 
ATOM   2655  N NE2 . GLN B  2 15  ? 31.212  23.078 15.239  1.00 46.43  ? 15   GLN B NE2 1 
ATOM   2656  N N   . GLY B  2 16  ? 34.380  25.449 10.898  1.00 38.99  ? 16   GLY B N   1 
ATOM   2657  C CA  . GLY B  2 16  ? 35.585  25.098 10.146  1.00 39.94  ? 16   GLY B CA  1 
ATOM   2658  C C   . GLY B  2 16  ? 36.811  25.976 10.344  1.00 38.55  ? 16   GLY B C   1 
ATOM   2659  O O   . GLY B  2 16  ? 37.893  25.629 9.877   1.00 39.86  ? 16   GLY B O   1 
ATOM   2660  N N   . MET B  2 17  ? 36.659  27.116 11.015  1.00 36.18  ? 17   MET B N   1 
ATOM   2661  C CA  . MET B  2 17  ? 37.800  27.986 11.313  1.00 35.25  ? 17   MET B CA  1 
ATOM   2662  C C   . MET B  2 17  ? 38.198  27.884 12.784  1.00 36.18  ? 17   MET B C   1 
ATOM   2663  O O   . MET B  2 17  ? 37.571  28.497 13.648  1.00 34.75  ? 17   MET B O   1 
ATOM   2664  C CB  . MET B  2 17  ? 37.475  29.434 10.964  1.00 32.30  ? 17   MET B CB  1 
ATOM   2665  C CG  . MET B  2 17  ? 38.678  30.356 11.056  1.00 31.77  ? 17   MET B CG  1 
ATOM   2666  S SD  . MET B  2 17  ? 38.300  32.004 10.457  1.00 28.95  ? 17   MET B SD  1 
ATOM   2667  C CE  . MET B  2 17  ? 36.981  32.438 11.584  1.00 27.58  ? 17   MET B CE  1 
ATOM   2668  N N   . VAL B  2 18  ? 39.255  27.123 13.054  1.00 38.77  ? 18   VAL B N   1 
ATOM   2669  C CA  . VAL B  2 18  ? 39.655  26.794 14.429  1.00 40.41  ? 18   VAL B CA  1 
ATOM   2670  C C   . VAL B  2 18  ? 40.887  27.557 14.935  1.00 40.44  ? 18   VAL B C   1 
ATOM   2671  O O   . VAL B  2 18  ? 41.134  27.605 16.138  1.00 41.18  ? 18   VAL B O   1 
ATOM   2672  C CB  . VAL B  2 18  ? 39.900  25.272 14.584  1.00 44.22  ? 18   VAL B CB  1 
ATOM   2673  C CG1 . VAL B  2 18  ? 38.727  24.484 14.017  1.00 44.72  ? 18   VAL B CG1 1 
ATOM   2674  C CG2 . VAL B  2 18  ? 41.203  24.844 13.922  1.00 46.49  ? 18   VAL B CG2 1 
ATOM   2675  N N   . ASP B  2 19  ? 41.649  28.156 14.025  1.00 39.87  ? 19   ASP B N   1 
ATOM   2676  C CA  . ASP B  2 19  ? 42.918  28.806 14.377  1.00 40.62  ? 19   ASP B CA  1 
ATOM   2677  C C   . ASP B  2 19  ? 42.784  30.315 14.650  1.00 37.87  ? 19   ASP B C   1 
ATOM   2678  O O   . ASP B  2 19  ? 43.788  31.019 14.777  1.00 38.41  ? 19   ASP B O   1 
ATOM   2679  C CB  . ASP B  2 19  ? 43.978  28.531 13.288  1.00 42.39  ? 19   ASP B CB  1 
ATOM   2680  C CG  . ASP B  2 19  ? 43.506  28.900 11.881  1.00 40.41  ? 19   ASP B CG  1 
ATOM   2681  O OD1 . ASP B  2 19  ? 42.319  29.250 11.703  1.00 37.96  ? 19   ASP B OD1 1 
ATOM   2682  O OD2 . ASP B  2 19  ? 44.329  28.822 10.941  1.00 41.55  ? 19   ASP B OD2 1 
ATOM   2683  N N   . GLY B  2 20  ? 41.554  30.812 14.748  1.00 35.29  ? 20   GLY B N   1 
ATOM   2684  C CA  . GLY B  2 20  ? 41.336  32.229 15.023  1.00 32.98  ? 20   GLY B CA  1 
ATOM   2685  C C   . GLY B  2 20  ? 39.890  32.596 15.280  1.00 30.74  ? 20   GLY B C   1 
ATOM   2686  O O   . GLY B  2 20  ? 38.989  31.780 15.086  1.00 30.85  ? 20   GLY B O   1 
ATOM   2687  N N   . TRP B  2 21  ? 39.677  33.837 15.712  1.00 29.04  ? 21   TRP B N   1 
ATOM   2688  C CA  . TRP B  2 21  ? 38.334  34.349 15.986  1.00 27.10  ? 21   TRP B CA  1 
ATOM   2689  C C   . TRP B  2 21  ? 37.682  34.921 14.734  1.00 25.64  ? 21   TRP B C   1 
ATOM   2690  O O   . TRP B  2 21  ? 36.476  34.763 14.531  1.00 24.86  ? 21   TRP B O   1 
ATOM   2691  C CB  . TRP B  2 21  ? 38.362  35.416 17.092  1.00 26.26  ? 21   TRP B CB  1 
ATOM   2692  C CG  . TRP B  2 21  ? 38.094  34.890 18.480  1.00 26.90  ? 21   TRP B CG  1 
ATOM   2693  C CD1 . TRP B  2 21  ? 37.318  33.812 18.829  1.00 27.56  ? 21   TRP B CD1 1 
ATOM   2694  C CD2 . TRP B  2 21  ? 38.570  35.448 19.706  1.00 27.13  ? 21   TRP B CD2 1 
ATOM   2695  N NE1 . TRP B  2 21  ? 37.305  33.655 20.194  1.00 28.15  ? 21   TRP B NE1 1 
ATOM   2696  C CE2 . TRP B  2 21  ? 38.064  34.647 20.757  1.00 27.80  ? 21   TRP B CE2 1 
ATOM   2697  C CE3 . TRP B  2 21  ? 39.382  36.543 20.020  1.00 27.11  ? 21   TRP B CE3 1 
ATOM   2698  C CZ2 . TRP B  2 21  ? 38.342  34.909 22.095  1.00 28.22  ? 21   TRP B CZ2 1 
ATOM   2699  C CZ3 . TRP B  2 21  ? 39.660  36.806 21.354  1.00 27.61  ? 21   TRP B CZ3 1 
ATOM   2700  C CH2 . TRP B  2 21  ? 39.139  35.992 22.376  1.00 28.06  ? 21   TRP B CH2 1 
ATOM   2701  N N   . TYR B  2 22  ? 38.478  35.604 13.917  1.00 25.56  ? 22   TYR B N   1 
ATOM   2702  C CA  . TYR B  2 22  ? 37.997  36.186 12.670  1.00 24.49  ? 22   TYR B CA  1 
ATOM   2703  C C   . TYR B  2 22  ? 38.927  35.784 11.538  1.00 25.60  ? 22   TYR B C   1 
ATOM   2704  O O   . TYR B  2 22  ? 40.128  35.601 11.745  1.00 27.01  ? 22   TYR B O   1 
ATOM   2705  C CB  . TYR B  2 22  ? 37.946  37.717 12.760  1.00 23.39  ? 22   TYR B CB  1 
ATOM   2706  C CG  . TYR B  2 22  ? 37.740  38.264 14.152  1.00 22.95  ? 22   TYR B CG  1 
ATOM   2707  C CD1 . TYR B  2 22  ? 36.510  38.158 14.789  1.00 22.05  ? 22   TYR B CD1 1 
ATOM   2708  C CD2 . TYR B  2 22  ? 38.779  38.888 14.834  1.00 23.68  ? 22   TYR B CD2 1 
ATOM   2709  C CE1 . TYR B  2 22  ? 36.318  38.664 16.064  1.00 21.71  ? 22   TYR B CE1 1 
ATOM   2710  C CE2 . TYR B  2 22  ? 38.598  39.395 16.106  1.00 23.38  ? 22   TYR B CE2 1 
ATOM   2711  C CZ  . TYR B  2 22  ? 37.367  39.281 16.714  1.00 22.30  ? 22   TYR B CZ  1 
ATOM   2712  O OH  . TYR B  2 22  ? 37.186  39.784 17.976  1.00 22.04  ? 22   TYR B OH  1 
ATOM   2713  N N   . GLY B  2 23  ? 38.373  35.656 10.340  1.00 25.20  ? 23   GLY B N   1 
ATOM   2714  C CA  . GLY B  2 23  ? 39.182  35.309 9.187   1.00 26.21  ? 23   GLY B CA  1 
ATOM   2715  C C   . GLY B  2 23  ? 38.407  35.251 7.894   1.00 25.62  ? 23   GLY B C   1 
ATOM   2716  O O   . GLY B  2 23  ? 37.318  35.822 7.784   1.00 24.39  ? 23   GLY B O   1 
ATOM   2717  N N   . TYR B  2 24  ? 38.981  34.536 6.925   1.00 26.79  ? 24   TYR B N   1 
ATOM   2718  C CA  . TYR B  2 24  ? 38.473  34.498 5.557   1.00 26.50  ? 24   TYR B CA  1 
ATOM   2719  C C   . TYR B  2 24  ? 38.158  33.079 5.117   1.00 27.68  ? 24   TYR B C   1 
ATOM   2720  O O   . TYR B  2 24  ? 38.782  32.128 5.579   1.00 29.20  ? 24   TYR B O   1 
ATOM   2721  C CB  . TYR B  2 24  ? 39.511  35.070 4.592   1.00 26.94  ? 24   TYR B CB  1 
ATOM   2722  C CG  . TYR B  2 24  ? 40.193  36.327 5.070   1.00 26.83  ? 24   TYR B CG  1 
ATOM   2723  C CD1 . TYR B  2 24  ? 41.225  36.265 5.992   1.00 28.00  ? 24   TYR B CD1 1 
ATOM   2724  C CD2 . TYR B  2 24  ? 39.817  37.577 4.588   1.00 25.95  ? 24   TYR B CD2 1 
ATOM   2725  C CE1 . TYR B  2 24  ? 41.861  37.409 6.433   1.00 28.27  ? 24   TYR B CE1 1 
ATOM   2726  C CE2 . TYR B  2 24  ? 40.446  38.733 5.027   1.00 26.27  ? 24   TYR B CE2 1 
ATOM   2727  C CZ  . TYR B  2 24  ? 41.469  38.641 5.950   1.00 27.41  ? 24   TYR B CZ  1 
ATOM   2728  O OH  . TYR B  2 24  ? 42.113  39.775 6.390   1.00 28.09  ? 24   TYR B OH  1 
ATOM   2729  N N   . HIS B  2 25  ? 37.188  32.947 4.219   1.00 27.37  ? 25   HIS B N   1 
ATOM   2730  C CA  . HIS B  2 25  ? 36.969  31.700 3.501   1.00 28.80  ? 25   HIS B CA  1 
ATOM   2731  C C   . HIS B  2 25  ? 36.949  31.973 2.007   1.00 28.62  ? 25   HIS B C   1 
ATOM   2732  O O   . HIS B  2 25  ? 36.133  32.763 1.530   1.00 27.54  ? 25   HIS B O   1 
ATOM   2733  C CB  . HIS B  2 25  ? 35.665  31.031 3.905   1.00 29.16  ? 25   HIS B CB  1 
ATOM   2734  C CG  . HIS B  2 25  ? 35.472  29.689 3.272   1.00 31.07  ? 25   HIS B CG  1 
ATOM   2735  N ND1 . HIS B  2 25  ? 34.756  29.510 2.107   1.00 31.17  ? 25   HIS B ND1 1 
ATOM   2736  C CD2 . HIS B  2 25  ? 35.929  28.464 3.624   1.00 33.13  ? 25   HIS B CD2 1 
ATOM   2737  C CE1 . HIS B  2 25  ? 34.762  28.230 1.782   1.00 33.21  ? 25   HIS B CE1 1 
ATOM   2738  N NE2 . HIS B  2 25  ? 35.469  27.574 2.685   1.00 34.50  ? 25   HIS B NE2 1 
ATOM   2739  N N   . HIS B  2 26  ? 37.851  31.317 1.282   1.00 29.97  ? 26   HIS B N   1 
ATOM   2740  C CA  . HIS B  2 26  ? 37.968  31.487 -0.163  1.00 29.98  ? 26   HIS B CA  1 
ATOM   2741  C C   . HIS B  2 26  ? 37.435  30.256 -0.879  1.00 31.30  ? 26   HIS B C   1 
ATOM   2742  O O   . HIS B  2 26  ? 37.450  29.168 -0.322  1.00 32.78  ? 26   HIS B O   1 
ATOM   2743  C CB  . HIS B  2 26  ? 39.428  31.733 -0.552  1.00 30.70  ? 26   HIS B CB  1 
ATOM   2744  C CG  . HIS B  2 26  ? 40.293  30.512 -0.485  1.00 32.85  ? 26   HIS B CG  1 
ATOM   2745  N ND1 . HIS B  2 26  ? 40.970  30.140 0.657   1.00 34.04  ? 26   HIS B ND1 1 
ATOM   2746  C CD2 . HIS B  2 26  ? 40.592  29.580 -1.420  1.00 34.32  ? 26   HIS B CD2 1 
ATOM   2747  C CE1 . HIS B  2 26  ? 41.647  29.030 0.423   1.00 36.24  ? 26   HIS B CE1 1 
ATOM   2748  N NE2 . HIS B  2 26  ? 41.434  28.670 -0.830  1.00 36.44  ? 26   HIS B NE2 1 
ATOM   2749  N N   . SER B  2 27  ? 36.939  30.441 -2.098  1.00 31.07  ? 27   SER B N   1 
ATOM   2750  C CA  . SER B  2 27  ? 36.602  29.318 -2.979  1.00 32.60  ? 27   SER B CA  1 
ATOM   2751  C C   . SER B  2 27  ? 36.879  29.695 -4.436  1.00 32.40  ? 27   SER B C   1 
ATOM   2752  O O   . SER B  2 27  ? 36.424  30.737 -4.913  1.00 31.10  ? 27   SER B O   1 
ATOM   2753  C CB  . SER B  2 27  ? 35.146  28.880 -2.796  1.00 32.96  ? 27   SER B CB  1 
ATOM   2754  O OG  . SER B  2 27  ? 34.246  29.838 -3.318  1.00 31.74  ? 27   SER B OG  1 
ATOM   2755  N N   . ASN B  2 28  ? 37.644  28.848 -5.123  1.00 33.97  ? 28   ASN B N   1 
ATOM   2756  C CA  . ASN B  2 28  ? 38.014  29.069 -6.520  1.00 34.02  ? 28   ASN B CA  1 
ATOM   2757  C C   . ASN B  2 28  ? 38.222  27.725 -7.226  1.00 36.18  ? 28   ASN B C   1 
ATOM   2758  O O   . ASN B  2 28  ? 37.877  26.682 -6.672  1.00 37.68  ? 28   ASN B O   1 
ATOM   2759  C CB  . ASN B  2 28  ? 39.253  29.975 -6.603  1.00 33.51  ? 28   ASN B CB  1 
ATOM   2760  C CG  . ASN B  2 28  ? 40.467  29.390 -5.908  1.00 34.96  ? 28   ASN B CG  1 
ATOM   2761  O OD1 . ASN B  2 28  ? 40.518  28.201 -5.612  1.00 36.62  ? 28   ASN B OD1 1 
ATOM   2762  N ND2 . ASN B  2 28  ? 41.460  30.232 -5.649  1.00 34.75  ? 28   ASN B ND2 1 
ATOM   2763  N N   . GLU B  2 29  ? 38.767  27.740 -8.440  1.00 36.64  ? 29   GLU B N   1 
ATOM   2764  C CA  . GLU B  2 29  ? 38.967  26.500 -9.196  1.00 38.80  ? 29   GLU B CA  1 
ATOM   2765  C C   . GLU B  2 29  ? 39.893  25.510 -8.485  1.00 40.89  ? 29   GLU B C   1 
ATOM   2766  O O   . GLU B  2 29  ? 39.700  24.300 -8.581  1.00 43.02  ? 29   GLU B O   1 
ATOM   2767  C CB  . GLU B  2 29  ? 39.526  26.795 -10.590 1.00 38.92  ? 29   GLU B CB  1 
ATOM   2768  C CG  . GLU B  2 29  ? 38.577  27.559 -11.508 1.00 37.60  ? 29   GLU B CG  1 
ATOM   2769  C CD  . GLU B  2 29  ? 39.005  27.522 -12.973 1.00 38.14  ? 29   GLU B CD  1 
ATOM   2770  O OE1 . GLU B  2 29  ? 40.159  27.121 -13.271 1.00 39.35  ? 29   GLU B OE1 1 
ATOM   2771  O OE2 . GLU B  2 29  ? 38.176  27.891 -13.833 1.00 37.61  ? 29   GLU B OE2 1 
ATOM   2772  N N   . GLN B  2 30  ? 40.897  26.030 -7.782  1.00 40.61  ? 30   GLN B N   1 
ATOM   2773  C CA  . GLN B  2 30  ? 41.882  25.198 -7.081  1.00 42.88  ? 30   GLN B CA  1 
ATOM   2774  C C   . GLN B  2 30  ? 41.339  24.559 -5.800  1.00 43.56  ? 30   GLN B C   1 
ATOM   2775  O O   . GLN B  2 30  ? 41.804  23.498 -5.394  1.00 46.20  ? 30   GLN B O   1 
ATOM   2776  C CB  . GLN B  2 30  ? 43.124  26.027 -6.750  1.00 42.75  ? 30   GLN B CB  1 
ATOM   2777  C CG  . GLN B  2 30  ? 43.914  26.458 -7.978  1.00 42.93  ? 30   GLN B CG  1 
ATOM   2778  C CD  . GLN B  2 30  ? 44.249  27.939 -7.961  1.00 41.17  ? 30   GLN B CD  1 
ATOM   2779  O OE1 . GLN B  2 30  ? 43.424  28.779 -8.347  1.00 39.12  ? 30   GLN B OE1 1 
ATOM   2780  N NE2 . GLN B  2 30  ? 45.464  28.271 -7.517  1.00 42.38  ? 30   GLN B NE2 1 
ATOM   2781  N N   . GLY B  2 31  ? 40.369  25.207 -5.161  1.00 41.42  ? 31   GLY B N   1 
ATOM   2782  C CA  . GLY B  2 31  ? 39.763  24.671 -3.942  1.00 42.00  ? 31   GLY B CA  1 
ATOM   2783  C C   . GLY B  2 31  ? 39.164  25.740 -3.053  1.00 39.46  ? 31   GLY B C   1 
ATOM   2784  O O   . GLY B  2 31  ? 38.933  26.862 -3.489  1.00 37.28  ? 31   GLY B O   1 
ATOM   2785  N N   . SER B  2 32  ? 38.919  25.379 -1.799  1.00 39.95  ? 32   SER B N   1 
ATOM   2786  C CA  . SER B  2 32  ? 38.392  26.307 -0.807  1.00 37.81  ? 32   SER B CA  1 
ATOM   2787  C C   . SER B  2 32  ? 39.038  26.074 0.550   1.00 38.70  ? 32   SER B C   1 
ATOM   2788  O O   . SER B  2 32  ? 39.595  25.007 0.800   1.00 41.25  ? 32   SER B O   1 
ATOM   2789  C CB  . SER B  2 32  ? 36.879  26.144 -0.694  1.00 37.43  ? 32   SER B CB  1 
ATOM   2790  O OG  . SER B  2 32  ? 36.532  24.796 -0.461  1.00 40.04  ? 32   SER B OG  1 
ATOM   2791  N N   . GLY B  2 33  ? 38.963  27.071 1.428   1.00 36.81  ? 33   GLY B N   1 
ATOM   2792  C CA  . GLY B  2 33  ? 39.541  26.937 2.764   1.00 37.61  ? 33   GLY B CA  1 
ATOM   2793  C C   . GLY B  2 33  ? 39.434  28.142 3.680   1.00 35.45  ? 33   GLY B C   1 
ATOM   2794  O O   . GLY B  2 33  ? 39.197  29.264 3.233   1.00 33.40  ? 33   GLY B O   1 
ATOM   2795  N N   . TYR B  2 34  ? 39.627  27.889 4.972   1.00 36.21  ? 34   TYR B N   1 
ATOM   2796  C CA  . TYR B  2 34  ? 39.591  28.922 6.000   1.00 34.55  ? 34   TYR B CA  1 
ATOM   2797  C C   . TYR B  2 34  ? 40.996  29.392 6.351   1.00 35.23  ? 34   TYR B C   1 
ATOM   2798  O O   . TYR B  2 34  ? 41.903  28.587 6.506   1.00 37.63  ? 34   TYR B O   1 
ATOM   2799  C CB  . TYR B  2 34  ? 38.924  28.387 7.264   1.00 35.11  ? 34   TYR B CB  1 
ATOM   2800  C CG  . TYR B  2 34  ? 37.509  27.901 7.059   1.00 34.93  ? 34   TYR B CG  1 
ATOM   2801  C CD1 . TYR B  2 34  ? 36.433  28.781 7.123   1.00 32.78  ? 34   TYR B CD1 1 
ATOM   2802  C CD2 . TYR B  2 34  ? 37.242  26.557 6.805   1.00 37.33  ? 34   TYR B CD2 1 
ATOM   2803  C CE1 . TYR B  2 34  ? 35.135  28.334 6.937   1.00 33.06  ? 34   TYR B CE1 1 
ATOM   2804  C CE2 . TYR B  2 34  ? 35.945  26.104 6.619   1.00 37.61  ? 34   TYR B CE2 1 
ATOM   2805  C CZ  . TYR B  2 34  ? 34.898  26.996 6.691   1.00 35.49  ? 34   TYR B CZ  1 
ATOM   2806  O OH  . TYR B  2 34  ? 33.610  26.557 6.511   1.00 36.23  ? 34   TYR B OH  1 
ATOM   2807  N N   . ALA B  2 35  ? 41.161  30.703 6.473   1.00 33.51  ? 35   ALA B N   1 
ATOM   2808  C CA  . ALA B  2 35  ? 42.400  31.293 6.959   1.00 34.36  ? 35   ALA B CA  1 
ATOM   2809  C C   . ALA B  2 35  ? 42.066  32.333 8.023   1.00 32.85  ? 35   ALA B C   1 
ATOM   2810  O O   . ALA B  2 35  ? 41.347  33.292 7.757   1.00 30.84  ? 35   ALA B O   1 
ATOM   2811  C CB  . ALA B  2 35  ? 43.163  31.937 5.818   1.00 34.40  ? 35   ALA B CB  1 
ATOM   2812  N N   . ALA B  2 36  ? 42.569  32.126 9.233   1.00 34.07  ? 36   ALA B N   1 
ATOM   2813  C CA  . ALA B  2 36  ? 42.358  33.072 10.316  1.00 32.92  ? 36   ALA B CA  1 
ATOM   2814  C C   . ALA B  2 36  ? 43.176  34.332 10.066  1.00 32.81  ? 36   ALA B C   1 
ATOM   2815  O O   . ALA B  2 36  ? 44.325  34.254 9.643   1.00 34.65  ? 36   ALA B O   1 
ATOM   2816  C CB  . ALA B  2 36  ? 42.742  32.451 11.651  1.00 34.53  ? 36   ALA B CB  1 
ATOM   2817  N N   . ASP B  2 37  ? 42.569  35.488 10.322  1.00 31.03  ? 37   ASP B N   1 
ATOM   2818  C CA  . ASP B  2 37  ? 43.269  36.765 10.283  1.00 31.25  ? 37   ASP B CA  1 
ATOM   2819  C C   . ASP B  2 37  ? 43.988  36.967 11.621  1.00 32.58  ? 37   ASP B C   1 
ATOM   2820  O O   . ASP B  2 37  ? 43.350  37.224 12.648  1.00 31.54  ? 37   ASP B O   1 
ATOM   2821  C CB  . ASP B  2 37  ? 42.281  37.900 10.027  1.00 29.18  ? 37   ASP B CB  1 
ATOM   2822  C CG  . ASP B  2 37  ? 42.967  39.221 9.788   1.00 29.77  ? 37   ASP B CG  1 
ATOM   2823  O OD1 . ASP B  2 37  ? 43.360  39.484 8.633   1.00 30.28  ? 37   ASP B OD1 1 
ATOM   2824  O OD2 . ASP B  2 37  ? 43.110  40.001 10.754  1.00 29.94  ? 37   ASP B OD2 1 
ATOM   2825  N N   . LYS B  2 38  ? 45.314  36.839 11.603  1.00 35.10  ? 38   LYS B N   1 
ATOM   2826  C CA  . LYS B  2 38  ? 46.121  36.886 12.829  1.00 36.99  ? 38   LYS B CA  1 
ATOM   2827  C C   . LYS B  2 38  ? 46.057  38.229 13.551  1.00 36.35  ? 38   LYS B C   1 
ATOM   2828  O O   . LYS B  2 38  ? 45.896  38.265 14.771  1.00 36.29  ? 38   LYS B O   1 
ATOM   2829  C CB  . LYS B  2 38  ? 47.589  36.539 12.533  1.00 40.28  ? 38   LYS B CB  1 
ATOM   2830  C CG  . LYS B  2 38  ? 47.870  35.045 12.437  1.00 42.04  ? 38   LYS B CG  1 
ATOM   2831  C CD  . LYS B  2 38  ? 49.368  34.742 12.454  1.00 45.88  ? 38   LYS B CD  1 
ATOM   2832  C CE  . LYS B  2 38  ? 50.000  34.884 11.073  1.00 46.86  ? 38   LYS B CE  1 
ATOM   2833  N NZ  . LYS B  2 38  ? 51.492  34.878 11.137  1.00 50.82  ? 38   LYS B NZ  1 
ATOM   2834  N N   . GLU B  2 39  ? 46.190  39.320 12.798  1.00 36.12  ? 39   GLU B N   1 
ATOM   2835  C CA  . GLU B  2 39  ? 46.232  40.670 13.378  1.00 36.13  ? 39   GLU B CA  1 
ATOM   2836  C C   . GLU B  2 39  ? 44.974  41.031 14.170  1.00 33.61  ? 39   GLU B C   1 
ATOM   2837  O O   . GLU B  2 39  ? 45.069  41.428 15.328  1.00 33.98  ? 39   GLU B O   1 
ATOM   2838  C CB  . GLU B  2 39  ? 46.487  41.730 12.291  1.00 36.65  ? 39   GLU B CB  1 
ATOM   2839  C CG  . GLU B  2 39  ? 45.994  43.134 12.655  1.00 36.09  ? 39   GLU B CG  1 
ATOM   2840  C CD  . GLU B  2 39  ? 46.711  44.237 11.897  1.00 38.08  ? 39   GLU B CD  1 
ATOM   2841  O OE1 . GLU B  2 39  ? 47.030  44.037 10.700  1.00 38.64  ? 39   GLU B OE1 1 
ATOM   2842  O OE2 . GLU B  2 39  ? 46.966  45.304 12.511  1.00 39.37  ? 39   GLU B OE2 1 
ATOM   2843  N N   . SER B  2 40  ? 43.808  40.923 13.544  1.00 31.27  ? 40   SER B N   1 
ATOM   2844  C CA  . SER B  2 40  ? 42.560  41.282 14.217  1.00 29.19  ? 40   SER B CA  1 
ATOM   2845  C C   . SER B  2 40  ? 42.284  40.352 15.398  1.00 28.92  ? 40   SER B C   1 
ATOM   2846  O O   . SER B  2 40  ? 41.784  40.795 16.435  1.00 28.24  ? 40   SER B O   1 
ATOM   2847  C CB  . SER B  2 40  ? 41.377  41.281 13.243  1.00 27.36  ? 40   SER B CB  1 
ATOM   2848  O OG  . SER B  2 40  ? 41.198  40.013 12.639  1.00 27.20  ? 40   SER B OG  1 
ATOM   2849  N N   . THR B  2 41  ? 42.630  39.076 15.245  1.00 29.69  ? 41   THR B N   1 
ATOM   2850  C CA  . THR B  2 41  ? 42.452  38.089 16.307  1.00 29.99  ? 41   THR B CA  1 
ATOM   2851  C C   . THR B  2 41  ? 43.326  38.403 17.526  1.00 31.51  ? 41   THR B C   1 
ATOM   2852  O O   . THR B  2 41  ? 42.843  38.398 18.658  1.00 30.97  ? 41   THR B O   1 
ATOM   2853  C CB  . THR B  2 41  ? 42.769  36.663 15.801  1.00 31.28  ? 41   THR B CB  1 
ATOM   2854  O OG1 . THR B  2 41  ? 41.923  36.351 14.689  1.00 29.96  ? 41   THR B OG1 1 
ATOM   2855  C CG2 . THR B  2 41  ? 42.551  35.625 16.894  1.00 32.08  ? 41   THR B CG2 1 
ATOM   2856  N N   . GLN B  2 42  ? 44.608  38.670 17.292  1.00 33.62  ? 42   GLN B N   1 
ATOM   2857  C CA  . GLN B  2 42  ? 45.544  38.948 18.385  1.00 35.63  ? 42   GLN B CA  1 
ATOM   2858  C C   . GLN B  2 42  ? 45.153  40.215 19.133  1.00 34.54  ? 42   GLN B C   1 
ATOM   2859  O O   . GLN B  2 42  ? 45.279  40.286 20.353  1.00 35.12  ? 42   GLN B O   1 
ATOM   2860  C CB  . GLN B  2 42  ? 46.977  39.081 17.856  1.00 38.52  ? 42   GLN B CB  1 
ATOM   2861  C CG  . GLN B  2 42  ? 48.034  39.219 18.948  1.00 41.33  ? 42   GLN B CG  1 
ATOM   2862  C CD  . GLN B  2 42  ? 48.009  38.068 19.940  1.00 42.24  ? 42   GLN B CD  1 
ATOM   2863  O OE1 . GLN B  2 42  ? 47.835  38.270 21.144  1.00 42.18  ? 42   GLN B OE1 1 
ATOM   2864  N NE2 . GLN B  2 42  ? 48.168  36.849 19.434  1.00 43.27  ? 42   GLN B NE2 1 
ATOM   2865  N N   . LYS B  2 43  ? 44.681  41.208 18.385  1.00 33.17  ? 43   LYS B N   1 
ATOM   2866  C CA  . LYS B  2 43  ? 44.184  42.461 18.959  1.00 32.26  ? 43   LYS B CA  1 
ATOM   2867  C C   . LYS B  2 43  ? 42.993  42.208 19.876  1.00 30.14  ? 43   LYS B C   1 
ATOM   2868  O O   . LYS B  2 43  ? 42.881  42.821 20.939  1.00 30.15  ? 43   LYS B O   1 
ATOM   2869  C CB  . LYS B  2 43  ? 43.767  43.416 17.838  1.00 31.48  ? 43   LYS B CB  1 
ATOM   2870  C CG  . LYS B  2 43  ? 44.183  44.863 18.038  1.00 32.82  ? 43   LYS B CG  1 
ATOM   2871  C CD  . LYS B  2 43  ? 44.758  45.415 16.739  1.00 34.14  ? 43   LYS B CD  1 
ATOM   2872  C CE  . LYS B  2 43  ? 44.691  46.932 16.652  1.00 35.04  ? 43   LYS B CE  1 
ATOM   2873  N NZ  . LYS B  2 43  ? 44.701  47.352 15.218  1.00 35.40  ? 43   LYS B NZ  1 
ATOM   2874  N N   . ALA B  2 44  ? 42.108  41.308 19.452  1.00 28.52  ? 44   ALA B N   1 
ATOM   2875  C CA  . ALA B  2 44  ? 40.954  40.922 20.253  1.00 26.89  ? 44   ALA B CA  1 
ATOM   2876  C C   . ALA B  2 44  ? 41.385  40.166 21.500  1.00 28.00  ? 44   ALA B C   1 
ATOM   2877  O O   . ALA B  2 44  ? 40.844  40.385 22.580  1.00 27.37  ? 44   ALA B O   1 
ATOM   2878  C CB  . ALA B  2 44  ? 39.991  40.078 19.431  1.00 25.64  ? 44   ALA B CB  1 
ATOM   2879  N N   . ILE B  2 45  ? 42.354  39.269 21.348  1.00 29.86  ? 45   ILE B N   1 
ATOM   2880  C CA  . ILE B  2 45  ? 42.881  38.512 22.482  1.00 31.52  ? 45   ILE B CA  1 
ATOM   2881  C C   . ILE B  2 45  ? 43.504  39.439 23.526  1.00 32.43  ? 45   ILE B C   1 
ATOM   2882  O O   . ILE B  2 45  ? 43.291  39.257 24.723  1.00 32.55  ? 45   ILE B O   1 
ATOM   2883  C CB  . ILE B  2 45  ? 43.892  37.434 22.023  1.00 33.99  ? 45   ILE B CB  1 
ATOM   2884  C CG1 . ILE B  2 45  ? 43.136  36.228 21.457  1.00 33.45  ? 45   ILE B CG1 1 
ATOM   2885  C CG2 . ILE B  2 45  ? 44.788  36.989 23.173  1.00 36.59  ? 45   ILE B CG2 1 
ATOM   2886  C CD1 . ILE B  2 45  ? 43.991  35.286 20.633  1.00 35.66  ? 45   ILE B CD1 1 
ATOM   2887  N N   . ASP B  2 46  ? 44.264  40.431 23.070  1.00 33.26  ? 46   ASP B N   1 
ATOM   2888  C CA  . ASP B  2 46  ? 44.885  41.398 23.973  1.00 34.51  ? 46   ASP B CA  1 
ATOM   2889  C C   . ASP B  2 46  ? 43.838  42.221 24.718  1.00 32.43  ? 46   ASP B C   1 
ATOM   2890  O O   . ASP B  2 46  ? 43.926  42.390 25.934  1.00 32.97  ? 46   ASP B O   1 
ATOM   2891  C CB  . ASP B  2 46  ? 45.829  42.328 23.207  1.00 36.16  ? 46   ASP B CB  1 
ATOM   2892  C CG  . ASP B  2 46  ? 47.009  41.592 22.590  1.00 38.77  ? 46   ASP B CG  1 
ATOM   2893  O OD1 . ASP B  2 46  ? 47.243  40.419 22.946  1.00 39.76  ? 46   ASP B OD1 1 
ATOM   2894  O OD2 . ASP B  2 46  ? 47.706  42.188 21.741  1.00 40.11  ? 46   ASP B OD2 1 
ATOM   2895  N N   . GLY B  2 47  ? 42.843  42.713 23.989  1.00 30.25  ? 47   GLY B N   1 
ATOM   2896  C CA  . GLY B  2 47  ? 41.797  43.545 24.574  1.00 28.55  ? 47   GLY B CA  1 
ATOM   2897  C C   . GLY B  2 47  ? 41.002  42.846 25.660  1.00 27.51  ? 47   GLY B C   1 
ATOM   2898  O O   . GLY B  2 47  ? 40.739  43.423 26.718  1.00 27.37  ? 47   GLY B O   1 
ATOM   2899  N N   . VAL B  2 48  ? 40.621  41.598 25.396  1.00 27.06  ? 48   VAL B N   1 
ATOM   2900  C CA  . VAL B  2 48  ? 39.837  40.797 26.338  1.00 26.43  ? 48   VAL B CA  1 
ATOM   2901  C C   . VAL B  2 48  ? 40.676  40.349 27.536  1.00 28.29  ? 48   VAL B C   1 
ATOM   2902  O O   . VAL B  2 48  ? 40.173  40.285 28.654  1.00 27.96  ? 48   VAL B O   1 
ATOM   2903  C CB  . VAL B  2 48  ? 39.200  39.580 25.627  1.00 25.94  ? 48   VAL B CB  1 
ATOM   2904  C CG1 . VAL B  2 48  ? 38.638  38.575 26.626  1.00 26.19  ? 48   VAL B CG1 1 
ATOM   2905  C CG2 . VAL B  2 48  ? 38.108  40.051 24.670  1.00 24.07  ? 48   VAL B CG2 1 
ATOM   2906  N N   . THR B  2 49  ? 41.947  40.042 27.307  1.00 30.48  ? 49   THR B N   1 
ATOM   2907  C CA  . THR B  2 49  ? 42.839  39.677 28.399  1.00 32.78  ? 49   THR B CA  1 
ATOM   2908  C C   . THR B  2 49  ? 42.971  40.836 29.384  1.00 32.88  ? 49   THR B C   1 
ATOM   2909  O O   . THR B  2 49  ? 42.758  40.662 30.587  1.00 33.09  ? 49   THR B O   1 
ATOM   2910  C CB  . THR B  2 49  ? 44.230  39.272 27.877  1.00 35.55  ? 49   THR B CB  1 
ATOM   2911  O OG1 . THR B  2 49  ? 44.107  38.110 27.050  1.00 35.74  ? 49   THR B OG1 1 
ATOM   2912  C CG2 . THR B  2 49  ? 45.180  38.969 29.027  1.00 38.36  ? 49   THR B CG2 1 
ATOM   2913  N N   . ASN B  2 50  ? 43.317  42.013 28.863  1.00 32.98  ? 50   ASN B N   1 
ATOM   2914  C CA  . ASN B  2 50  ? 43.471  43.218 29.687  1.00 33.41  ? 50   ASN B CA  1 
ATOM   2915  C C   . ASN B  2 50  ? 42.211  43.523 30.476  1.00 31.27  ? 50   ASN B C   1 
ATOM   2916  O O   . ASN B  2 50  ? 42.271  43.888 31.648  1.00 31.80  ? 50   ASN B O   1 
ATOM   2917  C CB  . ASN B  2 50  ? 43.810  44.427 28.813  1.00 33.77  ? 50   ASN B CB  1 
ATOM   2918  C CG  . ASN B  2 50  ? 45.195  44.338 28.200  1.00 36.53  ? 50   ASN B CG  1 
ATOM   2919  O OD1 . ASN B  2 50  ? 46.168  44.068 28.890  1.00 39.04  ? 50   ASN B OD1 1 
ATOM   2920  N ND2 . ASN B  2 50  ? 45.287  44.571 26.901  1.00 36.31  ? 50   ASN B ND2 1 
ATOM   2921  N N   . LYS B  2 51  ? 41.071  43.373 29.809  1.00 29.11  ? 51   LYS B N   1 
ATOM   2922  C CA  . LYS B  2 51  ? 39.758  43.594 30.411  1.00 27.23  ? 51   LYS B CA  1 
ATOM   2923  C C   . LYS B  2 51  ? 39.503  42.704 31.622  1.00 27.48  ? 51   LYS B C   1 
ATOM   2924  O O   . LYS B  2 51  ? 39.022  43.164 32.654  1.00 27.03  ? 51   LYS B O   1 
ATOM   2925  C CB  . LYS B  2 51  ? 38.690  43.325 29.362  1.00 25.42  ? 51   LYS B CB  1 
ATOM   2926  C CG  . LYS B  2 51  ? 37.265  43.327 29.873  1.00 23.76  ? 51   LYS B CG  1 
ATOM   2927  C CD  . LYS B  2 51  ? 36.329  43.031 28.714  1.00 22.55  ? 51   LYS B CD  1 
ATOM   2928  C CE  . LYS B  2 51  ? 35.256  44.083 28.580  1.00 21.44  ? 51   LYS B CE  1 
ATOM   2929  N NZ  . LYS B  2 51  ? 34.747  44.192 27.197  1.00 20.84  ? 51   LYS B NZ  1 
ATOM   2930  N N   . VAL B  2 52  ? 39.808  41.424 31.476  1.00 28.46  ? 52   VAL B N   1 
ATOM   2931  C CA  . VAL B  2 52  ? 39.623  40.470 32.557  1.00 29.23  ? 52   VAL B CA  1 
ATOM   2932  C C   . VAL B  2 52  ? 40.534  40.825 33.735  1.00 31.10  ? 52   VAL B C   1 
ATOM   2933  O O   . VAL B  2 52  ? 40.092  40.815 34.885  1.00 30.92  ? 52   VAL B O   1 
ATOM   2934  C CB  . VAL B  2 52  ? 39.875  39.024 32.066  1.00 30.44  ? 52   VAL B CB  1 
ATOM   2935  C CG1 . VAL B  2 52  ? 39.942  38.044 33.233  1.00 32.01  ? 52   VAL B CG1 1 
ATOM   2936  C CG2 . VAL B  2 52  ? 38.783  38.609 31.085  1.00 28.75  ? 52   VAL B CG2 1 
ATOM   2937  N N   . ASN B  2 53  ? 41.792  41.153 33.443  1.00 33.16  ? 53   ASN B N   1 
ATOM   2938  C CA  . ASN B  2 53  ? 42.752  41.553 34.482  1.00 35.47  ? 53   ASN B CA  1 
ATOM   2939  C C   . ASN B  2 53  ? 42.362  42.880 35.128  1.00 34.60  ? 53   ASN B C   1 
ATOM   2940  O O   . ASN B  2 53  ? 42.466  43.038 36.341  1.00 35.35  ? 53   ASN B O   1 
ATOM   2941  C CB  . ASN B  2 53  ? 44.169  41.665 33.912  1.00 38.14  ? 53   ASN B CB  1 
ATOM   2942  C CG  . ASN B  2 53  ? 44.665  40.366 33.305  1.00 39.64  ? 53   ASN B CG  1 
ATOM   2943  O OD1 . ASN B  2 53  ? 44.168  39.287 33.624  1.00 39.51  ? 53   ASN B OD1 1 
ATOM   2944  N ND2 . ASN B  2 53  ? 45.651  40.465 32.420  1.00 41.38  ? 53   ASN B ND2 1 
ATOM   2945  N N   . SER B  2 54  ? 41.910  43.826 34.306  1.00 33.30  ? 54   SER B N   1 
ATOM   2946  C CA  . SER B  2 54  ? 41.415  45.111 34.801  1.00 32.63  ? 54   SER B CA  1 
ATOM   2947  C C   . SER B  2 54  ? 40.266  44.895 35.765  1.00 31.14  ? 54   SER B C   1 
ATOM   2948  O O   . SER B  2 54  ? 40.237  45.482 36.846  1.00 31.52  ? 54   SER B O   1 
ATOM   2949  C CB  . SER B  2 54  ? 40.951  46.007 33.647  1.00 31.41  ? 54   SER B CB  1 
ATOM   2950  O OG  . SER B  2 54  ? 42.052  46.629 33.013  1.00 33.38  ? 54   SER B OG  1 
ATOM   2951  N N   . ILE B  2 55  ? 39.321  44.052 35.353  1.00 29.78  ? 55   ILE B N   1 
ATOM   2952  C CA  . ILE B  2 55  ? 38.156  43.708 36.168  1.00 28.65  ? 55   ILE B CA  1 
ATOM   2953  C C   . ILE B  2 55  ? 38.578  43.090 37.499  1.00 30.25  ? 55   ILE B C   1 
ATOM   2954  O O   . ILE B  2 55  ? 38.100  43.502 38.552  1.00 29.93  ? 55   ILE B O   1 
ATOM   2955  C CB  . ILE B  2 55  ? 37.198  42.763 35.402  1.00 27.37  ? 55   ILE B CB  1 
ATOM   2956  C CG1 . ILE B  2 55  ? 36.331  43.584 34.442  1.00 25.76  ? 55   ILE B CG1 1 
ATOM   2957  C CG2 . ILE B  2 55  ? 36.303  41.981 36.357  1.00 27.02  ? 55   ILE B CG2 1 
ATOM   2958  C CD1 . ILE B  2 55  ? 35.596  42.779 33.391  1.00 24.89  ? 55   ILE B CD1 1 
ATOM   2959  N N   . ILE B  2 56  ? 39.479  42.113 37.446  1.00 32.36  ? 56   ILE B N   1 
ATOM   2960  C CA  . ILE B  2 56  ? 39.964  41.451 38.657  1.00 34.36  ? 56   ILE B CA  1 
ATOM   2961  C C   . ILE B  2 56  ? 40.619  42.463 39.603  1.00 35.73  ? 56   ILE B C   1 
ATOM   2962  O O   . ILE B  2 56  ? 40.274  42.519 40.788  1.00 35.78  ? 56   ILE B O   1 
ATOM   2963  C CB  . ILE B  2 56  ? 40.962  40.321 38.313  1.00 36.74  ? 56   ILE B CB  1 
ATOM   2964  C CG1 . ILE B  2 56  ? 40.235  39.160 37.622  1.00 36.01  ? 56   ILE B CG1 1 
ATOM   2965  C CG2 . ILE B  2 56  ? 41.680  39.821 39.567  1.00 39.29  ? 56   ILE B CG2 1 
ATOM   2966  C CD1 . ILE B  2 56  ? 41.156  38.212 36.878  1.00 38.13  ? 56   ILE B CD1 1 
ATOM   2967  N N   . ASP B  2 57  ? 41.549  43.261 39.075  1.00 37.20  ? 57   ASP B N   1 
ATOM   2968  C CA  . ASP B  2 57  ? 42.320  44.222 39.887  1.00 39.18  ? 57   ASP B CA  1 
ATOM   2969  C C   . ASP B  2 57  ? 41.455  45.256 40.604  1.00 37.86  ? 57   ASP B C   1 
ATOM   2970  O O   . ASP B  2 57  ? 41.720  45.605 41.749  1.00 39.04  ? 57   ASP B O   1 
ATOM   2971  C CB  . ASP B  2 57  ? 43.365  44.940 39.029  1.00 40.86  ? 57   ASP B CB  1 
ATOM   2972  C CG  . ASP B  2 57  ? 44.626  44.118 38.839  1.00 43.88  ? 57   ASP B CG  1 
ATOM   2973  O OD1 . ASP B  2 57  ? 45.231  43.718 39.865  1.00 46.14  ? 57   ASP B OD1 1 
ATOM   2974  O OD2 . ASP B  2 57  ? 45.019  43.879 37.670  1.00 44.23  ? 57   ASP B OD2 1 
ATOM   2975  N N   . LYS B  2 58  ? 40.423  45.748 39.932  1.00 35.83  ? 58   LYS B N   1 
ATOM   2976  C CA  . LYS B  2 58  ? 39.518  46.717 40.548  1.00 34.79  ? 58   LYS B CA  1 
ATOM   2977  C C   . LYS B  2 58  ? 38.757  46.132 41.734  1.00 34.42  ? 58   LYS B C   1 
ATOM   2978  O O   . LYS B  2 58  ? 38.497  46.832 42.713  1.00 34.50  ? 58   LYS B O   1 
ATOM   2979  C CB  . LYS B  2 58  ? 38.558  47.315 39.507  1.00 32.82  ? 58   LYS B CB  1 
ATOM   2980  C CG  . LYS B  2 58  ? 38.882  48.755 39.114  1.00 33.62  ? 58   LYS B CG  1 
ATOM   2981  C CD  . LYS B  2 58  ? 40.382  49.039 39.076  1.00 36.29  ? 58   LYS B CD  1 
ATOM   2982  C CE  . LYS B  2 58  ? 40.683  50.469 38.691  1.00 37.54  ? 58   LYS B CE  1 
ATOM   2983  N NZ  . LYS B  2 58  ? 42.151  50.720 38.724  1.00 40.65  ? 58   LYS B NZ  1 
ATOM   2984  N N   . MET B  2 59  ? 38.432  44.846 41.654  1.00 34.47  ? 59   MET B N   1 
ATOM   2985  C CA  . MET B  2 59  ? 37.735  44.156 42.738  1.00 34.42  ? 59   MET B CA  1 
ATOM   2986  C C   . MET B  2 59  ? 38.707  43.657 43.809  1.00 37.04  ? 59   MET B C   1 
ATOM   2987  O O   . MET B  2 59  ? 38.307  43.454 44.955  1.00 37.10  ? 59   MET B O   1 
ATOM   2988  C CB  . MET B  2 59  ? 36.920  42.989 42.177  1.00 33.49  ? 59   MET B CB  1 
ATOM   2989  C CG  . MET B  2 59  ? 35.969  43.393 41.058  1.00 31.55  ? 59   MET B CG  1 
ATOM   2990  S SD  . MET B  2 59  ? 34.783  44.628 41.608  1.00 30.20  ? 59   MET B SD  1 
ATOM   2991  C CE  . MET B  2 59  ? 33.573  43.665 42.507  1.00 29.61  ? 59   MET B CE  1 
ATOM   2992  N N   . ASN B  2 60  ? 39.975  43.471 43.433  1.00 39.52  ? 60   ASN B N   1 
ATOM   2993  C CA  . ASN B  2 60  ? 41.019  42.976 44.352  1.00 42.64  ? 60   ASN B CA  1 
ATOM   2994  C C   . ASN B  2 60  ? 40.997  43.637 45.736  1.00 43.38  ? 60   ASN B C   1 
ATOM   2995  O O   . ASN B  2 60  ? 41.105  42.953 46.755  1.00 44.59  ? 60   ASN B O   1 
ATOM   2996  C CB  . ASN B  2 60  ? 42.416  43.101 43.708  1.00 45.13  ? 60   ASN B CB  1 
ATOM   2997  C CG  . ASN B  2 60  ? 43.532  43.277 44.733  1.00 48.40  ? 60   ASN B CG  1 
ATOM   2998  O OD1 . ASN B  2 60  ? 43.569  44.273 45.463  1.00 48.61  ? 60   ASN B OD1 1 
ATOM   2999  N ND2 . ASN B  2 60  ? 44.460  42.320 44.779  1.00 51.26  ? 60   ASN B ND2 1 
ATOM   3000  N N   . THR B  2 61  ? 40.867  44.962 45.774  1.00 42.97  ? 61   THR B N   1 
ATOM   3001  C CA  . THR B  2 61  ? 40.759  45.679 47.056  1.00 43.54  ? 61   THR B CA  1 
ATOM   3002  C C   . THR B  2 61  ? 39.294  46.049 47.301  1.00 40.80  ? 61   THR B C   1 
ATOM   3003  O O   . THR B  2 61  ? 38.707  46.861 46.575  1.00 39.37  ? 61   THR B O   1 
ATOM   3004  C CB  . THR B  2 61  ? 41.711  46.906 47.182  1.00 45.60  ? 61   THR B CB  1 
ATOM   3005  O OG1 . THR B  2 61  ? 41.062  47.949 47.921  1.00 44.86  ? 61   THR B OG1 1 
ATOM   3006  C CG2 . THR B  2 61  ? 42.161  47.452 45.819  1.00 45.81  ? 61   THR B CG2 1 
ATOM   3007  N N   . GLN B  2 62  ? 38.726  45.419 48.328  1.00 40.47  ? 62   GLN B N   1 
ATOM   3008  C CA  . GLN B  2 62  ? 37.290  45.443 48.600  1.00 38.19  ? 62   GLN B CA  1 
ATOM   3009  C C   . GLN B  2 62  ? 37.030  44.985 50.044  1.00 38.64  ? 62   GLN B C   1 
ATOM   3010  O O   . GLN B  2 62  ? 37.883  44.328 50.656  1.00 40.89  ? 62   GLN B O   1 
ATOM   3011  C CB  . GLN B  2 62  ? 36.562  44.550 47.583  1.00 36.99  ? 62   GLN B CB  1 
ATOM   3012  C CG  . GLN B  2 62  ? 35.483  43.630 48.147  1.00 36.53  ? 62   GLN B CG  1 
ATOM   3013  C CD  . GLN B  2 62  ? 34.838  42.768 47.080  1.00 35.91  ? 62   GLN B CD  1 
ATOM   3014  O OE1 . GLN B  2 62  ? 35.101  42.936 45.882  1.00 35.63  ? 62   GLN B OE1 1 
ATOM   3015  N NE2 . GLN B  2 62  ? 33.979  41.838 47.507  1.00 36.01  ? 62   GLN B NE2 1 
ATOM   3016  N N   . PHE B  2 63  ? 35.854  45.327 50.572  1.00 36.73  ? 63   PHE B N   1 
ATOM   3017  C CA  . PHE B  2 63  ? 35.510  45.090 51.983  1.00 36.91  ? 63   PHE B CA  1 
ATOM   3018  C C   . PHE B  2 63  ? 35.706  43.637 52.443  1.00 38.12  ? 63   PHE B C   1 
ATOM   3019  O O   . PHE B  2 63  ? 35.367  42.695 51.719  1.00 37.94  ? 63   PHE B O   1 
ATOM   3020  C CB  . PHE B  2 63  ? 34.060  45.517 52.259  1.00 34.92  ? 63   PHE B CB  1 
ATOM   3021  C CG  . PHE B  2 63  ? 33.689  45.481 53.715  1.00 35.29  ? 63   PHE B CG  1 
ATOM   3022  C CD1 . PHE B  2 63  ? 34.107  46.490 54.576  1.00 35.86  ? 63   PHE B CD1 1 
ATOM   3023  C CD2 . PHE B  2 63  ? 32.938  44.428 54.231  1.00 35.31  ? 63   PHE B CD2 1 
ATOM   3024  C CE1 . PHE B  2 63  ? 33.777  46.453 55.921  1.00 36.25  ? 63   PHE B CE1 1 
ATOM   3025  C CE2 . PHE B  2 63  ? 32.603  44.387 55.574  1.00 35.82  ? 63   PHE B CE2 1 
ATOM   3026  C CZ  . PHE B  2 63  ? 33.023  45.400 56.420  1.00 36.14  ? 63   PHE B CZ  1 
ATOM   3027  N N   . GLU B  2 64  ? 36.252  43.478 53.649  1.00 39.51  ? 64   GLU B N   1 
ATOM   3028  C CA  . GLU B  2 64  ? 36.422  42.172 54.281  1.00 41.14  ? 64   GLU B CA  1 
ATOM   3029  C C   . GLU B  2 64  ? 35.736  42.166 55.648  1.00 40.90  ? 64   GLU B C   1 
ATOM   3030  O O   . GLU B  2 64  ? 36.036  43.004 56.506  1.00 41.22  ? 64   GLU B O   1 
ATOM   3031  C CB  . GLU B  2 64  ? 37.906  41.857 54.472  1.00 44.12  ? 64   GLU B CB  1 
ATOM   3032  C CG  . GLU B  2 64  ? 38.741  41.912 53.202  1.00 44.64  ? 64   GLU B CG  1 
ATOM   3033  C CD  . GLU B  2 64  ? 40.211  41.607 53.451  1.00 48.09  ? 64   GLU B CD  1 
ATOM   3034  O OE1 . GLU B  2 64  ? 40.583  41.304 54.610  1.00 50.15  ? 64   GLU B OE1 1 
ATOM   3035  O OE2 . GLU B  2 64  ? 40.996  41.675 52.480  1.00 48.93  ? 64   GLU B OE2 1 
ATOM   3036  N N   . ALA B  2 65  ? 34.832  41.210 55.857  1.00 40.43  ? 65   ALA B N   1 
ATOM   3037  C CA  . ALA B  2 65  ? 34.106  41.101 57.122  1.00 40.28  ? 65   ALA B CA  1 
ATOM   3038  C C   . ALA B  2 65  ? 35.024  40.641 58.256  1.00 42.72  ? 65   ALA B C   1 
ATOM   3039  O O   . ALA B  2 65  ? 35.972  39.884 58.032  1.00 44.88  ? 65   ALA B O   1 
ATOM   3040  C CB  . ALA B  2 65  ? 32.926  40.150 56.979  1.00 39.97  ? 65   ALA B CB  1 
ATOM   3041  N N   . VAL B  2 66  ? 34.732  41.116 59.467  1.00 42.40  ? 66   VAL B N   1 
ATOM   3042  C CA  . VAL B  2 66  ? 35.477  40.740 60.672  1.00 44.78  ? 66   VAL B CA  1 
ATOM   3043  C C   . VAL B  2 66  ? 34.485  40.341 61.770  1.00 44.59  ? 66   VAL B C   1 
ATOM   3044  O O   . VAL B  2 66  ? 33.420  40.953 61.912  1.00 42.44  ? 66   VAL B O   1 
ATOM   3045  C CB  . VAL B  2 66  ? 36.384  41.895 61.166  1.00 45.24  ? 66   VAL B CB  1 
ATOM   3046  C CG1 . VAL B  2 66  ? 37.178  41.479 62.401  1.00 48.29  ? 66   VAL B CG1 1 
ATOM   3047  C CG2 . VAL B  2 66  ? 37.331  42.348 60.060  1.00 45.40  ? 66   VAL B CG2 1 
ATOM   3048  N N   . GLY B  2 67  ? 34.841  39.310 62.532  1.00 47.04  ? 67   GLY B N   1 
ATOM   3049  C CA  . GLY B  2 67  ? 34.007  38.821 63.623  1.00 47.45  ? 67   GLY B CA  1 
ATOM   3050  C C   . GLY B  2 67  ? 34.131  39.691 64.859  1.00 47.17  ? 67   GLY B C   1 
ATOM   3051  O O   . GLY B  2 67  ? 35.226  39.862 65.399  1.00 49.12  ? 67   GLY B O   1 
ATOM   3052  N N   . ARG B  2 68  ? 33.004  40.242 65.305  1.00 44.88  ? 68   ARG B N   1 
ATOM   3053  C CA  . ARG B  2 68  ? 32.956  41.089 66.495  1.00 44.45  ? 68   ARG B CA  1 
ATOM   3054  C C   . ARG B  2 68  ? 31.844  40.595 67.402  1.00 44.53  ? 68   ARG B C   1 
ATOM   3055  O O   . ARG B  2 68  ? 30.739  40.316 66.939  1.00 43.34  ? 68   ARG B O   1 
ATOM   3056  C CB  . ARG B  2 68  ? 32.705  42.545 66.101  1.00 41.77  ? 68   ARG B CB  1 
ATOM   3057  C CG  . ARG B  2 68  ? 33.963  43.315 65.741  1.00 42.21  ? 68   ARG B CG  1 
ATOM   3058  C CD  . ARG B  2 68  ? 33.633  44.709 65.208  1.00 39.84  ? 68   ARG B CD  1 
ATOM   3059  N NE  . ARG B  2 68  ? 34.475  45.047 64.065  1.00 39.73  ? 68   ARG B NE  1 
ATOM   3060  C CZ  . ARG B  2 68  ? 34.118  44.952 62.783  1.00 38.22  ? 68   ARG B CZ  1 
ATOM   3061  N NH1 . ARG B  2 68  ? 32.898  44.576 62.402  1.00 36.59  ? 68   ARG B NH1 1 
ATOM   3062  N NH2 . ARG B  2 68  ? 35.008  45.269 61.853  1.00 38.54  ? 68   ARG B NH2 1 
ATOM   3063  N N   . GLU B  2 69  ? 32.139  40.504 68.694  1.00 46.11  ? 69   GLU B N   1 
ATOM   3064  C CA  . GLU B  2 69  ? 31.215  39.939 69.666  1.00 46.80  ? 69   GLU B CA  1 
ATOM   3065  C C   . GLU B  2 69  ? 30.646  41.029 70.559  1.00 45.05  ? 69   GLU B C   1 
ATOM   3066  O O   . GLU B  2 69  ? 31.369  41.922 70.990  1.00 44.91  ? 69   GLU B O   1 
ATOM   3067  C CB  . GLU B  2 69  ? 31.941  38.906 70.525  1.00 50.50  ? 69   GLU B CB  1 
ATOM   3068  C CG  . GLU B  2 69  ? 32.435  37.689 69.750  1.00 52.74  ? 69   GLU B CG  1 
ATOM   3069  C CD  . GLU B  2 69  ? 31.483  36.510 69.842  1.00 54.27  ? 69   GLU B CD  1 
ATOM   3070  O OE1 . GLU B  2 69  ? 30.255  36.707 69.691  1.00 52.52  ? 69   GLU B OE1 1 
ATOM   3071  O OE2 . GLU B  2 69  ? 31.968  35.383 70.077  1.00 57.71  ? 69   GLU B OE2 1 
ATOM   3072  N N   . PHE B  2 70  ? 29.350  40.939 70.841  1.00 43.95  ? 70   PHE B N   1 
ATOM   3073  C CA  . PHE B  2 70  ? 28.665  41.890 71.713  1.00 42.57  ? 70   PHE B CA  1 
ATOM   3074  C C   . PHE B  2 70  ? 27.795  41.147 72.720  1.00 43.92  ? 70   PHE B C   1 
ATOM   3075  O O   . PHE B  2 70  ? 27.220  40.108 72.400  1.00 44.97  ? 70   PHE B O   1 
ATOM   3076  C CB  . PHE B  2 70  ? 27.801  42.837 70.880  1.00 39.78  ? 70   PHE B CB  1 
ATOM   3077  C CG  . PHE B  2 70  ? 28.535  43.482 69.739  1.00 38.43  ? 70   PHE B CG  1 
ATOM   3078  C CD1 . PHE B  2 70  ? 28.578  42.876 68.491  1.00 38.08  ? 70   PHE B CD1 1 
ATOM   3079  C CD2 . PHE B  2 70  ? 29.186  44.693 69.914  1.00 37.73  ? 70   PHE B CD2 1 
ATOM   3080  C CE1 . PHE B  2 70  ? 29.251  43.469 67.440  1.00 36.97  ? 70   PHE B CE1 1 
ATOM   3081  C CE2 . PHE B  2 70  ? 29.863  45.291 68.865  1.00 36.86  ? 70   PHE B CE2 1 
ATOM   3082  C CZ  . PHE B  2 70  ? 29.895  44.679 67.628  1.00 36.41  ? 70   PHE B CZ  1 
ATOM   3083  N N   . ASN B  2 71  ? 27.693  41.679 73.935  1.00 44.06  ? 71   ASN B N   1 
ATOM   3084  C CA  . ASN B  2 71  ? 26.890  41.031 74.972  1.00 45.54  ? 71   ASN B CA  1 
ATOM   3085  C C   . ASN B  2 71  ? 25.395  41.346 74.816  1.00 44.01  ? 71   ASN B C   1 
ATOM   3086  O O   . ASN B  2 71  ? 24.981  41.968 73.835  1.00 41.88  ? 71   ASN B O   1 
ATOM   3087  C CB  . ASN B  2 71  ? 27.430  41.348 76.385  1.00 46.82  ? 71   ASN B CB  1 
ATOM   3088  C CG  . ASN B  2 71  ? 27.134  42.768 76.843  1.00 44.80  ? 71   ASN B CG  1 
ATOM   3089  O OD1 . ASN B  2 71  ? 26.011  43.253 76.727  1.00 43.27  ? 71   ASN B OD1 1 
ATOM   3090  N ND2 . ASN B  2 71  ? 28.141  43.432 77.396  1.00 45.19  ? 71   ASN B ND2 1 
ATOM   3091  N N   . ASN B  2 72  ? 24.599  40.908 75.790  1.00 45.36  ? 72   ASN B N   1 
ATOM   3092  C CA  . ASN B  2 72  ? 23.139  40.956 75.701  1.00 44.83  ? 72   ASN B CA  1 
ATOM   3093  C C   . ASN B  2 72  ? 22.528  42.359 75.816  1.00 42.50  ? 72   ASN B C   1 
ATOM   3094  O O   . ASN B  2 72  ? 21.398  42.579 75.380  1.00 41.83  ? 72   ASN B O   1 
ATOM   3095  C CB  . ASN B  2 72  ? 22.536  40.038 76.771  1.00 47.54  ? 72   ASN B CB  1 
ATOM   3096  C CG  . ASN B  2 72  ? 21.084  39.697 76.498  1.00 48.06  ? 72   ASN B CG  1 
ATOM   3097  O OD1 . ASN B  2 72  ? 20.722  39.329 75.376  1.00 47.82  ? 72   ASN B OD1 1 
ATOM   3098  N ND2 . ASN B  2 72  ? 20.242  39.816 77.522  1.00 49.00  ? 72   ASN B ND2 1 
ATOM   3099  N N   . LEU B  2 73  ? 23.264  43.295 76.412  1.00 41.63  ? 73   LEU B N   1 
ATOM   3100  C CA  . LEU B  2 73  ? 22.823  44.686 76.509  1.00 39.76  ? 73   LEU B CA  1 
ATOM   3101  C C   . LEU B  2 73  ? 23.661  45.599 75.610  1.00 38.03  ? 73   LEU B C   1 
ATOM   3102  O O   . LEU B  2 73  ? 23.873  46.773 75.917  1.00 37.20  ? 73   LEU B O   1 
ATOM   3103  C CB  . LEU B  2 73  ? 22.867  45.146 77.964  1.00 40.49  ? 73   LEU B CB  1 
ATOM   3104  C CG  . LEU B  2 73  ? 21.779  44.529 78.852  1.00 42.00  ? 73   LEU B CG  1 
ATOM   3105  C CD1 . LEU B  2 73  ? 22.109  44.733 80.323  1.00 43.09  ? 73   LEU B CD1 1 
ATOM   3106  C CD2 . LEU B  2 73  ? 20.407  45.107 78.513  1.00 41.10  ? 73   LEU B CD2 1 
ATOM   3107  N N   . GLU B  2 74  ? 24.125  45.037 74.495  1.00 37.74  ? 74   GLU B N   1 
ATOM   3108  C CA  . GLU B  2 74  ? 24.813  45.780 73.447  1.00 36.23  ? 74   GLU B CA  1 
ATOM   3109  C C   . GLU B  2 74  ? 24.183  45.443 72.098  1.00 35.29  ? 74   GLU B C   1 
ATOM   3110  O O   . GLU B  2 74  ? 24.880  45.283 71.097  1.00 34.80  ? 74   GLU B O   1 
ATOM   3111  C CB  . GLU B  2 74  ? 26.290  45.406 73.431  1.00 37.19  ? 74   GLU B CB  1 
ATOM   3112  C CG  . GLU B  2 74  ? 27.053  45.880 74.643  1.00 38.22  ? 74   GLU B CG  1 
ATOM   3113  C CD  . GLU B  2 74  ? 28.524  45.581 74.528  1.00 39.54  ? 74   GLU B CD  1 
ATOM   3114  O OE1 . GLU B  2 74  ? 28.872  44.437 74.171  1.00 40.75  ? 74   GLU B OE1 1 
ATOM   3115  O OE2 . GLU B  2 74  ? 29.332  46.494 74.784  1.00 39.67  ? 74   GLU B OE2 1 
ATOM   3116  N N   . ARG B  2 75  ? 22.858  45.336 72.082  1.00 35.25  ? 75   ARG B N   1 
ATOM   3117  C CA  . ARG B  2 75  ? 22.135  44.880 70.899  1.00 34.89  ? 75   ARG B CA  1 
ATOM   3118  C C   . ARG B  2 75  ? 22.111  45.921 69.790  1.00 33.05  ? 75   ARG B C   1 
ATOM   3119  O O   . ARG B  2 75  ? 22.112  45.571 68.614  1.00 32.53  ? 75   ARG B O   1 
ATOM   3120  C CB  . ARG B  2 75  ? 20.702  44.478 71.261  1.00 35.97  ? 75   ARG B CB  1 
ATOM   3121  C CG  . ARG B  2 75  ? 20.596  43.182 72.050  1.00 38.25  ? 75   ARG B CG  1 
ATOM   3122  C CD  . ARG B  2 75  ? 20.739  41.971 71.139  1.00 39.25  ? 75   ARG B CD  1 
ATOM   3123  N NE  . ARG B  2 75  ? 20.841  40.715 71.889  1.00 41.89  ? 75   ARG B NE  1 
ATOM   3124  C CZ  . ARG B  2 75  ? 21.951  39.983 72.045  1.00 43.08  ? 75   ARG B CZ  1 
ATOM   3125  N NH1 . ARG B  2 75  ? 23.110  40.356 71.501  1.00 41.85  ? 75   ARG B NH1 1 
ATOM   3126  N NH2 . ARG B  2 75  ? 21.899  38.855 72.758  1.00 45.88  ? 75   ARG B NH2 1 
ATOM   3127  N N   . ARG B  2 76  ? 22.082  47.194 70.164  1.00 32.27  ? 76   ARG B N   1 
ATOM   3128  C CA  . ARG B  2 76  ? 22.074  48.274 69.182  1.00 30.97  ? 76   ARG B CA  1 
ATOM   3129  C C   . ARG B  2 76  ? 23.346  48.281 68.333  1.00 30.36  ? 76   ARG B C   1 
ATOM   3130  O O   . ARG B  2 76  ? 23.271  48.349 67.109  1.00 29.55  ? 76   ARG B O   1 
ATOM   3131  C CB  . ARG B  2 76  ? 21.911  49.625 69.872  1.00 30.82  ? 76   ARG B CB  1 
ATOM   3132  C CG  . ARG B  2 76  ? 20.537  49.870 70.462  1.00 31.41  ? 76   ARG B CG  1 
ATOM   3133  C CD  . ARG B  2 76  ? 20.564  51.126 71.314  1.00 31.57  ? 76   ARG B CD  1 
ATOM   3134  N NE  . ARG B  2 76  ? 21.492  50.975 72.435  1.00 32.02  ? 76   ARG B NE  1 
ATOM   3135  C CZ  . ARG B  2 76  ? 22.078  51.972 73.096  1.00 32.19  ? 76   ARG B CZ  1 
ATOM   3136  N NH1 . ARG B  2 76  ? 21.853  53.240 72.770  1.00 32.04  ? 76   ARG B NH1 1 
ATOM   3137  N NH2 . ARG B  2 76  ? 22.909  51.694 74.093  1.00 32.84  ? 76   ARG B NH2 1 
ATOM   3138  N N   . ILE B  2 77  ? 24.505  48.214 68.988  1.00 30.97  ? 77   ILE B N   1 
ATOM   3139  C CA  . ILE B  2 77  ? 25.787  48.205 68.276  1.00 30.89  ? 77   ILE B CA  1 
ATOM   3140  C C   . ILE B  2 77  ? 26.061  46.880 67.563  1.00 31.29  ? 77   ILE B C   1 
ATOM   3141  O O   . ILE B  2 77  ? 26.758  46.856 66.550  1.00 30.90  ? 77   ILE B O   1 
ATOM   3142  C CB  . ILE B  2 77  ? 26.985  48.592 69.177  1.00 31.88  ? 77   ILE B CB  1 
ATOM   3143  C CG1 . ILE B  2 77  ? 27.167  47.613 70.337  1.00 33.36  ? 77   ILE B CG1 1 
ATOM   3144  C CG2 . ILE B  2 77  ? 26.811  50.011 69.698  1.00 31.66  ? 77   ILE B CG2 1 
ATOM   3145  C CD1 . ILE B  2 77  ? 28.478  47.793 71.077  1.00 34.76  ? 77   ILE B CD1 1 
ATOM   3146  N N   . GLU B  2 78  ? 25.517  45.788 68.086  1.00 32.33  ? 78   GLU B N   1 
ATOM   3147  C CA  . GLU B  2 78  ? 25.562  44.508 67.391  1.00 33.07  ? 78   GLU B CA  1 
ATOM   3148  C C   . GLU B  2 78  ? 24.791  44.599 66.078  1.00 31.89  ? 78   GLU B C   1 
ATOM   3149  O O   . GLU B  2 78  ? 25.219  44.063 65.061  1.00 31.81  ? 78   GLU B O   1 
ATOM   3150  C CB  . GLU B  2 78  ? 24.977  43.400 68.269  1.00 34.85  ? 78   GLU B CB  1 
ATOM   3151  C CG  . GLU B  2 78  ? 25.085  41.995 67.692  1.00 36.26  ? 78   GLU B CG  1 
ATOM   3152  C CD  . GLU B  2 78  ? 24.715  40.929 68.710  1.00 38.65  ? 78   GLU B CD  1 
ATOM   3153  O OE1 . GLU B  2 78  ? 23.584  40.998 69.254  1.00 38.91  ? 78   GLU B OE1 1 
ATOM   3154  O OE2 . GLU B  2 78  ? 25.549  40.025 68.975  1.00 40.58  ? 78   GLU B OE2 1 
ATOM   3155  N N   . ASN B  2 79  ? 23.654  45.284 66.117  1.00 31.25  ? 79   ASN B N   1 
ATOM   3156  C CA  . ASN B  2 79  ? 22.812  45.474 64.945  1.00 30.46  ? 79   ASN B CA  1 
ATOM   3157  C C   . ASN B  2 79  ? 23.439  46.441 63.948  1.00 29.13  ? 79   ASN B C   1 
ATOM   3158  O O   . ASN B  2 79  ? 23.357  46.239 62.738  1.00 28.56  ? 79   ASN B O   1 
ATOM   3159  C CB  . ASN B  2 79  ? 21.440  45.996 65.370  1.00 30.64  ? 79   ASN B CB  1 
ATOM   3160  C CG  . ASN B  2 79  ? 20.458  46.060 64.217  1.00 30.38  ? 79   ASN B CG  1 
ATOM   3161  O OD1 . ASN B  2 79  ? 20.251  45.073 63.512  1.00 30.92  ? 79   ASN B OD1 1 
ATOM   3162  N ND2 . ASN B  2 79  ? 19.832  47.211 64.029  1.00 29.89  ? 79   ASN B ND2 1 
ATOM   3163  N N   . LEU B  2 80  ? 24.056  47.494 64.473  1.00 28.90  ? 80   LEU B N   1 
ATOM   3164  C CA  . LEU B  2 80  ? 24.785  48.464 63.662  1.00 28.15  ? 80   LEU B CA  1 
ATOM   3165  C C   . LEU B  2 80  ? 25.894  47.741 62.923  1.00 28.31  ? 80   LEU B C   1 
ATOM   3166  O O   . LEU B  2 80  ? 26.069  47.911 61.723  1.00 27.61  ? 80   LEU B O   1 
ATOM   3167  C CB  . LEU B  2 80  ? 25.376  49.560 64.556  1.00 28.45  ? 80   LEU B CB  1 
ATOM   3168  C CG  . LEU B  2 80  ? 25.911  50.853 63.933  1.00 28.14  ? 80   LEU B CG  1 
ATOM   3169  C CD1 . LEU B  2 80  ? 26.197  51.869 65.028  1.00 28.89  ? 80   LEU B CD1 1 
ATOM   3170  C CD2 . LEU B  2 80  ? 27.163  50.622 63.106  1.00 28.19  ? 80   LEU B CD2 1 
ATOM   3171  N N   . ASN B  2 81  ? 26.632  46.923 63.662  1.00 29.53  ? 81   ASN B N   1 
ATOM   3172  C CA  . ASN B  2 81  ? 27.712  46.133 63.105  1.00 30.24  ? 81   ASN B CA  1 
ATOM   3173  C C   . ASN B  2 81  ? 27.239  45.203 61.994  1.00 30.10  ? 81   ASN B C   1 
ATOM   3174  O O   . ASN B  2 81  ? 27.892  45.095 60.965  1.00 29.82  ? 81   ASN B O   1 
ATOM   3175  C CB  . ASN B  2 81  ? 28.371  45.318 64.207  1.00 31.95  ? 81   ASN B CB  1 
ATOM   3176  C CG  . ASN B  2 81  ? 29.531  44.498 63.703  1.00 33.08  ? 81   ASN B CG  1 
ATOM   3177  O OD1 . ASN B  2 81  ? 30.513  45.045 63.214  1.00 33.09  ? 81   ASN B OD1 1 
ATOM   3178  N ND2 . ASN B  2 81  ? 29.431  43.182 63.824  1.00 34.39  ? 81   ASN B ND2 1 
ATOM   3179  N N   . LYS B  2 82  ? 26.105  44.539 62.204  1.00 30.60  ? 82   LYS B N   1 
ATOM   3180  C CA  . LYS B  2 82  ? 25.560  43.622 61.208  1.00 30.88  ? 82   LYS B CA  1 
ATOM   3181  C C   . LYS B  2 82  ? 25.183  44.361 59.937  1.00 29.53  ? 82   LYS B C   1 
ATOM   3182  O O   . LYS B  2 82  ? 25.524  43.924 58.845  1.00 29.30  ? 82   LYS B O   1 
ATOM   3183  C CB  . LYS B  2 82  ? 24.336  42.866 61.741  1.00 31.98  ? 82   LYS B CB  1 
ATOM   3184  C CG  . LYS B  2 82  ? 23.629  42.032 60.670  1.00 32.38  ? 82   LYS B CG  1 
ATOM   3185  C CD  . LYS B  2 82  ? 22.722  40.946 61.248  1.00 34.40  ? 82   LYS B CD  1 
ATOM   3186  C CE  . LYS B  2 82  ? 21.267  41.399 61.369  1.00 34.42  ? 82   LYS B CE  1 
ATOM   3187  N NZ  . LYS B  2 82  ? 20.417  40.380 62.057  1.00 36.76  ? 82   LYS B NZ  1 
ATOM   3188  N N   . LYS B  2 83  ? 24.476  45.476 60.090  1.00 28.95  ? 83   LYS B N   1 
ATOM   3189  C CA  . LYS B  2 83  ? 24.029  46.265 58.941  1.00 28.05  ? 83   LYS B CA  1 
ATOM   3190  C C   . LYS B  2 83  ? 25.195  46.840 58.159  1.00 27.43  ? 83   LYS B C   1 
ATOM   3191  O O   . LYS B  2 83  ? 25.159  46.887 56.934  1.00 26.86  ? 83   LYS B O   1 
ATOM   3192  C CB  . LYS B  2 83  ? 23.064  47.375 59.381  1.00 27.99  ? 83   LYS B CB  1 
ATOM   3193  C CG  . LYS B  2 83  ? 21.589  46.977 59.326  1.00 28.72  ? 83   LYS B CG  1 
ATOM   3194  C CD  . LYS B  2 83  ? 21.337  45.545 59.803  1.00 29.93  ? 83   LYS B CD  1 
ATOM   3195  C CE  . LYS B  2 83  ? 19.913  45.080 59.530  1.00 31.00  ? 83   LYS B CE  1 
ATOM   3196  N NZ  . LYS B  2 83  ? 19.046  45.222 60.738  1.00 32.09  ? 83   LYS B NZ  1 
ATOM   3197  N N   . MET B  2 84  ? 26.226  47.271 58.872  1.00 27.85  ? 84   MET B N   1 
ATOM   3198  C CA  . MET B  2 84  ? 27.433  47.766 58.236  1.00 27.80  ? 84   MET B CA  1 
ATOM   3199  C C   . MET B  2 84  ? 28.072  46.672 57.380  1.00 28.05  ? 84   MET B C   1 
ATOM   3200  O O   . MET B  2 84  ? 28.354  46.898 56.203  1.00 27.46  ? 84   MET B O   1 
ATOM   3201  C CB  . MET B  2 84  ? 28.422  48.252 59.290  1.00 28.73  ? 84   MET B CB  1 
ATOM   3202  C CG  . MET B  2 84  ? 29.496  49.175 58.748  1.00 29.01  ? 84   MET B CG  1 
ATOM   3203  S SD  . MET B  2 84  ? 31.106  48.778 59.432  1.00 30.86  ? 84   MET B SD  1 
ATOM   3204  C CE  . MET B  2 84  ? 31.438  47.286 58.511  1.00 31.01  ? 84   MET B CE  1 
ATOM   3205  N N   . GLU B  2 85  ? 28.267  45.488 57.961  1.00 29.15  ? 85   GLU B N   1 
ATOM   3206  C CA  . GLU B  2 85  ? 28.912  44.379 57.247  1.00 29.88  ? 85   GLU B CA  1 
ATOM   3207  C C   . GLU B  2 85  ? 28.051  43.877 56.081  1.00 29.15  ? 85   GLU B C   1 
ATOM   3208  O O   . GLU B  2 85  ? 28.556  43.680 54.979  1.00 28.89  ? 85   GLU B O   1 
ATOM   3209  C CB  . GLU B  2 85  ? 29.290  43.234 58.202  1.00 31.75  ? 85   GLU B CB  1 
ATOM   3210  C CG  . GLU B  2 85  ? 30.222  43.673 59.332  1.00 32.87  ? 85   GLU B CG  1 
ATOM   3211  C CD  . GLU B  2 85  ? 31.359  42.703 59.631  1.00 35.12  ? 85   GLU B CD  1 
ATOM   3212  O OE1 . GLU B  2 85  ? 31.111  41.626 60.219  1.00 36.64  ? 85   GLU B OE1 1 
ATOM   3213  O OE2 . GLU B  2 85  ? 32.520  43.038 59.311  1.00 35.85  ? 85   GLU B OE2 1 
ATOM   3214  N N   . ASP B  2 86  ? 26.756  43.690 56.321  1.00 29.03  ? 86   ASP B N   1 
ATOM   3215  C CA  . ASP B  2 86  ? 25.812  43.318 55.257  1.00 28.60  ? 86   ASP B CA  1 
ATOM   3216  C C   . ASP B  2 86  ? 25.704  44.362 54.158  1.00 27.14  ? 86   ASP B C   1 
ATOM   3217  O O   . ASP B  2 86  ? 25.581  44.019 52.980  1.00 26.84  ? 86   ASP B O   1 
ATOM   3218  C CB  . ASP B  2 86  ? 24.410  43.083 55.829  1.00 29.22  ? 86   ASP B CB  1 
ATOM   3219  C CG  . ASP B  2 86  ? 24.169  41.645 56.196  1.00 31.02  ? 86   ASP B CG  1 
ATOM   3220  O OD1 . ASP B  2 86  ? 24.484  40.764 55.364  1.00 31.68  ? 86   ASP B OD1 1 
ATOM   3221  O OD2 . ASP B  2 86  ? 23.650  41.392 57.302  1.00 32.12  ? 86   ASP B OD2 1 
ATOM   3222  N N   . GLY B  2 87  ? 25.724  45.629 54.552  1.00 26.46  ? 87   GLY B N   1 
ATOM   3223  C CA  . GLY B  2 87  ? 25.605  46.732 53.612  1.00 25.55  ? 87   GLY B CA  1 
ATOM   3224  C C   . GLY B  2 87  ? 26.725  46.764 52.592  1.00 25.15  ? 87   GLY B C   1 
ATOM   3225  O O   . GLY B  2 87  ? 26.478  46.965 51.401  1.00 24.65  ? 87   GLY B O   1 
ATOM   3226  N N   . PHE B  2 88  ? 27.956  46.570 53.059  1.00 25.62  ? 88   PHE B N   1 
ATOM   3227  C CA  . PHE B  2 88  ? 29.117  46.556 52.176  1.00 25.63  ? 88   PHE B CA  1 
ATOM   3228  C C   . PHE B  2 88  ? 29.122  45.330 51.262  1.00 25.69  ? 88   PHE B C   1 
ATOM   3229  O O   . PHE B  2 88  ? 29.536  45.426 50.107  1.00 25.32  ? 88   PHE B O   1 
ATOM   3230  C CB  . PHE B  2 88  ? 30.419  46.624 52.977  1.00 26.71  ? 88   PHE B CB  1 
ATOM   3231  C CG  . PHE B  2 88  ? 30.759  48.003 53.468  1.00 26.89  ? 88   PHE B CG  1 
ATOM   3232  C CD1 . PHE B  2 88  ? 31.008  49.032 52.572  1.00 26.63  ? 88   PHE B CD1 1 
ATOM   3233  C CD2 . PHE B  2 88  ? 30.846  48.274 54.825  1.00 27.59  ? 88   PHE B CD2 1 
ATOM   3234  C CE1 . PHE B  2 88  ? 31.328  50.305 53.017  1.00 27.27  ? 88   PHE B CE1 1 
ATOM   3235  C CE2 . PHE B  2 88  ? 31.171  49.544 55.278  1.00 28.06  ? 88   PHE B CE2 1 
ATOM   3236  C CZ  . PHE B  2 88  ? 31.413  50.561 54.372  1.00 28.01  ? 88   PHE B CZ  1 
ATOM   3237  N N   . LEU B  2 89  ? 28.667  44.184 51.766  1.00 26.36  ? 89   LEU B N   1 
ATOM   3238  C CA  . LEU B  2 89  ? 28.545  42.993 50.925  1.00 26.79  ? 89   LEU B CA  1 
ATOM   3239  C C   . LEU B  2 89  ? 27.592  43.225 49.756  1.00 25.75  ? 89   LEU B C   1 
ATOM   3240  O O   . LEU B  2 89  ? 27.861  42.791 48.645  1.00 25.59  ? 89   LEU B O   1 
ATOM   3241  C CB  . LEU B  2 89  ? 28.055  41.793 51.728  1.00 28.16  ? 89   LEU B CB  1 
ATOM   3242  C CG  . LEU B  2 89  ? 28.990  41.246 52.807  1.00 29.77  ? 89   LEU B CG  1 
ATOM   3243  C CD1 . LEU B  2 89  ? 28.344  40.019 53.445  1.00 31.38  ? 89   LEU B CD1 1 
ATOM   3244  C CD2 . LEU B  2 89  ? 30.385  40.930 52.262  1.00 30.54  ? 89   LEU B CD2 1 
ATOM   3245  N N   . ASP B  2 90  ? 26.480  43.904 50.020  1.00 25.28  ? 90   ASP B N   1 
ATOM   3246  C CA  . ASP B  2 90  ? 25.498  44.216 48.982  1.00 24.70  ? 90   ASP B CA  1 
ATOM   3247  C C   . ASP B  2 90  ? 26.058  45.197 47.966  1.00 23.71  ? 90   ASP B C   1 
ATOM   3248  O O   . ASP B  2 90  ? 25.806  45.062 46.770  1.00 23.47  ? 90   ASP B O   1 
ATOM   3249  C CB  . ASP B  2 90  ? 24.223  44.798 49.593  1.00 24.91  ? 90   ASP B CB  1 
ATOM   3250  C CG  . ASP B  2 90  ? 23.486  43.802 50.461  1.00 26.13  ? 90   ASP B CG  1 
ATOM   3251  O OD1 . ASP B  2 90  ? 23.712  42.579 50.302  1.00 26.97  ? 90   ASP B OD1 1 
ATOM   3252  O OD2 . ASP B  2 90  ? 22.677  44.251 51.305  1.00 26.56  ? 90   ASP B OD2 1 
ATOM   3253  N N   . VAL B  2 91  ? 26.798  46.188 48.450  1.00 23.40  ? 91   VAL B N   1 
ATOM   3254  C CA  . VAL B  2 91  ? 27.449  47.160 47.578  1.00 22.90  ? 91   VAL B CA  1 
ATOM   3255  C C   . VAL B  2 91  ? 28.448  46.464 46.664  1.00 22.84  ? 91   VAL B C   1 
ATOM   3256  O O   . VAL B  2 91  ? 28.434  46.681 45.453  1.00 22.44  ? 91   VAL B O   1 
ATOM   3257  C CB  . VAL B  2 91  ? 28.167  48.264 48.384  1.00 23.27  ? 91   VAL B CB  1 
ATOM   3258  C CG1 . VAL B  2 91  ? 29.083  49.091 47.491  1.00 23.41  ? 91   VAL B CG1 1 
ATOM   3259  C CG2 . VAL B  2 91  ? 27.148  49.165 49.068  1.00 23.36  ? 91   VAL B CG2 1 
ATOM   3260  N N   . TRP B  2 92  ? 29.304  45.625 47.242  1.00 23.42  ? 92   TRP B N   1 
ATOM   3261  C CA  . TRP B  2 92  ? 30.333  44.939 46.464  1.00 23.76  ? 92   TRP B CA  1 
ATOM   3262  C C   . TRP B  2 92  ? 29.782  43.806 45.594  1.00 23.58  ? 92   TRP B C   1 
ATOM   3263  O O   . TRP B  2 92  ? 30.326  43.532 44.528  1.00 23.53  ? 92   TRP B O   1 
ATOM   3264  C CB  . TRP B  2 92  ? 31.463  44.444 47.370  1.00 25.05  ? 92   TRP B CB  1 
ATOM   3265  C CG  . TRP B  2 92  ? 32.373  45.557 47.793  1.00 25.54  ? 92   TRP B CG  1 
ATOM   3266  C CD1 . TRP B  2 92  ? 32.522  46.067 49.052  1.00 26.13  ? 92   TRP B CD1 1 
ATOM   3267  C CD2 . TRP B  2 92  ? 33.240  46.322 46.947  1.00 25.74  ? 92   TRP B CD2 1 
ATOM   3268  N NE1 . TRP B  2 92  ? 33.439  47.093 49.043  1.00 26.83  ? 92   TRP B NE1 1 
ATOM   3269  C CE2 . TRP B  2 92  ? 33.892  47.270 47.762  1.00 26.68  ? 92   TRP B CE2 1 
ATOM   3270  C CE3 . TRP B  2 92  ? 33.534  46.292 45.580  1.00 25.46  ? 92   TRP B CE3 1 
ATOM   3271  C CZ2 . TRP B  2 92  ? 34.824  48.175 47.257  1.00 27.55  ? 92   TRP B CZ2 1 
ATOM   3272  C CZ3 . TRP B  2 92  ? 34.459  47.196 45.077  1.00 26.15  ? 92   TRP B CZ3 1 
ATOM   3273  C CH2 . TRP B  2 92  ? 35.093  48.124 45.916  1.00 27.30  ? 92   TRP B CH2 1 
ATOM   3274  N N   . THR B  2 93  ? 28.704  43.162 46.035  1.00 23.70  ? 93   THR B N   1 
ATOM   3275  C CA  . THR B  2 93  ? 28.036  42.154 45.214  1.00 23.89  ? 93   THR B CA  1 
ATOM   3276  C C   . THR B  2 93  ? 27.434  42.820 43.976  1.00 22.86  ? 93   THR B C   1 
ATOM   3277  O O   . THR B  2 93  ? 27.594  42.331 42.859  1.00 22.81  ? 93   THR B O   1 
ATOM   3278  C CB  . THR B  2 93  ? 26.929  41.417 45.992  1.00 24.71  ? 93   THR B CB  1 
ATOM   3279  O OG1 . THR B  2 93  ? 27.515  40.698 47.079  1.00 25.94  ? 93   THR B OG1 1 
ATOM   3280  C CG2 . THR B  2 93  ? 26.190  40.433 45.096  1.00 25.31  ? 93   THR B CG2 1 
ATOM   3281  N N   . TYR B  2 94  ? 26.757  43.941 44.191  1.00 22.24  ? 94   TYR B N   1 
ATOM   3282  C CA  . TYR B  2 94  ? 26.133  44.699 43.113  1.00 21.64  ? 94   TYR B CA  1 
ATOM   3283  C C   . TYR B  2 94  ? 27.168  45.153 42.082  1.00 21.15  ? 94   TYR B C   1 
ATOM   3284  O O   . TYR B  2 94  ? 26.959  45.001 40.883  1.00 20.90  ? 94   TYR B O   1 
ATOM   3285  C CB  . TYR B  2 94  ? 25.389  45.903 43.703  1.00 21.57  ? 94   TYR B CB  1 
ATOM   3286  C CG  . TYR B  2 94  ? 24.993  46.969 42.709  1.00 21.34  ? 94   TYR B CG  1 
ATOM   3287  C CD1 . TYR B  2 94  ? 25.863  48.003 42.385  1.00 21.12  ? 94   TYR B CD1 1 
ATOM   3288  C CD2 . TYR B  2 94  ? 23.739  46.958 42.113  1.00 21.74  ? 94   TYR B CD2 1 
ATOM   3289  C CE1 . TYR B  2 94  ? 25.497  48.987 41.486  1.00 21.31  ? 94   TYR B CE1 1 
ATOM   3290  C CE2 . TYR B  2 94  ? 23.368  47.937 41.209  1.00 21.90  ? 94   TYR B CE2 1 
ATOM   3291  C CZ  . TYR B  2 94  ? 24.251  48.946 40.901  1.00 21.67  ? 94   TYR B CZ  1 
ATOM   3292  O OH  . TYR B  2 94  ? 23.886  49.914 40.004  1.00 22.21  ? 94   TYR B OH  1 
ATOM   3293  N N   . ASN B  2 95  ? 28.277  45.708 42.566  1.00 21.21  ? 95   ASN B N   1 
ATOM   3294  C CA  . ASN B  2 95  ? 29.386  46.137 41.712  1.00 21.16  ? 95   ASN B CA  1 
ATOM   3295  C C   . ASN B  2 95  ? 29.891  45.031 40.808  1.00 21.23  ? 95   ASN B C   1 
ATOM   3296  O O   . ASN B  2 95  ? 30.078  45.242 39.607  1.00 20.94  ? 95   ASN B O   1 
ATOM   3297  C CB  . ASN B  2 95  ? 30.552  46.648 42.561  1.00 21.84  ? 95   ASN B CB  1 
ATOM   3298  C CG  . ASN B  2 95  ? 30.264  47.990 43.202  1.00 22.00  ? 95   ASN B CG  1 
ATOM   3299  O OD1 . ASN B  2 95  ? 29.200  48.573 42.997  1.00 21.67  ? 95   ASN B OD1 1 
ATOM   3300  N ND2 . ASN B  2 95  ? 31.213  48.488 43.987  1.00 22.82  ? 95   ASN B ND2 1 
ATOM   3301  N N   . ALA B  2 96  ? 30.112  43.858 41.399  1.00 21.82  ? 96   ALA B N   1 
ATOM   3302  C CA  . ALA B  2 96  ? 30.620  42.690 40.677  1.00 22.31  ? 96   ALA B CA  1 
ATOM   3303  C C   . ALA B  2 96  ? 29.653  42.246 39.588  1.00 21.80  ? 96   ALA B C   1 
ATOM   3304  O O   . ALA B  2 96  ? 30.039  42.085 38.440  1.00 21.64  ? 96   ALA B O   1 
ATOM   3305  C CB  . ALA B  2 96  ? 30.865  41.542 41.644  1.00 23.56  ? 96   ALA B CB  1 
ATOM   3306  N N   . GLU B  2 97  ? 28.392  42.066 39.957  1.00 21.75  ? 97   GLU B N   1 
ATOM   3307  C CA  . GLU B  2 97  ? 27.384  41.561 39.028  1.00 21.77  ? 97   GLU B CA  1 
ATOM   3308  C C   . GLU B  2 97  ? 27.060  42.551 37.913  1.00 20.84  ? 97   GLU B C   1 
ATOM   3309  O O   . GLU B  2 97  ? 26.799  42.150 36.780  1.00 20.89  ? 97   GLU B O   1 
ATOM   3310  C CB  . GLU B  2 97  ? 26.108  41.187 39.784  1.00 22.48  ? 97   GLU B CB  1 
ATOM   3311  C CG  . GLU B  2 97  ? 26.309  40.040 40.761  1.00 23.79  ? 97   GLU B CG  1 
ATOM   3312  C CD  . GLU B  2 97  ? 25.026  39.594 41.425  1.00 24.87  ? 97   GLU B CD  1 
ATOM   3313  O OE1 . GLU B  2 97  ? 23.996  40.277 41.253  1.00 24.63  ? 97   GLU B OE1 1 
ATOM   3314  O OE2 . GLU B  2 97  ? 25.044  38.554 42.118  1.00 26.33  ? 97   GLU B OE2 1 
ATOM   3315  N N   . LEU B  2 98  ? 27.068  43.839 38.239  1.00 20.25  ? 98   LEU B N   1 
ATOM   3316  C CA  . LEU B  2 98  ? 26.799  44.875 37.256  1.00 19.78  ? 98   LEU B CA  1 
ATOM   3317  C C   . LEU B  2 98  ? 27.963  44.977 36.282  1.00 19.44  ? 98   LEU B C   1 
ATOM   3318  O O   . LEU B  2 98  ? 27.759  44.991 35.078  1.00 19.30  ? 98   LEU B O   1 
ATOM   3319  C CB  . LEU B  2 98  ? 26.566  46.225 37.929  1.00 19.79  ? 98   LEU B CB  1 
ATOM   3320  C CG  . LEU B  2 98  ? 26.168  47.365 36.987  1.00 19.91  ? 98   LEU B CG  1 
ATOM   3321  C CD1 . LEU B  2 98  ? 24.770  47.130 36.429  1.00 20.34  ? 98   LEU B CD1 1 
ATOM   3322  C CD2 . LEU B  2 98  ? 26.241  48.709 37.697  1.00 20.32  ? 98   LEU B CD2 1 
ATOM   3323  N N   . LEU B  2 99  ? 29.180  45.041 36.810  1.00 19.53  ? 99   LEU B N   1 
ATOM   3324  C CA  . LEU B  2 99  ? 30.374  45.137 35.976  1.00 19.61  ? 99   LEU B CA  1 
ATOM   3325  C C   . LEU B  2 99  ? 30.437  43.984 34.976  1.00 19.55  ? 99   LEU B C   1 
ATOM   3326  O O   . LEU B  2 99  ? 30.758  44.182 33.807  1.00 19.38  ? 99   LEU B O   1 
ATOM   3327  C CB  . LEU B  2 99  ? 31.643  45.139 36.840  1.00 20.32  ? 99   LEU B CB  1 
ATOM   3328  C CG  . LEU B  2 99  ? 32.976  45.371 36.112  1.00 20.95  ? 99   LEU B CG  1 
ATOM   3329  C CD1 . LEU B  2 99  ? 32.987  46.710 35.390  1.00 20.92  ? 99   LEU B CD1 1 
ATOM   3330  C CD2 . LEU B  2 99  ? 34.142  45.287 37.084  1.00 22.13  ? 99   LEU B CD2 1 
ATOM   3331  N N   . VAL B  2 100 ? 30.129  42.782 35.445  1.00 19.89  ? 100  VAL B N   1 
ATOM   3332  C CA  . VAL B  2 100 ? 30.113  41.612 34.581  1.00 20.23  ? 100  VAL B CA  1 
ATOM   3333  C C   . VAL B  2 100 ? 29.060  41.780 33.477  1.00 19.72  ? 100  VAL B C   1 
ATOM   3334  O O   . VAL B  2 100 ? 29.377  41.622 32.304  1.00 19.59  ? 100  VAL B O   1 
ATOM   3335  C CB  . VAL B  2 100 ? 29.921  40.311 35.399  1.00 21.26  ? 100  VAL B CB  1 
ATOM   3336  C CG1 . VAL B  2 100 ? 29.543  39.136 34.507  1.00 21.95  ? 100  VAL B CG1 1 
ATOM   3337  C CG2 . VAL B  2 100 ? 31.199  39.995 36.161  1.00 22.14  ? 100  VAL B CG2 1 
ATOM   3338  N N   . LEU B  2 101 ? 27.830  42.120 33.858  1.00 19.63  ? 101  LEU B N   1 
ATOM   3339  C CA  . LEU B  2 101 ? 26.749  42.398 32.897  1.00 19.57  ? 101  LEU B CA  1 
ATOM   3340  C C   . LEU B  2 101 ? 27.114  43.439 31.825  1.00 19.01  ? 101  LEU B C   1 
ATOM   3341  O O   . LEU B  2 101 ? 26.903  43.215 30.630  1.00 19.05  ? 101  LEU B O   1 
ATOM   3342  C CB  . LEU B  2 101 ? 25.499  42.879 33.638  1.00 19.91  ? 101  LEU B CB  1 
ATOM   3343  C CG  . LEU B  2 101 ? 24.319  41.916 33.785  1.00 21.02  ? 101  LEU B CG  1 
ATOM   3344  C CD1 . LEU B  2 101 ? 24.747  40.503 34.142  1.00 21.74  ? 101  LEU B CD1 1 
ATOM   3345  C CD2 . LEU B  2 101 ? 23.357  42.466 34.827  1.00 21.47  ? 101  LEU B CD2 1 
ATOM   3346  N N   . MET B  2 102 ? 27.644  44.578 32.261  1.00 18.72  ? 102  MET B N   1 
ATOM   3347  C CA  . MET B  2 102 ? 27.959  45.673 31.352  1.00 18.64  ? 102  MET B CA  1 
ATOM   3348  C C   . MET B  2 102 ? 29.121  45.340 30.424  1.00 18.50  ? 102  MET B C   1 
ATOM   3349  O O   . MET B  2 102 ? 29.072  45.624 29.223  1.00 18.52  ? 102  MET B O   1 
ATOM   3350  C CB  . MET B  2 102 ? 28.289  46.938 32.139  1.00 18.89  ? 102  MET B CB  1 
ATOM   3351  C CG  . MET B  2 102 ? 27.113  47.484 32.928  1.00 19.24  ? 102  MET B CG  1 
ATOM   3352  S SD  . MET B  2 102 ? 27.400  49.144 33.584  1.00 19.96  ? 102  MET B SD  1 
ATOM   3353  C CE  . MET B  2 102 ? 28.870  48.854 34.575  1.00 19.78  ? 102  MET B CE  1 
ATOM   3354  N N   . GLU B  2 103 ? 30.169  44.746 30.986  1.00 18.59  ? 103  GLU B N   1 
ATOM   3355  C CA  . GLU B  2 103 ? 31.367  44.442 30.224  1.00 18.80  ? 103  GLU B CA  1 
ATOM   3356  C C   . GLU B  2 103 ? 31.195  43.223 29.316  1.00 18.75  ? 103  GLU B C   1 
ATOM   3357  O O   . GLU B  2 103 ? 31.808  43.164 28.256  1.00 18.84  ? 103  GLU B O   1 
ATOM   3358  C CB  . GLU B  2 103 ? 32.563  44.276 31.162  1.00 19.45  ? 103  GLU B CB  1 
ATOM   3359  C CG  . GLU B  2 103 ? 33.034  45.582 31.806  1.00 19.85  ? 103  GLU B CG  1 
ATOM   3360  C CD  . GLU B  2 103 ? 33.474  46.646 30.804  1.00 20.23  ? 103  GLU B CD  1 
ATOM   3361  O OE1 . GLU B  2 103 ? 33.880  46.296 29.682  1.00 20.28  ? 103  GLU B OE1 1 
ATOM   3362  O OE2 . GLU B  2 103 ? 33.410  47.854 31.135  1.00 20.72  ? 103  GLU B OE2 1 
ATOM   3363  N N   . ASN B  2 104 ? 30.377  42.258 29.728  1.00 18.85  ? 104  ASN B N   1 
ATOM   3364  C CA  . ASN B  2 104 ? 29.975  41.164 28.842  1.00 19.13  ? 104  ASN B CA  1 
ATOM   3365  C C   . ASN B  2 104 ? 29.314  41.694 27.582  1.00 18.78  ? 104  ASN B C   1 
ATOM   3366  O O   . ASN B  2 104 ? 29.589  41.225 26.481  1.00 18.85  ? 104  ASN B O   1 
ATOM   3367  C CB  . ASN B  2 104 ? 28.978  40.226 29.529  1.00 19.72  ? 104  ASN B CB  1 
ATOM   3368  C CG  . ASN B  2 104 ? 29.642  39.224 30.440  1.00 20.58  ? 104  ASN B CG  1 
ATOM   3369  O OD1 . ASN B  2 104 ? 30.860  39.088 30.450  1.00 20.85  ? 104  ASN B OD1 1 
ATOM   3370  N ND2 . ASN B  2 104 ? 28.835  38.511 31.211  1.00 21.37  ? 104  ASN B ND2 1 
ATOM   3371  N N   . GLU B  2 105 ? 28.421  42.663 27.758  1.00 17.73  ? 105  GLU B N   1 
ATOM   3372  C CA  . GLU B  2 105 ? 27.738  43.272 26.630  1.00 17.59  ? 105  GLU B CA  1 
ATOM   3373  C C   . GLU B  2 105 ? 28.724  44.010 25.737  1.00 16.04  ? 105  GLU B C   1 
ATOM   3374  O O   . GLU B  2 105 ? 28.637  43.941 24.517  1.00 15.19  ? 105  GLU B O   1 
ATOM   3375  C CB  . GLU B  2 105 ? 26.654  44.232 27.103  1.00 19.82  ? 105  GLU B CB  1 
ATOM   3376  C CG  . GLU B  2 105 ? 25.617  44.511 26.031  1.00 20.62  ? 105  GLU B CG  1 
ATOM   3377  C CD  . GLU B  2 105 ? 24.388  45.177 26.597  1.00 23.69  ? 105  GLU B CD  1 
ATOM   3378  O OE1 . GLU B  2 105 ? 24.558  46.202 27.298  1.00 24.84  ? 105  GLU B OE1 1 
ATOM   3379  O OE2 . GLU B  2 105 ? 23.262  44.667 26.357  1.00 25.46  ? 105  GLU B OE2 1 
ATOM   3380  N N   . ARG B  2 106 ? 29.663  44.717 26.347  1.00 16.11  ? 106  ARG B N   1 
ATOM   3381  C CA  . ARG B  2 106 ? 30.697  45.388 25.573  1.00 15.32  ? 106  ARG B CA  1 
ATOM   3382  C C   . ARG B  2 106 ? 31.624  44.402 24.859  1.00 13.71  ? 106  ARG B C   1 
ATOM   3383  O O   . ARG B  2 106 ? 32.070  44.677 23.753  1.00 13.07  ? 106  ARG B O   1 
ATOM   3384  C CB  . ARG B  2 106 ? 31.513  46.327 26.450  1.00 16.52  ? 106  ARG B CB  1 
ATOM   3385  C CG  . ARG B  2 106 ? 30.742  47.544 26.926  1.00 18.56  ? 106  ARG B CG  1 
ATOM   3386  C CD  . ARG B  2 106 ? 31.665  48.742 27.066  1.00 19.98  ? 106  ARG B CD  1 
ATOM   3387  N NE  . ARG B  2 106 ? 31.608  49.654 25.911  1.00 20.53  ? 106  ARG B NE  1 
ATOM   3388  C CZ  . ARG B  2 106 ? 32.632  50.394 25.475  1.00 21.42  ? 106  ARG B CZ  1 
ATOM   3389  N NH1 . ARG B  2 106 ? 33.829  50.324 26.057  1.00 21.83  ? 106  ARG B NH1 1 
ATOM   3390  N NH2 . ARG B  2 106 ? 32.470  51.214 24.433  1.00 22.37  ? 106  ARG B NH2 1 
ATOM   3391  N N   . THR B  2 107 ? 31.899  43.260 25.482  1.00 13.48  ? 107  THR B N   1 
ATOM   3392  C CA  . THR B  2 107 ? 32.761  42.241 24.883  1.00 12.59  ? 107  THR B CA  1 
ATOM   3393  C C   . THR B  2 107 ? 32.141  41.648 23.617  1.00 11.75  ? 107  THR B C   1 
ATOM   3394  O O   . THR B  2 107 ? 32.823  41.480 22.616  1.00 11.09  ? 107  THR B O   1 
ATOM   3395  C CB  . THR B  2 107 ? 33.089  41.109 25.881  1.00 13.28  ? 107  THR B CB  1 
ATOM   3396  O OG1 . THR B  2 107 ? 33.882  41.628 26.951  1.00 14.22  ? 107  THR B OG1 1 
ATOM   3397  C CG2 . THR B  2 107 ? 33.867  39.994 25.206  1.00 13.00  ? 107  THR B CG2 1 
ATOM   3398  N N   . LEU B  2 108 ? 30.851  41.341 23.656  1.00 12.17  ? 108  LEU B N   1 
ATOM   3399  C CA  . LEU B  2 108 ? 30.176  40.806 22.478  1.00 11.90  ? 108  LEU B CA  1 
ATOM   3400  C C   . LEU B  2 108 ? 30.166  41.819 21.329  1.00 11.34  ? 108  LEU B C   1 
ATOM   3401  O O   . LEU B  2 108 ? 30.416  41.468 20.176  1.00 10.77  ? 108  LEU B O   1 
ATOM   3402  C CB  . LEU B  2 108 ? 28.751  40.378 22.824  1.00 13.28  ? 108  LEU B CB  1 
ATOM   3403  C CG  . LEU B  2 108 ? 28.611  39.294 23.897  1.00 14.46  ? 108  LEU B CG  1 
ATOM   3404  C CD1 . LEU B  2 108 ? 27.171  38.821 23.948  1.00 16.41  ? 108  LEU B CD1 1 
ATOM   3405  C CD2 . LEU B  2 108 ? 29.544  38.118 23.658  1.00 14.15  ? 108  LEU B CD2 1 
ATOM   3406  N N   . ASP B  2 109 ? 29.891  43.075 21.659  1.00 11.90  ? 109  ASP B N   1 
ATOM   3407  C CA  . ASP B  2 109 ? 29.901  44.147 20.674  1.00 12.00  ? 109  ASP B CA  1 
ATOM   3408  C C   . ASP B  2 109 ? 31.301  44.420 20.122  1.00 11.30  ? 109  ASP B C   1 
ATOM   3409  O O   . ASP B  2 109 ? 31.443  44.813 18.974  1.00 11.32  ? 109  ASP B O   1 
ATOM   3410  C CB  . ASP B  2 109 ? 29.335  45.422 21.288  1.00 13.48  ? 109  ASP B CB  1 
ATOM   3411  C CG  . ASP B  2 109 ? 27.845  45.330 21.570  1.00 14.90  ? 109  ASP B CG  1 
ATOM   3412  O OD1 . ASP B  2 109 ? 27.123  44.614 20.831  1.00 14.97  ? 109  ASP B OD1 1 
ATOM   3413  O OD2 . ASP B  2 109 ? 27.395  46.011 22.528  1.00 16.42  ? 109  ASP B OD2 1 
ATOM   3414  N N   . PHE B  2 110 ? 32.321  44.233 20.952  1.00 11.15  ? 110  PHE B N   1 
ATOM   3415  C CA  . PHE B  2 110 ? 33.717  44.385 20.542  1.00 11.14  ? 110  PHE B CA  1 
ATOM   3416  C C   . PHE B  2 110 ? 34.044  43.377 19.436  1.00 10.40  ? 110  PHE B C   1 
ATOM   3417  O O   . PHE B  2 110 ? 34.640  43.725 18.419  1.00 10.66  ? 110  PHE B O   1 
ATOM   3418  C CB  . PHE B  2 110 ? 34.622  44.193 21.767  1.00 11.65  ? 110  PHE B CB  1 
ATOM   3419  C CG  . PHE B  2 110 ? 36.097  44.240 21.472  1.00 12.35  ? 110  PHE B CG  1 
ATOM   3420  C CD1 . PHE B  2 110 ? 36.677  45.355 20.890  1.00 13.47  ? 110  PHE B CD1 1 
ATOM   3421  C CD2 . PHE B  2 110 ? 36.918  43.182 21.830  1.00 12.55  ? 110  PHE B CD2 1 
ATOM   3422  C CE1 . PHE B  2 110 ? 38.042  45.396 20.641  1.00 14.77  ? 110  PHE B CE1 1 
ATOM   3423  C CE2 . PHE B  2 110 ? 38.281  43.220 21.588  1.00 13.84  ? 110  PHE B CE2 1 
ATOM   3424  C CZ  . PHE B  2 110 ? 38.845  44.325 20.989  1.00 14.97  ? 110  PHE B CZ  1 
ATOM   3425  N N   . HIS B  2 111 ? 33.635  42.131 19.637  1.00 9.92   ? 111  HIS B N   1 
ATOM   3426  C CA  . HIS B  2 111 ? 33.795  41.095 18.629  1.00 9.66   ? 111  HIS B CA  1 
ATOM   3427  C C   . HIS B  2 111 ? 33.029  41.432 17.351  1.00 9.51   ? 111  HIS B C   1 
ATOM   3428  O O   . HIS B  2 111 ? 33.518  41.209 16.247  1.00 9.59   ? 111  HIS B O   1 
ATOM   3429  C CB  . HIS B  2 111 ? 33.321  39.745 19.170  1.00 9.86   ? 111  HIS B CB  1 
ATOM   3430  C CG  . HIS B  2 111 ? 34.246  39.141 20.181  1.00 10.45  ? 111  HIS B CG  1 
ATOM   3431  N ND1 . HIS B  2 111 ? 35.540  38.774 19.877  1.00 11.02  ? 111  HIS B ND1 1 
ATOM   3432  C CD2 . HIS B  2 111 ? 34.061  38.824 21.484  1.00 11.00  ? 111  HIS B CD2 1 
ATOM   3433  C CE1 . HIS B  2 111 ? 36.114  38.270 20.954  1.00 11.94  ? 111  HIS B CE1 1 
ATOM   3434  N NE2 . HIS B  2 111 ? 35.238  38.289 21.942  1.00 11.85  ? 111  HIS B NE2 1 
ATOM   3435  N N   . ASP B  2 112 ? 31.823  41.963 17.512  1.00 9.70   ? 112  ASP B N   1 
ATOM   3436  C CA  . ASP B  2 112 ? 30.994  42.350 16.379  1.00 10.07  ? 112  ASP B CA  1 
ATOM   3437  C C   . ASP B  2 112 ? 31.675  43.468 15.580  1.00 10.42  ? 112  ASP B C   1 
ATOM   3438  O O   . ASP B  2 112 ? 31.688  43.450 14.353  1.00 10.68  ? 112  ASP B O   1 
ATOM   3439  C CB  . ASP B  2 112 ? 29.625  42.806 16.888  1.00 10.90  ? 112  ASP B CB  1 
ATOM   3440  C CG  . ASP B  2 112 ? 28.586  42.886 15.794  1.00 11.82  ? 112  ASP B CG  1 
ATOM   3441  O OD1 . ASP B  2 112 ? 28.848  42.430 14.664  1.00 11.64  ? 112  ASP B OD1 1 
ATOM   3442  O OD2 . ASP B  2 112 ? 27.495  43.409 16.077  1.00 13.10  ? 112  ASP B OD2 1 
ATOM   3443  N N   . SER B  2 113 ? 32.251  44.427 16.299  1.00 10.82  ? 113  SER B N   1 
ATOM   3444  C CA  . SER B  2 113 ? 32.994  45.528 15.707  1.00 11.82  ? 113  SER B CA  1 
ATOM   3445  C C   . SER B  2 113 ? 34.227  45.051 14.925  1.00 11.89  ? 113  SER B C   1 
ATOM   3446  O O   . SER B  2 113 ? 34.507  45.546 13.831  1.00 12.83  ? 113  SER B O   1 
ATOM   3447  C CB  . SER B  2 113 ? 33.422  46.501 16.808  1.00 12.68  ? 113  SER B CB  1 
ATOM   3448  O OG  . SER B  2 113 ? 34.388  47.418 16.345  1.00 14.14  ? 113  SER B OG  1 
ATOM   3449  N N   . ASN B  2 114 ? 34.967  44.108 15.498  1.00 11.38  ? 114  ASN B N   1 
ATOM   3450  C CA  . ASN B  2 114 ? 36.171  43.582 14.860  1.00 11.99  ? 114  ASN B CA  1 
ATOM   3451  C C   . ASN B  2 114 ? 35.875  42.886 13.533  1.00 11.89  ? 114  ASN B C   1 
ATOM   3452  O O   . ASN B  2 114 ? 36.636  43.021 12.582  1.00 12.95  ? 114  ASN B O   1 
ATOM   3453  C CB  . ASN B  2 114 ? 36.893  42.605 15.794  1.00 11.89  ? 114  ASN B CB  1 
ATOM   3454  C CG  . ASN B  2 114 ? 37.497  43.288 17.004  1.00 12.61  ? 114  ASN B CG  1 
ATOM   3455  O OD1 . ASN B  2 114 ? 37.886  44.450 16.951  1.00 13.77  ? 114  ASN B OD1 1 
ATOM   3456  N ND2 . ASN B  2 114 ? 37.582  42.560 18.104  1.00 12.36  ? 114  ASN B ND2 1 
ATOM   3457  N N   . VAL B  2 115 ? 34.777  42.140 13.490  1.00 11.06  ? 115  VAL B N   1 
ATOM   3458  C CA  . VAL B  2 115 ? 34.339  41.456 12.275  1.00 11.30  ? 115  VAL B CA  1 
ATOM   3459  C C   . VAL B  2 115 ? 33.959  42.480 11.207  1.00 12.09  ? 115  VAL B C   1 
ATOM   3460  O O   . VAL B  2 115 ? 34.315  42.339 10.033  1.00 12.94  ? 115  VAL B O   1 
ATOM   3461  C CB  . VAL B  2 115 ? 33.121  40.543 12.551  1.00 10.85  ? 115  VAL B CB  1 
ATOM   3462  C CG1 . VAL B  2 115 ? 32.546  39.993 11.254  1.00 11.52  ? 115  VAL B CG1 1 
ATOM   3463  C CG2 . VAL B  2 115 ? 33.495  39.395 13.482  1.00 10.69  ? 115  VAL B CG2 1 
ATOM   3464  N N   . LYS B  2 116 ? 33.226  43.505 11.630  1.00 12.24  ? 116  LYS B N   1 
ATOM   3465  C CA  . LYS B  2 116 ? 32.786  44.585 10.749  1.00 13.51  ? 116  LYS B CA  1 
ATOM   3466  C C   . LYS B  2 116 ? 33.972  45.325 10.140  1.00 14.84  ? 116  LYS B C   1 
ATOM   3467  O O   . LYS B  2 116 ? 33.999  45.609 8.943   1.00 16.08  ? 116  LYS B O   1 
ATOM   3468  C CB  . LYS B  2 116 ? 31.945  45.580 11.545  1.00 13.95  ? 116  LYS B CB  1 
ATOM   3469  C CG  . LYS B  2 116 ? 30.677  46.022 10.862  1.00 15.16  ? 116  LYS B CG  1 
ATOM   3470  C CD  . LYS B  2 116 ? 30.950  46.931 9.688   1.00 16.97  ? 116  LYS B CD  1 
ATOM   3471  C CE  . LYS B  2 116 ? 29.706  47.093 8.833   1.00 18.41  ? 116  LYS B CE  1 
ATOM   3472  N NZ  . LYS B  2 116 ? 28.755  48.030 9.482   1.00 19.82  ? 116  LYS B NZ  1 
ATOM   3473  N N   . ASN B  2 117 ? 34.946  45.651 10.980  1.00 15.05  ? 117  ASN B N   1 
ATOM   3474  C CA  . ASN B  2 117 ? 36.111  46.399 10.546  1.00 16.99  ? 117  ASN B CA  1 
ATOM   3475  C C   . ASN B  2 117 ? 36.973  45.586 9.587   1.00 17.59  ? 117  ASN B C   1 
ATOM   3476  O O   . ASN B  2 117 ? 37.537  46.124 8.630   1.00 19.64  ? 117  ASN B O   1 
ATOM   3477  C CB  . ASN B  2 117 ? 36.922  46.858 11.756  1.00 17.48  ? 117  ASN B CB  1 
ATOM   3478  C CG  . ASN B  2 117 ? 36.190  47.897 12.587  1.00 17.79  ? 117  ASN B CG  1 
ATOM   3479  O OD1 . ASN B  2 117 ? 35.244  48.535 12.120  1.00 18.37  ? 117  ASN B OD1 1 
ATOM   3480  N ND2 . ASN B  2 117 ? 36.637  48.085 13.821  1.00 17.87  ? 117  ASN B ND2 1 
ATOM   3481  N N   . LEU B  2 118 ? 37.051  44.287 9.839   1.00 16.28  ? 118  LEU B N   1 
ATOM   3482  C CA  . LEU B  2 118 ? 37.751  43.375 8.947   1.00 17.11  ? 118  LEU B CA  1 
ATOM   3483  C C   . LEU B  2 118 ? 37.011  43.254 7.613   1.00 17.46  ? 118  LEU B C   1 
ATOM   3484  O O   . LEU B  2 118 ? 37.630  43.202 6.550   1.00 19.14  ? 118  LEU B O   1 
ATOM   3485  C CB  . LEU B  2 118 ? 37.889  42.000 9.605   1.00 16.07  ? 118  LEU B CB  1 
ATOM   3486  C CG  . LEU B  2 118 ? 38.602  40.915 8.805   1.00 17.30  ? 118  LEU B CG  1 
ATOM   3487  C CD1 . LEU B  2 118 ? 39.972  41.389 8.351   1.00 19.77  ? 118  LEU B CD1 1 
ATOM   3488  C CD2 . LEU B  2 118 ? 38.709  39.649 9.635   1.00 16.77  ? 118  LEU B CD2 1 
ATOM   3489  N N   . TYR B  2 119 ? 35.684  43.219 7.674   1.00 16.30  ? 119  TYR B N   1 
ATOM   3490  C CA  . TYR B  2 119 ? 34.878  43.147 6.466   1.00 16.98  ? 119  TYR B CA  1 
ATOM   3491  C C   . TYR B  2 119 ? 35.061  44.391 5.612   1.00 18.95  ? 119  TYR B C   1 
ATOM   3492  O O   . TYR B  2 119 ? 35.246  44.296 4.402   1.00 20.46  ? 119  TYR B O   1 
ATOM   3493  C CB  . TYR B  2 119 ? 33.404  42.970 6.810   1.00 15.98  ? 119  TYR B CB  1 
ATOM   3494  C CG  . TYR B  2 119 ? 32.506  42.993 5.598   1.00 17.17  ? 119  TYR B CG  1 
ATOM   3495  C CD1 . TYR B  2 119 ? 32.372  41.865 4.790   1.00 17.63  ? 119  TYR B CD1 1 
ATOM   3496  C CD2 . TYR B  2 119 ? 31.794  44.137 5.251   1.00 18.32  ? 119  TYR B CD2 1 
ATOM   3497  C CE1 . TYR B  2 119 ? 31.547  41.874 3.677   1.00 19.06  ? 119  TYR B CE1 1 
ATOM   3498  C CE2 . TYR B  2 119 ? 30.971  44.157 4.136   1.00 19.84  ? 119  TYR B CE2 1 
ATOM   3499  C CZ  . TYR B  2 119 ? 30.851  43.021 3.354   1.00 20.15  ? 119  TYR B CZ  1 
ATOM   3500  O OH  . TYR B  2 119 ? 30.040  43.015 2.247   1.00 21.96  ? 119  TYR B OH  1 
ATOM   3501  N N   . ASP B  2 120 ? 35.002  45.557 6.244   1.00 19.35  ? 120  ASP B N   1 
ATOM   3502  C CA  . ASP B  2 120 ? 35.153  46.815 5.532   1.00 21.79  ? 120  ASP B CA  1 
ATOM   3503  C C   . ASP B  2 120 ? 36.564  46.959 4.958   1.00 23.82  ? 120  ASP B C   1 
ATOM   3504  O O   . ASP B  2 120 ? 36.740  47.481 3.860   1.00 26.19  ? 120  ASP B O   1 
ATOM   3505  C CB  . ASP B  2 120 ? 34.830  47.995 6.456   1.00 22.27  ? 120  ASP B CB  1 
ATOM   3506  C CG  . ASP B  2 120 ? 33.354  48.070 6.831   1.00 21.38  ? 120  ASP B CG  1 
ATOM   3507  O OD1 . ASP B  2 120 ? 32.485  47.713 6.002   1.00 21.63  ? 120  ASP B OD1 1 
ATOM   3508  O OD2 . ASP B  2 120 ? 33.060  48.515 7.958   1.00 20.90  ? 120  ASP B OD2 1 
ATOM   3509  N N   . LYS B  2 121 ? 37.560  46.500 5.707   1.00 23.36  ? 121  LYS B N   1 
ATOM   3510  C CA  . LYS B  2 121 ? 38.958  46.527 5.268   1.00 25.78  ? 121  LYS B CA  1 
ATOM   3511  C C   . LYS B  2 121 ? 39.103  45.856 3.910   1.00 26.92  ? 121  LYS B C   1 
ATOM   3512  O O   . LYS B  2 121 ? 39.751  46.384 3.014   1.00 29.90  ? 121  LYS B O   1 
ATOM   3513  C CB  . LYS B  2 121 ? 39.832  45.812 6.299   1.00 25.02  ? 121  LYS B CB  1 
ATOM   3514  C CG  . LYS B  2 121 ? 41.331  45.892 6.073   1.00 28.06  ? 121  LYS B CG  1 
ATOM   3515  C CD  . LYS B  2 121 ? 42.057  45.107 7.164   1.00 27.45  ? 121  LYS B CD  1 
ATOM   3516  C CE  . LYS B  2 121 ? 43.513  45.526 7.331   1.00 31.03  ? 121  LYS B CE  1 
ATOM   3517  N NZ  . LYS B  2 121 ? 44.425  44.857 6.361   1.00 33.67  ? 121  LYS B NZ  1 
ATOM   3518  N N   . VAL B  2 122 ? 38.480  44.692 3.771   1.00 24.98  ? 122  VAL B N   1 
ATOM   3519  C CA  . VAL B  2 122 ? 38.456  43.965 2.516   1.00 26.05  ? 122  VAL B CA  1 
ATOM   3520  C C   . VAL B  2 122 ? 37.634  44.717 1.469   1.00 27.33  ? 122  VAL B C   1 
ATOM   3521  O O   . VAL B  2 122 ? 38.089  44.923 0.343   1.00 29.92  ? 122  VAL B O   1 
ATOM   3522  C CB  . VAL B  2 122 ? 37.909  42.542 2.730   1.00 24.07  ? 122  VAL B CB  1 
ATOM   3523  C CG1 . VAL B  2 122 ? 37.611  41.850 1.405   1.00 25.34  ? 122  VAL B CG1 1 
ATOM   3524  C CG2 . VAL B  2 122 ? 38.907  41.737 3.545   1.00 23.88  ? 122  VAL B CG2 1 
ATOM   3525  N N   . ARG B  2 123 ? 36.434  45.137 1.845   1.00 25.97  ? 123  ARG B N   1 
ATOM   3526  C CA  . ARG B  2 123 ? 35.557  45.866 0.938   1.00 27.53  ? 123  ARG B CA  1 
ATOM   3527  C C   . ARG B  2 123 ? 36.272  47.060 0.310   1.00 30.81  ? 123  ARG B C   1 
ATOM   3528  O O   . ARG B  2 123 ? 36.163  47.292 -0.898  1.00 33.17  ? 123  ARG B O   1 
ATOM   3529  C CB  . ARG B  2 123 ? 34.316  46.349 1.686   1.00 26.19  ? 123  ARG B CB  1 
ATOM   3530  C CG  . ARG B  2 123 ? 33.227  46.908 0.788   1.00 27.94  ? 123  ARG B CG  1 
ATOM   3531  C CD  . ARG B  2 123 ? 32.041  47.412 1.595   1.00 27.25  ? 123  ARG B CD  1 
ATOM   3532  N NE  . ARG B  2 123 ? 32.448  48.308 2.680   1.00 27.05  ? 123  ARG B NE  1 
ATOM   3533  C CZ  . ARG B  2 123 ? 32.832  49.577 2.525   1.00 29.57  ? 123  ARG B CZ  1 
ATOM   3534  N NH1 . ARG B  2 123 ? 32.883  50.149 1.323   1.00 32.53  ? 123  ARG B NH1 1 
ATOM   3535  N NH2 . ARG B  2 123 ? 33.182  50.284 3.591   1.00 29.53  ? 123  ARG B NH2 1 
ATOM   3536  N N   . LEU B  2 124 ? 37.004  47.805 1.138   1.00 31.41  ? 124  LEU B N   1 
ATOM   3537  C CA  . LEU B  2 124 ? 37.710  49.013 0.696   1.00 35.14  ? 124  LEU B CA  1 
ATOM   3538  C C   . LEU B  2 124 ? 38.879  48.721 -0.256  1.00 37.95  ? 124  LEU B C   1 
ATOM   3539  O O   . LEU B  2 124 ? 39.241  49.572 -1.068  1.00 41.62  ? 124  LEU B O   1 
ATOM   3540  C CB  . LEU B  2 124 ? 38.203  49.817 1.908   1.00 35.36  ? 124  LEU B CB  1 
ATOM   3541  C CG  . LEU B  2 124 ? 37.104  50.451 2.776   1.00 33.97  ? 124  LEU B CG  1 
ATOM   3542  C CD1 . LEU B  2 124 ? 37.627  50.831 4.159   1.00 33.41  ? 124  LEU B CD1 1 
ATOM   3543  C CD2 . LEU B  2 124 ? 36.483  51.657 2.084   1.00 37.07  ? 124  LEU B CD2 1 
ATOM   3544  N N   . GLN B  2 125 ? 39.467  47.531 -0.146  1.00 36.77  ? 125  GLN B N   1 
ATOM   3545  C CA  . GLN B  2 125 ? 40.511  47.096 -1.072  1.00 39.66  ? 125  GLN B CA  1 
ATOM   3546  C C   . GLN B  2 125 ? 39.920  46.727 -2.417  1.00 40.65  ? 125  GLN B C   1 
ATOM   3547  O O   . GLN B  2 125 ? 40.388  47.185 -3.457  1.00 44.28  ? 125  GLN B O   1 
ATOM   3548  C CB  . GLN B  2 125 ? 41.248  45.873 -0.535  1.00 38.44  ? 125  GLN B CB  1 
ATOM   3549  C CG  . GLN B  2 125 ? 42.118  46.135 0.675   1.00 38.55  ? 125  GLN B CG  1 
ATOM   3550  C CD  . GLN B  2 125 ? 42.839  44.883 1.120   1.00 37.97  ? 125  GLN B CD  1 
ATOM   3551  O OE1 . GLN B  2 125 ? 43.729  44.398 0.426   1.00 40.84  ? 125  GLN B OE1 1 
ATOM   3552  N NE2 . GLN B  2 125 ? 42.457  44.348 2.275   1.00 34.75  ? 125  GLN B NE2 1 
ATOM   3553  N N   . LEU B  2 126 ? 38.896  45.882 -2.386  1.00 37.86  ? 126  LEU B N   1 
ATOM   3554  C CA  . LEU B  2 126 ? 38.310  45.350 -3.608  1.00 38.86  ? 126  LEU B CA  1 
ATOM   3555  C C   . LEU B  2 126 ? 37.591  46.418 -4.418  1.00 41.10  ? 126  LEU B C   1 
ATOM   3556  O O   . LEU B  2 126 ? 37.652  46.402 -5.638  1.00 43.84  ? 126  LEU B O   1 
ATOM   3557  C CB  . LEU B  2 126 ? 37.363  44.187 -3.294  1.00 35.78  ? 126  LEU B CB  1 
ATOM   3558  C CG  . LEU B  2 126 ? 37.969  43.013 -2.513  1.00 34.01  ? 126  LEU B CG  1 
ATOM   3559  C CD1 . LEU B  2 126 ? 37.053  41.800 -2.568  1.00 32.36  ? 126  LEU B CD1 1 
ATOM   3560  C CD2 . LEU B  2 126 ? 39.351  42.659 -3.035  1.00 36.72  ? 126  LEU B CD2 1 
ATOM   3561  N N   . ARG B  2 127 ? 36.927  47.352 -3.743  1.00 40.46  ? 127  ARG B N   1 
ATOM   3562  C CA  . ARG B  2 127 ? 36.207  48.434 -4.422  1.00 43.07  ? 127  ARG B CA  1 
ATOM   3563  C C   . ARG B  2 127 ? 35.226  47.840 -5.449  1.00 43.57  ? 127  ARG B C   1 
ATOM   3564  O O   . ARG B  2 127 ? 34.468  46.932 -5.102  1.00 40.89  ? 127  ARG B O   1 
ATOM   3565  C CB  . ARG B  2 127 ? 37.201  49.456 -5.015  1.00 47.38  ? 127  ARG B CB  1 
ATOM   3566  C CG  . ARG B  2 127 ? 37.831  50.341 -3.945  1.00 47.72  ? 127  ARG B CG  1 
ATOM   3567  C CD  . ARG B  2 127 ? 39.318  50.637 -4.143  1.00 51.03  ? 127  ARG B CD  1 
ATOM   3568  N NE  . ARG B  2 127 ? 39.778  51.344 -5.354  1.00 56.18  ? 127  ARG B NE  1 
ATOM   3569  C CZ  . ARG B  2 127 ? 39.115  52.250 -6.085  1.00 59.06  ? 127  ARG B CZ  1 
ATOM   3570  N NH1 . ARG B  2 127 ? 37.877  52.647 -5.801  1.00 57.60  ? 127  ARG B NH1 1 
ATOM   3571  N NH2 . ARG B  2 127 ? 39.723  52.784 -7.143  1.00 64.10  ? 127  ARG B NH2 1 
ATOM   3572  N N   . ASP B  2 128 ? 35.242  48.310 -6.695  1.00 47.31  ? 128  ASP B N   1 
ATOM   3573  C CA  . ASP B  2 128 ? 34.298  47.821 -7.702  1.00 48.31  ? 128  ASP B CA  1 
ATOM   3574  C C   . ASP B  2 128 ? 34.847  46.646 -8.529  1.00 48.82  ? 128  ASP B C   1 
ATOM   3575  O O   . ASP B  2 128 ? 34.294  46.319 -9.579  1.00 50.70  ? 128  ASP B O   1 
ATOM   3576  C CB  . ASP B  2 128 ? 33.852  48.971 -8.622  1.00 52.50  ? 128  ASP B CB  1 
ATOM   3577  C CG  . ASP B  2 128 ? 34.989  49.540 -9.458  1.00 56.52  ? 128  ASP B CG  1 
ATOM   3578  O OD1 . ASP B  2 128 ? 36.153  49.139 -9.247  1.00 56.23  ? 128  ASP B OD1 1 
ATOM   3579  O OD2 . ASP B  2 128 ? 34.715  50.393 -10.331 1.00 60.53  ? 128  ASP B OD2 1 
ATOM   3580  N N   . ASN B  2 129 ? 35.927  46.018 -8.061  1.00 47.61  ? 129  ASN B N   1 
ATOM   3581  C CA  . ASN B  2 129 ? 36.483  44.824 -8.715  1.00 48.28  ? 129  ASN B CA  1 
ATOM   3582  C C   . ASN B  2 129 ? 35.821  43.506 -8.276  1.00 45.23  ? 129  ASN B C   1 
ATOM   3583  O O   . ASN B  2 129 ? 36.217  42.433 -8.745  1.00 45.94  ? 129  ASN B O   1 
ATOM   3584  C CB  . ASN B  2 129 ? 38.002  44.737 -8.488  1.00 49.45  ? 129  ASN B CB  1 
ATOM   3585  C CG  . ASN B  2 129 ? 38.796  45.654 -9.410  1.00 54.11  ? 129  ASN B CG  1 
ATOM   3586  O OD1 . ASN B  2 129 ? 38.250  46.557 -10.054 1.00 56.33  ? 129  ASN B OD1 1 
ATOM   3587  N ND2 . ASN B  2 129 ? 40.103  45.419 -9.476  1.00 56.18  ? 129  ASN B ND2 1 
ATOM   3588  N N   . ALA B  2 130 ? 34.820  43.586 -7.393  1.00 42.36  ? 130  ALA B N   1 
ATOM   3589  C CA  . ALA B  2 130 ? 34.061  42.408 -6.959  1.00 40.04  ? 130  ALA B CA  1 
ATOM   3590  C C   . ALA B  2 130 ? 32.625  42.778 -6.600  1.00 38.99  ? 130  ALA B C   1 
ATOM   3591  O O   . ALA B  2 130 ? 32.353  43.916 -6.239  1.00 39.02  ? 130  ALA B O   1 
ATOM   3592  C CB  . ALA B  2 130 ? 34.743  41.760 -5.767  1.00 37.40  ? 130  ALA B CB  1 
ATOM   3593  N N   . LYS B  2 131 ? 31.716  41.809 -6.699  1.00 38.62  ? 131  LYS B N   1 
ATOM   3594  C CA  . LYS B  2 131 ? 30.314  41.993 -6.310  1.00 38.12  ? 131  LYS B CA  1 
ATOM   3595  C C   . LYS B  2 131 ? 30.148  41.804 -4.805  1.00 34.88  ? 131  LYS B C   1 
ATOM   3596  O O   . LYS B  2 131 ? 30.521  40.765 -4.271  1.00 33.33  ? 131  LYS B O   1 
ATOM   3597  C CB  . LYS B  2 131 ? 29.419  40.971 -7.013  1.00 39.78  ? 131  LYS B CB  1 
ATOM   3598  C CG  . LYS B  2 131 ? 29.422  41.028 -8.533  1.00 43.35  ? 131  LYS B CG  1 
ATOM   3599  C CD  . LYS B  2 131 ? 28.838  39.743 -9.119  1.00 44.97  ? 131  LYS B CD  1 
ATOM   3600  C CE  . LYS B  2 131 ? 28.247  39.930 -10.512 1.00 48.90  ? 131  LYS B CE  1 
ATOM   3601  N NZ  . LYS B  2 131 ? 27.019  40.785 -10.499 1.00 50.16  ? 131  LYS B NZ  1 
ATOM   3602  N N   . GLU B  2 132 ? 29.586  42.800 -4.125  1.00 34.24  ? 132  GLU B N   1 
ATOM   3603  C CA  . GLU B  2 132 ? 29.250  42.669 -2.710  1.00 31.62  ? 132  GLU B CA  1 
ATOM   3604  C C   . GLU B  2 132 ? 27.933  41.898 -2.580  1.00 32.05  ? 132  GLU B C   1 
ATOM   3605  O O   . GLU B  2 132 ? 26.861  42.439 -2.838  1.00 33.83  ? 132  GLU B O   1 
ATOM   3606  C CB  . GLU B  2 132 ? 29.144  44.046 -2.055  1.00 31.39  ? 132  GLU B CB  1 
ATOM   3607  C CG  . GLU B  2 132 ? 28.919  43.999 -0.552  1.00 28.88  ? 132  GLU B CG  1 
ATOM   3608  C CD  . GLU B  2 132 ? 29.107  45.345 0.129   1.00 28.84  ? 132  GLU B CD  1 
ATOM   3609  O OE1 . GLU B  2 132 ? 28.971  46.395 -0.534  1.00 31.24  ? 132  GLU B OE1 1 
ATOM   3610  O OE2 . GLU B  2 132 ? 29.394  45.350 1.341   1.00 26.79  ? 132  GLU B OE2 1 
ATOM   3611  N N   . LEU B  2 133 ? 28.026  40.632 -2.183  1.00 31.00  ? 133  LEU B N   1 
ATOM   3612  C CA  . LEU B  2 133 ? 26.869  39.723 -2.192  1.00 32.24  ? 133  LEU B CA  1 
ATOM   3613  C C   . LEU B  2 133 ? 25.811  40.013 -1.119  1.00 31.82  ? 133  LEU B C   1 
ATOM   3614  O O   . LEU B  2 133 ? 24.642  39.665 -1.301  1.00 33.93  ? 133  LEU B O   1 
ATOM   3615  C CB  . LEU B  2 133 ? 27.341  38.263 -2.084  1.00 31.83  ? 133  LEU B CB  1 
ATOM   3616  C CG  . LEU B  2 133 ? 27.568  37.494 -3.392  1.00 34.25  ? 133  LEU B CG  1 
ATOM   3617  C CD1 . LEU B  2 133 ? 28.049  38.378 -4.533  1.00 35.58  ? 133  LEU B CD1 1 
ATOM   3618  C CD2 . LEU B  2 133 ? 28.539  36.346 -3.166  1.00 33.64  ? 133  LEU B CD2 1 
ATOM   3619  N N   . GLY B  2 134 ? 26.217  40.639 -0.015  1.00 29.58  ? 134  GLY B N   1 
ATOM   3620  C CA  . GLY B  2 134 ? 25.301  40.968 1.079   1.00 29.34  ? 134  GLY B CA  1 
ATOM   3621  C C   . GLY B  2 134 ? 25.363  40.009 2.259   1.00 27.70  ? 134  GLY B C   1 
ATOM   3622  O O   . GLY B  2 134 ? 24.644  40.193 3.246   1.00 27.59  ? 134  GLY B O   1 
ATOM   3623  N N   . ASN B  2 135 ? 26.231  39.001 2.169   1.00 26.88  ? 135  ASN B N   1 
ATOM   3624  C CA  . ASN B  2 135 ? 26.312  37.938 3.178   1.00 26.00  ? 135  ASN B CA  1 
ATOM   3625  C C   . ASN B  2 135 ? 27.693  37.801 3.826   1.00 23.49  ? 135  ASN B C   1 
ATOM   3626  O O   . ASN B  2 135 ? 27.961  36.829 4.533   1.00 23.02  ? 135  ASN B O   1 
ATOM   3627  C CB  . ASN B  2 135 ? 25.915  36.602 2.545   1.00 28.43  ? 135  ASN B CB  1 
ATOM   3628  C CG  . ASN B  2 135 ? 26.800  36.223 1.373   1.00 29.33  ? 135  ASN B CG  1 
ATOM   3629  O OD1 . ASN B  2 135 ? 27.786  36.897 1.073   1.00 28.12  ? 135  ASN B OD1 1 
ATOM   3630  N ND2 . ASN B  2 135 ? 26.446  35.149 0.698   1.00 32.14  ? 135  ASN B ND2 1 
ATOM   3631  N N   . GLY B  2 136 ? 28.565  38.772 3.577   1.00 22.38  ? 136  GLY B N   1 
ATOM   3632  C CA  . GLY B  2 136 ? 29.949  38.698 4.038   1.00 20.75  ? 136  GLY B CA  1 
ATOM   3633  C C   . GLY B  2 136 ? 30.921  38.266 2.952   1.00 21.70  ? 136  GLY B C   1 
ATOM   3634  O O   . GLY B  2 136 ? 32.136  38.308 3.154   1.00 21.11  ? 136  GLY B O   1 
ATOM   3635  N N   . CYS B  2 137 ? 30.391  37.865 1.799   1.00 23.55  ? 137  CYS B N   1 
ATOM   3636  C CA  . CYS B  2 137 ? 31.218  37.392 0.696   1.00 25.01  ? 137  CYS B CA  1 
ATOM   3637  C C   . CYS B  2 137 ? 31.337  38.422 -0.418  1.00 26.20  ? 137  CYS B C   1 
ATOM   3638  O O   . CYS B  2 137 ? 30.442  39.245 -0.629  1.00 26.64  ? 137  CYS B O   1 
ATOM   3639  C CB  . CYS B  2 137 ? 30.668  36.086 0.127   1.00 26.93  ? 137  CYS B CB  1 
ATOM   3640  S SG  . CYS B  2 137 ? 30.568  34.752 1.341   1.00 26.51  ? 137  CYS B SG  1 
ATOM   3641  N N   . PHE B  2 138 ? 32.469  38.360 -1.114  1.00 27.18  ? 138  PHE B N   1 
ATOM   3642  C CA  . PHE B  2 138 ? 32.723  39.167 -2.294  1.00 29.01  ? 138  PHE B CA  1 
ATOM   3643  C C   . PHE B  2 138 ? 33.015  38.236 -3.451  1.00 31.41  ? 138  PHE B C   1 
ATOM   3644  O O   . PHE B  2 138 ? 33.918  37.416 -3.360  1.00 31.77  ? 138  PHE B O   1 
ATOM   3645  C CB  . PHE B  2 138 ? 33.922  40.076 -2.068  1.00 28.79  ? 138  PHE B CB  1 
ATOM   3646  C CG  . PHE B  2 138 ? 33.705  41.099 -0.996  1.00 26.96  ? 138  PHE B CG  1 
ATOM   3647  C CD1 . PHE B  2 138 ? 33.097  42.311 -1.289  1.00 27.71  ? 138  PHE B CD1 1 
ATOM   3648  C CD2 . PHE B  2 138 ? 34.108  40.848 0.311   1.00 24.88  ? 138  PHE B CD2 1 
ATOM   3649  C CE1 . PHE B  2 138 ? 32.897  43.254 -0.302  1.00 26.52  ? 138  PHE B CE1 1 
ATOM   3650  C CE2 . PHE B  2 138 ? 33.910  41.791 1.303   1.00 23.51  ? 138  PHE B CE2 1 
ATOM   3651  C CZ  . PHE B  2 138 ? 33.300  42.993 0.995   1.00 24.36  ? 138  PHE B CZ  1 
ATOM   3652  N N   . GLU B  2 139 ? 32.253  38.369 -4.532  1.00 33.44  ? 139  GLU B N   1 
ATOM   3653  C CA  . GLU B  2 139 ? 32.420  37.537 -5.713  1.00 36.17  ? 139  GLU B CA  1 
ATOM   3654  C C   . GLU B  2 139 ? 33.183  38.320 -6.777  1.00 38.31  ? 139  GLU B C   1 
ATOM   3655  O O   . GLU B  2 139 ? 32.738  39.380 -7.212  1.00 39.05  ? 139  GLU B O   1 
ATOM   3656  C CB  . GLU B  2 139 ? 31.053  37.113 -6.231  1.00 37.65  ? 139  GLU B CB  1 
ATOM   3657  C CG  . GLU B  2 139 ? 31.084  36.214 -7.450  1.00 40.88  ? 139  GLU B CG  1 
ATOM   3658  C CD  . GLU B  2 139 ? 29.695  35.962 -7.988  1.00 42.89  ? 139  GLU B CD  1 
ATOM   3659  O OE1 . GLU B  2 139 ? 28.848  35.447 -7.223  1.00 42.18  ? 139  GLU B OE1 1 
ATOM   3660  O OE2 . GLU B  2 139 ? 29.441  36.306 -9.164  1.00 45.58  ? 139  GLU B OE2 1 
ATOM   3661  N N   . PHE B  2 140 ? 34.325  37.783 -7.202  1.00 39.84  ? 140  PHE B N   1 
ATOM   3662  C CA  . PHE B  2 140 ? 35.241  38.500 -8.095  1.00 42.26  ? 140  PHE B CA  1 
ATOM   3663  C C   . PHE B  2 140 ? 34.778  38.497 -9.550  1.00 45.57  ? 140  PHE B C   1 
ATOM   3664  O O   . PHE B  2 140 ? 34.195  37.523 -10.021 1.00 46.71  ? 140  PHE B O   1 
ATOM   3665  C CB  . PHE B  2 140 ? 36.646  37.896 -8.008  1.00 43.29  ? 140  PHE B CB  1 
ATOM   3666  C CG  . PHE B  2 140 ? 37.290  38.057 -6.664  1.00 40.79  ? 140  PHE B CG  1 
ATOM   3667  C CD1 . PHE B  2 140 ? 37.117  37.100 -5.676  1.00 38.80  ? 140  PHE B CD1 1 
ATOM   3668  C CD2 . PHE B  2 140 ? 38.071  39.170 -6.384  1.00 40.92  ? 140  PHE B CD2 1 
ATOM   3669  C CE1 . PHE B  2 140 ? 37.712  37.247 -4.434  1.00 36.81  ? 140  PHE B CE1 1 
ATOM   3670  C CE2 . PHE B  2 140 ? 38.668  39.326 -5.144  1.00 39.02  ? 140  PHE B CE2 1 
ATOM   3671  C CZ  . PHE B  2 140 ? 38.489  38.363 -4.168  1.00 36.87  ? 140  PHE B CZ  1 
ATOM   3672  N N   . TYR B  2 141 ? 35.045  39.592 -10.256 1.00 47.57  ? 141  TYR B N   1 
ATOM   3673  C CA  . TYR B  2 141 ? 34.798  39.648 -11.701 1.00 51.34  ? 141  TYR B CA  1 
ATOM   3674  C C   . TYR B  2 141 ? 35.890  38.894 -12.447 1.00 54.22  ? 141  TYR B C   1 
ATOM   3675  O O   . TYR B  2 141 ? 35.626  38.235 -13.452 1.00 56.93  ? 141  TYR B O   1 
ATOM   3676  C CB  . TYR B  2 141 ? 34.724  41.096 -12.195 1.00 53.01  ? 141  TYR B CB  1 
ATOM   3677  C CG  . TYR B  2 141 ? 33.545  41.847 -11.627 1.00 51.25  ? 141  TYR B CG  1 
ATOM   3678  C CD1 . TYR B  2 141 ? 32.243  41.454 -11.919 1.00 51.60  ? 141  TYR B CD1 1 
ATOM   3679  C CD2 . TYR B  2 141 ? 33.727  42.932 -10.781 1.00 49.75  ? 141  TYR B CD2 1 
ATOM   3680  C CE1 . TYR B  2 141 ? 31.157  42.129 -11.393 1.00 50.57  ? 141  TYR B CE1 1 
ATOM   3681  C CE2 . TYR B  2 141 ? 32.648  43.614 -10.249 1.00 48.60  ? 141  TYR B CE2 1 
ATOM   3682  C CZ  . TYR B  2 141 ? 31.365  43.209 -10.559 1.00 49.06  ? 141  TYR B CZ  1 
ATOM   3683  O OH  . TYR B  2 141 ? 30.289  43.886 -10.032 1.00 48.52  ? 141  TYR B OH  1 
ATOM   3684  N N   . HIS B  2 142 ? 37.115  39.003 -11.944 1.00 54.10  ? 142  HIS B N   1 
ATOM   3685  C CA  . HIS B  2 142 ? 38.253  38.263 -12.479 1.00 57.09  ? 142  HIS B CA  1 
ATOM   3686  C C   . HIS B  2 142 ? 38.417  36.941 -11.744 1.00 55.73  ? 142  HIS B C   1 
ATOM   3687  O O   . HIS B  2 142 ? 37.979  36.790 -10.600 1.00 52.21  ? 142  HIS B O   1 
ATOM   3688  C CB  . HIS B  2 142 ? 39.544  39.086 -12.364 1.00 58.66  ? 142  HIS B CB  1 
ATOM   3689  C CG  . HIS B  2 142 ? 39.843  39.561 -10.975 1.00 55.41  ? 142  HIS B CG  1 
ATOM   3690  N ND1 . HIS B  2 142 ? 40.717  38.906 -10.134 1.00 54.74  ? 142  HIS B ND1 1 
ATOM   3691  C CD2 . HIS B  2 142 ? 39.376  40.624 -10.278 1.00 53.07  ? 142  HIS B CD2 1 
ATOM   3692  C CE1 . HIS B  2 142 ? 40.779  39.550 -8.982  1.00 51.96  ? 142  HIS B CE1 1 
ATOM   3693  N NE2 . HIS B  2 142 ? 39.974  40.595 -9.044  1.00 50.89  ? 142  HIS B NE2 1 
ATOM   3694  N N   . LYS B  2 143 ? 39.049  35.983 -12.412 1.00 59.01  ? 143  LYS B N   1 
ATOM   3695  C CA  . LYS B  2 143 ? 39.413  34.723 -11.782 1.00 58.82  ? 143  LYS B CA  1 
ATOM   3696  C C   . LYS B  2 143 ? 40.482  35.021 -10.735 1.00 57.64  ? 143  LYS B C   1 
ATOM   3697  O O   . LYS B  2 143 ? 41.476  35.684 -11.033 1.00 59.83  ? 143  LYS B O   1 
ATOM   3698  C CB  . LYS B  2 143 ? 39.939  33.746 -12.830 1.00 63.46  ? 143  LYS B CB  1 
ATOM   3699  C CG  . LYS B  2 143 ? 40.024  32.305 -12.366 1.00 64.05  ? 143  LYS B CG  1 
ATOM   3700  C CD  . LYS B  2 143 ? 40.587  31.417 -13.468 1.00 69.35  ? 143  LYS B CD  1 
ATOM   3701  C CE  . LYS B  2 143 ? 41.204  30.143 -12.913 1.00 71.02  ? 143  LYS B CE  1 
ATOM   3702  N NZ  . LYS B  2 143 ? 42.516  30.370 -12.240 1.00 71.48  ? 143  LYS B NZ  1 
ATOM   3703  N N   . CYS B  2 144 ? 40.268  34.547 -9.509  1.00 54.63  ? 144  CYS B N   1 
ATOM   3704  C CA  . CYS B  2 144 ? 41.157  34.858 -8.391  1.00 53.32  ? 144  CYS B CA  1 
ATOM   3705  C C   . CYS B  2 144 ? 41.794  33.581 -7.838  1.00 54.48  ? 144  CYS B C   1 
ATOM   3706  O O   . CYS B  2 144 ? 41.162  32.830 -7.094  1.00 52.44  ? 144  CYS B O   1 
ATOM   3707  C CB  . CYS B  2 144 ? 40.374  35.596 -7.301  1.00 48.86  ? 144  CYS B CB  1 
ATOM   3708  S SG  . CYS B  2 144 ? 41.362  36.303 -5.960  1.00 47.35  ? 144  CYS B SG  1 
ATOM   3709  N N   . ASP B  2 145 ? 43.048  33.337 -8.218  1.00 58.33  ? 145  ASP B N   1 
ATOM   3710  C CA  . ASP B  2 145 ? 43.784  32.152 -7.761  1.00 60.46  ? 145  ASP B CA  1 
ATOM   3711  C C   . ASP B  2 145 ? 44.214  32.306 -6.291  1.00 58.04  ? 145  ASP B C   1 
ATOM   3712  O O   . ASP B  2 145 ? 43.893  33.306 -5.651  1.00 54.59  ? 145  ASP B O   1 
ATOM   3713  C CB  . ASP B  2 145 ? 44.980  31.859 -8.689  1.00 66.09  ? 145  ASP B CB  1 
ATOM   3714  C CG  . ASP B  2 145 ? 46.045  32.950 -8.666  1.00 67.62  ? 145  ASP B CG  1 
ATOM   3715  O OD1 . ASP B  2 145 ? 45.931  33.906 -7.876  1.00 64.38  ? 145  ASP B OD1 1 
ATOM   3716  O OD2 . ASP B  2 145 ? 47.008  32.848 -9.451  1.00 72.59  ? 145  ASP B OD2 1 
ATOM   3717  N N   . ASN B  2 146 ? 44.935  31.318 -5.763  1.00 60.23  ? 146  ASN B N   1 
ATOM   3718  C CA  . ASN B  2 146 ? 45.348  31.334 -4.353  1.00 58.44  ? 146  ASN B CA  1 
ATOM   3719  C C   . ASN B  2 146 ? 46.330  32.453 -4.000  1.00 58.99  ? 146  ASN B C   1 
ATOM   3720  O O   . ASN B  2 146 ? 46.368  32.904 -2.858  1.00 56.36  ? 146  ASN B O   1 
ATOM   3721  C CB  . ASN B  2 146 ? 45.932  29.978 -3.946  1.00 61.53  ? 146  ASN B CB  1 
ATOM   3722  C CG  . ASN B  2 146 ? 44.900  28.863 -3.968  1.00 60.90  ? 146  ASN B CG  1 
ATOM   3723  O OD1 . ASN B  2 146 ? 43.695  29.106 -4.048  1.00 57.58  ? 146  ASN B OD1 1 
ATOM   3724  N ND2 . ASN B  2 146 ? 45.372  27.630 -3.896  1.00 64.69  ? 146  ASN B ND2 1 
ATOM   3725  N N   . GLU B  2 147 ? 47.111  32.906 -4.975  1.00 62.87  ? 147  GLU B N   1 
ATOM   3726  C CA  . GLU B  2 147 ? 47.977  34.073 -4.788  1.00 64.09  ? 147  GLU B CA  1 
ATOM   3727  C C   . GLU B  2 147 ? 47.129  35.348 -4.756  1.00 60.27  ? 147  GLU B C   1 
ATOM   3728  O O   . GLU B  2 147 ? 47.350  36.234 -3.927  1.00 58.71  ? 147  GLU B O   1 
ATOM   3729  C CB  . GLU B  2 147 ? 49.024  34.175 -5.902  1.00 70.01  ? 147  GLU B CB  1 
ATOM   3730  C CG  . GLU B  2 147 ? 49.952  32.972 -6.026  1.00 74.94  ? 147  GLU B CG  1 
ATOM   3731  C CD  . GLU B  2 147 ? 49.429  31.915 -6.986  1.00 76.51  ? 147  GLU B CD  1 
ATOM   3732  O OE1 . GLU B  2 147 ? 48.442  31.228 -6.641  1.00 73.23  ? 147  GLU B OE1 1 
ATOM   3733  O OE2 . GLU B  2 147 ? 49.997  31.779 -8.094  1.00 81.39  ? 147  GLU B OE2 1 
ATOM   3734  N N   . CYS B  2 148 ? 46.163  35.429 -5.669  1.00 59.30  ? 148  CYS B N   1 
ATOM   3735  C CA  . CYS B  2 148 ? 45.203  36.532 -5.706  1.00 56.06  ? 148  CYS B CA  1 
ATOM   3736  C C   . CYS B  2 148 ? 44.426  36.618 -4.389  1.00 51.35  ? 148  CYS B C   1 
ATOM   3737  O O   . CYS B  2 148 ? 44.223  37.707 -3.853  1.00 49.36  ? 148  CYS B O   1 
ATOM   3738  C CB  . CYS B  2 148 ? 44.248  36.360 -6.895  1.00 56.18  ? 148  CYS B CB  1 
ATOM   3739  S SG  . CYS B  2 148 ? 42.786  37.422 -6.890  1.00 52.13  ? 148  CYS B SG  1 
ATOM   3740  N N   . MET B  2 149 ? 44.008  35.469 -3.866  1.00 50.17  ? 149  MET B N   1 
ATOM   3741  C CA  . MET B  2 149 ? 43.327  35.419 -2.572  1.00 46.29  ? 149  MET B CA  1 
ATOM   3742  C C   . MET B  2 149 ? 44.259  35.862 -1.447  1.00 46.59  ? 149  MET B C   1 
ATOM   3743  O O   . MET B  2 149 ? 43.836  36.544 -0.515  1.00 43.51  ? 149  MET B O   1 
ATOM   3744  C CB  . MET B  2 149 ? 42.820  34.007 -2.278  1.00 45.78  ? 149  MET B CB  1 
ATOM   3745  C CG  . MET B  2 149 ? 41.765  33.486 -3.240  1.00 45.83  ? 149  MET B CG  1 
ATOM   3746  S SD  . MET B  2 149 ? 40.232  34.420 -3.205  1.00 41.84  ? 149  MET B SD  1 
ATOM   3747  C CE  . MET B  2 149 ? 39.165  33.350 -4.168  1.00 43.20  ? 149  MET B CE  1 
ATOM   3748  N N   . GLU B  2 150 ? 45.527  35.469 -1.537  1.00 50.94  ? 150  GLU B N   1 
ATOM   3749  C CA  . GLU B  2 150 ? 46.518  35.826 -0.523  1.00 52.30  ? 150  GLU B CA  1 
ATOM   3750  C C   . GLU B  2 150 ? 46.771  37.335 -0.464  1.00 52.66  ? 150  GLU B C   1 
ATOM   3751  O O   . GLU B  2 150 ? 47.040  37.869 0.609   1.00 51.74  ? 150  GLU B O   1 
ATOM   3752  C CB  . GLU B  2 150 ? 47.833  35.069 -0.767  1.00 57.47  ? 150  GLU B CB  1 
ATOM   3753  C CG  . GLU B  2 150 ? 48.942  35.325 0.253   1.00 59.37  ? 150  GLU B CG  1 
ATOM   3754  C CD  . GLU B  2 150 ? 48.544  34.978 1.678   1.00 56.09  ? 150  GLU B CD  1 
ATOM   3755  O OE1 . GLU B  2 150 ? 47.783  34.009 1.870   1.00 54.24  ? 150  GLU B OE1 1 
ATOM   3756  O OE2 . GLU B  2 150 ? 48.995  35.674 2.612   1.00 55.79  ? 150  GLU B OE2 1 
ATOM   3757  N N   . SER B  2 151 ? 46.685  38.014 -1.608  1.00 54.73  ? 151  SER B N   1 
ATOM   3758  C CA  . SER B  2 151 ? 46.887  39.466 -1.661  1.00 55.79  ? 151  SER B CA  1 
ATOM   3759  C C   . SER B  2 151 ? 45.761  40.226 -0.947  1.00 51.75  ? 151  SER B C   1 
ATOM   3760  O O   . SER B  2 151 ? 45.991  41.283 -0.352  1.00 51.81  ? 151  SER B O   1 
ATOM   3761  C CB  . SER B  2 151 ? 47.005  39.947 -3.109  1.00 58.95  ? 151  SER B CB  1 
ATOM   3762  O OG  . SER B  2 151 ? 45.788  39.774 -3.808  1.00 56.57  ? 151  SER B OG  1 
ATOM   3763  N N   . VAL B  2 152 ? 44.548  39.683 -1.013  1.00 49.04  ? 152  VAL B N   1 
ATOM   3764  C CA  . VAL B  2 152 ? 43.404  40.256 -0.308  1.00 45.50  ? 152  VAL B CA  1 
ATOM   3765  C C   . VAL B  2 152 ? 43.610  40.080 1.195   1.00 44.24  ? 152  VAL B C   1 
ATOM   3766  O O   . VAL B  2 152 ? 43.359  40.998 1.978   1.00 42.65  ? 152  VAL B O   1 
ATOM   3767  C CB  . VAL B  2 152 ? 42.076  39.592 -0.737  1.00 43.05  ? 152  VAL B CB  1 
ATOM   3768  C CG1 . VAL B  2 152 ? 40.900  40.206 0.013   1.00 39.48  ? 152  VAL B CG1 1 
ATOM   3769  C CG2 . VAL B  2 152 ? 41.868  39.725 -2.241  1.00 45.28  ? 152  VAL B CG2 1 
ATOM   3770  N N   . ARG B  2 153 ? 44.069  38.896 1.587   1.00 45.67  ? 153  ARG B N   1 
ATOM   3771  C CA  . ARG B  2 153 ? 44.425  38.627 2.978   1.00 45.42  ? 153  ARG B CA  1 
ATOM   3772  C C   . ARG B  2 153 ? 45.646  39.444 3.421   1.00 49.26  ? 153  ARG B C   1 
ATOM   3773  O O   . ARG B  2 153 ? 45.690  39.940 4.547   1.00 47.89  ? 153  ARG B O   1 
ATOM   3774  C CB  . ARG B  2 153 ? 44.678  37.129 3.184   1.00 46.01  ? 153  ARG B CB  1 
ATOM   3775  C CG  . ARG B  2 153 ? 43.404  36.321 3.336   1.00 42.85  ? 153  ARG B CG  1 
ATOM   3776  C CD  . ARG B  2 153 ? 43.665  34.853 3.653   1.00 44.11  ? 153  ARG B CD  1 
ATOM   3777  N NE  . ARG B  2 153 ? 43.294  33.988 2.532   1.00 45.58  ? 153  ARG B NE  1 
ATOM   3778  C CZ  . ARG B  2 153 ? 44.139  33.393 1.692   1.00 49.39  ? 153  ARG B CZ  1 
ATOM   3779  N NH1 . ARG B  2 153 ? 45.454  33.529 1.821   1.00 52.38  ? 153  ARG B NH1 1 
ATOM   3780  N NH2 . ARG B  2 153 ? 43.655  32.639 0.710   1.00 50.74  ? 153  ARG B NH2 1 
ATOM   3781  N N   . ASN B  2 154 ? 46.629  39.563 2.529   1.00 55.28  ? 154  ASN B N   1 
ATOM   3782  C CA  . ASN B  2 154 ? 47.814  40.410 2.732   1.00 60.28  ? 154  ASN B CA  1 
ATOM   3783  C C   . ASN B  2 154 ? 47.498  41.850 3.123   1.00 58.16  ? 154  ASN B C   1 
ATOM   3784  O O   . ASN B  2 154 ? 48.194  42.441 3.950   1.00 59.64  ? 154  ASN B O   1 
ATOM   3785  C CB  . ASN B  2 154 ? 48.626  40.494 1.435   1.00 67.50  ? 154  ASN B CB  1 
ATOM   3786  C CG  . ASN B  2 154 ? 49.744  39.477 1.349   1.00 75.29  ? 154  ASN B CG  1 
ATOM   3787  O OD1 . ASN B  2 154 ? 50.037  38.756 2.301   1.00 75.45  ? 154  ASN B OD1 1 
ATOM   3788  N ND2 . ASN B  2 154 ? 50.388  39.431 0.182   1.00 84.83  ? 154  ASN B ND2 1 
ATOM   3789  N N   . GLY B  2 155 ? 46.456  42.406 2.507   1.00 54.87  ? 155  GLY B N   1 
ATOM   3790  C CA  . GLY B  2 155 ? 46.245  43.849 2.460   1.00 54.37  ? 155  GLY B CA  1 
ATOM   3791  C C   . GLY B  2 155 ? 46.894  44.432 1.213   1.00 58.06  ? 155  GLY B C   1 
ATOM   3792  O O   . GLY B  2 155 ? 46.994  45.649 1.072   1.00 60.03  ? 155  GLY B O   1 
ATOM   3793  N N   . THR B  2 156 ? 47.311  43.553 0.300   1.00 59.28  ? 156  THR B N   1 
ATOM   3794  C CA  . THR B  2 156 ? 48.150  43.913 -0.847  1.00 63.86  ? 156  THR B CA  1 
ATOM   3795  C C   . THR B  2 156 ? 47.408  43.787 -2.184  1.00 63.24  ? 156  THR B C   1 
ATOM   3796  O O   . THR B  2 156 ? 48.007  43.954 -3.245  1.00 67.56  ? 156  THR B O   1 
ATOM   3797  C CB  . THR B  2 156 ? 49.406  43.010 -0.864  1.00 67.55  ? 156  THR B CB  1 
ATOM   3798  O OG1 . THR B  2 156 ? 50.158  43.226 0.336   1.00 68.41  ? 156  THR B OG1 1 
ATOM   3799  C CG2 . THR B  2 156 ? 50.312  43.280 -2.067  1.00 73.54  ? 156  THR B CG2 1 
ATOM   3800  N N   . TYR B  2 157 ? 46.106  43.515 -2.140  1.00 58.26  ? 157  TYR B N   1 
ATOM   3801  C CA  . TYR B  2 157 ? 45.326  43.315 -3.366  1.00 57.79  ? 157  TYR B CA  1 
ATOM   3802  C C   . TYR B  2 157 ? 45.515  44.473 -4.349  1.00 61.33  ? 157  TYR B C   1 
ATOM   3803  O O   . TYR B  2 157 ? 45.147  45.612 -4.055  1.00 60.98  ? 157  TYR B O   1 
ATOM   3804  C CB  . TYR B  2 157 ? 43.838  43.150 -3.044  1.00 52.80  ? 157  TYR B CB  1 
ATOM   3805  C CG  . TYR B  2 157 ? 42.978  42.984 -4.279  1.00 52.90  ? 157  TYR B CG  1 
ATOM   3806  C CD1 . TYR B  2 157 ? 42.919  41.766 -4.951  1.00 53.32  ? 157  TYR B CD1 1 
ATOM   3807  C CD2 . TYR B  2 157 ? 42.237  44.047 -4.783  1.00 53.09  ? 157  TYR B CD2 1 
ATOM   3808  C CE1 . TYR B  2 157 ? 42.138  41.610 -6.084  1.00 53.88  ? 157  TYR B CE1 1 
ATOM   3809  C CE2 . TYR B  2 157 ? 41.456  43.900 -5.917  1.00 53.73  ? 157  TYR B CE2 1 
ATOM   3810  C CZ  . TYR B  2 157 ? 41.409  42.681 -6.562  1.00 54.01  ? 157  TYR B CZ  1 
ATOM   3811  O OH  . TYR B  2 157 ? 40.631  42.536 -7.684  1.00 54.92  ? 157  TYR B OH  1 
ATOM   3812  N N   . ASP B  2 158 ? 46.080  44.173 -5.515  1.00 65.10  ? 158  ASP B N   1 
ATOM   3813  C CA  . ASP B  2 158 ? 46.391  45.208 -6.497  1.00 69.42  ? 158  ASP B CA  1 
ATOM   3814  C C   . ASP B  2 158 ? 45.176  45.517 -7.371  1.00 68.17  ? 158  ASP B C   1 
ATOM   3815  O O   . ASP B  2 158 ? 44.960  44.883 -8.410  1.00 69.36  ? 158  ASP B O   1 
ATOM   3816  C CB  . ASP B  2 158 ? 47.592  44.804 -7.359  1.00 74.89  ? 158  ASP B CB  1 
ATOM   3817  C CG  . ASP B  2 158 ? 48.263  45.996 -8.017  1.00 80.49  ? 158  ASP B CG  1 
ATOM   3818  O OD1 . ASP B  2 158 ? 48.592  46.967 -7.302  1.00 81.44  ? 158  ASP B OD1 1 
ATOM   3819  O OD2 . ASP B  2 158 ? 48.470  45.966 -9.246  1.00 84.38  ? 158  ASP B OD2 1 
ATOM   3820  N N   . TYR B  2 159 ? 44.388  46.498 -6.932  1.00 66.13  ? 159  TYR B N   1 
ATOM   3821  C CA  . TYR B  2 159 ? 43.208  46.951 -7.667  1.00 65.39  ? 159  TYR B CA  1 
ATOM   3822  C C   . TYR B  2 159 ? 43.535  47.354 -9.117  1.00 70.59  ? 159  TYR B C   1 
ATOM   3823  O O   . TYR B  2 159 ? 42.862  46.894 -10.042 1.00 70.61  ? 159  TYR B O   1 
ATOM   3824  C CB  . TYR B  2 159 ? 42.509  48.093 -6.905  1.00 63.68  ? 159  TYR B CB  1 
ATOM   3825  C CG  . TYR B  2 159 ? 41.389  48.760 -7.667  1.00 64.18  ? 159  TYR B CG  1 
ATOM   3826  C CD1 . TYR B  2 159 ? 40.085  48.281 -7.580  1.00 60.41  ? 159  TYR B CD1 1 
ATOM   3827  C CD2 . TYR B  2 159 ? 41.631  49.873 -8.472  1.00 68.96  ? 159  TYR B CD2 1 
ATOM   3828  C CE1 . TYR B  2 159 ? 39.056  48.887 -8.274  1.00 61.45  ? 159  TYR B CE1 1 
ATOM   3829  C CE2 . TYR B  2 159 ? 40.607  50.485 -9.175  1.00 69.98  ? 159  TYR B CE2 1 
ATOM   3830  C CZ  . TYR B  2 159 ? 39.321  49.989 -9.071  1.00 66.25  ? 159  TYR B CZ  1 
ATOM   3831  O OH  . TYR B  2 159 ? 38.306  50.600 -9.767  1.00 67.86  ? 159  TYR B OH  1 
ATOM   3832  N N   . PRO B  2 160 ? 44.574  48.195 -9.324  1.00 75.45  ? 160  PRO B N   1 
ATOM   3833  C CA  . PRO B  2 160 ? 44.931  48.612 -10.693 1.00 81.01  ? 160  PRO B CA  1 
ATOM   3834  C C   . PRO B  2 160 ? 45.257  47.480 -11.685 1.00 82.69  ? 160  PRO B C   1 
ATOM   3835  O O   . PRO B  2 160 ? 45.079  47.666 -12.892 1.00 86.11  ? 160  PRO B O   1 
ATOM   3836  C CB  . PRO B  2 160 ? 46.167  49.496 -10.479 1.00 85.96  ? 160  PRO B CB  1 
ATOM   3837  C CG  . PRO B  2 160 ? 46.020  50.018 -9.094  1.00 82.87  ? 160  PRO B CG  1 
ATOM   3838  C CD  . PRO B  2 160 ? 45.403  48.890 -8.318  1.00 76.54  ? 160  PRO B CD  1 
ATOM   3839  N N   . GLN B  2 161 ? 45.732  46.336 -11.192 1.00 80.88  ? 161  GLN B N   1 
ATOM   3840  C CA  . GLN B  2 161 ? 46.039  45.190 -12.062 1.00 82.73  ? 161  GLN B CA  1 
ATOM   3841  C C   . GLN B  2 161 ? 44.767  44.532 -12.599 1.00 79.71  ? 161  GLN B C   1 
ATOM   3842  O O   . GLN B  2 161 ? 44.682  44.208 -13.786 1.00 82.62  ? 161  GLN B O   1 
ATOM   3843  C CB  . GLN B  2 161 ? 46.879  44.144 -11.317 1.00 82.02  ? 161  GLN B CB  1 
ATOM   3844  C CG  . GLN B  2 161 ? 47.211  42.893 -12.130 1.00 84.17  ? 161  GLN B CG  1 
ATOM   3845  C CD  . GLN B  2 161 ? 47.829  41.784 -11.294 1.00 83.05  ? 161  GLN B CD  1 
ATOM   3846  O OE1 . GLN B  2 161 ? 47.936  41.892 -10.069 1.00 80.15  ? 161  GLN B OE1 1 
ATOM   3847  N NE2 . GLN B  2 161 ? 48.228  40.703 -11.955 1.00 85.68  ? 161  GLN B NE2 1 
ATOM   3848  N N   . TYR B  2 162 ? 43.792  44.331 -11.716 1.00 74.31  ? 162  TYR B N   1 
ATOM   3849  C CA  . TYR B  2 162 ? 42.555  43.641 -12.073 1.00 71.57  ? 162  TYR B CA  1 
ATOM   3850  C C   . TYR B  2 162 ? 41.427  44.592 -12.503 1.00 71.45  ? 162  TYR B C   1 
ATOM   3851  O O   . TYR B  2 162 ? 40.298  44.145 -12.726 1.00 69.48  ? 162  TYR B O   1 
ATOM   3852  C CB  . TYR B  2 162 ? 42.085  42.777 -10.897 1.00 66.41  ? 162  TYR B CB  1 
ATOM   3853  C CG  . TYR B  2 162 ? 43.111  41.763 -10.426 1.00 66.78  ? 162  TYR B CG  1 
ATOM   3854  C CD1 . TYR B  2 162 ? 43.326  40.576 -11.129 1.00 68.61  ? 162  TYR B CD1 1 
ATOM   3855  C CD2 . TYR B  2 162 ? 43.865  41.989 -9.275  1.00 65.76  ? 162  TYR B CD2 1 
ATOM   3856  C CE1 . TYR B  2 162 ? 44.264  39.647 -10.699 1.00 69.58  ? 162  TYR B CE1 1 
ATOM   3857  C CE2 . TYR B  2 162 ? 44.803  41.067 -8.835  1.00 66.62  ? 162  TYR B CE2 1 
ATOM   3858  C CZ  . TYR B  2 162 ? 44.999  39.897 -9.548  1.00 68.60  ? 162  TYR B CZ  1 
ATOM   3859  O OH  . TYR B  2 162 ? 45.934  38.983 -9.113  1.00 70.07  ? 162  TYR B OH  1 
ATOM   3860  N N   . SER B  2 163 ? 41.726  45.888 -12.621 1.00 74.20  ? 163  SER B N   1 
ATOM   3861  C CA  . SER B  2 163 ? 40.721  46.880 -13.030 1.00 74.88  ? 163  SER B CA  1 
ATOM   3862  C C   . SER B  2 163 ? 40.653  46.970 -14.553 1.00 79.44  ? 163  SER B C   1 
ATOM   3863  O O   . SER B  2 163 ? 40.065  47.903 -15.104 1.00 81.70  ? 163  SER B O   1 
ATOM   3864  C CB  . SER B  2 163 ? 41.018  48.267 -12.420 1.00 76.16  ? 163  SER B CB  1 
ATOM   3865  O OG  . SER B  2 163 ? 42.035  48.939 -13.145 1.00 81.93  ? 163  SER B OG  1 
ATOM   3866  N N   . ASP C  1 1   ? 42.788  65.175 -8.471  1.00 30.79  ? 1    ASP C N   1 
ATOM   3867  C CA  . ASP C  1 1   ? 42.309  65.987 -7.316  1.00 31.27  ? 1    ASP C CA  1 
ATOM   3868  C C   . ASP C  1 1   ? 41.565  65.104 -6.311  1.00 29.73  ? 1    ASP C C   1 
ATOM   3869  O O   . ASP C  1 1   ? 40.839  64.191 -6.702  1.00 28.67  ? 1    ASP C O   1 
ATOM   3870  C CB  . ASP C  1 1   ? 41.407  67.129 -7.799  1.00 32.74  ? 1    ASP C CB  1 
ATOM   3871  C CG  . ASP C  1 1   ? 42.095  68.032 -8.815  1.00 34.51  ? 1    ASP C CG  1 
ATOM   3872  O OD1 . ASP C  1 1   ? 43.255  67.750 -9.188  1.00 34.54  ? 1    ASP C OD1 1 
ATOM   3873  O OD2 . ASP C  1 1   ? 41.475  69.026 -9.246  1.00 36.15  ? 1    ASP C OD2 1 
ATOM   3874  N N   . GLN C  1 2   ? 41.756  65.380 -5.021  1.00 29.73  ? 2    GLN C N   1 
ATOM   3875  C CA  . GLN C  1 2   ? 41.131  64.590 -3.960  1.00 28.40  ? 2    GLN C CA  1 
ATOM   3876  C C   . GLN C  1 2   ? 40.812  65.396 -2.707  1.00 28.88  ? 2    GLN C C   1 
ATOM   3877  O O   . GLN C  1 2   ? 41.459  66.404 -2.419  1.00 30.12  ? 2    GLN C O   1 
ATOM   3878  C CB  . GLN C  1 2   ? 42.028  63.412 -3.573  1.00 27.34  ? 2    GLN C CB  1 
ATOM   3879  C CG  . GLN C  1 2   ? 43.392  63.809 -3.031  1.00 28.12  ? 2    GLN C CG  1 
ATOM   3880  C CD  . GLN C  1 2   ? 44.147  62.639 -2.425  1.00 27.26  ? 2    GLN C CD  1 
ATOM   3881  O OE1 . GLN C  1 2   ? 44.845  62.798 -1.421  1.00 27.63  ? 2    GLN C OE1 1 
ATOM   3882  N NE2 . GLN C  1 2   ? 44.013  61.459 -3.026  1.00 26.33  ? 2    GLN C NE2 1 
ATOM   3883  N N   . ILE C  1 3   ? 39.808  64.932 -1.971  1.00 28.00  ? 3    ILE C N   1 
ATOM   3884  C CA  . ILE C  1 3   ? 39.509  65.451 -0.641  1.00 28.22  ? 3    ILE C CA  1 
ATOM   3885  C C   . ILE C  1 3   ? 39.554  64.296 0.357   1.00 26.69  ? 3    ILE C C   1 
ATOM   3886  O O   . ILE C  1 3   ? 39.053  63.209 0.076   1.00 25.65  ? 3    ILE C O   1 
ATOM   3887  C CB  . ILE C  1 3   ? 38.146  66.184 -0.592  1.00 29.15  ? 3    ILE C CB  1 
ATOM   3888  C CG1 . ILE C  1 3   ? 37.997  66.943 0.734   1.00 29.81  ? 3    ILE C CG1 1 
ATOM   3889  C CG2 . ILE C  1 3   ? 36.980  65.222 -0.794  1.00 28.23  ? 3    ILE C CG2 1 
ATOM   3890  C CD1 . ILE C  1 3   ? 36.996  68.075 0.677   1.00 31.53  ? 3    ILE C CD1 1 
ATOM   3891  N N   . CYS C  1 4   ? 40.175  64.534 1.510   1.00 26.72  ? 4    CYS C N   1 
ATOM   3892  C CA  . CYS C  1 4   ? 40.345  63.501 2.524   1.00 25.49  ? 4    CYS C CA  1 
ATOM   3893  C C   . CYS C  1 4   ? 39.652  63.895 3.809   1.00 25.36  ? 4    CYS C C   1 
ATOM   3894  O O   . CYS C  1 4   ? 39.497  65.076 4.091   1.00 26.51  ? 4    CYS C O   1 
ATOM   3895  C CB  . CYS C  1 4   ? 41.827  63.262 2.803   1.00 25.68  ? 4    CYS C CB  1 
ATOM   3896  S SG  . CYS C  1 4   ? 42.803  62.876 1.331   1.00 26.11  ? 4    CYS C SG  1 
ATOM   3897  N N   . ILE C  1 5   ? 39.229  62.895 4.578   1.00 24.07  ? 5    ILE C N   1 
ATOM   3898  C CA  . ILE C  1 5   ? 38.721  63.124 5.921   1.00 23.88  ? 5    ILE C CA  1 
ATOM   3899  C C   . ILE C  1 5   ? 39.767  62.610 6.894   1.00 23.26  ? 5    ILE C C   1 
ATOM   3900  O O   . ILE C  1 5   ? 40.349  61.545 6.685   1.00 22.54  ? 5    ILE C O   1 
ATOM   3901  C CB  . ILE C  1 5   ? 37.381  62.413 6.155   1.00 23.28  ? 5    ILE C CB  1 
ATOM   3902  C CG1 . ILE C  1 5   ? 36.376  62.813 5.074   1.00 23.99  ? 5    ILE C CG1 1 
ATOM   3903  C CG2 . ILE C  1 5   ? 36.831  62.728 7.542   1.00 23.38  ? 5    ILE C CG2 1 
ATOM   3904  C CD1 . ILE C  1 5   ? 35.880  64.235 5.183   1.00 25.43  ? 5    ILE C CD1 1 
ATOM   3905  N N   . GLY C  1 6   ? 40.025  63.391 7.937   1.00 23.74  ? 6    GLY C N   1 
ATOM   3906  C CA  . GLY C  1 6   ? 41.066  63.062 8.900   1.00 23.50  ? 6    GLY C CA  1 
ATOM   3907  C C   . GLY C  1 6   ? 40.849  63.723 10.237  1.00 23.81  ? 6    GLY C C   1 
ATOM   3908  O O   . GLY C  1 6   ? 39.875  64.449 10.437  1.00 24.27  ? 6    GLY C O   1 
ATOM   3909  N N   . TYR C  1 7   ? 41.776  63.475 11.148  1.00 23.72  ? 7    TYR C N   1 
ATOM   3910  C CA  . TYR C  1 7   ? 41.625  63.898 12.531  1.00 23.92  ? 7    TYR C CA  1 
ATOM   3911  C C   . TYR C  1 7   ? 42.920  64.478 13.079  1.00 25.03  ? 7    TYR C C   1 
ATOM   3912  O O   . TYR C  1 7   ? 43.996  64.266 12.531  1.00 25.41  ? 7    TYR C O   1 
ATOM   3913  C CB  . TYR C  1 7   ? 41.138  62.725 13.402  1.00 22.63  ? 7    TYR C CB  1 
ATOM   3914  C CG  . TYR C  1 7   ? 41.999  61.478 13.335  1.00 21.95  ? 7    TYR C CG  1 
ATOM   3915  C CD1 . TYR C  1 7   ? 41.834  60.544 12.322  1.00 21.31  ? 7    TYR C CD1 1 
ATOM   3916  C CD2 . TYR C  1 7   ? 42.970  61.232 14.292  1.00 22.18  ? 7    TYR C CD2 1 
ATOM   3917  C CE1 . TYR C  1 7   ? 42.619  59.407 12.260  1.00 21.02  ? 7    TYR C CE1 1 
ATOM   3918  C CE2 . TYR C  1 7   ? 43.760  60.096 14.239  1.00 21.93  ? 7    TYR C CE2 1 
ATOM   3919  C CZ  . TYR C  1 7   ? 43.579  59.188 13.225  1.00 21.38  ? 7    TYR C CZ  1 
ATOM   3920  O OH  . TYR C  1 7   ? 44.371  58.067 13.178  1.00 21.42  ? 7    TYR C OH  1 
ATOM   3921  N N   . HIS C  1 8   ? 42.781  65.211 14.175  1.00 25.73  ? 8    HIS C N   1 
ATOM   3922  C CA  . HIS C  1 8   ? 43.872  65.952 14.803  1.00 27.16  ? 8    HIS C CA  1 
ATOM   3923  C C   . HIS C  1 8   ? 44.940  65.037 15.390  1.00 26.94  ? 8    HIS C C   1 
ATOM   3924  O O   . HIS C  1 8   ? 44.629  63.999 15.965  1.00 25.73  ? 8    HIS C O   1 
ATOM   3925  C CB  . HIS C  1 8   ? 43.285  66.824 15.918  1.00 27.79  ? 8    HIS C CB  1 
ATOM   3926  C CG  . HIS C  1 8   ? 44.274  67.731 16.580  1.00 29.52  ? 8    HIS C CG  1 
ATOM   3927  N ND1 . HIS C  1 8   ? 44.874  68.784 15.923  1.00 31.39  ? 8    HIS C ND1 1 
ATOM   3928  C CD2 . HIS C  1 8   ? 44.738  67.767 17.851  1.00 29.85  ? 8    HIS C CD2 1 
ATOM   3929  C CE1 . HIS C  1 8   ? 45.682  69.417 16.755  1.00 32.87  ? 8    HIS C CE1 1 
ATOM   3930  N NE2 . HIS C  1 8   ? 45.615  68.821 17.933  1.00 31.94  ? 8    HIS C NE2 1 
ATOM   3931  N N   . ALA C  1 9   ? 46.199  65.425 15.227  1.00 28.43  ? 9    ALA C N   1 
ATOM   3932  C CA  . ALA C  1 9   ? 47.299  64.847 16.000  1.00 28.89  ? 9    ALA C CA  1 
ATOM   3933  C C   . ALA C  1 9   ? 48.110  65.999 16.572  1.00 31.04  ? 9    ALA C C   1 
ATOM   3934  O O   . ALA C  1 9   ? 47.923  67.144 16.170  1.00 32.21  ? 9    ALA C O   1 
ATOM   3935  C CB  . ALA C  1 9   ? 48.162  63.953 15.132  1.00 28.88  ? 9    ALA C CB  1 
ATOM   3936  N N   . ASN C  1 10  ? 48.992  65.706 17.519  1.00 31.85  ? 10   ASN C N   1 
ATOM   3937  C CA  . ASN C  1 10  ? 49.865  66.731 18.095  1.00 34.21  ? 10   ASN C CA  1 
ATOM   3938  C C   . ASN C  1 10  ? 51.059  66.119 18.830  1.00 35.27  ? 10   ASN C C   1 
ATOM   3939  O O   . ASN C  1 10  ? 51.274  64.910 18.763  1.00 34.28  ? 10   ASN C O   1 
ATOM   3940  C CB  . ASN C  1 10  ? 49.069  67.689 19.000  1.00 34.45  ? 10   ASN C CB  1 
ATOM   3941  C CG  . ASN C  1 10  ? 48.549  67.025 20.261  1.00 33.09  ? 10   ASN C CG  1 
ATOM   3942  O OD1 . ASN C  1 10  ? 48.896  65.889 20.585  1.00 32.21  ? 10   ASN C OD1 1 
ATOM   3943  N ND2 . ASN C  1 10  ? 47.702  67.739 20.982  1.00 33.10  ? 10   ASN C ND2 1 
ATOM   3944  N N   . ASN C  1 11  ? 51.833  66.958 19.519  1.00 37.64  ? 11   ASN C N   1 
ATOM   3945  C CA  . ASN C  1 11  ? 53.052  66.520 20.212  1.00 39.24  ? 11   ASN C CA  1 
ATOM   3946  C C   . ASN C  1 11  ? 52.824  66.071 21.668  1.00 38.55  ? 11   ASN C C   1 
ATOM   3947  O O   . ASN C  1 11  ? 53.784  65.879 22.414  1.00 39.99  ? 11   ASN C O   1 
ATOM   3948  C CB  . ASN C  1 11  ? 54.129  67.624 20.141  1.00 42.41  ? 11   ASN C CB  1 
ATOM   3949  C CG  . ASN C  1 11  ? 53.725  68.903 20.869  1.00 43.52  ? 11   ASN C CG  1 
ATOM   3950  O OD1 . ASN C  1 11  ? 52.710  68.942 21.573  1.00 42.07  ? 11   ASN C OD1 1 
ATOM   3951  N ND2 . ASN C  1 11  ? 54.522  69.960 20.698  1.00 46.38  ? 11   ASN C ND2 1 
ATOM   3952  N N   . SER C  1 12  ? 51.560  65.904 22.057  1.00 36.55  ? 12   SER C N   1 
ATOM   3953  C CA  . SER C  1 12  ? 51.198  65.495 23.415  1.00 35.80  ? 12   SER C CA  1 
ATOM   3954  C C   . SER C  1 12  ? 51.685  64.084 23.730  1.00 35.30  ? 12   SER C C   1 
ATOM   3955  O O   . SER C  1 12  ? 51.634  63.199 22.875  1.00 34.47  ? 12   SER C O   1 
ATOM   3956  C CB  . SER C  1 12  ? 49.677  65.560 23.609  1.00 33.81  ? 12   SER C CB  1 
ATOM   3957  O OG  . SER C  1 12  ? 49.290  65.125 24.903  1.00 33.01  ? 12   SER C OG  1 
ATOM   3958  N N   . THR C  1 13  ? 52.154  63.894 24.965  1.00 36.10  ? 13   THR C N   1 
ATOM   3959  C CA  . THR C  1 13  ? 52.551  62.579 25.472  1.00 35.82  ? 13   THR C CA  1 
ATOM   3960  C C   . THR C  1 13  ? 51.662  62.119 26.629  1.00 34.39  ? 13   THR C C   1 
ATOM   3961  O O   . THR C  1 13  ? 51.935  61.090 27.243  1.00 34.34  ? 13   THR C O   1 
ATOM   3962  C CB  . THR C  1 13  ? 54.017  62.583 25.956  1.00 38.34  ? 13   THR C CB  1 
ATOM   3963  O OG1 . THR C  1 13  ? 54.222  63.670 26.870  1.00 39.70  ? 13   THR C OG1 1 
ATOM   3964  C CG2 . THR C  1 13  ? 54.975  62.713 24.775  1.00 39.91  ? 13   THR C CG2 1 
ATOM   3965  N N   . GLU C  1 14  ? 50.601  62.869 26.922  1.00 33.49  ? 14   GLU C N   1 
ATOM   3966  C CA  . GLU C  1 14  ? 49.666  62.486 27.977  1.00 32.17  ? 14   GLU C CA  1 
ATOM   3967  C C   . GLU C  1 14  ? 48.975  61.165 27.651  1.00 30.29  ? 14   GLU C C   1 
ATOM   3968  O O   . GLU C  1 14  ? 48.516  60.960 26.531  1.00 29.45  ? 14   GLU C O   1 
ATOM   3969  C CB  . GLU C  1 14  ? 48.611  63.570 28.197  1.00 31.87  ? 14   GLU C CB  1 
ATOM   3970  C CG  . GLU C  1 14  ? 49.169  64.866 28.764  1.00 33.94  ? 14   GLU C CG  1 
ATOM   3971  C CD  . GLU C  1 14  ? 48.359  65.391 29.942  1.00 33.85  ? 14   GLU C CD  1 
ATOM   3972  O OE1 . GLU C  1 14  ? 48.217  64.650 30.950  1.00 33.22  ? 14   GLU C OE1 1 
ATOM   3973  O OE2 . GLU C  1 14  ? 47.860  66.542 29.859  1.00 34.64  ? 14   GLU C OE2 1 
ATOM   3974  N N   . GLN C  1 15  ? 48.904  60.282 28.643  1.00 29.81  ? 15   GLN C N   1 
ATOM   3975  C CA  . GLN C  1 15  ? 48.318  58.961 28.477  1.00 28.46  ? 15   GLN C CA  1 
ATOM   3976  C C   . GLN C  1 15  ? 47.130  58.776 29.409  1.00 27.11  ? 15   GLN C C   1 
ATOM   3977  O O   . GLN C  1 15  ? 47.066  59.386 30.471  1.00 27.37  ? 15   GLN C O   1 
ATOM   3978  C CB  . GLN C  1 15  ? 49.353  57.885 28.775  1.00 29.56  ? 15   GLN C CB  1 
ATOM   3979  C CG  . GLN C  1 15  ? 50.658  58.053 28.020  1.00 31.29  ? 15   GLN C CG  1 
ATOM   3980  C CD  . GLN C  1 15  ? 51.630  56.921 28.274  1.00 32.61  ? 15   GLN C CD  1 
ATOM   3981  O OE1 . GLN C  1 15  ? 52.263  56.411 27.351  1.00 33.42  ? 15   GLN C OE1 1 
ATOM   3982  N NE2 . GLN C  1 15  ? 51.757  56.523 29.534  1.00 33.08  ? 15   GLN C NE2 1 
ATOM   3983  N N   . VAL C  1 16  ? 46.190  57.933 28.995  1.00 25.75  ? 16   VAL C N   1 
ATOM   3984  C CA  . VAL C  1 16  ? 45.052  57.571 29.829  1.00 24.70  ? 16   VAL C CA  1 
ATOM   3985  C C   . VAL C  1 16  ? 44.877  56.065 29.794  1.00 24.37  ? 16   VAL C C   1 
ATOM   3986  O O   . VAL C  1 16  ? 45.315  55.416 28.849  1.00 24.57  ? 16   VAL C O   1 
ATOM   3987  C CB  . VAL C  1 16  ? 43.747  58.253 29.366  1.00 23.70  ? 16   VAL C CB  1 
ATOM   3988  C CG1 . VAL C  1 16  ? 43.911  59.765 29.367  1.00 24.31  ? 16   VAL C CG1 1 
ATOM   3989  C CG2 . VAL C  1 16  ? 43.318  57.757 27.990  1.00 23.08  ? 16   VAL C CG2 1 
ATOM   3990  N N   . ASP C  1 17  ? 44.236  55.519 30.823  1.00 24.07  ? 17   ASP C N   1 
ATOM   3991  C CA  . ASP C  1 17  ? 43.907  54.100 30.859  1.00 23.99  ? 17   ASP C CA  1 
ATOM   3992  C C   . ASP C  1 17  ? 42.449  53.878 30.471  1.00 22.97  ? 17   ASP C C   1 
ATOM   3993  O O   . ASP C  1 17  ? 41.595  54.741 30.681  1.00 22.34  ? 17   ASP C O   1 
ATOM   3994  C CB  . ASP C  1 17  ? 44.156  53.519 32.252  1.00 24.64  ? 17   ASP C CB  1 
ATOM   3995  C CG  . ASP C  1 17  ? 45.629  53.442 32.606  1.00 26.06  ? 17   ASP C CG  1 
ATOM   3996  O OD1 . ASP C  1 17  ? 46.466  53.224 31.706  1.00 26.81  ? 17   ASP C OD1 1 
ATOM   3997  O OD2 . ASP C  1 17  ? 45.953  53.585 33.805  1.00 26.70  ? 17   ASP C OD2 1 
ATOM   3998  N N   . THR C  1 18  ? 42.195  52.710 29.886  1.00 23.06  ? 18   THR C N   1 
ATOM   3999  C CA  . THR C  1 18  ? 40.849  52.214 29.609  1.00 22.55  ? 18   THR C CA  1 
ATOM   4000  C C   . THR C  1 18  ? 40.784  50.779 30.113  1.00 23.36  ? 18   THR C C   1 
ATOM   4001  O O   . THR C  1 18  ? 41.774  50.253 30.619  1.00 24.28  ? 18   THR C O   1 
ATOM   4002  C CB  . THR C  1 18  ? 40.527  52.240 28.099  1.00 22.09  ? 18   THR C CB  1 
ATOM   4003  O OG1 . THR C  1 18  ? 41.363  51.308 27.407  1.00 22.66  ? 18   THR C OG1 1 
ATOM   4004  C CG2 . THR C  1 18  ? 40.742  53.623 27.523  1.00 21.68  ? 18   THR C CG2 1 
ATOM   4005  N N   . ILE C  1 19  ? 39.633  50.139 29.965  1.00 23.44  ? 19   ILE C N   1 
ATOM   4006  C CA  . ILE C  1 19  ? 39.469  48.753 30.405  1.00 24.50  ? 19   ILE C CA  1 
ATOM   4007  C C   . ILE C  1 19  ? 40.369  47.801 29.603  1.00 25.57  ? 19   ILE C C   1 
ATOM   4008  O O   . ILE C  1 19  ? 41.052  46.949 30.170  1.00 26.64  ? 19   ILE C O   1 
ATOM   4009  C CB  . ILE C  1 19  ? 37.997  48.297 30.271  1.00 24.49  ? 19   ILE C CB  1 
ATOM   4010  C CG1 . ILE C  1 19  ? 37.073  49.135 31.167  1.00 23.96  ? 19   ILE C CG1 1 
ATOM   4011  C CG2 . ILE C  1 19  ? 37.847  46.821 30.611  1.00 25.76  ? 19   ILE C CG2 1 
ATOM   4012  C CD1 . ILE C  1 19  ? 37.184  48.838 32.648  1.00 24.44  ? 19   ILE C CD1 1 
ATOM   4013  N N   . MET C  1 20  ? 40.366  47.959 28.282  1.00 25.50  ? 20   MET C N   1 
ATOM   4014  C CA  . MET C  1 20  ? 41.074  47.045 27.390  1.00 26.65  ? 20   MET C CA  1 
ATOM   4015  C C   . MET C  1 20  ? 42.523  47.424 27.115  1.00 27.40  ? 20   MET C C   1 
ATOM   4016  O O   . MET C  1 20  ? 43.294  46.601 26.613  1.00 28.46  ? 20   MET C O   1 
ATOM   4017  C CB  . MET C  1 20  ? 40.356  46.975 26.050  1.00 26.14  ? 20   MET C CB  1 
ATOM   4018  C CG  . MET C  1 20  ? 38.987  46.339 26.107  1.00 26.28  ? 20   MET C CG  1 
ATOM   4019  S SD  . MET C  1 20  ? 38.400  46.045 24.436  1.00 26.21  ? 20   MET C SD  1 
ATOM   4020  C CE  . MET C  1 20  ? 36.844  45.251 24.787  1.00 26.95  ? 20   MET C CE  1 
ATOM   4021  N N   . GLU C  1 21  ? 42.890  48.669 27.401  1.00 27.21  ? 21   GLU C N   1 
ATOM   4022  C CA  . GLU C  1 21  ? 44.226  49.145 27.075  1.00 28.18  ? 21   GLU C CA  1 
ATOM   4023  C C   . GLU C  1 21  ? 44.697  50.197 28.066  1.00 28.54  ? 21   GLU C C   1 
ATOM   4024  O O   . GLU C  1 21  ? 43.940  51.091 28.450  1.00 27.58  ? 21   GLU C O   1 
ATOM   4025  C CB  . GLU C  1 21  ? 44.244  49.711 25.658  1.00 27.62  ? 21   GLU C CB  1 
ATOM   4026  C CG  . GLU C  1 21  ? 45.619  49.713 25.010  1.00 28.70  ? 21   GLU C CG  1 
ATOM   4027  C CD  . GLU C  1 21  ? 45.606  50.262 23.588  1.00 28.22  ? 21   GLU C CD  1 
ATOM   4028  O OE1 . GLU C  1 21  ? 44.506  50.392 22.997  1.00 27.26  ? 21   GLU C OE1 1 
ATOM   4029  O OE2 . GLU C  1 21  ? 46.701  50.560 23.059  1.00 28.96  ? 21   GLU C OE2 1 
ATOM   4030  N N   . LYS C  1 22  ? 45.959  50.081 28.468  1.00 30.42  ? 22   LYS C N   1 
ATOM   4031  C CA  . LYS C  1 22  ? 46.573  51.016 29.398  1.00 31.25  ? 22   LYS C CA  1 
ATOM   4032  C C   . LYS C  1 22  ? 47.593  51.872 28.674  1.00 32.37  ? 22   LYS C C   1 
ATOM   4033  O O   . LYS C  1 22  ? 48.134  51.462 27.655  1.00 32.95  ? 22   LYS C O   1 
ATOM   4034  C CB  . LYS C  1 22  ? 47.240  50.255 30.547  1.00 32.65  ? 22   LYS C CB  1 
ATOM   4035  C CG  . LYS C  1 22  ? 46.350  50.050 31.765  1.00 32.20  ? 22   LYS C CG  1 
ATOM   4036  C CD  . LYS C  1 22  ? 46.145  48.563 32.065  1.00 33.18  ? 22   LYS C CD  1 
ATOM   4037  C CE  . LYS C  1 22  ? 47.369  48.003 32.775  1.00 35.20  ? 22   LYS C CE  1 
ATOM   4038  N NZ  . LYS C  1 22  ? 47.366  48.318 34.235  1.00 35.39  ? 22   LYS C NZ  1 
ATOM   4039  N N   . ASN C  1 23  ? 47.845  53.061 29.211  1.00 33.23  ? 23   ASN C N   1 
ATOM   4040  C CA  . ASN C  1 23  ? 48.853  53.973 28.672  1.00 34.82  ? 23   ASN C CA  1 
ATOM   4041  C C   . ASN C  1 23  ? 48.599  54.348 27.209  1.00 32.95  ? 23   ASN C C   1 
ATOM   4042  O O   . ASN C  1 23  ? 49.512  54.342 26.384  1.00 33.78  ? 23   ASN C O   1 
ATOM   4043  C CB  . ASN C  1 23  ? 50.266  53.388 28.865  1.00 38.64  ? 23   ASN C CB  1 
ATOM   4044  C CG  . ASN C  1 23  ? 50.653  53.265 30.330  1.00 42.13  ? 23   ASN C CG  1 
ATOM   4045  O OD1 . ASN C  1 23  ? 50.080  53.942 31.190  1.00 41.76  ? 23   ASN C OD1 1 
ATOM   4046  N ND2 . ASN C  1 23  ? 51.635  52.404 30.624  1.00 47.24  ? 23   ASN C ND2 1 
ATOM   4047  N N   . VAL C  1 24  ? 47.347  54.683 26.908  1.00 30.31  ? 24   VAL C N   1 
ATOM   4048  C CA  . VAL C  1 24  ? 46.952  55.157 25.580  1.00 28.82  ? 24   VAL C CA  1 
ATOM   4049  C C   . VAL C  1 24  ? 47.267  56.650 25.454  1.00 28.51  ? 24   VAL C C   1 
ATOM   4050  O O   . VAL C  1 24  ? 46.715  57.463 26.192  1.00 28.02  ? 24   VAL C O   1 
ATOM   4051  C CB  . VAL C  1 24  ? 45.439  54.942 25.339  1.00 27.31  ? 24   VAL C CB  1 
ATOM   4052  C CG1 . VAL C  1 24  ? 45.008  55.548 24.010  1.00 26.71  ? 24   VAL C CG1 1 
ATOM   4053  C CG2 . VAL C  1 24  ? 45.091  53.459 25.395  1.00 27.20  ? 24   VAL C CG2 1 
ATOM   4054  N N   . THR C  1 25  ? 48.144  57.008 24.518  1.00 28.71  ? 25   THR C N   1 
ATOM   4055  C CA  . THR C  1 25  ? 48.520  58.408 24.317  1.00 28.97  ? 25   THR C CA  1 
ATOM   4056  C C   . THR C  1 25  ? 47.386  59.173 23.645  1.00 27.53  ? 25   THR C C   1 
ATOM   4057  O O   . THR C  1 25  ? 46.874  58.743 22.609  1.00 26.69  ? 25   THR C O   1 
ATOM   4058  C CB  . THR C  1 25  ? 49.778  58.552 23.441  1.00 30.38  ? 25   THR C CB  1 
ATOM   4059  O OG1 . THR C  1 25  ? 50.763  57.598 23.847  1.00 31.52  ? 25   THR C OG1 1 
ATOM   4060  C CG2 . THR C  1 25  ? 50.355  59.950 23.567  1.00 31.68  ? 25   THR C CG2 1 
ATOM   4061  N N   . VAL C  1 26  ? 47.008  60.305 24.234  1.00 27.30  ? 26   VAL C N   1 
ATOM   4062  C CA  . VAL C  1 26  ? 45.901  61.116 23.728  1.00 26.36  ? 26   VAL C CA  1 
ATOM   4063  C C   . VAL C  1 26  ? 46.341  62.545 23.481  1.00 27.48  ? 26   VAL C C   1 
ATOM   4064  O O   . VAL C  1 26  ? 47.313  63.013 24.067  1.00 28.84  ? 26   VAL C O   1 
ATOM   4065  C CB  . VAL C  1 26  ? 44.688  61.117 24.683  1.00 25.38  ? 26   VAL C CB  1 
ATOM   4066  C CG1 . VAL C  1 26  ? 44.060  59.736 24.735  1.00 24.19  ? 26   VAL C CG1 1 
ATOM   4067  C CG2 . VAL C  1 26  ? 45.078  61.589 26.078  1.00 26.11  ? 26   VAL C CG2 1 
ATOM   4068  N N   . THR C  1 27  ? 45.606  63.233 22.615  1.00 27.10  ? 27   THR C N   1 
ATOM   4069  C CA  . THR C  1 27  ? 45.943  64.599 22.231  1.00 28.43  ? 27   THR C CA  1 
ATOM   4070  C C   . THR C  1 27  ? 45.657  65.576 23.361  1.00 29.14  ? 27   THR C C   1 
ATOM   4071  O O   . THR C  1 27  ? 46.384  66.550 23.543  1.00 30.96  ? 27   THR C O   1 
ATOM   4072  C CB  . THR C  1 27  ? 45.176  65.052 20.969  1.00 28.13  ? 27   THR C CB  1 
ATOM   4073  O OG1 . THR C  1 27  ? 43.768  65.081 21.231  1.00 27.10  ? 27   THR C OG1 1 
ATOM   4074  C CG2 . THR C  1 27  ? 45.457  64.119 19.805  1.00 27.42  ? 27   THR C CG2 1 
ATOM   4075  N N   . HIS C  1 28  ? 44.581  65.326 24.100  1.00 27.93  ? 28   HIS C N   1 
ATOM   4076  C CA  . HIS C  1 28  ? 44.208  66.162 25.233  1.00 28.51  ? 28   HIS C CA  1 
ATOM   4077  C C   . HIS C  1 28  ? 43.687  65.294 26.353  1.00 27.29  ? 28   HIS C C   1 
ATOM   4078  O O   . HIS C  1 28  ? 43.069  64.255 26.111  1.00 25.93  ? 28   HIS C O   1 
ATOM   4079  C CB  . HIS C  1 28  ? 43.137  67.171 24.830  1.00 28.89  ? 28   HIS C CB  1 
ATOM   4080  C CG  . HIS C  1 28  ? 43.521  68.012 23.657  1.00 30.11  ? 28   HIS C CG  1 
ATOM   4081  N ND1 . HIS C  1 28  ? 43.433  67.557 22.359  1.00 29.43  ? 28   HIS C ND1 1 
ATOM   4082  C CD2 . HIS C  1 28  ? 44.012  69.271 23.583  1.00 32.12  ? 28   HIS C CD2 1 
ATOM   4083  C CE1 . HIS C  1 28  ? 43.849  68.501 21.537  1.00 30.90  ? 28   HIS C CE1 1 
ATOM   4084  N NE2 . HIS C  1 28  ? 44.205  69.551 22.254  1.00 32.61  ? 28   HIS C NE2 1 
ATOM   4085  N N   . ALA C  1 29  ? 43.925  65.735 27.579  1.00 27.97  ? 29   ALA C N   1 
ATOM   4086  C CA  . ALA C  1 29  ? 43.488  65.014 28.762  1.00 27.06  ? 29   ALA C CA  1 
ATOM   4087  C C   . ALA C  1 29  ? 43.212  66.006 29.877  1.00 27.98  ? 29   ALA C C   1 
ATOM   4088  O O   . ALA C  1 29  ? 43.513  67.191 29.750  1.00 29.50  ? 29   ALA C O   1 
ATOM   4089  C CB  . ALA C  1 29  ? 44.550  64.016 29.190  1.00 26.99  ? 29   ALA C CB  1 
ATOM   4090  N N   . GLN C  1 30  ? 42.622  65.523 30.963  1.00 27.24  ? 30   GLN C N   1 
ATOM   4091  C CA  . GLN C  1 30  ? 42.360  66.368 32.118  1.00 28.12  ? 30   GLN C CA  1 
ATOM   4092  C C   . GLN C  1 30  ? 42.579  65.597 33.408  1.00 27.58  ? 30   GLN C C   1 
ATOM   4093  O O   . GLN C  1 30  ? 41.814  64.690 33.740  1.00 26.30  ? 30   GLN C O   1 
ATOM   4094  C CB  . GLN C  1 30  ? 40.938  66.937 32.078  1.00 28.04  ? 30   GLN C CB  1 
ATOM   4095  C CG  . GLN C  1 30  ? 40.673  67.954 33.181  1.00 29.29  ? 30   GLN C CG  1 
ATOM   4096  C CD  . GLN C  1 30  ? 39.394  68.746 32.981  1.00 29.84  ? 30   GLN C CD  1 
ATOM   4097  O OE1 . GLN C  1 30  ? 38.912  68.908 31.861  1.00 29.90  ? 30   GLN C OE1 1 
ATOM   4098  N NE2 . GLN C  1 30  ? 38.840  69.255 34.075  1.00 30.48  ? 30   GLN C NE2 1 
ATOM   4099  N N   . ASP C  1 31  ? 43.631  65.968 34.131  1.00 28.73  ? 31   ASP C N   1 
ATOM   4100  C CA  . ASP C  1 31  ? 43.868  65.431 35.461  1.00 28.58  ? 31   ASP C CA  1 
ATOM   4101  C C   . ASP C  1 31  ? 42.809  65.996 36.406  1.00 28.47  ? 31   ASP C C   1 
ATOM   4102  O O   . ASP C  1 31  ? 42.537  67.200 36.397  1.00 29.55  ? 31   ASP C O   1 
ATOM   4103  C CB  . ASP C  1 31  ? 45.269  65.801 35.949  1.00 30.24  ? 31   ASP C CB  1 
ATOM   4104  C CG  . ASP C  1 31  ? 45.729  64.949 37.119  1.00 30.14  ? 31   ASP C CG  1 
ATOM   4105  O OD1 . ASP C  1 31  ? 44.883  64.305 37.777  1.00 28.95  ? 31   ASP C OD1 1 
ATOM   4106  O OD2 . ASP C  1 31  ? 46.953  64.926 37.378  1.00 31.50  ? 31   ASP C OD2 1 
ATOM   4107  N N   . ILE C  1 32  ? 42.206  65.114 37.197  1.00 27.30  ? 32   ILE C N   1 
ATOM   4108  C CA  . ILE C  1 32  ? 41.165  65.501 38.152  1.00 27.20  ? 32   ILE C CA  1 
ATOM   4109  C C   . ILE C  1 32  ? 41.544  65.175 39.603  1.00 27.37  ? 32   ILE C C   1 
ATOM   4110  O O   . ILE C  1 32  ? 40.738  65.362 40.514  1.00 27.31  ? 32   ILE C O   1 
ATOM   4111  C CB  . ILE C  1 32  ? 39.818  64.835 37.800  1.00 25.91  ? 32   ILE C CB  1 
ATOM   4112  C CG1 . ILE C  1 32  ? 39.973  63.320 37.650  1.00 24.71  ? 32   ILE C CG1 1 
ATOM   4113  C CG2 . ILE C  1 32  ? 39.262  65.429 36.517  1.00 26.06  ? 32   ILE C CG2 1 
ATOM   4114  C CD1 . ILE C  1 32  ? 38.665  62.572 37.730  1.00 23.77  ? 32   ILE C CD1 1 
ATOM   4115  N N   . LEU C  1 33  ? 42.770  64.705 39.813  1.00 27.75  ? 33   LEU C N   1 
ATOM   4116  C CA  . LEU C  1 33  ? 43.254  64.341 41.140  1.00 28.10  ? 33   LEU C CA  1 
ATOM   4117  C C   . LEU C  1 33  ? 44.306  65.332 41.634  1.00 29.95  ? 33   LEU C C   1 
ATOM   4118  O O   . LEU C  1 33  ? 45.373  65.465 41.030  1.00 30.91  ? 33   LEU C O   1 
ATOM   4119  C CB  . LEU C  1 33  ? 43.868  62.943 41.099  1.00 27.51  ? 33   LEU C CB  1 
ATOM   4120  C CG  . LEU C  1 33  ? 44.331  62.350 42.429  1.00 27.85  ? 33   LEU C CG  1 
ATOM   4121  C CD1 . LEU C  1 33  ? 43.137  62.078 43.327  1.00 26.96  ? 33   LEU C CD1 1 
ATOM   4122  C CD2 . LEU C  1 33  ? 45.121  61.072 42.190  1.00 27.83  ? 33   LEU C CD2 1 
ATOM   4123  N N   . GLU C  1 34  ? 44.011  66.015 42.737  1.00 30.66  ? 34   GLU C N   1 
ATOM   4124  C CA  . GLU C  1 34  ? 45.000  66.873 43.387  1.00 32.61  ? 34   GLU C CA  1 
ATOM   4125  C C   . GLU C  1 34  ? 45.983  66.026 44.192  1.00 32.97  ? 34   GLU C C   1 
ATOM   4126  O O   . GLU C  1 34  ? 45.594  65.343 45.137  1.00 32.20  ? 34   GLU C O   1 
ATOM   4127  C CB  . GLU C  1 34  ? 44.324  67.903 44.294  1.00 33.38  ? 34   GLU C CB  1 
ATOM   4128  C CG  . GLU C  1 34  ? 45.301  68.854 44.970  1.00 35.64  ? 34   GLU C CG  1 
ATOM   4129  C CD  . GLU C  1 34  ? 46.317  69.421 43.999  1.00 37.18  ? 34   GLU C CD  1 
ATOM   4130  O OE1 . GLU C  1 34  ? 45.918  70.158 43.074  1.00 37.53  ? 34   GLU C OE1 1 
ATOM   4131  O OE2 . GLU C  1 34  ? 47.512  69.093 44.140  1.00 38.19  ? 34   GLU C OE2 1 
ATOM   4132  N N   . LYS C  1 35  ? 47.258  66.089 43.822  1.00 34.39  ? 35   LYS C N   1 
ATOM   4133  C CA  . LYS C  1 35  ? 48.288  65.235 44.423  1.00 35.08  ? 35   LYS C CA  1 
ATOM   4134  C C   . LYS C  1 35  ? 49.191  65.958 45.431  1.00 37.31  ? 35   LYS C C   1 
ATOM   4135  O O   . LYS C  1 35  ? 49.916  65.297 46.181  1.00 38.00  ? 35   LYS C O   1 
ATOM   4136  C CB  . LYS C  1 35  ? 49.146  64.587 43.323  1.00 35.31  ? 35   LYS C CB  1 
ATOM   4137  C CG  . LYS C  1 35  ? 48.591  63.274 42.789  1.00 33.40  ? 35   LYS C CG  1 
ATOM   4138  C CD  . LYS C  1 35  ? 49.360  62.782 41.568  1.00 33.74  ? 35   LYS C CD  1 
ATOM   4139  C CE  . LYS C  1 35  ? 48.618  63.037 40.261  1.00 32.54  ? 35   LYS C CE  1 
ATOM   4140  N NZ  . LYS C  1 35  ? 48.206  64.454 40.039  1.00 33.02  ? 35   LYS C NZ  1 
ATOM   4141  N N   . THR C  1 36  ? 49.134  67.292 45.472  1.00 38.64  ? 36   THR C N   1 
ATOM   4142  C CA  . THR C  1 36  ? 50.068  68.080 46.287  1.00 41.18  ? 36   THR C CA  1 
ATOM   4143  C C   . THR C  1 36  ? 49.417  68.852 47.438  1.00 41.60  ? 36   THR C C   1 
ATOM   4144  O O   . THR C  1 36  ? 48.220  69.134 47.422  1.00 40.33  ? 36   THR C O   1 
ATOM   4145  C CB  . THR C  1 36  ? 50.852  69.095 45.427  1.00 43.31  ? 36   THR C CB  1 
ATOM   4146  O OG1 . THR C  1 36  ? 49.952  70.061 44.870  1.00 43.04  ? 36   THR C OG1 1 
ATOM   4147  C CG2 . THR C  1 36  ? 51.606  68.388 44.312  1.00 43.28  ? 36   THR C CG2 1 
ATOM   4148  N N   . HIS C  1 37  ? 50.246  69.179 48.430  1.00 43.64  ? 37   HIS C N   1 
ATOM   4149  C CA  . HIS C  1 37  ? 49.882  70.047 49.552  1.00 44.66  ? 37   HIS C CA  1 
ATOM   4150  C C   . HIS C  1 37  ? 51.126  70.859 49.925  1.00 47.90  ? 37   HIS C C   1 
ATOM   4151  O O   . HIS C  1 37  ? 52.232  70.513 49.506  1.00 49.12  ? 37   HIS C O   1 
ATOM   4152  C CB  . HIS C  1 37  ? 49.403  69.213 50.746  1.00 43.31  ? 37   HIS C CB  1 
ATOM   4153  C CG  . HIS C  1 37  ? 50.413  68.221 51.237  1.00 43.84  ? 37   HIS C CG  1 
ATOM   4154  N ND1 . HIS C  1 37  ? 51.188  68.442 52.355  1.00 45.79  ? 37   HIS C ND1 1 
ATOM   4155  C CD2 . HIS C  1 37  ? 50.783  67.009 50.757  1.00 42.93  ? 37   HIS C CD2 1 
ATOM   4156  C CE1 . HIS C  1 37  ? 51.988  67.408 52.548  1.00 46.08  ? 37   HIS C CE1 1 
ATOM   4157  N NE2 . HIS C  1 37  ? 51.762  66.525 51.592  1.00 44.41  ? 37   HIS C NE2 1 
ATOM   4158  N N   . ASN C  1 38  ? 50.957  71.931 50.700  1.00 49.53  ? 38   ASN C N   1 
ATOM   4159  C CA  . ASN C  1 38  ? 52.101  72.787 51.071  1.00 52.95  ? 38   ASN C CA  1 
ATOM   4160  C C   . ASN C  1 38  ? 52.971  72.227 52.210  1.00 54.07  ? 38   ASN C C   1 
ATOM   4161  O O   . ASN C  1 38  ? 54.123  72.630 52.369  1.00 56.97  ? 38   ASN C O   1 
ATOM   4162  C CB  . ASN C  1 38  ? 51.656  74.233 51.377  1.00 54.72  ? 38   ASN C CB  1 
ATOM   4163  C CG  . ASN C  1 38  ? 50.735  74.338 52.581  1.00 53.82  ? 38   ASN C CG  1 
ATOM   4164  O OD1 . ASN C  1 38  ? 50.569  73.389 53.347  1.00 52.22  ? 38   ASN C OD1 1 
ATOM   4165  N ND2 . ASN C  1 38  ? 50.131  75.508 52.752  1.00 55.04  ? 38   ASN C ND2 1 
ATOM   4166  N N   . GLY C  1 39  ? 52.411  71.315 53.000  1.00 52.04  ? 39   GLY C N   1 
ATOM   4167  C CA  . GLY C  1 39  ? 53.155  70.618 54.060  1.00 52.86  ? 39   GLY C CA  1 
ATOM   4168  C C   . GLY C  1 39  ? 53.049  71.289 55.417  1.00 54.20  ? 39   GLY C C   1 
ATOM   4169  O O   . GLY C  1 39  ? 53.803  70.960 56.339  1.00 55.56  ? 39   GLY C O   1 
ATOM   4170  N N   . LYS C  1 40  ? 52.096  72.211 55.545  1.00 53.91  ? 40   LYS C N   1 
ATOM   4171  C CA  . LYS C  1 40  ? 51.995  73.077 56.712  1.00 55.60  ? 40   LYS C CA  1 
ATOM   4172  C C   . LYS C  1 40  ? 50.598  73.080 57.319  1.00 53.52  ? 40   LYS C C   1 
ATOM   4173  O O   . LYS C  1 40  ? 49.605  72.854 56.629  1.00 51.34  ? 40   LYS C O   1 
ATOM   4174  C CB  . LYS C  1 40  ? 52.371  74.504 56.318  1.00 58.51  ? 40   LYS C CB  1 
ATOM   4175  C CG  . LYS C  1 40  ? 53.863  74.716 56.119  1.00 61.61  ? 40   LYS C CG  1 
ATOM   4176  C CD  . LYS C  1 40  ? 54.138  75.758 55.048  1.00 63.62  ? 40   LYS C CD  1 
ATOM   4177  C CE  . LYS C  1 40  ? 55.620  76.079 54.959  1.00 67.23  ? 40   LYS C CE  1 
ATOM   4178  N NZ  . LYS C  1 40  ? 55.929  76.968 53.804  1.00 69.18  ? 40   LYS C NZ  1 
ATOM   4179  N N   . LEU C  1 41  ? 50.539  73.345 58.620  1.00 54.42  ? 41   LEU C N   1 
ATOM   4180  C CA  . LEU C  1 41  ? 49.279  73.577 59.319  1.00 53.12  ? 41   LEU C CA  1 
ATOM   4181  C C   . LEU C  1 41  ? 48.969  75.073 59.223  1.00 55.16  ? 41   LEU C C   1 
ATOM   4182  O O   . LEU C  1 41  ? 49.788  75.909 59.613  1.00 58.11  ? 41   LEU C O   1 
ATOM   4183  C CB  . LEU C  1 41  ? 49.391  73.119 60.778  1.00 53.21  ? 41   LEU C CB  1 
ATOM   4184  C CG  . LEU C  1 41  ? 49.392  71.602 61.077  1.00 51.08  ? 41   LEU C CG  1 
ATOM   4185  C CD1 . LEU C  1 41  ? 48.150  71.192 61.858  1.00 49.03  ? 41   LEU C CD1 1 
ATOM   4186  C CD2 . LEU C  1 41  ? 49.540  70.713 59.840  1.00 49.51  ? 41   LEU C CD2 1 
ATOM   4187  N N   . CYS C  1 42  ? 47.789  75.397 58.696  1.00 53.83  ? 42   CYS C N   1 
ATOM   4188  C CA  . CYS C  1 42  ? 47.465  76.764 58.292  1.00 55.84  ? 42   CYS C CA  1 
ATOM   4189  C C   . CYS C  1 42  ? 46.198  77.293 58.941  1.00 55.54  ? 42   CYS C C   1 
ATOM   4190  O O   . CYS C  1 42  ? 45.377  76.532 59.446  1.00 53.27  ? 42   CYS C O   1 
ATOM   4191  C CB  . CYS C  1 42  ? 47.275  76.839 56.764  1.00 55.16  ? 42   CYS C CB  1 
ATOM   4192  S SG  . CYS C  1 42  ? 48.711  76.528 55.691  1.00 56.08  ? 42   CYS C SG  1 
ATOM   4193  N N   . ASP C  1 43  ? 46.045  78.614 58.898  1.00 58.11  ? 43   ASP C N   1 
ATOM   4194  C CA  . ASP C  1 43  ? 44.787  79.260 59.254  1.00 58.26  ? 43   ASP C CA  1 
ATOM   4195  C C   . ASP C  1 43  ? 43.720  78.839 58.254  1.00 55.93  ? 43   ASP C C   1 
ATOM   4196  O O   . ASP C  1 43  ? 43.978  78.808 57.051  1.00 55.68  ? 43   ASP C O   1 
ATOM   4197  C CB  . ASP C  1 43  ? 44.930  80.788 59.230  1.00 61.93  ? 43   ASP C CB  1 
ATOM   4198  C CG  . ASP C  1 43  ? 45.842  81.318 60.328  1.00 64.62  ? 43   ASP C CG  1 
ATOM   4199  O OD1 . ASP C  1 43  ? 46.311  80.523 61.167  1.00 63.58  ? 43   ASP C OD1 1 
ATOM   4200  O OD2 . ASP C  1 43  ? 46.093  82.541 60.351  1.00 67.98  ? 43   ASP C OD2 1 
ATOM   4201  N N   . LEU C  1 44  ? 42.529  78.515 58.750  1.00 54.38  ? 44   LEU C N   1 
ATOM   4202  C CA  . LEU C  1 44  ? 41.404  78.159 57.885  1.00 52.51  ? 44   LEU C CA  1 
ATOM   4203  C C   . LEU C  1 44  ? 40.473  79.354 57.727  1.00 54.51  ? 44   LEU C C   1 
ATOM   4204  O O   . LEU C  1 44  ? 39.906  79.839 58.704  1.00 55.60  ? 44   LEU C O   1 
ATOM   4205  C CB  . LEU C  1 44  ? 40.623  76.979 58.464  1.00 49.75  ? 44   LEU C CB  1 
ATOM   4206  C CG  . LEU C  1 44  ? 39.591  76.342 57.524  1.00 47.62  ? 44   LEU C CG  1 
ATOM   4207  C CD1 . LEU C  1 44  ? 40.276  75.424 56.520  1.00 45.93  ? 44   LEU C CD1 1 
ATOM   4208  C CD2 . LEU C  1 44  ? 38.536  75.572 58.308  1.00 45.91  ? 44   LEU C CD2 1 
ATOM   4209  N N   . ASP C  1 45  ? 40.324  79.824 56.493  1.00 55.17  ? 45   ASP C N   1 
ATOM   4210  C CA  . ASP C  1 45  ? 39.477  80.977 56.191  1.00 57.40  ? 45   ASP C CA  1 
ATOM   4211  C C   . ASP C  1 45  ? 39.921  82.211 56.989  1.00 60.87  ? 45   ASP C C   1 
ATOM   4212  O O   . ASP C  1 45  ? 39.094  83.035 57.390  1.00 62.71  ? 45   ASP C O   1 
ATOM   4213  C CB  . ASP C  1 45  ? 38.006  80.641 56.485  1.00 56.12  ? 45   ASP C CB  1 
ATOM   4214  C CG  . ASP C  1 45  ? 37.038  81.478 55.666  1.00 57.72  ? 45   ASP C CG  1 
ATOM   4215  O OD1 . ASP C  1 45  ? 36.939  81.238 54.443  1.00 56.86  ? 45   ASP C OD1 1 
ATOM   4216  O OD2 . ASP C  1 45  ? 36.373  82.365 56.245  1.00 59.98  ? 45   ASP C OD2 1 
ATOM   4217  N N   . GLY C  1 46  ? 41.230  82.321 57.222  1.00 61.96  ? 46   GLY C N   1 
ATOM   4218  C CA  . GLY C  1 46  ? 41.798  83.398 58.040  1.00 65.37  ? 46   GLY C CA  1 
ATOM   4219  C C   . GLY C  1 46  ? 41.784  83.125 59.536  1.00 65.05  ? 46   GLY C C   1 
ATOM   4220  O O   . GLY C  1 46  ? 42.539  83.748 60.283  1.00 67.52  ? 46   GLY C O   1 
ATOM   4221  N N   . VAL C  1 47  ? 40.938  82.187 59.971  1.00 62.12  ? 47   VAL C N   1 
ATOM   4222  C CA  . VAL C  1 47  ? 40.730  81.901 61.394  1.00 61.69  ? 47   VAL C CA  1 
ATOM   4223  C C   . VAL C  1 47  ? 41.746  80.869 61.882  1.00 60.02  ? 47   VAL C C   1 
ATOM   4224  O O   . VAL C  1 47  ? 41.765  79.734 61.403  1.00 57.24  ? 47   VAL C O   1 
ATOM   4225  C CB  . VAL C  1 47  ? 39.303  81.373 61.655  1.00 59.63  ? 47   VAL C CB  1 
ATOM   4226  C CG1 . VAL C  1 47  ? 39.093  81.101 63.137  1.00 59.36  ? 47   VAL C CG1 1 
ATOM   4227  C CG2 . VAL C  1 47  ? 38.263  82.361 61.144  1.00 61.45  ? 47   VAL C CG2 1 
ATOM   4228  N N   . LYS C  1 48  ? 42.568  81.266 62.850  1.00 61.95  ? 48   LYS C N   1 
ATOM   4229  C CA  . LYS C  1 48  ? 43.692  80.449 63.312  1.00 61.18  ? 48   LYS C CA  1 
ATOM   4230  C C   . LYS C  1 48  ? 43.232  79.190 64.054  1.00 58.13  ? 48   LYS C C   1 
ATOM   4231  O O   . LYS C  1 48  ? 42.280  79.248 64.836  1.00 57.70  ? 48   LYS C O   1 
ATOM   4232  C CB  . LYS C  1 48  ? 44.598  81.273 64.239  1.00 64.44  ? 48   LYS C CB  1 
ATOM   4233  C CG  . LYS C  1 48  ? 46.043  80.803 64.277  1.00 65.01  ? 48   LYS C CG  1 
ATOM   4234  C CD  . LYS C  1 48  ? 46.670  80.980 65.646  1.00 66.80  ? 48   LYS C CD  1 
ATOM   4235  C CE  . LYS C  1 48  ? 48.115  80.560 65.619  1.00 67.79  ? 48   LYS C CE  1 
ATOM   4236  N NZ  . LYS C  1 48  ? 48.581  80.046 66.930  1.00 67.90  ? 48   LYS C NZ  1 
ATOM   4237  N N   . PRO C  1 49  ? 43.905  78.046 63.812  1.00 56.19  ? 49   PRO C N   1 
ATOM   4238  C CA  . PRO C  1 49  ? 43.613  76.868 64.631  1.00 53.83  ? 49   PRO C CA  1 
ATOM   4239  C C   . PRO C  1 49  ? 44.147  76.991 66.050  1.00 55.18  ? 49   PRO C C   1 
ATOM   4240  O O   . PRO C  1 49  ? 45.145  77.676 66.278  1.00 57.74  ? 49   PRO C O   1 
ATOM   4241  C CB  . PRO C  1 49  ? 44.365  75.745 63.913  1.00 52.14  ? 49   PRO C CB  1 
ATOM   4242  C CG  . PRO C  1 49  ? 45.478  76.437 63.206  1.00 54.38  ? 49   PRO C CG  1 
ATOM   4243  C CD  . PRO C  1 49  ? 44.863  77.724 62.737  1.00 56.07  ? 49   PRO C CD  1 
ATOM   4244  N N   . LEU C  1 50  ? 43.484  76.319 66.985  1.00 53.59  ? 50   LEU C N   1 
ATOM   4245  C CA  . LEU C  1 50  ? 44.004  76.158 68.334  1.00 54.40  ? 50   LEU C CA  1 
ATOM   4246  C C   . LEU C  1 50  ? 45.032  75.038 68.306  1.00 53.47  ? 50   LEU C C   1 
ATOM   4247  O O   . LEU C  1 50  ? 44.672  73.866 68.212  1.00 51.04  ? 50   LEU C O   1 
ATOM   4248  C CB  . LEU C  1 50  ? 42.871  75.825 69.313  1.00 53.11  ? 50   LEU C CB  1 
ATOM   4249  C CG  . LEU C  1 50  ? 43.244  75.313 70.709  1.00 53.21  ? 50   LEU C CG  1 
ATOM   4250  C CD1 . LEU C  1 50  ? 44.276  76.207 71.382  1.00 56.23  ? 50   LEU C CD1 1 
ATOM   4251  C CD2 . LEU C  1 50  ? 41.996  75.201 71.570  1.00 52.27  ? 50   LEU C CD2 1 
ATOM   4252  N N   . ILE C  1 51  ? 46.309  75.402 68.367  1.00 55.69  ? 51   ILE C N   1 
ATOM   4253  C CA  . ILE C  1 51  ? 47.384  74.416 68.382  1.00 55.42  ? 51   ILE C CA  1 
ATOM   4254  C C   . ILE C  1 51  ? 47.843  74.216 69.818  1.00 56.49  ? 51   ILE C C   1 
ATOM   4255  O O   . ILE C  1 51  ? 48.475  75.096 70.405  1.00 59.24  ? 51   ILE C O   1 
ATOM   4256  C CB  . ILE C  1 51  ? 48.570  74.839 67.490  1.00 57.41  ? 51   ILE C CB  1 
ATOM   4257  C CG1 . ILE C  1 51  ? 48.050  75.272 66.115  1.00 56.74  ? 51   ILE C CG1 1 
ATOM   4258  C CG2 . ILE C  1 51  ? 49.578  73.697 67.368  1.00 57.00  ? 51   ILE C CG2 1 
ATOM   4259  C CD1 . ILE C  1 51  ? 49.096  75.313 65.022  1.00 57.85  ? 51   ILE C CD1 1 
ATOM   4260  N N   . LEU C  1 52  ? 47.528  73.050 70.373  1.00 54.48  ? 52   LEU C N   1 
ATOM   4261  C CA  . LEU C  1 52  ? 47.838  72.749 71.771  1.00 55.23  ? 52   LEU C CA  1 
ATOM   4262  C C   . LEU C  1 52  ? 49.324  72.439 71.997  1.00 57.22  ? 52   LEU C C   1 
ATOM   4263  O O   . LEU C  1 52  ? 49.780  72.383 73.140  1.00 58.55  ? 52   LEU C O   1 
ATOM   4264  C CB  . LEU C  1 52  ? 46.971  71.587 72.262  1.00 52.58  ? 52   LEU C CB  1 
ATOM   4265  C CG  . LEU C  1 52  ? 45.455  71.788 72.135  1.00 50.80  ? 52   LEU C CG  1 
ATOM   4266  C CD1 . LEU C  1 52  ? 44.712  70.520 72.520  1.00 48.43  ? 52   LEU C CD1 1 
ATOM   4267  C CD2 . LEU C  1 52  ? 44.980  72.956 72.985  1.00 52.38  ? 52   LEU C CD2 1 
ATOM   4268  N N   . ARG C  1 53  ? 50.064  72.244 70.906  1.00 57.57  ? 53   ARG C N   1 
ATOM   4269  C CA  . ARG C  1 53  ? 51.490  71.938 70.950  1.00 59.71  ? 53   ARG C CA  1 
ATOM   4270  C C   . ARG C  1 53  ? 51.704  70.610 71.699  1.00 58.77  ? 53   ARG C C   1 
ATOM   4271  O O   . ARG C  1 53  ? 51.278  69.563 71.202  1.00 56.46  ? 53   ARG C O   1 
ATOM   4272  C CB  . ARG C  1 53  ? 52.292  73.120 71.526  1.00 63.32  ? 53   ARG C CB  1 
ATOM   4273  C CG  . ARG C  1 53  ? 53.793  73.033 71.273  1.00 66.07  ? 53   ARG C CG  1 
ATOM   4274  C CD  . ARG C  1 53  ? 54.575  74.166 71.936  1.00 69.94  ? 53   ARG C CD  1 
ATOM   4275  N NE  . ARG C  1 53  ? 54.888  75.253 71.001  1.00 71.93  ? 53   ARG C NE  1 
ATOM   4276  C CZ  . ARG C  1 53  ? 54.192  76.384 70.854  1.00 72.43  ? 53   ARG C CZ  1 
ATOM   4277  N NH1 . ARG C  1 53  ? 53.105  76.634 71.583  1.00 71.10  ? 53   ARG C NH1 1 
ATOM   4278  N NH2 . ARG C  1 53  ? 54.593  77.286 69.963  1.00 74.49  ? 53   ARG C NH2 1 
ATOM   4279  N N   . ASP C  1 54  ? 52.331  70.636 72.875  1.00 60.71  ? 54   ASP C N   1 
ATOM   4280  C CA  . ASP C  1 54  ? 52.555  69.419 73.661  1.00 60.16  ? 54   ASP C CA  1 
ATOM   4281  C C   . ASP C  1 54  ? 51.489  69.191 74.741  1.00 58.53  ? 54   ASP C C   1 
ATOM   4282  O O   . ASP C  1 54  ? 51.513  68.165 75.420  1.00 57.94  ? 54   ASP C O   1 
ATOM   4283  C CB  . ASP C  1 54  ? 53.949  69.449 74.295  1.00 63.44  ? 54   ASP C CB  1 
ATOM   4284  C CG  . ASP C  1 54  ? 55.060  69.311 73.269  1.00 65.03  ? 54   ASP C CG  1 
ATOM   4285  O OD1 . ASP C  1 54  ? 55.062  68.313 72.516  1.00 63.47  ? 54   ASP C OD1 1 
ATOM   4286  O OD2 . ASP C  1 54  ? 55.939  70.196 73.219  1.00 68.04  ? 54   ASP C OD2 1 
ATOM   4287  N N   . CYS C  1 55  ? 50.567  70.141 74.904  1.00 58.04  ? 55   CYS C N   1 
ATOM   4288  C CA  . CYS C  1 55  ? 49.442  69.969 75.829  1.00 56.47  ? 55   CYS C CA  1 
ATOM   4289  C C   . CYS C  1 55  ? 48.331  69.132 75.186  1.00 53.27  ? 55   CYS C C   1 
ATOM   4290  O O   . CYS C  1 55  ? 48.147  69.156 73.969  1.00 52.27  ? 55   CYS C O   1 
ATOM   4291  C CB  . CYS C  1 55  ? 48.880  71.324 76.284  1.00 57.56  ? 55   CYS C CB  1 
ATOM   4292  S SG  . CYS C  1 55  ? 49.910  72.199 77.490  1.00 61.28  ? 55   CYS C SG  1 
ATOM   4293  N N   . SER C  1 56  ? 47.606  68.384 76.014  1.00 51.83  ? 56   SER C N   1 
ATOM   4294  C CA  . SER C  1 56  ? 46.435  67.634 75.569  1.00 49.10  ? 56   SER C CA  1 
ATOM   4295  C C   . SER C  1 56  ? 45.175  68.455 75.826  1.00 48.38  ? 56   SER C C   1 
ATOM   4296  O O   . SER C  1 56  ? 45.237  69.551 76.381  1.00 49.97  ? 56   SER C O   1 
ATOM   4297  C CB  . SER C  1 56  ? 46.339  66.299 76.310  1.00 48.26  ? 56   SER C CB  1 
ATOM   4298  O OG  . SER C  1 56  ? 45.771  66.471 77.600  1.00 48.47  ? 56   SER C OG  1 
ATOM   4299  N N   . VAL C  1 57  ? 44.030  67.911 75.426  1.00 46.20  ? 57   VAL C N   1 
ATOM   4300  C CA  . VAL C  1 57  ? 42.746  68.578 75.639  1.00 45.61  ? 57   VAL C CA  1 
ATOM   4301  C C   . VAL C  1 57  ? 42.434  68.617 77.133  1.00 46.19  ? 57   VAL C C   1 
ATOM   4302  O O   . VAL C  1 57  ? 41.920  69.614 77.642  1.00 47.07  ? 57   VAL C O   1 
ATOM   4303  C CB  . VAL C  1 57  ? 41.606  67.872 74.870  1.00 43.39  ? 57   VAL C CB  1 
ATOM   4304  C CG1 . VAL C  1 57  ? 40.257  68.498 75.194  1.00 43.13  ? 57   VAL C CG1 1 
ATOM   4305  C CG2 . VAL C  1 57  ? 41.863  67.927 73.369  1.00 42.84  ? 57   VAL C CG2 1 
ATOM   4306  N N   . ALA C  1 58  ? 42.753  67.525 77.825  1.00 45.81  ? 58   ALA C N   1 
ATOM   4307  C CA  . ALA C  1 58  ? 42.593  67.446 79.277  1.00 46.45  ? 58   ALA C CA  1 
ATOM   4308  C C   . ALA C  1 58  ? 43.481  68.473 79.987  1.00 48.79  ? 58   ALA C C   1 
ATOM   4309  O O   . ALA C  1 58  ? 43.006  69.224 80.845  1.00 49.61  ? 58   ALA C O   1 
ATOM   4310  C CB  . ALA C  1 58  ? 42.917  66.043 79.766  1.00 45.91  ? 58   ALA C CB  1 
ATOM   4311  N N   . GLY C  1 59  ? 44.762  68.503 79.619  1.00 50.03  ? 59   GLY C N   1 
ATOM   4312  C CA  . GLY C  1 59  ? 45.713  69.458 80.181  1.00 52.60  ? 59   GLY C CA  1 
ATOM   4313  C C   . GLY C  1 59  ? 45.245  70.894 80.030  1.00 53.58  ? 59   GLY C C   1 
ATOM   4314  O O   . GLY C  1 59  ? 45.329  71.686 80.973  1.00 55.33  ? 59   GLY C O   1 
ATOM   4315  N N   . TRP C  1 60  ? 44.745  71.227 78.844  1.00 52.61  ? 60   TRP C N   1 
ATOM   4316  C CA  . TRP C  1 60  ? 44.207  72.558 78.571  1.00 53.62  ? 60   TRP C CA  1 
ATOM   4317  C C   . TRP C  1 60  ? 42.970  72.847 79.426  1.00 53.21  ? 60   TRP C C   1 
ATOM   4318  O O   . TRP C  1 60  ? 42.915  73.864 80.120  1.00 55.13  ? 60   TRP C O   1 
ATOM   4319  C CB  . TRP C  1 60  ? 43.897  72.705 77.072  1.00 52.59  ? 60   TRP C CB  1 
ATOM   4320  C CG  . TRP C  1 60  ? 42.931  73.803 76.715  1.00 53.01  ? 60   TRP C CG  1 
ATOM   4321  C CD1 . TRP C  1 60  ? 42.883  75.059 77.237  1.00 55.31  ? 60   TRP C CD1 1 
ATOM   4322  C CD2 . TRP C  1 60  ? 41.892  73.739 75.730  1.00 51.37  ? 60   TRP C CD2 1 
ATOM   4323  N NE1 . TRP C  1 60  ? 41.869  75.780 76.654  1.00 55.28  ? 60   TRP C NE1 1 
ATOM   4324  C CE2 . TRP C  1 60  ? 41.246  74.993 75.723  1.00 52.87  ? 60   TRP C CE2 1 
ATOM   4325  C CE3 . TRP C  1 60  ? 41.443  72.742 74.855  1.00 48.98  ? 60   TRP C CE3 1 
ATOM   4326  C CZ2 . TRP C  1 60  ? 40.169  75.276 74.876  1.00 52.10  ? 60   TRP C CZ2 1 
ATOM   4327  C CZ3 . TRP C  1 60  ? 40.372  73.025 74.013  1.00 48.12  ? 60   TRP C CZ3 1 
ATOM   4328  C CH2 . TRP C  1 60  ? 39.749  74.281 74.029  1.00 49.68  ? 60   TRP C CH2 1 
ATOM   4329  N N   . LEU C  1 61  ? 41.994  71.944 79.390  1.00 50.97  ? 61   LEU C N   1 
ATOM   4330  C CA  . LEU C  1 61  ? 40.705  72.180 80.051  1.00 50.57  ? 61   LEU C CA  1 
ATOM   4331  C C   . LEU C  1 61  ? 40.788  72.175 81.580  1.00 51.57  ? 61   LEU C C   1 
ATOM   4332  O O   . LEU C  1 61  ? 40.145  72.994 82.238  1.00 52.60  ? 61   LEU C O   1 
ATOM   4333  C CB  . LEU C  1 61  ? 39.656  71.170 79.574  1.00 48.13  ? 61   LEU C CB  1 
ATOM   4334  C CG  . LEU C  1 61  ? 39.165  71.329 78.130  1.00 47.19  ? 61   LEU C CG  1 
ATOM   4335  C CD1 . LEU C  1 61  ? 38.040  70.341 77.861  1.00 45.13  ? 61   LEU C CD1 1 
ATOM   4336  C CD2 . LEU C  1 61  ? 38.705  72.750 77.838  1.00 48.72  ? 61   LEU C CD2 1 
ATOM   4337  N N   . LEU C  1 62  ? 41.573  71.259 82.143  1.00 51.40  ? 62   LEU C N   1 
ATOM   4338  C CA  . LEU C  1 62  ? 41.792  71.234 83.594  1.00 52.50  ? 62   LEU C CA  1 
ATOM   4339  C C   . LEU C  1 62  ? 42.693  72.376 84.065  1.00 55.26  ? 62   LEU C C   1 
ATOM   4340  O O   . LEU C  1 62  ? 42.674  72.731 85.238  1.00 56.50  ? 62   LEU C O   1 
ATOM   4341  C CB  . LEU C  1 62  ? 42.379  69.893 84.033  1.00 51.73  ? 62   LEU C CB  1 
ATOM   4342  C CG  . LEU C  1 62  ? 41.407  68.722 83.918  1.00 49.45  ? 62   LEU C CG  1 
ATOM   4343  C CD1 . LEU C  1 62  ? 42.148  67.403 84.052  1.00 48.99  ? 62   LEU C CD1 1 
ATOM   4344  C CD2 . LEU C  1 62  ? 40.300  68.830 84.957  1.00 49.28  ? 62   LEU C CD2 1 
ATOM   4345  N N   . GLY C  1 63  ? 43.466  72.958 83.150  1.00 56.38  ? 63   GLY C N   1 
ATOM   4346  C CA  . GLY C  1 63  ? 44.341  74.076 83.482  1.00 59.33  ? 63   GLY C CA  1 
ATOM   4347  C C   . GLY C  1 63  ? 45.657  73.611 84.072  1.00 60.71  ? 63   GLY C C   1 
ATOM   4348  O O   . GLY C  1 63  ? 46.104  74.126 85.092  1.00 62.80  ? 63   GLY C O   1 
ATOM   4349  N N   . ASN C  1 64  ? 46.273  72.626 83.427  1.00 59.73  ? 64   ASN C N   1 
ATOM   4350  C CA  . ASN C  1 64  ? 47.608  72.169 83.794  1.00 61.34  ? 64   ASN C CA  1 
ATOM   4351  C C   . ASN C  1 64  ? 48.594  73.345 83.676  1.00 64.55  ? 64   ASN C C   1 
ATOM   4352  O O   . ASN C  1 64  ? 48.559  74.076 82.684  1.00 64.94  ? 64   ASN C O   1 
ATOM   4353  C CB  . ASN C  1 64  ? 47.992  70.971 82.902  1.00 59.77  ? 64   ASN C CB  1 
ATOM   4354  C CG  . ASN C  1 64  ? 49.469  70.601 82.969  1.00 61.80  ? 64   ASN C CG  1 
ATOM   4355  O OD1 . ASN C  1 64  ? 50.341  71.459 83.079  1.00 64.51  ? 64   ASN C OD1 1 
ATOM   4356  N ND2 . ASN C  1 64  ? 49.756  69.308 82.857  1.00 60.74  ? 64   ASN C ND2 1 
ATOM   4357  N N   . PRO C  1 65  ? 49.464  73.539 84.692  1.00 67.05  ? 65   PRO C N   1 
ATOM   4358  C CA  . PRO C  1 65  ? 50.382  74.696 84.740  1.00 70.56  ? 65   PRO C CA  1 
ATOM   4359  C C   . PRO C  1 65  ? 51.317  74.873 83.530  1.00 71.80  ? 65   PRO C C   1 
ATOM   4360  O O   . PRO C  1 65  ? 51.775  75.987 83.271  1.00 74.41  ? 65   PRO C O   1 
ATOM   4361  C CB  . PRO C  1 65  ? 51.207  74.451 86.013  1.00 72.61  ? 65   PRO C CB  1 
ATOM   4362  C CG  . PRO C  1 65  ? 50.963  73.034 86.400  1.00 70.27  ? 65   PRO C CG  1 
ATOM   4363  C CD  . PRO C  1 65  ? 49.603  72.687 85.886  1.00 66.91  ? 65   PRO C CD  1 
ATOM   4364  N N   . MET C  1 66  ? 51.598  73.791 82.808  1.00 70.17  ? 66   MET C N   1 
ATOM   4365  C CA  . MET C  1 66  ? 52.398  73.856 81.579  1.00 71.04  ? 66   MET C CA  1 
ATOM   4366  C C   . MET C  1 66  ? 51.593  74.428 80.411  1.00 69.58  ? 66   MET C C   1 
ATOM   4367  O O   . MET C  1 66  ? 52.160  74.868 79.408  1.00 70.73  ? 66   MET C O   1 
ATOM   4368  C CB  . MET C  1 66  ? 52.889  72.459 81.187  1.00 69.73  ? 66   MET C CB  1 
ATOM   4369  C CG  . MET C  1 66  ? 53.668  71.716 82.261  1.00 71.12  ? 66   MET C CG  1 
ATOM   4370  S SD  . MET C  1 66  ? 55.179  72.572 82.734  1.00 76.02  ? 66   MET C SD  1 
ATOM   4371  C CE  . MET C  1 66  ? 56.170  71.197 83.317  1.00 76.95  ? 66   MET C CE  1 
ATOM   4372  N N   . CYS C  1 67  ? 50.270  74.409 80.546  1.00 67.21  ? 67   CYS C N   1 
ATOM   4373  C CA  . CYS C  1 67  ? 49.363  74.873 79.503  1.00 65.73  ? 67   CYS C CA  1 
ATOM   4374  C C   . CYS C  1 67  ? 48.845  76.283 79.801  1.00 67.51  ? 67   CYS C C   1 
ATOM   4375  O O   . CYS C  1 67  ? 47.694  76.612 79.498  1.00 66.12  ? 67   CYS C O   1 
ATOM   4376  C CB  . CYS C  1 67  ? 48.215  73.876 79.378  1.00 62.17  ? 67   CYS C CB  1 
ATOM   4377  S SG  . CYS C  1 67  ? 48.810  72.174 79.218  1.00 60.51  ? 67   CYS C SG  1 
ATOM   4378  N N   . ASP C  1 68  ? 49.713  77.108 80.387  1.00 70.87  ? 68   ASP C N   1 
ATOM   4379  C CA  . ASP C  1 68  ? 49.418  78.517 80.650  1.00 73.29  ? 68   ASP C CA  1 
ATOM   4380  C C   . ASP C  1 68  ? 49.206  79.308 79.363  1.00 73.79  ? 68   ASP C C   1 
ATOM   4381  O O   . ASP C  1 68  ? 48.576  80.361 79.377  1.00 75.07  ? 68   ASP C O   1 
ATOM   4382  C CB  . ASP C  1 68  ? 50.552  79.168 81.459  1.00 77.13  ? 68   ASP C CB  1 
ATOM   4383  C CG  . ASP C  1 68  ? 50.485  78.842 82.943  1.00 77.29  ? 68   ASP C CG  1 
ATOM   4384  O OD1 . ASP C  1 68  ? 49.602  78.062 83.359  1.00 74.43  ? 68   ASP C OD1 1 
ATOM   4385  O OD2 . ASP C  1 68  ? 51.321  79.372 83.704  1.00 80.46  ? 68   ASP C OD2 1 
ATOM   4386  N N   . GLU C  1 69  ? 49.746  78.814 78.253  1.00 72.99  ? 69   GLU C N   1 
ATOM   4387  C CA  . GLU C  1 69  ? 49.491  79.419 76.952  1.00 73.07  ? 69   GLU C CA  1 
ATOM   4388  C C   . GLU C  1 69  ? 47.993  79.437 76.632  1.00 70.55  ? 69   GLU C C   1 
ATOM   4389  O O   . GLU C  1 69  ? 47.508  80.363 75.980  1.00 71.50  ? 69   GLU C O   1 
ATOM   4390  C CB  . GLU C  1 69  ? 50.250  78.660 75.862  1.00 72.12  ? 69   GLU C CB  1 
ATOM   4391  C CG  . GLU C  1 69  ? 50.129  79.270 74.472  1.00 72.40  ? 69   GLU C CG  1 
ATOM   4392  C CD  . GLU C  1 69  ? 50.933  78.526 73.420  1.00 71.65  ? 69   GLU C CD  1 
ATOM   4393  O OE1 . GLU C  1 69  ? 51.765  77.665 73.784  1.00 71.63  ? 69   GLU C OE1 1 
ATOM   4394  O OE2 . GLU C  1 69  ? 50.730  78.807 72.219  1.00 71.21  ? 69   GLU C OE2 1 
ATOM   4395  N N   . PHE C  1 70  ? 47.271  78.425 77.114  1.00 67.66  ? 70   PHE C N   1 
ATOM   4396  C CA  . PHE C  1 70  ? 45.885  78.187 76.714  1.00 65.06  ? 70   PHE C CA  1 
ATOM   4397  C C   . PHE C  1 70  ? 44.833  78.569 77.772  1.00 65.15  ? 70   PHE C C   1 
ATOM   4398  O O   . PHE C  1 70  ? 43.741  77.999 77.801  1.00 62.74  ? 70   PHE C O   1 
ATOM   4399  C CB  . PHE C  1 70  ? 45.737  76.721 76.285  1.00 61.74  ? 70   PHE C CB  1 
ATOM   4400  C CG  . PHE C  1 70  ? 46.834  76.256 75.363  1.00 61.80  ? 70   PHE C CG  1 
ATOM   4401  C CD1 . PHE C  1 70  ? 46.950  76.784 74.085  1.00 62.21  ? 70   PHE C CD1 1 
ATOM   4402  C CD2 . PHE C  1 70  ? 47.771  75.320 75.783  1.00 61.70  ? 70   PHE C CD2 1 
ATOM   4403  C CE1 . PHE C  1 70  ? 47.963  76.372 73.236  1.00 62.42  ? 70   PHE C CE1 1 
ATOM   4404  C CE2 . PHE C  1 70  ? 48.788  74.904 74.939  1.00 62.05  ? 70   PHE C CE2 1 
ATOM   4405  C CZ  . PHE C  1 70  ? 48.885  75.432 73.663  1.00 62.37  ? 70   PHE C CZ  1 
ATOM   4406  N N   . ILE C  1 71  ? 45.162  79.535 78.629  1.00 68.14  ? 71   ILE C N   1 
ATOM   4407  C CA  . ILE C  1 71  ? 44.160  80.191 79.489  1.00 68.91  ? 71   ILE C CA  1 
ATOM   4408  C C   . ILE C  1 71  ? 43.501  81.320 78.687  1.00 70.37  ? 71   ILE C C   1 
ATOM   4409  O O   . ILE C  1 71  ? 44.194  82.130 78.063  1.00 72.75  ? 71   ILE C O   1 
ATOM   4410  C CB  . ILE C  1 71  ? 44.761  80.723 80.824  1.00 71.59  ? 71   ILE C CB  1 
ATOM   4411  C CG1 . ILE C  1 71  ? 43.820  81.732 81.505  1.00 73.21  ? 71   ILE C CG1 1 
ATOM   4412  C CG2 . ILE C  1 71  ? 46.121  81.385 80.616  1.00 74.74  ? 71   ILE C CG2 1 
ATOM   4413  C CD1 . ILE C  1 71  ? 44.123  81.966 82.972  1.00 74.95  ? 71   ILE C CD1 1 
ATOM   4414  N N   . ASN C  1 72  ? 42.166  81.362 78.700  1.00 69.18  ? 72   ASN C N   1 
ATOM   4415  C CA  . ASN C  1 72  ? 41.388  82.330 77.909  1.00 70.43  ? 72   ASN C CA  1 
ATOM   4416  C C   . ASN C  1 72  ? 41.758  82.352 76.417  1.00 70.06  ? 72   ASN C C   1 
ATOM   4417  O O   . ASN C  1 72  ? 42.085  83.402 75.863  1.00 72.80  ? 72   ASN C O   1 
ATOM   4418  C CB  . ASN C  1 72  ? 41.506  83.742 78.509  1.00 74.39  ? 72   ASN C CB  1 
ATOM   4419  C CG  . ASN C  1 72  ? 40.814  83.866 79.855  1.00 74.84  ? 72   ASN C CG  1 
ATOM   4420  O OD1 . ASN C  1 72  ? 40.202  82.915 80.345  1.00 72.22  ? 72   ASN C OD1 1 
ATOM   4421  N ND2 . ASN C  1 72  ? 40.904  85.048 80.460  1.00 78.37  ? 72   ASN C ND2 1 
ATOM   4422  N N   . VAL C  1 73  ? 41.696  81.190 75.774  1.00 66.89  ? 73   VAL C N   1 
ATOM   4423  C CA  . VAL C  1 73  ? 42.042  81.081 74.349  1.00 66.22  ? 73   VAL C CA  1 
ATOM   4424  C C   . VAL C  1 73  ? 41.061  81.828 73.439  1.00 66.74  ? 73   VAL C C   1 
ATOM   4425  O O   . VAL C  1 73  ? 39.868  81.906 73.741  1.00 66.24  ? 73   VAL C O   1 
ATOM   4426  C CB  . VAL C  1 73  ? 42.125  79.613 73.863  1.00 62.73  ? 73   VAL C CB  1 
ATOM   4427  C CG1 . VAL C  1 73  ? 43.358  78.934 74.434  1.00 62.73  ? 73   VAL C CG1 1 
ATOM   4428  C CG2 . VAL C  1 73  ? 40.858  78.831 74.203  1.00 60.16  ? 73   VAL C CG2 1 
ATOM   4429  N N   . PRO C  1 74  ? 41.562  82.372 72.313  1.00 67.93  ? 74   PRO C N   1 
ATOM   4430  C CA  . PRO C  1 74  ? 40.670  82.960 71.321  1.00 68.24  ? 74   PRO C CA  1 
ATOM   4431  C C   . PRO C  1 74  ? 39.963  81.863 70.532  1.00 64.65  ? 74   PRO C C   1 
ATOM   4432  O O   . PRO C  1 74  ? 40.374  80.697 70.587  1.00 62.15  ? 74   PRO C O   1 
ATOM   4433  C CB  . PRO C  1 74  ? 41.621  83.746 70.419  1.00 70.63  ? 74   PRO C CB  1 
ATOM   4434  C CG  . PRO C  1 74  ? 42.903  82.992 70.490  1.00 69.86  ? 74   PRO C CG  1 
ATOM   4435  C CD  . PRO C  1 74  ? 42.968  82.386 71.866  1.00 69.03  ? 74   PRO C CD  1 
ATOM   4436  N N   . GLU C  1 75  ? 38.916  82.231 69.800  1.00 64.59  ? 75   GLU C N   1 
ATOM   4437  C CA  . GLU C  1 75  ? 38.157  81.248 69.035  1.00 61.48  ? 75   GLU C CA  1 
ATOM   4438  C C   . GLU C  1 75  ? 39.027  80.610 67.955  1.00 59.93  ? 75   GLU C C   1 
ATOM   4439  O O   . GLU C  1 75  ? 39.947  81.240 67.428  1.00 61.71  ? 75   GLU C O   1 
ATOM   4440  C CB  . GLU C  1 75  ? 36.891  81.862 68.429  1.00 62.26  ? 75   GLU C CB  1 
ATOM   4441  C CG  . GLU C  1 75  ? 37.083  82.578 67.106  1.00 63.64  ? 75   GLU C CG  1 
ATOM   4442  C CD  . GLU C  1 75  ? 35.768  83.047 66.522  1.00 64.32  ? 75   GLU C CD  1 
ATOM   4443  O OE1 . GLU C  1 75  ? 35.104  83.906 67.145  1.00 66.72  ? 75   GLU C OE1 1 
ATOM   4444  O OE2 . GLU C  1 75  ? 35.400  82.554 65.436  1.00 62.63  ? 75   GLU C OE2 1 
ATOM   4445  N N   . TRP C  1 76  ? 38.715  79.357 67.637  1.00 56.77  ? 76   TRP C N   1 
ATOM   4446  C CA  . TRP C  1 76  ? 39.526  78.552 66.731  1.00 55.09  ? 76   TRP C CA  1 
ATOM   4447  C C   . TRP C  1 76  ? 38.673  78.014 65.587  1.00 53.03  ? 76   TRP C C   1 
ATOM   4448  O O   . TRP C  1 76  ? 37.480  77.764 65.758  1.00 52.08  ? 76   TRP C O   1 
ATOM   4449  C CB  . TRP C  1 76  ? 40.165  77.386 67.491  1.00 53.38  ? 76   TRP C CB  1 
ATOM   4450  C CG  . TRP C  1 76  ? 39.160  76.492 68.165  1.00 51.34  ? 76   TRP C CG  1 
ATOM   4451  C CD1 . TRP C  1 76  ? 38.538  75.399 67.624  1.00 48.78  ? 76   TRP C CD1 1 
ATOM   4452  C CD2 . TRP C  1 76  ? 38.646  76.626 69.495  1.00 51.90  ? 76   TRP C CD2 1 
ATOM   4453  N NE1 . TRP C  1 76  ? 37.672  74.844 68.539  1.00 47.81  ? 76   TRP C NE1 1 
ATOM   4454  C CE2 . TRP C  1 76  ? 37.720  75.578 69.695  1.00 49.62  ? 76   TRP C CE2 1 
ATOM   4455  C CE3 . TRP C  1 76  ? 38.878  77.529 70.539  1.00 54.24  ? 76   TRP C CE3 1 
ATOM   4456  C CZ2 . TRP C  1 76  ? 37.031  75.408 70.897  1.00 49.58  ? 76   TRP C CZ2 1 
ATOM   4457  C CZ3 . TRP C  1 76  ? 38.191  77.361 71.733  1.00 54.08  ? 76   TRP C CZ3 1 
ATOM   4458  C CH2 . TRP C  1 76  ? 37.279  76.308 71.902  1.00 51.75  ? 76   TRP C CH2 1 
ATOM   4459  N N   . SER C  1 77  ? 39.292  77.848 64.423  1.00 52.52  ? 77   SER C N   1 
ATOM   4460  C CA  . SER C  1 77  ? 38.649  77.194 63.287  1.00 50.40  ? 77   SER C CA  1 
ATOM   4461  C C   . SER C  1 77  ? 38.617  75.687 63.520  1.00 47.54  ? 77   SER C C   1 
ATOM   4462  O O   . SER C  1 77  ? 37.596  75.031 63.302  1.00 45.84  ? 77   SER C O   1 
ATOM   4463  C CB  . SER C  1 77  ? 39.412  77.505 62.003  1.00 50.95  ? 77   SER C CB  1 
ATOM   4464  O OG  . SER C  1 77  ? 40.811  77.417 62.214  1.00 51.69  ? 77   SER C OG  1 
ATOM   4465  N N   . TYR C  1 78  ? 39.751  75.153 63.963  1.00 47.27  ? 78   TYR C N   1 
ATOM   4466  C CA  . TYR C  1 78  ? 39.870  73.746 64.331  1.00 45.03  ? 78   TYR C CA  1 
ATOM   4467  C C   . TYR C  1 78  ? 40.965  73.590 65.389  1.00 45.93  ? 78   TYR C C   1 
ATOM   4468  O O   . TYR C  1 78  ? 41.716  74.529 65.646  1.00 48.15  ? 78   TYR C O   1 
ATOM   4469  C CB  . TYR C  1 78  ? 40.172  72.892 63.091  1.00 43.29  ? 78   TYR C CB  1 
ATOM   4470  C CG  . TYR C  1 78  ? 41.466  73.242 62.382  1.00 44.40  ? 78   TYR C CG  1 
ATOM   4471  C CD1 . TYR C  1 78  ? 41.539  74.327 61.506  1.00 45.89  ? 78   TYR C CD1 1 
ATOM   4472  C CD2 . TYR C  1 78  ? 42.617  72.487 62.585  1.00 44.21  ? 78   TYR C CD2 1 
ATOM   4473  C CE1 . TYR C  1 78  ? 42.724  74.648 60.856  1.00 47.12  ? 78   TYR C CE1 1 
ATOM   4474  C CE2 . TYR C  1 78  ? 43.804  72.801 61.940  1.00 45.50  ? 78   TYR C CE2 1 
ATOM   4475  C CZ  . TYR C  1 78  ? 43.853  73.882 61.078  1.00 46.93  ? 78   TYR C CZ  1 
ATOM   4476  O OH  . TYR C  1 78  ? 45.035  74.190 60.445  1.00 48.39  ? 78   TYR C OH  1 
ATOM   4477  N N   . ILE C  1 79  ? 41.048  72.409 65.995  1.00 44.42  ? 79   ILE C N   1 
ATOM   4478  C CA  . ILE C  1 79  ? 42.030  72.139 67.046  1.00 45.29  ? 79   ILE C CA  1 
ATOM   4479  C C   . ILE C  1 79  ? 43.080  71.148 66.554  1.00 44.63  ? 79   ILE C C   1 
ATOM   4480  O O   . ILE C  1 79  ? 42.765  70.233 65.797  1.00 42.80  ? 79   ILE C O   1 
ATOM   4481  C CB  . ILE C  1 79  ? 41.350  71.583 68.314  1.00 44.53  ? 79   ILE C CB  1 
ATOM   4482  C CG1 . ILE C  1 79  ? 40.397  72.629 68.899  1.00 45.61  ? 79   ILE C CG1 1 
ATOM   4483  C CG2 . ILE C  1 79  ? 42.390  71.189 69.357  1.00 45.35  ? 79   ILE C CG2 1 
ATOM   4484  C CD1 . ILE C  1 79  ? 39.393  72.071 69.885  1.00 44.61  ? 79   ILE C CD1 1 
ATOM   4485  N N   . VAL C  1 80  ? 44.325  71.336 66.988  1.00 46.40  ? 80   VAL C N   1 
ATOM   4486  C CA  . VAL C  1 80  ? 45.418  70.435 66.626  1.00 46.31  ? 80   VAL C CA  1 
ATOM   4487  C C   . VAL C  1 80  ? 46.073  69.863 67.882  1.00 47.09  ? 80   VAL C C   1 
ATOM   4488  O O   . VAL C  1 80  ? 46.563  70.606 68.736  1.00 49.11  ? 80   VAL C O   1 
ATOM   4489  C CB  . VAL C  1 80  ? 46.485  71.141 65.763  1.00 48.11  ? 80   VAL C CB  1 
ATOM   4490  C CG1 . VAL C  1 80  ? 47.564  70.155 65.326  1.00 48.03  ? 80   VAL C CG1 1 
ATOM   4491  C CG2 . VAL C  1 80  ? 45.838  71.786 64.547  1.00 47.63  ? 80   VAL C CG2 1 
ATOM   4492  N N   . GLU C  1 81  ? 46.084  68.536 67.970  1.00 45.71  ? 81   GLU C N   1 
ATOM   4493  C CA  . GLU C  1 81  ? 46.628  67.817 69.110  1.00 46.35  ? 81   GLU C CA  1 
ATOM   4494  C C   . GLU C  1 81  ? 47.572  66.734 68.605  1.00 46.43  ? 81   GLU C C   1 
ATOM   4495  O O   . GLU C  1 81  ? 47.303  66.099 67.593  1.00 44.98  ? 81   GLU C O   1 
ATOM   4496  C CB  . GLU C  1 81  ? 45.487  67.181 69.907  1.00 44.73  ? 81   GLU C CB  1 
ATOM   4497  C CG  . GLU C  1 81  ? 45.906  66.528 71.217  1.00 45.41  ? 81   GLU C CG  1 
ATOM   4498  C CD  . GLU C  1 81  ? 44.768  65.792 71.906  1.00 43.83  ? 81   GLU C CD  1 
ATOM   4499  O OE1 . GLU C  1 81  ? 43.985  65.104 71.209  1.00 42.06  ? 81   GLU C OE1 1 
ATOM   4500  O OE2 . GLU C  1 81  ? 44.663  65.891 73.150  1.00 44.52  ? 81   GLU C OE2 1 
ATOM   4501  N N   . LYS C  1 82  ? 48.678  66.523 69.309  1.00 48.39  ? 82   LYS C N   1 
ATOM   4502  C CA  . LYS C  1 82  ? 49.624  65.467 68.949  1.00 48.92  ? 82   LYS C CA  1 
ATOM   4503  C C   . LYS C  1 82  ? 49.075  64.077 69.283  1.00 47.40  ? 82   LYS C C   1 
ATOM   4504  O O   . LYS C  1 82  ? 48.065  63.940 69.981  1.00 46.18  ? 82   LYS C O   1 
ATOM   4505  C CB  . LYS C  1 82  ? 50.970  65.689 69.648  1.00 51.77  ? 82   LYS C CB  1 
ATOM   4506  C CG  . LYS C  1 82  ? 51.836  66.736 68.971  1.00 53.81  ? 82   LYS C CG  1 
ATOM   4507  C CD  . LYS C  1 82  ? 53.162  66.920 69.692  1.00 56.94  ? 82   LYS C CD  1 
ATOM   4508  C CE  . LYS C  1 82  ? 54.170  67.663 68.829  1.00 59.17  ? 82   LYS C CE  1 
ATOM   4509  N NZ  . LYS C  1 82  ? 53.854  69.112 68.708  1.00 59.98  ? 82   LYS C NZ  1 
ATOM   4510  N N   . ALA C  1 83  ? 49.748  63.050 68.771  1.00 47.75  ? 83   ALA C N   1 
ATOM   4511  C CA  . ALA C  1 83  ? 49.364  61.664 69.031  1.00 46.80  ? 83   ALA C CA  1 
ATOM   4512  C C   . ALA C  1 83  ? 49.609  61.273 70.491  1.00 48.10  ? 83   ALA C C   1 
ATOM   4513  O O   . ALA C  1 83  ? 48.790  60.575 71.091  1.00 47.08  ? 83   ALA C O   1 
ATOM   4514  C CB  . ALA C  1 83  ? 50.110  60.723 68.096  1.00 47.13  ? 83   ALA C CB  1 
ATOM   4515  N N   . ASN C  1 84  ? 50.726  61.732 71.059  1.00 50.63  ? 84   ASN C N   1 
ATOM   4516  C CA  . ASN C  1 84  ? 51.082  61.417 72.447  1.00 52.13  ? 84   ASN C CA  1 
ATOM   4517  C C   . ASN C  1 84  ? 51.606  62.642 73.214  1.00 54.08  ? 84   ASN C C   1 
ATOM   4518  O O   . ASN C  1 84  ? 52.777  62.681 73.598  1.00 56.60  ? 84   ASN C O   1 
ATOM   4519  C CB  . ASN C  1 84  ? 52.125  60.289 72.474  1.00 53.85  ? 84   ASN C CB  1 
ATOM   4520  C CG  . ASN C  1 84  ? 51.652  59.037 71.748  1.00 52.36  ? 84   ASN C CG  1 
ATOM   4521  O OD1 . ASN C  1 84  ? 50.648  58.428 72.130  1.00 50.81  ? 84   ASN C OD1 1 
ATOM   4522  N ND2 . ASN C  1 84  ? 52.365  58.652 70.689  1.00 53.00  ? 84   ASN C ND2 1 
ATOM   4523  N N   . PRO C  1 85  ? 50.733  63.642 73.455  1.00 53.16  ? 85   PRO C N   1 
ATOM   4524  C CA  . PRO C  1 85  ? 51.168  64.866 74.140  1.00 55.13  ? 85   PRO C CA  1 
ATOM   4525  C C   . PRO C  1 85  ? 51.675  64.592 75.551  1.00 56.84  ? 85   PRO C C   1 
ATOM   4526  O O   . PRO C  1 85  ? 51.004  63.898 76.318  1.00 55.74  ? 85   PRO C O   1 
ATOM   4527  C CB  . PRO C  1 85  ? 49.893  65.725 74.184  1.00 53.52  ? 85   PRO C CB  1 
ATOM   4528  C CG  . PRO C  1 85  ? 48.990  65.151 73.148  1.00 50.96  ? 85   PRO C CG  1 
ATOM   4529  C CD  . PRO C  1 85  ? 49.297  63.685 73.129  1.00 50.52  ? 85   PRO C CD  1 
ATOM   4530  N N   . VAL C  1 86  ? 52.849  65.130 75.881  1.00 59.69  ? 86   VAL C N   1 
ATOM   4531  C CA  . VAL C  1 86  ? 53.469  64.894 77.191  1.00 61.68  ? 86   VAL C CA  1 
ATOM   4532  C C   . VAL C  1 86  ? 52.733  65.591 78.343  1.00 61.40  ? 86   VAL C C   1 
ATOM   4533  O O   . VAL C  1 86  ? 52.637  65.038 79.440  1.00 61.69  ? 86   VAL C O   1 
ATOM   4534  C CB  . VAL C  1 86  ? 54.969  65.296 77.221  1.00 65.21  ? 86   VAL C CB  1 
ATOM   4535  C CG1 . VAL C  1 86  ? 55.757  64.495 76.193  1.00 65.74  ? 86   VAL C CG1 1 
ATOM   4536  C CG2 . VAL C  1 86  ? 55.160  66.795 77.007  1.00 66.64  ? 86   VAL C CG2 1 
ATOM   4537  N N   . ASN C  1 87  ? 52.230  66.801 78.094  1.00 61.05  ? 87   ASN C N   1 
ATOM   4538  C CA  . ASN C  1 87  ? 51.530  67.582 79.120  1.00 60.99  ? 87   ASN C CA  1 
ATOM   4539  C C   . ASN C  1 87  ? 50.047  67.231 79.168  1.00 57.92  ? 87   ASN C C   1 
ATOM   4540  O O   . ASN C  1 87  ? 49.192  68.016 78.746  1.00 56.91  ? 87   ASN C O   1 
ATOM   4541  C CB  . ASN C  1 87  ? 51.704  69.088 78.880  1.00 62.65  ? 87   ASN C CB  1 
ATOM   4542  C CG  . ASN C  1 87  ? 53.105  69.581 79.198  1.00 66.19  ? 87   ASN C CG  1 
ATOM   4543  O OD1 . ASN C  1 87  ? 53.810  69.003 80.026  1.00 67.62  ? 87   ASN C OD1 1 
ATOM   4544  N ND2 . ASN C  1 87  ? 53.508  70.667 78.549  1.00 67.85  ? 87   ASN C ND2 1 
ATOM   4545  N N   . ASP C  1 88  ? 49.756  66.042 79.685  1.00 56.69  ? 88   ASP C N   1 
ATOM   4546  C CA  . ASP C  1 88  ? 48.387  65.569 79.833  1.00 54.08  ? 88   ASP C CA  1 
ATOM   4547  C C   . ASP C  1 88  ? 47.985  65.741 81.308  1.00 54.53  ? 88   ASP C C   1 
ATOM   4548  O O   . ASP C  1 88  ? 47.994  66.866 81.821  1.00 55.76  ? 88   ASP C O   1 
ATOM   4549  C CB  . ASP C  1 88  ? 48.285  64.117 79.330  1.00 52.63  ? 88   ASP C CB  1 
ATOM   4550  C CG  . ASP C  1 88  ? 46.845  63.631 79.189  1.00 50.09  ? 88   ASP C CG  1 
ATOM   4551  O OD1 . ASP C  1 88  ? 45.905  64.447 79.298  1.00 49.30  ? 88   ASP C OD1 1 
ATOM   4552  O OD2 . ASP C  1 88  ? 46.653  62.418 78.967  1.00 49.12  ? 88   ASP C OD2 1 
ATOM   4553  N N   . LEU C  1 89  ? 47.648  64.648 81.990  1.00 53.68  ? 89   LEU C N   1 
ATOM   4554  C CA  . LEU C  1 89  ? 47.325  64.686 83.411  1.00 54.16  ? 89   LEU C CA  1 
ATOM   4555  C C   . LEU C  1 89  ? 48.623  64.625 84.206  1.00 56.69  ? 89   LEU C C   1 
ATOM   4556  O O   . LEU C  1 89  ? 49.206  63.550 84.370  1.00 57.20  ? 89   LEU C O   1 
ATOM   4557  C CB  . LEU C  1 89  ? 46.398  63.515 83.784  1.00 52.42  ? 89   LEU C CB  1 
ATOM   4558  C CG  . LEU C  1 89  ? 44.873  63.727 83.765  1.00 50.44  ? 89   LEU C CG  1 
ATOM   4559  C CD1 . LEU C  1 89  ? 44.423  64.867 82.861  1.00 49.88  ? 89   LEU C CD1 1 
ATOM   4560  C CD2 . LEU C  1 89  ? 44.167  62.432 83.386  1.00 48.73  ? 89   LEU C CD2 1 
ATOM   4561  N N   . CYS C  1 90  ? 49.078  65.786 84.678  1.00 58.51  ? 90   CYS C N   1 
ATOM   4562  C CA  . CYS C  1 90  ? 50.322  65.882 85.442  1.00 61.30  ? 90   CYS C CA  1 
ATOM   4563  C C   . CYS C  1 90  ? 50.241  65.030 86.704  1.00 61.49  ? 90   CYS C C   1 
ATOM   4564  O O   . CYS C  1 90  ? 51.108  64.192 86.949  1.00 62.84  ? 90   CYS C O   1 
ATOM   4565  C CB  . CYS C  1 90  ? 50.659  67.341 85.779  1.00 63.36  ? 90   CYS C CB  1 
ATOM   4566  S SG  . CYS C  1 90  ? 49.306  68.337 86.455  1.00 62.37  ? 90   CYS C SG  1 
ATOM   4567  N N   . TYR C  1 91  ? 49.191  65.240 87.492  1.00 60.28  ? 91   TYR C N   1 
ATOM   4568  C CA  . TYR C  1 91  ? 48.866  64.339 88.590  1.00 59.99  ? 91   TYR C CA  1 
ATOM   4569  C C   . TYR C  1 91  ? 48.105  63.147 88.003  1.00 57.65  ? 91   TYR C C   1 
ATOM   4570  O O   . TYR C  1 91  ? 47.096  63.347 87.320  1.00 55.62  ? 91   TYR C O   1 
ATOM   4571  C CB  . TYR C  1 91  ? 48.013  65.047 89.643  1.00 59.80  ? 91   TYR C CB  1 
ATOM   4572  C CG  . TYR C  1 91  ? 47.957  64.317 90.969  1.00 60.35  ? 91   TYR C CG  1 
ATOM   4573  C CD1 . TYR C  1 91  ? 47.055  63.277 91.178  1.00 58.59  ? 91   TYR C CD1 1 
ATOM   4574  C CD2 . TYR C  1 91  ? 48.814  64.661 92.012  1.00 62.83  ? 91   TYR C CD2 1 
ATOM   4575  C CE1 . TYR C  1 91  ? 47.005  62.603 92.388  1.00 59.25  ? 91   TYR C CE1 1 
ATOM   4576  C CE2 . TYR C  1 91  ? 48.771  63.994 93.227  1.00 63.42  ? 91   TYR C CE2 1 
ATOM   4577  C CZ  . TYR C  1 91  ? 47.864  62.966 93.411  1.00 61.60  ? 91   TYR C CZ  1 
ATOM   4578  O OH  . TYR C  1 91  ? 47.818  62.301 94.617  1.00 62.32  ? 91   TYR C OH  1 
ATOM   4579  N N   . PRO C  1 92  ? 48.570  61.907 88.267  1.00 58.15  ? 92   PRO C N   1 
ATOM   4580  C CA  . PRO C  1 92  ? 47.988  60.739 87.587  1.00 56.35  ? 92   PRO C CA  1 
ATOM   4581  C C   . PRO C  1 92  ? 46.504  60.548 87.874  1.00 54.23  ? 92   PRO C C   1 
ATOM   4582  O O   . PRO C  1 92  ? 46.017  60.956 88.933  1.00 54.43  ? 92   PRO C O   1 
ATOM   4583  C CB  . PRO C  1 92  ? 48.776  59.550 88.159  1.00 57.99  ? 92   PRO C CB  1 
ATOM   4584  C CG  . PRO C  1 92  ? 49.922  60.134 88.898  1.00 60.67  ? 92   PRO C CG  1 
ATOM   4585  C CD  . PRO C  1 92  ? 49.509  61.502 89.326  1.00 60.52  ? 92   PRO C CD  1 
ATOM   4586  N N   . GLY C  1 93  ? 45.801  59.923 86.937  1.00 52.38  ? 93   GLY C N   1 
ATOM   4587  C CA  . GLY C  1 93  ? 44.379  59.661 87.103  1.00 50.59  ? 93   GLY C CA  1 
ATOM   4588  C C   . GLY C  1 93  ? 43.658  59.314 85.816  1.00 48.72  ? 93   GLY C C   1 
ATOM   4589  O O   . GLY C  1 93  ? 44.272  58.879 84.839  1.00 48.70  ? 93   GLY C O   1 
ATOM   4590  N N   . ASP C  1 94  ? 42.342  59.504 85.836  1.00 47.28  ? 94   ASP C N   1 
ATOM   4591  C CA  . ASP C  1 94  ? 41.495  59.295 84.674  1.00 45.57  ? 94   ASP C CA  1 
ATOM   4592  C C   . ASP C  1 94  ? 40.660  60.536 84.434  1.00 44.76  ? 94   ASP C C   1 
ATOM   4593  O O   . ASP C  1 94  ? 40.453  61.351 85.340  1.00 45.39  ? 94   ASP C O   1 
ATOM   4594  C CB  . ASP C  1 94  ? 40.558  58.108 84.892  1.00 44.94  ? 94   ASP C CB  1 
ATOM   4595  C CG  . ASP C  1 94  ? 41.303  56.804 85.094  1.00 45.95  ? 94   ASP C CG  1 
ATOM   4596  O OD1 . ASP C  1 94  ? 41.967  56.340 84.140  1.00 46.01  ? 94   ASP C OD1 1 
ATOM   4597  O OD2 . ASP C  1 94  ? 41.211  56.235 86.204  1.00 46.84  ? 94   ASP C OD2 1 
ATOM   4598  N N   . PHE C  1 95  ? 40.190  60.667 83.199  1.00 43.50  ? 95   PHE C N   1 
ATOM   4599  C CA  . PHE C  1 95  ? 39.240  61.697 82.827  1.00 42.76  ? 95   PHE C CA  1 
ATOM   4600  C C   . PHE C  1 95  ? 37.982  60.961 82.378  1.00 41.46  ? 95   PHE C C   1 
ATOM   4601  O O   . PHE C  1 95  ? 38.011  60.192 81.411  1.00 40.68  ? 95   PHE C O   1 
ATOM   4602  C CB  . PHE C  1 95  ? 39.816  62.559 81.707  1.00 42.73  ? 95   PHE C CB  1 
ATOM   4603  C CG  . PHE C  1 95  ? 39.227  63.940 81.632  1.00 42.90  ? 95   PHE C CG  1 
ATOM   4604  C CD1 . PHE C  1 95  ? 37.878  64.127 81.358  1.00 42.01  ? 95   PHE C CD1 1 
ATOM   4605  C CD2 . PHE C  1 95  ? 40.027  65.056 81.824  1.00 44.25  ? 95   PHE C CD2 1 
ATOM   4606  C CE1 . PHE C  1 95  ? 37.341  65.401 81.283  1.00 42.49  ? 95   PHE C CE1 1 
ATOM   4607  C CE2 . PHE C  1 95  ? 39.494  66.331 81.747  1.00 44.73  ? 95   PHE C CE2 1 
ATOM   4608  C CZ  . PHE C  1 95  ? 38.149  66.504 81.479  1.00 43.85  ? 95   PHE C CZ  1 
ATOM   4609  N N   . ASN C  1 96  ? 36.889  61.181 83.099  1.00 41.41  ? 96   ASN C N   1 
ATOM   4610  C CA  . ASN C  1 96  ? 35.657  60.446 82.865  1.00 40.61  ? 96   ASN C CA  1 
ATOM   4611  C C   . ASN C  1 96  ? 34.928  60.948 81.622  1.00 39.69  ? 96   ASN C C   1 
ATOM   4612  O O   . ASN C  1 96  ? 34.743  62.157 81.456  1.00 39.91  ? 96   ASN C O   1 
ATOM   4613  C CB  . ASN C  1 96  ? 34.743  60.557 84.083  1.00 41.17  ? 96   ASN C CB  1 
ATOM   4614  C CG  . ASN C  1 96  ? 33.667  59.491 84.097  1.00 40.85  ? 96   ASN C CG  1 
ATOM   4615  O OD1 . ASN C  1 96  ? 33.963  58.299 84.239  1.00 40.97  ? 96   ASN C OD1 1 
ATOM   4616  N ND2 . ASN C  1 96  ? 32.411  59.909 83.950  1.00 40.70  ? 96   ASN C ND2 1 
ATOM   4617  N N   . ASP C  1 97  ? 34.508  60.010 80.770  1.00 38.85  ? 97   ASP C N   1 
ATOM   4618  C CA  . ASP C  1 97  ? 33.871  60.313 79.482  1.00 38.00  ? 97   ASP C CA  1 
ATOM   4619  C C   . ASP C  1 97  ? 34.661  61.361 78.700  1.00 37.82  ? 97   ASP C C   1 
ATOM   4620  O O   . ASP C  1 97  ? 34.103  62.341 78.195  1.00 37.78  ? 97   ASP C O   1 
ATOM   4621  C CB  . ASP C  1 97  ? 32.411  60.752 79.677  1.00 38.20  ? 97   ASP C CB  1 
ATOM   4622  C CG  . ASP C  1 97  ? 31.488  59.597 80.045  1.00 38.33  ? 97   ASP C CG  1 
ATOM   4623  O OD1 . ASP C  1 97  ? 31.855  58.426 79.823  1.00 38.18  ? 97   ASP C OD1 1 
ATOM   4624  O OD2 . ASP C  1 97  ? 30.380  59.866 80.554  1.00 38.89  ? 97   ASP C OD2 1 
ATOM   4625  N N   . TYR C  1 98  ? 35.968  61.134 78.612  1.00 37.92  ? 98   TYR C N   1 
ATOM   4626  C CA  . TYR C  1 98  ? 36.899  62.055 77.960  1.00 38.10  ? 98   TYR C CA  1 
ATOM   4627  C C   . TYR C  1 98  ? 36.645  62.134 76.455  1.00 37.10  ? 98   TYR C C   1 
ATOM   4628  O O   . TYR C  1 98  ? 36.702  63.213 75.860  1.00 37.26  ? 98   TYR C O   1 
ATOM   4629  C CB  . TYR C  1 98  ? 38.327  61.579 78.242  1.00 38.77  ? 98   TYR C CB  1 
ATOM   4630  C CG  . TYR C  1 98  ? 39.449  62.457 77.727  1.00 39.46  ? 98   TYR C CG  1 
ATOM   4631  C CD1 . TYR C  1 98  ? 39.424  63.842 77.890  1.00 40.21  ? 98   TYR C CD1 1 
ATOM   4632  C CD2 . TYR C  1 98  ? 40.569  61.889 77.115  1.00 39.67  ? 98   TYR C CD2 1 
ATOM   4633  C CE1 . TYR C  1 98  ? 40.466  64.636 77.429  1.00 41.15  ? 98   TYR C CE1 1 
ATOM   4634  C CE2 . TYR C  1 98  ? 41.613  62.672 76.654  1.00 40.56  ? 98   TYR C CE2 1 
ATOM   4635  C CZ  . TYR C  1 98  ? 41.560  64.042 76.813  1.00 41.31  ? 98   TYR C CZ  1 
ATOM   4636  O OH  . TYR C  1 98  ? 42.601  64.812 76.353  1.00 42.48  ? 98   TYR C OH  1 
ATOM   4637  N N   . GLU C  1 99  ? 36.347  60.985 75.855  1.00 36.21  ? 99   GLU C N   1 
ATOM   4638  C CA  . GLU C  1 99  ? 36.128  60.886 74.416  1.00 35.27  ? 99   GLU C CA  1 
ATOM   4639  C C   . GLU C  1 99  ? 34.799  61.528 74.017  1.00 34.90  ? 99   GLU C C   1 
ATOM   4640  O O   . GLU C  1 99  ? 34.698  62.164 72.967  1.00 34.57  ? 99   GLU C O   1 
ATOM   4641  C CB  . GLU C  1 99  ? 36.162  59.423 73.964  1.00 34.74  ? 99   GLU C CB  1 
ATOM   4642  C CG  . GLU C  1 99  ? 37.541  58.771 74.017  1.00 35.22  ? 99   GLU C CG  1 
ATOM   4643  C CD  . GLU C  1 99  ? 38.002  58.429 75.426  1.00 36.25  ? 99   GLU C CD  1 
ATOM   4644  O OE1 . GLU C  1 99  ? 37.160  58.046 76.269  1.00 36.36  ? 99   GLU C OE1 1 
ATOM   4645  O OE2 . GLU C  1 99  ? 39.215  58.542 75.688  1.00 37.07  ? 99   GLU C OE2 1 
ATOM   4646  N N   . GLU C  1 100 ? 33.785  61.358 74.860  1.00 35.11  ? 100  GLU C N   1 
ATOM   4647  C CA  . GLU C  1 100 ? 32.499  62.022 74.657  1.00 35.20  ? 100  GLU C CA  1 
ATOM   4648  C C   . GLU C  1 100 ? 32.623  63.543 74.784  1.00 35.95  ? 100  GLU C C   1 
ATOM   4649  O O   . GLU C  1 100 ? 31.925  64.283 74.093  1.00 36.10  ? 100  GLU C O   1 
ATOM   4650  C CB  . GLU C  1 100 ? 31.458  61.490 75.647  1.00 35.62  ? 100  GLU C CB  1 
ATOM   4651  C CG  . GLU C  1 100 ? 30.922  60.116 75.292  1.00 35.15  ? 100  GLU C CG  1 
ATOM   4652  C CD  . GLU C  1 100 ? 30.027  60.137 74.066  1.00 34.76  ? 100  GLU C CD  1 
ATOM   4653  O OE1 . GLU C  1 100 ? 29.139  61.010 73.987  1.00 35.27  ? 100  GLU C OE1 1 
ATOM   4654  O OE2 . GLU C  1 100 ? 30.205  59.278 73.178  1.00 34.11  ? 100  GLU C OE2 1 
ATOM   4655  N N   . LEU C  1 101 ? 33.508  64.002 75.666  1.00 36.65  ? 101  LEU C N   1 
ATOM   4656  C CA  . LEU C  1 101 ? 33.762  65.435 75.815  1.00 37.67  ? 101  LEU C CA  1 
ATOM   4657  C C   . LEU C  1 101 ? 34.516  65.965 74.602  1.00 37.51  ? 101  LEU C C   1 
ATOM   4658  O O   . LEU C  1 101 ? 34.172  67.015 74.062  1.00 38.07  ? 101  LEU C O   1 
ATOM   4659  C CB  . LEU C  1 101 ? 34.558  65.727 77.094  1.00 38.66  ? 101  LEU C CB  1 
ATOM   4660  C CG  . LEU C  1 101 ? 34.833  67.202 77.411  1.00 40.09  ? 101  LEU C CG  1 
ATOM   4661  C CD1 . LEU C  1 101 ? 33.563  68.036 77.344  1.00 40.68  ? 101  LEU C CD1 1 
ATOM   4662  C CD2 . LEU C  1 101 ? 35.478  67.324 78.782  1.00 41.11  ? 101  LEU C CD2 1 
ATOM   4663  N N   . LYS C  1 102 ? 35.548  65.232 74.190  1.00 36.93  ? 102  LYS C N   1 
ATOM   4664  C CA  . LYS C  1 102 ? 36.290  65.551 72.973  1.00 36.75  ? 102  LYS C CA  1 
ATOM   4665  C C   . LYS C  1 102 ? 35.376  65.605 71.750  1.00 35.95  ? 102  LYS C C   1 
ATOM   4666  O O   . LYS C  1 102 ? 35.569  66.428 70.856  1.00 36.21  ? 102  LYS C O   1 
ATOM   4667  C CB  . LYS C  1 102 ? 37.398  64.524 72.737  1.00 36.31  ? 102  LYS C CB  1 
ATOM   4668  C CG  . LYS C  1 102 ? 38.728  64.883 73.372  1.00 37.56  ? 102  LYS C CG  1 
ATOM   4669  C CD  . LYS C  1 102 ? 39.684  63.703 73.312  1.00 37.38  ? 102  LYS C CD  1 
ATOM   4670  C CE  . LYS C  1 102 ? 41.097  64.129 72.948  1.00 38.48  ? 102  LYS C CE  1 
ATOM   4671  N NZ  . LYS C  1 102 ? 41.907  62.956 72.521  1.00 38.28  ? 102  LYS C NZ  1 
ATOM   4672  N N   . HIS C  1 103 ? 34.385  64.721 71.709  1.00 35.14  ? 103  HIS C N   1 
ATOM   4673  C CA  . HIS C  1 103 ? 33.410  64.740 70.632  1.00 34.61  ? 103  HIS C CA  1 
ATOM   4674  C C   . HIS C  1 103 ? 32.578  66.019 70.681  1.00 35.68  ? 103  HIS C C   1 
ATOM   4675  O O   . HIS C  1 103 ? 32.237  66.580 69.647  1.00 35.75  ? 103  HIS C O   1 
ATOM   4676  C CB  . HIS C  1 103 ? 32.495  63.516 70.694  1.00 33.89  ? 103  HIS C CB  1 
ATOM   4677  C CG  . HIS C  1 103 ? 31.448  63.500 69.625  1.00 33.53  ? 103  HIS C CG  1 
ATOM   4678  N ND1 . HIS C  1 103 ? 31.710  63.099 68.333  1.00 32.67  ? 103  HIS C ND1 1 
ATOM   4679  C CD2 . HIS C  1 103 ? 30.144  63.862 69.650  1.00 34.10  ? 103  HIS C CD2 1 
ATOM   4680  C CE1 . HIS C  1 103 ? 30.608  63.200 67.612  1.00 32.68  ? 103  HIS C CE1 1 
ATOM   4681  N NE2 . HIS C  1 103 ? 29.644  63.661 68.388  1.00 33.61  ? 103  HIS C NE2 1 
ATOM   4682  N N   . LEU C  1 104 ? 32.257  66.468 71.889  1.00 36.71  ? 104  LEU C N   1 
ATOM   4683  C CA  . LEU C  1 104 ? 31.496  67.702 72.086  1.00 38.12  ? 104  LEU C CA  1 
ATOM   4684  C C   . LEU C  1 104 ? 32.243  68.910 71.509  1.00 39.06  ? 104  LEU C C   1 
ATOM   4685  O O   . LEU C  1 104 ? 31.625  69.830 70.974  1.00 39.98  ? 104  LEU C O   1 
ATOM   4686  C CB  . LEU C  1 104 ? 31.214  67.918 73.581  1.00 39.09  ? 104  LEU C CB  1 
ATOM   4687  C CG  . LEU C  1 104 ? 29.774  68.215 74.003  1.00 40.00  ? 104  LEU C CG  1 
ATOM   4688  C CD1 . LEU C  1 104 ? 28.840  67.081 73.608  1.00 39.10  ? 104  LEU C CD1 1 
ATOM   4689  C CD2 . LEU C  1 104 ? 29.725  68.432 75.507  1.00 40.94  ? 104  LEU C CD2 1 
ATOM   4690  N N   . LEU C  1 105 ? 33.571  68.887 71.618  1.00 42.85  ? 105  LEU C N   1 
ATOM   4691  C CA  . LEU C  1 105 ? 34.437  69.945 71.086  1.00 43.86  ? 105  LEU C CA  1 
ATOM   4692  C C   . LEU C  1 105 ? 34.404  70.085 69.572  1.00 44.66  ? 105  LEU C C   1 
ATOM   4693  O O   . LEU C  1 105 ? 34.752  71.143 69.046  1.00 45.81  ? 105  LEU C O   1 
ATOM   4694  C CB  . LEU C  1 105 ? 35.890  69.708 71.500  1.00 43.62  ? 105  LEU C CB  1 
ATOM   4695  C CG  . LEU C  1 105 ? 36.312  70.148 72.892  1.00 43.65  ? 105  LEU C CG  1 
ATOM   4696  C CD1 . LEU C  1 105 ? 37.732  69.669 73.150  1.00 43.52  ? 105  LEU C CD1 1 
ATOM   4697  C CD2 . LEU C  1 105 ? 36.220  71.663 73.023  1.00 44.94  ? 105  LEU C CD2 1 
ATOM   4698  N N   . SER C  1 106 ? 34.022  69.020 68.869  1.00 44.28  ? 106  SER C N   1 
ATOM   4699  C CA  . SER C  1 106 ? 33.868  69.088 67.416  1.00 45.24  ? 106  SER C CA  1 
ATOM   4700  C C   . SER C  1 106 ? 32.710  70.013 67.010  1.00 46.39  ? 106  SER C C   1 
ATOM   4701  O O   . SER C  1 106 ? 32.661  70.480 65.875  1.00 47.62  ? 106  SER C O   1 
ATOM   4702  C CB  . SER C  1 106 ? 33.682  67.686 66.812  1.00 44.72  ? 106  SER C CB  1 
ATOM   4703  O OG  . SER C  1 106 ? 32.426  67.122 67.144  1.00 44.36  ? 106  SER C OG  1 
ATOM   4704  N N   . ARG C  1 107 ? 31.786  70.267 67.937  1.00 46.24  ? 107  ARG C N   1 
ATOM   4705  C CA  . ARG C  1 107 ? 30.689  71.226 67.728  1.00 47.52  ? 107  ARG C CA  1 
ATOM   4706  C C   . ARG C  1 107 ? 30.966  72.612 68.327  1.00 48.34  ? 107  ARG C C   1 
ATOM   4707  O O   . ARG C  1 107 ? 30.072  73.459 68.342  1.00 49.45  ? 107  ARG C O   1 
ATOM   4708  C CB  . ARG C  1 107 ? 29.377  70.690 68.331  1.00 47.16  ? 107  ARG C CB  1 
ATOM   4709  C CG  . ARG C  1 107 ? 28.582  69.742 67.441  1.00 47.37  ? 107  ARG C CG  1 
ATOM   4710  C CD  . ARG C  1 107 ? 27.081  69.858 67.707  1.00 48.04  ? 107  ARG C CD  1 
ATOM   4711  N NE  . ARG C  1 107 ? 26.399  68.565 67.548  1.00 47.64  ? 107  ARG C NE  1 
ATOM   4712  C CZ  . ARG C  1 107 ? 25.597  68.212 66.538  1.00 48.71  ? 107  ARG C CZ  1 
ATOM   4713  N NH1 . ARG C  1 107 ? 25.312  69.047 65.537  1.00 50.32  ? 107  ARG C NH1 1 
ATOM   4714  N NH2 . ARG C  1 107 ? 25.058  66.994 66.537  1.00 48.36  ? 107  ARG C NH2 1 
ATOM   4715  N N   . ILE C  1 108 ? 32.185  72.848 68.813  1.00 48.01  ? 108  ILE C N   1 
ATOM   4716  C CA  . ILE C  1 108 ? 32.498  74.074 69.555  1.00 48.86  ? 108  ILE C CA  1 
ATOM   4717  C C   . ILE C  1 108 ? 33.662  74.853 68.931  1.00 49.97  ? 108  ILE C C   1 
ATOM   4718  O O   . ILE C  1 108 ? 34.726  74.293 68.657  1.00 49.41  ? 108  ILE C O   1 
ATOM   4719  C CB  . ILE C  1 108 ? 32.800  73.768 71.043  1.00 47.80  ? 108  ILE C CB  1 
ATOM   4720  C CG1 . ILE C  1 108 ? 31.558  73.174 71.718  1.00 47.06  ? 108  ILE C CG1 1 
ATOM   4721  C CG2 . ILE C  1 108 ? 33.231  75.032 71.781  1.00 48.93  ? 108  ILE C CG2 1 
ATOM   4722  C CD1 . ILE C  1 108 ? 31.802  72.610 73.101  1.00 46.00  ? 108  ILE C CD1 1 
ATOM   4723  N N   . ASN C  1 109 ? 33.442  76.154 68.733  1.00 51.71  ? 109  ASN C N   1 
ATOM   4724  C CA  . ASN C  1 109 ? 34.447  77.059 68.167  1.00 53.18  ? 109  ASN C CA  1 
ATOM   4725  C C   . ASN C  1 109 ? 35.070  78.024 69.178  1.00 54.00  ? 109  ASN C C   1 
ATOM   4726  O O   . ASN C  1 109 ? 36.189  78.498 68.960  1.00 54.87  ? 109  ASN C O   1 
ATOM   4727  C CB  . ASN C  1 109 ? 33.850  77.865 67.010  1.00 55.07  ? 109  ASN C CB  1 
ATOM   4728  C CG  . ASN C  1 109 ? 34.070  77.204 65.668  1.00 55.08  ? 109  ASN C CG  1 
ATOM   4729  O OD1 . ASN C  1 109 ? 34.843  77.690 64.845  1.00 56.38  ? 109  ASN C OD1 1 
ATOM   4730  N ND2 . ASN C  1 109 ? 33.405  76.086 65.444  1.00 53.82  ? 109  ASN C ND2 1 
ATOM   4731  N N   . HIS C  1 110 ? 34.358  78.331 70.264  1.00 53.94  ? 110  HIS C N   1 
ATOM   4732  C CA  . HIS C  1 110 ? 34.911  79.221 71.285  1.00 54.89  ? 110  HIS C CA  1 
ATOM   4733  C C   . HIS C  1 110 ? 34.400  78.973 72.701  1.00 54.05  ? 110  HIS C C   1 
ATOM   4734  O O   . HIS C  1 110 ? 33.198  78.830 72.938  1.00 53.75  ? 110  HIS C O   1 
ATOM   4735  C CB  . HIS C  1 110 ? 34.665  80.685 70.910  1.00 57.36  ? 110  HIS C CB  1 
ATOM   4736  C CG  . HIS C  1 110 ? 35.540  81.651 71.649  1.00 58.80  ? 110  HIS C CG  1 
ATOM   4737  N ND1 . HIS C  1 110 ? 35.120  82.914 72.010  1.00 60.90  ? 110  HIS C ND1 1 
ATOM   4738  C CD2 . HIS C  1 110 ? 36.809  81.532 72.110  1.00 58.64  ? 110  HIS C CD2 1 
ATOM   4739  C CE1 . HIS C  1 110 ? 36.096  83.533 72.649  1.00 61.99  ? 110  HIS C CE1 1 
ATOM   4740  N NE2 . HIS C  1 110 ? 37.131  82.717 72.723  1.00 60.65  ? 110  HIS C NE2 1 
ATOM   4741  N N   . PHE C  1 111 ? 35.348  78.936 73.634  1.00 53.88  ? 111  PHE C N   1 
ATOM   4742  C CA  . PHE C  1 111 ? 35.060  78.921 75.060  1.00 53.65  ? 111  PHE C CA  1 
ATOM   4743  C C   . PHE C  1 111 ? 35.392  80.291 75.640  1.00 55.85  ? 111  PHE C C   1 
ATOM   4744  O O   . PHE C  1 111 ? 36.357  80.927 75.210  1.00 57.10  ? 111  PHE C O   1 
ATOM   4745  C CB  . PHE C  1 111 ? 35.916  77.875 75.786  1.00 52.18  ? 111  PHE C CB  1 
ATOM   4746  C CG  . PHE C  1 111 ? 35.358  76.476 75.755  1.00 50.14  ? 111  PHE C CG  1 
ATOM   4747  C CD1 . PHE C  1 111 ? 34.006  76.230 75.973  1.00 49.67  ? 111  PHE C CD1 1 
ATOM   4748  C CD2 . PHE C  1 111 ? 36.204  75.395 75.561  1.00 48.90  ? 111  PHE C CD2 1 
ATOM   4749  C CE1 . PHE C  1 111 ? 33.512  74.937 75.965  1.00 48.03  ? 111  PHE C CE1 1 
ATOM   4750  C CE2 . PHE C  1 111 ? 35.713  74.103 75.554  1.00 47.28  ? 111  PHE C CE2 1 
ATOM   4751  C CZ  . PHE C  1 111 ? 34.366  73.873 75.757  1.00 46.86  ? 111  PHE C CZ  1 
ATOM   4752  N N   . GLU C  1 112 ? 34.592  80.736 76.609  1.00 56.50  ? 112  GLU C N   1 
ATOM   4753  C CA  . GLU C  1 112 ? 34.953  81.875 77.460  1.00 58.57  ? 112  GLU C CA  1 
ATOM   4754  C C   . GLU C  1 112 ? 34.991  81.412 78.911  1.00 57.95  ? 112  GLU C C   1 
ATOM   4755  O O   . GLU C  1 112 ? 34.014  80.876 79.422  1.00 56.99  ? 112  GLU C O   1 
ATOM   4756  C CB  . GLU C  1 112 ? 33.963  83.031 77.306  1.00 60.54  ? 112  GLU C CB  1 
ATOM   4757  C CG  . GLU C  1 112 ? 34.499  84.347 77.854  1.00 63.16  ? 112  GLU C CG  1 
ATOM   4758  C CD  . GLU C  1 112 ? 33.434  85.422 77.967  1.00 65.23  ? 112  GLU C CD  1 
ATOM   4759  O OE1 . GLU C  1 112 ? 32.595  85.524 77.043  1.00 65.40  ? 112  GLU C OE1 1 
ATOM   4760  O OE2 . GLU C  1 112 ? 33.444  86.166 78.976  1.00 66.90  ? 112  GLU C OE2 1 
ATOM   4761  N N   . LYS C  1 113 ? 36.121  81.615 79.571  1.00 58.70  ? 113  LYS C N   1 
ATOM   4762  C CA  . LYS C  1 113 ? 36.293  81.149 80.941  1.00 58.36  ? 113  LYS C CA  1 
ATOM   4763  C C   . LYS C  1 113 ? 35.663  82.123 81.939  1.00 60.25  ? 113  LYS C C   1 
ATOM   4764  O O   . LYS C  1 113 ? 35.787  83.340 81.787  1.00 62.43  ? 113  LYS C O   1 
ATOM   4765  C CB  . LYS C  1 113 ? 37.780  80.984 81.235  1.00 58.70  ? 113  LYS C CB  1 
ATOM   4766  C CG  . LYS C  1 113 ? 38.089  80.204 82.499  1.00 58.09  ? 113  LYS C CG  1 
ATOM   4767  C CD  . LYS C  1 113 ? 39.217  79.211 82.272  1.00 56.95  ? 113  LYS C CD  1 
ATOM   4768  C CE  . LYS C  1 113 ? 40.543  79.877 81.931  1.00 58.54  ? 113  LYS C CE  1 
ATOM   4769  N NZ  . LYS C  1 113 ? 41.592  78.858 81.644  1.00 57.47  ? 113  LYS C NZ  1 
ATOM   4770  N N   . ILE C  1 114 ? 34.976  81.583 82.946  1.00 59.58  ? 114  ILE C N   1 
ATOM   4771  C CA  . ILE C  1 114 ? 34.423  82.397 84.033  1.00 61.44  ? 114  ILE C CA  1 
ATOM   4772  C C   . ILE C  1 114 ? 34.574  81.709 85.386  1.00 61.06  ? 114  ILE C C   1 
ATOM   4773  O O   . ILE C  1 114 ? 34.606  80.477 85.471  1.00 59.06  ? 114  ILE C O   1 
ATOM   4774  C CB  . ILE C  1 114 ? 32.929  82.735 83.826  1.00 61.70  ? 114  ILE C CB  1 
ATOM   4775  C CG1 . ILE C  1 114 ? 32.102  81.462 83.594  1.00 59.30  ? 114  ILE C CG1 1 
ATOM   4776  C CG2 . ILE C  1 114 ? 32.755  83.720 82.677  1.00 62.99  ? 114  ILE C CG2 1 
ATOM   4777  C CD1 . ILE C  1 114 ? 30.652  81.611 83.998  1.00 59.74  ? 114  ILE C CD1 1 
ATOM   4778  N N   . GLN C  1 115 ? 34.659  82.521 86.438  1.00 63.20  ? 115  GLN C N   1 
ATOM   4779  C CA  . GLN C  1 115 ? 34.766  82.028 87.805  1.00 63.38  ? 115  GLN C CA  1 
ATOM   4780  C C   . GLN C  1 115 ? 33.371  81.783 88.377  1.00 63.09  ? 115  GLN C C   1 
ATOM   4781  O O   . GLN C  1 115 ? 32.536  82.689 88.388  1.00 64.55  ? 115  GLN C O   1 
ATOM   4782  C CB  . GLN C  1 115 ? 35.524  83.040 88.669  1.00 66.16  ? 115  GLN C CB  1 
ATOM   4783  C CG  . GLN C  1 115 ? 35.577  82.706 90.151  1.00 66.93  ? 115  GLN C CG  1 
ATOM   4784  C CD  . GLN C  1 115 ? 36.434  83.685 90.932  1.00 69.87  ? 115  GLN C CD  1 
ATOM   4785  O OE1 . GLN C  1 115 ? 37.660  83.577 90.948  1.00 70.28  ? 115  GLN C OE1 1 
ATOM   4786  N NE2 . GLN C  1 115 ? 35.792  84.638 91.596  1.00 72.13  ? 115  GLN C NE2 1 
ATOM   4787  N N   . ILE C  1 116 ? 33.129  80.560 88.845  1.00 61.39  ? 116  ILE C N   1 
ATOM   4788  C CA  . ILE C  1 116 ? 31.857  80.207 89.497  1.00 61.21  ? 116  ILE C CA  1 
ATOM   4789  C C   . ILE C  1 116 ? 32.020  80.085 91.021  1.00 62.49  ? 116  ILE C C   1 
ATOM   4790  O O   . ILE C  1 116 ? 31.176  80.570 91.778  1.00 63.93  ? 116  ILE C O   1 
ATOM   4791  C CB  . ILE C  1 116 ? 31.213  78.922 88.909  1.00 58.65  ? 116  ILE C CB  1 
ATOM   4792  C CG1 . ILE C  1 116 ? 32.261  77.844 88.614  1.00 56.93  ? 116  ILE C CG1 1 
ATOM   4793  C CG2 . ILE C  1 116 ? 30.440  79.248 87.635  1.00 58.12  ? 116  ILE C CG2 1 
ATOM   4794  C CD1 . ILE C  1 116 ? 31.712  76.437 88.684  1.00 55.02  ? 116  ILE C CD1 1 
ATOM   4795  N N   . ILE C  1 117 ? 33.102  79.444 91.460  1.00 62.16  ? 117  ILE C N   1 
ATOM   4796  C CA  . ILE C  1 117 ? 33.475  79.398 92.876  1.00 63.75  ? 117  ILE C CA  1 
ATOM   4797  C C   . ILE C  1 117 ? 34.790  80.166 93.042  1.00 65.59  ? 117  ILE C C   1 
ATOM   4798  O O   . ILE C  1 117 ? 35.808  79.768 92.469  1.00 64.71  ? 117  ILE C O   1 
ATOM   4799  C CB  . ILE C  1 117 ? 33.631  77.937 93.377  1.00 62.21  ? 117  ILE C CB  1 
ATOM   4800  C CG1 . ILE C  1 117 ? 32.293  77.386 93.890  1.00 61.72  ? 117  ILE C CG1 1 
ATOM   4801  C CG2 . ILE C  1 117 ? 34.692  77.813 94.474  1.00 63.74  ? 117  ILE C CG2 1 
ATOM   4802  C CD1 . ILE C  1 117 ? 31.358  76.910 92.800  1.00 59.64  ? 117  ILE C CD1 1 
ATOM   4803  N N   . PRO C  1 118 ? 34.775  81.278 93.804  1.00 68.34  ? 118  PRO C N   1 
ATOM   4804  C CA  . PRO C  1 118 ? 36.054  81.939 94.092  1.00 70.38  ? 118  PRO C CA  1 
ATOM   4805  C C   . PRO C  1 118 ? 36.916  81.141 95.077  1.00 70.75  ? 118  PRO C C   1 
ATOM   4806  O O   . PRO C  1 118 ? 36.390  80.520 96.003  1.00 70.73  ? 118  PRO C O   1 
ATOM   4807  C CB  . PRO C  1 118 ? 35.640  83.298 94.688  1.00 73.40  ? 118  PRO C CB  1 
ATOM   4808  C CG  . PRO C  1 118 ? 34.193  83.470 94.355  1.00 72.71  ? 118  PRO C CG  1 
ATOM   4809  C CD  . PRO C  1 118 ? 33.620  82.091 94.229  1.00 69.87  ? 118  PRO C CD  1 
ATOM   4810  N N   . LYS C  1 119 ? 38.229  81.161 94.865  1.00 71.26  ? 119  LYS C N   1 
ATOM   4811  C CA  . LYS C  1 119 ? 39.167  80.413 95.703  1.00 71.81  ? 119  LYS C CA  1 
ATOM   4812  C C   . LYS C  1 119 ? 39.217  80.987 97.121  1.00 74.91  ? 119  LYS C C   1 
ATOM   4813  O O   . LYS C  1 119 ? 39.327  80.244 98.099  1.00 75.32  ? 119  LYS C O   1 
ATOM   4814  C CB  . LYS C  1 119 ? 40.562  80.439 95.075  1.00 71.98  ? 119  LYS C CB  1 
ATOM   4815  C CG  . LYS C  1 119 ? 41.496  79.347 95.564  1.00 71.69  ? 119  LYS C CG  1 
ATOM   4816  C CD  . LYS C  1 119 ? 42.786  79.357 94.760  1.00 71.69  ? 119  LYS C CD  1 
ATOM   4817  C CE  . LYS C  1 119 ? 43.891  78.571 95.444  1.00 72.53  ? 119  LYS C CE  1 
ATOM   4818  N NZ  . LYS C  1 119 ? 45.218  78.855 94.831  1.00 73.43  ? 119  LYS C NZ  1 
ATOM   4819  N N   . SER C  1 120 ? 39.134  82.313 97.216  1.00 77.31  ? 120  SER C N   1 
ATOM   4820  C CA  . SER C  1 120 ? 39.067  83.012 98.500  1.00 80.56  ? 120  SER C CA  1 
ATOM   4821  C C   . SER C  1 120 ? 37.831  82.615 99.308  1.00 80.34  ? 120  SER C C   1 
ATOM   4822  O O   . SER C  1 120 ? 37.861  82.623 100.535 1.00 82.47  ? 120  SER C O   1 
ATOM   4823  C CB  . SER C  1 120 ? 39.049  84.524 98.269  1.00 83.02  ? 120  SER C CB  1 
ATOM   4824  O OG  . SER C  1 120 ? 37.934  84.900 97.477  1.00 81.75  ? 120  SER C OG  1 
ATOM   4825  N N   . SER C  1 121 ? 36.750  82.269 98.611  1.00 77.98  ? 121  SER C N   1 
ATOM   4826  C CA  . SER C  1 121 ? 35.471  81.948 99.253  1.00 77.79  ? 121  SER C CA  1 
ATOM   4827  C C   . SER C  1 121 ? 35.491  80.774 100.229 1.00 77.43  ? 121  SER C C   1 
ATOM   4828  O O   . SER C  1 121 ? 34.566  80.629 101.028 1.00 78.10  ? 121  SER C O   1 
ATOM   4829  C CB  . SER C  1 121 ? 34.413  81.640 98.202  1.00 75.14  ? 121  SER C CB  1 
ATOM   4830  O OG  . SER C  1 121 ? 34.218  82.730 97.329  1.00 75.68  ? 121  SER C OG  1 
ATOM   4831  N N   . TRP C  1 122 ? 36.507  79.922 100.140 1.00 76.49  ? 122  TRP C N   1 
ATOM   4832  C CA  . TRP C  1 122 ? 36.615  78.766 101.023 1.00 76.34  ? 122  TRP C CA  1 
ATOM   4833  C C   . TRP C  1 122 ? 37.145  79.198 102.382 1.00 79.81  ? 122  TRP C C   1 
ATOM   4834  O O   . TRP C  1 122 ? 38.309  78.966 102.706 1.00 80.90  ? 122  TRP C O   1 
ATOM   4835  C CB  . TRP C  1 122 ? 37.515  77.701 100.399 1.00 74.27  ? 122  TRP C CB  1 
ATOM   4836  C CG  . TRP C  1 122 ? 36.962  77.159 99.118  1.00 71.04  ? 122  TRP C CG  1 
ATOM   4837  C CD1 . TRP C  1 122 ? 37.422  77.400 97.857  1.00 69.63  ? 122  TRP C CD1 1 
ATOM   4838  C CD2 . TRP C  1 122 ? 35.828  76.298 98.975  1.00 69.05  ? 122  TRP C CD2 1 
ATOM   4839  N NE1 . TRP C  1 122 ? 36.651  76.732 96.936  1.00 66.91  ? 122  TRP C NE1 1 
ATOM   4840  C CE2 . TRP C  1 122 ? 35.663  76.050 97.596  1.00 66.50  ? 122  TRP C CE2 1 
ATOM   4841  C CE3 . TRP C  1 122 ? 34.938  75.709 99.881  1.00 69.36  ? 122  TRP C CE3 1 
ATOM   4842  C CZ2 . TRP C  1 122 ? 34.641  75.232 97.099  1.00 64.30  ? 122  TRP C CZ2 1 
ATOM   4843  C CZ3 . TRP C  1 122 ? 33.923  74.899 99.388  1.00 67.14  ? 122  TRP C CZ3 1 
ATOM   4844  C CH2 . TRP C  1 122 ? 33.783  74.668 98.007  1.00 64.67  ? 122  TRP C CH2 1 
ATOM   4845  N N   . SER C  1 123 ? 36.273  79.827 103.168 1.00 81.75  ? 123  SER C N   1 
ATOM   4846  C CA  . SER C  1 123 ? 36.643  80.404 104.463 1.00 85.46  ? 123  SER C CA  1 
ATOM   4847  C C   . SER C  1 123 ? 36.728  79.353 105.569 1.00 86.16  ? 123  SER C C   1 
ATOM   4848  O O   . SER C  1 123 ? 37.461  79.534 106.538 1.00 89.03  ? 123  SER C O   1 
ATOM   4849  C CB  . SER C  1 123 ? 35.638  81.489 104.866 1.00 87.43  ? 123  SER C CB  1 
ATOM   4850  O OG  . SER C  1 123 ? 34.328  80.959 104.975 1.00 86.03  ? 123  SER C OG  1 
ATOM   4851  N N   . SER C  1 124 ? 35.970  78.268 105.423 1.00 83.80  ? 124  SER C N   1 
ATOM   4852  C CA  . SER C  1 124 ? 35.932  77.187 106.410 1.00 84.38  ? 124  SER C CA  1 
ATOM   4853  C C   . SER C  1 124 ? 36.914  76.042 106.095 1.00 82.91  ? 124  SER C C   1 
ATOM   4854  O O   . SER C  1 124 ? 37.075  75.122 106.899 1.00 83.63  ? 124  SER C O   1 
ATOM   4855  C CB  . SER C  1 124 ? 34.504  76.643 106.509 1.00 83.03  ? 124  SER C CB  1 
ATOM   4856  O OG  . SER C  1 124 ? 34.397  75.640 107.501 1.00 83.85  ? 124  SER C OG  1 
ATOM   4857  N N   . HIS C  1 125 ? 37.562  76.103 104.932 1.00 81.08  ? 125  HIS C N   1 
ATOM   4858  C CA  . HIS C  1 125 ? 38.525  75.082 104.511 1.00 79.73  ? 125  HIS C CA  1 
ATOM   4859  C C   . HIS C  1 125 ? 39.832  75.724 104.067 1.00 80.76  ? 125  HIS C C   1 
ATOM   4860  O O   . HIS C  1 125 ? 39.889  76.930 103.821 1.00 81.88  ? 125  HIS C O   1 
ATOM   4861  C CB  . HIS C  1 125 ? 37.951  74.250 103.360 1.00 76.01  ? 125  HIS C CB  1 
ATOM   4862  C CG  . HIS C  1 125 ? 36.779  73.406 103.752 1.00 75.03  ? 125  HIS C CG  1 
ATOM   4863  N ND1 . HIS C  1 125 ? 35.494  73.900 103.811 1.00 74.88  ? 125  HIS C ND1 1 
ATOM   4864  C CD2 . HIS C  1 125 ? 36.698  72.101 104.105 1.00 74.36  ? 125  HIS C CD2 1 
ATOM   4865  C CE1 . HIS C  1 125 ? 34.672  72.936 104.187 1.00 74.16  ? 125  HIS C CE1 1 
ATOM   4866  N NE2 . HIS C  1 125 ? 35.377  71.834 104.370 1.00 73.84  ? 125  HIS C NE2 1 
ATOM   4867  N N   . GLU C  1 126 ? 40.880  74.911 103.968 1.00 80.61  ? 126  GLU C N   1 
ATOM   4868  C CA  . GLU C  1 126 ? 42.164  75.368 103.448 1.00 81.43  ? 126  GLU C CA  1 
ATOM   4869  C C   . GLU C  1 126 ? 42.218  75.071 101.952 1.00 78.30  ? 126  GLU C C   1 
ATOM   4870  O O   . GLU C  1 126 ? 41.965  73.939 101.533 1.00 76.05  ? 126  GLU C O   1 
ATOM   4871  C CB  . GLU C  1 126 ? 43.310  74.673 104.182 1.00 83.29  ? 126  GLU C CB  1 
ATOM   4872  C CG  . GLU C  1 126 ? 44.697  75.185 103.823 1.00 84.71  ? 126  GLU C CG  1 
ATOM   4873  C CD  . GLU C  1 126 ? 44.906  76.649 104.182 1.00 87.56  ? 126  GLU C CD  1 
ATOM   4874  O OE1 . GLU C  1 126 ? 44.818  76.997 105.382 1.00 90.48  ? 126  GLU C OE1 1 
ATOM   4875  O OE2 . GLU C  1 126 ? 45.172  77.448 103.256 1.00 87.05  ? 126  GLU C OE2 1 
ATOM   4876  N N   . ALA C  1 127 ? 42.542  76.088 101.153 1.00 78.40  ? 127  ALA C N   1 
ATOM   4877  C CA  . ALA C  1 127 ? 42.475  75.989 99.686  1.00 75.59  ? 127  ALA C CA  1 
ATOM   4878  C C   . ALA C  1 127 ? 43.802  76.237 98.957  1.00 76.02  ? 127  ALA C C   1 
ATOM   4879  O O   . ALA C  1 127 ? 43.917  75.921 97.770  1.00 73.76  ? 127  ALA C O   1 
ATOM   4880  C CB  . ALA C  1 127 ? 41.414  76.945 99.160  1.00 74.93  ? 127  ALA C CB  1 
ATOM   4881  N N   . SER C  1 128 ? 44.795  76.785 99.656  1.00 79.06  ? 128  SER C N   1 
ATOM   4882  C CA  . SER C  1 128 ? 46.045  77.227 99.023  1.00 80.00  ? 128  SER C CA  1 
ATOM   4883  C C   . SER C  1 128 ? 47.198  76.227 99.147  1.00 80.32  ? 128  SER C C   1 
ATOM   4884  O O   . SER C  1 128 ? 48.273  76.452 98.588  1.00 80.99  ? 128  SER C O   1 
ATOM   4885  C CB  . SER C  1 128 ? 46.473  78.579 99.603  1.00 83.47  ? 128  SER C CB  1 
ATOM   4886  O OG  . SER C  1 128 ? 45.619  79.611 99.141  1.00 83.20  ? 128  SER C OG  1 
ATOM   4887  N N   . LEU C  1 129 ? 46.976  75.131 99.868  1.00 80.04  ? 129  LEU C N   1 
ATOM   4888  C CA  . LEU C  1 129 ? 48.010  74.117 100.073 1.00 80.63  ? 129  LEU C CA  1 
ATOM   4889  C C   . LEU C  1 129 ? 47.744  72.849 99.259  1.00 77.52  ? 129  LEU C C   1 
ATOM   4890  O O   . LEU C  1 129 ? 48.458  71.856 99.403  1.00 77.84  ? 129  LEU C O   1 
ATOM   4891  C CB  . LEU C  1 129 ? 48.129  73.774 101.563 1.00 83.26  ? 129  LEU C CB  1 
ATOM   4892  C CG  . LEU C  1 129 ? 48.851  74.797 102.447 1.00 87.17  ? 129  LEU C CG  1 
ATOM   4893  C CD1 . LEU C  1 129 ? 47.979  76.005 102.744 1.00 88.04  ? 129  LEU C CD1 1 
ATOM   4894  C CD2 . LEU C  1 129 ? 49.281  74.135 103.746 1.00 89.75  ? 129  LEU C CD2 1 
ATOM   4895  N N   . GLY C  1 130 ? 46.731  72.889 98.396  1.00 74.85  ? 130  GLY C N   1 
ATOM   4896  C CA  . GLY C  1 130 ? 46.373  71.744 97.564  1.00 71.93  ? 130  GLY C CA  1 
ATOM   4897  C C   . GLY C  1 130 ? 47.193  71.641 96.288  1.00 70.77  ? 130  GLY C C   1 
ATOM   4898  O O   . GLY C  1 130 ? 46.665  71.815 95.182  1.00 68.57  ? 130  GLY C O   1 
ATOM   4899  N N   . VAL C  1 131 ? 48.482  71.342 96.447  1.00 72.41  ? 131  VAL C N   1 
ATOM   4900  C CA  . VAL C  1 131 ? 49.416  71.233 95.321  1.00 71.80  ? 131  VAL C CA  1 
ATOM   4901  C C   . VAL C  1 131 ? 50.173  69.903 95.363  1.00 71.85  ? 131  VAL C C   1 
ATOM   4902  O O   . VAL C  1 131 ? 50.014  69.117 96.296  1.00 72.63  ? 131  VAL C O   1 
ATOM   4903  C CB  . VAL C  1 131 ? 50.427  72.405 95.305  1.00 74.23  ? 131  VAL C CB  1 
ATOM   4904  C CG1 . VAL C  1 131 ? 49.699  73.740 95.394  1.00 74.74  ? 131  VAL C CG1 1 
ATOM   4905  C CG2 . VAL C  1 131 ? 51.447  72.272 96.433  1.00 77.38  ? 131  VAL C CG2 1 
ATOM   4906  N N   . SER C  1 132 ? 50.993  69.663 94.343  1.00 71.31  ? 132  SER C N   1 
ATOM   4907  C CA  . SER C  1 132 ? 51.778  68.434 94.244  1.00 71.45  ? 132  SER C CA  1 
ATOM   4908  C C   . SER C  1 132 ? 53.020  68.638 93.383  1.00 72.06  ? 132  SER C C   1 
ATOM   4909  O O   . SER C  1 132 ? 53.048  69.508 92.509  1.00 71.43  ? 132  SER C O   1 
ATOM   4910  C CB  . SER C  1 132 ? 50.927  67.305 93.656  1.00 68.74  ? 132  SER C CB  1 
ATOM   4911  O OG  . SER C  1 132 ? 51.728  66.201 93.266  1.00 68.76  ? 132  SER C OG  1 
ATOM   4912  N N   . SER C  1 133 ? 54.037  67.817 93.632  1.00 73.38  ? 133  SER C N   1 
ATOM   4913  C CA  . SER C  1 133 ? 55.271  67.839 92.852  1.00 74.05  ? 133  SER C CA  1 
ATOM   4914  C C   . SER C  1 133 ? 55.068  67.272 91.441  1.00 71.20  ? 133  SER C C   1 
ATOM   4915  O O   . SER C  1 133 ? 55.903  67.486 90.562  1.00 71.51  ? 133  SER C O   1 
ATOM   4916  C CB  . SER C  1 133 ? 56.368  67.055 93.576  1.00 76.56  ? 133  SER C CB  1 
ATOM   4917  O OG  . SER C  1 133 ? 56.005  65.694 93.724  1.00 75.46  ? 133  SER C OG  1 
ATOM   4918  N N   . ALA C  1 134 ? 53.967  66.547 91.236  1.00 68.55  ? 134  ALA C N   1 
ATOM   4919  C CA  . ALA C  1 134 ? 53.620  65.999 89.923  1.00 65.88  ? 134  ALA C CA  1 
ATOM   4920  C C   . ALA C  1 134 ? 53.223  67.089 88.922  1.00 64.50  ? 134  ALA C C   1 
ATOM   4921  O O   . ALA C  1 134 ? 53.460  66.939 87.725  1.00 63.40  ? 134  ALA C O   1 
ATOM   4922  C CB  . ALA C  1 134 ? 52.506  64.974 90.057  1.00 63.93  ? 134  ALA C CB  1 
ATOM   4923  N N   . CYS C  1 135 ? 52.621  68.173 89.414  1.00 64.68  ? 135  CYS C N   1 
ATOM   4924  C CA  . CYS C  1 135 ? 52.315  69.351 88.594  1.00 63.99  ? 135  CYS C CA  1 
ATOM   4925  C C   . CYS C  1 135 ? 53.190  70.544 89.010  1.00 66.55  ? 135  CYS C C   1 
ATOM   4926  O O   . CYS C  1 135 ? 52.748  71.395 89.782  1.00 67.52  ? 135  CYS C O   1 
ATOM   4927  C CB  . CYS C  1 135 ? 50.832  69.727 88.725  1.00 62.39  ? 135  CYS C CB  1 
ATOM   4928  S SG  . CYS C  1 135 ? 49.671  68.365 88.472  1.00 59.68  ? 135  CYS C SG  1 
ATOM   4929  N N   . PRO C  1 136 ? 54.441  70.604 88.510  1.00 67.80  ? 136  PRO C N   1 
ATOM   4930  C CA  . PRO C  1 136 ? 55.337  71.712 88.845  1.00 70.54  ? 136  PRO C CA  1 
ATOM   4931  C C   . PRO C  1 136 ? 55.175  72.945 87.950  1.00 70.39  ? 136  PRO C C   1 
ATOM   4932  O O   . PRO C  1 136 ? 54.968  72.810 86.743  1.00 68.62  ? 136  PRO C O   1 
ATOM   4933  C CB  . PRO C  1 136 ? 56.722  71.100 88.637  1.00 72.07  ? 136  PRO C CB  1 
ATOM   4934  C CG  . PRO C  1 136 ? 56.517  70.114 87.544  1.00 69.63  ? 136  PRO C CG  1 
ATOM   4935  C CD  . PRO C  1 136 ? 55.153  69.535 87.784  1.00 67.22  ? 136  PRO C CD  1 
ATOM   4936  N N   . TYR C  1 137 ? 55.283  74.130 88.553  1.00 72.46  ? 137  TYR C N   1 
ATOM   4937  C CA  . TYR C  1 137 ? 55.277  75.404 87.828  1.00 73.07  ? 137  TYR C CA  1 
ATOM   4938  C C   . TYR C  1 137 ? 56.382  76.317 88.361  1.00 76.61  ? 137  TYR C C   1 
ATOM   4939  O O   . TYR C  1 137 ? 56.388  76.659 89.543  1.00 78.50  ? 137  TYR C O   1 
ATOM   4940  C CB  . TYR C  1 137 ? 53.918  76.095 87.977  1.00 71.98  ? 137  TYR C CB  1 
ATOM   4941  C CG  . TYR C  1 137 ? 53.856  77.496 87.393  1.00 73.15  ? 137  TYR C CG  1 
ATOM   4942  C CD1 . TYR C  1 137 ? 53.917  77.706 86.012  1.00 72.14  ? 137  TYR C CD1 1 
ATOM   4943  C CD2 . TYR C  1 137 ? 53.720  78.614 88.221  1.00 75.46  ? 137  TYR C CD2 1 
ATOM   4944  C CE1 . TYR C  1 137 ? 53.855  78.986 85.477  1.00 73.44  ? 137  TYR C CE1 1 
ATOM   4945  C CE2 . TYR C  1 137 ? 53.654  79.896 87.693  1.00 76.77  ? 137  TYR C CE2 1 
ATOM   4946  C CZ  . TYR C  1 137 ? 53.721  80.077 86.323  1.00 75.76  ? 137  TYR C CZ  1 
ATOM   4947  O OH  . TYR C  1 137 ? 53.659  81.349 85.803  1.00 77.29  ? 137  TYR C OH  1 
ATOM   4948  N N   . GLN C  1 138 ? 57.306  76.706 87.482  1.00 77.65  ? 138  GLN C N   1 
ATOM   4949  C CA  . GLN C  1 138 ? 58.461  77.545 87.842  1.00 81.24  ? 138  GLN C CA  1 
ATOM   4950  C C   . GLN C  1 138 ? 59.290  76.959 88.991  1.00 83.31  ? 138  GLN C C   1 
ATOM   4951  O O   . GLN C  1 138 ? 59.721  77.682 89.895  1.00 86.31  ? 138  GLN C O   1 
ATOM   4952  C CB  . GLN C  1 138 ? 58.018  78.974 88.181  1.00 82.93  ? 138  GLN C CB  1 
ATOM   4953  C CG  . GLN C  1 138 ? 57.056  79.570 87.166  1.00 81.01  ? 138  GLN C CG  1 
ATOM   4954  C CD  . GLN C  1 138 ? 57.218  81.071 86.993  1.00 83.55  ? 138  GLN C CD  1 
ATOM   4955  O OE1 . GLN C  1 138 ? 57.399  81.805 87.965  1.00 86.21  ? 138  GLN C OE1 1 
ATOM   4956  N NE2 . GLN C  1 138 ? 57.144  81.535 85.749  1.00 82.94  ? 138  GLN C NE2 1 
ATOM   4957  N N   . GLY C  1 139 ? 59.497  75.644 88.950  1.00 81.88  ? 139  GLY C N   1 
ATOM   4958  C CA  . GLY C  1 139 ? 60.315  74.944 89.942  1.00 83.85  ? 139  GLY C CA  1 
ATOM   4959  C C   . GLY C  1 139 ? 59.629  74.671 91.271  1.00 83.96  ? 139  GLY C C   1 
ATOM   4960  O O   . GLY C  1 139 ? 60.241  74.110 92.179  1.00 85.83  ? 139  GLY C O   1 
ATOM   4961  N N   . LYS C  1 140 ? 58.358  75.057 91.379  1.00 82.10  ? 140  LYS C N   1 
ATOM   4962  C CA  . LYS C  1 140 ? 57.588  74.920 92.612  1.00 82.26  ? 140  LYS C CA  1 
ATOM   4963  C C   . LYS C  1 140 ? 56.351  74.071 92.354  1.00 78.66  ? 140  LYS C C   1 
ATOM   4964  O O   . LYS C  1 140 ? 55.857  74.015 91.228  1.00 76.16  ? 140  LYS C O   1 
ATOM   4965  C CB  . LYS C  1 140 ? 57.188  76.303 93.134  1.00 84.03  ? 140  LYS C CB  1 
ATOM   4966  C CG  . LYS C  1 140 ? 58.352  77.084 93.727  1.00 88.15  ? 140  LYS C CG  1 
ATOM   4967  C CD  . LYS C  1 140 ? 58.343  78.549 93.312  1.00 89.58  ? 140  LYS C CD  1 
ATOM   4968  C CE  . LYS C  1 140 ? 59.633  79.256 93.708  1.00 93.78  ? 140  LYS C CE  1 
ATOM   4969  N NZ  . LYS C  1 140 ? 59.639  79.691 95.132  1.00 96.80  ? 140  LYS C NZ  1 
ATOM   4970  N N   . SER C  1 141 ? 55.859  73.417 93.402  1.00 78.62  ? 141  SER C N   1 
ATOM   4971  C CA  . SER C  1 141 ? 54.693  72.539 93.297  1.00 75.56  ? 141  SER C CA  1 
ATOM   4972  C C   . SER C  1 141 ? 53.421  73.344 93.036  1.00 73.95  ? 141  SER C C   1 
ATOM   4973  O O   . SER C  1 141 ? 53.165  74.349 93.699  1.00 75.64  ? 141  SER C O   1 
ATOM   4974  C CB  . SER C  1 141 ? 54.532  71.706 94.571  1.00 76.44  ? 141  SER C CB  1 
ATOM   4975  O OG  . SER C  1 141 ? 55.617  70.808 94.731  1.00 77.73  ? 141  SER C OG  1 
ATOM   4976  N N   . SER C  1 142 ? 52.631  72.889 92.067  1.00 70.87  ? 142  SER C N   1 
ATOM   4977  C CA  . SER C  1 142 ? 51.419  73.586 91.644  1.00 69.26  ? 142  SER C CA  1 
ATOM   4978  C C   . SER C  1 142 ? 50.300  72.568 91.418  1.00 66.34  ? 142  SER C C   1 
ATOM   4979  O O   . SER C  1 142 ? 50.413  71.413 91.838  1.00 65.94  ? 142  SER C O   1 
ATOM   4980  C CB  . SER C  1 142 ? 51.704  74.383 90.365  1.00 68.92  ? 142  SER C CB  1 
ATOM   4981  O OG  . SER C  1 142 ? 50.611  75.208 90.005  1.00 67.94  ? 142  SER C OG  1 
ATOM   4982  N N   . PHE C  1 143 ? 49.219  72.998 90.771  1.00 64.55  ? 143  PHE C N   1 
ATOM   4983  C CA  . PHE C  1 143 ? 48.108  72.104 90.444  1.00 61.89  ? 143  PHE C CA  1 
ATOM   4984  C C   . PHE C  1 143 ? 47.313  72.642 89.253  1.00 60.15  ? 143  PHE C C   1 
ATOM   4985  O O   . PHE C  1 143 ? 47.533  73.770 88.811  1.00 61.11  ? 143  PHE C O   1 
ATOM   4986  C CB  . PHE C  1 143 ? 47.194  71.933 91.667  1.00 62.15  ? 143  PHE C CB  1 
ATOM   4987  C CG  . PHE C  1 143 ? 46.356  70.681 91.637  1.00 60.04  ? 143  PHE C CG  1 
ATOM   4988  C CD1 . PHE C  1 143 ? 46.957  69.428 91.609  1.00 59.67  ? 143  PHE C CD1 1 
ATOM   4989  C CD2 . PHE C  1 143 ? 44.967  70.754 91.646  1.00 58.67  ? 143  PHE C CD2 1 
ATOM   4990  C CE1 . PHE C  1 143 ? 46.192  68.272 91.586  1.00 58.00  ? 143  PHE C CE1 1 
ATOM   4991  C CE2 . PHE C  1 143 ? 44.196  69.601 91.625  1.00 56.97  ? 143  PHE C CE2 1 
ATOM   4992  C CZ  . PHE C  1 143 ? 44.809  68.358 91.595  1.00 56.65  ? 143  PHE C CZ  1 
ATOM   4993  N N   . PHE C  1 144 ? 46.404  71.821 88.730  1.00 57.82  ? 144  PHE C N   1 
ATOM   4994  C CA  . PHE C  1 144 ? 45.456  72.259 87.707  1.00 56.27  ? 144  PHE C CA  1 
ATOM   4995  C C   . PHE C  1 144 ? 44.800  73.569 88.157  1.00 57.44  ? 144  PHE C C   1 
ATOM   4996  O O   . PHE C  1 144 ? 44.097  73.597 89.163  1.00 57.84  ? 144  PHE C O   1 
ATOM   4997  C CB  . PHE C  1 144 ? 44.364  71.204 87.472  1.00 54.04  ? 144  PHE C CB  1 
ATOM   4998  C CG  . PHE C  1 144 ? 44.885  69.827 87.144  1.00 53.06  ? 144  PHE C CG  1 
ATOM   4999  C CD1 . PHE C  1 144 ? 45.427  69.545 85.895  1.00 52.26  ? 144  PHE C CD1 1 
ATOM   5000  C CD2 . PHE C  1 144 ? 44.811  68.803 88.083  1.00 53.13  ? 144  PHE C CD2 1 
ATOM   5001  C CE1 . PHE C  1 144 ? 45.894  68.272 85.598  1.00 51.56  ? 144  PHE C CE1 1 
ATOM   5002  C CE2 . PHE C  1 144 ? 45.278  67.531 87.791  1.00 52.45  ? 144  PHE C CE2 1 
ATOM   5003  C CZ  . PHE C  1 144 ? 45.819  67.264 86.547  1.00 51.67  ? 144  PHE C CZ  1 
ATOM   5004  N N   . ARG C  1 145 ? 45.028  74.645 87.409  1.00 58.18  ? 145  ARG C N   1 
ATOM   5005  C CA  . ARG C  1 145 ? 44.590  75.988 87.808  1.00 59.81  ? 145  ARG C CA  1 
ATOM   5006  C C   . ARG C  1 145 ? 43.076  76.189 87.887  1.00 58.85  ? 145  ARG C C   1 
ATOM   5007  O O   . ARG C  1 145 ? 42.610  77.086 88.589  1.00 60.35  ? 145  ARG C O   1 
ATOM   5008  C CB  . ARG C  1 145 ? 45.153  77.036 86.850  1.00 60.83  ? 145  ARG C CB  1 
ATOM   5009  C CG  . ARG C  1 145 ? 46.664  77.051 86.754  1.00 62.27  ? 145  ARG C CG  1 
ATOM   5010  C CD  . ARG C  1 145 ? 47.145  78.379 86.209  1.00 64.19  ? 145  ARG C CD  1 
ATOM   5011  N NE  . ARG C  1 145 ? 48.574  78.351 85.922  1.00 65.50  ? 145  ARG C NE  1 
ATOM   5012  C CZ  . ARG C  1 145 ? 49.535  78.464 86.836  1.00 67.66  ? 145  ARG C CZ  1 
ATOM   5013  N NH1 . ARG C  1 145 ? 49.248  78.605 88.129  1.00 68.80  ? 145  ARG C NH1 1 
ATOM   5014  N NH2 . ARG C  1 145 ? 50.802  78.430 86.453  1.00 68.87  ? 145  ARG C NH2 1 
ATOM   5015  N N   . ASN C  1 146 ? 42.312  75.380 87.161  1.00 56.62  ? 146  ASN C N   1 
ATOM   5016  C CA  . ASN C  1 146 ? 40.863  75.575 87.076  1.00 55.78  ? 146  ASN C CA  1 
ATOM   5017  C C   . ASN C  1 146 ? 40.075  74.945 88.221  1.00 55.54  ? 146  ASN C C   1 
ATOM   5018  O O   . ASN C  1 146 ? 38.905  75.278 88.422  1.00 55.42  ? 146  ASN C O   1 
ATOM   5019  C CB  . ASN C  1 146 ? 40.339  75.075 85.726  1.00 53.77  ? 146  ASN C CB  1 
ATOM   5020  C CG  . ASN C  1 146 ? 40.745  75.980 84.578  1.00 54.33  ? 146  ASN C CG  1 
ATOM   5021  O OD1 . ASN C  1 146 ? 40.621  77.201 84.672  1.00 55.94  ? 146  ASN C OD1 1 
ATOM   5022  N ND2 . ASN C  1 146 ? 41.235  75.391 83.492  1.00 53.23  ? 146  ASN C ND2 1 
ATOM   5023  N N   . VAL C  1 147 ? 40.711  74.047 88.971  1.00 55.67  ? 147  VAL C N   1 
ATOM   5024  C CA  . VAL C  1 147 ? 40.062  73.409 90.119  1.00 55.74  ? 147  VAL C CA  1 
ATOM   5025  C C   . VAL C  1 147 ? 40.911  73.507 91.389  1.00 57.86  ? 147  VAL C C   1 
ATOM   5026  O O   . VAL C  1 147 ? 42.140  73.530 91.326  1.00 58.78  ? 147  VAL C O   1 
ATOM   5027  C CB  . VAL C  1 147 ? 39.711  71.934 89.832  1.00 53.75  ? 147  VAL C CB  1 
ATOM   5028  C CG1 . VAL C  1 147 ? 38.577  71.840 88.821  1.00 52.01  ? 147  VAL C CG1 1 
ATOM   5029  C CG2 . VAL C  1 147 ? 40.930  71.154 89.348  1.00 53.36  ? 147  VAL C CG2 1 
ATOM   5030  N N   . VAL C  1 148 ? 40.239  73.555 92.537  1.00 58.83  ? 148  VAL C N   1 
ATOM   5031  C CA  . VAL C  1 148 ? 40.892  73.749 93.835  1.00 61.20  ? 148  VAL C CA  1 
ATOM   5032  C C   . VAL C  1 148 ? 40.940  72.433 94.619  1.00 60.97  ? 148  VAL C C   1 
ATOM   5033  O O   . VAL C  1 148 ? 39.901  71.830 94.893  1.00 60.00  ? 148  VAL C O   1 
ATOM   5034  C CB  . VAL C  1 148 ? 40.140  74.800 94.686  1.00 62.96  ? 148  VAL C CB  1 
ATOM   5035  C CG1 . VAL C  1 148 ? 40.986  75.238 95.874  1.00 65.82  ? 148  VAL C CG1 1 
ATOM   5036  C CG2 . VAL C  1 148 ? 39.756  76.007 93.841  1.00 63.02  ? 148  VAL C CG2 1 
ATOM   5037  N N   . TRP C  1 149 ? 42.146  71.996 94.976  1.00 62.09  ? 149  TRP C N   1 
ATOM   5038  C CA  . TRP C  1 149 ? 42.321  70.835 95.846  1.00 62.53  ? 149  TRP C CA  1 
ATOM   5039  C C   . TRP C  1 149 ? 42.147  71.283 97.307  1.00 65.01  ? 149  TRP C C   1 
ATOM   5040  O O   . TRP C  1 149 ? 43.040  71.899 97.893  1.00 67.33  ? 149  TRP C O   1 
ATOM   5041  C CB  . TRP C  1 149 ? 43.702  70.207 95.623  1.00 63.00  ? 149  TRP C CB  1 
ATOM   5042  C CG  . TRP C  1 149 ? 43.908  68.855 96.270  1.00 63.23  ? 149  TRP C CG  1 
ATOM   5043  C CD1 . TRP C  1 149 ? 43.063  68.209 97.131  1.00 63.34  ? 149  TRP C CD1 1 
ATOM   5044  C CD2 . TRP C  1 149 ? 45.051  68.001 96.120  1.00 63.65  ? 149  TRP C CD2 1 
ATOM   5045  N NE1 . TRP C  1 149 ? 43.602  67.002 97.509  1.00 63.79  ? 149  TRP C NE1 1 
ATOM   5046  C CE2 . TRP C  1 149 ? 44.822  66.852 96.906  1.00 64.00  ? 149  TRP C CE2 1 
ATOM   5047  C CE3 . TRP C  1 149 ? 46.242  68.094 95.392  1.00 63.93  ? 149  TRP C CE3 1 
ATOM   5048  C CZ2 . TRP C  1 149 ? 45.741  65.803 96.984  1.00 64.66  ? 149  TRP C CZ2 1 
ATOM   5049  C CZ3 . TRP C  1 149 ? 47.155  67.051 95.472  1.00 64.54  ? 149  TRP C CZ3 1 
ATOM   5050  C CH2 . TRP C  1 149 ? 46.899  65.921 96.262  1.00 64.96  ? 149  TRP C CH2 1 
ATOM   5051  N N   . LEU C  1 150 ? 40.988  70.969 97.885  1.00 64.67  ? 150  LEU C N   1 
ATOM   5052  C CA  . LEU C  1 150 ? 40.648  71.417 99.236  1.00 67.02  ? 150  LEU C CA  1 
ATOM   5053  C C   . LEU C  1 150 ? 41.123  70.428 100.296 1.00 68.44  ? 150  LEU C C   1 
ATOM   5054  O O   . LEU C  1 150 ? 41.029  69.211 100.109 1.00 67.09  ? 150  LEU C O   1 
ATOM   5055  C CB  . LEU C  1 150 ? 39.134  71.622 99.373  1.00 66.25  ? 150  LEU C CB  1 
ATOM   5056  C CG  . LEU C  1 150 ? 38.507  72.777 98.587  1.00 65.61  ? 150  LEU C CG  1 
ATOM   5057  C CD1 . LEU C  1 150 ? 36.997  72.764 98.776  1.00 64.95  ? 150  LEU C CD1 1 
ATOM   5058  C CD2 . LEU C  1 150 ? 39.087  74.123 99.002  1.00 68.11  ? 150  LEU C CD2 1 
ATOM   5059  N N   . ILE C  1 151 ? 41.625  70.968 101.407 1.00 71.38  ? 151  ILE C N   1 
ATOM   5060  C CA  . ILE C  1 151 ? 42.052  70.168 102.559 1.00 73.34  ? 151  ILE C CA  1 
ATOM   5061  C C   . ILE C  1 151 ? 41.531  70.766 103.870 1.00 75.92  ? 151  ILE C C   1 
ATOM   5062  O O   . ILE C  1 151 ? 41.061  71.906 103.909 1.00 76.56  ? 151  ILE C O   1 
ATOM   5063  C CB  . ILE C  1 151 ? 43.592  70.024 102.618 1.00 74.93  ? 151  ILE C CB  1 
ATOM   5064  C CG1 . ILE C  1 151 ? 44.258  71.371 102.934 1.00 77.44  ? 151  ILE C CG1 1 
ATOM   5065  C CG2 . ILE C  1 151 ? 44.116  69.441 101.311 1.00 72.51  ? 151  ILE C CG2 1 
ATOM   5066  C CD1 . ILE C  1 151 ? 45.771  71.352 102.883 1.00 79.09  ? 151  ILE C CD1 1 
ATOM   5067  N N   . LYS C  1 152 ? 41.629  69.978 104.937 1.00 77.59  ? 152  LYS C N   1 
ATOM   5068  C CA  . LYS C  1 152 ? 41.151  70.369 106.271 1.00 80.31  ? 152  LYS C CA  1 
ATOM   5069  C C   . LYS C  1 152 ? 41.857  71.615 106.822 1.00 83.31  ? 152  LYS C C   1 
ATOM   5070  O O   . LYS C  1 152 ? 43.039  71.839 106.546 1.00 84.12  ? 152  LYS C O   1 
ATOM   5071  C CB  . LYS C  1 152 ? 41.346  69.203 107.247 1.00 81.79  ? 152  LYS C CB  1 
ATOM   5072  C CG  . LYS C  1 152 ? 42.805  68.896 107.556 1.00 83.79  ? 152  LYS C CG  1 
ATOM   5073  C CD  . LYS C  1 152 ? 42.982  67.525 108.186 1.00 84.59  ? 152  LYS C CD  1 
ATOM   5074  C CE  . LYS C  1 152 ? 44.343  67.406 108.853 1.00 87.69  ? 152  LYS C CE  1 
ATOM   5075  N NZ  . LYS C  1 152 ? 44.435  66.195 109.713 1.00 89.30  ? 152  LYS C NZ  1 
ATOM   5076  N N   . LYS C  1 153 ? 41.126  72.413 107.603 1.00 85.13  ? 153  LYS C N   1 
ATOM   5077  C CA  . LYS C  1 153 ? 41.697  73.574 108.296 1.00 88.51  ? 153  LYS C CA  1 
ATOM   5078  C C   . LYS C  1 153 ? 41.713  73.340 109.808 1.00 91.93  ? 153  LYS C C   1 
ATOM   5079  O O   . LYS C  1 153 ? 40.678  73.042 110.406 1.00 92.04  ? 153  LYS C O   1 
ATOM   5080  C CB  . LYS C  1 153 ? 40.907  74.846 107.979 1.00 88.40  ? 153  LYS C CB  1 
ATOM   5081  C CG  . LYS C  1 153 ? 41.724  76.123 108.139 1.00 91.15  ? 153  LYS C CG  1 
ATOM   5082  C CD  . LYS C  1 153 ? 40.859  77.295 108.574 1.00 92.85  ? 153  LYS C CD  1 
ATOM   5083  C CE  . LYS C  1 153 ? 39.919  77.771 107.477 1.00 90.10  ? 153  LYS C CE  1 
ATOM   5084  N NZ  . LYS C  1 153 ? 40.539  78.528 106.355 1.00 89.25  ? 153  LYS C NZ  1 
ATOM   5085  N N   . ASN C  1 154 ? 42.892  73.490 110.411 1.00 94.91  ? 154  ASN C N   1 
ATOM   5086  C CA  . ASN C  1 154 ? 43.111  73.220 111.840 1.00 98.58  ? 154  ASN C CA  1 
ATOM   5087  C C   . ASN C  1 154 ? 42.618  71.830 112.263 1.00 97.77  ? 154  ASN C C   1 
ATOM   5088  O O   . ASN C  1 154 ? 41.994  71.668 113.316 1.00 99.72  ? 154  ASN C O   1 
ATOM   5089  C CB  . ASN C  1 154 ? 42.483  74.318 112.715 1.00 101.38 ? 154  ASN C CB  1 
ATOM   5090  C CG  . ASN C  1 154 ? 43.098  74.383 114.108 1.00 106.02 ? 154  ASN C CG  1 
ATOM   5091  O OD1 . ASN C  1 154 ? 44.264  74.035 114.300 1.00 107.64 ? 154  ASN C OD1 1 
ATOM   5092  N ND2 . ASN C  1 154 ? 42.317  74.835 115.086 1.00 108.44 ? 154  ASN C ND2 1 
ATOM   5093  N N   . SER C  1 155 ? 42.907  70.838 111.421 1.00 95.02  ? 155  SER C N   1 
ATOM   5094  C CA  . SER C  1 155 ? 42.602  69.436 111.706 1.00 94.32  ? 155  SER C CA  1 
ATOM   5095  C C   . SER C  1 155 ? 41.094  69.146 111.753 1.00 92.60  ? 155  SER C C   1 
ATOM   5096  O O   . SER C  1 155 ? 40.643  68.339 112.562 1.00 93.72  ? 155  SER C O   1 
ATOM   5097  C CB  . SER C  1 155 ? 43.284  69.007 113.018 1.00 98.30  ? 155  SER C CB  1 
ATOM   5098  O OG  . SER C  1 155 ? 43.500  67.607 113.058 1.00 97.78  ? 155  SER C OG  1 
ATOM   5099  N N   . THR C  1 156 ? 40.321  69.813 110.897 1.00 90.12  ? 156  THR C N   1 
ATOM   5100  C CA  . THR C  1 156 ? 38.877  69.556 110.780 1.00 88.30  ? 156  THR C CA  1 
ATOM   5101  C C   . THR C  1 156 ? 38.423  69.812 109.344 1.00 84.63  ? 156  THR C C   1 
ATOM   5102  O O   . THR C  1 156 ? 38.705  70.874 108.790 1.00 84.41  ? 156  THR C O   1 
ATOM   5103  C CB  . THR C  1 156 ? 38.021  70.456 111.712 1.00 90.59  ? 156  THR C CB  1 
ATOM   5104  O OG1 . THR C  1 156 ? 37.761  71.714 111.074 1.00 89.84  ? 156  THR C OG1 1 
ATOM   5105  C CG2 . THR C  1 156 ? 38.691  70.704 113.069 1.00 94.88  ? 156  THR C CG2 1 
ATOM   5106  N N   . TYR C  1 157 ? 37.728  68.844 108.747 1.00 82.00  ? 157  TYR C N   1 
ATOM   5107  C CA  . TYR C  1 157 ? 37.144  69.011 107.412 1.00 78.65  ? 157  TYR C CA  1 
ATOM   5108  C C   . TYR C  1 157 ? 35.617  69.032 107.528 1.00 77.95  ? 157  TYR C C   1 
ATOM   5109  O O   . TYR C  1 157 ? 34.970  67.982 107.474 1.00 76.75  ? 157  TYR C O   1 
ATOM   5110  C CB  . TYR C  1 157 ? 37.598  67.890 106.468 1.00 76.17  ? 157  TYR C CB  1 
ATOM   5111  C CG  . TYR C  1 157 ? 37.393  68.191 104.987 1.00 73.06  ? 157  TYR C CG  1 
ATOM   5112  C CD1 . TYR C  1 157 ? 36.126  68.138 104.405 1.00 71.01  ? 157  TYR C CD1 1 
ATOM   5113  C CD2 . TYR C  1 157 ? 38.470  68.525 104.171 1.00 72.38  ? 157  TYR C CD2 1 
ATOM   5114  C CE1 . TYR C  1 157 ? 35.940  68.408 103.057 1.00 68.44  ? 157  TYR C CE1 1 
ATOM   5115  C CE2 . TYR C  1 157 ? 38.294  68.795 102.822 1.00 69.78  ? 157  TYR C CE2 1 
ATOM   5116  C CZ  . TYR C  1 157 ? 37.026  68.735 102.267 1.00 67.83  ? 157  TYR C CZ  1 
ATOM   5117  O OH  . TYR C  1 157 ? 36.851  69.003 100.924 1.00 65.47  ? 157  TYR C OH  1 
ATOM   5118  N N   . PRO C  1 158 ? 35.035  70.231 107.708 1.00 78.96  ? 158  PRO C N   1 
ATOM   5119  C CA  . PRO C  1 158 ? 33.577  70.329 107.780 1.00 78.47  ? 158  PRO C CA  1 
ATOM   5120  C C   . PRO C  1 158 ? 32.916  70.057 106.434 1.00 75.14  ? 158  PRO C C   1 
ATOM   5121  O O   . PRO C  1 158 ? 33.533  70.258 105.386 1.00 73.39  ? 158  PRO C O   1 
ATOM   5122  C CB  . PRO C  1 158 ? 33.330  71.777 108.230 1.00 80.56  ? 158  PRO C CB  1 
ATOM   5123  C CG  . PRO C  1 158 ? 34.577  72.515 107.898 1.00 81.14  ? 158  PRO C CG  1 
ATOM   5124  C CD  . PRO C  1 158 ? 35.697  71.524 107.963 1.00 81.03  ? 158  PRO C CD  1 
ATOM   5125  N N   . THR C  1 159 ? 31.671  69.595 106.475 1.00 74.52  ? 159  THR C N   1 
ATOM   5126  C CA  . THR C  1 159 ? 30.931  69.268 105.263 1.00 71.70  ? 159  THR C CA  1 
ATOM   5127  C C   . THR C  1 159 ? 30.770  70.513 104.395 1.00 71.02  ? 159  THR C C   1 
ATOM   5128  O O   . THR C  1 159 ? 30.472  71.600 104.898 1.00 72.83  ? 159  THR C O   1 
ATOM   5129  C CB  . THR C  1 159 ? 29.540  68.677 105.584 1.00 71.60  ? 159  THR C CB  1 
ATOM   5130  O OG1 . THR C  1 159 ? 29.678  67.595 106.512 1.00 72.85  ? 159  THR C OG1 1 
ATOM   5131  C CG2 . THR C  1 159 ? 28.858  68.162 104.322 1.00 68.71  ? 159  THR C CG2 1 
ATOM   5132  N N   . ILE C  1 160 ? 30.990  70.337 103.092 1.00 68.67  ? 160  ILE C N   1 
ATOM   5133  C CA  . ILE C  1 160 ? 30.861  71.410 102.109 1.00 67.91  ? 160  ILE C CA  1 
ATOM   5134  C C   . ILE C  1 160 ? 29.489  71.321 101.459 1.00 66.62  ? 160  ILE C C   1 
ATOM   5135  O O   . ILE C  1 160 ? 29.098  70.254 101.003 1.00 64.94  ? 160  ILE C O   1 
ATOM   5136  C CB  . ILE C  1 160 ? 31.937  71.292 101.007 1.00 66.13  ? 160  ILE C CB  1 
ATOM   5137  C CG1 . ILE C  1 160 ? 33.332  71.497 101.605 1.00 67.78  ? 160  ILE C CG1 1 
ATOM   5138  C CG2 . ILE C  1 160 ? 31.677  72.300 99.892  1.00 65.11  ? 160  ILE C CG2 1 
ATOM   5139  C CD1 . ILE C  1 160 ? 34.469  71.039 100.717 1.00 66.30  ? 160  ILE C CD1 1 
ATOM   5140  N N   . LYS C  1 161 ? 28.762  72.435 101.428 1.00 67.72  ? 161  LYS C N   1 
ATOM   5141  C CA  . LYS C  1 161 ? 27.509  72.522 100.678 1.00 66.70  ? 161  LYS C CA  1 
ATOM   5142  C C   . LYS C  1 161 ? 27.549  73.769 99.806  1.00 66.81  ? 161  LYS C C   1 
ATOM   5143  O O   . LYS C  1 161 ? 27.415  74.885 100.304 1.00 68.85  ? 161  LYS C O   1 
ATOM   5144  C CB  . LYS C  1 161 ? 26.299  72.561 101.615 1.00 68.32  ? 161  LYS C CB  1 
ATOM   5145  C CG  . LYS C  1 161 ? 26.144  71.316 102.474 1.00 68.64  ? 161  LYS C CG  1 
ATOM   5146  C CD  . LYS C  1 161 ? 24.795  71.271 103.176 1.00 69.97  ? 161  LYS C CD  1 
ATOM   5147  C CE  . LYS C  1 161 ? 24.662  70.016 104.030 1.00 70.50  ? 161  LYS C CE  1 
ATOM   5148  N NZ  . LYS C  1 161 ? 23.547  70.110 105.020 1.00 72.59  ? 161  LYS C NZ  1 
ATOM   5149  N N   . ARG C  1 162 ? 27.744  73.574 98.504  1.00 64.94  ? 162  ARG C N   1 
ATOM   5150  C CA  . ARG C  1 162 ? 27.881  74.689 97.572  1.00 65.08  ? 162  ARG C CA  1 
ATOM   5151  C C   . ARG C  1 162 ? 26.972  74.520 96.356  1.00 63.68  ? 162  ARG C C   1 
ATOM   5152  O O   . ARG C  1 162 ? 26.839  73.425 95.808  1.00 61.79  ? 162  ARG C O   1 
ATOM   5153  C CB  . ARG C  1 162 ? 29.342  74.865 97.136  1.00 64.62  ? 162  ARG C CB  1 
ATOM   5154  C CG  . ARG C  1 162 ? 30.244  75.565 98.135  1.00 66.90  ? 162  ARG C CG  1 
ATOM   5155  C CD  . ARG C  1 162 ? 29.735  76.949 98.553  1.00 69.17  ? 162  ARG C CD  1 
ATOM   5156  N NE  . ARG C  1 162 ? 30.698  77.994 98.218  1.00 70.19  ? 162  ARG C NE  1 
ATOM   5157  C CZ  . ARG C  1 162 ? 31.822  78.203 98.895  1.00 71.68  ? 162  ARG C CZ  1 
ATOM   5158  N NH1 . ARG C  1 162 ? 32.134  77.443 99.940  1.00 72.35  ? 162  ARG C NH1 1 
ATOM   5159  N NH2 . ARG C  1 162 ? 32.642  79.169 98.523  1.00 72.70  ? 162  ARG C NH2 1 
ATOM   5160  N N   . SER C  1 163 ? 26.343  75.621 95.958  1.00 65.04  ? 163  SER C N   1 
ATOM   5161  C CA  . SER C  1 163 ? 25.418  75.641 94.840  1.00 64.33  ? 163  SER C CA  1 
ATOM   5162  C C   . SER C  1 163 ? 25.748  76.813 93.920  1.00 65.29  ? 163  SER C C   1 
ATOM   5163  O O   . SER C  1 163 ? 26.025  77.913 94.395  1.00 67.25  ? 163  SER C O   1 
ATOM   5164  C CB  . SER C  1 163 ? 23.984  75.771 95.359  1.00 65.43  ? 163  SER C CB  1 
ATOM   5165  O OG  . SER C  1 163 ? 23.050  75.799 94.294  1.00 64.60  ? 163  SER C OG  1 
ATOM   5166  N N   . TYR C  1 164 ? 25.732  76.574 92.609  1.00 64.41  ? 164  TYR C N   1 
ATOM   5167  C CA  . TYR C  1 164 ? 25.870  77.653 91.629  1.00 65.59  ? 164  TYR C CA  1 
ATOM   5168  C C   . TYR C  1 164 ? 24.706  77.673 90.642  1.00 65.97  ? 164  TYR C C   1 
ATOM   5169  O O   . TYR C  1 164 ? 24.388  76.652 90.039  1.00 64.16  ? 164  TYR C O   1 
ATOM   5170  C CB  . TYR C  1 164 ? 27.175  77.544 90.840  1.00 64.32  ? 164  TYR C CB  1 
ATOM   5171  C CG  . TYR C  1 164 ? 27.173  78.480 89.655  1.00 64.57  ? 164  TYR C CG  1 
ATOM   5172  C CD1 . TYR C  1 164 ? 27.449  79.836 89.815  1.00 66.70  ? 164  TYR C CD1 1 
ATOM   5173  C CD2 . TYR C  1 164 ? 26.836  78.024 88.382  1.00 62.99  ? 164  TYR C CD2 1 
ATOM   5174  C CE1 . TYR C  1 164 ? 27.421  80.706 88.735  1.00 67.21  ? 164  TYR C CE1 1 
ATOM   5175  C CE2 . TYR C  1 164 ? 26.805  78.884 87.295  1.00 63.48  ? 164  TYR C CE2 1 
ATOM   5176  C CZ  . TYR C  1 164 ? 27.099  80.223 87.474  1.00 65.58  ? 164  TYR C CZ  1 
ATOM   5177  O OH  . TYR C  1 164 ? 27.070  81.080 86.399  1.00 66.29  ? 164  TYR C OH  1 
ATOM   5178  N N   . ASN C  1 165 ? 24.110  78.852 90.461  1.00 68.98  ? 165  ASN C N   1 
ATOM   5179  C CA  . ASN C  1 165 ? 23.015  79.056 89.514  1.00 70.21  ? 165  ASN C CA  1 
ATOM   5180  C C   . ASN C  1 165 ? 23.527  79.655 88.203  1.00 69.01  ? 165  ASN C C   1 
ATOM   5181  O O   . ASN C  1 165 ? 24.129  80.728 88.202  1.00 70.44  ? 165  ASN C O   1 
ATOM   5182  C CB  . ASN C  1 165 ? 21.973  79.995 90.129  1.00 74.72  ? 165  ASN C CB  1 
ATOM   5183  C CG  . ASN C  1 165 ? 20.641  79.967 89.400  1.00 77.70  ? 165  ASN C CG  1 
ATOM   5184  O OD1 . ASN C  1 165 ? 20.532  79.455 88.286  1.00 76.09  ? 165  ASN C OD1 1 
ATOM   5185  N ND2 . ASN C  1 165 ? 19.617  80.528 90.036  1.00 83.44  ? 165  ASN C ND2 1 
ATOM   5186  N N   . ASN C  1 166 ? 23.276  78.965 87.091  1.00 66.35  ? 166  ASN C N   1 
ATOM   5187  C CA  . ASN C  1 166 ? 23.714  79.431 85.775  1.00 65.32  ? 166  ASN C CA  1 
ATOM   5188  C C   . ASN C  1 166 ? 22.817  80.546 85.234  1.00 66.64  ? 166  ASN C C   1 
ATOM   5189  O O   . ASN C  1 166 ? 21.818  80.285 84.559  1.00 66.41  ? 166  ASN C O   1 
ATOM   5190  C CB  . ASN C  1 166 ? 23.770  78.264 84.781  1.00 63.00  ? 166  ASN C CB  1 
ATOM   5191  C CG  . ASN C  1 166 ? 24.504  78.621 83.500  1.00 62.60  ? 166  ASN C CG  1 
ATOM   5192  O OD1 . ASN C  1 166 ? 25.311  79.552 83.470  1.00 63.60  ? 166  ASN C OD1 1 
ATOM   5193  N ND2 . ASN C  1 166 ? 24.232  77.877 82.434  1.00 61.23  ? 166  ASN C ND2 1 
ATOM   5194  N N   . THR C  1 167 ? 23.189  81.788 85.538  1.00 67.95  ? 167  THR C N   1 
ATOM   5195  C CA  . THR C  1 167 ? 22.435  82.968 85.103  1.00 69.75  ? 167  THR C CA  1 
ATOM   5196  C C   . THR C  1 167 ? 22.811  83.443 83.691  1.00 69.42  ? 167  THR C C   1 
ATOM   5197  O O   . THR C  1 167 ? 22.143  84.318 83.134  1.00 71.28  ? 167  THR C O   1 
ATOM   5198  C CB  . THR C  1 167 ? 22.635  84.146 86.077  1.00 72.25  ? 167  THR C CB  1 
ATOM   5199  O OG1 . THR C  1 167 ? 24.032  84.447 86.187  1.00 72.20  ? 167  THR C OG1 1 
ATOM   5200  C CG2 . THR C  1 167 ? 22.075  83.805 87.448  1.00 72.64  ? 167  THR C CG2 1 
ATOM   5201  N N   . ASN C  1 168 ? 23.877  82.878 83.123  1.00 67.08  ? 168  ASN C N   1 
ATOM   5202  C CA  . ASN C  1 168 ? 24.264  83.180 81.740  1.00 66.64  ? 168  ASN C CA  1 
ATOM   5203  C C   . ASN C  1 168 ? 23.265  82.501 80.819  1.00 65.32  ? 168  ASN C C   1 
ATOM   5204  O O   . ASN C  1 168 ? 22.760  81.433 81.153  1.00 63.75  ? 168  ASN C O   1 
ATOM   5205  C CB  . ASN C  1 168 ? 25.668  82.658 81.393  1.00 65.00  ? 168  ASN C CB  1 
ATOM   5206  C CG  . ASN C  1 168 ? 26.637  82.722 82.558  1.00 65.12  ? 168  ASN C CG  1 
ATOM   5207  O OD1 . ASN C  1 168 ? 27.413  83.671 82.681  1.00 66.72  ? 168  ASN C OD1 1 
ATOM   5208  N ND2 . ASN C  1 168 ? 26.605  81.704 83.415  1.00 63.62  ? 168  ASN C ND2 1 
ATOM   5209  N N   . GLN C  1 169 ? 22.977  83.107 79.670  1.00 66.00  ? 169  GLN C N   1 
ATOM   5210  C CA  . GLN C  1 169 ? 22.126  82.448 78.678  1.00 65.01  ? 169  GLN C CA  1 
ATOM   5211  C C   . GLN C  1 169 ? 22.985  81.586 77.733  1.00 62.70  ? 169  GLN C C   1 
ATOM   5212  O O   . GLN C  1 169 ? 22.999  81.770 76.517  1.00 63.13  ? 169  GLN C O   1 
ATOM   5213  C CB  . GLN C  1 169 ? 21.219  83.444 77.936  1.00 67.46  ? 169  GLN C CB  1 
ATOM   5214  C CG  . GLN C  1 169 ? 21.908  84.538 77.132  1.00 69.14  ? 169  GLN C CG  1 
ATOM   5215  C CD  . GLN C  1 169 ? 21.048  85.042 75.977  1.00 70.97  ? 169  GLN C CD  1 
ATOM   5216  O OE1 . GLN C  1 169 ? 20.235  84.302 75.413  1.00 70.28  ? 169  GLN C OE1 1 
ATOM   5217  N NE2 . GLN C  1 169 ? 21.233  86.302 75.611  1.00 73.48  ? 169  GLN C NE2 1 
ATOM   5218  N N   . GLU C  1 170 ? 23.705  80.644 78.336  1.00 60.33  ? 170  GLU C N   1 
ATOM   5219  C CA  . GLU C  1 170 ? 24.597  79.729 77.633  1.00 58.14  ? 170  GLU C CA  1 
ATOM   5220  C C   . GLU C  1 170 ? 24.643  78.401 78.386  1.00 55.88  ? 170  GLU C C   1 
ATOM   5221  O O   . GLU C  1 170 ? 24.375  78.350 79.590  1.00 55.95  ? 170  GLU C O   1 
ATOM   5222  C CB  . GLU C  1 170 ? 26.023  80.295 77.551  1.00 58.32  ? 170  GLU C CB  1 
ATOM   5223  C CG  . GLU C  1 170 ? 26.238  81.389 76.511  1.00 60.12  ? 170  GLU C CG  1 
ATOM   5224  C CD  . GLU C  1 170 ? 26.242  82.798 77.087  1.00 62.54  ? 170  GLU C CD  1 
ATOM   5225  O OE1 . GLU C  1 170 ? 25.676  83.020 78.180  1.00 63.17  ? 170  GLU C OE1 1 
ATOM   5226  O OE2 . GLU C  1 170 ? 26.818  83.696 76.438  1.00 64.00  ? 170  GLU C OE2 1 
ATOM   5227  N N   . ASP C  1 171 ? 24.970  77.330 77.668  1.00 53.99  ? 171  ASP C N   1 
ATOM   5228  C CA  . ASP C  1 171 ? 25.378  76.078 78.297  1.00 51.95  ? 171  ASP C CA  1 
ATOM   5229  C C   . ASP C  1 171 ? 26.733  76.341 78.955  1.00 51.57  ? 171  ASP C C   1 
ATOM   5230  O O   . ASP C  1 171 ? 27.516  77.164 78.467  1.00 52.33  ? 171  ASP C O   1 
ATOM   5231  C CB  . ASP C  1 171 ? 25.508  74.941 77.268  1.00 50.54  ? 171  ASP C CB  1 
ATOM   5232  C CG  . ASP C  1 171 ? 24.166  74.494 76.686  1.00 50.79  ? 171  ASP C CG  1 
ATOM   5233  O OD1 . ASP C  1 171 ? 23.107  74.681 77.324  1.00 51.56  ? 171  ASP C OD1 1 
ATOM   5234  O OD2 . ASP C  1 171 ? 24.179  73.929 75.572  1.00 50.35  ? 171  ASP C OD2 1 
ATOM   5235  N N   . LEU C  1 172 ? 27.000  75.652 80.061  1.00 50.54  ? 172  LEU C N   1 
ATOM   5236  C CA  . LEU C  1 172 ? 28.242  75.842 80.800  1.00 50.40  ? 172  LEU C CA  1 
ATOM   5237  C C   . LEU C  1 172 ? 28.933  74.512 81.070  1.00 48.60  ? 172  LEU C C   1 
ATOM   5238  O O   . LEU C  1 172 ? 28.332  73.598 81.632  1.00 47.85  ? 172  LEU C O   1 
ATOM   5239  C CB  . LEU C  1 172 ? 27.962  76.547 82.126  1.00 51.71  ? 172  LEU C CB  1 
ATOM   5240  C CG  . LEU C  1 172 ? 29.213  77.062 82.845  1.00 52.38  ? 172  LEU C CG  1 
ATOM   5241  C CD1 . LEU C  1 172 ? 29.616  78.425 82.300  1.00 54.05  ? 172  LEU C CD1 1 
ATOM   5242  C CD2 . LEU C  1 172 ? 28.988  77.133 84.348  1.00 53.16  ? 172  LEU C CD2 1 
ATOM   5243  N N   . LEU C  1 173 ? 30.200  74.420 80.672  1.00 48.07  ? 173  LEU C N   1 
ATOM   5244  C CA  . LEU C  1 173 ? 31.013  73.243 80.953  1.00 46.69  ? 173  LEU C CA  1 
ATOM   5245  C C   . LEU C  1 173 ? 31.648  73.361 82.335  1.00 47.18  ? 173  LEU C C   1 
ATOM   5246  O O   . LEU C  1 173 ? 32.566  74.157 82.538  1.00 48.13  ? 173  LEU C O   1 
ATOM   5247  C CB  . LEU C  1 173 ? 32.112  73.074 79.905  1.00 46.20  ? 173  LEU C CB  1 
ATOM   5248  C CG  . LEU C  1 173 ? 33.122  71.950 80.182  1.00 45.17  ? 173  LEU C CG  1 
ATOM   5249  C CD1 . LEU C  1 173 ? 32.460  70.580 80.128  1.00 43.91  ? 173  LEU C CD1 1 
ATOM   5250  C CD2 . LEU C  1 173 ? 34.277  72.026 79.200  1.00 45.13  ? 173  LEU C CD2 1 
ATOM   5251  N N   . VAL C  1 174 ? 31.163  72.547 83.268  1.00 46.66  ? 174  VAL C N   1 
ATOM   5252  C CA  . VAL C  1 174 ? 31.687  72.506 84.626  1.00 47.23  ? 174  VAL C CA  1 
ATOM   5253  C C   . VAL C  1 174 ? 32.571  71.269 84.786  1.00 46.18  ? 174  VAL C C   1 
ATOM   5254  O O   . VAL C  1 174 ? 32.176  70.164 84.412  1.00 45.02  ? 174  VAL C O   1 
ATOM   5255  C CB  . VAL C  1 174 ? 30.549  72.445 85.667  1.00 47.76  ? 174  VAL C CB  1 
ATOM   5256  C CG1 . VAL C  1 174 ? 31.099  72.647 87.072  1.00 48.87  ? 174  VAL C CG1 1 
ATOM   5257  C CG2 . VAL C  1 174 ? 29.482  73.485 85.359  1.00 48.70  ? 174  VAL C CG2 1 
ATOM   5258  N N   . LEU C  1 175 ? 33.765  71.470 85.339  1.00 46.81  ? 175  LEU C N   1 
ATOM   5259  C CA  . LEU C  1 175 ? 34.697  70.385 85.631  1.00 46.23  ? 175  LEU C CA  1 
ATOM   5260  C C   . LEU C  1 175 ? 34.950  70.306 87.131  1.00 47.28  ? 175  LEU C C   1 
ATOM   5261  O O   . LEU C  1 175 ? 35.082  71.332 87.793  1.00 48.69  ? 175  LEU C O   1 
ATOM   5262  C CB  . LEU C  1 175 ? 36.032  70.628 84.929  1.00 46.34  ? 175  LEU C CB  1 
ATOM   5263  C CG  . LEU C  1 175 ? 36.005  70.832 83.417  1.00 45.64  ? 175  LEU C CG  1 
ATOM   5264  C CD1 . LEU C  1 175 ? 37.381  71.248 82.918  1.00 46.21  ? 175  LEU C CD1 1 
ATOM   5265  C CD2 . LEU C  1 175 ? 35.533  69.569 82.718  1.00 44.16  ? 175  LEU C CD2 1 
ATOM   5266  N N   . TRP C  1 176 ? 35.027  69.087 87.656  1.00 46.78  ? 176  TRP C N   1 
ATOM   5267  C CA  . TRP C  1 176 ? 35.437  68.861 89.040  1.00 47.92  ? 176  TRP C CA  1 
ATOM   5268  C C   . TRP C  1 176 ? 36.136  67.509 89.167  1.00 47.44  ? 176  TRP C C   1 
ATOM   5269  O O   . TRP C  1 176 ? 36.247  66.765 88.192  1.00 46.19  ? 176  TRP C O   1 
ATOM   5270  C CB  . TRP C  1 176 ? 34.236  68.950 89.989  1.00 48.49  ? 176  TRP C CB  1 
ATOM   5271  C CG  . TRP C  1 176 ? 33.238  67.844 89.829  1.00 47.37  ? 176  TRP C CG  1 
ATOM   5272  C CD1 . TRP C  1 176 ? 33.142  66.708 90.582  1.00 47.43  ? 176  TRP C CD1 1 
ATOM   5273  C CD2 . TRP C  1 176 ? 32.190  67.771 88.859  1.00 46.28  ? 176  TRP C CD2 1 
ATOM   5274  N NE1 . TRP C  1 176 ? 32.100  65.934 90.138  1.00 46.45  ? 176  TRP C NE1 1 
ATOM   5275  C CE2 . TRP C  1 176 ? 31.498  66.564 89.081  1.00 45.74  ? 176  TRP C CE2 1 
ATOM   5276  C CE3 . TRP C  1 176 ? 31.768  68.613 87.822  1.00 45.92  ? 176  TRP C CE3 1 
ATOM   5277  C CZ2 . TRP C  1 176 ? 30.407  66.175 88.302  1.00 44.87  ? 176  TRP C CZ2 1 
ATOM   5278  C CZ3 . TRP C  1 176 ? 30.686  68.227 87.052  1.00 45.06  ? 176  TRP C CZ3 1 
ATOM   5279  C CH2 . TRP C  1 176 ? 30.018  67.019 87.296  1.00 44.55  ? 176  TRP C CH2 1 
ATOM   5280  N N   . GLY C  1 177 ? 36.609  67.197 90.368  1.00 48.66  ? 177  GLY C N   1 
ATOM   5281  C CA  . GLY C  1 177 ? 37.347  65.959 90.590  1.00 48.62  ? 177  GLY C CA  1 
ATOM   5282  C C   . GLY C  1 177 ? 37.195  65.371 91.976  1.00 49.84  ? 177  GLY C C   1 
ATOM   5283  O O   . GLY C  1 177 ? 36.712  66.028 92.902  1.00 50.98  ? 177  GLY C O   1 
ATOM   5284  N N   . ILE C  1 178 ? 37.611  64.114 92.097  1.00 49.76  ? 178  ILE C N   1 
ATOM   5285  C CA  . ILE C  1 178 ? 37.703  63.421 93.375  1.00 51.18  ? 178  ILE C CA  1 
ATOM   5286  C C   . ILE C  1 178 ? 39.137  62.916 93.512  1.00 52.10  ? 178  ILE C C   1 
ATOM   5287  O O   . ILE C  1 178 ? 39.756  62.529 92.520  1.00 51.17  ? 178  ILE C O   1 
ATOM   5288  C CB  . ILE C  1 178 ? 36.700  62.238 93.462  1.00 50.55  ? 178  ILE C CB  1 
ATOM   5289  C CG1 . ILE C  1 178 ? 36.528  61.779 94.926  1.00 52.30  ? 178  ILE C CG1 1 
ATOM   5290  C CG2 . ILE C  1 178 ? 37.103  61.110 92.513  1.00 49.47  ? 178  ILE C CG2 1 
ATOM   5291  C CD1 . ILE C  1 178 ? 36.310  60.293 95.142  1.00 52.41  ? 178  ILE C CD1 1 
ATOM   5292  N N   . HIS C  1 179 ? 39.669  62.934 94.732  1.00 54.11  ? 179  HIS C N   1 
ATOM   5293  C CA  . HIS C  1 179 ? 41.007  62.406 94.987  1.00 55.39  ? 179  HIS C CA  1 
ATOM   5294  C C   . HIS C  1 179 ? 40.951  61.022 95.627  1.00 56.15  ? 179  HIS C C   1 
ATOM   5295  O O   . HIS C  1 179 ? 40.214  60.798 96.593  1.00 57.03  ? 179  HIS C O   1 
ATOM   5296  C CB  . HIS C  1 179 ? 41.807  63.347 95.885  1.00 57.53  ? 179  HIS C CB  1 
ATOM   5297  C CG  . HIS C  1 179 ? 43.137  62.795 96.293  1.00 59.21  ? 179  HIS C CG  1 
ATOM   5298  N ND1 . HIS C  1 179 ? 43.481  62.580 97.611  1.00 61.59  ? 179  HIS C ND1 1 
ATOM   5299  C CD2 . HIS C  1 179 ? 44.195  62.384 95.556  1.00 59.04  ? 179  HIS C CD2 1 
ATOM   5300  C CE1 . HIS C  1 179 ? 44.702  62.081 97.669  1.00 62.85  ? 179  HIS C CE1 1 
ATOM   5301  N NE2 . HIS C  1 179 ? 45.157  61.951 96.436  1.00 61.33  ? 179  HIS C NE2 1 
ATOM   5302  N N   . HIS C  1 180 ? 41.752  60.106 95.087  1.00 56.03  ? 180  HIS C N   1 
ATOM   5303  C CA  . HIS C  1 180 ? 41.883  58.757 95.622  1.00 57.04  ? 180  HIS C CA  1 
ATOM   5304  C C   . HIS C  1 180 ? 43.223  58.654 96.351  1.00 59.37  ? 180  HIS C C   1 
ATOM   5305  O O   . HIS C  1 180 ? 44.278  58.685 95.710  1.00 59.40  ? 180  HIS C O   1 
ATOM   5306  C CB  . HIS C  1 180 ? 41.821  57.736 94.488  1.00 55.55  ? 180  HIS C CB  1 
ATOM   5307  C CG  . HIS C  1 180 ? 40.547  57.779 93.703  1.00 53.51  ? 180  HIS C CG  1 
ATOM   5308  N ND1 . HIS C  1 180 ? 39.599  56.783 93.774  1.00 53.20  ? 180  HIS C ND1 1 
ATOM   5309  C CD2 . HIS C  1 180 ? 40.065  58.693 92.827  1.00 51.89  ? 180  HIS C CD2 1 
ATOM   5310  C CE1 . HIS C  1 180 ? 38.587  57.080 92.979  1.00 51.47  ? 180  HIS C CE1 1 
ATOM   5311  N NE2 . HIS C  1 180 ? 38.844  58.235 92.394  1.00 50.66  ? 180  HIS C NE2 1 
ATOM   5312  N N   . PRO C  1 181 ? 43.192  58.541 97.693  1.00 61.50  ? 181  PRO C N   1 
ATOM   5313  C CA  . PRO C  1 181 ? 44.424  58.490 98.479  1.00 64.07  ? 181  PRO C CA  1 
ATOM   5314  C C   . PRO C  1 181 ? 45.061  57.101 98.487  1.00 65.06  ? 181  PRO C C   1 
ATOM   5315  O O   . PRO C  1 181 ? 44.406  56.115 98.150  1.00 64.08  ? 181  PRO C O   1 
ATOM   5316  C CB  . PRO C  1 181 ? 43.951  58.871 99.881  1.00 66.00  ? 181  PRO C CB  1 
ATOM   5317  C CG  . PRO C  1 181 ? 42.555  58.354 99.947  1.00 64.80  ? 181  PRO C CG  1 
ATOM   5318  C CD  . PRO C  1 181 ? 41.994  58.446 98.550  1.00 61.84  ? 181  PRO C CD  1 
ATOM   5319  N N   . ASN C  1 182 ? 46.330  57.039 98.881  1.00 67.22  ? 182  ASN C N   1 
ATOM   5320  C CA  . ASN C  1 182 ? 47.090  55.785 98.896  1.00 68.56  ? 182  ASN C CA  1 
ATOM   5321  C C   . ASN C  1 182 ? 46.631  54.785 99.955  1.00 70.34  ? 182  ASN C C   1 
ATOM   5322  O O   . ASN C  1 182 ? 46.482  53.596 99.662  1.00 70.20  ? 182  ASN C O   1 
ATOM   5323  C CB  . ASN C  1 182 ? 48.580  56.080 99.081  1.00 70.69  ? 182  ASN C CB  1 
ATOM   5324  C CG  . ASN C  1 182 ? 49.206  56.673 97.838  1.00 69.14  ? 182  ASN C CG  1 
ATOM   5325  O OD1 . ASN C  1 182 ? 49.406  55.971 96.855  1.00 67.98  ? 182  ASN C OD1 1 
ATOM   5326  N ND2 . ASN C  1 182 ? 49.505  57.967 97.869  1.00 69.30  ? 182  ASN C ND2 1 
ATOM   5327  N N   . ASP C  1 183 ? 46.419  55.271 101.178 1.00 72.20  ? 183  ASP C N   1 
ATOM   5328  C CA  . ASP C  1 183 ? 46.026  54.418 102.308 1.00 74.33  ? 183  ASP C CA  1 
ATOM   5329  C C   . ASP C  1 183 ? 45.140  55.161 103.314 1.00 75.01  ? 183  ASP C C   1 
ATOM   5330  O O   . ASP C  1 183 ? 44.932  56.371 103.199 1.00 74.07  ? 183  ASP C O   1 
ATOM   5331  C CB  . ASP C  1 183 ? 47.272  53.843 103.001 1.00 77.60  ? 183  ASP C CB  1 
ATOM   5332  C CG  . ASP C  1 183 ? 48.307  54.910 103.350 1.00 79.19  ? 183  ASP C CG  1 
ATOM   5333  O OD1 . ASP C  1 183 ? 47.929  55.988 103.855 1.00 79.34  ? 183  ASP C OD1 1 
ATOM   5334  O OD2 . ASP C  1 183 ? 49.510  54.660 103.126 1.00 80.52  ? 183  ASP C OD2 1 
ATOM   5335  N N   . ALA C  1 184 ? 44.624  54.423 104.298 1.00 76.83  ? 184  ALA C N   1 
ATOM   5336  C CA  . ALA C  1 184 ? 43.740  54.983 105.331 1.00 77.83  ? 184  ALA C CA  1 
ATOM   5337  C C   . ALA C  1 184 ? 44.406  56.089 106.155 1.00 79.99  ? 184  ALA C C   1 
ATOM   5338  O O   . ALA C  1 184 ? 43.731  57.012 106.618 1.00 79.98  ? 184  ALA C O   1 
ATOM   5339  C CB  . ALA C  1 184 ? 43.237  53.877 106.250 1.00 79.84  ? 184  ALA C CB  1 
ATOM   5340  N N   . ALA C  1 185 ? 45.723  55.989 106.334 1.00 82.04  ? 185  ALA C N   1 
ATOM   5341  C CA  . ALA C  1 185 ? 46.495  57.003 107.056 1.00 84.41  ? 185  ALA C CA  1 
ATOM   5342  C C   . ALA C  1 185 ? 46.564  58.327 106.290 1.00 82.46  ? 185  ALA C C   1 
ATOM   5343  O O   . ALA C  1 185 ? 46.511  59.402 106.891 1.00 83.64  ? 185  ALA C O   1 
ATOM   5344  C CB  . ALA C  1 185 ? 47.897  56.488 107.345 1.00 87.15  ? 185  ALA C CB  1 
ATOM   5345  N N   . GLU C  1 186 ? 46.682  58.245 104.968 1.00 79.70  ? 186  GLU C N   1 
ATOM   5346  C CA  . GLU C  1 186 ? 46.718  59.440 104.123 1.00 77.80  ? 186  GLU C CA  1 
ATOM   5347  C C   . GLU C  1 186 ? 45.344  60.103 104.012 1.00 75.85  ? 186  GLU C C   1 
ATOM   5348  O O   . GLU C  1 186 ? 45.249  61.331 103.953 1.00 75.64  ? 186  GLU C O   1 
ATOM   5349  C CB  . GLU C  1 186 ? 47.252  59.099 102.731 1.00 75.62  ? 186  GLU C CB  1 
ATOM   5350  C CG  . GLU C  1 186 ? 47.450  60.316 101.840 1.00 74.03  ? 186  GLU C CG  1 
ATOM   5351  C CD  . GLU C  1 186 ? 48.409  60.059 100.696 1.00 73.06  ? 186  GLU C CD  1 
ATOM   5352  O OE1 . GLU C  1 186 ? 48.010  59.379 99.726  1.00 70.74  ? 186  GLU C OE1 1 
ATOM   5353  O OE2 . GLU C  1 186 ? 49.559  60.546 100.762 1.00 74.78  ? 186  GLU C OE2 1 
ATOM   5354  N N   . GLN C  1 187 ? 44.289  59.289 103.973 1.00 74.62  ? 187  GLN C N   1 
ATOM   5355  C CA  . GLN C  1 187 ? 42.913  59.794 103.979 1.00 73.14  ? 187  GLN C CA  1 
ATOM   5356  C C   . GLN C  1 187 ? 42.676  60.698 105.188 1.00 75.48  ? 187  GLN C C   1 
ATOM   5357  O O   . GLN C  1 187 ? 42.171  61.816 105.050 1.00 74.74  ? 187  GLN C O   1 
ATOM   5358  C CB  . GLN C  1 187 ? 41.911  58.626 103.979 1.00 72.25  ? 187  GLN C CB  1 
ATOM   5359  C CG  . GLN C  1 187 ? 40.455  59.012 104.232 1.00 71.37  ? 187  GLN C CG  1 
ATOM   5360  C CD  . GLN C  1 187 ? 39.919  60.021 103.225 1.00 68.79  ? 187  GLN C CD  1 
ATOM   5361  O OE1 . GLN C  1 187 ? 40.093  59.858 102.018 1.00 66.58  ? 187  GLN C OE1 1 
ATOM   5362  N NE2 . GLN C  1 187 ? 39.258  61.064 103.718 1.00 69.25  ? 187  GLN C NE2 1 
ATOM   5363  N N   . THR C  1 188 ? 43.053  60.209 106.366 1.00 78.53  ? 188  THR C N   1 
ATOM   5364  C CA  . THR C  1 188 ? 42.903  60.972 107.603 1.00 81.24  ? 188  THR C CA  1 
ATOM   5365  C C   . THR C  1 188 ? 43.845  62.184 107.639 1.00 82.53  ? 188  THR C C   1 
ATOM   5366  O O   . THR C  1 188 ? 43.457  63.266 108.077 1.00 83.32  ? 188  THR C O   1 
ATOM   5367  C CB  . THR C  1 188 ? 43.160  60.099 108.846 1.00 84.49  ? 188  THR C CB  1 
ATOM   5368  O OG1 . THR C  1 188 ? 44.464  59.510 108.758 1.00 85.84  ? 188  THR C OG1 1 
ATOM   5369  C CG2 . THR C  1 188 ? 42.107  58.996 108.968 1.00 83.72  ? 188  THR C CG2 1 
ATOM   5370  N N   . LYS C  1 189 ? 45.076  62.003 107.168 1.00 82.91  ? 189  LYS C N   1 
ATOM   5371  C CA  . LYS C  1 189 ? 46.051  63.095 107.127 1.00 84.27  ? 189  LYS C CA  1 
ATOM   5372  C C   . LYS C  1 189 ? 45.548  64.302 106.328 1.00 82.18  ? 189  LYS C C   1 
ATOM   5373  O O   . LYS C  1 189 ? 45.754  65.445 106.733 1.00 83.78  ? 189  LYS C O   1 
ATOM   5374  C CB  . LYS C  1 189 ? 47.381  62.606 106.545 1.00 84.57  ? 189  LYS C CB  1 
ATOM   5375  C CG  . LYS C  1 189 ? 48.397  63.713 106.300 1.00 85.67  ? 189  LYS C CG  1 
ATOM   5376  C CD  . LYS C  1 189 ? 49.812  63.166 106.181 1.00 87.34  ? 189  LYS C CD  1 
ATOM   5377  C CE  . LYS C  1 189 ? 50.825  64.268 105.900 1.00 88.55  ? 189  LYS C CE  1 
ATOM   5378  N NZ  . LYS C  1 189 ? 51.065  64.454 104.440 1.00 85.66  ? 189  LYS C NZ  1 
ATOM   5379  N N   . LEU C  1 190 ? 44.890  64.038 105.201 1.00 78.85  ? 190  LEU C N   1 
ATOM   5380  C CA  . LEU C  1 190 ? 44.417  65.095 104.306 1.00 76.80  ? 190  LEU C CA  1 
ATOM   5381  C C   . LEU C  1 190 ? 43.060  65.662 104.712 1.00 76.32  ? 190  LEU C C   1 
ATOM   5382  O O   . LEU C  1 190 ? 42.884  66.881 104.778 1.00 76.84  ? 190  LEU C O   1 
ATOM   5383  C CB  . LEU C  1 190 ? 44.321  64.562 102.876 1.00 73.66  ? 190  LEU C CB  1 
ATOM   5384  C CG  . LEU C  1 190 ? 45.637  64.554 102.098 1.00 73.74  ? 190  LEU C CG  1 
ATOM   5385  C CD1 . LEU C  1 190 ? 45.688  63.399 101.108 1.00 71.57  ? 190  LEU C CD1 1 
ATOM   5386  C CD2 . LEU C  1 190 ? 45.828  65.882 101.384 1.00 73.19  ? 190  LEU C CD2 1 
ATOM   5387  N N   . TYR C  1 191 ? 42.103  64.769 104.959 1.00 75.44  ? 191  TYR C N   1 
ATOM   5388  C CA  . TYR C  1 191 ? 40.706  65.153 105.191 1.00 74.68  ? 191  TYR C CA  1 
ATOM   5389  C C   . TYR C  1 191 ? 40.153  64.709 106.552 1.00 76.93  ? 191  TYR C C   1 
ATOM   5390  O O   . TYR C  1 191 ? 39.055  65.115 106.935 1.00 76.98  ? 191  TYR C O   1 
ATOM   5391  C CB  . TYR C  1 191 ? 39.836  64.580 104.070 1.00 71.37  ? 191  TYR C CB  1 
ATOM   5392  C CG  . TYR C  1 191 ? 40.519  64.593 102.716 1.00 69.24  ? 191  TYR C CG  1 
ATOM   5393  C CD1 . TYR C  1 191 ? 40.589  65.762 101.960 1.00 68.29  ? 191  TYR C CD1 1 
ATOM   5394  C CD2 . TYR C  1 191 ? 41.116  63.442 102.202 1.00 68.42  ? 191  TYR C CD2 1 
ATOM   5395  C CE1 . TYR C  1 191 ? 41.218  65.781 100.725 1.00 66.53  ? 191  TYR C CE1 1 
ATOM   5396  C CE2 . TYR C  1 191 ? 41.748  63.453 100.971 1.00 66.67  ? 191  TYR C CE2 1 
ATOM   5397  C CZ  . TYR C  1 191 ? 41.797  64.626 100.238 1.00 65.72  ? 191  TYR C CZ  1 
ATOM   5398  O OH  . TYR C  1 191 ? 42.423  64.646 99.017  1.00 64.16  ? 191  TYR C OH  1 
ATOM   5399  N N   . GLN C  1 192 ? 40.905  63.868 107.262 1.00 78.91  ? 192  GLN C N   1 
ATOM   5400  C CA  . GLN C  1 192 ? 40.554  63.383 108.603 1.00 81.52  ? 192  GLN C CA  1 
ATOM   5401  C C   . GLN C  1 192 ? 39.401  62.385 108.640 1.00 80.32  ? 192  GLN C C   1 
ATOM   5402  O O   . GLN C  1 192 ? 39.534  61.313 109.234 1.00 81.73  ? 192  GLN C O   1 
ATOM   5403  C CB  . GLN C  1 192 ? 40.282  64.541 109.563 1.00 83.88  ? 192  GLN C CB  1 
ATOM   5404  C CG  . GLN C  1 192 ? 40.646  64.195 110.996 1.00 87.69  ? 192  GLN C CG  1 
ATOM   5405  C CD  . GLN C  1 192 ? 40.632  65.400 111.901 1.00 90.42  ? 192  GLN C CD  1 
ATOM   5406  O OE1 . GLN C  1 192 ? 41.658  65.772 112.465 1.00 93.13  ? 192  GLN C OE1 1 
ATOM   5407  N NE2 . GLN C  1 192 ? 39.470  66.027 112.036 1.00 89.91  ? 192  GLN C NE2 1 
ATOM   5408  N N   . ASN C  1 193 ? 38.278  62.733 108.021 1.00 77.96  ? 193  ASN C N   1 
ATOM   5409  C CA  . ASN C  1 193 ? 37.107  61.859 108.004 1.00 76.88  ? 193  ASN C CA  1 
ATOM   5410  C C   . ASN C  1 193 ? 37.439  60.556 107.269 1.00 75.35  ? 193  ASN C C   1 
ATOM   5411  O O   . ASN C  1 193 ? 37.876  60.595 106.118 1.00 73.14  ? 193  ASN C O   1 
ATOM   5412  C CB  . ASN C  1 193 ? 35.912  62.557 107.340 1.00 74.68  ? 193  ASN C CB  1 
ATOM   5413  C CG  . ASN C  1 193 ? 35.677  63.963 107.876 1.00 76.04  ? 193  ASN C CG  1 
ATOM   5414  O OD1 . ASN C  1 193 ? 36.543  64.539 108.533 1.00 78.28  ? 193  ASN C OD1 1 
ATOM   5415  N ND2 . ASN C  1 193 ? 34.507  64.523 107.592 1.00 74.88  ? 193  ASN C ND2 1 
ATOM   5416  N N   . PRO C  1 194 ? 37.245  59.399 107.935 1.00 76.72  ? 194  PRO C N   1 
ATOM   5417  C CA  . PRO C  1 194 ? 37.660  58.124 107.345 1.00 75.85  ? 194  PRO C CA  1 
ATOM   5418  C C   . PRO C  1 194 ? 36.842  57.748 106.111 1.00 72.62  ? 194  PRO C C   1 
ATOM   5419  O O   . PRO C  1 194 ? 37.408  57.307 105.110 1.00 70.98  ? 194  PRO C O   1 
ATOM   5420  C CB  . PRO C  1 194 ? 37.427  57.116 108.478 1.00 78.50  ? 194  PRO C CB  1 
ATOM   5421  C CG  . PRO C  1 194 ? 36.359  57.721 109.321 1.00 79.56  ? 194  PRO C CG  1 
ATOM   5422  C CD  . PRO C  1 194 ? 36.522  59.212 109.209 1.00 79.17  ? 194  PRO C CD  1 
ATOM   5423  N N   . THR C  1 195 ? 35.527  57.931 106.195 1.00 71.90  ? 195  THR C N   1 
ATOM   5424  C CA  . THR C  1 195 ? 34.613  57.613 105.108 1.00 69.18  ? 195  THR C CA  1 
ATOM   5425  C C   . THR C  1 195 ? 34.065  58.923 104.556 1.00 67.54  ? 195  THR C C   1 
ATOM   5426  O O   . THR C  1 195 ? 33.465  59.706 105.295 1.00 68.67  ? 195  THR C O   1 
ATOM   5427  C CB  . THR C  1 195 ? 33.454  56.724 105.604 1.00 69.89  ? 195  THR C CB  1 
ATOM   5428  O OG1 . THR C  1 195 ? 33.969  55.698 106.461 1.00 72.26  ? 195  THR C OG1 1 
ATOM   5429  C CG2 . THR C  1 195 ? 32.721  56.080 104.434 1.00 67.46  ? 195  THR C CG2 1 
ATOM   5430  N N   . THR C  1 196 ? 34.284  59.165 103.265 1.00 65.08  ? 196  THR C N   1 
ATOM   5431  C CA  . THR C  1 196 ? 33.900  60.430 102.640 1.00 63.65  ? 196  THR C CA  1 
ATOM   5432  C C   . THR C  1 196 ? 33.161  60.213 101.327 1.00 61.00  ? 196  THR C C   1 
ATOM   5433  O O   . THR C  1 196 ? 33.203  59.127 100.749 1.00 60.10  ? 196  THR C O   1 
ATOM   5434  C CB  . THR C  1 196 ? 35.128  61.322 102.375 1.00 63.75  ? 196  THR C CB  1 
ATOM   5435  O OG1 . THR C  1 196 ? 36.063  60.620 101.549 1.00 62.70  ? 196  THR C OG1 1 
ATOM   5436  C CG2 . THR C  1 196 ? 35.799  61.713 103.686 1.00 66.62  ? 196  THR C CG2 1 
ATOM   5437  N N   . TYR C  1 197 ? 32.488  61.264 100.867 1.00 60.00  ? 197  TYR C N   1 
ATOM   5438  C CA  . TYR C  1 197 ? 31.716  61.218 99.633  1.00 57.73  ? 197  TYR C CA  1 
ATOM   5439  C C   . TYR C  1 197 ? 31.704  62.574 98.940  1.00 56.80  ? 197  TYR C C   1 
ATOM   5440  O O   . TYR C  1 197 ? 32.090  63.587 99.525  1.00 58.02  ? 197  TYR C O   1 
ATOM   5441  C CB  . TYR C  1 197 ? 30.274  60.805 99.928  1.00 57.89  ? 197  TYR C CB  1 
ATOM   5442  C CG  . TYR C  1 197 ? 29.510  61.840 100.722 1.00 59.14  ? 197  TYR C CG  1 
ATOM   5443  C CD1 . TYR C  1 197 ? 29.547  61.840 102.114 1.00 61.51  ? 197  TYR C CD1 1 
ATOM   5444  C CD2 . TYR C  1 197 ? 28.760  62.827 100.083 1.00 58.17  ? 197  TYR C CD2 1 
ATOM   5445  C CE1 . TYR C  1 197 ? 28.859  62.791 102.848 1.00 62.86  ? 197  TYR C CE1 1 
ATOM   5446  C CE2 . TYR C  1 197 ? 28.066  63.779 100.807 1.00 59.52  ? 197  TYR C CE2 1 
ATOM   5447  C CZ  . TYR C  1 197 ? 28.119  63.757 102.191 1.00 61.85  ? 197  TYR C CZ  1 
ATOM   5448  O OH  . TYR C  1 197 ? 27.436  64.701 102.921 1.00 63.38  ? 197  TYR C OH  1 
ATOM   5449  N N   . ILE C  1 198 ? 31.251  62.573 97.687  1.00 54.84  ? 198  ILE C N   1 
ATOM   5450  C CA  . ILE C  1 198 ? 30.973  63.800 96.942  1.00 54.01  ? 198  ILE C CA  1 
ATOM   5451  C C   . ILE C  1 198 ? 29.684  63.612 96.157  1.00 52.77  ? 198  ILE C C   1 
ATOM   5452  O O   . ILE C  1 198 ? 29.630  62.792 95.238  1.00 51.40  ? 198  ILE C O   1 
ATOM   5453  C CB  . ILE C  1 198 ? 32.094  64.153 95.947  1.00 52.94  ? 198  ILE C CB  1 
ATOM   5454  C CG1 . ILE C  1 198 ? 33.462  64.040 96.625  1.00 54.20  ? 198  ILE C CG1 1 
ATOM   5455  C CG2 . ILE C  1 198 ? 31.869  65.550 95.373  1.00 52.63  ? 198  ILE C CG2 1 
ATOM   5456  C CD1 . ILE C  1 198 ? 34.609  64.516 95.769  1.00 53.54  ? 198  ILE C CD1 1 
ATOM   5457  N N   . SER C  1 199 ? 28.652  64.369 96.517  1.00 53.45  ? 199  SER C N   1 
ATOM   5458  C CA  . SER C  1 199 ? 27.385  64.315 95.801  1.00 52.58  ? 199  SER C CA  1 
ATOM   5459  C C   . SER C  1 199 ? 27.231  65.556 94.930  1.00 51.98  ? 199  SER C C   1 
ATOM   5460  O O   . SER C  1 199 ? 27.400  66.678 95.404  1.00 53.03  ? 199  SER C O   1 
ATOM   5461  C CB  . SER C  1 199 ? 26.213  64.180 96.775  1.00 53.95  ? 199  SER C CB  1 
ATOM   5462  O OG  . SER C  1 199 ? 26.218  65.218 97.732  1.00 55.60  ? 199  SER C OG  1 
ATOM   5463  N N   . VAL C  1 200 ? 26.923  65.338 93.654  1.00 50.49  ? 200  VAL C N   1 
ATOM   5464  C CA  . VAL C  1 200 ? 26.741  66.418 92.688  1.00 49.98  ? 200  VAL C CA  1 
ATOM   5465  C C   . VAL C  1 200 ? 25.365  66.286 92.047  1.00 49.62  ? 200  VAL C C   1 
ATOM   5466  O O   . VAL C  1 200 ? 24.996  65.212 91.569  1.00 48.83  ? 200  VAL C O   1 
ATOM   5467  C CB  . VAL C  1 200 ? 27.813  66.385 91.580  1.00 48.68  ? 200  VAL C CB  1 
ATOM   5468  C CG1 . VAL C  1 200 ? 27.865  67.723 90.852  1.00 48.69  ? 200  VAL C CG1 1 
ATOM   5469  C CG2 . VAL C  1 200 ? 29.178  66.044 92.162  1.00 49.00  ? 200  VAL C CG2 1 
ATOM   5470  N N   . GLY C  1 201 ? 24.611  67.381 92.037  1.00 50.45  ? 201  GLY C N   1 
ATOM   5471  C CA  . GLY C  1 201 ? 23.253  67.374 91.512  1.00 50.49  ? 201  GLY C CA  1 
ATOM   5472  C C   . GLY C  1 201 ? 23.002  68.517 90.551  1.00 50.49  ? 201  GLY C C   1 
ATOM   5473  O O   . GLY C  1 201 ? 23.527  69.615 90.729  1.00 51.17  ? 201  GLY C O   1 
ATOM   5474  N N   . THR C  1 202 ? 22.220  68.236 89.512  1.00 49.91  ? 202  THR C N   1 
ATOM   5475  C CA  . THR C  1 202 ? 21.648  69.264 88.643  1.00 50.31  ? 202  THR C CA  1 
ATOM   5476  C C   . THR C  1 202 ? 20.199  68.851 88.399  1.00 50.76  ? 202  THR C C   1 
ATOM   5477  O O   . THR C  1 202 ? 19.661  68.018 89.136  1.00 51.16  ? 202  THR C O   1 
ATOM   5478  C CB  . THR C  1 202 ? 22.411  69.402 87.301  1.00 49.15  ? 202  THR C CB  1 
ATOM   5479  O OG1 . THR C  1 202 ? 22.109  68.294 86.442  1.00 48.10  ? 202  THR C OG1 1 
ATOM   5480  C CG2 . THR C  1 202 ? 23.917  69.478 87.528  1.00 48.62  ? 202  THR C CG2 1 
ATOM   5481  N N   . SER C  1 203 ? 19.562  69.427 87.385  1.00 50.96  ? 203  SER C N   1 
ATOM   5482  C CA  . SER C  1 203 ? 18.246  68.958 86.965  1.00 51.38  ? 203  SER C CA  1 
ATOM   5483  C C   . SER C  1 203 ? 18.334  67.521 86.458  1.00 50.13  ? 203  SER C C   1 
ATOM   5484  O O   . SER C  1 203 ? 17.407  66.737 86.649  1.00 50.60  ? 203  SER C O   1 
ATOM   5485  C CB  . SER C  1 203 ? 17.669  69.864 85.880  1.00 52.01  ? 203  SER C CB  1 
ATOM   5486  O OG  . SER C  1 203 ? 18.570  69.986 84.797  1.00 50.92  ? 203  SER C OG  1 
ATOM   5487  N N   . THR C  1 204 ? 19.456  67.181 85.828  1.00 48.73  ? 204  THR C N   1 
ATOM   5488  C CA  . THR C  1 204 ? 19.659  65.850 85.262  1.00 47.67  ? 204  THR C CA  1 
ATOM   5489  C C   . THR C  1 204 ? 20.629  65.008 86.085  1.00 47.01  ? 204  THR C C   1 
ATOM   5490  O O   . THR C  1 204 ? 20.383  63.824 86.310  1.00 46.94  ? 204  THR C O   1 
ATOM   5491  C CB  . THR C  1 204 ? 20.180  65.931 83.810  1.00 46.76  ? 204  THR C CB  1 
ATOM   5492  O OG1 . THR C  1 204 ? 21.449  66.595 83.783  1.00 46.16  ? 204  THR C OG1 1 
ATOM   5493  C CG2 . THR C  1 204 ? 19.195  66.686 82.930  1.00 47.62  ? 204  THR C CG2 1 
ATOM   5494  N N   . LEU C  1 205 ? 21.728  65.612 86.531  1.00 46.75  ? 205  LEU C N   1 
ATOM   5495  C CA  . LEU C  1 205 ? 22.788  64.860 87.197  1.00 46.24  ? 205  LEU C CA  1 
ATOM   5496  C C   . LEU C  1 205 ? 22.383  64.394 88.603  1.00 47.22  ? 205  LEU C C   1 
ATOM   5497  O O   . LEU C  1 205 ? 21.819  65.161 89.386  1.00 48.41  ? 205  LEU C O   1 
ATOM   5498  C CB  . LEU C  1 205 ? 24.074  65.691 87.265  1.00 45.97  ? 205  LEU C CB  1 
ATOM   5499  C CG  . LEU C  1 205 ? 25.367  64.949 87.626  1.00 45.41  ? 205  LEU C CG  1 
ATOM   5500  C CD1 . LEU C  1 205 ? 25.611  63.767 86.695  1.00 44.36  ? 205  LEU C CD1 1 
ATOM   5501  C CD2 . LEU C  1 205 ? 26.555  65.903 87.603  1.00 45.41  ? 205  LEU C CD2 1 
ATOM   5502  N N   . ASN C  1 206 ? 22.663  63.123 88.893  1.00 46.95  ? 206  ASN C N   1 
ATOM   5503  C CA  . ASN C  1 206 ? 22.457  62.539 90.218  1.00 47.93  ? 206  ASN C CA  1 
ATOM   5504  C C   . ASN C  1 206 ? 23.643  61.650 90.573  1.00 47.55  ? 206  ASN C C   1 
ATOM   5505  O O   . ASN C  1 206 ? 23.571  60.421 90.492  1.00 47.44  ? 206  ASN C O   1 
ATOM   5506  C CB  . ASN C  1 206 ? 21.155  61.736 90.266  1.00 48.58  ? 206  ASN C CB  1 
ATOM   5507  C CG  . ASN C  1 206 ? 20.842  61.209 91.659  1.00 49.89  ? 206  ASN C CG  1 
ATOM   5508  O OD1 . ASN C  1 206 ? 21.321  61.739 92.662  1.00 50.57  ? 206  ASN C OD1 1 
ATOM   5509  N ND2 . ASN C  1 206 ? 20.026  60.164 91.725  1.00 50.45  ? 206  ASN C ND2 1 
ATOM   5510  N N   . GLN C  1 207 ? 24.728  62.295 90.983  1.00 47.56  ? 207  GLN C N   1 
ATOM   5511  C CA  . GLN C  1 207 ? 26.005  61.630 91.188  1.00 47.29  ? 207  GLN C CA  1 
ATOM   5512  C C   . GLN C  1 207 ? 26.379  61.573 92.668  1.00 48.65  ? 207  GLN C C   1 
ATOM   5513  O O   . GLN C  1 207 ? 26.052  62.477 93.434  1.00 49.63  ? 207  GLN C O   1 
ATOM   5514  C CB  . GLN C  1 207 ? 27.076  62.377 90.396  1.00 46.42  ? 207  GLN C CB  1 
ATOM   5515  C CG  . GLN C  1 207 ? 28.497  61.885 90.594  1.00 46.33  ? 207  GLN C CG  1 
ATOM   5516  C CD  . GLN C  1 207 ? 29.471  62.593 89.673  1.00 45.55  ? 207  GLN C CD  1 
ATOM   5517  O OE1 . GLN C  1 207 ? 30.307  63.376 90.126  1.00 46.11  ? 207  GLN C OE1 1 
ATOM   5518  N NE2 . GLN C  1 207 ? 29.357  62.335 88.371  1.00 44.43  ? 207  GLN C NE2 1 
ATOM   5519  N N   . ARG C  1 208 ? 27.050  60.493 93.060  1.00 48.90  ? 208  ARG C N   1 
ATOM   5520  C CA  . ARG C  1 208 ? 27.652  60.386 94.387  1.00 50.33  ? 208  ARG C CA  1 
ATOM   5521  C C   . ARG C  1 208 ? 28.937  59.565 94.306  1.00 50.19  ? 208  ARG C C   1 
ATOM   5522  O O   . ARG C  1 208 ? 28.896  58.356 94.078  1.00 50.09  ? 208  ARG C O   1 
ATOM   5523  C CB  . ARG C  1 208 ? 26.685  59.756 95.390  1.00 51.69  ? 208  ARG C CB  1 
ATOM   5524  C CG  . ARG C  1 208 ? 27.024  60.101 96.832  1.00 53.49  ? 208  ARG C CG  1 
ATOM   5525  C CD  . ARG C  1 208 ? 26.394  59.131 97.816  1.00 55.00  ? 208  ARG C CD  1 
ATOM   5526  N NE  . ARG C  1 208 ? 26.640  59.536 99.198  1.00 56.95  ? 208  ARG C NE  1 
ATOM   5527  C CZ  . ARG C  1 208 ? 25.984  60.505 99.839  1.00 57.97  ? 208  ARG C CZ  1 
ATOM   5528  N NH1 . ARG C  1 208 ? 25.024  61.199 99.234  1.00 57.24  ? 208  ARG C NH1 1 
ATOM   5529  N NH2 . ARG C  1 208 ? 26.291  60.786 101.103 1.00 59.95  ? 208  ARG C NH2 1 
ATOM   5530  N N   . LEU C  1 209 ? 30.072  60.234 94.490  1.00 50.42  ? 209  LEU C N   1 
ATOM   5531  C CA  . LEU C  1 209 ? 31.382  59.606 94.351  1.00 50.41  ? 209  LEU C CA  1 
ATOM   5532  C C   . LEU C  1 209 ? 31.964  59.281 95.716  1.00 52.30  ? 209  LEU C C   1 
ATOM   5533  O O   . LEU C  1 209 ? 31.823  60.063 96.650  1.00 53.49  ? 209  LEU C O   1 
ATOM   5534  C CB  . LEU C  1 209 ? 32.338  60.546 93.613  1.00 49.65  ? 209  LEU C CB  1 
ATOM   5535  C CG  . LEU C  1 209 ? 31.872  61.082 92.258  1.00 48.04  ? 209  LEU C CG  1 
ATOM   5536  C CD1 . LEU C  1 209 ? 32.862  62.112 91.733  1.00 47.74  ? 209  LEU C CD1 1 
ATOM   5537  C CD2 . LEU C  1 209 ? 31.683  59.946 91.260  1.00 46.97  ? 209  LEU C CD2 1 
ATOM   5538  N N   . VAL C  1 210 ? 32.615  58.125 95.821  1.00 52.79  ? 210  VAL C N   1 
ATOM   5539  C CA  . VAL C  1 210 ? 33.349  57.744 97.028  1.00 54.79  ? 210  VAL C CA  1 
ATOM   5540  C C   . VAL C  1 210 ? 34.795  57.388 96.650  1.00 54.86  ? 210  VAL C C   1 
ATOM   5541  O O   . VAL C  1 210 ? 35.024  56.762 95.611  1.00 53.65  ? 210  VAL C O   1 
ATOM   5542  C CB  . VAL C  1 210 ? 32.671  56.571 97.783  1.00 56.02  ? 210  VAL C CB  1 
ATOM   5543  C CG1 . VAL C  1 210 ? 31.215  56.905 98.080  1.00 56.04  ? 210  VAL C CG1 1 
ATOM   5544  C CG2 . VAL C  1 210 ? 32.770  55.263 97.006  1.00 55.39  ? 210  VAL C CG2 1 
ATOM   5545  N N   . PRO C  1 211 ? 35.777  57.800 97.479  1.00 56.44  ? 211  PRO C N   1 
ATOM   5546  C CA  . PRO C  1 211 ? 37.170  57.451 97.176  1.00 56.79  ? 211  PRO C CA  1 
ATOM   5547  C C   . PRO C  1 211 ? 37.453  55.953 97.276  1.00 57.58  ? 211  PRO C C   1 
ATOM   5548  O O   . PRO C  1 211 ? 37.128  55.319 98.282  1.00 59.22  ? 211  PRO C O   1 
ATOM   5549  C CB  . PRO C  1 211 ? 37.973  58.207 98.244  1.00 58.76  ? 211  PRO C CB  1 
ATOM   5550  C CG  . PRO C  1 211 ? 37.068  59.279 98.732  1.00 58.86  ? 211  PRO C CG  1 
ATOM   5551  C CD  . PRO C  1 211 ? 35.681  58.722 98.626  1.00 58.02  ? 211  PRO C CD  1 
ATOM   5552  N N   . ARG C  1 212 ? 38.040  55.404 96.219  1.00 56.58  ? 212  ARG C N   1 
ATOM   5553  C CA  . ARG C  1 212 ? 38.499  54.020 96.195  1.00 57.50  ? 212  ARG C CA  1 
ATOM   5554  C C   . ARG C  1 212 ? 39.982  53.974 96.565  1.00 59.10  ? 212  ARG C C   1 
ATOM   5555  O O   . ARG C  1 212 ? 40.815  54.568 95.882  1.00 58.41  ? 212  ARG C O   1 
ATOM   5556  C CB  . ARG C  1 212 ? 38.284  53.405 94.806  1.00 55.73  ? 212  ARG C CB  1 
ATOM   5557  C CG  . ARG C  1 212 ? 36.875  53.588 94.259  1.00 54.14  ? 212  ARG C CG  1 
ATOM   5558  C CD  . ARG C  1 212 ? 36.630  52.738 93.021  1.00 52.95  ? 212  ARG C CD  1 
ATOM   5559  N NE  . ARG C  1 212 ? 37.562  53.048 91.938  1.00 51.93  ? 212  ARG C NE  1 
ATOM   5560  C CZ  . ARG C  1 212 ? 37.480  54.108 91.132  1.00 50.41  ? 212  ARG C CZ  1 
ATOM   5561  N NH1 . ARG C  1 212 ? 36.503  55.002 91.266  1.00 49.69  ? 212  ARG C NH1 1 
ATOM   5562  N NH2 . ARG C  1 212 ? 38.391  54.283 90.181  1.00 49.78  ? 212  ARG C NH2 1 
ATOM   5563  N N   . ILE C  1 213 ? 40.302  53.271 97.650  1.00 61.44  ? 213  ILE C N   1 
ATOM   5564  C CA  . ILE C  1 213 ? 41.684  53.150 98.120  1.00 63.42  ? 213  ILE C CA  1 
ATOM   5565  C C   . ILE C  1 213 ? 42.336  51.892 97.538  1.00 63.88  ? 213  ILE C C   1 
ATOM   5566  O O   . ILE C  1 213 ? 41.721  50.824 97.490  1.00 64.03  ? 213  ILE C O   1 
ATOM   5567  C CB  . ILE C  1 213 ? 41.755  53.140 99.668  1.00 66.11  ? 213  ILE C CB  1 
ATOM   5568  C CG1 . ILE C  1 213 ? 41.261  54.484 100.219 1.00 65.93  ? 213  ILE C CG1 1 
ATOM   5569  C CG2 . ILE C  1 213 ? 43.178  52.875 100.150 1.00 68.45  ? 213  ILE C CG2 1 
ATOM   5570  C CD1 . ILE C  1 213 ? 40.989  54.489 101.708 1.00 68.43  ? 213  ILE C CD1 1 
ATOM   5571  N N   . ALA C  1 214 ? 43.578  52.041 97.081  1.00 64.25  ? 214  ALA C N   1 
ATOM   5572  C CA  . ALA C  1 214 ? 44.361  50.926 96.556  1.00 65.04  ? 214  ALA C CA  1 
ATOM   5573  C C   . ALA C  1 214 ? 45.841  51.294 96.520  1.00 66.31  ? 214  ALA C C   1 
ATOM   5574  O O   . ALA C  1 214 ? 46.195  52.474 96.450  1.00 65.78  ? 214  ALA C O   1 
ATOM   5575  C CB  . ALA C  1 214 ? 43.880  50.546 95.161  1.00 62.75  ? 214  ALA C CB  1 
ATOM   5576  N N   . THR C  1 215 ? 46.697  50.279 96.579  1.00 68.22  ? 215  THR C N   1 
ATOM   5577  C CA  . THR C  1 215 ? 48.137  50.472 96.436  1.00 69.58  ? 215  THR C CA  1 
ATOM   5578  C C   . THR C  1 215 ? 48.449  50.499 94.946  1.00 67.63  ? 215  THR C C   1 
ATOM   5579  O O   . THR C  1 215 ? 48.170  49.537 94.231  1.00 67.02  ? 215  THR C O   1 
ATOM   5580  C CB  . THR C  1 215 ? 48.942  49.348 97.118  1.00 72.68  ? 215  THR C CB  1 
ATOM   5581  O OG1 . THR C  1 215 ? 48.382  49.067 98.407  1.00 74.43  ? 215  THR C OG1 1 
ATOM   5582  C CG2 . THR C  1 215 ? 50.405  49.751 97.277  1.00 74.59  ? 215  THR C CG2 1 
ATOM   5583  N N   . ARG C  1 216 ? 49.015  51.605 94.478  1.00 66.85  ? 216  ARG C N   1 
ATOM   5584  C CA  . ARG C  1 216 ? 49.203  51.817 93.049  1.00 64.91  ? 216  ARG C CA  1 
ATOM   5585  C C   . ARG C  1 216 ? 50.653  52.138 92.725  1.00 66.22  ? 216  ARG C C   1 
ATOM   5586  O O   . ARG C  1 216 ? 51.398  52.627 93.576  1.00 68.15  ? 216  ARG C O   1 
ATOM   5587  C CB  . ARG C  1 216 ? 48.299  52.952 92.571  1.00 62.37  ? 216  ARG C CB  1 
ATOM   5588  C CG  . ARG C  1 216 ? 46.817  52.686 92.780  1.00 61.07  ? 216  ARG C CG  1 
ATOM   5589  C CD  . ARG C  1 216 ? 45.986  53.928 92.506  1.00 59.09  ? 216  ARG C CD  1 
ATOM   5590  N NE  . ARG C  1 216 ? 45.905  54.816 93.669  1.00 60.15  ? 216  ARG C NE  1 
ATOM   5591  C CZ  . ARG C  1 216 ? 44.919  54.827 94.572  1.00 60.38  ? 216  ARG C CZ  1 
ATOM   5592  N NH1 . ARG C  1 216 ? 43.890  53.990 94.485  1.00 59.64  ? 216  ARG C NH1 1 
ATOM   5593  N NH2 . ARG C  1 216 ? 44.963  55.689 95.581  1.00 61.55  ? 216  ARG C NH2 1 
ATOM   5594  N N   . SER C  1 217 ? 51.040  51.855 91.485  1.00 65.35  ? 217  SER C N   1 
ATOM   5595  C CA  . SER C  1 217 ? 52.377  52.170 91.002  1.00 66.48  ? 217  SER C CA  1 
ATOM   5596  C C   . SER C  1 217 ? 52.548  53.682 90.903  1.00 65.82  ? 217  SER C C   1 
ATOM   5597  O O   . SER C  1 217 ? 51.582  54.408 90.665  1.00 63.77  ? 217  SER C O   1 
ATOM   5598  C CB  . SER C  1 217 ? 52.615  51.523 89.636  1.00 65.52  ? 217  SER C CB  1 
ATOM   5599  O OG  . SER C  1 217 ? 52.229  50.158 89.649  1.00 66.01  ? 217  SER C OG  1 
ATOM   5600  N N   . LYS C  1 218 ? 53.775  54.151 91.107  1.00 67.85  ? 218  LYS C N   1 
ATOM   5601  C CA  . LYS C  1 218 ? 54.078  55.574 90.989  1.00 67.68  ? 218  LYS C CA  1 
ATOM   5602  C C   . LYS C  1 218 ? 54.023  56.000 89.533  1.00 65.49  ? 218  LYS C C   1 
ATOM   5603  O O   . LYS C  1 218 ? 54.717  55.441 88.686  1.00 65.76  ? 218  LYS C O   1 
ATOM   5604  C CB  . LYS C  1 218 ? 55.457  55.907 91.569  1.00 70.79  ? 218  LYS C CB  1 
ATOM   5605  C CG  . LYS C  1 218 ? 55.423  56.355 93.020  1.00 72.90  ? 218  LYS C CG  1 
ATOM   5606  C CD  . LYS C  1 218 ? 56.730  56.048 93.732  1.00 76.61  ? 218  LYS C CD  1 
ATOM   5607  C CE  . LYS C  1 218 ? 56.671  56.444 95.199  1.00 79.04  ? 218  LYS C CE  1 
ATOM   5608  N NZ  . LYS C  1 218 ? 57.196  55.359 96.072  1.00 82.05  ? 218  LYS C NZ  1 
ATOM   5609  N N   . VAL C  1 219 ? 53.170  56.976 89.255  1.00 63.45  ? 219  VAL C N   1 
ATOM   5610  C CA  . VAL C  1 219 ? 53.132  57.640 87.967  1.00 61.68  ? 219  VAL C CA  1 
ATOM   5611  C C   . VAL C  1 219 ? 53.424  59.109 88.255  1.00 62.17  ? 219  VAL C C   1 
ATOM   5612  O O   . VAL C  1 219 ? 52.793  59.704 89.126  1.00 62.17  ? 219  VAL C O   1 
ATOM   5613  C CB  . VAL C  1 219 ? 51.758  57.451 87.295  1.00 59.06  ? 219  VAL C CB  1 
ATOM   5614  C CG1 . VAL C  1 219 ? 51.645  58.292 86.029  1.00 57.50  ? 219  VAL C CG1 1 
ATOM   5615  C CG2 . VAL C  1 219 ? 51.524  55.977 86.988  1.00 58.84  ? 219  VAL C CG2 1 
ATOM   5616  N N   . ASN C  1 220 ? 54.400  59.680 87.552  1.00 62.79  ? 220  ASN C N   1 
ATOM   5617  C CA  . ASN C  1 220 ? 54.883  61.037 87.844  1.00 63.87  ? 220  ASN C CA  1 
ATOM   5618  C C   . ASN C  1 220 ? 55.234  61.240 89.326  1.00 66.14  ? 220  ASN C C   1 
ATOM   5619  O O   . ASN C  1 220 ? 54.964  62.298 89.900  1.00 66.54  ? 220  ASN C O   1 
ATOM   5620  C CB  . ASN C  1 220 ? 53.862  62.091 87.386  1.00 61.94  ? 220  ASN C CB  1 
ATOM   5621  C CG  . ASN C  1 220 ? 53.878  62.312 85.886  1.00 60.51  ? 220  ASN C CG  1 
ATOM   5622  O OD1 . ASN C  1 220 ? 54.293  61.442 85.115  1.00 60.30  ? 220  ASN C OD1 1 
ATOM   5623  N ND2 . ASN C  1 220 ? 53.418  63.485 85.461  1.00 59.71  ? 220  ASN C ND2 1 
ATOM   5624  N N   . GLY C  1 221 ? 55.831  60.218 89.935  1.00 67.80  ? 221  GLY C N   1 
ATOM   5625  C CA  . GLY C  1 221 ? 56.278  60.289 91.327  1.00 70.38  ? 221  GLY C CA  1 
ATOM   5626  C C   . GLY C  1 221 ? 55.175  60.250 92.373  1.00 69.99  ? 221  GLY C C   1 
ATOM   5627  O O   . GLY C  1 221 ? 55.426  60.535 93.543  1.00 72.13  ? 221  GLY C O   1 
ATOM   5628  N N   . GLN C  1 222 ? 53.959  59.895 91.962  1.00 67.44  ? 222  GLN C N   1 
ATOM   5629  C CA  . GLN C  1 222 ? 52.814  59.848 92.869  1.00 66.97  ? 222  GLN C CA  1 
ATOM   5630  C C   . GLN C  1 222 ? 51.991  58.589 92.631  1.00 65.37  ? 222  GLN C C   1 
ATOM   5631  O O   . GLN C  1 222 ? 51.736  58.217 91.485  1.00 63.50  ? 222  GLN C O   1 
ATOM   5632  C CB  . GLN C  1 222 ? 51.932  61.088 92.683  1.00 65.54  ? 222  GLN C CB  1 
ATOM   5633  C CG  . GLN C  1 222 ? 52.623  62.412 93.001  1.00 67.31  ? 222  GLN C CG  1 
ATOM   5634  C CD  . GLN C  1 222 ? 53.130  62.496 94.435  1.00 70.44  ? 222  GLN C CD  1 
ATOM   5635  O OE1 . GLN C  1 222 ? 52.491  61.996 95.359  1.00 70.94  ? 222  GLN C OE1 1 
ATOM   5636  N NE2 . GLN C  1 222 ? 54.281  63.133 94.624  1.00 72.68  ? 222  GLN C NE2 1 
ATOM   5637  N N   . SER C  1 223 ? 51.586  57.937 93.719  1.00 66.32  ? 223  SER C N   1 
ATOM   5638  C CA  . SER C  1 223 ? 50.735  56.745 93.653  1.00 65.19  ? 223  SER C CA  1 
ATOM   5639  C C   . SER C  1 223 ? 49.259  57.076 93.923  1.00 63.42  ? 223  SER C C   1 
ATOM   5640  O O   . SER C  1 223 ? 48.388  56.218 93.766  1.00 62.32  ? 223  SER C O   1 
ATOM   5641  C CB  . SER C  1 223 ? 51.239  55.677 94.628  1.00 67.71  ? 223  SER C CB  1 
ATOM   5642  O OG  . SER C  1 223 ? 52.404  55.045 94.133  1.00 68.92  ? 223  SER C OG  1 
ATOM   5643  N N   . GLY C  1 224 ? 48.985  58.317 94.328  1.00 63.30  ? 224  GLY C N   1 
ATOM   5644  C CA  . GLY C  1 224 ? 47.615  58.806 94.465  1.00 61.65  ? 224  GLY C CA  1 
ATOM   5645  C C   . GLY C  1 224 ? 47.010  59.117 93.107  1.00 58.90  ? 224  GLY C C   1 
ATOM   5646  O O   . GLY C  1 224 ? 47.735  59.389 92.146  1.00 58.42  ? 224  GLY C O   1 
ATOM   5647  N N   . ARG C  1 225 ? 45.681  59.085 93.030  1.00 57.26  ? 225  ARG C N   1 
ATOM   5648  C CA  . ARG C  1 225 ? 44.969  59.287 91.764  1.00 54.81  ? 225  ARG C CA  1 
ATOM   5649  C C   . ARG C  1 225 ? 43.902  60.377 91.859  1.00 53.82  ? 225  ARG C C   1 
ATOM   5650  O O   . ARG C  1 225 ? 43.292  60.575 92.910  1.00 54.61  ? 225  ARG C O   1 
ATOM   5651  C CB  . ARG C  1 225 ? 44.328  57.975 91.300  1.00 53.79  ? 225  ARG C CB  1 
ATOM   5652  C CG  . ARG C  1 225 ? 45.322  56.875 90.958  1.00 54.59  ? 225  ARG C CG  1 
ATOM   5653  C CD  . ARG C  1 225 ? 46.053  57.154 89.654  1.00 53.73  ? 225  ARG C CD  1 
ATOM   5654  N NE  . ARG C  1 225 ? 47.004  56.093 89.311  1.00 54.65  ? 225  ARG C NE  1 
ATOM   5655  C CZ  . ARG C  1 225 ? 48.269  56.021 89.733  1.00 56.57  ? 225  ARG C CZ  1 
ATOM   5656  N NH1 . ARG C  1 225 ? 48.784  56.948 90.539  1.00 57.86  ? 225  ARG C NH1 1 
ATOM   5657  N NH2 . ARG C  1 225 ? 49.031  55.003 89.345  1.00 57.40  ? 225  ARG C NH2 1 
ATOM   5658  N N   . MET C  1 226 ? 43.699  61.084 90.752  1.00 52.26  ? 226  MET C N   1 
ATOM   5659  C CA  . MET C  1 226 ? 42.646  62.084 90.636  1.00 51.29  ? 226  MET C CA  1 
ATOM   5660  C C   . MET C  1 226 ? 41.742  61.687 89.483  1.00 49.22  ? 226  MET C C   1 
ATOM   5661  O O   . MET C  1 226 ? 42.207  61.519 88.362  1.00 48.44  ? 226  MET C O   1 
ATOM   5662  C CB  . MET C  1 226 ? 43.240  63.466 90.364  1.00 51.77  ? 226  MET C CB  1 
ATOM   5663  C CG  . MET C  1 226 ? 43.918  64.102 91.566  1.00 53.97  ? 226  MET C CG  1 
ATOM   5664  S SD  . MET C  1 226 ? 42.767  64.877 92.717  1.00 54.65  ? 226  MET C SD  1 
ATOM   5665  C CE  . MET C  1 226 ? 43.917  65.619 93.869  1.00 57.52  ? 226  MET C CE  1 
ATOM   5666  N N   . GLU C  1 227 ? 40.452  61.537 89.762  1.00 48.52  ? 227  GLU C N   1 
ATOM   5667  C CA  . GLU C  1 227 ? 39.482  61.162 88.744  1.00 46.82  ? 227  GLU C CA  1 
ATOM   5668  C C   . GLU C  1 227 ? 38.586  62.358 88.464  1.00 46.14  ? 227  GLU C C   1 
ATOM   5669  O O   . GLU C  1 227 ? 37.921  62.861 89.371  1.00 46.75  ? 227  GLU C O   1 
ATOM   5670  C CB  . GLU C  1 227 ? 38.663  59.964 89.218  1.00 46.80  ? 227  GLU C CB  1 
ATOM   5671  C CG  . GLU C  1 227 ? 37.872  59.283 88.117  1.00 45.42  ? 227  GLU C CG  1 
ATOM   5672  C CD  . GLU C  1 227 ? 37.248  57.974 88.563  1.00 45.73  ? 227  GLU C CD  1 
ATOM   5673  O OE1 . GLU C  1 227 ? 37.364  57.620 89.757  1.00 46.98  ? 227  GLU C OE1 1 
ATOM   5674  O OE2 . GLU C  1 227 ? 36.639  57.295 87.710  1.00 44.90  ? 227  GLU C OE2 1 
ATOM   5675  N N   . PHE C  1 228 ? 38.580  62.815 87.214  1.00 45.06  ? 228  PHE C N   1 
ATOM   5676  C CA  . PHE C  1 228 ? 37.897  64.056 86.850  1.00 44.71  ? 228  PHE C CA  1 
ATOM   5677  C C   . PHE C  1 228 ? 36.587  63.807 86.109  1.00 43.51  ? 228  PHE C C   1 
ATOM   5678  O O   . PHE C  1 228 ? 36.507  62.947 85.233  1.00 42.65  ? 228  PHE C O   1 
ATOM   5679  C CB  . PHE C  1 228 ? 38.830  64.943 86.028  1.00 44.81  ? 228  PHE C CB  1 
ATOM   5680  C CG  . PHE C  1 228 ? 39.990  65.472 86.819  1.00 46.27  ? 228  PHE C CG  1 
ATOM   5681  C CD1 . PHE C  1 228 ? 39.845  66.605 87.608  1.00 47.37  ? 228  PHE C CD1 1 
ATOM   5682  C CD2 . PHE C  1 228 ? 41.216  64.820 86.804  1.00 46.77  ? 228  PHE C CD2 1 
ATOM   5683  C CE1 . PHE C  1 228 ? 40.906  67.091 88.352  1.00 48.98  ? 228  PHE C CE1 1 
ATOM   5684  C CE2 . PHE C  1 228 ? 42.281  65.301 87.546  1.00 48.36  ? 228  PHE C CE2 1 
ATOM   5685  C CZ  . PHE C  1 228 ? 42.126  66.437 88.323  1.00 49.48  ? 228  PHE C CZ  1 
ATOM   5686  N N   . PHE C  1 229 ? 35.565  64.569 86.490  1.00 43.68  ? 229  PHE C N   1 
ATOM   5687  C CA  . PHE C  1 229 ? 34.225  64.443 85.930  1.00 42.90  ? 229  PHE C CA  1 
ATOM   5688  C C   . PHE C  1 229 ? 33.752  65.785 85.393  1.00 42.97  ? 229  PHE C C   1 
ATOM   5689  O O   . PHE C  1 229 ? 34.278  66.841 85.765  1.00 43.79  ? 229  PHE C O   1 
ATOM   5690  C CB  . PHE C  1 229 ? 33.250  63.943 86.995  1.00 43.31  ? 229  PHE C CB  1 
ATOM   5691  C CG  . PHE C  1 229 ? 33.554  62.559 87.486  1.00 43.41  ? 229  PHE C CG  1 
ATOM   5692  C CD1 . PHE C  1 229 ? 34.555  62.348 88.428  1.00 44.37  ? 229  PHE C CD1 1 
ATOM   5693  C CD2 . PHE C  1 229 ? 32.845  61.463 87.008  1.00 42.79  ? 229  PHE C CD2 1 
ATOM   5694  C CE1 . PHE C  1 229 ? 34.844  61.072 88.884  1.00 44.70  ? 229  PHE C CE1 1 
ATOM   5695  C CE2 . PHE C  1 229 ? 33.127  60.185 87.463  1.00 43.13  ? 229  PHE C CE2 1 
ATOM   5696  C CZ  . PHE C  1 229 ? 34.128  59.989 88.402  1.00 44.09  ? 229  PHE C CZ  1 
ATOM   5697  N N   . TRP C  1 230 ? 32.749  65.735 84.521  1.00 42.29  ? 230  TRP C N   1 
ATOM   5698  C CA  . TRP C  1 230 ? 32.218  66.943 83.910  1.00 42.50  ? 230  TRP C CA  1 
ATOM   5699  C C   . TRP C  1 230 ? 30.721  66.858 83.651  1.00 42.33  ? 230  TRP C C   1 
ATOM   5700  O O   . TRP C  1 230 ? 30.125  65.784 83.699  1.00 41.88  ? 230  TRP C O   1 
ATOM   5701  C CB  . TRP C  1 230 ? 32.955  67.229 82.604  1.00 42.10  ? 230  TRP C CB  1 
ATOM   5702  C CG  . TRP C  1 230 ? 32.835  66.146 81.579  1.00 41.13  ? 230  TRP C CG  1 
ATOM   5703  C CD1 . TRP C  1 230 ? 33.643  65.053 81.445  1.00 40.69  ? 230  TRP C CD1 1 
ATOM   5704  C CD2 . TRP C  1 230 ? 31.860  66.053 80.536  1.00 40.76  ? 230  TRP C CD2 1 
ATOM   5705  N NE1 . TRP C  1 230 ? 33.230  64.284 80.387  1.00 40.05  ? 230  TRP C NE1 1 
ATOM   5706  C CE2 . TRP C  1 230 ? 32.136  64.873 79.812  1.00 40.09  ? 230  TRP C CE2 1 
ATOM   5707  C CE3 . TRP C  1 230 ? 30.777  66.851 80.144  1.00 41.12  ? 230  TRP C CE3 1 
ATOM   5708  C CZ2 . TRP C  1 230 ? 31.370  64.471 78.712  1.00 39.81  ? 230  TRP C CZ2 1 
ATOM   5709  C CZ3 . TRP C  1 230 ? 30.015  66.450 79.049  1.00 40.84  ? 230  TRP C CZ3 1 
ATOM   5710  C CH2 . TRP C  1 230 ? 30.316  65.270 78.348  1.00 40.19  ? 230  TRP C CH2 1 
ATOM   5711  N N   . THR C  1 231 ? 30.126  68.015 83.391  1.00 42.92  ? 231  THR C N   1 
ATOM   5712  C CA  . THR C  1 231 ? 28.745  68.093 82.941  1.00 42.99  ? 231  THR C CA  1 
ATOM   5713  C C   . THR C  1 231 ? 28.551  69.365 82.130  1.00 43.63  ? 231  THR C C   1 
ATOM   5714  O O   . THR C  1 231 ? 29.392  70.266 82.162  1.00 44.17  ? 231  THR C O   1 
ATOM   5715  C CB  . THR C  1 231 ? 27.759  68.088 84.125  1.00 43.68  ? 231  THR C CB  1 
ATOM   5716  O OG1 . THR C  1 231 ? 26.423  67.923 83.636  1.00 43.74  ? 231  THR C OG1 1 
ATOM   5717  C CG2 . THR C  1 231 ? 27.850  69.386 84.929  1.00 44.91  ? 231  THR C CG2 1 
ATOM   5718  N N   . ILE C  1 232 ? 27.452  69.422 81.388  1.00 43.78  ? 232  ILE C N   1 
ATOM   5719  C CA  . ILE C  1 232 ? 27.020  70.657 80.747  1.00 44.77  ? 232  ILE C CA  1 
ATOM   5720  C C   . ILE C  1 232 ? 25.852  71.174 81.567  1.00 45.85  ? 232  ILE C C   1 
ATOM   5721  O O   . ILE C  1 232 ? 24.811  70.528 81.656  1.00 45.77  ? 232  ILE C O   1 
ATOM   5722  C CB  . ILE C  1 232 ? 26.644  70.449 79.259  1.00 44.51  ? 232  ILE C CB  1 
ATOM   5723  C CG1 . ILE C  1 232 ? 27.832  70.793 78.353  1.00 44.32  ? 232  ILE C CG1 1 
ATOM   5724  C CG2 . ILE C  1 232 ? 25.482  71.344 78.839  1.00 45.73  ? 232  ILE C CG2 1 
ATOM   5725  C CD1 . ILE C  1 232 ? 29.120  70.082 78.696  1.00 43.42  ? 232  ILE C CD1 1 
ATOM   5726  N N   . LEU C  1 233 ? 26.048  72.331 82.188  1.00 47.06  ? 233  LEU C N   1 
ATOM   5727  C CA  . LEU C  1 233 ? 25.016  72.956 82.999  1.00 48.38  ? 233  LEU C CA  1 
ATOM   5728  C C   . LEU C  1 233 ? 24.219  73.916 82.123  1.00 49.54  ? 233  LEU C C   1 
ATOM   5729  O O   . LEU C  1 233 ? 24.751  74.918 81.639  1.00 50.30  ? 233  LEU C O   1 
ATOM   5730  C CB  . LEU C  1 233 ? 25.655  73.692 84.181  1.00 49.33  ? 233  LEU C CB  1 
ATOM   5731  C CG  . LEU C  1 233 ? 24.723  74.305 85.228  1.00 50.83  ? 233  LEU C CG  1 
ATOM   5732  C CD1 . LEU C  1 233 ? 23.854  73.246 85.894  1.00 50.39  ? 233  LEU C CD1 1 
ATOM   5733  C CD2 . LEU C  1 233 ? 25.549  75.057 86.260  1.00 51.92  ? 233  LEU C CD2 1 
ATOM   5734  N N   . LYS C  1 234 ? 22.945  73.597 81.914  1.00 62.75  ? 234  LYS C N   1 
ATOM   5735  C CA  . LYS C  1 234 ? 22.077  74.403 81.059  1.00 64.44  ? 234  LYS C CA  1 
ATOM   5736  C C   . LYS C  1 234 ? 21.707  75.725 81.734  1.00 65.95  ? 234  LYS C C   1 
ATOM   5737  O O   . LYS C  1 234 ? 21.857  75.859 82.951  1.00 65.70  ? 234  LYS C O   1 
ATOM   5738  C CB  . LYS C  1 234 ? 20.820  73.608 80.691  1.00 65.05  ? 234  LYS C CB  1 
ATOM   5739  C CG  . LYS C  1 234 ? 21.090  72.518 79.665  1.00 64.32  ? 234  LYS C CG  1 
ATOM   5740  C CD  . LYS C  1 234 ? 19.892  71.605 79.470  1.00 65.11  ? 234  LYS C CD  1 
ATOM   5741  C CE  . LYS C  1 234 ? 20.053  70.764 78.213  1.00 65.06  ? 234  LYS C CE  1 
ATOM   5742  N NZ  . LYS C  1 234 ? 18.901  69.848 77.994  1.00 66.19  ? 234  LYS C NZ  1 
ATOM   5743  N N   . PRO C  1 235 ? 21.235  76.714 80.948  1.00 67.77  ? 235  PRO C N   1 
ATOM   5744  C CA  . PRO C  1 235 ? 20.917  78.014 81.541  1.00 69.47  ? 235  PRO C CA  1 
ATOM   5745  C C   . PRO C  1 235 ? 19.751  77.929 82.516  1.00 70.19  ? 235  PRO C C   1 
ATOM   5746  O O   . PRO C  1 235 ? 18.850  77.108 82.326  1.00 70.18  ? 235  PRO C O   1 
ATOM   5747  C CB  . PRO C  1 235 ? 20.536  78.884 80.333  1.00 71.42  ? 235  PRO C CB  1 
ATOM   5748  C CG  . PRO C  1 235 ? 20.945  78.123 79.124  1.00 70.57  ? 235  PRO C CG  1 
ATOM   5749  C CD  . PRO C  1 235 ? 20.913  76.680 79.511  1.00 68.64  ? 235  PRO C CD  1 
ATOM   5750  N N   . ASN C  1 236 ? 19.786  78.762 83.555  1.00 71.00  ? 236  ASN C N   1 
ATOM   5751  C CA  . ASN C  1 236 ? 18.711  78.838 84.545  1.00 71.89  ? 236  ASN C CA  1 
ATOM   5752  C C   . ASN C  1 236 ? 18.666  77.605 85.460  1.00 70.23  ? 236  ASN C C   1 
ATOM   5753  O O   . ASN C  1 236 ? 17.731  77.450 86.248  1.00 70.87  ? 236  ASN C O   1 
ATOM   5754  C CB  . ASN C  1 236 ? 17.351  79.039 83.843  1.00 73.76  ? 236  ASN C CB  1 
ATOM   5755  C CG  . ASN C  1 236 ? 16.552  80.202 84.406  1.00 76.05  ? 236  ASN C CG  1 
ATOM   5756  O OD1 . ASN C  1 236 ? 16.769  80.647 85.531  1.00 76.36  ? 236  ASN C OD1 1 
ATOM   5757  N ND2 . ASN C  1 236 ? 15.615  80.705 83.610  1.00 78.13  ? 236  ASN C ND2 1 
ATOM   5758  N N   . ASP C  1 237 ? 19.684  76.747 85.362  1.00 68.36  ? 237  ASP C N   1 
ATOM   5759  C CA  . ASP C  1 237 ? 19.784  75.533 86.169  1.00 66.94  ? 237  ASP C CA  1 
ATOM   5760  C C   . ASP C  1 237 ? 20.976  75.671 87.111  1.00 66.18  ? 237  ASP C C   1 
ATOM   5761  O O   . ASP C  1 237 ? 21.953  76.356 86.796  1.00 66.21  ? 237  ASP C O   1 
ATOM   5762  C CB  . ASP C  1 237 ? 19.956  74.302 85.269  1.00 65.75  ? 237  ASP C CB  1 
ATOM   5763  C CG  . ASP C  1 237 ? 19.860  72.981 86.036  1.00 64.78  ? 237  ASP C CG  1 
ATOM   5764  O OD1 . ASP C  1 237 ? 19.129  72.916 87.049  1.00 65.35  ? 237  ASP C OD1 1 
ATOM   5765  O OD2 . ASP C  1 237 ? 20.517  72.002 85.616  1.00 63.61  ? 237  ASP C OD2 1 
ATOM   5766  N N   . ALA C  1 238 ? 20.888  75.011 88.263  1.00 65.74  ? 238  ALA C N   1 
ATOM   5767  C CA  . ALA C  1 238 ? 21.911  75.109 89.294  1.00 65.47  ? 238  ALA C CA  1 
ATOM   5768  C C   . ALA C  1 238 ? 22.621  73.777 89.506  1.00 64.05  ? 238  ALA C C   1 
ATOM   5769  O O   . ALA C  1 238 ? 22.017  72.712 89.351  1.00 63.53  ? 238  ALA C O   1 
ATOM   5770  C CB  . ALA C  1 238 ? 21.286  75.584 90.597  1.00 66.63  ? 238  ALA C CB  1 
ATOM   5771  N N   . ILE C  1 239 ? 23.904  73.845 89.858  1.00 63.68  ? 239  ILE C N   1 
ATOM   5772  C CA  . ILE C  1 239 ? 24.666  72.658 90.256  1.00 62.73  ? 239  ILE C CA  1 
ATOM   5773  C C   . ILE C  1 239 ? 24.919  72.686 91.770  1.00 63.55  ? 239  ILE C C   1 
ATOM   5774  O O   . ILE C  1 239 ? 25.260  73.729 92.326  1.00 64.63  ? 239  ILE C O   1 
ATOM   5775  C CB  . ILE C  1 239 ? 25.989  72.513 89.461  1.00 61.86  ? 239  ILE C CB  1 
ATOM   5776  C CG1 . ILE C  1 239 ? 26.630  71.149 89.737  1.00 61.04  ? 239  ILE C CG1 1 
ATOM   5777  C CG2 . ILE C  1 239 ? 26.970  73.640 89.773  1.00 62.70  ? 239  ILE C CG2 1 
ATOM   5778  C CD1 . ILE C  1 239 ? 27.581  70.691 88.652  1.00 59.99  ? 239  ILE C CD1 1 
ATOM   5779  N N   . ASN C  1 240 ? 24.736  71.538 92.425  1.00 63.31  ? 240  ASN C N   1 
ATOM   5780  C CA  . ASN C  1 240 ? 24.859  71.431 93.880  1.00 64.30  ? 240  ASN C CA  1 
ATOM   5781  C C   . ASN C  1 240 ? 25.927  70.427 94.293  1.00 64.06  ? 240  ASN C C   1 
ATOM   5782  O O   . ASN C  1 240 ? 25.850  69.254 93.934  1.00 63.30  ? 240  ASN C O   1 
ATOM   5783  C CB  . ASN C  1 240 ? 23.531  70.997 94.494  1.00 64.80  ? 240  ASN C CB  1 
ATOM   5784  C CG  . ASN C  1 240 ? 22.407  71.976 94.219  1.00 65.35  ? 240  ASN C CG  1 
ATOM   5785  O OD1 . ASN C  1 240 ? 22.550  73.179 94.438  1.00 66.22  ? 240  ASN C OD1 1 
ATOM   5786  N ND2 . ASN C  1 240 ? 21.273  71.463 93.743  1.00 65.14  ? 240  ASN C ND2 1 
ATOM   5787  N N   . PHE C  1 241 ? 26.907  70.893 95.064  1.00 64.99  ? 241  PHE C N   1 
ATOM   5788  C CA  . PHE C  1 241 ? 27.973  70.041 95.583  1.00 65.26  ? 241  PHE C CA  1 
ATOM   5789  C C   . PHE C  1 241 ? 27.826  69.836 97.085  1.00 66.84  ? 241  PHE C C   1 
ATOM   5790  O O   . PHE C  1 241 ? 27.559  70.786 97.818  1.00 68.05  ? 241  PHE C O   1 
ATOM   5791  C CB  . PHE C  1 241 ? 29.334  70.670 95.296  1.00 65.52  ? 241  PHE C CB  1 
ATOM   5792  C CG  . PHE C  1 241 ? 29.709  70.658 93.847  1.00 64.04  ? 241  PHE C CG  1 
ATOM   5793  C CD1 . PHE C  1 241 ? 30.302  69.537 93.284  1.00 63.08  ? 241  PHE C CD1 1 
ATOM   5794  C CD2 . PHE C  1 241 ? 29.467  71.762 93.043  1.00 63.80  ? 241  PHE C CD2 1 
ATOM   5795  C CE1 . PHE C  1 241 ? 30.652  69.517 91.947  1.00 61.81  ? 241  PHE C CE1 1 
ATOM   5796  C CE2 . PHE C  1 241 ? 29.815  71.750 91.703  1.00 62.63  ? 241  PHE C CE2 1 
ATOM   5797  C CZ  . PHE C  1 241 ? 30.407  70.624 91.153  1.00 61.57  ? 241  PHE C CZ  1 
ATOM   5798  N N   . GLU C  1 242 ? 27.989  68.594 97.533  1.00 67.02  ? 242  GLU C N   1 
ATOM   5799  C CA  . GLU C  1 242 ? 28.114  68.290 98.956  1.00 68.83  ? 242  GLU C CA  1 
ATOM   5800  C C   . GLU C  1 242 ? 29.221  67.256 99.159  1.00 69.34  ? 242  GLU C C   1 
ATOM   5801  O O   . GLU C  1 242 ? 29.203  66.195 98.531  1.00 68.39  ? 242  GLU C O   1 
ATOM   5802  C CB  . GLU C  1 242 ? 26.789  67.782 99.535  1.00 69.15  ? 242  GLU C CB  1 
ATOM   5803  C CG  . GLU C  1 242 ? 26.805  67.555 101.044 1.00 71.26  ? 242  GLU C CG  1 
ATOM   5804  C CD  . GLU C  1 242 ? 25.506  66.964 101.568 1.00 71.63  ? 242  GLU C CD  1 
ATOM   5805  O OE1 . GLU C  1 242 ? 24.431  67.550 101.321 1.00 71.07  ? 242  GLU C OE1 1 
ATOM   5806  O OE2 . GLU C  1 242 ? 25.556  65.913 102.238 1.00 72.68  ? 242  GLU C OE2 1 
ATOM   5807  N N   . SER C  1 243 ? 30.184  67.572 100.026 1.00 71.08  ? 243  SER C N   1 
ATOM   5808  C CA  . SER C  1 243 ? 31.281  66.651 100.320 1.00 72.05  ? 243  SER C CA  1 
ATOM   5809  C C   . SER C  1 243 ? 31.889  66.865 101.704 1.00 74.79  ? 243  SER C C   1 
ATOM   5810  O O   . SER C  1 243 ? 32.039  68.001 102.158 1.00 75.85  ? 243  SER C O   1 
ATOM   5811  C CB  . SER C  1 243 ? 32.381  66.781 99.267  1.00 71.03  ? 243  SER C CB  1 
ATOM   5812  O OG  . SER C  1 243 ? 33.470  65.921 99.560  1.00 72.19  ? 243  SER C OG  1 
ATOM   5813  N N   . ASN C  1 244 ? 32.241  65.757 102.355 1.00 76.19  ? 244  ASN C N   1 
ATOM   5814  C CA  . ASN C  1 244 ? 32.971  65.774 103.628 1.00 79.18  ? 244  ASN C CA  1 
ATOM   5815  C C   . ASN C  1 244 ? 34.439  65.356 103.462 1.00 80.21  ? 244  ASN C C   1 
ATOM   5816  O O   . ASN C  1 244 ? 35.144  65.150 104.452 1.00 82.98  ? 244  ASN C O   1 
ATOM   5817  C CB  . ASN C  1 244 ? 32.279  64.868 104.658 1.00 80.72  ? 244  ASN C CB  1 
ATOM   5818  C CG  . ASN C  1 244 ? 32.158  63.429 104.188 1.00 80.01  ? 244  ASN C CG  1 
ATOM   5819  O OD1 . ASN C  1 244 ? 32.104  63.162 102.986 1.00 77.72  ? 244  ASN C OD1 1 
ATOM   5820  N ND2 . ASN C  1 244 ? 32.108  62.494 105.130 1.00 82.19  ? 244  ASN C ND2 1 
ATOM   5821  N N   . GLY C  1 245 ? 34.893  65.227 102.214 1.00 78.17  ? 245  GLY C N   1 
ATOM   5822  C CA  . GLY C  1 245 ? 36.297  64.930 101.935 1.00 79.00  ? 245  GLY C CA  1 
ATOM   5823  C C   . GLY C  1 245 ? 36.614  64.580 100.490 1.00 76.50  ? 245  GLY C C   1 
ATOM   5824  O O   . GLY C  1 245 ? 35.733  64.186 99.722  1.00 74.30  ? 245  GLY C O   1 
ATOM   5825  N N   . ASN C  1 246 ? 37.892  64.732 100.140 1.00 77.10  ? 246  ASN C N   1 
ATOM   5826  C CA  . ASN C  1 246 ? 38.457  64.316 98.844  1.00 75.22  ? 246  ASN C CA  1 
ATOM   5827  C C   . ASN C  1 246 ? 37.924  65.075 97.619  1.00 72.42  ? 246  ASN C C   1 
ATOM   5828  O O   . ASN C  1 246 ? 38.007  64.579 96.496  1.00 70.55  ? 246  ASN C O   1 
ATOM   5829  C CB  . ASN C  1 246 ? 38.302  62.799 98.642  1.00 74.91  ? 246  ASN C CB  1 
ATOM   5830  C CG  . ASN C  1 246 ? 38.799  61.992 99.834  1.00 77.95  ? 246  ASN C CG  1 
ATOM   5831  O OD1 . ASN C  1 246 ? 38.168  61.978 100.891 1.00 79.41  ? 246  ASN C OD1 1 
ATOM   5832  N ND2 . ASN C  1 246 ? 39.926  61.305 99.665  1.00 79.07  ? 246  ASN C ND2 1 
ATOM   5833  N N   . PHE C  1 247 ? 37.424  66.290 97.837  1.00 72.42  ? 247  PHE C N   1 
ATOM   5834  C CA  . PHE C  1 247 ? 36.747  67.062 96.791  1.00 70.17  ? 247  PHE C CA  1 
ATOM   5835  C C   . PHE C  1 247 ? 37.681  68.037 96.085  1.00 70.08  ? 247  PHE C C   1 
ATOM   5836  O O   . PHE C  1 247 ? 38.374  68.825 96.728  1.00 72.07  ? 247  PHE C O   1 
ATOM   5837  C CB  . PHE C  1 247 ? 35.557  67.814 97.400  1.00 70.36  ? 247  PHE C CB  1 
ATOM   5838  C CG  . PHE C  1 247 ? 34.776  68.652 96.417  1.00 68.50  ? 247  PHE C CG  1 
ATOM   5839  C CD1 . PHE C  1 247 ? 34.301  68.113 95.228  1.00 66.31  ? 247  PHE C CD1 1 
ATOM   5840  C CD2 . PHE C  1 247 ? 34.477  69.979 96.708  1.00 69.26  ? 247  PHE C CD2 1 
ATOM   5841  C CE1 . PHE C  1 247 ? 33.570  68.881 94.340  1.00 64.97  ? 247  PHE C CE1 1 
ATOM   5842  C CE2 . PHE C  1 247 ? 33.743  70.752 95.823  1.00 67.89  ? 247  PHE C CE2 1 
ATOM   5843  C CZ  . PHE C  1 247 ? 33.290  70.202 94.638  1.00 65.78  ? 247  PHE C CZ  1 
ATOM   5844  N N   . ILE C  1 248 ? 37.693  67.965 94.757  1.00 67.99  ? 248  ILE C N   1 
ATOM   5845  C CA  . ILE C  1 248 ? 38.412  68.926 93.932  1.00 67.72  ? 248  ILE C CA  1 
ATOM   5846  C C   . ILE C  1 248 ? 37.374  69.888 93.365  1.00 66.55  ? 248  ILE C C   1 
ATOM   5847  O O   . ILE C  1 248 ? 36.662  69.567 92.414  1.00 64.61  ? 248  ILE C O   1 
ATOM   5848  C CB  . ILE C  1 248 ? 39.207  68.244 92.799  1.00 66.45  ? 248  ILE C CB  1 
ATOM   5849  C CG1 . ILE C  1 248 ? 39.927  66.986 93.301  1.00 67.41  ? 248  ILE C CG1 1 
ATOM   5850  C CG2 . ILE C  1 248 ? 40.214  69.214 92.204  1.00 66.91  ? 248  ILE C CG2 1 
ATOM   5851  C CD1 . ILE C  1 248 ? 40.822  67.197 94.508  1.00 70.26  ? 248  ILE C CD1 1 
ATOM   5852  N N   . ALA C  1 249 ? 37.281  71.063 93.978  1.00 68.04  ? 249  ALA C N   1 
ATOM   5853  C CA  . ALA C  1 249 ? 36.224  72.019 93.662  1.00 67.47  ? 249  ALA C CA  1 
ATOM   5854  C C   . ALA C  1 249 ? 36.520  72.783 92.376  1.00 66.62  ? 249  ALA C C   1 
ATOM   5855  O O   . ALA C  1 249 ? 37.679  73.031 92.059  1.00 67.27  ? 249  ALA C O   1 
ATOM   5856  C CB  . ALA C  1 249 ? 36.039  72.994 94.817  1.00 69.66  ? 249  ALA C CB  1 
ATOM   5857  N N   . PRO C  1 250 ? 35.467  73.157 91.631  1.00 65.40  ? 250  PRO C N   1 
ATOM   5858  C CA  . PRO C  1 250 ? 35.653  74.010 90.463  1.00 65.02  ? 250  PRO C CA  1 
ATOM   5859  C C   . PRO C  1 250 ? 35.871  75.476 90.825  1.00 67.06  ? 250  PRO C C   1 
ATOM   5860  O O   . PRO C  1 250 ? 34.999  76.089 91.427  1.00 67.90  ? 250  PRO C O   1 
ATOM   5861  C CB  . PRO C  1 250 ? 34.337  73.852 89.697  1.00 63.47  ? 250  PRO C CB  1 
ATOM   5862  C CG  . PRO C  1 250 ? 33.333  73.466 90.719  1.00 63.68  ? 250  PRO C CG  1 
ATOM   5863  C CD  . PRO C  1 250 ? 34.075  72.686 91.761  1.00 64.42  ? 250  PRO C CD  1 
ATOM   5864  N N   . GLU C  1 251 ? 37.029  76.025 90.467  1.00 68.06  ? 251  GLU C N   1 
ATOM   5865  C CA  . GLU C  1 251 ? 37.236  77.473 90.501  1.00 70.07  ? 251  GLU C CA  1 
ATOM   5866  C C   . GLU C  1 251 ? 36.585  78.086 89.264  1.00 69.19  ? 251  GLU C C   1 
ATOM   5867  O O   . GLU C  1 251 ? 35.708  78.949 89.373  1.00 69.99  ? 251  GLU C O   1 
ATOM   5868  C CB  . GLU C  1 251 ? 38.734  77.822 90.548  1.00 71.76  ? 251  GLU C CB  1 
ATOM   5869  C CG  . GLU C  1 251 ? 39.195  78.519 91.820  1.00 74.71  ? 251  GLU C CG  1 
ATOM   5870  C CD  . GLU C  1 251 ? 39.411  80.011 91.634  1.00 76.97  ? 251  GLU C CD  1 
ATOM   5871  O OE1 . GLU C  1 251 ? 40.326  80.382 90.872  1.00 77.53  ? 251  GLU C OE1 1 
ATOM   5872  O OE2 . GLU C  1 251 ? 38.681  80.815 92.253  1.00 78.37  ? 251  GLU C OE2 1 
ATOM   5873  N N   . TYR C  1 252 ? 37.016  77.613 88.094  1.00 67.70  ? 252  TYR C N   1 
ATOM   5874  C CA  . TYR C  1 252 ? 36.542  78.120 86.806  1.00 67.07  ? 252  TYR C CA  1 
ATOM   5875  C C   . TYR C  1 252 ? 35.755  77.074 86.015  1.00 64.71  ? 252  TYR C C   1 
ATOM   5876  O O   . TYR C  1 252 ? 36.047  75.873 86.070  1.00 63.37  ? 252  TYR C O   1 
ATOM   5877  C CB  . TYR C  1 252 ? 37.723  78.598 85.960  1.00 67.72  ? 252  TYR C CB  1 
ATOM   5878  C CG  . TYR C  1 252 ? 38.492  79.743 86.575  1.00 70.45  ? 252  TYR C CG  1 
ATOM   5879  C CD1 . TYR C  1 252 ? 38.059  81.056 86.426  1.00 72.26  ? 252  TYR C CD1 1 
ATOM   5880  C CD2 . TYR C  1 252 ? 39.651  79.514 87.310  1.00 71.56  ? 252  TYR C CD2 1 
ATOM   5881  C CE1 . TYR C  1 252 ? 38.758  82.110 86.992  1.00 75.09  ? 252  TYR C CE1 1 
ATOM   5882  C CE2 . TYR C  1 252 ? 40.359  80.559 87.878  1.00 74.42  ? 252  TYR C CE2 1 
ATOM   5883  C CZ  . TYR C  1 252 ? 39.908  81.858 87.719  1.00 76.18  ? 252  TYR C CZ  1 
ATOM   5884  O OH  . TYR C  1 252 ? 40.608  82.902 88.282  1.00 79.31  ? 252  TYR C OH  1 
ATOM   5885  N N   . ALA C  1 253 ? 34.752  77.552 85.283  1.00 64.54  ? 253  ALA C N   1 
ATOM   5886  C CA  . ALA C  1 253 ? 33.974  76.729 84.364  1.00 62.77  ? 253  ALA C CA  1 
ATOM   5887  C C   . ALA C  1 253 ? 33.917  77.436 83.013  1.00 63.09  ? 253  ALA C C   1 
ATOM   5888  O O   . ALA C  1 253 ? 33.722  78.652 82.950  1.00 64.77  ? 253  ALA C O   1 
ATOM   5889  C CB  . ALA C  1 253 ? 32.573  76.508 84.912  1.00 62.58  ? 253  ALA C CB  1 
ATOM   5890  N N   . TYR C  1 254 ? 34.089  76.672 81.938  1.00 61.71  ? 254  TYR C N   1 
ATOM   5891  C CA  . TYR C  1 254 ? 34.116  77.237 80.591  1.00 62.08  ? 254  TYR C CA  1 
ATOM   5892  C C   . TYR C  1 254 ? 32.713  77.534 80.076  1.00 62.46  ? 254  TYR C C   1 
ATOM   5893  O O   . TYR C  1 254 ? 31.772  76.783 80.325  1.00 61.64  ? 254  TYR C O   1 
ATOM   5894  C CB  . TYR C  1 254 ? 34.838  76.296 79.628  1.00 60.63  ? 254  TYR C CB  1 
ATOM   5895  C CG  . TYR C  1 254 ? 36.330  76.236 79.849  1.00 60.71  ? 254  TYR C CG  1 
ATOM   5896  C CD1 . TYR C  1 254 ? 37.180  77.147 79.230  1.00 61.90  ? 254  TYR C CD1 1 
ATOM   5897  C CD2 . TYR C  1 254 ? 36.895  75.271 80.674  1.00 59.88  ? 254  TYR C CD2 1 
ATOM   5898  C CE1 . TYR C  1 254 ? 38.550  77.098 79.422  1.00 62.20  ? 254  TYR C CE1 1 
ATOM   5899  C CE2 . TYR C  1 254 ? 38.263  75.215 80.875  1.00 60.24  ? 254  TYR C CE2 1 
ATOM   5900  C CZ  . TYR C  1 254 ? 39.090  76.131 80.247  1.00 61.38  ? 254  TYR C CZ  1 
ATOM   5901  O OH  . TYR C  1 254 ? 40.454  76.085 80.443  1.00 61.96  ? 254  TYR C OH  1 
ATOM   5902  N N   . LYS C  1 255 ? 32.594  78.634 79.344  1.00 63.99  ? 255  LYS C N   1 
ATOM   5903  C CA  . LYS C  1 255 ? 31.323  79.096 78.801  1.00 64.93  ? 255  LYS C CA  1 
ATOM   5904  C C   . LYS C  1 255 ? 31.363  78.879 77.298  1.00 64.72  ? 255  LYS C C   1 
ATOM   5905  O O   . LYS C  1 255 ? 32.336  79.257 76.649  1.00 65.11  ? 255  LYS C O   1 
ATOM   5906  C CB  . LYS C  1 255 ? 31.149  80.582 79.118  1.00 67.35  ? 255  LYS C CB  1 
ATOM   5907  C CG  . LYS C  1 255 ? 29.751  81.011 79.526  1.00 68.42  ? 255  LYS C CG  1 
ATOM   5908  C CD  . LYS C  1 255 ? 29.796  82.296 80.356  1.00 70.61  ? 255  LYS C CD  1 
ATOM   5909  C CE  . LYS C  1 255 ? 29.456  83.540 79.559  1.00 73.11  ? 255  LYS C CE  1 
ATOM   5910  N NZ  . LYS C  1 255 ? 29.095  84.668 80.460  1.00 75.36  ? 255  LYS C NZ  1 
ATOM   5911  N N   . ILE C  1 256 ? 30.312  78.277 76.749  1.00 64.31  ? 256  ILE C N   1 
ATOM   5912  C CA  . ILE C  1 256 ? 30.286  77.921 75.330  1.00 64.20  ? 256  ILE C CA  1 
ATOM   5913  C C   . ILE C  1 256 ? 29.566  79.023 74.556  1.00 66.52  ? 256  ILE C C   1 
ATOM   5914  O O   . ILE C  1 256 ? 28.349  78.986 74.387  1.00 67.30  ? 256  ILE C O   1 
ATOM   5915  C CB  . ILE C  1 256 ? 29.599  76.556 75.073  1.00 62.82  ? 256  ILE C CB  1 
ATOM   5916  C CG1 . ILE C  1 256 ? 29.804  75.599 76.257  1.00 61.14  ? 256  ILE C CG1 1 
ATOM   5917  C CG2 . ILE C  1 256 ? 30.122  75.951 73.778  1.00 62.26  ? 256  ILE C CG2 1 
ATOM   5918  C CD1 . ILE C  1 256 ? 29.296  74.191 76.021  1.00 59.94  ? 256  ILE C CD1 1 
ATOM   5919  N N   . VAL C  1 257 ? 30.323  80.015 74.100  1.00 67.87  ? 257  VAL C N   1 
ATOM   5920  C CA  . VAL C  1 257 ? 29.728  81.173 73.424  1.00 70.53  ? 257  VAL C CA  1 
ATOM   5921  C C   . VAL C  1 257 ? 29.384  80.883 71.957  1.00 71.11  ? 257  VAL C C   1 
ATOM   5922  O O   . VAL C  1 257 ? 28.343  81.335 71.462  1.00 73.03  ? 257  VAL C O   1 
ATOM   5923  C CB  . VAL C  1 257 ? 30.603  82.449 73.545  1.00 72.33  ? 257  VAL C CB  1 
ATOM   5924  C CG1 . VAL C  1 257 ? 30.662  82.914 74.993  1.00 72.55  ? 257  VAL C CG1 1 
ATOM   5925  C CG2 . VAL C  1 257 ? 32.008  82.239 72.994  1.00 71.53  ? 257  VAL C CG2 1 
ATOM   5926  N N   . LYS C  1 258 ? 30.246  80.130 71.273  1.00 69.65  ? 258  LYS C N   1 
ATOM   5927  C CA  . LYS C  1 258 ? 30.020  79.769 69.868  1.00 70.20  ? 258  LYS C CA  1 
ATOM   5928  C C   . LYS C  1 258 ? 29.998  78.264 69.628  1.00 67.98  ? 258  LYS C C   1 
ATOM   5929  O O   . LYS C  1 258 ? 30.911  77.547 70.041  1.00 65.91  ? 258  LYS C O   1 
ATOM   5930  C CB  . LYS C  1 258 ? 31.080  80.405 68.959  1.00 71.21  ? 258  LYS C CB  1 
ATOM   5931  C CG  . LYS C  1 258 ? 30.542  81.521 68.074  1.00 74.40  ? 258  LYS C CG  1 
ATOM   5932  C CD  . LYS C  1 258 ? 31.020  81.391 66.634  1.00 75.12  ? 258  LYS C CD  1 
ATOM   5933  C CE  . LYS C  1 258 ? 32.500  81.702 66.478  1.00 74.73  ? 258  LYS C CE  1 
ATOM   5934  N NZ  . LYS C  1 258 ? 32.786  82.210 65.106  1.00 76.83  ? 258  LYS C NZ  1 
ATOM   5935  N N   . LYS C  1 259 ? 28.945  77.804 68.952  1.00 68.72  ? 259  LYS C N   1 
ATOM   5936  C CA  . LYS C  1 259 ? 28.843  76.428 68.476  1.00 67.29  ? 259  LYS C CA  1 
ATOM   5937  C C   . LYS C  1 259 ? 28.910  76.425 66.955  1.00 68.63  ? 259  LYS C C   1 
ATOM   5938  O O   . LYS C  1 259 ? 28.021  76.961 66.292  1.00 71.01  ? 259  LYS C O   1 
ATOM   5939  C CB  . LYS C  1 259 ? 27.525  75.794 68.928  1.00 67.39  ? 259  LYS C CB  1 
ATOM   5940  C CG  . LYS C  1 259 ? 27.465  75.469 70.409  1.00 65.79  ? 259  LYS C CG  1 
ATOM   5941  C CD  . LYS C  1 259 ? 26.075  75.012 70.825  1.00 66.34  ? 259  LYS C CD  1 
ATOM   5942  C CE  . LYS C  1 259 ? 26.017  74.736 72.320  1.00 64.93  ? 259  LYS C CE  1 
ATOM   5943  N NZ  . LYS C  1 259 ? 24.636  74.444 72.794  1.00 65.72  ? 259  LYS C NZ  1 
ATOM   5944  N N   . GLY C  1 260 ? 29.963  75.828 66.406  1.00 67.29  ? 260  GLY C N   1 
ATOM   5945  C CA  . GLY C  1 260 ? 30.126  75.737 64.955  1.00 68.48  ? 260  GLY C CA  1 
ATOM   5946  C C   . GLY C  1 260 ? 30.799  74.452 64.517  1.00 66.61  ? 260  GLY C C   1 
ATOM   5947  O O   . GLY C  1 260 ? 31.036  73.554 65.324  1.00 64.51  ? 260  GLY C O   1 
ATOM   5948  N N   . ASP C  1 261 ? 31.108  74.367 63.228  1.00 67.58  ? 261  ASP C N   1 
ATOM   5949  C CA  . ASP C  1 261 ? 31.844  73.229 62.696  1.00 66.07  ? 261  ASP C CA  1 
ATOM   5950  C C   . ASP C  1 261 ? 33.310  73.344 63.078  1.00 64.31  ? 261  ASP C C   1 
ATOM   5951  O O   . ASP C  1 261 ? 33.962  74.345 62.787  1.00 65.22  ? 261  ASP C O   1 
ATOM   5952  C CB  . ASP C  1 261 ? 31.697  73.135 61.173  1.00 67.93  ? 261  ASP C CB  1 
ATOM   5953  C CG  . ASP C  1 261 ? 30.358  72.560 60.750  1.00 69.47  ? 261  ASP C CG  1 
ATOM   5954  O OD1 . ASP C  1 261 ? 29.639  72.018 61.620  1.00 68.71  ? 261  ASP C OD1 1 
ATOM   5955  O OD2 . ASP C  1 261 ? 30.027  72.642 59.545  1.00 71.66  ? 261  ASP C OD2 1 
ATOM   5956  N N   . SER C  1 262 ? 33.810  72.313 63.747  1.00 62.07  ? 262  SER C N   1 
ATOM   5957  C CA  . SER C  1 262 ? 35.200  72.251 64.170  1.00 60.49  ? 262  SER C CA  1 
ATOM   5958  C C   . SER C  1 262 ? 35.632  70.789 64.177  1.00 58.74  ? 262  SER C C   1 
ATOM   5959  O O   . SER C  1 262 ? 34.816  69.894 63.940  1.00 58.83  ? 262  SER C O   1 
ATOM   5960  C CB  . SER C  1 262 ? 35.358  72.875 65.560  1.00 59.92  ? 262  SER C CB  1 
ATOM   5961  O OG  . SER C  1 262 ? 36.668  72.698 66.074  1.00 58.57  ? 262  SER C OG  1 
ATOM   5962  N N   . THR C  1 263 ? 36.913  70.547 64.434  1.00 57.42  ? 263  THR C N   1 
ATOM   5963  C CA  . THR C  1 263 ? 37.431  69.186 64.490  1.00 55.92  ? 263  THR C CA  1 
ATOM   5964  C C   . THR C  1 263 ? 38.732  69.139 65.280  1.00 54.68  ? 263  THR C C   1 
ATOM   5965  O O   . THR C  1 263 ? 39.508  70.097 65.268  1.00 55.11  ? 263  THR C O   1 
ATOM   5966  C CB  . THR C  1 263 ? 37.646  68.607 63.072  1.00 56.38  ? 263  THR C CB  1 
ATOM   5967  O OG1 . THR C  1 263 ? 37.653  67.178 63.132  1.00 55.40  ? 263  THR C OG1 1 
ATOM   5968  C CG2 . THR C  1 263 ? 38.954  69.089 62.449  1.00 56.38  ? 263  THR C CG2 1 
ATOM   5969  N N   . ILE C  1 264 ? 38.955  68.028 65.976  1.00 53.43  ? 264  ILE C N   1 
ATOM   5970  C CA  . ILE C  1 264 ? 40.224  67.794 66.647  1.00 52.51  ? 264  ILE C CA  1 
ATOM   5971  C C   . ILE C  1 264 ? 41.098  66.968 65.715  1.00 52.13  ? 264  ILE C C   1 
ATOM   5972  O O   . ILE C  1 264 ? 40.871  65.775 65.515  1.00 51.68  ? 264  ILE C O   1 
ATOM   5973  C CB  . ILE C  1 264 ? 40.053  67.101 68.008  1.00 51.67  ? 264  ILE C CB  1 
ATOM   5974  C CG1 . ILE C  1 264 ? 39.184  67.970 68.920  1.00 52.16  ? 264  ILE C CG1 1 
ATOM   5975  C CG2 . ILE C  1 264 ? 41.413  66.874 68.658  1.00 51.08  ? 264  ILE C CG2 1 
ATOM   5976  C CD1 . ILE C  1 264 ? 38.620  67.236 70.114  1.00 51.62  ? 264  ILE C CD1 1 
ATOM   5977  N N   . MET C  1 265 ? 42.092  67.639 65.145  1.00 47.38  ? 265  MET C N   1 
ATOM   5978  C CA  . MET C  1 265 ? 42.992  67.066 64.162  1.00 45.81  ? 265  MET C CA  1 
ATOM   5979  C C   . MET C  1 265 ? 44.222  66.510 64.870  1.00 46.31  ? 265  MET C C   1 
ATOM   5980  O O   . MET C  1 265 ? 44.788  67.160 65.749  1.00 47.82  ? 265  MET C O   1 
ATOM   5981  C CB  . MET C  1 265 ? 43.394  68.167 63.187  1.00 45.92  ? 265  MET C CB  1 
ATOM   5982  C CG  . MET C  1 265 ? 44.104  67.709 61.933  1.00 44.45  ? 265  MET C CG  1 
ATOM   5983  S SD  . MET C  1 265 ? 44.359  69.111 60.827  1.00 45.20  ? 265  MET C SD  1 
ATOM   5984  C CE  . MET C  1 265 ? 42.690  69.425 60.247  1.00 44.82  ? 265  MET C CE  1 
ATOM   5985  N N   . LYS C  1 266 ? 44.624  65.302 64.494  1.00 45.49  ? 266  LYS C N   1 
ATOM   5986  C CA  . LYS C  1 266 ? 45.791  64.661 65.080  1.00 46.51  ? 266  LYS C CA  1 
ATOM   5987  C C   . LYS C  1 266 ? 46.990  64.865 64.167  1.00 46.71  ? 266  LYS C C   1 
ATOM   5988  O O   . LYS C  1 266 ? 47.016  64.360 63.044  1.00 45.58  ? 266  LYS C O   1 
ATOM   5989  C CB  . LYS C  1 266 ? 45.535  63.168 65.301  1.00 46.46  ? 266  LYS C CB  1 
ATOM   5990  C CG  . LYS C  1 266 ? 44.624  62.860 66.481  1.00 47.34  ? 266  LYS C CG  1 
ATOM   5991  C CD  . LYS C  1 266 ? 45.299  63.186 67.802  1.00 49.01  ? 266  LYS C CD  1 
ATOM   5992  C CE  . LYS C  1 266 ? 44.580  62.553 68.978  1.00 50.22  ? 266  LYS C CE  1 
ATOM   5993  N NZ  . LYS C  1 266 ? 45.349  62.719 70.247  1.00 51.93  ? 266  LYS C NZ  1 
ATOM   5994  N N   . SER C  1 267 ? 47.981  65.607 64.655  1.00 48.57  ? 267  SER C N   1 
ATOM   5995  C CA  . SER C  1 267 ? 49.156  65.943 63.859  1.00 49.65  ? 267  SER C CA  1 
ATOM   5996  C C   . SER C  1 267 ? 50.352  66.322 64.729  1.00 52.56  ? 267  SER C C   1 
ATOM   5997  O O   . SER C  1 267 ? 50.200  66.955 65.781  1.00 53.66  ? 267  SER C O   1 
ATOM   5998  C CB  . SER C  1 267 ? 48.826  67.099 62.913  1.00 49.21  ? 267  SER C CB  1 
ATOM   5999  O OG  . SER C  1 267 ? 49.952  67.464 62.131  1.00 50.67  ? 267  SER C OG  1 
ATOM   6000  N N   . GLU C  1 268 ? 51.541  65.929 64.276  1.00 54.23  ? 268  GLU C N   1 
ATOM   6001  C CA  . GLU C  1 268 ? 52.792  66.287 64.948  1.00 57.70  ? 268  GLU C CA  1 
ATOM   6002  C C   . GLU C  1 268 ? 53.318  67.626 64.437  1.00 59.59  ? 268  GLU C C   1 
ATOM   6003  O O   . GLU C  1 268 ? 54.253  68.182 65.010  1.00 62.94  ? 268  GLU C O   1 
ATOM   6004  C CB  . GLU C  1 268 ? 53.856  65.203 64.732  1.00 59.58  ? 268  GLU C CB  1 
ATOM   6005  C CG  . GLU C  1 268 ? 53.402  63.782 65.046  1.00 58.42  ? 268  GLU C CG  1 
ATOM   6006  C CD  . GLU C  1 268 ? 52.890  63.622 66.465  1.00 58.43  ? 268  GLU C CD  1 
ATOM   6007  O OE1 . GLU C  1 268 ? 53.617  64.005 67.411  1.00 60.96  ? 268  GLU C OE1 1 
ATOM   6008  O OE2 . GLU C  1 268 ? 51.760  63.105 66.629  1.00 56.20  ? 268  GLU C OE2 1 
ATOM   6009  N N   . LEU C  1 269 ? 52.721  68.138 63.361  1.00 57.92  ? 269  LEU C N   1 
ATOM   6010  C CA  . LEU C  1 269 ? 53.167  69.388 62.744  1.00 60.04  ? 269  LEU C CA  1 
ATOM   6011  C C   . LEU C  1 269 ? 52.827  70.595 63.605  1.00 61.61  ? 269  LEU C C   1 
ATOM   6012  O O   . LEU C  1 269 ? 51.912  70.547 64.430  1.00 60.11  ? 269  LEU C O   1 
ATOM   6013  C CB  . LEU C  1 269 ? 52.555  69.556 61.348  1.00 57.89  ? 269  LEU C CB  1 
ATOM   6014  C CG  . LEU C  1 269 ? 53.106  68.619 60.269  1.00 57.31  ? 269  LEU C CG  1 
ATOM   6015  C CD1 . LEU C  1 269 ? 52.208  68.620 59.045  1.00 54.45  ? 269  LEU C CD1 1 
ATOM   6016  C CD2 . LEU C  1 269 ? 54.524  69.006 59.881  1.00 61.30  ? 269  LEU C CD2 1 
ATOM   6017  N N   . GLU C  1 270 ? 53.570  71.678 63.389  1.00 65.16  ? 270  GLU C N   1 
ATOM   6018  C CA  . GLU C  1 270 ? 53.426  72.898 64.191  1.00 67.75  ? 270  GLU C CA  1 
ATOM   6019  C C   . GLU C  1 270 ? 52.576  73.931 63.425  1.00 67.57  ? 270  GLU C C   1 
ATOM   6020  O O   . GLU C  1 270 ? 51.392  73.682 63.197  1.00 64.37  ? 270  GLU C O   1 
ATOM   6021  C CB  . GLU C  1 270 ? 54.797  73.431 64.679  1.00 72.77  ? 270  GLU C CB  1 
ATOM   6022  C CG  . GLU C  1 270 ? 55.978  73.205 63.735  1.00 75.14  ? 270  GLU C CG  1 
ATOM   6023  C CD  . GLU C  1 270 ? 57.292  73.772 64.258  1.00 80.90  ? 270  GLU C CD  1 
ATOM   6024  O OE1 . GLU C  1 270 ? 57.315  74.354 65.365  1.00 82.97  ? 270  GLU C OE1 1 
ATOM   6025  O OE2 . GLU C  1 270 ? 58.316  73.629 63.555  1.00 83.75  ? 270  GLU C OE2 1 
ATOM   6026  N N   . TYR C  1 271 ? 53.153  75.060 63.017  1.00 71.45  ? 271  TYR C N   1 
ATOM   6027  C CA  . TYR C  1 271 ? 52.376  76.153 62.432  1.00 72.29  ? 271  TYR C CA  1 
ATOM   6028  C C   . TYR C  1 271 ? 53.137  76.806 61.277  1.00 75.34  ? 271  TYR C C   1 
ATOM   6029  O O   . TYR C  1 271 ? 54.259  77.286 61.456  1.00 79.75  ? 271  TYR C O   1 
ATOM   6030  C CB  . TYR C  1 271 ? 52.055  77.191 63.514  1.00 75.29  ? 271  TYR C CB  1 
ATOM   6031  C CG  . TYR C  1 271 ? 51.135  78.309 63.068  1.00 76.71  ? 271  TYR C CG  1 
ATOM   6032  C CD1 . TYR C  1 271 ? 49.833  78.042 62.652  1.00 73.27  ? 271  TYR C CD1 1 
ATOM   6033  C CD2 . TYR C  1 271 ? 51.562  79.635 63.078  1.00 82.13  ? 271  TYR C CD2 1 
ATOM   6034  C CE1 . TYR C  1 271 ? 48.987  79.062 62.249  1.00 75.17  ? 271  TYR C CE1 1 
ATOM   6035  C CE2 . TYR C  1 271 ? 50.722  80.661 62.680  1.00 84.10  ? 271  TYR C CE2 1 
ATOM   6036  C CZ  . TYR C  1 271 ? 49.437  80.371 62.265  1.00 80.60  ? 271  TYR C CZ  1 
ATOM   6037  O OH  . TYR C  1 271 ? 48.608  81.396 61.870  1.00 83.17  ? 271  TYR C OH  1 
ATOM   6038  N N   . GLY C  1 272 ? 52.521  76.823 60.097  1.00 73.35  ? 272  GLY C N   1 
ATOM   6039  C CA  . GLY C  1 272 ? 53.152  77.384 58.900  1.00 76.05  ? 272  GLY C CA  1 
ATOM   6040  C C   . GLY C  1 272 ? 53.000  78.888 58.732  1.00 80.62  ? 272  GLY C C   1 
ATOM   6041  O O   . GLY C  1 272 ? 53.682  79.490 57.896  1.00 84.18  ? 272  GLY C O   1 
ATOM   6042  N N   . ASN C  1 273 ? 52.113  79.494 59.523  1.00 81.05  ? 273  ASN C N   1 
ATOM   6043  C CA  . ASN C  1 273 ? 51.786  80.923 59.409  1.00 85.67  ? 273  ASN C CA  1 
ATOM   6044  C C   . ASN C  1 273 ? 51.245  81.272 58.016  1.00 85.33  ? 273  ASN C C   1 
ATOM   6045  O O   . ASN C  1 273 ? 51.524  82.334 57.459  1.00 90.11  ? 273  ASN C O   1 
ATOM   6046  C CB  . ASN C  1 273 ? 52.996  81.788 59.786  1.00 92.09  ? 273  ASN C CB  1 
ATOM   6047  C CG  . ASN C  1 273 ? 52.598  83.051 60.530  1.00 96.83  ? 273  ASN C CG  1 
ATOM   6048  O OD1 . ASN C  1 273 ? 53.086  83.315 61.628  1.00 99.62  ? 273  ASN C OD1 1 
ATOM   6049  N ND2 . ASN C  1 273 ? 51.693  83.828 59.943  1.00 98.07  ? 273  ASN C ND2 1 
ATOM   6050  N N   . CYS C  1 274 ? 50.447  80.350 57.487  1.00 79.92  ? 274  CYS C N   1 
ATOM   6051  C CA  . CYS C  1 274 ? 49.858  80.443 56.157  1.00 78.66  ? 274  CYS C CA  1 
ATOM   6052  C C   . CYS C  1 274 ? 48.342  80.546 56.301  1.00 76.67  ? 274  CYS C C   1 
ATOM   6053  O O   . CYS C  1 274 ? 47.815  80.540 57.416  1.00 76.45  ? 274  CYS C O   1 
ATOM   6054  C CB  . CYS C  1 274 ? 50.222  79.184 55.356  1.00 74.32  ? 274  CYS C CB  1 
ATOM   6055  S SG  . CYS C  1 274 ? 50.234  77.694 56.382  1.00 69.68  ? 274  CYS C SG  1 
ATOM   6056  N N   . ASN C  1 275 ? 47.648  80.642 55.171  1.00 75.60  ? 275  ASN C N   1 
ATOM   6057  C CA  . ASN C  1 275 ? 46.189  80.624 55.143  1.00 73.88  ? 275  ASN C CA  1 
ATOM   6058  C C   . ASN C  1 275 ? 45.698  79.624 54.097  1.00 69.14  ? 275  ASN C C   1 
ATOM   6059  O O   . ASN C  1 275 ? 46.359  79.410 53.080  1.00 68.53  ? 275  ASN C O   1 
ATOM   6060  C CB  . ASN C  1 275 ? 45.652  82.025 54.835  1.00 79.01  ? 275  ASN C CB  1 
ATOM   6061  C CG  . ASN C  1 275 ? 44.141  82.114 54.960  1.00 78.50  ? 275  ASN C CG  1 
ATOM   6062  O OD1 . ASN C  1 275 ? 43.574  81.753 55.986  1.00 77.27  ? 275  ASN C OD1 1 
ATOM   6063  N ND2 . ASN C  1 275 ? 43.483  82.598 53.915  1.00 79.88  ? 275  ASN C ND2 1 
ATOM   6064  N N   . THR C  1 276 ? 44.547  79.006 54.349  1.00 66.16  ? 276  THR C N   1 
ATOM   6065  C CA  . THR C  1 276 ? 43.971  78.054 53.399  1.00 62.06  ? 276  THR C CA  1 
ATOM   6066  C C   . THR C  1 276 ? 42.449  77.997 53.492  1.00 61.50  ? 276  THR C C   1 
ATOM   6067  O O   . THR C  1 276 ? 41.846  78.593 54.383  1.00 64.03  ? 276  THR C O   1 
ATOM   6068  C CB  . THR C  1 276 ? 44.554  76.637 53.598  1.00 57.86  ? 276  THR C CB  1 
ATOM   6069  O OG1 . THR C  1 276 ? 44.160  75.793 52.508  1.00 54.58  ? 276  THR C OG1 1 
ATOM   6070  C CG2 . THR C  1 276 ? 44.091  76.013 54.920  1.00 56.44  ? 276  THR C CG2 1 
ATOM   6071  N N   . LYS C  1 277 ? 41.845  77.287 52.544  1.00 58.64  ? 277  LYS C N   1 
ATOM   6072  C CA  . LYS C  1 277 ? 40.411  77.016 52.542  1.00 58.06  ? 277  LYS C CA  1 
ATOM   6073  C C   . LYS C  1 277 ? 40.090  75.528 52.734  1.00 53.78  ? 277  LYS C C   1 
ATOM   6074  O O   . LYS C  1 277 ? 38.922  75.146 52.851  1.00 53.46  ? 277  LYS C O   1 
ATOM   6075  C CB  . LYS C  1 277 ? 39.805  77.528 51.231  1.00 59.31  ? 277  LYS C CB  1 
ATOM   6076  C CG  . LYS C  1 277 ? 39.522  79.038 51.277  1.00 64.78  ? 277  LYS C CG  1 
ATOM   6077  C CD  . LYS C  1 277 ? 38.037  79.390 51.356  1.00 67.23  ? 277  LYS C CD  1 
ATOM   6078  C CE  . LYS C  1 277 ? 37.291  78.940 50.109  1.00 65.65  ? 277  LYS C CE  1 
ATOM   6079  N NZ  . LYS C  1 277 ? 35.834  78.790 50.369  1.00 67.06  ? 277  LYS C NZ  1 
ATOM   6080  N N   . CYS C  1 278 ? 41.133  74.704 52.769  1.00 51.16  ? 278  CYS C N   1 
ATOM   6081  C CA  . CYS C  1 278 ? 40.999  73.270 52.965  1.00 47.69  ? 278  CYS C CA  1 
ATOM   6082  C C   . CYS C  1 278 ? 42.241  72.777 53.684  1.00 46.89  ? 278  CYS C C   1 
ATOM   6083  O O   . CYS C  1 278 ? 43.357  72.953 53.185  1.00 47.19  ? 278  CYS C O   1 
ATOM   6084  C CB  . CYS C  1 278 ? 40.875  72.564 51.618  1.00 45.31  ? 278  CYS C CB  1 
ATOM   6085  S SG  . CYS C  1 278 ? 40.858  70.758 51.723  1.00 41.75  ? 278  CYS C SG  1 
ATOM   6086  N N   . GLN C  1 279 ? 42.055  72.161 54.848  1.00 46.31  ? 279  GLN C N   1 
ATOM   6087  C CA  . GLN C  1 279 ? 43.184  71.750 55.675  1.00 46.13  ? 279  GLN C CA  1 
ATOM   6088  C C   . GLN C  1 279 ? 43.187  70.252 55.941  1.00 43.64  ? 279  GLN C C   1 
ATOM   6089  O O   . GLN C  1 279 ? 42.140  69.655 56.166  1.00 42.75  ? 279  GLN C O   1 
ATOM   6090  C CB  . GLN C  1 279 ? 43.159  72.505 57.003  1.00 48.55  ? 279  GLN C CB  1 
ATOM   6091  C CG  . GLN C  1 279 ? 44.362  72.237 57.895  1.00 48.97  ? 279  GLN C CG  1 
ATOM   6092  C CD  . GLN C  1 279 ? 45.631  72.883 57.376  1.00 50.76  ? 279  GLN C CD  1 
ATOM   6093  O OE1 . GLN C  1 279 ? 45.672  74.091 57.161  1.00 53.47  ? 279  GLN C OE1 1 
ATOM   6094  N NE2 . GLN C  1 279 ? 46.677  72.086 57.183  1.00 49.87  ? 279  GLN C NE2 1 
ATOM   6095  N N   . THR C  1 280 ? 44.383  69.666 55.921  1.00 43.20  ? 280  THR C N   1 
ATOM   6096  C CA  . THR C  1 280 ? 44.594  68.278 56.317  1.00 41.79  ? 280  THR C CA  1 
ATOM   6097  C C   . THR C  1 280 ? 45.677  68.206 57.406  1.00 43.26  ? 280  THR C C   1 
ATOM   6098  O O   . THR C  1 280 ? 46.441  69.158 57.590  1.00 45.21  ? 280  THR C O   1 
ATOM   6099  C CB  . THR C  1 280 ? 45.025  67.396 55.120  1.00 40.26  ? 280  THR C CB  1 
ATOM   6100  O OG1 . THR C  1 280 ? 46.447  67.449 54.945  1.00 41.38  ? 280  THR C OG1 1 
ATOM   6101  C CG2 . THR C  1 280 ? 44.338  67.841 53.835  1.00 39.48  ? 280  THR C CG2 1 
ATOM   6102  N N   . PRO C  1 281 ? 45.741  67.072 58.134  1.00 42.80  ? 281  PRO C N   1 
ATOM   6103  C CA  . PRO C  1 281 ? 46.837  66.819 59.092  1.00 44.35  ? 281  PRO C CA  1 
ATOM   6104  C C   . PRO C  1 281 ? 48.237  66.733 58.455  1.00 45.59  ? 281  PRO C C   1 
ATOM   6105  O O   . PRO C  1 281 ? 49.240  66.855 59.165  1.00 47.64  ? 281  PRO C O   1 
ATOM   6106  C CB  . PRO C  1 281 ? 46.469  65.472 59.734  1.00 43.56  ? 281  PRO C CB  1 
ATOM   6107  C CG  . PRO C  1 281 ? 45.097  65.125 59.278  1.00 41.97  ? 281  PRO C CG  1 
ATOM   6108  C CD  . PRO C  1 281 ? 44.624  66.120 58.268  1.00 41.43  ? 281  PRO C CD  1 
ATOM   6109  N N   . MET C  1 282 ? 48.291  66.503 57.141  1.00 44.74  ? 282  MET C N   1 
ATOM   6110  C CA  . MET C  1 282 ? 49.545  66.474 56.372  1.00 46.28  ? 282  MET C CA  1 
ATOM   6111  C C   . MET C  1 282 ? 49.956  67.876 55.932  1.00 48.02  ? 282  MET C C   1 
ATOM   6112  O O   . MET C  1 282 ? 51.140  68.165 55.757  1.00 50.58  ? 282  MET C O   1 
ATOM   6113  C CB  . MET C  1 282 ? 49.367  65.628 55.110  1.00 44.81  ? 282  MET C CB  1 
ATOM   6114  C CG  . MET C  1 282 ? 48.844  64.218 55.347  1.00 43.59  ? 282  MET C CG  1 
ATOM   6115  S SD  . MET C  1 282 ? 50.180  63.029 55.536  1.00 46.08  ? 282  MET C SD  1 
ATOM   6116  C CE  . MET C  1 282 ? 50.696  62.871 53.824  1.00 46.03  ? 282  MET C CE  1 
ATOM   6117  N N   . GLY C  1 283 ? 48.961  68.735 55.730  1.00 47.19  ? 283  GLY C N   1 
ATOM   6118  C CA  . GLY C  1 283 ? 49.174  70.078 55.204  1.00 49.15  ? 283  GLY C CA  1 
ATOM   6119  C C   . GLY C  1 283 ? 47.905  70.627 54.575  1.00 47.78  ? 283  GLY C C   1 
ATOM   6120  O O   . GLY C  1 283 ? 46.863  69.972 54.592  1.00 45.41  ? 283  GLY C O   1 
ATOM   6121  N N   . ALA C  1 284 ? 47.995  71.826 54.009  1.00 49.83  ? 284  ALA C N   1 
ATOM   6122  C CA  . ALA C  1 284 ? 46.834  72.500 53.430  1.00 49.47  ? 284  ALA C CA  1 
ATOM   6123  C C   . ALA C  1 284 ? 46.716  72.243 51.927  1.00 48.06  ? 284  ALA C C   1 
ATOM   6124  O O   . ALA C  1 284 ? 47.696  71.883 51.266  1.00 48.23  ? 284  ALA C O   1 
ATOM   6125  C CB  . ALA C  1 284 ? 46.914  73.992 53.702  1.00 53.17  ? 284  ALA C CB  1 
ATOM   6126  N N   . ILE C  1 285 ? 45.509  72.445 51.400  1.00 47.04  ? 285  ILE C N   1 
ATOM   6127  C CA  . ILE C  1 285 ? 45.203  72.197 49.987  1.00 45.60  ? 285  ILE C CA  1 
ATOM   6128  C C   . ILE C  1 285 ? 44.683  73.462 49.295  1.00 47.82  ? 285  ILE C C   1 
ATOM   6129  O O   . ILE C  1 285 ? 43.820  74.170 49.821  1.00 49.28  ? 285  ILE C O   1 
ATOM   6130  C CB  . ILE C  1 285 ? 44.190  71.031 49.830  1.00 42.44  ? 285  ILE C CB  1 
ATOM   6131  C CG1 . ILE C  1 285 ? 44.935  69.697 49.731  1.00 40.55  ? 285  ILE C CG1 1 
ATOM   6132  C CG2 . ILE C  1 285 ? 43.310  71.204 48.597  1.00 41.76  ? 285  ILE C CG2 1 
ATOM   6133  C CD1 . ILE C  1 285 ? 44.099  68.492 50.102  1.00 38.40  ? 285  ILE C CD1 1 
ATOM   6134  N N   . ASN C  1 286 ? 45.230  73.726 48.110  1.00 48.47  ? 286  ASN C N   1 
ATOM   6135  C CA  . ASN C  1 286 ? 44.786  74.816 47.251  1.00 50.71  ? 286  ASN C CA  1 
ATOM   6136  C C   . ASN C  1 286 ? 44.680  74.306 45.819  1.00 48.79  ? 286  ASN C C   1 
ATOM   6137  O O   . ASN C  1 286 ? 45.657  74.320 45.069  1.00 49.52  ? 286  ASN C O   1 
ATOM   6138  C CB  . ASN C  1 286 ? 45.765  75.996 47.326  1.00 55.05  ? 286  ASN C CB  1 
ATOM   6139  C CG  . ASN C  1 286 ? 45.370  77.147 46.413  1.00 58.10  ? 286  ASN C CG  1 
ATOM   6140  O OD1 . ASN C  1 286 ? 44.185  77.369 46.155  1.00 57.85  ? 286  ASN C OD1 1 
ATOM   6141  N ND2 . ASN C  1 286 ? 46.362  77.887 45.920  1.00 61.55  ? 286  ASN C ND2 1 
ATOM   6142  N N   . SER C  1 287 ? 43.495  73.833 45.447  1.00 46.64  ? 287  SER C N   1 
ATOM   6143  C CA  . SER C  1 287 ? 43.275  73.365 44.087  1.00 44.92  ? 287  SER C CA  1 
ATOM   6144  C C   . SER C  1 287 ? 41.811  73.410 43.679  1.00 44.41  ? 287  SER C C   1 
ATOM   6145  O O   . SER C  1 287 ? 40.912  73.455 44.518  1.00 44.76  ? 287  SER C O   1 
ATOM   6146  C CB  . SER C  1 287 ? 43.822  71.945 43.912  1.00 41.85  ? 287  SER C CB  1 
ATOM   6147  O OG  . SER C  1 287 ? 42.916  70.972 44.390  1.00 39.51  ? 287  SER C OG  1 
ATOM   6148  N N   . SER C  1 288 ? 41.596  73.384 42.369  1.00 43.91  ? 288  SER C N   1 
ATOM   6149  C CA  . SER C  1 288 ? 40.260  73.369 41.785  1.00 43.71  ? 288  SER C CA  1 
ATOM   6150  C C   . SER C  1 288 ? 39.850  71.953 41.365  1.00 40.23  ? 288  SER C C   1 
ATOM   6151  O O   . SER C  1 288 ? 38.773  71.755 40.807  1.00 40.01  ? 288  SER C O   1 
ATOM   6152  C CB  . SER C  1 288 ? 40.218  74.326 40.587  1.00 45.96  ? 288  SER C CB  1 
ATOM   6153  O OG  . SER C  1 288 ? 41.481  74.380 39.934  1.00 46.01  ? 288  SER C OG  1 
ATOM   6154  N N   . MET C  1 289 ? 40.700  70.970 41.656  1.00 38.06  ? 289  MET C N   1 
ATOM   6155  C CA  . MET C  1 289 ? 40.425  69.581 41.297  1.00 35.34  ? 289  MET C CA  1 
ATOM   6156  C C   . MET C  1 289 ? 39.196  69.076 42.047  1.00 35.04  ? 289  MET C C   1 
ATOM   6157  O O   . MET C  1 289 ? 38.931  69.518 43.162  1.00 36.37  ? 289  MET C O   1 
ATOM   6158  C CB  . MET C  1 289 ? 41.603  68.677 41.662  1.00 34.08  ? 289  MET C CB  1 
ATOM   6159  C CG  . MET C  1 289 ? 42.930  69.026 41.011  1.00 34.89  ? 289  MET C CG  1 
ATOM   6160  S SD  . MET C  1 289 ? 42.919  68.764 39.232  1.00 34.10  ? 289  MET C SD  1 
ATOM   6161  C CE  . MET C  1 289 ? 44.646  68.332 38.993  1.00 34.66  ? 289  MET C CE  1 
ATOM   6162  N N   . PRO C  1 290 ? 38.439  68.147 41.440  1.00 33.68  ? 290  PRO C N   1 
ATOM   6163  C CA  . PRO C  1 290 ? 37.329  67.522 42.159  1.00 33.88  ? 290  PRO C CA  1 
ATOM   6164  C C   . PRO C  1 290 ? 37.779  66.502 43.208  1.00 32.79  ? 290  PRO C C   1 
ATOM   6165  O O   . PRO C  1 290 ? 37.007  66.179 44.111  1.00 33.62  ? 290  PRO C O   1 
ATOM   6166  C CB  . PRO C  1 290 ? 36.552  66.819 41.047  1.00 33.29  ? 290  PRO C CB  1 
ATOM   6167  C CG  . PRO C  1 290 ? 37.582  66.522 40.019  1.00 31.65  ? 290  PRO C CG  1 
ATOM   6168  C CD  . PRO C  1 290 ? 38.507  67.698 40.039  1.00 32.47  ? 290  PRO C CD  1 
ATOM   6169  N N   . PHE C  1 291 ? 39.007  66.001 43.076  1.00 31.40  ? 291  PHE C N   1 
ATOM   6170  C CA  . PHE C  1 291 ? 39.535  64.949 43.945  1.00 30.72  ? 291  PHE C CA  1 
ATOM   6171  C C   . PHE C  1 291 ? 40.908  65.290 44.489  1.00 30.78  ? 291  PHE C C   1 
ATOM   6172  O O   . PHE C  1 291 ? 41.618  66.121 43.928  1.00 31.21  ? 291  PHE C O   1 
ATOM   6173  C CB  . PHE C  1 291 ? 39.704  63.650 43.165  1.00 29.69  ? 291  PHE C CB  1 
ATOM   6174  C CG  . PHE C  1 291 ? 38.423  62.979 42.806  1.00 29.96  ? 291  PHE C CG  1 
ATOM   6175  C CD1 . PHE C  1 291 ? 37.696  62.304 43.771  1.00 30.95  ? 291  PHE C CD1 1 
ATOM   6176  C CD2 . PHE C  1 291 ? 37.960  62.988 41.498  1.00 29.65  ? 291  PHE C CD2 1 
ATOM   6177  C CE1 . PHE C  1 291 ? 36.517  61.663 43.446  1.00 31.90  ? 291  PHE C CE1 1 
ATOM   6178  C CE2 . PHE C  1 291 ? 36.781  62.345 41.165  1.00 30.38  ? 291  PHE C CE2 1 
ATOM   6179  C CZ  . PHE C  1 291 ? 36.063  61.683 42.143  1.00 31.67  ? 291  PHE C CZ  1 
ATOM   6180  N N   . HIS C  1 292 ? 41.283  64.602 45.565  1.00 30.71  ? 292  HIS C N   1 
ATOM   6181  C CA  . HIS C  1 292 ? 42.652  64.621 46.072  1.00 31.08  ? 292  HIS C CA  1 
ATOM   6182  C C   . HIS C  1 292 ? 42.962  63.282 46.737  1.00 30.94  ? 292  HIS C C   1 
ATOM   6183  O O   . HIS C  1 292 ? 42.057  62.476 46.953  1.00 30.70  ? 292  HIS C O   1 
ATOM   6184  C CB  . HIS C  1 292 ? 42.837  65.765 47.068  1.00 32.37  ? 292  HIS C CB  1 
ATOM   6185  C CG  . HIS C  1 292 ? 42.178  65.525 48.388  1.00 32.70  ? 292  HIS C CG  1 
ATOM   6186  N ND1 . HIS C  1 292 ? 42.881  65.156 49.511  1.00 33.24  ? 292  HIS C ND1 1 
ATOM   6187  C CD2 . HIS C  1 292 ? 40.878  65.578 48.758  1.00 32.95  ? 292  HIS C CD2 1 
ATOM   6188  C CE1 . HIS C  1 292 ? 42.044  65.003 50.521  1.00 33.61  ? 292  HIS C CE1 1 
ATOM   6189  N NE2 . HIS C  1 292 ? 40.821  65.253 50.091  1.00 33.57  ? 292  HIS C NE2 1 
ATOM   6190  N N   . ASN C  1 293 ? 44.232  63.046 47.060  1.00 31.64  ? 293  ASN C N   1 
ATOM   6191  C CA  . ASN C  1 293 ? 44.650  61.795 47.704  1.00 32.19  ? 293  ASN C CA  1 
ATOM   6192  C C   . ASN C  1 293 ? 45.610  62.005 48.877  1.00 33.60  ? 293  ASN C C   1 
ATOM   6193  O O   . ASN C  1 293 ? 46.405  61.123 49.212  1.00 34.79  ? 293  ASN C O   1 
ATOM   6194  C CB  . ASN C  1 293 ? 45.289  60.869 46.668  1.00 32.37  ? 293  ASN C CB  1 
ATOM   6195  C CG  . ASN C  1 293 ? 46.614  61.391 46.155  1.00 33.43  ? 293  ASN C CG  1 
ATOM   6196  O OD1 . ASN C  1 293 ? 46.904  62.582 46.246  1.00 33.78  ? 293  ASN C OD1 1 
ATOM   6197  N ND2 . ASN C  1 293 ? 47.427  60.500 45.611  1.00 34.55  ? 293  ASN C ND2 1 
ATOM   6198  N N   . ILE C  1 294 ? 45.517  63.169 49.509  1.00 33.87  ? 294  ILE C N   1 
ATOM   6199  C CA  . ILE C  1 294 ? 46.435  63.562 50.580  1.00 35.45  ? 294  ILE C CA  1 
ATOM   6200  C C   . ILE C  1 294 ? 46.114  62.848 51.894  1.00 35.75  ? 294  ILE C C   1 
ATOM   6201  O O   . ILE C  1 294 ? 46.956  62.136 52.443  1.00 37.07  ? 294  ILE C O   1 
ATOM   6202  C CB  . ILE C  1 294 ? 46.407  65.094 50.810  1.00 36.14  ? 294  ILE C CB  1 
ATOM   6203  C CG1 . ILE C  1 294 ? 46.691  65.857 49.508  1.00 36.29  ? 294  ILE C CG1 1 
ATOM   6204  C CG2 . ILE C  1 294 ? 47.409  65.496 51.880  1.00 38.18  ? 294  ILE C CG2 1 
ATOM   6205  C CD1 . ILE C  1 294 ? 47.895  65.362 48.733  1.00 37.21  ? 294  ILE C CD1 1 
ATOM   6206  N N   . HIS C  1 295 ? 44.895  63.043 52.390  1.00 35.00  ? 295  HIS C N   1 
ATOM   6207  C CA  . HIS C  1 295 ? 44.486  62.507 53.687  1.00 35.58  ? 295  HIS C CA  1 
ATOM   6208  C C   . HIS C  1 295 ? 42.950  62.530 53.811  1.00 35.03  ? 295  HIS C C   1 
ATOM   6209  O O   . HIS C  1 295 ? 42.326  63.516 53.424  1.00 34.70  ? 295  HIS C O   1 
ATOM   6210  C CB  . HIS C  1 295 ? 45.124  63.346 54.799  1.00 36.81  ? 295  HIS C CB  1 
ATOM   6211  C CG  . HIS C  1 295 ? 45.197  62.651 56.122  1.00 37.82  ? 295  HIS C CG  1 
ATOM   6212  N ND1 . HIS C  1 295 ? 44.104  62.507 56.944  1.00 37.87  ? 295  HIS C ND1 1 
ATOM   6213  C CD2 . HIS C  1 295 ? 46.236  62.078 56.775  1.00 39.23  ? 295  HIS C CD2 1 
ATOM   6214  C CE1 . HIS C  1 295 ? 44.459  61.862 58.041  1.00 39.05  ? 295  HIS C CE1 1 
ATOM   6215  N NE2 . HIS C  1 295 ? 45.749  61.593 57.965  1.00 39.87  ? 295  HIS C NE2 1 
ATOM   6216  N N   . PRO C  1 296 ? 42.337  61.451 54.349  1.00 35.52  ? 296  PRO C N   1 
ATOM   6217  C CA  . PRO C  1 296 ? 40.866  61.385 54.460  1.00 35.79  ? 296  PRO C CA  1 
ATOM   6218  C C   . PRO C  1 296 ? 40.230  62.468 55.343  1.00 36.56  ? 296  PRO C C   1 
ATOM   6219  O O   . PRO C  1 296 ? 39.229  63.068 54.962  1.00 36.80  ? 296  PRO C O   1 
ATOM   6220  C CB  . PRO C  1 296 ? 40.614  59.995 55.070  1.00 37.03  ? 296  PRO C CB  1 
ATOM   6221  C CG  . PRO C  1 296 ? 41.906  59.584 55.676  1.00 37.56  ? 296  PRO C CG  1 
ATOM   6222  C CD  . PRO C  1 296 ? 42.971  60.207 54.824  1.00 36.52  ? 296  PRO C CD  1 
ATOM   6223  N N   . LEU C  1 297 ? 40.803  62.692 56.518  1.00 37.34  ? 297  LEU C N   1 
ATOM   6224  C CA  . LEU C  1 297 ? 40.269  63.658 57.478  1.00 38.49  ? 297  LEU C CA  1 
ATOM   6225  C C   . LEU C  1 297 ? 40.647  65.092 57.113  1.00 38.44  ? 297  LEU C C   1 
ATOM   6226  O O   . LEU C  1 297 ? 41.770  65.531 57.363  1.00 38.59  ? 297  LEU C O   1 
ATOM   6227  C CB  . LEU C  1 297 ? 40.765  63.332 58.893  1.00 39.52  ? 297  LEU C CB  1 
ATOM   6228  C CG  . LEU C  1 297 ? 40.508  61.903 59.385  1.00 40.27  ? 297  LEU C CG  1 
ATOM   6229  C CD1 . LEU C  1 297 ? 41.309  61.616 60.647  1.00 41.27  ? 297  LEU C CD1 1 
ATOM   6230  C CD2 . LEU C  1 297 ? 39.025  61.664 59.621  1.00 41.57  ? 297  LEU C CD2 1 
ATOM   6231  N N   . THR C  1 298 ? 39.703  65.818 56.522  1.00 38.82  ? 298  THR C N   1 
ATOM   6232  C CA  . THR C  1 298 ? 39.917  67.221 56.177  1.00 39.53  ? 298  THR C CA  1 
ATOM   6233  C C   . THR C  1 298 ? 38.843  68.103 56.800  1.00 41.73  ? 298  THR C C   1 
ATOM   6234  O O   . THR C  1 298 ? 37.817  67.617 57.275  1.00 42.56  ? 298  THR C O   1 
ATOM   6235  C CB  . THR C  1 298 ? 39.951  67.444 54.648  1.00 38.51  ? 298  THR C CB  1 
ATOM   6236  O OG1 . THR C  1 298 ? 38.627  67.365 54.104  1.00 38.89  ? 298  THR C OG1 1 
ATOM   6237  C CG2 . THR C  1 298 ? 40.836  66.412 53.975  1.00 36.69  ? 298  THR C CG2 1 
ATOM   6238  N N   . ILE C  1 299 ? 39.108  69.404 56.798  1.00 43.24  ? 299  ILE C N   1 
ATOM   6239  C CA  . ILE C  1 299 ? 38.174  70.403 57.303  1.00 46.08  ? 299  ILE C CA  1 
ATOM   6240  C C   . ILE C  1 299 ? 38.122  71.534 56.278  1.00 47.36  ? 299  ILE C C   1 
ATOM   6241  O O   . ILE C  1 299 ? 39.153  71.923 55.721  1.00 46.79  ? 299  ILE C O   1 
ATOM   6242  C CB  . ILE C  1 299 ? 38.582  70.908 58.721  1.00 47.75  ? 299  ILE C CB  1 
ATOM   6243  C CG1 . ILE C  1 299 ? 37.712  72.089 59.197  1.00 51.29  ? 299  ILE C CG1 1 
ATOM   6244  C CG2 . ILE C  1 299 ? 40.057  71.293 58.771  1.00 47.36  ? 299  ILE C CG2 1 
ATOM   6245  C CD1 . ILE C  1 299 ? 36.466  71.682 59.953  1.00 52.83  ? 299  ILE C CD1 1 
ATOM   6246  N N   . GLY C  1 300 ? 36.915  72.029 56.014  1.00 49.56  ? 300  GLY C N   1 
ATOM   6247  C CA  . GLY C  1 300 ? 36.710  73.150 55.104  1.00 51.61  ? 300  GLY C CA  1 
ATOM   6248  C C   . GLY C  1 300 ? 36.150  72.722 53.764  1.00 50.46  ? 300  GLY C C   1 
ATOM   6249  O O   . GLY C  1 300 ? 35.647  71.606 53.615  1.00 48.74  ? 300  GLY C O   1 
ATOM   6250  N N   . GLU C  1 301 ? 36.240  73.623 52.787  1.00 51.82  ? 301  GLU C N   1 
ATOM   6251  C CA  . GLU C  1 301 ? 35.760  73.360 51.434  1.00 50.99  ? 301  GLU C CA  1 
ATOM   6252  C C   . GLU C  1 301 ? 36.831  72.593 50.674  1.00 47.34  ? 301  GLU C C   1 
ATOM   6253  O O   . GLU C  1 301 ? 37.789  73.180 50.170  1.00 47.37  ? 301  GLU C O   1 
ATOM   6254  C CB  . GLU C  1 301 ? 35.426  74.673 50.715  1.00 54.38  ? 301  GLU C CB  1 
ATOM   6255  C CG  . GLU C  1 301 ? 34.680  74.496 49.396  1.00 54.28  ? 301  GLU C CG  1 
ATOM   6256  C CD  . GLU C  1 301 ? 33.223  74.079 49.569  1.00 55.98  ? 301  GLU C CD  1 
ATOM   6257  O OE1 . GLU C  1 301 ? 32.752  73.956 50.725  1.00 57.45  ? 301  GLU C OE1 1 
ATOM   6258  O OE2 . GLU C  1 301 ? 32.541  73.882 48.536  1.00 56.21  ? 301  GLU C OE2 1 
ATOM   6259  N N   . CYS C  1 302 ? 36.654  71.277 50.594  1.00 44.80  ? 302  CYS C N   1 
ATOM   6260  C CA  . CYS C  1 302 ? 37.676  70.392 50.056  1.00 41.75  ? 302  CYS C CA  1 
ATOM   6261  C C   . CYS C  1 302 ? 37.174  69.536 48.897  1.00 40.07  ? 302  CYS C C   1 
ATOM   6262  O O   . CYS C  1 302 ? 35.978  69.250 48.801  1.00 40.97  ? 302  CYS C O   1 
ATOM   6263  C CB  . CYS C  1 302 ? 38.182  69.464 51.161  1.00 40.54  ? 302  CYS C CB  1 
ATOM   6264  S SG  . CYS C  1 302 ? 39.024  70.319 52.509  1.00 42.25  ? 302  CYS C SG  1 
ATOM   6265  N N   . PRO C  1 303 ? 38.099  69.112 48.018  1.00 38.01  ? 303  PRO C N   1 
ATOM   6266  C CA  . PRO C  1 303 ? 37.762  68.068 47.055  1.00 36.27  ? 303  PRO C CA  1 
ATOM   6267  C C   . PRO C  1 303 ? 37.589  66.730 47.776  1.00 35.34  ? 303  PRO C C   1 
ATOM   6268  O O   . PRO C  1 303 ? 37.945  66.619 48.953  1.00 35.69  ? 303  PRO C O   1 
ATOM   6269  C CB  . PRO C  1 303 ? 38.968  68.044 46.110  1.00 34.86  ? 303  PRO C CB  1 
ATOM   6270  C CG  . PRO C  1 303 ? 40.087  68.675 46.859  1.00 35.62  ? 303  PRO C CG  1 
ATOM   6271  C CD  . PRO C  1 303 ? 39.478  69.608 47.859  1.00 37.81  ? 303  PRO C CD  1 
ATOM   6272  N N   . LYS C  1 304 ? 37.052  65.728 47.087  1.00 34.54  ? 304  LYS C N   1 
ATOM   6273  C CA  . LYS C  1 304 ? 36.785  64.436 47.716  1.00 34.43  ? 304  LYS C CA  1 
ATOM   6274  C C   . LYS C  1 304 ? 38.048  63.590 47.768  1.00 32.83  ? 304  LYS C C   1 
ATOM   6275  O O   . LYS C  1 304 ? 38.843  63.584 46.828  1.00 31.69  ? 304  LYS C O   1 
ATOM   6276  C CB  . LYS C  1 304 ? 35.683  63.688 46.970  1.00 35.05  ? 304  LYS C CB  1 
ATOM   6277  C CG  . LYS C  1 304 ? 34.372  64.460 46.876  1.00 37.35  ? 304  LYS C CG  1 
ATOM   6278  C CD  . LYS C  1 304 ? 33.646  64.530 48.218  1.00 39.69  ? 304  LYS C CD  1 
ATOM   6279  C CE  . LYS C  1 304 ? 33.055  65.911 48.483  1.00 41.98  ? 304  LYS C CE  1 
ATOM   6280  N NZ  . LYS C  1 304 ? 31.804  65.839 49.295  1.00 45.31  ? 304  LYS C NZ  1 
ATOM   6281  N N   . TYR C  1 305 ? 38.233  62.882 48.874  1.00 33.18  ? 305  TYR C N   1 
ATOM   6282  C CA  . TYR C  1 305 ? 39.411  62.053 49.049  1.00 32.44  ? 305  TYR C CA  1 
ATOM   6283  C C   . TYR C  1 305 ? 39.217  60.692 48.394  1.00 32.36  ? 305  TYR C C   1 
ATOM   6284  O O   . TYR C  1 305 ? 38.170  60.058 48.552  1.00 33.43  ? 305  TYR C O   1 
ATOM   6285  C CB  . TYR C  1 305 ? 39.740  61.865 50.529  1.00 33.33  ? 305  TYR C CB  1 
ATOM   6286  C CG  . TYR C  1 305 ? 40.885  60.906 50.751  1.00 33.33  ? 305  TYR C CG  1 
ATOM   6287  C CD1 . TYR C  1 305 ? 42.201  61.305 50.548  1.00 33.00  ? 305  TYR C CD1 1 
ATOM   6288  C CD2 . TYR C  1 305 ? 40.652  59.593 51.139  1.00 34.33  ? 305  TYR C CD2 1 
ATOM   6289  C CE1 . TYR C  1 305 ? 43.252  60.424 50.741  1.00 33.71  ? 305  TYR C CE1 1 
ATOM   6290  C CE2 . TYR C  1 305 ? 41.696  58.706 51.335  1.00 35.00  ? 305  TYR C CE2 1 
ATOM   6291  C CZ  . TYR C  1 305 ? 42.994  59.127 51.135  1.00 34.69  ? 305  TYR C CZ  1 
ATOM   6292  O OH  . TYR C  1 305 ? 44.037  58.255 51.327  1.00 36.00  ? 305  TYR C OH  1 
ATOM   6293  N N   . VAL C  1 306 ? 40.235  60.257 47.656  1.00 31.57  ? 306  VAL C N   1 
ATOM   6294  C CA  . VAL C  1 306 ? 40.287  58.902 47.119  1.00 31.98  ? 306  VAL C CA  1 
ATOM   6295  C C   . VAL C  1 306 ? 41.686  58.341 47.331  1.00 32.44  ? 306  VAL C C   1 
ATOM   6296  O O   . VAL C  1 306 ? 42.643  59.095 47.485  1.00 32.11  ? 306  VAL C O   1 
ATOM   6297  C CB  . VAL C  1 306 ? 39.911  58.847 45.618  1.00 31.15  ? 306  VAL C CB  1 
ATOM   6298  C CG1 . VAL C  1 306 ? 38.412  59.025 45.436  1.00 31.63  ? 306  VAL C CG1 1 
ATOM   6299  C CG2 . VAL C  1 306 ? 40.673  59.893 44.815  1.00 29.87  ? 306  VAL C CG2 1 
ATOM   6300  N N   . LYS C  1 307 ? 41.797  57.017 47.330  1.00 33.82  ? 307  LYS C N   1 
ATOM   6301  C CA  . LYS C  1 307 ? 43.084  56.339 47.500  1.00 35.11  ? 307  LYS C CA  1 
ATOM   6302  C C   . LYS C  1 307 ? 43.892  56.195 46.199  1.00 34.92  ? 307  LYS C C   1 
ATOM   6303  O O   . LYS C  1 307 ? 44.929  55.535 46.192  1.00 36.64  ? 307  LYS C O   1 
ATOM   6304  C CB  . LYS C  1 307 ? 42.869  54.946 48.101  1.00 37.51  ? 307  LYS C CB  1 
ATOM   6305  C CG  . LYS C  1 307 ? 42.484  54.934 49.566  1.00 38.48  ? 307  LYS C CG  1 
ATOM   6306  C CD  . LYS C  1 307 ? 42.604  53.523 50.119  1.00 41.52  ? 307  LYS C CD  1 
ATOM   6307  C CE  . LYS C  1 307 ? 41.867  53.359 51.438  1.00 42.84  ? 307  LYS C CE  1 
ATOM   6308  N NZ  . LYS C  1 307 ? 41.987  51.971 51.974  1.00 46.37  ? 307  LYS C NZ  1 
ATOM   6309  N N   . SER C  1 308 ? 43.432  56.798 45.107  1.00 33.27  ? 308  SER C N   1 
ATOM   6310  C CA  . SER C  1 308 ? 44.099  56.644 43.817  1.00 33.19  ? 308  SER C CA  1 
ATOM   6311  C C   . SER C  1 308 ? 45.428  57.391 43.781  1.00 33.53  ? 308  SER C C   1 
ATOM   6312  O O   . SER C  1 308 ? 45.595  58.416 44.446  1.00 33.06  ? 308  SER C O   1 
ATOM   6313  C CB  . SER C  1 308 ? 43.208  57.155 42.677  1.00 31.46  ? 308  SER C CB  1 
ATOM   6314  O OG  . SER C  1 308 ? 41.851  56.821 42.893  1.00 31.43  ? 308  SER C OG  1 
ATOM   6315  N N   . ASN C  1 309 ? 46.365  56.862 42.998  1.00 34.86  ? 309  ASN C N   1 
ATOM   6316  C CA  . ASN C  1 309 ? 47.590  57.574 42.653  1.00 35.73  ? 309  ASN C CA  1 
ATOM   6317  C C   . ASN C  1 309 ? 47.406  58.424 41.403  1.00 34.24  ? 309  ASN C C   1 
ATOM   6318  O O   . ASN C  1 309 ? 48.157  59.377 41.184  1.00 34.79  ? 309  ASN C O   1 
ATOM   6319  C CB  . ASN C  1 309 ? 48.739  56.590 42.427  1.00 38.70  ? 309  ASN C CB  1 
ATOM   6320  C CG  . ASN C  1 309 ? 49.255  55.988 43.721  1.00 40.97  ? 309  ASN C CG  1 
ATOM   6321  O OD1 . ASN C  1 309 ? 49.495  56.702 44.702  1.00 40.92  ? 309  ASN C OD1 1 
ATOM   6322  N ND2 . ASN C  1 309 ? 49.442  54.668 43.732  1.00 43.34  ? 309  ASN C ND2 1 
ATOM   6323  N N   . ARG C  1 310 ? 46.408  58.082 40.589  1.00 32.80  ? 310  ARG C N   1 
ATOM   6324  C CA  . ARG C  1 310 ? 46.238  58.711 39.281  1.00 31.66  ? 310  ARG C CA  1 
ATOM   6325  C C   . ARG C  1 310 ? 44.785  58.664 38.789  1.00 29.78  ? 310  ARG C C   1 
ATOM   6326  O O   . ARG C  1 310 ? 44.189  57.590 38.703  1.00 30.03  ? 310  ARG C O   1 
ATOM   6327  C CB  . ARG C  1 310 ? 47.148  58.003 38.271  1.00 33.29  ? 310  ARG C CB  1 
ATOM   6328  C CG  . ARG C  1 310 ? 47.369  58.761 36.975  1.00 32.85  ? 310  ARG C CG  1 
ATOM   6329  C CD  . ARG C  1 310 ? 48.216  57.960 35.999  1.00 34.78  ? 310  ARG C CD  1 
ATOM   6330  N NE  . ARG C  1 310 ? 47.901  58.322 34.616  1.00 33.78  ? 310  ARG C NE  1 
ATOM   6331  C CZ  . ARG C  1 310 ? 48.439  59.341 33.944  1.00 34.17  ? 310  ARG C CZ  1 
ATOM   6332  N NH1 . ARG C  1 310 ? 49.351  60.137 34.502  1.00 35.81  ? 310  ARG C NH1 1 
ATOM   6333  N NH2 . ARG C  1 310 ? 48.061  59.567 32.692  1.00 33.29  ? 310  ARG C NH2 1 
ATOM   6334  N N   . LEU C  1 311 ? 44.227  59.836 38.478  1.00 28.44  ? 311  LEU C N   1 
ATOM   6335  C CA  . LEU C  1 311 ? 42.918  59.941 37.818  1.00 27.20  ? 311  LEU C CA  1 
ATOM   6336  C C   . LEU C  1 311 ? 42.976  60.949 36.668  1.00 26.58  ? 311  LEU C C   1 
ATOM   6337  O O   . LEU C  1 311 ? 42.958  62.159 36.891  1.00 26.62  ? 311  LEU C O   1 
ATOM   6338  C CB  . LEU C  1 311 ? 41.829  60.362 38.805  1.00 26.90  ? 311  LEU C CB  1 
ATOM   6339  C CG  . LEU C  1 311 ? 41.433  59.383 39.912  1.00 27.64  ? 311  LEU C CG  1 
ATOM   6340  C CD1 . LEU C  1 311 ? 40.427  60.052 40.836  1.00 27.68  ? 311  LEU C CD1 1 
ATOM   6341  C CD2 . LEU C  1 311 ? 40.858  58.094 39.351  1.00 28.20  ? 311  LEU C CD2 1 
ATOM   6342  N N   . VAL C  1 312 ? 43.050  60.440 35.442  1.00 26.34  ? 312  VAL C N   1 
ATOM   6343  C CA  . VAL C  1 312 ? 43.145  61.281 34.255  1.00 25.99  ? 312  VAL C CA  1 
ATOM   6344  C C   . VAL C  1 312 ? 42.037  60.922 33.270  1.00 25.13  ? 312  VAL C C   1 
ATOM   6345  O O   . VAL C  1 312 ? 41.897  59.763 32.884  1.00 25.26  ? 312  VAL C O   1 
ATOM   6346  C CB  . VAL C  1 312 ? 44.508  61.113 33.557  1.00 27.09  ? 312  VAL C CB  1 
ATOM   6347  C CG1 . VAL C  1 312 ? 44.632  62.074 32.381  1.00 27.15  ? 312  VAL C CG1 1 
ATOM   6348  C CG2 . VAL C  1 312 ? 45.642  61.334 34.548  1.00 28.54  ? 312  VAL C CG2 1 
ATOM   6349  N N   . LEU C  1 313 ? 41.258  61.926 32.879  1.00 24.72  ? 313  LEU C N   1 
ATOM   6350  C CA  . LEU C  1 313 ? 40.188  61.759 31.902  1.00 24.31  ? 313  LEU C CA  1 
ATOM   6351  C C   . LEU C  1 313 ? 40.662  62.146 30.514  1.00 24.23  ? 313  LEU C C   1 
ATOM   6352  O O   . LEU C  1 313 ? 41.255  63.208 30.338  1.00 24.74  ? 313  LEU C O   1 
ATOM   6353  C CB  . LEU C  1 313 ? 38.987  62.638 32.256  1.00 24.63  ? 313  LEU C CB  1 
ATOM   6354  C CG  . LEU C  1 313 ? 38.061  62.115 33.346  1.00 25.07  ? 313  LEU C CG  1 
ATOM   6355  C CD1 . LEU C  1 313 ? 37.122  63.216 33.816  1.00 26.07  ? 313  LEU C CD1 1 
ATOM   6356  C CD2 . LEU C  1 313 ? 37.277  60.911 32.846  1.00 25.33  ? 313  LEU C CD2 1 
ATOM   6357  N N   . ALA C  1 314 ? 40.381  61.294 29.529  1.00 23.95  ? 314  ALA C N   1 
ATOM   6358  C CA  . ALA C  1 314 ? 40.603  61.644 28.133  1.00 23.92  ? 314  ALA C CA  1 
ATOM   6359  C C   . ALA C  1 314 ? 39.591  62.701 27.736  1.00 24.05  ? 314  ALA C C   1 
ATOM   6360  O O   . ALA C  1 314 ? 38.399  62.541 27.987  1.00 24.17  ? 314  ALA C O   1 
ATOM   6361  C CB  . ALA C  1 314 ? 40.459  60.425 27.238  1.00 23.82  ? 314  ALA C CB  1 
ATOM   6362  N N   . THR C  1 315 ? 40.080  63.796 27.164  1.00 24.65  ? 315  THR C N   1 
ATOM   6363  C CA  . THR C  1 315 ? 39.224  64.791 26.523  1.00 25.39  ? 315  THR C CA  1 
ATOM   6364  C C   . THR C  1 315 ? 39.387  64.702 25.014  1.00 25.39  ? 315  THR C C   1 
ATOM   6365  O O   . THR C  1 315 ? 38.412  64.708 24.277  1.00 25.52  ? 315  THR C O   1 
ATOM   6366  C CB  . THR C  1 315 ? 39.546  66.227 26.986  1.00 26.83  ? 315  THR C CB  1 
ATOM   6367  O OG1 . THR C  1 315 ? 40.964  66.430 27.005  1.00 27.34  ? 315  THR C OG1 1 
ATOM   6368  C CG2 . THR C  1 315 ? 38.983  66.475 28.378  1.00 27.16  ? 315  THR C CG2 1 
ATOM   6369  N N   . GLY C  1 316 ? 40.630  64.609 24.565  1.00 25.61  ? 316  GLY C N   1 
ATOM   6370  C CA  . GLY C  1 316 ? 40.927  64.491 23.156  1.00 25.84  ? 316  GLY C CA  1 
ATOM   6371  C C   . GLY C  1 316 ? 40.855  63.059 22.678  1.00 24.94  ? 316  GLY C C   1 
ATOM   6372  O O   . GLY C  1 316 ? 40.332  62.180 23.364  1.00 24.27  ? 316  GLY C O   1 
ATOM   6373  N N   . LEU C  1 317 ? 41.408  62.829 21.495  1.00 25.37  ? 317  LEU C N   1 
ATOM   6374  C CA  . LEU C  1 317 ? 41.339  61.531 20.844  1.00 25.05  ? 317  LEU C CA  1 
ATOM   6375  C C   . LEU C  1 317 ? 42.705  60.863 20.843  1.00 26.06  ? 317  LEU C C   1 
ATOM   6376  O O   . LEU C  1 317 ? 43.700  61.464 21.241  1.00 27.06  ? 317  LEU C O   1 
ATOM   6377  C CB  . LEU C  1 317 ? 40.777  61.671 19.421  1.00 25.06  ? 317  LEU C CB  1 
ATOM   6378  C CG  . LEU C  1 317 ? 41.365  62.732 18.484  1.00 26.04  ? 317  LEU C CG  1 
ATOM   6379  C CD1 . LEU C  1 317 ? 42.635  62.220 17.832  1.00 27.02  ? 317  LEU C CD1 1 
ATOM   6380  C CD2 . LEU C  1 317 ? 40.354  63.149 17.428  1.00 26.03  ? 317  LEU C CD2 1 
ATOM   6381  N N   . ARG C  1 318 ? 42.734  59.608 20.413  1.00 26.40  ? 318  ARG C N   1 
ATOM   6382  C CA  . ARG C  1 318 ? 43.963  58.827 20.374  1.00 28.09  ? 318  ARG C CA  1 
ATOM   6383  C C   . ARG C  1 318 ? 44.989  59.505 19.479  1.00 29.66  ? 318  ARG C C   1 
ATOM   6384  O O   . ARG C  1 318 ? 44.736  59.743 18.298  1.00 29.62  ? 318  ARG C O   1 
ATOM   6385  C CB  . ARG C  1 318 ? 43.667  57.416 19.871  1.00 28.58  ? 318  ARG C CB  1 
ATOM   6386  C CG  . ARG C  1 318 ? 44.880  56.510 19.755  1.00 30.91  ? 318  ARG C CG  1 
ATOM   6387  C CD  . ARG C  1 318 ? 44.488  55.169 19.159  1.00 31.86  ? 318  ARG C CD  1 
ATOM   6388  N NE  . ARG C  1 318 ? 43.764  54.333 20.116  1.00 31.81  ? 318  ARG C NE  1 
ATOM   6389  C CZ  . ARG C  1 318 ? 44.313  53.380 20.864  1.00 33.80  ? 318  ARG C CZ  1 
ATOM   6390  N NH1 . ARG C  1 318 ? 45.615  53.116 20.788  1.00 36.15  ? 318  ARG C NH1 1 
ATOM   6391  N NH2 . ARG C  1 318 ? 43.554  52.681 21.701  1.00 33.97  ? 318  ARG C NH2 1 
ATOM   6392  N N   . ASN C  1 319 ? 46.147  59.810 20.055  1.00 31.52  ? 319  ASN C N   1 
ATOM   6393  C CA  . ASN C  1 319 ? 47.189  60.554 19.366  1.00 33.81  ? 319  ASN C CA  1 
ATOM   6394  C C   . ASN C  1 319 ? 48.117  59.614 18.605  1.00 36.36  ? 319  ASN C C   1 
ATOM   6395  O O   . ASN C  1 319 ? 48.493  58.554 19.105  1.00 37.44  ? 319  ASN C O   1 
ATOM   6396  C CB  . ASN C  1 319 ? 47.975  61.388 20.372  1.00 35.17  ? 319  ASN C CB  1 
ATOM   6397  C CG  . ASN C  1 319 ? 48.880  62.407 19.717  1.00 37.77  ? 319  ASN C CG  1 
ATOM   6398  O OD1 . ASN C  1 319 ? 48.853  62.597 18.505  1.00 38.29  ? 319  ASN C OD1 1 
ATOM   6399  N ND2 . ASN C  1 319 ? 49.694  63.073 20.525  1.00 39.78  ? 319  ASN C ND2 1 
ATOM   6400  N N   . SER C  1 320 ? 48.485  60.021 17.394  1.00 37.91  ? 320  SER C N   1 
ATOM   6401  C CA  . SER C  1 320 ? 49.232  59.170 16.468  1.00 40.49  ? 320  SER C CA  1 
ATOM   6402  C C   . SER C  1 320 ? 50.743  59.169 16.738  1.00 44.66  ? 320  SER C C   1 
ATOM   6403  O O   . SER C  1 320 ? 51.281  60.145 17.262  1.00 45.95  ? 320  SER C O   1 
ATOM   6404  C CB  . SER C  1 320 ? 48.973  59.625 15.028  1.00 40.44  ? 320  SER C CB  1 
ATOM   6405  O OG  . SER C  1 320 ? 47.585  59.596 14.742  1.00 37.31  ? 320  SER C OG  1 
ATOM   6406  N N   . PRO C  1 321 ? 51.429  58.061 16.386  1.00 47.48  ? 321  PRO C N   1 
ATOM   6407  C CA  . PRO C  1 321 ? 52.889  57.982 16.436  1.00 52.26  ? 321  PRO C CA  1 
ATOM   6408  C C   . PRO C  1 321 ? 53.524  58.386 15.110  1.00 55.07  ? 321  PRO C C   1 
ATOM   6409  O O   . PRO C  1 321 ? 53.668  59.575 14.832  1.00 55.48  ? 321  PRO C O   1 
ATOM   6410  C CB  . PRO C  1 321 ? 53.137  56.500 16.708  1.00 54.01  ? 321  PRO C CB  1 
ATOM   6411  C CG  . PRO C  1 321 ? 52.017  55.816 15.997  1.00 51.24  ? 321  PRO C CG  1 
ATOM   6412  C CD  . PRO C  1 321 ? 50.829  56.743 16.095  1.00 46.70  ? 321  PRO C CD  1 
ATOM   6413  N N   . GLY D  2 1   ? 39.867  50.954 17.123  1.00 22.72  ? 1    GLY D N   1 
ATOM   6414  C CA  . GLY D  2 1   ? 38.634  51.463 17.782  1.00 21.32  ? 1    GLY D CA  1 
ATOM   6415  C C   . GLY D  2 1   ? 37.377  50.836 17.219  1.00 21.67  ? 1    GLY D C   1 
ATOM   6416  O O   . GLY D  2 1   ? 37.397  50.240 16.143  1.00 22.73  ? 1    GLY D O   1 
ATOM   6417  N N   . LEU D  2 2   ? 36.275  51.002 17.943  1.00 21.07  ? 2    LEU D N   1 
ATOM   6418  C CA  . LEU D  2 2   ? 35.019  50.349 17.597  1.00 21.91  ? 2    LEU D CA  1 
ATOM   6419  C C   . LEU D  2 2   ? 34.491  50.725 16.215  1.00 22.11  ? 2    LEU D C   1 
ATOM   6420  O O   . LEU D  2 2   ? 33.880  49.900 15.542  1.00 23.53  ? 2    LEU D O   1 
ATOM   6421  C CB  . LEU D  2 2   ? 33.948  50.656 18.648  1.00 21.42  ? 2    LEU D CB  1 
ATOM   6422  C CG  . LEU D  2 2   ? 34.028  49.895 19.966  1.00 21.76  ? 2    LEU D CG  1 
ATOM   6423  C CD1 . LEU D  2 2   ? 32.897  50.332 20.876  1.00 21.39  ? 2    LEU D CD1 1 
ATOM   6424  C CD2 . LEU D  2 2   ? 33.978  48.394 19.743  1.00 23.69  ? 2    LEU D CD2 1 
ATOM   6425  N N   . PHE D  2 3   ? 34.728  51.965 15.799  1.00 20.97  ? 3    PHE D N   1 
ATOM   6426  C CA  . PHE D  2 3   ? 34.122  52.487 14.572  1.00 21.11  ? 3    PHE D CA  1 
ATOM   6427  C C   . PHE D  2 3   ? 35.049  52.425 13.370  1.00 21.44  ? 3    PHE D C   1 
ATOM   6428  O O   . PHE D  2 3   ? 34.638  52.726 12.256  1.00 21.68  ? 3    PHE D O   1 
ATOM   6429  C CB  . PHE D  2 3   ? 33.545  53.878 14.835  1.00 20.10  ? 3    PHE D CB  1 
ATOM   6430  C CG  . PHE D  2 3   ? 32.426  53.840 15.829  1.00 20.33  ? 3    PHE D CG  1 
ATOM   6431  C CD1 . PHE D  2 3   ? 31.133  53.552 15.422  1.00 21.53  ? 3    PHE D CD1 1 
ATOM   6432  C CD2 . PHE D  2 3   ? 32.684  53.977 17.182  1.00 19.70  ? 3    PHE D CD2 1 
ATOM   6433  C CE1 . PHE D  2 3   ? 30.110  53.458 16.341  1.00 22.17  ? 3    PHE D CE1 1 
ATOM   6434  C CE2 . PHE D  2 3   ? 31.666  53.881 18.108  1.00 20.10  ? 3    PHE D CE2 1 
ATOM   6435  C CZ  . PHE D  2 3   ? 30.377  53.619 17.688  1.00 21.38  ? 3    PHE D CZ  1 
ATOM   6436  N N   . GLY D  2 4   ? 36.293  52.015 13.612  1.00 21.74  ? 4    GLY D N   1 
ATOM   6437  C CA  . GLY D  2 4   ? 37.191  51.584 12.552  1.00 22.76  ? 4    GLY D CA  1 
ATOM   6438  C C   . GLY D  2 4   ? 37.837  52.677 11.738  1.00 22.14  ? 4    GLY D C   1 
ATOM   6439  O O   . GLY D  2 4   ? 38.495  52.382 10.747  1.00 23.11  ? 4    GLY D O   1 
ATOM   6440  N N   . ALA D  2 5   ? 37.669  53.932 12.152  1.00 20.91  ? 5    ALA D N   1 
ATOM   6441  C CA  . ALA D  2 5   ? 38.198  55.073 11.403  1.00 20.54  ? 5    ALA D CA  1 
ATOM   6442  C C   . ALA D  2 5   ? 39.551  55.497 11.944  1.00 20.76  ? 5    ALA D C   1 
ATOM   6443  O O   . ALA D  2 5   ? 40.551  55.420 11.240  1.00 21.63  ? 5    ALA D O   1 
ATOM   6444  C CB  . ALA D  2 5   ? 37.218  56.232 11.442  1.00 19.66  ? 5    ALA D CB  1 
ATOM   6445  N N   . ILE D  2 6   ? 39.573  55.936 13.199  1.00 20.31  ? 6    ILE D N   1 
ATOM   6446  C CA  . ILE D  2 6   ? 40.806  56.380 13.857  1.00 20.88  ? 6    ILE D CA  1 
ATOM   6447  C C   . ILE D  2 6   ? 41.758  55.203 14.036  1.00 22.24  ? 6    ILE D C   1 
ATOM   6448  O O   . ILE D  2 6   ? 41.385  54.185 14.616  1.00 22.44  ? 6    ILE D O   1 
ATOM   6449  C CB  . ILE D  2 6   ? 40.512  57.031 15.225  1.00 20.23  ? 6    ILE D CB  1 
ATOM   6450  C CG1 . ILE D  2 6   ? 39.819  58.380 15.016  1.00 19.64  ? 6    ILE D CG1 1 
ATOM   6451  C CG2 . ILE D  2 6   ? 41.791  57.213 16.030  1.00 21.17  ? 6    ILE D CG2 1 
ATOM   6452  C CD1 . ILE D  2 6   ? 39.359  59.055 16.289  1.00 19.29  ? 6    ILE D CD1 1 
ATOM   6453  N N   . ALA D  2 7   ? 42.981  55.348 13.531  1.00 23.61  ? 7    ALA D N   1 
ATOM   6454  C CA  . ALA D  2 7   ? 43.961  54.261 13.513  1.00 25.51  ? 7    ALA D CA  1 
ATOM   6455  C C   . ALA D  2 7   ? 43.382  53.014 12.857  1.00 26.02  ? 7    ALA D C   1 
ATOM   6456  O O   . ALA D  2 7   ? 43.696  51.898 13.250  1.00 27.37  ? 7    ALA D O   1 
ATOM   6457  C CB  . ALA D  2 7   ? 44.439  53.950 14.925  1.00 26.03  ? 7    ALA D CB  1 
ATOM   6458  N N   . GLY D  2 8   ? 42.532  53.217 11.857  1.00 25.29  ? 8    GLY D N   1 
ATOM   6459  C CA  . GLY D  2 8   ? 41.824  52.129 11.200  1.00 25.98  ? 8    GLY D CA  1 
ATOM   6460  C C   . GLY D  2 8   ? 42.027  52.243 9.707   1.00 26.72  ? 8    GLY D C   1 
ATOM   6461  O O   . GLY D  2 8   ? 43.121  51.977 9.219   1.00 28.39  ? 8    GLY D O   1 
ATOM   6462  N N   . PHE D  2 9   ? 40.985  52.643 8.982   1.00 25.77  ? 9    PHE D N   1 
ATOM   6463  C CA  . PHE D  2 9   ? 41.128  52.896 7.552   1.00 26.29  ? 9    PHE D CA  1 
ATOM   6464  C C   . PHE D  2 9   ? 41.753  54.271 7.318   1.00 25.66  ? 9    PHE D C   1 
ATOM   6465  O O   . PHE D  2 9   ? 42.252  54.541 6.231   1.00 26.39  ? 9    PHE D O   1 
ATOM   6466  C CB  . PHE D  2 9   ? 39.804  52.686 6.781   1.00 25.98  ? 9    PHE D CB  1 
ATOM   6467  C CG  . PHE D  2 9   ? 38.782  53.779 6.963   1.00 24.25  ? 9    PHE D CG  1 
ATOM   6468  C CD1 . PHE D  2 9   ? 38.748  54.867 6.105   1.00 23.63  ? 9    PHE D CD1 1 
ATOM   6469  C CD2 . PHE D  2 9   ? 37.819  53.688 7.955   1.00 23.60  ? 9    PHE D CD2 1 
ATOM   6470  C CE1 . PHE D  2 9   ? 37.800  55.863 6.259   1.00 22.55  ? 9    PHE D CE1 1 
ATOM   6471  C CE2 . PHE D  2 9   ? 36.867  54.683 8.116   1.00 22.53  ? 9    PHE D CE2 1 
ATOM   6472  C CZ  . PHE D  2 9   ? 36.858  55.773 7.268   1.00 22.08  ? 9    PHE D CZ  1 
ATOM   6473  N N   . ILE D  2 10  ? 41.733  55.125 8.343   1.00 24.68  ? 10   ILE D N   1 
ATOM   6474  C CA  . ILE D  2 10  ? 42.532  56.357 8.366   1.00 24.72  ? 10   ILE D CA  1 
ATOM   6475  C C   . ILE D  2 10  ? 43.714  56.130 9.304   1.00 25.98  ? 10   ILE D C   1 
ATOM   6476  O O   . ILE D  2 10  ? 43.598  56.292 10.520  1.00 25.46  ? 10   ILE D O   1 
ATOM   6477  C CB  . ILE D  2 10  ? 41.707  57.569 8.834   1.00 23.27  ? 10   ILE D CB  1 
ATOM   6478  C CG1 . ILE D  2 10  ? 40.428  57.695 7.998   1.00 22.48  ? 10   ILE D CG1 1 
ATOM   6479  C CG2 . ILE D  2 10  ? 42.529  58.843 8.729   1.00 23.74  ? 10   ILE D CG2 1 
ATOM   6480  C CD1 . ILE D  2 10  ? 39.428  58.689 8.546   1.00 21.51  ? 10   ILE D CD1 1 
ATOM   6481  N N   . GLU D  2 11  ? 44.847  55.743 8.729   1.00 27.96  ? 11   GLU D N   1 
ATOM   6482  C CA  . GLU D  2 11  ? 45.997  55.265 9.501   1.00 29.88  ? 11   GLU D CA  1 
ATOM   6483  C C   . GLU D  2 11  ? 46.482  56.184 10.617  1.00 29.88  ? 11   GLU D C   1 
ATOM   6484  O O   . GLU D  2 11  ? 46.938  55.703 11.654  1.00 30.71  ? 11   GLU D O   1 
ATOM   6485  C CB  . GLU D  2 11  ? 47.185  55.013 8.578   1.00 32.39  ? 11   GLU D CB  1 
ATOM   6486  C CG  . GLU D  2 11  ? 47.171  53.685 7.849   1.00 33.78  ? 11   GLU D CG  1 
ATOM   6487  C CD  . GLU D  2 11  ? 48.502  53.429 7.166   1.00 36.82  ? 11   GLU D CD  1 
ATOM   6488  O OE1 . GLU D  2 11  ? 48.910  54.277 6.329   1.00 37.14  ? 11   GLU D OE1 1 
ATOM   6489  O OE2 . GLU D  2 11  ? 49.144  52.397 7.480   1.00 39.18  ? 11   GLU D OE2 1 
ATOM   6490  N N   . GLY D  2 12  ? 46.422  57.492 10.390  1.00 29.31  ? 12   GLY D N   1 
ATOM   6491  C CA  . GLY D  2 12  ? 46.974  58.455 11.340  1.00 29.92  ? 12   GLY D CA  1 
ATOM   6492  C C   . GLY D  2 12  ? 46.325  59.824 11.308  1.00 28.79  ? 12   GLY D C   1 
ATOM   6493  O O   . GLY D  2 12  ? 45.616  60.172 10.358  1.00 27.77  ? 12   GLY D O   1 
ATOM   6494  N N   . GLY D  2 13  ? 46.571  60.592 12.367  1.00 29.25  ? 13   GLY D N   1 
ATOM   6495  C CA  . GLY D  2 13  ? 46.060  61.950 12.490  1.00 28.85  ? 13   GLY D CA  1 
ATOM   6496  C C   . GLY D  2 13  ? 46.922  62.961 11.754  1.00 30.80  ? 13   GLY D C   1 
ATOM   6497  O O   . GLY D  2 13  ? 47.947  62.612 11.164  1.00 32.53  ? 13   GLY D O   1 
ATOM   6498  N N   . TRP D  2 14  ? 46.498  64.221 11.796  1.00 30.87  ? 14   TRP D N   1 
ATOM   6499  C CA  . TRP D  2 14  ? 47.162  65.295 11.080  1.00 32.80  ? 14   TRP D CA  1 
ATOM   6500  C C   . TRP D  2 14  ? 47.715  66.344 12.034  1.00 34.93  ? 14   TRP D C   1 
ATOM   6501  O O   . TRP D  2 14  ? 46.965  67.129 12.613  1.00 34.54  ? 14   TRP D O   1 
ATOM   6502  C CB  . TRP D  2 14  ? 46.187  65.963 10.110  1.00 31.68  ? 14   TRP D CB  1 
ATOM   6503  C CG  . TRP D  2 14  ? 45.753  65.097 8.972   1.00 30.20  ? 14   TRP D CG  1 
ATOM   6504  C CD1 . TRP D  2 14  ? 46.438  64.056 8.424   1.00 30.57  ? 14   TRP D CD1 1 
ATOM   6505  C CD2 . TRP D  2 14  ? 44.545  65.227 8.211   1.00 28.56  ? 14   TRP D CD2 1 
ATOM   6506  N NE1 . TRP D  2 14  ? 45.726  63.517 7.383   1.00 29.26  ? 14   TRP D NE1 1 
ATOM   6507  C CE2 . TRP D  2 14  ? 44.561  64.218 7.229   1.00 27.92  ? 14   TRP D CE2 1 
ATOM   6508  C CE3 . TRP D  2 14  ? 43.450  66.096 8.269   1.00 27.93  ? 14   TRP D CE3 1 
ATOM   6509  C CZ2 . TRP D  2 14  ? 43.523  64.051 6.311   1.00 26.58  ? 14   TRP D CZ2 1 
ATOM   6510  C CZ3 . TRP D  2 14  ? 42.420  65.927 7.359   1.00 26.68  ? 14   TRP D CZ3 1 
ATOM   6511  C CH2 . TRP D  2 14  ? 42.465  64.913 6.391   1.00 25.98  ? 14   TRP D CH2 1 
ATOM   6512  N N   . GLN D  2 15  ? 49.038  66.355 12.175  1.00 37.59  ? 15   GLN D N   1 
ATOM   6513  C CA  . GLN D  2 15  ? 49.746  67.438 12.866  1.00 40.51  ? 15   GLN D CA  1 
ATOM   6514  C C   . GLN D  2 15  ? 49.416  68.794 12.225  1.00 41.43  ? 15   GLN D C   1 
ATOM   6515  O O   . GLN D  2 15  ? 49.407  69.819 12.905  1.00 43.15  ? 15   GLN D O   1 
ATOM   6516  C CB  . GLN D  2 15  ? 51.263  67.223 12.798  1.00 43.80  ? 15   GLN D CB  1 
ATOM   6517  C CG  . GLN D  2 15  ? 51.785  65.954 13.462  1.00 43.85  ? 15   GLN D CG  1 
ATOM   6518  C CD  . GLN D  2 15  ? 52.090  66.118 14.943  1.00 45.19  ? 15   GLN D CD  1 
ATOM   6519  O OE1 . GLN D  2 15  ? 51.745  65.255 15.752  1.00 43.66  ? 15   GLN D OE1 1 
ATOM   6520  N NE2 . GLN D  2 15  ? 52.750  67.216 15.305  1.00 48.38  ? 15   GLN D NE2 1 
ATOM   6521  N N   . GLY D  2 16  ? 49.154  68.786 10.917  1.00 40.51  ? 16   GLY D N   1 
ATOM   6522  C CA  . GLY D  2 16  ? 48.859  70.002 10.159  1.00 41.49  ? 16   GLY D CA  1 
ATOM   6523  C C   . GLY D  2 16  ? 47.485  70.626 10.355  1.00 39.88  ? 16   GLY D C   1 
ATOM   6524  O O   . GLY D  2 16  ? 47.248  71.738 9.889   1.00 41.24  ? 16   GLY D O   1 
ATOM   6525  N N   . MET D  2 17  ? 46.573  69.927 11.028  1.00 37.32  ? 17   MET D N   1 
ATOM   6526  C CA  . MET D  2 17  ? 45.251  70.484 11.325  1.00 36.23  ? 17   MET D CA  1 
ATOM   6527  C C   . MET D  2 17  ? 45.141  70.882 12.795  1.00 37.13  ? 17   MET D C   1 
ATOM   6528  O O   . MET D  2 17  ? 44.920  70.035 13.658  1.00 35.60  ? 17   MET D O   1 
ATOM   6529  C CB  . MET D  2 17  ? 44.158  69.481 10.974  1.00 33.09  ? 17   MET D CB  1 
ATOM   6530  C CG  . MET D  2 17  ? 42.758  70.066 11.061  1.00 32.41  ? 17   MET D CG  1 
ATOM   6531  S SD  . MET D  2 17  ? 41.519  68.912 10.464  1.00 29.42  ? 17   MET D SD  1 
ATOM   6532  C CE  . MET D  2 17  ? 41.800  67.554 11.593  1.00 28.00  ? 17   MET D CE  1 
ATOM   6533  N N   . VAL D  2 18  ? 45.274  72.179 13.066  1.00 39.83  ? 18   VAL D N   1 
ATOM   6534  C CA  . VAL D  2 18  ? 45.358  72.693 14.440  1.00 41.50  ? 18   VAL D CA  1 
ATOM   6535  C C   . VAL D  2 18  ? 44.081  73.383 14.942  1.00 41.40  ? 18   VAL D C   1 
ATOM   6536  O O   . VAL D  2 18  ? 43.913  73.575 16.145  1.00 42.11  ? 18   VAL D O   1 
ATOM   6537  C CB  . VAL D  2 18  ? 46.553  73.664 14.596  1.00 45.58  ? 18   VAL D CB  1 
ATOM   6538  C CG1 . VAL D  2 18  ? 47.822  73.039 14.031  1.00 46.26  ? 18   VAL D CG1 1 
ATOM   6539  C CG2 . VAL D  2 18  ? 46.275  75.007 13.930  1.00 47.96  ? 18   VAL D CG2 1 
ATOM   6540  N N   . ASP D  2 19  ? 43.183  73.742 14.028  1.00 40.75  ? 19   ASP D N   1 
ATOM   6541  C CA  . ASP D  2 19  ? 41.984  74.519 14.375  1.00 41.43  ? 19   ASP D CA  1 
ATOM   6542  C C   . ASP D  2 19  ? 40.741  73.649 14.642  1.00 38.40  ? 19   ASP D C   1 
ATOM   6543  O O   . ASP D  2 19  ? 39.632  74.168 14.775  1.00 38.92  ? 19   ASP D O   1 
ATOM   6544  C CB  . ASP D  2 19  ? 41.696  75.574 13.284  1.00 43.34  ? 19   ASP D CB  1 
ATOM   6545  C CG  . ASP D  2 19  ? 41.617  74.980 11.877  1.00 41.29  ? 19   ASP D CG  1 
ATOM   6546  O OD1 . ASP D  2 19  ? 41.902  73.774 11.703  1.00 38.74  ? 19   ASP D OD1 1 
ATOM   6547  O OD2 . ASP D  2 19  ? 41.275  75.728 10.937  1.00 42.49  ? 19   ASP D OD2 1 
ATOM   6548  N N   . GLY D  2 20  ? 40.924  72.336 14.741  1.00 35.66  ? 20   GLY D N   1 
ATOM   6549  C CA  . GLY D  2 20  ? 39.806  71.440 15.023  1.00 33.14  ? 20   GLY D CA  1 
ATOM   6550  C C   . GLY D  2 20  ? 40.211  70.004 15.283  1.00 30.78  ? 20   GLY D C   1 
ATOM   6551  O O   . GLY D  2 20  ? 41.367  69.630 15.091  1.00 30.97  ? 20   GLY D O   1 
ATOM   6552  N N   . TRP D  2 21  ? 39.244  69.199 15.715  1.00 28.91  ? 21   TRP D N   1 
ATOM   6553  C CA  . TRP D  2 21  ? 39.471  67.777 15.990  1.00 26.88  ? 21   TRP D CA  1 
ATOM   6554  C C   . TRP D  2 21  ? 39.297  66.922 14.742  1.00 25.36  ? 21   TRP D C   1 
ATOM   6555  O O   . TRP D  2 21  ? 40.038  65.959 14.538  1.00 24.63  ? 21   TRP D O   1 
ATOM   6556  C CB  . TRP D  2 21  ? 38.536  67.273 17.096  1.00 25.95  ? 21   TRP D CB  1 
ATOM   6557  C CG  . TRP D  2 21  ? 39.128  67.308 18.481  1.00 26.60  ? 21   TRP D CG  1 
ATOM   6558  C CD1 . TRP D  2 21  ? 40.450  67.178 18.829  1.00 27.33  ? 21   TRP D CD1 1 
ATOM   6559  C CD2 . TRP D  2 21  ? 38.408  67.442 19.706  1.00 26.79  ? 21   TRP D CD2 1 
ATOM   6560  N NE1 . TRP D  2 21  ? 40.593  67.244 20.192  1.00 27.91  ? 21   TRP D NE1 1 
ATOM   6561  C CE2 . TRP D  2 21  ? 39.355  67.405 20.755  1.00 27.49  ? 21   TRP D CE2 1 
ATOM   6562  C CE3 . TRP D  2 21  ? 37.052  67.595 20.021  1.00 26.71  ? 21   TRP D CE3 1 
ATOM   6563  C CZ2 . TRP D  2 21  ? 38.990  67.515 22.094  1.00 27.88  ? 21   TRP D CZ2 1 
ATOM   6564  C CZ3 . TRP D  2 21  ? 36.687  67.707 21.355  1.00 27.20  ? 21   TRP D CZ3 1 
ATOM   6565  C CH2 . TRP D  2 21  ? 37.653  67.663 22.377  1.00 27.66  ? 21   TRP D CH2 1 
ATOM   6566  N N   . TYR D  2 22  ? 38.307  67.268 13.925  1.00 25.21  ? 22   TYR D N   1 
ATOM   6567  C CA  . TYR D  2 22  ? 38.043  66.564 12.676  1.00 24.10  ? 22   TYR D CA  1 
ATOM   6568  C C   . TYR D  2 22  ? 37.930  67.573 11.545  1.00 25.23  ? 22   TYR D C   1 
ATOM   6569  O O   . TYR D  2 22  ? 37.488  68.705 11.752  1.00 26.66  ? 22   TYR D O   1 
ATOM   6570  C CB  . TYR D  2 22  ? 36.745  65.758 12.764  1.00 22.93  ? 22   TYR D CB  1 
ATOM   6571  C CG  . TYR D  2 22  ? 36.375  65.308 14.156  1.00 22.46  ? 22   TYR D CG  1 
ATOM   6572  C CD1 . TYR D  2 22  ? 37.079  64.294 14.789  1.00 21.57  ? 22   TYR D CD1 1 
ATOM   6573  C CD2 . TYR D  2 22  ? 35.318  65.898 14.838  1.00 23.15  ? 22   TYR D CD2 1 
ATOM   6574  C CE1 . TYR D  2 22  ? 36.738  63.875 16.064  1.00 21.20  ? 22   TYR D CE1 1 
ATOM   6575  C CE2 . TYR D  2 22  ? 34.973  65.490 16.110  1.00 22.84  ? 22   TYR D CE2 1 
ATOM   6576  C CZ  . TYR D  2 22  ? 35.685  64.480 16.717  1.00 21.75  ? 22   TYR D CZ  1 
ATOM   6577  O OH  . TYR D  2 22  ? 35.342  64.074 17.978  1.00 21.49  ? 22   TYR D OH  1 
ATOM   6578  N N   . GLY D  2 23  ? 38.316  67.157 10.346  1.00 24.83  ? 23   GLY D N   1 
ATOM   6579  C CA  . GLY D  2 23  ? 38.211  68.028 9.192   1.00 25.86  ? 23   GLY D CA  1 
ATOM   6580  C C   . GLY D  2 23  ? 38.651  67.384 7.900   1.00 25.28  ? 23   GLY D C   1 
ATOM   6581  O O   . GLY D  2 23  ? 38.699  66.158 7.787   1.00 24.02  ? 23   GLY D O   1 
ATOM   6582  N N   . TYR D  2 24  ? 38.988  68.236 6.933   1.00 26.50  ? 24   TYR D N   1 
ATOM   6583  C CA  . TYR D  2 24  ? 39.276  67.816 5.565   1.00 26.23  ? 24   TYR D CA  1 
ATOM   6584  C C   . TYR D  2 24  ? 40.662  68.254 5.126   1.00 27.53  ? 24   TYR D C   1 
ATOM   6585  O O   . TYR D  2 24  ? 41.175  69.265 5.589   1.00 29.11  ? 24   TYR D O   1 
ATOM   6586  C CB  . TYR D  2 24  ? 38.262  68.430 4.599   1.00 26.61  ? 24   TYR D CB  1 
ATOM   6587  C CG  . TYR D  2 24  ? 36.833  68.396 5.079   1.00 26.42  ? 24   TYR D CG  1 
ATOM   6588  C CD1 . TYR D  2 24  ? 36.371  69.323 6.000   1.00 27.61  ? 24   TYR D CD1 1 
ATOM   6589  C CD2 . TYR D  2 24  ? 35.936  67.447 4.597   1.00 25.48  ? 24   TYR D CD2 1 
ATOM   6590  C CE1 . TYR D  2 24  ? 35.060  69.306 6.440   1.00 27.83  ? 24   TYR D CE1 1 
ATOM   6591  C CE2 . TYR D  2 24  ? 34.619  67.420 5.031   1.00 25.75  ? 24   TYR D CE2 1 
ATOM   6592  C CZ  . TYR D  2 24  ? 34.187  68.353 5.953   1.00 26.91  ? 24   TYR D CZ  1 
ATOM   6593  O OH  . TYR D  2 24  ? 32.882  68.343 6.392   1.00 27.59  ? 24   TYR D OH  1 
ATOM   6594  N N   . HIS D  2 25  ? 41.259  67.478 4.228   1.00 27.27  ? 25   HIS D N   1 
ATOM   6595  C CA  . HIS D  2 25  ? 42.446  67.907 3.510   1.00 28.84  ? 25   HIS D CA  1 
ATOM   6596  C C   . HIS D  2 25  ? 42.215  67.752 2.018   1.00 28.62  ? 25   HIS D C   1 
ATOM   6597  O O   . HIS D  2 25  ? 41.944  66.651 1.541   1.00 27.54  ? 25   HIS D O   1 
ATOM   6598  C CB  . HIS D  2 25  ? 43.677  67.110 3.915   1.00 29.35  ? 25   HIS D CB  1 
ATOM   6599  C CG  . HIS D  2 25  ? 44.936  67.613 3.282   1.00 31.48  ? 25   HIS D CG  1 
ATOM   6600  N ND1 . HIS D  2 25  ? 45.450  67.079 2.119   1.00 31.70  ? 25   HIS D ND1 1 
ATOM   6601  C CD2 . HIS D  2 25  ? 45.771  68.618 3.635   1.00 33.69  ? 25   HIS D CD2 1 
ATOM   6602  C CE1 . HIS D  2 25  ? 46.557  67.721 1.794   1.00 33.95  ? 25   HIS D CE1 1 
ATOM   6603  N NE2 . HIS D  2 25  ? 46.775  68.659 2.699   1.00 35.28  ? 25   HIS D NE2 1 
ATOM   6604  N N   . HIS D  2 26  ? 42.338  68.859 1.291   1.00 30.02  ? 26   HIS D N   1 
ATOM   6605  C CA  . HIS D  2 26  ? 42.139  68.873 -0.155  1.00 30.01  ? 26   HIS D CA  1 
ATOM   6606  C C   . HIS D  2 26  ? 43.475  69.023 -0.867  1.00 31.55  ? 26   HIS D C   1 
ATOM   6607  O O   . HIS D  2 26  ? 44.409  69.582 -0.311  1.00 33.19  ? 26   HIS D O   1 
ATOM   6608  C CB  . HIS D  2 26  ? 41.198  70.017 -0.548  1.00 30.62  ? 26   HIS D CB  1 
ATOM   6609  C CG  . HIS D  2 26  ? 41.827  71.376 -0.478  1.00 32.87  ? 26   HIS D CG  1 
ATOM   6610  N ND1 . HIS D  2 26  ? 41.809  72.149 0.663   1.00 34.06  ? 26   HIS D ND1 1 
ATOM   6611  C CD2 . HIS D  2 26  ? 42.486  72.101 -1.413  1.00 34.47  ? 26   HIS D CD2 1 
ATOM   6612  C CE1 . HIS D  2 26  ? 42.434  73.290 0.430   1.00 36.44  ? 26   HIS D CE1 1 
ATOM   6613  N NE2 . HIS D  2 26  ? 42.855  73.285 -0.822  1.00 36.72  ? 26   HIS D NE2 1 
ATOM   6614  N N   . SER D  2 27  ? 43.565  68.500 -2.086  1.00 31.35  ? 27   SER D N   1 
ATOM   6615  C CA  . SER D  2 27  ? 44.708  68.770 -2.966  1.00 33.09  ? 27   SER D CA  1 
ATOM   6616  C C   . SER D  2 27  ? 44.246  68.820 -4.425  1.00 32.85  ? 27   SER D C   1 
ATOM   6617  O O   . SER D  2 27  ? 43.567  67.909 -4.901  1.00 31.41  ? 27   SER D O   1 
ATOM   6618  C CB  . SER D  2 27  ? 45.814  67.729 -2.781  1.00 33.64  ? 27   SER D CB  1 
ATOM   6619  O OG  . SER D  2 27  ? 45.435  66.472 -3.305  1.00 32.37  ? 27   SER D OG  1 
ATOM   6620  N N   . ASN D  2 28  ? 44.597  69.905 -5.112  1.00 34.53  ? 28   ASN D N   1 
ATOM   6621  C CA  . ASN D  2 28  ? 44.222  70.117 -6.510  1.00 34.57  ? 28   ASN D CA  1 
ATOM   6622  C C   . ASN D  2 28  ? 45.284  70.970 -7.214  1.00 36.98  ? 28   ASN D C   1 
ATOM   6623  O O   . ASN D  2 28  ? 46.359  71.190 -6.660  1.00 38.66  ? 28   ASN D O   1 
ATOM   6624  C CB  . ASN D  2 28  ? 42.818  70.741 -6.595  1.00 33.84  ? 28   ASN D CB  1 
ATOM   6625  C CG  . ASN D  2 28  ? 42.719  72.088 -5.905  1.00 35.33  ? 28   ASN D CG  1 
ATOM   6626  O OD1 . ASN D  2 28  ? 43.725  72.723 -5.606  1.00 37.15  ? 28   ASN D OD1 1 
ATOM   6627  N ND2 . ASN D  2 28  ? 41.494  72.530 -5.648  1.00 34.96  ? 28   ASN D ND2 1 
ATOM   6628  N N   . GLU D  2 29  ? 45.001  71.434 -8.429  1.00 37.46  ? 29   GLU D N   1 
ATOM   6629  C CA  . GLU D  2 29  ? 45.977  72.224 -9.185  1.00 39.89  ? 29   GLU D CA  1 
ATOM   6630  C C   . GLU D  2 29  ? 46.373  73.521 -8.475  1.00 42.11  ? 29   GLU D C   1 
ATOM   6631  O O   . GLU D  2 29  ? 47.519  73.955 -8.569  1.00 44.51  ? 29   GLU D O   1 
ATOM   6632  C CB  . GLU D  2 29  ? 45.445  72.560 -10.582 1.00 39.96  ? 29   GLU D CB  1 
ATOM   6633  C CG  . GLU D  2 29  ? 45.258  71.356 -11.497 1.00 38.58  ? 29   GLU D CG  1 
ATOM   6634  C CD  . GLU D  2 29  ? 45.085  71.744 -12.963 1.00 39.14  ? 29   GLU D CD  1 
ATOM   6635  O OE1 . GLU D  2 29  ? 44.851  72.941 -13.264 1.00 40.35  ? 29   GLU D OE1 1 
ATOM   6636  O OE2 . GLU D  2 29  ? 45.176  70.840 -13.822 1.00 38.60  ? 29   GLU D OE2 1 
ATOM   6637  N N   . GLN D  2 30  ? 45.420  74.133 -7.774  1.00 41.67  ? 30   GLN D N   1 
ATOM   6638  C CA  . GLN D  2 30  ? 45.650  75.403 -7.073  1.00 44.06  ? 30   GLN D CA  1 
ATOM   6639  C C   . GLN D  2 30  ? 46.473  75.251 -5.792  1.00 44.85  ? 30   GLN D C   1 
ATOM   6640  O O   . GLN D  2 30  ? 47.161  76.182 -5.386  1.00 47.71  ? 30   GLN D O   1 
ATOM   6641  C CB  . GLN D  2 30  ? 44.312  76.067 -6.746  1.00 43.76  ? 30   GLN D CB  1 
ATOM   6642  C CG  . GLN D  2 30  ? 43.546  76.536 -7.976  1.00 43.89  ? 30   GLN D CG  1 
ATOM   6643  C CD  . GLN D  2 30  ? 42.094  76.088 -7.960  1.00 41.87  ? 30   GLN D CD  1 
ATOM   6644  O OE1 . GLN D  2 30  ? 41.777  74.953 -8.344  1.00 39.69  ? 30   GLN D OE1 1 
ATOM   6645  N NE2 . GLN D  2 30  ? 41.201  76.976 -7.518  1.00 43.05  ? 30   GLN D NE2 1 
ATOM   6646  N N   . GLY D  2 31  ? 46.393  74.088 -5.151  1.00 42.56  ? 31   GLY D N   1 
ATOM   6647  C CA  . GLY D  2 31  ? 47.157  73.831 -3.930  1.00 43.23  ? 31   GLY D CA  1 
ATOM   6648  C C   . GLY D  2 31  ? 46.527  72.780 -3.041  1.00 40.45  ? 31   GLY D C   1 
ATOM   6649  O O   . GLY D  2 31  ? 45.672  72.017 -3.478  1.00 38.05  ? 31   GLY D O   1 
ATOM   6650  N N   . SER D  2 32  ? 46.963  72.745 -1.786  1.00 41.01  ? 32   SER D N   1 
ATOM   6651  C CA  . SER D  2 32  ? 46.421  71.824 -0.794  1.00 38.71  ? 32   SER D CA  1 
ATOM   6652  C C   . SER D  2 32  ? 46.299  72.501 0.563   1.00 39.59  ? 32   SER D C   1 
ATOM   6653  O O   . SER D  2 32  ? 46.943  73.517 0.811   1.00 42.35  ? 32   SER D O   1 
ATOM   6654  C CB  . SER D  2 32  ? 47.315  70.594 -0.679  1.00 38.43  ? 32   SER D CB  1 
ATOM   6655  O OG  . SER D  2 32  ? 48.656  70.963 -0.445  1.00 41.31  ? 32   SER D OG  1 
ATOM   6656  N N   . GLY D  2 33  ? 45.474  71.938 1.442   1.00 37.51  ? 33   GLY D N   1 
ATOM   6657  C CA  . GLY D  2 33  ? 45.298  72.507 2.775   1.00 38.30  ? 33   GLY D CA  1 
ATOM   6658  C C   . GLY D  2 33  ? 44.305  71.813 3.689   1.00 35.93  ? 33   GLY D C   1 
ATOM   6659  O O   . GLY D  2 33  ? 43.449  71.050 3.242   1.00 33.71  ? 33   GLY D O   1 
ATOM   6660  N N   . TYR D  2 34  ? 44.427  72.107 4.981   1.00 36.71  ? 34   TYR D N   1 
ATOM   6661  C CA  . TYR D  2 34  ? 43.550  71.563 6.008   1.00 34.89  ? 34   TYR D CA  1 
ATOM   6662  C C   . TYR D  2 34  ? 42.443  72.546 6.356   1.00 35.52  ? 34   TYR D C   1 
ATOM   6663  O O   . TYR D  2 34  ? 42.690  73.735 6.509   1.00 38.07  ? 34   TYR D O   1 
ATOM   6664  C CB  . TYR D  2 34  ? 44.346  71.253 7.272   1.00 35.53  ? 34   TYR D CB  1 
ATOM   6665  C CG  . TYR D  2 34  ? 45.474  70.267 7.069   1.00 35.48  ? 34   TYR D CG  1 
ATOM   6666  C CD1 . TYR D  2 34  ? 45.248  68.896 7.136   1.00 33.24  ? 34   TYR D CD1 1 
ATOM   6667  C CD2 . TYR D  2 34  ? 46.772  70.705 6.816   1.00 38.11  ? 34   TYR D CD2 1 
ATOM   6668  C CE1 . TYR D  2 34  ? 46.282  67.993 6.954   1.00 33.67  ? 34   TYR D CE1 1 
ATOM   6669  C CE2 . TYR D  2 34  ? 47.810  69.805 6.632   1.00 38.55  ? 34   TYR D CE2 1 
ATOM   6670  C CZ  . TYR D  2 34  ? 47.560  68.452 6.708   1.00 36.34  ? 34   TYR D CZ  1 
ATOM   6671  O OH  . TYR D  2 34  ? 48.584  67.553 6.530   1.00 37.26  ? 34   TYR D OH  1 
ATOM   6672  N N   . ALA D  2 35  ? 41.223  72.038 6.478   1.00 33.61  ? 35   ALA D N   1 
ATOM   6673  C CA  . ALA D  2 35  ? 40.093  72.820 6.964   1.00 34.40  ? 35   ALA D CA  1 
ATOM   6674  C C   . ALA D  2 35  ? 39.360  72.009 8.028   1.00 32.76  ? 35   ALA D C   1 
ATOM   6675  O O   . ALA D  2 35  ? 38.888  70.908 7.763   1.00 30.64  ? 35   ALA D O   1 
ATOM   6676  C CB  . ALA D  2 35  ? 39.156  73.159 5.824   1.00 34.40  ? 35   ALA D CB  1 
ATOM   6677  N N   . ALA D  2 36  ? 39.287  72.550 9.239   1.00 34.00  ? 36   ALA D N   1 
ATOM   6678  C CA  . ALA D  2 36  ? 38.568  71.897 10.320  1.00 32.73  ? 36   ALA D CA  1 
ATOM   6679  C C   . ALA D  2 36  ? 37.067  71.980 10.072  1.00 32.54  ? 36   ALA D C   1 
ATOM   6680  O O   . ALA D  2 36  ? 36.562  73.014 9.645   1.00 34.45  ? 36   ALA D O   1 
ATOM   6681  C CB  . ALA D  2 36  ? 38.915  72.542 11.653  1.00 34.42  ? 36   ALA D CB  1 
ATOM   6682  N N   . ASP D  2 37  ? 36.367  70.879 10.330  1.00 30.64  ? 37   ASP D N   1 
ATOM   6683  C CA  . ASP D  2 37  ? 34.910  70.848 10.289  1.00 30.81  ? 37   ASP D CA  1 
ATOM   6684  C C   . ASP D  2 37  ? 34.375  71.368 11.627  1.00 32.15  ? 37   ASP D C   1 
ATOM   6685  O O   . ASP D  2 37  ? 34.473  70.690 12.652  1.00 31.08  ? 37   ASP D O   1 
ATOM   6686  C CB  . ASP D  2 37  ? 34.420  69.424 10.032  1.00 28.64  ? 37   ASP D CB  1 
ATOM   6687  C CG  . ASP D  2 37  ? 32.930  69.358 9.791   1.00 29.22  ? 37   ASP D CG  1 
ATOM   6688  O OD1 . ASP D  2 37  ? 32.508  69.566 8.636   1.00 29.70  ? 37   ASP D OD1 1 
ATOM   6689  O OD2 . ASP D  2 37  ? 32.184  69.094 10.759  1.00 29.38  ? 37   ASP D OD2 1 
ATOM   6690  N N   . LYS D  2 38  ? 33.823  72.580 11.610  1.00 34.76  ? 38   LYS D N   1 
ATOM   6691  C CA  . LYS D  2 38  ? 33.381  73.257 12.836  1.00 36.71  ? 38   LYS D CA  1 
ATOM   6692  C C   . LYS D  2 38  ? 32.249  72.533 13.560  1.00 36.01  ? 38   LYS D C   1 
ATOM   6693  O O   . LYS D  2 38  ? 32.300  72.373 14.778  1.00 35.95  ? 38   LYS D O   1 
ATOM   6694  C CB  . LYS D  2 38  ? 32.951  74.702 12.540  1.00 40.16  ? 38   LYS D CB  1 
ATOM   6695  C CG  . LYS D  2 38  ? 34.106  75.690 12.443  1.00 42.02  ? 38   LYS D CG  1 
ATOM   6696  C CD  . LYS D  2 38  ? 33.623  77.139 12.460  1.00 46.06  ? 38   LYS D CD  1 
ATOM   6697  C CE  . LYS D  2 38  ? 33.184  77.616 11.081  1.00 47.10  ? 38   LYS D CE  1 
ATOM   6698  N NZ  . LYS D  2 38  ? 32.445  78.913 11.148  1.00 51.29  ? 38   LYS D NZ  1 
ATOM   6699  N N   . GLU D  2 39  ? 31.236  72.102 12.807  1.00 35.75  ? 39   GLU D N   1 
ATOM   6700  C CA  . GLU D  2 39  ? 30.045  71.465 13.388  1.00 35.75  ? 39   GLU D CA  1 
ATOM   6701  C C   . GLU D  2 39  ? 30.359  70.192 14.178  1.00 33.12  ? 39   GLU D C   1 
ATOM   6702  O O   . GLU D  2 39  ? 29.972  70.078 15.338  1.00 33.50  ? 39   GLU D O   1 
ATOM   6703  C CB  . GLU D  2 39  ? 29.000  71.159 12.304  1.00 36.28  ? 39   GLU D CB  1 
ATOM   6704  C CG  . GLU D  2 39  ? 28.030  70.030 12.666  1.00 35.69  ? 39   GLU D CG  1 
ATOM   6705  C CD  . GLU D  2 39  ? 26.715  70.105 11.909  1.00 37.77  ? 39   GLU D CD  1 
ATOM   6706  O OE1 . GLU D  2 39  ? 26.725  70.493 10.716  1.00 38.36  ? 39   GLU D OE1 1 
ATOM   6707  O OE2 . GLU D  2 39  ? 25.666  69.783 12.521  1.00 39.12  ? 39   GLU D OE2 1 
ATOM   6708  N N   . SER D  2 40  ? 31.035  69.237 13.551  1.00 30.69  ? 40   SER D N   1 
ATOM   6709  C CA  . SER D  2 40  ? 31.351  67.979 14.224  1.00 28.53  ? 40   SER D CA  1 
ATOM   6710  C C   . SER D  2 40  ? 32.294  68.206 15.405  1.00 28.25  ? 40   SER D C   1 
ATOM   6711  O O   . SER D  2 40  ? 32.163  67.548 16.440  1.00 27.52  ? 40   SER D O   1 
ATOM   6712  C CB  . SER D  2 40  ? 31.945  66.956 13.249  1.00 26.65  ? 40   SER D CB  1 
ATOM   6713  O OG  . SER D  2 40  ? 33.133  67.434 12.645  1.00 26.50  ? 40   SER D OG  1 
ATOM   6714  N N   . THR D  2 41  ? 33.226  69.144 15.251  1.00 29.06  ? 41   THR D N   1 
ATOM   6715  C CA  . THR D  2 41  ? 34.173  69.482 16.312  1.00 29.37  ? 41   THR D CA  1 
ATOM   6716  C C   . THR D  2 41  ? 33.468  70.081 17.532  1.00 30.94  ? 41   THR D C   1 
ATOM   6717  O O   . THR D  2 41  ? 33.714  69.665 18.663  1.00 30.35  ? 41   THR D O   1 
ATOM   6718  C CB  . THR D  2 41  ? 35.250  70.467 15.804  1.00 30.73  ? 41   THR D CB  1 
ATOM   6719  O OG1 . THR D  2 41  ? 35.943  69.888 14.693  1.00 29.37  ? 41   THR D OG1 1 
ATOM   6720  C CG2 . THR D  2 41  ? 36.259  70.796 16.897  1.00 31.58  ? 41   THR D CG2 1 
ATOM   6721  N N   . GLN D  2 42  ? 32.595  71.058 17.299  1.00 33.13  ? 42   GLN D N   1 
ATOM   6722  C CA  . GLN D  2 42  ? 31.887  71.728 18.392  1.00 35.22  ? 42   GLN D CA  1 
ATOM   6723  C C   . GLN D  2 42  ? 30.988  70.756 19.142  1.00 34.09  ? 42   GLN D C   1 
ATOM   6724  O O   . GLN D  2 42  ? 30.865  70.829 20.363  1.00 34.70  ? 42   GLN D O   1 
ATOM   6725  C CB  . GLN D  2 42  ? 31.056  72.902 17.866  1.00 38.24  ? 42   GLN D CB  1 
ATOM   6726  C CG  . GLN D  2 42  ? 30.409  73.749 18.957  1.00 41.18  ? 42   GLN D CG  1 
ATOM   6727  C CD  . GLN D  2 42  ? 31.418  74.302 19.948  1.00 42.11  ? 42   GLN D CD  1 
ATOM   6728  O OE1 . GLN D  2 42  ? 31.331  74.049 21.151  1.00 42.03  ? 42   GLN D OE1 1 
ATOM   6729  N NE2 . GLN D  2 42  ? 32.393  75.050 19.443  1.00 43.19  ? 42   GLN D NE2 1 
ATOM   6730  N N   . LYS D  2 43  ? 30.362  69.853 18.394  1.00 32.70  ? 43   LYS D N   1 
ATOM   6731  C CA  . LYS D  2 43  ? 29.527  68.794 18.969  1.00 31.76  ? 43   LYS D CA  1 
ATOM   6732  C C   . LYS D  2 43  ? 30.341  67.889 19.884  1.00 29.56  ? 43   LYS D C   1 
ATOM   6733  O O   . LYS D  2 43  ? 29.867  67.486 20.947  1.00 29.57  ? 43   LYS D O   1 
ATOM   6734  C CB  . LYS D  2 43  ? 28.904  67.956 17.848  1.00 30.96  ? 43   LYS D CB  1 
ATOM   6735  C CG  . LYS D  2 43  ? 27.441  67.597 18.052  1.00 32.38  ? 43   LYS D CG  1 
ATOM   6736  C CD  . LYS D  2 43  ? 26.674  67.821 16.754  1.00 33.75  ? 43   LYS D CD  1 
ATOM   6737  C CE  . LYS D  2 43  ? 25.392  67.009 16.672  1.00 34.74  ? 43   LYS D CE  1 
ATOM   6738  N NZ  . LYS D  2 43  ? 25.024  66.808 15.240  1.00 35.09  ? 43   LYS D NZ  1 
ATOM   6739  N N   . ALA D  2 44  ? 31.562  67.573 19.457  1.00 27.88  ? 44   ALA D N   1 
ATOM   6740  C CA  . ALA D  2 44  ? 32.476  66.769 20.257  1.00 26.20  ? 44   ALA D CA  1 
ATOM   6741  C C   . ALA D  2 44  ? 32.918  67.519 21.506  1.00 27.32  ? 44   ALA D C   1 
ATOM   6742  O O   . ALA D  2 44  ? 32.999  66.942 22.585  1.00 26.65  ? 44   ALA D O   1 
ATOM   6743  C CB  . ALA D  2 44  ? 33.685  66.356 19.433  1.00 24.92  ? 44   ALA D CB  1 
ATOM   6744  N N   . ILE D  2 45  ? 33.209  68.806 21.354  1.00 29.26  ? 45   ILE D N   1 
ATOM   6745  C CA  . ILE D  2 45  ? 33.602  69.644 22.488  1.00 30.97  ? 45   ILE D CA  1 
ATOM   6746  C C   . ILE D  2 45  ? 32.487  69.723 23.535  1.00 31.96  ? 45   ILE D C   1 
ATOM   6747  O O   . ILE D  2 45  ? 32.753  69.626 24.731  1.00 32.07  ? 45   ILE D O   1 
ATOM   6748  C CB  . ILE D  2 45  ? 34.029  71.056 22.028  1.00 33.52  ? 45   ILE D CB  1 
ATOM   6749  C CG1 . ILE D  2 45  ? 35.450  71.004 21.459  1.00 32.93  ? 45   ILE D CG1 1 
ATOM   6750  C CG2 . ILE D  2 45  ? 33.966  72.056 23.179  1.00 36.22  ? 45   ILE D CG2 1 
ATOM   6751  C CD1 . ILE D  2 45  ? 35.837  72.213 20.635  1.00 35.22  ? 45   ILE D CD1 1 
ATOM   6752  N N   . ASP D  2 46  ? 31.248  69.883 23.080  1.00 32.88  ? 46   ASP D N   1 
ATOM   6753  C CA  . ASP D  2 46  ? 30.102  69.933 23.985  1.00 34.22  ? 46   ASP D CA  1 
ATOM   6754  C C   . ASP D  2 46  ? 29.916  68.614 24.730  1.00 32.07  ? 46   ASP D C   1 
ATOM   6755  O O   . ASP D  2 46  ? 29.726  68.604 25.945  1.00 32.64  ? 46   ASP D O   1 
ATOM   6756  C CB  . ASP D  2 46  ? 28.822  70.285 23.220  1.00 35.98  ? 46   ASP D CB  1 
ATOM   6757  C CG  . ASP D  2 46  ? 28.869  71.674 22.602  1.00 38.71  ? 46   ASP D CG  1 
ATOM   6758  O OD1 . ASP D  2 46  ? 29.767  72.463 22.956  1.00 39.72  ? 46   ASP D OD1 1 
ATOM   6759  O OD2 . ASP D  2 46  ? 28.004  71.977 21.754  1.00 40.13  ? 46   ASP D OD2 1 
ATOM   6760  N N   . GLY D  2 47  ? 29.983  67.507 24.001  1.00 29.85  ? 47   GLY D N   1 
ATOM   6761  C CA  . GLY D  2 47  ? 29.788  66.185 24.585  1.00 28.12  ? 47   GLY D CA  1 
ATOM   6762  C C   . GLY D  2 47  ? 30.795  65.842 25.669  1.00 27.04  ? 47   GLY D C   1 
ATOM   6763  O O   . GLY D  2 47  ? 30.428  65.328 26.727  1.00 26.88  ? 47   GLY D O   1 
ATOM   6764  N N   . VAL D  2 48  ? 32.066  66.140 25.404  1.00 26.59  ? 48   VAL D N   1 
ATOM   6765  C CA  . VAL D  2 48  ? 33.152  65.866 26.344  1.00 25.95  ? 48   VAL D CA  1 
ATOM   6766  C C   . VAL D  2 48  ? 33.122  66.817 27.543  1.00 27.89  ? 48   VAL D C   1 
ATOM   6767  O O   . VAL D  2 48  ? 33.426  66.412 28.661  1.00 27.54  ? 48   VAL D O   1 
ATOM   6768  C CB  . VAL D  2 48  ? 34.523  65.924 25.632  1.00 25.44  ? 48   VAL D CB  1 
ATOM   6769  C CG1 . VAL D  2 48  ? 35.674  65.939 26.631  1.00 25.69  ? 48   VAL D CG1 1 
ATOM   6770  C CG2 . VAL D  2 48  ? 34.661  64.742 24.674  1.00 23.54  ? 48   VAL D CG2 1 
ATOM   6771  N N   . THR D  2 49  ? 32.750  68.071 27.316  1.00 30.21  ? 49   THR D N   1 
ATOM   6772  C CA  . THR D  2 49  ? 32.619  69.028 28.407  1.00 32.63  ? 49   THR D CA  1 
ATOM   6773  C C   . THR D  2 49  ? 31.549  68.565 29.394  1.00 32.80  ? 49   THR D C   1 
ATOM   6774  O O   . THR D  2 49  ? 31.808  68.464 30.597  1.00 32.98  ? 49   THR D O   1 
ATOM   6775  C CB  . THR D  2 49  ? 32.272  70.434 27.885  1.00 35.53  ? 49   THR D CB  1 
ATOM   6776  O OG1 . THR D  2 49  ? 33.338  70.908 27.056  1.00 35.72  ? 49   THR D OG1 1 
ATOM   6777  C CG2 . THR D  2 49  ? 32.059  71.408 29.034  1.00 38.46  ? 49   THR D CG2 1 
ATOM   6778  N N   . ASN D  2 50  ? 30.358  68.270 28.874  1.00 32.99  ? 50   ASN D N   1 
ATOM   6779  C CA  . ASN D  2 50  ? 29.238  67.798 29.699  1.00 33.53  ? 50   ASN D CA  1 
ATOM   6780  C C   . ASN D  2 50  ? 29.604  66.552 30.487  1.00 31.30  ? 50   ASN D C   1 
ATOM   6781  O O   . ASN D  2 50  ? 29.261  66.424 31.658  1.00 31.86  ? 50   ASN D O   1 
ATOM   6782  C CB  . ASN D  2 50  ? 28.022  67.488 28.827  1.00 33.97  ? 50   ASN D CB  1 
ATOM   6783  C CG  . ASN D  2 50  ? 27.407  68.730 28.215  1.00 36.88  ? 50   ASN D CG  1 
ATOM   6784  O OD1 . ASN D  2 50  ? 27.154  69.709 28.904  1.00 39.53  ? 50   ASN D OD1 1 
ATOM   6785  N ND2 . ASN D  2 50  ? 27.157  68.691 26.915  1.00 36.68  ? 50   ASN D ND2 1 
ATOM   6786  N N   . LYS D  2 51  ? 30.302  65.641 29.820  1.00 29.09  ? 51   LYS D N   1 
ATOM   6787  C CA  . LYS D  2 51  ? 30.768  64.393 30.419  1.00 27.18  ? 51   LYS D CA  1 
ATOM   6788  C C   . LYS D  2 51  ? 31.668  64.620 31.628  1.00 27.44  ? 51   LYS D C   1 
ATOM   6789  O O   . LYS D  2 51  ? 31.511  63.973 32.661  1.00 26.98  ? 51   LYS D O   1 
ATOM   6790  C CB  . LYS D  2 51  ? 31.536  63.603 29.369  1.00 25.30  ? 51   LYS D CB  1 
ATOM   6791  C CG  . LYS D  2 51  ? 32.248  62.368 29.879  1.00 23.60  ? 51   LYS D CG  1 
ATOM   6792  C CD  . LYS D  2 51  ? 32.973  61.705 28.722  1.00 22.36  ? 51   LYS D CD  1 
ATOM   6793  C CE  . LYS D  2 51  ? 32.598  60.250 28.589  1.00 21.28  ? 51   LYS D CE  1 
ATOM   6794  N NZ  . LYS D  2 51  ? 32.759  59.754 27.206  1.00 20.71  ? 51   LYS D NZ  1 
ATOM   6795  N N   . VAL D  2 52  ? 32.625  65.525 31.481  1.00 28.46  ? 52   VAL D N   1 
ATOM   6796  C CA  . VAL D  2 52  ? 33.544  65.842 32.561  1.00 29.23  ? 52   VAL D CA  1 
ATOM   6797  C C   . VAL D  2 52  ? 32.782  66.452 33.741  1.00 31.22  ? 52   VAL D C   1 
ATOM   6798  O O   . VAL D  2 52  ? 33.012  66.072 34.891  1.00 31.02  ? 52   VAL D O   1 
ATOM   6799  C CB  . VAL D  2 52  ? 34.668  66.784 32.070  1.00 30.46  ? 52   VAL D CB  1 
ATOM   6800  C CG1 . VAL D  2 52  ? 35.486  67.329 33.237  1.00 32.02  ? 52   VAL D CG1 1 
ATOM   6801  C CG2 . VAL D  2 52  ? 35.573  66.049 31.088  1.00 28.74  ? 52   VAL D CG2 1 
ATOM   6802  N N   . ASN D  2 53  ? 31.870  67.379 33.451  1.00 33.45  ? 53   ASN D N   1 
ATOM   6803  C CA  . ASN D  2 53  ? 31.044  68.007 34.491  1.00 35.92  ? 53   ASN D CA  1 
ATOM   6804  C C   . ASN D  2 53  ? 30.092  67.004 35.138  1.00 35.05  ? 53   ASN D C   1 
ATOM   6805  O O   . ASN D  2 53  ? 29.901  67.016 36.352  1.00 35.80  ? 53   ASN D O   1 
ATOM   6806  C CB  . ASN D  2 53  ? 30.238  69.179 33.923  1.00 38.76  ? 53   ASN D CB  1 
ATOM   6807  C CG  . ASN D  2 53  ? 31.115  70.260 33.315  1.00 40.30  ? 53   ASN D CG  1 
ATOM   6808  O OD1 . ASN D  2 53  ? 32.299  70.368 33.633  1.00 40.12  ? 53   ASN D OD1 1 
ATOM   6809  N ND2 . ASN D  2 53  ? 30.535  71.066 32.433  1.00 42.18  ? 53   ASN D ND2 1 
ATOM   6810  N N   . SER D  2 54  ? 29.497  66.141 34.315  1.00 33.77  ? 54   SER D N   1 
ATOM   6811  C CA  . SER D  2 54  ? 28.631  65.072 34.810  1.00 33.15  ? 54   SER D CA  1 
ATOM   6812  C C   . SER D  2 54  ? 29.392  64.182 35.772  1.00 31.54  ? 54   SER D C   1 
ATOM   6813  O O   . SER D  2 54  ? 28.898  63.865 36.855  1.00 32.00  ? 54   SER D O   1 
ATOM   6814  C CB  . SER D  2 54  ? 28.085  64.223 33.656  1.00 31.96  ? 54   SER D CB  1 
ATOM   6815  O OG  . SER D  2 54  ? 26.995  64.865 33.025  1.00 34.07  ? 54   SER D OG  1 
ATOM   6816  N N   . ILE D  2 55  ? 30.594  63.786 35.358  1.00 30.04  ? 55   ILE D N   1 
ATOM   6817  C CA  . ILE D  2 55  ? 31.475  62.952 36.173  1.00 28.81  ? 55   ILE D CA  1 
ATOM   6818  C C   . ILE D  2 55  ? 31.799  63.626 37.504  1.00 30.39  ? 55   ILE D C   1 
ATOM   6819  O O   . ILE D  2 55  ? 31.682  63.005 38.558  1.00 30.07  ? 55   ILE D O   1 
ATOM   6820  C CB  . ILE D  2 55  ? 32.773  62.595 35.405  1.00 27.43  ? 55   ILE D CB  1 
ATOM   6821  C CG1 . ILE D  2 55  ? 32.493  61.434 34.445  1.00 25.84  ? 55   ILE D CG1 1 
ATOM   6822  C CG2 . ILE D  2 55  ? 33.896  62.209 36.361  1.00 27.02  ? 55   ILE D CG2 1 
ATOM   6823  C CD1 . ILE D  2 55  ? 33.559  61.199 33.394  1.00 24.94  ? 55   ILE D CD1 1 
ATOM   6824  N N   . ILE D  2 56  ? 32.196  64.894 37.452  1.00 32.49  ? 56   ILE D N   1 
ATOM   6825  C CA  . ILE D  2 56  ? 32.526  65.645 38.662  1.00 34.50  ? 56   ILE D CA  1 
ATOM   6826  C C   . ILE D  2 56  ? 31.324  65.705 39.612  1.00 35.96  ? 56   ILE D C   1 
ATOM   6827  O O   . ILE D  2 56  ? 31.449  65.377 40.796  1.00 35.96  ? 56   ILE D O   1 
ATOM   6828  C CB  . ILE D  2 56  ? 33.004  67.076 38.319  1.00 36.92  ? 56   ILE D CB  1 
ATOM   6829  C CG1 . ILE D  2 56  ? 34.374  67.026 37.628  1.00 36.14  ? 56   ILE D CG1 1 
ATOM   6830  C CG2 . ILE D  2 56  ? 33.080  67.945 39.572  1.00 39.51  ? 56   ILE D CG2 1 
ATOM   6831  C CD1 . ILE D  2 56  ? 34.736  68.297 36.883  1.00 38.34  ? 56   ILE D CD1 1 
ATOM   6832  N N   . ASP D  2 57  ? 30.167  66.112 39.086  1.00 37.55  ? 57   ASP D N   1 
ATOM   6833  C CA  . ASP D  2 57  ? 28.952  66.297 39.900  1.00 39.63  ? 57   ASP D CA  1 
ATOM   6834  C C   . ASP D  2 57  ? 28.490  65.030 40.617  1.00 38.23  ? 57   ASP D C   1 
ATOM   6835  O O   . ASP D  2 57  ? 28.056  65.084 41.762  1.00 39.46  ? 57   ASP D O   1 
ATOM   6836  C CB  . ASP D  2 57  ? 27.806  66.844 39.045  1.00 41.52  ? 57   ASP D CB  1 
ATOM   6837  C CG  . ASP D  2 57  ? 27.889  68.346 38.858  1.00 44.69  ? 57   ASP D CG  1 
ATOM   6838  O OD1 . ASP D  2 57  ? 27.934  69.067 39.886  1.00 47.07  ? 57   ASP D OD1 1 
ATOM   6839  O OD2 . ASP D  2 57  ? 27.899  68.808 37.689  1.00 45.10  ? 57   ASP D OD2 1 
ATOM   6840  N N   . LYS D  2 58  ? 28.577  63.891 39.942  1.00 36.08  ? 58   LYS D N   1 
ATOM   6841  C CA  . LYS D  2 58  ? 28.191  62.623 40.558  1.00 34.96  ? 58   LYS D CA  1 
ATOM   6842  C C   . LYS D  2 58  ? 29.082  62.256 41.740  1.00 34.35  ? 58   LYS D C   1 
ATOM   6843  O O   . LYS D  2 58  ? 28.608  61.680 42.720  1.00 34.48  ? 58   LYS D O   1 
ATOM   6844  C CB  . LYS D  2 58  ? 28.152  61.493 39.516  1.00 33.01  ? 58   LYS D CB  1 
ATOM   6845  C CG  . LYS D  2 58  ? 26.742  61.054 39.126  1.00 34.01  ? 58   LYS D CG  1 
ATOM   6846  C CD  . LYS D  2 58  ? 25.748  62.212 39.087  1.00 36.85  ? 58   LYS D CD  1 
ATOM   6847  C CE  . LYS D  2 58  ? 24.359  61.760 38.697  1.00 38.32  ? 58   LYS D CE  1 
ATOM   6848  N NZ  . LYS D  2 58  ? 23.412  62.908 38.722  1.00 41.60  ? 58   LYS D NZ  1 
ATOM   6849  N N   . MET D  2 59  ? 30.358  62.615 41.657  1.00 34.11  ? 59   MET D N   1 
ATOM   6850  C CA  . MET D  2 59  ? 31.304  62.355 42.742  1.00 33.87  ? 59   MET D CA  1 
ATOM   6851  C C   . MET D  2 59  ? 31.254  63.447 43.816  1.00 36.40  ? 59   MET D C   1 
ATOM   6852  O O   . MET D  2 59  ? 31.631  63.201 44.961  1.00 36.45  ? 59   MET D O   1 
ATOM   6853  C CB  . MET D  2 59  ? 32.721  62.232 42.179  1.00 32.83  ? 59   MET D CB  1 
ATOM   6854  C CG  . MET D  2 59  ? 32.843  61.207 41.061  1.00 30.92  ? 59   MET D CG  1 
ATOM   6855  S SD  . MET D  2 59  ? 32.363  59.563 41.612  1.00 29.64  ? 59   MET D SD  1 
ATOM   6856  C CE  . MET D  2 59  ? 33.801  58.990 42.509  1.00 28.93  ? 59   MET D CE  1 
ATOM   6857  N N   . ASN D  2 60  ? 30.780  64.638 43.443  1.00 38.84  ? 60   ASN D N   1 
ATOM   6858  C CA  . ASN D  2 60  ? 30.685  65.788 44.362  1.00 41.93  ? 60   ASN D CA  1 
ATOM   6859  C C   . ASN D  2 60  ? 30.123  65.436 45.748  1.00 42.57  ? 60   ASN D C   1 
ATOM   6860  O O   . ASN D  2 60  ? 30.662  65.871 46.766  1.00 43.73  ? 60   ASN D O   1 
ATOM   6861  C CB  . ASN D  2 60  ? 29.878  66.936 43.717  1.00 44.59  ? 60   ASN D CB  1 
ATOM   6862  C CG  . ASN D  2 60  ? 29.164  67.814 44.739  1.00 48.00  ? 60   ASN D CG  1 
ATOM   6863  O OD1 . ASN D  2 60  ? 28.286  67.345 45.473  1.00 48.30  ? 60   ASN D OD1 1 
ATOM   6864  N ND2 . ASN D  2 60  ? 29.522  69.098 44.780  1.00 50.94  ? 60   ASN D ND2 1 
ATOM   6865  N N   . THR D  2 61  ? 29.042  64.660 45.785  1.00 42.05  ? 61   THR D N   1 
ATOM   6866  C CA  . THR D  2 61  ? 28.476  64.207 47.065  1.00 42.57  ? 61   THR D CA  1 
ATOM   6867  C C   . THR D  2 61  ? 28.889  62.755 47.308  1.00 39.69  ? 61   THR D C   1 
ATOM   6868  O O   . THR D  2 61  ? 28.479  61.841 46.581  1.00 38.21  ? 61   THR D O   1 
ATOM   6869  C CB  . THR D  2 61  ? 26.938  64.418 47.193  1.00 44.80  ? 61   THR D CB  1 
ATOM   6870  O OG1 . THR D  2 61  ? 26.360  63.335 47.935  1.00 44.02  ? 61   THR D OG1 1 
ATOM   6871  C CG2 . THR D  2 61  ? 26.239  64.533 45.831  1.00 45.13  ? 61   THR D CG2 1 
ATOM   6872  N N   . GLN D  2 62  ? 29.718  62.577 48.335  1.00 39.22  ? 62   GLN D N   1 
ATOM   6873  C CA  . GLN D  2 62  ? 30.413  61.321 48.604  1.00 36.77  ? 62   GLN D CA  1 
ATOM   6874  C C   . GLN D  2 62  ? 30.940  61.327 50.048  1.00 37.20  ? 62   GLN D C   1 
ATOM   6875  O O   . GLN D  2 62  ? 31.085  62.394 50.658  1.00 39.38  ? 62   GLN D O   1 
ATOM   6876  C CB  . GLN D  2 62  ? 31.549  61.136 47.585  1.00 35.37  ? 62   GLN D CB  1 
ATOM   6877  C CG  . GLN D  2 62  ? 32.886  60.658 48.146  1.00 34.68  ? 62   GLN D CG  1 
ATOM   6878  C CD  . GLN D  2 62  ? 33.953  60.525 47.077  1.00 33.88  ? 62   GLN D CD  1 
ATOM   6879  O OE1 . GLN D  2 62  ? 33.676  60.676 45.882  1.00 33.61  ? 62   GLN D OE1 1 
ATOM   6880  N NE2 . GLN D  2 62  ? 35.186  60.247 47.503  1.00 33.84  ? 62   GLN D NE2 1 
ATOM   6881  N N   . PHE D  2 63  ? 31.231  60.137 50.575  1.00 35.32  ? 63   PHE D N   1 
ATOM   6882  C CA  . PHE D  2 63  ? 31.610  59.958 51.983  1.00 35.55  ? 63   PHE D CA  1 
ATOM   6883  C C   . PHE D  2 63  ? 32.773  60.851 52.442  1.00 36.73  ? 63   PHE D C   1 
ATOM   6884  O O   . PHE D  2 63  ? 33.757  61.029 51.717  1.00 36.50  ? 63   PHE D O   1 
ATOM   6885  C CB  . PHE D  2 63  ? 31.961  58.488 52.257  1.00 33.56  ? 63   PHE D CB  1 
ATOM   6886  C CG  . PHE D  2 63  ? 32.174  58.185 53.712  1.00 33.89  ? 63   PHE D CG  1 
ATOM   6887  C CD1 . PHE D  2 63  ? 31.089  58.044 54.570  1.00 34.55  ? 63   PHE D CD1 1 
ATOM   6888  C CD2 . PHE D  2 63  ? 33.462  58.059 54.229  1.00 33.80  ? 63   PHE D CD2 1 
ATOM   6889  C CE1 . PHE D  2 63  ? 31.284  57.776 55.916  1.00 34.94  ? 63   PHE D CE1 1 
ATOM   6890  C CE2 . PHE D  2 63  ? 33.661  57.788 55.572  1.00 34.27  ? 63   PHE D CE2 1 
ATOM   6891  C CZ  . PHE D  2 63  ? 32.573  57.648 56.416  1.00 34.69  ? 63   PHE D CZ  1 
ATOM   6892  N N   . GLU D  2 64  ? 32.638  61.406 53.649  1.00 38.22  ? 64   GLU D N   1 
ATOM   6893  C CA  . GLU D  2 64  ? 33.687  62.204 54.278  1.00 39.81  ? 64   GLU D CA  1 
ATOM   6894  C C   . GLU D  2 64  ? 34.036  61.614 55.645  1.00 39.57  ? 64   GLU D C   1 
ATOM   6895  O O   . GLU D  2 64  ? 33.159  61.460 56.505  1.00 40.00  ? 64   GLU D O   1 
ATOM   6896  C CB  . GLU D  2 64  ? 33.224  63.648 54.471  1.00 42.84  ? 64   GLU D CB  1 
ATOM   6897  C CG  . GLU D  2 64  ? 32.759  64.343 53.203  1.00 43.43  ? 64   GLU D CG  1 
ATOM   6898  C CD  . GLU D  2 64  ? 32.294  65.771 53.454  1.00 47.00  ? 64   GLU D CD  1 
ATOM   6899  O OE1 . GLU D  2 64  ? 32.378  66.245 54.611  1.00 49.09  ? 64   GLU D OE1 1 
ATOM   6900  O OE2 . GLU D  2 64  ? 31.838  66.418 52.485  1.00 47.96  ? 64   GLU D OE2 1 
ATOM   6901  N N   . ALA D  2 65  ? 35.315  61.307 55.852  1.00 39.08  ? 65   ALA D N   1 
ATOM   6902  C CA  . ALA D  2 65  ? 35.769  60.730 57.119  1.00 38.95  ? 65   ALA D CA  1 
ATOM   6903  C C   . ALA D  2 65  ? 35.722  61.757 58.248  1.00 41.46  ? 65   ALA D C   1 
ATOM   6904  O O   . ALA D  2 65  ? 35.916  62.955 58.018  1.00 43.65  ? 65   ALA D O   1 
ATOM   6905  C CB  . ALA D  2 65  ? 37.178  60.174 56.975  1.00 38.54  ? 65   ALA D CB  1 
ATOM   6906  N N   . VAL D  2 66  ? 35.452  61.272 59.461  1.00 41.25  ? 66   VAL D N   1 
ATOM   6907  C CA  . VAL D  2 66  ? 35.423  62.114 60.660  1.00 43.72  ? 66   VAL D CA  1 
ATOM   6908  C C   . VAL D  2 66  ? 36.247  61.442 61.761  1.00 43.48  ? 66   VAL D C   1 
ATOM   6909  O O   . VAL D  2 66  ? 36.226  60.213 61.905  1.00 41.34  ? 66   VAL D O   1 
ATOM   6910  C CB  . VAL D  2 66  ? 33.975  62.358 61.152  1.00 44.41  ? 66   VAL D CB  1 
ATOM   6911  C CG1 . VAL D  2 66  ? 33.957  63.259 62.383  1.00 47.53  ? 66   VAL D CG1 1 
ATOM   6912  C CG2 . VAL D  2 66  ? 33.120  62.962 60.043  1.00 44.73  ? 66   VAL D CG2 1 
ATOM   6913  N N   . GLY D  2 67  ? 36.977  62.256 62.522  1.00 45.92  ? 67   GLY D N   1 
ATOM   6914  C CA  . GLY D  2 67  ? 37.805  61.767 63.616  1.00 46.23  ? 67   GLY D CA  1 
ATOM   6915  C C   . GLY D  2 67  ? 36.981  61.455 64.850  1.00 46.01  ? 67   GLY D C   1 
ATOM   6916  O O   . GLY D  2 67  ? 36.298  62.330 65.387  1.00 48.04  ? 67   GLY D O   1 
ATOM   6917  N N   . ARG D  2 68  ? 37.047  60.204 65.297  1.00 43.69  ? 68   ARG D N   1 
ATOM   6918  C CA  . ARG D  2 68  ? 36.334  59.749 66.488  1.00 43.30  ? 68   ARG D CA  1 
ATOM   6919  C C   . ARG D  2 68  ? 37.314  59.028 67.395  1.00 43.24  ? 68   ARG D C   1 
ATOM   6920  O O   . ARG D  2 68  ? 38.108  58.211 66.930  1.00 42.01  ? 68   ARG D O   1 
ATOM   6921  C CB  . ARG D  2 68  ? 35.182  58.817 66.097  1.00 40.78  ? 68   ARG D CB  1 
ATOM   6922  C CG  . ARG D  2 68  ? 33.892  59.557 65.757  1.00 41.48  ? 68   ARG D CG  1 
ATOM   6923  C CD  . ARG D  2 68  ? 32.729  58.663 65.364  1.00 39.54  ? 68   ARG D CD  1 
ATOM   6924  N NE  . ARG D  2 68  ? 32.984  57.930 64.137  1.00 37.31  ? 68   ARG D NE  1 
ATOM   6925  C CZ  . ARG D  2 68  ? 32.754  58.395 62.913  1.00 37.05  ? 68   ARG D CZ  1 
ATOM   6926  N NH1 . ARG D  2 68  ? 32.258  59.607 62.730  1.00 38.95  ? 68   ARG D NH1 1 
ATOM   6927  N NH2 . ARG D  2 68  ? 33.032  57.643 61.861  1.00 35.12  ? 68   ARG D NH2 1 
ATOM   6928  N N   . GLU D  2 69  ? 37.253  59.334 68.686  1.00 44.76  ? 69   GLU D N   1 
ATOM   6929  C CA  . GLU D  2 69  ? 38.210  58.817 69.657  1.00 45.32  ? 69   GLU D CA  1 
ATOM   6930  C C   . GLU D  2 69  ? 37.551  57.783 70.555  1.00 43.57  ? 69   GLU D C   1 
ATOM   6931  O O   . GLU D  2 69  ? 36.416  57.965 70.987  1.00 43.50  ? 69   GLU D O   1 
ATOM   6932  C CB  . GLU D  2 69  ? 38.743  59.964 70.514  1.00 48.97  ? 69   GLU D CB  1 
ATOM   6933  C CG  . GLU D  2 69  ? 39.549  60.999 69.739  1.00 51.19  ? 69   GLU D CG  1 
ATOM   6934  C CD  . GLU D  2 69  ? 41.047  60.767 69.836  1.00 52.65  ? 69   GLU D CD  1 
ATOM   6935  O OE1 . GLU D  2 69  ? 41.491  59.605 69.688  1.00 50.89  ? 69   GLU D OE1 1 
ATOM   6936  O OE2 . GLU D  2 69  ? 41.777  61.752 70.073  1.00 56.07  ? 69   GLU D OE2 1 
ATOM   6937  N N   . PHE D  2 70  ? 38.276  56.704 70.836  1.00 42.41  ? 70   PHE D N   1 
ATOM   6938  C CA  . PHE D  2 70  ? 37.793  55.637 71.709  1.00 41.04  ? 70   PHE D CA  1 
ATOM   6939  C C   . PHE D  2 70  ? 38.872  55.251 72.716  1.00 42.29  ? 70   PHE D C   1 
ATOM   6940  O O   . PHE D  2 70  ? 40.058  55.266 72.395  1.00 43.29  ? 70   PHE D O   1 
ATOM   6941  C CB  . PHE D  2 70  ? 37.397  54.418 70.878  1.00 38.33  ? 70   PHE D CB  1 
ATOM   6942  C CG  . PHE D  2 70  ? 36.468  54.733 69.739  1.00 37.07  ? 70   PHE D CG  1 
ATOM   6943  C CD1 . PHE D  2 70  ? 36.969  55.069 68.490  1.00 36.70  ? 70   PHE D CD1 1 
ATOM   6944  C CD2 . PHE D  2 70  ? 35.094  54.693 69.916  1.00 36.50  ? 70   PHE D CD2 1 
ATOM   6945  C CE1 . PHE D  2 70  ? 36.116  55.356 67.438  1.00 35.67  ? 70   PHE D CE1 1 
ATOM   6946  C CE2 . PHE D  2 70  ? 34.235  54.983 68.868  1.00 35.73  ? 70   PHE D CE2 1 
ATOM   6947  C CZ  . PHE D  2 70  ? 34.747  55.315 67.628  1.00 35.24  ? 70   PHE D CZ  1 
ATOM   6948  N N   . ASN D  2 71  ? 38.464  54.901 73.931  1.00 42.44  ? 71   ASN D N   1 
ATOM   6949  C CA  . ASN D  2 71  ? 39.426  54.526 74.967  1.00 43.82  ? 71   ASN D CA  1 
ATOM   6950  C C   . ASN D  2 71  ? 39.893  53.071 74.813  1.00 42.33  ? 71   ASN D C   1 
ATOM   6951  O O   . ASN D  2 71  ? 39.556  52.401 73.832  1.00 40.31  ? 71   ASN D O   1 
ATOM   6952  C CB  . ASN D  2 71  ? 38.885  54.839 76.378  1.00 45.07  ? 71   ASN D CB  1 
ATOM   6953  C CG  . ASN D  2 71  ? 37.800  53.879 76.837  1.00 43.17  ? 71   ASN D CG  1 
ATOM   6954  O OD1 . ASN D  2 71  ? 37.936  52.663 76.725  1.00 41.69  ? 71   ASN D OD1 1 
ATOM   6955  N ND2 . ASN D  2 71  ? 36.724  54.426 77.392  1.00 43.64  ? 71   ASN D ND2 1 
ATOM   6956  N N   . ASN D  2 72  ? 40.669  52.597 75.788  1.00 43.62  ? 72   ASN D N   1 
ATOM   6957  C CA  . ASN D  2 72  ? 41.351  51.305 75.701  1.00 43.14  ? 72   ASN D CA  1 
ATOM   6958  C C   . ASN D  2 72  ? 40.436  50.080 75.818  1.00 40.94  ? 72   ASN D C   1 
ATOM   6959  O O   . ASN D  2 72  ? 40.804  48.989 75.381  1.00 40.37  ? 72   ASN D O   1 
ATOM   6960  C CB  . ASN D  2 72  ? 42.448  51.233 76.770  1.00 45.75  ? 72   ASN D CB  1 
ATOM   6961  C CG  . ASN D  2 72  ? 43.458  50.138 76.495  1.00 46.33  ? 72   ASN D CG  1 
ATOM   6962  O OD1 . ASN D  2 72  ? 43.961  50.008 75.375  1.00 46.16  ? 72   ASN D OD1 1 
ATOM   6963  N ND2 . ASN D  2 72  ? 43.766  49.343 77.516  1.00 47.26  ? 72   ASN D ND2 1 
ATOM   6964  N N   . LEU D  2 73  ? 39.260  50.257 76.415  1.00 40.12  ? 73   LEU D N   1 
ATOM   6965  C CA  . LEU D  2 73  ? 38.269  49.185 76.514  1.00 38.42  ? 73   LEU D CA  1 
ATOM   6966  C C   . LEU D  2 73  ? 37.059  49.459 75.615  1.00 36.80  ? 73   LEU D C   1 
ATOM   6967  O O   . LEU D  2 73  ? 35.935  49.060 75.923  1.00 36.11  ? 73   LEU D O   1 
ATOM   6968  C CB  . LEU D  2 73  ? 37.847  48.997 77.969  1.00 39.13  ? 73   LEU D CB  1 
ATOM   6969  C CG  . LEU D  2 73  ? 38.923  48.359 78.855  1.00 40.57  ? 73   LEU D CG  1 
ATOM   6970  C CD1 . LEU D  2 73  ? 38.584  48.545 80.328  1.00 41.61  ? 73   LEU D CD1 1 
ATOM   6971  C CD2 . LEU D  2 73  ? 39.101  46.882 78.516  1.00 39.84  ? 73   LEU D CD2 1 
ATOM   6972  N N   . GLU D  2 74  ? 37.317  50.138 74.498  1.00 36.48  ? 74   GLU D N   1 
ATOM   6973  C CA  . GLU D  2 74  ? 36.329  50.363 73.452  1.00 35.09  ? 74   GLU D CA  1 
ATOM   6974  C C   . GLU D  2 74  ? 36.929  49.980 72.102  1.00 34.18  ? 74   GLU D C   1 
ATOM   6975  O O   . GLU D  2 74  ? 36.723  50.666 71.101  1.00 33.69  ? 74   GLU D O   1 
ATOM   6976  C CB  . GLU D  2 74  ? 35.921  51.831 73.434  1.00 35.98  ? 74   GLU D CB  1 
ATOM   6977  C CG  . GLU D  2 74  ? 35.133  52.262 74.647  1.00 37.04  ? 74   GLU D CG  1 
ATOM   6978  C CD  . GLU D  2 74  ? 34.664  53.689 74.531  1.00 38.34  ? 74   GLU D CD  1 
ATOM   6979  O OE1 . GLU D  2 74  ? 35.482  54.557 74.172  1.00 39.43  ? 74   GLU D OE1 1 
ATOM   6980  O OE2 . GLU D  2 74  ? 33.473  53.941 74.786  1.00 38.64  ? 74   GLU D OE2 1 
ATOM   6981  N N   . ARG D  2 75  ? 37.681  48.884 72.087  1.00 34.19  ? 75   ARG D N   1 
ATOM   6982  C CA  . ARG D  2 75  ? 38.439  48.484 70.904  1.00 33.87  ? 75   ARG D CA  1 
ATOM   6983  C C   . ARG D  2 75  ? 37.547  47.948 69.799  1.00 32.19  ? 75   ARG D C   1 
ATOM   6984  O O   . ARG D  2 75  ? 37.851  48.119 68.622  1.00 31.69  ? 75   ARG D O   1 
ATOM   6985  C CB  . ARG D  2 75  ? 39.501  47.440 71.264  1.00 34.99  ? 75   ARG D CB  1 
ATOM   6986  C CG  . ARG D  2 75  ? 40.679  47.994 72.053  1.00 37.12  ? 75   ARG D CG  1 
ATOM   6987  C CD  . ARG D  2 75  ? 41.658  48.719 71.142  1.00 38.06  ? 75   ARG D CD  1 
ATOM   6988  N NE  . ARG D  2 75  ? 42.698  49.429 71.894  1.00 40.57  ? 75   ARG D NE  1 
ATOM   6989  C CZ  . ARG D  2 75  ? 42.786  50.756 72.045  1.00 41.64  ? 75   ARG D CZ  1 
ATOM   6990  N NH1 . ARG D  2 75  ? 41.888  51.579 71.499  1.00 40.39  ? 75   ARG D NH1 1 
ATOM   6991  N NH2 . ARG D  2 75  ? 43.792  51.271 72.756  1.00 44.36  ? 75   ARG D NH2 1 
ATOM   6992  N N   . ARG D  2 76  ? 36.458  47.289 70.176  1.00 31.55  ? 76   ARG D N   1 
ATOM   6993  C CA  . ARG D  2 76  ? 35.525  46.742 69.196  1.00 30.44  ? 76   ARG D CA  1 
ATOM   6994  C C   . ARG D  2 76  ? 34.884  47.840 68.346  1.00 29.79  ? 76   ARG D C   1 
ATOM   6995  O O   . ARG D  2 76  ? 34.866  47.739 67.121  1.00 29.04  ? 76   ARG D O   1 
ATOM   6996  C CB  . ARG D  2 76  ? 34.436  45.927 69.885  1.00 30.46  ? 76   ARG D CB  1 
ATOM   6997  C CG  . ARG D  2 76  ? 34.914  44.611 70.469  1.00 31.15  ? 76   ARG D CG  1 
ATOM   6998  C CD  . ARG D  2 76  ? 33.817  44.000 71.320  1.00 31.48  ? 76   ARG D CD  1 
ATOM   6999  N NE  . ARG D  2 76  ? 33.483  44.870 72.447  1.00 31.81  ? 76   ARG D NE  1 
ATOM   7000  C CZ  . ARG D  2 76  ? 32.325  44.871 73.106  1.00 32.12  ? 76   ARG D CZ  1 
ATOM   7001  N NH1 . ARG D  2 76  ? 31.342  44.041 72.775  1.00 32.25  ? 76   ARG D NH1 1 
ATOM   7002  N NH2 . ARG D  2 76  ? 32.147  45.720 74.110  1.00 32.65  ? 76   ARG D NH2 1 
ATOM   7003  N N   . ILE D  2 77  ? 34.364  48.878 68.999  1.00 30.31  ? 77   ILE D N   1 
ATOM   7004  C CA  . ILE D  2 77  ? 33.736  49.995 68.286  1.00 30.21  ? 77   ILE D CA  1 
ATOM   7005  C C   . ILE D  2 77  ? 34.751  50.889 67.570  1.00 30.46  ? 77   ILE D C   1 
ATOM   7006  O O   . ILE D  2 77  ? 34.424  51.506 66.557  1.00 30.07  ? 77   ILE D O   1 
ATOM   7007  C CB  . ILE D  2 77  ? 32.804  50.844 69.185  1.00 31.22  ? 77   ILE D CB  1 
ATOM   7008  C CG1 . ILE D  2 77  ? 33.564  51.491 70.343  1.00 32.53  ? 77   ILE D CG1 1 
ATOM   7009  C CG2 . ILE D  2 77  ? 31.660  49.988 69.707  1.00 31.21  ? 77   ILE D CG2 1 
ATOM   7010  C CD1 . ILE D  2 77  ? 32.757  52.538 71.085  1.00 33.94  ? 77   ILE D CD1 1 
ATOM   7011  N N   . GLU D  2 78  ? 35.969  50.961 68.093  1.00 31.38  ? 78   GLU D N   1 
ATOM   7012  C CA  . GLU D  2 78  ? 37.058  51.639 67.397  1.00 32.02  ? 78   GLU D CA  1 
ATOM   7013  C C   . GLU D  2 78  ? 37.362  50.922 66.085  1.00 30.93  ? 78   GLU D C   1 
ATOM   7014  O O   . GLU D  2 78  ? 37.612  51.561 65.067  1.00 30.82  ? 78   GLU D O   1 
ATOM   7015  C CB  . GLU D  2 78  ? 38.311  51.683 68.274  1.00 33.67  ? 78   GLU D CB  1 
ATOM   7016  C CG  . GLU D  2 78  ? 39.473  52.476 67.694  1.00 34.98  ? 78   GLU D CG  1 
ATOM   7017  C CD  . GLU D  2 78  ? 40.585  52.686 68.711  1.00 37.28  ? 78   GLU D CD  1 
ATOM   7018  O OE1 . GLU D  2 78  ? 41.088  51.673 69.257  1.00 37.58  ? 78   GLU D OE1 1 
ATOM   7019  O OE2 . GLU D  2 78  ? 40.954  53.858 68.973  1.00 39.11  ? 78   GLU D OE2 1 
ATOM   7020  N N   . ASN D  2 79  ? 37.337  49.596 66.127  1.00 30.43  ? 79   ASN D N   1 
ATOM   7021  C CA  . ASN D  2 79  ? 37.593  48.768 64.956  1.00 29.78  ? 79   ASN D CA  1 
ATOM   7022  C C   . ASN D  2 79  ? 36.440  48.827 63.959  1.00 28.55  ? 79   ASN D C   1 
ATOM   7023  O O   . ASN D  2 79  ? 36.655  48.858 62.750  1.00 28.03  ? 79   ASN D O   1 
ATOM   7024  C CB  . ASN D  2 79  ? 37.825  47.318 65.384  1.00 30.13  ? 79   ASN D CB  1 
ATOM   7025  C CG  . ASN D  2 79  ? 38.260  46.432 64.232  1.00 30.04  ? 79   ASN D CG  1 
ATOM   7026  O OD1 . ASN D  2 79  ? 39.213  46.747 63.526  1.00 30.55  ? 79   ASN D OD1 1 
ATOM   7027  N ND2 . ASN D  2 79  ? 37.578  45.313 64.048  1.00 29.76  ? 79   ASN D ND2 1 
ATOM   7028  N N   . LEU D  2 80  ? 35.218  48.835 64.483  1.00 28.37  ? 80   LEU D N   1 
ATOM   7029  C CA  . LEU D  2 80  ? 34.015  48.984 63.672  1.00 27.75  ? 80   LEU D CA  1 
ATOM   7030  C C   . LEU D  2 80  ? 34.091  50.305 62.932  1.00 27.77  ? 80   LEU D C   1 
ATOM   7031  O O   . LEU D  2 80  ? 33.853  50.371 61.731  1.00 27.12  ? 80   LEU D O   1 
ATOM   7032  C CB  . LEU D  2 80  ? 32.770  48.954 64.568  1.00 28.16  ? 80   LEU D CB  1 
ATOM   7033  C CG  . LEU D  2 80  ? 31.382  48.772 63.944  1.00 28.06  ? 80   LEU D CG  1 
ATOM   7034  C CD1 . LEU D  2 80  ? 30.357  48.515 65.040  1.00 28.95  ? 80   LEU D CD1 1 
ATOM   7035  C CD2 . LEU D  2 80  ? 30.959  49.972 63.116  1.00 28.06  ? 80   LEU D CD2 1 
ATOM   7036  N N   . ASN D  2 81  ? 34.431  51.354 63.669  1.00 28.80  ? 81   ASN D N   1 
ATOM   7037  C CA  . ASN D  2 81  ? 34.575  52.683 63.110  1.00 29.39  ? 81   ASN D CA  1 
ATOM   7038  C C   . ASN D  2 81  ? 35.618  52.736 61.999  1.00 29.18  ? 81   ASN D C   1 
ATOM   7039  O O   . ASN D  2 81  ? 35.385  53.355 60.969  1.00 28.91  ? 81   ASN D O   1 
ATOM   7040  C CB  . ASN D  2 81  ? 34.952  53.662 64.211  1.00 30.97  ? 81   ASN D CB  1 
ATOM   7041  C CG  . ASN D  2 81  ? 35.084  55.075 63.704  1.00 32.01  ? 81   ASN D CG  1 
ATOM   7042  O OD1 . ASN D  2 81  ? 34.119  55.648 63.215  1.00 32.09  ? 81   ASN D OD1 1 
ATOM   7043  N ND2 . ASN D  2 81  ? 36.271  55.649 63.825  1.00 33.19  ? 81   ASN D ND2 1 
ATOM   7044  N N   . LYS D  2 82  ? 36.759  52.086 62.211  1.00 29.63  ? 82   LYS D N   1 
ATOM   7045  C CA  . LYS D  2 82  ? 37.827  52.069 61.215  1.00 29.88  ? 82   LYS D CA  1 
ATOM   7046  C C   . LYS D  2 82  ? 37.374  51.370 59.946  1.00 28.65  ? 82   LYS D C   1 
ATOM   7047  O O   . LYS D  2 82  ? 37.581  51.883 58.853  1.00 28.42  ? 82   LYS D O   1 
ATOM   7048  C CB  . LYS D  2 82  ? 39.094  51.387 61.749  1.00 30.97  ? 82   LYS D CB  1 
ATOM   7049  C CG  . LYS D  2 82  ? 40.167  51.187 60.677  1.00 31.39  ? 82   LYS D CG  1 
ATOM   7050  C CD  . LYS D  2 82  ? 41.560  50.941 61.252  1.00 33.39  ? 82   LYS D CD  1 
ATOM   7051  C CE  . LYS D  2 82  ? 41.893  49.455 61.375  1.00 33.57  ? 82   LYS D CE  1 
ATOM   7052  N NZ  . LYS D  2 82  ? 43.203  49.225 62.060  1.00 35.91  ? 82   LYS D NZ  1 
ATOM   7053  N N   . LYS D  2 83  ? 36.760  50.202 60.101  1.00 28.21  ? 83   LYS D N   1 
ATOM   7054  C CA  . LYS D  2 83  ? 36.296  49.419 58.951  1.00 27.48  ? 83   LYS D CA  1 
ATOM   7055  C C   . LYS D  2 83  ? 35.213  50.139 58.166  1.00 26.86  ? 83   LYS D C   1 
ATOM   7056  O O   . LYS D  2 83  ? 35.195  50.088 56.943  1.00 26.31  ? 83   LYS D O   1 
ATOM   7057  C CB  . LYS D  2 83  ? 35.815  48.029 59.395  1.00 27.60  ? 83   LYS D CB  1 
ATOM   7058  C CG  . LYS D  2 83  ? 36.894  46.950 59.344  1.00 28.43  ? 83   LYS D CG  1 
ATOM   7059  C CD  . LYS D  2 83  ? 38.261  47.447 59.819  1.00 29.49  ? 83   LYS D CD  1 
ATOM   7060  C CE  . LYS D  2 83  ? 39.374  46.443 59.546  1.00 30.69  ? 83   LYS D CE  1 
ATOM   7061  N NZ  . LYS D  2 83  ? 39.684  45.623 60.753  1.00 31.84  ? 83   LYS D NZ  1 
ATOM   7062  N N   . MET D  2 84  ? 34.326  50.820 58.876  1.00 27.27  ? 84   MET D N   1 
ATOM   7063  C CA  . MET D  2 84  ? 33.300  51.623 58.240  1.00 27.26  ? 84   MET D CA  1 
ATOM   7064  C C   . MET D  2 84  ? 33.934  52.718 57.383  1.00 27.40  ? 84   MET D C   1 
ATOM   7065  O O   . MET D  2 84  ? 33.597  52.852 56.206  1.00 26.83  ? 84   MET D O   1 
ATOM   7066  C CB  . MET D  2 84  ? 32.385  52.242 59.292  1.00 28.22  ? 84   MET D CB  1 
ATOM   7067  C CG  . MET D  2 84  ? 31.050  52.715 58.747  1.00 28.64  ? 84   MET D CG  1 
ATOM   7068  S SD  . MET D  2 84  ? 30.591  54.314 59.427  1.00 30.45  ? 84   MET D SD  1 
ATOM   7069  C CE  . MET D  2 84  ? 31.723  55.340 58.509  1.00 30.43  ? 84   MET D CE  1 
ATOM   7070  N N   . GLU D  2 85  ? 34.863  53.480 57.966  1.00 28.36  ? 85   GLU D N   1 
ATOM   7071  C CA  . GLU D  2 85  ? 35.502  54.594 57.253  1.00 29.00  ? 85   GLU D CA  1 
ATOM   7072  C C   . GLU D  2 85  ? 36.371  54.098 56.089  1.00 28.29  ? 85   GLU D C   1 
ATOM   7073  O O   . GLU D  2 85  ? 36.289  54.631 54.984  1.00 28.04  ? 85   GLU D O   1 
ATOM   7074  C CB  . GLU D  2 85  ? 36.304  55.494 58.207  1.00 30.76  ? 85   GLU D CB  1 
ATOM   7075  C CG  . GLU D  2 85  ? 35.457  56.087 59.334  1.00 31.88  ? 85   GLU D CG  1 
ATOM   7076  C CD  . GLU D  2 85  ? 35.736  57.557 59.630  1.00 34.07  ? 85   GLU D CD  1 
ATOM   7077  O OE1 . GLU D  2 85  ? 36.801  57.878 60.213  1.00 35.48  ? 85   GLU D OE1 1 
ATOM   7078  O OE2 . GLU D  2 85  ? 34.867  58.398 59.307  1.00 34.85  ? 85   GLU D OE2 1 
ATOM   7079  N N   . ASP D  2 86  ? 37.175  53.067 56.330  1.00 28.18  ? 86   ASP D N   1 
ATOM   7080  C CA  . ASP D  2 86  ? 37.966  52.432 55.266  1.00 27.81  ? 86   ASP D CA  1 
ATOM   7081  C C   . ASP D  2 86  ? 37.112  51.820 54.163  1.00 26.49  ? 86   ASP D C   1 
ATOM   7082  O O   . ASP D  2 86  ? 37.473  51.880 52.985  1.00 26.19  ? 86   ASP D O   1 
ATOM   7083  C CB  . ASP D  2 86  ? 38.865  51.331 55.838  1.00 28.48  ? 86   ASP D CB  1 
ATOM   7084  C CG  . ASP D  2 86  ? 40.232  51.833 56.203  1.00 30.20  ? 86   ASP D CG  1 
ATOM   7085  O OD1 . ASP D  2 86  ? 40.840  52.544 55.370  1.00 30.82  ? 86   ASP D OD1 1 
ATOM   7086  O OD2 . ASP D  2 86  ? 40.710  51.508 57.308  1.00 31.28  ? 86   ASP D OD2 1 
ATOM   7087  N N   . GLY D  2 87  ? 36.003  51.206 54.557  1.00 25.92  ? 87   GLY D N   1 
ATOM   7088  C CA  . GLY D  2 87  ? 35.109  50.549 53.618  1.00 25.18  ? 87   GLY D CA  1 
ATOM   7089  C C   . GLY D  2 87  ? 34.522  51.502 52.599  1.00 24.73  ? 87   GLY D C   1 
ATOM   7090  O O   . GLY D  2 87  ? 34.471  51.188 51.408  1.00 24.32  ? 87   GLY D O   1 
ATOM   7091  N N   . PHE D  2 88  ? 34.082  52.669 53.065  1.00 25.08  ? 88   PHE D N   1 
ATOM   7092  C CA  . PHE D  2 88  ? 33.519  53.683 52.178  1.00 25.05  ? 88   PHE D CA  1 
ATOM   7093  C C   . PHE D  2 88  ? 34.579  54.297 51.262  1.00 24.99  ? 88   PHE D C   1 
ATOM   7094  O O   . PHE D  2 88  ? 34.290  54.607 50.109  1.00 24.61  ? 88   PHE D O   1 
ATOM   7095  C CB  . PHE D  2 88  ? 32.811  54.780 52.977  1.00 26.09  ? 88   PHE D CB  1 
ATOM   7096  C CG  . PHE D  2 88  ? 31.444  54.390 53.466  1.00 26.39  ? 88   PHE D CG  1 
ATOM   7097  C CD1 . PHE D  2 88  ? 30.432  54.086 52.568  1.00 26.25  ? 88   PHE D CD1 1 
ATOM   7098  C CD2 . PHE D  2 88  ? 31.165  54.332 54.822  1.00 27.10  ? 88   PHE D CD2 1 
ATOM   7099  C CE1 . PHE D  2 88  ? 29.171  53.727 53.011  1.00 27.06  ? 88   PHE D CE1 1 
ATOM   7100  C CE2 . PHE D  2 88  ? 29.903  53.981 55.273  1.00 27.73  ? 88   PHE D CE2 1 
ATOM   7101  C CZ  . PHE D  2 88  ? 28.905  53.677 54.365  1.00 27.83  ? 88   PHE D CZ  1 
ATOM   7102  N N   . LEU D  2 89  ? 35.799  54.471 51.766  1.00 25.58  ? 89   LEU D N   1 
ATOM   7103  C CA  . LEU D  2 89  ? 36.894  54.958 50.928  1.00 25.94  ? 89   LEU D CA  1 
ATOM   7104  C C   . LEU D  2 89  ? 37.166  54.015 49.759  1.00 25.00  ? 89   LEU D C   1 
ATOM   7105  O O   . LEU D  2 89  ? 37.409  54.466 48.649  1.00 24.83  ? 89   LEU D O   1 
ATOM   7106  C CB  . LEU D  2 89  ? 38.178  55.130 51.732  1.00 27.24  ? 89   LEU D CB  1 
ATOM   7107  C CG  . LEU D  2 89  ? 38.189  56.214 52.811  1.00 28.75  ? 89   LEU D CG  1 
ATOM   7108  C CD1 . LEU D  2 89  ? 39.575  56.263 53.448  1.00 30.30  ? 89   LEU D CD1 1 
ATOM   7109  C CD2 . LEU D  2 89  ? 37.769  57.580 52.264  1.00 29.51  ? 89   LEU D CD2 1 
ATOM   7110  N N   . ASP D  2 90  ? 37.130  52.712 50.024  1.00 24.61  ? 90   ASP D N   1 
ATOM   7111  C CA  . ASP D  2 90  ? 37.349  51.703 48.987  1.00 24.16  ? 90   ASP D CA  1 
ATOM   7112  C C   . ASP D  2 90  ? 36.221  51.696 47.971  1.00 23.24  ? 90   ASP D C   1 
ATOM   7113  O O   . ASP D  2 90  ? 36.464  51.552 46.775  1.00 23.05  ? 90   ASP D O   1 
ATOM   7114  C CB  . ASP D  2 90  ? 37.479  50.308 49.600  1.00 24.49  ? 90   ASP D CB  1 
ATOM   7115  C CG  . ASP D  2 90  ? 38.708  50.165 50.467  1.00 25.67  ? 90   ASP D CG  1 
ATOM   7116  O OD1 . ASP D  2 90  ? 39.655  50.972 50.307  1.00 26.41  ? 90   ASP D OD1 1 
ATOM   7117  O OD2 . ASP D  2 90  ? 38.721  49.244 51.314  1.00 26.15  ? 90   ASP D OD2 1 
ATOM   7118  N N   . VAL D  2 91  ? 34.993  51.844 48.454  1.00 22.99  ? 91   VAL D N   1 
ATOM   7119  C CA  . VAL D  2 91  ? 33.826  51.932 47.581  1.00 22.60  ? 91   VAL D CA  1 
ATOM   7120  C C   . VAL D  2 91  ? 33.935  53.147 46.668  1.00 22.47  ? 91   VAL D C   1 
ATOM   7121  O O   . VAL D  2 91  ? 33.748  53.028 45.456  1.00 22.15  ? 91   VAL D O   1 
ATOM   7122  C CB  . VAL D  2 91  ? 32.510  52.005 48.387  1.00 23.03  ? 91   VAL D CB  1 
ATOM   7123  C CG1 . VAL D  2 91  ? 31.336  52.390 47.497  1.00 23.24  ? 91   VAL D CG1 1 
ATOM   7124  C CG2 . VAL D  2 91  ? 32.233  50.671 49.068  1.00 23.25  ? 91   VAL D CG2 1 
ATOM   7125  N N   . TRP D  2 92  ? 34.236  54.306 47.246  1.00 22.94  ? 92   TRP D N   1 
ATOM   7126  C CA  . TRP D  2 92  ? 34.313  55.541 46.468  1.00 23.24  ? 92   TRP D CA  1 
ATOM   7127  C C   . TRP D  2 92  ? 35.566  55.624 45.595  1.00 23.07  ? 92   TRP D C   1 
ATOM   7128  O O   . TRP D  2 92  ? 35.533  56.239 44.529  1.00 23.03  ? 92   TRP D O   1 
ATOM   7129  C CB  . TRP D  2 92  ? 34.182  56.771 47.372  1.00 24.45  ? 92   TRP D CB  1 
ATOM   7130  C CG  . TRP D  2 92  ? 32.766  57.005 47.795  1.00 25.00  ? 92   TRP D CG  1 
ATOM   7131  C CD1 . TRP D  2 92  ? 32.249  56.878 49.055  1.00 25.61  ? 92   TRP D CD1 1 
ATOM   7132  C CD2 . TRP D  2 92  ? 31.671  57.376 46.950  1.00 25.29  ? 92   TRP D CD2 1 
ATOM   7133  N NE1 . TRP D  2 92  ? 30.903  57.162 49.047  1.00 26.42  ? 92   TRP D NE1 1 
ATOM   7134  C CE2 . TRP D  2 92  ? 30.524  57.468 47.767  1.00 26.31  ? 92   TRP D CE2 1 
ATOM   7135  C CE3 . TRP D  2 92  ? 31.549  57.645 45.582  1.00 25.01  ? 92   TRP D CE3 1 
ATOM   7136  C CZ2 . TRP D  2 92  ? 29.272  57.822 47.263  1.00 27.31  ? 92   TRP D CZ2 1 
ATOM   7137  C CZ3 . TRP D  2 92  ? 30.303  57.997 45.080  1.00 25.82  ? 92   TRP D CZ3 1 
ATOM   7138  C CH2 . TRP D  2 92  ? 29.180  58.084 45.921  1.00 27.08  ? 92   TRP D CH2 1 
ATOM   7139  N N   . THR D  2 93  ? 36.660  55.010 46.036  1.00 23.21  ? 93   THR D N   1 
ATOM   7140  C CA  . THR D  2 93  ? 37.868  54.941 45.216  1.00 23.44  ? 93   THR D CA  1 
ATOM   7141  C C   . THR D  2 93  ? 37.585  54.093 43.976  1.00 22.55  ? 93   THR D C   1 
ATOM   7142  O O   . THR D  2 93  ? 37.933  54.475 42.861  1.00 22.54  ? 93   THR D O   1 
ATOM   7143  C CB  . THR D  2 93  ? 39.059  54.347 45.994  1.00 24.26  ? 93   THR D CB  1 
ATOM   7144  O OG1 . THR D  2 93  ? 39.390  55.212 47.083  1.00 25.37  ? 93   THR D OG1 1 
ATOM   7145  C CG2 . THR D  2 93  ? 40.281  54.199 45.097  1.00 24.93  ? 93   THR D CG2 1 
ATOM   7146  N N   . TYR D  2 94  ? 36.954  52.945 44.190  1.00 22.08  ? 94   TYR D N   1 
ATOM   7147  C CA  . TYR D  2 94  ? 36.609  52.023 43.113  1.00 21.65  ? 94   TYR D CA  1 
ATOM   7148  C C   . TYR D  2 94  ? 35.698  52.689 42.082  1.00 21.18  ? 94   TYR D C   1 
ATOM   7149  O O   . TYR D  2 94  ? 35.940  52.591 40.883  1.00 20.95  ? 94   TYR D O   1 
ATOM   7150  C CB  . TYR D  2 94  ? 35.941  50.779 43.705  1.00 21.72  ? 94   TYR D CB  1 
ATOM   7151  C CG  . TYR D  2 94  ? 35.218  49.905 42.713  1.00 21.64  ? 94   TYR D CG  1 
ATOM   7152  C CD1 . TYR D  2 94  ? 33.888  50.144 42.386  1.00 21.46  ? 94   TYR D CD1 1 
ATOM   7153  C CD2 . TYR D  2 94  ? 35.855  48.829 42.115  1.00 22.18  ? 94   TYR D CD2 1 
ATOM   7154  C CE1 . TYR D  2 94  ? 33.218  49.339 41.482  1.00 21.79  ? 94   TYR D CE1 1 
ATOM   7155  C CE2 . TYR D  2 94  ? 35.193  48.023 41.209  1.00 22.51  ? 94   TYR D CE2 1 
ATOM   7156  C CZ  . TYR D  2 94  ? 33.879  48.281 40.899  1.00 22.27  ? 94   TYR D CZ  1 
ATOM   7157  O OH  . TYR D  2 94  ? 33.225  47.482 40.001  1.00 22.98  ? 94   TYR D OH  1 
ATOM   7158  N N   . ASN D  2 95  ? 34.660  53.369 42.567  1.00 21.26  ? 95   ASN D N   1 
ATOM   7159  C CA  . ASN D  2 95  ? 33.744  54.124 41.714  1.00 21.27  ? 95   ASN D CA  1 
ATOM   7160  C C   . ASN D  2 95  ? 34.455  55.118 40.808  1.00 21.24  ? 95   ASN D C   1 
ATOM   7161  O O   . ASN D  2 95  ? 34.179  55.178 39.609  1.00 20.98  ? 95   ASN D O   1 
ATOM   7162  C CB  . ASN D  2 95  ? 32.724  54.883 42.565  1.00 21.98  ? 95   ASN D CB  1 
ATOM   7163  C CG  . ASN D  2 95  ? 31.707  53.966 43.215  1.00 22.34  ? 95   ASN D CG  1 
ATOM   7164  O OD1 . ASN D  2 95  ? 31.722  52.750 43.006  1.00 22.18  ? 95   ASN D OD1 1 
ATOM   7165  N ND2 . ASN D  2 95  ? 30.808  54.546 44.002  1.00 23.23  ? 95   ASN D ND2 1 
ATOM   7166  N N   . ALA D  2 96  ? 35.362  55.895 41.399  1.00 21.73  ? 96   ALA D N   1 
ATOM   7167  C CA  . ALA D  2 96  ? 36.119  56.918 40.681  1.00 22.16  ? 96   ALA D CA  1 
ATOM   7168  C C   . ALA D  2 96  ? 36.985  56.305 39.591  1.00 21.70  ? 96   ALA D C   1 
ATOM   7169  O O   . ALA D  2 96  ? 36.935  56.725 38.443  1.00 21.53  ? 96   ALA D O   1 
ATOM   7170  C CB  . ALA D  2 96  ? 36.992  57.702 41.651  1.00 23.34  ? 96   ALA D CB  1 
ATOM   7171  N N   . GLU D  2 97  ? 37.772  55.302 39.961  1.00 21.68  ? 97   GLU D N   1 
ATOM   7172  C CA  . GLU D  2 97  ? 38.716  54.687 39.032  1.00 21.78  ? 97   GLU D CA  1 
ATOM   7173  C C   . GLU D  2 97  ? 38.020  53.911 37.917  1.00 20.91  ? 97   GLU D C   1 
ATOM   7174  O O   . GLU D  2 97  ? 38.499  53.885 36.782  1.00 21.00  ? 97   GLU D O   1 
ATOM   7175  C CB  . GLU D  2 97  ? 39.674  53.768 39.785  1.00 22.60  ? 97   GLU D CB  1 
ATOM   7176  C CG  . GLU D  2 97  ? 40.566  54.511 40.765  1.00 23.84  ? 97   GLU D CG  1 
ATOM   7177  C CD  . GLU D  2 97  ? 41.591  53.618 41.423  1.00 25.02  ? 97   GLU D CD  1 
ATOM   7178  O OE1 . GLU D  2 97  ? 41.509  52.383 41.247  1.00 24.91  ? 97   GLU D OE1 1 
ATOM   7179  O OE2 . GLU D  2 97  ? 42.484  54.155 42.119  1.00 26.48  ? 97   GLU D OE2 1 
ATOM   7180  N N   . LEU D  2 98  ? 36.898  53.275 38.243  1.00 20.30  ? 98   LEU D N   1 
ATOM   7181  C CA  . LEU D  2 98  ? 36.137  52.526 37.257  1.00 19.89  ? 98   LEU D CA  1 
ATOM   7182  C C   . LEU D  2 98  ? 35.471  53.483 36.284  1.00 19.45  ? 98   LEU D C   1 
ATOM   7183  O O   . LEU D  2 98  ? 35.561  53.299 35.081  1.00 19.33  ? 98   LEU D O   1 
ATOM   7184  C CB  . LEU D  2 98  ? 35.079  51.647 37.930  1.00 19.99  ? 98   LEU D CB  1 
ATOM   7185  C CG  . LEU D  2 98  ? 34.292  50.734 36.987  1.00 20.25  ? 98   LEU D CG  1 
ATOM   7186  C CD1 . LEU D  2 98  ? 35.196  49.643 36.429  1.00 20.83  ? 98   LEU D CD1 1 
ATOM   7187  C CD2 . LEU D  2 98  ? 33.095  50.124 37.696  1.00 20.76  ? 98   LEU D CD2 1 
ATOM   7188  N N   . LEU D  2 99  ? 34.806  54.505 36.813  1.00 19.43  ? 99   LEU D N   1 
ATOM   7189  C CA  . LEU D  2 99  ? 34.125  55.493 35.979  1.00 19.46  ? 99   LEU D CA  1 
ATOM   7190  C C   . LEU D  2 99  ? 35.092  56.126 34.981  1.00 19.34  ? 99   LEU D C   1 
ATOM   7191  O O   . LEU D  2 99  ? 34.763  56.303 33.812  1.00 19.18  ? 99   LEU D O   1 
ATOM   7192  C CB  . LEU D  2 99  ? 33.488  56.589 36.842  1.00 20.12  ? 99   LEU D CB  1 
ATOM   7193  C CG  . LEU D  2 99  ? 32.623  57.629 36.114  1.00 20.76  ? 99   LEU D CG  1 
ATOM   7194  C CD1 . LEU D  2 99  ? 31.459  56.969 35.394  1.00 20.82  ? 99   LEU D CD1 1 
ATOM   7195  C CD2 . LEU D  2 99  ? 32.113  58.683 37.085  1.00 21.93  ? 99   LEU D CD2 1 
ATOM   7196  N N   . VAL D  2 100 ? 36.288  56.457 35.449  1.00 19.62  ? 100  VAL D N   1 
ATOM   7197  C CA  . VAL D  2 100 ? 37.312  57.026 34.584  1.00 19.93  ? 100  VAL D CA  1 
ATOM   7198  C C   . VAL D  2 100 ? 37.697  56.031 33.479  1.00 19.51  ? 100  VAL D C   1 
ATOM   7199  O O   . VAL D  2 100 ? 37.673  56.382 32.307  1.00 19.39  ? 100  VAL D O   1 
ATOM   7200  C CB  . VAL D  2 100 ? 38.531  57.511 35.404  1.00 20.93  ? 100  VAL D CB  1 
ATOM   7201  C CG1 . VAL D  2 100 ? 39.739  57.770 34.512  1.00 21.67  ? 100  VAL D CG1 1 
ATOM   7202  C CG2 . VAL D  2 100 ? 38.163  58.777 36.164  1.00 21.71  ? 100  VAL D CG2 1 
ATOM   7203  N N   . LEU D  2 101 ? 38.014  54.796 33.859  1.00 19.50  ? 101  LEU D N   1 
ATOM   7204  C CA  . LEU D  2 101 ? 38.312  53.722 32.899  1.00 19.56  ? 101  LEU D CA  1 
ATOM   7205  C C   . LEU D  2 101 ? 37.229  53.519 31.829  1.00 19.03  ? 101  LEU D C   1 
ATOM   7206  O O   . LEU D  2 101 ? 37.529  53.444 30.633  1.00 19.13  ? 101  LEU D O   1 
ATOM   7207  C CB  . LEU D  2 101 ? 38.519  52.397 33.639  1.00 20.03  ? 101  LEU D CB  1 
ATOM   7208  C CG  . LEU D  2 101 ? 39.940  51.855 33.787  1.00 21.25  ? 101  LEU D CG  1 
ATOM   7209  C CD1 . LEU D  2 101 ? 40.949  52.933 34.145  1.00 21.89  ? 101  LEU D CD1 1 
ATOM   7210  C CD2 . LEU D  2 101 ? 39.945  50.749 34.828  1.00 21.80  ? 101  LEU D CD2 1 
ATOM   7211  N N   . MET D  2 102 ? 35.977  53.413 32.264  1.00 18.71  ? 102  MET D N   1 
ATOM   7212  C CA  . MET D  2 102 ? 34.872  53.135 31.355  1.00 18.68  ? 102  MET D CA  1 
ATOM   7213  C C   . MET D  2 102 ? 34.581  54.308 30.427  1.00 18.43  ? 102  MET D C   1 
ATOM   7214  O O   . MET D  2 102 ? 34.359  54.122 29.226  1.00 18.48  ? 102  MET D O   1 
ATOM   7215  C CB  . MET D  2 102 ? 33.611  52.789 32.141  1.00 18.97  ? 102  MET D CB  1 
ATOM   7216  C CG  . MET D  2 102 ? 33.721  51.497 32.928  1.00 19.45  ? 102  MET D CG  1 
ATOM   7217  S SD  . MET D  2 102 ? 32.141  50.918 33.586  1.00 20.28  ? 102  MET D SD  1 
ATOM   7218  C CE  . MET D  2 102 ? 31.657  52.337 34.575  1.00 19.95  ? 102  MET D CE  1 
ATOM   7219  N N   . GLU D  2 103 ? 34.572  55.511 30.990  1.00 18.40  ? 103  GLU D N   1 
ATOM   7220  C CA  . GLU D  2 103 ? 34.235  56.705 30.230  1.00 18.55  ? 103  GLU D CA  1 
ATOM   7221  C C   . GLU D  2 103 ? 35.376  57.167 29.323  1.00 18.48  ? 103  GLU D C   1 
ATOM   7222  O O   . GLU D  2 103 ? 35.122  57.726 28.263  1.00 18.53  ? 103  GLU D O   1 
ATOM   7223  C CB  . GLU D  2 103 ? 33.781  57.822 31.169  1.00 19.12  ? 103  GLU D CB  1 
ATOM   7224  C CG  . GLU D  2 103 ? 32.417  57.576 31.812  1.00 19.56  ? 103  GLU D CG  1 
ATOM   7225  C CD  . GLU D  2 103 ? 31.276  57.420 30.809  1.00 20.01  ? 103  GLU D CD  1 
ATOM   7226  O OE1 . GLU D  2 103 ? 31.375  57.948 29.689  1.00 20.03  ? 103  GLU D OE1 1 
ATOM   7227  O OE2 . GLU D  2 103 ? 30.263  56.762 31.138  1.00 20.58  ? 103  GLU D OE2 1 
ATOM   7228  N N   . ASN D  2 104 ? 36.622  56.935 29.734  1.00 18.62  ? 104  ASN D N   1 
ATOM   7229  C CA  . ASN D  2 104 ? 37.772  57.133 28.847  1.00 18.95  ? 104  ASN D CA  1 
ATOM   7230  C C   . ASN D  2 104 ? 37.644  56.295 27.586  1.00 18.70  ? 104  ASN D C   1 
ATOM   7231  O O   . ASN D  2 104 ? 37.910  56.770 26.484  1.00 18.78  ? 104  ASN D O   1 
ATOM   7232  C CB  . ASN D  2 104 ? 39.081  56.740 29.533  1.00 19.58  ? 104  ASN D CB  1 
ATOM   7233  C CG  . ASN D  2 104 ? 39.617  57.816 30.442  1.00 20.38  ? 104  ASN D CG  1 
ATOM   7234  O OD1 . ASN D  2 104 ? 39.124  58.935 30.453  1.00 20.56  ? 104  ASN D OD1 1 
ATOM   7235  N ND2 . ASN D  2 104 ? 40.639  57.476 31.215  1.00 21.22  ? 104  ASN D ND2 1 
ATOM   7236  N N   . GLU D  2 105 ? 37.251  55.040 27.761  1.00 17.63  ? 105  GLU D N   1 
ATOM   7237  C CA  . GLU D  2 105 ? 37.065  54.150 26.633  1.00 17.49  ? 105  GLU D CA  1 
ATOM   7238  C C   . GLU D  2 105 ? 35.933  54.639 25.740  1.00 15.95  ? 105  GLU D C   1 
ATOM   7239  O O   . GLU D  2 105 ? 36.032  54.591 24.520  1.00 15.18  ? 105  GLU D O   1 
ATOM   7240  C CB  . GLU D  2 105 ? 36.776  52.729 27.104  1.00 19.51  ? 105  GLU D CB  1 
ATOM   7241  C CG  . GLU D  2 105 ? 37.057  51.688 26.037  1.00 20.35  ? 105  GLU D CG  1 
ATOM   7242  C CD  . GLU D  2 105 ? 37.106  50.292 26.613  1.00 23.28  ? 105  GLU D CD  1 
ATOM   7243  O OE1 . GLU D  2 105 ? 36.138  49.925 27.319  1.00 24.21  ? 105  GLU D OE1 1 
ATOM   7244  O OE2 . GLU D  2 105 ? 38.112  49.576 26.377  1.00 25.13  ? 105  GLU D OE2 1 
ATOM   7245  N N   . ARG D  2 106 ? 34.853  55.098 26.352  1.00 15.96  ? 106  ARG D N   1 
ATOM   7246  C CA  . ARG D  2 106 ? 33.754  55.654 25.581  1.00 15.21  ? 106  ARG D CA  1 
ATOM   7247  C C   . ARG D  2 106 ? 34.143  56.945 24.864  1.00 13.82  ? 106  ARG D C   1 
ATOM   7248  O O   . ARG D  2 106 ? 33.678  57.193 23.760  1.00 13.22  ? 106  ARG D O   1 
ATOM   7249  C CB  . ARG D  2 106 ? 32.532  55.889 26.459  1.00 16.28  ? 106  ARG D CB  1 
ATOM   7250  C CG  . ARG D  2 106 ? 31.863  54.611 26.932  1.00 18.14  ? 106  ARG D CG  1 
ATOM   7251  C CD  . ARG D  2 106 ? 30.363  54.807 27.069  1.00 19.43  ? 106  ARG D CD  1 
ATOM   7252  N NE  . ARG D  2 106 ? 29.604  54.300 25.912  1.00 19.96  ? 106  ARG D NE  1 
ATOM   7253  C CZ  . ARG D  2 106 ? 28.447  54.812 25.476  1.00 20.84  ? 106  ARG D CZ  1 
ATOM   7254  N NH1 . ARG D  2 106 ? 27.901  55.878 26.063  1.00 21.27  ? 106  ARG D NH1 1 
ATOM   7255  N NH2 . ARG D  2 106 ? 27.822  54.262 24.433  1.00 21.76  ? 106  ARG D NH2 1 
ATOM   7256  N N   . THR D  2 107 ? 34.995  57.755 25.488  1.00 13.74  ? 107  THR D N   1 
ATOM   7257  C CA  . THR D  2 107 ? 35.443  59.009 24.889  1.00 13.06  ? 107  THR D CA  1 
ATOM   7258  C C   . THR D  2 107 ? 36.262  58.765 23.619  1.00 12.35  ? 107  THR D C   1 
ATOM   7259  O O   . THR D  2 107 ? 36.066  59.442 22.619  1.00 11.78  ? 107  THR D O   1 
ATOM   7260  C CB  . THR D  2 107 ? 36.258  59.860 25.884  1.00 13.87  ? 107  THR D CB  1 
ATOM   7261  O OG1 . THR D  2 107 ? 35.412  60.290 26.955  1.00 14.71  ? 107  THR D OG1 1 
ATOM   7262  C CG2 . THR D  2 107 ? 36.832  61.096 25.208  1.00 13.82  ? 107  THR D CG2 1 
ATOM   7263  N N   . LEU D  2 108 ? 37.172  57.803 23.655  1.00 12.78  ? 108  LEU D N   1 
ATOM   7264  C CA  . LEU D  2 108 ? 37.971  57.491 22.478  1.00 12.62  ? 108  LEU D CA  1 
ATOM   7265  C C   . LEU D  2 108 ? 37.095  56.975 21.331  1.00 11.99  ? 108  LEU D C   1 
ATOM   7266  O O   . LEU D  2 108 ? 37.270  57.366 20.179  1.00 11.52  ? 108  LEU D O   1 
ATOM   7267  C CB  . LEU D  2 108 ? 39.058  56.477 22.823  1.00 14.00  ? 108  LEU D CB  1 
ATOM   7268  C CG  . LEU D  2 108 ? 40.067  56.898 23.896  1.00 15.27  ? 108  LEU D CG  1 
ATOM   7269  C CD1 . LEU D  2 108 ? 41.199  55.890 23.943  1.00 17.26  ? 108  LEU D CD1 1 
ATOM   7270  C CD2 . LEU D  2 108 ? 40.615  58.296 23.658  1.00 15.14  ? 108  LEU D CD2 1 
ATOM   7271  N N   . ASP D  2 109 ? 36.148  56.105 21.661  1.00 12.39  ? 109  ASP D N   1 
ATOM   7272  C CA  . ASP D  2 109 ? 35.213  55.578 20.680  1.00 12.38  ? 109  ASP D CA  1 
ATOM   7273  C C   . ASP D  2 109 ? 34.273  56.656 20.130  1.00 11.65  ? 109  ASP D C   1 
ATOM   7274  O O   . ASP D  2 109 ? 33.861  56.581 18.979  1.00 11.66  ? 109  ASP D O   1 
ATOM   7275  C CB  . ASP D  2 109 ? 34.388  54.451 21.293  1.00 13.69  ? 109  ASP D CB  1 
ATOM   7276  C CG  . ASP D  2 109 ? 35.210  53.205 21.577  1.00 15.14  ? 109  ASP D CG  1 
ATOM   7277  O OD1 . ASP D  2 109 ? 36.191  52.937 20.840  1.00 15.40  ? 109  ASP D OD1 1 
ATOM   7278  O OD2 . ASP D  2 109 ? 34.843  52.479 22.536  1.00 16.56  ? 109  ASP D OD2 1 
ATOM   7279  N N   . PHE D  2 110 ? 33.925  57.634 20.961  1.00 11.46  ? 110  PHE D N   1 
ATOM   7280  C CA  . PHE D  2 110 ? 33.096  58.764 20.550  1.00 11.44  ? 110  PHE D CA  1 
ATOM   7281  C C   . PHE D  2 110 ? 33.802  59.553 19.441  1.00 10.87  ? 110  PHE D C   1 
ATOM   7282  O O   . PHE D  2 110 ? 33.205  59.895 18.425  1.00 11.11  ? 110  PHE D O   1 
ATOM   7283  C CB  . PHE D  2 110 ? 32.816  59.645 21.774  1.00 11.95  ? 110  PHE D CB  1 
ATOM   7284  C CG  . PHE D  2 110 ? 32.037  60.900 21.480  1.00 12.69  ? 110  PHE D CG  1 
ATOM   7285  C CD1 . PHE D  2 110 ? 30.782  60.845 20.894  1.00 13.67  ? 110  PHE D CD1 1 
ATOM   7286  C CD2 . PHE D  2 110 ? 32.542  62.140 21.839  1.00 13.04  ? 110  PHE D CD2 1 
ATOM   7287  C CE1 . PHE D  2 110 ? 30.065  62.004 20.646  1.00 15.02  ? 110  PHE D CE1 1 
ATOM   7288  C CE2 . PHE D  2 110 ? 31.828  63.301 21.598  1.00 14.39  ? 110  PHE D CE2 1 
ATOM   7289  C CZ  . PHE D  2 110 ? 30.587  63.235 21.000  1.00 15.40  ? 110  PHE D CZ  1 
ATOM   7290  N N   . HIS D  2 111 ? 35.085  59.827 19.640  1.00 10.55  ? 111  HIS D N   1 
ATOM   7291  C CA  . HIS D  2 111 ? 35.903  60.485 18.631  1.00 10.43  ? 111  HIS D CA  1 
ATOM   7292  C C   . HIS D  2 111 ? 36.001  59.653 17.357  1.00 10.23  ? 111  HIS D C   1 
ATOM   7293  O O   . HIS D  2 111 ? 35.944  60.187 16.250  1.00 10.36  ? 111  HIS D O   1 
ATOM   7294  C CB  . HIS D  2 111 ? 37.306  60.747 19.175  1.00 10.79  ? 111  HIS D CB  1 
ATOM   7295  C CG  . HIS D  2 111 ? 37.362  61.848 20.187  1.00 11.46  ? 111  HIS D CG  1 
ATOM   7296  N ND1 . HIS D  2 111 ? 37.038  63.151 19.882  1.00 12.12  ? 111  HIS D ND1 1 
ATOM   7297  C CD2 . HIS D  2 111 ? 37.731  61.846 21.489  1.00 12.02  ? 111  HIS D CD2 1 
ATOM   7298  C CE1 . HIS D  2 111 ? 37.191  63.901 20.958  1.00 13.11  ? 111  HIS D CE1 1 
ATOM   7299  N NE2 . HIS D  2 111 ? 37.610  63.132 21.946  1.00 12.96  ? 111  HIS D NE2 1 
ATOM   7300  N N   . ASP D  2 112 ? 36.146  58.342 17.519  1.00 10.31  ? 112  ASP D N   1 
ATOM   7301  C CA  . ASP D  2 112 ? 36.222  57.432 16.386  1.00 10.61  ? 112  ASP D CA  1 
ATOM   7302  C C   . ASP D  2 112 ? 34.910  57.470 15.588  1.00 10.80  ? 112  ASP D C   1 
ATOM   7303  O O   . ASP D  2 112 ? 34.918  57.478 14.359  1.00 11.09  ? 112  ASP D O   1 
ATOM   7304  C CB  . ASP D  2 112 ? 36.514  56.018 16.895  1.00 11.36  ? 112  ASP D CB  1 
ATOM   7305  C CG  . ASP D  2 112 ? 36.966  55.079 15.804  1.00 12.28  ? 112  ASP D CG  1 
ATOM   7306  O OD1 . ASP D  2 112 ? 37.223  55.532 14.671  1.00 12.14  ? 112  ASP D OD1 1 
ATOM   7307  O OD2 . ASP D  2 112 ? 37.056  53.869 16.089  1.00 13.51  ? 112  ASP D OD2 1 
ATOM   7308  N N   . SER D  2 113 ? 33.792  57.490 16.307  1.00 11.06  ? 113  SER D N   1 
ATOM   7309  C CA  . SER D  2 113 ? 32.464  57.573 15.712  1.00 11.93  ? 113  SER D CA  1 
ATOM   7310  C C   . SER D  2 113 ? 32.259  58.873 14.931  1.00 12.07  ? 113  SER D C   1 
ATOM   7311  O O   . SER D  2 113 ? 31.692  58.867 13.836  1.00 12.94  ? 113  SER D O   1 
ATOM   7312  C CB  . SER D  2 113 ? 31.408  57.456 16.813  1.00 12.67  ? 113  SER D CB  1 
ATOM   7313  O OG  . SER D  2 113 ? 30.132  57.839 16.350  1.00 14.02  ? 113  SER D OG  1 
ATOM   7314  N N   . ASN D  2 114 ? 32.703  59.987 15.504  1.00 11.70  ? 114  ASN D N   1 
ATOM   7315  C CA  . ASN D  2 114 ? 32.559  61.292 14.865  1.00 12.37  ? 114  ASN D CA  1 
ATOM   7316  C C   . ASN D  2 114 ? 33.310  61.381 13.538  1.00 12.31  ? 114  ASN D C   1 
ATOM   7317  O O   . ASN D  2 114 ? 32.814  61.968 12.584  1.00 13.39  ? 114  ASN D O   1 
ATOM   7318  C CB  . ASN D  2 114 ? 33.044  62.404 15.799  1.00 12.42  ? 114  ASN D CB  1 
ATOM   7319  C CG  . ASN D  2 114 ? 32.157  62.575 17.015  1.00 13.08  ? 114  ASN D CG  1 
ATOM   7320  O OD1 . ASN D  2 114 ? 30.954  62.332 16.964  1.00 14.11  ? 114  ASN D OD1 1 
ATOM   7321  N ND2 . ASN D  2 114 ? 32.747  63.018 18.114  1.00 12.92  ? 114  ASN D ND2 1 
ATOM   7322  N N   . VAL D  2 115 ? 34.508  60.805 13.496  1.00 11.51  ? 115  VAL D N   1 
ATOM   7323  C CA  . VAL D  2 115 ? 35.317  60.767 12.278  1.00 11.76  ? 115  VAL D CA  1 
ATOM   7324  C C   . VAL D  2 115 ? 34.616  59.924 11.209  1.00 12.36  ? 115  VAL D C   1 
ATOM   7325  O O   . VAL D  2 115 ? 34.559  60.303 10.036  1.00 13.16  ? 115  VAL D O   1 
ATOM   7326  C CB  . VAL D  2 115 ? 36.717  60.167 12.551  1.00 11.40  ? 115  VAL D CB  1 
ATOM   7327  C CG1 . VAL D  2 115 ? 37.481  59.941 11.252  1.00 12.08  ? 115  VAL D CG1 1 
ATOM   7328  C CG2 . VAL D  2 115 ? 37.523  61.066 13.480  1.00 11.41  ? 115  VAL D CG2 1 
ATOM   7329  N N   . LYS D  2 116 ? 34.094  58.778 11.633  1.00 12.37  ? 116  LYS D N   1 
ATOM   7330  C CA  . LYS D  2 116 ? 33.377  57.856 10.755  1.00 13.47  ? 116  LYS D CA  1 
ATOM   7331  C C   . LYS D  2 116 ? 32.140  58.509 10.145  1.00 14.69  ? 116  LYS D C   1 
ATOM   7332  O O   . LYS D  2 116 ? 31.883  58.395 8.948   1.00 15.83  ? 116  LYS D O   1 
ATOM   7333  C CB  . LYS D  2 116 ? 32.937  56.630 11.553  1.00 13.81  ? 116  LYS D CB  1 
ATOM   7334  C CG  . LYS D  2 116 ? 33.187  55.311 10.870  1.00 14.96  ? 116  LYS D CG  1 
ATOM   7335  C CD  . LYS D  2 116 ? 32.261  55.094 9.696   1.00 16.64  ? 116  LYS D CD  1 
ATOM   7336  C CE  . LYS D  2 116 ? 32.741  53.937 8.840   1.00 18.05  ? 116  LYS D CE  1 
ATOM   7337  N NZ  . LYS D  2 116 ? 32.403  52.646 9.490   1.00 19.39  ? 116  LYS D NZ  1 
ATOM   7338  N N   . ASN D  2 117 ? 31.371  59.188 10.986  1.00 14.88  ? 117  ASN D N   1 
ATOM   7339  C CA  . ASN D  2 117 ? 30.143  59.827 10.550  1.00 16.73  ? 117  ASN D CA  1 
ATOM   7340  C C   . ASN D  2 117 ? 30.421  60.976 9.587   1.00 17.41  ? 117  ASN D C   1 
ATOM   7341  O O   . ASN D  2 117 ? 29.668  61.202 8.634   1.00 19.35  ? 117  ASN D O   1 
ATOM   7342  C CB  . ASN D  2 117 ? 29.345  60.308 11.759  1.00 17.21  ? 117  ASN D CB  1 
ATOM   7343  C CG  . ASN D  2 117 ? 28.811  59.161 12.596  1.00 17.39  ? 117  ASN D CG  1 
ATOM   7344  O OD1 . ASN D  2 117 ? 28.729  58.020 12.138  1.00 17.86  ? 117  ASN D OD1 1 
ATOM   7345  N ND2 . ASN D  2 117 ? 28.430  59.463 13.832  1.00 17.47  ? 117  ASN D ND2 1 
ATOM   7346  N N   . LEU D  2 118 ? 31.507  61.694 9.840   1.00 16.28  ? 118  LEU D N   1 
ATOM   7347  C CA  . LEU D  2 118 ? 31.940  62.761 8.953   1.00 17.21  ? 118  LEU D CA  1 
ATOM   7348  C C   . LEU D  2 118 ? 32.412  62.179 7.618   1.00 17.52  ? 118  LEU D C   1 
ATOM   7349  O O   . LEU D  2 118 ? 32.150  62.744 6.556   1.00 19.18  ? 118  LEU D O   1 
ATOM   7350  C CB  . LEU D  2 118 ? 33.061  63.571 9.610   1.00 16.35  ? 118  LEU D CB  1 
ATOM   7351  C CG  . LEU D  2 118 ? 33.645  64.730 8.810   1.00 17.68  ? 118  LEU D CG  1 
ATOM   7352  C CD1 . LEU D  2 118 ? 32.549  65.680 8.357   1.00 20.11  ? 118  LEU D CD1 1 
ATOM   7353  C CD2 . LEU D  2 118 ? 34.688  65.456 9.640   1.00 17.33  ? 118  LEU D CD2 1 
ATOM   7354  N N   . TYR D  2 119 ? 33.108  61.051 7.678   1.00 16.35  ? 119  TYR D N   1 
ATOM   7355  C CA  . TYR D  2 119 ? 33.576  60.389 6.471   1.00 16.97  ? 119  TYR D CA  1 
ATOM   7356  C C   . TYR D  2 119 ? 32.404  59.926 5.618   1.00 18.76  ? 119  TYR D C   1 
ATOM   7357  O O   . TYR D  2 119 ? 32.395  60.133 4.408   1.00 20.21  ? 119  TYR D O   1 
ATOM   7358  C CB  . TYR D  2 119 ? 34.467  59.198 6.815   1.00 16.00  ? 119  TYR D CB  1 
ATOM   7359  C CG  . TYR D  2 119 ? 34.895  58.407 5.602   1.00 17.12  ? 119  TYR D CG  1 
ATOM   7360  C CD1 . TYR D  2 119 ? 35.938  58.853 4.794   1.00 17.63  ? 119  TYR D CD1 1 
ATOM   7361  C CD2 . TYR D  2 119 ? 34.259  57.219 5.256   1.00 18.14  ? 119  TYR D CD2 1 
ATOM   7362  C CE1 . TYR D  2 119 ? 36.337  58.135 3.680   1.00 19.00  ? 119  TYR D CE1 1 
ATOM   7363  C CE2 . TYR D  2 119 ? 34.652  56.495 4.142   1.00 19.60  ? 119  TYR D CE2 1 
ATOM   7364  C CZ  . TYR D  2 119 ? 35.692  56.959 3.358   1.00 19.96  ? 119  TYR D CZ  1 
ATOM   7365  O OH  . TYR D  2 119 ? 36.099  56.262 2.249   1.00 21.72  ? 119  TYR D OH  1 
ATOM   7366  N N   . ASP D  2 120 ? 31.424  59.292 6.251   1.00 19.10  ? 120  ASP D N   1 
ATOM   7367  C CA  . ASP D  2 120 ? 30.257  58.793 5.538   1.00 21.39  ? 120  ASP D CA  1 
ATOM   7368  C C   . ASP D  2 120 ? 29.424  59.944 4.963   1.00 23.40  ? 120  ASP D C   1 
ATOM   7369  O O   . ASP D  2 120 ? 28.890  59.839 3.866   1.00 25.62  ? 120  ASP D O   1 
ATOM   7370  C CB  . ASP D  2 120 ? 29.396  57.924 6.463   1.00 21.80  ? 120  ASP D CB  1 
ATOM   7371  C CG  . ASP D  2 120 ? 30.068  56.608 6.835   1.00 20.93  ? 120  ASP D CG  1 
ATOM   7372  O OD1 . ASP D  2 120 ? 30.814  56.036 6.008   1.00 21.17  ? 120  ASP D OD1 1 
ATOM   7373  O OD2 . ASP D  2 120 ? 29.831  56.129 7.963   1.00 20.47  ? 120  ASP D OD2 1 
ATOM   7374  N N   . LYS D  2 121 ? 29.324  61.038 5.713   1.00 23.08  ? 121  LYS D N   1 
ATOM   7375  C CA  . LYS D  2 121 ? 28.607  62.236 5.275   1.00 25.49  ? 121  LYS D CA  1 
ATOM   7376  C C   . LYS D  2 121 ? 29.118  62.696 3.915   1.00 26.63  ? 121  LYS D C   1 
ATOM   7377  O O   . LYS D  2 121 ? 28.339  62.999 3.019   1.00 29.48  ? 121  LYS D O   1 
ATOM   7378  C CB  . LYS D  2 121 ? 28.791  63.350 6.305   1.00 24.89  ? 121  LYS D CB  1 
ATOM   7379  C CG  . LYS D  2 121 ? 27.973  64.611 6.076   1.00 27.97  ? 121  LYS D CG  1 
ATOM   7380  C CD  . LYS D  2 121 ? 28.288  65.632 7.167   1.00 27.54  ? 121  LYS D CD  1 
ATOM   7381  C CE  . LYS D  2 121 ? 27.197  66.683 7.331   1.00 31.14  ? 121  LYS D CE  1 
ATOM   7382  N NZ  . LYS D  2 121 ? 27.323  67.808 6.362   1.00 33.83  ? 121  LYS D NZ  1 
ATOM   7383  N N   . VAL D  2 122 ? 30.437  62.734 3.775   1.00 24.81  ? 122  VAL D N   1 
ATOM   7384  C CA  . VAL D  2 122 ? 31.078  63.080 2.521   1.00 25.90  ? 122  VAL D CA  1 
ATOM   7385  C C   . VAL D  2 122 ? 30.836  61.994 1.474   1.00 27.03  ? 122  VAL D C   1 
ATOM   7386  O O   . VAL D  2 122 ? 30.430  62.285 0.349   1.00 29.50  ? 122  VAL D O   1 
ATOM   7387  C CB  . VAL D  2 122 ? 32.586  63.318 2.735   1.00 24.05  ? 122  VAL D CB  1 
ATOM   7388  C CG1 . VAL D  2 122 ? 33.334  63.404 1.410   1.00 25.26  ? 122  VAL D CG1 1 
ATOM   7389  C CG2 . VAL D  2 122 ? 32.786  64.586 3.551   1.00 24.02  ? 122  VAL D CG2 1 
ATOM   7390  N N   . ARG D  2 123 ? 31.071  60.744 1.852   1.00 25.70  ? 123  ARG D N   1 
ATOM   7391  C CA  . ARG D  2 123 ? 30.877  59.620 0.943   1.00 27.14  ? 123  ARG D CA  1 
ATOM   7392  C C   . ARG D  2 123 ? 29.486  59.648 0.316   1.00 30.29  ? 123  ARG D C   1 
ATOM   7393  O O   . ARG D  2 123 ? 29.339  59.437 -0.892  1.00 32.51  ? 123  ARG D O   1 
ATOM   7394  C CB  . ARG D  2 123 ? 31.077  58.303 1.690   1.00 25.84  ? 123  ARG D CB  1 
ATOM   7395  C CG  . ARG D  2 123 ? 31.133  57.082 0.791   1.00 27.50  ? 123  ARG D CG  1 
ATOM   7396  C CD  . ARG D  2 123 ? 31.290  55.803 1.600   1.00 26.86  ? 123  ARG D CD  1 
ATOM   7397  N NE  . ARG D  2 123 ? 30.311  55.711 2.687   1.00 26.68  ? 123  ARG D NE  1 
ATOM   7398  C CZ  . ARG D  2 123 ? 29.019  55.412 2.535   1.00 29.08  ? 123  ARG D CZ  1 
ATOM   7399  N NH1 . ARG D  2 123 ? 28.496  55.168 1.333   1.00 31.92  ? 123  ARG D NH1 1 
ATOM   7400  N NH2 . ARG D  2 123 ? 28.235  55.365 3.601   1.00 29.04  ? 123  ARG D NH2 1 
ATOM   7401  N N   . LEU D  2 124 ? 28.476  59.912 1.144   1.00 30.92  ? 124  LEU D N   1 
ATOM   7402  C CA  . LEU D  2 124 ? 27.076  59.920 0.704   1.00 34.54  ? 124  LEU D CA  1 
ATOM   7403  C C   . LEU D  2 124 ? 26.744  61.079 -0.248  1.00 37.32  ? 124  LEU D C   1 
ATOM   7404  O O   . LEU D  2 124 ? 25.826  60.969 -1.059  1.00 40.84  ? 124  LEU D O   1 
ATOM   7405  C CB  . LEU D  2 124 ? 26.134  59.945 1.916   1.00 34.79  ? 124  LEU D CB  1 
ATOM   7406  C CG  . LEU D  2 124 ? 26.133  58.675 2.783   1.00 33.40  ? 124  LEU D CG  1 
ATOM   7407  C CD1 . LEU D  2 124 ? 25.544  58.940 4.166   1.00 32.92  ? 124  LEU D CD1 1 
ATOM   7408  C CD2 . LEU D  2 124 ? 25.396  57.537 2.092   1.00 36.34  ? 124  LEU D CD2 1 
ATOM   7409  N N   . GLN D  2 125 ? 27.482  62.183 -0.138  1.00 36.28  ? 125  GLN D N   1 
ATOM   7410  C CA  . GLN D  2 125 ? 27.340  63.305 -1.064  1.00 39.14  ? 125  GLN D CA  1 
ATOM   7411  C C   . GLN D  2 125 ? 27.953  62.974 -2.409  1.00 40.02  ? 125  GLN D C   1 
ATOM   7412  O O   . GLN D  2 125 ? 27.323  63.153 -3.448  1.00 43.51  ? 125  GLN D O   1 
ATOM   7413  C CB  . GLN D  2 125 ? 28.034  64.554 -0.527  1.00 38.10  ? 125  GLN D CB  1 
ATOM   7414  C CG  . GLN D  2 125 ? 27.374  65.177 0.682   1.00 38.34  ? 125  GLN D CG  1 
ATOM   7415  C CD  . GLN D  2 125 ? 28.099  66.427 1.127   1.00 37.96  ? 125  GLN D CD  1 
ATOM   7416  O OE1 . GLN D  2 125 ? 28.076  67.443 0.431   1.00 40.86  ? 125  GLN D OE1 1 
ATOM   7417  N NE2 . GLN D  2 125 ? 28.754  66.362 2.282   1.00 34.89  ? 125  GLN D NE2 1 
ATOM   7418  N N   . LEU D  2 126 ? 29.196  62.506 -2.379  1.00 37.31  ? 126  LEU D N   1 
ATOM   7419  C CA  . LEU D  2 126 ? 29.950  62.264 -3.600  1.00 38.23  ? 126  LEU D CA  1 
ATOM   7420  C C   . LEU D  2 126 ? 29.379  61.109 -4.410  1.00 40.31  ? 126  LEU D C   1 
ATOM   7421  O O   . LEU D  2 126 ? 29.362  61.169 -5.631  1.00 42.88  ? 126  LEU D O   1 
ATOM   7422  C CB  . LEU D  2 126 ? 31.431  62.023 -3.288  1.00 35.27  ? 126  LEU D CB  1 
ATOM   7423  C CG  . LEU D  2 126 ? 32.148  63.133 -2.507  1.00 33.69  ? 126  LEU D CG  1 
ATOM   7424  C CD1 . LEU D  2 126 ? 33.656  62.945 -2.563  1.00 32.12  ? 126  LEU D CD1 1 
ATOM   7425  C CD2 . LEU D  2 126 ? 31.765  64.508 -3.028  1.00 36.39  ? 126  LEU D CD2 1 
ATOM   7426  N N   . ARG D  2 127 ? 28.901  60.069 -3.734  1.00 39.71  ? 127  ARG D N   1 
ATOM   7427  C CA  . ARG D  2 127 ? 28.322  58.904 -4.413  1.00 42.20  ? 127  ARG D CA  1 
ATOM   7428  C C   . ARG D  2 127 ? 29.326  58.346 -5.440  1.00 42.63  ? 127  ARG D C   1 
ATOM   7429  O O   . ARG D  2 127 ? 30.490  58.143 -5.095  1.00 40.05  ? 127  ARG D O   1 
ATOM   7430  C CB  . ARG D  2 127 ? 26.940  59.256 -5.006  1.00 46.36  ? 127  ARG D CB  1 
ATOM   7431  C CG  . ARG D  2 127 ? 25.860  59.362 -3.935  1.00 46.77  ? 127  ARG D CG  1 
ATOM   7432  C CD  . ARG D  2 127 ? 24.862  60.505 -4.133  1.00 50.03  ? 127  ARG D CD  1 
ATOM   7433  N NE  . ARG D  2 127 ? 24.021  60.551 -5.343  1.00 54.99  ? 127  ARG D NE  1 
ATOM   7434  C CZ  . ARG D  2 127 ? 23.565  59.525 -6.073  1.00 57.72  ? 127  ARG D CZ  1 
ATOM   7435  N NH1 . ARG D  2 127 ? 23.839  58.254 -5.789  1.00 56.27  ? 127  ARG D NH1 1 
ATOM   7436  N NH2 . ARG D  2 127 ? 22.797  59.785 -7.131  1.00 62.59  ? 127  ARG D NH2 1 
ATOM   7437  N N   . ASP D  2 128 ? 28.909  58.124 -6.686  1.00 46.21  ? 128  ASP D N   1 
ATOM   7438  C CA  . ASP D  2 128 ? 29.803  57.551 -7.695  1.00 47.16  ? 128  ASP D CA  1 
ATOM   7439  C C   . ASP D  2 128 ? 30.547  58.613 -8.523  1.00 47.61  ? 128  ASP D C   1 
ATOM   7440  O O   . ASP D  2 128 ? 31.106  58.297 -9.571  1.00 49.36  ? 128  ASP D O   1 
ATOM   7441  C CB  . ASP D  2 128 ? 29.027  56.591 -8.615  1.00 51.15  ? 128  ASP D CB  1 
ATOM   7442  C CG  . ASP D  2 128 ? 27.967  57.295 -9.452  1.00 54.99  ? 128  ASP D CG  1 
ATOM   7443  O OD1 . ASP D  2 128 ? 27.734  58.504 -9.240  1.00 54.73  ? 128  ASP D OD1 1 
ATOM   7444  O OD2 . ASP D  2 128 ? 27.364  56.633 -10.324 1.00 58.82  ? 128  ASP D OD2 1 
ATOM   7445  N N   . ASN D  2 129 ? 30.553  59.863 -8.055  1.00 46.52  ? 129  ASN D N   1 
ATOM   7446  C CA  . ASN D  2 129 ? 31.312  60.940 -8.709  1.00 47.16  ? 129  ASN D CA  1 
ATOM   7447  C C   . ASN D  2 129 ? 32.784  61.023 -8.270  1.00 44.26  ? 129  ASN D C   1 
ATOM   7448  O O   . ASN D  2 129 ? 33.518  61.903 -8.738  1.00 44.99  ? 129  ASN D O   1 
ATOM   7449  C CB  . ASN D  2 129 ? 30.631  62.300 -8.481  1.00 48.38  ? 129  ASN D CB  1 
ATOM   7450  C CG  . ASN D  2 129 ? 29.438  62.531 -9.400  1.00 52.87  ? 129  ASN D CG  1 
ATOM   7451  O OD1 . ASN D  2 129 ? 28.927  61.607 -10.045 1.00 54.94  ? 129  ASN D OD1 1 
ATOM   7452  N ND2 . ASN D  2 129 ? 28.991  63.781 -9.468  1.00 54.95  ? 129  ASN D ND2 1 
ATOM   7453  N N   . ALA D  2 130 ? 33.215  60.117 -7.387  1.00 41.50  ? 130  ALA D N   1 
ATOM   7454  C CA  . ALA D  2 130 ? 34.614  60.045 -6.952  1.00 39.32  ? 130  ALA D CA  1 
ATOM   7455  C C   . ALA D  2 130 ? 35.008  58.616 -6.594  1.00 38.31  ? 130  ALA D C   1 
ATOM   7456  O O   . ALA D  2 130 ? 34.156  57.813 -6.236  1.00 38.32  ? 130  ALA D O   1 
ATOM   7457  C CB  . ALA D  2 130 ? 34.838  60.959 -5.761  1.00 36.87  ? 130  ALA D CB  1 
ATOM   7458  N N   . LYS D  2 131 ? 36.300  58.309 -6.693  1.00 38.02  ? 131  LYS D N   1 
ATOM   7459  C CA  . LYS D  2 131 ? 36.835  57.001 -6.305  1.00 37.60  ? 131  LYS D CA  1 
ATOM   7460  C C   . LYS D  2 131 ? 37.083  56.953 -4.800  1.00 34.58  ? 131  LYS D C   1 
ATOM   7461  O O   . LYS D  2 131 ? 37.802  57.794 -4.268  1.00 33.15  ? 131  LYS D O   1 
ATOM   7462  C CB  . LYS D  2 131 ? 38.166  56.732 -7.009  1.00 39.26  ? 131  LYS D CB  1 
ATOM   7463  C CG  . LYS D  2 131 ? 38.112  56.705 -8.529  1.00 42.62  ? 131  LYS D CG  1 
ATOM   7464  C CD  . LYS D  2 131 ? 39.517  56.836 -9.116  1.00 44.27  ? 131  LYS D CD  1 
ATOM   7465  C CE  . LYS D  2 131 ? 39.646  56.227 -10.509 1.00 48.01  ? 131  LYS D CE  1 
ATOM   7466  N NZ  . LYS D  2 131 ? 39.512  54.737 -10.493 1.00 49.28  ? 131  LYS D NZ  1 
ATOM   7467  N N   . GLU D  2 132 ? 36.500  55.969 -4.120  1.00 33.97  ? 132  GLU D N   1 
ATOM   7468  C CA  . GLU D  2 132 ? 36.785  55.741 -2.708  1.00 31.54  ? 132  GLU D CA  1 
ATOM   7469  C C   . GLU D  2 132 ? 38.110  54.984 -2.584  1.00 32.16  ? 132  GLU D C   1 
ATOM   7470  O O   . GLU D  2 132 ? 38.174  53.784 -2.842  1.00 33.92  ? 132  GLU D O   1 
ATOM   7471  C CB  . GLU D  2 132 ? 35.648  54.962 -2.050  1.00 31.24  ? 132  GLU D CB  1 
ATOM   7472  C CG  . GLU D  2 132 ? 35.804  54.790 -0.547  1.00 28.85  ? 132  GLU D CG  1 
ATOM   7473  C CD  . GLU D  2 132 ? 34.545  54.283 0.137   1.00 28.73  ? 132  GLU D CD  1 
ATOM   7474  O OE1 . GLU D  2 132 ? 33.702  53.642 -0.527  1.00 30.97  ? 132  GLU D OE1 1 
ATOM   7475  O OE2 . GLU D  2 132 ? 34.398  54.533 1.349   1.00 26.73  ? 132  GLU D OE2 1 
ATOM   7476  N N   . LEU D  2 133 ? 39.163  55.695 -2.187  1.00 31.30  ? 133  LEU D N   1 
ATOM   7477  C CA  . LEU D  2 133 ? 40.526  55.144 -2.195  1.00 32.70  ? 133  LEU D CA  1 
ATOM   7478  C C   . LEU D  2 133 ? 40.803  54.079 -1.126  1.00 32.48  ? 133  LEU D C   1 
ATOM   7479  O O   . LEU D  2 133 ? 41.688  53.241 -1.307  1.00 34.64  ? 133  LEU D O   1 
ATOM   7480  C CB  . LEU D  2 133 ? 41.557  56.280 -2.086  1.00 32.39  ? 133  LEU D CB  1 
ATOM   7481  C CG  . LEU D  2 133 ? 42.110  56.860 -3.396  1.00 34.72  ? 133  LEU D CG  1 
ATOM   7482  C CD1 . LEU D  2 133 ? 41.102  56.837 -4.536  1.00 35.82  ? 133  LEU D CD1 1 
ATOM   7483  C CD2 . LEU D  2 133 ? 42.622  58.274 -3.169  1.00 34.20  ? 133  LEU D CD2 1 
ATOM   7484  N N   . GLY D  2 134 ? 40.058  54.118 -0.023  1.00 30.38  ? 134  GLY D N   1 
ATOM   7485  C CA  . GLY D  2 134 ? 40.235  53.160 1.073   1.00 30.29  ? 134  GLY D CA  1 
ATOM   7486  C C   . GLY D  2 134 ? 41.037  53.694 2.252   1.00 28.88  ? 134  GLY D C   1 
ATOM   7487  O O   . GLY D  2 134 ? 41.233  52.980 3.245   1.00 28.88  ? 134  GLY D O   1 
ATOM   7488  N N   . ASN D  2 135 ? 41.477  54.950 2.162   1.00 28.15  ? 135  ASN D N   1 
ATOM   7489  C CA  . ASN D  2 135 ? 42.357  55.550 3.173   1.00 27.46  ? 135  ASN D CA  1 
ATOM   7490  C C   . ASN D  2 135 ? 41.790  56.812 3.821   1.00 24.82  ? 135  ASN D C   1 
ATOM   7491  O O   . ASN D  2 135 ? 42.502  57.529 4.528   1.00 24.51  ? 135  ASN D O   1 
ATOM   7492  C CB  . ASN D  2 135 ? 43.713  55.871 2.540   1.00 30.14  ? 135  ASN D CB  1 
ATOM   7493  C CG  . ASN D  2 135 ? 43.599  56.830 1.371   1.00 31.03  ? 135  ASN D CG  1 
ATOM   7494  O OD1 . ASN D  2 135 ? 42.523  57.345 1.070   1.00 29.73  ? 135  ASN D OD1 1 
ATOM   7495  N ND2 . ASN D  2 135 ? 44.708  57.056 0.692   1.00 33.91  ? 135  ASN D ND2 1 
ATOM   7496  N N   . GLY D  2 136 ? 40.512  57.085 3.577   1.00 23.39  ? 136  GLY D N   1 
ATOM   7497  C CA  . GLY D  2 136 ? 39.887  58.323 4.036   1.00 21.67  ? 136  GLY D CA  1 
ATOM   7498  C C   . GLY D  2 136 ? 39.774  59.380 2.950   1.00 22.43  ? 136  GLY D C   1 
ATOM   7499  O O   . GLY D  2 136 ? 39.137  60.414 3.153   1.00 21.82  ? 136  GLY D O   1 
ATOM   7500  N N   . CYS D  2 137 ? 40.384  59.119 1.796   1.00 24.13  ? 137  CYS D N   1 
ATOM   7501  C CA  . CYS D  2 137 ? 40.382  60.072 0.696   1.00 25.45  ? 137  CYS D CA  1 
ATOM   7502  C C   . CYS D  2 137 ? 39.430  59.665 -0.415  1.00 26.37  ? 137  CYS D C   1 
ATOM   7503  O O   . CYS D  2 137 ? 39.162  58.480 -0.626  1.00 26.73  ? 137  CYS D O   1 
ATOM   7504  C CB  . CYS D  2 137 ? 41.790  60.248 0.128   1.00 27.45  ? 137  CYS D CB  1 
ATOM   7505  S SG  . CYS D  2 137 ? 43.000  60.822 1.338   1.00 27.27  ? 137  CYS D SG  1 
ATOM   7506  N N   . PHE D  2 138 ? 38.921  60.676 -1.112  1.00 27.18  ? 138  PHE D N   1 
ATOM   7507  C CA  . PHE D  2 138 ? 38.097  60.495 -2.290  1.00 28.77  ? 138  PHE D CA  1 
ATOM   7508  C C   . PHE D  2 138 ? 38.761  61.213 -3.448  1.00 31.07  ? 138  PHE D C   1 
ATOM   7509  O O   . PHE D  2 138 ? 39.019  62.406 -3.359  1.00 31.53  ? 138  PHE D O   1 
ATOM   7510  C CB  . PHE D  2 138 ? 36.711  61.085 -2.063  1.00 28.49  ? 138  PHE D CB  1 
ATOM   7511  C CG  . PHE D  2 138 ? 35.930  60.391 -0.988  1.00 26.69  ? 138  PHE D CG  1 
ATOM   7512  C CD1 . PHE D  2 138 ? 35.183  59.257 -1.281  1.00 27.32  ? 138  PHE D CD1 1 
ATOM   7513  C CD2 . PHE D  2 138 ? 35.948  60.865 0.318   1.00 24.75  ? 138  PHE D CD2 1 
ATOM   7514  C CE1 . PHE D  2 138 ? 34.467  58.611 -0.294  1.00 26.15  ? 138  PHE D CE1 1 
ATOM   7515  C CE2 . PHE D  2 138 ? 35.230  60.225 1.309   1.00 23.40  ? 138  PHE D CE2 1 
ATOM   7516  C CZ  . PHE D  2 138 ? 34.492  59.095 1.003   1.00 24.13  ? 138  PHE D CZ  1 
ATOM   7517  N N   . GLU D  2 139 ? 39.025  60.486 -4.530  1.00 32.91  ? 139  GLU D N   1 
ATOM   7518  C CA  . GLU D  2 139 ? 39.657  61.046 -5.711  1.00 35.50  ? 139  GLU D CA  1 
ATOM   7519  C C   . GLU D  2 139 ? 38.596  61.319 -6.775  1.00 37.42  ? 139  GLU D C   1 
ATOM   7520  O O   . GLU D  2 139 ? 37.898  60.404 -7.211  1.00 38.02  ? 139  GLU D O   1 
ATOM   7521  C CB  . GLU D  2 139 ? 40.703  60.070 -6.232  1.00 36.94  ? 139  GLU D CB  1 
ATOM   7522  C CG  . GLU D  2 139 ? 41.465  60.541 -7.454  1.00 40.03  ? 139  GLU D CG  1 
ATOM   7523  C CD  . GLU D  2 139 ? 42.372  59.455 -7.989  1.00 41.98  ? 139  GLU D CD  1 
ATOM   7524  O OE1 . GLU D  2 139 ? 43.242  58.979 -7.228  1.00 41.45  ? 139  GLU D OE1 1 
ATOM   7525  O OE2 . GLU D  2 139 ? 42.201  59.062 -9.163  1.00 44.46  ? 139  GLU D OE2 1 
ATOM   7526  N N   . PHE D  2 140 ? 38.493  62.577 -7.199  1.00 38.89  ? 140  PHE D N   1 
ATOM   7527  C CA  . PHE D  2 140 ? 37.416  63.016 -8.091  1.00 41.10  ? 140  PHE D CA  1 
ATOM   7528  C C   . PHE D  2 140 ? 37.648  62.619 -9.547  1.00 44.17  ? 140  PHE D C   1 
ATOM   7529  O O   . PHE D  2 140 ? 38.782  62.597 -10.020 1.00 45.28  ? 140  PHE D O   1 
ATOM   7530  C CB  . PHE D  2 140 ? 37.240  64.535 -8.003  1.00 42.17  ? 140  PHE D CB  1 
ATOM   7531  C CG  . PHE D  2 140 ? 36.780  65.014 -6.659  1.00 39.87  ? 140  PHE D CG  1 
ATOM   7532  C CD1 . PHE D  2 140 ? 37.697  65.340 -5.670  1.00 38.09  ? 140  PHE D CD1 1 
ATOM   7533  C CD2 . PHE D  2 140 ? 35.427  65.142 -6.381  1.00 39.97  ? 140  PHE D CD2 1 
ATOM   7534  C CE1 . PHE D  2 140 ? 37.274  65.784 -4.429  1.00 36.26  ? 140  PHE D CE1 1 
ATOM   7535  C CE2 . PHE D  2 140 ? 34.996  65.582 -5.141  1.00 38.24  ? 140  PHE D CE2 1 
ATOM   7536  C CZ  . PHE D  2 140 ? 35.921  65.905 -4.164  1.00 36.30  ? 140  PHE D CZ  1 
ATOM   7537  N N   . TYR D  2 141 ? 36.564  62.306 -10.253 1.00 45.99  ? 141  TYR D N   1 
ATOM   7538  C CA  . TYR D  2 141 ? 36.636  62.059 -11.697 1.00 49.51  ? 141  TYR D CA  1 
ATOM   7539  C C   . TYR D  2 141 ? 36.743  63.380 -12.446 1.00 52.28  ? 141  TYR D C   1 
ATOM   7540  O O   . TYR D  2 141 ? 37.445  63.480 -13.452 1.00 54.83  ? 141  TYR D O   1 
ATOM   7541  C CB  . TYR D  2 141 ? 35.418  61.272 -12.187 1.00 51.01  ? 141  TYR D CB  1 
ATOM   7542  C CG  . TYR D  2 141 ? 35.354  59.877 -11.619 1.00 49.34  ? 141  TYR D CG  1 
ATOM   7543  C CD1 . TYR D  2 141 ? 36.341  58.942 -11.912 1.00 49.71  ? 141  TYR D CD1 1 
ATOM   7544  C CD2 . TYR D  2 141 ? 34.323  59.496 -10.775 1.00 47.94  ? 141  TYR D CD2 1 
ATOM   7545  C CE1 . TYR D  2 141 ? 36.294  57.663 -11.389 1.00 48.79  ? 141  TYR D CE1 1 
ATOM   7546  C CE2 . TYR D  2 141 ? 34.267  58.219 -10.244 1.00 46.88  ? 141  TYR D CE2 1 
ATOM   7547  C CZ  . TYR D  2 141 ? 35.254  57.306 -10.555 1.00 47.35  ? 141  TYR D CZ  1 
ATOM   7548  O OH  . TYR D  2 141 ? 35.199  56.036 -10.027 1.00 46.89  ? 141  TYR D OH  1 
ATOM   7549  N N   . HIS D  2 142 ? 36.041  64.389 -11.941 1.00 52.24  ? 142  HIS D N   1 
ATOM   7550  C CA  . HIS D  2 142 ? 36.119  65.745 -12.474 1.00 55.16  ? 142  HIS D CA  1 
ATOM   7551  C C   . HIS D  2 142 ? 37.185  66.546 -11.739 1.00 54.01  ? 142  HIS D C   1 
ATOM   7552  O O   . HIS D  2 142 ? 37.533  66.241 -10.596 1.00 50.72  ? 142  HIS D O   1 
ATOM   7553  C CB  . HIS D  2 142 ? 34.764  66.455 -12.359 1.00 56.71  ? 142  HIS D CB  1 
ATOM   7554  C CG  . HIS D  2 142 ? 34.204  66.480 -10.972 1.00 53.71  ? 142  HIS D CG  1 
ATOM   7555  N ND1 . HIS D  2 142 ? 34.335  67.565 -10.132 1.00 53.24  ? 142  HIS D ND1 1 
ATOM   7556  C CD2 . HIS D  2 142 ? 33.514  65.545 -10.274 1.00 51.43  ? 142  HIS D CD2 1 
ATOM   7557  C CE1 . HIS D  2 142 ? 33.745  67.298 -8.979  1.00 50.63  ? 142  HIS D CE1 1 
ATOM   7558  N NE2 . HIS D  2 142 ? 33.240  66.079 -9.040  1.00 49.47  ? 142  HIS D NE2 1 
ATOM   7559  N N   . LYS D  2 143 ? 37.702  67.570 -12.407 1.00 57.22  ? 143  LYS D N   1 
ATOM   7560  C CA  . LYS D  2 143 ? 38.618  68.511 -11.778 1.00 57.24  ? 143  LYS D CA  1 
ATOM   7561  C C   . LYS D  2 143 ? 37.829  69.294 -10.732 1.00 56.27  ? 143  LYS D C   1 
ATOM   7562  O O   . LYS D  2 143 ? 36.759  69.825 -11.032 1.00 58.38  ? 143  LYS D O   1 
ATOM   7563  C CB  . LYS D  2 143 ? 39.208  69.453 -12.826 1.00 61.72  ? 143  LYS D CB  1 
ATOM   7564  C CG  . LYS D  2 143 ? 40.418  70.241 -12.360 1.00 62.49  ? 143  LYS D CG  1 
ATOM   7565  C CD  . LYS D  2 143 ? 40.912  71.169 -13.463 1.00 67.60  ? 143  LYS D CD  1 
ATOM   7566  C CE  . LYS D  2 143 ? 41.708  72.339 -12.907 1.00 69.47  ? 143  LYS D CE  1 
ATOM   7567  N NZ  . LYS D  2 143 ? 40.856  73.365 -12.236 1.00 70.09  ? 143  LYS D NZ  1 
ATOM   7568  N N   . CYS D  2 144 ? 38.345  69.344 -9.506  1.00 53.51  ? 144  CYS D N   1 
ATOM   7569  C CA  . CYS D  2 144 ? 37.632  69.959 -8.388  1.00 52.38  ? 144  CYS D CA  1 
ATOM   7570  C C   . CYS D  2 144 ? 38.424  71.148 -7.837  1.00 53.74  ? 144  CYS D C   1 
ATOM   7571  O O   . CYS D  2 144 ? 39.390  70.974 -7.092  1.00 51.87  ? 144  CYS D O   1 
ATOM   7572  C CB  . CYS D  2 144 ? 37.382  68.912 -7.297  1.00 48.06  ? 144  CYS D CB  1 
ATOM   7573  S SG  . CYS D  2 144 ? 36.274  69.414 -5.956  1.00 46.72  ? 144  CYS D SG  1 
ATOM   7574  N N   . ASP D  2 145 ? 38.012  72.356 -8.217  1.00 57.56  ? 145  ASP D N   1 
ATOM   7575  C CA  . ASP D  2 145 ? 38.672  73.585 -7.760  1.00 59.87  ? 145  ASP D CA  1 
ATOM   7576  C C   . ASP D  2 145 ? 38.321  73.883 -6.291  1.00 57.73  ? 145  ASP D C   1 
ATOM   7577  O O   . ASP D  2 145 ? 37.615  73.103 -5.650  1.00 54.30  ? 145  ASP D O   1 
ATOM   7578  C CB  . ASP D  2 145 ? 38.331  74.766 -8.690  1.00 65.37  ? 145  ASP D CB  1 
ATOM   7579  C CG  . ASP D  2 145 ? 36.855  75.146 -8.667  1.00 66.86  ? 145  ASP D CG  1 
ATOM   7580  O OD1 . ASP D  2 145 ? 36.082  74.572 -7.876  1.00 63.69  ? 145  ASP D OD1 1 
ATOM   7581  O OD2 . ASP D  2 145 ? 36.463  76.031 -9.454  1.00 71.72  ? 145  ASP D OD2 1 
ATOM   7582  N N   . ASN D  2 146 ? 38.818  75.001 -5.763  1.00 60.13  ? 146  ASN D N   1 
ATOM   7583  C CA  . ASN D  2 146 ? 38.601  75.352 -4.353  1.00 58.60  ? 146  ASN D CA  1 
ATOM   7584  C C   . ASN D  2 146 ? 37.142  75.647 -4.001  1.00 59.20  ? 146  ASN D C   1 
ATOM   7585  O O   . ASN D  2 146 ? 36.732  75.453 -2.860  1.00 56.70  ? 146  ASN D O   1 
ATOM   7586  C CB  . ASN D  2 146 ? 39.485  76.533 -3.947  1.00 61.88  ? 146  ASN D CB  1 
ATOM   7587  C CG  . ASN D  2 146 ? 40.966  76.193 -3.970  1.00 61.29  ? 146  ASN D CG  1 
ATOM   7588  O OD1 . ASN D  2 146 ? 41.358  75.028 -4.045  1.00 57.85  ? 146  ASN D OD1 1 
ATOM   7589  N ND2 . ASN D  2 146 ? 41.799  77.218 -3.901  1.00 65.23  ? 146  ASN D ND2 1 
ATOM   7590  N N   . GLU D  2 147 ? 36.361  76.099 -4.977  1.00 62.95  ? 147  GLU D N   1 
ATOM   7591  C CA  . GLU D  2 147 ? 34.919  76.267 -4.790  1.00 64.19  ? 147  GLU D CA  1 
ATOM   7592  C C   . GLU D  2 147 ? 34.235  74.895 -4.757  1.00 60.26  ? 147  GLU D C   1 
ATOM   7593  O O   . GLU D  2 147 ? 33.356  74.645 -3.929  1.00 58.86  ? 147  GLU D O   1 
ATOM   7594  C CB  . GLU D  2 147 ? 34.309  77.122 -5.903  1.00 69.95  ? 147  GLU D CB  1 
ATOM   7595  C CG  . GLU D  2 147 ? 34.889  78.527 -6.030  1.00 75.02  ? 147  GLU D CG  1 
ATOM   7596  C CD  . GLU D  2 147 ? 36.065  78.598 -6.992  1.00 76.45  ? 147  GLU D CD  1 
ATOM   7597  O OE1 . GLU D  2 147 ? 37.153  78.085 -6.646  1.00 73.26  ? 147  GLU D OE1 1 
ATOM   7598  O OE2 . GLU D  2 147 ? 35.898  79.156 -8.100  1.00 81.15  ? 147  GLU D OE2 1 
ATOM   7599  N N   . CYS D  2 148 ? 34.645  74.017 -5.670  1.00 59.09  ? 148  CYS D N   1 
ATOM   7600  C CA  . CYS D  2 148 ? 34.166  72.635 -5.706  1.00 55.70  ? 148  CYS D CA  1 
ATOM   7601  C C   . CYS D  2 148 ? 34.478  71.919 -4.388  1.00 51.18  ? 148  CYS D C   1 
ATOM   7602  O O   . CYS D  2 148 ? 33.634  71.200 -3.852  1.00 49.19  ? 148  CYS D O   1 
ATOM   7603  C CB  . CYS D  2 148 ? 34.791  71.891 -6.894  1.00 55.57  ? 148  CYS D CB  1 
ATOM   7604  S SG  . CYS D  2 148 ? 34.597  70.093 -6.885  1.00 51.39  ? 148  CYS D SG  1 
ATOM   7605  N N   . MET D  2 149 ? 35.684  72.128 -3.865  1.00 50.16  ? 149  MET D N   1 
ATOM   7606  C CA  . MET D  2 149 ? 36.065  71.563 -2.572  1.00 46.44  ? 149  MET D CA  1 
ATOM   7607  C C   . MET D  2 149 ? 35.216  72.152 -1.448  1.00 46.92  ? 149  MET D C   1 
ATOM   7608  O O   . MET D  2 149 ? 34.835  71.445 -0.515  1.00 43.95  ? 149  MET D O   1 
ATOM   7609  C CB  . MET D  2 149 ? 37.542  71.827 -2.278  1.00 46.06  ? 149  MET D CB  1 
ATOM   7610  C CG  . MET D  2 149 ? 38.519  71.170 -3.239  1.00 45.96  ? 149  MET D CG  1 
ATOM   7611  S SD  . MET D  2 149 ? 38.473  69.374 -3.202  1.00 41.85  ? 149  MET D SD  1 
ATOM   7612  C CE  . MET D  2 149 ? 39.932  68.983 -4.165  1.00 43.12  ? 149  MET D CE  1 
ATOM   7613  N N   . GLU D  2 150 ? 34.926  73.446 -1.539  1.00 51.33  ? 150  GLU D N   1 
ATOM   7614  C CA  . GLU D  2 150 ? 34.123  74.128 -0.525  1.00 52.86  ? 150  GLU D CA  1 
ATOM   7615  C C   . GLU D  2 150 ? 32.689  73.596 -0.466  1.00 53.02  ? 150  GLU D C   1 
ATOM   7616  O O   . GLU D  2 150 ? 32.091  73.565 0.608   1.00 52.20  ? 150  GLU D O   1 
ATOM   7617  C CB  . GLU D  2 150 ? 34.125  75.646 -0.771  1.00 58.18  ? 150  GLU D CB  1 
ATOM   7618  C CG  . GLU D  2 150 ? 33.352  76.482 0.248   1.00 60.33  ? 150  GLU D CG  1 
ATOM   7619  C CD  . GLU D  2 150 ? 33.850  76.311 1.673   1.00 57.32  ? 150  GLU D CD  1 
ATOM   7620  O OE1 . GLU D  2 150 ? 35.070  76.131 1.866   1.00 55.62  ? 150  GLU D OE1 1 
ATOM   7621  O OE2 . GLU D  2 150 ? 33.022  76.356 2.608   1.00 57.16  ? 150  GLU D OE2 1 
ATOM   7622  N N   . SER D  2 151 ? 32.143  73.182 -1.608  1.00 54.79  ? 151  SER D N   1 
ATOM   7623  C CA  . SER D  2 151 ? 30.782  72.635 -1.660  1.00 55.68  ? 151  SER D CA  1 
ATOM   7624  C C   . SER D  2 151 ? 30.682  71.282 -0.945  1.00 51.55  ? 151  SER D C   1 
ATOM   7625  O O   . SER D  2 151 ? 29.652  70.957 -0.349  1.00 51.58  ? 151  SER D O   1 
ATOM   7626  C CB  . SER D  2 151 ? 30.306  72.497 -3.107  1.00 58.59  ? 151  SER D CB  1 
ATOM   7627  O OG  . SER D  2 151 ? 31.062  71.528 -3.806  1.00 56.07  ? 151  SER D OG  1 
ATOM   7628  N N   . VAL D  2 152 ? 31.757  70.499 -1.011  1.00 48.79  ? 152  VAL D N   1 
ATOM   7629  C CA  . VAL D  2 152 ? 31.831  69.222 -0.305  1.00 45.20  ? 152  VAL D CA  1 
ATOM   7630  C C   . VAL D  2 152 ? 31.880  69.490 1.198   1.00 44.13  ? 152  VAL D C   1 
ATOM   7631  O O   . VAL D  2 152 ? 31.210  68.815 1.982   1.00 42.55  ? 152  VAL D O   1 
ATOM   7632  C CB  . VAL D  2 152 ? 33.068  68.401 -0.732  1.00 42.69  ? 152  VAL D CB  1 
ATOM   7633  C CG1 . VAL D  2 152 ? 33.121  67.075 0.018   1.00 39.12  ? 152  VAL D CG1 1 
ATOM   7634  C CG2 . VAL D  2 152 ? 33.056  68.155 -2.237  1.00 44.70  ? 152  VAL D CG2 1 
ATOM   7635  N N   . ARG D  2 153 ? 32.677  70.480 1.589   1.00 45.72  ? 153  ARG D N   1 
ATOM   7636  C CA  . ARG D  2 153 ? 32.732  70.924 2.980   1.00 45.67  ? 153  ARG D CA  1 
ATOM   7637  C C   . ARG D  2 153 ? 31.418  71.577 3.423   1.00 49.55  ? 153  ARG D C   1 
ATOM   7638  O O   . ARG D  2 153 ? 30.967  71.370 4.549   1.00 48.34  ? 153  ARG D O   1 
ATOM   7639  C CB  . ARG D  2 153 ? 33.906  71.887 3.187   1.00 46.41  ? 153  ARG D CB  1 
ATOM   7640  C CG  . ARG D  2 153 ? 35.241  71.181 3.340   1.00 43.25  ? 153  ARG D CG  1 
ATOM   7641  C CD  . ARG D  2 153 ? 36.382  72.137 3.657   1.00 44.71  ? 153  ARG D CD  1 
ATOM   7642  N NE  . ARG D  2 153 ? 37.318  72.245 2.534   1.00 46.14  ? 153  ARG D NE  1 
ATOM   7643  C CZ  . ARG D  2 153 ? 37.414  73.275 1.694   1.00 49.90  ? 153  ARG D CZ  1 
ATOM   7644  N NH1 . ARG D  2 153 ? 36.643  74.349 1.822   1.00 52.92  ? 153  ARG D NH1 1 
ATOM   7645  N NH2 . ARG D  2 153 ? 38.308  73.230 0.710   1.00 51.13  ? 153  ARG D NH2 1 
ATOM   7646  N N   . ASN D  2 154 ? 30.824  72.369 2.529   1.00 55.51  ? 154  ASN D N   1 
ATOM   7647  C CA  . ASN D  2 154 ? 29.498  72.974 2.731   1.00 60.53  ? 154  ASN D CA  1 
ATOM   7648  C C   . ASN D  2 154 ? 28.407  71.983 3.123   1.00 58.38  ? 154  ASN D C   1 
ATOM   7649  O O   . ASN D  2 154 ? 27.549  72.292 3.951   1.00 59.93  ? 154  ASN D O   1 
ATOM   7650  C CB  . ASN D  2 154 ? 29.018  73.641 1.434   1.00 67.54  ? 154  ASN D CB  1 
ATOM   7651  C CG  . ASN D  2 154 ? 29.354  75.116 1.347   1.00 75.25  ? 154  ASN D CG  1 
ATOM   7652  O OD1 . ASN D  2 154 ? 29.835  75.722 2.303   1.00 75.54  ? 154  ASN D OD1 1 
ATOM   7653  N ND2 . ASN D  2 154 ? 29.084  75.706 0.176   1.00 84.38  ? 154  ASN D ND2 1 
ATOM   7654  N N   . GLY D  2 155 ? 28.446  70.801 2.508   1.00 55.01  ? 155  GLY D N   1 
ATOM   7655  C CA  . GLY D  2 155 ? 27.302  69.897 2.464   1.00 54.45  ? 155  GLY D CA  1 
ATOM   7656  C C   . GLY D  2 155 ? 26.473  70.172 1.218   1.00 58.05  ? 155  GLY D C   1 
ATOM   7657  O O   . GLY D  2 155 ? 25.367  69.654 1.078   1.00 60.00  ? 155  GLY D O   1 
ATOM   7658  N N   . THR D  2 156 ? 27.027  70.971 0.305   1.00 59.28  ? 156  THR D N   1 
ATOM   7659  C CA  . THR D  2 156 ? 26.297  71.519 -0.843  1.00 63.68  ? 156  THR D CA  1 
ATOM   7660  C C   . THR D  2 156 ? 26.773  70.935 -2.180  1.00 62.84  ? 156  THR D C   1 
ATOM   7661  O O   . THR D  2 156 ? 26.331  71.371 -3.241  1.00 66.99  ? 156  THR D O   1 
ATOM   7662  C CB  . THR D  2 156 ? 26.457  73.057 -0.861  1.00 67.55  ? 156  THR D CB  1 
ATOM   7663  O OG1 . THR D  2 156 ? 25.895  73.604 0.338   1.00 68.61  ? 156  THR D OG1 1 
ATOM   7664  C CG2 . THR D  2 156 ? 25.771  73.710 -2.066  1.00 73.43  ? 156  THR D CG2 1 
ATOM   7665  N N   . TYR D  2 157 ? 27.656  69.939 -2.136  1.00 57.81  ? 157  TYR D N   1 
ATOM   7666  C CA  . TYR D  2 157 ? 28.219  69.362 -3.361  1.00 57.11  ? 157  TYR D CA  1 
ATOM   7667  C C   . TYR D  2 157 ? 27.123  68.946 -4.343  1.00 60.42  ? 157  TYR D C   1 
ATOM   7668  O O   . TYR D  2 157 ? 26.318  68.062 -4.048  1.00 59.98  ? 157  TYR D O   1 
ATOM   7669  C CB  . TYR D  2 157 ? 29.105  68.155 -3.039  1.00 52.13  ? 157  TYR D CB  1 
ATOM   7670  C CG  . TYR D  2 157 ? 29.677  67.492 -4.273  1.00 52.03  ? 157  TYR D CG  1 
ATOM   7671  C CD1 . TYR D  2 157 ? 30.764  68.046 -4.945  1.00 52.42  ? 157  TYR D CD1 1 
ATOM   7672  C CD2 . TYR D  2 157 ? 29.123  66.320 -4.778  1.00 52.05  ? 157  TYR D CD2 1 
ATOM   7673  C CE1 . TYR D  2 157 ? 31.287  67.447 -6.078  1.00 52.80  ? 157  TYR D CE1 1 
ATOM   7674  C CE2 . TYR D  2 157 ? 29.639  65.714 -5.911  1.00 52.49  ? 157  TYR D CE2 1 
ATOM   7675  C CZ  . TYR D  2 157 ? 30.720  66.280 -6.556  1.00 52.78  ? 157  TYR D CZ  1 
ATOM   7676  O OH  . TYR D  2 157 ? 31.232  65.676 -7.679  1.00 53.54  ? 157  TYR D OH  1 
ATOM   7677  N N   . ASP D  2 158 ? 27.102  69.584 -5.510  1.00 64.04  ? 158  ASP D N   1 
ATOM   7678  C CA  . ASP D  2 158 ? 26.049  69.339 -6.491  1.00 68.14  ? 158  ASP D CA  1 
ATOM   7679  C C   . ASP D  2 158 ? 26.386  68.131 -7.365  1.00 66.70  ? 158  ASP D C   1 
ATOM   7680  O O   . ASP D  2 158 ? 27.042  68.260 -8.404  1.00 67.77  ? 158  ASP D O   1 
ATOM   7681  C CB  . ASP D  2 158 ? 25.801  70.583 -7.353  1.00 73.54  ? 158  ASP D CB  1 
ATOM   7682  C CG  . ASP D  2 158 ? 24.433  70.571 -8.010  1.00 78.95  ? 158  ASP D CG  1 
ATOM   7683  O OD1 . ASP D  2 158 ? 23.428  70.374 -7.293  1.00 79.90  ? 158  ASP D OD1 1 
ATOM   7684  O OD2 . ASP D  2 158 ? 24.355  70.765 -9.240  1.00 82.67  ? 158  ASP D OD2 1 
ATOM   7685  N N   . TYR D  2 159 ? 25.927  66.960 -6.925  1.00 64.62  ? 159  TYR D N   1 
ATOM   7686  C CA  . TYR D  2 159 ? 26.121  65.712 -7.660  1.00 63.70  ? 159  TYR D CA  1 
ATOM   7687  C C   . TYR D  2 159 ? 25.609  65.797 -9.110  1.00 68.63  ? 159  TYR D C   1 
ATOM   7688  O O   . TYR D  2 159 ? 26.341  65.439 -10.034 1.00 68.52  ? 159  TYR D O   1 
ATOM   7689  C CB  . TYR D  2 159 ? 25.478  64.538 -6.898  1.00 62.04  ? 159  TYR D CB  1 
ATOM   7690  C CG  . TYR D  2 159 ? 25.456  63.234 -7.660  1.00 62.39  ? 159  TYR D CG  1 
ATOM   7691  C CD1 . TYR D  2 159 ? 26.520  62.342 -7.572  1.00 58.66  ? 159  TYR D CD1 1 
ATOM   7692  C CD2 . TYR D  2 159 ? 24.369  62.890 -8.465  1.00 66.99  ? 159  TYR D CD2 1 
ATOM   7693  C CE1 . TYR D  2 159 ? 26.506  61.147 -8.266  1.00 59.58  ? 159  TYR D CE1 1 
ATOM   7694  C CE2 . TYR D  2 159 ? 24.348  61.698 -9.167  1.00 67.87  ? 159  TYR D CE2 1 
ATOM   7695  C CZ  . TYR D  2 159 ? 25.418  60.828 -9.063  1.00 64.20  ? 159  TYR D CZ  1 
ATOM   7696  O OH  . TYR D  2 159 ? 25.394  59.641 -9.758  1.00 65.69  ? 159  TYR D OH  1 
ATOM   7697  N N   . PRO D  2 160 ? 24.364  66.284 -9.316  1.00 73.39  ? 160  PRO D N   1 
ATOM   7698  C CA  . PRO D  2 160 ? 23.823  66.381 -10.684 1.00 78.70  ? 160  PRO D CA  1 
ATOM   7699  C C   . PRO D  2 160 ? 24.644  67.221 -11.677 1.00 80.29  ? 160  PRO D C   1 
ATOM   7700  O O   . PRO D  2 160 ? 24.569  66.975 -12.884 1.00 83.46  ? 160  PRO D O   1 
ATOM   7701  C CB  . PRO D  2 160 ? 22.441  67.012 -10.471 1.00 83.65  ? 160  PRO D CB  1 
ATOM   7702  C CG  . PRO D  2 160 ? 22.061  66.626 -9.085  1.00 80.75  ? 160  PRO D CG  1 
ATOM   7703  C CD  . PRO D  2 160 ? 23.347  66.652 -8.310  1.00 74.60  ? 160  PRO D CD  1 
ATOM   7704  N N   . GLN D  2 161 ? 25.400  68.204 -11.185 1.00 78.66  ? 161  GLN D N   1 
ATOM   7705  C CA  . GLN D  2 161 ? 26.239  69.041 -12.055 1.00 80.44  ? 161  GLN D CA  1 
ATOM   7706  C C   . GLN D  2 161 ? 27.442  68.265 -12.592 1.00 77.35  ? 161  GLN D C   1 
ATOM   7707  O O   . GLN D  2 161 ? 27.766  68.351 -13.779 1.00 80.08  ? 161  GLN D O   1 
ATOM   7708  C CB  . GLN D  2 161 ? 26.727  70.291 -11.310 1.00 79.95  ? 161  GLN D CB  1 
ATOM   7709  C CG  . GLN D  2 161 ? 27.647  71.200 -12.124 1.00 82.04  ? 161  GLN D CG  1 
ATOM   7710  C CD  . GLN D  2 161 ? 28.303  72.288 -11.288 1.00 81.18  ? 161  GLN D CD  1 
ATOM   7711  O OE1 . GLN D  2 161 ? 28.154  72.330 -10.064 1.00 78.52  ? 161  GLN D OE1 1 
ATOM   7712  N NE2 . GLN D  2 161 ? 29.041  73.173 -11.950 1.00 83.77  ? 161  GLN D NE2 1 
ATOM   7713  N N   . TYR D  2 162 ? 28.101  67.520 -11.710 1.00 72.12  ? 162  TYR D N   1 
ATOM   7714  C CA  . TYR D  2 162 ? 29.315  66.791 -12.066 1.00 69.37  ? 162  TYR D CA  1 
ATOM   7715  C C   . TYR D  2 162 ? 29.052  65.339 -12.494 1.00 69.13  ? 162  TYR D C   1 
ATOM   7716  O O   . TYR D  2 162 ? 30.002  64.582 -12.717 1.00 67.18  ? 162  TYR D O   1 
ATOM   7717  C CB  . TYR D  2 162 ? 30.298  66.816 -10.890 1.00 64.47  ? 162  TYR D CB  1 
ATOM   7718  C CG  . TYR D  2 162 ? 30.666  68.211 -10.420 1.00 65.01  ? 162  TYR D CG  1 
ATOM   7719  C CD1 . TYR D  2 162 ? 31.587  68.989 -11.126 1.00 66.80  ? 162  TYR D CD1 1 
ATOM   7720  C CD2 . TYR D  2 162 ? 30.095  68.753 -9.269  1.00 64.19  ? 162  TYR D CD2 1 
ATOM   7721  C CE1 . TYR D  2 162 ? 31.926  70.266 -10.697 1.00 67.94  ? 162  TYR D CE1 1 
ATOM   7722  C CE2 . TYR D  2 162 ? 30.427  70.027 -8.831  1.00 65.23  ? 162  TYR D CE2 1 
ATOM   7723  C CZ  . TYR D  2 162 ? 31.342  70.781 -9.546  1.00 67.19  ? 162  TYR D CZ  1 
ATOM   7724  O OH  . TYR D  2 162 ? 31.672  72.047 -9.110  1.00 68.82  ? 162  TYR D OH  1 
ATOM   7725  N N   . SER D  2 163 ? 27.778  64.952 -12.613 1.00 71.78  ? 163  SER D N   1 
ATOM   7726  C CA  . SER D  2 163 ? 27.418  63.586 -13.022 1.00 72.30  ? 163  SER D CA  1 
ATOM   7727  C C   . SER D  2 163 ? 27.373  63.479 -14.545 1.00 76.56  ? 163  SER D C   1 
ATOM   7728  O O   . SER D  2 163 ? 26.857  62.504 -15.094 1.00 78.62  ? 163  SER D O   1 
ATOM   7729  C CB  . SER D  2 163 ? 26.068  63.153 -12.411 1.00 73.61  ? 163  SER D CB  1 
ATOM   7730  O OG  . SER D  2 163 ? 24.978  63.700 -13.134 1.00 79.19  ? 163  SER D OG  1 
ATOM   7731  N N   . ASP E  1 1   ? 10.602  56.167 -8.505  1.00 33.28  ? 1    ASP E N   1 
ATOM   7732  C CA  . ASP E  1 1   ? 10.129  55.359 -7.342  1.00 33.77  ? 1    ASP E CA  1 
ATOM   7733  C C   . ASP E  1 1   ? 11.257  55.164 -6.328  1.00 32.16  ? 1    ASP E C   1 
ATOM   7734  O O   . ASP E  1 1   ? 12.414  54.990 -6.710  1.00 31.01  ? 1    ASP E O   1 
ATOM   7735  C CB  . ASP E  1 1   ? 9.591   54.002 -7.814  1.00 35.16  ? 1    ASP E CB  1 
ATOM   7736  C CG  . ASP E  1 1   ? 8.474   54.137 -8.838  1.00 36.97  ? 1    ASP E CG  1 
ATOM   7737  O OD1 . ASP E  1 1   ? 8.140   55.278 -9.222  1.00 37.08  ? 1    ASP E OD1 1 
ATOM   7738  O OD2 . ASP E  1 1   ? 7.930   53.097 -9.265  1.00 38.51  ? 1    ASP E OD2 1 
ATOM   7739  N N   . GLN E  1 2   ? 10.913  55.205 -5.042  1.00 32.21  ? 2    GLN E N   1 
ATOM   7740  C CA  . GLN E  1 2   ? 11.905  55.075 -3.975  1.00 30.84  ? 2    GLN E CA  1 
ATOM   7741  C C   . GLN E  1 2   ? 11.366  54.400 -2.722  1.00 31.36  ? 2    GLN E C   1 
ATOM   7742  O O   . GLN E  1 2   ? 10.171  54.451 -2.438  1.00 32.73  ? 2    GLN E O   1 
ATOM   7743  C CB  . GLN E  1 2   ? 12.468  56.448 -3.597  1.00 29.80  ? 2    GLN E CB  1 
ATOM   7744  C CG  . GLN E  1 2   ? 11.436  57.427 -3.061  1.00 30.68  ? 2    GLN E CG  1 
ATOM   7745  C CD  . GLN E  1 2   ? 12.061  58.674 -2.464  1.00 29.83  ? 2    GLN E CD  1 
ATOM   7746  O OE1 . GLN E  1 2   ? 11.579  59.193 -1.456  1.00 30.22  ? 2    GLN E OE1 1 
ATOM   7747  N NE2 . GLN E  1 2   ? 13.137  59.158 -3.075  1.00 28.85  ? 2    GLN E NE2 1 
ATOM   7748  N N   . ILE E  1 3   ? 12.270  53.766 -1.983  1.00 30.42  ? 3    ILE E N   1 
ATOM   7749  C CA  . ILE E  1 3   ? 11.973  53.250 -0.653  1.00 30.66  ? 3    ILE E CA  1 
ATOM   7750  C C   . ILE E  1 3   ? 12.950  53.872 0.342   1.00 29.15  ? 3    ILE E C   1 
ATOM   7751  O O   . ILE E  1 3   ? 14.140  53.989 0.059   1.00 28.03  ? 3    ILE E O   1 
ATOM   7752  C CB  . ILE E  1 3   ? 12.025  51.705 -0.600  1.00 31.43  ? 3    ILE E CB  1 
ATOM   7753  C CG1 . ILE E  1 3   ? 11.443  51.199 0.724   1.00 32.08  ? 3    ILE E CG1 1 
ATOM   7754  C CG2 . ILE E  1 3   ? 13.443  51.182 -0.799  1.00 30.36  ? 3    ILE E CG2 1 
ATOM   7755  C CD1 . ILE E  1 3   ? 10.970  49.763 0.671   1.00 33.70  ? 3    ILE E CD1 1 
ATOM   7756  N N   . CYS E  1 4   ? 12.433  54.291 1.493   1.00 29.31  ? 4    CYS E N   1 
ATOM   7757  C CA  . CYS E  1 4   ? 13.240  54.961 2.503   1.00 28.11  ? 4    CYS E CA  1 
ATOM   7758  C C   . CYS E  1 4   ? 13.242  54.168 3.790   1.00 27.95  ? 4    CYS E C   1 
ATOM   7759  O O   . CYS E  1 4   ? 12.297  53.442 4.074   1.00 29.10  ? 4    CYS E O   1 
ATOM   7760  C CB  . CYS E  1 4   ? 12.701  56.364 2.777   1.00 28.47  ? 4    CYS E CB  1 
ATOM   7761  S SG  . CYS E  1 4   ? 12.543  57.396 1.302   1.00 29.01  ? 4    CYS E SG  1 
ATOM   7762  N N   . ILE E  1 5   ? 14.315  54.305 4.559   1.00 26.62  ? 5    ILE E N   1 
ATOM   7763  C CA  . ILE E  1 5   ? 14.369  53.755 5.900   1.00 26.41  ? 5    ILE E CA  1 
ATOM   7764  C C   . ILE E  1 5   ? 14.287  54.926 6.864   1.00 25.91  ? 5    ILE E C   1 
ATOM   7765  O O   . ILE E  1 5   ? 14.921  55.960 6.653   1.00 25.20  ? 5    ILE E O   1 
ATOM   7766  C CB  . ILE E  1 5   ? 15.657  52.951 6.137   1.00 25.65  ? 5    ILE E CB  1 
ATOM   7767  C CG1 . ILE E  1 5   ? 15.816  51.876 5.061   1.00 26.24  ? 5    ILE E CG1 1 
ATOM   7768  C CG2 . ILE E  1 5   ? 15.663  52.322 7.526   1.00 25.69  ? 5    ILE E CG2 1 
ATOM   7769  C CD1 . ILE E  1 5   ? 14.837  50.734 5.177   1.00 27.67  ? 5    ILE E CD1 1 
ATOM   7770  N N   . GLY E  1 6   ? 13.487  54.762 7.911   1.00 26.45  ? 6    GLY E N   1 
ATOM   7771  C CA  . GLY E  1 6   ? 13.259  55.831 8.873   1.00 26.28  ? 6    GLY E CA  1 
ATOM   7772  C C   . GLY E  1 6   ? 12.793  55.312 10.209  1.00 26.59  ? 6    GLY E C   1 
ATOM   7773  O O   . GLY E  1 6   ? 12.643  54.108 10.407  1.00 26.98  ? 6    GLY E O   1 
ATOM   7774  N N   . TYR E  1 7   ? 12.550  56.236 11.122  1.00 26.58  ? 7    TYR E N   1 
ATOM   7775  C CA  . TYR E  1 7   ? 12.262  55.886 12.504  1.00 26.75  ? 7    TYR E CA  1 
ATOM   7776  C C   . TYR E  1 7   ? 11.107  56.709 13.053  1.00 27.96  ? 7    TYR E C   1 
ATOM   7777  O O   . TYR E  1 7   ? 10.750  57.747 12.507  1.00 28.43  ? 7    TYR E O   1 
ATOM   7778  C CB  . TYR E  1 7   ? 13.523  56.049 13.374  1.00 25.39  ? 7    TYR E CB  1 
ATOM   7779  C CG  . TYR E  1 7   ? 14.172  57.417 13.309  1.00 24.76  ? 7    TYR E CG  1 
ATOM   7780  C CD1 . TYR E  1 7   ? 15.062  57.744 12.298  1.00 24.10  ? 7    TYR E CD1 1 
ATOM   7781  C CD2 . TYR E  1 7   ? 13.895  58.379 14.267  1.00 25.06  ? 7    TYR E CD2 1 
ATOM   7782  C CE1 . TYR E  1 7   ? 15.649  58.995 12.238  1.00 23.83  ? 7    TYR E CE1 1 
ATOM   7783  C CE2 . TYR E  1 7   ? 14.481  59.632 14.217  1.00 24.82  ? 7    TYR E CE2 1 
ATOM   7784  C CZ  . TYR E  1 7   ? 15.357  59.934 13.203  1.00 24.25  ? 7    TYR E CZ  1 
ATOM   7785  O OH  . TYR E  1 7   ? 15.924  61.184 13.158  1.00 24.29  ? 7    TYR E OH  1 
ATOM   7786  N N   . HIS E  1 8   ? 10.542  56.216 14.148  1.00 28.61  ? 8    HIS E N   1 
ATOM   7787  C CA  . HIS E  1 8   ? 9.354   56.785 14.777  1.00 30.09  ? 8    HIS E CA  1 
ATOM   7788  C C   . HIS E  1 8   ? 9.608   58.167 15.367  1.00 29.91  ? 8    HIS E C   1 
ATOM   7789  O O   . HIS E  1 8   ? 10.664  58.419 15.941  1.00 28.66  ? 8    HIS E O   1 
ATOM   7790  C CB  . HIS E  1 8   ? 8.894   55.836 15.889  1.00 30.65  ? 8    HIS E CB  1 
ATOM   7791  C CG  . HIS E  1 8   ? 7.612   56.237 16.551  1.00 32.39  ? 8    HIS E CG  1 
ATOM   7792  N ND1 . HIS E  1 8   ? 6.400   56.232 15.894  1.00 34.28  ? 8    HIS E ND1 1 
ATOM   7793  C CD2 . HIS E  1 8   ? 7.349   56.622 17.822  1.00 32.71  ? 8    HIS E CD2 1 
ATOM   7794  C CE1 . HIS E  1 8   ? 5.448   56.614 16.726  1.00 35.77  ? 8    HIS E CE1 1 
ATOM   7795  N NE2 . HIS E  1 8   ? 5.997   56.855 17.903  1.00 34.81  ? 8    HIS E NE2 1 
ATOM   7796  N N   . ALA E  1 9   ? 8.638   59.062 15.206  1.00 31.45  ? 9    ALA E N   1 
ATOM   7797  C CA  . ALA E  1 9   ? 8.586   60.304 15.977  1.00 31.94  ? 9    ALA E CA  1 
ATOM   7798  C C   . ALA E  1 9   ? 7.183   60.432 16.543  1.00 34.07  ? 9    ALA E C   1 
ATOM   7799  O O   . ALA E  1 9   ? 6.288   59.693 16.143  1.00 35.24  ? 9    ALA E O   1 
ATOM   7800  C CB  . ALA E  1 9   ? 8.929   61.498 15.109  1.00 31.97  ? 9    ALA E CB  1 
ATOM   7801  N N   . ASN E  1 10  ? 6.996   61.340 17.493  1.00 34.84  ? 10   ASN E N   1 
ATOM   7802  C CA  . ASN E  1 10  ? 5.674   61.578 18.074  1.00 37.15  ? 10   ASN E CA  1 
ATOM   7803  C C   . ASN E  1 10  ? 5.604   62.918 18.812  1.00 38.18  ? 10   ASN E C   1 
ATOM   7804  O O   . ASN E  1 10  ? 6.543   63.708 18.747  1.00 37.20  ? 10   ASN E O   1 
ATOM   7805  C CB  . ASN E  1 10  ? 5.247   60.405 18.977  1.00 37.31  ? 10   ASN E CB  1 
ATOM   7806  C CG  . ASN E  1 10  ? 6.083   60.284 20.239  1.00 35.88  ? 10   ASN E CG  1 
ATOM   7807  O OD1 . ASN E  1 10  ? 6.888   61.155 20.566  1.00 35.00  ? 10   ASN E OD1 1 
ATOM   7808  N ND2 . ASN E  1 10  ? 5.889   59.191 20.957  1.00 35.81  ? 10   ASN E ND2 1 
ATOM   7809  N N   . ASN E  1 11  ? 4.490   63.165 19.503  1.00 40.46  ? 11   ASN E N   1 
ATOM   7810  C CA  . ASN E  1 11  ? 4.259   64.436 20.199  1.00 41.97  ? 11   ASN E CA  1 
ATOM   7811  C C   . ASN E  1 11  ? 4.761   64.460 21.654  1.00 41.23  ? 11   ASN E C   1 
ATOM   7812  O O   . ASN E  1 11  ? 4.449   65.387 22.401  1.00 42.60  ? 11   ASN E O   1 
ATOM   7813  C CB  . ASN E  1 11  ? 2.765   64.813 20.130  1.00 45.13  ? 11   ASN E CB  1 
ATOM   7814  C CG  . ASN E  1 11  ? 1.862   63.821 20.856  1.00 46.18  ? 11   ASN E CG  1 
ATOM   7815  O OD1 . ASN E  1 11  ? 2.338   62.923 21.559  1.00 44.69  ? 11   ASN E OD1 1 
ATOM   7816  N ND2 . ASN E  1 11  ? 0.546   63.978 20.684  1.00 48.98  ? 11   ASN E ND2 1 
ATOM   7817  N N   . SER E  1 12  ? 5.542   63.450 22.041  1.00 39.22  ? 12   SER E N   1 
ATOM   7818  C CA  . SER E  1 12  ? 6.080   63.340 23.399  1.00 38.39  ? 12   SER E CA  1 
ATOM   7819  C C   . SER E  1 12  ? 7.060   64.466 23.711  1.00 37.86  ? 12   SER E C   1 
ATOM   7820  O O   . SER E  1 12  ? 7.849   64.867 22.855  1.00 37.05  ? 12   SER E O   1 
ATOM   7821  C CB  . SER E  1 12  ? 6.783   61.991 23.592  1.00 36.40  ? 12   SER E CB  1 
ATOM   7822  O OG  . SER E  1 12  ? 7.353   61.874 24.885  1.00 35.54  ? 12   SER E OG  1 
ATOM   7823  N N   . THR E  1 13  ? 6.990   64.970 24.944  1.00 38.58  ? 13   THR E N   1 
ATOM   7824  C CA  . THR E  1 13  ? 7.926   65.973 25.448  1.00 38.25  ? 13   THR E CA  1 
ATOM   7825  C C   . THR E  1 13  ? 8.770   65.435 26.605  1.00 36.77  ? 13   THR E C   1 
ATOM   7826  O O   . THR E  1 13  ? 9.523   66.188 27.219  1.00 36.62  ? 13   THR E O   1 
ATOM   7827  C CB  . THR E  1 13  ? 7.188   67.240 25.929  1.00 40.71  ? 13   THR E CB  1 
ATOM   7828  O OG1 . THR E  1 13  ? 6.141   66.875 26.841  1.00 42.02  ? 13   THR E OG1 1 
ATOM   7829  C CG2 . THR E  1 13  ? 6.603   68.004 24.748  1.00 42.30  ? 13   THR E CG2 1 
ATOM   7830  N N   . GLU E  1 14  ? 8.651   64.140 26.899  1.00 35.90  ? 14   GLU E N   1 
ATOM   7831  C CA  . GLU E  1 14  ? 9.450   63.522 27.957  1.00 34.57  ? 14   GLU E CA  1 
ATOM   7832  C C   . GLU E  1 14  ? 10.939  63.584 27.635  1.00 32.76  ? 14   GLU E C   1 
ATOM   7833  O O   . GLU E  1 14  ? 11.349  63.290 26.513  1.00 31.94  ? 14   GLU E O   1 
ATOM   7834  C CB  . GLU E  1 14  ? 9.042   62.064 28.176  1.00 34.17  ? 14   GLU E CB  1 
ATOM   7835  C CG  . GLU E  1 14  ? 7.642   61.899 28.745  1.00 36.14  ? 14   GLU E CG  1 
ATOM   7836  C CD  . GLU E  1 14  ? 7.596   60.937 29.924  1.00 35.88  ? 14   GLU E CD  1 
ATOM   7837  O OE1 . GLU E  1 14  ? 8.307   61.191 30.930  1.00 35.17  ? 14   GLU E OE1 1 
ATOM   7838  O OE2 . GLU E  1 14  ? 6.851   59.927 29.843  1.00 36.58  ? 14   GLU E OE2 1 
ATOM   7839  N N   . GLN E  1 15  ? 11.736  63.966 28.628  1.00 32.29  ? 15   GLN E N   1 
ATOM   7840  C CA  . GLN E  1 15  ? 13.174  64.119 28.459  1.00 30.97  ? 15   GLN E CA  1 
ATOM   7841  C C   . GLN E  1 15  ? 13.931  63.181 29.386  1.00 29.62  ? 15   GLN E C   1 
ATOM   7842  O O   . GLN E  1 15  ? 13.438  62.822 30.452  1.00 29.90  ? 15   GLN E O   1 
ATOM   7843  C CB  . GLN E  1 15  ? 13.587  65.556 28.760  1.00 31.99  ? 15   GLN E CB  1 
ATOM   7844  C CG  . GLN E  1 15  ? 12.787  66.602 28.006  1.00 33.71  ? 15   GLN E CG  1 
ATOM   7845  C CD  . GLN E  1 15  ? 13.273  68.012 28.265  1.00 34.97  ? 15   GLN E CD  1 
ATOM   7846  O OE1 . GLN E  1 15  ? 13.401  68.815 27.342  1.00 35.72  ? 15   GLN E OE1 1 
ATOM   7847  N NE2 . GLN E  1 15  ? 13.552  68.320 29.523  1.00 35.37  ? 15   GLN E NE2 1 
ATOM   7848  N N   . VAL E  1 16  ? 15.131  62.792 28.972  1.00 28.29  ? 16   VAL E N   1 
ATOM   7849  C CA  . VAL E  1 16  ? 16.020  61.987 29.808  1.00 27.21  ? 16   VAL E CA  1 
ATOM   7850  C C   . VAL E  1 16  ? 17.411  62.586 29.772  1.00 26.85  ? 16   VAL E C   1 
ATOM   7851  O O   . VAL E  1 16  ? 17.753  63.296 28.829  1.00 27.09  ? 16   VAL E O   1 
ATOM   7852  C CB  . VAL E  1 16  ? 16.085  60.517 29.346  1.00 26.21  ? 16   VAL E CB  1 
ATOM   7853  C CG1 . VAL E  1 16  ? 14.694  59.902 29.349  1.00 26.89  ? 16   VAL E CG1 1 
ATOM   7854  C CG2 . VAL E  1 16  ? 16.726  60.396 27.969  1.00 25.59  ? 16   VAL E CG2 1 
ATOM   7855  N N   . ASP E  1 17  ? 18.204  62.305 30.802  1.00 26.49  ? 17   ASP E N   1 
ATOM   7856  C CA  . ASP E  1 17  ? 19.598  62.737 30.842  1.00 26.33  ? 17   ASP E CA  1 
ATOM   7857  C C   . ASP E  1 17  ? 20.522  61.592 30.451  1.00 25.27  ? 17   ASP E C   1 
ATOM   7858  O O   . ASP E  1 17  ? 20.203  60.419 30.658  1.00 24.66  ? 17   ASP E O   1 
ATOM   7859  C CB  . ASP E  1 17  ? 19.975  63.243 32.236  1.00 26.87  ? 17   ASP E CB  1 
ATOM   7860  C CG  . ASP E  1 17  ? 19.299  64.554 32.592  1.00 28.31  ? 17   ASP E CG  1 
ATOM   7861  O OD1 . ASP E  1 17  ? 19.066  65.389 31.692  1.00 29.13  ? 17   ASP E OD1 1 
ATOM   7862  O OD2 . ASP E  1 17  ? 19.012  64.759 33.790  1.00 28.85  ? 17   ASP E OD2 1 
ATOM   7863  N N   . THR E  1 18  ? 21.657  61.962 29.866  1.00 25.32  ? 18   THR E N   1 
ATOM   7864  C CA  . THR E  1 18  ? 22.763  61.049 29.588  1.00 24.72  ? 18   THR E CA  1 
ATOM   7865  C C   . THR E  1 18  ? 24.038  61.720 30.089  1.00 25.42  ? 18   THR E C   1 
ATOM   7866  O O   . THR E  1 18  ? 23.994  62.838 30.597  1.00 26.35  ? 18   THR E O   1 
ATOM   7867  C CB  . THR E  1 18  ? 22.903  60.757 28.078  1.00 24.30  ? 18   THR E CB  1 
ATOM   7868  O OG1 . THR E  1 18  ? 23.289  61.949 27.386  1.00 24.89  ? 18   THR E OG1 1 
ATOM   7869  C CG2 . THR E  1 18  ? 21.601  60.248 27.504  1.00 24.03  ? 18   THR E CG2 1 
ATOM   7870  N N   . ILE E  1 19  ? 25.172  61.051 29.939  1.00 25.37  ? 19   ILE E N   1 
ATOM   7871  C CA  . ILE E  1 19  ? 26.451  61.606 30.385  1.00 26.29  ? 19   ILE E CA  1 
ATOM   7872  C C   . ILE E  1 19  ? 26.822  62.858 29.581  1.00 27.38  ? 19   ILE E C   1 
ATOM   7873  O O   . ILE E  1 19  ? 27.215  63.879 30.147  1.00 28.43  ? 19   ILE E O   1 
ATOM   7874  C CB  . ILE E  1 19  ? 27.585  60.562 30.257  1.00 26.09  ? 19   ILE E CB  1 
ATOM   7875  C CG1 . ILE E  1 19  ? 27.322  59.343 31.157  1.00 25.53  ? 19   ILE E CG1 1 
ATOM   7876  C CG2 . ILE E  1 19  ? 28.936  61.175 30.596  1.00 27.18  ? 19   ILE E CG2 1 
ATOM   7877  C CD1 . ILE E  1 19  ? 27.521  59.593 32.638  1.00 25.95  ? 19   ILE E CD1 1 
ATOM   7878  N N   . MET E  1 20  ? 26.688  62.770 28.261  1.00 27.35  ? 20   MET E N   1 
ATOM   7879  C CA  . MET E  1 20  ? 27.121  63.840 27.363  1.00 28.44  ? 20   MET E CA  1 
ATOM   7880  C C   . MET E  1 20  ? 26.065  64.904 27.090  1.00 29.32  ? 20   MET E C   1 
ATOM   7881  O O   . MET E  1 20  ? 26.390  65.979 26.584  1.00 30.33  ? 20   MET E O   1 
ATOM   7882  C CB  . MET E  1 20  ? 27.538  63.249 26.024  1.00 27.89  ? 20   MET E CB  1 
ATOM   7883  C CG  . MET E  1 20  ? 28.771  62.380 26.086  1.00 27.82  ? 20   MET E CG  1 
ATOM   7884  S SD  . MET E  1 20  ? 29.327  62.012 24.423  1.00 27.66  ? 20   MET E SD  1 
ATOM   7885  C CE  . MET E  1 20  ? 30.776  61.034 24.786  1.00 28.08  ? 20   MET E CE  1 
ATOM   7886  N N   . GLU E  1 21  ? 24.805  64.598 27.380  1.00 29.28  ? 21   GLU E N   1 
ATOM   7887  C CA  . GLU E  1 21  ? 23.720  65.512 27.058  1.00 30.40  ? 21   GLU E CA  1 
ATOM   7888  C C   . GLU E  1 21  ? 22.573  65.389 28.051  1.00 30.89  ? 21   GLU E C   1 
ATOM   7889  O O   . GLU E  1 21  ? 22.180  64.285 28.432  1.00 29.90  ? 21   GLU E O   1 
ATOM   7890  C CB  . GLU E  1 21  ? 23.220  65.242 25.639  1.00 29.92  ? 21   GLU E CB  1 
ATOM   7891  C CG  . GLU E  1 21  ? 22.529  66.431 24.992  1.00 31.05  ? 21   GLU E CG  1 
ATOM   7892  C CD  . GLU E  1 21  ? 22.066  66.146 23.569  1.00 30.63  ? 21   GLU E CD  1 
ATOM   7893  O OE1 . GLU E  1 21  ? 22.504  65.128 22.980  1.00 29.61  ? 21   GLU E OE1 1 
ATOM   7894  O OE2 . GLU E  1 21  ? 21.258  66.943 23.040  1.00 31.45  ? 21   GLU E OE2 1 
ATOM   7895  N N   . LYS E  1 22  ? 22.041  66.539 28.455  1.00 32.87  ? 22   LYS E N   1 
ATOM   7896  C CA  . LYS E  1 22  ? 20.922  66.597 29.384  1.00 33.87  ? 22   LYS E CA  1 
ATOM   7897  C C   . LYS E  1 22  ? 19.671  67.049 28.659  1.00 35.13  ? 22   LYS E C   1 
ATOM   7898  O O   . LYS E  1 22  ? 19.753  67.723 27.639  1.00 35.71  ? 22   LYS E O   1 
ATOM   7899  C CB  . LYS E  1 22  ? 21.241  67.554 30.533  1.00 35.28  ? 22   LYS E CB  1 
ATOM   7900  C CG  . LYS E  1 22  ? 21.865  66.889 31.752  1.00 34.77  ? 22   LYS E CG  1 
ATOM   7901  C CD  . LYS E  1 22  ? 23.250  67.465 32.053  1.00 35.69  ? 22   LYS E CD  1 
ATOM   7902  C CE  . LYS E  1 22  ? 23.115  68.809 32.760  1.00 37.71  ? 22   LYS E CE  1 
ATOM   7903  N NZ  . LYS E  1 22  ? 22.840  68.654 34.220  1.00 37.87  ? 22   LYS E NZ  1 
ATOM   7904  N N   . ASN E  1 23  ? 18.516  66.665 29.193  1.00 36.10  ? 23   ASN E N   1 
ATOM   7905  C CA  . ASN E  1 23  ? 17.221  67.081 28.655  1.00 37.78  ? 23   ASN E CA  1 
ATOM   7906  C C   . ASN E  1 23  ? 17.021  66.674 27.193  1.00 35.97  ? 23   ASN E C   1 
ATOM   7907  O O   . ASN E  1 23  ? 16.572  67.467 26.368  1.00 36.82  ? 23   ASN E O   1 
ATOM   7908  C CB  . ASN E  1 23  ? 17.018  68.597 28.853  1.00 41.64  ? 23   ASN E CB  1 
ATOM   7909  C CG  . ASN E  1 23  ? 16.928  68.991 30.319  1.00 45.11  ? 23   ASN E CG  1 
ATOM   7910  O OD1 . ASN E  1 23  ? 16.633  68.158 31.178  1.00 44.45  ? 23   ASN E OD1 1 
ATOM   7911  N ND2 . ASN E  1 23  ? 17.173  70.282 30.614  1.00 50.60  ? 23   ASN E ND2 1 
ATOM   7912  N N   . VAL E  1 24  ? 17.362  65.425 26.890  1.00 33.36  ? 24   VAL E N   1 
ATOM   7913  C CA  . VAL E  1 24  ? 17.151  64.847 25.561  1.00 31.96  ? 24   VAL E CA  1 
ATOM   7914  C C   . VAL E  1 24  ? 15.704  64.366 25.432  1.00 31.75  ? 24   VAL E C   1 
ATOM   7915  O O   . VAL E  1 24  ? 15.276  63.484 26.174  1.00 31.29  ? 24   VAL E O   1 
ATOM   7916  C CB  . VAL E  1 24  ? 18.097  63.646 25.320  1.00 30.41  ? 24   VAL E CB  1 
ATOM   7917  C CG1 . VAL E  1 24  ? 17.789  62.969 23.993  1.00 29.89  ? 24   VAL E CG1 1 
ATOM   7918  C CG2 . VAL E  1 24  ? 19.554  64.091 25.375  1.00 30.23  ? 24   VAL E CG2 1 
ATOM   7919  N N   . THR E  1 25  ? 14.954  64.948 24.498  1.00 31.99  ? 25   THR E N   1 
ATOM   7920  C CA  . THR E  1 25  ? 13.554  64.574 24.299  1.00 32.30  ? 25   THR E CA  1 
ATOM   7921  C C   . THR E  1 25  ? 13.459  63.208 23.627  1.00 30.88  ? 25   THR E C   1 
ATOM   7922  O O   . THR E  1 25  ? 14.089  62.982 22.591  1.00 30.02  ? 25   THR E O   1 
ATOM   7923  C CB  . THR E  1 25  ? 12.799  65.593 23.425  1.00 33.77  ? 25   THR E CB  1 
ATOM   7924  O OG1 . THR E  1 25  ? 13.129  66.924 23.834  1.00 34.87  ? 25   THR E OG1 1 
ATOM   7925  C CG2 . THR E  1 25  ? 11.300  65.391 23.548  1.00 35.10  ? 25   THR E CG2 1 
ATOM   7926  N N   . VAL E  1 26  ? 12.667  62.313 24.215  1.00 30.62  ? 26   VAL E N   1 
ATOM   7927  C CA  . VAL E  1 26  ? 12.521  60.951 23.710  1.00 29.68  ? 26   VAL E CA  1 
ATOM   7928  C C   . VAL E  1 26  ? 11.063  60.615 23.462  1.00 30.86  ? 26   VAL E C   1 
ATOM   7929  O O   . VAL E  1 26  ? 10.172  61.223 24.048  1.00 32.22  ? 26   VAL E O   1 
ATOM   7930  C CB  . VAL E  1 26  ? 13.130  59.901 24.666  1.00 28.61  ? 26   VAL E CB  1 
ATOM   7931  C CG1 . VAL E  1 26  ? 14.640  60.048 24.716  1.00 27.36  ? 26   VAL E CG1 1 
ATOM   7932  C CG2 . VAL E  1 26  ? 12.526  59.998 26.059  1.00 29.31  ? 26   VAL E CG2 1 
ATOM   7933  N N   . THR E  1 27  ? 10.835  59.636 22.595  1.00 30.49  ? 27   THR E N   1 
ATOM   7934  C CA  . THR E  1 27  ? 9.485   59.243 22.206  1.00 31.86  ? 27   THR E CA  1 
ATOM   7935  C C   . THR E  1 27  ? 8.784   58.499 23.333  1.00 32.51  ? 27   THR E C   1 
ATOM   7936  O O   . THR E  1 27  ? 7.577   58.644 23.519  1.00 34.32  ? 27   THR E O   1 
ATOM   7937  C CB  . THR E  1 27  ? 9.478   58.355 20.944  1.00 31.58  ? 27   THR E CB  1 
ATOM   7938  O OG1 . THR E  1 27  ? 10.160  57.122 21.205  1.00 30.51  ? 27   THR E OG1 1 
ATOM   7939  C CG2 . THR E  1 27  ? 10.144  59.067 19.782  1.00 30.91  ? 27   THR E CG2 1 
ATOM   7940  N N   . HIS E  1 28  ? 9.542   57.695 24.071  1.00 31.25  ? 28   HIS E N   1 
ATOM   7941  C CA  . HIS E  1 28  ? 9.009   56.952 25.209  1.00 31.76  ? 28   HIS E CA  1 
ATOM   7942  C C   . HIS E  1 28  ? 10.019  56.935 26.334  1.00 30.49  ? 28   HIS E C   1 
ATOM   7943  O O   . HIS E  1 28  ? 11.228  56.925 26.094  1.00 29.11  ? 28   HIS E O   1 
ATOM   7944  C CB  . HIS E  1 28  ? 8.674   55.521 24.804  1.00 32.09  ? 28   HIS E CB  1 
ATOM   7945  C CG  . HIS E  1 28  ? 7.755   55.433 23.629  1.00 33.36  ? 28   HIS E CG  1 
ATOM   7946  N ND1 . HIS E  1 28  ? 8.192   55.592 22.332  1.00 32.72  ? 28   HIS E ND1 1 
ATOM   7947  C CD2 . HIS E  1 28  ? 6.420   55.224 23.555  1.00 35.36  ? 28   HIS E CD2 1 
ATOM   7948  C CE1 . HIS E  1 28  ? 7.167   55.476 21.509  1.00 34.22  ? 28   HIS E CE1 1 
ATOM   7949  N NE2 . HIS E  1 28  ? 6.080   55.252 22.225  1.00 35.90  ? 28   HIS E NE2 1 
ATOM   7950  N N   . ALA E  1 29  ? 9.517   56.922 27.560  1.00 31.14  ? 29   ALA E N   1 
ATOM   7951  C CA  . ALA E  1 29  ? 10.359  56.909 28.747  1.00 30.17  ? 29   ALA E CA  1 
ATOM   7952  C C   . ALA E  1 29  ? 9.641   56.174 29.862  1.00 31.03  ? 29   ALA E C   1 
ATOM   7953  O O   . ALA E  1 29  ? 8.466   55.837 29.732  1.00 32.56  ? 29   ALA E O   1 
ATOM   7954  C CB  . ALA E  1 29  ? 10.691  58.327 29.173  1.00 30.13  ? 29   ALA E CB  1 
ATOM   7955  N N   . GLN E  1 30  ? 10.353  55.907 30.949  1.00 30.23  ? 30   GLN E N   1 
ATOM   7956  C CA  . GLN E  1 30  ? 9.752   55.255 32.105  1.00 31.03  ? 30   GLN E CA  1 
ATOM   7957  C C   . GLN E  1 30  ? 10.309  55.830 33.395  1.00 30.47  ? 30   GLN E C   1 
ATOM   7958  O O   . GLN E  1 30  ? 11.478  55.627 33.725  1.00 29.15  ? 30   GLN E O   1 
ATOM   7959  C CB  . GLN E  1 30  ? 9.977   53.741 32.063  1.00 30.88  ? 30   GLN E CB  1 
ATOM   7960  C CG  . GLN E  1 30  ? 9.234   52.998 33.166  1.00 32.05  ? 30   GLN E CG  1 
ATOM   7961  C CD  . GLN E  1 30  ? 9.197   51.492 32.966  1.00 32.52  ? 30   GLN E CD  1 
ATOM   7962  O OE1 . GLN E  1 30  ? 9.302   50.994 31.845  1.00 32.60  ? 30   GLN E OE1 1 
ATOM   7963  N NE2 . GLN E  1 30  ? 9.031   50.759 34.060  1.00 33.06  ? 30   GLN E NE2 1 
ATOM   7964  N N   . ASP E  1 31  ? 9.461   56.554 34.119  1.00 31.66  ? 31   ASP E N   1 
ATOM   7965  C CA  . ASP E  1 31  ? 9.808   57.034 35.446  1.00 31.47  ? 31   ASP E CA  1 
ATOM   7966  C C   . ASP E  1 31  ? 9.848   55.833 36.390  1.00 31.27  ? 31   ASP E C   1 
ATOM   7967  O O   . ASP E  1 31  ? 8.943   54.994 36.382  1.00 32.32  ? 31   ASP E O   1 
ATOM   7968  C CB  . ASP E  1 31  ? 8.785   58.063 35.932  1.00 33.17  ? 31   ASP E CB  1 
ATOM   7969  C CG  . ASP E  1 31  ? 9.291   58.888 37.103  1.00 33.06  ? 31   ASP E CG  1 
ATOM   7970  O OD1 . ASP E  1 31  ? 10.272  58.477 37.762  1.00 31.84  ? 31   ASP E OD1 1 
ATOM   7971  O OD2 . ASP E  1 31  ? 8.700   59.957 37.364  1.00 34.49  ? 31   ASP E OD2 1 
ATOM   7972  N N   . ILE E  1 32  ? 10.911  55.754 37.183  1.00 30.05  ? 32   ILE E N   1 
ATOM   7973  C CA  . ILE E  1 32  ? 11.097  54.661 38.137  1.00 29.85  ? 32   ILE E CA  1 
ATOM   7974  C C   . ILE E  1 32  ? 11.188  55.150 39.590  1.00 29.94  ? 32   ILE E C   1 
ATOM   7975  O O   . ILE E  1 32  ? 11.428  54.358 40.499  1.00 29.78  ? 32   ILE E O   1 
ATOM   7976  C CB  . ILE E  1 32  ? 12.349  53.828 37.784  1.00 28.50  ? 32   ILE E CB  1 
ATOM   7977  C CG1 . ILE E  1 32  ? 13.581  54.721 37.636  1.00 27.32  ? 32   ILE E CG1 1 
ATOM   7978  C CG2 . ILE E  1 32  ? 12.115  53.049 36.503  1.00 28.67  ? 32   ILE E CG2 1 
ATOM   7979  C CD1 . ILE E  1 32  ? 14.884  53.960 37.719  1.00 26.30  ? 32   ILE E CD1 1 
ATOM   7980  N N   . LEU E  1 33  ? 10.980  56.448 39.801  1.00 30.35  ? 33   LEU E N   1 
ATOM   7981  C CA  . LEU E  1 33  ? 11.054  57.049 41.128  1.00 30.62  ? 33   LEU E CA  1 
ATOM   7982  C C   . LEU E  1 33  ? 9.671   57.464 41.621  1.00 32.46  ? 33   LEU E C   1 
ATOM   7983  O O   . LEU E  1 33  ? 9.022   58.321 41.016  1.00 33.47  ? 33   LEU E O   1 
ATOM   7984  C CB  . LEU E  1 33  ? 11.959  58.278 41.086  1.00 30.04  ? 33   LEU E CB  1 
ATOM   7985  C CG  . LEU E  1 33  ? 12.244  58.975 42.413  1.00 30.31  ? 33   LEU E CG  1 
ATOM   7986  C CD1 . LEU E  1 33  ? 13.073  58.077 43.312  1.00 29.33  ? 33   LEU E CD1 1 
ATOM   7987  C CD2 . LEU E  1 33  ? 12.955  60.297 42.175  1.00 30.30  ? 33   LEU E CD2 1 
ATOM   7988  N N   . GLU E  1 34  ? 9.224   56.866 42.723  1.00 33.08  ? 34   GLU E N   1 
ATOM   7989  C CA  . GLU E  1 34  ? 7.988   57.294 43.372  1.00 34.98  ? 34   GLU E CA  1 
ATOM   7990  C C   . GLU E  1 34  ? 8.229   58.570 44.180  1.00 35.32  ? 34   GLU E C   1 
ATOM   7991  O O   . GLU E  1 34  ? 9.016   58.574 45.123  1.00 34.50  ? 34   GLU E O   1 
ATOM   7992  C CB  . GLU E  1 34  ? 7.433   56.194 44.280  1.00 35.64  ? 34   GLU E CB  1 
ATOM   7993  C CG  . GLU E  1 34  ? 6.121   56.565 44.957  1.00 37.83  ? 34   GLU E CG  1 
ATOM   7994  C CD  . GLU E  1 34  ? 5.122   57.164 43.985  1.00 39.40  ? 34   GLU E CD  1 
ATOM   7995  O OE1 . GLU E  1 34  ? 4.683   56.450 43.058  1.00 39.79  ? 34   GLU E OE1 1 
ATOM   7996  O OE2 . GLU E  1 34  ? 4.810   58.362 44.126  1.00 40.40  ? 34   GLU E OE2 1 
ATOM   7997  N N   . LYS E  1 35  ? 7.536   59.644 43.811  1.00 36.76  ? 35   LYS E N   1 
ATOM   7998  C CA  . LYS E  1 35  ? 7.762   60.963 44.412  1.00 37.41  ? 35   LYS E CA  1 
ATOM   7999  C C   . LYS E  1 35  ? 6.688   61.384 45.422  1.00 39.53  ? 35   LYS E C   1 
ATOM   8000  O O   . LYS E  1 35  ? 6.898   62.343 46.169  1.00 40.17  ? 35   LYS E O   1 
ATOM   8001  C CB  . LYS E  1 35  ? 7.896   62.028 43.312  1.00 37.74  ? 35   LYS E CB  1 
ATOM   8002  C CG  . LYS E  1 35  ? 9.312   62.203 42.777  1.00 35.89  ? 35   LYS E CG  1 
ATOM   8003  C CD  . LYS E  1 35  ? 9.353   63.114 41.556  1.00 36.30  ? 35   LYS E CD  1 
ATOM   8004  C CE  . LYS E  1 35  ? 9.505   62.343 40.249  1.00 35.19  ? 35   LYS E CE  1 
ATOM   8005  N NZ  . LYS E  1 35  ? 8.483   61.280 40.026  1.00 35.68  ? 35   LYS E NZ  1 
ATOM   8006  N N   . THR E  1 36  ? 5.561   60.668 45.464  1.00 40.82  ? 36   THR E N   1 
ATOM   8007  C CA  . THR E  1 36  ? 4.411   61.081 46.278  1.00 43.23  ? 36   THR E CA  1 
ATOM   8008  C C   . THR E  1 36  ? 4.065   60.131 47.426  1.00 43.53  ? 36   THR E C   1 
ATOM   8009  O O   . THR E  1 36  ? 4.419   58.952 47.408  1.00 42.27  ? 36   THR E O   1 
ATOM   8010  C CB  . THR E  1 36  ? 3.142   61.254 45.416  1.00 45.37  ? 36   THR E CB  1 
ATOM   8011  O OG1 . THR E  1 36  ? 2.757   59.993 44.854  1.00 45.11  ? 36   THR E OG1 1 
ATOM   8012  C CG2 . THR E  1 36  ? 3.379   62.263 44.301  1.00 45.43  ? 36   THR E CG2 1 
ATOM   8013  N N   . HIS E  1 37  ? 3.364   60.682 48.419  1.00 45.44  ? 37   HIS E N   1 
ATOM   8014  C CA  . HIS E  1 37  ? 2.794   59.932 49.541  1.00 46.32  ? 37   HIS E CA  1 
ATOM   8015  C C   . HIS E  1 37  ? 1.467   60.601 49.914  1.00 49.44  ? 37   HIS E C   1 
ATOM   8016  O O   . HIS E  1 37  ? 1.213   61.732 49.496  1.00 50.68  ? 37   HIS E O   1 
ATOM   8017  C CB  . HIS E  1 37  ? 3.756   59.933 50.736  1.00 44.92  ? 37   HIS E CB  1 
ATOM   8018  C CG  . HIS E  1 37  ? 4.110   61.302 51.227  1.00 45.41  ? 37   HIS E CG  1 
ATOM   8019  N ND1 . HIS E  1 37  ? 3.532   61.862 52.344  1.00 47.23  ? 37   HIS E ND1 1 
ATOM   8020  C CD2 . HIS E  1 37  ? 4.972   62.230 50.745  1.00 44.58  ? 37   HIS E CD2 1 
ATOM   8021  C CE1 . HIS E  1 37  ? 4.026   63.072 52.537  1.00 47.52  ? 37   HIS E CE1 1 
ATOM   8022  N NE2 . HIS E  1 37  ? 4.903   63.319 51.580  1.00 45.97  ? 37   HIS E NE2 1 
ATOM   8023  N N   . ASN E  1 38  ? 0.623   59.918 50.690  1.00 50.93  ? 38   ASN E N   1 
ATOM   8024  C CA  . ASN E  1 38  ? -0.691  60.480 51.063  1.00 54.20  ? 38   ASN E CA  1 
ATOM   8025  C C   . ASN E  1 38  ? -0.639  61.514 52.201  1.00 55.23  ? 38   ASN E C   1 
ATOM   8026  O O   . ASN E  1 38  ? -1.568  62.308 52.363  1.00 58.01  ? 38   ASN E O   1 
ATOM   8027  C CB  . ASN E  1 38  ? -1.720  59.371 51.372  1.00 55.85  ? 38   ASN E CB  1 
ATOM   8028  C CG  . ASN E  1 38  ? -1.349  58.520 52.575  1.00 54.87  ? 38   ASN E CG  1 
ATOM   8029  O OD1 . ASN E  1 38  ? -0.445  58.852 53.341  1.00 53.29  ? 38   ASN E OD1 1 
ATOM   8030  N ND2 . ASN E  1 38  ? -2.055  57.410 52.745  1.00 55.99  ? 38   ASN E ND2 1 
ATOM   8031  N N   . GLY E  1 39  ? 0.433   61.486 52.990  1.00 53.23  ? 39   GLY E N   1 
ATOM   8032  C CA  . GLY E  1 39  ? 0.662   62.477 54.051  1.00 53.97  ? 39   GLY E CA  1 
ATOM   8033  C C   . GLY E  1 39  ? 0.133   62.050 55.408  1.00 55.16  ? 39   GLY E C   1 
ATOM   8034  O O   . GLY E  1 39  ? 0.039   62.868 56.331  1.00 56.42  ? 39   GLY E O   1 
ATOM   8035  N N   . LYS E  1 40  ? -0.187  60.762 55.537  1.00 54.84  ? 40   LYS E N   1 
ATOM   8036  C CA  . LYS E  1 40  ? -0.885  60.241 56.706  1.00 56.36  ? 40   LYS E CA  1 
ATOM   8037  C C   . LYS E  1 40  ? -0.188  59.030 57.312  1.00 54.29  ? 40   LYS E C   1 
ATOM   8038  O O   . LYS E  1 40  ? 0.503   58.284 56.622  1.00 52.24  ? 40   LYS E O   1 
ATOM   8039  C CB  . LYS E  1 40  ? -2.311  59.853 56.314  1.00 59.16  ? 40   LYS E CB  1 
ATOM   8040  C CG  . LYS E  1 40  ? -3.243  61.038 56.117  1.00 62.16  ? 40   LYS E CG  1 
ATOM   8041  C CD  . LYS E  1 40  ? -4.284  60.754 55.047  1.00 64.15  ? 40   LYS E CD  1 
ATOM   8042  C CE  . LYS E  1 40  ? -5.303  61.876 54.959  1.00 67.63  ? 40   LYS E CE  1 
ATOM   8043  N NZ  . LYS E  1 40  ? -6.227  61.700 53.805  1.00 69.57  ? 40   LYS E NZ  1 
ATOM   8044  N N   . LEU E  1 41  ? -0.388  58.846 58.613  1.00 55.05  ? 41   LEU E N   1 
ATOM   8045  C CA  . LEU E  1 41  ? 0.042   57.639 59.311  1.00 53.73  ? 41   LEU E CA  1 
ATOM   8046  C C   . LEU E  1 41  ? -1.095  56.622 59.214  1.00 55.67  ? 41   LEU E C   1 
ATOM   8047  O O   . LEU E  1 41  ? -2.230  56.911 59.606  1.00 58.48  ? 41   LEU E O   1 
ATOM   8048  C CB  . LEU E  1 41  ? 0.383   57.966 60.770  1.00 53.70  ? 41   LEU E CB  1 
ATOM   8049  C CG  . LEU E  1 41  ? 1.695   58.727 61.069  1.00 51.66  ? 41   LEU E CG  1 
ATOM   8050  C CD1 . LEU E  1 41  ? 2.672   57.855 61.848  1.00 49.60  ? 41   LEU E CD1 1 
ATOM   8051  C CD2 . LEU E  1 41  ? 2.391   59.300 59.832  1.00 50.26  ? 41   LEU E CD2 1 
ATOM   8052  N N   . CYS E  1 42  ? -0.785  55.438 58.688  1.00 54.42  ? 42   CYS E N   1 
ATOM   8053  C CA  . CYS E  1 42  ? -1.806  54.473 58.285  1.00 56.35  ? 42   CYS E CA  1 
ATOM   8054  C C   . CYS E  1 42  ? -1.630  53.110 58.932  1.00 55.95  ? 42   CYS E C   1 
ATOM   8055  O O   . CYS E  1 42  ? -0.561  52.781 59.437  1.00 53.72  ? 42   CYS E O   1 
ATOM   8056  C CB  . CYS E  1 42  ? -1.776  54.271 56.757  1.00 55.84  ? 42   CYS E CB  1 
ATOM   8057  S SG  . CYS E  1 42  ? -2.228  55.671 55.685  1.00 56.89  ? 42   CYS E SG  1 
ATOM   8058  N N   . ASP E  1 43  ? -2.696  52.316 58.888  1.00 58.38  ? 43   ASP E N   1 
ATOM   8059  C CA  . ASP E  1 43  ? -2.627  50.904 59.244  1.00 58.45  ? 43   ASP E CA  1 
ATOM   8060  C C   . ASP E  1 43  ? -1.732  50.189 58.244  1.00 56.28  ? 43   ASP E C   1 
ATOM   8061  O O   . ASP E  1 43  ? -1.833  50.431 57.042  1.00 56.16  ? 43   ASP E O   1 
ATOM   8062  C CB  . ASP E  1 43  ? -4.022  50.263 59.221  1.00 61.93  ? 43   ASP E CB  1 
ATOM   8063  C CG  . ASP E  1 43  ? -4.937  50.786 60.322  1.00 64.42  ? 43   ASP E CG  1 
ATOM   8064  O OD1 . ASP E  1 43  ? -4.483  51.590 61.162  1.00 63.38  ? 43   ASP E OD1 1 
ATOM   8065  O OD2 . ASP E  1 43  ? -6.121  50.393 60.345  1.00 67.60  ? 43   ASP E OD2 1 
ATOM   8066  N N   . LEU E  1 44  ? -0.855  49.321 58.740  1.00 54.72  ? 44   LEU E N   1 
ATOM   8067  C CA  . LEU E  1 44  ? 0.017   48.526 57.874  1.00 52.96  ? 44   LEU E CA  1 
ATOM   8068  C C   . LEU E  1 44  ? -0.552  47.125 57.713  1.00 54.83  ? 44   LEU E C   1 
ATOM   8069  O O   . LEU E  1 44  ? -0.688  46.390 58.691  1.00 55.78  ? 44   LEU E O   1 
ATOM   8070  C CB  . LEU E  1 44  ? 1.431   48.441 58.452  1.00 50.25  ? 44   LEU E CB  1 
ATOM   8071  C CG  . LEU E  1 44  ? 2.500   47.868 57.513  1.00 48.23  ? 44   LEU E CG  1 
ATOM   8072  C CD1 . LEU E  1 44  ? 2.951   48.922 56.509  1.00 46.72  ? 44   LEU E CD1 1 
ATOM   8073  C CD2 . LEU E  1 44  ? 3.694   47.340 58.294  1.00 46.49  ? 44   LEU E CD2 1 
ATOM   8074  N N   . ASP E  1 45  ? -0.885  46.759 56.477  1.00 55.54  ? 45   ASP E N   1 
ATOM   8075  C CA  . ASP E  1 45  ? -1.461  45.447 56.178  1.00 57.64  ? 45   ASP E CA  1 
ATOM   8076  C C   . ASP E  1 45  ? -2.750  45.215 56.976  1.00 60.89  ? 45   ASP E C   1 
ATOM   8077  O O   . ASP E  1 45  ? -3.050  44.089 57.380  1.00 62.57  ? 45   ASP E O   1 
ATOM   8078  C CB  . ASP E  1 45  ? -0.434  44.341 56.472  1.00 56.33  ? 45   ASP E CB  1 
ATOM   8079  C CG  . ASP E  1 45  ? -0.679  43.081 55.659  1.00 57.89  ? 45   ASP E CG  1 
ATOM   8080  O OD1 . ASP E  1 45  ? -0.421  43.110 54.437  1.00 57.16  ? 45   ASP E OD1 1 
ATOM   8081  O OD2 . ASP E  1 45  ? -1.116  42.064 56.244  1.00 59.97  ? 45   ASP E OD2 1 
ATOM   8082  N N   . GLY E  1 46  ? -3.499  46.293 57.209  1.00 61.97  ? 46   GLY E N   1 
ATOM   8083  C CA  . GLY E  1 46  ? -4.715  46.248 58.030  1.00 65.16  ? 46   GLY E CA  1 
ATOM   8084  C C   . GLY E  1 46  ? -4.471  46.372 59.526  1.00 64.73  ? 46   GLY E C   1 
ATOM   8085  O O   . GLY E  1 46  ? -5.388  46.712 60.274  1.00 67.04  ? 46   GLY E O   1 
ATOM   8086  N N   . VAL E  1 47  ? -3.235  46.108 59.960  1.00 61.89  ? 47   VAL E N   1 
ATOM   8087  C CA  . VAL E  1 47  ? -2.881  46.069 61.383  1.00 61.34  ? 47   VAL E CA  1 
ATOM   8088  C C   . VAL E  1 47  ? -2.498  47.467 61.869  1.00 59.78  ? 47   VAL E C   1 
ATOM   8089  O O   . VAL E  1 47  ? -1.525  48.050 61.391  1.00 57.18  ? 47   VAL E O   1 
ATOM   8090  C CB  . VAL E  1 47  ? -1.709  45.098 61.642  1.00 59.30  ? 47   VAL E CB  1 
ATOM   8091  C CG1 . VAL E  1 47  ? -1.368  45.052 63.124  1.00 58.92  ? 47   VAL E CG1 1 
ATOM   8092  C CG2 . VAL E  1 47  ? -2.043  43.704 61.131  1.00 61.02  ? 47   VAL E CG2 1 
ATOM   8093  N N   . LYS E  1 48  ? -3.252  47.980 62.839  1.00 61.57  ? 48   LYS E N   1 
ATOM   8094  C CA  . LYS E  1 48  ? -3.109  49.363 63.304  1.00 60.85  ? 48   LYS E CA  1 
ATOM   8095  C C   . LYS E  1 48  ? -1.785  49.591 64.043  1.00 57.88  ? 48   LYS E C   1 
ATOM   8096  O O   . LYS E  1 48  ? -1.359  48.737 64.824  1.00 57.39  ? 48   LYS E O   1 
ATOM   8097  C CB  . LYS E  1 48  ? -4.278  49.736 64.235  1.00 63.90  ? 48   LYS E CB  1 
ATOM   8098  C CG  . LYS E  1 48  ? -4.597  51.231 64.288  1.00 64.50  ? 48   LYS E CG  1 
ATOM   8099  C CD  . LYS E  1 48  ? -5.057  51.709 65.667  1.00 66.09  ? 48   LYS E CD  1 
ATOM   8100  C CE  . LYS E  1 48  ? -5.345  53.247 65.693  1.00 66.92  ? 48   LYS E CE  1 
ATOM   8101  N NZ  . LYS E  1 48  ? -6.778  53.626 65.473  1.00 70.72  ? 48   LYS E NZ  1 
ATOM   8102  N N   . PRO E  1 49  ? -1.130  50.745 63.800  1.00 56.08  ? 49   PRO E N   1 
ATOM   8103  C CA  . PRO E  1 49  ? 0.035   51.082 64.619  1.00 53.77  ? 49   PRO E CA  1 
ATOM   8104  C C   . PRO E  1 49  ? -0.340  51.482 66.040  1.00 54.96  ? 49   PRO E C   1 
ATOM   8105  O O   . PRO E  1 49  ? -1.432  52.004 66.269  1.00 57.38  ? 49   PRO E O   1 
ATOM   8106  C CB  . PRO E  1 49  ? 0.630   52.296 63.902  1.00 52.26  ? 49   PRO E CB  1 
ATOM   8107  C CG  . PRO E  1 49  ? -0.527  52.914 63.197  1.00 54.48  ? 49   PRO E CG  1 
ATOM   8108  C CD  . PRO E  1 49  ? -1.334  51.739 62.729  1.00 56.09  ? 49   PRO E CD  1 
ATOM   8109  N N   . LEU E  1 50  ? 0.575   51.244 66.974  1.00 53.35  ? 50   LEU E N   1 
ATOM   8110  C CA  . LEU E  1 50  ? 0.455   51.775 68.322  1.00 54.03  ? 50   LEU E CA  1 
ATOM   8111  C C   . LEU E  1 50  ? 0.909   53.227 68.295  1.00 53.22  ? 50   LEU E C   1 
ATOM   8112  O O   . LEU E  1 50  ? 2.104   53.502 68.200  1.00 50.92  ? 50   LEU E O   1 
ATOM   8113  C CB  . LEU E  1 50  ? 1.310   50.962 69.301  1.00 52.69  ? 50   LEU E CB  1 
ATOM   8114  C CG  . LEU E  1 50  ? 1.567   51.541 70.697  1.00 52.69  ? 50   LEU E CG  1 
ATOM   8115  C CD1 . LEU E  1 50  ? 0.277   51.987 71.370  1.00 55.53  ? 50   LEU E CD1 1 
ATOM   8116  C CD2 . LEU E  1 50  ? 2.289   50.516 71.557  1.00 51.68  ? 50   LEU E CD2 1 
ATOM   8117  N N   . ILE E  1 51  ? -0.045  54.151 68.357  1.00 55.37  ? 51   ILE E N   1 
ATOM   8118  C CA  . ILE E  1 51  ? 0.271   55.576 68.372  1.00 55.17  ? 51   ILE E CA  1 
ATOM   8119  C C   . ILE E  1 51  ? 0.214   56.072 69.807  1.00 56.10  ? 51   ILE E C   1 
ATOM   8120  O O   . ILE E  1 51  ? -0.863  56.178 70.396  1.00 58.66  ? 51   ILE E O   1 
ATOM   8121  C CB  . ILE E  1 51  ? -0.690  56.392 67.482  1.00 57.17  ? 51   ILE E CB  1 
ATOM   8122  C CG1 . ILE E  1 51  ? -0.804  55.725 66.106  1.00 56.63  ? 51   ILE E CG1 1 
ATOM   8123  C CG2 . ILE E  1 51  ? -0.207  57.835 67.360  1.00 56.85  ? 51   ILE E CG2 1 
ATOM   8124  C CD1 . ILE E  1 51  ? -1.365  56.609 65.014  1.00 57.81  ? 51   ILE E CD1 1 
ATOM   8125  N N   . LEU E  1 52  ? 1.381   56.384 70.362  1.00 54.16  ? 52   LEU E N   1 
ATOM   8126  C CA  . LEU E  1 52  ? 1.486   56.802 71.759  1.00 54.78  ? 52   LEU E CA  1 
ATOM   8127  C C   . LEU E  1 52  ? 1.008   58.242 71.986  1.00 56.71  ? 52   LEU E C   1 
ATOM   8128  O O   . LEU E  1 52  ? 0.831   58.666 73.129  1.00 57.89  ? 52   LEU E O   1 
ATOM   8129  C CB  . LEU E  1 52  ? 2.927   56.634 72.250  1.00 52.21  ? 52   LEU E CB  1 
ATOM   8130  C CG  . LEU E  1 52  ? 3.512   55.222 72.123  1.00 50.48  ? 52   LEU E CG  1 
ATOM   8131  C CD1 . LEU E  1 52  ? 4.982   55.212 72.507  1.00 48.18  ? 52   LEU E CD1 1 
ATOM   8132  C CD2 . LEU E  1 52  ? 2.739   54.225 72.974  1.00 51.89  ? 52   LEU E CD2 1 
ATOM   8133  N N   . ARG E  1 53  ? 0.807   58.981 70.895  1.00 57.17  ? 53   ARG E N   1 
ATOM   8134  C CA  . ARG E  1 53  ? 0.360   60.370 70.940  1.00 59.23  ? 53   ARG E CA  1 
ATOM   8135  C C   . ARG E  1 53  ? 1.403   61.220 71.689  1.00 58.31  ? 53   ARG E C   1 
ATOM   8136  O O   . ARG E  1 53  ? 2.521   61.376 71.192  1.00 56.15  ? 53   ARG E O   1 
ATOM   8137  C CB  . ARG E  1 53  ? -1.065  60.472 71.518  1.00 62.60  ? 53   ARG E CB  1 
ATOM   8138  C CG  . ARG E  1 53  ? -1.743  61.816 71.265  1.00 65.26  ? 53   ARG E CG  1 
ATOM   8139  C CD  . ARG E  1 53  ? -3.115  61.924 71.924  1.00 68.85  ? 53   ARG E CD  1 
ATOM   8140  N NE  . ARG E  1 53  ? -4.212  61.649 70.989  1.00 70.79  ? 53   ARG E NE  1 
ATOM   8141  C CZ  . ARG E  1 53  ? -4.843  60.481 70.844  1.00 71.23  ? 53   ARG E CZ  1 
ATOM   8142  N NH1 . ARG E  1 53  ? -4.515  59.415 71.571  1.00 69.87  ? 53   ARG E NH1 1 
ATOM   8143  N NH2 . ARG E  1 53  ? -5.826  60.376 69.954  1.00 73.26  ? 53   ARG E NH2 1 
ATOM   8144  N N   . ASP E  1 54  ? 1.066   61.750 72.865  1.00 60.07  ? 54   ASP E N   1 
ATOM   8145  C CA  . ASP E  1 54  ? 2.007   62.555 73.651  1.00 59.51  ? 54   ASP E CA  1 
ATOM   8146  C C   . ASP E  1 54  ? 2.736   61.747 74.729  1.00 57.85  ? 54   ASP E C   1 
ATOM   8147  O O   . ASP E  1 54  ? 3.616   62.281 75.407  1.00 57.25  ? 54   ASP E O   1 
ATOM   8148  C CB  . ASP E  1 54  ? 1.284   63.746 74.287  1.00 62.62  ? 54   ASP E CB  1 
ATOM   8149  C CG  . ASP E  1 54  ? 0.844   64.777 73.261  1.00 64.26  ? 54   ASP E CG  1 
ATOM   8150  O OD1 . ASP E  1 54  ? 1.706   65.279 72.507  1.00 62.87  ? 54   ASP E OD1 1 
ATOM   8151  O OD2 . ASP E  1 54  ? -0.363  65.092 73.214  1.00 67.13  ? 54   ASP E OD2 1 
ATOM   8152  N N   . CYS E  1 55  ? 2.377   60.472 74.890  1.00 57.32  ? 55   CYS E N   1 
ATOM   8153  C CA  . CYS E  1 55  ? 3.091   59.582 75.815  1.00 55.71  ? 55   CYS E CA  1 
ATOM   8154  C C   . CYS E  1 55  ? 4.373   59.040 75.172  1.00 52.72  ? 55   CYS E C   1 
ATOM   8155  O O   . CYS E  1 55  ? 4.443   58.870 73.956  1.00 51.86  ? 55   CYS E O   1 
ATOM   8156  C CB  . CYS E  1 55  ? 2.200   58.419 76.271  1.00 56.66  ? 55   CYS E CB  1 
ATOM   8157  S SG  . CYS E  1 55  ? 0.927   58.873 77.476  1.00 60.09  ? 55   CYS E SG  1 
ATOM   8158  N N   . SER E  1 56  ? 5.383   58.786 76.001  1.00 51.27  ? 56   SER E N   1 
ATOM   8159  C CA  . SER E  1 56  ? 6.619   58.149 75.555  1.00 48.69  ? 56   SER E CA  1 
ATOM   8160  C C   . SER E  1 56  ? 6.539   56.648 75.811  1.00 47.94  ? 56   SER E C   1 
ATOM   8161  O O   . SER E  1 56  ? 5.559   56.152 76.368  1.00 49.39  ? 56   SER E O   1 
ATOM   8162  C CB  . SER E  1 56  ? 7.823   58.735 76.297  1.00 47.84  ? 56   SER E CB  1 
ATOM   8163  O OG  . SER E  1 56  ? 7.959   58.158 77.586  1.00 47.91  ? 56   SER E OG  1 
ATOM   8164  N N   . VAL E  1 57  ? 7.582   55.928 75.410  1.00 45.87  ? 57   VAL E N   1 
ATOM   8165  C CA  . VAL E  1 57  ? 7.647   54.483 75.624  1.00 45.24  ? 57   VAL E CA  1 
ATOM   8166  C C   . VAL E  1 57  ? 7.769   54.194 77.120  1.00 45.67  ? 57   VAL E C   1 
ATOM   8167  O O   . VAL E  1 57  ? 7.162   53.250 77.629  1.00 46.45  ? 57   VAL E O   1 
ATOM   8168  C CB  . VAL E  1 57  ? 8.827   53.849 74.858  1.00 43.14  ? 57   VAL E CB  1 
ATOM   8169  C CG1 . VAL E  1 57  ? 8.961   52.368 75.182  1.00 42.80  ? 57   VAL E CG1 1 
ATOM   8170  C CG2 . VAL E  1 57  ? 8.651   54.044 73.357  1.00 42.75  ? 57   VAL E CG2 1 
ATOM   8171  N N   . ALA E  1 58  ? 8.555   55.016 77.814  1.00 45.29  ? 58   ALA E N   1 
ATOM   8172  C CA  . ALA E  1 58  ? 8.703   54.917 79.266  1.00 45.78  ? 58   ALA E CA  1 
ATOM   8173  C C   . ALA E  1 58  ? 7.371   55.171 79.976  1.00 47.97  ? 58   ALA E C   1 
ATOM   8174  O O   . ALA E  1 58  ? 6.958   54.385 80.832  1.00 48.64  ? 58   ALA E O   1 
ATOM   8175  C CB  . ALA E  1 58  ? 9.756   55.898 79.755  1.00 45.25  ? 58   ALA E CB  1 
ATOM   8176  N N   . GLY E  1 59  ? 6.705   56.265 79.607  1.00 49.24  ? 59   GLY E N   1 
ATOM   8177  C CA  . GLY E  1 59  ? 5.400   56.612 80.169  1.00 51.65  ? 59   GLY E CA  1 
ATOM   8178  C C   . GLY E  1 59  ? 4.390   55.488 80.018  1.00 52.56  ? 59   GLY E C   1 
ATOM   8179  O O   . GLY E  1 59  ? 3.665   55.164 80.959  1.00 54.12  ? 59   GLY E O   1 
ATOM   8180  N N   . TRP E  1 60  ? 4.352   54.889 78.832  1.00 51.74  ? 60   TRP E N   1 
ATOM   8181  C CA  . TRP E  1 60  ? 3.470   53.757 78.560  1.00 52.67  ? 60   TRP E CA  1 
ATOM   8182  C C   . TRP E  1 60  ? 3.839   52.543 79.417  1.00 52.15  ? 60   TRP E C   1 
ATOM   8183  O O   . TRP E  1 60  ? 2.986   51.985 80.107  1.00 53.86  ? 60   TRP E O   1 
ATOM   8184  C CB  . TRP E  1 60  ? 3.500   53.413 77.059  1.00 51.81  ? 60   TRP E CB  1 
ATOM   8185  C CG  . TRP E  1 60  ? 3.034   52.027 76.702  1.00 52.21  ? 60   TRP E CG  1 
ATOM   8186  C CD1 . TRP E  1 60  ? 1.969   51.357 77.225  1.00 54.34  ? 60   TRP E CD1 1 
ATOM   8187  C CD2 . TRP E  1 60  ? 3.608   51.160 75.716  1.00 50.71  ? 60   TRP E CD2 1 
ATOM   8188  N NE1 . TRP E  1 60  ? 1.853   50.118 76.641  1.00 54.31  ? 60   TRP E NE1 1 
ATOM   8189  C CE2 . TRP E  1 60  ? 2.846   49.973 75.709  1.00 52.10  ? 60   TRP E CE2 1 
ATOM   8190  C CE3 . TRP E  1 60  ? 4.698   51.269 74.843  1.00 48.51  ? 60   TRP E CE3 1 
ATOM   8191  C CZ2 . TRP E  1 60  ? 3.139   48.899 74.862  1.00 51.39  ? 60   TRP E CZ2 1 
ATOM   8192  C CZ3 . TRP E  1 60  ? 4.988   50.201 74.001  1.00 47.72  ? 60   TRP E CZ3 1 
ATOM   8193  C CH2 . TRP E  1 60  ? 4.211   49.033 74.017  1.00 49.16  ? 60   TRP E CH2 1 
ATOM   8194  N N   . LEU E  1 61  ? 5.110   52.149 79.380  1.00 49.99  ? 61   LEU E N   1 
ATOM   8195  C CA  . LEU E  1 61  ? 5.550   50.914 80.039  1.00 49.49  ? 61   LEU E CA  1 
ATOM   8196  C C   . LEU E  1 61  ? 5.513   50.988 81.567  1.00 50.28  ? 61   LEU E C   1 
ATOM   8197  O O   . LEU E  1 61  ? 5.125   50.021 82.224  1.00 51.17  ? 61   LEU E O   1 
ATOM   8198  C CB  . LEU E  1 61  ? 6.950   50.510 79.562  1.00 47.19  ? 61   LEU E CB  1 
ATOM   8199  C CG  . LEU E  1 61  ? 7.057   50.008 78.118  1.00 46.39  ? 61   LEU E CG  1 
ATOM   8200  C CD1 . LEU E  1 61  ? 8.476   49.525 77.850  1.00 44.42  ? 61   LEU E CD1 1 
ATOM   8201  C CD2 . LEU E  1 61  ? 6.057   48.897 77.827  1.00 47.84  ? 61   LEU E CD2 1 
ATOM   8202  N N   . LEU E  1 62  ? 5.913   52.125 82.130  1.00 50.09  ? 62   LEU E N   1 
ATOM   8203  C CA  . LEU E  1 62  ? 5.824   52.328 83.580  1.00 51.00  ? 62   LEU E CA  1 
ATOM   8204  C C   . LEU E  1 62  ? 4.383   52.536 84.051  1.00 53.57  ? 62   LEU E C   1 
ATOM   8205  O O   . LEU E  1 62  ? 4.086   52.343 85.223  1.00 54.62  ? 62   LEU E O   1 
ATOM   8206  C CB  . LEU E  1 62  ? 6.692   53.507 84.020  1.00 50.27  ? 62   LEU E CB  1 
ATOM   8207  C CG  . LEU E  1 62  ? 8.192   53.250 83.907  1.00 48.10  ? 62   LEU E CG  1 
ATOM   8208  C CD1 . LEU E  1 62  ? 8.965   54.552 84.042  1.00 47.70  ? 62   LEU E CD1 1 
ATOM   8209  C CD2 . LEU E  1 62  ? 8.653   52.238 84.946  1.00 47.81  ? 62   LEU E CD2 1 
ATOM   8210  N N   . GLY E  1 63  ? 3.493   52.914 83.137  1.00 54.71  ? 63   GLY E N   1 
ATOM   8211  C CA  . GLY E  1 63  ? 2.089   53.112 83.467  1.00 57.48  ? 63   GLY E CA  1 
ATOM   8212  C C   . GLY E  1 63  ? 1.834   54.485 84.056  1.00 58.78  ? 63   GLY E C   1 
ATOM   8213  O O   . GLY E  1 63  ? 1.163   54.614 85.078  1.00 60.66  ? 63   GLY E O   1 
ATOM   8214  N N   . ASN E  1 64  ? 2.379   55.511 83.411  1.00 57.95  ? 64   ASN E N   1 
ATOM   8215  C CA  . ASN E  1 64  ? 2.107   56.896 83.780  1.00 59.49  ? 64   ASN E CA  1 
ATOM   8216  C C   . ASN E  1 64  ? 0.596   57.163 83.661  1.00 62.54  ? 64   ASN E C   1 
ATOM   8217  O O   . ASN E  1 64  ? -0.021  56.766 82.671  1.00 62.99  ? 64   ASN E O   1 
ATOM   8218  C CB  . ASN E  1 64  ? 2.953   57.827 82.889  1.00 58.12  ? 64   ASN E CB  1 
ATOM   8219  C CG  . ASN E  1 64  ? 2.533   59.291 82.957  1.00 60.09  ? 64   ASN E CG  1 
ATOM   8220  O OD1 . ASN E  1 64  ? 1.354   59.617 83.066  1.00 62.64  ? 64   ASN E OD1 1 
ATOM   8221  N ND2 . ASN E  1 64  ? 3.510   60.186 82.844  1.00 59.14  ? 64   ASN E ND2 1 
ATOM   8222  N N   . PRO E  1 65  ? -0.009  57.818 84.677  1.00 64.84  ? 65   PRO E N   1 
ATOM   8223  C CA  . PRO E  1 65  ? -1.471  58.032 84.726  1.00 68.15  ? 65   PRO E CA  1 
ATOM   8224  C C   . PRO E  1 65  ? -2.093  58.752 83.517  1.00 69.46  ? 65   PRO E C   1 
ATOM   8225  O O   . PRO E  1 65  ? -3.288  58.592 83.260  1.00 71.95  ? 65   PRO E O   1 
ATOM   8226  C CB  . PRO E  1 65  ? -1.672  58.871 85.999  1.00 69.99  ? 65   PRO E CB  1 
ATOM   8227  C CG  . PRO E  1 65  ? -0.323  59.368 86.386  1.00 67.77  ? 65   PRO E CG  1 
ATOM   8228  C CD  . PRO E  1 65  ? 0.659   58.364 85.873  1.00 64.62  ? 65   PRO E CD  1 
ATOM   8229  N N   . MET E  1 66  ? -1.296  59.536 82.793  1.00 68.01  ? 66   MET E N   1 
ATOM   8230  C CA  . MET E  1 66  ? -1.752  60.197 81.567  1.00 68.96  ? 66   MET E CA  1 
ATOM   8231  C C   . MET E  1 66  ? -1.846  59.212 80.400  1.00 67.66  ? 66   MET E C   1 
ATOM   8232  O O   . MET E  1 66  ? -2.508  59.483 79.396  1.00 68.84  ? 66   MET E O   1 
ATOM   8233  C CB  . MET E  1 66  ? -0.788  61.321 81.175  1.00 67.81  ? 66   MET E CB  1 
ATOM   8234  C CG  . MET E  1 66  ? -0.536  62.367 82.248  1.00 69.06  ? 66   MET E CG  1 
ATOM   8235  S SD  . MET E  1 66  ? -2.032  63.246 82.720  1.00 73.67  ? 66   MET E SD  1 
ATOM   8236  C CE  . MET E  1 66  ? -1.340  64.794 83.301  1.00 74.56  ? 66   MET E CE  1 
ATOM   8237  N N   . CYS E  1 67  ? -1.168  58.077 80.535  1.00 65.37  ? 67   CYS E N   1 
ATOM   8238  C CA  . CYS E  1 67  ? -1.115  57.061 79.492  1.00 64.03  ? 67   CYS E CA  1 
ATOM   8239  C C   . CYS E  1 67  ? -2.075  55.907 79.790  1.00 65.65  ? 67   CYS E C   1 
ATOM   8240  O O   . CYS E  1 67  ? -1.784  54.746 79.486  1.00 64.32  ? 67   CYS E O   1 
ATOM   8241  C CB  . CYS E  1 67  ? 0.324   56.566 79.366  1.00 60.66  ? 67   CYS E CB  1 
ATOM   8242  S SG  . CYS E  1 67  ? 1.499   57.933 79.205  1.00 59.15  ? 67   CYS E SG  1 
ATOM   8243  N N   . ASP E  1 68  ? -3.224  56.245 80.377  1.00 68.77  ? 68   ASP E N   1 
ATOM   8244  C CA  . ASP E  1 68  ? -4.296  55.285 80.640  1.00 71.00  ? 68   ASP E CA  1 
ATOM   8245  C C   . ASP E  1 68  ? -4.874  54.705 79.352  1.00 71.57  ? 68   ASP E C   1 
ATOM   8246  O O   . ASP E  1 68  ? -5.469  53.632 79.367  1.00 72.75  ? 68   ASP E O   1 
ATOM   8247  C CB  . ASP E  1 68  ? -5.427  55.941 81.447  1.00 74.56  ? 68   ASP E CB  1 
ATOM   8248  C CG  . ASP E  1 68  ? -5.111  56.047 82.931  1.00 74.57  ? 68   ASP E CG  1 
ATOM   8249  O OD1 . ASP E  1 68  ? -3.995  55.674 83.347  1.00 71.82  ? 68   ASP E OD1 1 
ATOM   8250  O OD2 . ASP E  1 68  ? -5.991  56.505 83.693  1.00 77.51  ? 68   ASP E OD2 1 
ATOM   8251  N N   . GLU E  1 69  ? -4.718  55.420 78.243  1.00 70.95  ? 69   GLU E N   1 
ATOM   8252  C CA  . GLU E  1 69  ? -5.114  54.895 76.942  1.00 71.13  ? 69   GLU E CA  1 
ATOM   8253  C C   . GLU E  1 69  ? -4.380  53.590 76.620  1.00 68.73  ? 69   GLU E C   1 
ATOM   8254  O O   . GLU E  1 69  ? -4.939  52.706 75.969  1.00 69.67  ? 69   GLU E O   1 
ATOM   8255  C CB  . GLU E  1 69  ? -4.838  55.932 75.851  1.00 70.38  ? 69   GLU E CB  1 
ATOM   8256  C CG  . GLU E  1 69  ? -5.306  55.520 74.462  1.00 70.77  ? 69   GLU E CG  1 
ATOM   8257  C CD  . GLU E  1 69  ? -5.065  56.588 73.409  1.00 70.20  ? 69   GLU E CD  1 
ATOM   8258  O OE1 . GLU E  1 69  ? -4.736  57.740 73.773  1.00 70.19  ? 69   GLU E OE1 1 
ATOM   8259  O OE2 . GLU E  1 69  ? -5.207  56.271 72.209  1.00 69.89  ? 69   GLU E OE2 1 
ATOM   8260  N N   . PHE E  1 70  ? -3.142  53.471 77.102  1.00 65.93  ? 70   PHE E N   1 
ATOM   8261  C CA  . PHE E  1 70  ? -2.244  52.389 76.702  1.00 63.46  ? 70   PHE E CA  1 
ATOM   8262  C C   . PHE E  1 70  ? -2.048  51.288 77.759  1.00 63.39  ? 70   PHE E C   1 
ATOM   8263  O O   . PHE E  1 70  ? -1.008  50.628 77.788  1.00 61.08  ? 70   PHE E O   1 
ATOM   8264  C CB  . PHE E  1 70  ? -0.900  52.996 76.273  1.00 60.39  ? 70   PHE E CB  1 
ATOM   8265  C CG  . PHE E  1 70  ? -1.047  54.179 75.351  1.00 60.58  ? 70   PHE E CG  1 
ATOM   8266  C CD1 . PHE E  1 70  ? -1.564  54.015 74.074  1.00 61.09  ? 70   PHE E CD1 1 
ATOM   8267  C CD2 . PHE E  1 70  ? -0.706  55.459 75.771  1.00 60.50  ? 70   PHE E CD2 1 
ATOM   8268  C CE1 . PHE E  1 70  ? -1.717  55.098 73.227  1.00 61.41  ? 70   PHE E CE1 1 
ATOM   8269  C CE2 . PHE E  1 70  ? -0.857  56.547 74.928  1.00 60.95  ? 70   PHE E CE2 1 
ATOM   8270  C CZ  . PHE E  1 70  ? -1.364  56.367 73.654  1.00 61.37  ? 70   PHE E CZ  1 
ATOM   8271  N N   . ILE E  1 71  ? -3.049  51.090 78.617  1.00 66.10  ? 71   ILE E N   1 
ATOM   8272  C CA  . ILE E  1 71  ? -3.114  49.895 79.477  1.00 66.67  ? 71   ILE E CA  1 
ATOM   8273  C C   . ILE E  1 71  ? -3.762  48.759 78.675  1.00 68.05  ? 71   ILE E C   1 
ATOM   8274  O O   . ILE E  1 71  ? -4.811  48.954 78.051  1.00 70.37  ? 71   ILE E O   1 
ATOM   8275  C CB  . ILE E  1 71  ? -3.876  50.148 80.812  1.00 69.10  ? 71   ILE E CB  1 
ATOM   8276  C CG1 . ILE E  1 71  ? -4.279  48.829 81.494  1.00 70.52  ? 71   ILE E CG1 1 
ATOM   8277  C CG2 . ILE E  1 71  ? -5.128  50.995 80.605  1.00 72.12  ? 71   ILE E CG2 1 
ATOM   8278  C CD1 . ILE E  1 71  ? -4.632  48.974 82.961  1.00 72.02  ? 71   ILE E CD1 1 
ATOM   8279  N N   . ASN E  1 72  ? -3.130  47.582 78.687  1.00 66.84  ? 72   ASN E N   1 
ATOM   8280  C CA  . ASN E  1 72  ? -3.581  46.422 77.896  1.00 68.02  ? 72   ASN E CA  1 
ATOM   8281  C C   . ASN E  1 72  ? -3.786  46.730 76.405  1.00 67.78  ? 72   ASN E C   1 
ATOM   8282  O O   . ASN E  1 72  ? -4.860  46.491 75.852  1.00 70.33  ? 72   ASN E O   1 
ATOM   8283  C CB  . ASN E  1 72  ? -4.863  45.820 78.497  1.00 71.70  ? 72   ASN E CB  1 
ATOM   8284  C CG  . ASN E  1 72  ? -4.625  45.160 79.844  1.00 71.98  ? 72   ASN E CG  1 
ATOM   8285  O OD1 . ASN E  1 72  ? -3.494  45.104 80.332  1.00 69.45  ? 72   ASN E OD1 1 
ATOM   8286  N ND2 . ASN E  1 72  ? -5.694  44.650 80.453  1.00 75.24  ? 72   ASN E ND2 1 
ATOM   8287  N N   . VAL E  1 73  ? -2.747  47.258 75.761  1.00 64.83  ? 73   VAL E N   1 
ATOM   8288  C CA  . VAL E  1 73  ? -2.826  47.613 74.336  1.00 64.33  ? 73   VAL E CA  1 
ATOM   8289  C C   . VAL E  1 73  ? -2.981  46.391 73.426  1.00 64.85  ? 73   VAL E C   1 
ATOM   8290  O O   . VAL E  1 73  ? -2.453  45.318 73.730  1.00 64.31  ? 73   VAL E O   1 
ATOM   8291  C CB  . VAL E  1 73  ? -1.597  48.420 73.852  1.00 61.09  ? 73   VAL E CB  1 
ATOM   8292  C CG1 . VAL E  1 73  ? -1.625  49.828 74.422  1.00 61.09  ? 73   VAL E CG1 1 
ATOM   8293  C CG2 . VAL E  1 73  ? -0.285  47.715 74.192  1.00 58.59  ? 73   VAL E CG2 1 
ATOM   8294  N N   . PRO E  1 74  ? -3.700  46.553 72.300  1.00 66.08  ? 74   PRO E N   1 
ATOM   8295  C CA  . PRO E  1 74  ? -3.764  45.486 71.309  1.00 66.45  ? 74   PRO E CA  1 
ATOM   8296  C C   . PRO E  1 74  ? -2.461  45.422 70.521  1.00 63.14  ? 74   PRO E C   1 
ATOM   8297  O O   . PRO E  1 74  ? -1.659  46.362 70.575  1.00 60.81  ? 74   PRO E O   1 
ATOM   8298  C CB  . PRO E  1 74  ? -4.923  45.916 70.407  1.00 68.81  ? 74   PRO E CB  1 
ATOM   8299  C CG  . PRO E  1 74  ? -4.912  47.403 70.478  1.00 68.10  ? 74   PRO E CG  1 
ATOM   8300  C CD  . PRO E  1 74  ? -4.419  47.762 71.854  1.00 67.19  ? 74   PRO E CD  1 
ATOM   8301  N N   . GLU E  1 75  ? -2.256  44.332 69.787  1.00 63.13  ? 75   GLU E N   1 
ATOM   8302  C CA  . GLU E  1 75  ? -1.025  44.167 69.021  1.00 60.24  ? 75   GLU E CA  1 
ATOM   8303  C C   . GLU E  1 75  ? -0.910  45.240 67.940  1.00 58.91  ? 75   GLU E C   1 
ATOM   8304  O O   . GLU E  1 75  ? -1.917  45.722 67.415  1.00 60.68  ? 75   GLU E O   1 
ATOM   8305  C CB  . GLU E  1 75  ? -0.923  42.764 68.414  1.00 60.97  ? 75   GLU E CB  1 
ATOM   8306  C CG  . GLU E  1 75  ? -1.639  42.572 67.092  1.00 62.40  ? 75   GLU E CG  1 
ATOM   8307  C CD  . GLU E  1 75  ? -1.386  41.199 66.506  1.00 63.03  ? 75   GLU E CD  1 
ATOM   8308  O OE1 . GLU E  1 75  ? -1.798  40.194 67.129  1.00 65.22  ? 75   GLU E OE1 1 
ATOM   8309  O OE2 . GLU E  1 75  ? -0.773  41.129 65.421  1.00 61.50  ? 75   GLU E OE2 1 
ATOM   8310  N N   . TRP E  1 76  ? 0.330   45.596 67.619  1.00 55.95  ? 76   TRP E N   1 
ATOM   8311  C CA  . TRP E  1 76  ? 0.620   46.701 66.715  1.00 54.47  ? 76   TRP E CA  1 
ATOM   8312  C C   . TRP E  1 76  ? 1.509   46.230 65.573  1.00 52.60  ? 76   TRP E C   1 
ATOM   8313  O O   . TRP E  1 76  ? 2.324   45.324 65.743  1.00 51.64  ? 76   TRP E O   1 
ATOM   8314  C CB  . TRP E  1 76  ? 1.312   47.837 67.477  1.00 52.82  ? 76   TRP E CB  1 
ATOM   8315  C CG  . TRP E  1 76  ? 2.590   47.413 68.151  1.00 50.78  ? 76   TRP E CG  1 
ATOM   8316  C CD1 . TRP E  1 76  ? 3.849   47.422 67.611  1.00 48.36  ? 76   TRP E CD1 1 
ATOM   8317  C CD2 . TRP E  1 76  ? 2.731   46.901 69.483  1.00 51.17  ? 76   TRP E CD2 1 
ATOM   8318  N NE1 . TRP E  1 76  ? 4.762   46.952 68.526  1.00 47.32  ? 76   TRP E NE1 1 
ATOM   8319  C CE2 . TRP E  1 76  ? 4.103   46.626 69.683  1.00 48.94  ? 76   TRP E CE2 1 
ATOM   8320  C CE3 . TRP E  1 76  ? 1.832   46.649 70.526  1.00 53.31  ? 76   TRP E CE3 1 
ATOM   8321  C CZ2 . TRP E  1 76  ? 4.596   46.115 70.885  1.00 48.77  ? 76   TRP E CZ2 1 
ATOM   8322  C CZ3 . TRP E  1 76  ? 2.322   46.139 71.721  1.00 53.04  ? 76   TRP E CZ3 1 
ATOM   8323  C CH2 . TRP E  1 76  ? 3.692   45.877 71.890  1.00 50.77  ? 76   TRP E CH2 1 
ATOM   8324  N N   . SER E  1 77  ? 1.343   46.850 64.409  1.00 52.25  ? 77   SER E N   1 
ATOM   8325  C CA  . SER E  1 77  ? 2.234   46.623 63.272  1.00 50.31  ? 77   SER E CA  1 
ATOM   8326  C C   . SER E  1 77  ? 3.556   47.350 63.506  1.00 47.58  ? 77   SER E C   1 
ATOM   8327  O O   . SER E  1 77  ? 4.634   46.793 63.289  1.00 45.94  ? 77   SER E O   1 
ATOM   8328  C CB  . SER E  1 77  ? 1.583   47.129 61.989  1.00 50.96  ? 77   SER E CB  1 
ATOM   8329  O OG  . SER E  1 77  ? 0.960   48.384 62.202  1.00 51.71  ? 77   SER E OG  1 
ATOM   8330  N N   . TYR E  1 78  ? 3.452   48.600 63.948  1.00 47.36  ? 78   TYR E N   1 
ATOM   8331  C CA  . TYR E  1 78  ? 4.611   49.406 64.318  1.00 45.22  ? 78   TYR E CA  1 
ATOM   8332  C C   . TYR E  1 78  ? 4.197   50.432 65.375  1.00 46.04  ? 78   TYR E C   1 
ATOM   8333  O O   . TYR E  1 78  ? 3.009   50.612 65.633  1.00 48.18  ? 78   TYR E O   1 
ATOM   8334  C CB  . TYR E  1 78  ? 5.199   50.096 63.079  1.00 43.69  ? 78   TYR E CB  1 
ATOM   8335  C CG  . TYR E  1 78  ? 4.246   51.041 62.372  1.00 44.88  ? 78   TYR E CG  1 
ATOM   8336  C CD1 . TYR E  1 78  ? 3.269   50.561 61.496  1.00 46.37  ? 78   TYR E CD1 1 
ATOM   8337  C CD2 . TYR E  1 78  ? 4.325   52.417 62.575  1.00 44.74  ? 78   TYR E CD2 1 
ATOM   8338  C CE1 . TYR E  1 78  ? 2.396   51.426 60.847  1.00 47.65  ? 78   TYR E CE1 1 
ATOM   8339  C CE2 . TYR E  1 78  ? 3.457   53.288 61.932  1.00 46.08  ? 78   TYR E CE2 1 
ATOM   8340  C CZ  . TYR E  1 78  ? 2.494   52.788 61.070  1.00 47.51  ? 78   TYR E CZ  1 
ATOM   8341  O OH  . TYR E  1 78  ? 1.636   53.659 60.437  1.00 48.99  ? 78   TYR E OH  1 
ATOM   8342  N N   . ILE E  1 79  ? 5.178   51.095 65.982  1.00 44.57  ? 79   ILE E N   1 
ATOM   8343  C CA  . ILE E  1 79  ? 4.920   52.081 67.033  1.00 45.34  ? 79   ILE E CA  1 
ATOM   8344  C C   . ILE E  1 79  ? 5.251   53.486 66.542  1.00 44.79  ? 79   ILE E C   1 
ATOM   8345  O O   . ILE E  1 79  ? 6.202   53.673 65.785  1.00 43.09  ? 79   ILE E O   1 
ATOM   8346  C CB  . ILE E  1 79  ? 5.742   51.771 68.301  1.00 44.49  ? 79   ILE E CB  1 
ATOM   8347  C CG1 . ILE E  1 79  ? 5.316   50.421 68.885  1.00 45.42  ? 79   ILE E CG1 1 
ATOM   8348  C CG2 . ILE E  1 79  ? 5.565   52.868 69.344  1.00 45.24  ? 79   ILE E CG2 1 
ATOM   8349  C CD1 . ILE E  1 79  ? 6.301   49.832 69.873  1.00 44.34  ? 79   ILE E CD1 1 
ATOM   8350  N N   . VAL E  1 80  ? 4.465   54.469 66.976  1.00 46.48  ? 80   VAL E N   1 
ATOM   8351  C CA  . VAL E  1 80  ? 4.699   55.867 66.615  1.00 46.45  ? 80   VAL E CA  1 
ATOM   8352  C C   . VAL E  1 80  ? 4.866   56.721 67.871  1.00 47.10  ? 80   VAL E C   1 
ATOM   8353  O O   . VAL E  1 80  ? 3.979   56.772 68.724  1.00 48.95  ? 80   VAL E O   1 
ATOM   8354  C CB  . VAL E  1 80  ? 3.554   56.438 65.751  1.00 48.28  ? 80   VAL E CB  1 
ATOM   8355  C CG1 . VAL E  1 80  ? 3.866   57.866 65.315  1.00 48.28  ? 80   VAL E CG1 1 
ATOM   8356  C CG2 . VAL E  1 80  ? 3.319   55.556 64.536  1.00 47.88  ? 80   VAL E CG2 1 
ATOM   8357  N N   . GLU E  1 81  ? 6.009   57.395 67.957  1.00 45.76  ? 81   GLU E N   1 
ATOM   8358  C CA  . GLU E  1 81  ? 6.359   58.225 69.099  1.00 46.29  ? 81   GLU E CA  1 
ATOM   8359  C C   . GLU E  1 81  ? 6.822   59.586 68.594  1.00 46.42  ? 81   GLU E C   1 
ATOM   8360  O O   . GLU E  1 81  ? 7.508   59.671 67.582  1.00 45.11  ? 81   GLU E O   1 
ATOM   8361  C CB  . GLU E  1 81  ? 7.483   57.555 69.894  1.00 44.64  ? 81   GLU E CB  1 
ATOM   8362  C CG  . GLU E  1 81  ? 7.839   58.244 71.203  1.00 45.21  ? 81   GLU E CG  1 
ATOM   8363  C CD  . GLU E  1 81  ? 9.046   57.628 71.892  1.00 43.62  ? 81   GLU E CD  1 
ATOM   8364  O OE1 . GLU E  1 81  ? 10.033  57.292 71.194  1.00 41.95  ? 81   GLU E OE1 1 
ATOM   8365  O OE2 . GLU E  1 81  ? 9.014   57.487 73.136  1.00 44.17  ? 81   GLU E OE2 1 
ATOM   8366  N N   . LYS E  1 82  ? 6.452   60.646 69.300  1.00 48.22  ? 82   LYS E N   1 
ATOM   8367  C CA  . LYS E  1 82  ? 6.892   61.993 68.939  1.00 48.75  ? 82   LYS E CA  1 
ATOM   8368  C C   . LYS E  1 82  ? 8.369   62.214 69.273  1.00 47.22  ? 82   LYS E C   1 
ATOM   8369  O O   . LYS E  1 82  ? 8.995   61.408 69.968  1.00 45.96  ? 82   LYS E O   1 
ATOM   8370  C CB  . LYS E  1 82  ? 6.026   63.048 69.638  1.00 51.47  ? 82   LYS E CB  1 
ATOM   8371  C CG  . LYS E  1 82  ? 4.685   63.274 68.962  1.00 53.47  ? 82   LYS E CG  1 
ATOM   8372  C CD  . LYS E  1 82  ? 3.862   64.328 69.684  1.00 56.43  ? 82   LYS E CD  1 
ATOM   8373  C CE  . LYS E  1 82  ? 2.714   64.828 68.821  1.00 58.64  ? 82   LYS E CE  1 
ATOM   8374  N NZ  . LYS E  1 82  ? 1.617   63.830 68.701  1.00 59.39  ? 82   LYS E NZ  1 
ATOM   8375  N N   . ALA E  1 83  ? 8.920   63.310 68.758  1.00 47.57  ? 83   ALA E N   1 
ATOM   8376  C CA  . ALA E  1 83  ? 10.313  63.669 69.014  1.00 46.57  ? 83   ALA E CA  1 
ATOM   8377  C C   . ALA E  1 83  ? 10.530  64.078 70.475  1.00 47.65  ? 83   ALA E C   1 
ATOM   8378  O O   . ALA E  1 83  ? 11.547  63.722 71.074  1.00 46.54  ? 83   ALA E O   1 
ATOM   8379  C CB  . ALA E  1 83  ? 10.753  64.784 68.077  1.00 46.99  ? 83   ALA E CB  1 
ATOM   8380  N N   . ASN E  1 84  ? 9.573   64.814 71.044  1.00 50.02  ? 84   ASN E N   1 
ATOM   8381  C CA  . ASN E  1 84  ? 9.670   65.283 72.430  1.00 51.33  ? 84   ASN E CA  1 
ATOM   8382  C C   . ASN E  1 84  ? 8.353   65.124 73.202  1.00 53.12  ? 84   ASN E C   1 
ATOM   8383  O O   . ASN E  1 84  ? 7.734   66.118 73.587  1.00 55.53  ? 84   ASN E O   1 
ATOM   8384  C CB  . ASN E  1 84  ? 10.122  66.752 72.450  1.00 52.99  ? 84   ASN E CB  1 
ATOM   8385  C CG  . ASN E  1 84  ? 11.440  66.970 71.716  1.00 51.59  ? 84   ASN E CG  1 
ATOM   8386  O OD1 . ASN E  1 84  ? 12.474  66.413 72.097  1.00 50.05  ? 84   ASN E OD1 1 
ATOM   8387  N ND2 . ASN E  1 84  ? 11.409  67.779 70.655  1.00 52.30  ? 84   ASN E ND2 1 
ATOM   8388  N N   . PRO E  1 85  ? 7.924   63.868 73.443  1.00 52.18  ? 85   PRO E N   1 
ATOM   8389  C CA  . PRO E  1 85  ? 6.648   63.633 74.127  1.00 54.00  ? 85   PRO E CA  1 
ATOM   8390  C C   . PRO E  1 85  ? 6.632   64.210 75.538  1.00 55.53  ? 85   PRO E C   1 
ATOM   8391  O O   . PRO E  1 85  ? 7.568   63.974 76.306  1.00 54.41  ? 85   PRO E O   1 
ATOM   8392  C CB  . PRO E  1 85  ? 6.540   62.099 74.171  1.00 52.42  ? 85   PRO E CB  1 
ATOM   8393  C CG  . PRO E  1 85  ? 7.489   61.604 73.136  1.00 50.04  ? 85   PRO E CG  1 
ATOM   8394  C CD  . PRO E  1 85  ? 8.604   62.603 73.116  1.00 49.65  ? 85   PRO E CD  1 
ATOM   8395  N N   . VAL E  1 86  ? 5.579   64.958 75.868  1.00 58.24  ? 86   VAL E N   1 
ATOM   8396  C CA  . VAL E  1 86  ? 5.473   65.610 77.180  1.00 60.05  ? 86   VAL E CA  1 
ATOM   8397  C C   . VAL E  1 86  ? 5.236   64.627 78.332  1.00 59.69  ? 86   VAL E C   1 
ATOM   8398  O O   . VAL E  1 86  ? 5.767   64.818 79.428  1.00 59.79  ? 86   VAL E O   1 
ATOM   8399  C CB  . VAL E  1 86  ? 4.375   66.707 77.212  1.00 63.45  ? 86   VAL E CB  1 
ATOM   8400  C CG1 . VAL E  1 86  ? 4.673   67.791 76.184  1.00 64.08  ? 86   VAL E CG1 1 
ATOM   8401  C CG2 . VAL E  1 86  ? 2.980   66.123 76.998  1.00 64.80  ? 86   VAL E CG2 1 
ATOM   8402  N N   . ASN E  1 87  ? 4.439   63.586 78.083  1.00 59.42  ? 87   ASN E N   1 
ATOM   8403  C CA  . ASN E  1 87  ? 4.116   62.587 79.107  1.00 59.30  ? 87   ASN E CA  1 
ATOM   8404  C C   . ASN E  1 87  ? 5.162   61.479 79.154  1.00 56.40  ? 87   ASN E C   1 
ATOM   8405  O O   . ASN E  1 87  ? 4.910   60.346 78.732  1.00 55.45  ? 87   ASN E O   1 
ATOM   8406  C CB  . ASN E  1 87  ? 2.725   61.983 78.866  1.00 60.88  ? 87   ASN E CB  1 
ATOM   8407  C CG  . ASN E  1 87  ? 1.599   62.949 79.185  1.00 64.26  ? 87   ASN E CG  1 
ATOM   8408  O OD1 . ASN E  1 87  ? 1.745   63.848 80.015  1.00 65.59  ? 87   ASN E OD1 1 
ATOM   8409  N ND2 . ASN E  1 87  ? 0.455   62.755 78.535  1.00 65.89  ? 87   ASN E ND2 1 
ATOM   8410  N N   . ASP E  1 88  ? 6.338   61.821 79.672  1.00 55.25  ? 88   ASP E N   1 
ATOM   8411  C CA  . ASP E  1 88  ? 7.432   60.872 79.820  1.00 52.77  ? 88   ASP E CA  1 
ATOM   8412  C C   . ASP E  1 88  ? 7.485   60.437 81.294  1.00 53.10  ? 88   ASP E C   1 
ATOM   8413  O O   . ASP E  1 88  ? 6.506   59.882 81.808  1.00 54.23  ? 88   ASP E O   1 
ATOM   8414  C CB  . ASP E  1 88  ? 8.740   61.511 79.319  1.00 51.46  ? 88   ASP E CB  1 
ATOM   8415  C CG  . ASP E  1 88  ? 9.881   60.507 79.177  1.00 49.02  ? 88   ASP E CG  1 
ATOM   8416  O OD1 . ASP E  1 88  ? 9.644   59.285 79.285  1.00 48.22  ? 88   ASP E OD1 1 
ATOM   8417  O OD2 . ASP E  1 88  ? 11.028  60.950 78.957  1.00 48.13  ? 88   ASP E OD2 1 
ATOM   8418  N N   . LEU E  1 89  ? 8.600   60.692 81.976  1.00 52.29  ? 89   LEU E N   1 
ATOM   8419  C CA  . LEU E  1 89  ? 8.727   60.393 83.398  1.00 52.65  ? 89   LEU E CA  1 
ATOM   8420  C C   . LEU E  1 89  ? 8.131   61.550 84.191  1.00 55.07  ? 89   LEU E C   1 
ATOM   8421  O O   . LEU E  1 89  ? 8.772   62.591 84.358  1.00 55.58  ? 89   LEU E O   1 
ATOM   8422  C CB  . LEU E  1 89  ? 10.205  60.176 83.771  1.00 50.95  ? 89   LEU E CB  1 
ATOM   8423  C CG  . LEU E  1 89  ? 10.785  58.749 83.753  1.00 49.01  ? 89   LEU E CG  1 
ATOM   8424  C CD1 . LEU E  1 89  ? 10.024  57.789 82.848  1.00 48.52  ? 89   LEU E CD1 1 
ATOM   8425  C CD2 . LEU E  1 89  ? 12.260  58.785 83.376  1.00 47.41  ? 89   LEU E CD2 1 
ATOM   8426  N N   . CYS E  1 90  ? 6.897   61.363 84.662  1.00 56.77  ? 90   CYS E N   1 
ATOM   8427  C CA  . CYS E  1 90  ? 6.192   62.391 85.427  1.00 59.41  ? 90   CYS E CA  1 
ATOM   8428  C C   . CYS E  1 90  ? 6.971   62.746 86.692  1.00 59.52  ? 90   CYS E C   1 
ATOM   8429  O O   . CYS E  1 90  ? 7.264   63.916 86.936  1.00 60.83  ? 90   CYS E O   1 
ATOM   8430  C CB  . CYS E  1 90  ? 4.760   61.953 85.764  1.00 61.29  ? 90   CYS E CB  1 
ATOM   8431  S SG  . CYS E  1 90  ? 4.575   60.283 86.439  1.00 60.23  ? 90   CYS E SG  1 
ATOM   8432  N N   . TYR E  1 91  ? 7.313   61.731 87.481  1.00 58.28  ? 91   TYR E N   1 
ATOM   8433  C CA  . TYR E  1 91  ? 8.257   61.900 88.580  1.00 57.94  ? 91   TYR E CA  1 
ATOM   8434  C C   . TYR E  1 91  ? 9.671   61.836 87.993  1.00 55.78  ? 91   TYR E C   1 
ATOM   8435  O O   . TYR E  1 91  ? 10.002  60.863 87.309  1.00 53.88  ? 91   TYR E O   1 
ATOM   8436  C CB  . TYR E  1 91  ? 8.069   60.807 89.632  1.00 57.62  ? 91   TYR E CB  1 
ATOM   8437  C CG  . TYR E  1 91  ? 8.729   61.123 90.959  1.00 58.05  ? 91   TYR E CG  1 
ATOM   8438  C CD1 . TYR E  1 91  ? 10.081  60.861 91.169  1.00 56.36  ? 91   TYR E CD1 1 
ATOM   8439  C CD2 . TYR E  1 91  ? 8.002   61.696 92.002  1.00 60.33  ? 91   TYR E CD2 1 
ATOM   8440  C CE1 . TYR E  1 91  ? 10.688  61.156 92.380  1.00 56.89  ? 91   TYR E CE1 1 
ATOM   8441  C CE2 . TYR E  1 91  ? 8.601   61.992 93.216  1.00 60.79  ? 91   TYR E CE2 1 
ATOM   8442  C CZ  . TYR E  1 91  ? 9.943   61.720 93.401  1.00 59.05  ? 91   TYR E CZ  1 
ATOM   8443  O OH  . TYR E  1 91  ? 10.541  62.012 94.607  1.00 59.64  ? 91   TYR E OH  1 
ATOM   8444  N N   . PRO E  1 92  ? 10.514  62.856 88.261  1.00 56.27  ? 92   PRO E N   1 
ATOM   8445  C CA  . PRO E  1 92  ? 11.815  62.937 87.580  1.00 54.62  ? 92   PRO E CA  1 
ATOM   8446  C C   . PRO E  1 92  ? 12.722  61.748 87.868  1.00 52.54  ? 92   PRO E C   1 
ATOM   8447  O O   . PRO E  1 92  ? 12.611  61.123 88.927  1.00 52.62  ? 92   PRO E O   1 
ATOM   8448  C CB  . PRO E  1 92  ? 12.451  64.214 88.152  1.00 56.18  ? 92   PRO E CB  1 
ATOM   8449  C CG  . PRO E  1 92  ? 11.372  64.915 88.890  1.00 58.68  ? 92   PRO E CG  1 
ATOM   8450  C CD  . PRO E  1 92  ? 10.393  63.874 89.318  1.00 58.46  ? 92   PRO E CD  1 
ATOM   8451  N N   . GLY E  1 93  ? 13.614  61.449 86.931  1.00 50.85  ? 93   GLY E N   1 
ATOM   8452  C CA  . GLY E  1 93  ? 14.551  60.351 87.098  1.00 49.09  ? 93   GLY E CA  1 
ATOM   8453  C C   . GLY E  1 93  ? 15.211  59.902 85.810  1.00 47.41  ? 93   GLY E C   1 
ATOM   8454  O O   . GLY E  1 93  ? 15.283  60.652 84.833  1.00 47.49  ? 93   GLY E O   1 
ATOM   8455  N N   . ASP E  1 94  ? 15.703  58.667 85.829  1.00 45.99  ? 94   ASP E N   1 
ATOM   8456  C CA  . ASP E  1 94  ? 16.312  58.039 84.668  1.00 44.42  ? 94   ASP E CA  1 
ATOM   8457  C C   . ASP E  1 94  ? 15.658  56.693 84.427  1.00 43.61  ? 94   ASP E C   1 
ATOM   8458  O O   . ASP E  1 94  ? 15.053  56.108 85.331  1.00 44.13  ? 94   ASP E O   1 
ATOM   8459  C CB  . ASP E  1 94  ? 17.808  57.825 84.890  1.00 43.77  ? 94   ASP E CB  1 
ATOM   8460  C CG  . ASP E  1 94  ? 18.562  59.124 85.097  1.00 44.76  ? 94   ASP E CG  1 
ATOM   8461  O OD1 . ASP E  1 94  ? 18.634  59.934 84.146  1.00 44.93  ? 94   ASP E OD1 1 
ATOM   8462  O OD2 . ASP E  1 94  ? 19.095  59.328 86.208  1.00 45.53  ? 94   ASP E OD2 1 
ATOM   8463  N N   . PHE E  1 95  ? 15.780  56.222 83.192  1.00 42.48  ? 95   PHE E N   1 
ATOM   8464  C CA  . PHE E  1 95  ? 15.361  54.885 82.819  1.00 41.76  ? 95   PHE E CA  1 
ATOM   8465  C C   . PHE E  1 95  ? 16.629  54.164 82.369  1.00 40.48  ? 95   PHE E C   1 
ATOM   8466  O O   . PHE E  1 95  ? 17.282  54.574 81.404  1.00 39.81  ? 95   PHE E O   1 
ATOM   8467  C CB  . PHE E  1 95  ? 14.325  54.955 81.697  1.00 41.84  ? 95   PHE E CB  1 
ATOM   8468  C CG  . PHE E  1 95  ? 13.424  53.755 81.620  1.00 41.98  ? 95   PHE E CG  1 
ATOM   8469  C CD1 . PHE E  1 95  ? 13.937  52.493 81.348  1.00 41.09  ? 95   PHE E CD1 1 
ATOM   8470  C CD2 . PHE E  1 95  ? 12.059  53.889 81.814  1.00 43.29  ? 95   PHE E CD2 1 
ATOM   8471  C CE1 . PHE E  1 95  ? 13.103  51.391 81.274  1.00 41.52  ? 95   PHE E CE1 1 
ATOM   8472  C CE2 . PHE E  1 95  ? 11.222  52.791 81.740  1.00 43.72  ? 95   PHE E CE2 1 
ATOM   8473  C CZ  . PHE E  1 95  ? 11.744  51.539 81.471  1.00 42.84  ? 95   PHE E CZ  1 
ATOM   8474  N N   . ASN E  1 96  ? 16.984  53.106 83.089  1.00 40.31  ? 96   ASN E N   1 
ATOM   8475  C CA  . ASN E  1 96  ? 18.237  52.407 82.856  1.00 39.48  ? 96   ASN E CA  1 
ATOM   8476  C C   . ASN E  1 96  ? 18.166  51.526 81.614  1.00 38.63  ? 96   ASN E C   1 
ATOM   8477  O O   . ASN E  1 96  ? 17.211  50.763 81.448  1.00 38.83  ? 96   ASN E O   1 
ATOM   8478  C CB  . ASN E  1 96  ? 18.597  51.560 84.076  1.00 39.88  ? 96   ASN E CB  1 
ATOM   8479  C CG  . ASN E  1 96  ? 20.057  51.161 84.091  1.00 39.51  ? 96   ASN E CG  1 
ATOM   8480  O OD1 . ASN E  1 96  ? 20.942  52.013 84.232  1.00 39.62  ? 96   ASN E OD1 1 
ATOM   8481  N ND2 . ASN E  1 96  ? 20.322  49.864 83.946  1.00 39.32  ? 96   ASN E ND2 1 
ATOM   8482  N N   . ASP E  1 97  ? 19.189  51.630 80.762  1.00 37.84  ? 97   ASP E N   1 
ATOM   8483  C CA  . ASP E  1 97  ? 19.244  50.929 79.471  1.00 37.05  ? 97   ASP E CA  1 
ATOM   8484  C C   . ASP E  1 97  ? 17.939  51.089 78.691  1.00 37.00  ? 97   ASP E C   1 
ATOM   8485  O O   . ASP E  1 97  ? 17.370  50.116 78.188  1.00 36.96  ? 97   ASP E O   1 
ATOM   8486  C CB  . ASP E  1 97  ? 19.594  49.446 79.667  1.00 37.10  ? 97   ASP E CB  1 
ATOM   8487  C CG  . ASP E  1 97  ? 21.057  49.226 80.027  1.00 37.10  ? 97   ASP E CG  1 
ATOM   8488  O OD1 . ASP E  1 97  ? 21.887  50.127 79.791  1.00 36.92  ? 97   ASP E OD1 1 
ATOM   8489  O OD2 . ASP E  1 97  ? 21.380  48.137 80.543  1.00 37.52  ? 97   ASP E OD2 1 
ATOM   8490  N N   . TYR E  1 98  ? 17.481  52.334 78.604  1.00 37.21  ? 98   TYR E N   1 
ATOM   8491  C CA  . TYR E  1 98  ? 16.219  52.679 77.954  1.00 37.50  ? 98   TYR E CA  1 
ATOM   8492  C C   . TYR E  1 98  ? 16.276  52.422 76.446  1.00 36.67  ? 98   TYR E C   1 
ATOM   8493  O O   . TYR E  1 98  ? 15.313  51.932 75.852  1.00 36.85  ? 98   TYR E O   1 
ATOM   8494  C CB  . TYR E  1 98  ? 15.918  54.153 78.234  1.00 38.21  ? 98   TYR E CB  1 
ATOM   8495  C CG  . TYR E  1 98  ? 14.596  54.687 77.719  1.00 38.97  ? 98   TYR E CG  1 
ATOM   8496  C CD1 . TYR E  1 98  ? 13.409  53.972 77.880  1.00 39.67  ? 98   TYR E CD1 1 
ATOM   8497  C CD2 . TYR E  1 98  ? 14.528  55.940 77.106  1.00 39.28  ? 98   TYR E CD2 1 
ATOM   8498  C CE1 . TYR E  1 98  ? 12.201  54.478 77.418  1.00 40.64  ? 98   TYR E CE1 1 
ATOM   8499  C CE2 . TYR E  1 98  ? 13.327  56.453 76.644  1.00 40.21  ? 98   TYR E CE2 1 
ATOM   8500  C CZ  . TYR E  1 98  ? 12.167  55.721 76.802  1.00 40.90  ? 98   TYR E CZ  1 
ATOM   8501  O OH  . TYR E  1 98  ? 10.980  56.239 76.341  1.00 42.10  ? 98   TYR E OH  1 
ATOM   8502  N N   . GLU E  1 99  ? 17.422  52.739 75.846  1.00 35.86  ? 99   GLU E N   1 
ATOM   8503  C CA  . GLU E  1 99  ? 17.619  52.597 74.408  1.00 35.07  ? 99   GLU E CA  1 
ATOM   8504  C C   . GLU E  1 99  ? 17.727  51.125 74.009  1.00 34.67  ? 99   GLU E C   1 
ATOM   8505  O O   . GLU E  1 99  ? 17.226  50.720 72.960  1.00 34.46  ? 99   GLU E O   1 
ATOM   8506  C CB  . GLU E  1 99  ? 18.870  53.356 73.957  1.00 34.58  ? 99   GLU E CB  1 
ATOM   8507  C CG  . GLU E  1 99  ? 18.744  54.875 74.007  1.00 35.12  ? 99   GLU E CG  1 
ATOM   8508  C CD  . GLU E  1 99  ? 18.805  55.445 75.414  1.00 36.04  ? 99   GLU E CD  1 
ATOM   8509  O OE1 . GLU E  1 99  ? 19.561  54.909 76.259  1.00 36.04  ? 99   GLU E OE1 1 
ATOM   8510  O OE2 . GLU E  1 99  ? 18.100  56.440 75.674  1.00 36.89  ? 99   GLU E OE2 1 
ATOM   8511  N N   . GLU E  1 100 ? 18.381  50.331 74.851  1.00 34.76  ? 100  GLU E N   1 
ATOM   8512  C CA  . GLU E  1 100 ? 18.449  48.885 74.650  1.00 34.77  ? 100  GLU E CA  1 
ATOM   8513  C C   . GLU E  1 100 ? 17.070  48.233 74.778  1.00 35.47  ? 100  GLU E C   1 
ATOM   8514  O O   . GLU E  1 100 ? 16.776  47.260 74.087  1.00 35.63  ? 100  GLU E O   1 
ATOM   8515  C CB  . GLU E  1 100 ? 19.429  48.250 75.640  1.00 35.04  ? 100  GLU E CB  1 
ATOM   8516  C CG  . GLU E  1 100 ? 20.887  48.468 75.286  1.00 34.58  ? 100  GLU E CG  1 
ATOM   8517  C CD  . GLU E  1 100 ? 21.317  47.669 74.067  1.00 34.24  ? 100  GLU E CD  1 
ATOM   8518  O OE1 . GLU E  1 100 ? 21.000  46.464 73.997  1.00 34.70  ? 100  GLU E OE1 1 
ATOM   8519  O OE2 . GLU E  1 100 ? 21.975  48.244 73.175  1.00 33.69  ? 100  GLU E OE2 1 
ATOM   8520  N N   . LEU E  1 101 ? 16.230  48.770 75.660  1.00 36.10  ? 101  LEU E N   1 
ATOM   8521  C CA  . LEU E  1 101 ? 14.860  48.275 75.808  1.00 37.07  ? 101  LEU E CA  1 
ATOM   8522  C C   . LEU E  1 101 ? 14.021  48.664 74.597  1.00 37.03  ? 101  LEU E C   1 
ATOM   8523  O O   . LEU E  1 101 ? 13.286  47.840 74.055  1.00 37.58  ? 101  LEU E O   1 
ATOM   8524  C CB  . LEU E  1 101 ? 14.211  48.818 77.086  1.00 37.96  ? 101  LEU E CB  1 
ATOM   8525  C CG  . LEU E  1 101 ? 12.797  48.318 77.404  1.00 39.31  ? 101  LEU E CG  1 
ATOM   8526  C CD1 . LEU E  1 101 ? 12.711  46.800 77.337  1.00 39.80  ? 101  LEU E CD1 1 
ATOM   8527  C CD2 . LEU E  1 101 ? 12.368  48.815 78.774  1.00 40.21  ? 101  LEU E CD2 1 
ATOM   8528  N N   . LYS E  1 102 ? 14.141  49.923 74.184  1.00 36.55  ? 102  LYS E N   1 
ATOM   8529  C CA  . LYS E  1 102 ? 13.496  50.406 72.964  1.00 36.49  ? 102  LYS E CA  1 
ATOM   8530  C C   . LYS E  1 102 ? 13.906  49.587 71.742  1.00 35.74  ? 102  LYS E C   1 
ATOM   8531  O O   . LYS E  1 102 ? 13.098  49.344 70.848  1.00 36.06  ? 102  LYS E O   1 
ATOM   8532  C CB  . LYS E  1 102 ? 13.832  51.878 72.727  1.00 36.15  ? 102  LYS E CB  1 
ATOM   8533  C CG  . LYS E  1 102 ? 12.855  52.851 73.360  1.00 37.37  ? 102  LYS E CG  1 
ATOM   8534  C CD  . LYS E  1 102 ? 13.400  54.270 73.298  1.00 37.25  ? 102  LYS E CD  1 
ATOM   8535  C CE  . LYS E  1 102 ? 12.324  55.280 72.933  1.00 38.39  ? 102  LYS E CE  1 
ATOM   8536  N NZ  . LYS E  1 102 ? 12.934  56.568 72.505  1.00 38.27  ? 102  LYS E NZ  1 
ATOM   8537  N N   . HIS E  1 103 ? 15.167  49.171 71.702  1.00 34.90  ? 103  HIS E N   1 
ATOM   8538  C CA  . HIS E  1 103 ? 15.639  48.318 70.625  1.00 34.38  ? 103  HIS E CA  1 
ATOM   8539  C C   . HIS E  1 103 ? 14.947  46.959 70.674  1.00 35.34  ? 103  HIS E C   1 
ATOM   8540  O O   . HIS E  1 103 ? 14.634  46.383 69.639  1.00 35.44  ? 103  HIS E O   1 
ATOM   8541  C CB  . HIS E  1 103 ? 17.158  48.138 70.690  1.00 33.62  ? 103  HIS E CB  1 
ATOM   8542  C CG  . HIS E  1 103 ? 17.698  47.239 69.623  1.00 33.26  ? 103  HIS E CG  1 
ATOM   8543  N ND1 . HIS E  1 103 ? 17.918  47.666 68.332  1.00 32.53  ? 103  HIS E ND1 1 
ATOM   8544  C CD2 . HIS E  1 103 ? 18.037  45.930 69.649  1.00 33.71  ? 103  HIS E CD2 1 
ATOM   8545  C CE1 . HIS E  1 103 ? 18.382  46.662 67.612  1.00 32.51  ? 103  HIS E CE1 1 
ATOM   8546  N NE2 . HIS E  1 103 ? 18.463  45.597 68.388  1.00 33.28  ? 103  HIS E NE2 1 
ATOM   8547  N N   . LEU E  1 104 ? 14.717  46.457 71.881  1.00 36.21  ? 104  LEU E N   1 
ATOM   8548  C CA  . LEU E  1 104 ? 14.031  45.180 72.079  1.00 37.50  ? 104  LEU E CA  1 
ATOM   8549  C C   . LEU E  1 104 ? 12.611  45.221 71.501  1.00 38.47  ? 104  LEU E C   1 
ATOM   8550  O O   . LEU E  1 104 ? 12.127  44.226 70.964  1.00 39.34  ? 104  LEU E O   1 
ATOM   8551  C CB  . LEU E  1 104 ? 13.985  44.827 73.575  1.00 38.31  ? 104  LEU E CB  1 
ATOM   8552  C CG  . LEU E  1 104 ? 14.449  43.432 73.996  1.00 39.05  ? 104  LEU E CG  1 
ATOM   8553  C CD1 . LEU E  1 104 ? 15.898  43.190 73.600  1.00 38.16  ? 104  LEU E CD1 1 
ATOM   8554  C CD2 . LEU E  1 104 ? 14.287  43.280 75.499  1.00 39.83  ? 104  LEU E CD2 1 
ATOM   8555  N N   . LEU E  1 105 ? 11.968  46.383 71.609  1.00 44.97  ? 105  LEU E N   1 
ATOM   8556  C CA  . LEU E  1 105 ? 10.620  46.605 71.076  1.00 45.76  ? 105  LEU E CA  1 
ATOM   8557  C C   . LEU E  1 105 ? 10.517  46.507 69.560  1.00 46.22  ? 105  LEU E C   1 
ATOM   8558  O O   . LEU E  1 105 ? 9.427   46.277 69.034  1.00 47.15  ? 105  LEU E O   1 
ATOM   8559  C CB  . LEU E  1 105 ? 10.099  47.982 71.490  1.00 45.53  ? 105  LEU E CB  1 
ATOM   8560  C CG  . LEU E  1 105 ? 9.505   48.127 72.881  1.00 45.75  ? 105  LEU E CG  1 
ATOM   8561  C CD1 . LEU E  1 105 ? 9.210   49.595 73.138  1.00 45.59  ? 105  LEU E CD1 1 
ATOM   8562  C CD2 . LEU E  1 105 ? 8.242   47.287 73.013  1.00 46.90  ? 105  LEU E CD2 1 
ATOM   8563  N N   . SER E  1 106 ? 11.627  46.711 68.858  1.00 45.78  ? 106  SER E N   1 
ATOM   8564  C CA  . SER E  1 106 ? 11.645  46.543 67.406  1.00 46.38  ? 106  SER E CA  1 
ATOM   8565  C C   . SER E  1 106 ? 11.423  45.077 67.001  1.00 47.39  ? 106  SER E C   1 
ATOM   8566  O O   . SER E  1 106 ? 11.047  44.802 65.863  1.00 48.25  ? 106  SER E O   1 
ATOM   8567  C CB  . SER E  1 106 ? 12.954  47.081 66.804  1.00 45.82  ? 106  SER E CB  1 
ATOM   8568  O OG  . SER E  1 106 ? 14.071  46.269 67.136  1.00 45.60  ? 106  SER E OG  1 
ATOM   8569  N N   . ARG E  1 107 ? 11.666  44.149 67.928  1.00 47.46  ? 107  ARG E N   1 
ATOM   8570  C CA  . ARG E  1 107 ? 11.387  42.719 67.717  1.00 48.61  ? 107  ARG E CA  1 
ATOM   8571  C C   . ARG E  1 107 ? 10.047  42.265 68.316  1.00 49.45  ? 107  ARG E C   1 
ATOM   8572  O O   . ARG E  1 107 ? 9.762   41.067 68.330  1.00 50.48  ? 107  ARG E O   1 
ATOM   8573  C CB  . ARG E  1 107 ? 12.507  41.849 68.317  1.00 48.43  ? 107  ARG E CB  1 
ATOM   8574  C CG  . ARG E  1 107 ? 13.723  41.623 67.422  1.00 48.48  ? 107  ARG E CG  1 
ATOM   8575  C CD  . ARG E  1 107 ? 14.355  40.253 67.689  1.00 49.16  ? 107  ARG E CD  1 
ATOM   8576  N NE  . ARG E  1 107 ? 15.817  40.249 67.545  1.00 48.80  ? 107  ARG E NE  1 
ATOM   8577  C CZ  . ARG E  1 107 ? 16.512  39.695 66.545  1.00 49.59  ? 107  ARG E CZ  1 
ATOM   8578  N NH1 . ARG E  1 107 ? 15.912  39.066 65.533  1.00 50.85  ? 107  ARG E NH1 1 
ATOM   8579  N NH2 . ARG E  1 107 ? 17.841  39.774 66.559  1.00 49.28  ? 107  ARG E NH2 1 
ATOM   8580  N N   . ILE E  1 108 ? 9.234   43.203 68.802  1.00 49.20  ? 108  ILE E N   1 
ATOM   8581  C CA  . ILE E  1 108 ? 8.017   42.860 69.543  1.00 50.06  ? 108  ILE E CA  1 
ATOM   8582  C C   . ILE E  1 108 ? 6.760   43.478 68.919  1.00 50.86  ? 108  ILE E C   1 
ATOM   8583  O O   . ILE E  1 108 ? 6.713   44.679 68.644  1.00 50.27  ? 108  ILE E O   1 
ATOM   8584  C CB  . ILE E  1 108 ? 8.131   43.276 71.031  1.00 49.36  ? 108  ILE E CB  1 
ATOM   8585  C CG1 . ILE E  1 108 ? 9.267   42.496 71.705  1.00 48.87  ? 108  ILE E CG1 1 
ATOM   8586  C CG2 . ILE E  1 108 ? 6.822   43.014 71.769  1.00 50.45  ? 108  ILE E CG2 1 
ATOM   8587  C CD1 . ILE E  1 108 ? 9.632   42.988 73.090  1.00 48.14  ? 108  ILE E CD1 1 
ATOM   8588  N N   . ASN E  1 109 ? 5.744   42.638 68.721  1.00 52.36  ? 109  ASN E N   1 
ATOM   8589  C CA  . ASN E  1 109 ? 4.460   43.057 68.155  1.00 53.46  ? 109  ASN E CA  1 
ATOM   8590  C C   . ASN E  1 109 ? 3.314   43.114 69.165  1.00 54.30  ? 109  ASN E C   1 
ATOM   8591  O O   . ASN E  1 109 ? 2.343   43.842 68.946  1.00 54.91  ? 109  ASN E O   1 
ATOM   8592  C CB  . ASN E  1 109 ? 4.060   42.134 66.997  1.00 54.92  ? 109  ASN E CB  1 
ATOM   8593  C CG  . ASN E  1 109 ? 4.521   42.654 65.654  1.00 54.66  ? 109  ASN E CG  1 
ATOM   8594  O OD1 . ASN E  1 109 ? 3.713   43.079 64.832  1.00 55.56  ? 109  ASN E OD1 1 
ATOM   8595  N ND2 . ASN E  1 109 ? 5.822   42.636 65.428  1.00 53.60  ? 109  ASN E ND2 1 
ATOM   8596  N N   . HIS E  1 110 ? 3.404   42.343 70.250  1.00 54.49  ? 110  HIS E N   1 
ATOM   8597  C CA  . HIS E  1 110 ? 2.355   42.373 71.271  1.00 55.46  ? 110  HIS E CA  1 
ATOM   8598  C C   . HIS E  1 110 ? 2.825   42.054 72.688  1.00 55.00  ? 110  HIS E C   1 
ATOM   8599  O O   . HIS E  1 110 ? 3.551   41.085 72.925  1.00 54.84  ? 110  HIS E O   1 
ATOM   8600  C CB  . HIS E  1 110 ? 1.211   41.427 70.893  1.00 57.55  ? 110  HIS E CB  1 
ATOM   8601  C CG  . HIS E  1 110 ? -0.064  41.701 71.631  1.00 58.85  ? 110  HIS E CG  1 
ATOM   8602  N ND1 . HIS E  1 110 ? -0.948  40.705 71.989  1.00 60.76  ? 110  HIS E ND1 1 
ATOM   8603  C CD2 . HIS E  1 110 ? -0.595  42.858 72.093  1.00 58.70  ? 110  HIS E CD2 1 
ATOM   8604  C CE1 . HIS E  1 110 ? -1.973  41.239 72.629  1.00 61.73  ? 110  HIS E CE1 1 
ATOM   8605  N NE2 . HIS E  1 110 ? -1.784  42.544 72.705  1.00 60.51  ? 110  HIS E NE2 1 
ATOM   8606  N N   . PHE E  1 111 ? 2.379   42.891 73.620  1.00 54.94  ? 111  PHE E N   1 
ATOM   8607  C CA  . PHE E  1 111 ? 2.538   42.649 75.046  1.00 54.97  ? 111  PHE E CA  1 
ATOM   8608  C C   . PHE E  1 111 ? 1.189   42.252 75.626  1.00 56.93  ? 111  PHE E C   1 
ATOM   8609  O O   . PHE E  1 111 ? 0.155   42.769 75.194  1.00 57.88  ? 111  PHE E O   1 
ATOM   8610  C CB  . PHE E  1 111 ? 3.016   43.914 75.773  1.00 53.73  ? 111  PHE E CB  1 
ATOM   8611  C CG  . PHE E  1 111 ? 4.507   44.132 75.744  1.00 51.98  ? 111  PHE E CG  1 
ATOM   8612  C CD1 . PHE E  1 111 ? 5.397   43.085 75.963  1.00 51.67  ? 111  PHE E CD1 1 
ATOM   8613  C CD2 . PHE E  1 111 ? 5.019   45.406 75.549  1.00 50.81  ? 111  PHE E CD2 1 
ATOM   8614  C CE1 . PHE E  1 111 ? 6.763   43.303 75.954  1.00 50.25  ? 111  PHE E CE1 1 
ATOM   8615  C CE2 . PHE E  1 111 ? 6.384   45.627 75.543  1.00 49.43  ? 111  PHE E CE2 1 
ATOM   8616  C CZ  . PHE E  1 111 ? 7.257   44.575 75.747  1.00 49.15  ? 111  PHE E CZ  1 
ATOM   8617  N N   . GLU E  1 112 ? 1.203   41.337 76.595  1.00 57.69  ? 112  GLU E N   1 
ATOM   8618  C CA  . GLU E  1 112 ? 0.037   41.081 77.443  1.00 59.56  ? 112  GLU E CA  1 
ATOM   8619  C C   . GLU E  1 112 ? 0.419   41.346 78.894  1.00 59.22  ? 112  GLU E C   1 
ATOM   8620  O O   . GLU E  1 112 ? 1.369   40.767 79.407  1.00 58.52  ? 112  GLU E O   1 
ATOM   8621  C CB  . GLU E  1 112 ? -0.469  39.646 77.289  1.00 61.32  ? 112  GLU E CB  1 
ATOM   8622  C CG  . GLU E  1 112 ? -1.879  39.452 77.835  1.00 63.61  ? 112  GLU E CG  1 
ATOM   8623  C CD  . GLU E  1 112 ? -2.277  37.993 77.950  1.00 65.50  ? 112  GLU E CD  1 
ATOM   8624  O OE1 . GLU E  1 112 ? -1.937  37.211 77.031  1.00 65.56  ? 112  GLU E OE1 1 
ATOM   8625  O OE2 . GLU E  1 112 ? -2.932  37.632 78.958  1.00 67.06  ? 112  GLU E OE2 1 
ATOM   8626  N N   . LYS E  1 113 ? -0.324  42.224 79.554  1.00 59.89  ? 113  LYS E N   1 
ATOM   8627  C CA  . LYS E  1 113 ? -0.010  42.605 80.927  1.00 59.77  ? 113  LYS E CA  1 
ATOM   8628  C C   . LYS E  1 113 ? -0.537  41.570 81.923  1.00 61.57  ? 113  LYS E C   1 
ATOM   8629  O O   . LYS E  1 113 ? -1.653  41.069 81.770  1.00 63.44  ? 113  LYS E O   1 
ATOM   8630  C CB  . LYS E  1 113 ? -0.611  43.974 81.221  1.00 60.00  ? 113  LYS E CB  1 
ATOM   8631  C CG  . LYS E  1 113 ? -0.090  44.630 82.486  1.00 59.59  ? 113  LYS E CG  1 
ATOM   8632  C CD  . LYS E  1 113 ? 0.208   46.105 82.259  1.00 58.50  ? 113  LYS E CD  1 
ATOM   8633  C CE  . LYS E  1 113 ? -1.032  46.920 81.917  1.00 59.76  ? 113  LYS E CE  1 
ATOM   8634  N NZ  . LYS E  1 113 ? -0.674  48.338 81.630  1.00 58.72  ? 113  LYS E NZ  1 
ATOM   8635  N N   . ILE E  1 114 ? 0.273   41.245 82.930  1.00 61.14  ? 114  ILE E N   1 
ATOM   8636  C CA  . ILE E  1 114 ? -0.156  40.359 84.016  1.00 62.90  ? 114  ILE E CA  1 
ATOM   8637  C C   . ILE E  1 114 ? 0.363   40.835 85.370  1.00 62.68  ? 114  ILE E C   1 
ATOM   8638  O O   . ILE E  1 114 ? 1.414   41.479 85.455  1.00 60.94  ? 114  ILE E O   1 
ATOM   8639  C CB  . ILE E  1 114 ? 0.299   38.896 83.809  1.00 63.20  ? 114  ILE E CB  1 
ATOM   8640  C CG1 . ILE E  1 114 ? 1.815   38.815 83.579  1.00 61.10  ? 114  ILE E CG1 1 
ATOM   8641  C CG2 . ILE E  1 114 ? -0.466  38.253 82.659  1.00 64.23  ? 114  ILE E CG2 1 
ATOM   8642  C CD1 . ILE E  1 114 ? 2.409   37.483 83.983  1.00 61.59  ? 114  ILE E CD1 1 
ATOM   8643  N N   . GLN E  1 115 ? -0.384  40.504 86.419  1.00 64.65  ? 115  GLN E N   1 
ATOM   8644  C CA  . GLN E  1 115 ? -0.011  40.845 87.786  1.00 64.90  ? 115  GLN E CA  1 
ATOM   8645  C C   . GLN E  1 115 ? 0.897   39.758 88.359  1.00 64.76  ? 115  GLN E C   1 
ATOM   8646  O O   . GLN E  1 115 ? 0.529   38.582 88.372  1.00 66.09  ? 115  GLN E O   1 
ATOM   8647  C CB  . GLN E  1 115 ? -1.269  40.997 88.647  1.00 67.33  ? 115  GLN E CB  1 
ATOM   8648  C CG  . GLN E  1 115 ? -1.008  41.210 90.130  1.00 68.07  ? 115  GLN E CG  1 
ATOM   8649  C CD  . GLN E  1 115 ? -2.285  41.466 90.911  1.00 70.63  ? 115  GLN E CD  1 
ATOM   8650  O OE1 . GLN E  1 115 ? -2.805  42.582 90.923  1.00 70.89  ? 115  GLN E OE1 1 
ATOM   8651  N NE2 . GLN E  1 115 ? -2.794  40.434 91.573  1.00 72.67  ? 115  GLN E NE2 1 
ATOM   8652  N N   . ILE E  1 116 ? 2.076   40.160 88.829  1.00 63.31  ? 116  ILE E N   1 
ATOM   8653  C CA  . ILE E  1 116 ? 3.017   39.236 89.483  1.00 63.23  ? 116  ILE E CA  1 
ATOM   8654  C C   . ILE E  1 116 ? 3.038   39.438 91.006  1.00 64.39  ? 116  ILE E C   1 
ATOM   8655  O O   . ILE E  1 116 ? 3.041   38.466 91.764  1.00 65.71  ? 116  ILE E O   1 
ATOM   8656  C CB  . ILE E  1 116 ? 4.454   39.320 88.897  1.00 60.95  ? 116  ILE E CB  1 
ATOM   8657  C CG1 . ILE E  1 116 ? 4.866   40.767 88.601  1.00 59.37  ? 116  ILE E CG1 1 
ATOM   8658  C CG2 . ILE E  1 116 ? 4.560   38.488 87.624  1.00 60.47  ? 116  ILE E CG2 1 
ATOM   8659  C CD1 . ILE E  1 116 ? 6.358   40.995 88.673  1.00 57.67  ? 116  ILE E CD1 1 
ATOM   8660  N N   . ILE E  1 117 ? 3.051   40.696 91.445  1.00 64.09  ? 117  ILE E N   1 
ATOM   8661  C CA  . ILE E  1 117 ? 2.902   41.043 92.861  1.00 65.50  ? 117  ILE E CA  1 
ATOM   8662  C C   . ILE E  1 117 ? 1.580   41.800 93.025  1.00 67.08  ? 117  ILE E C   1 
ATOM   8663  O O   . ILE E  1 117 ? 1.419   42.880 92.451  1.00 66.26  ? 117  ILE E O   1 
ATOM   8664  C CB  . ILE E  1 117 ? 4.089   41.909 93.363  1.00 64.11  ? 117  ILE E CB  1 
ATOM   8665  C CG1 . ILE E  1 117 ? 5.235   41.025 93.879  1.00 63.68  ? 117  ILE E CG1 1 
ATOM   8666  C CG2 . ILE E  1 117 ? 3.666   42.890 94.461  1.00 65.41  ? 117  ILE E CG2 1 
ATOM   8667  C CD1 . ILE E  1 117 ? 6.117   40.455 92.791  1.00 61.86  ? 117  ILE E CD1 1 
ATOM   8668  N N   . PRO E  1 118 ? 0.619   41.230 93.780  1.00 69.53  ? 118  PRO E N   1 
ATOM   8669  C CA  . PRO E  1 118 ? -0.592  42.008 94.068  1.00 71.29  ? 118  PRO E CA  1 
ATOM   8670  C C   . PRO E  1 118 ? -0.330  43.153 95.053  1.00 71.56  ? 118  PRO E C   1 
ATOM   8671  O O   . PRO E  1 118 ? 0.470   43.007 95.980  1.00 71.55  ? 118  PRO E O   1 
ATOM   8672  C CB  . PRO E  1 118 ? -1.563  40.971 94.662  1.00 73.97  ? 118  PRO E CB  1 
ATOM   8673  C CG  . PRO E  1 118 ? -0.989  39.632 94.330  1.00 73.44  ? 118  PRO E CG  1 
ATOM   8674  C CD  . PRO E  1 118 ? 0.492   39.824 94.206  1.00 70.94  ? 118  PRO E CD  1 
ATOM   8675  N N   . LYS E  1 119 ? -1.001  44.281 94.840  1.00 71.96  ? 119  LYS E N   1 
ATOM   8676  C CA  . LYS E  1 119 ? -0.823  45.468 95.677  1.00 72.41  ? 119  LYS E CA  1 
ATOM   8677  C C   . LYS E  1 119 ? -1.345  45.224 97.096  1.00 75.14  ? 119  LYS E C   1 
ATOM   8678  O O   . LYS E  1 119 ? -0.757  45.691 98.075  1.00 75.47  ? 119  LYS E O   1 
ATOM   8679  C CB  . LYS E  1 119 ? -1.542  46.664 95.049  1.00 72.47  ? 119  LYS E CB  1 
ATOM   8680  C CG  . LYS E  1 119 ? -1.063  48.019 95.538  1.00 72.16  ? 119  LYS E CG  1 
ATOM   8681  C CD  . LYS E  1 119 ? -1.713  49.131 94.732  1.00 72.06  ? 119  LYS E CD  1 
ATOM   8682  C CE  . LYS E  1 119 ? -1.584  50.481 95.416  1.00 72.73  ? 119  LYS E CE  1 
ATOM   8683  N NZ  . LYS E  1 119 ? -2.492  51.490 94.802  1.00 73.42  ? 119  LYS E NZ  1 
ATOM   8684  N N   . SER E  1 120 ? -2.452  44.491 97.191  1.00 77.28  ? 120  SER E N   1 
ATOM   8685  C CA  . SER E  1 120 ? -3.024  44.086 98.475  1.00 80.13  ? 120  SER E CA  1 
ATOM   8686  C C   . SER E  1 120 ? -2.066  43.213 99.283  1.00 79.98  ? 120  SER E C   1 
ATOM   8687  O O   . SER E  1 120 ? -2.086  43.236 100.510 1.00 81.81  ? 120  SER E O   1 
ATOM   8688  C CB  . SER E  1 120 ? -4.326  43.317 98.245  1.00 82.32  ? 120  SER E CB  1 
ATOM   8689  O OG  . SER E  1 120 ? -4.096  42.162 97.451  1.00 81.28  ? 120  SER E OG  1 
ATOM   8690  N N   . SER E  1 121 ? -1.229  42.446 98.587  1.00 77.98  ? 121  SER E N   1 
ATOM   8691  C CA  . SER E  1 121 ? -0.315  41.496 99.232  1.00 77.85  ? 121  SER E CA  1 
ATOM   8692  C C   . SER E  1 121 ? 0.696   42.098 100.206 1.00 77.46  ? 121  SER E C   1 
ATOM   8693  O O   . SER E  1 121 ? 1.284   41.370 101.005 1.00 78.01  ? 121  SER E O   1 
ATOM   8694  C CB  . SER E  1 121 ? 0.479   40.732 98.181  1.00 75.60  ? 121  SER E CB  1 
ATOM   8695  O OG  . SER E  1 121 ? -0.367  40.022 97.306  1.00 76.13  ? 121  SER E OG  1 
ATOM   8696  N N   . TRP E  1 122 ? 0.931   43.403 100.115 1.00 76.57  ? 122  TRP E N   1 
ATOM   8697  C CA  . TRP E  1 122 ? 1.878   44.074 100.999 1.00 76.35  ? 122  TRP E CA  1 
ATOM   8698  C C   . TRP E  1 122 ? 1.236   44.320 102.357 1.00 79.33  ? 122  TRP E C   1 
ATOM   8699  O O   . TRP E  1 122 ? 0.852   45.443 102.679 1.00 80.23  ? 122  TRP E O   1 
ATOM   8700  C CB  . TRP E  1 122 ? 2.349   45.388 100.375 1.00 74.51  ? 122  TRP E CB  1 
ATOM   8701  C CG  . TRP E  1 122 ? 3.093   45.183 99.100  1.00 71.72  ? 122  TRP E CG  1 
ATOM   8702  C CD1 . TRP E  1 122 ? 2.655   45.461 97.837  1.00 70.53  ? 122  TRP E CD1 1 
ATOM   8703  C CD2 . TRP E  1 122 ? 4.406   44.633 98.958  1.00 69.98  ? 122  TRP E CD2 1 
ATOM   8704  N NE1 . TRP E  1 122 ? 3.622   45.130 96.916  1.00 68.15  ? 122  TRP E NE1 1 
ATOM   8705  C CE2 . TRP E  1 122 ? 4.707   44.616 97.577  1.00 67.78  ? 122  TRP E CE2 1 
ATOM   8706  C CE3 . TRP E  1 122 ? 5.362   44.156 99.864  1.00 70.19  ? 122  TRP E CE3 1 
ATOM   8707  C CZ2 . TRP E  1 122 ? 5.926   44.143 97.081  1.00 65.84  ? 122  TRP E CZ2 1 
ATOM   8708  C CZ3 . TRP E  1 122 ? 6.570   43.685 99.372  1.00 68.24  ? 122  TRP E CZ3 1 
ATOM   8709  C CH2 . TRP E  1 122 ? 6.842   43.681 97.991  1.00 66.11  ? 122  TRP E CH2 1 
ATOM   8710  N N   . SER E  1 123 ? 1.125   43.251 103.145 1.00 81.03  ? 123  SER E N   1 
ATOM   8711  C CA  . SER E  1 123 ? 0.437   43.283 104.437 1.00 84.20  ? 123  SER E CA  1 
ATOM   8712  C C   . SER E  1 123 ? 1.301   43.884 105.544 1.00 84.69  ? 123  SER E C   1 
ATOM   8713  O O   . SER E  1 123 ? 0.775   44.431 106.511 1.00 87.12  ? 123  SER E O   1 
ATOM   8714  C CB  . SER E  1 123 ? -0.001  41.871 104.840 1.00 85.97  ? 123  SER E CB  1 
ATOM   8715  O OG  . SER E  1 123 ? 1.114   41.002 104.951 1.00 84.74  ? 123  SER E OG  1 
ATOM   8716  N N   . SER E  1 124 ? 2.620   43.770 105.401 1.00 82.59  ? 124  SER E N   1 
ATOM   8717  C CA  . SER E  1 124 ? 3.571   44.280 106.391 1.00 82.95  ? 124  SER E CA  1 
ATOM   8718  C C   . SER E  1 124 ? 4.071   45.703 106.077 1.00 81.62  ? 124  SER E C   1 
ATOM   8719  O O   . SER E  1 124 ? 4.787   46.304 106.881 1.00 82.10  ? 124  SER E O   1 
ATOM   8720  C CB  . SER E  1 124 ? 4.757   43.315 106.492 1.00 81.73  ? 124  SER E CB  1 
ATOM   8721  O OG  . SER E  1 124 ? 5.676   43.726 107.485 1.00 82.29  ? 124  SER E OG  1 
ATOM   8722  N N   . HIS E  1 125 ? 3.697   46.233 104.912 1.00 80.11  ? 125  HIS E N   1 
ATOM   8723  C CA  . HIS E  1 125 ? 4.101   47.578 104.491 1.00 78.89  ? 125  HIS E CA  1 
ATOM   8724  C C   . HIS E  1 125 ? 2.891   48.389 104.044 1.00 79.84  ? 125  HIS E C   1 
ATOM   8725  O O   . HIS E  1 125 ? 1.820   47.835 103.795 1.00 80.88  ? 125  HIS E O   1 
ATOM   8726  C CB  . HIS E  1 125 ? 5.111   47.496 103.342 1.00 75.67  ? 125  HIS E CB  1 
ATOM   8727  C CG  . HIS E  1 125 ? 6.427   46.904 103.736 1.00 74.74  ? 125  HIS E CG  1 
ATOM   8728  N ND1 . HIS E  1 125 ? 6.642   45.544 103.797 1.00 74.64  ? 125  HIS E ND1 1 
ATOM   8729  C CD2 . HIS E  1 125 ? 7.596   47.486 104.092 1.00 74.03  ? 125  HIS E CD2 1 
ATOM   8730  C CE1 . HIS E  1 125 ? 7.886   45.314 104.176 1.00 73.91  ? 125  HIS E CE1 1 
ATOM   8731  N NE2 . HIS E  1 125 ? 8.488   46.476 104.358 1.00 73.53  ? 125  HIS E NE2 1 
ATOM   8732  N N   . GLU E  1 126 ? 3.072   49.704 103.947 1.00 79.67  ? 126  GLU E N   1 
ATOM   8733  C CA  . GLU E  1 126 ? 2.036   50.588 103.425 1.00 80.41  ? 126  GLU E CA  1 
ATOM   8734  C C   . GLU E  1 126 ? 2.269   50.784 101.929 1.00 77.76  ? 126  GLU E C   1 
ATOM   8735  O O   . GLU E  1 126 ? 3.377   51.129 101.511 1.00 75.77  ? 126  GLU E O   1 
ATOM   8736  C CB  . GLU E  1 126 ? 2.064   51.927 104.158 1.00 81.93  ? 126  GLU E CB  1 
ATOM   8737  C CG  . GLU E  1 126 ? 0.929   52.873 103.798 1.00 83.17  ? 126  GLU E CG  1 
ATOM   8738  C CD  . GLU E  1 126 ? -0.443  52.322 104.155 1.00 85.69  ? 126  GLU E CD  1 
ATOM   8739  O OE1 . GLU E  1 126 ? -0.703  52.072 105.355 1.00 88.19  ? 126  GLU E OE1 1 
ATOM   8740  O OE2 . GLU E  1 126 ? -1.267  52.153 103.228 1.00 85.31  ? 126  GLU E OE2 1 
ATOM   8741  N N   . ALA E  1 127 ? 1.228   50.554 101.129 1.00 77.92  ? 127  ALA E N   1 
ATOM   8742  C CA  . ALA E  1 127 ? 1.352   50.544 99.663  1.00 75.52  ? 127  ALA E CA  1 
ATOM   8743  C C   . ALA E  1 127 ? 0.474   51.568 98.933  1.00 75.85  ? 127  ALA E C   1 
ATOM   8744  O O   . ALA E  1 127 ? 0.694   51.828 97.747  1.00 73.89  ? 127  ALA E O   1 
ATOM   8745  C CB  . ALA E  1 127 ? 1.054   49.146 99.138  1.00 75.03  ? 127  ALA E CB  1 
ATOM   8746  N N   . SER E  1 128 ? -0.499  52.155 99.630  1.00 78.44  ? 128  SER E N   1 
ATOM   8747  C CA  . SER E  1 128 ? -1.503  53.017 98.995  1.00 79.19  ? 128  SER E CA  1 
ATOM   8748  C C   . SER E  1 128 ? -1.212  54.515 99.119  1.00 79.37  ? 128  SER E C   1 
ATOM   8749  O O   . SER E  1 128 ? -1.944  55.334 98.559  1.00 79.91  ? 128  SER E O   1 
ATOM   8750  C CB  . SER E  1 128 ? -2.889  52.712 99.572  1.00 82.21  ? 128  SER E CB  1 
ATOM   8751  O OG  . SER E  1 128 ? -3.354  51.456 99.111  1.00 82.05  ? 128  SER E OG  1 
ATOM   8752  N N   . LEU E  1 129 ? -0.153  54.871 99.842  1.00 79.08  ? 129  LEU E N   1 
ATOM   8753  C CA  . LEU E  1 129 ? 0.208   56.274 100.050 1.00 79.50  ? 129  LEU E CA  1 
ATOM   8754  C C   . LEU E  1 129 ? 1.442   56.677 99.241  1.00 76.77  ? 129  LEU E C   1 
ATOM   8755  O O   . LEU E  1 129 ? 1.944   57.791 99.384  1.00 77.00  ? 129  LEU E O   1 
ATOM   8756  C CB  . LEU E  1 129 ? 0.440   56.550 101.540 1.00 81.73  ? 129  LEU E CB  1 
ATOM   8757  C CG  . LEU E  1 129 ? -0.808  56.664 102.421 1.00 85.10  ? 129  LEU E CG  1 
ATOM   8758  C CD1 . LEU E  1 129 ? -1.419  55.305 102.717 1.00 85.92  ? 129  LEU E CD1 1 
ATOM   8759  C CD2 . LEU E  1 129 ? -0.453  57.367 103.720 1.00 87.26  ? 129  LEU E CD2 1 
ATOM   8760  N N   . GLY E  1 130 ? 1.914   55.780 98.379  1.00 74.49  ? 130  GLY E N   1 
ATOM   8761  C CA  . GLY E  1 130 ? 3.084   56.043 97.546  1.00 71.92  ? 130  GLY E CA  1 
ATOM   8762  C C   . GLY E  1 130 ? 2.766   56.804 96.269  1.00 70.85  ? 130  GLY E C   1 
ATOM   8763  O O   . GLY E  1 130 ? 2.878   56.260 95.163  1.00 68.95  ? 130  GLY E O   1 
ATOM   8764  N N   . VAL E  1 131 ? 2.383   58.071 96.428  1.00 72.18  ? 131  VAL E N   1 
ATOM   8765  C CA  . VAL E  1 131 ? 2.011   58.934 95.302  1.00 71.55  ? 131  VAL E CA  1 
ATOM   8766  C C   . VAL E  1 131 ? 2.785   60.254 95.345  1.00 71.49  ? 131  VAL E C   1 
ATOM   8767  O O   . VAL E  1 131 ? 3.543   60.509 96.280  1.00 72.17  ? 131  VAL E O   1 
ATOM   8768  C CB  . VAL E  1 131 ? 0.489   59.224 95.288  1.00 73.64  ? 131  VAL E CB  1 
ATOM   8769  C CG1 . VAL E  1 131 ? -0.303  57.926 95.376  1.00 74.15  ? 131  VAL E CG1 1 
ATOM   8770  C CG2 . VAL E  1 131 ? 0.095   60.174 96.415  1.00 76.33  ? 131  VAL E CG2 1 
ATOM   8771  N N   . SER E  1 132 ? 2.584   61.084 94.325  1.00 70.90  ? 132  SER E N   1 
ATOM   8772  C CA  . SER E  1 132 ? 3.255   62.379 94.227  1.00 70.91  ? 132  SER E CA  1 
ATOM   8773  C C   . SER E  1 132 ? 2.460   63.351 93.364  1.00 71.36  ? 132  SER E C   1 
ATOM   8774  O O   . SER E  1 132 ? 1.690   62.941 92.492  1.00 70.81  ? 132  SER E O   1 
ATOM   8775  C CB  . SER E  1 132 ? 4.657   62.205 93.640  1.00 68.57  ? 132  SER E CB  1 
ATOM   8776  O OG  . SER E  1 132 ? 5.212   63.451 93.250  1.00 68.54  ? 132  SER E OG  1 
ATOM   8777  N N   . SER E  1 133 ? 2.663   64.643 93.612  1.00 72.48  ? 133  SER E N   1 
ATOM   8778  C CA  . SER E  1 133 ? 2.023   65.702 92.833  1.00 72.98  ? 133  SER E CA  1 
ATOM   8779  C C   . SER E  1 133 ? 2.615   65.809 91.423  1.00 70.45  ? 133  SER E C   1 
ATOM   8780  O O   . SER E  1 133 ? 2.012   66.424 90.543  1.00 70.63  ? 133  SER E O   1 
ATOM   8781  C CB  . SER E  1 133 ? 2.154   67.045 93.556  1.00 75.09  ? 133  SER E CB  1 
ATOM   8782  O OG  . SER E  1 133 ? 3.515   67.410 93.703  1.00 74.15  ? 133  SER E OG  1 
ATOM   8783  N N   . ALA E  1 134 ? 3.794   65.217 91.218  1.00 68.21  ? 134  ALA E N   1 
ATOM   8784  C CA  . ALA E  1 134 ? 4.442   65.188 89.905  1.00 65.84  ? 134  ALA E CA  1 
ATOM   8785  C C   . ALA E  1 134 ? 3.698   64.299 88.904  1.00 64.61  ? 134  ALA E C   1 
ATOM   8786  O O   . ALA E  1 134 ? 3.708   64.580 87.708  1.00 63.57  ? 134  ALA E O   1 
ATOM   8787  C CB  . ALA E  1 134 ? 5.888   64.736 90.041  1.00 64.20  ? 134  ALA E CB  1 
ATOM   8788  N N   . CYS E  1 135 ? 3.060   63.236 89.396  1.00 64.84  ? 135  CYS E N   1 
ATOM   8789  C CA  . CYS E  1 135 ? 2.192   62.383 88.576  1.00 64.23  ? 135  CYS E CA  1 
ATOM   8790  C C   . CYS E  1 135 ? 0.721   62.544 88.993  1.00 66.42  ? 135  CYS E C   1 
ATOM   8791  O O   . CYS E  1 135 ? 0.205   61.737 89.766  1.00 67.34  ? 135  CYS E O   1 
ATOM   8792  C CB  . CYS E  1 135 ? 2.607   60.911 88.709  1.00 62.95  ? 135  CYS E CB  1 
ATOM   8793  S SG  . CYS E  1 135 ? 4.368   60.586 88.456  1.00 60.64  ? 135  CYS E SG  1 
ATOM   8794  N N   . PRO E  1 136 ? 0.043   63.597 88.493  1.00 67.37  ? 136  PRO E N   1 
ATOM   8795  C CA  . PRO E  1 136 ? -1.365  63.819 88.828  1.00 69.69  ? 136  PRO E CA  1 
ATOM   8796  C C   . PRO E  1 136 ? -2.354  63.061 87.934  1.00 69.48  ? 136  PRO E C   1 
ATOM   8797  O O   . PRO E  1 136 ? -2.134  62.948 86.727  1.00 67.86  ? 136  PRO E O   1 
ATOM   8798  C CB  . PRO E  1 136 ? -1.528  65.324 88.620  1.00 70.88  ? 136  PRO E CB  1 
ATOM   8799  C CG  . PRO E  1 136 ? -0.572  65.639 87.525  1.00 68.71  ? 136  PRO E CG  1 
ATOM   8800  C CD  . PRO E  1 136 ? 0.612   64.748 87.765  1.00 66.76  ? 136  PRO E CD  1 
ATOM   8801  N N   . TYR E  1 137 ? -3.434  62.562 88.539  1.00 71.29  ? 137  TYR E N   1 
ATOM   8802  C CA  . TYR E  1 137 ? -4.536  61.917 87.817  1.00 71.74  ? 137  TYR E CA  1 
ATOM   8803  C C   . TYR E  1 137 ? -5.879  62.416 88.354  1.00 74.73  ? 137  TYR E C   1 
ATOM   8804  O O   . TYR E  1 137 ? -6.176  62.251 89.538  1.00 76.47  ? 137  TYR E O   1 
ATOM   8805  C CB  . TYR E  1 137 ? -4.453  60.395 87.967  1.00 70.90  ? 137  TYR E CB  1 
ATOM   8806  C CG  . TYR E  1 137 ? -5.635  59.638 87.385  1.00 71.83  ? 137  TYR E CG  1 
ATOM   8807  C CD1 . TYR E  1 137 ? -5.849  59.585 86.006  1.00 70.81  ? 137  TYR E CD1 1 
ATOM   8808  C CD2 . TYR E  1 137 ? -6.532  58.960 88.215  1.00 73.89  ? 137  TYR E CD2 1 
ATOM   8809  C CE1 . TYR E  1 137 ? -6.926  58.889 85.473  1.00 71.85  ? 137  TYR E CE1 1 
ATOM   8810  C CE2 . TYR E  1 137 ? -7.609  58.260 87.689  1.00 74.95  ? 137  TYR E CE2 1 
ATOM   8811  C CZ  . TYR E  1 137 ? -7.802  58.228 86.320  1.00 73.92  ? 137  TYR E CZ  1 
ATOM   8812  O OH  . TYR E  1 137 ? -8.872  57.535 85.802  1.00 75.15  ? 137  TYR E OH  1 
ATOM   8813  N N   . GLN E  1 138 ? -6.681  63.019 87.476  1.00 75.45  ? 138  GLN E N   1 
ATOM   8814  C CA  . GLN E  1 138 ? -7.985  63.598 87.838  1.00 78.44  ? 138  GLN E CA  1 
ATOM   8815  C C   . GLN E  1 138 ? -7.890  64.611 88.983  1.00 80.27  ? 138  GLN E C   1 
ATOM   8816  O O   . GLN E  1 138 ? -8.730  64.627 89.887  1.00 82.88  ? 138  GLN E O   1 
ATOM   8817  C CB  . GLN E  1 138 ? -8.999  62.499 88.182  1.00 79.94  ? 138  GLN E CB  1 
ATOM   8818  C CG  . GLN E  1 138 ? -9.035  61.366 87.169  1.00 78.26  ? 138  GLN E CG  1 
ATOM   8819  C CD  . GLN E  1 138 ? -10.415 60.752 87.002  1.00 80.38  ? 138  GLN E CD  1 
ATOM   8820  O OE1 . GLN E  1 138 ? -11.137 60.542 87.976  1.00 82.73  ? 138  GLN E OE1 1 
ATOM   8821  N NE2 . GLN E  1 138 ? -10.784 60.453 85.759  1.00 79.71  ? 138  GLN E NE2 1 
ATOM   8822  N N   . GLY E  1 139 ? -6.855  65.449 88.938  1.00 79.04  ? 139  GLY E N   1 
ATOM   8823  C CA  . GLY E  1 139 ? -6.658  66.512 89.925  1.00 80.75  ? 139  GLY E CA  1 
ATOM   8824  C C   . GLY E  1 139 ? -6.076  66.057 91.253  1.00 81.02  ? 139  GLY E C   1 
ATOM   8825  O O   . GLY E  1 139 ? -5.895  66.871 92.158  1.00 82.65  ? 139  GLY E O   1 
ATOM   8826  N N   . LYS E  1 140 ? -5.773  64.765 91.364  1.00 79.54  ? 140  LYS E N   1 
ATOM   8827  C CA  . LYS E  1 140 ? -5.267  64.171 92.598  1.00 79.83  ? 140  LYS E CA  1 
ATOM   8828  C C   . LYS E  1 140 ? -3.916  63.522 92.340  1.00 76.81  ? 140  LYS E C   1 
ATOM   8829  O O   . LYS E  1 140 ? -3.620  63.120 91.215  1.00 74.63  ? 140  LYS E O   1 
ATOM   8830  C CB  . LYS E  1 140 ? -6.264  63.134 93.125  1.00 81.42  ? 140  LYS E CB  1 
ATOM   8831  C CG  . LYS E  1 140 ? -7.521  63.753 93.719  1.00 84.90  ? 140  LYS E CG  1 
ATOM   8832  C CD  . LYS E  1 140 ? -8.787  63.012 93.308  1.00 86.09  ? 140  LYS E CD  1 
ATOM   8833  C CE  . LYS E  1 140 ? -10.044 63.777 93.704  1.00 89.60  ? 140  LYS E CE  1 
ATOM   8834  N NZ  . LYS E  1 140 ? -10.421 63.569 95.129  1.00 92.29  ? 140  LYS E NZ  1 
ATOM   8835  N N   . SER E  1 141 ? -3.101  63.425 93.388  1.00 76.87  ? 141  SER E N   1 
ATOM   8836  C CA  . SER E  1 141 ? -1.759  62.852 93.282  1.00 74.30  ? 141  SER E CA  1 
ATOM   8837  C C   . SER E  1 141 ? -1.819  61.346 93.021  1.00 72.97  ? 141  SER E C   1 
ATOM   8838  O O   . SER E  1 141 ? -2.563  60.623 93.684  1.00 74.49  ? 141  SER E O   1 
ATOM   8839  C CB  . SER E  1 141 ? -0.956  63.129 94.556  1.00 75.12  ? 141  SER E CB  1 
ATOM   8840  O OG  . SER E  1 141 ? -0.721  64.518 94.717  1.00 76.16  ? 141  SER E OG  1 
ATOM   8841  N N   . SER E  1 142 ? -1.030  60.889 92.052  1.00 70.31  ? 142  SER E N   1 
ATOM   8842  C CA  . SER E  1 142 ? -1.028  59.491 91.630  1.00 68.97  ? 142  SER E CA  1 
ATOM   8843  C C   . SER E  1 142 ? 0.413   59.031 91.402  1.00 66.49  ? 142  SER E C   1 
ATOM   8844  O O   . SER E  1 142 ? 1.356   59.706 91.822  1.00 66.14  ? 142  SER E O   1 
ATOM   8845  C CB  . SER E  1 142 ? -1.861  59.337 90.351  1.00 68.58  ? 142  SER E CB  1 
ATOM   8846  O OG  . SER E  1 142 ? -2.030  57.977 89.993  1.00 67.79  ? 142  SER E OG  1 
ATOM   8847  N N   . PHE E  1 143 ? 0.581   57.881 90.754  1.00 64.97  ? 143  PHE E N   1 
ATOM   8848  C CA  . PHE E  1 143 ? 1.911   57.365 90.427  1.00 62.70  ? 143  PHE E CA  1 
ATOM   8849  C C   . PHE E  1 143 ? 1.843   56.406 89.237  1.00 61.18  ? 143  PHE E C   1 
ATOM   8850  O O   . PHE E  1 143 ? 0.755   56.030 88.796  1.00 62.00  ? 143  PHE E O   1 
ATOM   8851  C CB  . PHE E  1 143 ? 2.515   56.658 91.651  1.00 63.03  ? 143  PHE E CB  1 
ATOM   8852  C CG  . PHE E  1 143 ? 4.017   56.556 91.621  1.00 61.21  ? 143  PHE E CG  1 
ATOM   8853  C CD1 . PHE E  1 143 ? 4.803   57.703 91.594  1.00 60.82  ? 143  PHE E CD1 1 
ATOM   8854  C CD2 . PHE E  1 143 ? 4.648   55.316 91.633  1.00 60.08  ? 143  PHE E CD2 1 
ATOM   8855  C CE1 . PHE E  1 143 ? 6.186   57.618 91.570  1.00 59.36  ? 143  PHE E CE1 1 
ATOM   8856  C CE2 . PHE E  1 143 ? 6.032   55.225 91.610  1.00 58.59  ? 143  PHE E CE2 1 
ATOM   8857  C CZ  . PHE E  1 143 ? 6.803   56.378 91.580  1.00 58.24  ? 143  PHE E CZ  1 
ATOM   8858  N N   . PHE E  1 144 ? 3.009   56.028 88.716  1.00 59.15  ? 144  PHE E N   1 
ATOM   8859  C CA  . PHE E  1 144 ? 3.103   54.988 87.693  1.00 57.79  ? 144  PHE E CA  1 
ATOM   8860  C C   . PHE E  1 144 ? 2.297   53.762 88.141  1.00 58.88  ? 144  PHE E C   1 
ATOM   8861  O O   . PHE E  1 144 ? 2.623   53.141 89.147  1.00 59.33  ? 144  PHE E O   1 
ATOM   8862  C CB  . PHE E  1 144 ? 4.563   54.570 87.458  1.00 55.88  ? 144  PHE E CB  1 
ATOM   8863  C CG  . PHE E  1 144 ? 5.496   55.710 87.131  1.00 54.96  ? 144  PHE E CG  1 
ATOM   8864  C CD1 . PHE E  1 144 ? 5.468   56.321 85.883  1.00 54.14  ? 144  PHE E CD1 1 
ATOM   8865  C CD2 . PHE E  1 144 ? 6.419   56.158 88.070  1.00 55.04  ? 144  PHE E CD2 1 
ATOM   8866  C CE1 . PHE E  1 144 ? 6.337   57.362 85.586  1.00 53.46  ? 144  PHE E CE1 1 
ATOM   8867  C CE2 . PHE E  1 144 ? 7.287   57.197 87.779  1.00 54.39  ? 144  PHE E CE2 1 
ATOM   8868  C CZ  . PHE E  1 144 ? 7.247   57.800 86.535  1.00 53.60  ? 144  PHE E CZ  1 
ATOM   8869  N N   . ARG E  1 145 ? 1.253   53.421 87.392  1.00 59.46  ? 145  ARG E N   1 
ATOM   8870  C CA  . ARG E  1 145 ? 0.309   52.370 87.792  1.00 60.93  ? 145  ARG E CA  1 
ATOM   8871  C C   . ARG E  1 145 ? 0.892   50.960 87.872  1.00 60.19  ? 145  ARG E C   1 
ATOM   8872  O O   . ARG E  1 145 ? 0.349   50.108 88.573  1.00 61.56  ? 145  ARG E O   1 
ATOM   8873  C CB  . ARG E  1 145 ? -0.881  52.332 86.834  1.00 61.72  ? 145  ARG E CB  1 
ATOM   8874  C CG  . ARG E  1 145 ? -1.651  53.632 86.739  1.00 62.86  ? 145  ARG E CG  1 
ATOM   8875  C CD  . ARG E  1 145 ? -3.043  53.383 86.195  1.00 64.43  ? 145  ARG E CD  1 
ATOM   8876  N NE  . ARG E  1 145 ? -3.734  54.634 85.909  1.00 65.43  ? 145  ARG E NE  1 
ATOM   8877  C CZ  . ARG E  1 145 ? -4.311  55.410 86.824  1.00 67.31  ? 145  ARG E CZ  1 
ATOM   8878  N NH1 . ARG E  1 145 ? -4.289  55.090 88.118  1.00 68.44  ? 145  ARG E NH1 1 
ATOM   8879  N NH2 . ARG E  1 145 ? -4.915  56.525 86.443  1.00 68.22  ? 145  ARG E NH2 1 
ATOM   8880  N N   . ASN E  1 146 ? 1.974   50.704 87.145  1.00 58.23  ? 146  ASN E N   1 
ATOM   8881  C CA  . ASN E  1 146 ? 2.531   49.352 87.060  1.00 57.57  ? 146  ASN E CA  1 
ATOM   8882  C C   . ASN E  1 146 ? 3.471   48.984 88.204  1.00 57.44  ? 146  ASN E C   1 
ATOM   8883  O O   . ASN E  1 146 ? 3.767   47.804 88.404  1.00 57.40  ? 146  ASN E O   1 
ATOM   8884  C CB  . ASN E  1 146 ? 3.227   49.148 85.710  1.00 55.75  ? 146  ASN E CB  1 
ATOM   8885  C CG  . ASN E  1 146 ? 2.240   49.047 84.562  1.00 56.15  ? 146  ASN E CG  1 
ATOM   8886  O OD1 . ASN E  1 146 ? 1.249   48.326 84.654  1.00 57.58  ? 146  ASN E OD1 1 
ATOM   8887  N ND2 . ASN E  1 146 ? 2.504   49.769 83.478  1.00 55.07  ? 146  ASN E ND2 1 
ATOM   8888  N N   . VAL E  1 147 ? 3.929   49.983 88.956  1.00 57.52  ? 147  VAL E N   1 
ATOM   8889  C CA  . VAL E  1 147 ? 4.805   49.741 90.103  1.00 57.63  ? 147  VAL E CA  1 
ATOM   8890  C C   . VAL E  1 147 ? 4.293   50.426 91.373  1.00 59.47  ? 147  VAL E C   1 
ATOM   8891  O O   . VAL E  1 147 ? 3.660   51.481 91.309  1.00 60.20  ? 147  VAL E O   1 
ATOM   8892  C CB  . VAL E  1 147 ? 6.259   50.176 89.818  1.00 55.85  ? 147  VAL E CB  1 
ATOM   8893  C CG1 . VAL E  1 147 ? 6.908   49.241 88.808  1.00 54.33  ? 147  VAL E CG1 1 
ATOM   8894  C CG2 . VAL E  1 147 ? 6.324   51.622 89.334  1.00 55.43  ? 147  VAL E CG2 1 
ATOM   8895  N N   . VAL E  1 148 ? 4.586   49.820 92.521  1.00 60.34  ? 148  VAL E N   1 
ATOM   8896  C CA  . VAL E  1 148 ? 4.092   50.290 93.817  1.00 62.39  ? 148  VAL E CA  1 
ATOM   8897  C C   . VAL E  1 148 ? 5.203   50.991 94.603  1.00 62.13  ? 148  VAL E C   1 
ATOM   8898  O O   . VAL E  1 148 ? 6.245   50.393 94.878  1.00 61.28  ? 148  VAL E O   1 
ATOM   8899  C CB  . VAL E  1 148 ? 3.556   49.115 94.666  1.00 64.01  ? 148  VAL E CB  1 
ATOM   8900  C CG1 . VAL E  1 148 ? 2.751   49.629 95.854  1.00 66.49  ? 148  VAL E CG1 1 
ATOM   8901  C CG2 . VAL E  1 148 ? 2.703   48.178 93.821  1.00 64.11  ? 148  VAL E CG2 1 
ATOM   8902  N N   . TRP E  1 149 ? 4.977   52.253 94.959  1.00 63.03  ? 149  TRP E N   1 
ATOM   8903  C CA  . TRP E  1 149 ? 5.896   52.986 95.829  1.00 63.34  ? 149  TRP E CA  1 
ATOM   8904  C C   . TRP E  1 149 ? 5.596   52.611 97.291  1.00 65.54  ? 149  TRP E C   1 
ATOM   8905  O O   . TRP E  1 149 ? 4.614   53.077 97.875  1.00 67.56  ? 149  TRP E O   1 
ATOM   8906  C CB  . TRP E  1 149 ? 5.750   54.496 95.605  1.00 63.64  ? 149  TRP E CB  1 
ATOM   8907  C CG  . TRP E  1 149 ? 6.817   55.351 96.254  1.00 63.72  ? 149  TRP E CG  1 
ATOM   8908  C CD1 . TRP E  1 149 ? 7.798   54.942 97.117  1.00 63.78  ? 149  TRP E CD1 1 
ATOM   8909  C CD2 . TRP E  1 149 ? 6.984   56.768 96.105  1.00 63.99  ? 149  TRP E CD2 1 
ATOM   8910  N NE1 . TRP E  1 149 ? 8.572   56.012 97.496  1.00 64.07  ? 149  TRP E NE1 1 
ATOM   8911  C CE2 . TRP E  1 149 ? 8.093   57.144 96.893  1.00 64.22  ? 149  TRP E CE2 1 
ATOM   8912  C CE3 . TRP E  1 149 ? 6.310   57.752 95.376  1.00 64.18  ? 149  TRP E CE3 1 
ATOM   8913  C CZ2 . TRP E  1 149 ? 8.542   58.465 96.973  1.00 64.70  ? 149  TRP E CZ2 1 
ATOM   8914  C CZ3 . TRP E  1 149 ? 6.757   59.066 95.458  1.00 64.62  ? 149  TRP E CZ3 1 
ATOM   8915  C CH2 . TRP E  1 149 ? 7.862   59.409 96.251  1.00 64.90  ? 149  TRP E CH2 1 
ATOM   8916  N N   . LEU E  1 150 ? 6.446   51.765 97.870  1.00 65.28  ? 150  LEU E N   1 
ATOM   8917  C CA  . LEU E  1 150 ? 6.227   51.247 99.220  1.00 67.35  ? 150  LEU E CA  1 
ATOM   8918  C C   . LEU E  1 150 ? 6.844   52.152 100.281 1.00 68.52  ? 150  LEU E C   1 
ATOM   8919  O O   . LEU E  1 150 ? 7.944   52.680 100.095 1.00 67.30  ? 150  LEU E O   1 
ATOM   8920  C CB  . LEU E  1 150 ? 6.804   49.834 99.360  1.00 66.72  ? 150  LEU E CB  1 
ATOM   8921  C CG  . LEU E  1 150 ? 6.118   48.714 98.572  1.00 66.26  ? 150  LEU E CG  1 
ATOM   8922  C CD1 . LEU E  1 150 ? 6.883   47.414 98.762  1.00 65.70  ? 150  LEU E CD1 1 
ATOM   8923  C CD2 . LEU E  1 150 ? 4.662   48.543 98.985  1.00 68.48  ? 150  LEU E CD2 1 
ATOM   8924  N N   . ILE E  1 151 ? 6.124   52.318 101.391 1.00 71.11  ? 151  ILE E N   1 
ATOM   8925  C CA  . ILE E  1 151 ? 6.600   53.089 102.543 1.00 72.74  ? 151  ILE E CA  1 
ATOM   8926  C C   . ILE E  1 151 ? 6.338   52.340 103.855 1.00 74.99  ? 151  ILE E C   1 
ATOM   8927  O O   . ILE E  1 151 ? 5.586   51.362 103.892 1.00 75.62  ? 151  ILE E O   1 
ATOM   8928  C CB  . ILE E  1 151 ? 5.955   54.495 102.601 1.00 74.10  ? 151  ILE E CB  1 
ATOM   8929  C CG1 . ILE E  1 151 ? 4.454   54.398 102.914 1.00 76.33  ? 151  ILE E CG1 1 
ATOM   8930  C CG2 . ILE E  1 151 ? 6.200   55.241 101.294 1.00 72.00  ? 151  ILE E CG2 1 
ATOM   8931  C CD1 . ILE E  1 151 ? 3.715   55.718 102.864 1.00 77.73  ? 151  ILE E CD1 1 
ATOM   8932  N N   . LYS E  1 152 ? 6.969   52.820 104.922 1.00 76.36  ? 152  LYS E N   1 
ATOM   8933  C CA  . LYS E  1 152 ? 6.867   52.212 106.255 1.00 78.68  ? 152  LYS E CA  1 
ATOM   8934  C C   . LYS E  1 152 ? 5.435   52.201 106.804 1.00 81.35  ? 152  LYS E C   1 
ATOM   8935  O O   . LYS E  1 152 ? 4.651   53.111 106.526 1.00 82.09  ? 152  LYS E O   1 
ATOM   8936  C CB  . LYS E  1 152 ? 7.779   52.963 107.232 1.00 79.80  ? 152  LYS E CB  1 
ATOM   8937  C CG  . LYS E  1 152 ? 7.316   54.380 107.540 1.00 81.49  ? 152  LYS E CG  1 
ATOM   8938  C CD  . LYS E  1 152 ? 8.414   55.217 108.171 1.00 82.03  ? 152  LYS E CD  1 
ATOM   8939  C CE  . LYS E  1 152 ? 7.837   56.457 108.838 1.00 84.65  ? 152  LYS E CE  1 
ATOM   8940  N NZ  . LYS E  1 152 ? 8.838   57.142 109.699 1.00 85.86  ? 152  LYS E NZ  1 
ATOM   8941  N N   . LYS E  1 153 ? 5.107   51.169 107.584 1.00 82.96  ? 153  LYS E N   1 
ATOM   8942  C CA  . LYS E  1 153 ? 3.814   51.083 108.275 1.00 85.94  ? 153  LYS E CA  1 
ATOM   8943  C C   . LYS E  1 153 ? 4.006   51.215 109.787 1.00 88.78  ? 153  LYS E C   1 
ATOM   8944  O O   . LYS E  1 153 ? 4.780   50.467 110.387 1.00 88.79  ? 153  LYS E O   1 
ATOM   8945  C CB  . LYS E  1 153 ? 3.108   49.762 107.957 1.00 85.96  ? 153  LYS E CB  1 
ATOM   8946  C CG  . LYS E  1 153 ? 1.593   49.830 108.113 1.00 88.40  ? 153  LYS E CG  1 
ATOM   8947  C CD  . LYS E  1 153 ? 1.010   48.495 108.547 1.00 89.92  ? 153  LYS E CD  1 
ATOM   8948  C CE  . LYS E  1 153 ? 1.069   47.443 107.450 1.00 87.66  ? 153  LYS E CE  1 
ATOM   8949  N NZ  . LYS E  1 153 ? 0.107   47.601 106.326 1.00 87.02  ? 153  LYS E NZ  1 
ATOM   8950  N N   . ASN E  1 154 ? 3.286   52.162 110.388 1.00 91.34  ? 154  ASN E N   1 
ATOM   8951  C CA  . ASN E  1 154 ? 3.409   52.488 111.816 1.00 94.38  ? 154  ASN E CA  1 
ATOM   8952  C C   . ASN E  1 154 ? 4.858   52.756 112.243 1.00 93.54  ? 154  ASN E C   1 
ATOM   8953  O O   . ASN E  1 154 ? 5.309   52.295 113.296 1.00 95.10  ? 154  ASN E O   1 
ATOM   8954  C CB  . ASN E  1 154 ? 2.769   51.397 112.693 1.00 96.81  ? 154  ASN E CB  1 
ATOM   8955  C CG  . ASN E  1 154 ? 2.405   51.902 114.085 1.00 100.69 ? 154  ASN E CG  1 
ATOM   8956  O OD1 . ASN E  1 154 ? 2.124   53.085 114.274 1.00 102.03 ? 154  ASN E OD1 1 
ATOM   8957  N ND2 . ASN E  1 154 ? 2.406   51.002 115.065 1.00 102.70 ? 154  ASN E ND2 1 
ATOM   8958  N N   . SER E  1 155 ? 5.575   53.503 111.403 1.00 91.18  ? 155  SER E N   1 
ATOM   8959  C CA  . SER E  1 155 ? 6.941   53.938 111.690 1.00 90.44  ? 155  SER E CA  1 
ATOM   8960  C C   . SER E  1 155 ? 7.946   52.775 111.739 1.00 88.91  ? 155  SER E C   1 
ATOM   8961  O O   . SER E  1 155 ? 8.869   52.788 112.548 1.00 89.71  ? 155  SER E O   1 
ATOM   8962  C CB  . SER E  1 155 ? 6.971   54.743 113.001 1.00 93.70  ? 155  SER E CB  1 
ATOM   8963  O OG  . SER E  1 155 ? 8.075   55.628 113.042 1.00 93.13  ? 155  SER E OG  1 
ATOM   8964  N N   . THR E  1 156 ? 7.756   51.771 110.883 1.00 86.91  ? 156  THR E N   1 
ATOM   8965  C CA  . THR E  1 156 ? 8.700   50.649 110.768 1.00 85.31  ? 156  THR E CA  1 
ATOM   8966  C C   . THR E  1 156 ? 8.708   50.126 109.332 1.00 82.31  ? 156  THR E C   1 
ATOM   8967  O O   . THR E  1 156 ? 7.648   49.841 108.776 1.00 82.27  ? 156  THR E O   1 
ATOM   8968  C CB  . THR E  1 156 ? 8.347   49.458 111.699 1.00 87.25  ? 156  THR E CB  1 
ATOM   8969  O OG1 . THR E  1 156 ? 7.388   48.604 111.059 1.00 86.78  ? 156  THR E OG1 1 
ATOM   8970  C CG2 . THR E  1 156 ? 7.794   49.915 113.054 1.00 90.84  ? 156  THR E CG2 1 
ATOM   8971  N N   . TYR E  1 157 ? 9.896   50.008 108.737 1.00 80.01  ? 157  TYR E N   1 
ATOM   8972  C CA  . TYR E  1 157 ? 10.046  49.420 107.401 1.00 77.25  ? 157  TYR E CA  1 
ATOM   8973  C C   . TYR E  1 157 ? 10.789  48.087 107.519 1.00 76.60  ? 157  TYR E C   1 
ATOM   8974  O O   . TYR E  1 157 ? 12.022  48.052 107.468 1.00 75.45  ? 157  TYR E O   1 
ATOM   8975  C CB  . TYR E  1 157 ? 10.792  50.373 106.459 1.00 75.10  ? 157  TYR E CB  1 
ATOM   8976  C CG  . TYR E  1 157 ? 10.636  50.046 104.979 1.00 72.56  ? 157  TYR E CG  1 
ATOM   8977  C CD1 . TYR E  1 157 ? 11.317  48.975 104.398 1.00 70.81  ? 157  TYR E CD1 1 
ATOM   8978  C CD2 . TYR E  1 157 ? 9.810   50.811 104.161 1.00 72.08  ? 157  TYR E CD2 1 
ATOM   8979  C CE1 . TYR E  1 157 ? 11.178  48.679 103.050 1.00 68.71  ? 157  TYR E CE1 1 
ATOM   8980  C CE2 . TYR E  1 157 ? 9.667   50.523 102.812 1.00 69.93  ? 157  TYR E CE2 1 
ATOM   8981  C CZ  . TYR E  1 157 ? 10.352  49.456 102.258 1.00 68.27  ? 157  TYR E CZ  1 
ATOM   8982  O OH  . TYR E  1 157 ? 10.210  49.169 100.915 1.00 66.32  ? 157  TYR E OH  1 
ATOM   8983  N N   . PRO E  1 158 ? 10.041  46.984 107.700 1.00 77.56  ? 158  PRO E N   1 
ATOM   8984  C CA  . PRO E  1 158 ? 10.684  45.673 107.774 1.00 77.11  ? 158  PRO E CA  1 
ATOM   8985  C C   . PRO E  1 158 ? 11.252  45.238 106.428 1.00 74.32  ? 158  PRO E C   1 
ATOM   8986  O O   . PRO E  1 158 ? 10.772  45.671 105.379 1.00 72.92  ? 158  PRO E O   1 
ATOM   8987  C CB  . PRO E  1 158 ? 9.554   44.736 108.222 1.00 79.00  ? 158  PRO E CB  1 
ATOM   8988  C CG  . PRO E  1 158 ? 8.291   45.446 107.886 1.00 79.64  ? 158  PRO E CG  1 
ATOM   8989  C CD  . PRO E  1 158 ? 8.590   46.911 107.951 1.00 79.46  ? 158  PRO E CD  1 
ATOM   8990  N N   . THR E  1 159 ? 12.275  44.392 106.471 1.00 73.71  ? 159  THR E N   1 
ATOM   8991  C CA  . THR E  1 159 ? 12.931  43.916 105.260 1.00 71.33  ? 159  THR E CA  1 
ATOM   8992  C C   . THR E  1 159 ? 11.934  43.151 104.391 1.00 70.97  ? 159  THR E C   1 
ATOM   8993  O O   . THR E  1 159 ? 11.140  42.352 104.896 1.00 72.60  ? 159  THR E O   1 
ATOM   8994  C CB  . THR E  1 159 ? 14.138  43.009 105.584 1.00 71.08  ? 159  THR E CB  1 
ATOM   8995  O OG1 . THR E  1 159 ? 15.005  43.670 106.513 1.00 71.95  ? 159  THR E OG1 1 
ATOM   8996  C CG2 . THR E  1 159 ? 14.927  42.672 104.325 1.00 68.61  ? 159  THR E CG2 1 
ATOM   8997  N N   . ILE E  1 160 ? 11.979  43.427 103.089 1.00 69.05  ? 160  ILE E N   1 
ATOM   8998  C CA  . ILE E  1 160 ? 11.117  42.779 102.104 1.00 68.57  ? 160  ILE E CA  1 
ATOM   8999  C C   . ILE E  1 160 ? 11.880  41.636 101.455 1.00 67.49  ? 160  ILE E C   1 
ATOM   9000  O O   . ILE E  1 160 ? 13.001  41.829 101.000 1.00 65.95  ? 160  ILE E O   1 
ATOM   9001  C CB  . ILE E  1 160 ? 10.685  43.770 101.001 1.00 67.10  ? 160  ILE E CB  1 
ATOM   9002  C CG1 . ILE E  1 160 ? 9.808   44.875 101.596 1.00 68.54  ? 160  ILE E CG1 1 
ATOM   9003  C CG2 . ILE E  1 160 ? 9.946   43.041 99.883  1.00 66.35  ? 160  ILE E CG2 1 
ATOM   9004  C CD1 . ILE E  1 160 ? 9.638   46.089 100.708 1.00 67.27  ? 160  ILE E CD1 1 
ATOM   9005  N N   . LYS E  1 161 ? 11.278  40.449 101.425 1.00 68.58  ? 161  LYS E N   1 
ATOM   9006  C CA  . LYS E  1 161 ? 11.833  39.314 100.685 1.00 67.77  ? 161  LYS E CA  1 
ATOM   9007  C C   . LYS E  1 161 ? 10.744  38.717 99.809  1.00 68.08  ? 161  LYS E C   1 
ATOM   9008  O O   . LYS E  1 161 ? 9.820   38.074 100.305 1.00 69.93  ? 161  LYS E O   1 
ATOM   9009  C CB  . LYS E  1 161 ? 12.396  38.252 101.632 1.00 69.07  ? 161  LYS E CB  1 
ATOM   9010  C CG  . LYS E  1 161 ? 13.550  38.746 102.488 1.00 69.12  ? 161  LYS E CG  1 
ATOM   9011  C CD  . LYS E  1 161 ? 14.259  37.612 103.213 1.00 70.18  ? 161  LYS E CD  1 
ATOM   9012  C CE  . LYS E  1 161 ? 15.413  38.136 104.063 1.00 70.40  ? 161  LYS E CE  1 
ATOM   9013  N NZ  . LYS E  1 161 ? 15.833  37.182 105.143 1.00 72.20  ? 161  LYS E NZ  1 
ATOM   9014  N N   . ARG E  1 162 ? 10.846  38.952 98.506  1.00 66.57  ? 162  ARG E N   1 
ATOM   9015  C CA  . ARG E  1 162 ? 9.830   38.514 97.570  1.00 66.85  ? 162  ARG E CA  1 
ATOM   9016  C C   . ARG E  1 162 ? 10.417  37.817 96.367  1.00 65.75  ? 162  ARG E C   1 
ATOM   9017  O O   . ARG E  1 162 ? 11.403  38.276 95.800  1.00 64.00  ? 162  ARG E O   1 
ATOM   9018  C CB  . ARG E  1 162 ? 9.085   39.733 97.049  1.00 66.23  ? 162  ARG E CB  1 
ATOM   9019  C CG  . ARG E  1 162 ? 7.586   39.560 96.987  1.00 67.68  ? 162  ARG E CG  1 
ATOM   9020  C CD  . ARG E  1 162 ? 6.906   39.018 98.216  1.00 70.13  ? 162  ARG E CD  1 
ATOM   9021  N NE  . ARG E  1 162 ? 5.493   39.354 98.085  1.00 71.36  ? 162  ARG E NE  1 
ATOM   9022  C CZ  . ARG E  1 162 ? 4.782   40.217 98.822  1.00 72.68  ? 162  ARG E CZ  1 
ATOM   9023  N NH1 . ARG E  1 162 ? 5.280   40.854 99.883  1.00 73.21  ? 162  ARG E NH1 1 
ATOM   9024  N NH2 . ARG E  1 162 ? 3.511   40.421 98.501  1.00 73.73  ? 162  ARG E NH2 1 
ATOM   9025  N N   . SER E  1 163 ? 9.752   36.744 95.952  1.00 67.10  ? 163  SER E N   1 
ATOM   9026  C CA  . SER E  1 163 ? 10.189  35.937 94.832  1.00 66.56  ? 163  SER E CA  1 
ATOM   9027  C C   . SER E  1 163 ? 9.009   35.638 93.910  1.00 67.58  ? 163  SER E C   1 
ATOM   9028  O O   . SER E  1 163 ? 7.916   35.329 94.383  1.00 69.38  ? 163  SER E O   1 
ATOM   9029  C CB  . SER E  1 163 ? 10.791  34.633 95.351  1.00 67.48  ? 163  SER E CB  1 
ATOM   9030  O OG  . SER E  1 163 ? 11.235  33.812 94.286  1.00 66.76  ? 163  SER E OG  1 
ATOM   9031  N N   . TYR E  1 164 ? 9.225   35.748 92.600  1.00 66.91  ? 164  TYR E N   1 
ATOM   9032  C CA  . TYR E  1 164 ? 8.222   35.331 91.619  1.00 68.10  ? 164  TYR E CA  1 
ATOM   9033  C C   . TYR E  1 164 ? 8.789   34.313 90.633  1.00 68.55  ? 164  TYR E C   1 
ATOM   9034  O O   . TYR E  1 164 ? 9.835   34.548 90.031  1.00 66.87  ? 164  TYR E O   1 
ATOM   9035  C CB  . TYR E  1 164 ? 7.666   36.516 90.832  1.00 66.97  ? 164  TYR E CB  1 
ATOM   9036  C CG  . TYR E  1 164 ? 6.858   36.046 89.646  1.00 67.19  ? 164  TYR E CG  1 
ATOM   9037  C CD1 . TYR E  1 164 ? 5.546   35.607 89.805  1.00 69.09  ? 164  TYR E CD1 1 
ATOM   9038  C CD2 . TYR E  1 164 ? 7.424   35.981 88.374  1.00 65.77  ? 164  TYR E CD2 1 
ATOM   9039  C CE1 . TYR E  1 164 ? 4.809   35.146 88.725  1.00 69.53  ? 164  TYR E CE1 1 
ATOM   9040  C CE2 . TYR E  1 164 ? 6.696   35.522 87.288  1.00 66.18  ? 164  TYR E CE2 1 
ATOM   9041  C CZ  . TYR E  1 164 ? 5.389   35.108 87.466  1.00 68.07  ? 164  TYR E CZ  1 
ATOM   9042  O OH  . TYR E  1 164 ? 4.664   34.654 86.391  1.00 68.67  ? 164  TYR E OH  1 
ATOM   9043  N N   . ASN E  1 165 ? 8.067   33.207 90.452  1.00 71.42  ? 165  ASN E N   1 
ATOM   9044  C CA  . ASN E  1 165 ? 8.440   32.156 89.508  1.00 72.69  ? 165  ASN E CA  1 
ATOM   9045  C C   . ASN E  1 165 ? 7.668   32.297 88.197  1.00 71.47  ? 165  ASN E C   1 
ATOM   9046  O O   . ASN E  1 165 ? 6.437   32.282 88.196  1.00 72.75  ? 165  ASN E O   1 
ATOM   9047  C CB  . ASN E  1 165 ? 8.152   30.785 90.124  1.00 77.04  ? 165  ASN E CB  1 
ATOM   9048  C CG  . ASN E  1 165 ? 8.862   29.654 89.405  1.00 80.09  ? 165  ASN E CG  1 
ATOM   9049  O OD1 . ASN E  1 165 ? 9.342   29.809 88.283  1.00 78.69  ? 165  ASN E OD1 1 
ATOM   9050  N ND2 . ASN E  1 165 ? 8.929   28.501 90.057  1.00 85.70  ? 165  ASN E ND2 1 
ATOM   9051  N N   . ASN E  1 166 ? 8.393   32.424 87.086  1.00 68.90  ? 166  ASN E N   1 
ATOM   9052  C CA  . ASN E  1 166 ? 7.770   32.571 85.769  1.00 67.84  ? 166  ASN E CA  1 
ATOM   9053  C C   . ASN E  1 166 ? 7.253   31.236 85.230  1.00 68.92  ? 166  ASN E C   1 
ATOM   9054  O O   . ASN E  1 166 ? 7.979   30.502 84.554  1.00 68.71  ? 166  ASN E O   1 
ATOM   9055  C CB  . ASN E  1 166 ? 8.752   33.202 84.774  1.00 65.67  ? 166  ASN E CB  1 
ATOM   9056  C CG  . ASN E  1 166 ? 8.075   33.657 83.493  1.00 65.24  ? 166  ASN E CG  1 
ATOM   9057  O OD1 . ASN E  1 166 ? 6.867   33.892 83.464  1.00 66.11  ? 166  ASN E OD1 1 
ATOM   9058  N ND2 . ASN E  1 166 ? 8.855   33.794 82.427  1.00 63.98  ? 166  ASN E ND2 1 
ATOM   9059  N N   . THR E  1 167 ? 5.992   30.937 85.535  1.00 69.99  ? 167  THR E N   1 
ATOM   9060  C CA  . THR E  1 167 ? 5.349   29.694 85.101  1.00 71.48  ? 167  THR E CA  1 
ATOM   9061  C C   . THR E  1 167 ? 4.753   29.779 83.690  1.00 71.01  ? 167  THR E C   1 
ATOM   9062  O O   . THR E  1 167 ? 4.335   28.762 83.132  1.00 72.61  ? 167  THR E O   1 
ATOM   9063  C CB  . THR E  1 167 ? 4.226   29.281 86.072  1.00 73.76  ? 167  THR E CB  1 
ATOM   9064  O OG1 . THR E  1 167 ? 3.268   30.342 86.180  1.00 73.69  ? 167  THR E OG1 1 
ATOM   9065  C CG2 . THR E  1 167 ? 4.798   28.967 87.445  1.00 74.17  ? 167  THR E CG2 1 
ATOM   9066  N N   . ASN E  1 168 ? 4.707   30.984 83.122  1.00 68.81  ? 168  ASN E N   1 
ATOM   9067  C CA  . ASN E  1 168 ? 4.252   31.166 81.741  1.00 68.27  ? 168  ASN E CA  1 
ATOM   9068  C C   . ASN E  1 168 ? 5.333   30.643 80.816  1.00 67.02  ? 168  ASN E C   1 
ATOM   9069  O O   . ASN E  1 168 ? 6.514   30.740 81.146  1.00 65.66  ? 168  ASN E O   1 
ATOM   9070  C CB  . ASN E  1 168 ? 4.001   32.642 81.393  1.00 66.75  ? 168  ASN E CB  1 
ATOM   9071  C CG  . ASN E  1 168 ? 3.459   33.450 82.555  1.00 66.89  ? 168  ASN E CG  1 
ATOM   9072  O OD1 . ASN E  1 168 ? 2.250   33.652 82.671  1.00 68.25  ? 168  ASN E OD1 1 
ATOM   9073  N ND2 . ASN E  1 168 ? 4.356   33.933 83.411  1.00 65.63  ? 168  ASN E ND2 1 
ATOM   9074  N N   . GLN E  1 169 ? 4.950   30.093 79.666  1.00 67.49  ? 169  GLN E N   1 
ATOM   9075  C CA  . GLN E  1 169 ? 5.943   29.686 78.670  1.00 66.49  ? 169  GLN E CA  1 
ATOM   9076  C C   . GLN E  1 169 ? 6.256   30.864 77.727  1.00 64.30  ? 169  GLN E C   1 
ATOM   9077  O O   . GLN E  1 169 ? 6.087   30.785 76.512  1.00 64.55  ? 169  GLN E O   1 
ATOM   9078  C CB  . GLN E  1 169 ? 5.527   28.405 77.926  1.00 68.60  ? 169  GLN E CB  1 
ATOM   9079  C CG  . GLN E  1 169 ? 4.230   28.463 77.129  1.00 69.97  ? 169  GLN E CG  1 
ATOM   9080  C CD  . GLN E  1 169 ? 4.210   27.478 75.963  1.00 71.47  ? 169  GLN E CD  1 
ATOM   9081  O OE1 . GLN E  1 169 ? 5.253   27.132 75.400  1.00 70.83  ? 169  GLN E OE1 1 
ATOM   9082  N NE2 . GLN E  1 169 ? 3.017   27.033 75.587  1.00 73.60  ? 169  GLN E NE2 1 
ATOM   9083  N N   . GLU E  1 170 ? 6.717   31.956 78.331  1.00 62.21  ? 170  GLU E N   1 
ATOM   9084  C CA  . GLU E  1 170 ? 7.065   33.186 77.628  1.00 60.14  ? 170  GLU E CA  1 
ATOM   9085  C C   . GLU E  1 170 ? 8.194   33.891 78.379  1.00 58.17  ? 170  GLU E C   1 
ATOM   9086  O O   . GLU E  1 170 ? 8.374   33.682 79.582  1.00 58.35  ? 170  GLU E O   1 
ATOM   9087  C CB  . GLU E  1 170 ? 5.863   34.139 77.547  1.00 60.26  ? 170  GLU E CB  1 
ATOM   9088  C CG  . GLU E  1 170 ? 4.806   33.781 76.509  1.00 61.72  ? 170  GLU E CG  1 
ATOM   9089  C CD  . GLU E  1 170 ? 3.582   33.084 77.085  1.00 63.92  ? 170  GLU E CD  1 
ATOM   9090  O OE1 . GLU E  1 170 ? 3.667   32.489 78.184  1.00 64.62  ? 170  GLU E OE1 1 
ATOM   9091  O OE2 . GLU E  1 170 ? 2.518   33.134 76.430  1.00 65.09  ? 170  GLU E OE2 1 
ATOM   9092  N N   . ASP E  1 171 ? 8.959   34.709 77.660  1.00 56.38  ? 171  ASP E N   1 
ATOM   9093  C CA  . ASP E  1 171 ? 9.840   35.687 78.289  1.00 54.58  ? 171  ASP E CA  1 
ATOM   9094  C C   . ASP E  1 171 ? 8.938   36.730 78.945  1.00 54.26  ? 171  ASP E C   1 
ATOM   9095  O O   . ASP E  1 171 ? 7.833   36.998 78.458  1.00 54.88  ? 171  ASP E O   1 
ATOM   9096  C CB  . ASP E  1 171 ? 10.759  36.368 77.259  1.00 53.22  ? 171  ASP E CB  1 
ATOM   9097  C CG  . ASP E  1 171 ? 11.820  35.429 76.676  1.00 53.39  ? 171  ASP E CG  1 
ATOM   9098  O OD1 . ASP E  1 171 ? 12.187  34.418 77.315  1.00 54.16  ? 171  ASP E OD1 1 
ATOM   9099  O OD2 . ASP E  1 171 ? 12.304  35.723 75.563  1.00 52.87  ? 171  ASP E OD2 1 
ATOM   9100  N N   . LEU E  1 172 ? 9.400   37.304 80.053  1.00 53.38  ? 172  LEU E N   1 
ATOM   9101  C CA  . LEU E  1 172 ? 8.614   38.285 80.792  1.00 53.28  ? 172  LEU E CA  1 
ATOM   9102  C C   . LEU E  1 172 ? 9.419   39.550 81.062  1.00 51.63  ? 172  LEU E C   1 
ATOM   9103  O O   . LEU E  1 172 ? 10.512  39.487 81.625  1.00 50.98  ? 172  LEU E O   1 
ATOM   9104  C CB  . LEU E  1 172 ? 8.143   37.691 82.117  1.00 54.55  ? 172  LEU E CB  1 
ATOM   9105  C CG  . LEU E  1 172 ? 7.073   38.518 82.836  1.00 55.19  ? 172  LEU E CG  1 
ATOM   9106  C CD1 . LEU E  1 172 ? 5.690   38.186 82.291  1.00 56.63  ? 172  LEU E CD1 1 
ATOM   9107  C CD2 . LEU E  1 172 ? 7.122   38.288 84.339  1.00 55.98  ? 172  LEU E CD2 1 
ATOM   9108  N N   . LEU E  1 173 ? 8.866   40.694 80.663  1.00 51.07  ? 173  LEU E N   1 
ATOM   9109  C CA  . LEU E  1 173 ? 9.478   41.986 80.944  1.00 49.81  ? 173  LEU E CA  1 
ATOM   9110  C C   . LEU E  1 173 ? 9.059   42.476 82.325  1.00 50.31  ? 173  LEU E C   1 
ATOM   9111  O O   . LEU E  1 173 ? 7.910   42.873 82.529  1.00 51.16  ? 173  LEU E O   1 
ATOM   9112  C CB  . LEU E  1 173 ? 9.076   43.023 79.895  1.00 49.25  ? 173  LEU E CB  1 
ATOM   9113  C CG  . LEU E  1 173 ? 9.543   44.460 80.172  1.00 48.31  ? 173  LEU E CG  1 
ATOM   9114  C CD1 . LEU E  1 173 ? 11.059  44.573 80.119  1.00 47.18  ? 173  LEU E CD1 1 
ATOM   9115  C CD2 . LEU E  1 173 ? 8.900   45.423 79.190  1.00 48.15  ? 173  LEU E CD2 1 
ATOM   9116  N N   . VAL E  1 174 ? 10.006  42.464 83.258  1.00 49.89  ? 174  VAL E N   1 
ATOM   9117  C CA  . VAL E  1 174 ? 9.778   42.939 84.616  1.00 50.45  ? 174  VAL E CA  1 
ATOM   9118  C C   . VAL E  1 174 ? 10.404  44.324 84.775  1.00 49.47  ? 174  VAL E C   1 
ATOM   9119  O O   . VAL E  1 174 ? 11.560  44.534 84.402  1.00 48.38  ? 174  VAL E O   1 
ATOM   9120  C CB  . VAL E  1 174 ? 10.399  41.985 85.657  1.00 50.96  ? 174  VAL E CB  1 
ATOM   9121  C CG1 . VAL E  1 174 ? 9.948   42.361 87.061  1.00 52.00  ? 174  VAL E CG1 1 
ATOM   9122  C CG2 . VAL E  1 174 ? 10.033  40.540 85.351  1.00 51.83  ? 174  VAL E CG2 1 
ATOM   9123  N N   . LEU E  1 175 ? 9.633   45.256 85.330  1.00 50.03  ? 175  LEU E N   1 
ATOM   9124  C CA  . LEU E  1 175 ? 10.106  46.606 85.621  1.00 49.48  ? 175  LEU E CA  1 
ATOM   9125  C C   . LEU E  1 175 ? 10.048  46.865 87.121  1.00 50.46  ? 175  LEU E C   1 
ATOM   9126  O O   . LEU E  1 175 ? 9.095   46.467 87.782  1.00 51.77  ? 175  LEU E O   1 
ATOM   9127  C CB  . LEU E  1 175 ? 9.228   47.641 84.919  1.00 49.52  ? 175  LEU E CB  1 
ATOM   9128  C CG  . LEU E  1 175 ? 9.066   47.516 83.406  1.00 48.82  ? 175  LEU E CG  1 
ATOM   9129  C CD1 . LEU E  1 175 ? 8.019   48.500 82.907  1.00 49.24  ? 175  LEU E CD1 1 
ATOM   9130  C CD2 . LEU E  1 175 ? 10.397  47.738 82.708  1.00 47.44  ? 175  LEU E CD2 1 
ATOM   9131  N N   . TRP E  1 176 ? 11.066  47.542 87.646  1.00 49.98  ? 176  TRP E N   1 
ATOM   9132  C CA  . TRP E  1 176 ? 11.057  48.011 89.031  1.00 51.01  ? 176  TRP E CA  1 
ATOM   9133  C C   . TRP E  1 176 ? 11.879  49.292 89.158  1.00 50.52  ? 176  TRP E C   1 
ATOM   9134  O O   . TRP E  1 176 ? 12.468  49.760 88.184  1.00 49.37  ? 176  TRP E O   1 
ATOM   9135  C CB  . TRP E  1 176 ? 11.579  46.927 89.981  1.00 51.53  ? 176  TRP E CB  1 
ATOM   9136  C CG  . TRP E  1 176 ? 13.034  46.616 89.824  1.00 50.49  ? 176  TRP E CG  1 
ATOM   9137  C CD1 . TRP E  1 176 ? 14.065  47.101 90.577  1.00 50.47  ? 176  TRP E CD1 1 
ATOM   9138  C CD2 . TRP E  1 176 ? 13.621  45.744 88.854  1.00 49.52  ? 176  TRP E CD2 1 
ATOM   9139  N NE1 . TRP E  1 176 ? 15.257  46.584 90.136  1.00 49.55  ? 176  TRP E NE1 1 
ATOM   9140  C CE2 . TRP E  1 176 ? 15.013  45.748 89.078  1.00 48.96  ? 176  TRP E CE2 1 
ATOM   9141  C CE3 . TRP E  1 176 ? 13.104  44.959 87.816  1.00 49.23  ? 176  TRP E CE3 1 
ATOM   9142  C CZ2 . TRP E  1 176 ? 15.896  44.997 88.300  1.00 48.15  ? 176  TRP E CZ2 1 
ATOM   9143  C CZ3 . TRP E  1 176 ? 13.981  44.213 87.047  1.00 48.43  ? 176  TRP E CZ3 1 
ATOM   9144  C CH2 . TRP E  1 176 ? 15.361  44.238 87.293  1.00 47.90  ? 176  TRP E CH2 1 
ATOM   9145  N N   . GLY E  1 177 ? 11.911  49.858 90.360  1.00 51.59  ? 177  GLY E N   1 
ATOM   9146  C CA  . GLY E  1 177 ? 12.612  51.117 90.582  1.00 51.48  ? 177  GLY E CA  1 
ATOM   9147  C C   . GLY E  1 177 ? 13.195  51.279 91.970  1.00 52.52  ? 177  GLY E C   1 
ATOM   9148  O O   . GLY E  1 177 ? 12.868  50.532 92.895  1.00 53.55  ? 177  GLY E O   1 
ATOM   9149  N N   . ILE E  1 178 ? 14.075  52.267 92.092  1.00 52.38  ? 178  ILE E N   1 
ATOM   9150  C CA  . ILE E  1 178 ? 14.628  52.691 93.371  1.00 53.55  ? 178  ILE E CA  1 
ATOM   9151  C C   . ILE E  1 178 ? 14.348  54.187 93.508  1.00 54.34  ? 178  ILE E C   1 
ATOM   9152  O O   . ILE E  1 178 ? 14.375  54.916 92.515  1.00 53.51  ? 178  ILE E O   1 
ATOM   9153  C CB  . ILE E  1 178 ? 16.154  52.415 93.459  1.00 52.90  ? 178  ILE E CB  1 
ATOM   9154  C CG1 . ILE E  1 178 ? 16.636  52.496 94.924  1.00 54.35  ? 178  ILE E CG1 1 
ATOM   9155  C CG2 . ILE E  1 178 ? 16.931  53.328 92.511  1.00 51.89  ? 178  ILE E CG2 1 
ATOM   9156  C CD1 . ILE E  1 178 ? 18.030  53.050 95.142  1.00 54.31  ? 178  ILE E CD1 1 
ATOM   9157  N N   . HIS E  1 179 ? 14.065  54.638 94.728  1.00 56.08  ? 179  HIS E N   1 
ATOM   9158  C CA  . HIS E  1 179 ? 13.853  56.060 94.983  1.00 57.16  ? 179  HIS E CA  1 
ATOM   9159  C C   . HIS E  1 179 ? 15.080  56.704 95.625  1.00 57.71  ? 179  HIS E C   1 
ATOM   9160  O O   . HIS E  1 179 ? 15.642  56.178 96.590  1.00 58.42  ? 179  HIS E O   1 
ATOM   9161  C CB  . HIS E  1 179 ? 12.637  56.283 95.880  1.00 59.06  ? 179  HIS E CB  1 
ATOM   9162  C CG  . HIS E  1 179 ? 12.451  57.712 96.288  1.00 60.47  ? 179  HIS E CG  1 
ATOM   9163  N ND1 . HIS E  1 179 ? 12.464  58.118 97.604  1.00 62.49  ? 179  HIS E ND1 1 
ATOM   9164  C CD2 . HIS E  1 179 ? 12.278  58.834 95.550  1.00 60.30  ? 179  HIS E CD2 1 
ATOM   9165  C CE1 . HIS E  1 179 ? 12.287  59.425 97.662  1.00 63.54  ? 179  HIS E CE1 1 
ATOM   9166  N NE2 . HIS E  1 179 ? 12.172  59.884 96.429  1.00 62.24  ? 179  HIS E NE2 1 
ATOM   9167  N N   . HIS E  1 180 ? 15.473  57.856 95.086  1.00 57.57  ? 180  HIS E N   1 
ATOM   9168  C CA  . HIS E  1 180 ? 16.575  58.643 95.620  1.00 58.35  ? 180  HIS E CA  1 
ATOM   9169  C C   . HIS E  1 180 ? 15.994  59.857 96.348  1.00 60.36  ? 180  HIS E C   1 
ATOM   9170  O O   . HIS E  1 180 ? 15.440  60.754 95.707  1.00 60.41  ? 180  HIS E O   1 
ATOM   9171  C CB  . HIS E  1 180 ? 17.493  59.099 94.486  1.00 57.00  ? 180  HIS E CB  1 
ATOM   9172  C CG  . HIS E  1 180 ? 18.094  57.972 93.702  1.00 55.23  ? 180  HIS E CG  1 
ATOM   9173  N ND1 . HIS E  1 180 ? 19.431  57.650 93.772  1.00 54.86  ? 180  HIS E ND1 1 
ATOM   9174  C CD2 . HIS E  1 180 ? 17.544  57.099 92.825  1.00 53.91  ? 180  HIS E CD2 1 
ATOM   9175  C CE1 . HIS E  1 180 ? 19.680  56.625 92.979  1.00 53.38  ? 180  HIS E CE1 1 
ATOM   9176  N NE2 . HIS E  1 180 ? 18.552  56.270 92.392  1.00 52.78  ? 180  HIS E NE2 1 
ATOM   9177  N N   . PRO E  1 181 ? 16.106  59.885 97.691  1.00 62.16  ? 181  PRO E N   1 
ATOM   9178  C CA  . PRO E  1 181 ? 15.534  60.979 98.475  1.00 64.37  ? 181  PRO E CA  1 
ATOM   9179  C C   . PRO E  1 181 ? 16.418  62.224 98.484  1.00 65.13  ? 181  PRO E C   1 
ATOM   9180  O O   . PRO E  1 181 ? 17.600  62.149 98.148  1.00 64.21  ? 181  PRO E O   1 
ATOM   9181  C CB  . PRO E  1 181 ? 15.440  60.379 99.879  1.00 66.00  ? 181  PRO E CB  1 
ATOM   9182  C CG  . PRO E  1 181 ? 16.585  59.427 99.945  1.00 64.89  ? 181  PRO E CG  1 
ATOM   9183  C CD  . PRO E  1 181 ? 16.786  58.895 98.548  1.00 62.40  ? 181  PRO E CD  1 
ATOM   9184  N N   . ASN E  1 182 ? 15.838  63.354 98.876  1.00 66.99  ? 182  ASN E N   1 
ATOM   9185  C CA  . ASN E  1 182 ? 16.545  64.639 98.892  1.00 68.07  ? 182  ASN E CA  1 
ATOM   9186  C C   . ASN E  1 182 ? 17.640  64.740 99.952  1.00 69.48  ? 182  ASN E C   1 
ATOM   9187  O O   . ASN E  1 182 ? 18.744  65.204 99.660  1.00 69.28  ? 182  ASN E O   1 
ATOM   9188  C CB  . ASN E  1 182 ? 15.544  65.783 99.076  1.00 69.94  ? 182  ASN E CB  1 
ATOM   9189  C CG  . ASN E  1 182 ? 14.719  66.028 97.833  1.00 68.68  ? 182  ASN E CG  1 
ATOM   9190  O OD1 . ASN E  1 182 ? 15.227  66.553 96.851  1.00 67.65  ? 182  ASN E OD1 1 
ATOM   9191  N ND2 . ASN E  1 182 ? 13.448  65.639 97.862  1.00 68.89  ? 182  ASN E ND2 1 
ATOM   9192  N N   . ASP E  1 183 ? 17.324  64.313 101.175 1.00 71.08  ? 183  ASP E N   1 
ATOM   9193  C CA  . ASP E  1 183 ? 18.259  64.398 102.306 1.00 72.78  ? 183  ASP E CA  1 
ATOM   9194  C C   . ASP E  1 183 ? 18.057  63.258 103.313 1.00 73.35  ? 183  ASP E C   1 
ATOM   9195  O O   . ASP E  1 183 ? 17.112  62.475 103.197 1.00 72.65  ? 183  ASP E O   1 
ATOM   9196  C CB  . ASP E  1 183 ? 18.135  65.765 103.000 1.00 75.53  ? 183  ASP E CB  1 
ATOM   9197  C CG  . ASP E  1 183 ? 16.694  66.130 103.347 1.00 77.01  ? 183  ASP E CG  1 
ATOM   9198  O OD1 . ASP E  1 183 ? 15.947  65.263 103.852 1.00 77.18  ? 183  ASP E OD1 1 
ATOM   9199  O OD2 . ASP E  1 183 ? 16.310  67.296 103.122 1.00 78.17  ? 183  ASP E OD2 1 
ATOM   9200  N N   . ALA E  1 184 ? 18.953  63.179 104.298 1.00 74.77  ? 184  ALA E N   1 
ATOM   9201  C CA  . ALA E  1 184 ? 18.908  62.133 105.331 1.00 75.57  ? 184  ALA E CA  1 
ATOM   9202  C C   . ALA E  1 184 ? 17.616  62.158 106.152 1.00 77.51  ? 184  ALA E C   1 
ATOM   9203  O O   . ALA E  1 184 ? 17.153  61.114 106.616 1.00 77.53  ? 184  ALA E O   1 
ATOM   9204  C CB  . ALA E  1 184 ? 20.117  62.249 106.251 1.00 77.08  ? 184  ALA E CB  1 
ATOM   9205  N N   . ALA E  1 185 ? 17.046  63.349 106.330 1.00 79.32  ? 185  ALA E N   1 
ATOM   9206  C CA  . ALA E  1 185 ? 15.781  63.512 107.050 1.00 81.44  ? 185  ALA E CA  1 
ATOM   9207  C C   . ALA E  1 185 ? 14.600  62.910 106.284 1.00 79.96  ? 185  ALA E C   1 
ATOM   9208  O O   . ALA E  1 185 ? 13.693  62.330 106.885 1.00 81.03  ? 185  ALA E O   1 
ATOM   9209  C CB  . ALA E  1 185 ? 15.527  64.985 107.340 1.00 83.77  ? 185  ALA E CB  1 
ATOM   9210  N N   . GLU E  1 186 ? 14.613  63.054 104.961 1.00 77.69  ? 186  GLU E N   1 
ATOM   9211  C CA  . GLU E  1 186 ? 13.560  62.491 104.115 1.00 76.23  ? 186  GLU E CA  1 
ATOM   9212  C C   . GLU E  1 186 ? 13.671  60.969 104.004 1.00 74.57  ? 186  GLU E C   1 
ATOM   9213  O O   . GLU E  1 186 ? 12.655  60.274 103.944 1.00 74.50  ? 186  GLU E O   1 
ATOM   9214  C CB  . GLU E  1 186 ? 13.590  63.125 102.725 1.00 74.45  ? 186  GLU E CB  1 
ATOM   9215  C CG  . GLU E  1 186 ? 12.438  62.689 101.833 1.00 73.24  ? 186  GLU E CG  1 
ATOM   9216  C CD  . GLU E  1 186 ? 12.183  63.650 100.691 1.00 72.51  ? 186  GLU E CD  1 
ATOM   9217  O OE1 . GLU E  1 186 ? 12.972  63.641 99.720  1.00 70.47  ? 186  GLU E OE1 1 
ATOM   9218  O OE2 . GLU E  1 186 ? 11.186  64.404 100.757 1.00 73.99  ? 186  GLU E OE2 1 
ATOM   9219  N N   . GLN E  1 187 ? 14.903  60.463 103.967 1.00 73.42  ? 187  GLN E N   1 
ATOM   9220  C CA  . GLN E  1 187 ? 15.153  59.019 103.974 1.00 72.15  ? 187  GLN E CA  1 
ATOM   9221  C C   . GLN E  1 187 ? 14.485  58.363 105.182 1.00 74.15  ? 187  GLN E C   1 
ATOM   9222  O O   . GLN E  1 187 ? 13.771  57.367 105.043 1.00 73.62  ? 187  GLN E O   1 
ATOM   9223  C CB  . GLN E  1 187 ? 16.665  58.733 103.976 1.00 71.24  ? 187  GLN E CB  1 
ATOM   9224  C CG  . GLN E  1 187 ? 17.058  57.280 104.230 1.00 70.45  ? 187  GLN E CG  1 
ATOM   9225  C CD  . GLN E  1 187 ? 16.453  56.312 103.223 1.00 68.38  ? 187  GLN E CD  1 
ATOM   9226  O OE1 . GLN E  1 187 ? 16.508  56.543 102.016 1.00 66.55  ? 187  GLN E OE1 1 
ATOM   9227  N NE2 . GLN E  1 187 ? 15.879  55.219 103.716 1.00 68.82  ? 187  GLN E NE2 1 
ATOM   9228  N N   . THR E  1 188 ? 14.718  58.935 106.361 1.00 76.64  ? 188  THR E N   1 
ATOM   9229  C CA  . THR E  1 188 ? 14.131  58.422 107.595 1.00 78.93  ? 188  THR E CA  1 
ATOM   9230  C C   . THR E  1 188 ? 12.612  58.632 107.626 1.00 80.15  ? 188  THR E C   1 
ATOM   9231  O O   . THR E  1 188 ? 11.867  57.756 108.066 1.00 80.89  ? 188  THR E O   1 
ATOM   9232  C CB  . THR E  1 188 ? 14.757  59.081 108.841 1.00 81.54  ? 188  THR E CB  1 
ATOM   9233  O OG1 . THR E  1 188 ? 14.617  60.505 108.754 1.00 82.70  ? 188  THR E OG1 1 
ATOM   9234  C CG2 . THR E  1 188 ? 16.239  58.720 108.966 1.00 80.71  ? 188  THR E CG2 1 
ATOM   9235  N N   . LYS E  1 189 ? 12.155  59.788 107.153 1.00 80.51  ? 189  LYS E N   1 
ATOM   9236  C CA  . LYS E  1 189 ? 10.722  60.087 107.113 1.00 81.80  ? 189  LYS E CA  1 
ATOM   9237  C C   . LYS E  1 189 ? 9.929   59.048 106.315 1.00 80.13  ? 189  LYS E C   1 
ATOM   9238  O O   . LYS E  1 189 ? 8.835   58.656 106.718 1.00 81.56  ? 189  LYS E O   1 
ATOM   9239  C CB  . LYS E  1 189 ? 10.482  61.484 106.532 1.00 82.08  ? 189  LYS E CB  1 
ATOM   9240  C CG  . LYS E  1 189 ? 9.015   61.811 106.283 1.00 83.13  ? 189  LYS E CG  1 
ATOM   9241  C CD  . LYS E  1 189 ? 8.781   63.309 106.165 1.00 84.54  ? 189  LYS E CD  1 
ATOM   9242  C CE  . LYS E  1 189 ? 7.322   63.636 105.879 1.00 85.66  ? 189  LYS E CE  1 
ATOM   9243  N NZ  . LYS E  1 189 ? 7.046   63.752 104.420 1.00 83.26  ? 189  LYS E NZ  1 
ATOM   9244  N N   . LEU E  1 190 ? 10.487  58.611 105.190 1.00 77.32  ? 190  LEU E N   1 
ATOM   9245  C CA  . LEU E  1 190 ? 9.810   57.673 104.293 1.00 75.68  ? 190  LEU E CA  1 
ATOM   9246  C C   . LEU E  1 190 ? 9.996   56.214 104.701 1.00 75.27  ? 190  LEU E C   1 
ATOM   9247  O O   . LEU E  1 190 ? 9.028   55.453 104.765 1.00 75.80  ? 190  LEU E O   1 
ATOM   9248  C CB  . LEU E  1 190 ? 10.321  57.857 102.864 1.00 73.02  ? 190  LEU E CB  1 
ATOM   9249  C CG  . LEU E  1 190 ? 9.671   59.000 102.086 1.00 73.15  ? 190  LEU E CG  1 
ATOM   9250  C CD1 . LEU E  1 190 ? 10.647  59.623 101.098 1.00 71.25  ? 190  LEU E CD1 1 
ATOM   9251  C CD2 . LEU E  1 190 ? 8.426   58.503 101.371 1.00 72.80  ? 190  LEU E CD2 1 
ATOM   9252  N N   . TYR E  1 191 ? 11.246  55.832 104.951 1.00 74.39  ? 191  TYR E N   1 
ATOM   9253  C CA  . TYR E  1 191 ? 11.612  54.431 105.183 1.00 73.72  ? 191  TYR E CA  1 
ATOM   9254  C C   . TYR E  1 191 ? 12.271  54.174 106.544 1.00 75.50  ? 191  TYR E C   1 
ATOM   9255  O O   . TYR E  1 191 ? 12.468  53.020 106.928 1.00 75.52  ? 191  TYR E O   1 
ATOM   9256  C CB  . TYR E  1 191 ? 12.545  53.964 104.063 1.00 70.89  ? 191  TYR E CB  1 
ATOM   9257  C CG  . TYR E  1 191 ? 12.195  54.548 102.708 1.00 69.15  ? 191  TYR E CG  1 
ATOM   9258  C CD1 . TYR E  1 191 ? 11.147  54.025 101.951 1.00 68.47  ? 191  TYR E CD1 1 
ATOM   9259  C CD2 . TYR E  1 191 ? 12.892  55.641 102.197 1.00 68.39  ? 191  TYR E CD2 1 
ATOM   9260  C CE1 . TYR E  1 191 ? 10.819  54.560 100.715 1.00 67.01  ? 191  TYR E CE1 1 
ATOM   9261  C CE2 . TYR E  1 191 ? 12.568  56.183 100.965 1.00 66.95  ? 191  TYR E CE2 1 
ATOM   9262  C CZ  . TYR E  1 191 ? 11.530  55.638 100.229 1.00 66.24  ? 191  TYR E CZ  1 
ATOM   9263  O OH  . TYR E  1 191 ? 11.202  56.169 99.008  1.00 64.94  ? 191  TYR E OH  1 
ATOM   9264  N N   . GLN E  1 192 ? 12.622  55.246 107.254 1.00 77.08  ? 192  GLN E N   1 
ATOM   9265  C CA  . GLN E  1 192 ? 13.215  55.183 108.597 1.00 79.13  ? 192  GLN E CA  1 
ATOM   9266  C C   . GLN E  1 192 ? 14.658  54.685 108.637 1.00 77.95  ? 192  GLN E C   1 
ATOM   9267  O O   . GLN E  1 192 ? 15.518  55.334 109.233 1.00 78.99  ? 192  GLN E O   1 
ATOM   9268  C CB  . GLN E  1 192 ? 12.347  54.370 109.555 1.00 81.19  ? 192  GLN E CB  1 
ATOM   9269  C CG  . GLN E  1 192 ? 12.460  54.859 110.989 1.00 84.29  ? 192  GLN E CG  1 
ATOM   9270  C CD  . GLN E  1 192 ? 11.423  54.246 111.892 1.00 86.66  ? 192  GLN E CD  1 
ATOM   9271  O OE1 . GLN E  1 192 ? 10.587  54.950 112.454 1.00 89.01  ? 192  GLN E OE1 1 
ATOM   9272  N NE2 . GLN E  1 192 ? 11.459  52.926 112.028 1.00 86.24  ? 192  GLN E NE2 1 
ATOM   9273  N N   . ASN E  1 193 ? 14.919  53.538 108.019 1.00 75.96  ? 193  ASN E N   1 
ATOM   9274  C CA  . ASN E  1 193 ? 16.262  52.959 108.003 1.00 74.88  ? 193  ASN E CA  1 
ATOM   9275  C C   . ASN E  1 193 ? 17.226  53.896 107.268 1.00 73.49  ? 193  ASN E C   1 
ATOM   9276  O O   . ASN E  1 193 ? 16.974  54.257 106.118 1.00 71.71  ? 193  ASN E O   1 
ATOM   9277  C CB  . ASN E  1 193 ? 16.254  51.575 107.339 1.00 73.08  ? 193  ASN E CB  1 
ATOM   9278  C CG  . ASN E  1 193 ? 15.153  50.670 107.876 1.00 74.35  ? 193  ASN E CG  1 
ATOM   9279  O OD1 . ASN E  1 193 ? 14.220  51.132 108.532 1.00 76.32  ? 193  ASN E OD1 1 
ATOM   9280  N ND2 . ASN E  1 193 ? 15.253  49.377 107.591 1.00 73.40  ? 193  ASN E ND2 1 
ATOM   9281  N N   . PRO E  1 194 ? 18.325  54.303 107.934 1.00 74.45  ? 194  PRO E N   1 
ATOM   9282  C CA  . PRO E  1 194 ? 19.222  55.303 107.347 1.00 73.62  ? 194  PRO E CA  1 
ATOM   9283  C C   . PRO E  1 194 ? 19.958  54.785 106.114 1.00 70.87  ? 194  PRO E C   1 
ATOM   9284  O O   . PRO E  1 194 ? 20.056  55.495 105.112 1.00 69.54  ? 194  PRO E O   1 
ATOM   9285  C CB  . PRO E  1 194 ? 20.209  55.604 108.481 1.00 75.65  ? 194  PRO E CB  1 
ATOM   9286  C CG  . PRO E  1 194 ? 20.218  54.377 109.323 1.00 76.49  ? 194  PRO E CG  1 
ATOM   9287  C CD  . PRO E  1 194 ? 18.846  53.772 109.210 1.00 76.35  ? 194  PRO E CD  1 
ATOM   9288  N N   . THR E  1 195 ? 20.457  53.554 106.198 1.00 70.18  ? 195  THR E N   1 
ATOM   9289  C CA  . THR E  1 195 ? 21.191  52.922 105.110 1.00 67.83  ? 195  THR E CA  1 
ATOM   9290  C C   . THR E  1 195 ? 20.331  51.791 104.558 1.00 66.59  ? 195  THR E C   1 
ATOM   9291  O O   . THR E  1 195 ? 19.951  50.881 105.297 1.00 67.55  ? 195  THR E O   1 
ATOM   9292  C CB  . THR E  1 195 ? 22.539  52.364 105.607 1.00 68.20  ? 195  THR E CB  1 
ATOM   9293  O OG1 . THR E  1 195 ? 23.168  53.324 106.464 1.00 70.06  ? 195  THR E OG1 1 
ATOM   9294  C CG2 . THR E  1 195 ? 23.464  52.051 104.439 1.00 66.10  ? 195  THR E CG2 1 
ATOM   9295  N N   . THR E  1 196 ? 20.012  51.861 103.268 1.00 64.62  ? 196  THR E N   1 
ATOM   9296  C CA  . THR E  1 196 ? 19.109  50.895 102.642 1.00 63.55  ? 196  THR E CA  1 
ATOM   9297  C C   . THR E  1 196 ? 19.667  50.363 101.330 1.00 61.29  ? 196  THR E C   1 
ATOM   9298  O O   . THR E  1 196 ? 20.588  50.942 100.753 1.00 60.43  ? 196  THR E O   1 
ATOM   9299  C CB  . THR E  1 196 ? 17.723  51.513 102.376 1.00 63.82  ? 196  THR E CB  1 
ATOM   9300  O OG1 . THR E  1 196 ? 17.865  52.674 101.549 1.00 62.94  ? 196  THR E OG1 1 
ATOM   9301  C CG2 . THR E  1 196 ? 17.047  51.899 103.685 1.00 66.27  ? 196  THR E CG2 1 
ATOM   9302  N N   . TYR E  1 197 ? 19.094  49.255 100.870 1.00 60.52  ? 197  TYR E N   1 
ATOM   9303  C CA  . TYR E  1 197 ? 19.521  48.609 99.636  1.00 58.59  ? 197  TYR E CA  1 
ATOM   9304  C C   . TYR E  1 197 ? 18.355  47.919 98.942  1.00 57.95  ? 197  TYR E C   1 
ATOM   9305  O O   . TYR E  1 197 ? 17.282  47.749 99.525  1.00 59.09  ? 197  TYR E O   1 
ATOM   9306  C CB  . TYR E  1 197 ? 20.599  47.566 99.934  1.00 58.60  ? 197  TYR E CB  1 
ATOM   9307  C CG  . TYR E  1 197 ? 20.082  46.388 100.727 1.00 59.70  ? 197  TYR E CG  1 
ATOM   9308  C CD1 . TYR E  1 197 ? 20.061  46.421 102.119 1.00 61.64  ? 197  TYR E CD1 1 
ATOM   9309  C CD2 . TYR E  1 197 ? 19.603  45.245 100.088 1.00 58.98  ? 197  TYR E CD2 1 
ATOM   9310  C CE1 . TYR E  1 197 ? 19.580  45.349 102.854 1.00 62.82  ? 197  TYR E CE1 1 
ATOM   9311  C CE2 . TYR E  1 197 ? 19.123  44.168 100.812 1.00 60.18  ? 197  TYR E CE2 1 
ATOM   9312  C CZ  . TYR E  1 197 ? 19.113  44.225 102.198 1.00 62.09  ? 197  TYR E CZ  1 
ATOM   9313  O OH  . TYR E  1 197 ? 18.637  43.162 102.926 1.00 63.42  ? 197  TYR E OH  1 
ATOM   9314  N N   . ILE E  1 198 ? 18.584  47.527 97.690  1.00 56.28  ? 198  ILE E N   1 
ATOM   9315  C CA  . ILE E  1 198 ? 17.661  46.673 96.943  1.00 55.68  ? 198  ILE E CA  1 
ATOM   9316  C C   . ILE E  1 198 ? 18.468  45.652 96.158  1.00 54.55  ? 198  ILE E C   1 
ATOM   9317  O O   . ILE E  1 198 ? 19.206  46.015 95.241  1.00 53.31  ? 198  ILE E O   1 
ATOM   9318  C CB  . ILE E  1 198 ? 16.796  47.469 95.946  1.00 54.87  ? 198  ILE E CB  1 
ATOM   9319  C CG1 . ILE E  1 198 ? 16.209  48.710 96.623  1.00 55.97  ? 198  ILE E CG1 1 
ATOM   9320  C CG2 . ILE E  1 198 ? 15.699  46.576 95.372  1.00 54.75  ? 198  ILE E CG2 1 
ATOM   9321  C CD1 . ILE E  1 198 ? 15.225  49.466 95.767  1.00 55.50  ? 198  ILE E CD1 1 
ATOM   9322  N N   . SER E  1 199 ? 18.327  44.379 96.519  1.00 55.13  ? 199  SER E N   1 
ATOM   9323  C CA  . SER E  1 199 ? 19.008  43.308 95.805  1.00 54.33  ? 199  SER E CA  1 
ATOM   9324  C C   . SER E  1 199 ? 18.012  42.553 94.933  1.00 53.94  ? 199  SER E C   1 
ATOM   9325  O O   . SER E  1 199 ? 16.955  42.139 95.406  1.00 54.96  ? 199  SER E O   1 
ATOM   9326  C CB  . SER E  1 199 ? 19.708  42.360 96.782  1.00 55.40  ? 199  SER E CB  1 
ATOM   9327  O OG  . SER E  1 199 ? 18.805  41.846 97.738  1.00 56.90  ? 199  SER E OG  1 
ATOM   9328  N N   . VAL E  1 200 ? 18.357  42.396 93.657  1.00 52.62  ? 200  VAL E N   1 
ATOM   9329  C CA  . VAL E  1 200 ? 17.514  41.699 92.690  1.00 52.27  ? 200  VAL E CA  1 
ATOM   9330  C C   . VAL E  1 200 ? 18.318  40.573 92.048  1.00 51.87  ? 200  VAL E C   1 
ATOM   9331  O O   . VAL E  1 200 ? 19.434  40.791 91.570  1.00 51.07  ? 200  VAL E O   1 
ATOM   9332  C CB  . VAL E  1 200 ? 17.008  42.645 91.581  1.00 51.19  ? 200  VAL E CB  1 
ATOM   9333  C CG1 . VAL E  1 200 ? 15.825  42.022 90.850  1.00 51.32  ? 200  VAL E CG1 1 
ATOM   9334  C CG2 . VAL E  1 200 ? 16.620  43.997 92.163  1.00 51.46  ? 200  VAL E CG2 1 
ATOM   9335  N N   . GLY E  1 201 ? 17.748  39.373 92.037  1.00 52.62  ? 201  GLY E N   1 
ATOM   9336  C CA  . GLY E  1 201 ? 18.435  38.201 91.510  1.00 52.57  ? 201  GLY E CA  1 
ATOM   9337  C C   . GLY E  1 201 ? 17.572  37.415 90.546  1.00 52.64  ? 201  GLY E C   1 
ATOM   9338  O O   . GLY E  1 201 ? 16.358  37.322 90.723  1.00 53.36  ? 201  GLY E O   1 
ATOM   9339  N N   . THR E  1 202 ? 18.208  36.878 89.507  1.00 52.03  ? 202  THR E N   1 
ATOM   9340  C CA  . THR E  1 202 ? 17.605  35.869 88.638  1.00 52.42  ? 202  THR E CA  1 
ATOM   9341  C C   . THR E  1 202 ? 18.685  34.821 88.394  1.00 52.70  ? 202  THR E C   1 
ATOM   9342  O O   . THR E  1 202 ? 19.676  34.771 89.131  1.00 52.88  ? 202  THR E O   1 
ATOM   9343  C CB  . THR E  1 202 ? 17.104  36.461 87.296  1.00 51.41  ? 202  THR E CB  1 
ATOM   9344  O OG1 . THR E  1 202 ? 18.214  36.756 86.438  1.00 50.36  ? 202  THR E OG1 1 
ATOM   9345  C CG2 . THR E  1 202 ? 16.284  37.726 87.524  1.00 51.00  ? 202  THR E CG2 1 
ATOM   9346  N N   . SER E  1 203 ? 18.505  33.982 87.379  1.00 52.91  ? 203  SER E N   1 
ATOM   9347  C CA  . SER E  1 203 ? 19.570  33.077 86.959  1.00 53.19  ? 203  SER E CA  1 
ATOM   9348  C C   . SER E  1 203 ? 20.772  33.873 86.452  1.00 51.98  ? 203  SER E C   1 
ATOM   9349  O O   . SER E  1 203 ? 21.915  33.462 86.644  1.00 52.26  ? 203  SER E O   1 
ATOM   9350  C CB  . SER E  1 203 ? 19.076  32.124 85.873  1.00 53.78  ? 203  SER E CB  1 
ATOM   9351  O OG  . SER E  1 203 ? 18.519  32.842 84.790  1.00 52.86  ? 203  SER E OG  1 
ATOM   9352  N N   . THR E  1 204 ? 20.505  35.015 85.822  1.00 50.79  ? 204  THR E N   1 
ATOM   9353  C CA  . THR E  1 204 ? 21.556  35.855 85.258  1.00 49.75  ? 204  THR E CA  1 
ATOM   9354  C C   . THR E  1 204 ? 21.799  37.116 86.082  1.00 49.16  ? 204  THR E C   1 
ATOM   9355  O O   . THR E  1 204 ? 22.948  37.496 86.310  1.00 48.97  ? 204  THR E O   1 
ATOM   9356  C CB  . THR E  1 204 ? 21.227  36.264 83.807  1.00 48.96  ? 204  THR E CB  1 
ATOM   9357  O OG1 . THR E  1 204 ? 20.018  37.034 83.780  1.00 48.55  ? 204  THR E OG1 1 
ATOM   9358  C CG2 . THR E  1 204 ? 21.064  35.035 82.926  1.00 49.71  ? 204  THR E CG2 1 
ATOM   9359  N N   . LEU E  1 205 ? 20.727  37.764 86.528  1.00 49.08  ? 205  LEU E N   1 
ATOM   9360  C CA  . LEU E  1 205 ? 20.848  39.058 87.197  1.00 48.64  ? 205  LEU E CA  1 
ATOM   9361  C C   . LEU E  1 205 ? 21.453  38.939 88.604  1.00 49.45  ? 205  LEU E C   1 
ATOM   9362  O O   . LEU E  1 205 ? 21.071  38.066 89.385  1.00 50.46  ? 205  LEU E O   1 
ATOM   9363  C CB  . LEU E  1 205 ? 19.484  39.756 87.264  1.00 48.54  ? 205  LEU E CB  1 
ATOM   9364  C CG  . LEU E  1 205 ? 19.479  41.248 87.627  1.00 48.03  ? 205  LEU E CG  1 
ATOM   9365  C CD1 . LEU E  1 205 ? 20.383  42.050 86.697  1.00 47.01  ? 205  LEU E CD1 1 
ATOM   9366  C CD2 . LEU E  1 205 ? 18.060  41.799 87.601  1.00 48.14  ? 205  LEU E CD2 1 
ATOM   9367  N N   . ASN E  1 206 ? 22.411  39.818 88.897  1.00 49.14  ? 206  ASN E N   1 
ATOM   9368  C CA  . ASN E  1 206 ? 23.020  39.929 90.225  1.00 49.95  ? 206  ASN E CA  1 
ATOM   9369  C C   . ASN E  1 206 ? 23.196  41.401 90.584  1.00 49.62  ? 206  ASN E C   1 
ATOM   9370  O O   . ASN E  1 206 ? 24.296  41.955 90.503  1.00 49.40  ? 206  ASN E O   1 
ATOM   9371  C CB  . ASN E  1 206 ? 24.368  39.203 90.270  1.00 50.35  ? 206  ASN E CB  1 
ATOM   9372  C CG  . ASN E  1 206 ? 24.984  39.194 91.660  1.00 51.37  ? 206  ASN E CG  1 
ATOM   9373  O OD1 . ASN E  1 206 ? 24.287  39.343 92.665  1.00 52.04  ? 206  ASN E OD1 1 
ATOM   9374  N ND2 . ASN E  1 206 ? 26.297  39.011 91.722  1.00 51.66  ? 206  ASN E ND2 1 
ATOM   9375  N N   . GLN E  1 207 ? 22.095  42.018 90.991  1.00 49.79  ? 207  GLN E N   1 
ATOM   9376  C CA  . GLN E  1 207 ? 22.033  43.456 91.195  1.00 49.58  ? 207  GLN E CA  1 
ATOM   9377  C C   . GLN E  1 207 ? 21.892  43.808 92.675  1.00 50.74  ? 207  GLN E C   1 
ATOM   9378  O O   . GLN E  1 207 ? 21.270  43.073 93.440  1.00 51.66  ? 207  GLN E O   1 
ATOM   9379  C CB  . GLN E  1 207 ? 20.850  44.010 90.402  1.00 48.96  ? 207  GLN E CB  1 
ATOM   9380  C CG  . GLN E  1 207 ? 20.564  45.488 90.600  1.00 48.88  ? 207  GLN E CG  1 
ATOM   9381  C CD  . GLN E  1 207 ? 19.466  45.979 89.678  1.00 48.30  ? 207  GLN E CD  1 
ATOM   9382  O OE1 . GLN E  1 207 ? 18.369  46.310 90.128  1.00 48.86  ? 207  GLN E OE1 1 
ATOM   9383  N NE2 . GLN E  1 207 ? 19.749  46.009 88.374  1.00 47.30  ? 207  GLN E NE2 1 
ATOM   9384  N N   . ARG E  1 208 ? 22.489  44.930 93.067  1.00 50.87  ? 208  ARG E N   1 
ATOM   9385  C CA  . ARG E  1 208 ? 22.278  45.504 94.394  1.00 52.08  ? 208  ARG E CA  1 
ATOM   9386  C C   . ARG E  1 208 ? 22.346  47.027 94.312  1.00 51.95  ? 208  ARG E C   1 
ATOM   9387  O O   . ARG E  1 208 ? 23.416  47.597 94.087  1.00 51.73  ? 208  ARG E O   1 
ATOM   9388  C CB  . ARG E  1 208 ? 23.306  44.981 95.399  1.00 53.10  ? 208  ARG E CB  1 
ATOM   9389  C CG  . ARG E  1 208 ? 22.838  45.103 96.841  1.00 54.64  ? 208  ARG E CG  1 
ATOM   9390  C CD  . ARG E  1 208 ? 23.992  45.042 97.827  1.00 55.73  ? 208  ARG E CD  1 
ATOM   9391  N NE  . ARG E  1 208 ? 23.519  45.052 99.210  1.00 57.39  ? 208  ARG E NE  1 
ATOM   9392  C CZ  . ARG E  1 208 ? 23.005  44.000 99.850  1.00 58.31  ? 208  ARG E CZ  1 
ATOM   9393  N NH1 . ARG E  1 208 ? 22.883  42.821 99.244  1.00 57.75  ? 208  ARG E NH1 1 
ATOM   9394  N NH2 . ARG E  1 208 ? 22.604  44.126 101.113 1.00 59.97  ? 208  ARG E NH2 1 
ATOM   9395  N N   . LEU E  1 209 ? 21.200  47.677 94.495  1.00 52.25  ? 209  LEU E N   1 
ATOM   9396  C CA  . LEU E  1 209 ? 21.089  49.126 94.355  1.00 52.23  ? 209  LEU E CA  1 
ATOM   9397  C C   . LEU E  1 209 ? 21.077  49.793 95.720  1.00 53.81  ? 209  LEU E C   1 
ATOM   9398  O O   . LEU E  1 209 ? 20.471  49.278 96.654  1.00 54.87  ? 209  LEU E O   1 
ATOM   9399  C CB  . LEU E  1 209 ? 19.799  49.485 93.615  1.00 51.73  ? 209  LEU E CB  1 
ATOM   9400  C CG  . LEU E  1 209 ? 19.570  48.814 92.259  1.00 50.40  ? 209  LEU E CG  1 
ATOM   9401  C CD1 . LEU E  1 209 ? 18.184  49.155 91.733  1.00 50.27  ? 209  LEU E CD1 1 
ATOM   9402  C CD2 . LEU E  1 209 ? 20.649  49.218 91.263  1.00 49.37  ? 209  LEU E CD2 1 
ATOM   9403  N N   . VAL E  1 210 ? 21.753  50.935 95.826  1.00 54.12  ? 210  VAL E N   1 
ATOM   9404  C CA  . VAL E  1 210 ? 21.716  51.760 97.033  1.00 55.78  ? 210  VAL E CA  1 
ATOM   9405  C C   . VAL E  1 210 ? 21.304  53.190 96.655  1.00 55.88  ? 210  VAL E C   1 
ATOM   9406  O O   . VAL E  1 210 ? 21.732  53.700 95.615  1.00 54.82  ? 210  VAL E O   1 
ATOM   9407  C CB  . VAL E  1 210 ? 23.070  51.758 97.790  1.00 56.64  ? 210  VAL E CB  1 
ATOM   9408  C CG1 . VAL E  1 210 ? 23.508  50.331 98.088  1.00 56.60  ? 210  VAL E CG1 1 
ATOM   9409  C CG2 . VAL E  1 210 ? 24.155  52.497 97.013  1.00 55.99  ? 210  VAL E CG2 1 
ATOM   9410  N N   . PRO E  1 211 ? 20.456  53.834 97.484  1.00 57.29  ? 211  PRO E N   1 
ATOM   9411  C CA  . PRO E  1 211 ? 20.062  55.214 97.180  1.00 57.63  ? 211  PRO E CA  1 
ATOM   9412  C C   . PRO E  1 211 ? 21.218  56.208 97.278  1.00 58.17  ? 211  PRO E C   1 
ATOM   9413  O O   . PRO E  1 211 ? 21.928  56.244 98.285  1.00 59.45  ? 211  PRO E O   1 
ATOM   9414  C CB  . PRO E  1 211 ? 19.004  55.532 98.246  1.00 59.38  ? 211  PRO E CB  1 
ATOM   9415  C CG  . PRO E  1 211 ? 18.527  54.213 98.734  1.00 59.51  ? 211  PRO E CG  1 
ATOM   9416  C CD  . PRO E  1 211 ? 19.702  53.290 98.629  1.00 58.68  ? 211  PRO E CD  1 
ATOM   9417  N N   . ARG E  1 212 ? 21.400  56.989 96.220  1.00 57.32  ? 212  ARG E N   1 
ATOM   9418  C CA  . ARG E  1 212 ? 22.369  58.080 96.197  1.00 58.00  ? 212  ARG E CA  1 
ATOM   9419  C C   . ARG E  1 212 ? 21.667  59.385 96.567  1.00 59.42  ? 212  ARG E C   1 
ATOM   9420  O O   . ARG E  1 212 ? 20.736  59.811 95.883  1.00 58.93  ? 212  ARG E O   1 
ATOM   9421  C CB  . ARG E  1 212 ? 23.010  58.200 94.808  1.00 56.45  ? 212  ARG E CB  1 
ATOM   9422  C CG  . ARG E  1 212 ? 23.558  56.889 94.262  1.00 55.06  ? 212  ARG E CG  1 
ATOM   9423  C CD  . ARG E  1 212 ? 24.418  57.102 93.024  1.00 53.99  ? 212  ARG E CD  1 
ATOM   9424  N NE  . ARG E  1 212 ? 23.685  57.757 91.941  1.00 53.20  ? 212  ARG E NE  1 
ATOM   9425  C CZ  . ARG E  1 212 ? 22.808  57.156 91.134  1.00 51.99  ? 212  ARG E CZ  1 
ATOM   9426  N NH1 . ARG E  1 212 ? 22.524  55.863 91.266  1.00 51.42  ? 212  ARG E NH1 1 
ATOM   9427  N NH2 . ARG E  1 212 ? 22.201  57.859 90.185  1.00 51.50  ? 212  ARG E NH2 1 
ATOM   9428  N N   . ILE E  1 213 ? 22.115  60.014 97.652  1.00 61.34  ? 213  ILE E N   1 
ATOM   9429  C CA  . ILE E  1 213 ? 21.529  61.271 98.120  1.00 63.07  ? 213  ILE E CA  1 
ATOM   9430  C C   . ILE E  1 213 ? 22.293  62.464 97.537  1.00 63.40  ? 213  ILE E C   1 
ATOM   9431  O O   . ILE E  1 213 ? 23.526  62.467 97.492  1.00 63.42  ? 213  ILE E O   1 
ATOM   9432  C CB  . ILE E  1 213 ? 21.501  61.338 99.668  1.00 65.31  ? 213  ILE E CB  1 
ATOM   9433  C CG1 . ILE E  1 213 ? 20.584  60.239 100.218 1.00 65.24  ? 213  ILE E CG1 1 
ATOM   9434  C CG2 . ILE E  1 213 ? 21.021  62.704 100.149 1.00 67.33  ? 213  ILE E CG2 1 
ATOM   9435  C CD1 . ILE E  1 213 ? 20.715  60.001 101.707 1.00 67.29  ? 213  ILE E CD1 1 
ATOM   9436  N N   . ALA E  1 214 ? 21.544  63.464 97.080  1.00 63.81  ? 214  ALA E N   1 
ATOM   9437  C CA  . ALA E  1 214 ? 22.118  64.702 96.557  1.00 64.44  ? 214  ALA E CA  1 
ATOM   9438  C C   . ALA E  1 214 ? 21.060  65.801 96.521  1.00 65.61  ? 214  ALA E C   1 
ATOM   9439  O O   . ALA E  1 214 ? 19.862  65.519 96.450  1.00 65.26  ? 214  ALA E O   1 
ATOM   9440  C CB  . ALA E  1 214 ? 22.690  64.476 95.163  1.00 62.47  ? 214  ALA E CB  1 
ATOM   9441  N N   . THR E  1 215 ? 21.511  67.051 96.580  1.00 67.18  ? 215  THR E N   1 
ATOM   9442  C CA  . THR E  1 215 ? 20.623  68.200 96.437  1.00 68.39  ? 215  THR E CA  1 
ATOM   9443  C C   . THR E  1 215 ? 20.445  68.460 94.949  1.00 66.75  ? 215  THR E C   1 
ATOM   9444  O O   . THR E  1 215 ? 21.418  68.700 94.236  1.00 66.15  ? 215  THR E O   1 
ATOM   9445  C CB  . THR E  1 215 ? 21.193  69.458 97.123  1.00 70.98  ? 215  THR E CB  1 
ATOM   9446  O OG1 . THR E  1 215 ? 21.713  69.113 98.412  1.00 72.40  ? 215  THR E OG1 1 
ATOM   9447  C CG2 . THR E  1 215 ? 20.111  70.524 97.281  1.00 72.69  ? 215  THR E CG2 1 
ATOM   9448  N N   . ARG E  1 216 ? 19.205  68.398 94.479  1.00 66.15  ? 216  ARG E N   1 
ATOM   9449  C CA  . ARG E  1 216 ? 18.930  68.454 93.050  1.00 64.48  ? 216  ARG E CA  1 
ATOM   9450  C C   . ARG E  1 216 ? 17.928  69.547 92.724  1.00 65.62  ? 216  ARG E C   1 
ATOM   9451  O O   . ARG E  1 216 ? 17.131  69.949 93.573  1.00 67.31  ? 216  ARG E O   1 
ATOM   9452  C CB  . ARG E  1 216 ? 18.400  67.103 92.572  1.00 62.38  ? 216  ARG E CB  1 
ATOM   9453  C CG  . ARG E  1 216 ? 19.371  65.952 92.782  1.00 61.23  ? 216  ARG E CG  1 
ATOM   9454  C CD  . ARG E  1 216 ? 18.711  64.613 92.506  1.00 59.60  ? 216  ARG E CD  1 
ATOM   9455  N NE  . ARG E  1 216 ? 17.981  64.100 93.669  1.00 60.58  ? 216  ARG E NE  1 
ATOM   9456  C CZ  . ARG E  1 216 ? 18.464  63.241 94.571  1.00 60.77  ? 216  ARG E CZ  1 
ATOM   9457  N NH1 . ARG E  1 216 ? 19.703  62.766 94.485  1.00 60.05  ? 216  ARG E NH1 1 
ATOM   9458  N NH2 . ARG E  1 216 ? 17.694  62.848 95.580  1.00 61.84  ? 216  ARG E NH2 1 
ATOM   9459  N N   . SER E  1 217 ? 17.981  70.023 91.483  1.00 64.81  ? 217  SER E N   1 
ATOM   9460  C CA  . SER E  1 217 ? 17.041  71.025 90.999  1.00 65.77  ? 217  SER E CA  1 
ATOM   9461  C C   . SER E  1 217 ? 15.646  70.417 90.899  1.00 65.24  ? 217  SER E C   1 
ATOM   9462  O O   . SER E  1 217 ? 15.501  69.217 90.659  1.00 63.51  ? 217  SER E O   1 
ATOM   9463  C CB  . SER E  1 217 ? 17.482  71.555 89.633  1.00 64.88  ? 217  SER E CB  1 
ATOM   9464  O OG  . SER E  1 217 ? 18.856  71.905 89.645  1.00 65.24  ? 217  SER E OG  1 
ATOM   9465  N N   . LYS E  1 218 ? 14.626  71.245 91.101  1.00 66.95  ? 218  LYS E N   1 
ATOM   9466  C CA  . LYS E  1 218 ? 13.242  70.797 90.979  1.00 66.81  ? 218  LYS E CA  1 
ATOM   9467  C C   . LYS E  1 218 ? 12.901  70.535 89.523  1.00 64.91  ? 218  LYS E C   1 
ATOM   9468  O O   . LYS E  1 218 ? 13.041  71.414 88.675  1.00 65.07  ? 218  LYS E O   1 
ATOM   9469  C CB  . LYS E  1 218 ? 12.264  71.826 91.558  1.00 69.42  ? 218  LYS E CB  1 
ATOM   9470  C CG  . LYS E  1 218 ? 11.890  71.573 93.008  1.00 71.22  ? 218  LYS E CG  1 
ATOM   9471  C CD  . LYS E  1 218 ? 11.501  72.857 93.720  1.00 74.31  ? 218  LYS E CD  1 
ATOM   9472  C CE  . LYS E  1 218 ? 11.183  72.607 95.186  1.00 76.33  ? 218  LYS E CE  1 
ATOM   9473  N NZ  . LYS E  1 218 ? 11.858  73.604 96.061  1.00 78.87  ? 218  LYS E NZ  1 
ATOM   9474  N N   . VAL E  1 219 ? 12.481  69.308 89.245  1.00 63.23  ? 219  VAL E N   1 
ATOM   9475  C CA  . VAL E  1 219 ? 11.928  68.943 87.956  1.00 61.68  ? 219  VAL E CA  1 
ATOM   9476  C C   . VAL E  1 219 ? 10.511  68.459 88.242  1.00 62.16  ? 219  VAL E C   1 
ATOM   9477  O O   . VAL E  1 219 ? 10.310  67.617 89.114  1.00 62.26  ? 219  VAL E O   1 
ATOM   9478  C CB  . VAL E  1 219 ? 12.780  67.846 87.286  1.00 59.42  ? 219  VAL E CB  1 
ATOM   9479  C CG1 . VAL E  1 219 ? 12.112  67.327 86.019  1.00 58.03  ? 219  VAL E CG1 1 
ATOM   9480  C CG2 . VAL E  1 219 ? 14.175  68.380 86.980  1.00 59.16  ? 219  VAL E CG2 1 
ATOM   9481  N N   . ASN E  1 220 ? 9.529   69.019 87.537  1.00 62.64  ? 220  ASN E N   1 
ATOM   9482  C CA  . ASN E  1 220 ? 8.113   68.760 87.828  1.00 63.61  ? 220  ASN E CA  1 
ATOM   9483  C C   . ASN E  1 220 ? 7.761   68.963 89.309  1.00 65.64  ? 220  ASN E C   1 
ATOM   9484  O O   . ASN E  1 220 ? 6.979   68.201 89.883  1.00 66.07  ? 220  ASN E O   1 
ATOM   9485  C CB  . ASN E  1 220 ? 7.711   67.350 87.371  1.00 61.98  ? 220  ASN E CB  1 
ATOM   9486  C CG  . ASN E  1 220 ? 7.516   67.252 85.870  1.00 60.64  ? 220  ASN E CG  1 
ATOM   9487  O OD1 . ASN E  1 220 ? 8.060   68.048 85.101  1.00 60.37  ? 220  ASN E OD1 1 
ATOM   9488  N ND2 . ASN E  1 220 ? 6.731   66.267 85.445  1.00 59.95  ? 220  ASN E ND2 1 
ATOM   9489  N N   . GLY E  1 221 ? 8.347   69.991 89.919  1.00 67.07  ? 221  GLY E N   1 
ATOM   9490  C CA  . GLY E  1 221 ? 8.058   70.343 91.309  1.00 69.35  ? 221  GLY E CA  1 
ATOM   9491  C C   . GLY E  1 221 ? 8.640   69.408 92.357  1.00 69.09  ? 221  GLY E C   1 
ATOM   9492  O O   . GLY E  1 221 ? 8.268   69.484 93.527  1.00 70.97  ? 221  GLY E O   1 
ATOM   9493  N N   . GLN E  1 222 ? 9.557   68.533 91.947  1.00 66.92  ? 222  GLN E N   1 
ATOM   9494  C CA  . GLN E  1 222 ? 10.170  67.566 92.856  1.00 66.57  ? 222  GLN E CA  1 
ATOM   9495  C C   . GLN E  1 222 ? 11.672  67.483 92.619  1.00 65.16  ? 222  GLN E C   1 
ATOM   9496  O O   . GLN E  1 222 ? 12.123  67.448 91.475  1.00 63.49  ? 222  GLN E O   1 
ATOM   9497  C CB  . GLN E  1 222 ? 9.537   66.181 92.670  1.00 65.39  ? 222  GLN E CB  1 
ATOM   9498  C CG  . GLN E  1 222 ? 8.046   66.118 92.986  1.00 66.95  ? 222  GLN E CG  1 
ATOM   9499  C CD  . GLN E  1 222 ? 7.719   66.515 94.420  1.00 69.63  ? 222  GLN E CD  1 
ATOM   9500  O OE1 . GLN E  1 222 ? 8.472   66.212 95.346  1.00 70.13  ? 222  GLN E OE1 1 
ATOM   9501  N NE2 . GLN E  1 222 ? 6.591   67.194 94.609  1.00 71.57  ? 222  GLN E NE2 1 
ATOM   9502  N N   . SER E  1 223 ? 12.438  67.458 93.709  1.00 65.97  ? 223  SER E N   1 
ATOM   9503  C CA  . SER E  1 223 ? 13.896  67.316 93.645  1.00 64.95  ? 223  SER E CA  1 
ATOM   9504  C C   . SER E  1 223 ? 14.347  65.872 93.915  1.00 63.44  ? 223  SER E C   1 
ATOM   9505  O O   . SER E  1 223 ? 15.525  65.548 93.761  1.00 62.45  ? 223  SER E O   1 
ATOM   9506  C CB  . SER E  1 223 ? 14.567  68.288 94.621  1.00 67.06  ? 223  SER E CB  1 
ATOM   9507  O OG  . SER E  1 223 ? 14.532  69.613 94.126  1.00 68.06  ? 223  SER E OG  1 
ATOM   9508  N N   . GLY E  1 224 ? 13.409  65.015 94.318  1.00 63.42  ? 224  GLY E N   1 
ATOM   9509  C CA  . GLY E  1 224 ? 13.670  63.583 94.458  1.00 62.04  ? 224  GLY E CA  1 
ATOM   9510  C C   . GLY E  1 224 ? 13.704  62.904 93.102  1.00 59.69  ? 224  GLY E C   1 
ATOM   9511  O O   . GLY E  1 224 ? 13.106  63.396 92.140  1.00 59.26  ? 224  GLY E O   1 
ATOM   9512  N N   . ARG E  1 225 ? 14.397  61.769 93.026  1.00 58.27  ? 225  ARG E N   1 
ATOM   9513  C CA  . ARG E  1 225 ? 14.578  61.052 91.761  1.00 56.17  ? 225  ARG E CA  1 
ATOM   9514  C C   . ARG E  1 225 ? 14.165  59.583 91.856  1.00 55.39  ? 225  ARG E C   1 
ATOM   9515  O O   . ARG E  1 225 ? 14.299  58.955 92.905  1.00 56.09  ? 225  ARG E O   1 
ATOM   9516  C CB  . ARG E  1 225 ? 16.035  61.152 91.298  1.00 55.20  ? 225  ARG E CB  1 
ATOM   9517  C CG  . ARG E  1 225 ? 16.492  62.562 90.955  1.00 55.81  ? 225  ARG E CG  1 
ATOM   9518  C CD  . ARG E  1 225 ? 15.886  63.055 89.650  1.00 55.06  ? 225  ARG E CD  1 
ATOM   9519  N NE  . ARG E  1 225 ? 16.330  64.409 89.307  1.00 55.78  ? 225  ARG E NE  1 
ATOM   9520  C CZ  . ARG E  1 225 ? 15.760  65.540 89.729  1.00 57.43  ? 225  ARG E CZ  1 
ATOM   9521  N NH1 . ARG E  1 225 ? 14.697  65.523 90.532  1.00 58.61  ? 225  ARG E NH1 1 
ATOM   9522  N NH2 . ARG E  1 225 ? 16.262  66.710 89.342  1.00 58.09  ? 225  ARG E NH2 1 
ATOM   9523  N N   . MET E  1 226 ? 13.655  59.053 90.748  1.00 54.09  ? 226  MET E N   1 
ATOM   9524  C CA  . MET E  1 226 ? 13.318  57.641 90.631  1.00 53.31  ? 226  MET E CA  1 
ATOM   9525  C C   . MET E  1 226 ? 14.114  57.056 89.478  1.00 51.49  ? 226  MET E C   1 
ATOM   9526  O O   . MET E  1 226 ? 14.027  57.541 88.355  1.00 50.76  ? 226  MET E O   1 
ATOM   9527  C CB  . MET E  1 226 ? 11.824  57.465 90.357  1.00 53.79  ? 226  MET E CB  1 
ATOM   9528  C CG  . MET E  1 226 ? 10.932  57.734 91.557  1.00 55.74  ? 226  MET E CG  1 
ATOM   9529  S SD  . MET E  1 226 ? 10.836  56.349 92.708  1.00 56.41  ? 226  MET E SD  1 
ATOM   9530  C CE  . MET E  1 226 ? 9.618   56.976 93.859  1.00 58.92  ? 226  MET E CE  1 
ATOM   9531  N N   . GLU E  1 227 ? 14.889  56.015 89.758  1.00 47.71  ? 227  GLU E N   1 
ATOM   9532  C CA  . GLU E  1 227 ? 15.698  55.363 88.741  1.00 45.61  ? 227  GLU E CA  1 
ATOM   9533  C C   . GLU E  1 227 ? 15.110  53.988 88.461  1.00 45.07  ? 227  GLU E C   1 
ATOM   9534  O O   . GLU E  1 227 ? 15.007  53.162 89.366  1.00 46.08  ? 227  GLU E O   1 
ATOM   9535  C CB  . GLU E  1 227 ? 17.144  55.252 89.216  1.00 45.70  ? 227  GLU E CB  1 
ATOM   9536  C CG  . GLU E  1 227 ? 18.131  54.908 88.114  1.00 43.94  ? 227  GLU E CG  1 
ATOM   9537  C CD  . GLU E  1 227 ? 19.576  55.023 88.561  1.00 44.49  ? 227  GLU E CD  1 
ATOM   9538  O OE1 . GLU E  1 227 ? 19.825  55.299 89.757  1.00 46.21  ? 227  GLU E OE1 1 
ATOM   9539  O OE2 . GLU E  1 227 ? 20.469  54.837 87.706  1.00 43.44  ? 227  GLU E OE2 1 
ATOM   9540  N N   . PHE E  1 228 ? 14.721  53.753 87.208  1.00 43.67  ? 228  PHE E N   1 
ATOM   9541  C CA  . PHE E  1 228 ? 13.988  52.542 86.842  1.00 43.54  ? 228  PHE E CA  1 
ATOM   9542  C C   . PHE E  1 228 ? 14.860  51.533 86.103  1.00 42.20  ? 228  PHE E C   1 
ATOM   9543  O O   . PHE E  1 228 ? 15.645  51.895 85.226  1.00 40.91  ? 228  PHE E O   1 
ATOM   9544  C CB  . PHE E  1 228 ? 12.754  52.906 86.018  1.00 43.60  ? 228  PHE E CB  1 
ATOM   9545  C CG  . PHE E  1 228 ? 11.714  53.647 86.808  1.00 45.44  ? 228  PHE E CG  1 
ATOM   9546  C CD1 . PHE E  1 228 ? 10.806  52.956 87.599  1.00 47.17  ? 228  PHE E CD1 1 
ATOM   9547  C CD2 . PHE E  1 228 ? 11.664  55.035 86.792  1.00 45.73  ? 228  PHE E CD2 1 
ATOM   9548  C CE1 . PHE E  1 228 ? 9.854   53.632 88.343  1.00 49.21  ? 228  PHE E CE1 1 
ATOM   9549  C CE2 . PHE E  1 228 ? 10.715  55.718 87.534  1.00 47.77  ? 228  PHE E CE2 1 
ATOM   9550  C CZ  . PHE E  1 228 ? 9.809   55.015 88.312  1.00 49.55  ? 228  PHE E CZ  1 
ATOM   9551  N N   . PHE E  1 229 ? 14.711  50.267 86.485  1.00 42.76  ? 229  PHE E N   1 
ATOM   9552  C CA  . PHE E  1 229 ? 15.490  49.168 85.925  1.00 42.00  ? 229  PHE E CA  1 
ATOM   9553  C C   . PHE E  1 229 ? 14.565  48.087 85.388  1.00 42.39  ? 229  PHE E C   1 
ATOM   9554  O O   . PHE E  1 229 ? 13.386  48.015 85.759  1.00 43.52  ? 229  PHE E O   1 
ATOM   9555  C CB  . PHE E  1 229 ? 16.410  48.575 86.991  1.00 42.72  ? 229  PHE E CB  1 
ATOM   9556  C CG  . PHE E  1 229 ? 17.454  49.531 87.484  1.00 42.67  ? 229  PHE E CG  1 
ATOM   9557  C CD1 . PHE E  1 229 ? 17.136  50.502 88.426  1.00 43.68  ? 229  PHE E CD1 1 
ATOM   9558  C CD2 . PHE E  1 229 ? 18.757  49.465 87.006  1.00 41.98  ? 229  PHE E CD2 1 
ATOM   9559  C CE1 . PHE E  1 229 ? 18.096  51.390 88.883  1.00 44.00  ? 229  PHE E CE1 1 
ATOM   9560  C CE2 . PHE E  1 229 ? 19.722  50.349 87.461  1.00 42.31  ? 229  PHE E CE2 1 
ATOM   9561  C CZ  . PHE E  1 229 ? 19.391  51.313 88.401  1.00 43.33  ? 229  PHE E CZ  1 
ATOM   9562  N N   . TRP E  1 230 ? 15.108  47.245 84.515  1.00 41.74  ? 230  TRP E N   1 
ATOM   9563  C CA  . TRP E  1 230 ? 14.329  46.182 83.902  1.00 42.35  ? 230  TRP E CA  1 
ATOM   9564  C C   . TRP E  1 230 ? 15.152  44.930 83.640  1.00 42.47  ? 230  TRP E C   1 
ATOM   9565  O O   . TRP E  1 230 ? 16.379  44.950 83.694  1.00 41.88  ? 230  TRP E O   1 
ATOM   9566  C CB  . TRP E  1 230 ? 13.712  46.678 82.597  1.00 41.69  ? 230  TRP E CB  1 
ATOM   9567  C CG  . TRP E  1 230 ? 14.711  47.116 81.572  1.00 40.19  ? 230  TRP E CG  1 
ATOM   9568  C CD1 . TRP E  1 230 ? 15.252  48.360 81.438  1.00 39.14  ? 230  TRP E CD1 1 
ATOM   9569  C CD2 . TRP E  1 230 ? 15.279  46.317 80.528  1.00 39.87  ? 230  TRP E CD2 1 
ATOM   9570  N NE1 . TRP E  1 230 ? 16.124  48.387 80.380  1.00 38.14  ? 230  TRP E NE1 1 
ATOM   9571  C CE2 . TRP E  1 230 ? 16.161  47.145 79.804  1.00 38.58  ? 230  TRP E CE2 1 
ATOM   9572  C CE3 . TRP E  1 230 ? 15.129  44.980 80.135  1.00 40.81  ? 230  TRP E CE3 1 
ATOM   9573  C CZ2 . TRP E  1 230 ? 16.890  46.683 78.705  1.00 38.22  ? 230  TRP E CZ2 1 
ATOM   9574  C CZ3 . TRP E  1 230 ? 15.858  44.520 79.041  1.00 40.49  ? 230  TRP E CZ3 1 
ATOM   9575  C CH2 . TRP E  1 230 ? 16.727  45.370 78.341  1.00 39.20  ? 230  TRP E CH2 1 
ATOM   9576  N N   . THR E  1 231 ? 14.448  43.836 83.377  1.00 43.59  ? 231  THR E N   1 
ATOM   9577  C CA  . THR E  1 231 ? 15.070  42.600 82.930  1.00 44.05  ? 231  THR E CA  1 
ATOM   9578  C C   . THR E  1 231 ? 14.066  41.797 82.120  1.00 45.19  ? 231  THR E C   1 
ATOM   9579  O O   . THR E  1 231 ? 12.867  42.073 82.154  1.00 45.88  ? 231  THR E O   1 
ATOM   9580  C CB  . THR E  1 231 ? 15.568  41.749 84.116  1.00 45.09  ? 231  THR E CB  1 
ATOM   9581  O OG1 . THR E  1 231 ? 16.378  40.673 83.630  1.00 45.51  ? 231  THR E OG1 1 
ATOM   9582  C CG2 . THR E  1 231 ? 14.399  41.179 84.921  1.00 46.73  ? 231  THR E CG2 1 
ATOM   9583  N N   . ILE E  1 232 ? 14.566  40.816 81.380  1.00 45.72  ? 232  ILE E N   1 
ATOM   9584  C CA  . ILE E  1 232 ? 13.712  39.822 80.740  1.00 47.40  ? 232  ILE E CA  1 
ATOM   9585  C C   . ILE E  1 232 ? 13.848  38.551 81.559  1.00 49.11  ? 232  ILE E C   1 
ATOM   9586  O O   . ILE E  1 232 ? 14.928  37.974 81.648  1.00 49.12  ? 232  ILE E O   1 
ATOM   9587  C CB  . ILE E  1 232 ? 14.079  39.600 79.251  1.00 47.20  ? 232  ILE E CB  1 
ATOM   9588  C CG1 . ILE E  1 232 ? 13.190  40.458 78.345  1.00 46.74  ? 232  ILE E CG1 1 
ATOM   9589  C CG2 . ILE E  1 232 ? 13.887  38.144 78.832  1.00 49.31  ? 232  ILE E CG2 1 
ATOM   9590  C CD1 . ILE E  1 232 ? 13.162  41.930 78.688  1.00 45.03  ? 232  ILE E CD1 1 
ATOM   9591  N N   . LEU E  1 233 ? 12.747  38.143 82.181  1.00 50.77  ? 233  LEU E N   1 
ATOM   9592  C CA  . LEU E  1 233 ? 12.721  36.938 82.993  1.00 52.66  ? 233  LEU E CA  1 
ATOM   9593  C C   . LEU E  1 233 ? 12.287  35.765 82.118  1.00 54.68  ? 233  LEU E C   1 
ATOM   9594  O O   . LEU E  1 233 ? 11.156  35.726 81.633  1.00 55.87  ? 233  LEU E O   1 
ATOM   9595  C CB  . LEU E  1 233 ? 11.767  37.124 84.174  1.00 53.65  ? 233  LEU E CB  1 
ATOM   9596  C CG  . LEU E  1 233 ? 11.702  36.009 85.221  1.00 55.54  ? 233  LEU E CG  1 
ATOM   9597  C CD1 . LEU E  1 233 ? 13.053  35.787 85.887  1.00 54.79  ? 233  LEU E CD1 1 
ATOM   9598  C CD2 . LEU E  1 233 ? 10.639  36.349 86.252  1.00 56.65  ? 233  LEU E CD2 1 
ATOM   9599  N N   . LYS E  1 234 ? 13.200  34.823 81.910  1.00 55.39  ? 234  LYS E N   1 
ATOM   9600  C CA  . LYS E  1 234 ? 12.938  33.667 81.054  1.00 57.62  ? 234  LYS E CA  1 
ATOM   9601  C C   . LYS E  1 234 ? 11.980  32.686 81.728  1.00 60.34  ? 234  LYS E C   1 
ATOM   9602  O O   . LYS E  1 234 ? 11.791  32.749 82.946  1.00 60.45  ? 234  LYS E O   1 
ATOM   9603  C CB  . LYS E  1 234 ? 14.256  32.976 80.687  1.00 57.77  ? 234  LYS E CB  1 
ATOM   9604  C CG  . LYS E  1 234 ? 15.068  33.754 79.661  1.00 55.95  ? 234  LYS E CG  1 
ATOM   9605  C CD  . LYS E  1 234 ? 16.458  33.174 79.472  1.00 56.24  ? 234  LYS E CD  1 
ATOM   9606  C CE  . LYS E  1 234 ? 17.112  33.735 78.219  1.00 55.20  ? 234  LYS E CE  1 
ATOM   9607  N NZ  . LYS E  1 234 ? 18.482  33.195 78.006  1.00 55.82  ? 234  LYS E NZ  1 
ATOM   9608  N N   . PRO E  1 235 ? 11.358  31.783 80.942  1.00 62.81  ? 235  PRO E N   1 
ATOM   9609  C CA  . PRO E  1 235 ? 10.393  30.857 81.535  1.00 65.71  ? 235  PRO E CA  1 
ATOM   9610  C C   . PRO E  1 235 ? 11.051  29.890 82.511  1.00 66.82  ? 235  PRO E C   1 
ATOM   9611  O O   . PRO E  1 235 ? 12.213  29.521 82.321  1.00 66.33  ? 235  PRO E O   1 
ATOM   9612  C CB  . PRO E  1 235 ? 9.831   30.091 80.327  1.00 68.14  ? 235  PRO E CB  1 
ATOM   9613  C CG  . PRO E  1 235 ? 10.285  30.827 79.117  1.00 66.33  ? 235  PRO E CG  1 
ATOM   9614  C CD  . PRO E  1 235 ? 11.550  31.521 79.505  1.00 63.35  ? 235  PRO E CD  1 
ATOM   9615  N N   . ASN E  1 236 ? 10.312  29.502 83.550  1.00 68.53  ? 236  ASN E N   1 
ATOM   9616  C CA  . ASN E  1 236 ? 10.785  28.535 84.542  1.00 69.96  ? 236  ASN E CA  1 
ATOM   9617  C C   . ASN E  1 236 ? 11.874  29.115 85.458  1.00 67.63  ? 236  ASN E C   1 
ATOM   9618  O O   . ASN E  1 236 ? 12.478  28.385 86.244  1.00 68.60  ? 236  ASN E O   1 
ATOM   9619  C CB  . ASN E  1 236 ? 11.293  27.257 83.840  1.00 72.15  ? 236  ASN E CB  1 
ATOM   9620  C CG  . ASN E  1 236 ? 10.691  25.981 84.406  1.00 75.69  ? 236  ASN E CG  1 
ATOM   9621  O OD1 . ASN E  1 236 ? 10.201  25.946 85.533  1.00 76.57  ? 236  ASN E OD1 1 
ATOM   9622  N ND2 . ASN E  1 236 ? 10.726  24.919 83.611  1.00 78.21  ? 236  ASN E ND2 1 
ATOM   9623  N N   . ASP E  1 237 ? 12.107  30.425 85.358  1.00 64.87  ? 237  ASP E N   1 
ATOM   9624  C CA  . ASP E  1 237 ? 13.109  31.119 86.165  1.00 62.78  ? 237  ASP E CA  1 
ATOM   9625  C C   . ASP E  1 237 ? 12.396  32.084 87.106  1.00 62.04  ? 237  ASP E C   1 
ATOM   9626  O O   . ASP E  1 237 ? 11.313  32.587 86.791  1.00 62.24  ? 237  ASP E O   1 
ATOM   9627  C CB  . ASP E  1 237 ? 14.089  31.884 85.264  1.00 60.47  ? 237  ASP E CB  1 
ATOM   9628  C CG  . ASP E  1 237 ? 15.281  32.463 86.032  1.00 58.87  ? 237  ASP E CG  1 
ATOM   9629  O OD1 . ASP E  1 237 ? 15.703  31.862 87.045  1.00 59.88  ? 237  ASP E OD1 1 
ATOM   9630  O OD2 . ASP E  1 237 ? 15.801  33.522 85.610  1.00 56.76  ? 237  ASP E OD2 1 
ATOM   9631  N N   . ALA E  1 238 ? 13.011  32.338 88.257  1.00 61.44  ? 238  ALA E N   1 
ATOM   9632  C CA  . ALA E  1 238 ? 12.414  33.174 89.288  1.00 61.19  ? 238  ALA E CA  1 
ATOM   9633  C C   . ALA E  1 238 ? 13.211  34.455 89.500  1.00 58.77  ? 238  ALA E C   1 
ATOM   9634  O O   . ALA E  1 238 ? 14.435  34.465 89.345  1.00 57.71  ? 238  ALA E O   1 
ATOM   9635  C CB  . ALA E  1 238 ? 12.315  32.396 90.592  1.00 63.12  ? 238  ALA E CB  1 
ATOM   9636  N N   . ILE E  1 239 ? 12.509  35.532 89.851  1.00 58.18  ? 239  ILE E N   1 
ATOM   9637  C CA  . ILE E  1 239 ? 13.155  36.786 90.250  1.00 56.37  ? 239  ILE E CA  1 
ATOM   9638  C C   . ILE E  1 239 ? 13.002  36.990 91.764  1.00 57.43  ? 239  ILE E C   1 
ATOM   9639  O O   . ILE E  1 239 ? 11.928  36.762 92.319  1.00 59.14  ? 239  ILE E O   1 
ATOM   9640  C CB  . ILE E  1 239 ? 12.619  38.003 89.454  1.00 54.95  ? 239  ILE E CB  1 
ATOM   9641  C CG1 . ILE E  1 239 ? 13.478  39.241 89.731  1.00 53.20  ? 239  ILE E CG1 1 
ATOM   9642  C CG2 . ILE E  1 239 ? 11.152  38.289 89.766  1.00 56.35  ? 239  ILE E CG2 1 
ATOM   9643  C CD1 . ILE E  1 239 ? 13.400  40.293 88.647  1.00 51.49  ? 239  ILE E CD1 1 
ATOM   9644  N N   . ASN E  1 240 ? 14.086  37.404 92.420  1.00 56.69  ? 240  ASN E N   1 
ATOM   9645  C CA  . ASN E  1 240 ? 14.116  37.563 93.874  1.00 57.87  ? 240  ASN E CA  1 
ATOM   9646  C C   . ASN E  1 240 ? 14.449  38.992 94.288  1.00 56.83  ? 240  ASN E C   1 
ATOM   9647  O O   . ASN E  1 240 ? 15.504  39.511 93.931  1.00 55.40  ? 240  ASN E O   1 
ATOM   9648  C CB  . ASN E  1 240 ? 15.155  36.628 94.487  1.00 58.68  ? 240  ASN E CB  1 
ATOM   9649  C CG  . ASN E  1 240 ? 14.866  35.165 94.210  1.00 60.10  ? 240  ASN E CG  1 
ATOM   9650  O OD1 . ASN E  1 240 ? 13.753  34.689 94.433  1.00 61.66  ? 240  ASN E OD1 1 
ATOM   9651  N ND2 . ASN E  1 240 ? 15.874  34.440 93.730  1.00 59.91  ? 240  ASN E ND2 1 
ATOM   9652  N N   . PHE E  1 241 ? 13.554  39.606 95.059  1.00 57.84  ? 241  PHE E N   1 
ATOM   9653  C CA  . PHE E  1 241 ? 13.754  40.955 95.581  1.00 57.43  ? 241  PHE E CA  1 
ATOM   9654  C C   . PHE E  1 241 ? 14.001  40.930 97.085  1.00 59.17  ? 241  PHE E C   1 
ATOM   9655  O O   . PHE E  1 241 ? 13.306  40.228 97.818  1.00 61.04  ? 241  PHE E O   1 
ATOM   9656  C CB  . PHE E  1 241 ? 12.528  41.817 95.292  1.00 57.62  ? 241  PHE E CB  1 
ATOM   9657  C CG  . PHE E  1 241 ? 12.355  42.151 93.844  1.00 55.87  ? 241  PHE E CG  1 
ATOM   9658  C CD1 . PHE E  1 241 ? 13.032  43.224 93.283  1.00 54.09  ? 241  PHE E CD1 1 
ATOM   9659  C CD2 . PHE E  1 241 ? 11.522  41.390 93.037  1.00 56.22  ? 241  PHE E CD2 1 
ATOM   9660  C CE1 . PHE E  1 241 ? 12.877  43.539 91.944  1.00 52.57  ? 241  PHE E CE1 1 
ATOM   9661  C CE2 . PHE E  1 241 ? 11.362  41.698 91.696  1.00 54.81  ? 241  PHE E CE2 1 
ATOM   9662  C CZ  . PHE E  1 241 ? 12.042  42.774 91.147  1.00 52.91  ? 241  PHE E CZ  1 
ATOM   9663  N N   . GLU E  1 242 ? 14.995  41.692 97.534  1.00 58.75  ? 242  GLU E N   1 
ATOM   9664  C CA  . GLU E  1 242 ? 15.194  41.954 98.959  1.00 60.57  ? 242  GLU E CA  1 
ATOM   9665  C C   . GLU E  1 242 ? 15.537  43.430 99.160  1.00 60.27  ? 242  GLU E C   1 
ATOM   9666  O O   . GLU E  1 242 ? 16.466  43.944 98.532  1.00 58.77  ? 242  GLU E O   1 
ATOM   9667  C CB  . GLU E  1 242 ? 16.295  41.059 99.541  1.00 61.23  ? 242  GLU E CB  1 
ATOM   9668  C CG  . GLU E  1 242 ? 16.482  41.187 101.049 1.00 63.48  ? 242  GLU E CG  1 
ATOM   9669  C CD  . GLU E  1 242 ? 17.640  40.355 101.575 1.00 64.22  ? 242  GLU E CD  1 
ATOM   9670  O OE1 . GLU E  1 242 ? 17.665  39.129 101.333 1.00 64.33  ? 242  GLU E OE1 1 
ATOM   9671  O OE2 . GLU E  1 242 ? 18.524  40.925 102.246 1.00 64.97  ? 242  GLU E OE2 1 
ATOM   9672  N N   . SER E  1 243 ? 14.782  44.108 100.024 1.00 61.93  ? 243  SER E N   1 
ATOM   9673  C CA  . SER E  1 243 ? 15.032  45.519 100.317 1.00 62.17  ? 243  SER E CA  1 
ATOM   9674  C C   . SER E  1 243 ? 14.541  45.939 101.701 1.00 64.94  ? 243  SER E C   1 
ATOM   9675  O O   . SER E  1 243 ? 13.481  45.503 102.154 1.00 66.48  ? 243  SER E O   1 
ATOM   9676  C CB  . SER E  1 243 ? 14.370  46.406 99.264  1.00 60.76  ? 243  SER E CB  1 
ATOM   9677  O OG  . SER E  1 243 ? 14.571  47.779 99.558  1.00 61.26  ? 243  SER E OG  1 
ATOM   9678  N N   . ASN E  1 244 ? 15.324  46.798 102.353 1.00 65.83  ? 244  ASN E N   1 
ATOM   9679  C CA  . ASN E  1 244 ? 14.942  47.423 103.625 1.00 68.69  ? 244  ASN E CA  1 
ATOM   9680  C C   . ASN E  1 244 ? 14.572  48.903 103.458 1.00 69.05  ? 244  ASN E C   1 
ATOM   9681  O O   . ASN E  1 244 ? 14.395  49.616 104.449 1.00 71.58  ? 244  ASN E O   1 
ATOM   9682  C CB  . ASN E  1 244 ? 16.070  47.277 104.658 1.00 70.22  ? 244  ASN E CB  1 
ATOM   9683  C CG  . ASN E  1 244 ? 17.379  47.891 104.188 1.00 69.01  ? 244  ASN E CG  1 
ATOM   9684  O OD1 . ASN E  1 244 ? 17.639  47.975 102.987 1.00 66.51  ? 244  ASN E OD1 1 
ATOM   9685  N ND2 . ASN E  1 244 ? 18.212  48.314 105.132 1.00 71.03  ? 244  ASN E ND2 1 
ATOM   9686  N N   . GLY E  1 245 ? 14.459  49.360 102.210 1.00 66.73  ? 245  GLY E N   1 
ATOM   9687  C CA  . GLY E  1 245 ? 14.015  50.724 101.931 1.00 67.03  ? 245  GLY E CA  1 
ATOM   9688  C C   . GLY E  1 245 ? 14.162  51.172 100.487 1.00 64.25  ? 245  GLY E C   1 
ATOM   9689  O O   . GLY E  1 245 ? 14.944  50.605 99.720  1.00 62.07  ? 245  GLY E O   1 
ATOM   9690  N N   . ASN E  1 246 ? 13.391  52.202 100.135 1.00 64.59  ? 246  ASN E N   1 
ATOM   9691  C CA  . ASN E  1 246 ? 13.469  52.898 98.839  1.00 62.37  ? 246  ASN E CA  1 
ATOM   9692  C C   . ASN E  1 246 ? 13.083  52.057 97.614  1.00 59.96  ? 246  ASN E C   1 
ATOM   9693  O O   . ASN E  1 246 ? 13.471  52.377 96.491  1.00 57.81  ? 246  ASN E O   1 
ATOM   9694  C CB  . ASN E  1 246 ? 14.862  53.522 98.638  1.00 61.47  ? 246  ASN E CB  1 
ATOM   9695  C CG  . ASN E  1 246 ? 15.311  54.357 99.831  1.00 64.15  ? 246  ASN E CG  1 
ATOM   9696  O OD1 . ASN E  1 246 ? 15.637  53.818 100.888 1.00 65.80  ? 246  ASN E OD1 1 
ATOM   9697  N ND2 . ASN E  1 246 ? 15.343  55.676 99.661  1.00 64.79  ? 246  ASN E ND2 1 
ATOM   9698  N N   . PHE E  1 247 ? 12.279  51.017 97.831  1.00 60.61  ? 247  PHE E N   1 
ATOM   9699  C CA  . PHE E  1 247 ? 11.950  50.046 96.784  1.00 58.80  ? 247  PHE E CA  1 
ATOM   9700  C C   . PHE E  1 247 ? 10.640  50.367 96.076  1.00 59.01  ? 247  PHE E C   1 
ATOM   9701  O O   . PHE E  1 247 ? 9.610   50.573 96.716  1.00 61.30  ? 247  PHE E O   1 
ATOM   9702  C CB  . PHE E  1 247 ? 11.893  48.640 97.392  1.00 59.62  ? 247  PHE E CB  1 
ATOM   9703  C CG  . PHE E  1 247 ? 11.559  47.545 96.409  1.00 58.30  ? 247  PHE E CG  1 
ATOM   9704  C CD1 . PHE E  1 247 ? 12.265  47.402 95.220  1.00 55.84  ? 247  PHE E CD1 1 
ATOM   9705  C CD2 . PHE E  1 247 ? 10.559  46.624 96.697  1.00 59.82  ? 247  PHE E CD2 1 
ATOM   9706  C CE1 . PHE E  1 247 ? 11.965  46.385 94.331  1.00 54.98  ? 247  PHE E CE1 1 
ATOM   9707  C CE2 . PHE E  1 247 ? 10.257  45.602 95.812  1.00 58.98  ? 247  PHE E CE2 1 
ATOM   9708  C CZ  . PHE E  1 247 ? 10.961  45.482 94.628  1.00 56.58  ? 247  PHE E CZ  1 
ATOM   9709  N N   . ILE E  1 248 ? 10.698  50.413 94.747  1.00 56.85  ? 248  ILE E N   1 
ATOM   9710  C CA  . ILE E  1 248 ? 9.508   50.555 93.921  1.00 56.99  ? 248  ILE E CA  1 
ATOM   9711  C C   . ILE E  1 248 ? 9.195   49.175 93.354  1.00 56.48  ? 248  ILE E C   1 
ATOM   9712  O O   . ILE E  1 248 ? 9.830   48.719 92.405  1.00 54.41  ? 248  ILE E O   1 
ATOM   9713  C CB  . ILE E  1 248 ? 9.701   51.585 92.789  1.00 55.25  ? 248  ILE E CB  1 
ATOM   9714  C CG1 . ILE E  1 248 ? 10.429  52.837 93.292  1.00 55.47  ? 248  ILE E CG1 1 
ATOM   9715  C CG2 . ILE E  1 248 ? 8.358   51.972 92.193  1.00 56.19  ? 248  ILE E CG2 1 
ATOM   9716  C CD1 . ILE E  1 248 ? 9.799   53.507 94.498  1.00 58.34  ? 248  ILE E CD1 1 
ATOM   9717  N N   . ALA E  1 249 ? 8.223   48.508 93.965  1.00 58.67  ? 249  ALA E N   1 
ATOM   9718  C CA  . ALA E  1 249 ? 7.924   47.116 93.649  1.00 58.81  ? 249  ALA E CA  1 
ATOM   9719  C C   . ALA E  1 249 ? 7.115   46.989 92.362  1.00 58.40  ? 249  ALA E C   1 
ATOM   9720  O O   . ALA E  1 249 ? 6.320   47.868 92.044  1.00 59.10  ? 249  ALA E O   1 
ATOM   9721  C CB  . ALA E  1 249 ? 7.169   46.468 94.802  1.00 61.62  ? 249  ALA E CB  1 
ATOM   9722  N N   . PRO E  1 250 ? 7.319   45.890 91.617  1.00 57.53  ? 250  PRO E N   1 
ATOM   9723  C CA  . PRO E  1 250 ? 6.487   45.623 90.448  1.00 57.67  ? 250  PRO E CA  1 
ATOM   9724  C C   . PRO E  1 250 ? 5.106   45.079 90.810  1.00 60.70  ? 250  PRO E C   1 
ATOM   9725  O O   . PRO E  1 250 ? 5.011   44.017 91.413  1.00 62.04  ? 250  PRO E O   1 
ATOM   9726  C CB  . PRO E  1 250 ? 7.283   44.562 89.684  1.00 56.12  ? 250  PRO E CB  1 
ATOM   9727  C CG  . PRO E  1 250 ? 8.118   43.886 90.707  1.00 56.23  ? 250  PRO E CG  1 
ATOM   9728  C CD  . PRO E  1 250 ? 8.422   44.920 91.749  1.00 56.43  ? 250  PRO E CD  1 
ATOM   9729  N N   . GLU E  1 251 ? 4.053   45.807 90.449  1.00 62.01  ? 251  GLU E N   1 
ATOM   9730  C CA  . GLU E  1 251 ? 2.696   45.262 90.484  1.00 65.05  ? 251  GLU E CA  1 
ATOM   9731  C C   . GLU E  1 251 ? 2.492   44.391 89.247  1.00 64.72  ? 251  GLU E C   1 
ATOM   9732  O O   . GLU E  1 251 ? 2.182   43.200 89.356  1.00 66.22  ? 251  GLU E O   1 
ATOM   9733  C CB  . GLU E  1 251 ? 1.645   46.385 90.528  1.00 66.93  ? 251  GLU E CB  1 
ATOM   9734  C CG  . GLU E  1 251 ? 0.809   46.436 91.798  1.00 70.27  ? 251  GLU E CG  1 
ATOM   9735  C CD  . GLU E  1 251 ? -0.590  45.878 91.610  1.00 73.66  ? 251  GLU E CD  1 
ATOM   9736  O OE1 . GLU E  1 251 ? -1.368  46.486 90.848  1.00 74.58  ? 251  GLU E OE1 1 
ATOM   9737  O OE2 . GLU E  1 251 ? -0.924  44.845 92.229  1.00 75.65  ? 251  GLU E OE2 1 
ATOM   9738  N N   . TYR E  1 252 ? 2.690   45.000 88.078  1.00 62.91  ? 252  TYR E N   1 
ATOM   9739  C CA  . TYR E  1 252 ? 2.489   44.336 86.790  1.00 62.71  ? 252  TYR E CA  1 
ATOM   9740  C C   . TYR E  1 252 ? 3.790   44.177 85.999  1.00 59.57  ? 252  TYR E C   1 
ATOM   9741  O O   . TYR E  1 252 ? 4.683   45.032 86.052  1.00 57.32  ? 252  TYR E O   1 
ATOM   9742  C CB  . TYR E  1 252 ? 1.485   45.119 85.943  1.00 63.78  ? 252  TYR E CB  1 
ATOM   9743  C CG  . TYR E  1 252 ? 0.109   45.213 86.557  1.00 67.42  ? 252  TYR E CG  1 
ATOM   9744  C CD1 . TYR E  1 252 ? -0.813  44.181 86.407  1.00 70.30  ? 252  TYR E CD1 1 
ATOM   9745  C CD2 . TYR E  1 252 ? -0.273  46.333 87.290  1.00 68.32  ? 252  TYR E CD2 1 
ATOM   9746  C CE1 . TYR E  1 252 ? -2.076  44.261 86.970  1.00 74.00  ? 252  TYR E CE1 1 
ATOM   9747  C CE2 . TYR E  1 252 ? -1.533  46.424 87.856  1.00 72.00  ? 252  TYR E CE2 1 
ATOM   9748  C CZ  . TYR E  1 252 ? -2.433  45.384 87.694  1.00 74.83  ? 252  TYR E CZ  1 
ATOM   9749  O OH  . TYR E  1 252 ? -3.688  45.470 88.253  1.00 78.82  ? 252  TYR E OH  1 
ATOM   9750  N N   . ALA E  1 253 ? 3.876   43.069 85.267  1.00 59.78  ? 253  ALA E N   1 
ATOM   9751  C CA  . ALA E  1 253 ? 4.978   42.806 84.351  1.00 57.37  ? 253  ALA E CA  1 
ATOM   9752  C C   . ALA E  1 253 ? 4.397   42.399 83.000  1.00 58.20  ? 253  ALA E C   1 
ATOM   9753  O O   . ALA E  1 253 ? 3.439   41.625 82.937  1.00 60.86  ? 253  ALA E O   1 
ATOM   9754  C CB  . ALA E  1 253 ? 5.869   41.703 84.901  1.00 57.07  ? 253  ALA E CB  1 
ATOM   9755  N N   . TYR E  1 254 ? 4.971   42.931 81.925  1.00 56.17  ? 254  TYR E N   1 
ATOM   9756  C CA  . TYR E  1 254 ? 4.467   42.674 80.579  1.00 56.92  ? 254  TYR E CA  1 
ATOM   9757  C C   . TYR E  1 254 ? 4.913   41.310 80.065  1.00 57.47  ? 254  TYR E C   1 
ATOM   9758  O O   . TYR E  1 254 ? 6.034   40.871 80.314  1.00 56.04  ? 254  TYR E O   1 
ATOM   9759  C CB  . TYR E  1 254 ? 4.921   43.770 79.618  1.00 54.70  ? 254  TYR E CB  1 
ATOM   9760  C CG  . TYR E  1 254 ? 4.226   45.092 79.837  1.00 54.84  ? 254  TYR E CG  1 
ATOM   9761  C CD1 . TYR E  1 254 ? 3.012   45.371 79.218  1.00 56.85  ? 254  TYR E CD1 1 
ATOM   9762  C CD2 . TYR E  1 254 ? 4.780   46.065 80.660  1.00 53.29  ? 254  TYR E CD2 1 
ATOM   9763  C CE1 . TYR E  1 254 ? 2.370   46.583 79.408  1.00 57.28  ? 254  TYR E CE1 1 
ATOM   9764  C CE2 . TYR E  1 254 ? 4.146   47.280 80.859  1.00 53.73  ? 254  TYR E CE2 1 
ATOM   9765  C CZ  . TYR E  1 254 ? 2.939   47.536 80.230  1.00 55.71  ? 254  TYR E CZ  1 
ATOM   9766  O OH  . TYR E  1 254 ? 2.295   48.739 80.427  1.00 56.45  ? 254  TYR E OH  1 
ATOM   9767  N N   . LYS E  1 255 ? 4.019   40.657 79.333  1.00 59.87  ? 255  LYS E N   1 
ATOM   9768  C CA  . LYS E  1 255 ? 4.255   39.325 78.790  1.00 61.12  ? 255  LYS E CA  1 
ATOM   9769  C C   . LYS E  1 255 ? 4.425   39.472 77.287  1.00 60.61  ? 255  LYS E C   1 
ATOM   9770  O O   . LYS E  1 255 ? 3.611   40.124 76.636  1.00 61.34  ? 255  LYS E O   1 
ATOM   9771  C CB  . LYS E  1 255 ? 3.053   38.428 79.107  1.00 64.85  ? 255  LYS E CB  1 
ATOM   9772  C CG  . LYS E  1 255 ? 3.385   37.005 79.521  1.00 66.29  ? 255  LYS E CG  1 
ATOM   9773  C CD  . LYS E  1 255 ? 2.261   36.380 80.348  1.00 69.68  ? 255  LYS E CD  1 
ATOM   9774  C CE  . LYS E  1 255 ? 1.478   35.333 79.542  1.00 73.20  ? 255  LYS E CE  1 
ATOM   9775  N NZ  . LYS E  1 255 ? 0.038   35.686 79.433  1.00 76.09  ? 255  LYS E NZ  1 
ATOM   9776  N N   . ILE E  1 256 ? 5.473   38.864 76.738  1.00 59.58  ? 256  ILE E N   1 
ATOM   9777  C CA  . ILE E  1 256 ? 5.794   39.018 75.319  1.00 59.02  ? 256  ILE E CA  1 
ATOM   9778  C C   . ILE E  1 256 ? 5.199   37.844 74.545  1.00 62.18  ? 256  ILE E C   1 
ATOM   9779  O O   . ILE E  1 256 ? 5.840   36.807 74.376  1.00 62.83  ? 256  ILE E O   1 
ATOM   9780  C CB  . ILE E  1 256 ? 7.319   39.106 75.064  1.00 56.38  ? 256  ILE E CB  1 
ATOM   9781  C CG1 . ILE E  1 256 ? 8.045   39.761 76.247  1.00 54.10  ? 256  ILE E CG1 1 
ATOM   9782  C CG2 . ILE E  1 256 ? 7.583   39.862 73.767  1.00 55.17  ? 256  ILE E CG2 1 
ATOM   9783  C CD1 . ILE E  1 256 ? 9.518   40.027 76.011  1.00 51.70  ? 256  ILE E CD1 1 
ATOM   9784  N N   . VAL E  1 257 ? 3.964   38.005 74.085  1.00 64.46  ? 257  VAL E N   1 
ATOM   9785  C CA  . VAL E  1 257 ? 3.259   36.911 73.408  1.00 68.08  ? 257  VAL E CA  1 
ATOM   9786  C C   . VAL E  1 257 ? 3.683   36.757 71.941  1.00 68.22  ? 257  VAL E C   1 
ATOM   9787  O O   . VAL E  1 257 ? 3.812   35.629 71.447  1.00 70.40  ? 257  VAL E O   1 
ATOM   9788  C CB  . VAL E  1 257 ? 1.717   37.030 73.527  1.00 71.20  ? 257  VAL E CB  1 
ATOM   9789  C CG1 . VAL E  1 257 ? 1.285   36.850 74.973  1.00 71.97  ? 257  VAL E CG1 1 
ATOM   9790  C CG2 . VAL E  1 257 ? 1.196   38.352 72.976  1.00 70.34  ? 257  VAL E CG2 1 
ATOM   9791  N N   . LYS E  1 258 ? 3.905   37.881 71.258  1.00 66.09  ? 258  LYS E N   1 
ATOM   9792  C CA  . LYS E  1 258 ? 4.329   37.866 69.854  1.00 66.12  ? 258  LYS E CA  1 
ATOM   9793  C C   . LYS E  1 258 ? 5.644   38.598 69.618  1.00 62.46  ? 258  LYS E C   1 
ATOM   9794  O O   . LYS E  1 258 ? 5.806   39.748 70.029  1.00 59.93  ? 258  LYS E O   1 
ATOM   9795  C CB  . LYS E  1 258 ? 3.249   38.466 68.945  1.00 67.82  ? 258  LYS E CB  1 
ATOM   9796  C CG  . LYS E  1 258 ? 2.554   37.442 68.060  1.00 71.92  ? 258  LYS E CG  1 
ATOM   9797  C CD  . LYS E  1 258 ? 2.427   37.921 66.619  1.00 72.45  ? 258  LYS E CD  1 
ATOM   9798  C CE  . LYS E  1 258 ? 1.415   39.045 66.464  1.00 72.72  ? 258  LYS E CE  1 
ATOM   9799  N NZ  . LYS E  1 258 ? 0.832   39.038 65.092  1.00 75.32  ? 258  LYS E NZ  1 
ATOM   9800  N N   . LYS E  1 259 ? 6.568   37.915 68.944  1.00 62.53  ? 259  LYS E N   1 
ATOM   9801  C CA  . LYS E  1 259 ? 7.810   38.516 68.467  1.00 59.76  ? 259  LYS E CA  1 
ATOM   9802  C C   . LYS E  1 259 ? 7.779   38.574 66.945  1.00 60.85  ? 259  LYS E C   1 
ATOM   9803  O O   . LYS E  1 259 ? 7.760   37.536 66.281  1.00 63.45  ? 259  LYS E O   1 
ATOM   9804  C CB  . LYS E  1 259 ? 9.018   37.692 68.919  1.00 59.21  ? 259  LYS E CB  1 
ATOM   9805  C CG  . LYS E  1 259 ? 9.330   37.804 70.400  1.00 57.62  ? 259  LYS E CG  1 
ATOM   9806  C CD  . LYS E  1 259 ? 10.423  36.832 70.816  1.00 57.76  ? 259  LYS E CD  1 
ATOM   9807  C CE  . LYS E  1 259 ? 10.691  36.919 72.311  1.00 56.46  ? 259  LYS E CE  1 
ATOM   9808  N NZ  . LYS E  1 259 ? 11.635  35.870 72.785  1.00 57.07  ? 259  LYS E NZ  1 
ATOM   9809  N N   . GLY E  1 260 ? 7.770   39.786 66.395  1.00 59.08  ? 260  GLY E N   1 
ATOM   9810  C CA  . GLY E  1 260 ? 7.769   39.974 64.944  1.00 59.97  ? 260  GLY E CA  1 
ATOM   9811  C C   . GLY E  1 260 ? 8.544   41.201 64.504  1.00 56.99  ? 260  GLY E C   1 
ATOM   9812  O O   . GLY E  1 260 ? 9.201   41.856 65.312  1.00 54.27  ? 260  GLY E O   1 
ATOM   9813  N N   . ASP E  1 261 ? 8.464   41.510 63.215  1.00 57.73  ? 261  ASP E N   1 
ATOM   9814  C CA  . ASP E  1 261 ? 9.079   42.718 62.683  1.00 55.27  ? 261  ASP E CA  1 
ATOM   9815  C C   . ASP E  1 261 ? 8.243   43.928 63.066  1.00 54.12  ? 261  ASP E C   1 
ATOM   9816  O O   . ASP E  1 261 ? 7.049   43.991 62.775  1.00 56.10  ? 261  ASP E O   1 
ATOM   9817  C CB  . ASP E  1 261 ? 9.234   42.641 61.158  1.00 56.71  ? 261  ASP E CB  1 
ATOM   9818  C CG  . ASP E  1 261 ? 10.407  41.779 60.732  1.00 57.23  ? 261  ASP E CG  1 
ATOM   9819  O OD1 . ASP E  1 261 ? 11.240  41.434 61.600  1.00 55.99  ? 261  ASP E OD1 1 
ATOM   9820  O OD2 . ASP E  1 261 ? 10.500  41.452 59.527  1.00 59.12  ? 261  ASP E OD2 1 
ATOM   9821  N N   . SER E  1 262 ? 8.884   44.878 63.733  1.00 51.20  ? 262  SER E N   1 
ATOM   9822  C CA  . SER E  1 262 ? 8.241   46.112 64.155  1.00 50.06  ? 262  SER E CA  1 
ATOM   9823  C C   . SER E  1 262 ? 9.292   47.217 64.163  1.00 47.15  ? 262  SER E C   1 
ATOM   9824  O O   . SER E  1 262 ? 10.476  46.959 63.928  1.00 46.21  ? 262  SER E O   1 
ATOM   9825  C CB  . SER E  1 262 ? 7.622   45.936 65.547  1.00 50.29  ? 262  SER E CB  1 
ATOM   9826  O OG  . SER E  1 262 ? 7.120   47.159 66.061  1.00 49.22  ? 262  SER E OG  1 
ATOM   9827  N N   . THR E  1 263 ? 8.860   48.447 64.421  1.00 46.05  ? 263  THR E N   1 
ATOM   9828  C CA  . THR E  1 263 ? 9.780   49.576 64.477  1.00 43.54  ? 263  THR E CA  1 
ATOM   9829  C C   . THR E  1 263 ? 9.170   50.725 65.267  1.00 42.77  ? 263  THR E C   1 
ATOM   9830  O O   . THR E  1 263 ? 7.951   50.919 65.255  1.00 44.27  ? 263  THR E O   1 
ATOM   9831  C CB  . THR E  1 263 ? 10.173  50.053 63.058  1.00 43.37  ? 263  THR E CB  1 
ATOM   9832  O OG1 . THR E  1 263 ? 11.405  50.773 63.116  1.00 41.21  ? 263  THR E OG1 1 
ATOM   9833  C CG2 . THR E  1 263 ? 9.099   50.944 62.434  1.00 44.17  ? 263  THR E CG2 1 
ATOM   9834  N N   . ILE E  1 264 ? 10.021  51.475 65.961  1.00 40.74  ? 264  ILE E N   1 
ATOM   9835  C CA  . ILE E  1 264 ? 9.586   52.691 66.631  1.00 40.08  ? 264  ILE E CA  1 
ATOM   9836  C C   . ILE E  1 264 ? 9.862   53.862 65.697  1.00 39.20  ? 264  ILE E C   1 
ATOM   9837  O O   . ILE E  1 264 ? 11.009  54.266 65.500  1.00 37.68  ? 264  ILE E O   1 
ATOM   9838  C CB  . ILE E  1 264 ? 10.272  52.890 67.993  1.00 38.79  ? 264  ILE E CB  1 
ATOM   9839  C CG1 . ILE E  1 264 ? 9.955   51.702 68.906  1.00 39.82  ? 264  ILE E CG1 1 
ATOM   9840  C CG2 . ILE E  1 264 ? 9.788   54.182 68.643  1.00 38.51  ? 264  ILE E CG2 1 
ATOM   9841  C CD1 . ILE E  1 264 ? 10.873  51.581 70.102  1.00 38.70  ? 264  ILE E CD1 1 
ATOM   9842  N N   . MET E  1 265 ? 8.783   54.385 65.130  1.00 46.64  ? 265  MET E N   1 
ATOM   9843  C CA  . MET E  1 265 ? 8.828   55.453 64.148  1.00 44.99  ? 265  MET E CA  1 
ATOM   9844  C C   . MET E  1 265 ? 8.693   56.799 64.856  1.00 45.35  ? 265  MET E C   1 
ATOM   9845  O O   . MET E  1 265 ? 7.848   56.963 65.736  1.00 46.64  ? 265  MET E O   1 
ATOM   9846  C CB  . MET E  1 265 ? 7.673   55.251 63.174  1.00 44.82  ? 265  MET E CB  1 
ATOM   9847  C CG  . MET E  1 265 ? 7.714   56.097 61.921  1.00 43.30  ? 265  MET E CG  1 
ATOM   9848  S SD  . MET E  1 265 ? 6.373   55.615 60.814  1.00 43.76  ? 265  MET E SD  1 
ATOM   9849  C CE  . MET E  1 265 ? 6.937   54.013 60.234  1.00 43.58  ? 265  MET E CE  1 
ATOM   9850  N N   . LYS E  1 266 ? 9.537   57.751 64.479  1.00 44.63  ? 266  LYS E N   1 
ATOM   9851  C CA  . LYS E  1 266 ? 9.507   59.083 65.066  1.00 45.53  ? 266  LYS E CA  1 
ATOM   9852  C C   . LYS E  1 266 ? 8.729   60.019 64.157  1.00 45.40  ? 266  LYS E C   1 
ATOM   9853  O O   . LYS E  1 266 ? 9.151   60.293 63.032  1.00 44.34  ? 266  LYS E O   1 
ATOM   9854  C CB  . LYS E  1 266 ? 10.928  59.610 65.286  1.00 45.81  ? 266  LYS E CB  1 
ATOM   9855  C CG  . LYS E  1 266 ? 11.653  58.973 66.465  1.00 46.95  ? 266  LYS E CG  1 
ATOM   9856  C CD  . LYS E  1 266 ? 11.034  59.394 67.787  1.00 48.46  ? 266  LYS E CD  1 
ATOM   9857  C CE  . LYS E  1 266 ? 11.943  59.087 68.962  1.00 49.98  ? 266  LYS E CE  1 
ATOM   9858  N NZ  . LYS E  1 266 ? 11.413  59.670 70.232  1.00 51.53  ? 266  LYS E NZ  1 
ATOM   9859  N N   . SER E  1 267 ? 7.590   60.504 64.646  1.00 46.89  ? 267  SER E N   1 
ATOM   9860  C CA  . SER E  1 267 ? 6.710   61.354 63.851  1.00 47.62  ? 267  SER E CA  1 
ATOM   9861  C C   . SER E  1 267 ? 5.785   62.200 64.722  1.00 50.18  ? 267  SER E C   1 
ATOM   9862  O O   . SER E  1 267 ? 5.314   61.751 65.771  1.00 51.17  ? 267  SER E O   1 
ATOM   9863  C CB  . SER E  1 267 ? 5.874   60.489 62.905  1.00 47.03  ? 267  SER E CB  1 
ATOM   9864  O OG  . SER E  1 267 ? 4.996   61.282 62.122  1.00 48.19  ? 267  SER E OG  1 
ATOM   9865  N N   . GLU E  1 268 ? 5.529   63.425 64.269  1.00 51.64  ? 268  GLU E N   1 
ATOM   9866  C CA  . GLU E  1 268 ? 4.593   64.329 64.938  1.00 54.72  ? 268  GLU E CA  1 
ATOM   9867  C C   . GLU E  1 268 ? 3.169   64.115 64.428  1.00 56.24  ? 268  GLU E C   1 
ATOM   9868  O O   . GLU E  1 268 ? 2.219   64.644 65.003  1.00 59.22  ? 268  GLU E O   1 
ATOM   9869  C CB  . GLU E  1 268 ? 4.997   65.794 64.723  1.00 56.56  ? 268  GLU E CB  1 
ATOM   9870  C CG  . GLU E  1 268 ? 6.454   66.111 65.036  1.00 55.78  ? 268  GLU E CG  1 
ATOM   9871  C CD  . GLU E  1 268 ? 6.850   65.745 66.454  1.00 55.92  ? 268  GLU E CD  1 
ATOM   9872  O OE1 . GLU E  1 268 ? 6.157   66.183 67.401  1.00 58.19  ? 268  GLU E OE1 1 
ATOM   9873  O OE2 . GLU E  1 268 ? 7.864   65.023 66.614  1.00 54.06  ? 268  GLU E OE2 1 
ATOM   9874  N N   . LEU E  1 269 ? 3.025   63.341 63.353  1.00 54.64  ? 269  LEU E N   1 
ATOM   9875  C CA  . LEU E  1 269 ? 1.720   63.100 62.738  1.00 56.44  ? 269  LEU E CA  1 
ATOM   9876  C C   . LEU E  1 269 ? 0.845   62.200 63.600  1.00 57.82  ? 269  LEU E C   1 
ATOM   9877  O O   . LEU E  1 269 ? 1.344   61.433 64.424  1.00 56.50  ? 269  LEU E O   1 
ATOM   9878  C CB  . LEU E  1 269 ? 1.881   62.487 61.342  1.00 54.45  ? 269  LEU E CB  1 
ATOM   9879  C CG  . LEU E  1 269 ? 2.415   63.434 60.262  1.00 53.95  ? 269  LEU E CG  1 
ATOM   9880  C CD1 . LEU E  1 269 ? 2.865   62.657 59.037  1.00 51.31  ? 269  LEU E CD1 1 
ATOM   9881  C CD2 . LEU E  1 269 ? 1.370   64.468 59.874  1.00 57.57  ? 269  LEU E CD2 1 
ATOM   9882  N N   . GLU E  1 270 ? -0.464  62.300 63.384  1.00 60.98  ? 270  GLU E N   1 
ATOM   9883  C CA  . GLU E  1 270 ? -1.448  61.566 64.185  1.00 63.33  ? 270  GLU E CA  1 
ATOM   9884  C C   . GLU E  1 270 ? -1.916  60.313 63.420  1.00 63.17  ? 270  GLU E C   1 
ATOM   9885  O O   . GLU E  1 270 ? -1.107  59.414 63.192  1.00 60.29  ? 270  GLU E O   1 
ATOM   9886  C CB  . GLU E  1 270 ? -2.598  62.488 64.668  1.00 67.88  ? 270  GLU E CB  1 
ATOM   9887  C CG  . GLU E  1 270 ? -2.994  63.618 63.716  1.00 70.04  ? 270  GLU E CG  1 
ATOM   9888  C CD  . GLU E  1 270 ? -4.148  64.470 64.230  1.00 75.33  ? 270  GLU E CD  1 
ATOM   9889  O OE1 . GLU E  1 270 ? -4.663  64.207 65.339  1.00 77.20  ? 270  GLU E OE1 1 
ATOM   9890  O OE2 . GLU E  1 270 ? -4.540  65.419 63.517  1.00 77.99  ? 270  GLU E OE2 1 
ATOM   9891  N N   . TYR E  1 271 ? -3.183  60.245 63.014  1.00 66.72  ? 271  TYR E N   1 
ATOM   9892  C CA  . TYR E  1 271 ? -3.739  59.024 62.430  1.00 67.55  ? 271  TYR E CA  1 
ATOM   9893  C C   . TYR E  1 271 ? -4.686  59.356 61.276  1.00 70.39  ? 271  TYR E C   1 
ATOM   9894  O O   . TYR E  1 271 ? -5.663  60.088 61.455  1.00 74.43  ? 271  TYR E O   1 
ATOM   9895  C CB  . TYR E  1 271 ? -4.475  58.228 63.511  1.00 70.35  ? 271  TYR E CB  1 
ATOM   9896  C CG  . TYR E  1 271 ? -4.981  56.871 63.065  1.00 71.78  ? 271  TYR E CG  1 
ATOM   9897  C CD1 . TYR E  1 271 ? -4.098  55.879 62.646  1.00 68.71  ? 271  TYR E CD1 1 
ATOM   9898  C CD2 . TYR E  1 271 ? -6.343  56.575 63.078  1.00 76.85  ? 271  TYR E CD2 1 
ATOM   9899  C CE1 . TYR E  1 271 ? -4.556  54.636 62.243  1.00 70.61  ? 271  TYR E CE1 1 
ATOM   9900  C CE2 . TYR E  1 271 ? -6.809  55.335 62.678  1.00 78.84  ? 271  TYR E CE2 1 
ATOM   9901  C CZ  . TYR E  1 271 ? -5.914  54.368 62.262  1.00 75.71  ? 271  TYR E CZ  1 
ATOM   9902  O OH  . TYR E  1 271 ? -6.389  53.137 61.865  1.00 78.29  ? 271  TYR E OH  1 
ATOM   9903  N N   . GLY E  1 272 ? -4.390  58.817 60.094  1.00 68.60  ? 272  GLY E N   1 
ATOM   9904  C CA  . GLY E  1 272 ? -5.194  59.083 58.897  1.00 71.16  ? 272  GLY E CA  1 
ATOM   9905  C C   . GLY E  1 272 ? -6.423  58.200 58.732  1.00 75.52  ? 272  GLY E C   1 
ATOM   9906  O O   . GLY E  1 272 ? -7.285  58.488 57.897  1.00 78.88  ? 272  GLY E O   1 
ATOM   9907  N N   . ASN E  1 273 ? -6.502  57.127 59.522  1.00 75.96  ? 273  ASN E N   1 
ATOM   9908  C CA  . ASN E  1 273 ? -7.571  56.128 59.407  1.00 80.40  ? 273  ASN E CA  1 
ATOM   9909  C C   . ASN E  1 273 ? -7.602  55.486 58.015  1.00 80.24  ? 273  ASN E C   1 
ATOM   9910  O O   . ASN E  1 273 ? -8.661  55.194 57.459  1.00 84.84  ? 273  ASN E O   1 
ATOM   9911  C CB  . ASN E  1 273 ? -8.927  56.738 59.787  1.00 86.37  ? 273  ASN E CB  1 
ATOM   9912  C CG  . ASN E  1 273 ? -9.818  55.760 60.530  1.00 90.88  ? 273  ASN E CG  1 
ATOM   9913  O OD1 . ASN E  1 273 ? -10.290 56.048 61.629  1.00 93.38  ? 273  ASN E OD1 1 
ATOM   9914  N ND2 . ASN E  1 273 ? -10.036 54.588 59.942  1.00 92.22  ? 273  ASN E ND2 1 
ATOM   9915  N N   . CYS E  1 274 ? -6.404  55.259 57.484  1.00 75.19  ? 274  CYS E N   1 
ATOM   9916  C CA  . CYS E  1 274 ? -6.188  54.704 56.153  1.00 74.12  ? 274  CYS E CA  1 
ATOM   9917  C C   . CYS E  1 274 ? -5.519  53.339 56.295  1.00 72.42  ? 274  CYS E C   1 
ATOM   9918  O O   . CYS E  1 274 ? -5.249  52.885 57.410  1.00 72.22  ? 274  CYS E O   1 
ATOM   9919  C CB  . CYS E  1 274 ? -5.284  55.650 55.352  1.00 69.96  ? 274  CYS E CB  1 
ATOM   9920  S SG  . CYS E  1 274 ? -4.001  56.404 56.378  1.00 65.46  ? 274  CYS E SG  1 
ATOM   9921  N N   . ASN E  1 275 ? -5.256  52.692 55.164  1.00 71.56  ? 275  ASN E N   1 
ATOM   9922  C CA  . ASN E  1 275 ? -4.511  51.438 55.135  1.00 70.11  ? 275  ASN E CA  1 
ATOM   9923  C C   . ASN E  1 275 ? -3.400  51.515 54.089  1.00 65.67  ? 275  ASN E C   1 
ATOM   9924  O O   . ASN E  1 275 ? -3.546  52.196 53.073  1.00 65.04  ? 275  ASN E O   1 
ATOM   9925  C CB  . ASN E  1 275 ? -5.454  50.272 54.825  1.00 75.13  ? 275  ASN E CB  1 
ATOM   9926  C CG  . ASN E  1 275 ? -4.775  48.919 54.947  1.00 74.81  ? 275  ASN E CG  1 
ATOM   9927  O OD1 . ASN E  1 275 ? -4.180  48.607 55.975  1.00 73.67  ? 275  ASN E OD1 1 
ATOM   9928  N ND2 . ASN E  1 275 ? -4.862  48.109 53.901  1.00 76.25  ? 275  ASN E ND2 1 
ATOM   9929  N N   . THR E  1 276 ? -2.289  50.828 54.341  1.00 62.99  ? 276  THR E N   1 
ATOM   9930  C CA  . THR E  1 276 ? -1.178  50.805 53.391  1.00 59.17  ? 276  THR E CA  1 
ATOM   9931  C C   . THR E  1 276 ? -0.368  49.515 53.481  1.00 58.86  ? 276  THR E C   1 
ATOM   9932  O O   . THR E  1 276 ? -0.580  48.695 54.374  1.00 61.36  ? 276  THR E O   1 
ATOM   9933  C CB  . THR E  1 276 ? -0.242  52.020 53.590  1.00 55.08  ? 276  THR E CB  1 
ATOM   9934  O OG1 . THR E  1 276 ? 0.685   52.103 52.501  1.00 52.00  ? 276  THR E OG1 1 
ATOM   9935  C CG2 . THR E  1 276 ? 0.531   51.930 54.911  1.00 53.78  ? 276  THR E CG2 1 
ATOM   9936  N N   . LYS E  1 277 ? 0.547   49.344 52.533  1.00 56.24  ? 277  LYS E N   1 
ATOM   9937  C CA  . LYS E  1 277 ? 1.497   48.229 52.544  1.00 55.92  ? 277  LYS E CA  1 
ATOM   9938  C C   . LYS E  1 277 ? 2.944   48.706 52.726  1.00 51.88  ? 277  LYS E C   1 
ATOM   9939  O O   . LYS E  1 277 ? 3.861   47.892 52.835  1.00 51.71  ? 277  LYS E O   1 
ATOM   9940  C CB  . LYS E  1 277 ? 1.367   47.407 51.258  1.00 57.26  ? 277  LYS E CB  1 
ATOM   9941  C CG  . LYS E  1 277 ? 0.394   46.238 51.331  1.00 62.48  ? 277  LYS E CG  1 
ATOM   9942  C CD  . LYS E  1 277 ? 0.785   45.127 50.359  1.00 63.77  ? 277  LYS E CD  1 
ATOM   9943  C CE  . LYS E  1 277 ? 2.131   44.475 50.672  1.00 62.40  ? 277  LYS E CE  1 
ATOM   9944  N NZ  . LYS E  1 277 ? 2.220   43.104 50.092  1.00 65.91  ? 277  LYS E NZ  1 
ATOM   9945  N N   . CYS E  1 278 ? 3.136   50.022 52.761  1.00 49.30  ? 278  CYS E N   1 
ATOM   9946  C CA  . CYS E  1 278 ? 4.447   50.627 52.953  1.00 46.06  ? 278  CYS E CA  1 
ATOM   9947  C C   . CYS E  1 278 ? 4.255   51.951 53.672  1.00 45.18  ? 278  CYS E C   1 
ATOM   9948  O O   . CYS E  1 278 ? 3.546   52.829 53.173  1.00 45.32  ? 278  CYS E O   1 
ATOM   9949  C CB  . CYS E  1 278 ? 5.121   50.874 51.603  1.00 43.77  ? 278  CYS E CB  1 
ATOM   9950  S SG  . CYS E  1 278 ? 6.693   51.762 51.707  1.00 40.46  ? 278  CYS E SG  1 
ATOM   9951  N N   . GLN E  1 279 ? 4.883   52.097 54.837  1.00 44.73  ? 279  GLN E N   1 
ATOM   9952  C CA  . GLN E  1 279 ? 4.674   53.279 55.665  1.00 44.48  ? 279  GLN E CA  1 
ATOM   9953  C C   . GLN E  1 279 ? 5.969   54.030 55.931  1.00 42.24  ? 279  GLN E C   1 
ATOM   9954  O O   . GLN E  1 279 ? 7.011   53.422 56.152  1.00 41.56  ? 279  GLN E O   1 
ATOM   9955  C CB  . GLN E  1 279 ? 4.034   52.879 56.993  1.00 46.79  ? 279  GLN E CB  1 
ATOM   9956  C CG  . GLN E  1 279 ? 3.665   54.054 57.886  1.00 47.06  ? 279  GLN E CG  1 
ATOM   9957  C CD  . GLN E  1 279 ? 2.471   54.829 57.367  1.00 48.54  ? 279  GLN E CD  1 
ATOM   9958  O OE1 . GLN E  1 279 ? 1.404   54.260 57.152  1.00 51.07  ? 279  GLN E OE1 1 
ATOM   9959  N NE2 . GLN E  1 279 ? 2.638   56.133 57.174  1.00 47.62  ? 279  GLN E NE2 1 
ATOM   9960  N N   . THR E  1 280 ? 5.877   55.359 55.911  1.00 41.75  ? 280  THR E N   1 
ATOM   9961  C CA  . THR E  1 280 ? 6.973   56.237 56.307  1.00 40.55  ? 280  THR E CA  1 
ATOM   9962  C C   . THR E  1 280 ? 6.495   57.208 57.398  1.00 41.94  ? 280  THR E C   1 
ATOM   9963  O O   . THR E  1 280 ? 5.287   57.397 57.581  1.00 43.63  ? 280  THR E O   1 
ATOM   9964  C CB  . THR E  1 280 ? 7.520   57.052 55.109  1.00 39.06  ? 280  THR E CB  1 
ATOM   9965  O OG1 . THR E  1 280 ? 6.763   58.258 54.934  1.00 39.95  ? 280  THR E OG1 1 
ATOM   9966  C CG2 . THR E  1 280 ? 7.477   56.236 53.825  1.00 38.28  ? 280  THR E CG2 1 
ATOM   9967  N N   . PRO E  1 281 ? 7.442   57.830 58.125  1.00 41.70  ? 281  PRO E N   1 
ATOM   9968  C CA  . PRO E  1 281 ? 7.114   58.908 59.082  1.00 43.14  ? 281  PRO E CA  1 
ATOM   9969  C C   . PRO E  1 281 ? 6.487   60.163 58.445  1.00 44.15  ? 281  PRO E C   1 
ATOM   9970  O O   . PRO E  1 281 ? 5.880   60.971 59.156  1.00 46.01  ? 281  PRO E O   1 
ATOM   9971  C CB  . PRO E  1 281 ? 8.464   59.264 59.722  1.00 42.67  ? 281  PRO E CB  1 
ATOM   9972  C CG  . PRO E  1 281 ? 9.450   58.251 59.265  1.00 41.36  ? 281  PRO E CG  1 
ATOM   9973  C CD  . PRO E  1 281 ? 8.826   57.343 58.257  1.00 40.69  ? 281  PRO E CD  1 
ATOM   9974  N N   . MET E  1 282 ? 6.658   60.325 57.131  1.00 43.33  ? 282  MET E N   1 
ATOM   9975  C CA  . MET E  1 282 ? 6.055   61.426 56.363  1.00 44.66  ? 282  MET E CA  1 
ATOM   9976  C C   . MET E  1 282 ? 4.634   61.079 55.925  1.00 46.06  ? 282  MET E C   1 
ATOM   9977  O O   . MET E  1 282 ? 3.792   61.961 55.749  1.00 48.33  ? 282  MET E O   1 
ATOM   9978  C CB  . MET E  1 282 ? 6.877   61.695 55.099  1.00 43.33  ? 282  MET E CB  1 
ATOM   9979  C CG  . MET E  1 282 ? 8.357   61.952 55.336  1.00 42.44  ? 282  MET E CG  1 
ATOM   9980  S SD  . MET E  1 282 ? 8.707   63.706 55.529  1.00 44.90  ? 282  MET E SD  1 
ATOM   9981  C CE  . MET E  1 282 ? 8.595   64.226 53.815  1.00 44.77  ? 282  MET E CE  1 
ATOM   9982  N N   . GLY E  1 283 ? 4.390   59.787 55.722  1.00 45.23  ? 283  GLY E N   1 
ATOM   9983  C CA  . GLY E  1 283 ? 3.121   59.301 55.195  1.00 46.91  ? 283  GLY E CA  1 
ATOM   9984  C C   . GLY E  1 283 ? 3.281   57.928 54.567  1.00 45.65  ? 283  GLY E C   1 
ATOM   9985  O O   . GLY E  1 283 ? 4.370   57.354 54.584  1.00 43.54  ? 283  GLY E O   1 
ATOM   9986  N N   . ALA E  1 284 ? 2.199   57.408 54.000  1.00 47.47  ? 284  ALA E N   1 
ATOM   9987  C CA  . ALA E  1 284 ? 2.197   56.066 53.421  1.00 47.18  ? 284  ALA E CA  1 
ATOM   9988  C C   . ALA E  1 284 ? 2.478   56.093 51.918  1.00 45.82  ? 284  ALA E C   1 
ATOM   9989  O O   . ALA E  1 284 ? 2.299   57.121 51.258  1.00 45.89  ? 284  ALA E O   1 
ATOM   9990  C CB  . ALA E  1 284 ? 0.866   55.387 53.695  1.00 50.65  ? 284  ALA E CB  1 
ATOM   9991  N N   . ILE E  1 285 ? 2.907   54.947 51.390  1.00 44.94  ? 285  ILE E N   1 
ATOM   9992  C CA  . ILE E  1 285 ? 3.272   54.808 49.975  1.00 43.57  ? 285  ILE E CA  1 
ATOM   9993  C C   . ILE E  1 285 ? 2.434   53.728 49.283  1.00 45.72  ? 285  ILE E C   1 
ATOM   9994  O O   . ILE E  1 285 ? 2.253   52.625 49.809  1.00 47.21  ? 285  ILE E O   1 
ATOM   9995  C CB  . ILE E  1 285 ? 4.787   54.512 49.817  1.00 40.64  ? 285  ILE E CB  1 
ATOM   9996  C CG1 . ILE E  1 285 ? 5.571   55.825 49.717  1.00 38.81  ? 285  ILE E CG1 1 
ATOM   9997  C CG2 . ILE E  1 285 ? 5.076   53.664 48.584  1.00 40.02  ? 285  ILE E CG2 1 
ATOM   9998  C CD1 . ILE E  1 285 ? 7.033   55.703 50.089  1.00 36.89  ? 285  ILE E CD1 1 
ATOM   9999  N N   . ASN E  1 286 ? 1.933   54.069 48.097  1.00 46.27  ? 286  ASN E N   1 
ATOM   10000 C CA  . ASN E  1 286 ? 1.211   53.140 47.237  1.00 48.44  ? 286  ASN E CA  1 
ATOM   10001 C C   . ASN E  1 286 ? 1.708   53.304 45.805  1.00 46.57  ? 286  ASN E C   1 
ATOM   10002 O O   . ASN E  1 286 ? 1.207   54.144 45.054  1.00 47.21  ? 286  ASN E O   1 
ATOM   10003 C CB  . ASN E  1 286 ? -0.301  53.402 47.310  1.00 52.56  ? 286  ASN E CB  1 
ATOM   10004 C CG  . ASN E  1 286 ? -1.101  52.488 46.395  1.00 55.53  ? 286  ASN E CG  1 
ATOM   10005 O OD1 . ASN E  1 286 ? -0.704  51.349 46.138  1.00 55.42  ? 286  ASN E OD1 1 
ATOM   10006 N ND2 . ASN E  1 286 ? -2.233  52.982 45.898  1.00 58.79  ? 286  ASN E ND2 1 
ATOM   10007 N N   . SER E  1 287 ? 2.708   52.513 45.433  1.00 44.58  ? 287  SER E N   1 
ATOM   10008 C CA  . SER E  1 287 ? 3.223   52.556 44.071  1.00 42.90  ? 287  SER E CA  1 
ATOM   10009 C C   . SER E  1 287 ? 3.917   51.266 43.661  1.00 42.49  ? 287  SER E C   1 
ATOM   10010 O O   . SER E  1 287 ? 4.328   50.465 44.499  1.00 42.91  ? 287  SER E O   1 
ATOM   10011 C CB  . SER E  1 287 ? 4.180   53.740 43.897  1.00 39.89  ? 287  SER E CB  1 
ATOM   10012 O OG  . SER E  1 287 ? 5.477   53.442 44.374  1.00 37.72  ? 287  SER E OG  1 
ATOM   10013 N N   . SER E  1 288 ? 4.043   51.093 42.351  1.00 41.99  ? 288  SER E N   1 
ATOM   10014 C CA  . SER E  1 288 ? 4.723   49.945 41.765  1.00 41.86  ? 288  SER E CA  1 
ATOM   10015 C C   . SER E  1 288 ? 6.157   50.298 41.345  1.00 38.48  ? 288  SER E C   1 
ATOM   10016 O O   . SER E  1 288 ? 6.867   49.463 40.787  1.00 38.31  ? 288  SER E O   1 
ATOM   10017 C CB  . SER E  1 288 ? 3.917   49.433 40.566  1.00 44.03  ? 288  SER E CB  1 
ATOM   10018 O OG  . SER E  1 288 ? 3.244   50.500 39.912  1.00 43.99  ? 288  SER E OG  1 
ATOM   10019 N N   . MET E  1 289 ? 6.585   51.525 41.637  1.00 36.33  ? 289  MET E N   1 
ATOM   10020 C CA  . MET E  1 289 ? 7.928   51.979 41.279  1.00 33.70  ? 289  MET E CA  1 
ATOM   10021 C C   . MET E  1 289 ? 8.977   51.166 42.028  1.00 33.49  ? 289  MET E C   1 
ATOM   10022 O O   . MET E  1 289 ? 8.726   50.714 43.143  1.00 34.86  ? 289  MET E O   1 
ATOM   10023 C CB  . MET E  1 289 ? 8.122   53.451 41.645  1.00 32.47  ? 289  MET E CB  1 
ATOM   10024 C CG  . MET E  1 289 ? 7.156   54.426 40.995  1.00 33.17  ? 289  MET E CG  1 
ATOM   10025 S SD  . MET E  1 289 ? 7.385   54.546 39.215  1.00 32.36  ? 289  MET E SD  1 
ATOM   10026 C CE  . MET E  1 289 ? 6.899   56.260 38.978  1.00 32.81  ? 289  MET E CE  1 
ATOM   10027 N N   . PRO E  1 290 ? 10.161  50.979 41.423  1.00 32.16  ? 290  PRO E N   1 
ATOM   10028 C CA  . PRO E  1 290 ? 11.259  50.327 42.143  1.00 32.47  ? 290  PRO E CA  1 
ATOM   10029 C C   . PRO E  1 290 ? 11.917  51.225 43.193  1.00 31.49  ? 290  PRO E C   1 
ATOM   10030 O O   . PRO E  1 290 ? 12.580  50.716 44.094  1.00 32.43  ? 290  PRO E O   1 
ATOM   10031 C CB  . PRO E  1 290 ? 12.257  50.006 41.030  1.00 31.86  ? 290  PRO E CB  1 
ATOM   10032 C CG  . PRO E  1 290 ? 12.000  51.047 40.002  1.00 30.13  ? 290  PRO E CG  1 
ATOM   10033 C CD  . PRO E  1 290 ? 10.519  51.262 40.022  1.00 30.88  ? 290  PRO E CD  1 
ATOM   10034 N N   . PHE E  1 291 ? 11.737  52.539 43.063  1.00 30.05  ? 291  PHE E N   1 
ATOM   10035 C CA  . PHE E  1 291 ? 12.383  53.523 43.931  1.00 29.46  ? 291  PHE E CA  1 
ATOM   10036 C C   . PHE E  1 291 ? 11.404  54.542 44.475  1.00 29.44  ? 291  PHE E C   1 
ATOM   10037 O O   . PHE E  1 291 ? 10.329  54.742 43.913  1.00 29.73  ? 291  PHE E O   1 
ATOM   10038 C CB  . PHE E  1 291 ? 13.426  54.317 43.151  1.00 28.44  ? 291  PHE E CB  1 
ATOM   10039 C CG  . PHE E  1 291 ? 14.648  53.542 42.792  1.00 28.77  ? 291  PHE E CG  1 
ATOM   10040 C CD1 . PHE E  1 291 ? 15.596  53.248 43.757  1.00 29.90  ? 291  PHE E CD1 1 
ATOM   10041 C CD2 . PHE E  1 291 ? 14.871  53.138 41.483  1.00 28.34  ? 291  PHE E CD2 1 
ATOM   10042 C CE1 . PHE E  1 291 ? 16.740  52.547 43.435  1.00 30.90  ? 291  PHE E CE1 1 
ATOM   10043 C CE2 . PHE E  1 291 ? 16.017  52.436 41.150  1.00 29.11  ? 291  PHE E CE2 1 
ATOM   10044 C CZ  . PHE E  1 291 ? 16.950  52.143 42.131  1.00 30.55  ? 291  PHE E CZ  1 
ATOM   10045 N N   . HIS E  1 292 ? 11.812  55.210 45.550  1.00 29.47  ? 292  HIS E N   1 
ATOM   10046 C CA  . HIS E  1 292 ? 11.114  56.386 46.058  1.00 29.76  ? 292  HIS E CA  1 
ATOM   10047 C C   . HIS E  1 292 ? 12.118  57.323 46.721  1.00 29.76  ? 292  HIS E C   1 
ATOM   10048 O O   . HIS E  1 292 ? 13.267  56.941 46.939  1.00 29.69  ? 292  HIS E O   1 
ATOM   10049 C CB  . HIS E  1 292 ? 10.029  55.974 47.053  1.00 30.98  ? 292  HIS E CB  1 
ATOM   10050 C CG  . HIS E  1 292 ? 10.566  55.523 48.373  1.00 31.46  ? 292  HIS E CG  1 
ATOM   10051 N ND1 . HIS E  1 292 ? 10.538  56.317 49.496  1.00 32.02  ? 292  HIS E ND1 1 
ATOM   10052 C CD2 . HIS E  1 292 ? 11.165  54.369 48.744  1.00 31.85  ? 292  HIS E CD2 1 
ATOM   10053 C CE1 . HIS E  1 292 ? 11.085  55.668 50.506  1.00 32.56  ? 292  HIS E CE1 1 
ATOM   10054 N NE2 . HIS E  1 292 ? 11.476  54.482 50.077  1.00 32.58  ? 292  HIS E NE2 1 
ATOM   10055 N N   . ASN E  1 293 ? 11.688  58.541 47.044  1.00 30.41  ? 293  ASN E N   1 
ATOM   10056 C CA  . ASN E  1 293 ? 12.562  59.528 47.688  1.00 31.08  ? 293  ASN E CA  1 
ATOM   10057 C C   . ASN E  1 293 ? 11.896  60.257 48.860  1.00 32.45  ? 293  ASN E C   1 
ATOM   10058 O O   . ASN E  1 293 ? 12.262  61.385 49.196  1.00 33.66  ? 293  ASN E O   1 
ATOM   10059 C CB  . ASN E  1 293 ? 13.046  60.543 46.652  1.00 31.23  ? 293  ASN E CB  1 
ATOM   10060 C CG  . ASN E  1 293 ? 11.932  61.431 46.138  1.00 32.07  ? 293  ASN E CG  1 
ATOM   10061 O OD1 . ASN E  1 293 ? 10.753  61.088 46.233  1.00 32.30  ? 293  ASN E OD1 1 
ATOM   10062 N ND2 . ASN E  1 293 ? 12.299  62.581 45.594  1.00 33.15  ? 293  ASN E ND2 1 
ATOM   10063 N N   . ILE E  1 294 ? 10.936  59.594 49.493  1.00 32.66  ? 294  ILE E N   1 
ATOM   10064 C CA  . ILE E  1 294 ? 10.138  60.191 50.565  1.00 34.15  ? 294  ILE E CA  1 
ATOM   10065 C C   . ILE E  1 294 ? 10.918  60.271 51.879  1.00 34.67  ? 294  ILE E C   1 
ATOM   10066 O O   . ILE E  1 294 ? 11.109  61.356 52.429  1.00 36.00  ? 294  ILE E O   1 
ATOM   10067 C CB  . ILE E  1 294 ? 8.823   59.400 50.796  1.00 34.68  ? 294  ILE E CB  1 
ATOM   10068 C CG1 . ILE E  1 294 ? 8.019   59.265 49.494  1.00 34.66  ? 294  ILE E CG1 1 
ATOM   10069 C CG2 . ILE E  1 294 ? 7.973   60.068 51.867  1.00 36.56  ? 294  ILE E CG2 1 
ATOM   10070 C CD1 . ILE E  1 294 ? 7.846   60.555 48.720  1.00 35.45  ? 294  ILE E CD1 1 
ATOM   10071 N N   . HIS E  1 295 ? 11.357  59.118 52.376  1.00 34.11  ? 295  HIS E N   1 
ATOM   10072 C CA  . HIS E  1 295 ? 12.022  59.034 53.673  1.00 34.91  ? 295  HIS E CA  1 
ATOM   10073 C C   . HIS E  1 295 ? 12.769  57.692 53.798  1.00 34.57  ? 295  HIS E C   1 
ATOM   10074 O O   . HIS E  1 295 ? 12.229  56.658 53.409  1.00 34.17  ? 295  HIS E O   1 
ATOM   10075 C CB  . HIS E  1 295 ? 10.974  59.166 54.784  1.00 36.03  ? 295  HIS E CB  1 
ATOM   10076 C CG  . HIS E  1 295 ? 11.535  59.577 56.107  1.00 37.20  ? 295  HIS E CG  1 
ATOM   10077 N ND1 . HIS E  1 295 ? 12.213  58.704 56.927  1.00 37.47  ? 295  HIS E ND1 1 
ATOM   10078 C CD2 . HIS E  1 295 ? 11.512  60.763 56.760  1.00 38.58  ? 295  HIS E CD2 1 
ATOM   10079 C CE1 . HIS E  1 295 ? 12.595  59.335 58.023  1.00 38.77  ? 295  HIS E CE1 1 
ATOM   10080 N NE2 . HIS E  1 295 ? 12.179  60.586 57.948  1.00 39.43  ? 295  HIS E NE2 1 
ATOM   10081 N N   . PRO E  1 296 ? 14.010  57.701 54.337  1.00 35.31  ? 296  PRO E N   1 
ATOM   10082 C CA  . PRO E  1 296 ? 14.805  56.461 54.443  1.00 35.76  ? 296  PRO E CA  1 
ATOM   10083 C C   . PRO E  1 296 ? 14.186  55.371 55.325  1.00 36.52  ? 296  PRO E C   1 
ATOM   10084 O O   . PRO E  1 296 ? 14.168  54.204 54.944  1.00 36.76  ? 296  PRO E O   1 
ATOM   10085 C CB  . PRO E  1 296 ? 16.135  56.938 55.052  1.00 37.25  ? 296  PRO E CB  1 
ATOM   10086 C CG  . PRO E  1 296 ? 15.844  58.264 55.658  1.00 37.74  ? 296  PRO E CG  1 
ATOM   10087 C CD  . PRO E  1 296 ? 14.771  58.873 54.807  1.00 36.43  ? 296  PRO E CD  1 
ATOM   10088 N N   . LEU E  1 297 ? 13.705  55.756 56.499  1.00 37.30  ? 297  LEU E N   1 
ATOM   10089 C CA  . LEU E  1 297 ? 13.138  54.809 57.460  1.00 38.44  ? 297  LEU E CA  1 
ATOM   10090 C C   . LEU E  1 297 ? 11.707  54.417 57.096  1.00 38.13  ? 297  LEU E C   1 
ATOM   10091 O O   . LEU E  1 297 ? 10.765  55.169 57.347  1.00 38.08  ? 297  LEU E O   1 
ATOM   10092 C CB  . LEU E  1 297 ? 13.173  55.402 58.873  1.00 39.56  ? 297  LEU E CB  1 
ATOM   10093 C CG  . LEU E  1 297 ? 14.539  55.897 59.365  1.00 40.59  ? 297  LEU E CG  1 
ATOM   10094 C CD1 . LEU E  1 297 ? 14.388  56.734 60.627  1.00 41.63  ? 297  LEU E CD1 1 
ATOM   10095 C CD2 . LEU E  1 297 ? 15.490  54.732 59.600  1.00 42.14  ? 297  LEU E CD2 1 
ATOM   10096 N N   . THR E  1 298 ? 11.551  53.235 56.506  1.00 38.48  ? 298  THR E N   1 
ATOM   10097 C CA  . THR E  1 298 ? 10.229  52.718 56.160  1.00 38.95  ? 298  THR E CA  1 
ATOM   10098 C C   . THR E  1 298 ? 10.004  51.344 56.780  1.00 41.18  ? 298  THR E C   1 
ATOM   10099 O O   . THR E  1 298 ? 10.939  50.698 57.252  1.00 42.21  ? 298  THR E O   1 
ATOM   10100 C CB  . THR E  1 298 ? 10.018  52.636 54.630  1.00 37.81  ? 298  THR E CB  1 
ATOM   10101 O OG1 . THR E  1 298 ? 10.749  51.529 54.085  1.00 38.30  ? 298  THR E OG1 1 
ATOM   10102 C CG2 . THR E  1 298 ? 10.468  53.917 53.958  1.00 36.00  ? 298  THR E CG2 1 
ATOM   10103 N N   . ILE E  1 299 ? 8.745   50.922 56.779  1.00 42.47  ? 299  ILE E N   1 
ATOM   10104 C CA  . ILE E  1 299 ? 8.348   49.613 57.285  1.00 45.29  ? 299  ILE E CA  1 
ATOM   10105 C C   . ILE E  1 299 ? 7.395   49.003 56.260  1.00 46.38  ? 299  ILE E C   1 
ATOM   10106 O O   . ILE E  1 299 ? 6.543   49.701 55.705  1.00 45.63  ? 299  ILE E O   1 
ATOM   10107 C CB  . ILE E  1 299 ? 7.708   49.714 58.703  1.00 46.88  ? 299  ILE E CB  1 
ATOM   10108 C CG1 . ILE E  1 299 ? 7.120   48.370 59.180  1.00 50.35  ? 299  ILE E CG1 1 
ATOM   10109 C CG2 . ILE E  1 299 ? 6.637   50.798 58.755  1.00 46.25  ? 299  ILE E CG2 1 
ATOM   10110 C CD1 . ILE E  1 299 ? 8.097   47.495 59.938  1.00 52.11  ? 299  ILE E CD1 1 
ATOM   10111 N N   . GLY E  1 300 ? 7.569   47.710 55.996  1.00 48.65  ? 300  GLY E N   1 
ATOM   10112 C CA  . GLY E  1 300 ? 6.699   46.971 55.087  1.00 50.55  ? 300  GLY E CA  1 
ATOM   10113 C C   . GLY E  1 300 ? 7.348   46.700 53.745  1.00 49.48  ? 300  GLY E C   1 
ATOM   10114 O O   . GLY E  1 300 ? 8.566   46.823 53.593  1.00 47.95  ? 300  GLY E O   1 
ATOM   10115 N N   . GLU E  1 301 ? 6.523   46.329 52.769  1.00 50.69  ? 301  GLU E N   1 
ATOM   10116 C CA  . GLU E  1 301 ? 6.988   46.044 51.413  1.00 49.90  ? 301  GLU E CA  1 
ATOM   10117 C C   . GLU E  1 301 ? 7.120   47.357 50.654  1.00 46.23  ? 301  GLU E C   1 
ATOM   10118 O O   . GLU E  1 301 ? 6.133   47.896 50.152  1.00 46.10  ? 301  GLU E O   1 
ATOM   10119 C CB  . GLU E  1 301 ? 6.011   45.103 50.700  1.00 53.15  ? 301  GLU E CB  1 
ATOM   10120 C CG  . GLU E  1 301 ? 6.515   44.545 49.374  1.00 53.11  ? 301  GLU E CG  1 
ATOM   10121 C CD  . GLU E  1 301 ? 7.601   43.488 49.531  1.00 54.94  ? 301  GLU E CD  1 
ATOM   10122 O OE1 . GLU E  1 301 ? 7.957   43.136 50.682  1.00 56.51  ? 301  GLU E OE1 1 
ATOM   10123 O OE2 . GLU E  1 301 ? 8.098   43.001 48.491  1.00 55.18  ? 301  GLU E OE2 1 
ATOM   10124 N N   . CYS E  1 302 ? 8.348   47.861 50.573  1.00 43.82  ? 302  CYS E N   1 
ATOM   10125 C CA  . CYS E  1 302 ? 8.603   49.192 50.038  1.00 40.74  ? 302  CYS E CA  1 
ATOM   10126 C C   . CYS E  1 302 ? 9.593   49.188 48.880  1.00 39.11  ? 302  CYS E C   1 
ATOM   10127 O O   . CYS E  1 302 ? 10.439  48.295 48.782  1.00 40.09  ? 302  CYS E O   1 
ATOM   10128 C CB  . CYS E  1 302 ? 9.152   50.092 51.143  1.00 39.65  ? 302  CYS E CB  1 
ATOM   10129 S SG  . CYS E  1 302 ? 7.992   50.393 52.492  1.00 41.24  ? 302  CYS E SG  1 
ATOM   10130 N N   . PRO E  1 303 ? 9.494   50.199 48.000  1.00 36.96  ? 303  PRO E N   1 
ATOM   10131 C CA  . PRO E  1 303 ? 10.566  50.430 47.037  1.00 35.28  ? 303  PRO E CA  1 
ATOM   10132 C C   . PRO E  1 303 ? 11.809  50.951 47.758  1.00 34.51  ? 303  PRO E C   1 
ATOM   10133 O O   . PRO E  1 303 ? 11.729  51.313 48.935  1.00 34.92  ? 303  PRO E O   1 
ATOM   10134 C CB  . PRO E  1 303 ? 9.984   51.487 46.091  1.00 33.74  ? 303  PRO E CB  1 
ATOM   10135 C CG  . PRO E  1 303 ? 8.878   52.139 46.841  1.00 34.41  ? 303  PRO E CG  1 
ATOM   10136 C CD  . PRO E  1 303 ? 8.374   51.145 47.841  1.00 36.61  ? 303  PRO E CD  1 
ATOM   10137 N N   . LYS E  1 304 ? 12.946  50.983 47.069  1.00 33.74  ? 304  LYS E N   1 
ATOM   10138 C CA  . LYS E  1 304 ? 14.197  51.393 47.699  1.00 33.78  ? 304  LYS E CA  1 
ATOM   10139 C C   . LYS E  1 304 ? 14.296  52.911 47.753  1.00 32.18  ? 304  LYS E C   1 
ATOM   10140 O O   . LYS E  1 304 ? 13.911  53.603 46.810  1.00 30.89  ? 304  LYS E O   1 
ATOM   10141 C CB  . LYS E  1 304 ? 15.395  50.811 46.950  1.00 34.45  ? 304  LYS E CB  1 
ATOM   10142 C CG  . LYS E  1 304 ? 15.382  49.290 46.853  1.00 36.70  ? 304  LYS E CG  1 
ATOM   10143 C CD  . LYS E  1 304 ? 15.688  48.623 48.193  1.00 39.20  ? 304  LYS E CD  1 
ATOM   10144 C CE  . LYS E  1 304 ? 14.789  47.420 48.457  1.00 41.40  ? 304  LYS E CE  1 
ATOM   10145 N NZ  . LYS E  1 304 ? 15.477  46.372 49.264  1.00 44.84  ? 304  LYS E NZ  1 
ATOM   10146 N N   . TYR E  1 305 ? 14.814  53.425 48.862  1.00 32.67  ? 305  TYR E N   1 
ATOM   10147 C CA  . TYR E  1 305 ? 14.949  54.859 49.035  1.00 31.94  ? 305  TYR E CA  1 
ATOM   10148 C C   . TYR E  1 305 ? 16.226  55.369 48.376  1.00 31.94  ? 305  TYR E C   1 
ATOM   10149 O O   . TYR E  1 305 ? 17.299  54.780 48.536  1.00 33.17  ? 305  TYR E O   1 
ATOM   10150 C CB  . TYR E  1 305 ? 14.951  55.239 50.513  1.00 32.93  ? 305  TYR E CB  1 
ATOM   10151 C CG  . TYR E  1 305 ? 15.210  56.711 50.734  1.00 32.95  ? 305  TYR E CG  1 
ATOM   10152 C CD1 . TYR E  1 305 ? 14.207  57.652 50.530  1.00 32.43  ? 305  TYR E CD1 1 
ATOM   10153 C CD2 . TYR E  1 305 ? 16.465  57.164 51.123  1.00 34.14  ? 305  TYR E CD2 1 
ATOM   10154 C CE1 . TYR E  1 305 ? 14.444  59.003 50.721  1.00 33.13  ? 305  TYR E CE1 1 
ATOM   10155 C CE2 . TYR E  1 305 ? 16.711  58.512 51.317  1.00 34.82  ? 305  TYR E CE2 1 
ATOM   10156 C CZ  . TYR E  1 305 ? 15.697  59.427 51.114  1.00 34.33  ? 305  TYR E CZ  1 
ATOM   10157 O OH  . TYR E  1 305 ? 15.931  60.769 51.306  1.00 35.66  ? 305  TYR E OH  1 
ATOM   10158 N N   . VAL E  1 306 ? 16.096  56.469 47.638  1.00 31.04  ? 306  VAL E N   1 
ATOM   10159 C CA  . VAL E  1 306 ? 17.245  57.192 47.102  1.00 31.51  ? 306  VAL E CA  1 
ATOM   10160 C C   . VAL E  1 306 ? 17.033  58.686 47.313  1.00 31.92  ? 306  VAL E C   1 
ATOM   10161 O O   . VAL E  1 306 ? 15.904  59.138 47.470  1.00 31.46  ? 306  VAL E O   1 
ATOM   10162 C CB  . VAL E  1 306 ? 17.481  56.892 45.603  1.00 30.55  ? 306  VAL E CB  1 
ATOM   10163 C CG1 . VAL E  1 306 ? 18.076  55.507 45.422  1.00 31.07  ? 306  VAL E CG1 1 
ATOM   10164 C CG2 . VAL E  1 306 ? 16.195  57.031 44.800  1.00 29.06  ? 306  VAL E CG2 1 
ATOM   10165 N N   . LYS E  1 307 ? 18.126  59.443 47.313  1.00 33.40  ? 307  LYS E N   1 
ATOM   10166 C CA  . LYS E  1 307 ? 18.074  60.897 47.481  1.00 34.66  ? 307  LYS E CA  1 
ATOM   10167 C C   . LYS E  1 307 ? 17.798  61.668 46.181  1.00 34.28  ? 307  LYS E C   1 
ATOM   10168 O O   . LYS E  1 307 ? 17.856  62.896 46.172  1.00 35.97  ? 307  LYS E O   1 
ATOM   10169 C CB  . LYS E  1 307 ? 19.389  61.405 48.083  1.00 37.25  ? 307  LYS E CB  1 
ATOM   10170 C CG  . LYS E  1 307 ? 19.590  61.077 49.548  1.00 38.42  ? 307  LYS E CG  1 
ATOM   10171 C CD  . LYS E  1 307 ? 20.752  61.883 50.103  1.00 41.65  ? 307  LYS E CD  1 
ATOM   10172 C CE  . LYS E  1 307 ? 21.260  61.323 51.421  1.00 43.21  ? 307  LYS E CE  1 
ATOM   10173 N NZ  . LYS E  1 307 ? 22.403  62.117 51.961  1.00 46.95  ? 307  LYS E NZ  1 
ATOM   10174 N N   . SER E  1 308 ? 17.500  60.968 45.090  1.00 32.51  ? 308  SER E N   1 
ATOM   10175 C CA  . SER E  1 308 ? 17.299  61.624 43.799  1.00 32.25  ? 308  SER E CA  1 
ATOM   10176 C C   . SER E  1 308 ? 15.989  62.401 43.764  1.00 32.42  ? 308  SER E C   1 
ATOM   10177 O O   . SER E  1 308 ? 15.019  62.035 44.432  1.00 31.92  ? 308  SER E O   1 
ATOM   10178 C CB  . SER E  1 308 ? 17.302  60.597 42.661  1.00 30.45  ? 308  SER E CB  1 
ATOM   10179 O OG  . SER E  1 308 ? 18.269  59.586 42.880  1.00 30.54  ? 308  SER E OG  1 
ATOM   10180 N N   . ASN E  1 309 ? 15.980  63.479 42.984  1.00 33.63  ? 309  ASN E N   1 
ATOM   10181 C CA  . ASN E  1 309 ? 14.751  64.187 42.640  1.00 34.29  ? 309  ASN E CA  1 
ATOM   10182 C C   . ASN E  1 309 ? 14.106  63.603 41.389  1.00 32.63  ? 309  ASN E C   1 
ATOM   10183 O O   . ASN E  1 309 ? 12.904  63.776 41.170  1.00 33.02  ? 309  ASN E O   1 
ATOM   10184 C CB  . ASN E  1 309 ? 15.029  65.673 42.413  1.00 37.21  ? 309  ASN E CB  1 
ATOM   10185 C CG  . ASN E  1 309 ? 15.294  66.423 43.706  1.00 39.61  ? 309  ASN E CG  1 
ATOM   10186 O OD1 . ASN E  1 309 ? 14.558  66.273 44.689  1.00 39.59  ? 309  ASN E OD1 1 
ATOM   10187 N ND2 . ASN E  1 309 ? 16.343  67.248 43.714  1.00 42.08  ? 309  ASN E ND2 1 
ATOM   10188 N N   . ARG E  1 310 ? 14.900  62.910 40.574  1.00 31.18  ? 310  ARG E N   1 
ATOM   10189 C CA  . ARG E  1 310 ? 14.441  62.448 39.268  1.00 29.89  ? 310  ARG E CA  1 
ATOM   10190 C C   . ARG E  1 310 ? 15.206  61.212 38.779  1.00 28.06  ? 310  ARG E C   1 
ATOM   10191 O O   . ARG E  1 310 ? 16.435  61.232 38.690  1.00 28.39  ? 310  ARG E O   1 
ATOM   10192 C CB  . ARG E  1 310 ? 14.598  63.588 38.257  1.00 31.38  ? 310  ARG E CB  1 
ATOM   10193 C CG  . ARG E  1 310 ? 13.830  63.401 36.960  1.00 30.77  ? 310  ARG E CG  1 
ATOM   10194 C CD  . ARG E  1 310 ? 14.102  64.534 35.982  1.00 32.58  ? 310  ARG E CD  1 
ATOM   10195 N NE  . ARG E  1 310 ? 13.946  64.081 34.598  1.00 31.47  ? 310  ARG E NE  1 
ATOM   10196 C CZ  . ARG E  1 310 ? 12.793  64.037 33.927  1.00 31.75  ? 310  ARG E CZ  1 
ATOM   10197 N NH1 . ARG E  1 310 ? 11.648  64.428 34.486  1.00 33.35  ? 310  ARG E NH1 1 
ATOM   10198 N NH2 . ARG E  1 310 ? 12.785  63.598 32.673  1.00 30.78  ? 310  ARG E NH2 1 
ATOM   10199 N N   . LEU E  1 311 ? 14.470  60.142 38.469  1.00 26.67  ? 311  LEU E N   1 
ATOM   10200 C CA  . LEU E  1 311 ? 15.032  58.958 37.807  1.00 25.42  ? 311  LEU E CA  1 
ATOM   10201 C C   . LEU E  1 311 ? 14.130  58.509 36.655  1.00 24.66  ? 311  LEU E C   1 
ATOM   10202 O O   . LEU E  1 311 ? 13.094  57.884 36.877  1.00 24.68  ? 311  LEU E O   1 
ATOM   10203 C CB  . LEU E  1 311 ? 15.213  57.803 38.792  1.00 25.24  ? 311  LEU E CB  1 
ATOM   10204 C CG  . LEU E  1 311 ? 16.259  57.948 39.901  1.00 26.15  ? 311  LEU E CG  1 
ATOM   10205 C CD1 . LEU E  1 311 ? 16.181  56.743 40.823  1.00 26.30  ? 311  LEU E CD1 1 
ATOM   10206 C CD2 . LEU E  1 311 ? 17.664  58.093 39.339  1.00 26.74  ? 311  LEU E CD2 1 
ATOM   10207 N N   . VAL E  1 312 ? 14.534  58.829 35.429  1.00 24.31  ? 312  VAL E N   1 
ATOM   10208 C CA  . VAL E  1 312 ? 13.761  58.485 34.240  1.00 23.82  ? 312  VAL E CA  1 
ATOM   10209 C C   . VAL E  1 312 ? 14.629  57.706 33.258  1.00 22.90  ? 312  VAL E C   1 
ATOM   10210 O O   . VAL E  1 312 ? 15.702  58.166 32.869  1.00 23.00  ? 312  VAL E O   1 
ATOM   10211 C CB  . VAL E  1 312 ? 13.224  59.747 33.540  1.00 24.81  ? 312  VAL E CB  1 
ATOM   10212 C CG1 . VAL E  1 312 ? 12.331  59.372 32.364  1.00 24.76  ? 312  VAL E CG1 1 
ATOM   10213 C CG2 . VAL E  1 312 ? 12.466  60.620 34.530  1.00 26.29  ? 312  VAL E CG2 1 
ATOM   10214 N N   . LEU E  1 313 ? 14.152  56.526 32.868  1.00 22.44  ? 313  LEU E N   1 
ATOM   10215 C CA  . LEU E  1 313 ? 14.833  55.685 31.889  1.00 21.93  ? 313  LEU E CA  1 
ATOM   10216 C C   . LEU E  1 313 ? 14.263  55.901 30.500  1.00 21.70  ? 313  LEU E C   1 
ATOM   10217 O O   . LEU E  1 313 ? 13.045  55.884 30.323  1.00 22.20  ? 313  LEU E O   1 
ATOM   10218 C CB  . LEU E  1 313 ? 14.673  54.206 32.242  1.00 22.29  ? 313  LEU E CB  1 
ATOM   10219 C CG  . LEU E  1 313 ? 15.588  53.667 33.335  1.00 22.86  ? 313  LEU E CG  1 
ATOM   10220 C CD1 . LEU E  1 313 ? 15.104  52.304 33.804  1.00 23.88  ? 313  LEU E CD1 1 
ATOM   10221 C CD2 . LEU E  1 313 ? 17.023  53.591 32.837  1.00 23.08  ? 313  LEU E CD2 1 
ATOM   10222 N N   . ALA E  1 314 ? 15.141  56.083 29.516  1.00 21.30  ? 314  ALA E N   1 
ATOM   10223 C CA  . ALA E  1 314 ? 14.724  56.101 28.119  1.00 21.13  ? 314  ALA E CA  1 
ATOM   10224 C C   . ALA E  1 314 ? 14.315  54.696 27.723  1.00 21.22  ? 314  ALA E C   1 
ATOM   10225 O O   . ALA E  1 314 ? 15.050  53.744 27.974  1.00 21.35  ? 314  ALA E O   1 
ATOM   10226 C CB  . ALA E  1 314 ? 15.849  56.587 27.220  1.00 20.91  ? 314  ALA E CB  1 
ATOM   10227 N N   . THR E  1 315 ? 13.124  54.572 27.147  1.00 21.79  ? 315  THR E N   1 
ATOM   10228 C CA  . THR E  1 315 ? 12.695  53.335 26.504  1.00 22.46  ? 315  THR E CA  1 
ATOM   10229 C C   . THR E  1 315 ? 12.695  53.526 24.995  1.00 22.31  ? 315  THR E C   1 
ATOM   10230 O O   . THR E  1 315 ? 13.182  52.679 24.258  1.00 22.31  ? 315  THR E O   1 
ATOM   10231 C CB  . THR E  1 315 ? 11.290  52.892 26.966  1.00 23.98  ? 315  THR E CB  1 
ATOM   10232 O OG1 . THR E  1 315 ? 10.402  54.016 26.984  1.00 24.51  ? 315  THR E OG1 1 
ATOM   10233 C CG2 . THR E  1 315 ? 11.356  52.283 28.359  1.00 24.42  ? 315  THR E CG2 1 
ATOM   10234 N N   . GLY E  1 316 ? 12.150  54.649 24.546  1.00 22.53  ? 316  GLY E N   1 
ATOM   10235 C CA  . GLY E  1 316 ? 12.099  54.966 23.134  1.00 22.65  ? 316  GLY E CA  1 
ATOM   10236 C C   . GLY E  1 316 ? 13.372  55.627 22.656  1.00 21.67  ? 316  GLY E C   1 
ATOM   10237 O O   . GLY E  1 316 ? 14.398  55.614 23.339  1.00 21.03  ? 316  GLY E O   1 
ATOM   10238 N N   . LEU E  1 317 ? 13.292  56.213 21.470  1.00 22.00  ? 317  LEU E N   1 
ATOM   10239 C CA  . LEU E  1 317 ? 14.453  56.804 20.817  1.00 21.57  ? 317  LEU E CA  1 
ATOM   10240 C C   . LEU E  1 317 ? 14.343  58.322 20.819  1.00 22.63  ? 317  LEU E C   1 
ATOM   10241 O O   . LEU E  1 317 ? 13.324  58.879 21.218  1.00 23.70  ? 317  LEU E O   1 
ATOM   10242 C CB  . LEU E  1 317 ? 14.614  56.247 19.393  1.00 21.38  ? 317  LEU E CB  1 
ATOM   10243 C CG  . LEU E  1 317 ? 13.402  56.227 18.456  1.00 22.35  ? 317  LEU E CG  1 
ATOM   10244 C CD1 . LEU E  1 317 ? 13.207  57.584 17.807  1.00 23.28  ? 317  LEU E CD1 1 
ATOM   10245 C CD2 . LEU E  1 317 ? 13.547  55.144 17.398  1.00 22.20  ? 317  LEU E CD2 1 
ATOM   10246 N N   . ARG E  1 318 ? 15.412  58.977 20.387  1.00 22.90  ? 318  ARG E N   1 
ATOM   10247 C CA  . ARG E  1 318 ? 15.473  60.430 20.352  1.00 24.63  ? 318  ARG E CA  1 
ATOM   10248 C C   . ARG E  1 318 ? 14.370  60.977 19.457  1.00 26.16  ? 318  ARG E C   1 
ATOM   10249 O O   . ARG E  1 318 ? 14.292  60.642 18.276  1.00 25.98  ? 318  ARG E O   1 
ATOM   10250 C CB  . ARG E  1 318 ? 16.841  60.881 19.848  1.00 25.01  ? 318  ARG E CB  1 
ATOM   10251 C CG  . ARG E  1 318 ? 17.018  62.384 19.735  1.00 27.35  ? 318  ARG E CG  1 
ATOM   10252 C CD  . ARG E  1 318 ? 18.377  62.718 19.140  1.00 28.17  ? 318  ARG E CD  1 
ATOM   10253 N NE  . ARG E  1 318 ? 19.464  62.510 20.097  1.00 28.19  ? 318  ARG E NE  1 
ATOM   10254 C CZ  . ARG E  1 318 ? 20.013  63.465 20.846  1.00 30.26  ? 318  ARG E CZ  1 
ATOM   10255 N NH1 . ARG E  1 318 ? 19.585  64.723 20.773  1.00 32.60  ? 318  ARG E NH1 1 
ATOM   10256 N NH2 . ARG E  1 318 ? 20.999  63.158 21.682  1.00 30.49  ? 318  ARG E NH2 1 
ATOM   10257 N N   . ASN E  1 319 ? 13.525  61.824 20.035  1.00 28.14  ? 319  ASN E N   1 
ATOM   10258 C CA  . ASN E  1 319 ? 12.359  62.353 19.347  1.00 30.41  ? 319  ASN E CA  1 
ATOM   10259 C C   . ASN E  1 319 ? 12.707  63.629 18.590  1.00 32.88  ? 319  ASN E C   1 
ATOM   10260 O O   . ASN E  1 319 ? 13.436  64.486 19.090  1.00 33.95  ? 319  ASN E O   1 
ATOM   10261 C CB  . ASN E  1 319 ? 11.245  62.613 20.355  1.00 31.87  ? 319  ASN E CB  1 
ATOM   10262 C CG  . ASN E  1 319 ? 9.910   62.884 19.699  1.00 34.45  ? 319  ASN E CG  1 
ATOM   10263 O OD1 . ASN E  1 319 ? 9.758   62.764 18.488  1.00 34.86  ? 319  ASN E OD1 1 
ATOM   10264 N ND2 . ASN E  1 319 ? 8.927   63.256 20.507  1.00 36.55  ? 319  ASN E ND2 1 
ATOM   10265 N N   . SER E  1 320 ? 12.166  63.748 17.381  1.00 34.40  ? 320  SER E N   1 
ATOM   10266 C CA  . SER E  1 320 ? 12.521  64.831 16.460  1.00 36.90  ? 320  SER E CA  1 
ATOM   10267 C C   . SER E  1 320 ? 11.757  66.134 16.746  1.00 41.13  ? 320  SER E C   1 
ATOM   10268 O O   . SER E  1 320 ? 10.646  66.100 17.271  1.00 42.51  ? 320  SER E O   1 
ATOM   10269 C CB  . SER E  1 320 ? 12.258  64.383 15.019  1.00 36.76  ? 320  SER E CB  1 
ATOM   10270 O OG  . SER E  1 320 ? 12.988  63.199 14.729  1.00 33.59  ? 320  SER E OG  1 
ATOM   10271 N N   . PRO E  1 321 ? 12.363  67.291 16.410  1.00 43.89  ? 321  PRO E N   1 
ATOM   10272 C CA  . PRO E  1 321 ? 11.699  68.593 16.502  1.00 48.70  ? 321  PRO E CA  1 
ATOM   10273 C C   . PRO E  1 321 ? 10.997  68.981 15.203  1.00 51.63  ? 321  PRO E C   1 
ATOM   10274 O O   . PRO E  1 321 ? 9.878   68.539 14.948  1.00 52.34  ? 321  PRO E O   1 
ATOM   10275 C CB  . PRO E  1 321 ? 12.863  69.547 16.768  1.00 50.33  ? 321  PRO E CB  1 
ATOM   10276 C CG  . PRO E  1 321 ? 14.002  68.933 16.022  1.00 47.49  ? 321  PRO E CG  1 
ATOM   10277 C CD  . PRO E  1 321 ? 13.802  67.439 16.104  1.00 43.01  ? 321  PRO E CD  1 
ATOM   10278 N N   . GLY F  2 1   ? 24.342  60.818 17.105  1.00 22.95  ? 1    GLY F N   1 
ATOM   10279 C CA  . GLY F  2 1   ? 24.515  59.494 17.766  1.00 21.39  ? 1    GLY F CA  1 
ATOM   10280 C C   . GLY F  2 1   ? 25.682  58.712 17.200  1.00 21.81  ? 1    GLY F C   1 
ATOM   10281 O O   . GLY F  2 1   ? 26.194  59.029 16.126  1.00 23.05  ? 1    GLY F O   1 
ATOM   10282 N N   . LEU F  2 2   ? 26.087  57.674 17.923  1.00 21.10  ? 2    LEU F N   1 
ATOM   10283 C CA  . LEU F  2 2   ? 27.284  56.913 17.579  1.00 22.05  ? 2    LEU F CA  1 
ATOM   10284 C C   . LEU F  2 2   ? 27.224  56.266 16.201  1.00 22.51  ? 2    LEU F C   1 
ATOM   10285 O O   . LEU F  2 2   ? 28.245  56.153 15.527  1.00 24.12  ? 2    LEU F O   1 
ATOM   10286 C CB  . LEU F  2 2   ? 27.555  55.836 18.632  1.00 21.46  ? 2    LEU F CB  1 
ATOM   10287 C CG  . LEU F  2 2   ? 28.172  56.288 19.951  1.00 21.57  ? 2    LEU F CG  1 
ATOM   10288 C CD1 . LEU F  2 2   ? 28.358  55.092 20.864  1.00 21.16  ? 2    LEU F CD1 1 
ATOM   10289 C CD2 . LEU F  2 2   ? 29.497  56.995 19.726  1.00 23.53  ? 2    LEU F CD2 1 
ATOM   10290 N N   . PHE F  2 3   ? 26.031  55.851 15.785  1.00 21.41  ? 3    PHE F N   1 
ATOM   10291 C CA  . PHE F  2 3   ? 25.883  55.072 14.557  1.00 21.78  ? 3    PHE F CA  1 
ATOM   10292 C C   . PHE F  2 3   ? 25.463  55.906 13.360  1.00 22.25  ? 3    PHE F C   1 
ATOM   10293 O O   . PHE F  2 3   ? 25.408  55.402 12.243  1.00 22.71  ? 3    PHE F O   1 
ATOM   10294 C CB  . PHE F  2 3   ? 24.971  53.880 14.820  1.00 20.78  ? 3    PHE F CB  1 
ATOM   10295 C CG  . PHE F  2 3   ? 25.562  52.932 15.814  1.00 20.96  ? 3    PHE F CG  1 
ATOM   10296 C CD1 . PHE F  2 3   ? 26.454  51.954 15.406  1.00 22.36  ? 3    PHE F CD1 1 
ATOM   10297 C CD2 . PHE F  2 3   ? 25.312  53.086 17.168  1.00 20.11  ? 3    PHE F CD2 1 
ATOM   10298 C CE1 . PHE F  2 3   ? 27.045  51.112 16.327  1.00 22.99  ? 3    PHE F CE1 1 
ATOM   10299 C CE2 . PHE F  2 3   ? 25.902  52.250 18.094  1.00 20.49  ? 3    PHE F CE2 1 
ATOM   10300 C CZ  . PHE F  2 3   ? 26.769  51.260 17.672  1.00 21.98  ? 3    PHE F CZ  1 
ATOM   10301 N N   . GLY F  2 4   ? 25.202  57.188 13.602  1.00 22.46  ? 4    GLY F N   1 
ATOM   10302 C CA  . GLY F  2 4   ? 25.121  58.181 12.543  1.00 23.68  ? 4    GLY F CA  1 
ATOM   10303 C C   . GLY F  2 4   ? 23.846  58.198 11.731  1.00 23.19  ? 4    GLY F C   1 
ATOM   10304 O O   . GLY F  2 4   ? 23.774  58.916 10.740  1.00 24.32  ? 4    GLY F O   1 
ATOM   10305 N N   . ALA F  2 5   ? 22.844  57.425 12.142  1.00 21.86  ? 5    ALA F N   1 
ATOM   10306 C CA  . ALA F  2 5   ? 21.595  57.309 11.392  1.00 21.64  ? 5    ALA F CA  1 
ATOM   10307 C C   . ALA F  2 5   ? 20.550  58.267 11.934  1.00 21.84  ? 5    ALA F C   1 
ATOM   10308 O O   . ALA F  2 5   ? 20.118  59.173 11.231  1.00 22.88  ? 5    ALA F O   1 
ATOM   10309 C CB  . ALA F  2 5   ? 21.084  55.880 11.430  1.00 20.75  ? 5    ALA F CB  1 
ATOM   10310 N N   . ILE F  2 6   ? 20.164  58.069 13.191  1.00 21.20  ? 6    ILE F N   1 
ATOM   10311 C CA  . ILE F  2 6   ? 19.166  58.913 13.848  1.00 21.78  ? 6    ILE F CA  1 
ATOM   10312 C C   . ILE F  2 6   ? 19.708  60.324 14.024  1.00 23.17  ? 6    ILE F C   1 
ATOM   10313 O O   . ILE F  2 6   ? 20.773  60.511 14.607  1.00 23.22  ? 6    ILE F O   1 
ATOM   10314 C CB  . ILE F  2 6   ? 18.749  58.333 15.219  1.00 20.97  ? 6    ILE F CB  1 
ATOM   10315 C CG1 . ILE F  2 6   ? 17.929  57.058 15.010  1.00 20.43  ? 6    ILE F CG1 1 
ATOM   10316 C CG2 . ILE F  2 6   ? 17.949  59.348 16.022  1.00 21.94  ? 6    ILE F CG2 1 
ATOM   10317 C CD1 . ILE F  2 6   ? 17.574  56.322 16.282  1.00 19.98  ? 6    ILE F CD1 1 
ATOM   10318 N N   . ALA F  2 7   ? 18.968  61.310 13.523  1.00 24.75  ? 7    ALA F N   1 
ATOM   10319 C CA  . ALA F  2 7   ? 19.416  62.704 13.509  1.00 26.77  ? 7    ALA F CA  1 
ATOM   10320 C C   . ALA F  2 7   ? 20.786  62.825 12.855  1.00 27.30  ? 7    ALA F C   1 
ATOM   10321 O O   . ALA F  2 7   ? 21.595  63.655 13.248  1.00 28.63  ? 7    ALA F O   1 
ATOM   10322 C CB  . ALA F  2 7   ? 19.446  63.271 14.922  1.00 27.14  ? 7    ALA F CB  1 
ATOM   10323 N N   . GLY F  2 8   ? 21.033  61.989 11.853  1.00 26.62  ? 8    GLY F N   1 
ATOM   10324 C CA  . GLY F  2 8   ? 22.326  61.924 11.193  1.00 27.37  ? 8    GLY F CA  1 
ATOM   10325 C C   . GLY F  2 8   ? 22.123  62.043 9.703   1.00 28.40  ? 8    GLY F C   1 
ATOM   10326 O O   . GLY F  2 8   ? 21.807  63.125 9.216   1.00 30.30  ? 8    GLY F O   1 
ATOM   10327 N N   . PHE F  2 9   ? 22.300  60.942 8.977   1.00 27.48  ? 9    PHE F N   1 
ATOM   10328 C CA  . PHE F  2 9   ? 22.014  60.942 7.549   1.00 28.30  ? 9    PHE F CA  1 
ATOM   10329 C C   . PHE F  2 9   ? 20.508  60.799 7.315   1.00 27.68  ? 9    PHE F C   1 
ATOM   10330 O O   . PHE F  2 9   ? 20.025  61.091 6.226   1.00 28.67  ? 9    PHE F O   1 
ATOM   10331 C CB  . PHE F  2 9   ? 22.856  59.902 6.776   1.00 28.08  ? 9    PHE F CB  1 
ATOM   10332 C CG  . PHE F  2 9   ? 22.420  58.469 6.957   1.00 26.20  ? 9    PHE F CG  1 
ATOM   10333 C CD1 . PHE F  2 9   ? 21.493  57.896 6.099   1.00 25.69  ? 9    PHE F CD1 1 
ATOM   10334 C CD2 . PHE F  2 9   ? 22.982  57.678 7.948   1.00 25.31  ? 9    PHE F CD2 1 
ATOM   10335 C CE1 . PHE F  2 9   ? 21.108  56.575 6.251   1.00 24.49  ? 9    PHE F CE1 1 
ATOM   10336 C CE2 . PHE F  2 9   ? 22.601  56.356 8.105   1.00 24.15  ? 9    PHE F CE2 1 
ATOM   10337 C CZ  . PHE F  2 9   ? 21.661  55.803 7.256   1.00 23.83  ? 9    PHE F CZ  1 
ATOM   10338 N N   . ILE F  2 10  ? 19.780  60.350 8.339   1.00 26.44  ? 10   ILE F N   1 
ATOM   10339 C CA  . ILE F  2 10  ? 18.317  60.424 8.365   1.00 26.51  ? 10   ILE F CA  1 
ATOM   10340 C C   . ILE F  2 10  ? 17.926  61.561 9.302   1.00 27.75  ? 10   ILE F C   1 
ATOM   10341 O O   . ILE F  2 10  ? 17.840  61.379 10.515  1.00 27.00  ? 10   ILE F O   1 
ATOM   10342 C CB  . ILE F  2 10  ? 17.680  59.101 8.831   1.00 24.89  ? 10   ILE F CB  1 
ATOM   10343 C CG1 . ILE F  2 10  ? 18.207  57.930 7.991   1.00 24.11  ? 10   ILE F CG1 1 
ATOM   10344 C CG2 . ILE F  2 10  ? 16.163  59.176 8.727   1.00 25.48  ? 10   ILE F CG2 1 
ATOM   10345 C CD1 . ILE F  2 10  ? 17.847  56.566 8.537   1.00 22.99  ? 10   ILE F CD1 1 
ATOM   10346 N N   . GLU F  2 11  ? 17.694  62.736 8.726   1.00 30.00  ? 11   GLU F N   1 
ATOM   10347 C CA  . GLU F  2 11  ? 17.529  63.974 9.496   1.00 31.98  ? 11   GLU F CA  1 
ATOM   10348 C C   . GLU F  2 11  ? 16.488  63.935 10.608  1.00 31.91  ? 11   GLU F C   1 
ATOM   10349 O O   . GLU F  2 11  ? 16.677  64.565 11.649  1.00 32.66  ? 11   GLU F O   1 
ATOM   10350 C CB  . GLU F  2 11  ? 17.152  65.126 8.573   1.00 34.86  ? 11   GLU F CB  1 
ATOM   10351 C CG  . GLU F  2 11  ? 18.306  65.776 7.838   1.00 36.41  ? 11   GLU F CG  1 
ATOM   10352 C CD  . GLU F  2 11  ? 17.858  67.049 7.141   1.00 39.86  ? 11   GLU F CD  1 
ATOM   10353 O OE1 . GLU F  2 11  ? 16.920  66.968 6.307   1.00 40.36  ? 11   GLU F OE1 1 
ATOM   10354 O OE2 . GLU F  2 11  ? 18.424  68.127 7.442   1.00 42.37  ? 11   GLU F OE2 1 
ATOM   10355 N N   . GLY F  2 12  ? 15.385  63.229 10.377  1.00 31.43  ? 12   GLY F N   1 
ATOM   10356 C CA  . GLY F  2 12  ? 14.274  63.224 11.325  1.00 32.07  ? 12   GLY F CA  1 
ATOM   10357 C C   . GLY F  2 12  ? 13.416  61.977 11.291  1.00 30.90  ? 12   GLY F C   1 
ATOM   10358 O O   . GLY F  2 12  ? 13.465  61.194 10.339  1.00 29.90  ? 12   GLY F O   1 
ATOM   10359 N N   . GLY F  2 13  ? 12.631  61.801 12.351  1.00 31.38  ? 13   GLY F N   1 
ATOM   10360 C CA  . GLY F  2 13  ? 11.710  60.679 12.472  1.00 31.02  ? 13   GLY F CA  1 
ATOM   10361 C C   . GLY F  2 13  ? 10.398  60.923 11.741  1.00 33.35  ? 13   GLY F C   1 
ATOM   10362 O O   . GLY F  2 13  ? 10.183  61.987 11.157  1.00 35.31  ? 13   GLY F O   1 
ATOM   10363 N N   . TRP F  2 14  ? 9.521   59.925 11.786  1.00 33.52  ? 14   TRP F N   1 
ATOM   10364 C CA  . TRP F  2 14  ? 8.258   59.959 11.074  1.00 35.81  ? 14   TRP F CA  1 
ATOM   10365 C C   . TRP F  2 14  ? 7.073   59.913 12.029  1.00 38.10  ? 14   TRP F C   1 
ATOM   10366 O O   . TRP F  2 14  ? 6.769   58.869 12.609  1.00 37.60  ? 14   TRP F O   1 
ATOM   10367 C CB  . TRP F  2 14  ? 8.172   58.777 10.107  1.00 34.69  ? 14   TRP F CB  1 
ATOM   10368 C CG  . TRP F  2 14  ? 9.142   58.835 8.971   1.00 33.21  ? 14   TRP F CG  1 
ATOM   10369 C CD1 . TRP F  2 14  ? 9.701   59.951 8.425   1.00 33.75  ? 14   TRP F CD1 1 
ATOM   10370 C CD2 . TRP F  2 14  ? 9.635   57.726 8.209   1.00 31.52  ? 14   TRP F CD2 1 
ATOM   10371 N NE1 . TRP F  2 14  ? 10.522  59.605 7.383   1.00 32.38  ? 14   TRP F NE1 1 
ATOM   10372 C CE2 . TRP F  2 14  ? 10.498  58.245 7.227   1.00 31.01  ? 14   TRP F CE2 1 
ATOM   10373 C CE3 . TRP F  2 14  ? 9.431   56.345 8.265   1.00 30.82  ? 14   TRP F CE3 1 
ATOM   10374 C CZ2 . TRP F  2 14  ? 11.162  57.432 6.309   1.00 29.60  ? 14   TRP F CZ2 1 
ATOM   10375 C CZ3 . TRP F  2 14  ? 10.092  55.540 7.354   1.00 29.52  ? 14   TRP F CZ3 1 
ATOM   10376 C CH2 . TRP F  2 14  ? 10.945  56.086 6.386   1.00 28.87  ? 14   TRP F CH2 1 
ATOM   10377 N N   . GLN F  2 15  ? 6.398   61.053 12.169  1.00 41.04  ? 15   GLN F N   1 
ATOM   10378 C CA  . GLN F  2 15  ? 5.106   61.126 12.858  1.00 44.25  ? 15   GLN F CA  1 
ATOM   10379 C C   . GLN F  2 15  ? 4.103   60.156 12.218  1.00 45.25  ? 15   GLN F C   1 
ATOM   10380 O O   . GLN F  2 15  ? 3.222   59.633 12.899  1.00 47.13  ? 15   GLN F O   1 
ATOM   10381 C CB  . GLN F  2 15  ? 4.530   62.544 12.782  1.00 47.95  ? 15   GLN F CB  1 
ATOM   10382 C CG  . GLN F  2 15  ? 5.362   63.638 13.442  1.00 47.98  ? 15   GLN F CG  1 
ATOM   10383 C CD  . GLN F  2 15  ? 5.063   63.831 14.921  1.00 49.42  ? 15   GLN F CD  1 
ATOM   10384 O OE1 . GLN F  2 15  ? 5.978   63.972 15.729  1.00 47.64  ? 15   GLN F OE1 1 
ATOM   10385 N NE2 . GLN F  2 15  ? 3.783   63.849 15.280  1.00 53.00  ? 15   GLN F NE2 1 
ATOM   10386 N N   . GLY F  2 16  ? 4.243   59.933 10.910  1.00 44.26  ? 16   GLY F N   1 
ATOM   10387 C CA  . GLY F  2 16  ? 3.340   59.071 10.153  1.00 45.34  ? 16   GLY F CA  1 
ATOM   10388 C C   . GLY F  2 16  ? 3.484   57.569 10.346  1.00 43.46  ? 16   GLY F C   1 
ATOM   10389 O O   . GLY F  2 16  ? 2.639   56.810 9.879   1.00 44.99  ? 16   GLY F O   1 
ATOM   10390 N N   . MET F  2 17  ? 4.544   57.127 11.017  1.00 40.55  ? 17   MET F N   1 
ATOM   10391 C CA  . MET F  2 17  ? 4.723   55.702 11.312  1.00 39.24  ? 17   MET F CA  1 
ATOM   10392 C C   . MET F  2 17  ? 4.434   55.405 12.783  1.00 40.17  ? 17   MET F C   1 
ATOM   10393 O O   . MET F  2 17  ? 5.277   55.640 13.648  1.00 38.44  ? 17   MET F O   1 
ATOM   10394 C CB  . MET F  2 17  ? 6.136   55.258 10.960  1.00 35.73  ? 17   MET F CB  1 
ATOM   10395 C CG  . MET F  2 17  ? 6.329   53.755 11.046  1.00 34.92  ? 17   MET F CG  1 
ATOM   10396 S SD  . MET F  2 17  ? 7.946   53.258 10.449  1.00 31.59  ? 17   MET F SD  1 
ATOM   10397 C CE  . MET F  2 17  ? 8.981   54.181 11.583  1.00 30.00  ? 17   MET F CE  1 
ATOM   10398 N N   . VAL F  2 18  ? 3.245   54.870 13.054  1.00 43.12  ? 18   VAL F N   1 
ATOM   10399 C CA  . VAL F  2 18  ? 2.759   54.686 14.430  1.00 44.93  ? 18   VAL F CA  1 
ATOM   10400 C C   . VAL F  2 18  ? 2.801   53.236 14.933  1.00 44.78  ? 18   VAL F C   1 
ATOM   10401 O O   . VAL F  2 18  ? 2.720   52.997 16.135  1.00 45.57  ? 18   VAL F O   1 
ATOM   10402 C CB  . VAL F  2 18  ? 1.320   55.237 14.588  1.00 49.46  ? 18   VAL F CB  1 
ATOM   10403 C CG1 . VAL F  2 18  ? 1.226   56.648 14.024  1.00 50.25  ? 18   VAL F CG1 1 
ATOM   10404 C CG2 . VAL F  2 18  ? 0.296   54.324 13.923  1.00 52.06  ? 18   VAL F CG2 1 
ATOM   10405 N N   . ASP F  2 19  ? 2.936   52.278 14.022  1.00 44.04  ? 19   ASP F N   1 
ATOM   10406 C CA  . ASP F  2 19  ? 2.864   50.853 14.370  1.00 44.76  ? 19   ASP F CA  1 
ATOM   10407 C C   . ASP F  2 19  ? 4.240   50.213 14.634  1.00 41.43  ? 19   ASP F C   1 
ATOM   10408 O O   . ASP F  2 19  ? 4.348   48.992 14.766  1.00 41.98  ? 19   ASP F O   1 
ATOM   10409 C CB  . ASP F  2 19  ? 2.096   50.074 13.283  1.00 46.81  ? 19   ASP F CB  1 
ATOM   10410 C CG  . ASP F  2 19  ? 2.650   50.300 11.877  1.00 44.59  ? 19   ASP F CG  1 
ATOM   10411 O OD1 . ASP F  2 19  ? 3.548   51.153 11.700  1.00 41.85  ? 19   ASP F OD1 1 
ATOM   10412 O OD2 . ASP F  2 19  ? 2.174   49.626 10.937  1.00 45.85  ? 19   ASP F OD2 1 
ATOM   10413 N N   . GLY F  2 20  ? 5.286   51.029 14.730  1.00 38.44  ? 20   GLY F N   1 
ATOM   10414 C CA  . GLY F  2 20  ? 6.621   50.509 15.013  1.00 35.67  ? 20   GLY F CA  1 
ATOM   10415 C C   . GLY F  2 20  ? 7.660   51.577 15.273  1.00 33.08  ? 20   GLY F C   1 
ATOM   10416 O O   . GLY F  2 20  ? 7.406   52.765 15.079  1.00 33.29  ? 20   GLY F O   1 
ATOM   10417 N N   . TRP F  2 21  ? 8.840   51.142 15.707  1.00 31.02  ? 21   TRP F N   1 
ATOM   10418 C CA  . TRP F  2 21  ? 9.956   52.050 15.984  1.00 28.76  ? 21   TRP F CA  1 
ATOM   10419 C C   . TRP F  2 21  ? 10.783  52.330 14.734  1.00 27.13  ? 21   TRP F C   1 
ATOM   10420 O O   . TRP F  2 21  ? 11.246  53.456 14.531  1.00 26.29  ? 21   TRP F O   1 
ATOM   10421 C CB  . TRP F  2 21  ? 10.861  51.491 17.089  1.00 27.70  ? 21   TRP F CB  1 
ATOM   10422 C CG  . TRP F  2 21  ? 10.533  51.983 18.477  1.00 28.40  ? 21   TRP F CG  1 
ATOM   10423 C CD1 . TRP F  2 21  ? 9.983   53.192 18.826  1.00 29.22  ? 21   TRP F CD1 1 
ATOM   10424 C CD2 . TRP F  2 21  ? 10.781  51.295 19.701  1.00 28.58  ? 21   TRP F CD2 1 
ATOM   10425 N NE1 . TRP F  2 21  ? 9.855   53.282 20.188  1.00 29.84  ? 21   TRP F NE1 1 
ATOM   10426 C CE2 . TRP F  2 21  ? 10.339  52.133 20.751  1.00 29.36  ? 21   TRP F CE2 1 
ATOM   10427 C CE3 . TRP F  2 21  ? 11.330  50.047 20.015  1.00 28.49  ? 21   TRP F CE3 1 
ATOM   10428 C CZ2 . TRP F  2 21  ? 10.432  51.763 22.088  1.00 29.78  ? 21   TRP F CZ2 1 
ATOM   10429 C CZ3 . TRP F  2 21  ? 11.422  49.679 21.347  1.00 29.02  ? 21   TRP F CZ3 1 
ATOM   10430 C CH2 . TRP F  2 21  ? 10.975  50.535 22.369  1.00 29.54  ? 21   TRP F CH2 1 
ATOM   10431 N N   . TYR F  2 22  ? 10.980  51.300 13.915  1.00 27.00  ? 22   TYR F N   1 
ATOM   10432 C CA  . TYR F  2 22  ? 11.724  51.428 12.668  1.00 25.83  ? 22   TYR F CA  1 
ATOM   10433 C C   . TYR F  2 22  ? 10.909  50.822 11.537  1.00 27.10  ? 22   TYR F C   1 
ATOM   10434 O O   . TYR F  2 22  ? 10.150  49.873 11.743  1.00 28.66  ? 22   TYR F O   1 
ATOM   10435 C CB  . TYR F  2 22  ? 13.075  50.707 12.755  1.00 24.56  ? 22   TYR F CB  1 
ATOM   10436 C CG  . TYR F  2 22  ? 13.655  50.610 14.144  1.00 23.99  ? 22   TYR F CG  1 
ATOM   10437 C CD1 . TYR F  2 22  ? 14.176  51.728 14.781  1.00 22.98  ? 22   TYR F CD1 1 
ATOM   10438 C CD2 . TYR F  2 22  ? 13.676  49.399 14.825  1.00 24.77  ? 22   TYR F CD2 1 
ATOM   10439 C CE1 . TYR F  2 22  ? 14.708  51.641 16.056  1.00 22.51  ? 22   TYR F CE1 1 
ATOM   10440 C CE2 . TYR F  2 22  ? 14.201  49.304 16.099  1.00 24.38  ? 22   TYR F CE2 1 
ATOM   10441 C CZ  . TYR F  2 22  ? 14.718  50.425 16.705  1.00 23.12  ? 22   TYR F CZ  1 
ATOM   10442 O OH  . TYR F  2 22  ? 15.240  50.335 17.968  1.00 22.78  ? 22   TYR F OH  1 
ATOM   10443 N N   . GLY F  2 23  ? 11.075  51.367 10.339  1.00 26.68  ? 23   GLY F N   1 
ATOM   10444 C CA  . GLY F  2 23  ? 10.372  50.844 9.186   1.00 27.81  ? 23   GLY F CA  1 
ATOM   10445 C C   . GLY F  2 23  ? 10.708  51.550 7.896   1.00 27.22  ? 23   GLY F C   1 
ATOM   10446 O O   . GLY F  2 23  ? 11.746  52.209 7.788   1.00 25.88  ? 23   GLY F O   1 
ATOM   10447 N N   . TYR F  2 24  ? 9.805   51.412 6.926   1.00 28.52  ? 24   TYR F N   1 
ATOM   10448 C CA  . TYR F  2 24  ? 10.026  51.871 5.559   1.00 28.28  ? 24   TYR F CA  1 
ATOM   10449 C C   . TYR F  2 24  ? 8.956   52.856 5.119   1.00 29.69  ? 24   TYR F C   1 
ATOM   10450 O O   . TYR F  2 24  ? 7.823   52.794 5.581   1.00 31.37  ? 24   TYR F O   1 
ATOM   10451 C CB  . TYR F  2 24  ? 10.000  50.686 4.591   1.00 28.75  ? 24   TYR F CB  1 
ATOM   10452 C CG  . TYR F  2 24  ? 10.743  49.466 5.068   1.00 28.47  ? 24   TYR F CG  1 
ATOM   10453 C CD1 . TYR F  2 24  ? 10.173  48.604 5.992   1.00 29.66  ? 24   TYR F CD1 1 
ATOM   10454 C CD2 . TYR F  2 24  ? 12.014  49.164 4.586   1.00 27.51  ? 24   TYR F CD2 1 
ATOM   10455 C CE1 . TYR F  2 24  ? 10.846  47.478 6.430   1.00 29.85  ? 24   TYR F CE1 1 
ATOM   10456 C CE2 . TYR F  2 24  ? 12.695  48.037 5.020   1.00 27.75  ? 24   TYR F CE2 1 
ATOM   10457 C CZ  . TYR F  2 24  ? 12.106  47.197 5.941   1.00 28.90  ? 24   TYR F CZ  1 
ATOM   10458 O OH  . TYR F  2 24  ? 12.768  46.075 6.382   1.00 29.58  ? 24   TYR F OH  1 
ATOM   10459 N N   . HIS F  2 25  ? 9.330   53.760 4.221   1.00 29.42  ? 25   HIS F N   1 
ATOM   10460 C CA  . HIS F  2 25  ? 8.365   54.574 3.502   1.00 31.14  ? 25   HIS F CA  1 
ATOM   10461 C C   . HIS F  2 25  ? 8.615   54.453 2.009   1.00 31.02  ? 25   HIS F C   1 
ATOM   10462 O O   . HIS F  2 25  ? 9.705   54.763 1.531   1.00 29.88  ? 25   HIS F O   1 
ATOM   10463 C CB  . HIS F  2 25  ? 8.440   56.039 3.906   1.00 31.68  ? 25   HIS F CB  1 
ATOM   10464 C CG  . HIS F  2 25  ? 7.377   56.879 3.272   1.00 34.02  ? 25   HIS F CG  1 
ATOM   10465 N ND1 . HIS F  2 25  ? 7.582   57.586 2.107   1.00 34.46  ? 25   HIS F ND1 1 
ATOM   10466 C CD2 . HIS F  2 25  ? 6.089   57.099 3.625   1.00 36.44  ? 25   HIS F CD2 1 
ATOM   10467 C CE1 . HIS F  2 25  ? 6.473   58.224 1.782   1.00 36.98  ? 25   HIS F CE1 1 
ATOM   10468 N NE2 . HIS F  2 25  ? 5.552   57.945 2.686   1.00 38.30  ? 25   HIS F NE2 1 
ATOM   10469 N N   . HIS F  2 26  ? 7.594   54.003 1.284   1.00 32.51  ? 26   HIS F N   1 
ATOM   10470 C CA  . HIS F  2 26  ? 7.679   53.821 -0.163  1.00 32.62  ? 26   HIS F CA  1 
ATOM   10471 C C   . HIS F  2 26  ? 6.884   54.902 -0.877  1.00 34.39  ? 26   HIS F C   1 
ATOM   10472 O O   . HIS F  2 26  ? 5.934   55.433 -0.321  1.00 36.12  ? 26   HIS F O   1 
ATOM   10473 C CB  . HIS F  2 26  ? 7.157   52.434 -0.553  1.00 33.22  ? 26   HIS F CB  1 
ATOM   10474 C CG  . HIS F  2 26  ? 5.667   52.301 -0.482  1.00 35.60  ? 26   HIS F CG  1 
ATOM   10475 N ND1 . HIS F  2 26  ? 5.007   51.902 0.660   1.00 36.72  ? 26   HIS F ND1 1 
ATOM   10476 C CD2 . HIS F  2 26  ? 4.710   52.508 -1.417  1.00 37.41  ? 26   HIS F CD2 1 
ATOM   10477 C CE1 . HIS F  2 26  ? 3.707   51.875 0.428   1.00 39.30  ? 26   HIS F CE1 1 
ATOM   10478 N NE2 . HIS F  2 26  ? 3.500   52.239 -0.824  1.00 39.73  ? 26   HIS F NE2 1 
ATOM   10479 N N   . SER F  2 27  ? 7.292   55.239 -2.097  1.00 34.31  ? 27   SER F N   1 
ATOM   10480 C CA  . SER F  2 27  ? 6.490   56.090 -2.978  1.00 36.33  ? 27   SER F CA  1 
ATOM   10481 C C   . SER F  2 27  ? 6.676   55.661 -4.435  1.00 36.21  ? 27   SER F C   1 
ATOM   10482 O O   . SER F  2 27  ? 7.801   55.530 -4.912  1.00 34.76  ? 27   SER F O   1 
ATOM   10483 C CB  . SER F  2 27  ? 6.838   57.569 -2.796  1.00 37.04  ? 27   SER F CB  1 
ATOM   10484 O OG  . SER F  2 27  ? 8.112   57.870 -3.325  1.00 35.78  ? 27   SER F OG  1 
ATOM   10485 N N   . ASN F  2 28  ? 5.558   55.422 -5.121  1.00 38.04  ? 28   ASN F N   1 
ATOM   10486 C CA  . ASN F  2 28  ? 5.560   54.992 -6.519  1.00 38.22  ? 28   ASN F CA  1 
ATOM   10487 C C   . ASN F  2 28  ? 4.291   55.486 -7.225  1.00 40.89  ? 28   ASN F C   1 
ATOM   10488 O O   . ASN F  2 28  ? 3.563   56.308 -6.670  1.00 42.69  ? 28   ASN F O   1 
ATOM   10489 C CB  . ASN F  2 28  ? 5.720   53.464 -6.603  1.00 37.30  ? 28   ASN F CB  1 
ATOM   10490 C CG  . ASN F  2 28  ? 4.604   52.708 -5.910  1.00 38.67  ? 28   ASN F CG  1 
ATOM   10491 O OD1 . ASN F  2 28  ? 3.553   53.262 -5.610  1.00 40.61  ? 28   ASN F OD1 1 
ATOM   10492 N ND2 . ASN F  2 28  ? 4.831   51.426 -5.655  1.00 38.14  ? 28   ASN F ND2 1 
ATOM   10493 N N   . GLU F  2 29  ? 4.028   55.007 -8.439  1.00 41.47  ? 29   GLU F N   1 
ATOM   10494 C CA  . GLU F  2 29  ? 2.853   55.453 -9.194  1.00 44.17  ? 29   GLU F CA  1 
ATOM   10495 C C   . GLU F  2 29  ? 1.531   55.148 -8.479  1.00 46.39  ? 29   GLU F C   1 
ATOM   10496 O O   . GLU F  2 29  ? 0.581   55.923 -8.575  1.00 49.06  ? 29   GLU F O   1 
ATOM   10497 C CB  . GLU F  2 29  ? 2.823   54.818 -10.589 1.00 44.30  ? 29   GLU F CB  1 
ATOM   10498 C CG  . GLU F  2 29  ? 3.956   55.258 -11.511 1.00 43.04  ? 29   GLU F CG  1 
ATOM   10499 C CD  . GLU F  2 29  ? 3.702   54.910 -12.976 1.00 43.81  ? 29   GLU F CD  1 
ATOM   10500 O OE1 . GLU F  2 29  ? 2.785   54.108 -13.271 1.00 44.96  ? 29   GLU F OE1 1 
ATOM   10501 O OE2 . GLU F  2 29  ? 4.430   55.439 -13.840 1.00 43.50  ? 29   GLU F OE2 1 
ATOM   10502 N N   . GLN F  2 30  ? 1.480   54.021 -7.774  1.00 45.71  ? 30   GLN F N   1 
ATOM   10503 C CA  . GLN F  2 30  ? 0.268   53.587 -7.069  1.00 48.14  ? 30   GLN F CA  1 
ATOM   10504 C C   . GLN F  2 30  ? -0.011  54.376 -5.788  1.00 49.02  ? 30   GLN F C   1 
ATOM   10505 O O   . GLN F  2 30  ? -1.160  54.506 -5.380  1.00 52.03  ? 30   GLN F O   1 
ATOM   10506 C CB  . GLN F  2 30  ? 0.362   52.096 -6.742  1.00 47.55  ? 30   GLN F CB  1 
ATOM   10507 C CG  . GLN F  2 30  ? 0.333   51.199 -7.973  1.00 47.70  ? 30   GLN F CG  1 
ATOM   10508 C CD  . GLN F  2 30  ? 1.444   50.164 -7.962  1.00 45.44  ? 30   GLN F CD  1 
ATOM   10509 O OE1 . GLN F  2 30  ? 2.587   50.456 -8.347  1.00 43.21  ? 30   GLN F OE1 1 
ATOM   10510 N NE2 . GLN F  2 30  ? 1.120   48.947 -7.520  1.00 46.52  ? 30   GLN F NE2 1 
ATOM   10511 N N   . GLY F  2 31  ? 1.036   54.892 -5.153  1.00 46.69  ? 31   GLY F N   1 
ATOM   10512 C CA  . GLY F  2 31  ? 0.877   55.685 -3.934  1.00 47.45  ? 31   GLY F CA  1 
ATOM   10513 C C   . GLY F  2 31  ? 2.103   55.664 -3.047  1.00 44.47  ? 31   GLY F C   1 
ATOM   10514 O O   . GLY F  2 31  ? 3.191   55.305 -3.486  1.00 41.93  ? 31   GLY F O   1 
ATOM   10515 N N   . SER F  2 32  ? 1.916   56.060 -1.793  1.00 45.07  ? 32   SER F N   1 
ATOM   10516 C CA  . SER F  2 32  ? 2.985   56.053 -0.804  1.00 42.55  ? 32   SER F CA  1 
ATOM   10517 C C   . SER F  2 32  ? 2.461   55.614 0.553   1.00 43.39  ? 32   SER F C   1 
ATOM   10518 O O   . SER F  2 32  ? 1.258   55.664 0.802   1.00 46.36  ? 32   SER F O   1 
ATOM   10519 C CB  . SER F  2 32  ? 3.603   57.444 -0.692  1.00 42.40  ? 32   SER F CB  1 
ATOM   10520 O OG  . SER F  2 32  ? 2.613   58.420 -0.455  1.00 45.60  ? 32   SER F OG  1 
ATOM   10521 N N   . GLY F  2 33  ? 3.363   55.182 1.432   1.00 41.07  ? 33   GLY F N   1 
ATOM   10522 C CA  . GLY F  2 33  ? 2.959   54.748 2.765   1.00 41.82  ? 33   GLY F CA  1 
ATOM   10523 C C   . GLY F  2 33  ? 4.056   54.236 3.679   1.00 39.18  ? 33   GLY F C   1 
ATOM   10524 O O   . GLY F  2 33  ? 5.142   53.875 3.234   1.00 36.77  ? 33   GLY F O   1 
ATOM   10525 N N   . TYR F  2 34  ? 3.739   54.194 4.971   1.00 39.99  ? 34   TYR F N   1 
ATOM   10526 C CA  . TYR F  2 34  ? 4.645   53.704 5.997   1.00 37.95  ? 34   TYR F CA  1 
ATOM   10527 C C   . TYR F  2 34  ? 4.346   52.255 6.347   1.00 38.55  ? 34   TYR F C   1 
ATOM   10528 O O   . TYR F  2 34  ? 3.192   51.873 6.497   1.00 41.33  ? 34   TYR F O   1 
ATOM   10529 C CB  . TYR F  2 34  ? 4.516   54.548 7.259   1.00 38.63  ? 34   TYR F CB  1 
ATOM   10530 C CG  . TYR F  2 34  ? 4.808   56.016 7.058   1.00 38.66  ? 34   TYR F CG  1 
ATOM   10531 C CD1 . TYR F  2 34  ? 6.109   56.503 7.124   1.00 36.22  ? 34   TYR F CD1 1 
ATOM   10532 C CD2 . TYR F  2 34  ? 3.781   56.922 6.805   1.00 41.63  ? 34   TYR F CD2 1 
ATOM   10533 C CE1 . TYR F  2 34  ? 6.378   57.849 6.943   1.00 36.77  ? 34   TYR F CE1 1 
ATOM   10534 C CE2 . TYR F  2 34  ? 4.044   58.270 6.623   1.00 42.21  ? 34   TYR F CE2 1 
ATOM   10535 C CZ  . TYR F  2 34  ? 5.344   58.727 6.697   1.00 39.78  ? 34   TYR F CZ  1 
ATOM   10536 O OH  . TYR F  2 34  ? 5.612   60.062 6.525   1.00 40.86  ? 34   TYR F OH  1 
ATOM   10537 N N   . ALA F  2 35  ? 5.397   51.454 6.474   1.00 36.44  ? 35   ALA F N   1 
ATOM   10538 C CA  . ALA F  2 35  ? 5.285   50.085 6.959   1.00 37.21  ? 35   ALA F CA  1 
ATOM   10539 C C   . ALA F  2 35  ? 6.352   49.854 8.023   1.00 35.36  ? 35   ALA F C   1 
ATOM   10540 O O   . ALA F  2 35  ? 7.540   49.992 7.756   1.00 33.07  ? 35   ALA F O   1 
ATOM   10541 C CB  . ALA F  2 35  ? 5.458   49.102 5.816   1.00 37.23  ? 35   ALA F CB  1 
ATOM   10542 N N   . ALA F  2 36  ? 5.921   49.514 9.231   1.00 36.65  ? 36   ALA F N   1 
ATOM   10543 C CA  . ALA F  2 36  ? 6.844   49.212 10.309  1.00 35.22  ? 36   ALA F CA  1 
ATOM   10544 C C   . ALA F  2 36  ? 7.526   47.873 10.056  1.00 34.99  ? 36   ALA F C   1 
ATOM   10545 O O   . ALA F  2 36  ? 6.884   46.917 9.630   1.00 37.05  ? 36   ALA F O   1 
ATOM   10546 C CB  . ALA F  2 36  ? 6.113   49.186 11.643  1.00 37.04  ? 36   ALA F CB  1 
ATOM   10547 N N   . ASP F  2 37  ? 8.829   47.818 10.315  1.00 32.90  ? 37   ASP F N   1 
ATOM   10548 C CA  . ASP F  2 37  ? 9.586   46.574 10.276  1.00 33.07  ? 37   ASP F CA  1 
ATOM   10549 C C   . ASP F  2 37  ? 9.404   45.848 11.613  1.00 34.49  ? 37   ASP F C   1 
ATOM   10550 O O   . ASP F  2 37  ? 9.944   46.270 12.642  1.00 33.30  ? 37   ASP F O   1 
ATOM   10551 C CB  . ASP F  2 37  ? 11.065  46.864 10.022  1.00 30.73  ? 37   ASP F CB  1 
ATOM   10552 C CG  . ASP F  2 37  ? 11.869  45.608 9.780   1.00 31.38  ? 37   ASP F CG  1 
ATOM   10553 O OD1 . ASP F  2 37  ? 11.899  45.136 8.625   1.00 31.99  ? 37   ASP F OD1 1 
ATOM   10554 O OD2 . ASP F  2 37  ? 12.471  45.092 10.747  1.00 31.53  ? 37   ASP F OD2 1 
ATOM   10555 N N   . LYS F  2 38  ? 8.637   44.761 11.592  1.00 37.31  ? 38   LYS F N   1 
ATOM   10556 C CA  . LYS F  2 38  ? 8.275   44.035 12.816  1.00 39.43  ? 38   LYS F CA  1 
ATOM   10557 C C   . LYS F  2 38  ? 9.469   43.420 13.541  1.00 38.68  ? 38   LYS F C   1 
ATOM   10558 O O   . LYS F  2 38  ? 9.579   43.541 14.761  1.00 38.62  ? 38   LYS F O   1 
ATOM   10559 C CB  . LYS F  2 38  ? 7.243   42.937 12.514  1.00 43.17  ? 38   LYS F CB  1 
ATOM   10560 C CG  . LYS F  2 38  ? 5.807   43.437 12.415  1.00 45.18  ? 38   LYS F CG  1 
ATOM   10561 C CD  . LYS F  2 38  ? 4.799   42.289 12.425  1.00 49.55  ? 38   LYS F CD  1 
ATOM   10562 C CE  . LYS F  2 38  ? 4.613   41.671 11.043  1.00 50.61  ? 38   LYS F CE  1 
ATOM   10563 N NZ  . LYS F  2 38  ? 3.869   40.379 11.105  1.00 55.12  ? 38   LYS F NZ  1 
ATOM   10564 N N   . GLU F  2 39  ? 10.349  42.761 12.790  1.00 38.42  ? 39   GLU F N   1 
ATOM   10565 C CA  . GLU F  2 39  ? 11.498  42.051 13.369  1.00 38.44  ? 39   GLU F CA  1 
ATOM   10566 C C   . GLU F  2 39  ? 12.441  42.959 14.161  1.00 35.59  ? 39   GLU F C   1 
ATOM   10567 O O   . GLU F  2 39  ? 12.734  42.681 15.320  1.00 36.00  ? 39   GLU F O   1 
ATOM   10568 C CB  . GLU F  2 39  ? 12.288  41.302 12.283  1.00 39.02  ? 39   GLU F CB  1 
ATOM   10569 C CG  . GLU F  2 39  ? 13.751  41.029 12.644  1.00 38.37  ? 39   GLU F CG  1 
ATOM   10570 C CD  . GLU F  2 39  ? 14.348  39.855 11.886  1.00 40.69  ? 39   GLU F CD  1 
ATOM   10571 O OE1 . GLU F  2 39  ? 14.003  39.666 10.696  1.00 41.36  ? 39   GLU F OE1 1 
ATOM   10572 O OE2 . GLU F  2 39  ? 15.157  39.112 12.493  1.00 42.15  ? 39   GLU F OE2 1 
ATOM   10573 N N   . SER F  2 40  ? 12.928  44.024 13.535  1.00 32.98  ? 40   SER F N   1 
ATOM   10574 C CA  . SER F  2 40  ? 13.857  44.929 14.210  1.00 30.62  ? 40   SER F CA  1 
ATOM   10575 C C   . SER F  2 40  ? 13.187  45.630 15.392  1.00 30.30  ? 40   SER F C   1 
ATOM   10576 O O   . SER F  2 40  ? 13.822  45.845 16.428  1.00 29.47  ? 40   SER F O   1 
ATOM   10577 C CB  . SER F  2 40  ? 14.445  45.956 13.236  1.00 28.56  ? 40   SER F CB  1 
ATOM   10578 O OG  . SER F  2 40  ? 13.437  46.745 12.635  1.00 28.40  ? 40   SER F OG  1 
ATOM   10579 N N   . THR F  2 41  ? 11.908  45.965 15.239  1.00 31.25  ? 41   THR F N   1 
ATOM   10580 C CA  . THR F  2 41  ? 11.141  46.614 16.301  1.00 31.62  ? 41   THR F CA  1 
ATOM   10581 C C   . THR F  2 41  ? 10.978  45.702 17.520  1.00 33.38  ? 41   THR F C   1 
ATOM   10582 O O   . THR F  2 41  ? 11.215  46.123 18.651  1.00 32.73  ? 41   THR F O   1 
ATOM   10583 C CB  . THR F  2 41  ? 9.748   47.052 15.794  1.00 33.13  ? 41   THR F CB  1 
ATOM   10584 O OG1 . THR F  2 41  ? 9.901   47.941 14.683  1.00 31.65  ? 41   THR F OG1 1 
ATOM   10585 C CG2 . THR F  2 41  ? 8.957   47.760 16.887  1.00 34.06  ? 41   THR F CG2 1 
ATOM   10586 N N   . GLN F  2 42  ? 10.572  44.458 17.286  1.00 35.85  ? 42   GLN F N   1 
ATOM   10587 C CA  . GLN F  2 42  ? 10.348  43.508 18.379  1.00 38.22  ? 42   GLN F CA  1 
ATOM   10588 C C   . GLN F  2 42  ? 11.641  43.216 19.128  1.00 37.01  ? 42   GLN F C   1 
ATOM   10589 O O   . GLN F  2 42  ? 11.639  43.073 20.350  1.00 37.71  ? 42   GLN F O   1 
ATOM   10590 C CB  . GLN F  2 42  ? 9.750   42.200 17.852  1.00 41.57  ? 42   GLN F CB  1 
ATOM   10591 C CG  . GLN F  2 42  ? 9.343   41.216 18.944  1.00 44.86  ? 42   GLN F CG  1 
ATOM   10592 C CD  . GLN F  2 42  ? 8.359   41.812 19.936  1.00 45.92  ? 42   GLN F CD  1 
ATOM   10593 O OE1 . GLN F  2 42  ? 8.619   41.860 21.139  1.00 45.90  ? 42   GLN F OE1 1 
ATOM   10594 N NE2 . GLN F  2 42  ? 7.224   42.282 19.430  1.00 47.07  ? 42   GLN F NE2 1 
ATOM   10595 N N   . LYS F  2 43  ? 12.737  43.128 18.380  1.00 35.46  ? 43   LYS F N   1 
ATOM   10596 C CA  . LYS F  2 43  ? 14.071  42.937 18.953  1.00 34.44  ? 43   LYS F CA  1 
ATOM   10597 C C   . LYS F  2 43  ? 14.445  44.093 19.870  1.00 32.01  ? 43   LYS F C   1 
ATOM   10598 O O   . LYS F  2 43  ? 15.031  43.885 20.934  1.00 32.03  ? 43   LYS F O   1 
ATOM   10599 C CB  . LYS F  2 43  ? 15.107  42.822 17.831  1.00 33.53  ? 43   LYS F CB  1 
ATOM   10600 C CG  . LYS F  2 43  ? 16.155  41.740 18.029  1.00 35.10  ? 43   LYS F CG  1 
ATOM   10601 C CD  . LYS F  2 43  ? 16.347  40.967 16.731  1.00 36.63  ? 43   LYS F CD  1 
ATOM   10602 C CE  . LYS F  2 43  ? 17.697  40.271 16.644  1.00 37.73  ? 43   LYS F CE  1 
ATOM   10603 N NZ  . LYS F  2 43  ? 18.056  40.055 15.211  1.00 38.15  ? 43   LYS F NZ  1 
ATOM   10604 N N   . ALA F  2 44  ? 14.106  45.309 19.445  1.00 30.18  ? 44   ALA F N   1 
ATOM   10605 C CA  . ALA F  2 44  ? 14.344  46.504 20.246  1.00 28.30  ? 44   ALA F CA  1 
ATOM   10606 C C   . ALA F  2 44  ? 13.474  46.510 21.493  1.00 29.61  ? 44   ALA F C   1 
ATOM   10607 O O   . ALA F  2 44  ? 13.934  46.869 22.573  1.00 28.86  ? 44   ALA F O   1 
ATOM   10608 C CB  . ALA F  2 44  ? 14.093  47.759 19.423  1.00 26.85  ? 44   ALA F CB  1 
ATOM   10609 N N   . ILE F  2 45  ? 12.213  46.117 21.341  1.00 31.84  ? 45   ILE F N   1 
ATOM   10610 C CA  . ILE F  2 45  ? 11.293  46.038 22.476  1.00 33.82  ? 45   ILE F CA  1 
ATOM   10611 C C   . ILE F  2 45  ? 11.788  45.035 23.521  1.00 34.97  ? 45   ILE F C   1 
ATOM   10612 O O   . ILE F  2 45  ? 11.736  45.313 24.719  1.00 35.14  ? 45   ILE F O   1 
ATOM   10613 C CB  . ILE F  2 45  ? 9.856   45.697 22.018  1.00 36.68  ? 45   ILE F CB  1 
ATOM   10614 C CG1 . ILE F  2 45  ? 9.188   46.952 21.449  1.00 36.02  ? 45   ILE F CG1 1 
ATOM   10615 C CG2 . ILE F  2 45  ? 9.024   45.141 23.169  1.00 39.76  ? 45   ILE F CG2 1 
ATOM   10616 C CD1 . ILE F  2 45  ? 7.947   46.679 20.626  1.00 38.56  ? 45   ILE F CD1 1 
ATOM   10617 N N   . ASP F  2 46  ? 12.270  43.882 23.066  1.00 36.02  ? 46   ASP F N   1 
ATOM   10618 C CA  . ASP F  2 46  ? 12.798  42.863 23.970  1.00 37.57  ? 46   ASP F CA  1 
ATOM   10619 C C   . ASP F  2 46  ? 14.033  43.361 24.715  1.00 35.14  ? 46   ASP F C   1 
ATOM   10620 O O   . ASP F  2 46  ? 14.136  43.200 25.930  1.00 35.82  ? 46   ASP F O   1 
ATOM   10621 C CB  . ASP F  2 46  ? 13.134  41.579 23.206  1.00 39.55  ? 46   ASP F CB  1 
ATOM   10622 C CG  . ASP F  2 46  ? 11.908  40.923 22.589  1.00 42.58  ? 46   ASP F CG  1 
ATOM   10623 O OD1 . ASP F  2 46  ? 10.775  41.306 22.946  1.00 43.72  ? 46   ASP F OD1 1 
ATOM   10624 O OD2 . ASP F  2 46  ? 12.080  40.022 21.739  1.00 44.16  ? 46   ASP F OD2 1 
ATOM   10625 N N   . GLY F  2 47  ? 14.958  43.974 23.986  1.00 32.55  ? 47   GLY F N   1 
ATOM   10626 C CA  . GLY F  2 47  ? 16.199  44.467 24.570  1.00 30.53  ? 47   GLY F CA  1 
ATOM   10627 C C   . GLY F  2 47  ? 15.991  45.510 25.654  1.00 29.27  ? 47   GLY F C   1 
ATOM   10628 O O   . GLY F  2 47  ? 16.620  45.449 26.713  1.00 29.07  ? 47   GLY F O   1 
ATOM   10629 N N   . VAL F  2 48  ? 15.100  46.463 25.388  1.00 28.71  ? 48   VAL F N   1 
ATOM   10630 C CA  . VAL F  2 48  ? 14.793  47.541 26.330  1.00 27.94  ? 48   VAL F CA  1 
ATOM   10631 C C   . VAL F  2 48  ? 13.984  47.037 27.530  1.00 30.18  ? 48   VAL F C   1 
ATOM   10632 O O   . VAL F  2 48  ? 14.181  47.502 28.649  1.00 29.78  ? 48   VAL F O   1 
ATOM   10633 C CB  . VAL F  2 48  ? 14.056  48.698 25.620  1.00 27.35  ? 48   VAL F CB  1 
ATOM   10634 C CG1 . VAL F  2 48  ? 13.463  49.684 26.620  1.00 27.64  ? 48   VAL F CG1 1 
ATOM   10635 C CG2 . VAL F  2 48  ? 15.006  49.410 24.663  1.00 25.13  ? 48   VAL F CG2 1 
ATOM   10636 N N   . THR F  2 49  ? 13.085  46.087 27.304  1.00 32.82  ? 49   THR F N   1 
ATOM   10637 C CA  . THR F  2 49  ? 12.324  45.493 28.395  1.00 35.59  ? 49   THR F CA  1 
ATOM   10638 C C   . THR F  2 49  ? 13.261  44.800 29.379  1.00 35.76  ? 49   THR F C   1 
ATOM   10639 O O   . THR F  2 49  ? 13.218  45.072 30.582  1.00 36.03  ? 49   THR F O   1 
ATOM   10640 C CB  . THR F  2 49  ? 11.279  44.490 27.874  1.00 38.89  ? 49   THR F CB  1 
ATOM   10641 O OG1 . THR F  2 49  ? 10.333  45.176 27.047  1.00 39.06  ? 49   THR F OG1 1 
ATOM   10642 C CG2 . THR F  2 49  ? 10.544  43.816 29.022  1.00 42.28  ? 49   THR F CG2 1 
ATOM   10643 N N   . ASN F  2 50  ? 14.110  43.917 28.859  1.00 35.90  ? 50   ASN F N   1 
ATOM   10644 C CA  . ASN F  2 50  ? 15.080  43.183 29.682  1.00 36.49  ? 50   ASN F CA  1 
ATOM   10645 C C   . ASN F  2 50  ? 15.976  44.124 30.471  1.00 33.91  ? 50   ASN F C   1 
ATOM   10646 O O   . ASN F  2 50  ? 16.260  43.889 31.641  1.00 34.58  ? 50   ASN F O   1 
ATOM   10647 C CB  . ASN F  2 50  ? 15.958  42.285 28.810  1.00 36.95  ? 50   ASN F CB  1 
ATOM   10648 C CG  . ASN F  2 50  ? 15.190  41.133 28.198  1.00 40.26  ? 50   ASN F CG  1 
ATOM   10649 O OD1 . ASN F  2 50  ? 14.470  40.422 28.890  1.00 43.32  ? 50   ASN F OD1 1 
ATOM   10650 N ND2 . ASN F  2 50  ? 15.345  40.938 26.898  1.00 39.97  ? 50   ASN F ND2 1 
ATOM   10651 N N   . LYS F  2 51  ? 16.416  45.183 29.803  1.00 31.25  ? 51   LYS F N   1 
ATOM   10652 C CA  . LYS F  2 51  ? 17.260  46.212 30.403  1.00 28.97  ? 51   LYS F CA  1 
ATOM   10653 C C   . LYS F  2 51  ? 16.616  46.875 31.615  1.00 29.23  ? 51   LYS F C   1 
ATOM   10654 O O   . LYS F  2 51  ? 17.255  47.063 32.647  1.00 28.66  ? 51   LYS F O   1 
ATOM   10655 C CB  . LYS F  2 51  ? 17.557  47.273 29.355  1.00 26.77  ? 51   LYS F CB  1 
ATOM   10656 C CG  . LYS F  2 51  ? 18.269  48.506 29.866  1.00 24.76  ? 51   LYS F CG  1 
ATOM   10657 C CD  . LYS F  2 51  ? 18.480  49.467 28.708  1.00 23.29  ? 51   LYS F CD  1 
ATOM   10658 C CE  . LYS F  2 51  ? 19.928  49.870 28.575  1.00 21.95  ? 51   LYS F CE  1 
ATOM   10659 N NZ  . LYS F  2 51  ? 20.275  50.256 27.192  1.00 21.26  ? 51   LYS F NZ  1 
ATOM   10660 N N   . VAL F  2 52  ? 15.352  47.248 31.470  1.00 30.35  ? 52   VAL F N   1 
ATOM   10661 C CA  . VAL F  2 52  ? 14.616  47.883 32.550  1.00 31.22  ? 52   VAL F CA  1 
ATOM   10662 C C   . VAL F  2 52  ? 14.469  46.916 33.730  1.00 33.52  ? 52   VAL F C   1 
ATOM   10663 O O   . VAL F  2 52  ? 14.688  47.303 34.879  1.00 33.31  ? 52   VAL F O   1 
ATOM   10664 C CB  . VAL F  2 52  ? 13.240  48.386 32.060  1.00 32.63  ? 52   VAL F CB  1 
ATOM   10665 C CG1 . VAL F  2 52  ? 12.359  48.817 33.229  1.00 34.50  ? 52   VAL F CG1 1 
ATOM   10666 C CG2 . VAL F  2 52  ? 13.424  49.541 31.081  1.00 30.55  ? 52   VAL F CG2 1 
ATOM   10667 N N   . ASN F  2 53  ? 14.126  45.663 33.439  1.00 36.00  ? 53   ASN F N   1 
ATOM   10668 C CA  . ASN F  2 53  ? 14.001  44.631 34.476  1.00 38.81  ? 53   ASN F CA  1 
ATOM   10669 C C   . ASN F  2 53  ? 15.350  44.309 35.121  1.00 37.78  ? 53   ASN F C   1 
ATOM   10670 O O   . ASN F  2 53  ? 15.436  44.134 36.333  1.00 38.76  ? 53   ASN F O   1 
ATOM   10671 C CB  . ASN F  2 53  ? 13.390  43.348 33.905  1.00 42.03  ? 53   ASN F CB  1 
ATOM   10672 C CG  . ASN F  2 53  ? 12.016  43.567 33.299  1.00 43.74  ? 53   ASN F CG  1 
ATOM   10673 O OD1 . ASN F  2 53  ? 11.329  44.535 33.618  1.00 43.52  ? 53   ASN F OD1 1 
ATOM   10674 N ND2 . ASN F  2 53  ? 11.608  42.662 32.417  1.00 45.84  ? 53   ASN F ND2 1 
ATOM   10675 N N   . SER F  2 54  ? 16.394  44.229 34.298  1.00 36.15  ? 54   SER F N   1 
ATOM   10676 C CA  . SER F  2 54  ? 17.756  44.014 34.788  1.00 35.35  ? 54   SER F CA  1 
ATOM   10677 C C   . SER F  2 54  ? 18.147  45.117 35.751  1.00 33.44  ? 54   SER F C   1 
ATOM   10678 O O   . SER F  2 54  ? 18.669  44.848 36.834  1.00 33.97  ? 54   SER F O   1 
ATOM   10679 C CB  . SER F  2 54  ? 18.759  43.970 33.632  1.00 33.88  ? 54   SER F CB  1 
ATOM   10680 O OG  . SER F  2 54  ? 18.747  42.706 32.996  1.00 36.35  ? 54   SER F OG  1 
ATOM   10681 N N   . ILE F  2 55  ? 17.886  46.356 35.340  1.00 31.58  ? 55   ILE F N   1 
ATOM   10682 C CA  . ILE F  2 55  ? 18.164  47.533 36.158  1.00 30.07  ? 55   ILE F CA  1 
ATOM   10683 C C   . ILE F  2 55  ? 17.417  47.471 37.490  1.00 31.96  ? 55   ILE F C   1 
ATOM   10684 O O   . ILE F  2 55  ? 18.013  47.681 38.545  1.00 31.56  ? 55   ILE F O   1 
ATOM   10685 C CB  . ILE F  2 55  ? 17.820  48.838 35.395  1.00 28.41  ? 55   ILE F CB  1 
ATOM   10686 C CG1 . ILE F  2 55  ? 18.962  49.181 34.433  1.00 26.43  ? 55   ILE F CG1 1 
ATOM   10687 C CG2 . ILE F  2 55  ? 17.591  50.002 36.354  1.00 27.90  ? 55   ILE F CG2 1 
ATOM   10688 C CD1 . ILE F  2 55  ? 18.630  50.222 33.384  1.00 25.31  ? 55   ILE F CD1 1 
ATOM   10689 N N   . ILE F  2 56  ? 16.121  47.177 37.437  1.00 34.40  ? 56   ILE F N   1 
ATOM   10690 C CA  . ILE F  2 56  ? 15.306  47.086 38.648  1.00 36.78  ? 56   ILE F CA  1 
ATOM   10691 C C   . ILE F  2 56  ? 15.856  46.014 39.594  1.00 38.43  ? 56   ILE F C   1 
ATOM   10692 O O   . ILE F  2 56  ? 16.076  46.285 40.777  1.00 38.49  ? 56   ILE F O   1 
ATOM   10693 C CB  . ILE F  2 56  ? 13.828  46.786 38.304  1.00 39.67  ? 56   ILE F CB  1 
ATOM   10694 C CG1 . ILE F  2 56  ? 13.185  47.999 37.617  1.00 38.69  ? 56   ILE F CG1 1 
ATOM   10695 C CG2 . ILE F  2 56  ? 13.037  46.411 39.556  1.00 42.82  ? 56   ILE F CG2 1 
ATOM   10696 C CD1 . ILE F  2 56  ? 11.903  47.676 36.872  1.00 41.23  ? 56   ILE F CD1 1 
ATOM   10697 N N   . ASP F  2 57  ? 16.084  44.809 39.066  1.00 40.13  ? 57   ASP F N   1 
ATOM   10698 C CA  . ASP F  2 57  ? 16.531  43.662 39.877  1.00 42.54  ? 57   ASP F CA  1 
ATOM   10699 C C   . ASP F  2 57  ? 17.858  43.896 40.600  1.00 40.83  ? 57   ASP F C   1 
ATOM   10700 O O   . ASP F  2 57  ? 18.021  43.492 41.748  1.00 42.33  ? 57   ASP F O   1 
ATOM   10701 C CB  . ASP F  2 57  ? 16.639  42.399 39.018  1.00 44.65  ? 57   ASP F CB  1 
ATOM   10702 C CG  . ASP F  2 57  ? 15.301  41.712 38.822  1.00 48.31  ? 57   ASP F CG  1 
ATOM   10703 O OD1 . ASP F  2 57  ? 14.650  41.385 39.844  1.00 51.14  ? 57   ASP F OD1 1 
ATOM   10704 O OD2 . ASP F  2 57  ? 14.902  41.489 37.652  1.00 48.66  ? 57   ASP F OD2 1 
ATOM   10705 N N   . LYS F  2 58  ? 18.801  44.544 39.929  1.00 38.11  ? 58   LYS F N   1 
ATOM   10706 C CA  . LYS F  2 58  ? 20.090  44.844 40.545  1.00 36.71  ? 58   LYS F CA  1 
ATOM   10707 C C   . LYS F  2 58  ? 19.957  45.792 41.733  1.00 36.01  ? 58   LYS F C   1 
ATOM   10708 O O   . LYS F  2 58  ? 20.690  45.666 42.715  1.00 36.13  ? 58   LYS F O   1 
ATOM   10709 C CB  . LYS F  2 58  ? 21.086  45.389 39.504  1.00 34.23  ? 58   LYS F CB  1 
ATOM   10710 C CG  . LYS F  2 58  ? 22.179  44.409 39.103  1.00 35.23  ? 58   LYS F CG  1 
ATOM   10711 C CD  . LYS F  2 58  ? 21.635  43.001 38.885  1.00 38.49  ? 58   LYS F CD  1 
ATOM   10712 C CE  . LYS F  2 58  ? 22.719  41.952 39.002  1.00 40.47  ? 58   LYS F CE  1 
ATOM   10713 N NZ  . LYS F  2 58  ? 22.174  40.604 38.680  1.00 44.09  ? 58   LYS F NZ  1 
ATOM   10714 N N   . MET F  2 59  ? 19.009  46.720 41.649  1.00 35.73  ? 59   MET F N   1 
ATOM   10715 C CA  . MET F  2 59  ? 18.759  47.669 42.733  1.00 35.47  ? 59   MET F CA  1 
ATOM   10716 C C   . MET F  2 59  ? 17.837  47.079 43.803  1.00 38.58  ? 59   MET F C   1 
ATOM   10717 O O   . MET F  2 59  ? 17.858  47.529 44.948  1.00 38.70  ? 59   MET F O   1 
ATOM   10718 C CB  . MET F  2 59  ? 18.157  48.959 42.170  1.00 34.22  ? 59   MET F CB  1 
ATOM   10719 C CG  . MET F  2 59  ? 18.982  49.581 41.052  1.00 31.76  ? 59   MET F CG  1 
ATOM   10720 S SD  . MET F  2 59  ? 20.644  49.989 41.600  1.00 29.95  ? 59   MET F SD  1 
ATOM   10721 C CE  . MET F  2 59  ? 20.419  51.519 42.499  1.00 29.15  ? 59   MET F CE  1 
ATOM   10722 N N   . ASN F  2 60  ? 17.042  46.074 43.427  1.00 41.41  ? 60   ASN F N   1 
ATOM   10723 C CA  . ASN F  2 60  ? 16.090  45.421 44.343  1.00 45.09  ? 60   ASN F CA  1 
ATOM   10724 C C   . ASN F  2 60  ? 16.672  45.115 45.730  1.00 45.94  ? 60   ASN F C   1 
ATOM   10725 O O   . ASN F  2 60  ? 16.020  45.364 46.746  1.00 47.53  ? 60   ASN F O   1 
ATOM   10726 C CB  . ASN F  2 60  ? 15.501  44.145 43.699  1.00 48.17  ? 60   ASN F CB  1 
ATOM   10727 C CG  . ASN F  2 60  ? 15.090  43.093 44.724  1.00 52.23  ? 60   ASN F CG  1 
ATOM   10728 O OD1 . ASN F  2 60  ? 15.929  42.564 45.458  1.00 52.59  ? 60   ASN F OD1 1 
ATOM   10729 N ND2 . ASN F  2 60  ? 13.798  42.769 44.766  1.00 55.69  ? 60   ASN F ND2 1 
ATOM   10730 N N   . THR F  2 61  ? 17.882  44.563 45.772  1.00 45.23  ? 61   THR F N   1 
ATOM   10731 C CA  . THR F  2 61  ? 18.549  44.297 47.056  1.00 45.92  ? 61   THR F CA  1 
ATOM   10732 C C   . THR F  2 61  ? 19.603  45.376 47.302  1.00 42.44  ? 61   THR F C   1 
ATOM   10733 O O   . THR F  2 61  ? 20.601  45.475 46.579  1.00 40.58  ? 61   THR F O   1 
ATOM   10734 C CB  . THR F  2 61  ? 19.128  42.856 47.188  1.00 48.52  ? 61   THR F CB  1 
ATOM   10735 O OG1 . THR F  2 61  ? 20.350  42.892 47.935  1.00 47.54  ? 61   THR F OG1 1 
ATOM   10736 C CG2 . THR F  2 61  ? 19.382  42.190 45.829  1.00 48.75  ? 61   THR F CG2 1 
ATOM   10737 N N   . GLN F  2 62  ? 19.342  46.184 48.328  1.00 42.04  ? 62   GLN F N   1 
ATOM   10738 C CA  . GLN F  2 62  ? 20.084  47.411 48.600  1.00 39.10  ? 62   GLN F CA  1 
ATOM   10739 C C   . GLN F  2 62  ? 19.816  47.865 50.046  1.00 39.75  ? 62   GLN F C   1 
ATOM   10740 O O   . GLN F  2 62  ? 18.820  47.459 50.656  1.00 42.51  ? 62   GLN F O   1 
ATOM   10741 C CB  . GLN F  2 62  ? 19.679  48.489 47.581  1.00 37.35  ? 62   GLN F CB  1 
ATOM   10742 C CG  . GLN F  2 62  ? 19.425  49.886 48.144  1.00 36.47  ? 62   GLN F CG  1 
ATOM   10743 C CD  . GLN F  2 62  ? 19.004  50.873 47.075  1.00 35.39  ? 62   GLN F CD  1 
ATOM   10744 O OE1 . GLN F  2 62  ? 19.018  50.561 45.877  1.00 34.96  ? 62   GLN F OE1 1 
ATOM   10745 N NE2 . GLN F  2 62  ? 18.627  52.081 47.502  1.00 35.30  ? 62   GLN F NE2 1 
ATOM   10746 N N   . PHE F  2 63  ? 20.700  48.712 50.574  1.00 37.49  ? 63   PHE F N   1 
ATOM   10747 C CA  . PHE F  2 63  ? 20.668  49.131 51.984  1.00 37.88  ? 63   PHE F CA  1 
ATOM   10748 C C   . PHE F  2 63  ? 19.314  49.688 52.444  1.00 39.44  ? 63   PHE F C   1 
ATOM   10749 O O   . PHE F  2 63  ? 18.666  50.450 51.719  1.00 39.03  ? 63   PHE F O   1 
ATOM   10750 C CB  . PHE F  2 63  ? 21.764  50.173 52.258  1.00 35.29  ? 63   PHE F CB  1 
ATOM   10751 C CG  . PHE F  2 63  ? 21.921  50.512 53.712  1.00 35.81  ? 63   PHE F CG  1 
ATOM   10752 C CD1 . PHE F  2 63  ? 22.589  49.644 54.573  1.00 36.71  ? 63   PHE F CD1 1 
ATOM   10753 C CD2 . PHE F  2 63  ? 21.387  51.689 54.228  1.00 35.68  ? 63   PHE F CD2 1 
ATOM   10754 C CE1 . PHE F  2 63  ? 22.724  49.949 55.919  1.00 37.23  ? 63   PHE F CE1 1 
ATOM   10755 C CE2 . PHE F  2 63  ? 21.522  52.000 55.573  1.00 36.31  ? 63   PHE F CE2 1 
ATOM   10756 C CZ  . PHE F  2 63  ? 22.189  51.129 56.418  1.00 36.92  ? 63   PHE F CZ  1 
ATOM   10757 N N   . GLU F  2 64  ? 18.905  49.296 53.653  1.00 41.48  ? 64   GLU F N   1 
ATOM   10758 C CA  . GLU F  2 64  ? 17.689  49.802 54.287  1.00 43.55  ? 64   GLU F CA  1 
ATOM   10759 C C   . GLU F  2 64  ? 18.025  50.400 55.652  1.00 43.36  ? 64   GLU F C   1 
ATOM   10760 O O   . GLU F  2 64  ? 18.603  49.722 56.510  1.00 43.92  ? 64   GLU F O   1 
ATOM   10761 C CB  . GLU F  2 64  ? 16.675  48.675 54.484  1.00 47.37  ? 64   GLU F CB  1 
ATOM   10762 C CG  . GLU F  2 64  ? 16.302  47.919 53.218  1.00 48.00  ? 64   GLU F CG  1 
ATOM   10763 C CD  . GLU F  2 64  ? 15.301  46.802 53.479  1.00 52.37  ? 64   GLU F CD  1 
ATOM   10764 O OE1 . GLU F  2 64  ? 14.855  46.640 54.637  1.00 55.03  ? 64   GLU F OE1 1 
ATOM   10765 O OE2 . GLU F  2 64  ? 14.962  46.078 52.519  1.00 53.44  ? 64   GLU F OE2 1 
ATOM   10766 N N   . ALA F  2 65  ? 17.651  51.660 55.859  1.00 42.78  ? 65   ALA F N   1 
ATOM   10767 C CA  . ALA F  2 65  ? 17.922  52.346 57.123  1.00 42.72  ? 65   ALA F CA  1 
ATOM   10768 C C   . ALA F  2 65  ? 17.063  51.785 58.261  1.00 46.08  ? 65   ALA F C   1 
ATOM   10769 O O   . ALA F  2 65  ? 15.935  51.343 58.038  1.00 48.86  ? 65   ALA F O   1 
ATOM   10770 C CB  . ALA F  2 65  ? 17.692  53.844 56.977  1.00 42.04  ? 65   ALA F CB  1 
ATOM   10771 N N   . VAL F  2 66  ? 17.620  51.799 59.472  1.00 45.95  ? 66   VAL F N   1 
ATOM   10772 C CA  . VAL F  2 66  ? 16.925  51.342 60.677  1.00 49.22  ? 66   VAL F CA  1 
ATOM   10773 C C   . VAL F  2 66  ? 17.077  52.400 61.772  1.00 48.97  ? 66   VAL F C   1 
ATOM   10774 O O   . VAL F  2 66  ? 18.140  53.013 61.915  1.00 46.17  ? 66   VAL F O   1 
ATOM   10775 C CB  . VAL F  2 66  ? 17.472  49.979 61.172  1.00 50.14  ? 66   VAL F CB  1 
ATOM   10776 C CG1 . VAL F  2 66  ? 16.714  49.499 62.406  1.00 54.12  ? 66   VAL F CG1 1 
ATOM   10777 C CG2 . VAL F  2 66  ? 17.387  48.932 60.066  1.00 50.49  ? 66   VAL F CG2 1 
ATOM   10778 N N   . GLY F  2 67  ? 16.006  52.607 62.537  1.00 52.20  ? 67   GLY F N   1 
ATOM   10779 C CA  . GLY F  2 67  ? 16.002  53.572 63.632  1.00 52.69  ? 67   GLY F CA  1 
ATOM   10780 C C   . GLY F  2 67  ? 16.693  53.029 64.869  1.00 52.66  ? 67   GLY F C   1 
ATOM   10781 O O   . GLY F  2 67  ? 16.295  51.996 65.408  1.00 55.34  ? 67   GLY F O   1 
ATOM   10782 N N   . ARG F  2 68  ? 17.734  53.729 65.313  1.00 49.86  ? 68   ARG F N   1 
ATOM   10783 C CA  . ARG F  2 68  ? 18.492  53.349 66.501  1.00 49.61  ? 68   ARG F CA  1 
ATOM   10784 C C   . ARG F  2 68  ? 18.623  54.561 67.406  1.00 49.52  ? 68   ARG F C   1 
ATOM   10785 O O   . ARG F  2 68  ? 18.935  55.657 66.940  1.00 47.69  ? 68   ARG F O   1 
ATOM   10786 C CB  . ARG F  2 68  ? 19.878  52.838 66.106  1.00 46.39  ? 68   ARG F CB  1 
ATOM   10787 C CG  . ARG F  2 68  ? 19.914  51.362 65.748  1.00 47.32  ? 68   ARG F CG  1 
ATOM   10788 C CD  . ARG F  2 68  ? 21.284  50.949 65.212  1.00 44.44  ? 68   ARG F CD  1 
ATOM   10789 N NE  . ARG F  2 68  ? 21.151  50.052 64.068  1.00 44.50  ? 68   ARG F NE  1 
ATOM   10790 C CZ  . ARG F  2 68  ? 21.249  50.407 62.786  1.00 42.45  ? 68   ARG F CZ  1 
ATOM   10791 N NH1 . ARG F  2 68  ? 21.538  51.652 62.403  1.00 40.09  ? 68   ARG F NH1 1 
ATOM   10792 N NH2 . ARG F  2 68  ? 21.077  49.477 61.856  1.00 43.00  ? 68   ARG F NH2 1 
ATOM   10793 N N   . GLU F  2 69  ? 18.396  54.352 68.698  1.00 51.72  ? 69   GLU F N   1 
ATOM   10794 C CA  . GLU F  2 69  ? 18.367  55.437 69.670  1.00 52.42  ? 69   GLU F CA  1 
ATOM   10795 C C   . GLU F  2 69  ? 19.591  55.386 70.568  1.00 50.38  ? 69   GLU F C   1 
ATOM   10796 O O   . GLU F  2 69  ? 20.002  54.314 71.001  1.00 50.55  ? 69   GLU F O   1 
ATOM   10797 C CB  . GLU F  2 69  ? 17.107  55.329 70.525  1.00 57.11  ? 69   GLU F CB  1 
ATOM   10798 C CG  . GLU F  2 69  ? 15.807  55.506 69.747  1.00 59.76  ? 69   GLU F CG  1 
ATOM   10799 C CD  . GLU F  2 69  ? 15.264  56.920 69.828  1.00 61.22  ? 69   GLU F CD  1 
ATOM   10800 O OE1 . GLU F  2 69  ? 16.050  57.883 69.675  1.00 58.72  ? 69   GLU F OE1 1 
ATOM   10801 O OE2 . GLU F  2 69  ? 14.046  57.065 70.059  1.00 65.44  ? 69   GLU F OE2 1 
ATOM   10802 N N   . PHE F  2 70  ? 20.163  56.553 70.847  1.00 48.75  ? 70   PHE F N   1 
ATOM   10803 C CA  . PHE F  2 70  ? 21.331  56.670 71.717  1.00 47.05  ? 70   PHE F CA  1 
ATOM   10804 C C   . PHE F  2 70  ? 21.127  57.797 72.725  1.00 48.47  ? 70   PHE F C   1 
ATOM   10805 O O   . PHE F  2 70  ? 20.522  58.817 72.405  1.00 49.45  ? 70   PHE F O   1 
ATOM   10806 C CB  . PHE F  2 70  ? 22.586  56.939 70.883  1.00 43.38  ? 70   PHE F CB  1 
ATOM   10807 C CG  . PHE F  2 70  ? 22.776  55.979 69.743  1.00 41.95  ? 70   PHE F CG  1 
ATOM   10808 C CD1 . PHE F  2 70  ? 22.230  56.244 68.495  1.00 41.43  ? 70   PHE F CD1 1 
ATOM   10809 C CD2 . PHE F  2 70  ? 23.497  54.809 69.918  1.00 41.42  ? 70   PHE F CD2 1 
ATOM   10810 C CE1 . PHE F  2 70  ? 22.406  55.364 67.442  1.00 40.26  ? 70   PHE F CE1 1 
ATOM   10811 C CE2 . PHE F  2 70  ? 23.675  53.923 68.869  1.00 40.53  ? 70   PHE F CE2 1 
ATOM   10812 C CZ  . PHE F  2 70  ? 23.130  54.202 67.630  1.00 39.86  ? 70   PHE F CZ  1 
ATOM   10813 N N   . ASN F  2 71  ? 21.637  57.616 73.940  1.00 48.79  ? 71   ASN F N   1 
ATOM   10814 C CA  . ASN F  2 71  ? 21.484  58.637 74.978  1.00 50.36  ? 71   ASN F CA  1 
ATOM   10815 C C   . ASN F  2 71  ? 22.509  59.770 74.823  1.00 47.99  ? 71   ASN F C   1 
ATOM   10816 O O   . ASN F  2 71  ? 23.256  59.815 73.840  1.00 45.25  ? 71   ASN F O   1 
ATOM   10817 C CB  . ASN F  2 71  ? 21.488  58.008 76.389  1.00 52.24  ? 71   ASN F CB  1 
ATOM   10818 C CG  . ASN F  2 71  ? 22.865  57.547 76.845  1.00 49.83  ? 71   ASN F CG  1 
ATOM   10819 O OD1 . ASN F  2 71  ? 23.848  58.274 76.730  1.00 47.57  ? 71   ASN F OD1 1 
ATOM   10820 N ND2 . ASN F  2 71  ? 22.931  56.341 77.396  1.00 50.78  ? 71   ASN F ND2 1 
ATOM   10821 N N   . ASN F  2 72  ? 22.533  60.677 75.798  1.00 49.39  ? 72   ASN F N   1 
ATOM   10822 C CA  . ASN F  2 72  ? 23.312  61.913 75.711  1.00 48.20  ? 72   ASN F CA  1 
ATOM   10823 C C   . ASN F  2 72  ? 24.834  61.735 75.822  1.00 45.24  ? 72   ASN F C   1 
ATOM   10824 O O   . ASN F  2 72  ? 25.592  62.600 75.386  1.00 43.96  ? 72   ASN F O   1 
ATOM   10825 C CB  . ASN F  2 72  ? 22.827  62.898 76.783  1.00 51.24  ? 72   ASN F CB  1 
ATOM   10826 C CG  . ASN F  2 72  ? 23.268  64.323 76.509  1.00 51.24  ? 72   ASN F CG  1 
ATOM   10827 O OD1 . ASN F  2 72  ? 23.130  64.824 75.389  1.00 50.73  ? 72   ASN F OD1 1 
ATOM   10828 N ND2 . ASN F  2 72  ? 23.799  64.988 77.533  1.00 52.08  ? 72   ASN F ND2 1 
ATOM   10829 N N   . LEU F  2 73  ? 25.271  60.627 76.415  1.00 44.60  ? 73   LEU F N   1 
ATOM   10830 C CA  . LEU F  2 73  ? 26.694  60.306 76.510  1.00 42.26  ? 73   LEU F CA  1 
ATOM   10831 C C   . LEU F  2 73  ? 27.056  59.124 75.610  1.00 40.51  ? 73   LEU F C   1 
ATOM   10832 O O   . LEU F  2 73  ? 27.966  58.349 75.914  1.00 39.67  ? 73   LEU F O   1 
ATOM   10833 C CB  . LEU F  2 73  ? 27.071  60.031 77.965  1.00 43.28  ? 73   LEU F CB  1 
ATOM   10834 C CG  . LEU F  2 73  ? 27.090  61.281 78.853  1.00 44.66  ? 73   LEU F CG  1 
ATOM   10835 C CD1 . LEU F  2 73  ? 27.101  60.893 80.324  1.00 46.24  ? 73   LEU F CD1 1 
ATOM   10836 C CD2 . LEU F  2 73  ? 28.281  62.171 78.511  1.00 42.98  ? 73   LEU F CD2 1 
ATOM   10837 N N   . GLU F  2 74  ? 26.336  59.008 74.497  1.00 40.27  ? 74   GLU F N   1 
ATOM   10838 C CA  . GLU F  2 74  ? 26.633  58.042 73.447  1.00 38.70  ? 74   GLU F CA  1 
ATOM   10839 C C   . GLU F  2 74  ? 26.667  58.754 72.096  1.00 37.23  ? 74   GLU F C   1 
ATOM   10840 O O   . GLU F  2 74  ? 26.173  58.234 71.097  1.00 36.84  ? 74   GLU F O   1 
ATOM   10841 C CB  . GLU F  2 74  ? 25.568  56.952 73.431  1.00 40.40  ? 74   GLU F CB  1 
ATOM   10842 C CG  . GLU F  2 74  ? 25.595  56.053 74.643  1.00 42.05  ? 74   GLU F CG  1 
ATOM   10843 C CD  . GLU F  2 74  ? 24.597  54.931 74.528  1.00 44.15  ? 74   GLU F CD  1 
ATOM   10844 O OE1 . GLU F  2 74  ? 23.433  55.206 74.173  1.00 45.64  ? 74   GLU F OE1 1 
ATOM   10845 O OE2 . GLU F  2 74  ? 24.981  53.775 74.783  1.00 44.68  ? 74   GLU F OE2 1 
ATOM   10846 N N   . ARG F  2 75  ? 27.241  59.952 72.080  1.00 36.68  ? 75   ARG F N   1 
ATOM   10847 C CA  . ARG F  2 75  ? 27.204  60.810 70.901  1.00 35.92  ? 75   ARG F CA  1 
ATOM   10848 C C   . ARG F  2 75  ? 28.110  60.306 69.794  1.00 33.72  ? 75   ARG F C   1 
ATOM   10849 O O   . ARG F  2 75  ? 27.806  60.484 68.617  1.00 33.06  ? 75   ARG F O   1 
ATOM   10850 C CB  . ARG F  2 75  ? 27.578  62.251 71.262  1.00 36.64  ? 75   ARG F CB  1 
ATOM   10851 C CG  . ARG F  2 75  ? 26.511  62.994 72.052  1.00 39.31  ? 75   ARG F CG  1 
ATOM   10852 C CD  . ARG F  2 75  ? 25.391  63.480 71.145  1.00 40.50  ? 75   ARG F CD  1 
ATOM   10853 N NE  . ARG F  2 75  ? 24.257  64.023 71.899  1.00 43.68  ? 75   ARG F NE  1 
ATOM   10854 C CZ  . ARG F  2 75  ? 23.065  63.435 72.052  1.00 45.50  ? 75   ARG F CZ  1 
ATOM   10855 N NH1 . ARG F  2 75  ? 22.802  62.247 71.505  1.00 44.44  ? 75   ARG F NH1 1 
ATOM   10856 N NH2 . ARG F  2 75  ? 22.117  64.047 72.766  1.00 48.85  ? 75   ARG F NH2 1 
ATOM   10857 N N   . ARG F  2 76  ? 29.227  59.692 70.168  1.00 32.86  ? 76   ARG F N   1 
ATOM   10858 C CA  . ARG F  2 76  ? 30.164  59.161 69.184  1.00 31.30  ? 76   ARG F CA  1 
ATOM   10859 C C   . ARG F  2 76  ? 29.531  58.060 68.333  1.00 30.99  ? 76   ARG F C   1 
ATOM   10860 O O   . ARG F  2 76  ? 29.625  58.095 67.110  1.00 29.95  ? 76   ARG F O   1 
ATOM   10861 C CB  . ARG F  2 76  ? 31.417  58.625 69.869  1.00 31.14  ? 76   ARG F CB  1 
ATOM   10862 C CG  . ARG F  2 76  ? 32.323  59.694 70.451  1.00 31.34  ? 76   ARG F CG  1 
ATOM   10863 C CD  . ARG F  2 76  ? 33.399  59.045 71.299  1.00 31.63  ? 76   ARG F CD  1 
ATOM   10864 N NE  . ARG F  2 76  ? 32.810  58.329 72.432  1.00 32.64  ? 76   ARG F NE  1 
ATOM   10865 C CZ  . ARG F  2 76  ? 33.382  57.327 73.098  1.00 33.19  ? 76   ARG F CZ  1 
ATOM   10866 N NH1 . ARG F  2 76  ? 34.587  56.881 72.767  1.00 32.94  ? 76   ARG F NH1 1 
ATOM   10867 N NH2 . ARG F  2 76  ? 32.732  56.761 74.106  1.00 34.42  ? 76   ARG F NH2 1 
ATOM   10868 N N   . ILE F  2 77  ? 28.894  57.088 68.986  1.00 32.15  ? 77   ILE F N   1 
ATOM   10869 C CA  . ILE F  2 77  ? 28.243  55.986 68.273  1.00 32.44  ? 77   ILE F CA  1 
ATOM   10870 C C   . ILE F  2 77  ? 26.959  56.415 67.561  1.00 32.90  ? 77   ILE F C   1 
ATOM   10871 O O   . ILE F  2 77  ? 26.588  55.824 66.550  1.00 32.59  ? 77   ILE F O   1 
ATOM   10872 C CB  . ILE F  2 77  ? 27.976  54.754 69.174  1.00 34.15  ? 77   ILE F CB  1 
ATOM   10873 C CG1 . ILE F  2 77  ? 27.038  55.087 70.336  1.00 36.05  ? 77   ILE F CG1 1 
ATOM   10874 C CG2 . ILE F  2 77  ? 29.291  54.193 69.694  1.00 33.92  ? 77   ILE F CG2 1 
ATOM   10875 C CD1 . ILE F  2 77  ? 26.537  53.864 71.077  1.00 38.27  ? 77   ILE F CD1 1 
ATOM   10876 N N   . GLU F  2 78  ? 26.286  57.434 68.086  1.00 33.95  ? 78   GLU F N   1 
ATOM   10877 C CA  . GLU F  2 78  ? 25.152  58.037 67.393  1.00 34.74  ? 78   GLU F CA  1 
ATOM   10878 C C   . GLU F  2 78  ? 25.614  58.661 66.082  1.00 32.99  ? 78   GLU F C   1 
ATOM   10879 O O   . GLU F  2 78  ? 24.937  58.556 65.064  1.00 32.96  ? 78   GLU F O   1 
ATOM   10880 C CB  . GLU F  2 78  ? 24.490  59.098 68.272  1.00 36.67  ? 78   GLU F CB  1 
ATOM   10881 C CG  . GLU F  2 78  ? 23.220  59.710 67.698  1.00 38.32  ? 78   GLU F CG  1 
ATOM   10882 C CD  . GLU F  2 78  ? 22.487  60.568 68.718  1.00 41.07  ? 78   GLU F CD  1 
ATOM   10883 O OE1 . GLU F  2 78  ? 23.115  61.509 69.262  1.00 41.00  ? 78   GLU F OE1 1 
ATOM   10884 O OE2 . GLU F  2 78  ? 21.287  60.301 68.984  1.00 43.65  ? 78   GLU F OE2 1 
ATOM   10885 N N   . ASN F  2 79  ? 26.776  59.302 66.120  1.00 31.83  ? 79   ASN F N   1 
ATOM   10886 C CA  . ASN F  2 79  ? 27.361  59.935 64.948  1.00 30.53  ? 79   ASN F CA  1 
ATOM   10887 C C   . ASN F  2 79  ? 27.882  58.908 63.950  1.00 29.08  ? 79   ASN F C   1 
ATOM   10888 O O   . ASN F  2 79  ? 27.749  59.080 62.740  1.00 28.34  ? 79   ASN F O   1 
ATOM   10889 C CB  . ASN F  2 79  ? 28.501  60.863 65.375  1.00 30.32  ? 79   ASN F CB  1 
ATOM   10890 C CG  . ASN F  2 79  ? 29.045  61.687 64.225  1.00 29.65  ? 79   ASN F CG  1 
ATOM   10891 O OD1 . ASN F  2 79  ? 28.292  62.353 63.518  1.00 30.20  ? 79   ASN F OD1 1 
ATOM   10892 N ND2 . ASN F  2 79  ? 30.354  61.659 64.040  1.00 28.86  ? 79   ASN F ND2 1 
ATOM   10893 N N   . LEU F  2 80  ? 28.490  57.847 64.473  1.00 28.98  ? 80   LEU F N   1 
ATOM   10894 C CA  . LEU F  2 80  ? 28.966  56.732 63.660  1.00 28.26  ? 80   LEU F CA  1 
ATOM   10895 C C   . LEU F  2 80  ? 27.786  56.132 62.923  1.00 28.68  ? 80   LEU F C   1 
ATOM   10896 O O   . LEU F  2 80  ? 27.844  55.896 61.723  1.00 27.85  ? 80   LEU F O   1 
ATOM   10897 C CB  . LEU F  2 80  ? 29.620  55.671 64.553  1.00 28.90  ? 80   LEU F CB  1 
ATOM   10898 C CG  . LEU F  2 80  ? 30.471  54.559 63.930  1.00 28.72  ? 80   LEU F CG  1 
ATOM   10899 C CD1 . LEU F  2 80  ? 31.209  53.802 65.026  1.00 29.82  ? 80   LEU F CD1 1 
ATOM   10900 C CD2 . LEU F  2 80  ? 29.643  53.591 63.105  1.00 29.14  ? 80   LEU F CD2 1 
ATOM   10901 N N   . ASN F  2 81  ? 26.709  55.901 63.662  1.00 30.29  ? 81   ASN F N   1 
ATOM   10902 C CA  . ASN F  2 81  ? 25.484  55.360 63.107  1.00 31.34  ? 81   ASN F CA  1 
ATOM   10903 C C   . ASN F  2 81  ? 24.914  56.234 61.995  1.00 30.84  ? 81   ASN F C   1 
ATOM   10904 O O   . ASN F  2 81  ? 24.494  55.722 60.967  1.00 30.62  ? 81   ASN F O   1 
ATOM   10905 C CB  . ASN F  2 81  ? 24.448  55.197 64.211  1.00 33.63  ? 81   ASN F CB  1 
ATOM   10906 C CG  . ASN F  2 81  ? 23.158  54.602 63.707  1.00 35.27  ? 81   ASN F CG  1 
ATOM   10907 O OD1 . ASN F  2 81  ? 23.139  53.480 63.217  1.00 35.54  ? 81   ASN F OD1 1 
ATOM   10908 N ND2 . ASN F  2 81  ? 22.069  55.349 63.827  1.00 36.77  ? 81   ASN F ND2 1 
ATOM   10909 N N   . LYS F  2 82  ? 24.905  57.549 62.205  1.00 30.96  ? 82   LYS F N   1 
ATOM   10910 C CA  . LYS F  2 82  ? 24.382  58.481 61.210  1.00 30.95  ? 82   LYS F CA  1 
ATOM   10911 C C   . LYS F  2 82  ? 25.213  58.437 59.941  1.00 29.04  ? 82   LYS F C   1 
ATOM   10912 O O   . LYS F  2 82  ? 24.664  58.360 58.846  1.00 28.81  ? 82   LYS F O   1 
ATOM   10913 C CB  . LYS F  2 82  ? 24.336  59.919 61.744  1.00 31.94  ? 82   LYS F CB  1 
ATOM   10914 C CG  . LYS F  2 82  ? 23.968  60.947 60.671  1.00 32.18  ? 82   LYS F CG  1 
ATOM   10915 C CD  . LYS F  2 82  ? 23.481  62.275 61.246  1.00 34.34  ? 82   LYS F CD  1 
ATOM   10916 C CE  . LYS F  2 82  ? 24.599  63.310 61.368  1.00 33.93  ? 82   LYS F CE  1 
ATOM   10917 N NZ  . LYS F  2 82  ? 24.140  64.559 62.054  1.00 36.48  ? 82   LYS F NZ  1 
ATOM   10918 N N   . LYS F  2 83  ? 26.533  58.492 60.093  1.00 44.43  ? 83   LYS F N   1 
ATOM   10919 C CA  . LYS F  2 83  ? 27.440  58.485 58.942  1.00 42.78  ? 83   LYS F CA  1 
ATOM   10920 C C   . LYS F  2 83  ? 27.361  57.188 58.159  1.00 39.82  ? 83   LYS F C   1 
ATOM   10921 O O   . LYS F  2 83  ? 27.415  57.195 56.935  1.00 38.02  ? 83   LYS F O   1 
ATOM   10922 C CB  . LYS F  2 83  ? 28.883  58.769 59.383  1.00 44.58  ? 83   LYS F CB  1 
ATOM   10923 C CG  . LYS F  2 83  ? 29.272  60.245 59.330  1.00 47.28  ? 83   LYS F CG  1 
ATOM   10924 C CD  . LYS F  2 83  ? 28.159  61.178 59.808  1.00 49.26  ? 83   LYS F CD  1 
ATOM   10925 C CE  . LYS F  2 83  ? 28.468  62.644 59.538  1.00 52.19  ? 83   LYS F CE  1 
ATOM   10926 N NZ  . LYS F  2 83  ? 29.021  63.323 60.745  1.00 56.09  ? 83   LYS F NZ  1 
ATOM   10927 N N   . MET F  2 84  ? 27.214  56.080 58.870  1.00 39.70  ? 84   MET F N   1 
ATOM   10928 C CA  . MET F  2 84  ? 27.036  54.790 58.235  1.00 37.65  ? 84   MET F CA  1 
ATOM   10929 C C   . MET F  2 84  ? 25.771  54.787 57.377  1.00 36.18  ? 84   MET F C   1 
ATOM   10930 O O   . MET F  2 84  ? 25.824  54.423 56.203  1.00 34.19  ? 84   MET F O   1 
ATOM   10931 C CB  . MET F  2 84  ? 26.961  53.687 59.288  1.00 38.66  ? 84   MET F CB  1 
ATOM   10932 C CG  . MET F  2 84  ? 27.222  52.296 58.744  1.00 37.50  ? 84   MET F CG  1 
ATOM   10933 S SD  . MET F  2 84  ? 26.077  51.096 59.425  1.00 38.42  ? 84   MET F SD  1 
ATOM   10934 C CE  . MET F  2 84  ? 24.617  51.557 58.509  1.00 37.14  ? 84   MET F CE  1 
ATOM   10935 N N   . GLU F  2 85  ? 24.646  55.208 57.958  1.00 37.49  ? 85   GLU F N   1 
ATOM   10936 C CA  . GLU F  2 85  ? 23.363  55.200 57.246  1.00 36.81  ? 85   GLU F CA  1 
ATOM   10937 C C   . GLU F  2 85  ? 23.357  56.197 56.082  1.00 35.81  ? 85   GLU F C   1 
ATOM   10938 O O   . GLU F  2 85  ? 22.935  55.858 54.980  1.00 34.02  ? 85   GLU F O   1 
ATOM   10939 C CB  . GLU F  2 85  ? 22.183  55.444 58.201  1.00 39.30  ? 85   GLU F CB  1 
ATOM   10940 C CG  . GLU F  2 85  ? 22.096  54.417 59.331  1.00 40.61  ? 85   GLU F CG  1 
ATOM   10941 C CD  . GLU F  2 85  ? 20.687  53.919 59.631  1.00 42.21  ? 85   GLU F CD  1 
ATOM   10942 O OE1 . GLU F  2 85  ? 19.880  54.673 60.220  1.00 44.67  ? 85   GLU F OE1 1 
ATOM   10943 O OE2 . GLU F  2 85  ? 20.396  52.746 59.312  1.00 41.62  ? 85   GLU F OE2 1 
ATOM   10944 N N   . ASP F  2 86  ? 23.845  57.410 56.322  1.00 37.25  ? 86   ASP F N   1 
ATOM   10945 C CA  . ASP F  2 86  ? 23.996  58.411 55.258  1.00 36.89  ? 86   ASP F CA  1 
ATOM   10946 C C   . ASP F  2 86  ? 24.955  57.978 54.156  1.00 34.53  ? 86   ASP F C   1 
ATOM   10947 O O   . ASP F  2 86  ? 24.724  58.259 52.977  1.00 33.30  ? 86   ASP F O   1 
ATOM   10948 C CB  . ASP F  2 86  ? 24.496  59.742 55.828  1.00 39.71  ? 86   ASP F CB  1 
ATOM   10949 C CG  . ASP F  2 86  ? 23.373  60.674 56.192  1.00 42.31  ? 86   ASP F CG  1 
ATOM   10950 O OD1 . ASP F  2 86  ? 22.458  60.844 55.356  1.00 41.84  ? 86   ASP F OD1 1 
ATOM   10951 O OD2 . ASP F  2 86  ? 23.412  61.250 57.299  1.00 45.21  ? 86   ASP F OD2 1 
ATOM   10952 N N   . GLY F  2 87  ? 26.042  57.326 54.552  1.00 34.28  ? 87   GLY F N   1 
ATOM   10953 C CA  . GLY F  2 87  ? 27.058  56.876 53.614  1.00 32.78  ? 87   GLY F CA  1 
ATOM   10954 C C   . GLY F  2 87  ? 26.530  55.887 52.596  1.00 30.33  ? 87   GLY F C   1 
ATOM   10955 O O   . GLY F  2 87  ? 26.826  55.999 51.405  1.00 29.10  ? 87   GLY F O   1 
ATOM   10956 N N   . PHE F  2 88  ? 25.740  54.923 53.064  1.00 29.98  ? 88   PHE F N   1 
ATOM   10957 C CA  . PHE F  2 88  ? 25.141  53.927 52.180  1.00 28.24  ? 88   PHE F CA  1 
ATOM   10958 C C   . PHE F  2 88  ? 24.078  54.536 51.262  1.00 27.48  ? 88   PHE F C   1 
ATOM   10959 O O   . PHE F  2 88  ? 23.957  54.131 50.108  1.00 25.88  ? 88   PHE F O   1 
ATOM   10960 C CB  . PHE F  2 88  ? 24.546  52.766 52.980  1.00 28.88  ? 88   PHE F CB  1 
ATOM   10961 C CG  . PHE F  2 88  ? 25.568  51.777 53.470  1.00 29.39  ? 88   PHE F CG  1 
ATOM   10962 C CD1 . PHE F  2 88  ? 26.334  51.049 52.573  1.00 28.46  ? 88   PHE F CD1 1 
ATOM   10963 C CD2 . PHE F  2 88  ? 25.761  51.568 54.825  1.00 31.20  ? 88   PHE F CD2 1 
ATOM   10964 C CE1 . PHE F  2 88  ? 27.276  50.135 53.017  1.00 29.57  ? 88   PHE F CE1 1 
ATOM   10965 C CE2 . PHE F  2 88  ? 26.699  50.654 55.277  1.00 32.10  ? 88   PHE F CE2 1 
ATOM   10966 C CZ  . PHE F  2 88  ? 27.456  49.936 54.372  1.00 31.41  ? 88   PHE F CZ  1 
ATOM   10967 N N   . LEU F  2 89  ? 23.319  55.507 51.763  1.00 28.98  ? 89   LEU F N   1 
ATOM   10968 C CA  . LEU F  2 89  ? 22.353  56.212 50.920  1.00 28.92  ? 89   LEU F CA  1 
ATOM   10969 C C   . LEU F  2 89  ? 23.035  56.917 49.750  1.00 27.90  ? 89   LEU F C   1 
ATOM   10970 O O   . LEU F  2 89  ? 22.524  56.902 48.641  1.00 26.70  ? 89   LEU F O   1 
ATOM   10971 C CB  . LEU F  2 89  ? 21.559  57.238 51.723  1.00 31.52  ? 89   LEU F CB  1 
ATOM   10972 C CG  . LEU F  2 89  ? 20.616  56.703 52.802  1.00 33.21  ? 89   LEU F CG  1 
ATOM   10973 C CD1 . LEU F  2 89  ? 19.877  57.876 53.439  1.00 36.22  ? 89   LEU F CD1 1 
ATOM   10974 C CD2 . LEU F  2 89  ? 19.646  55.654 52.257  1.00 32.39  ? 89   LEU F CD2 1 
ATOM   10975 N N   . ASP F  2 90  ? 24.182  57.537 50.014  1.00 28.76  ? 90   ASP F N   1 
ATOM   10976 C CA  . ASP F  2 90  ? 24.948  58.229 48.977  1.00 28.46  ? 90   ASP F CA  1 
ATOM   10977 C C   . ASP F  2 90  ? 25.515  57.253 47.962  1.00 26.26  ? 90   ASP F C   1 
ATOM   10978 O O   . ASP F  2 90  ? 25.524  57.536 46.768  1.00 25.37  ? 90   ASP F O   1 
ATOM   10979 C CB  . ASP F  2 90  ? 26.091  59.038 49.590  1.00 30.55  ? 90   ASP F CB  1 
ATOM   10980 C CG  . ASP F  2 90  ? 25.602  60.179 50.452  1.00 33.33  ? 90   ASP F CG  1 
ATOM   10981 O OD1 . ASP F  2 90  ? 24.432  60.598 50.290  1.00 33.82  ? 90   ASP F OD1 1 
ATOM   10982 O OD2 . ASP F  2 90  ? 26.390  60.652 51.302  1.00 35.44  ? 90   ASP F OD2 1 
ATOM   10983 N N   . VAL F  2 91  ? 25.994  56.112 48.447  1.00 25.79  ? 91   VAL F N   1 
ATOM   10984 C CA  . VAL F  2 91  ? 26.507  55.057 47.579  1.00 24.31  ? 91   VAL F CA  1 
ATOM   10985 C C   . VAL F  2 91  ? 25.406  54.542 46.662  1.00 22.74  ? 91   VAL F C   1 
ATOM   10986 O O   . VAL F  2 91  ? 25.604  54.445 45.451  1.00 21.62  ? 91   VAL F O   1 
ATOM   10987 C CB  . VAL F  2 91  ? 27.099  53.883 48.391  1.00 24.80  ? 91   VAL F CB  1 
ATOM   10988 C CG1 . VAL F  2 91  ? 27.352  52.672 47.501  1.00 23.77  ? 91   VAL F CG1 1 
ATOM   10989 C CG2 . VAL F  2 91  ? 28.390  54.312 49.072  1.00 26.53  ? 91   VAL F CG2 1 
ATOM   10990 N N   . TRP F  2 92  ? 24.252  54.226 47.239  1.00 23.02  ? 92   TRP F N   1 
ATOM   10991 C CA  . TRP F  2 92  ? 23.144  53.682 46.460  1.00 22.13  ? 92   TRP F CA  1 
ATOM   10992 C C   . TRP F  2 92  ? 22.444  54.726 45.588  1.00 21.91  ? 92   TRP F C   1 
ATOM   10993 O O   . TRP F  2 92  ? 21.930  54.391 44.524  1.00 20.86  ? 92   TRP F O   1 
ATOM   10994 C CB  . TRP F  2 92  ? 22.147  52.957 47.365  1.00 23.19  ? 92   TRP F CB  1 
ATOM   10995 C CG  . TRP F  2 92  ? 22.655  51.613 47.790  1.00 23.42  ? 92   TRP F CG  1 
ATOM   10996 C CD1 . TRP F  2 92  ? 23.015  51.227 49.051  1.00 24.77  ? 92   TRP F CD1 1 
ATOM   10997 C CD2 . TRP F  2 92  ? 22.880  50.478 46.945  1.00 22.69  ? 92   TRP F CD2 1 
ATOM   10998 N NE1 . TRP F  2 92  ? 23.439  49.920 49.044  1.00 25.06  ? 92   TRP F NE1 1 
ATOM   10999 C CE2 . TRP F  2 92  ? 23.366  49.437 47.763  1.00 23.91  ? 92   TRP F CE2 1 
ATOM   11000 C CE3 . TRP F  2 92  ? 22.708  50.237 45.576  1.00 21.47  ? 92   TRP F CE3 1 
ATOM   11001 C CZ2 . TRP F  2 92  ? 23.683  48.173 47.258  1.00 24.22  ? 92   TRP F CZ2 1 
ATOM   11002 C CZ3 . TRP F  2 92  ? 23.023  48.981 45.074  1.00 21.60  ? 92   TRP F CZ3 1 
ATOM   11003 C CH2 . TRP F  2 92  ? 23.505  47.964 45.915  1.00 23.11  ? 92   TRP F CH2 1 
ATOM   11004 N N   . THR F  2 93  ? 22.429  55.981 46.027  1.00 23.26  ? 93   THR F N   1 
ATOM   11005 C CA  . THR F  2 93  ? 21.889  57.062 45.207  1.00 23.67  ? 93   THR F CA  1 
ATOM   11006 C C   . THR F  2 93  ? 22.766  57.243 43.971  1.00 22.46  ? 93   THR F C   1 
ATOM   11007 O O   . THR F  2 93  ? 22.265  57.355 42.855  1.00 21.71  ? 93   THR F O   1 
ATOM   11008 C CB  . THR F  2 93  ? 21.806  58.393 45.984  1.00 26.08  ? 93   THR F CB  1 
ATOM   11009 O OG1 . THR F  2 93  ? 20.891  58.250 47.073  1.00 27.60  ? 93   THR F OG1 1 
ATOM   11010 C CG2 . THR F  2 93  ? 21.327  59.525 45.087  1.00 26.99  ? 93   THR F CG2 1 
ATOM   11011 N N   . TYR F  2 94  ? 24.075  57.267 44.187  1.00 22.66  ? 94   TYR F N   1 
ATOM   11012 C CA  . TYR F  2 94  ? 25.047  57.431 43.111  1.00 22.15  ? 94   TYR F CA  1 
ATOM   11013 C C   . TYR F  2 94  ? 24.925  56.310 42.079  1.00 20.24  ? 94   TYR F C   1 
ATOM   11014 O O   . TYR F  2 94  ? 24.892  56.570 40.880  1.00 19.55  ? 94   TYR F O   1 
ATOM   11015 C CB  . TYR F  2 94  ? 26.460  57.471 43.704  1.00 23.27  ? 94   TYR F CB  1 
ATOM   11016 C CG  . TYR F  2 94  ? 27.579  57.283 42.710  1.00 23.04  ? 94   TYR F CG  1 
ATOM   11017 C CD1 . TYR F  2 94  ? 28.035  56.012 42.380  1.00 21.98  ? 94   TYR F CD1 1 
ATOM   11018 C CD2 . TYR F  2 94  ? 28.196  58.374 42.117  1.00 24.45  ? 94   TYR F CD2 1 
ATOM   11019 C CE1 . TYR F  2 94  ? 29.065  55.837 41.477  1.00 22.29  ? 94   TYR F CE1 1 
ATOM   11020 C CE2 . TYR F  2 94  ? 29.225  58.206 41.213  1.00 24.73  ? 94   TYR F CE2 1 
ATOM   11021 C CZ  . TYR F  2 94  ? 29.655  56.938 40.898  1.00 23.61  ? 94   TYR F CZ  1 
ATOM   11022 O OH  . TYR F  2 94  ? 30.678  56.771 39.999  1.00 24.39  ? 94   TYR F OH  1 
ATOM   11023 N N   . ASN F  2 95  ? 24.853  55.071 42.562  1.00 19.80  ? 95   ASN F N   1 
ATOM   11024 C CA  . ASN F  2 95  ? 24.662  53.898 41.709  1.00 18.61  ? 95   ASN F CA  1 
ATOM   11025 C C   . ASN F  2 95  ? 23.448  54.020 40.805  1.00 17.92  ? 95   ASN F C   1 
ATOM   11026 O O   . ASN F  2 95  ? 23.534  53.753 39.602  1.00 17.05  ? 95   ASN F O   1 
ATOM   11027 C CB  . ASN F  2 95  ? 24.515  52.633 42.559  1.00 18.94  ? 95   ASN F CB  1 
ATOM   11028 C CG  . ASN F  2 95  ? 25.822  52.206 43.202  1.00 19.86  ? 95   ASN F CG  1 
ATOM   11029 O OD1 . ASN F  2 95  ? 26.863  52.832 42.995  1.00 20.37  ? 95   ASN F OD1 1 
ATOM   11030 N ND2 . ASN F  2 95  ? 25.773  51.138 43.991  1.00 20.56  ? 95   ASN F ND2 1 
ATOM   11031 N N   . ALA F  2 96  ? 22.323  54.420 41.396  1.00 18.70  ? 96   ALA F N   1 
ATOM   11032 C CA  . ALA F  2 96  ? 21.059  54.564 40.674  1.00 18.64  ? 96   ALA F CA  1 
ATOM   11033 C C   . ALA F  2 96  ? 21.162  55.623 39.586  1.00 18.41  ? 96   ALA F C   1 
ATOM   11034 O O   . ALA F  2 96  ? 20.819  55.372 38.436  1.00 17.57  ? 96   ALA F O   1 
ATOM   11035 C CB  . ALA F  2 96  ? 19.942  54.927 41.642  1.00 20.29  ? 96   ALA F CB  1 
ATOM   11036 N N   . GLU F  2 97  ? 21.637  56.805 39.957  1.00 19.53  ? 97   GLU F N   1 
ATOM   11037 C CA  . GLU F  2 97  ? 21.696  57.932 39.028  1.00 20.09  ? 97   GLU F CA  1 
ATOM   11038 C C   . GLU F  2 97  ? 22.715  57.720 37.911  1.00 18.92  ? 97   GLU F C   1 
ATOM   11039 O O   . GLU F  2 97  ? 22.497  58.148 36.778  1.00 18.80  ? 97   GLU F O   1 
ATOM   11040 C CB  . GLU F  2 97  ? 22.012  59.221 39.781  1.00 22.34  ? 97   GLU F CB  1 
ATOM   11041 C CG  . GLU F  2 97  ? 20.920  59.620 40.758  1.00 24.15  ? 97   GLU F CG  1 
ATOM   11042 C CD  . GLU F  2 97  ? 21.175  60.956 41.415  1.00 26.95  ? 97   GLU F CD  1 
ATOM   11043 O OE1 . GLU F  2 97  ? 22.281  61.508 41.238  1.00 27.56  ? 97   GLU F OE1 1 
ATOM   11044 O OE2 . GLU F  2 97  ? 20.265  61.458 42.110  1.00 29.12  ? 97   GLU F OE2 1 
ATOM   11045 N N   . LEU F  2 98  ? 23.827  57.065 38.235  1.00 18.46  ? 98   LEU F N   1 
ATOM   11046 C CA  . LEU F  2 98  ? 24.856  56.781 37.250  1.00 17.87  ? 98   LEU F CA  1 
ATOM   11047 C C   . LEU F  2 98  ? 24.358  55.725 36.278  1.00 16.30  ? 98   LEU F C   1 
ATOM   11048 O O   . LEU F  2 98  ? 24.473  55.896 35.073  1.00 15.91  ? 98   LEU F O   1 
ATOM   11049 C CB  . LEU F  2 98  ? 26.142  56.302 37.923  1.00 18.46  ? 98   LEU F CB  1 
ATOM   11050 C CG  . LEU F  2 98  ? 27.327  56.079 36.981  1.00 18.73  ? 98   LEU F CG  1 
ATOM   11051 C CD1 . LEU F  2 98  ? 27.823  57.405 36.426  1.00 20.19  ? 98   LEU F CD1 1 
ATOM   11052 C CD2 . LEU F  2 98  ? 28.455  55.343 37.691  1.00 19.68  ? 98   LEU F CD2 1 
ATOM   11053 N N   . LEU F  2 99  ? 23.806  54.638 36.807  1.00 15.77  ? 99   LEU F N   1 
ATOM   11054 C CA  . LEU F  2 99  ? 23.292  53.558 35.971  1.00 14.89  ? 99   LEU F CA  1 
ATOM   11055 C C   . LEU F  2 99  ? 22.261  54.083 34.971  1.00 14.48  ? 99   LEU F C   1 
ATOM   11056 O O   . LEU F  2 99  ? 22.271  53.710 33.801  1.00 13.86  ? 99   LEU F O   1 
ATOM   11057 C CB  . LEU F  2 99  ? 22.659  52.459 36.832  1.00 15.17  ? 99   LEU F CB  1 
ATOM   11058 C CG  . LEU F  2 99  ? 22.191  51.190 36.102  1.00 15.00  ? 99   LEU F CG  1 
ATOM   11059 C CD1 . LEU F  2 99  ? 23.345  50.514 35.379  1.00 14.97  ? 99   LEU F CD1 1 
ATOM   11060 C CD2 . LEU F  2 99  ? 21.536  50.218 37.073  1.00 15.99  ? 99   LEU F CD2 1 
ATOM   11061 N N   . VAL F  2 100 ? 21.375  54.952 35.441  1.00 15.15  ? 100  VAL F N   1 
ATOM   11062 C CA  . VAL F  2 100 ? 20.370  55.553 34.575  1.00 15.33  ? 100  VAL F CA  1 
ATOM   11063 C C   . VAL F  2 100 ? 21.042  56.382 33.474  1.00 15.18  ? 100  VAL F C   1 
ATOM   11064 O O   . VAL F  2 100 ? 20.747  56.192 32.300  1.00 14.61  ? 100  VAL F O   1 
ATOM   11065 C CB  . VAL F  2 100 ? 19.339  56.368 35.396  1.00 16.90  ? 100  VAL F CB  1 
ATOM   11066 C CG1 . VAL F  2 100 ? 18.514  57.288 34.506  1.00 17.80  ? 100  VAL F CG1 1 
ATOM   11067 C CG2 . VAL F  2 100 ? 18.426  55.416 36.157  1.00 17.31  ? 100  VAL F CG2 1 
ATOM   11068 N N   . LEU F  2 101 ? 21.951  57.274 33.856  1.00 16.01  ? 101  LEU F N   1 
ATOM   11069 C CA  . LEU F  2 101 ? 22.731  58.070 32.896  1.00 16.50  ? 101  LEU F CA  1 
ATOM   11070 C C   . LEU F  2 101 ? 23.448  57.231 31.820  1.00 15.39  ? 101  LEU F C   1 
ATOM   11071 O O   . LEU F  2 101 ? 23.365  57.534 30.624  1.00 15.35  ? 101  LEU F O   1 
ATOM   11072 C CB  . LEU F  2 101 ? 23.776  58.910 33.636  1.00 18.08  ? 101  LEU F CB  1 
ATOM   11073 C CG  . LEU F  2 101 ? 23.537  60.413 33.784  1.00 20.38  ? 101  LEU F CG  1 
ATOM   11074 C CD1 . LEU F  2 101 ? 22.100  60.749 34.142  1.00 20.99  ? 101  LEU F CD1 1 
ATOM   11075 C CD2 . LEU F  2 101 ? 24.495  60.966 34.826  1.00 22.11  ? 101  LEU F CD2 1 
ATOM   11076 N N   . MET F  2 102 ? 24.165  56.200 32.252  1.00 14.85  ? 102  MET F N   1 
ATOM   11077 C CA  . MET F  2 102 ? 24.957  55.384 31.342  1.00 14.49  ? 102  MET F CA  1 
ATOM   11078 C C   . MET F  2 102 ? 24.084  54.549 30.413  1.00 13.43  ? 102  MET F C   1 
ATOM   11079 O O   . MET F  2 102 ? 24.357  54.450 29.211  1.00 13.34  ? 102  MET F O   1 
ATOM   11080 C CB  . MET F  2 102 ? 25.888  54.463 32.127  1.00 14.88  ? 102  MET F CB  1 
ATOM   11081 C CG  . MET F  2 102 ? 26.950  55.206 32.915  1.00 16.38  ? 102  MET F CG  1 
ATOM   11082 S SD  . MET F  2 102 ? 28.235  54.124 33.577  1.00 17.50  ? 102  MET F SD  1 
ATOM   11083 C CE  . MET F  2 102 ? 27.255  52.997 34.565  1.00 16.45  ? 102  MET F CE  1 
ATOM   11084 N N   . GLU F  2 103 ? 23.046  53.939 30.977  1.00 12.97  ? 103  GLU F N   1 
ATOM   11085 C CA  . GLU F  2 103 ? 22.184  53.053 30.217  1.00 12.46  ? 103  GLU F CA  1 
ATOM   11086 C C   . GLU F  2 103 ? 21.212  53.812 29.312  1.00 12.37  ? 103  GLU F C   1 
ATOM   11087 O O   . GLU F  2 103 ? 20.853  53.313 28.250  1.00 12.11  ? 103  GLU F O   1 
ATOM   11088 C CB  . GLU F  2 103 ? 21.443  52.105 31.155  1.00 12.73  ? 103  GLU F CB  1 
ATOM   11089 C CG  . GLU F  2 103 ? 22.339  51.045 31.796  1.00 13.19  ? 103  GLU F CG  1 
ATOM   11090 C CD  . GLU F  2 103 ? 23.043  50.135 30.792  1.00 13.49  ? 103  GLU F CD  1 
ATOM   11091 O OE1 . GLU F  2 103 ? 22.531  49.953 29.673  1.00 13.25  ? 103  GLU F OE1 1 
ATOM   11092 O OE2 . GLU F  2 103 ? 24.125  49.590 31.123  1.00 14.35  ? 103  GLU F OE2 1 
ATOM   11093 N N   . ASN F  2 104 ? 20.791  55.007 29.724  1.00 12.95  ? 104  ASN F N   1 
ATOM   11094 C CA  . ASN F  2 104 ? 20.044  55.904 28.839  1.00 13.41  ? 104  ASN F CA  1 
ATOM   11095 C C   . ASN F  2 104 ? 20.834  56.212 27.576  1.00 13.25  ? 104  ASN F C   1 
ATOM   11096 O O   . ASN F  2 104 ? 20.287  56.208 26.474  1.00 13.14  ? 104  ASN F O   1 
ATOM   11097 C CB  . ASN F  2 104 ? 19.732  57.236 29.525  1.00 14.77  ? 104  ASN F CB  1 
ATOM   11098 C CG  . ASN F  2 104 ? 18.534  57.160 30.437  1.00 15.58  ? 104  ASN F CG  1 
ATOM   11099 O OD1 . ASN F  2 104 ? 17.813  56.169 30.453  1.00 15.22  ? 104  ASN F OD1 1 
ATOM   11100 N ND2 . ASN F  2 104 ? 18.318  58.216 31.210  1.00 17.18  ? 104  ASN F ND2 1 
ATOM   11101 N N   . GLU F  2 105 ? 22.119  56.497 27.751  1.00 13.54  ? 105  GLU F N   1 
ATOM   11102 C CA  . GLU F  2 105 ? 22.984  56.783 26.622  1.00 13.92  ? 105  GLU F CA  1 
ATOM   11103 C C   . GLU F  2 105 ? 23.130  55.561 25.728  1.00 12.99  ? 105  GLU F C   1 
ATOM   11104 O O   . GLU F  2 105 ? 23.112  55.669 24.509  1.00 13.08  ? 105  GLU F O   1 
ATOM   11105 C CB  . GLU F  2 105 ? 24.357  57.240 27.095  1.00 15.11  ? 105  GLU F CB  1 
ATOM   11106 C CG  . GLU F  2 105 ? 25.119  58.003 26.026  1.00 16.52  ? 105  GLU F CG  1 
ATOM   11107 C CD  . GLU F  2 105 ? 26.304  58.737 26.599  1.00 18.50  ? 105  GLU F CD  1 
ATOM   11108 O OE1 . GLU F  2 105 ? 27.105  58.076 27.300  1.00 18.62  ? 105  GLU F OE1 1 
ATOM   11109 O OE2 . GLU F  2 105 ? 26.423  59.969 26.364  1.00 20.40  ? 105  GLU F OE2 1 
ATOM   11110 N N   . ARG F  2 106 ? 23.269  54.396 26.338  1.00 12.43  ? 106  ARG F N   1 
ATOM   11111 C CA  . ARG F  2 106 ? 23.332  53.168 25.564  1.00 12.19  ? 106  ARG F CA  1 
ATOM   11112 C C   . ARG F  2 106 ? 22.015  52.864 24.850  1.00 11.59  ? 106  ARG F C   1 
ATOM   11113 O O   . ARG F  2 106 ? 22.031  52.331 23.746  1.00 11.71  ? 106  ARG F O   1 
ATOM   11114 C CB  . ARG F  2 106 ? 23.738  51.989 26.440  1.00 12.56  ? 106  ARG F CB  1 
ATOM   11115 C CG  . ARG F  2 106 ? 25.180  52.046 26.914  1.00 13.62  ? 106  ARG F CG  1 
ATOM   11116 C CD  . ARG F  2 106 ? 25.755  50.645 27.051  1.00 14.64  ? 106  ARG F CD  1 
ATOM   11117 N NE  . ARG F  2 106 ? 26.581  50.235 25.901  1.00 15.84  ? 106  ARG F NE  1 
ATOM   11118 C CZ  . ARG F  2 106 ? 26.715  48.977 25.471  1.00 17.00  ? 106  ARG F CZ  1 
ATOM   11119 N NH1 . ARG F  2 106 ? 26.050  47.977 26.052  1.00 17.15  ? 106  ARG F NH1 1 
ATOM   11120 N NH2 . ARG F  2 106 ? 27.513  48.702 24.438  1.00 18.50  ? 106  ARG F NH2 1 
ATOM   11121 N N   . THR F  2 107 ? 20.887  53.198 25.476  1.00 11.27  ? 107  THR F N   1 
ATOM   11122 C CA  . THR F  2 107 ? 19.576  52.955 24.880  1.00 11.25  ? 107  THR F CA  1 
ATOM   11123 C C   . THR F  2 107 ? 19.373  53.786 23.611  1.00 11.24  ? 107  THR F C   1 
ATOM   11124 O O   . THR F  2 107 ? 18.888  53.276 22.609  1.00 11.30  ? 107  THR F O   1 
ATOM   11125 C CB  . THR F  2 107 ? 18.432  53.236 25.876  1.00 11.79  ? 107  THR F CB  1 
ATOM   11126 O OG1 . THR F  2 107 ? 18.484  52.287 26.945  1.00 11.92  ? 107  THR F OG1 1 
ATOM   11127 C CG2 . THR F  2 107 ? 17.076  53.115 25.200  1.00 12.58  ? 107  THR F CG2 1 
ATOM   11128 N N   . LEU F  2 108 ? 19.751  55.056 23.650  1.00 11.39  ? 108  LEU F N   1 
ATOM   11129 C CA  . LEU F  2 108 ? 19.626  55.903 22.473  1.00 11.82  ? 108  LEU F CA  1 
ATOM   11130 C C   . LEU F  2 108 ? 20.508  55.402 21.321  1.00 11.48  ? 108  LEU F C   1 
ATOM   11131 O O   . LEU F  2 108 ? 20.081  55.362 20.169  1.00 11.66  ? 108  LEU F O   1 
ATOM   11132 C CB  . LEU F  2 108 ? 19.966  57.351 22.817  1.00 12.88  ? 108  LEU F CB  1 
ATOM   11133 C CG  . LEU F  2 108 ? 19.098  58.014 23.890  1.00 13.75  ? 108  LEU F CG  1 
ATOM   11134 C CD1 . LEU F  2 108 ? 19.404  59.499 23.939  1.00 15.52  ? 108  LEU F CD1 1 
ATOM   11135 C CD2 . LEU F  2 108 ? 17.613  57.791 23.654  1.00 14.23  ? 108  LEU F CD2 1 
ATOM   11136 N N   . ASP F  2 109 ? 21.736  55.016 21.648  1.00 11.29  ? 109  ASP F N   1 
ATOM   11137 C CA  . ASP F  2 109 ? 22.661  54.470 20.665  1.00 11.53  ? 109  ASP F CA  1 
ATOM   11138 C C   . ASP F  2 109 ? 22.200  53.117 20.117  1.00 11.14  ? 109  ASP F C   1 
ATOM   11139 O O   . ASP F  2 109 ? 22.467  52.797 18.967  1.00 11.63  ? 109  ASP F O   1 
ATOM   11140 C CB  . ASP F  2 109 ? 24.048  54.323 21.280  1.00 12.17  ? 109  ASP F CB  1 
ATOM   11141 C CG  . ASP F  2 109 ? 24.714  55.660 21.563  1.00 13.24  ? 109  ASP F CG  1 
ATOM   11142 O OD1 . ASP F  2 109 ? 24.457  56.644 20.826  1.00 13.90  ? 109  ASP F OD1 1 
ATOM   11143 O OD2 . ASP F  2 109 ? 25.527  55.708 22.521  1.00 13.80  ? 109  ASP F OD2 1 
ATOM   11144 N N   . PHE F  2 110 ? 21.525  52.328 20.947  1.00 10.62  ? 110  PHE F N   1 
ATOM   11145 C CA  . PHE F  2 110 ? 20.958  51.044 20.538  1.00 10.86  ? 110  PHE F CA  1 
ATOM   11146 C C   . PHE F  2 110 ? 19.923  51.264 19.429  1.00 10.95  ? 110  PHE F C   1 
ATOM   11147 O O   . PHE F  2 110 ? 19.924  50.572 18.412  1.00 11.55  ? 110  PHE F O   1 
ATOM   11148 C CB  . PHE F  2 110 ? 20.337  50.359 21.766  1.00 10.88  ? 110  PHE F CB  1 
ATOM   11149 C CG  . PHE F  2 110 ? 19.642  49.057 21.475  1.00 11.87  ? 110  PHE F CG  1 
ATOM   11150 C CD1 . PHE F  2 110 ? 20.318  47.999 20.887  1.00 12.93  ? 110  PHE F CD1 1 
ATOM   11151 C CD2 . PHE F  2 110 ? 18.316  48.876 21.830  1.00 12.36  ? 110  PHE F CD2 1 
ATOM   11152 C CE1 . PHE F  2 110 ? 19.673  46.797 20.636  1.00 14.44  ? 110  PHE F CE1 1 
ATOM   11153 C CE2 . PHE F  2 110 ? 17.666  47.675 21.586  1.00 13.88  ? 110  PHE F CE2 1 
ATOM   11154 C CZ  . PHE F  2 110 ? 18.343  46.634 20.985  1.00 14.93  ? 110  PHE F CZ  1 
ATOM   11155 N N   . HIS F  2 111 ? 19.050  52.243 19.628  1.00 10.68  ? 111  HIS F N   1 
ATOM   11156 C CA  . HIS F  2 111 ? 18.070  52.619 18.620  1.00 11.11  ? 111  HIS F CA  1 
ATOM   11157 C C   . HIS F  2 111 ? 18.743  53.116 17.344  1.00 11.19  ? 111  HIS F C   1 
ATOM   11158 O O   . HIS F  2 111 ? 18.305  52.799 16.238  1.00 11.69  ? 111  HIS F O   1 
ATOM   11159 C CB  . HIS F  2 111 ? 17.140  53.699 19.163  1.00 11.48  ? 111  HIS F CB  1 
ATOM   11160 C CG  . HIS F  2 111 ? 16.160  53.196 20.175  1.00 11.97  ? 111  HIS F CG  1 
ATOM   11161 N ND1 . HIS F  2 111 ? 15.194  52.260 19.871  1.00 12.92  ? 111  HIS F ND1 1 
ATOM   11162 C CD2 . HIS F  2 111 ? 15.977  53.517 21.477  1.00 12.05  ? 111  HIS F CD2 1 
ATOM   11163 C CE1 . HIS F  2 111 ? 14.467  52.019 20.946  1.00 13.68  ? 111  HIS F CE1 1 
ATOM   11164 N NE2 . HIS F  2 111 ? 14.924  52.767 21.934  1.00 13.06  ? 111  HIS F NE2 1 
ATOM   11165 N N   . ASP F  2 112 ? 19.807  53.893 17.505  1.00 11.01  ? 112  ASP F N   1 
ATOM   11166 C CA  . ASP F  2 112 ? 20.559  54.417 16.373  1.00 11.55  ? 112  ASP F CA  1 
ATOM   11167 C C   . ASP F  2 112 ? 21.188  53.269 15.573  1.00 11.87  ? 112  ASP F C   1 
ATOM   11168 O O   . ASP F  2 112 ? 21.164  53.265 14.347  1.00 12.49  ? 112  ASP F O   1 
ATOM   11169 C CB  . ASP F  2 112 ? 21.635  55.375 16.883  1.00 11.96  ? 112  ASP F CB  1 
ATOM   11170 C CG  . ASP F  2 112 ? 22.222  56.234 15.792  1.00 13.17  ? 112  ASP F CG  1 
ATOM   11171 O OD1 . ASP F  2 112 ? 21.695  56.231 14.658  1.00 13.47  ? 112  ASP F OD1 1 
ATOM   11172 O OD2 . ASP F  2 112 ? 23.219  56.922 16.079  1.00 14.12  ? 112  ASP F OD2 1 
ATOM   11173 N N   . SER F  2 113 ? 21.731  52.293 16.291  1.00 11.77  ? 113  SER F N   1 
ATOM   11174 C CA  . SER F  2 113 ? 22.309  51.094 15.698  1.00 12.68  ? 113  SER F CA  1 
ATOM   11175 C C   . SER F  2 113 ? 21.278  50.264 14.916  1.00 13.09  ? 113  SER F C   1 
ATOM   11176 O O   . SER F  2 113 ? 21.569  49.775 13.820  1.00 14.16  ? 113  SER F O   1 
ATOM   11177 C CB  . SER F  2 113 ? 22.936  50.234 16.799  1.00 12.90  ? 113  SER F CB  1 
ATOM   11178 O OG  . SER F  2 113 ? 23.249  48.942 16.334  1.00 14.30  ? 113  SER F OG  1 
ATOM   11179 N N   . ASN F  2 114 ? 20.090  50.095 15.492  1.00 12.65  ? 114  ASN F N   1 
ATOM   11180 C CA  . ASN F  2 114 ? 19.031  49.316 14.856  1.00 13.54  ? 114  ASN F CA  1 
ATOM   11181 C C   . ASN F  2 114 ? 18.570  49.919 13.531  1.00 13.82  ? 114  ASN F C   1 
ATOM   11182 O O   . ASN F  2 114 ? 18.318  49.192 12.575  1.00 14.95  ? 114  ASN F O   1 
ATOM   11183 C CB  . ASN F  2 114 ? 17.829  49.179 15.788  1.00 13.50  ? 114  ASN F CB  1 
ATOM   11184 C CG  . ASN F  2 114 ? 18.118  48.318 16.997  1.00 13.74  ? 114  ASN F CG  1 
ATOM   11185 O OD1 . ASN F  2 114 ? 18.929  47.397 16.943  1.00 14.59  ? 114  ASN F OD1 1 
ATOM   11186 N ND2 . ASN F  2 114 ? 17.444  48.610 18.098  1.00 13.38  ? 114  ASN F ND2 1 
ATOM   11187 N N   . VAL F  2 115 ? 18.476  51.245 13.487  1.00 13.14  ? 115  VAL F N   1 
ATOM   11188 C CA  . VAL F  2 115 ? 18.110  51.966 12.269  1.00 13.66  ? 115  VAL F CA  1 
ATOM   11189 C C   . VAL F  2 115 ? 19.190  51.782 11.198  1.00 14.33  ? 115  VAL F C   1 
ATOM   11190 O O   . VAL F  2 115 ? 18.892  51.543 10.027  1.00 15.20  ? 115  VAL F O   1 
ATOM   11191 C CB  . VAL F  2 115 ? 17.928  53.476 12.544  1.00 13.37  ? 115  VAL F CB  1 
ATOM   11192 C CG1 . VAL F  2 115 ? 17.739  54.250 11.243  1.00 14.26  ? 115  VAL F CG1 1 
ATOM   11193 C CG2 . VAL F  2 115 ? 16.750  53.725 13.473  1.00 13.36  ? 115  VAL F CG2 1 
ATOM   11194 N N   . LYS F  2 116 ? 20.444  51.903 11.622  1.00 14.27  ? 116  LYS F N   1 
ATOM   11195 C CA  . LYS F  2 116 ? 21.603  51.742 10.742  1.00 15.46  ? 116  LYS F CA  1 
ATOM   11196 C C   . LYS F  2 116 ? 21.655  50.344 10.132  1.00 16.67  ? 116  LYS F C   1 
ATOM   11197 O O   . LYS F  2 116 ? 21.883  50.180 8.935   1.00 17.89  ? 116  LYS F O   1 
ATOM   11198 C CB  . LYS F  2 116 ? 22.882  51.975 11.539  1.00 15.64  ? 116  LYS F CB  1 
ATOM   11199 C CG  . LYS F  2 116 ? 23.898  52.854 10.854  1.00 16.91  ? 116  LYS F CG  1 
ATOM   11200 C CD  . LYS F  2 116 ? 24.550  52.164 9.680   1.00 18.74  ? 116  LYS F CD  1 
ATOM   11201 C CE  . LYS F  2 116 ? 25.312  53.161 8.825   1.00 20.32  ? 116  LYS F CE  1 
ATOM   11202 N NZ  . LYS F  2 116 ? 26.600  53.516 9.474   1.00 21.56  ? 116  LYS F NZ  1 
ATOM   11203 N N   . ASN F  2 117 ? 21.452  49.337 10.973  1.00 16.71  ? 117  ASN F N   1 
ATOM   11204 C CA  . ASN F  2 117 ? 21.516  47.955 10.538  1.00 18.49  ? 117  ASN F CA  1 
ATOM   11205 C C   . ASN F  2 117 ? 20.380  47.617 9.580   1.00 19.22  ? 117  ASN F C   1 
ATOM   11206 O O   . ASN F  2 117 ? 20.563  46.858 8.622   1.00 21.09  ? 117  ASN F O   1 
ATOM   11207 C CB  . ASN F  2 117 ? 21.502  47.024 11.746  1.00 18.72  ? 117  ASN F CB  1 
ATOM   11208 C CG  . ASN F  2 117 ? 22.766  47.132 12.580  1.00 18.72  ? 117  ASN F CG  1 
ATOM   11209 O OD1 . ASN F  2 117 ? 23.789  47.637 12.120  1.00 19.29  ? 117  ASN F OD1 1 
ATOM   11210 N ND2 . ASN F  2 117 ? 22.700  46.652 13.815  1.00 18.47  ? 117  ASN F ND2 1 
ATOM   11211 N N   . LEU F  2 118 ? 19.214  48.199 9.833   1.00 18.16  ? 118  LEU F N   1 
ATOM   11212 C CA  . LEU F  2 118 ? 18.073  48.048 8.941   1.00 19.07  ? 118  LEU F CA  1 
ATOM   11213 C C   . LEU F  2 118 ? 18.338  48.748 7.609   1.00 19.43  ? 118  LEU F C   1 
ATOM   11214 O O   . LEU F  2 118 ? 17.983  48.236 6.546   1.00 20.93  ? 118  LEU F O   1 
ATOM   11215 C CB  . LEU F  2 118 ? 16.811  48.618 9.598   1.00 18.29  ? 118  LEU F CB  1 
ATOM   11216 C CG  . LEU F  2 118 ? 15.514  48.544 8.797   1.00 19.56  ? 118  LEU F CG  1 
ATOM   11217 C CD1 . LEU F  2 118 ? 15.239  47.120 8.344   1.00 21.74  ? 118  LEU F CD1 1 
ATOM   11218 C CD2 . LEU F  2 118 ? 14.364  49.083 9.629   1.00 19.34  ? 118  LEU F CD2 1 
ATOM   11219 N N   . TYR F  2 119 ? 18.966  49.916 7.668   1.00 18.44  ? 119  TYR F N   1 
ATOM   11220 C CA  . TYR F  2 119 ? 19.308  50.648 6.460   1.00 19.10  ? 119  TYR F CA  1 
ATOM   11221 C C   . TYR F  2 119 ? 20.296  49.863 5.606   1.00 20.80  ? 119  TYR F C   1 
ATOM   11222 O O   . TYR F  2 119 ? 20.120  49.751 4.396   1.00 22.05  ? 119  TYR F O   1 
ATOM   11223 C CB  . TYR F  2 119 ? 19.894  52.015 6.803   1.00 18.32  ? 119  TYR F CB  1 
ATOM   11224 C CG  . TYR F  2 119 ? 20.364  52.781 5.593   1.00 19.45  ? 119  TYR F CG  1 
ATOM   11225 C CD1 . TYR F  2 119 ? 19.457  53.461 4.785   1.00 19.88  ? 119  TYR F CD1 1 
ATOM   11226 C CD2 . TYR F  2 119 ? 21.709  52.824 5.247   1.00 20.56  ? 119  TYR F CD2 1 
ATOM   11227 C CE1 . TYR F  2 119 ? 19.877  54.169 3.670   1.00 21.20  ? 119  TYR F CE1 1 
ATOM   11228 C CE2 . TYR F  2 119 ? 22.137  53.527 4.131   1.00 22.02  ? 119  TYR F CE2 1 
ATOM   11229 C CZ  . TYR F  2 119 ? 21.214  54.197 3.347   1.00 22.25  ? 119  TYR F CZ  1 
ATOM   11230 O OH  . TYR F  2 119 ? 21.614  54.898 2.241   1.00 23.93  ? 119  TYR F OH  1 
ATOM   11231 N N   . ASP F  2 120 ? 21.336  49.332 6.238   1.00 21.21  ? 120  ASP F N   1 
ATOM   11232 C CA  . ASP F  2 120 ? 22.352  48.569 5.526   1.00 23.47  ? 120  ASP F CA  1 
ATOM   11233 C C   . ASP F  2 120 ? 21.772  47.271 4.954   1.00 25.22  ? 120  ASP F C   1 
ATOM   11234 O O   . ASP F  2 120 ? 22.128  46.862 3.855   1.00 27.30  ? 120  ASP F O   1 
ATOM   11235 C CB  . ASP F  2 120 ? 23.537  48.261 6.448   1.00 23.94  ? 120  ASP F CB  1 
ATOM   11236 C CG  . ASP F  2 120 ? 24.343  49.504 6.818   1.00 23.24  ? 120  ASP F CG  1 
ATOM   11237 O OD1 . ASP F  2 120 ? 24.465  50.434 5.992   1.00 23.57  ? 120  ASP F OD1 1 
ATOM   11238 O OD2 . ASP F  2 120 ? 24.873  49.542 7.948   1.00 22.71  ? 120  ASP F OD2 1 
ATOM   11239 N N   . LYS F  2 121 ? 20.873  46.641 5.703   1.00 24.81  ? 121  LYS F N   1 
ATOM   11240 C CA  . LYS F  2 121 ? 20.193  45.420 5.265   1.00 26.94  ? 121  LYS F CA  1 
ATOM   11241 C C   . LYS F  2 121 ? 19.536  45.631 3.907   1.00 27.84  ? 121  LYS F C   1 
ATOM   11242 O O   . LYS F  2 121 ? 19.664  44.806 3.012   1.00 30.40  ? 121  LYS F O   1 
ATOM   11243 C CB  . LYS F  2 121 ? 19.137  45.023 6.299   1.00 26.31  ? 121  LYS F CB  1 
ATOM   11244 C CG  . LYS F  2 121 ? 18.453  43.686 6.074   1.00 29.05  ? 121  LYS F CG  1 
ATOM   11245 C CD  . LYS F  2 121 ? 17.412  43.451 7.166   1.00 28.63  ? 121  LYS F CD  1 
ATOM   11246 C CE  . LYS F  2 121 ? 17.048  41.980 7.335   1.00 31.94  ? 121  LYS F CE  1 
ATOM   11247 N NZ  . LYS F  2 121 ? 16.009  41.525 6.366   1.00 34.30  ? 121  LYS F NZ  1 
ATOM   11248 N N   . VAL F  2 122 ? 18.842  46.752 3.769   1.00 26.11  ? 122  VAL F N   1 
ATOM   11249 C CA  . VAL F  2 122 ? 18.223  47.136 2.514   1.00 26.89  ? 122  VAL F CA  1 
ATOM   11250 C C   . VAL F  2 122 ? 19.285  47.469 1.466   1.00 27.97  ? 122  VAL F C   1 
ATOM   11251 O O   . VAL F  2 122 ? 19.233  46.973 0.340   1.00 30.02  ? 122  VAL F O   1 
ATOM   11252 C CB  . VAL F  2 122 ? 17.264  48.325 2.727   1.00 25.15  ? 122  VAL F CB  1 
ATOM   11253 C CG1 . VAL F  2 122 ? 16.813  48.928 1.401   1.00 25.99  ? 122  VAL F CG1 1 
ATOM   11254 C CG2 . VAL F  2 122 ? 16.067  47.866 3.543   1.00 25.11  ? 122  VAL F CG2 1 
ATOM   11255 N N   . ARG F  2 123 ? 20.250  48.298 1.842   1.00 27.04  ? 123  ARG F N   1 
ATOM   11256 C CA  . ARG F  2 123 ? 21.319  48.693 0.931   1.00 28.50  ? 123  ARG F CA  1 
ATOM   11257 C C   . ARG F  2 123 ? 21.993  47.474 0.304   1.00 31.43  ? 123  ARG F C   1 
ATOM   11258 O O   . ARG F  2 123 ? 22.246  47.450 -0.905  1.00 33.36  ? 123  ARG F O   1 
ATOM   11259 C CB  . ARG F  2 123 ? 22.359  49.526 1.677   1.00 27.64  ? 123  ARG F CB  1 
ATOM   11260 C CG  . ARG F  2 123 ? 23.387  50.186 0.776   1.00 29.34  ? 123  ARG F CG  1 
ATOM   11261 C CD  . ARG F  2 123 ? 24.415  50.961 1.584   1.00 29.09  ? 123  ARG F CD  1 
ATOM   11262 N NE  . ARG F  2 123 ? 24.987  50.159 2.668   1.00 29.03  ? 123  ARG F NE  1 
ATOM   11263 C CZ  . ARG F  2 123 ? 25.891  49.189 2.512   1.00 31.43  ? 123  ARG F CZ  1 
ATOM   11264 N NH1 . ARG F  2 123 ? 26.358  48.857 1.309   1.00 34.15  ? 123  ARG F NH1 1 
ATOM   11265 N NH2 . ARG F  2 123 ? 26.328  48.533 3.577   1.00 31.45  ? 123  ARG F NH2 1 
ATOM   11266 N N   . LEU F  2 124 ? 22.270  46.468 1.131   1.00 32.19  ? 124  LEU F N   1 
ATOM   11267 C CA  . LEU F  2 124 ? 22.961  45.251 0.690   1.00 35.62  ? 124  LEU F CA  1 
ATOM   11268 C C   . LEU F  2 124 ? 22.121  44.384 -0.261  1.00 37.83  ? 124  LEU F C   1 
ATOM   11269 O O   . LEU F  2 124 ? 22.675  43.641 -1.070  1.00 41.08  ? 124  LEU F O   1 
ATOM   11270 C CB  . LEU F  2 124 ? 23.412  44.423 1.903   1.00 36.07  ? 124  LEU F CB  1 
ATOM   11271 C CG  . LEU F  2 124 ? 24.513  45.056 2.769   1.00 35.12  ? 124  LEU F CG  1 
ATOM   11272 C CD1 . LEU F  2 124 ? 24.581  44.411 4.152   1.00 34.70  ? 124  LEU F CD1 1 
ATOM   11273 C CD2 . LEU F  2 124 ? 25.866  44.988 2.076   1.00 38.17  ? 124  LEU F CD2 1 
ATOM   11274 N N   . GLN F  2 125 ? 20.797  44.471 -0.150  1.00 36.59  ? 125  GLN F N   1 
ATOM   11275 C CA  . GLN F  2 125 ? 19.894  43.785 -1.072  1.00 38.81  ? 125  GLN F CA  1 
ATOM   11276 C C   . GLN F  2 125 ? 19.870  44.480 -2.416  1.00 39.32  ? 125  GLN F C   1 
ATOM   11277 O O   . GLN F  2 125 ? 20.032  43.844 -3.455  1.00 42.24  ? 125  GLN F O   1 
ATOM   11278 C CB  . GLN F  2 125 ? 18.467  43.762 -0.532  1.00 37.65  ? 125  GLN F CB  1 
ATOM   11279 C CG  . GLN F  2 125 ? 18.259  42.879 0.677   1.00 38.10  ? 125  GLN F CG  1 
ATOM   11280 C CD  . GLN F  2 125 ? 16.813  42.883 1.124   1.00 37.60  ? 125  GLN F CD  1 
ATOM   11281 O OE1 . GLN F  2 125 ? 15.945  42.354 0.431   1.00 39.92  ? 125  GLN F OE1 1 
ATOM   11282 N NE2 . GLN F  2 125 ? 16.543  43.483 2.279   1.00 35.02  ? 125  GLN F NE2 1 
ATOM   11283 N N   . LEU F  2 126 ? 19.653  45.790 -2.385  1.00 36.86  ? 126  LEU F N   1 
ATOM   11284 C CA  . LEU F  2 126 ? 19.487  46.565 -3.607  1.00 37.37  ? 126  LEU F CA  1 
ATOM   11285 C C   . LEU F  2 126 ? 20.774  46.647 -4.418  1.00 39.47  ? 126  LEU F C   1 
ATOM   11286 O O   . LEU F  2 126 ? 20.729  46.600 -5.639  1.00 41.45  ? 126  LEU F O   1 
ATOM   11287 C CB  . LEU F  2 126 ? 18.957  47.969 -3.295  1.00 34.68  ? 126  LEU F CB  1 
ATOM   11288 C CG  . LEU F  2 126 ? 17.637  48.036 -2.514  1.00 33.13  ? 126  LEU F CG  1 
ATOM   11289 C CD1 . LEU F  2 126 ? 17.047  49.434 -2.569  1.00 31.65  ? 126  LEU F CD1 1 
ATOM   11290 C CD2 . LEU F  2 126 ? 16.638  47.015 -3.035  1.00 35.15  ? 126  LEU F CD2 1 
ATOM   11291 N N   . ARG F  2 127 ? 21.915  46.754 -3.745  1.00 39.52  ? 127  ARG F N   1 
ATOM   11292 C CA  . ARG F  2 127 ? 23.212  46.833 -4.426  1.00 42.12  ? 127  ARG F CA  1 
ATOM   11293 C C   . ARG F  2 127 ? 23.189  47.980 -5.454  1.00 42.35  ? 127  ARG F C   1 
ATOM   11294 O O   . ARG F  2 127 ? 22.786  49.092 -5.108  1.00 40.01  ? 127  ARG F O   1 
ATOM   11295 C CB  . ARG F  2 127 ? 23.596  45.460 -5.019  1.00 45.88  ? 127  ARG F CB  1 
ATOM   11296 C CG  . ARG F  2 127 ? 24.047  44.472 -3.948  1.00 46.65  ? 127  ARG F CG  1 
ATOM   11297 C CD  . ARG F  2 127 ? 23.555  43.038 -4.145  1.00 49.40  ? 127  ARG F CD  1 
ATOM   11298 N NE  . ARG F  2 127 ? 23.934  42.285 -5.357  1.00 53.78  ? 127  ARG F NE  1 
ATOM   11299 C CZ  . ARG F  2 127 ? 25.050  42.403 -6.090  1.00 56.59  ? 127  ARG F CZ  1 
ATOM   11300 N NH1 . ARG F  2 127 ? 26.016  43.274 -5.806  1.00 55.78  ? 127  ARG F NH1 1 
ATOM   11301 N NH2 . ARG F  2 127 ? 25.208  41.609 -7.147  1.00 60.80  ? 127  ARG F NH2 1 
ATOM   11302 N N   . ASP F  2 128 ? 23.587  47.730 -6.700  1.00 45.45  ? 128  ASP F N   1 
ATOM   11303 C CA  . ASP F  2 128 ? 23.637  48.791 -7.707  1.00 46.13  ? 128  ASP F CA  1 
ATOM   11304 C C   . ASP F  2 128 ? 22.344  48.906 -8.531  1.00 45.73  ? 128  ASP F C   1 
ATOM   11305 O O   . ASP F  2 128 ? 22.337  49.547 -9.583  1.00 46.99  ? 128  ASP F O   1 
ATOM   11306 C CB  . ASP F  2 128 ? 24.853  48.600 -8.631  1.00 50.02  ? 128  ASP F CB  1 
ATOM   11307 C CG  . ASP F  2 128 ? 24.771  47.331 -9.468  1.00 53.13  ? 128  ASP F CG  1 
ATOM   11308 O OD1 . ASP F  2 128 ? 23.843  46.524 -9.253  1.00 52.49  ? 128  ASP F OD1 1 
ATOM   11309 O OD2 . ASP F  2 128 ? 25.644  47.138 -10.345 1.00 56.78  ? 128  ASP F OD2 1 
ATOM   11310 N N   . ASN F  2 129 ? 21.260  48.286 -8.061  1.00 44.43  ? 129  ASN F N   1 
ATOM   11311 C CA  . ASN F  2 129 ? 19.949  48.404 -8.714  1.00 44.27  ? 129  ASN F CA  1 
ATOM   11312 C C   . ASN F  2 129 ? 19.141  49.639 -8.277  1.00 41.60  ? 129  ASN F C   1 
ATOM   11313 O O   . ASN F  2 129 ? 18.014  49.832 -8.745  1.00 41.64  ? 129  ASN F O   1 
ATOM   11314 C CB  . ASN F  2 129 ? 19.111  47.132 -8.487  1.00 45.10  ? 129  ASN F CB  1 
ATOM   11315 C CG  . ASN F  2 129 ? 19.506  45.984 -9.408  1.00 48.89  ? 129  ASN F CG  1 
ATOM   11316 O OD1 . ASN F  2 129 ? 20.558  46.007 -10.057 1.00 50.95  ? 129  ASN F OD1 1 
ATOM   11317 N ND2 . ASN F  2 129 ? 18.648  44.968 -9.473  1.00 50.37  ? 129  ASN F ND2 1 
ATOM   11318 N N   . ALA F  2 130 ? 19.712  50.467 -7.395  1.00 39.72  ? 130  ALA F N   1 
ATOM   11319 C CA  . ALA F  2 130 ? 19.076  51.714 -6.959  1.00 37.79  ? 130  ALA F CA  1 
ATOM   11320 C C   . ALA F  2 130 ? 20.114  52.771 -6.598  1.00 37.46  ? 130  ALA F C   1 
ATOM   11321 O O   . ALA F  2 130 ? 21.236  52.436 -6.239  1.00 37.95  ? 130  ALA F O   1 
ATOM   11322 C CB  . ALA F  2 130 ? 18.172  51.450 -5.768  1.00 35.70  ? 130  ALA F CB  1 
ATOM   11323 N N   . LYS F  2 131 ? 19.732  54.043 -6.698  1.00 37.17  ? 131  LYS F N   1 
ATOM   11324 C CA  . LYS F  2 131 ? 20.595  55.163 -6.311  1.00 37.35  ? 131  LYS F CA  1 
ATOM   11325 C C   . LYS F  2 131 ? 20.516  55.402 -4.807  1.00 35.03  ? 131  LYS F C   1 
ATOM   11326 O O   . LYS F  2 131 ? 19.429  55.605 -4.273  1.00 33.59  ? 131  LYS F O   1 
ATOM   11327 C CB  . LYS F  2 131 ? 20.160  56.448 -7.016  1.00 38.67  ? 131  LYS F CB  1 
ATOM   11328 C CG  . LYS F  2 131 ? 20.208  56.414 -8.536  1.00 41.20  ? 131  LYS F CG  1 
ATOM   11329 C CD  . LYS F  2 131 ? 19.388  57.564 -9.123  1.00 42.36  ? 131  LYS F CD  1 
ATOM   11330 C CE  . LYS F  2 131 ? 19.847  57.981 -10.517 1.00 45.41  ? 131  LYS F CE  1 
ATOM   11331 N NZ  . LYS F  2 131 ? 21.204  58.615 -10.504 1.00 47.23  ? 131  LYS F NZ  1 
ATOM   11332 N N   . GLU F  2 132 ? 21.660  55.391 -4.128  1.00 34.97  ? 132  GLU F N   1 
ATOM   11333 C CA  . GLU F  2 132 ? 21.714  55.754 -2.716  1.00 33.11  ? 132  GLU F CA  1 
ATOM   11334 C C   . GLU F  2 132 ? 21.707  57.282 -2.592  1.00 33.79  ? 132  GLU F C   1 
ATOM   11335 O O   . GLU F  2 132 ? 22.714  57.937 -2.848  1.00 35.73  ? 132  GLU F O   1 
ATOM   11336 C CB  . GLU F  2 132 ? 22.959  55.159 -2.059  1.00 33.29  ? 132  GLU F CB  1 
ATOM   11337 C CG  . GLU F  2 132 ? 23.030  55.381 -0.556  1.00 31.37  ? 132  GLU F CG  1 
ATOM   11338 C CD  . GLU F  2 132 ? 24.099  54.543 0.126   1.00 31.55  ? 132  GLU F CD  1 
ATOM   11339 O OE1 . GLU F  2 132 ? 25.076  54.133 -0.536  1.00 33.83  ? 132  GLU F OE1 1 
ATOM   11340 O OE2 . GLU F  2 132 ? 23.956  54.288 1.337   1.00 29.74  ? 132  GLU F OE2 1 
ATOM   11341 N N   . LEU F  2 133 ? 20.566  57.838 -2.193  1.00 32.75  ? 133  LEU F N   1 
ATOM   11342 C CA  . LEU F  2 133 ? 20.361  59.295 -2.201  1.00 34.09  ? 133  LEU F CA  1 
ATOM   11343 C C   . LEU F  2 133 ? 21.141  60.069 -1.131  1.00 34.29  ? 133  LEU F C   1 
ATOM   11344 O O   . LEU F  2 133 ? 21.425  61.255 -1.315  1.00 36.47  ? 133  LEU F O   1 
ATOM   11345 C CB  . LEU F  2 133 ? 18.862  59.619 -2.093  1.00 33.55  ? 133  LEU F CB  1 
ATOM   11346 C CG  . LEU F  2 133 ? 18.082  59.804 -3.402  1.00 35.19  ? 133  LEU F CG  1 
ATOM   11347 C CD1 . LEU F  2 133 ? 18.605  58.942 -4.542  1.00 35.86  ? 133  LEU F CD1 1 
ATOM   11348 C CD2 . LEU F  2 133 ? 16.602  59.539 -3.174  1.00 34.44  ? 133  LEU F CD2 1 
ATOM   11349 N N   . GLY F  2 134 ? 21.482  59.406 -0.027  1.00 32.40  ? 134  GLY F N   1 
ATOM   11350 C CA  . GLY F  2 134 ? 22.225  60.039 1.066   1.00 32.61  ? 134  GLY F CA  1 
ATOM   11351 C C   . GLY F  2 134 ? 21.365  60.470 2.246   1.00 31.24  ? 134  GLY F C   1 
ATOM   11352 O O   . GLY F  2 134 ? 21.884  60.998 3.237   1.00 31.38  ? 134  GLY F O   1 
ATOM   11353 N N   . ASN F  2 135 ? 20.058  60.219 2.158   1.00 30.28  ? 135  ASN F N   1 
ATOM   11354 C CA  . ASN F  2 135 ? 19.098  60.679 3.168   1.00 29.61  ? 135  ASN F CA  1 
ATOM   11355 C C   . ASN F  2 135 ? 18.291  59.552 3.819   1.00 27.06  ? 135  ASN F C   1 
ATOM   11356 O O   . ASN F  2 135 ? 17.312  59.809 4.524   1.00 26.82  ? 135  ASN F O   1 
ATOM   11357 C CB  . ASN F  2 135 ? 18.140  61.691 2.536   1.00 31.98  ? 135  ASN F CB  1 
ATOM   11358 C CG  . ASN F  2 135 ? 17.368  61.113 1.367   1.00 32.36  ? 135  ASN F CG  1 
ATOM   11359 O OD1 . ASN F  2 135 ? 17.460  59.923 1.065   1.00 30.96  ? 135  ASN F OD1 1 
ATOM   11360 N ND2 . ASN F  2 135 ? 16.616  61.959 0.690   1.00 34.89  ? 135  ASN F ND2 1 
ATOM   11361 N N   . GLY F  2 136 ? 18.695  58.311 3.574   1.00 25.65  ? 136  GLY F N   1 
ATOM   11362 C CA  . GLY F  2 136 ? 17.937  57.149 4.032   1.00 23.93  ? 136  GLY F CA  1 
ATOM   11363 C C   . GLY F  2 136 ? 17.081  56.521 2.944   1.00 24.41  ? 136  GLY F C   1 
ATOM   11364 O O   . GLY F  2 136 ? 16.507  55.450 3.146   1.00 23.72  ? 136  GLY F O   1 
ATOM   11365 N N   . CYS F  2 137 ? 17.001  57.179 1.791   1.00 25.89  ? 137  CYS F N   1 
ATOM   11366 C CA  . CYS F  2 137 ? 16.174  56.699 0.693   1.00 26.78  ? 137  CYS F CA  1 
ATOM   11367 C C   . CYS F  2 137 ? 17.002  56.076 -0.419  1.00 27.53  ? 137  CYS F C   1 
ATOM   11368 O O   . CYS F  2 137 ? 18.160  56.443 -0.632  1.00 28.06  ? 137  CYS F O   1 
ATOM   11369 C CB  . CYS F  2 137 ? 15.316  57.829 0.123   1.00 28.45  ? 137  CYS F CB  1 
ATOM   11370 S SG  . CYS F  2 137 ? 14.213  58.590 1.331   1.00 28.50  ? 137  CYS F SG  1 
ATOM   11371 N N   . PHE F  2 138 ? 16.378  55.129 -1.116  1.00 28.01  ? 138  PHE F N   1 
ATOM   11372 C CA  . PHE F  2 138 ? 16.944  54.506 -2.295  1.00 29.24  ? 138  PHE F CA  1 
ATOM   11373 C C   . PHE F  2 138 ? 15.991  54.717 -3.450  1.00 30.89  ? 138  PHE F C   1 
ATOM   11374 O O   . PHE F  2 138 ? 14.830  54.345 -3.360  1.00 31.06  ? 138  PHE F O   1 
ATOM   11375 C CB  . PHE F  2 138 ? 17.128  53.011 -2.069  1.00 28.92  ? 138  PHE F CB  1 
ATOM   11376 C CG  . PHE F  2 138 ? 18.120  52.685 -0.997  1.00 27.72  ? 138  PHE F CG  1 
ATOM   11377 C CD1 . PHE F  2 138 ? 19.475  52.606 -1.292  1.00 28.50  ? 138  PHE F CD1 1 
ATOM   11378 C CD2 . PHE F  2 138 ? 17.702  52.463 0.309   1.00 26.13  ? 138  PHE F CD2 1 
ATOM   11379 C CE1 . PHE F  2 138 ? 20.393  52.308 -0.304  1.00 27.79  ? 138  PHE F CE1 1 
ATOM   11380 C CE2 . PHE F  2 138 ? 18.618  52.164 1.300   1.00 25.18  ? 138  PHE F CE2 1 
ATOM   11381 C CZ  . PHE F  2 138 ? 19.964  52.090 0.993   1.00 26.02  ? 138  PHE F CZ  1 
ATOM   11382 N N   . GLU F  2 139 ? 16.488  55.307 -4.533  1.00 32.48  ? 139  GLU F N   1 
ATOM   11383 C CA  . GLU F  2 139 ? 15.686  55.576 -5.714  1.00 34.32  ? 139  GLU F CA  1 
ATOM   11384 C C   . GLU F  2 139 ? 15.982  54.522 -6.778  1.00 35.63  ? 139  GLU F C   1 
ATOM   11385 O O   . GLU F  2 139 ? 17.120  54.377 -7.214  1.00 36.27  ? 139  GLU F O   1 
ATOM   11386 C CB  . GLU F  2 139 ? 16.003  56.972 -6.233  1.00 35.71  ? 139  GLU F CB  1 
ATOM   11387 C CG  . GLU F  2 139 ? 15.207  57.394 -7.453  1.00 37.88  ? 139  GLU F CG  1 
ATOM   11388 C CD  . GLU F  2 139 ? 15.685  58.723 -7.992  1.00 39.78  ? 139  GLU F CD  1 
ATOM   11389 O OE1 . GLU F  2 139 ? 15.665  59.714 -7.229  1.00 39.80  ? 139  GLU F OE1 1 
ATOM   11390 O OE2 . GLU F  2 139 ? 16.112  58.769 -9.168  1.00 41.62  ? 139  GLU F OE2 1 
ATOM   11391 N N   . PHE F  2 140 ? 14.945  53.802 -7.202  1.00 36.53  ? 140  PHE F N   1 
ATOM   11392 C CA  . PHE F  2 140 ? 15.104  52.649 -8.097  1.00 38.10  ? 140  PHE F CA  1 
ATOM   11393 C C   . PHE F  2 140 ? 15.331  53.050 -9.553  1.00 40.34  ? 140  PHE F C   1 
ATOM   11394 O O   . PHE F  2 140 ? 14.781  54.044 -10.024 1.00 41.06  ? 140  PHE F O   1 
ATOM   11395 C CB  . PHE F  2 140 ? 13.877  51.735 -8.010  1.00 38.69  ? 140  PHE F CB  1 
ATOM   11396 C CG  . PHE F  2 140 ? 13.693  51.098 -6.666  1.00 37.16  ? 140  PHE F CG  1 
ATOM   11397 C CD1 . PHE F  2 140 ? 12.952  51.730 -5.677  1.00 35.93  ? 140  PHE F CD1 1 
ATOM   11398 C CD2 . PHE F  2 140 ? 14.261  49.863 -6.388  1.00 37.39  ? 140  PHE F CD2 1 
ATOM   11399 C CE1 . PHE F  2 140 ? 12.780  51.143 -4.436  1.00 34.74  ? 140  PHE F CE1 1 
ATOM   11400 C CE2 . PHE F  2 140 ? 14.093  49.269 -5.148  1.00 36.29  ? 140  PHE F CE2 1 
ATOM   11401 C CZ  . PHE F  2 140 ? 13.353  49.911 -4.170  1.00 34.87  ? 140  PHE F CZ  1 
ATOM   11402 N N   . TYR F  2 141 ? 16.143  52.269 -10.260 1.00 41.88  ? 141  TYR F N   1 
ATOM   11403 C CA  . TYR F  2 141 ? 16.317  52.454 -11.704 1.00 44.46  ? 141  TYR F CA  1 
ATOM   11404 C C   . TYR F  2 141 ? 15.118  51.887 -12.450 1.00 46.10  ? 141  TYR F C   1 
ATOM   11405 O O   . TYR F  2 141 ? 14.678  52.447 -13.454 1.00 47.73  ? 141  TYR F O   1 
ATOM   11406 C CB  . TYR F  2 141 ? 17.606  51.792 -12.197 1.00 45.97  ? 141  TYR F CB  1 
ATOM   11407 C CG  . TYR F  2 141 ? 18.846  52.435 -11.630 1.00 45.36  ? 141  TYR F CG  1 
ATOM   11408 C CD1 . TYR F  2 141 ? 19.160  53.760 -11.922 1.00 45.84  ? 141  TYR F CD1 1 
ATOM   11409 C CD2 . TYR F  2 141 ? 19.694  51.734 -10.783 1.00 44.76  ? 141  TYR F CD2 1 
ATOM   11410 C CE1 . TYR F  2 141 ? 20.289  54.360 -11.396 1.00 45.80  ? 141  TYR F CE1 1 
ATOM   11411 C CE2 . TYR F  2 141 ? 20.826  52.326 -10.251 1.00 44.57  ? 141  TYR F CE2 1 
ATOM   11412 C CZ  . TYR F  2 141 ? 21.119  53.638 -10.563 1.00 45.13  ? 141  TYR F CZ  1 
ATOM   11413 O OH  . TYR F  2 141 ? 22.244  54.230 -10.035 1.00 45.52  ? 141  TYR F OH  1 
ATOM   11414 N N   . HIS F  2 142 ? 14.598  50.772 -11.946 1.00 46.14  ? 142  HIS F N   1 
ATOM   11415 C CA  . HIS F  2 142 ? 13.386  50.159 -12.480 1.00 48.03  ? 142  HIS F CA  1 
ATOM   11416 C C   . HIS F  2 142 ? 12.160  50.681 -11.744 1.00 47.20  ? 142  HIS F C   1 
ATOM   11417 O O   . HIS F  2 142 ? 12.249  51.137 -10.601 1.00 45.01  ? 142  HIS F O   1 
ATOM   11418 C CB  . HIS F  2 142 ? 13.450  48.629 -12.365 1.00 49.38  ? 142  HIS F CB  1 
ATOM   11419 C CG  . HIS F  2 142 ? 13.710  48.133 -10.976 1.00 47.59  ? 142  HIS F CG  1 
ATOM   11420 N ND1 . HIS F  2 142 ? 12.705  47.704 -10.136 1.00 47.34  ? 142  HIS F ND1 1 
ATOM   11421 C CD2 . HIS F  2 142 ? 14.865  48.004 -10.279 1.00 46.30  ? 142  HIS F CD2 1 
ATOM   11422 C CE1 . HIS F  2 142 ? 13.232  47.328 -8.984  1.00 45.76  ? 142  HIS F CE1 1 
ATOM   11423 N NE2 . HIS F  2 142 ? 14.540  47.501 -9.044  1.00 45.04  ? 142  HIS F NE2 1 
ATOM   11424 N N   . LYS F  2 143 ? 11.014  50.616 -12.412 1.00 49.37  ? 143  LYS F N   1 
ATOM   11425 C CA  . LYS F  2 143 ? 9.741   50.939 -11.782 1.00 49.55  ? 143  LYS F CA  1 
ATOM   11426 C C   . LYS F  2 143 ? 9.459   49.864 -10.736 1.00 49.22  ? 143  LYS F C   1 
ATOM   11427 O O   . LYS F  2 143 ? 9.536   48.672 -11.034 1.00 50.83  ? 143  LYS F O   1 
ATOM   11428 C CB  . LYS F  2 143 ? 8.632   50.977 -12.830 1.00 52.57  ? 143  LYS F CB  1 
ATOM   11429 C CG  . LYS F  2 143 ? 7.343   51.629 -12.366 1.00 53.43  ? 143  LYS F CG  1 
ATOM   11430 C CD  . LYS F  2 143 ? 6.292   51.589 -13.471 1.00 56.95  ? 143  LYS F CD  1 
ATOM   11431 C CE  . LYS F  2 143 ? 4.881   51.692 -12.914 1.00 58.83  ? 143  LYS F CE  1 
ATOM   11432 N NZ  . LYS F  2 143 ? 4.420   50.442 -12.240 1.00 59.69  ? 143  LYS F NZ  1 
ATOM   11433 N N   . CYS F  2 144 ? 9.157   50.287 -9.511  1.00 47.56  ? 144  CYS F N   1 
ATOM   11434 C CA  . CYS F  2 144 ? 8.982   49.362 -8.393  1.00 47.15  ? 144  CYS F CA  1 
ATOM   11435 C C   . CYS F  2 144 ? 7.559   49.454 -7.842  1.00 48.53  ? 144  CYS F C   1 
ATOM   11436 O O   . CYS F  2 144 ? 7.228   50.379 -7.097  1.00 47.39  ? 144  CYS F O   1 
ATOM   11437 C CB  . CYS F  2 144 ? 10.015  49.670 -7.302  1.00 44.12  ? 144  CYS F CB  1 
ATOM   11438 S SG  . CYS F  2 144 ? 10.133  48.461 -5.960  1.00 43.59  ? 144  CYS F SG  1 
ATOM   11439 N N   . ASP F  2 145 ? 6.718   48.492 -8.219  1.00 51.52  ? 145  ASP F N   1 
ATOM   11440 C CA  . ASP F  2 145 ? 5.324   48.450 -7.763  1.00 53.75  ? 145  ASP F CA  1 
ATOM   11441 C C   . ASP F  2 145 ? 5.242   47.999 -6.295  1.00 52.73  ? 145  ASP F C   1 
ATOM   11442 O O   . ASP F  2 145 ? 6.271   47.779 -5.653  1.00 50.08  ? 145  ASP F O   1 
ATOM   11443 C CB  . ASP F  2 145 ? 4.472   47.563 -8.690  1.00 57.89  ? 145  ASP F CB  1 
ATOM   11444 C CG  . ASP F  2 145 ? 4.882   46.095 -8.666  1.00 59.15  ? 145  ASP F CG  1 
ATOM   11445 O OD1 . ASP F  2 145 ? 5.765   45.714 -7.875  1.00 56.89  ? 145  ASP F OD1 1 
ATOM   11446 O OD2 . ASP F  2 145 ? 4.311   45.311 -9.453  1.00 62.86  ? 145  ASP F OD2 1 
ATOM   11447 N N   . ASN F  2 146 ? 4.025   47.872 -5.767  1.00 55.17  ? 146  ASN F N   1 
ATOM   11448 C CA  . ASN F  2 146 ? 3.833   47.509 -4.355  1.00 54.64  ? 146  ASN F CA  1 
ATOM   11449 C C   . ASN F  2 146 ? 4.311   46.101 -4.002  1.00 55.26  ? 146  ASN F C   1 
ATOM   11450 O O   . ASN F  2 146 ? 4.681   45.843 -2.859  1.00 53.64  ? 146  ASN F O   1 
ATOM   11451 C CB  . ASN F  2 146 ? 2.368   47.685 -3.947  1.00 57.91  ? 146  ASN F CB  1 
ATOM   11452 C CG  . ASN F  2 146 ? 1.923   49.139 -3.967  1.00 57.53  ? 146  ASN F CG  1 
ATOM   11453 O OD1 . ASN F  2 146 ? 2.737   50.061 -4.044  1.00 54.44  ? 146  ASN F OD1 1 
ATOM   11454 N ND2 . ASN F  2 146 ? 0.618   49.349 -3.895  1.00 61.25  ? 146  ASN F ND2 1 
ATOM   11455 N N   . GLU F  2 147 ? 4.309   45.198 -4.977  1.00 58.02  ? 147  GLU F N   1 
ATOM   11456 C CA  . GLU F  2 147 ? 4.883   43.863 -4.789  1.00 59.23  ? 147  GLU F CA  1 
ATOM   11457 C C   . GLU F  2 147 ? 6.411   43.955 -4.758  1.00 55.78  ? 147  GLU F C   1 
ATOM   11458 O O   . GLU F  2 147 ? 7.067   43.322 -3.928  1.00 55.01  ? 147  GLU F O   1 
ATOM   11459 C CB  . GLU F  2 147 ? 4.444   42.904 -5.901  1.00 63.69  ? 147  GLU F CB  1 
ATOM   11460 C CG  . GLU F  2 147 ? 2.938   42.706 -6.026  1.00 68.12  ? 147  GLU F CG  1 
ATOM   11461 C CD  . GLU F  2 147 ? 2.288   43.687 -6.989  1.00 68.79  ? 147  GLU F CD  1 
ATOM   11462 O OE1 . GLU F  2 147 ? 2.187   44.887 -6.644  1.00 66.24  ? 147  GLU F OE1 1 
ATOM   11463 O OE2 . GLU F  2 147 ? 1.889   43.263 -8.097  1.00 72.17  ? 147  GLU F OE2 1 
ATOM   11464 N N   . CYS F  2 148 ? 6.966   44.748 -5.673  1.00 54.26  ? 148  CYS F N   1 
ATOM   11465 C CA  . CYS F  2 148 ? 8.401   45.025 -5.707  1.00 51.35  ? 148  CYS F CA  1 
ATOM   11466 C C   . CYS F  2 148 ? 8.867   45.657 -4.389  1.00 48.05  ? 148  CYS F C   1 
ATOM   11467 O O   . CYS F  2 148 ? 9.911   45.284 -3.852  1.00 46.64  ? 148  CYS F O   1 
ATOM   11468 C CB  . CYS F  2 148 ? 8.732   45.936 -6.896  1.00 50.65  ? 148  CYS F CB  1 
ATOM   11469 S SG  . CYS F  2 148 ? 10.386  46.666 -6.888  1.00 47.22  ? 148  CYS F SG  1 
ATOM   11470 N N   . MET F  2 149 ? 8.084   46.597 -3.866  1.00 47.35  ? 149  MET F N   1 
ATOM   11471 C CA  . MET F  2 149 ? 8.383   47.210 -2.573  1.00 44.67  ? 149  MET F CA  1 
ATOM   11472 C C   . MET F  2 149 ? 8.298   46.180 -1.449  1.00 45.58  ? 149  MET F C   1 
ATOM   11473 O O   . MET F  2 149 ? 9.099   46.205 -0.517  1.00 43.28  ? 149  MET F O   1 
ATOM   11474 C CB  . MET F  2 149 ? 7.416   48.357 -2.280  1.00 44.51  ? 149  MET F CB  1 
ATOM   11475 C CG  . MET F  2 149 ? 7.494   49.530 -3.243  1.00 44.04  ? 149  MET F CG  1 
ATOM   11476 S SD  . MET F  2 149 ? 9.070   50.388 -3.206  1.00 40.49  ? 149  MET F SD  1 
ATOM   11477 C CE  . MET F  2 149 ? 8.681   51.847 -4.171  1.00 41.28  ? 149  MET F CE  1 
ATOM   11478 N N   . GLU F  2 150 ? 7.323   45.281 -1.539  1.00 49.52  ? 150  GLU F N   1 
ATOM   11479 C CA  . GLU F  2 150 ? 7.132   44.247 -0.524  1.00 51.37  ? 150  GLU F CA  1 
ATOM   11480 C C   . GLU F  2 150 ? 8.309   43.270 -0.463  1.00 51.58  ? 150  GLU F C   1 
ATOM   11481 O O   . GLU F  2 150 ? 8.634   42.770 0.612   1.00 51.22  ? 150  GLU F O   1 
ATOM   11482 C CB  . GLU F  2 150 ? 5.815   43.490 -0.769  1.00 56.09  ? 150  GLU F CB  1 
ATOM   11483 C CG  . GLU F  2 150 ? 5.476   42.404 0.252   1.00 58.50  ? 150  GLU F CG  1 
ATOM   11484 C CD  . GLU F  2 150 ? 5.374   42.924 1.677   1.00 56.45  ? 150  GLU F CD  1 
ATOM   11485 O OE1 . GLU F  2 150 ? 4.922   44.071 1.867   1.00 55.08  ? 150  GLU F OE1 1 
ATOM   11486 O OE2 . GLU F  2 150 ? 5.749   42.187 2.613   1.00 56.65  ? 150  GLU F OE2 1 
ATOM   11487 N N   . SER F  2 151 ? 8.940   43.002 -1.605  1.00 52.79  ? 151  SER F N   1 
ATOM   11488 C CA  . SER F  2 151 ? 10.094  42.098 -1.656  1.00 53.71  ? 151  SER F CA  1 
ATOM   11489 C C   . SER F  2 151 ? 11.317  42.689 -0.942  1.00 50.47  ? 151  SER F C   1 
ATOM   11490 O O   . SER F  2 151 ? 12.113  41.959 -0.345  1.00 50.83  ? 151  SER F O   1 
ATOM   11491 C CB  . SER F  2 151 ? 10.451  41.754 -3.102  1.00 55.77  ? 151  SER F CB  1 
ATOM   11492 O OG  . SER F  2 151 ? 10.913  42.892 -3.802  1.00 53.27  ? 151  SER F OG  1 
ATOM   11493 N N   . VAL F  2 152 ? 11.459  44.012 -1.010  1.00 47.99  ? 152  VAL F N   1 
ATOM   11494 C CA  . VAL F  2 152 ? 12.528  44.716 -0.307  1.00 45.04  ? 152  VAL F CA  1 
ATOM   11495 C C   . VAL F  2 152 ? 12.272  44.625 1.196   1.00 44.58  ? 152  VAL F C   1 
ATOM   11496 O O   . VAL F  2 152 ? 13.191  44.383 1.980   1.00 43.40  ? 152  VAL F O   1 
ATOM   11497 C CB  . VAL F  2 152 ? 12.619  46.196 -0.736  1.00 42.64  ? 152  VAL F CB  1 
ATOM   11498 C CG1 . VAL F  2 152 ? 13.739  46.906 0.013   1.00 39.81  ? 152  VAL F CG1 1 
ATOM   11499 C CG2 . VAL F  2 152 ? 12.837  46.308 -2.240  1.00 43.94  ? 152  VAL F CG2 1 
ATOM   11500 N N   . ARG F  2 153 ? 11.016  44.822 1.587   1.00 46.16  ? 153  ARG F N   1 
ATOM   11501 C CA  . ARG F  2 153 ? 10.604  44.649 2.979   1.00 46.60  ? 153  ARG F CA  1 
ATOM   11502 C C   . ARG F  2 153 ? 10.696  43.183 3.424   1.00 50.40  ? 153  ARG F C   1 
ATOM   11503 O O   . ARG F  2 153 ? 11.101  42.898 4.550   1.00 49.47  ? 153  ARG F O   1 
ATOM   11504 C CB  . ARG F  2 153 ? 9.182   45.185 3.185   1.00 47.30  ? 153  ARG F CB  1 
ATOM   11505 C CG  . ARG F  2 153 ? 9.126   46.694 3.335   1.00 44.48  ? 153  ARG F CG  1 
ATOM   11506 C CD  . ARG F  2 153 ? 7.728   47.206 3.651   1.00 46.00  ? 153  ARG F CD  1 
ATOM   11507 N NE  . ARG F  2 153 ? 7.169   47.961 2.529   1.00 47.02  ? 153  ARG F NE  1 
ATOM   11508 C CZ  . ARG F  2 153 ? 6.230   47.530 1.689   1.00 50.21  ? 153  ARG F CZ  1 
ATOM   11509 N NH1 . ARG F  2 153 ? 5.682   46.325 1.820   1.00 53.02  ? 153  ARG F NH1 1 
ATOM   11510 N NH2 . ARG F  2 153 ? 5.823   48.326 0.706   1.00 51.02  ? 153  ARG F NH2 1 
ATOM   11511 N N   . ASN F  2 154 ? 10.305  42.272 2.531   1.00 55.80  ? 154  ASN F N   1 
ATOM   11512 C CA  . ASN F  2 154 ? 10.442  40.822 2.737   1.00 60.64  ? 154  ASN F CA  1 
ATOM   11513 C C   . ASN F  2 154 ? 11.846  40.375 3.129   1.00 58.78  ? 154  ASN F C   1 
ATOM   11514 O O   . ASN F  2 154 ? 12.008  39.479 3.958   1.00 60.47  ? 154  ASN F O   1 
ATOM   11515 C CB  . ASN F  2 154 ? 10.105  40.072 1.440   1.00 66.83  ? 154  ASN F CB  1 
ATOM   11516 C CG  . ASN F  2 154 ? 8.659   39.626 1.353   1.00 74.09  ? 154  ASN F CG  1 
ATOM   11517 O OD1 . ASN F  2 154 ? 7.893   39.742 2.309   1.00 74.87  ? 154  ASN F OD1 1 
ATOM   11518 N ND2 . ASN F  2 154 ? 8.283   39.096 0.182   1.00 82.25  ? 154  ASN F ND2 1 
ATOM   11519 N N   . GLY F  2 155 ? 12.850  40.998 2.513   1.00 55.52  ? 155  GLY F N   1 
ATOM   11520 C CA  . GLY F  2 155 ? 14.206  40.457 2.469   1.00 54.99  ? 155  GLY F CA  1 
ATOM   11521 C C   . GLY F  2 155 ? 14.382  39.599 1.224   1.00 57.92  ? 155  GLY F C   1 
ATOM   11522 O O   . GLY F  2 155 ? 15.383  38.903 1.085   1.00 59.74  ? 155  GLY F O   1 
ATOM   11523 N N   . THR F  2 156 ? 13.413  39.679 0.311   1.00 58.67  ? 156  THR F N   1 
ATOM   11524 C CA  . THR F  2 156 ? 13.304  38.772 -0.835  1.00 62.33  ? 156  THR F CA  1 
ATOM   11525 C C   . THR F  2 156 ? 13.572  39.474 -2.173  1.00 61.11  ? 156  THR F C   1 
ATOM   11526 O O   . THR F  2 156 ? 13.414  38.872 -3.234  1.00 64.43  ? 156  THR F O   1 
ATOM   11527 C CB  . THR F  2 156 ? 11.891  38.142 -0.853  1.00 65.70  ? 156  THR F CB  1 
ATOM   11528 O OG1 . THR F  2 156 ? 11.698  37.383 0.347   1.00 67.14  ? 156  THR F OG1 1 
ATOM   11529 C CG2 . THR F  2 156 ? 11.669  37.221 -2.056  1.00 70.54  ? 156  THR F CG2 1 
ATOM   11530 N N   . TYR F  2 157 ? 13.991  40.738 -2.130  1.00 56.62  ? 157  TYR F N   1 
ATOM   11531 C CA  . TYR F  2 157 ? 14.209  41.513 -3.357  1.00 55.61  ? 157  TYR F CA  1 
ATOM   11532 C C   . TYR F  2 157 ? 15.115  40.769 -4.339  1.00 58.56  ? 157  TYR F C   1 
ATOM   11533 O O   . TYR F  2 157 ? 16.284  40.514 -4.045  1.00 58.59  ? 157  TYR F O   1 
ATOM   11534 C CB  . TYR F  2 157 ? 14.811  42.885 -3.038  1.00 51.24  ? 157  TYR F CB  1 
ATOM   11535 C CG  . TYR F  2 157 ? 15.098  43.711 -4.274  1.00 50.66  ? 157  TYR F CG  1 
ATOM   11536 C CD1 . TYR F  2 157 ? 14.075  44.374 -4.946  1.00 50.49  ? 157  TYR F CD1 1 
ATOM   11537 C CD2 . TYR F  2 157 ? 16.389  43.817 -4.779  1.00 50.76  ? 157  TYR F CD2 1 
ATOM   11538 C CE1 . TYR F  2 157 ? 14.331  45.126 -6.080  1.00 50.36  ? 157  TYR F CE1 1 
ATOM   11539 C CE2 . TYR F  2 157 ? 16.654  44.566 -5.913  1.00 50.78  ? 157  TYR F CE2 1 
ATOM   11540 C CZ  . TYR F  2 157 ? 15.623  45.218 -6.558  1.00 50.45  ? 157  TYR F CZ  1 
ATOM   11541 O OH  . TYR F  2 157 ? 15.888  45.961 -7.683  1.00 50.71  ? 157  TYR F OH  1 
ATOM   11542 N N   . ASP F  2 158 ? 14.572  40.430 -5.504  1.00 61.38  ? 158  ASP F N   1 
ATOM   11543 C CA  . ASP F  2 158 ? 15.311  39.640 -6.484  1.00 65.01  ? 158  ASP F CA  1 
ATOM   11544 C C   . ASP F  2 158 ? 16.186  40.536 -7.360  1.00 63.67  ? 158  ASP F C   1 
ATOM   11545 O O   . ASP F  2 158 ? 15.745  41.039 -8.400  1.00 64.04  ? 158  ASP F O   1 
ATOM   11546 C CB  . ASP F  2 158 ? 14.359  38.802 -7.345  1.00 69.25  ? 158  ASP F CB  1 
ATOM   11547 C CG  . ASP F  2 158 ? 15.055  37.621 -8.001  1.00 74.10  ? 158  ASP F CG  1 
ATOM   11548 O OD1 . ASP F  2 158 ? 15.729  36.851 -7.282  1.00 75.61  ? 158  ASP F OD1 1 
ATOM   11549 O OD2 . ASP F  2 158 ? 14.922  37.456 -9.231  1.00 76.79  ? 158  ASP F OD2 1 
ATOM   11550 N N   . TYR F  2 159 ? 17.430  40.725 -6.923  1.00 62.49  ? 159  TYR F N   1 
ATOM   11551 C CA  . TYR F  2 159 ? 18.414  41.517 -7.661  1.00 61.71  ? 159  TYR F CA  1 
ATOM   11552 C C   . TYR F  2 159 ? 18.596  41.029 -9.110  1.00 65.64  ? 159  TYR F C   1 
ATOM   11553 O O   . TYR F  2 159 ? 18.533  41.840 -10.035 1.00 65.11  ? 159  TYR F O   1 
ATOM   11554 C CB  . TYR F  2 159 ? 19.753  41.549 -6.901  1.00 61.02  ? 159  TYR F CB  1 
ATOM   11555 C CG  . TYR F  2 159 ? 20.891  42.183 -7.666  1.00 61.47  ? 159  TYR F CG  1 
ATOM   11556 C CD1 . TYR F  2 159 ? 21.131  43.551 -7.582  1.00 58.19  ? 159  TYR F CD1 1 
ATOM   11557 C CD2 . TYR F  2 159 ? 21.731  41.413 -8.472  1.00 65.71  ? 159  TYR F CD2 1 
ATOM   11558 C CE1 . TYR F  2 159 ? 22.170  44.138 -8.278  1.00 59.20  ? 159  TYR F CE1 1 
ATOM   11559 C CE2 . TYR F  2 159 ? 22.772  41.992 -9.178  1.00 66.71  ? 159  TYR F CE2 1 
ATOM   11560 C CZ  . TYR F  2 159 ? 22.988  43.355 -9.075  1.00 63.52  ? 159  TYR F CZ  1 
ATOM   11561 O OH  . TYR F  2 159 ? 24.026  43.927 -9.773  1.00 65.18  ? 159  TYR F OH  1 
ATOM   11562 N N   . PRO F  2 160 ? 18.802  39.708 -9.315  1.00 70.02  ? 160  PRO F N   1 
ATOM   11563 C CA  . PRO F  2 160 ? 18.983  39.188 -10.684 1.00 74.27  ? 160  PRO F CA  1 
ATOM   11564 C C   . PRO F  2 160 ? 17.840  39.476 -11.675 1.00 74.73  ? 160  PRO F C   1 
ATOM   11565 O O   . PRO F  2 160 ? 18.088  39.534 -12.883 1.00 77.01  ? 160  PRO F O   1 
ATOM   11566 C CB  . PRO F  2 160 ? 19.128  37.676 -10.469 1.00 78.93  ? 160  PRO F CB  1 
ATOM   11567 C CG  . PRO F  2 160 ? 19.655  37.543 -9.083  1.00 77.20  ? 160  PRO F CG  1 
ATOM   11568 C CD  . PRO F  2 160 ? 18.990  38.644 -8.307  1.00 71.68  ? 160  PRO F CD  1 
ATOM   11569 N N   . GLN F  2 161 ? 16.611  39.639 -11.181 1.00 73.12  ? 161  GLN F N   1 
ATOM   11570 C CA  . GLN F  2 161 ? 15.465  39.947 -12.050 1.00 73.83  ? 161  GLN F CA  1 
ATOM   11571 C C   . GLN F  2 161 ? 15.533  41.377 -12.589 1.00 70.82  ? 161  GLN F C   1 
ATOM   11572 O O   . GLN F  2 161 ? 15.294  41.612 -13.775 1.00 72.35  ? 161  GLN F O   1 
ATOM   11573 C CB  . GLN F  2 161 ? 14.139  39.744 -11.303 1.00 73.36  ? 161  GLN F CB  1 
ATOM   11574 C CG  . GLN F  2 161 ? 12.889  40.085 -12.115 1.00 74.25  ? 161  GLN F CG  1 
ATOM   11575 C CD  . GLN F  2 161 ? 11.620  40.105 -11.277 1.00 73.63  ? 161  GLN F CD  1 
ATOM   11576 O OE1 . GLN F  2 161 ? 11.661  39.955 -10.053 1.00 72.07  ? 161  GLN F OE1 1 
ATOM   11577 N NE2 . GLN F  2 161 ? 10.483  40.301 -11.937 1.00 75.15  ? 161  GLN F NE2 1 
ATOM   11578 N N   . TYR F  2 162 ? 15.850  42.323 -11.708 1.00 66.94  ? 162  TYR F N   1 
ATOM   11579 C CA  . TYR F  2 162 ? 15.873  43.741 -12.067 1.00 64.38  ? 162  TYR F CA  1 
ATOM   11580 C C   . TYR F  2 162 ? 17.259  44.236 -12.504 1.00 64.68  ? 162  TYR F C   1 
ATOM   11581 O O   . TYR F  2 162 ? 17.453  45.433 -12.724 1.00 62.92  ? 162  TYR F O   1 
ATOM   11582 C CB  . TYR F  2 162 ? 15.365  44.581 -10.892 1.00 60.44  ? 162  TYR F CB  1 
ATOM   11583 C CG  . TYR F  2 162 ? 13.973  44.202 -10.422 1.00 60.68  ? 162  TYR F CG  1 
ATOM   11584 C CD1 . TYR F  2 162 ? 12.839  44.609 -11.127 1.00 61.49  ? 162  TYR F CD1 1 
ATOM   11585 C CD2 . TYR F  2 162 ? 13.790  43.435 -9.270  1.00 60.50  ? 162  TYR F CD2 1 
ATOM   11586 C CE1 . TYR F  2 162 ? 11.565  44.263 -10.698 1.00 62.40  ? 162  TYR F CE1 1 
ATOM   11587 C CE2 . TYR F  2 162 ? 12.521  43.084 -8.832  1.00 61.31  ? 162  TYR F CE2 1 
ATOM   11588 C CZ  . TYR F  2 162 ? 11.411  43.500 -9.546  1.00 62.37  ? 162  TYR F CZ  1 
ATOM   11589 O OH  . TYR F  2 162 ? 10.151  43.153 -9.110  1.00 63.71  ? 162  TYR F OH  1 
ATOM   11590 N N   . SER F  2 163 ? 18.219  43.323 -12.635 1.00 67.67  ? 163  SER F N   1 
ATOM   11591 C CA  . SER F  2 163 ? 19.558  43.686 -13.092 1.00 68.79  ? 163  SER F CA  1 
ATOM   11592 C C   . SER F  2 163 ? 19.574  43.759 -14.616 1.00 71.55  ? 163  SER F C   1 
ATOM   11593 O O   . SER F  2 163 ? 20.630  43.858 -15.234 1.00 73.62  ? 163  SER F O   1 
ATOM   11594 C CB  . SER F  2 163 ? 20.574  42.666 -12.590 1.00 71.25  ? 163  SER F CB  1 
ATOM   11595 O OG  . SER F  2 163 ? 21.910  43.119 -12.747 1.00 72.20  ? 163  SER F OG  1 
HETATM 11596 C C1  . NAG G  3 .   ? 18.521  31.245 31.938  1.00 30.03  ? 1322 NAG A C1  1 
HETATM 11597 C C2  . NAG G  3 .   ? 17.005  31.383 32.113  1.00 35.02  ? 1322 NAG A C2  1 
HETATM 11598 C C3  . NAG G  3 .   ? 16.522  30.836 33.462  1.00 36.25  ? 1322 NAG A C3  1 
HETATM 11599 C C4  . NAG G  3 .   ? 17.134  29.466 33.749  1.00 36.23  ? 1322 NAG A C4  1 
HETATM 11600 C C5  . NAG G  3 .   ? 18.651  29.618 33.679  1.00 35.57  ? 1322 NAG A C5  1 
HETATM 11601 C C6  . NAG G  3 .   ? 19.416  28.359 34.095  1.00 36.44  ? 1322 NAG A C6  1 
HETATM 11602 C C7  . NAG G  3 .   ? 15.929  33.327 31.038  1.00 37.71  ? 1322 NAG A C7  1 
HETATM 11603 C C8  . NAG G  3 .   ? 15.644  34.802 31.139  1.00 37.39  ? 1322 NAG A C8  1 
HETATM 11604 N N2  . NAG G  3 .   ? 16.633  32.791 32.038  1.00 36.81  ? 1322 NAG A N2  1 
HETATM 11605 O O3  . NAG G  3 .   ? 15.108  30.790 33.494  1.00 37.04  ? 1322 NAG A O3  1 
HETATM 11606 O O4  . NAG G  3 .   ? 16.714  28.999 35.017  1.00 37.95  ? 1322 NAG A O4  1 
HETATM 11607 O O5  . NAG G  3 .   ? 18.981  29.963 32.345  1.00 32.54  ? 1322 NAG A O5  1 
HETATM 11608 O O6  . NAG G  3 .   ? 19.432  27.426 33.033  1.00 37.78  ? 1322 NAG A O6  1 
HETATM 11609 O O7  . NAG G  3 .   ? 15.525  32.681 30.067  1.00 38.85  ? 1322 NAG A O7  1 
HETATM 11610 C C1  . NAG H  3 .   ? 59.955  46.324 89.462  1.00 30.71  ? 1323 NAG A C1  1 
HETATM 11611 C C2  . NAG H  3 .   ? 61.162  46.590 88.546  1.00 34.80  ? 1323 NAG A C2  1 
HETATM 11612 C C3  . NAG H  3 .   ? 61.670  48.027 88.724  1.00 35.17  ? 1323 NAG A C3  1 
HETATM 11613 C C4  . NAG H  3 .   ? 60.490  48.988 88.543  1.00 35.34  ? 1323 NAG A C4  1 
HETATM 11614 C C5  . NAG H  3 .   ? 59.409  48.615 89.561  1.00 34.70  ? 1323 NAG A C5  1 
HETATM 11615 C C6  . NAG H  3 .   ? 58.198  49.548 89.594  1.00 35.16  ? 1323 NAG A C6  1 
HETATM 11616 C C7  . NAG H  3 .   ? 62.589  44.869 89.713  1.00 40.72  ? 1323 NAG A C7  1 
HETATM 11617 C C8  . NAG H  3 .   ? 63.728  43.892 89.552  1.00 41.47  ? 1323 NAG A C8  1 
HETATM 11618 N N2  . NAG H  3 .   ? 62.239  45.590 88.628  1.00 37.42  ? 1323 NAG A N2  1 
HETATM 11619 O O3  . NAG H  3 .   ? 62.690  48.344 87.797  1.00 35.96  ? 1323 NAG A O3  1 
HETATM 11620 O O4  . NAG H  3 .   ? 60.894  50.342 88.646  1.00 36.57  ? 1323 NAG A O4  1 
HETATM 11621 O O5  . NAG H  3 .   ? 58.970  47.315 89.228  1.00 32.32  ? 1323 NAG A O5  1 
HETATM 11622 O O6  . NAG H  3 .   ? 57.440  49.255 90.751  1.00 36.01  ? 1323 NAG A O6  1 
HETATM 11623 O O7  . NAG H  3 .   ? 62.053  44.954 90.820  1.00 42.87  ? 1323 NAG A O7  1 
HETATM 11624 C C1  . SIA I  4 .   ? 29.649  23.599 96.436  1.00 51.40  ? 1324 SIA A C1  1 
HETATM 11625 C C2  . SIA I  4 .   ? 29.320  23.727 97.908  1.00 51.00  ? 1324 SIA A C2  1 
HETATM 11626 C C3  . SIA I  4 .   ? 30.306  22.879 98.715  1.00 49.61  ? 1324 SIA A C3  1 
HETATM 11627 C C4  . SIA I  4 .   ? 31.710  23.469 98.646  1.00 48.19  ? 1324 SIA A C4  1 
HETATM 11628 C C5  . SIA I  4 .   ? 31.673  24.925 99.102  1.00 46.92  ? 1324 SIA A C5  1 
HETATM 11629 C C6  . SIA I  4 .   ? 30.664  25.724 98.272  1.00 45.76  ? 1324 SIA A C6  1 
HETATM 11630 C C7  . SIA I  4 .   ? 30.528  27.203 98.655  1.00 43.83  ? 1324 SIA A C7  1 
HETATM 11631 C C8  . SIA I  4 .   ? 29.329  27.880 97.976  1.00 43.10  ? 1324 SIA A C8  1 
HETATM 11632 C C9  . SIA I  4 .   ? 29.471  29.403 98.025  1.00 42.43  ? 1324 SIA A C9  1 
HETATM 11633 C C10 . SIA I  4 .   ? 33.543  26.436 99.538  1.00 46.57  ? 1324 SIA A C10 1 
HETATM 11634 C C11 . SIA I  4 .   ? 34.920  26.879 99.132  1.00 45.49  ? 1324 SIA A C11 1 
HETATM 11635 N N5  . SIA I  4 .   ? 33.003  25.455 98.817  1.00 46.55  ? 1324 SIA A N5  1 
HETATM 11636 O O1A . SIA I  4 .   ? 29.798  24.631 95.742  1.00 52.06  ? 1324 SIA A O1A 1 
HETATM 11637 O O1B . SIA I  4 .   ? 29.751  22.446 95.952  1.00 53.24  ? 1324 SIA A O1B 1 
HETATM 11638 O O4  . SIA I  4 .   ? 32.602  22.701 99.459  1.00 48.13  ? 1324 SIA A O4  1 
HETATM 11639 O O6  . SIA I  4 .   ? 29.375  25.095 98.349  1.00 47.45  ? 1324 SIA A O6  1 
HETATM 11640 O O7  . SIA I  4 .   ? 30.419  27.355 100.071 1.00 42.24  ? 1324 SIA A O7  1 
HETATM 11641 O O8  . SIA I  4 .   ? 29.225  27.461 96.605  1.00 42.82  ? 1324 SIA A O8  1 
HETATM 11642 O O9  . SIA I  4 .   ? 28.355  30.047 97.398  1.00 41.59  ? 1324 SIA A O9  1 
HETATM 11643 O O10 . SIA I  4 .   ? 32.949  26.952 100.471 1.00 45.65  ? 1324 SIA A O10 1 
HETATM 11644 C C1  . GLA J  5 .   ? 25.060  22.587 100.251 1.00 66.79  ? 1325 GLA A C1  1 
HETATM 11645 C C2  . GLA J  5 .   ? 26.279  22.287 99.376  1.00 64.10  ? 1325 GLA A C2  1 
HETATM 11646 C C3  . GLA J  5 .   ? 27.235  23.470 99.199  1.00 60.88  ? 1325 GLA A C3  1 
HETATM 11647 C C4  . GLA J  5 .   ? 26.497  24.788 99.004  1.00 61.06  ? 1325 GLA A C4  1 
HETATM 11648 C C5  . GLA J  5 .   ? 25.400  24.975 100.042 1.00 61.84  ? 1325 GLA A C5  1 
HETATM 11649 C C6  . GLA J  5 .   ? 24.690  26.310 99.810  1.00 60.42  ? 1325 GLA A C6  1 
HETATM 11650 O O2  . GLA J  5 .   ? 26.983  21.161 99.922  1.00 63.87  ? 1325 GLA A O2  1 
HETATM 11651 O O3  . GLA J  5 .   ? 28.000  23.186 98.027  1.00 56.12  ? 1325 GLA A O3  1 
HETATM 11652 O O4  . GLA J  5 .   ? 25.935  24.806 97.685  1.00 59.53  ? 1325 GLA A O4  1 
HETATM 11653 O O5  . GLA J  5 .   ? 24.490  23.873 99.947  1.00 65.19  ? 1325 GLA A O5  1 
HETATM 11654 O O6  . GLA J  5 .   ? 23.968  26.718 100.976 1.00 57.14  ? 1325 GLA A O6  1 
HETATM 11655 C C1  . NAG K  3 .   ? 22.996  19.487 103.458 1.00 80.58  ? 1326 NAG A C1  1 
HETATM 11656 C C2  . NAG K  3 .   ? 22.280  20.803 103.145 1.00 79.47  ? 1326 NAG A C2  1 
HETATM 11657 C C3  . NAG K  3 .   ? 23.045  21.536 102.035 1.00 78.15  ? 1326 NAG A C3  1 
HETATM 11658 C C4  . NAG K  3 .   ? 24.493  21.768 102.526 1.00 77.55  ? 1326 NAG A C4  1 
HETATM 11659 C C5  . NAG K  3 .   ? 25.127  20.403 102.845 1.00 79.09  ? 1326 NAG A C5  1 
HETATM 11660 C C6  . NAG K  3 .   ? 26.587  20.466 103.315 1.00 78.99  ? 1326 NAG A C6  1 
HETATM 11661 C C7  . NAG K  3 .   ? 19.810  20.977 103.068 1.00 77.01  ? 1326 NAG A C7  1 
HETATM 11662 C C8  . NAG K  3 .   ? 18.563  20.436 102.433 1.00 76.14  ? 1326 NAG A C8  1 
HETATM 11663 N N2  . NAG K  3 .   ? 20.954  20.418 102.658 1.00 79.00  ? 1326 NAG A N2  1 
HETATM 11664 O O1  . NAG K  3 .   ? 22.308  18.778 104.497 1.00 80.00  ? 1326 NAG A O1  1 
HETATM 11665 O O3  . NAG K  3 .   ? 22.397  22.763 101.642 1.00 77.38  ? 1326 NAG A O3  1 
HETATM 11666 O O4  . NAG K  3 .   ? 25.372  22.512 101.647 1.00 72.80  ? 1326 NAG A O4  1 
HETATM 11667 O O5  . NAG K  3 .   ? 24.347  19.751 103.857 1.00 81.23  ? 1326 NAG A O5  1 
HETATM 11668 O O6  . NAG K  3 .   ? 26.967  21.773 103.751 1.00 78.19  ? 1326 NAG A O6  1 
HETATM 11669 O O7  . NAG K  3 .   ? 19.764  21.881 103.887 1.00 75.90  ? 1326 NAG A O7  1 
HETATM 11670 C C1  . FUC L  6 .   ? 21.239  22.655 100.785 1.00 75.57  ? 1327 FUC A C1  1 
HETATM 11671 C C2  . FUC L  6 .   ? 21.030  23.935 99.957  1.00 74.64  ? 1327 FUC A C2  1 
HETATM 11672 C C3  . FUC L  6 .   ? 20.812  23.772 98.440  1.00 72.91  ? 1327 FUC A C3  1 
HETATM 11673 C C4  . FUC L  6 .   ? 21.092  22.392 97.836  1.00 74.77  ? 1327 FUC A C4  1 
HETATM 11674 C C5  . FUC L  6 .   ? 21.988  21.586 98.754  1.00 75.65  ? 1327 FUC A C5  1 
HETATM 11675 C C6  . FUC L  6 .   ? 22.352  20.209 98.199  1.00 74.73  ? 1327 FUC A C6  1 
HETATM 11676 O O2  . FUC L  6 .   ? 22.126  24.835 100.169 1.00 74.61  ? 1327 FUC A O2  1 
HETATM 11677 O O3  . FUC L  6 .   ? 19.449  24.123 98.180  1.00 69.22  ? 1327 FUC A O3  1 
HETATM 11678 O O4  . FUC L  6 .   ? 19.872  21.672 97.612  1.00 75.41  ? 1327 FUC A O4  1 
HETATM 11679 O O5  . FUC L  6 .   ? 21.298  21.457 99.995  1.00 75.89  ? 1327 FUC A O5  1 
HETATM 11680 C C1  . NAG M  3 .   ? 51.502  38.560 -0.086  1.00 40.84  ? 1164 NAG B C1  1 
HETATM 11681 C C2  . NAG M  3 .   ? 52.974  38.890 0.134   1.00 45.93  ? 1164 NAG B C2  1 
HETATM 11682 C C3  . NAG M  3 .   ? 53.694  39.079 -1.200  1.00 47.56  ? 1164 NAG B C3  1 
HETATM 11683 C C4  . NAG M  3 .   ? 53.379  37.930 -2.155  1.00 48.61  ? 1164 NAG B C4  1 
HETATM 11684 C C5  . NAG M  3 .   ? 51.862  37.780 -2.302  1.00 48.13  ? 1164 NAG B C5  1 
HETATM 11685 C C6  . NAG M  3 .   ? 51.490  36.625 -3.231  1.00 49.16  ? 1164 NAG B C6  1 
HETATM 11686 C C7  . NAG M  3 .   ? 53.026  40.109 2.262   1.00 47.85  ? 1164 NAG B C7  1 
HETATM 11687 C C8  . NAG M  3 .   ? 53.093  41.444 2.956   1.00 47.51  ? 1164 NAG B C8  1 
HETATM 11688 N N2  . NAG M  3 .   ? 53.042  40.111 0.926   1.00 46.72  ? 1164 NAG B N2  1 
HETATM 11689 O O3  . NAG M  3 .   ? 55.088  39.159 -0.994  1.00 48.10  ? 1164 NAG B O3  1 
HETATM 11690 O O4  . NAG M  3 .   ? 53.997  38.163 -3.408  1.00 49.99  ? 1164 NAG B O4  1 
HETATM 11691 O O5  . NAG M  3 .   ? 51.285  37.531 -1.033  1.00 44.85  ? 1164 NAG B O5  1 
HETATM 11692 O O6  . NAG M  3 .   ? 50.099  36.641 -3.475  1.00 49.57  ? 1164 NAG B O6  1 
HETATM 11693 O O7  . NAG M  3 .   ? 52.961  39.076 2.931   1.00 48.88  ? 1164 NAG B O7  1 
HETATM 11694 N N1  . EPE N  7 .   ? 28.651  31.536 3.468   1.00 51.89  ? 1165 EPE B N1  1 
HETATM 11695 C C2  . EPE N  7 .   ? 28.337  31.515 2.048   1.00 52.75  ? 1165 EPE B C2  1 
HETATM 11696 C C3  . EPE N  7 .   ? 27.097  32.386 1.930   1.00 51.98  ? 1165 EPE B C3  1 
HETATM 11697 N N4  . EPE N  7 .   ? 26.088  31.787 2.789   1.00 51.58  ? 1165 EPE B N4  1 
HETATM 11698 C C5  . EPE N  7 .   ? 26.347  31.638 4.219   1.00 51.75  ? 1165 EPE B C5  1 
HETATM 11699 C C6  . EPE N  7 .   ? 27.698  30.938 4.400   1.00 52.14  ? 1165 EPE B C6  1 
HETATM 11700 C C7  . EPE N  7 .   ? 24.825  31.363 2.199   1.00 51.20  ? 1165 EPE B C7  1 
HETATM 11701 C C8  . EPE N  7 .   ? 24.072  32.644 1.837   1.00 50.71  ? 1165 EPE B C8  1 
HETATM 11702 O O8  . EPE N  7 .   ? 24.187  32.898 0.430   1.00 50.25  ? 1165 EPE B O8  1 
HETATM 11703 C C9  . EPE N  7 .   ? 29.890  32.149 3.933   1.00 52.50  ? 1165 EPE B C9  1 
HETATM 11704 C C10 . EPE N  7 .   ? 31.077  31.334 3.409   1.00 54.88  ? 1165 EPE B C10 1 
HETATM 11705 S S   . EPE N  7 .   ? 31.026  29.739 3.896   1.00 60.10  ? 1165 EPE B S   1 
HETATM 11706 O O1S . EPE N  7 .   ? 30.313  29.601 5.192   1.00 63.00  ? 1165 EPE B O1S 1 
HETATM 11707 O O2S . EPE N  7 .   ? 32.407  29.220 4.060   1.00 58.87  ? 1165 EPE B O2S 1 
HETATM 11708 O O3S . EPE N  7 .   ? 30.316  28.932 2.872   1.00 61.95  ? 1165 EPE B O3S 1 
HETATM 11709 C C1  . NAG O  3 .   ? 52.104  52.215 31.980  1.00 27.38  ? 1322 NAG C C1  1 
HETATM 11710 C C2  . NAG O  3 .   ? 52.793  50.867 32.245  1.00 31.76  ? 1322 NAG C C2  1 
HETATM 11711 C C3  . NAG O  3 .   ? 53.446  50.815 33.632  1.00 32.11  ? 1322 NAG C C3  1 
HETATM 11712 C C4  . NAG O  3 .   ? 54.319  52.047 33.851  1.00 31.94  ? 1322 NAG C C4  1 
HETATM 11713 C C5  . NAG O  3 .   ? 53.416  53.268 33.690  1.00 31.45  ? 1322 NAG C C5  1 
HETATM 11714 C C6  . NAG O  3 .   ? 54.081  54.594 34.075  1.00 31.91  ? 1322 NAG C C6  1 
HETATM 11715 C C7  . NAG O  3 .   ? 51.732  49.016 31.020  1.00 34.53  ? 1322 NAG C C7  1 
HETATM 11716 C C8  . NAG O  3 .   ? 50.697  47.921 31.045  1.00 34.28  ? 1322 NAG C C8  1 
HETATM 11717 N N2  . NAG O  3 .   ? 51.842  49.767 32.121  1.00 33.32  ? 1322 NAG C N2  1 
HETATM 11718 O O3  . NAG O  3 .   ? 54.197  49.627 33.777  1.00 32.75  ? 1322 NAG C O3  1 
HETATM 11719 O O4  . NAG O  3 .   ? 54.911  51.997 35.134  1.00 33.61  ? 1322 NAG C O4  1 
HETATM 11720 O O5  . NAG O  3 .   ? 52.961  53.294 32.344  1.00 29.27  ? 1322 NAG C O5  1 
HETATM 11721 O O6  . NAG O  3 .   ? 54.765  55.150 32.974  1.00 33.25  ? 1322 NAG C O6  1 
HETATM 11722 O O7  . NAG O  3 .   ? 52.426  49.188 30.013  1.00 35.55  ? 1322 NAG C O7  1 
HETATM 11723 C C1  . NAG P  3 .   ? 18.292  80.561 89.465  1.00 31.14  ? 1323 NAG C C1  1 
HETATM 11724 C C2  . NAG P  3 .   ? 17.507  81.500 88.528  1.00 35.01  ? 1323 NAG C C2  1 
HETATM 11725 C C3  . NAG P  3 .   ? 15.997  81.286 88.679  1.00 35.78  ? 1323 NAG C C3  1 
HETATM 11726 C C4  . NAG P  3 .   ? 15.700  79.798 88.496  1.00 35.99  ? 1323 NAG C C4  1 
HETATM 11727 C C5  . NAG P  3 .   ? 16.510  79.003 89.519  1.00 35.22  ? 1323 NAG C C5  1 
HETATM 11728 C C6  . NAG P  3 .   ? 16.231  77.498 89.506  1.00 35.67  ? 1323 NAG C C6  1 
HETATM 11729 C C7  . NAG P  3 .   ? 18.032  83.659 89.726  1.00 39.66  ? 1323 NAG C C7  1 
HETATM 11730 C C8  . NAG P  3 .   ? 18.413  85.106 89.531  1.00 39.80  ? 1323 NAG C C8  1 
HETATM 11731 N N2  . NAG P  3 .   ? 17.873  82.923 88.607  1.00 37.20  ? 1323 NAG C N2  1 
HETATM 11732 O O3  . NAG P  3 .   ? 15.260  82.031 87.730  1.00 37.63  ? 1323 NAG C O3  1 
HETATM 11733 O O4  . NAG P  3 .   ? 14.310  79.555 88.591  1.00 37.89  ? 1323 NAG C O4  1 
HETATM 11734 O O5  . NAG P  3 .   ? 17.876  79.222 89.233  1.00 32.88  ? 1323 NAG C O5  1 
HETATM 11735 O O6  . NAG P  3 .   ? 16.869  76.892 90.613  1.00 35.99  ? 1323 NAG C O6  1 
HETATM 11736 O O7  . NAG P  3 .   ? 17.889  83.241 90.878  1.00 41.01  ? 1323 NAG C O7  1 
HETATM 11737 C C1  . SIA Q  4 .   ? 53.116  65.747 96.400  1.00 51.15  ? 1324 SIA C C1  1 
HETATM 11738 C C2  . SIA Q  4 .   ? 53.196  65.307 97.845  1.00 51.21  ? 1324 SIA C C2  1 
HETATM 11739 C C3  . SIA Q  4 .   ? 53.461  66.528 98.728  1.00 49.89  ? 1324 SIA C C3  1 
HETATM 11740 C C4  . SIA Q  4 .   ? 52.259  67.465 98.705  1.00 48.82  ? 1324 SIA C C4  1 
HETATM 11741 C C5  . SIA Q  4 .   ? 51.002  66.700 99.120  1.00 47.53  ? 1324 SIA C C5  1 
HETATM 11742 C C6  . SIA Q  4 .   ? 50.795  65.451 98.251  1.00 46.55  ? 1324 SIA C C6  1 
HETATM 11743 C C7  . SIA Q  4 .   ? 49.599  64.565 98.632  1.00 45.10  ? 1324 SIA C C7  1 
HETATM 11744 C C8  . SIA Q  4 .   ? 49.623  63.202 97.924  1.00 44.63  ? 1324 SIA C C8  1 
HETATM 11745 C C9  . SIA Q  4 .   ? 48.269  62.501 98.025  1.00 44.04  ? 1324 SIA C C9  1 
HETATM 11746 C C10 . SIA Q  4 .   ? 48.762  67.571 99.533  1.00 47.53  ? 1324 SIA C C10 1 
HETATM 11747 C C11 . SIA Q  4 .   ? 47.714  68.580 99.154  1.00 46.86  ? 1324 SIA C C11 1 
HETATM 11748 N N5  . SIA Q  4 .   ? 49.904  67.621 98.852  1.00 46.94  ? 1324 SIA C N5  1 
HETATM 11749 O O1A . SIA Q  4 .   ? 52.194  65.310 95.674  1.00 50.99  ? 1324 SIA C O1A 1 
HETATM 11750 O O1B . SIA Q  4 .   ? 53.995  66.533 95.971  1.00 51.65  ? 1324 SIA C O1B 1 
HETATM 11751 O O4  . SIA Q  4 .   ? 52.495  68.583 99.570  1.00 48.93  ? 1324 SIA C O4  1 
HETATM 11752 O O6  . SIA Q  4 .   ? 51.989  64.655 98.272  1.00 48.13  ? 1324 SIA C O6  1 
HETATM 11753 O O7  . SIA Q  4 .   ? 49.545  64.364 100.047 1.00 43.51  ? 1324 SIA C O7  1 
HETATM 11754 O O8  . SIA Q  4 .   ? 49.957  63.358 96.535  1.00 44.28  ? 1324 SIA C O8  1 
HETATM 11755 O O9  . SIA Q  4 .   ? 48.363  61.160 97.531  1.00 42.56  ? 1324 SIA C O9  1 
HETATM 11756 O O10 . SIA Q  4 .   ? 48.576  66.744 100.409 1.00 46.72  ? 1324 SIA C O10 1 
HETATM 11757 C C1  . GLA R  5 .   ? 56.219  62.096 100.110 1.00 66.34  ? 1325 GLA C C1  1 
HETATM 11758 C C2  . GLA R  5 .   ? 55.920  63.272 99.182  1.00 63.60  ? 1325 GLA C C2  1 
HETATM 11759 C C3  . GLA R  5 .   ? 54.431  63.552 99.021  1.00 60.23  ? 1325 GLA C C3  1 
HETATM 11760 C C4  . GLA R  5 .   ? 53.653  62.266 98.782  1.00 60.54  ? 1325 GLA C C4  1 
HETATM 11761 C C5  . GLA R  5 .   ? 53.968  61.242 99.863  1.00 62.60  ? 1325 GLA C C5  1 
HETATM 11762 C C6  . GLA R  5 .   ? 53.139  59.972 99.653  1.00 62.12  ? 1325 GLA C C6  1 
HETATM 11763 O O2  . GLA R  5 .   ? 56.585  64.442 99.678  1.00 63.74  ? 1325 GLA C O2  1 
HETATM 11764 O O3  . GLA R  5 .   ? 54.310  64.411 97.890  1.00 56.05  ? 1325 GLA C O3  1 
HETATM 11765 O O4  . GLA R  5 .   ? 54.005  61.757 97.492  1.00 57.12  ? 1325 GLA C O4  1 
HETATM 11766 O O5  . GLA R  5 .   ? 55.374  60.967 99.828  1.00 65.20  ? 1325 GLA C O5  1 
HETATM 11767 O O6  . GLA R  5 .   ? 53.289  59.072 100.758 1.00 59.90  ? 1325 GLA C O6  1 
HETATM 11768 C C1  . NAG S  3 .   ? 59.782  61.995 103.444 1.00 78.60  ? 1326 NAG C C1  1 
HETATM 11769 C C2  . NAG S  3 .   ? 59.070  60.692 103.090 1.00 77.17  ? 1326 NAG C C2  1 
HETATM 11770 C C3  . NAG S  3 .   ? 58.079  60.971 101.954 1.00 76.67  ? 1326 NAG C C3  1 
HETATM 11771 C C4  . NAG S  3 .   ? 57.086  62.056 102.433 1.00 76.34  ? 1326 NAG C C4  1 
HETATM 11772 C C5  . NAG S  3 .   ? 57.860  63.304 102.896 1.00 77.71  ? 1326 NAG C C5  1 
HETATM 11773 C C6  . NAG S  3 .   ? 56.982  64.435 103.452 1.00 77.79  ? 1326 NAG C C6  1 
HETATM 11774 C C7  . NAG S  3 .   ? 60.240  58.511 103.006 1.00 72.68  ? 1326 NAG C C7  1 
HETATM 11775 C C8  . NAG S  3 .   ? 61.397  57.767 102.407 1.00 71.92  ? 1326 NAG C C8  1 
HETATM 11776 N N2  . NAG S  3 .   ? 60.126  59.789 102.629 1.00 75.86  ? 1326 NAG C N2  1 
HETATM 11777 O O1  . NAG S  3 .   ? 60.774  61.772 104.456 1.00 79.47  ? 1326 NAG C O1  1 
HETATM 11778 O O3  . NAG S  3 .   ? 57.393  59.777 101.520 1.00 76.42  ? 1326 NAG C O3  1 
HETATM 11779 O O4  . NAG S  3 .   ? 56.079  62.475 101.483 1.00 71.54  ? 1326 NAG C O4  1 
HETATM 11780 O O5  . NAG S  3 .   ? 58.811  62.941 103.903 1.00 79.47  ? 1326 NAG C O5  1 
HETATM 11781 O O6  . NAG S  3 .   ? 55.676  63.989 103.820 1.00 78.20  ? 1326 NAG C O6  1 
HETATM 11782 O O7  . NAG S  3 .   ? 59.457  57.966 103.767 1.00 70.37  ? 1326 NAG C O7  1 
HETATM 11783 C C1  . FUC T  6 .   ? 58.111  58.876 100.648 1.00 75.45  ? 1327 FUC C C1  1 
HETATM 11784 C C2  . FUC T  6 .   ? 57.156  58.075 99.739  1.00 74.73  ? 1327 FUC C C2  1 
HETATM 11785 C C3  . FUC T  6 .   ? 57.649  57.823 98.303  1.00 72.99  ? 1327 FUC C C3  1 
HETATM 11786 C C4  . FUC T  6 .   ? 58.629  58.852 97.723  1.00 74.93  ? 1327 FUC C C4  1 
HETATM 11787 C C5  . FUC T  6 .   ? 58.747  60.058 98.638  1.00 75.65  ? 1327 FUC C C5  1 
HETATM 11788 C C6  . FUC T  6 .   ? 59.757  61.099 98.157  1.00 74.63  ? 1327 FUC C C6  1 
HETATM 11789 O O2  . FUC T  6 .   ? 55.866  58.695 99.671  1.00 74.92  ? 1327 FUC C O2  1 
HETATM 11790 O O3  . FUC T  6 .   ? 58.250  56.521 98.281  1.00 71.28  ? 1327 FUC C O3  1 
HETATM 11791 O O4  . FUC T  6 .   ? 59.927  58.270 97.528  1.00 75.49  ? 1327 FUC C O4  1 
HETATM 11792 O O5  . FUC T  6 .   ? 59.133  59.577 99.923  1.00 75.74  ? 1327 FUC C O5  1 
HETATM 11793 C C1  . NAG U  3 .   ? 29.324  77.109 -0.095  1.00 39.62  ? 1164 NAG D C1  1 
HETATM 11794 C C2  . NAG U  3 .   ? 28.146  78.094 -0.096  1.00 44.77  ? 1164 NAG D C2  1 
HETATM 11795 C C3  . NAG U  3 .   ? 27.733  78.594 -1.481  1.00 46.36  ? 1164 NAG D C3  1 
HETATM 11796 C C4  . NAG U  3 .   ? 28.968  79.004 -2.271  1.00 47.07  ? 1164 NAG D C4  1 
HETATM 11797 C C5  . NAG U  3 .   ? 29.863  77.770 -2.396  1.00 46.37  ? 1164 NAG D C5  1 
HETATM 11798 C C6  . NAG U  3 .   ? 31.104  78.051 -3.245  1.00 47.15  ? 1164 NAG D C6  1 
HETATM 11799 C C7  . NAG U  3 .   ? 26.957  77.481 1.944   1.00 46.26  ? 1164 NAG D C7  1 
HETATM 11800 C C8  . NAG U  3 .   ? 25.739  76.866 2.580   1.00 46.23  ? 1164 NAG D C8  1 
HETATM 11801 N N2  . NAG U  3 .   ? 27.008  77.517 0.609   1.00 45.19  ? 1164 NAG D N2  1 
HETATM 11802 O O3  . NAG U  3 .   ? 26.874  79.705 -1.334  1.00 47.42  ? 1164 NAG D O3  1 
HETATM 11803 O O4  . NAG U  3 .   ? 28.598  79.523 -3.538  1.00 47.88  ? 1164 NAG D O4  1 
HETATM 11804 O O5  . NAG U  3 .   ? 30.293  77.338 -1.115  1.00 42.89  ? 1164 NAG D O5  1 
HETATM 11805 O O6  . NAG U  3 .   ? 31.784  76.839 -3.504  1.00 47.33  ? 1164 NAG D O6  1 
HETATM 11806 O O7  . NAG U  3 .   ? 27.857  77.925 2.659   1.00 46.57  ? 1164 NAG D O7  1 
HETATM 11807 N N1  . EPE V  7 .   ? 46.564  60.608 3.807   1.00 54.75  ? 1165 EPE D N1  1 
HETATM 11808 C C2  . EPE V  7 .   ? 48.034  60.661 3.808   1.00 56.10  ? 1165 EPE D C2  1 
HETATM 11809 C C3  . EPE V  7 .   ? 48.598  59.236 3.835   1.00 55.86  ? 1165 EPE D C3  1 
HETATM 11810 N N4  . EPE V  7 .   ? 47.910  58.492 2.782   1.00 55.02  ? 1165 EPE D N4  1 
HETATM 11811 C C5  . EPE V  7 .   ? 46.457  58.483 2.725   1.00 53.31  ? 1165 EPE D C5  1 
HETATM 11812 C C6  . EPE V  7 .   ? 45.912  59.312 3.880   1.00 54.01  ? 1165 EPE D C6  1 
HETATM 11813 C C7  . EPE V  7 .   ? 48.654  57.757 1.760   1.00 56.05  ? 1165 EPE D C7  1 
HETATM 11814 C C8  . EPE V  7 .   ? 48.434  56.267 2.026   1.00 57.27  ? 1165 EPE D C8  1 
HETATM 11815 O O8  . EPE V  7 .   ? 47.350  55.760 1.236   1.00 57.25  ? 1165 EPE D O8  1 
HETATM 11816 C C9  . EPE V  7 .   ? 45.690  61.783 3.774   1.00 55.97  ? 1165 EPE D C9  1 
HETATM 11817 C C10 . EPE V  7 .   ? 46.322  62.933 2.997   1.00 59.15  ? 1165 EPE D C10 1 
HETATM 11818 S S   . EPE V  7 .   ? 47.239  63.914 3.984   1.00 64.66  ? 1165 EPE D S   1 
HETATM 11819 O O1S . EPE V  7 .   ? 47.500  63.272 5.295   1.00 65.15  ? 1165 EPE D O1S 1 
HETATM 11820 O O2S . EPE V  7 .   ? 46.517  65.187 4.213   1.00 63.58  ? 1165 EPE D O2S 1 
HETATM 11821 O O3S . EPE V  7 .   ? 48.542  64.206 3.334   1.00 66.77  ? 1165 EPE D O3S 1 
HETATM 11822 C C1  . NAG W  3 .   ? 17.114  70.803 31.977  1.00 28.27  ? 1322 NAG E C1  1 
HETATM 11823 C C2  . NAG W  3 .   ? 18.025  72.024 32.163  1.00 32.88  ? 1322 NAG E C2  1 
HETATM 11824 C C3  . NAG W  3 .   ? 17.828  72.729 33.508  1.00 34.11  ? 1322 NAG E C3  1 
HETATM 11825 C C4  . NAG W  3 .   ? 16.350  72.929 33.815  1.00 34.12  ? 1322 NAG E C4  1 
HETATM 11826 C C5  . NAG W  3 .   ? 15.658  71.567 33.760  1.00 33.30  ? 1322 NAG E C5  1 
HETATM 11827 C C6  . NAG W  3 .   ? 14.192  71.649 34.214  1.00 33.82  ? 1322 NAG E C6  1 
HETATM 11828 C C7  . NAG W  3 .   ? 20.208  72.037 31.006  1.00 35.03  ? 1322 NAG E C7  1 
HETATM 11829 C C8  . NAG W  3 .   ? 21.637  71.567 31.017  1.00 34.48  ? 1322 NAG E C8  1 
HETATM 11830 N N2  . NAG W  3 .   ? 19.432  71.646 32.027  1.00 34.41  ? 1322 NAG E N2  1 
HETATM 11831 O O3  . NAG W  3 .   ? 18.498  73.974 33.497  1.00 35.12  ? 1322 NAG E O3  1 
HETATM 11832 O O4  . NAG W  3 .   ? 16.218  73.514 35.095  1.00 35.66  ? 1322 NAG E O4  1 
HETATM 11833 O O5  . NAG W  3 .   ? 15.785  71.028 32.449  1.00 30.45  ? 1322 NAG E O5  1 
HETATM 11834 O O6  . NAG W  3 .   ? 13.270  71.444 33.162  1.00 34.98  ? 1322 NAG E O6  1 
HETATM 11835 O O7  . NAG W  3 .   ? 19.810  72.742 30.076  1.00 36.36  ? 1322 NAG E O7  1 
HETATM 11836 C C1  . NAG X  3 .   ? 9.608   27.378 89.465  1.00 32.17  ? 1323 NAG E C1  1 
HETATM 11837 C C2  . NAG X  3 .   ? 9.276   26.179 88.558  1.00 36.20  ? 1323 NAG E C2  1 
HETATM 11838 C C3  . NAG X  3 .   ? 10.294  25.055 88.771  1.00 36.65  ? 1323 NAG E C3  1 
HETATM 11839 C C4  . NAG X  3 .   ? 11.701  25.625 88.558  1.00 37.30  ? 1323 NAG E C4  1 
HETATM 11840 C C5  . NAG X  3 .   ? 11.898  26.766 89.562  1.00 36.81  ? 1323 NAG E C5  1 
HETATM 11841 C C6  . NAG X  3 .   ? 13.305  27.368 89.586  1.00 37.38  ? 1323 NAG E C6  1 
HETATM 11842 C C7  . NAG X  3 .   ? 7.103   25.640 89.705  1.00 42.35  ? 1323 NAG E C7  1 
HETATM 11843 C C8  . NAG X  3 .   ? 5.700   25.119 89.509  1.00 42.53  ? 1323 NAG E C8  1 
HETATM 11844 N N2  . NAG X  3 .   ? 7.887   25.705 88.613  1.00 38.77  ? 1323 NAG E N2  1 
HETATM 11845 O O3  . NAG X  3 .   ? 10.059  23.984 87.882  1.00 38.11  ? 1323 NAG E O3  1 
HETATM 11846 O O4  . NAG X  3 .   ? 12.703  24.627 88.657  1.00 37.98  ? 1323 NAG E O4  1 
HETATM 11847 O O5  . NAG X  3 .   ? 10.956  27.771 89.232  1.00 34.03  ? 1323 NAG E O5  1 
HETATM 11848 O O6  . NAG X  3 .   ? 13.444  28.155 90.754  1.00 38.15  ? 1323 NAG E O6  1 
HETATM 11849 O O7  . NAG X  3 .   ? 7.448   25.971 90.842  1.00 44.81  ? 1323 NAG E O7  1 
HETATM 11850 C C1  . SIA Y  4 .   ? 4.912   64.922 96.413  1.00 52.11  ? 1324 SIA E C1  1 
HETATM 11851 C C2  . SIA Y  4 .   ? 5.279   65.201 97.857  1.00 51.63  ? 1324 SIA E C2  1 
HETATM 11852 C C3  . SIA Y  4 .   ? 4.099   64.826 98.753  1.00 50.14  ? 1324 SIA E C3  1 
HETATM 11853 C C4  . SIA Y  4 .   ? 3.878   63.318 98.728  1.00 48.93  ? 1324 SIA E C4  1 
HETATM 11854 C C5  . SIA Y  4 .   ? 5.162   62.595 99.129  1.00 47.85  ? 1324 SIA E C5  1 
HETATM 11855 C C6  . SIA Y  4 .   ? 6.351   63.046 98.271  1.00 47.39  ? 1324 SIA E C6  1 
HETATM 11856 C C7  . SIA Y  4 .   ? 7.704   62.453 98.684  1.00 46.11  ? 1324 SIA E C7  1 
HETATM 11857 C C8  . SIA Y  4 .   ? 8.904   63.162 98.042  1.00 46.02  ? 1324 SIA E C8  1 
HETATM 11858 C C9  . SIA Y  4 .   ? 10.140  62.265 98.088  1.00 45.47  ? 1324 SIA E C9  1 
HETATM 11859 C C10 . SIA Y  4 .   ? 5.497   60.203 99.516  1.00 46.33  ? 1324 SIA E C10 1 
HETATM 11860 C C11 . SIA Y  4 .   ? 5.144   58.799 99.116  1.00 45.55  ? 1324 SIA E C11 1 
HETATM 11861 N N5  . SIA Y  4 .   ? 4.907   61.186 98.839  1.00 46.59  ? 1324 SIA E N5  1 
HETATM 11862 O O1A . SIA Y  4 .   ? 5.710   64.294 95.682  1.00 52.18  ? 1324 SIA E O1A 1 
HETATM 11863 O O1B . SIA Y  4 .   ? 3.812   65.351 95.989  1.00 52.07  ? 1324 SIA E O1B 1 
HETATM 11864 O O4  . SIA Y  4 .   ? 2.806   62.968 99.609  1.00 49.14  ? 1324 SIA E O4  1 
HETATM 11865 O O6  . SIA Y  4 .   ? 6.446   64.477 98.284  1.00 49.05  ? 1324 SIA E O6  1 
HETATM 11866 O O7  . SIA Y  4 .   ? 7.850   62.502 100.103 1.00 45.01  ? 1324 SIA E O7  1 
HETATM 11867 O O8  . SIA Y  4 .   ? 8.625   63.512 96.677  1.00 46.03  ? 1324 SIA E O8  1 
HETATM 11868 O O9  . SIA Y  4 .   ? 11.259  62.902 97.458  1.00 44.97  ? 1324 SIA E O9  1 
HETATM 11869 O O10 . SIA Y  4 .   ? 6.290   60.428 100.412 1.00 45.70  ? 1324 SIA E O10 1 
HETATM 11870 C C1  . GLA Z  5 .   ? 6.506   69.402 100.162 1.00 67.34  ? 1325 GLA E C1  1 
HETATM 11871 C C2  . GLA Z  5 .   ? 5.670   68.572 99.190  1.00 64.68  ? 1325 GLA E C2  1 
HETATM 11872 C C3  . GLA Z  5 .   ? 6.200   67.152 99.016  1.00 61.37  ? 1325 GLA E C3  1 
HETATM 11873 C C4  . GLA Z  5 .   ? 7.706   67.161 98.773  1.00 62.12  ? 1325 GLA E C4  1 
HETATM 11874 C C5  . GLA Z  5 .   ? 8.418   67.948 99.866  1.00 63.67  ? 1325 GLA E C5  1 
HETATM 11875 C C6  . GLA Z  5 .   ? 9.930   67.933 99.636  1.00 62.13  ? 1325 GLA E C6  1 
HETATM 11876 O O2  . GLA Z  5 .   ? 4.310   68.536 99.645  1.00 64.87  ? 1325 GLA E O2  1 
HETATM 11877 O O3  . GLA Z  5 .   ? 5.512   66.611 97.891  1.00 56.13  ? 1325 GLA E O3  1 
HETATM 11878 O O4  . GLA Z  5 .   ? 7.978   67.753 97.497  1.00 59.83  ? 1325 GLA E O4  1 
HETATM 11879 O O5  . GLA Z  5 .   ? 7.909   69.289 99.870  1.00 66.85  ? 1325 GLA E O5  1 
HETATM 11880 O O6  . GLA Z  5 .   ? 10.623  68.361 100.813 1.00 59.00  ? 1325 GLA E O6  1 
HETATM 11881 C C1  . NAG AA 3 .   ? 4.724   72.302 103.666 1.00 81.09  ? 1326 NAG E C1  1 
HETATM 11882 C C2  . NAG AA 3 .   ? 6.189   72.443 103.246 1.00 79.61  ? 1326 NAG E C2  1 
HETATM 11883 C C3  . NAG AA 3 .   ? 6.483   71.483 102.090 1.00 78.88  ? 1326 NAG E C3  1 
HETATM 11884 C C4  . NAG AA 3 .   ? 6.105   70.049 102.518 1.00 77.99  ? 1326 NAG E C4  1 
HETATM 11885 C C5  . NAG AA 3 .   ? 4.648   70.014 103.009 1.00 79.08  ? 1326 NAG E C5  1 
HETATM 11886 C C6  . NAG AA 3 .   ? 4.177   68.631 103.480 1.00 78.53  ? 1326 NAG E C6  1 
HETATM 11887 C C7  . NAG AA 3 .   ? 7.322   74.638 103.103 1.00 77.37  ? 1326 NAG E C7  1 
HETATM 11888 C C8  . NAG AA 3 .   ? 7.266   76.006 102.485 1.00 76.53  ? 1326 NAG E C8  1 
HETATM 11889 N N2  . NAG AA 3 .   ? 6.324   73.816 102.763 1.00 78.88  ? 1326 NAG E N2  1 
HETATM 11890 O O1  . NAG AA 3 .   ? 4.410   73.206 104.735 1.00 81.71  ? 1326 NAG E O1  1 
HETATM 11891 O O3  . NAG AA 3 .   ? 7.862   71.555 101.669 1.00 79.87  ? 1326 NAG E O3  1 
HETATM 11892 O O4  . NAG AA 3 .   ? 6.262   69.017 101.518 1.00 72.92  ? 1326 NAG E O4  1 
HETATM 11893 O O5  . NAG AA 3 .   ? 4.480   70.952 104.077 1.00 81.47  ? 1326 NAG E O5  1 
HETATM 11894 O O6  . NAG AA 3 .   ? 5.241   67.861 104.040 1.00 77.69  ? 1326 NAG E O6  1 
HETATM 11895 O O7  . NAG AA 3 .   ? 8.234   74.309 103.846 1.00 76.02  ? 1326 NAG E O7  1 
HETATM 11896 C C1  . FUC BA 6 .   ? 8.232   72.624 100.769 1.00 79.34  ? 1327 FUC E C1  1 
HETATM 11897 C C2  . FUC BA 6 .   ? 9.499   72.280 99.957  1.00 78.59  ? 1327 FUC E C2  1 
HETATM 11898 C C3  . FUC BA 6 .   ? 9.510   72.651 98.462  1.00 77.38  ? 1327 FUC E C3  1 
HETATM 11899 C C4  . FUC BA 6 .   ? 8.166   73.064 97.855  1.00 79.13  ? 1327 FUC E C4  1 
HETATM 11900 C C5  . FUC BA 6 .   ? 7.031   72.464 98.661  1.00 80.10  ? 1327 FUC E C5  1 
HETATM 11901 C C6  . FUC BA 6 .   ? 5.647   72.737 98.071  1.00 79.67  ? 1327 FUC E C6  1 
HETATM 11902 O O2  . FUC BA 6 .   ? 9.785   70.879 100.070 1.00 77.56  ? 1327 FUC E O2  1 
HETATM 11903 O O3  . FUC BA 6 .   ? 10.453  73.717 98.286  1.00 75.58  ? 1327 FUC E O3  1 
HETATM 11904 O O4  . FUC BA 6 .   ? 8.028   74.491 97.825  1.00 79.31  ? 1327 FUC E O4  1 
HETATM 11905 O O5  . FUC BA 6 .   ? 7.105   73.019 99.973  1.00 80.40  ? 1327 FUC E O5  1 
HETATM 11906 C C1  . NAG CA 3 .   ? 6.952   38.599 -0.103  1.00 40.49  ? 1164 NAG F C1  1 
HETATM 11907 C C2  . NAG CA 3 .   ? 6.668   37.087 -0.151  1.00 45.37  ? 1164 NAG F C2  1 
HETATM 11908 C C3  . NAG CA 3 .   ? 6.452   36.504 -1.549  1.00 46.74  ? 1164 NAG F C3  1 
HETATM 11909 C C4  . NAG CA 3 .   ? 5.571   37.424 -2.380  1.00 47.48  ? 1164 NAG F C4  1 
HETATM 11910 C C5  . NAG CA 3 .   ? 6.252   38.789 -2.422  1.00 46.66  ? 1164 NAG F C5  1 
HETATM 11911 C C6  . NAG CA 3 .   ? 5.516   39.765 -3.336  1.00 46.99  ? 1164 NAG F C6  1 
HETATM 11912 C C7  . NAG CA 3 .   ? 7.813   36.342 1.877   1.00 46.47  ? 1164 NAG F C7  1 
HETATM 11913 C C8  . NAG CA 3 .   ? 8.935   35.547 2.485   1.00 46.26  ? 1164 NAG F C8  1 
HETATM 11914 N N2  . NAG CA 3 .   ? 7.719   36.351 0.542   1.00 45.91  ? 1164 NAG F N2  1 
HETATM 11915 O O3  . NAG CA 3 .   ? 5.842   35.237 -1.432  1.00 47.51  ? 1164 NAG F O3  1 
HETATM 11916 O O4  . NAG CA 3 .   ? 5.374   36.886 -3.678  1.00 48.75  ? 1164 NAG F O4  1 
HETATM 11917 O O5  . NAG CA 3 .   ? 6.283   39.339 -1.117  1.00 43.70  ? 1164 NAG F O5  1 
HETATM 11918 O O6  . NAG CA 3 .   ? 6.238   40.973 -3.381  1.00 46.48  ? 1164 NAG F O6  1 
HETATM 11919 O O7  . NAG CA 3 .   ? 7.031   36.949 2.613   1.00 46.58  ? 1164 NAG F O7  1 
HETATM 11920 N N1  . EPE DA 7 .   ? 12.567  62.129 3.605   1.00 54.37  ? 1165 EPE F N1  1 
HETATM 11921 C C2  . EPE DA 7 .   ? 11.956  63.370 4.073   1.00 55.91  ? 1165 EPE F C2  1 
HETATM 11922 C C3  . EPE DA 7 .   ? 13.015  64.475 3.972   1.00 55.62  ? 1165 EPE F C3  1 
HETATM 11923 N N4  . EPE DA 7 .   ? 13.869  64.156 2.826   1.00 54.68  ? 1165 EPE F N4  1 
HETATM 11924 C C5  . EPE DA 7 .   ? 14.601  62.895 2.782   1.00 52.94  ? 1165 EPE F C5  1 
HETATM 11925 C C6  . EPE DA 7 .   ? 13.987  61.941 3.799   1.00 53.27  ? 1165 EPE F C6  1 
HETATM 11926 C C7  . EPE DA 7 .   ? 13.988  65.082 1.700   1.00 56.22  ? 1165 EPE F C7  1 
HETATM 11927 C C8  . EPE DA 7 .   ? 15.444  65.543 1.603   1.00 56.83  ? 1165 EPE F C8  1 
HETATM 11928 O O8  . EPE DA 7 .   ? 16.076  64.942 0.464   1.00 56.81  ? 1165 EPE F O8  1 
HETATM 11929 C C9  . EPE DA 7 .   ? 11.792  61.108 2.920   1.00 55.05  ? 1165 EPE F C9  1 
HETATM 11930 C C10 . EPE DA 7 .   ? 11.085  60.301 3.999   1.00 57.07  ? 1165 EPE F C10 1 
HETATM 11931 S S   . EPE DA 7 .   ? 9.448   60.607 3.974   1.00 62.28  ? 1165 EPE F S   1 
HETATM 11932 O O1S . EPE DA 7 .   ? 8.742   59.701 4.912   1.00 62.33  ? 1165 EPE F O1S 1 
HETATM 11933 O O2S . EPE DA 7 .   ? 8.916   60.365 2.613   1.00 66.19  ? 1165 EPE F O2S 1 
HETATM 11934 O O3S . EPE DA 7 .   ? 9.181   62.017 4.363   1.00 64.10  ? 1165 EPE F O3S 1 
HETATM 11935 O O   . HOH EA 8 .   ? 32.157  32.062 -7.276  1.00 21.28  ? 2001 HOH A O   1 
HETATM 11936 O O   . HOH EA 8 .   ? 40.090  29.778 -9.858  1.00 22.26  ? 2002 HOH A O   1 
HETATM 11937 O O   . HOH EA 8 .   ? 34.240  31.235 -0.228  1.00 20.15  ? 2003 HOH A O   1 
HETATM 11938 O O   . HOH EA 8 .   ? 28.391  33.280 -1.075  1.00 48.60  ? 2004 HOH A O   1 
HETATM 11939 O O   . HOH EA 8 .   ? 30.555  35.096 5.169   1.00 17.59  ? 2005 HOH A O   1 
HETATM 11940 O O   . HOH EA 8 .   ? 31.196  33.414 9.878   1.00 7.41   ? 2006 HOH A O   1 
HETATM 11941 O O   . HOH EA 8 .   ? 29.946  31.859 16.350  1.00 9.41   ? 2007 HOH A O   1 
HETATM 11942 O O   . HOH EA 8 .   ? 37.100  26.371 20.612  1.00 23.85  ? 2008 HOH A O   1 
HETATM 11943 O O   . HOH EA 8 .   ? 28.063  26.546 16.637  1.00 24.68  ? 2009 HOH A O   1 
HETATM 11944 O O   . HOH EA 8 .   ? 31.327  19.170 17.877  1.00 36.00  ? 2010 HOH A O   1 
HETATM 11945 O O   . HOH EA 8 .   ? 26.100  25.945 21.092  1.00 38.44  ? 2011 HOH A O   1 
HETATM 11946 O O   . HOH EA 8 .   ? 33.881  26.920 25.619  1.00 28.05  ? 2012 HOH A O   1 
HETATM 11947 O O   . HOH EA 8 .   ? 24.025  27.126 25.956  1.00 24.89  ? 2013 HOH A O   1 
HETATM 11948 O O   . HOH EA 8 .   ? 23.806  32.926 31.382  1.00 20.61  ? 2014 HOH A O   1 
HETATM 11949 O O   . HOH EA 8 .   ? 27.391  36.075 32.755  1.00 6.00   ? 2015 HOH A O   1 
HETATM 11950 O O   . HOH EA 8 .   ? 20.045  33.996 33.923  1.00 28.91  ? 2016 HOH A O   1 
HETATM 11951 O O   . HOH EA 8 .   ? 21.456  41.475 23.340  1.00 19.80  ? 2017 HOH A O   1 
HETATM 11952 O O   . HOH EA 8 .   ? 40.317  32.401 24.488  1.00 34.74  ? 2018 HOH A O   1 
HETATM 11953 O O   . HOH EA 8 .   ? 39.271  32.395 29.773  1.00 22.97  ? 2019 HOH A O   1 
HETATM 11954 O O   . HOH EA 8 .   ? 36.316  29.345 33.331  1.00 36.21  ? 2020 HOH A O   1 
HETATM 11955 O O   . HOH EA 8 .   ? 29.903  31.418 38.362  1.00 11.73  ? 2021 HOH A O   1 
HETATM 11956 O O   . HOH EA 8 .   ? 31.518  49.940 73.914  1.00 23.31  ? 2022 HOH A O   1 
HETATM 11957 O O   . HOH EA 8 .   ? 37.782  25.908 47.197  1.00 17.28  ? 2023 HOH A O   1 
HETATM 11958 O O   . HOH EA 8 .   ? 49.129  30.327 59.042  1.00 24.54  ? 2024 HOH A O   1 
HETATM 11959 O O   . HOH EA 8 .   ? 45.987  24.116 69.844  1.00 28.24  ? 2025 HOH A O   1 
HETATM 11960 O O   . HOH EA 8 .   ? 47.965  22.640 75.584  1.00 35.46  ? 2026 HOH A O   1 
HETATM 11961 O O   . HOH EA 8 .   ? 51.170  22.490 74.169  1.00 32.82  ? 2027 HOH A O   1 
HETATM 11962 O O   . HOH EA 8 .   ? 52.131  25.799 83.797  1.00 33.52  ? 2028 HOH A O   1 
HETATM 11963 O O   . HOH EA 8 .   ? 26.460  24.743 79.292  1.00 41.16  ? 2029 HOH A O   1 
HETATM 11964 O O   . HOH EA 8 .   ? 26.589  28.519 96.376  1.00 25.38  ? 2030 HOH A O   1 
HETATM 11965 O O   . HOH EA 8 .   ? 37.575  43.258 83.481  1.00 23.99  ? 2031 HOH A O   1 
HETATM 11966 O O   . HOH EA 8 .   ? 31.235  44.272 81.271  1.00 37.45  ? 2032 HOH A O   1 
HETATM 11967 O O   . HOH EA 8 .   ? 32.699  46.113 77.715  1.00 26.02  ? 2033 HOH A O   1 
HETATM 11968 O O   . HOH EA 8 .   ? 33.452  43.651 76.509  1.00 19.51  ? 2034 HOH A O   1 
HETATM 11969 O O   . HOH EA 8 .   ? 39.826  45.200 73.582  1.00 14.61  ? 2035 HOH A O   1 
HETATM 11970 O O   . HOH EA 8 .   ? 33.774  48.620 72.171  1.00 4.41   ? 2036 HOH A O   1 
HETATM 11971 O O   . HOH EA 8 .   ? 25.559  32.476 58.553  1.00 40.83  ? 2037 HOH A O   1 
HETATM 11972 O O   . HOH EA 8 .   ? 39.443  37.466 68.266  1.00 20.12  ? 2038 HOH A O   1 
HETATM 11973 O O   . HOH EA 8 .   ? 46.645  26.776 102.473 1.00 32.93  ? 2039 HOH A O   1 
HETATM 11974 O O   . HOH EA 8 .   ? 40.913  26.886 100.397 1.00 25.43  ? 2040 HOH A O   1 
HETATM 11975 O O   . HOH EA 8 .   ? 31.644  17.386 92.838  1.00 30.23  ? 2041 HOH A O   1 
HETATM 11976 O O   . HOH EA 8 .   ? 46.088  18.687 86.139  1.00 30.45  ? 2042 HOH A O   1 
HETATM 11977 O O   . HOH EA 8 .   ? 45.159  26.433 115.076 1.00 34.57  ? 2043 HOH A O   1 
HETATM 11978 O O   . HOH EA 8 .   ? 48.740  38.198 102.644 1.00 32.22  ? 2044 HOH A O   1 
HETATM 11979 O O   . HOH EA 8 .   ? 45.774  47.904 96.008  1.00 23.83  ? 2045 HOH A O   1 
HETATM 11980 O O   . HOH EA 8 .   ? 46.280  53.325 89.084  1.00 33.00  ? 2046 HOH A O   1 
HETATM 11981 O O   . HOH EA 8 .   ? 18.042  38.930 95.984  1.00 28.76  ? 2047 HOH A O   1 
HETATM 11982 O O   . HOH EA 8 .   ? 21.092  24.234 88.959  1.00 24.28  ? 2048 HOH A O   1 
HETATM 11983 O O   . HOH EA 8 .   ? 32.489  17.873 61.450  1.00 33.67  ? 2049 HOH A O   1 
HETATM 11984 O O   . HOH EA 8 .   ? 44.244  21.924 43.148  1.00 49.99  ? 2050 HOH A O   1 
HETATM 11985 O O   . HOH EA 8 .   ? 44.888  26.838 42.027  1.00 36.19  ? 2051 HOH A O   1 
HETATM 11986 O O   . HOH EA 8 .   ? 26.501  30.325 49.051  1.00 30.66  ? 2052 HOH A O   1 
HETATM 11987 O O   . HOH EA 8 .   ? 27.849  28.862 51.162  1.00 22.65  ? 2053 HOH A O   1 
HETATM 11988 O O   . HOH EA 8 .   ? 27.749  30.781 59.801  1.00 29.67  ? 2054 HOH A O   1 
HETATM 11989 O O   . HOH EA 8 .   ? 33.429  40.362 29.275  1.00 8.81   ? 2055 HOH A O   1 
HETATM 11990 O O   . HOH EA 8 .   ? 40.806  34.750 25.819  1.00 24.39  ? 2056 HOH A O   1 
HETATM 11991 O O   . HOH EA 8 .   ? 29.566  38.686 19.640  1.00 8.00   ? 2057 HOH A O   1 
HETATM 11992 O O   . HOH EA 8 .   ? 25.286  39.642 17.335  1.00 19.10  ? 2058 HOH A O   1 
HETATM 11993 O O   . HOH EA 8 .   ? 27.083  39.749 19.203  1.00 15.98  ? 2059 HOH A O   1 
HETATM 11994 O O   . HOH EA 8 .   ? 23.800  32.997 17.065  1.00 34.60  ? 2060 HOH A O   1 
HETATM 11995 O O   . HOH EA 8 .   ? 24.362  23.061 15.076  1.00 35.66  ? 2061 HOH A O   1 
HETATM 11996 O O   . HOH EA 8 .   ? 38.242  17.841 22.737  1.00 44.58  ? 2062 HOH A O   1 
HETATM 11997 O O   . HOH EA 8 .   ? 48.233  19.502 84.322  1.00 35.75  ? 2063 HOH A O   1 
HETATM 11998 O O   . HOH EA 8 .   ? 28.901  48.304 88.939  1.00 51.36  ? 2064 HOH A O   1 
HETATM 11999 O O   . HOH FA 8 .   ? 25.345  42.329 14.802  1.00 5.81   ? 2001 HOH B O   1 
HETATM 12000 O O   . HOH FA 8 .   ? 21.651  47.016 17.482  1.00 4.96   ? 2002 HOH B O   1 
HETATM 12001 O O   . HOH FA 8 .   ? 23.083  44.951 20.652  1.00 19.20  ? 2003 HOH B O   1 
HETATM 12002 O O   . HOH FA 8 .   ? 25.860  49.526 13.088  1.00 10.03  ? 2004 HOH B O   1 
HETATM 12003 O O   . HOH FA 8 .   ? 21.607  36.799 10.809  1.00 16.76  ? 2005 HOH B O   1 
HETATM 12004 O O   . HOH FA 8 .   ? 22.919  37.622 5.173   1.00 33.09  ? 2006 HOH B O   1 
HETATM 12005 O O   . HOH FA 8 .   ? 26.114  35.125 5.692   1.00 21.39  ? 2007 HOH B O   1 
HETATM 12006 O O   . HOH FA 8 .   ? 27.397  33.122 7.293   1.00 28.27  ? 2008 HOH B O   1 
HETATM 12007 O O   . HOH FA 8 .   ? 27.000  29.194 10.263  1.00 27.41  ? 2009 HOH B O   1 
HETATM 12008 O O   . HOH FA 8 .   ? 32.597  26.314 8.932   1.00 23.88  ? 2010 HOH B O   1 
HETATM 12009 O O   . HOH FA 8 .   ? 29.284  21.964 17.395  1.00 34.61  ? 2011 HOH B O   1 
HETATM 12010 O O   . HOH FA 8 .   ? 43.758  32.008 18.454  1.00 40.27  ? 2012 HOH B O   1 
HETATM 12011 O O   . HOH FA 8 .   ? 40.261  31.197 18.858  1.00 16.79  ? 2013 HOH B O   1 
HETATM 12012 O O   . HOH FA 8 .   ? 41.928  32.340 20.290  1.00 29.62  ? 2014 HOH B O   1 
HETATM 12013 O O   . HOH FA 8 .   ? 41.190  31.650 2.950   1.00 25.73  ? 2015 HOH B O   1 
HETATM 12014 O O   . HOH FA 8 .   ? 41.845  27.296 -3.252  1.00 17.56  ? 2016 HOH B O   1 
HETATM 12015 O O   . HOH FA 8 .   ? 37.714  24.908 -13.442 1.00 27.20  ? 2017 HOH B O   1 
HETATM 12016 O O   . HOH FA 8 .   ? 46.831  38.812 9.923   1.00 44.99  ? 2018 HOH B O   1 
HETATM 12017 O O   . HOH FA 8 .   ? 51.028  38.625 24.011  1.00 34.51  ? 2019 HOH B O   1 
HETATM 12018 O O   . HOH FA 8 .   ? 46.126  50.683 15.023  1.00 37.20  ? 2020 HOH B O   1 
HETATM 12019 O O   . HOH FA 8 .   ? 43.182  49.253 33.060  1.00 17.20  ? 2021 HOH B O   1 
HETATM 12020 O O   . HOH FA 8 .   ? 39.548  49.978 43.071  1.00 33.03  ? 2022 HOH B O   1 
HETATM 12021 O O   . HOH FA 8 .   ? 38.576  49.853 45.899  1.00 26.49  ? 2023 HOH B O   1 
HETATM 12022 O O   . HOH FA 8 .   ? 35.261  48.343 51.281  1.00 25.72  ? 2024 HOH B O   1 
HETATM 12023 O O   . HOH FA 8 .   ? 34.927  44.686 58.982  1.00 26.06  ? 2025 HOH B O   1 
HETATM 12024 O O   . HOH FA 8 .   ? 29.043  37.305 72.369  1.00 33.05  ? 2026 HOH B O   1 
HETATM 12025 O O   . HOH FA 8 .   ? 24.172  49.398 75.129  1.00 25.07  ? 2027 HOH B O   1 
HETATM 12026 O O   . HOH FA 8 .   ? 20.480  51.729 76.601  1.00 16.08  ? 2028 HOH B O   1 
HETATM 12027 O O   . HOH FA 8 .   ? 24.611  48.922 72.256  1.00 8.12   ? 2029 HOH B O   1 
HETATM 12028 O O   . HOH FA 8 .   ? 27.044  41.750 64.679  1.00 22.26  ? 2030 HOH B O   1 
HETATM 12029 O O   . HOH FA 8 .   ? 22.367  37.829 63.031  1.00 44.86  ? 2031 HOH B O   1 
HETATM 12030 O O   . HOH FA 8 .   ? 23.645  47.777 51.076  1.00 23.84  ? 2032 HOH B O   1 
HETATM 12031 O O   . HOH FA 8 .   ? 23.278  43.941 46.018  1.00 28.19  ? 2033 HOH B O   1 
HETATM 12032 O O   . HOH FA 8 .   ? 25.354  51.860 38.987  1.00 9.20   ? 2034 HOH B O   1 
HETATM 12033 O O   . HOH FA 8 .   ? 30.816  47.916 38.953  1.00 7.58   ? 2035 HOH B O   1 
HETATM 12034 O O   . HOH FA 8 .   ? 29.325  50.806 44.289  1.00 17.92  ? 2036 HOH B O   1 
HETATM 12035 O O   . HOH FA 8 .   ? 26.263  39.297 36.632  1.00 12.25  ? 2037 HOH B O   1 
HETATM 12036 O O   . HOH FA 8 .   ? 31.242  53.230 22.715  1.00 20.69  ? 2038 HOH B O   1 
HETATM 12037 O O   . HOH FA 8 .   ? 29.747  48.633 22.572  1.00 24.73  ? 2039 HOH B O   1 
HETATM 12038 O O   . HOH FA 8 .   ? 36.789  46.895 17.541  1.00 4.97   ? 2040 HOH B O   1 
HETATM 12039 O O   . HOH FA 8 .   ? 37.788  48.713 8.341   1.00 17.88  ? 2041 HOH B O   1 
HETATM 12040 O O   . HOH FA 8 .   ? 32.556  49.195 13.199  1.00 7.08   ? 2042 HOH B O   1 
HETATM 12041 O O   . HOH FA 8 .   ? 28.788  40.693 1.339   1.00 17.27  ? 2043 HOH B O   1 
HETATM 12042 O O   . HOH FA 8 .   ? 41.659  48.456 3.130   1.00 20.69  ? 2044 HOH B O   1 
HETATM 12043 O O   . HOH FA 8 .   ? 32.835  49.866 -5.506  1.00 33.97  ? 2045 HOH B O   1 
HETATM 12044 O O   . HOH FA 8 .   ? 34.887  54.135 -5.499  1.00 21.67  ? 2046 HOH B O   1 
HETATM 12045 O O   . HOH FA 8 .   ? 28.882  45.181 -5.547  1.00 24.15  ? 2047 HOH B O   1 
HETATM 12046 O O   . HOH FA 8 .   ? 43.650  42.649 -17.441 1.00 46.00  ? 2048 HOH B O   1 
HETATM 12047 O O   . HOH GA 8 .   ? 44.484  63.471 -7.367  1.00 27.17  ? 2001 HOH C O   1 
HETATM 12048 O O   . HOH GA 8 .   ? 42.556  71.705 -9.801  1.00 27.28  ? 2002 HOH C O   1 
HETATM 12049 O O   . HOH GA 8 .   ? 44.118  65.824 -0.243  1.00 20.63  ? 2003 HOH C O   1 
HETATM 12050 O O   . HOH GA 8 .   ? 42.701  60.605 5.141   1.00 16.55  ? 2004 HOH C O   1 
HETATM 12051 O O   . HOH GA 8 .   ? 43.905  62.136 9.825   1.00 9.81   ? 2005 HOH C O   1 
HETATM 12052 O O   . HOH GA 8 .   ? 45.786  61.783 16.385  1.00 15.11  ? 2006 HOH C O   1 
HETATM 12053 O O   . HOH GA 8 .   ? 47.146  70.652 20.335  1.00 32.86  ? 2007 HOH C O   1 
HETATM 12054 O O   . HOH GA 8 .   ? 51.278  62.588 16.545  1.00 28.90  ? 2008 HOH C O   1 
HETATM 12055 O O   . HOH GA 8 .   ? 53.228  61.604 21.130  1.00 41.94  ? 2009 HOH C O   1 
HETATM 12056 O O   . HOH GA 8 .   ? 47.979  67.729 25.524  1.00 29.86  ? 2010 HOH C O   1 
HETATM 12057 O O   . HOH GA 8 .   ? 52.884  58.931 25.908  1.00 27.78  ? 2011 HOH C O   1 
HETATM 12058 O O   . HOH GA 8 .   ? 47.933  56.038 31.447  1.00 18.35  ? 2012 HOH C O   1 
HETATM 12059 O O   . HOH GA 8 .   ? 43.338  57.393 32.811  1.00 14.39  ? 2013 HOH C O   1 
HETATM 12060 O O   . HOH GA 8 .   ? 48.921  51.981 33.820  1.00 31.44  ? 2014 HOH C O   1 
HETATM 12061 O O   . HOH GA 8 .   ? 44.221  51.259 35.005  1.00 27.01  ? 2015 HOH C O   1 
HETATM 12062 O O   . HOH GA 8 .   ? 41.809  49.587 23.229  1.00 24.10  ? 2016 HOH C O   1 
HETATM 12063 O O   . HOH GA 8 .   ? 47.986  56.291 20.989  1.00 30.90  ? 2017 HOH C O   1 
HETATM 12064 O O   . HOH GA 8 .   ? 40.410  70.389 24.601  1.00 32.57  ? 2018 HOH C O   1 
HETATM 12065 O O   . HOH GA 8 .   ? 40.321  69.762 29.648  1.00 25.28  ? 2019 HOH C O   1 
HETATM 12066 O O   . HOH GA 8 .   ? 44.627  68.792 33.172  1.00 33.98  ? 2020 HOH C O   1 
HETATM 12067 O O   . HOH GA 8 .   ? 46.169  61.871 38.311  1.00 13.26  ? 2021 HOH C O   1 
HETATM 12068 O O   . HOH GA 8 .   ? 47.172  71.523 47.219  1.00 17.35  ? 2022 HOH C O   1 
HETATM 12069 O O   . HOH GA 8 .   ? 44.060  79.547 69.889  1.00 35.60  ? 2023 HOH C O   1 
HETATM 12070 O O   . HOH GA 8 .   ? 43.555  84.993 74.095  1.00 40.85  ? 2024 HOH C O   1 
HETATM 12071 O O   . HOH GA 8 .   ? 39.300  84.073 83.870  1.00 32.48  ? 2025 HOH C O   1 
HETATM 12072 O O   . HOH GA 8 .   ? 47.362  58.613 72.368  1.00 32.25  ? 2026 HOH C O   1 
HETATM 12073 O O   . HOH GA 8 .   ? 52.517  62.273 79.079  1.00 40.86  ? 2027 HOH C O   1 
HETATM 12074 O O   . HOH GA 8 .   ? 50.412  60.537 96.387  1.00 23.65  ? 2028 HOH C O   1 
HETATM 12075 O O   . HOH GA 8 .   ? 32.305  62.748 83.645  1.00 22.44  ? 2029 HOH C O   1 
HETATM 12076 O O   . HOH GA 8 .   ? 31.781  57.291 77.595  1.00 30.96  ? 2030 HOH C O   1 
HETATM 12077 O O   . HOH GA 8 .   ? 34.064  58.705 76.564  1.00 20.54  ? 2031 HOH C O   1 
HETATM 12078 O O   . HOH GA 8 .   ? 35.637  61.368 70.351  1.00 16.48  ? 2032 HOH C O   1 
HETATM 12079 O O   . HOH GA 8 .   ? 29.271  63.711 73.557  1.00 10.06  ? 2033 HOH C O   1 
HETATM 12080 O O   . HOH GA 8 .   ? 30.166  56.880 75.137  1.00 19.83  ? 2034 HOH C O   1 
HETATM 12081 O O   . HOH GA 8 .   ? 29.397  56.776 72.247  1.00 7.21   ? 2035 HOH C O   1 
HETATM 12082 O O   . HOH GA 8 .   ? 40.372  55.395 19.086  1.00 17.84  ? 2036 HOH C O   1 
HETATM 12083 O O   . HOH GA 8 .   ? 44.594  73.601 100.318 1.00 29.70  ? 2037 HOH C O   1 
HETATM 12084 O O   . HOH GA 8 .   ? 48.959  82.289 86.289  1.00 33.91  ? 2038 HOH C O   1 
HETATM 12085 O O   . HOH GA 8 .   ? 42.522  77.563 115.037 1.00 47.25  ? 2039 HOH C O   1 
HETATM 12086 O O   . HOH GA 8 .   ? 31.099  74.912 102.755 1.00 36.15  ? 2040 HOH C O   1 
HETATM 12087 O O   . HOH GA 8 .   ? 24.120  67.368 96.163  1.00 27.56  ? 2041 HOH C O   1 
HETATM 12088 O O   . HOH GA 8 .   ? 19.005  65.190 88.996  1.00 33.90  ? 2042 HOH C O   1 
HETATM 12089 O O   . HOH GA 8 .   ? 23.521  69.140 84.287  1.00 19.27  ? 2043 HOH C O   1 
HETATM 12090 O O   . HOH GA 8 .   ? 45.467  84.095 89.144  1.00 43.89  ? 2044 HOH C O   1 
HETATM 12091 O O   . HOH GA 8 .   ? 47.419  79.463 42.748  1.00 50.04  ? 2045 HOH C O   1 
HETATM 12092 O O   . HOH GA 8 .   ? 43.147  76.794 41.807  1.00 51.28  ? 2046 HOH C O   1 
HETATM 12093 O O   . HOH GA 8 .   ? 49.244  59.734 48.736  1.00 32.69  ? 2047 HOH C O   1 
HETATM 12094 O O   . HOH GA 8 .   ? 49.444  61.431 51.118  1.00 23.69  ? 2048 HOH C O   1 
HETATM 12095 O O   . HOH GA 8 .   ? 47.985  60.066 59.453  1.00 33.85  ? 2049 HOH C O   1 
HETATM 12096 O O   . HOH GA 8 .   ? 42.938  57.065 35.736  1.00 16.16  ? 2050 HOH C O   1 
HETATM 12097 O O   . HOH GA 8 .   ? 36.700  60.616 29.334  1.00 5.65   ? 2051 HOH C O   1 
HETATM 12098 O O   . HOH GA 8 .   ? 37.887  69.792 25.525  1.00 25.40  ? 2052 HOH C O   1 
HETATM 12099 O O   . HOH GA 8 .   ? 40.138  58.091 19.660  1.00 9.47   ? 2053 HOH C O   1 
HETATM 12100 O O   . HOH GA 8 .   ? 41.558  53.851 17.299  1.00 18.21  ? 2054 HOH C O   1 
HETATM 12101 O O   . HOH GA 8 .   ? 45.888  51.936 17.726  1.00 37.87  ? 2055 HOH C O   1 
HETATM 12102 O O   . HOH GA 8 .   ? 47.868  55.703 17.270  1.00 37.64  ? 2056 HOH C O   1 
HETATM 12103 O O   . HOH GA 8 .   ? 53.966  75.545 23.098  1.00 42.66  ? 2057 HOH C O   1 
HETATM 12104 O O   . HOH GA 8 .   ? 47.321  83.923 84.353  1.00 35.55  ? 2058 HOH C O   1 
HETATM 12105 O O   . HOH GA 8 .   ? 47.340  55.914 54.627  1.00 54.52  ? 2059 HOH C O   1 
HETATM 12106 O O   . HOH GA 8 .   ? 31.887  53.011 88.983  1.00 53.27  ? 2060 HOH C O   1 
HETATM 12107 O O   . HOH HA 8 .   ? 39.070  52.522 14.839  1.00 4.72   ? 2001 HOH D O   1 
HETATM 12108 O O   . HOH HA 8 .   ? 37.895  49.201 20.632  1.00 14.47  ? 2002 HOH D O   1 
HETATM 12109 O O   . HOH HA 8 .   ? 39.391  49.552 10.443  1.00 19.79  ? 2003 HOH D O   1 
HETATM 12110 O O   . HOH HA 8 .   ? 56.459  68.775 17.369  1.00 49.06  ? 2004 HOH D O   1 
HETATM 12111 O O   . HOH HA 8 .   ? 45.676  51.932 10.787  1.00 20.77  ? 2005 HOH D O   1 
HETATM 12112 O O   . HOH HA 8 .   ? 44.246  52.805 4.903   1.00 27.64  ? 2006 HOH D O   1 
HETATM 12113 O O   . HOH HA 8 .   ? 44.928  56.642 5.631   1.00 26.05  ? 2007 HOH D O   1 
HETATM 12114 O O   . HOH HA 8 .   ? 49.740  60.264 10.628  1.00 30.10  ? 2008 HOH D O   1 
HETATM 12115 O O   . HOH HA 8 .   ? 49.405  66.778 8.908   1.00 26.71  ? 2009 HOH D O   1 
HETATM 12116 O O   . HOH HA 8 .   ? 54.761  65.887 17.558  1.00 33.54  ? 2010 HOH D O   1 
HETATM 12117 O O   . HOH HA 8 .   ? 43.307  77.785 15.309  1.00 33.31  ? 2011 HOH D O   1 
HETATM 12118 O O   . HOH HA 8 .   ? 38.867  73.815 18.400  1.00 37.07  ? 2012 HOH D O   1 
HETATM 12119 O O   . HOH HA 8 .   ? 41.351  71.013 18.852  1.00 14.50  ? 2013 HOH D O   1 
HETATM 12120 O O   . HOH HA 8 .   ? 39.554  71.952 20.220  1.00 30.38  ? 2014 HOH D O   1 
HETATM 12121 O O   . HOH HA 8 .   ? 31.258  72.810 9.913   1.00 38.16  ? 2015 HOH D O   1 
HETATM 12122 O O   . HOH HA 8 .   ? 29.438  76.705 23.807  1.00 33.10  ? 2016 HOH D O   1 
HETATM 12123 O O   . HOH HA 8 .   ? 30.937  69.891 37.142  1.00 42.36  ? 2017 HOH D O   1 
HETATM 12124 O O   . HOH HA 8 .   ? 24.329  64.612 32.807  1.00 16.01  ? 2018 HOH D O   1 
HETATM 12125 O O   . HOH HA 8 .   ? 29.221  64.462 52.394  1.00 43.43  ? 2019 HOH D O   1 
HETATM 12126 O O   . HOH HA 8 .   ? 28.996  57.892 51.187  1.00 17.68  ? 2020 HOH D O   1 
HETATM 12127 O O   . HOH HA 8 .   ? 32.377  59.946 59.011  1.00 23.52  ? 2021 HOH D O   1 
HETATM 12128 O O   . HOH HA 8 .   ? 42.044  57.930 71.971  1.00 36.12  ? 2022 HOH D O   1 
HETATM 12129 O O   . HOH HA 8 .   ? 34.527  50.545 78.119  1.00 26.82  ? 2023 HOH D O   1 
HETATM 12130 O O   . HOH HA 8 .   ? 30.979  52.786 74.342  1.00 17.52  ? 2024 HOH D O   1 
HETATM 12131 O O   . HOH HA 8 .   ? 38.718  54.275 64.699  1.00 20.27  ? 2025 HOH D O   1 
HETATM 12132 O O   . HOH HA 8 .   ? 44.169  52.683 62.959  1.00 36.72  ? 2026 HOH D O   1 
HETATM 12133 O O   . HOH HA 8 .   ? 31.553  54.488 39.025  1.00 8.18   ? 2027 HOH D O   1 
HETATM 12134 O O   . HOH HA 8 .   ? 29.132  52.785 44.386  1.00 23.43  ? 2028 HOH D O   1 
HETATM 12135 O O   . HOH HA 8 .   ? 41.165  55.054 36.504  1.00 10.91  ? 2029 HOH D O   1 
HETATM 12136 O O   . HOH HA 8 .   ? 26.681  52.465 22.688  1.00 16.83  ? 2030 HOH D O   1 
HETATM 12137 O O   . HOH HA 8 .   ? 36.034  50.087 22.730  1.00 12.19  ? 2031 HOH D O   1 
HETATM 12138 O O   . HOH HA 8 .   ? 39.090  53.267 20.635  1.00 28.94  ? 2032 HOH D O   1 
HETATM 12139 O O   . HOH HA 8 .   ? 29.276  60.147 17.465  1.00 7.72   ? 2033 HOH D O   1 
HETATM 12140 O O   . HOH HA 8 .   ? 30.731  63.459 12.734  1.00 20.85  ? 2034 HOH D O   1 
HETATM 12141 O O   . HOH HA 8 .   ? 29.399  55.268 13.139  1.00 7.95   ? 2035 HOH D O   1 
HETATM 12142 O O   . HOH HA 8 .   ? 38.757  56.137 1.333   1.00 13.33  ? 2036 HOH D O   1 
HETATM 12143 O O   . HOH HA 8 .   ? 25.676  63.821 3.171   1.00 18.52  ? 2037 HOH D O   1 
HETATM 12144 O O   . HOH HA 8 .   ? 29.203  55.198 -5.627  1.00 29.03  ? 2038 HOH D O   1 
HETATM 12145 O O   . HOH HA 8 .   ? 24.089  55.085 -5.748  1.00 17.80  ? 2039 HOH D O   1 
HETATM 12146 O O   . HOH HA 8 .   ? 45.152  53.787 -0.282  1.00 42.90  ? 2040 HOH D O   1 
HETATM 12147 O O   . HOH HA 8 .   ? 29.928  68.127 -17.623 1.00 47.10  ? 2041 HOH D O   1 
HETATM 12148 O O   . HOH IA 8 .   ? 11.123  58.476 -7.329  1.00 23.31  ? 2001 HOH E O   1 
HETATM 12149 O O   . HOH IA 8 .   ? 5.091   52.669 -9.820  1.00 22.48  ? 2002 HOH E O   1 
HETATM 12150 O O   . HOH IA 8 .   ? 9.282   57.060 -0.263  1.00 13.25  ? 2003 HOH E O   1 
HETATM 12151 O O   . HOH IA 8 .   ? 14.529  58.466 5.180   1.00 12.46  ? 2004 HOH E O   1 
HETATM 12152 O O   . HOH IA 8 .   ? 12.735  58.718 9.833   1.00 6.15   ? 2005 HOH E O   1 
HETATM 12153 O O   . HOH IA 8 .   ? 11.988  60.624 16.273  1.00 10.15  ? 2006 HOH E O   1 
HETATM 12154 O O   . HOH IA 8 .   ? 8.484   64.852 16.517  1.00 26.78  ? 2007 HOH E O   1 
HETATM 12155 O O   . HOH IA 8 .   ? 3.279   56.832 20.944  1.00 26.26  ? 2008 HOH E O   1 
HETATM 12156 O O   . HOH IA 8 .   ? 3.738   66.114 17.478  1.00 28.92  ? 2009 HOH E O   1 
HETATM 12157 O O   . HOH IA 8 .   ? 0.548   65.705 17.615  1.00 32.17  ? 2010 HOH E O   1 
HETATM 12158 O O   . HOH IA 8 .   ? 9.045   66.904 21.060  1.00 34.82  ? 2011 HOH E O   1 
HETATM 12159 O O   . HOH IA 8 .   ? 9.957   64.019 31.167  1.00 31.86  ? 2012 HOH E O   1 
HETATM 12160 O O   . HOH IA 8 .   ? 14.045  67.310 32.585  1.00 37.81  ? 2013 HOH E O   1 
HETATM 12161 O O   . HOH IA 8 .   ? 17.005  60.531 32.803  1.00 7.93   ? 2014 HOH E O   1 
HETATM 12162 O O   . HOH IA 8 .   ? 18.683  68.237 33.628  1.00 28.30  ? 2015 HOH E O   1 
HETATM 12163 O O   . HOH IA 8 .   ? 16.047  65.389 31.518  1.00 20.03  ? 2016 HOH E O   1 
HETATM 12164 O O   . HOH IA 8 .   ? 24.783  63.192 23.285  1.00 22.37  ? 2017 HOH E O   1 
HETATM 12165 O O   . HOH IA 8 .   ? 15.509  65.255 21.087  1.00 33.76  ? 2018 HOH E O   1 
HETATM 12166 O O   . HOH IA 8 .   ? 5.363   58.754 25.316  1.00 26.82  ? 2019 HOH E O   1 
HETATM 12167 O O   . HOH IA 8 .   ? 6.750   51.372 24.069  1.00 34.07  ? 2020 HOH E O   1 
HETATM 12168 O O   . HOH IA 8 .   ? 7.825   52.203 29.569  1.00 29.30  ? 2021 HOH E O   1 
HETATM 12169 O O   . HOH IA 8 .   ? 6.616   56.752 33.071  1.00 33.43  ? 2022 HOH E O   1 
HETATM 12170 O O   . HOH IA 8 .   ? 11.670  60.862 38.297  1.00 11.21  ? 2023 HOH E O   1 
HETATM 12171 O O   . HOH IA 8 .   ? 9.643   62.530 36.378  1.00 34.10  ? 2024 HOH E O   1 
HETATM 12172 O O   . HOH IA 8 .   ? 2.955   56.796 47.218  1.00 18.78  ? 2025 HOH E O   1 
HETATM 12173 O O   . HOH IA 8 .   ? -2.660  50.255 69.861  1.00 26.97  ? 2026 HOH E O   1 
HETATM 12174 O O   . HOH IA 8 .   ? -4.138  44.154 83.811  1.00 36.12  ? 2027 HOH E O   1 
HETATM 12175 O O   . HOH IA 8 .   ? 10.872  65.021 96.256  1.00 27.71  ? 2028 HOH E O   1 
HETATM 12176 O O   . HOH IA 8 .   ? 18.000  48.240 83.535  1.00 23.23  ? 2029 HOH E O   1 
HETATM 12177 O O   . HOH IA 8 .   ? 17.505  52.031 70.361  1.00 23.61  ? 2030 HOH E O   1 
HETATM 12178 O O   . HOH IA 8 .   ? 18.478  45.303 73.539  1.00 17.42  ? 2031 HOH E O   1 
HETATM 12179 O O   . HOH IA 8 .   ? 2.408   53.522 100.204 1.00 23.68  ? 2032 HOH E O   1 
HETATM 12180 O O   . HOH IA 8 .   ? -7.261  53.206 86.417  1.00 32.98  ? 2033 HOH E O   1 
HETATM 12181 O O   . HOH IA 8 .   ? -0.060  50.019 115.197 1.00 38.11  ? 2034 HOH E O   1 
HETATM 12182 O O   . HOH IA 8 .   ? 8.127   41.114 102.651 1.00 32.69  ? 2035 HOH E O   1 
HETATM 12183 O O   . HOH IA 8 .   ? 24.090  46.217 90.942  1.00 27.02  ? 2036 HOH E O   1 
HETATM 12184 O O   . HOH IA 8 .   ? 11.493  58.519 61.868  1.00 46.23  ? 2037 HOH E O   1 
HETATM 12185 O O   . HOH IA 8 .   ? -3.549  53.025 42.893  1.00 47.48  ? 2038 HOH E O   1 
HETATM 12186 O O   . HOH IA 8 .   ? 0.551   50.934 42.207  1.00 50.15  ? 2039 HOH E O   1 
HETATM 12187 O O   . HOH IA 8 .   ? 12.038  64.694 48.941  1.00 33.01  ? 2040 HOH E O   1 
HETATM 12188 O O   . HOH IA 8 .   ? 10.405  63.934 51.185  1.00 24.53  ? 2041 HOH E O   1 
HETATM 12189 O O   . HOH IA 8 .   ? 11.568  62.735 60.091  1.00 32.02  ? 2042 HOH E O   1 
HETATM 12190 O O   . HOH IA 8 .   ? 17.438  60.363 35.715  1.00 19.15  ? 2043 HOH E O   1 
HETATM 12191 O O   . HOH IA 8 .   ? 17.607  53.375 29.247  1.00 7.70   ? 2044 HOH E O   1 
HETATM 12192 O O   . HOH IA 8 .   ? 18.023  57.387 19.647  1.00 10.73  ? 2045 HOH E O   1 
HETATM 12193 O O   . HOH IA 8 .   ? 20.042  59.120 19.229  1.00 19.15  ? 2046 HOH E O   1 
HETATM 12194 O O   . HOH IA 8 .   ? 16.828  65.642 18.443  1.00 39.12  ? 2047 HOH E O   1 
HETATM 12195 O O   . HOH IA 8 .   ? 7.130   69.340 15.308  1.00 30.18  ? 2048 HOH E O   1 
HETATM 12196 O O   . HOH IA 8 .   ? -7.835  51.334 84.385  1.00 34.55  ? 2049 HOH E O   1 
HETATM 12197 O O   . HOH IA 8 .   ? -4.309  60.849 23.258  1.00 42.80  ? 2050 HOH E O   1 
HETATM 12198 O O   . HOH IA 8 .   ? 26.484  53.080 88.560  1.00 49.11  ? 2051 HOH E O   1 
HETATM 12199 O O   . HOH JA 8 .   ? 21.069  60.681 17.271  1.00 19.79  ? 2001 HOH F O   1 
HETATM 12200 O O   . HOH JA 8 .   ? 23.223  59.159 14.787  1.00 3.84   ? 2002 HOH F O   1 
HETATM 12201 O O   . HOH JA 8 .   ? 26.697  59.899 20.698  1.00 20.56  ? 2003 HOH F O   1 
HETATM 12202 O O   . HOH JA 8 .   ? 20.545  65.304 10.781  1.00 14.67  ? 2004 HOH F O   1 
HETATM 12203 O O   . HOH JA 8 .   ? 20.702  63.573 4.723   1.00 29.77  ? 2005 HOH F O   1 
HETATM 12204 O O   . HOH JA 8 .   ? 16.855  62.407 5.554   1.00 22.56  ? 2006 HOH F O   1 
HETATM 12205 O O   . HOH JA 8 .   ? 11.246  64.549 10.233  1.00 21.27  ? 2007 HOH F O   1 
HETATM 12206 O O   . HOH JA 8 .   ? 5.894   61.364 8.895   1.00 22.28  ? 2008 HOH F O   1 
HETATM 12207 O O   . HOH JA 8 .   ? 1.685   54.044 10.318  1.00 16.72  ? 2009 HOH F O   1 
HETATM 12208 O O   . HOH JA 8 .   ? 8.805   50.020 25.352  1.00 21.76  ? 2010 HOH F O   1 
HETATM 12209 O O   . HOH JA 8 .   ? 3.407   52.137 9.489   1.00 21.47  ? 2011 HOH F O   1 
HETATM 12210 O O   . HOH JA 8 .   ? 5.159   48.508 18.403  1.00 41.98  ? 2012 HOH F O   1 
HETATM 12211 O O   . HOH JA 8 .   ? 6.321   51.911 18.824  1.00 13.75  ? 2013 HOH F O   1 
HETATM 12212 O O   . HOH JA 8 .   ? 6.453   50.096 20.357  1.00 36.47  ? 2014 HOH F O   1 
HETATM 12213 O O   . HOH JA 8 .   ? 6.175   50.998 3.033   1.00 26.87  ? 2015 HOH F O   1 
HETATM 12214 O O   . HOH JA 8 .   ? 22.438  61.712 64.697  1.00 34.72  ? 2016 HOH F O   1 
HETATM 12215 O O   . HOH JA 8 .   ? 0.000   52.363 0.000   0.50 34.65  ? 2017 HOH F O   1 
HETATM 12216 O O   . HOH JA 8 .   ? 30.519  52.038 28.861  1.00 29.83  ? 2018 HOH F O   1 
HETATM 12217 O O   . HOH JA 8 .   ? 28.828  49.479 28.858  1.00 39.28  ? 2019 HOH F O   1 
HETATM 12218 O O   . HOH JA 8 .   ? 7.517   38.786 24.120  1.00 32.93  ? 2020 HOH F O   1 
HETATM 12219 O O   . HOH JA 8 .   ? 10.818  41.225 26.232  1.00 33.28  ? 2021 HOH F O   1 
HETATM 12220 O O   . HOH JA 8 .   ? 9.750   48.683 27.436  1.00 21.62  ? 2022 HOH F O   1 
HETATM 12221 O O   . HOH JA 8 .   ? 15.996  41.072 34.477  1.00 40.97  ? 2023 HOH F O   1 
HETATM 12222 O O   . HOH JA 8 .   ? 22.969  43.269 43.151  1.00 29.83  ? 2024 HOH F O   1 
HETATM 12223 O O   . HOH JA 8 .   ? 20.479  49.815 58.919  1.00 22.55  ? 2025 HOH F O   1 
HETATM 12224 O O   . HOH JA 8 .   ? 17.006  59.490 71.902  1.00 37.47  ? 2026 HOH F O   1 
HETATM 12225 O O   . HOH JA 8 .   ? 26.655  51.133 74.019  1.00 26.00  ? 2027 HOH F O   1 
HETATM 12226 O O   . HOH JA 8 .   ? 22.090  58.206 64.695  1.00 17.84  ? 2028 HOH F O   1 
HETATM 12227 O O   . HOH JA 8 .   ? 21.317  64.016 62.975  1.00 36.04  ? 2029 HOH F O   1 
HETATM 12228 O O   . HOH JA 8 .   ? 27.762  52.397 40.253  0.33 3.57   ? 2030 HOH F O   1 
HETATM 12229 O O   . HOH JA 8 .   ? 20.243  60.122 36.623  1.00 11.33  ? 2031 HOH F O   1 
HETATM 12230 O O   . HOH JA 8 .   ? 27.546  52.741 28.832  1.00 26.18  ? 2032 HOH F O   1 
HETATM 12231 O O   . HOH JA 8 .   ? 23.541  58.130 23.352  1.00 15.28  ? 2033 HOH F O   1 
HETATM 12232 O O   . HOH JA 8 .   ? 22.518  59.161 20.836  1.00 35.64  ? 2034 HOH F O   1 
HETATM 12233 O O   . HOH JA 8 .   ? 20.404  57.134 1.219   1.00 16.99  ? 2035 HOH F O   1 
HETATM 12234 O O   . HOH JA 8 .   ? 20.172  42.037 3.166   1.00 20.05  ? 2036 HOH F O   1 
HETATM 12235 O O   . HOH JA 8 .   ? 25.926  49.414 -5.547  1.00 29.81  ? 2037 HOH F O   1 
HETATM 12236 O O   . HOH JA 8 .   ? 26.243  56.324 -1.852  1.00 25.08  ? 2038 HOH F O   1 
HETATM 12237 O O   . HOH JA 8 .   ? 14.260  43.311 -17.594 1.00 41.55  ? 2039 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   ? 0.5448 0.3787 0.3809 0.2436  0.1211  -0.0449 1   ASP A N   
2     C CA  . ASP A 1   ? 0.5335 0.4151 0.3826 0.2598  0.1241  -0.0393 1   ASP A CA  
3     C C   . ASP A 1   ? 0.4782 0.3924 0.3765 0.2228  0.1222  -0.0358 1   ASP A C   
4     O O   . ASP A 1   ? 0.4396 0.3750 0.3705 0.1924  0.1213  -0.0358 1   ASP A O   
5     C CB  . ASP A 1   ? 0.5280 0.4886 0.3853 0.2889  0.1314  -0.0349 1   ASP A CB  
6     C CG  . ASP A 1   ? 0.5865 0.5188 0.3916 0.3322  0.1336  -0.0388 1   ASP A CG  
7     O OD1 . ASP A 1   ? 0.6345 0.4773 0.3936 0.3364  0.1286  -0.0449 1   ASP A OD1 
8     O OD2 . ASP A 1   ? 0.5890 0.5897 0.3957 0.3618  0.1399  -0.0353 1   ASP A OD2 
9     N N   . GLN A 2   ? 0.4803 0.3932 0.3782 0.2274  0.1211  -0.0330 2   GLN A N   
10    C CA  . GLN A 2   ? 0.4354 0.3726 0.3731 0.1960  0.1188  -0.0300 2   GLN A CA  
11    C C   . GLN A 2   ? 0.4304 0.4044 0.3753 0.2102  0.1204  -0.0245 2   GLN A C   
12    O O   . GLN A 2   ? 0.4701 0.4284 0.3813 0.2442  0.1217  -0.0242 2   GLN A O   
13    C CB  . GLN A 2   ? 0.4404 0.3151 0.3712 0.1708  0.1129  -0.0340 2   GLN A CB  
14    C CG  . GLN A 2   ? 0.4930 0.3026 0.3774 0.1860  0.1098  -0.0354 2   GLN A CG  
15    C CD  . GLN A 2   ? 0.4920 0.2590 0.3759 0.1547  0.1040  -0.0368 2   GLN A CD  
16    O OE1 . GLN A 2   ? 0.5152 0.2522 0.3792 0.1557  0.1014  -0.0352 2   GLN A OE1 
17    N NE2 . GLN A 2   ? 0.4671 0.2351 0.3712 0.1274  0.1018  -0.0396 2   GLN A NE2 
18    N N   . ILE A 3   ? 0.3862 0.4053 0.3704 0.1848  0.1196  -0.0204 3   ILE A N   
19    C CA  . ILE A 3   ? 0.3774 0.4270 0.3719 0.1900  0.1197  -0.0153 3   ILE A CA  
20    C C   . ILE A 3   ? 0.3549 0.3785 0.3670 0.1593  0.1149  -0.0162 3   ILE A C   
21    O O   . ILE A 3   ? 0.3294 0.3510 0.3611 0.1311  0.1121  -0.0180 3   ILE A O   
22    C CB  . ILE A 3   ? 0.3518 0.4906 0.3724 0.1897  0.1228  -0.0078 3   ILE A CB  
23    C CG1 . ILE A 3   ? 0.3511 0.5227 0.3758 0.2024  0.1231  -0.0023 3   ILE A CG1 
24    C CG2 . ILE A 3   ? 0.3146 0.4781 0.3658 0.1490  0.1197  -0.0059 3   ILE A CG2 
25    C CD1 . ILE A 3   ? 0.3423 0.6070 0.3798 0.2149  0.1268  0.0056  3   ILE A CD1 
26    N N   . CYS A 4   ? 0.3690 0.3714 0.3700 0.1678  0.1136  -0.0152 4   CYS A N   
27    C CA  . CYS A 4   ? 0.3526 0.3318 0.3666 0.1427  0.1095  -0.0159 4   CYS A CA  
28    C C   . CYS A 4   ? 0.3324 0.3521 0.3646 0.1420  0.1094  -0.0104 4   CYS A C   
29    O O   . CYS A 4   ? 0.3442 0.3953 0.3693 0.1664  0.1121  -0.0063 4   CYS A O   
30    C CB  . CYS A 4   ? 0.3914 0.3018 0.3718 0.1463  0.1069  -0.0192 4   CYS A CB  
31    S SG  . CYS A 4   ? 0.4269 0.2818 0.3758 0.1457  0.1055  -0.0251 4   CYS A SG  
32    N N   . ILE A 5   ? 0.3042 0.3246 0.3576 0.1160  0.1059  -0.0102 5   ILE A N   
33    C CA  . ILE A 5   ? 0.2897 0.3363 0.3559 0.1129  0.1047  -0.0056 5   ILE A CA  
34    C C   . ILE A 5   ? 0.3011 0.3019 0.3556 0.1103  0.1027  -0.0076 5   ILE A C   
35    O O   . ILE A 5   ? 0.3011 0.2675 0.3531 0.0950  0.1006  -0.0118 5   ILE A O   
36    C CB  . ILE A 5   ? 0.2587 0.3373 0.3499 0.0859  0.1012  -0.0035 5   ILE A CB  
37    C CG1 . ILE A 5   ? 0.2519 0.3714 0.3496 0.0813  0.1022  -0.0009 5   ILE A CG1 
38    C CG2 . ILE A 5   ? 0.2492 0.3542 0.3500 0.0823  0.0993  0.0016  5   ILE A CG2 
39    C CD1 . ILE A 5   ? 0.2555 0.4343 0.3551 0.0976  0.1055  0.0061  5   ILE A CD1 
40    N N   . GLY A 6   ? 0.3127 0.3173 0.3587 0.1250  0.1033  -0.0040 6   GLY A N   
41    C CA  . GLY A 6   ? 0.3299 0.2912 0.3597 0.1225  0.1013  -0.0047 6   GLY A CA  
42    C C   . GLY A 6   ? 0.3289 0.3100 0.3611 0.1319  0.1012  0.0000  6   GLY A C   
43    O O   . GLY A 6   ? 0.3143 0.3466 0.3616 0.1401  0.1024  0.0041  6   GLY A O   
44    N N   . TYR A 7   ? 0.3469 0.2894 0.3624 0.1289  0.0993  0.0001  7   TYR A N   
45    C CA  . TYR A 7   ? 0.3451 0.3014 0.3635 0.1341  0.0987  0.0043  7   TYR A CA  
46    C C   . TYR A 7   ? 0.3944 0.2980 0.3703 0.1501  0.0975  0.0051  7   TYR A C   
47    O O   . TYR A 7   ? 0.4295 0.2788 0.3727 0.1481  0.0960  0.0025  7   TYR A O   
48    C CB  . TYR A 7   ? 0.3114 0.2806 0.3570 0.1070  0.0964  0.0043  7   TYR A CB  
49    C CG  . TYR A 7   ? 0.3145 0.2473 0.3545 0.0868  0.0947  0.0007  7   TYR A CG  
50    C CD1 . TYR A 7   ? 0.2997 0.2330 0.3505 0.0729  0.0942  -0.0034 7   TYR A CD1 
51    C CD2 . TYR A 7   ? 0.3340 0.2370 0.3569 0.0806  0.0932  0.0022  7   TYR A CD2 
52    C CE1 . TYR A 7   ? 0.3027 0.2145 0.3493 0.0551  0.0925  -0.0059 7   TYR A CE1 
53    C CE2 . TYR A 7   ? 0.3378 0.2199 0.3559 0.0594  0.0915  0.0003  7   TYR A CE2 
54    C CZ  . TYR A 7   ? 0.3212 0.2112 0.3524 0.0475  0.0913  -0.0037 7   TYR A CZ  
55    O OH  . TYR A 7   ? 0.3255 0.2054 0.3525 0.0272  0.0895  -0.0049 7   TYR A OH  
56    N N   . HIS A 8   ? 0.4014 0.3191 0.3738 0.1644  0.0973  0.0092  8   HIS A N   
57    C CA  . HIS A 8   ? 0.4553 0.3226 0.3811 0.1843  0.0955  0.0108  8   HIS A CA  
58    C C   . HIS A 8   ? 0.4757 0.2879 0.3821 0.1587  0.0920  0.0104  8   HIS A C   
59    O O   . HIS A 8   ? 0.4389 0.2718 0.3769 0.1316  0.0918  0.0106  8   HIS A O   
60    C CB  . HIS A 8   ? 0.4484 0.3554 0.3829 0.2028  0.0959  0.0156  8   HIS A CB  
61    C CG  . HIS A 8   ? 0.5072 0.3648 0.3901 0.2296  0.0936  0.0174  8   HIS A CG  
62    N ND1 . HIS A 8   ? 0.5633 0.3874 0.3970 0.2666  0.0931  0.0162  8   HIS A ND1 
63    C CD2 . HIS A 8   ? 0.5241 0.3572 0.3916 0.2270  0.0910  0.0202  8   HIS A CD2 
64    C CE1 . HIS A 8   ? 0.6166 0.3917 0.4027 0.2861  0.0896  0.0181  8   HIS A CE1 
65    N NE2 . HIS A 8   ? 0.5923 0.3731 0.3996 0.2610  0.0884  0.0208  8   HIS A NE2 
66    N N   . ALA A 9   ? 0.5406 0.2822 0.3898 0.1672  0.0887  0.0101  9   ALA A N   
67    C CA  . ALA A 9   ? 0.5743 0.2627 0.3933 0.1436  0.0844  0.0121  9   ALA A CA  
68    C C   . ALA A 9   ? 0.6461 0.2762 0.4026 0.1707  0.0807  0.0147  9   ALA A C   
69    O O   . ALA A 9   ? 0.6723 0.3007 0.4067 0.2096  0.0815  0.0139  9   ALA A O   
70    C CB  . ALA A 9   ? 0.5941 0.2418 0.3938 0.1159  0.0816  0.0099  9   ALA A CB  
71    N N   . ASN A 10  ? 0.6816 0.2667 0.4074 0.1518  0.0763  0.0181  10  ASN A N   
72    C CA  . ASN A 10  ? 0.7624 0.2775 0.4173 0.1752  0.0711  0.0208  10  ASN A CA  
73    C C   . ASN A 10  ? 0.8116 0.2635 0.4233 0.1395  0.0648  0.0249  10  ASN A C   
74    O O   . ASN A 10  ? 0.7839 0.2514 0.4207 0.0979  0.0648  0.0257  10  ASN A O   
75    C CB  . ASN A 10  ? 0.7443 0.3039 0.4171 0.2096  0.0739  0.0229  10  ASN A CB  
76    C CG  . ASN A 10  ? 0.6898 0.2985 0.4118 0.1858  0.0759  0.0262  10  ASN A CG  
77    O OD1 . ASN A 10  ? 0.6728 0.2778 0.4089 0.1466  0.0751  0.0272  10  ASN A OD1 
78    N ND2 . ASN A 10  ? 0.6644 0.3232 0.4110 0.2103  0.0784  0.0281  10  ASN A ND2 
79    N N   . ASN A 11  ? 0.8897 0.2730 0.4337 0.1563  0.0590  0.0281  11  ASN A N   
80    C CA  . ASN A 11  ? 0.9523 0.2654 0.4411 0.1209  0.0515  0.0333  11  ASN A CA  
81    C C   . ASN A 11  ? 0.9151 0.2683 0.4386 0.1020  0.0534  0.0380  11  ASN A C   
82    O O   . ASN A 11  ? 0.9684 0.2669 0.4433 0.0764  0.0473  0.0434  11  ASN A O   
83    C CB  . ASN A 11  ? 1.0731 0.2713 0.4531 0.1462  0.0419  0.0343  11  ASN A CB  
84    C CG  . ASN A 11  ? 1.0940 0.2921 0.4561 0.1993  0.0426  0.0344  11  ASN A CG  
85    O OD1 . ASN A 11  ? 1.0208 0.3034 0.4511 0.2101  0.0495  0.0349  11  ASN A OD1 
86    N ND2 . ASN A 11  ? 1.2005 0.3011 0.4653 0.2339  0.0345  0.0339  11  ASN A ND2 
87    N N   . SER A 12  ? 0.8289 0.2744 0.4316 0.1127  0.0613  0.0364  12  SER A N   
88    C CA  . SER A 12  ? 0.7897 0.2781 0.4286 0.0990  0.0635  0.0401  12  SER A CA  
89    C C   . SER A 12  ? 0.7708 0.2731 0.4273 0.0483  0.0631  0.0430  12  SER A C   
90    O O   . SER A 12  ? 0.7424 0.2694 0.4250 0.0269  0.0647  0.0405  12  SER A O   
91    C CB  . SER A 12  ? 0.7059 0.2864 0.4208 0.1184  0.0706  0.0375  12  SER A CB  
92    O OG  . SER A 12  ? 0.6697 0.2887 0.4171 0.1055  0.0723  0.0407  12  SER A OG  
93    N N   . THR A 13  ? 0.7896 0.2797 0.4302 0.0308  0.0609  0.0486  13  THR A N   
94    C CA  . THR A 13  ? 0.7686 0.2876 0.4289 -0.0145 0.0612  0.0524  13  THR A CA  
95    C C   . THR A 13  ? 0.7039 0.2949 0.4231 -0.0132 0.0667  0.0530  13  THR A C   
96    O O   . THR A 13  ? 0.6870 0.3089 0.4224 -0.0446 0.0675  0.0564  13  THR A O   
97    C CB  . THR A 13  ? 0.8543 0.2964 0.4378 -0.0460 0.0530  0.0600  13  THR A CB  
98    O OG1 . THR A 13  ? 0.9044 0.2954 0.4425 -0.0219 0.0495  0.0628  13  THR A OG1 
99    C CG2 . THR A 13  ? 0.9219 0.2923 0.4441 -0.0597 0.0462  0.0599  13  THR A CG2 
100   N N   . GLU A 14  ? 0.6716 0.2920 0.4203 0.0224  0.0700  0.0501  14  GLU A N   
101   C CA  . GLU A 14  ? 0.6146 0.2981 0.4147 0.0245  0.0740  0.0503  14  GLU A CA  
102   C C   . GLU A 14  ? 0.5486 0.2981 0.4060 0.0070  0.0783  0.0468  14  GLU A C   
103   O O   . GLU A 14  ? 0.5251 0.2914 0.4033 0.0115  0.0798  0.0420  14  GLU A O   
104   C CB  . GLU A 14  ? 0.5962 0.3019 0.4146 0.0630  0.0756  0.0484  14  GLU A CB  
105   C CG  . GLU A 14  ? 0.6597 0.3106 0.4234 0.0876  0.0715  0.0520  14  GLU A CG  
106   C CD  . GLU A 14  ? 0.6365 0.3245 0.4234 0.1065  0.0727  0.0539  14  GLU A CD  
107   O OE1 . GLU A 14  ? 0.6109 0.3248 0.4206 0.0863  0.0739  0.0561  14  GLU A OE1 
108   O OE2 . GLU A 14  ? 0.6459 0.3412 0.4273 0.1420  0.0724  0.0533  14  GLU A OE2 
109   N N   . GLN A 15  ? 0.5235 0.3085 0.4021 -0.0105 0.0798  0.0490  15  GLN A N   
110   C CA  . GLN A 15  ? 0.4707 0.3154 0.3946 -0.0229 0.0830  0.0456  15  GLN A CA  
111   C C   . GLN A 15  ? 0.4255 0.3152 0.3867 -0.0087 0.0852  0.0438  15  GLN A C   
112   O O   . GLN A 15  ? 0.4354 0.3162 0.3874 -0.0005 0.0845  0.0471  15  GLN A O   
113   C CB  . GLN A 15  ? 0.4871 0.3411 0.3983 -0.0569 0.0825  0.0500  15  GLN A CB  
114   C CG  . GLN A 15  ? 0.5440 0.3460 0.4071 -0.0795 0.0783  0.0537  15  GLN A CG  
115   C CD  . GLN A 15  ? 0.5581 0.3831 0.4111 -0.1191 0.0773  0.0594  15  GLN A CD  
116   O OE1 . GLN A 15  ? 0.5740 0.3966 0.4150 -0.1410 0.0754  0.0600  15  GLN A OE1 
117   N NE2 . GLN A 15  ? 0.5544 0.4067 0.4117 -0.1294 0.0786  0.0640  15  GLN A NE2 
118   N N   . VAL A 16  ? 0.3807 0.3136 0.3785 -0.0058 0.0870  0.0385  16  VAL A N   
119   C CA  . VAL A 16  ? 0.3466 0.3156 0.3716 0.0044  0.0875  0.0364  16  VAL A CA  
120   C C   . VAL A 16  ? 0.3235 0.3318 0.3669 -0.0045 0.0887  0.0332  16  VAL A C   
121   O O   . VAL A 16  ? 0.3230 0.3382 0.3674 -0.0145 0.0894  0.0314  16  VAL A O   
122   C CB  . VAL A 16  ? 0.3251 0.3012 0.3675 0.0236  0.0863  0.0329  16  VAL A CB  
123   C CG1 . VAL A 16  ? 0.3480 0.2969 0.3725 0.0379  0.0853  0.0362  16  VAL A CG1 
124   C CG2 . VAL A 16  ? 0.3084 0.2939 0.3645 0.0231  0.0865  0.0277  16  VAL A CG2 
125   N N   . ASP A 17  ? 0.3082 0.3424 0.3628 0.0013  0.0887  0.0324  17  ASP A N   
126   C CA  . ASP A 17  ? 0.2908 0.3636 0.3583 0.0020  0.0894  0.0284  17  ASP A CA  
127   C C   . ASP A 17  ? 0.2722 0.3491 0.3518 0.0191  0.0865  0.0218  17  ASP A C   
128   O O   . ASP A 17  ? 0.2692 0.3296 0.3496 0.0274  0.0839  0.0219  17  ASP A O   
129   C CB  . ASP A 17  ? 0.2943 0.3912 0.3584 0.0000  0.0907  0.0314  17  ASP A CB  
130   C CG  . ASP A 17  ? 0.3169 0.4168 0.3652 -0.0233 0.0929  0.0387  17  ASP A CG  
131   O OD1 . ASP A 17  ? 0.3280 0.4268 0.3696 -0.0399 0.0933  0.0401  17  ASP A OD1 
132   O OD2 . ASP A 17  ? 0.3282 0.4303 0.3674 -0.0275 0.0935  0.0434  17  ASP A OD2 
133   N N   . THR A 18  ? 0.2642 0.3635 0.3492 0.0231  0.0863  0.0168  18  THR A N   
134   C CA  . THR A 18  ? 0.2584 0.3561 0.3437 0.0388  0.0821  0.0103  18  THR A CA  
135   C C   . THR A 18  ? 0.2625 0.3918 0.3426 0.0498  0.0821  0.0068  18  THR A C   
136   O O   . THR A 18  ? 0.2641 0.4247 0.3460 0.0430  0.0860  0.0101  18  THR A O   
137   C CB  . THR A 18  ? 0.2522 0.3389 0.3419 0.0385  0.0808  0.0064  18  THR A CB  
138   O OG1 . THR A 18  ? 0.2497 0.3601 0.3428 0.0336  0.0834  0.0049  18  THR A OG1 
139   C CG2 . THR A 18  ? 0.2518 0.3147 0.3449 0.0309  0.0817  0.0099  18  THR A CG2 
140   N N   . ILE A 19  ? 0.2708 0.3922 0.3397 0.0672  0.0771  0.0004  19  ILE A N   
141   C CA  . ILE A 19  ? 0.2825 0.4312 0.3390 0.0861  0.0762  -0.0040 19  ILE A CA  
142   C C   . ILE A 19  ? 0.2779 0.4686 0.3435 0.0849  0.0801  -0.0050 19  ILE A C   
143   O O   . ILE A 19  ? 0.2784 0.5168 0.3451 0.0888  0.0836  -0.0035 19  ILE A O   
144   C CB  . ILE A 19  ? 0.3036 0.4194 0.3334 0.1067  0.0680  -0.0112 19  ILE A CB  
145   C CG1 . ILE A 19  ? 0.3156 0.3948 0.3321 0.1044  0.0629  -0.0093 19  ILE A CG1 
146   C CG2 . ILE A 19  ? 0.3221 0.4627 0.3312 0.1340  0.0666  -0.0169 19  ILE A CG2 
147   C CD1 . ILE A 19  ? 0.3248 0.4174 0.3319 0.1136  0.0637  -0.0078 19  ILE A CD1 
148   N N   . MET A 20  ? 0.2748 0.4528 0.3467 0.0787  0.0794  -0.0071 20  MET A N   
149   C CA  . MET A 20  ? 0.2726 0.4888 0.3514 0.0779  0.0818  -0.0086 20  MET A CA  
150   C C   . MET A 20  ? 0.2682 0.5057 0.3619 0.0490  0.0869  -0.0013 20  MET A C   
151   O O   . MET A 20  ? 0.2657 0.5468 0.3643 0.0430  0.0889  -0.0006 20  MET A O   
152   C CB  . MET A 20  ? 0.2731 0.4621 0.3475 0.0847  0.0778  -0.0144 20  MET A CB  
153   C CG  . MET A 20  ? 0.2934 0.4575 0.3412 0.1121  0.0708  -0.0220 20  MET A CG  
154   S SD  . MET A 20  ? 0.2987 0.4396 0.3385 0.1179  0.0664  -0.0282 20  MET A SD  
155   C CE  . MET A 20  ? 0.3401 0.4392 0.3329 0.1494  0.0562  -0.0361 20  MET A CE  
156   N N   . GLU A 21  ? 0.2746 0.4798 0.3705 0.0312  0.0881  0.0041  21  GLU A N   
157   C CA  . GLU A 21  ? 0.2854 0.4915 0.3825 0.0035  0.0910  0.0108  21  GLU A CA  
158   C C   . GLU A 21  ? 0.3028 0.4831 0.3921 -0.0086 0.0921  0.0175  21  GLU A C   
159   O O   . GLU A 21  ? 0.3019 0.4481 0.3900 0.0015  0.0905  0.0167  21  GLU A O   
160   C CB  . GLU A 21  ? 0.2847 0.4592 0.3833 -0.0028 0.0899  0.0088  21  GLU A CB  
161   C CG  . GLU A 21  ? 0.2979 0.4784 0.3904 -0.0298 0.0912  0.0140  21  GLU A CG  
162   C CD  . GLU A 21  ? 0.3007 0.4474 0.3917 -0.0331 0.0899  0.0114  21  GLU A CD  
163   O OE1 . GLU A 21  ? 0.2880 0.4198 0.3870 -0.0145 0.0884  0.0053  21  GLU A OE1 
164   O OE2 . GLU A 21  ? 0.3200 0.4524 0.3975 -0.0559 0.0896  0.0158  21  GLU A OE2 
165   N N   . LYS A 22  ? 0.3255 0.5234 0.4064 -0.0321 0.0941  0.0247  22  LYS A N   
166   C CA  . LYS A 22  ? 0.3520 0.5213 0.4179 -0.0455 0.0944  0.0317  22  LYS A CA  
167   C C   . LYS A 22  ? 0.3876 0.5136 0.4328 -0.0682 0.0930  0.0364  22  LYS A C   
168   O O   . LYS A 22  ? 0.3925 0.5260 0.4351 -0.0819 0.0924  0.0362  22  LYS A O   
169   C CB  . LYS A 22  ? 0.3583 0.5736 0.4203 -0.0571 0.0966  0.0373  22  LYS A CB  
170   C CG  . LYS A 22  ? 0.3464 0.5755 0.4152 -0.0341 0.0972  0.0348  22  LYS A CG  
171   C CD  . LYS A 22  ? 0.3337 0.6259 0.4122 -0.0170 0.0987  0.0308  22  LYS A CD  
172   C CE  . LYS A 22  ? 0.3209 0.6010 0.4045 0.0167  0.0958  0.0208  22  LYS A CE  
173   N NZ  . LYS A 22  ? 0.3226 0.5728 0.4001 0.0337  0.0935  0.0190  22  LYS A NZ  
174   N N   . ASN A 23  ? 0.4231 0.5011 0.4490 -0.0701 0.0919  0.0404  23  ASN A N   
175   C CA  . ASN A 23  ? 0.4740 0.4975 0.4669 -0.0872 0.0893  0.0450  23  ASN A CA  
176   C C   . ASN A 23  ? 0.4557 0.4540 0.4503 -0.0792 0.0882  0.0399  23  ASN A C   
177   O O   . ASN A 23  ? 0.4815 0.4581 0.4535 -0.0988 0.0860  0.0422  23  ASN A O   
178   C CB  . ASN A 23  ? 0.5330 0.5665 0.5000 -0.1245 0.0880  0.0531  23  ASN A CB  
179   C CG  . ASN A 23  ? 0.5816 0.6309 0.5391 -0.1351 0.0887  0.0596  23  ASN A CG  
180   O OD1 . ASN A 23  ? 0.5814 0.6121 0.5410 -0.1159 0.0893  0.0590  23  ASN A OD1 
181   N ND2 . ASN A 23  ? 0.6489 0.7369 0.5955 -0.1675 0.0886  0.0666  23  ASN A ND2 
182   N N   . VAL A 24  ? 0.4116 0.4120 0.4295 -0.0523 0.0890  0.0336  24  VAL A N   
183   C CA  . VAL A 24  ? 0.3975 0.3768 0.4184 -0.0420 0.0883  0.0290  24  VAL A CA  
184   C C   . VAL A 24  ? 0.4221 0.3461 0.4150 -0.0335 0.0867  0.0315  24  VAL A C   
185   O O   . VAL A 24  ? 0.4186 0.3355 0.4129 -0.0166 0.0868  0.0324  24  VAL A O   
186   C CB  . VAL A 24  ? 0.3579 0.3623 0.4099 -0.0199 0.0889  0.0224  24  VAL A CB  
187   C CG1 . VAL A 24  ? 0.3546 0.3394 0.4087 -0.0106 0.0884  0.0187  24  VAL A CG1 
188   C CG2 . VAL A 24  ? 0.3349 0.3863 0.4054 -0.0211 0.0895  0.0188  24  VAL A CG2 
189   N N   . THR A 25  ? 0.4475 0.3326 0.4114 -0.0430 0.0848  0.0325  25  THR A N   
190   C CA  . THR A 25  ? 0.4830 0.3101 0.4104 -0.0293 0.0826  0.0343  25  THR A CA  
191   C C   . THR A 25  ? 0.4534 0.2893 0.4018 0.0000  0.0843  0.0294  25  THR A C   
192   O O   . THR A 25  ? 0.4279 0.2834 0.3977 0.0012  0.0854  0.0247  25  THR A O   
193   C CB  . THR A 25  ? 0.5360 0.3103 0.4168 -0.0470 0.0787  0.0364  25  THR A CB  
194   O OG1 . THR A 25  ? 0.5542 0.3354 0.4204 -0.0829 0.0767  0.0416  25  THR A OG1 
195   C CG2 . THR A 25  ? 0.5959 0.2998 0.4233 -0.0312 0.0750  0.0391  25  THR A CG2 
196   N N   . VAL A 26  ? 0.4572 0.2816 0.3977 0.0224  0.0841  0.0310  26  VAL A N   
197   C CA  . VAL A 26  ? 0.4314 0.2757 0.3914 0.0484  0.0855  0.0281  26  VAL A CA  
198   C C   . VAL A 26  ? 0.4744 0.2775 0.3953 0.0729  0.0841  0.0298  26  VAL A C   
199   O O   . VAL A 26  ? 0.5232 0.2791 0.4011 0.0736  0.0813  0.0335  26  VAL A O   
200   C CB  . VAL A 26  ? 0.3916 0.2815 0.3856 0.0559  0.0864  0.0285  26  VAL A CB  
201   C CG1 . VAL A 26  ? 0.3517 0.2783 0.3783 0.0398  0.0871  0.0253  26  VAL A CG1 
202   C CG2 . VAL A 26  ? 0.4121 0.2886 0.3886 0.0592  0.0853  0.0333  26  VAL A CG2 
203   N N   . THR A 27  ? 0.4600 0.2813 0.3920 0.0942  0.0855  0.0273  27  THR A N   
204   C CA  . THR A 27  ? 0.5022 0.2928 0.3966 0.1249  0.0846  0.0281  27  THR A CA  
205   C C   . THR A 27  ? 0.5106 0.3121 0.3980 0.1474  0.0839  0.0320  27  THR A C   
206   O O   . THR A 27  ? 0.5668 0.3232 0.4057 0.1704  0.0814  0.0339  27  THR A O   
207   C CB  . THR A 27  ? 0.4834 0.3040 0.3949 0.1422  0.0870  0.0249  27  THR A CB  
208   O OG1 . THR A 27  ? 0.4308 0.3199 0.3896 0.1440  0.0890  0.0255  27  THR A OG1 
209   C CG2 . THR A 27  ? 0.4756 0.2839 0.3923 0.1219  0.0874  0.0208  27  THR A CG2 
210   N N   . HIS A 28  ? 0.4601 0.3182 0.3912 0.1418  0.0853  0.0332  28  HIS A N   
211   C CA  . HIS A 28  ? 0.4621 0.3394 0.3922 0.1595  0.0843  0.0373  28  HIS A CA  
212   C C   . HIS A 28  ? 0.4251 0.3299 0.3862 0.1367  0.0841  0.0386  28  HIS A C   
213   O O   . HIS A 28  ? 0.3865 0.3176 0.3802 0.1157  0.0850  0.0360  28  HIS A O   
214   C CB  . HIS A 28  ? 0.4439 0.3764 0.3927 0.1846  0.0855  0.0383  28  HIS A CB  
215   C CG  . HIS A 28  ? 0.4770 0.3925 0.3976 0.2114  0.0864  0.0365  28  HIS A CG  
216   N ND1 . HIS A 28  ? 0.4647 0.3805 0.3949 0.2027  0.0882  0.0326  28  HIS A ND1 
217   C CD2 . HIS A 28  ? 0.5262 0.4215 0.4047 0.2499  0.0854  0.0379  28  HIS A CD2 
218   C CE1 . HIS A 28  ? 0.5038 0.4010 0.4004 0.2334  0.0885  0.0316  28  HIS A CE1 
219   N NE2 . HIS A 28  ? 0.5434 0.4274 0.4065 0.2641  0.0867  0.0346  28  HIS A NE2 
220   N N   . ALA A 29  ? 0.4421 0.3379 0.3885 0.1438  0.0825  0.0425  29  ALA A N   
221   C CA  . ALA A 29  ? 0.4141 0.3322 0.3838 0.1258  0.0820  0.0440  29  ALA A CA  
222   C C   . ALA A 29  ? 0.4251 0.3559 0.3873 0.1449  0.0802  0.0485  29  ALA A C   
223   O O   . ALA A 29  ? 0.4589 0.3775 0.3938 0.1730  0.0793  0.0504  29  ALA A O   
224   C CB  . ALA A 29  ? 0.4304 0.3108 0.3835 0.1020  0.0819  0.0442  29  ALA A CB  
225   N N   . GLN A 30  ? 0.3997 0.3560 0.3836 0.1323  0.0794  0.0500  30  GLN A N   
226   C CA  . GLN A 30  ? 0.4088 0.3789 0.3868 0.1474  0.0773  0.0545  30  GLN A CA  
227   C C   . GLN A 30  ? 0.4041 0.3640 0.3832 0.1296  0.0766  0.0560  30  GLN A C   
228   O O   . GLN A 30  ? 0.3696 0.3566 0.3767 0.1119  0.0764  0.0543  30  GLN A O   
229   C CB  . GLN A 30  ? 0.3782 0.4118 0.3862 0.1545  0.0758  0.0561  30  GLN A CB  
230   C CG  . GLN A 30  ? 0.3900 0.4454 0.3909 0.1727  0.0732  0.0614  30  GLN A CG  
231   C CD  . GLN A 30  ? 0.3683 0.4932 0.3925 0.1805  0.0712  0.0646  30  GLN A CD  
232   O OE1 . GLN A 30  ? 0.3566 0.5088 0.3932 0.1812  0.0722  0.0635  30  GLN A OE1 
233   N NE2 . GLN A 30  ? 0.3653 0.5222 0.3943 0.1842  0.0679  0.0693  30  GLN A NE2 
234   N N   . ASP A 31  ? 0.4442 0.3614 0.3874 0.1355  0.0757  0.0591  31  ASP A N   
235   C CA  . ASP A 31  ? 0.4445 0.3551 0.3853 0.1216  0.0751  0.0617  31  ASP A CA  
236   C C   . ASP A 31  ? 0.4237 0.3758 0.3835 0.1327  0.0729  0.0641  31  ASP A C   
237   O O   . ASP A 31  ? 0.4361 0.4014 0.3877 0.1575  0.0711  0.0666  31  ASP A O   
238   C CB  . ASP A 31  ? 0.5021 0.3514 0.3920 0.1235  0.0736  0.0654  31  ASP A CB  
239   C CG  . ASP A 31  ? 0.5041 0.3456 0.3905 0.1004  0.0739  0.0682  31  ASP A CG  
240   O OD1 . ASP A 31  ? 0.4635 0.3477 0.3848 0.0919  0.0749  0.0672  31  ASP A OD1 
241   O OD2 . ASP A 31  ? 0.5518 0.3422 0.3958 0.0900  0.0724  0.0716  31  ASP A OD2 
242   N N   . ILE A 32  ? 0.3944 0.3694 0.3772 0.1152  0.0726  0.0636  32  ILE A N   
243   C CA  . ILE A 32  ? 0.3773 0.3885 0.3755 0.1198  0.0694  0.0660  32  ILE A CA  
244   C C   . ILE A 32  ? 0.3876 0.3848 0.3749 0.1135  0.0688  0.0687  32  ILE A C   
245   O O   . ILE A 32  ? 0.3760 0.3988 0.3735 0.1145  0.0657  0.0707  32  ILE A O   
246   C CB  . ILE A 32  ? 0.3396 0.3891 0.3690 0.1058  0.0675  0.0630  32  ILE A CB  
247   C CG1 . ILE A 32  ? 0.3266 0.3634 0.3629 0.0866  0.0696  0.0582  32  ILE A CG1 
248   C CG2 . ILE A 32  ? 0.3305 0.4034 0.3704 0.1128  0.0673  0.0621  32  ILE A CG2 
249   C CD1 . ILE A 32  ? 0.3040 0.3638 0.3568 0.0752  0.0657  0.0552  32  ILE A CD1 
250   N N   . LEU A 33  ? 0.4122 0.3699 0.3763 0.1049  0.0712  0.0695  33  LEU A N   
251   C CA  . LEU A 33  ? 0.4251 0.3699 0.3763 0.0964  0.0712  0.0726  33  LEU A CA  
252   C C   . LEU A 33  ? 0.4756 0.3764 0.3844 0.1089  0.0695  0.0777  33  LEU A C   
253   O O   . LEU A 33  ? 0.5119 0.3690 0.3889 0.1067  0.0699  0.0786  33  LEU A O   
254   C CB  . LEU A 33  ? 0.4194 0.3589 0.3728 0.0724  0.0746  0.0709  33  LEU A CB  
255   C CG  . LEU A 33  ? 0.4284 0.3658 0.3720 0.0603  0.0754  0.0742  33  LEU A CG  
256   C CD1 . LEU A 33  ? 0.4002 0.3720 0.3668 0.0650  0.0737  0.0726  33  LEU A CD1 
257   C CD2 . LEU A 33  ? 0.4285 0.3688 0.3707 0.0374  0.0791  0.0737  33  LEU A CD2 
258   N N   . GLU A 34  ? 0.4841 0.3915 0.3867 0.1215  0.0668  0.0813  34  GLU A N   
259   C CA  . GLU A 34  ? 0.5380 0.3984 0.3942 0.1343  0.0644  0.0862  34  GLU A CA  
260   C C   . GLU A 34  ? 0.5599 0.3889 0.3944 0.1091  0.0657  0.0893  34  GLU A C   
261   O O   . GLU A 34  ? 0.5356 0.3914 0.3901 0.0968  0.0669  0.0898  34  GLU A O   
262   C CB  . GLU A 34  ? 0.5394 0.4230 0.3968 0.1578  0.0608  0.0892  34  GLU A CB  
263   C CG  . GLU A 34  ? 0.6009 0.4324 0.4047 0.1764  0.0575  0.0940  34  GLU A CG  
264   C CD  . GLU A 34  ? 0.6546 0.4282 0.4113 0.1898  0.0562  0.0938  34  GLU A CD  
265   O OE1 . GLU A 34  ? 0.6530 0.4437 0.4137 0.2145  0.0557  0.0915  34  GLU A OE1 
266   O OE2 . GLU A 34  ? 0.7020 0.4129 0.4146 0.1737  0.0552  0.0961  34  GLU A OE2 
267   N N   . LYS A 35  ? 0.6110 0.3828 0.4003 0.1005  0.0648  0.0917  35  LYS A N   
268   C CA  . LYS A 35  ? 0.6365 0.3823 0.4017 0.0693  0.0657  0.0959  35  LYS A CA  
269   C C   . LYS A 35  ? 0.7008 0.3898 0.4091 0.0723  0.0612  0.1027  35  LYS A C   
270   O O   . LYS A 35  ? 0.7199 0.3964 0.4101 0.0448  0.0616  0.1075  35  LYS A O   
271   C CB  . LYS A 35  ? 0.6536 0.3754 0.4032 0.0458  0.0667  0.0954  35  LYS A CB  
272   C CG  . LYS A 35  ? 0.5948 0.3750 0.3959 0.0277  0.0719  0.0908  35  LYS A CG  
273   C CD  . LYS A 35  ? 0.6110 0.3714 0.3980 0.0083  0.0724  0.0900  35  LYS A CD  
274   C CE  . LYS A 35  ? 0.5820 0.3577 0.3954 0.0266  0.0733  0.0834  35  LYS A CE  
275   N NZ  . LYS A 35  ? 0.5986 0.3529 0.3984 0.0615  0.0702  0.0823  35  LYS A NZ  
276   N N   . THR A 36  ? 0.7361 0.3946 0.4147 0.1063  0.0567  0.1033  36  THR A N   
277   C CA  . THR A 36  ? 0.8112 0.4015 0.4229 0.1141  0.0510  0.1093  36  THR A CA  
278   C C   . THR A 36  ? 0.8054 0.4171 0.4239 0.1407  0.0490  0.1109  36  THR A C   
279   O O   . THR A 36  ? 0.7529 0.4271 0.4203 0.1605  0.0506  0.1075  36  THR A O   
280   C CB  . THR A 36  ? 0.8847 0.3999 0.4310 0.1367  0.0452  0.1093  36  THR A CB  
281   O OG1 . THR A 36  ? 0.8632 0.4116 0.4309 0.1796  0.0452  0.1048  36  THR A OG1 
282   C CG2 . THR A 36  ? 0.9018 0.3861 0.4317 0.1077  0.0457  0.1084  36  THR A CG2 
283   N N   . HIS A 37  ? 0.8650 0.4225 0.4299 0.1378  0.0447  0.1169  37  HIS A N   
284   C CA  . HIS A 37  ? 0.8778 0.4392 0.4326 0.1650  0.0414  0.1194  37  HIS A CA  
285   C C   . HIS A 37  ? 0.9799 0.4429 0.4428 0.1753  0.0337  0.1248  37  HIS A C   
286   O O   . HIS A 37  ? 1.0348 0.4316 0.4468 0.1499  0.0313  0.1275  37  HIS A O   
287   C CB  . HIS A 37  ? 0.8311 0.4414 0.4266 0.1422  0.0450  0.1213  37  HIS A CB  
288   C CG  . HIS A 37  ? 0.8565 0.4363 0.4270 0.1003  0.0464  0.1262  37  HIS A CG  
289   N ND1 . HIS A 37  ? 0.9115 0.4441 0.4318 0.0921  0.0426  0.1330  37  HIS A ND1 
290   C CD2 . HIS A 37  ? 0.8366 0.4317 0.4238 0.0635  0.0509  0.1260  37  HIS A CD2 
291   C CE1 . HIS A 37  ? 0.9238 0.4469 0.4317 0.0493  0.0448  0.1374  37  HIS A CE1 
292   N NE2 . HIS A 37  ? 0.8782 0.4420 0.4271 0.0322  0.0499  0.1332  37  HIS A NE2 
293   N N   . ASN A 38  ? 1.0114 0.4618 0.4478 0.2112  0.0290  0.1267  38  ASN A N   
294   C CA  . ASN A 38  ? 1.1192 0.4669 0.4581 0.2273  0.0202  0.1315  38  ASN A CA  
295   C C   . ASN A 38  ? 1.1611 0.4613 0.4604 0.1898  0.0180  0.1388  38  ASN A C   
296   O O   . ASN A 38  ? 1.2597 0.4599 0.4687 0.1866  0.0100  0.1436  38  ASN A O   
297   C CB  . ASN A 38  ? 1.1465 0.4964 0.4631 0.2868  0.0151  0.1307  38  ASN A CB  
298   C CG  . ASN A 38  ? 1.0933 0.5141 0.4591 0.2944  0.0169  0.1322  38  ASN A CG  
299   O OD1 . ASN A 38  ? 1.0509 0.5015 0.4532 0.2573  0.0210  0.1343  38  ASN A OD1 
300   N ND2 . ASN A 38  ? 1.0985 0.5493 0.4628 0.3441  0.0136  0.1314  38  ASN A ND2 
301   N N   . GLY A 39  ? 1.0922 0.4617 0.4538 0.1623  0.0243  0.1397  39  GLY A N   
302   C CA  . GLY A 39  ? 1.1196 0.4629 0.4551 0.1226  0.0240  0.1469  39  GLY A CA  
303   C C   . GLY A 39  ? 1.1451 0.4767 0.4582 0.1426  0.0201  0.1508  39  GLY A C   
304   O O   . GLY A 39  ? 1.1875 0.4804 0.4607 0.1148  0.0180  0.1577  39  GLY A O   
305   N N   . LYS A 40  ? 1.1190 0.4897 0.4584 0.1889  0.0191  0.1469  40  LYS A N   
306   C CA  . LYS A 40  ? 1.1518 0.5080 0.4629 0.2170  0.0139  0.1502  40  LYS A CA  
307   C C   . LYS A 40  ? 1.0670 0.5231 0.4569 0.2313  0.0180  0.1473  40  LYS A C   
308   O O   . LYS A 40  ? 0.9963 0.5247 0.4516 0.2356  0.0226  0.1419  40  LYS A O   
309   C CB  . LYS A 40  ? 1.2315 0.5228 0.4722 0.2681  0.0053  0.1497  40  LYS A CB  
310   C CG  . LYS A 40  ? 1.3471 0.5118 0.4809 0.2577  -0.0027 0.1543  40  LYS A CG  
311   C CD  . LYS A 40  ? 1.4100 0.5201 0.4881 0.3035  -0.0089 0.1505  40  LYS A CD  
312   C CE  . LYS A 40  ? 1.5438 0.5108 0.4981 0.2964  -0.0197 0.1553  40  LYS A CE  
313   N NZ  . LYS A 40  ? 1.6099 0.5172 0.5048 0.3398  -0.0258 0.1508  40  LYS A NZ  
314   N N   . LEU A 41  ? 1.0813 0.5360 0.4588 0.2366  0.0154  0.1514  41  LEU A N   
315   C CA  . LEU A 41  ? 1.0191 0.5559 0.4550 0.2538  0.0165  0.1498  41  LEU A CA  
316   C C   . LEU A 41  ? 1.0511 0.5889 0.4621 0.3087  0.0098  0.1494  41  LEU A C   
317   O O   . LEU A 41  ? 1.1333 0.5989 0.4699 0.3334  0.0029  0.1530  41  LEU A O   
318   C CB  . LEU A 41  ? 1.0205 0.5562 0.4532 0.2329  0.0168  0.1545  41  LEU A CB  
319   C CG  . LEU A 41  ? 0.9744 0.5394 0.4457 0.1846  0.0243  0.1546  41  LEU A CG  
320   C CD1 . LEU A 41  ? 0.9040 0.5481 0.4385 0.1830  0.0270  0.1522  41  LEU A CD1 
321   C CD2 . LEU A 41  ? 0.9459 0.5219 0.4421 0.1600  0.0298  0.1508  41  LEU A CD2 
322   N N   . CYS A 42  ? 0.9905 0.6113 0.4597 0.3277  0.0113  0.1454  42  CYS A N   
323   C CA  . CYS A 42  ? 1.0149 0.6544 0.4670 0.3803  0.0062  0.1448  42  CYS A CA  
324   C C   . CYS A 42  ? 0.9647 0.6977 0.4660 0.3977  0.0043  0.1459  42  CYS A C   
325   O O   . CYS A 42  ? 0.9017 0.6895 0.4588 0.3669  0.0073  0.1456  42  CYS A O   
326   C CB  . CYS A 42  ? 0.9974 0.6557 0.4670 0.3894  0.0089  0.1400  42  CYS A CB  
327   S SG  . CYS A 42  ? 1.0673 0.6175 0.4707 0.3790  0.0089  0.1385  42  CYS A SG  
328   N N   . ASP A 43  ? 0.9986 0.7495 0.4741 0.4485  -0.0012 0.1473  43  ASP A N   
329   C CA  . ASP A 43  ? 0.9523 0.8066 0.4751 0.4669  -0.0037 0.1489  43  ASP A CA  
330   C C   . ASP A 43  ? 0.8777 0.8144 0.4699 0.4475  0.0006  0.1457  43  ASP A C   
331   O O   . ASP A 43  ? 0.8816 0.8049 0.4702 0.4529  0.0035  0.1423  43  ASP A O   
332   C CB  . ASP A 43  ? 1.0091 0.8721 0.4860 0.5305  -0.0104 0.1511  43  ASP A CB  
333   C CG  . ASP A 43  ? 1.0879 0.8730 0.4920 0.5543  -0.0165 0.1548  43  ASP A CG  
334   O OD1 . ASP A 43  ? 1.0939 0.8257 0.4876 0.5183  -0.0154 0.1563  43  ASP A OD1 
335   O OD2 . ASP A 43  ? 1.1477 0.9254 0.5016 0.6110  -0.0227 0.1562  43  ASP A OD2 
336   N N   . LEU A 44  ? 0.8159 0.8320 0.4658 0.4237  0.0003  0.1470  44  LEU A N   
337   C CA  . LEU A 44  ? 0.7520 0.8456 0.4620 0.4026  0.0025  0.1449  44  LEU A CA  
338   C C   . LEU A 44  ? 0.7420 0.9317 0.4698 0.4334  -0.0025 0.1489  44  LEU A C   
339   O O   . LEU A 44  ? 0.7384 0.9750 0.4730 0.4389  -0.0079 0.1536  44  LEU A O   
340   C CB  . LEU A 44  ? 0.6985 0.8131 0.4526 0.3534  0.0038  0.1440  44  LEU A CB  
341   C CG  . LEU A 44  ? 0.6418 0.8102 0.4467 0.3242  0.0058  0.1410  44  LEU A CG  
342   C CD1 . LEU A 44  ? 0.6392 0.7532 0.4420 0.3080  0.0129  0.1354  44  LEU A CD1 
343   C CD2 . LEU A 44  ? 0.6025 0.8042 0.4402 0.2872  0.0030  0.1415  44  LEU A CD2 
344   N N   . ASP A 45  ? 0.7385 0.9623 0.4734 0.4526  -0.0009 0.1474  45  ASP A N   
345   C CA  . ASP A 45  ? 0.7294 1.0566 0.4813 0.4829  -0.0051 0.1519  45  ASP A CA  
346   C C   . ASP A 45  ? 0.7839 1.1138 0.4903 0.5360  -0.0107 0.1561  45  ASP A C   
347   O O   . ASP A 45  ? 0.7713 1.1962 0.4958 0.5518  -0.0159 0.1618  45  ASP A O   
348   C CB  . ASP A 45  ? 0.6681 1.0884 0.4785 0.4417  -0.0083 0.1556  45  ASP A CB  
349   C CG  . ASP A 45  ? 0.6452 1.1793 0.4848 0.4542  -0.0107 0.1598  45  ASP A CG  
350   O OD1 . ASP A 45  ? 0.6285 1.1714 0.4834 0.4476  -0.0064 0.1568  45  ASP A OD1 
351   O OD2 . ASP A 45  ? 0.6444 1.2635 0.4916 0.4688  -0.0170 0.1667  45  ASP A OD2 
352   N N   . GLY A 46  ? 0.8488 1.0727 0.4918 0.5616  -0.0104 0.1537  46  GLY A N   
353   C CA  . GLY A 46  ? 0.9136 1.1157 0.5000 0.6129  -0.0165 0.1570  46  GLY A CA  
354   C C   . GLY A 46  ? 0.9139 1.0962 0.4969 0.5936  -0.0200 0.1603  46  GLY A C   
355   O O   . GLY A 46  ? 0.9781 1.1062 0.5028 0.6287  -0.0245 0.1621  46  GLY A O   
356   N N   . VAL A 47  ? 0.8477 1.0683 0.4876 0.5394  -0.0183 0.1609  47  VAL A N   
357   C CA  . VAL A 47  ? 0.8405 1.0567 0.4843 0.5189  -0.0217 0.1642  47  VAL A CA  
358   C C   . VAL A 47  ? 0.8633 0.9672 0.4777 0.4911  -0.0178 0.1612  47  VAL A C   
359   O O   . VAL A 47  ? 0.8303 0.9091 0.4695 0.4506  -0.0119 0.1573  47  VAL A O   
360   C CB  . VAL A 47  ? 0.7682 1.0735 0.4783 0.4742  -0.0233 0.1663  47  VAL A CB  
361   C CG1 . VAL A 47  ? 0.7668 1.0640 0.4760 0.4555  -0.0273 0.1694  47  VAL A CG1 
362   C CG2 . VAL A 47  ? 0.7453 1.1709 0.4850 0.4931  -0.0277 0.1709  47  VAL A CG2 
363   N N   . LYS A 48  ? 0.9213 0.9629 0.4815 0.5126  -0.0214 0.1637  48  LYS A N   
364   C CA  . LYS A 48  ? 0.9578 0.8909 0.4776 0.4897  -0.0185 0.1625  48  LYS A CA  
365   C C   . LYS A 48  ? 0.9043 0.8469 0.4672 0.4356  -0.0149 0.1622  48  LYS A C   
366   O O   . LYS A 48  ? 0.8686 0.8752 0.4656 0.4269  -0.0181 0.1646  48  LYS A O   
367   C CB  . LYS A 48  ? 1.0397 0.9064 0.4858 0.5265  -0.0248 0.1663  48  LYS A CB  
368   C CG  . LYS A 48  ? 1.1077 0.8478 0.4865 0.5153  -0.0236 0.1659  48  LYS A CG  
369   C CD  . LYS A 48  ? 1.1624 0.8429 0.4897 0.5191  -0.0285 0.1705  48  LYS A CD  
370   C CE  . LYS A 48  ? 1.2381 0.7928 0.4914 0.5035  -0.0286 0.1714  48  LYS A CE  
371   N NZ  . LYS A 48  ? 1.2593 0.7686 0.4897 0.4752  -0.0294 0.1760  48  LYS A NZ  
372   N N   . PRO A 49  ? 0.9021 0.7830 0.4604 0.3999  -0.0087 0.1593  49  PRO A N   
373   C CA  . PRO A 49  ? 0.8637 0.7478 0.4516 0.3562  -0.0053 0.1591  49  PRO A CA  
374   C C   . PRO A 49  ? 0.9037 0.7459 0.4533 0.3584  -0.0084 0.1636  49  PRO A C   
375   O O   . PRO A 49  ? 0.9731 0.7504 0.4604 0.3839  -0.0118 0.1665  49  PRO A O   
376   C CB  . PRO A 49  ? 0.8619 0.6940 0.4464 0.3249  0.0019  0.1556  49  PRO A CB  
377   C CG  . PRO A 49  ? 0.9281 0.6929 0.4540 0.3515  0.0004  0.1562  49  PRO A CG  
378   C CD  . PRO A 49  ? 0.9311 0.7469 0.4606 0.3965  -0.0046 0.1563  49  PRO A CD  
379   N N   . LEU A 50  ? 0.8653 0.7394 0.4468 0.3321  -0.0079 0.1641  50  LEU A N   
380   C CA  . LEU A 50  ? 0.8966 0.7302 0.4467 0.3255  -0.0093 0.1680  50  LEU A CA  
381   C C   . LEU A 50  ? 0.9131 0.6825 0.4426 0.2930  -0.0024 0.1675  50  LEU A C   
382   O O   . LEU A 50  ? 0.8673 0.6592 0.4346 0.2601  0.0034  0.1643  50  LEU A O   
383   C CB  . LEU A 50  ? 0.8517 0.7443 0.4418 0.3096  -0.0116 0.1684  50  LEU A CB  
384   C CG  . LEU A 50  ? 0.8696 0.7295 0.4393 0.2937  -0.0111 0.1713  50  LEU A CG  
385   C CD1 . LEU A 50  ? 0.9410 0.7412 0.4475 0.3202  -0.0154 0.1768  50  LEU A CD1 
386   C CD2 . LEU A 50  ? 0.8308 0.7512 0.4357 0.2846  -0.0155 0.1715  50  LEU A CD2 
387   N N   . ILE A 51  ? 0.9836 0.6735 0.4486 0.3021  -0.0038 0.1711  51  ILE A N   
388   C CA  . ILE A 51  ? 1.0091 0.6393 0.4466 0.2671  0.0015  0.1727  51  ILE A CA  
389   C C   . ILE A 51  ? 1.0406 0.6406 0.4473 0.2546  0.0003  0.1782  51  ILE A C   
390   O O   . ILE A 51  ? 1.1072 0.6537 0.4549 0.2767  -0.0061 0.1829  51  ILE A O   
391   C CB  . ILE A 51  ? 1.0772 0.6287 0.4534 0.2759  -0.0003 0.1740  51  ILE A CB  
392   C CG1 . ILE A 51  ? 1.0505 0.6353 0.4540 0.2977  -0.0001 0.1686  51  ILE A CG1 
393   C CG2 . ILE A 51  ? 1.0955 0.6007 0.4512 0.2306  0.0050  0.1763  51  ILE A CG2 
394   C CD1 . ILE A 51  ? 1.1025 0.6174 0.4583 0.2963  -0.0001 0.1682  51  ILE A CD1 
395   N N   . LEU A 52  ? 0.9968 0.6299 0.4398 0.2213  0.0063  0.1775  52  LEU A N   
396   C CA  . LEU A 52  ? 1.0177 0.6347 0.4394 0.2076  0.0062  0.1825  52  LEU A CA  
397   C C   . LEU A 52  ? 1.0862 0.6260 0.4442 0.1837  0.0074  0.1891  52  LEU A C   
398   O O   . LEU A 52  ? 1.1207 0.6340 0.4460 0.1742  0.0061  0.1947  52  LEU A O   
399   C CB  . LEU A 52  ? 0.9518 0.6318 0.4298 0.1839  0.0121  0.1790  52  LEU A CB  
400   C CG  . LEU A 52  ? 0.8923 0.6420 0.4254 0.1990  0.0093  0.1734  52  LEU A CG  
401   C CD1 . LEU A 52  ? 0.8421 0.6359 0.4163 0.1751  0.0143  0.1694  52  LEU A CD1 
402   C CD2 . LEU A 52  ? 0.9099 0.6690 0.4303 0.2277  0.0006  0.1764  52  LEU A CD2 
403   N N   . ARG A 53  ? 1.1093 0.6129 0.4468 0.1715  0.0091  0.1889  53  ARG A N   
404   C CA  . ARG A 53  ? 1.1811 0.6090 0.4524 0.1421  0.0088  0.1960  53  ARG A CA  
405   C C   . ARG A 53  ? 1.1565 0.6163 0.4473 0.0985  0.0166  0.1994  53  ARG A C   
406   O O   . ARG A 53  ? 1.0952 0.6143 0.4407 0.0792  0.0245  0.1951  53  ARG A O   
407   C CB  . ARG A 53  ? 1.2772 0.6171 0.4627 0.1650  -0.0013 0.2021  53  ARG A CB  
408   C CG  . ARG A 53  ? 1.3703 0.6123 0.4705 0.1368  -0.0050 0.2095  53  ARG A CG  
409   C CD  . ARG A 53  ? 1.4765 0.6205 0.4807 0.1601  -0.0165 0.2156  53  ARG A CD  
410   N NE  . ARG A 53  ? 1.5381 0.6171 0.4885 0.1994  -0.0249 0.2130  53  ARG A NE  
411   C CZ  . ARG A 53  ? 1.5339 0.6301 0.4911 0.2574  -0.0298 0.2079  53  ARG A CZ  
412   N NH1 . ARG A 53  ? 1.4708 0.6469 0.4871 0.2806  -0.0281 0.2053  53  ARG A NH1 
413   N NH2 . ARG A 53  ? 1.5976 0.6321 0.4983 0.2928  -0.0371 0.2058  53  ARG A NH2 
414   N N   . ASP A 54  ? 1.2052 0.6294 0.4506 0.0853  0.0144  0.2071  54  ASP A N   
415   C CA  . ASP A 54  ? 1.1856 0.6464 0.4463 0.0465  0.0219  0.2112  54  ASP A CA  
416   C C   . ASP A 54  ? 1.1315 0.6552 0.4397 0.0604  0.0244  0.2079  54  ASP A C   
417   O O   . ASP A 54  ? 1.1096 0.6733 0.4355 0.0353  0.0311  0.2100  54  ASP A O   
418   C CB  . ASP A 54  ? 1.2752 0.6616 0.4543 0.0155  0.0184  0.2228  54  ASP A CB  
419   C CG  . ASP A 54  ? 1.3298 0.6591 0.4603 -0.0131 0.0165  0.2272  54  ASP A CG  
420   O OD1 . ASP A 54  ? 1.2860 0.6644 0.4562 -0.0390 0.0240  0.2251  54  ASP A OD1 
421   O OD2 . ASP A 54  ? 1.4222 0.6539 0.4696 -0.0092 0.0067  0.2327  54  ASP A OD2 
422   N N   . CYS A 55  ? 1.1136 0.6483 0.4392 0.0998  0.0186  0.2032  55  CYS A N   
423   C CA  . CYS A 55  ? 1.0633 0.6565 0.4331 0.1122  0.0194  0.1997  55  CYS A CA  
424   C C   . CYS A 55  ? 0.9830 0.6494 0.4235 0.1104  0.0250  0.1908  55  CYS A C   
425   O O   . CYS A 55  ? 0.9614 0.6365 0.4227 0.1145  0.0258  0.1862  55  CYS A O   
426   C CB  . CYS A 55  ? 1.0796 0.6617 0.4376 0.1517  0.0098  0.1993  55  CYS A CB  
427   S SG  . CYS A 55  ? 1.1719 0.6752 0.4475 0.1588  0.0024  0.2091  55  CYS A SG  
428   N N   . SER A 56  ? 0.9449 0.6584 0.4160 0.1052  0.0282  0.1884  56  SER A N   
429   C CA  . SER A 56  ? 0.8800 0.6530 0.4071 0.1073  0.0312  0.1797  56  SER A CA  
430   C C   . SER A 56  ? 0.8566 0.6520 0.4054 0.1333  0.0230  0.1758  56  SER A C   
431   O O   . SER A 56  ? 0.8864 0.6596 0.4108 0.1512  0.0160  0.1799  56  SER A O   
432   C CB  . SER A 56  ? 0.8613 0.6694 0.4011 0.0893  0.0384  0.1789  56  SER A CB  
433   O OG  . SER A 56  ? 0.8644 0.6802 0.3997 0.0992  0.0347  0.1796  56  SER A OG  
434   N N   . VAL A 57  ? 0.8077 0.6472 0.3981 0.1344  0.0230  0.1685  57  VAL A N   
435   C CA  . VAL A 57  ? 0.7867 0.6530 0.3966 0.1511  0.0143  0.1656  57  VAL A CA  
436   C C   . VAL A 57  ? 0.7998 0.6675 0.3954 0.1535  0.0106  0.1682  57  VAL A C   
437   O O   . VAL A 57  ? 0.8081 0.6812 0.3987 0.1687  0.0021  0.1704  57  VAL A O   
438   C CB  . VAL A 57  ? 0.7422 0.6455 0.3899 0.1459  0.0141  0.1576  57  VAL A CB  
439   C CG1 . VAL A 57  ? 0.7287 0.6591 0.3896 0.1550  0.0036  0.1560  57  VAL A CG1 
440   C CG2 . VAL A 57  ? 0.7279 0.6316 0.3908 0.1450  0.0171  0.1551  57  VAL A CG2 
441   N N   . ALA A 58  ? 0.8022 0.6697 0.3905 0.1391  0.0172  0.1680  58  ALA A N   
442   C CA  . ALA A 58  ? 0.8185 0.6843 0.3894 0.1404  0.0150  0.1707  58  ALA A CA  
443   C C   . ALA A 58  ? 0.8625 0.6917 0.3965 0.1475  0.0119  0.1791  58  ALA A C   
444   O O   . ALA A 58  ? 0.8737 0.7031 0.3985 0.1606  0.0042  0.1812  58  ALA A O   
445   C CB  . ALA A 58  ? 0.8160 0.6932 0.3840 0.1256  0.0241  0.1693  58  ALA A CB  
446   N N   . GLY A 59  ? 0.8923 0.6872 0.4004 0.1380  0.0169  0.1841  59  GLY A N   
447   C CA  . GLY A 59  ? 0.9475 0.6929 0.4081 0.1444  0.0131  0.1922  59  GLY A CA  
448   C C   . GLY A 59  ? 0.9577 0.6967 0.4136 0.1745  0.0028  0.1925  59  GLY A C   
449   O O   . GLY A 59  ? 0.9904 0.7111 0.4184 0.1891  -0.0033 0.1971  59  GLY A O   
450   N N   . TRP A 60  ? 0.9305 0.6898 0.4133 0.1847  0.0011  0.1879  60  TRP A N   
451   C CA  . TRP A 60  ? 0.9347 0.7054 0.4186 0.2147  -0.0080 0.1882  60  TRP A CA  
452   C C   . TRP A 60  ? 0.9107 0.7273 0.4169 0.2228  -0.0151 0.1871  60  TRP A C   
453   O O   . TRP A 60  ? 0.9375 0.7513 0.4227 0.2440  -0.0227 0.1914  60  TRP A O   
454   C CB  . TRP A 60  ? 0.9069 0.6981 0.4185 0.2201  -0.0072 0.1835  60  TRP A CB  
455   C CG  . TRP A 60  ? 0.8908 0.7254 0.4221 0.2459  -0.0157 0.1826  60  TRP A CG  
456   C CD1 . TRP A 60  ? 0.9212 0.7579 0.4295 0.2754  -0.0241 0.1870  60  TRP A CD1 
457   C CD2 . TRP A 60  ? 0.8432 0.7306 0.4192 0.2439  -0.0170 0.1776  60  TRP A CD2 
458   N NE1 . TRP A 60  ? 0.8927 0.7892 0.4317 0.2911  -0.0301 0.1855  60  TRP A NE1 
459   C CE2 . TRP A 60  ? 0.8455 0.7719 0.4255 0.2700  -0.0260 0.1800  60  TRP A CE2 
460   C CE3 . TRP A 60  ? 0.8017 0.7087 0.4123 0.2225  -0.0117 0.1717  60  TRP A CE3 
461   C CZ2 . TRP A 60  ? 0.8075 0.7943 0.4253 0.2709  -0.0298 0.1775  60  TRP A CZ2 
462   C CZ3 . TRP A 60  ? 0.7667 0.7238 0.4117 0.2246  -0.0159 0.1686  60  TRP A CZ3 
463   C CH2 . TRP A 60  ? 0.7696 0.7672 0.4183 0.2465  -0.0248 0.1719  60  TRP A CH2 
464   N N   . LEU A 61  ? 0.8663 0.7217 0.4095 0.2060  -0.0136 0.1817  61  LEU A N   
465   C CA  . LEU A 61  ? 0.8470 0.7433 0.4080 0.2086  -0.0221 0.1805  61  LEU A CA  
466   C C   . LEU A 61  ? 0.8719 0.7544 0.4084 0.2088  -0.0247 0.1842  61  LEU A C   
467   O O   . LEU A 61  ? 0.8778 0.7816 0.4118 0.2207  -0.0341 0.1869  61  LEU A O   
468   C CB  . LEU A 61  ? 0.8060 0.7325 0.4002 0.1901  -0.0213 0.1734  61  LEU A CB  
469   C CG  . LEU A 61  ? 0.7774 0.7296 0.4001 0.1898  -0.0221 0.1697  61  LEU A CG  
470   C CD1 . LEU A 61  ? 0.7483 0.7213 0.3927 0.1713  -0.0236 0.1632  61  LEU A CD1 
471   C CD2 . LEU A 61  ? 0.7796 0.7644 0.4077 0.2089  -0.0313 0.1736  61  LEU A CD2 
472   N N   . LEU A 62  ? 0.8868 0.7392 0.4054 0.1947  -0.0165 0.1850  62  LEU A N   
473   C CA  . LEU A 62  ? 0.9141 0.7504 0.4060 0.1945  -0.0179 0.1891  62  LEU A CA  
474   C C   . LEU A 62  ? 0.9630 0.7627 0.4150 0.2122  -0.0217 0.1967  62  LEU A C   
475   O O   . LEU A 62  ? 0.9864 0.7779 0.4170 0.2185  -0.0262 0.2006  62  LEU A O   
476   C CB  . LEU A 62  ? 0.9163 0.7399 0.4001 0.1740  -0.0075 0.1884  62  LEU A CB  
477   C CG  . LEU A 62  ? 0.8802 0.7356 0.3915 0.1635  -0.0052 0.1806  62  LEU A CG  
478   C CD1 . LEU A 62  ? 0.8820 0.7347 0.3871 0.1478  0.0067  0.1799  62  LEU A CD1 
479   C CD2 . LEU A 62  ? 0.8799 0.7498 0.3895 0.1682  -0.0141 0.1790  62  LEU A CD2 
480   N N   . GLY A 63  ? 0.9839 0.7574 0.4211 0.2221  -0.0208 0.1986  63  GLY A N   
481   C CA  . GLY A 63  ? 1.0422 0.7698 0.4306 0.2438  -0.0258 0.2052  63  GLY A CA  
482   C C   . GLY A 63  ? 1.0917 0.7589 0.4326 0.2267  -0.0202 0.2108  63  GLY A C   
483   O O   . GLY A 63  ? 1.1370 0.7712 0.4370 0.2352  -0.0245 0.2165  63  GLY A O   
484   N N   . ASN A 64  ? 1.0853 0.7407 0.4300 0.2005  -0.0110 0.2098  64  ASN A N   
485   C CA  . ASN A 64  ? 1.1362 0.7381 0.4331 0.1774  -0.0059 0.2166  64  ASN A CA  
486   C C   . ASN A 64  ? 1.2124 0.7404 0.4439 0.1955  -0.0133 0.2228  64  ASN A C   
487   O O   . ASN A 64  ? 1.2184 0.7361 0.4478 0.2171  -0.0173 0.2203  64  ASN A O   
488   C CB  . ASN A 64  ? 1.1105 0.7262 0.4286 0.1472  0.0042  0.2143  64  ASN A CB  
489   C CG  . ASN A 64  ? 1.1683 0.7296 0.4331 0.1183  0.0083  0.2226  64  ASN A CG  
490   O OD1 . ASN A 64  ? 1.2370 0.7298 0.4414 0.1244  0.0020  0.2290  64  ASN A OD1 
491   N ND2 . ASN A 64  ? 1.1455 0.7374 0.4283 0.0861  0.0182  0.2229  64  ASN A ND2 
492   N N   . PRO A 65  ? 1.2766 0.7501 0.4495 0.1886  -0.0157 0.2307  65  PRO A N   
493   C CA  . PRO A 65  ? 1.3637 0.7544 0.4604 0.2096  -0.0248 0.2367  65  PRO A CA  
494   C C   . PRO A 65  ? 1.4096 0.7411 0.4664 0.2049  -0.0255 0.2379  65  PRO A C   
495   O O   . PRO A 65  ? 1.4748 0.7447 0.4749 0.2357  -0.0346 0.2398  65  PRO A O   
496   C CB  . PRO A 65  ? 1.4198 0.7639 0.4626 0.1878  -0.0250 0.2455  65  PRO A CB  
497   C CG  . PRO A 65  ? 1.3646 0.7665 0.4538 0.1502  -0.0138 0.2446  65  PRO A CG  
498   C CD  . PRO A 65  ? 1.2751 0.7606 0.4458 0.1626  -0.0105 0.2346  65  PRO A CD  
499   N N   . MET A 66  ? 1.3808 0.7298 0.4627 0.1687  -0.0164 0.2367  66  MET A N   
500   C CA  . MET A 66  ? 1.4174 0.7169 0.4676 0.1602  -0.0168 0.2373  66  MET A CA  
501   C C   . MET A 66  ? 1.3747 0.7090 0.4671 0.1943  -0.0187 0.2288  66  MET A C   
502   O O   . MET A 66  ? 1.4144 0.7000 0.4721 0.2028  -0.0219 0.2285  66  MET A O   
503   C CB  . MET A 66  ? 1.3935 0.7146 0.4633 0.1094  -0.0064 0.2391  66  MET A CB  
504   C CG  . MET A 66  ? 1.4282 0.7339 0.4640 0.0694  -0.0027 0.2482  66  MET A CG  
505   S SD  . MET A 66  ? 1.5649 0.7402 0.4770 0.0600  -0.0139 0.2605  66  MET A SD  
506   C CE  . MET A 66  ? 1.5853 0.7694 0.4766 -0.0091 -0.0056 0.2714  66  MET A CE  
507   N N   . CYS A 67  ? 1.2981 0.7155 0.4614 0.2116  -0.0172 0.2222  67  CYS A N   
508   C CA  . CYS A 67  ? 1.2501 0.7156 0.4603 0.2386  -0.0186 0.2148  67  CYS A CA  
509   C C   . CYS A 67  ? 1.2707 0.7421 0.4671 0.2873  -0.0288 0.2148  67  CYS A C   
510   O O   . CYS A 67  ? 1.2149 0.7577 0.4649 0.3066  -0.0305 0.2098  67  CYS A O   
511   C CB  . CYS A 67  ? 1.1579 0.7107 0.4499 0.2209  -0.0114 0.2084  67  CYS A CB  
512   S SG  . CYS A 67  ? 1.1369 0.6948 0.4432 0.1695  0.0007  0.2089  67  CYS A SG  
513   N N   . ASP A 68  ? 1.3562 0.7527 0.4761 0.3063  -0.0363 0.2208  68  ASP A N   
514   C CA  . ASP A 68  ? 1.3912 0.7858 0.4841 0.3585  -0.0467 0.2214  68  ASP A CA  
515   C C   . ASP A 68  ? 1.3921 0.7993 0.4889 0.3941  -0.0499 0.2170  68  ASP A C   
516   O O   . ASP A 68  ? 1.3911 0.8386 0.4939 0.4380  -0.0567 0.2160  68  ASP A O   
517   C CB  . ASP A 68  ? 1.4967 0.7914 0.4926 0.3720  -0.0546 0.2287  68  ASP A CB  
518   C CG  . ASP A 68  ? 1.4973 0.7964 0.4902 0.3548  -0.0545 0.2333  68  ASP A CG  
519   O OD1 . ASP A 68  ? 1.4189 0.7943 0.4816 0.3322  -0.0483 0.2307  68  ASP A OD1 
520   O OD2 . ASP A 68  ? 1.5826 0.8033 0.4972 0.3650  -0.0614 0.2396  68  ASP A OD2 
521   N N   . GLU A 69  ? 1.3964 0.7730 0.4883 0.3756  -0.0450 0.2149  69  GLU A N   
522   C CA  . GLU A 69  ? 1.3888 0.7840 0.4917 0.4056  -0.0465 0.2101  69  GLU A CA  
523   C C   . GLU A 69  ? 1.2938 0.8073 0.4870 0.4134  -0.0443 0.2049  69  GLU A C   
524   O O   . GLU A 69  ? 1.2896 0.8416 0.4915 0.4527  -0.0487 0.2027  69  GLU A O   
525   C CB  . GLU A 69  ? 1.3983 0.7476 0.4897 0.3747  -0.0406 0.2087  69  GLU A CB  
526   C CG  . GLU A 69  ? 1.3998 0.7560 0.4931 0.4054  -0.0421 0.2039  69  GLU A CG  
527   C CD  . GLU A 69  ? 1.4151 0.7203 0.4917 0.3735  -0.0372 0.2028  69  GLU A CD  
528   O OE1 . GLU A 69  ? 1.4415 0.6951 0.4901 0.3296  -0.0340 0.2071  69  GLU A OE1 
529   O OE2 . GLU A 69  ? 1.4014 0.7226 0.4926 0.3915  -0.0365 0.1981  69  GLU A OE2 
530   N N   . PHE A 70  ? 1.2246 0.7941 0.4788 0.3763  -0.0382 0.2034  70  PHE A N   
531   C CA  . PHE A 70  ? 1.1395 0.8083 0.4735 0.3710  -0.0363 0.1985  70  PHE A CA  
532   C C   . PHE A 70  ? 1.1119 0.8450 0.4742 0.3800  -0.0420 0.2000  70  PHE A C   
533   O O   . PHE A 70  ? 1.0467 0.8467 0.4672 0.3589  -0.0404 0.1970  70  PHE A O   
534   C CB  . PHE A 70  ? 1.0850 0.7681 0.4633 0.3246  -0.0264 0.1945  70  PHE A CB  
535   C CG  . PHE A 70  ? 1.1148 0.7359 0.4634 0.3095  -0.0211 0.1941  70  PHE A CG  
536   C CD1 . PHE A 70  ? 1.1222 0.7383 0.4667 0.3296  -0.0220 0.1914  70  PHE A CD1 
537   C CD2 . PHE A 70  ? 1.1397 0.7096 0.4609 0.2744  -0.0156 0.1973  70  PHE A CD2 
538   C CE1 . PHE A 70  ? 1.1549 0.7102 0.4676 0.3141  -0.0182 0.1912  70  PHE A CE1 
539   C CE2 . PHE A 70  ? 1.1715 0.6871 0.4622 0.2560  -0.0119 0.1980  70  PHE A CE2 
540   C CZ  . PHE A 70  ? 1.1802 0.6849 0.4655 0.2756  -0.0135 0.1948  70  PHE A CZ  
541   N N   . ILE A 71  ? 1.1678 0.8765 0.4833 0.4113  -0.0496 0.2048  71  ILE A N   
542   C CA  . ILE A 71  ? 1.1487 0.9253 0.4866 0.4284  -0.0571 0.2069  71  ILE A CA  
543   C C   . ILE A 71  ? 1.1399 0.9835 0.4948 0.4673  -0.0631 0.2064  71  ILE A C   
544   O O   . ILE A 71  ? 1.1926 1.0005 0.5038 0.5046  -0.0655 0.2069  71  ILE A O   
545   C CB  . ILE A 71  ? 1.2108 0.9384 0.4921 0.4459  -0.0630 0.2126  71  ILE A CB  
546   C CG1 . ILE A 71  ? 1.2015 1.0021 0.4972 0.4758  -0.0726 0.2153  71  ILE A CG1 
547   C CG2 . ILE A 71  ? 1.3016 0.9328 0.5003 0.4752  -0.0658 0.2154  71  ILE A CG2 
548   C CD1 . ILE A 71  ? 1.2424 1.0103 0.4994 0.4818  -0.0776 0.2203  71  ILE A CD1 
549   N N   . ASN A 72  ? 1.0800 1.0197 0.4935 0.4578  -0.0661 0.2058  72  ASN A N   
550   C CA  . ASN A 72  ? 1.0609 1.0849 0.5001 0.4864  -0.0714 0.2063  72  ASN A CA  
551   C C   . ASN A 72  ? 1.0602 1.0727 0.5014 0.4962  -0.0663 0.2024  72  ASN A C   
552   O O   . ASN A 72  ? 1.0985 1.1164 0.5107 0.5422  -0.0698 0.2034  72  ASN A O   
553   C CB  . ASN A 72  ? 1.1110 1.1554 0.5115 0.5390  -0.0810 0.2115  72  ASN A CB  
554   C CG  . ASN A 72  ? 1.1002 1.1863 0.5121 0.5299  -0.0877 0.2158  72  ASN A CG  
555   O OD1 . ASN A 72  ? 1.0575 1.1558 0.5043 0.4847  -0.0857 0.2145  72  ASN A OD1 
556   N ND2 . ASN A 72  ? 1.1436 1.2505 0.5220 0.5753  -0.0963 0.2206  72  ASN A ND2 
557   N N   . VAL A 73  ? 1.0193 1.0164 0.4919 0.4555  -0.0581 0.1977  73  VAL A N   
558   C CA  . VAL A 73  ? 1.0150 0.9981 0.4913 0.4595  -0.0528 0.1937  73  VAL A CA  
559   C C   . VAL A 73  ? 0.9792 1.0586 0.4940 0.4781  -0.0563 0.1937  73  VAL A C   
560   O O   . VAL A 73  ? 0.9355 1.0991 0.4936 0.4632  -0.0609 0.1957  73  VAL A O   
561   C CB  . VAL A 73  ? 0.9758 0.9298 0.4805 0.4111  -0.0434 0.1888  73  VAL A CB  
562   C CG1 . VAL A 73  ? 1.0190 0.8768 0.4782 0.3956  -0.0387 0.1895  73  VAL A CG1 
563   C CG2 . VAL A 73  ? 0.9114 0.9287 0.4728 0.3735  -0.0436 0.1872  73  VAL A CG2 
564   N N   . PRO A 74  ? 1.0016 1.0683 0.4971 0.5086  -0.0548 0.1920  74  PRO A N   
565   C CA  . PRO A 74  ? 0.9644 1.1255 0.4990 0.5221  -0.0566 0.1919  74  PRO A CA  
566   C C   . PRO A 74  ? 0.8973 1.0854 0.4882 0.4731  -0.0507 0.1877  74  PRO A C   
567   O O   . PRO A 74  ? 0.8870 1.0121 0.4796 0.4378  -0.0443 0.1840  74  PRO A O   
568   C CB  . PRO A 74  ? 1.0214 1.1388 0.5068 0.5708  -0.0559 0.1905  74  PRO A CB  
569   C CG  . PRO A 74  ? 1.0655 1.0574 0.5034 0.5561  -0.0508 0.1877  74  PRO A CG  
570   C CD  . PRO A 74  ? 1.0652 1.0268 0.4994 0.5269  -0.0514 0.1901  74  PRO A CD  
571   N N   . GLU A 75  ? 0.8545 1.1375 0.4881 0.4712  -0.0532 0.1888  75  GLU A N   
572   C CA  . GLU A 75  ? 0.7966 1.1050 0.4786 0.4258  -0.0492 0.1851  75  GLU A CA  
573   C C   . GLU A 75  ? 0.8015 1.0406 0.4732 0.4225  -0.0402 0.1791  75  GLU A C   
574   O O   . GLU A 75  ? 0.8448 1.0451 0.4784 0.4603  -0.0386 0.1784  75  GLU A O   
575   C CB  . GLU A 75  ? 0.7600 1.1839 0.4829 0.4230  -0.0548 0.1888  75  GLU A CB  
576   C CG  . GLU A 75  ? 0.7659 1.2227 0.4888 0.4556  -0.0523 0.1881  75  GLU A CG  
577   C CD  . GLU A 75  ? 0.7261 1.3041 0.4926 0.4432  -0.0575 0.1927  75  GLU A CD  
578   O OE1 . GLU A 75  ? 0.7280 1.3891 0.5002 0.4544  -0.0659 0.1999  75  GLU A OE1 
579   O OE2 . GLU A 75  ? 0.6951 1.2871 0.4887 0.4201  -0.0536 0.1898  75  GLU A OE2 
580   N N   . TRP A 76  ? 0.7608 0.9834 0.4622 0.3780  -0.0351 0.1746  76  TRP A N   
581   C CA  . TRP A 76  ? 0.7621 0.9196 0.4564 0.3671  -0.0265 0.1691  76  TRP A CA  
582   C C   . TRP A 76  ? 0.7114 0.9150 0.4508 0.3419  -0.0241 0.1656  76  TRP A C   
583   O O   . TRP A 76  ? 0.6745 0.9364 0.4480 0.3160  -0.0285 0.1666  76  TRP A O   
584   C CB  . TRP A 76  ? 0.7686 0.8533 0.4490 0.3382  -0.0215 0.1669  76  TRP A CB  
585   C CG  . TRP A 76  ? 0.7277 0.8424 0.4416 0.3008  -0.0231 0.1659  76  TRP A CG  
586   C CD1 . TRP A 76  ? 0.6874 0.8121 0.4336 0.2671  -0.0199 0.1611  76  TRP A CD1 
587   C CD2 . TRP A 76  ? 0.7304 0.8636 0.4419 0.2959  -0.0292 0.1695  76  TRP A CD2 
588   N NE1 . TRP A 76  ? 0.6701 0.8129 0.4290 0.2430  -0.0241 0.1613  76  TRP A NE1 
589   C CE2 . TRP A 76  ? 0.6943 0.8436 0.4338 0.2585  -0.0298 0.1665  76  TRP A CE2 
590   C CE3 . TRP A 76  ? 0.7640 0.8985 0.4482 0.3209  -0.0349 0.1748  76  TRP A CE3 
591   C CZ2 . TRP A 76  ? 0.6924 0.8563 0.4320 0.2443  -0.0359 0.1686  76  TRP A CZ2 
592   C CZ3 . TRP A 76  ? 0.7562 0.9114 0.4463 0.3053  -0.0404 0.1772  76  TRP A CZ3 
593   C CH2 . TRP A 76  ? 0.7211 0.8898 0.4382 0.2667  -0.0410 0.1740  76  TRP A CH2 
594   N N   . SER A 77  ? 0.7154 0.8879 0.4494 0.3483  -0.0182 0.1618  77  SER A N   
595   C CA  . SER A 77  ? 0.6711 0.8723 0.4432 0.3229  -0.0149 0.1578  77  SER A CA  
596   C C   . SER A 77  ? 0.6466 0.8074 0.4322 0.2815  -0.0102 0.1532  77  SER A C   
597   O O   . SER A 77  ? 0.6092 0.8042 0.4267 0.2524  -0.0118 0.1512  77  SER A O   
598   C CB  . SER A 77  ? 0.6888 0.8646 0.4463 0.3454  -0.0100 0.1550  77  SER A CB  
599   O OG  . SER A 77  ? 0.7386 0.8250 0.4478 0.3589  -0.0066 0.1541  77  SER A OG  
600   N N   . TYR A 78  ? 0.6736 0.7610 0.4293 0.2799  -0.0052 0.1519  78  TYR A N   
601   C CA  . TYR A 78  ? 0.6566 0.7102 0.4199 0.2461  -0.0002 0.1483  78  TYR A CA  
602   C C   . TYR A 78  ? 0.6962 0.6898 0.4206 0.2488  0.0018  0.1509  78  TYR A C   
603   O O   . TYR A 78  ? 0.7403 0.7057 0.4276 0.2759  -0.0005 0.1547  78  TYR A O   
604   C CB  . TYR A 78  ? 0.6383 0.6730 0.4148 0.2307  0.0067  0.1430  78  TYR A CB  
605   C CG  . TYR A 78  ? 0.6752 0.6580 0.4190 0.2477  0.0108  0.1432  78  TYR A CG  
606   C CD1 . TYR A 78  ? 0.6903 0.6865 0.4254 0.2774  0.0086  0.1440  78  TYR A CD1 
607   C CD2 . TYR A 78  ? 0.7005 0.6209 0.4171 0.2333  0.0163  0.1430  78  TYR A CD2 
608   C CE1 . TYR A 78  ? 0.7346 0.6724 0.4298 0.2941  0.0110  0.1438  78  TYR A CE1 
609   C CE2 . TYR A 78  ? 0.7444 0.6087 0.4219 0.2440  0.0182  0.1438  78  TYR A CE2 
610   C CZ  . TYR A 78  ? 0.7638 0.6314 0.4281 0.2754  0.0152  0.1438  78  TYR A CZ  
611   O OH  . TYR A 78  ? 0.8171 0.6185 0.4331 0.2870  0.0158  0.1443  78  TYR A OH  
612   N N   . ILE A 79  ? 0.6847 0.6589 0.4136 0.2218  0.0058  0.1490  79  ILE A N   
613   C CA  . ILE A 79  ? 0.7202 0.6447 0.4143 0.2181  0.0081  0.1522  79  ILE A CA  
614   C C   . ILE A 79  ? 0.7302 0.6105 0.4117 0.1982  0.0163  0.1506  79  ILE A C   
615   O O   . ILE A 79  ? 0.6962 0.5936 0.4061 0.1806  0.0208  0.1457  79  ILE A O   
616   C CB  . ILE A 79  ? 0.7052 0.6484 0.4094 0.2038  0.0060  0.1525  79  ILE A CB  
617   C CG1 . ILE A 79  ? 0.7026 0.6887 0.4134 0.2204  -0.0033 0.1556  79  ILE A CG1 
618   C CG2 . ILE A 79  ? 0.7400 0.6359 0.4097 0.1967  0.0095  0.1561  79  ILE A CG2 
619   C CD1 . ILE A 79  ? 0.6829 0.6945 0.4083 0.2033  -0.0073 0.1548  79  ILE A CD1 
620   N N   . VAL A 80  ? 0.7814 0.6050 0.4167 0.1997  0.0175  0.1552  80  VAL A N   
621   C CA  . VAL A 80  ? 0.7995 0.5826 0.4159 0.1754  0.0242  0.1557  80  VAL A CA  
622   C C   . VAL A 80  ? 0.8252 0.5842 0.4159 0.1571  0.0263  0.1605  80  VAL A C   
623   O O   . VAL A 80  ? 0.8710 0.5948 0.4215 0.1689  0.0218  0.1659  80  VAL A O   
624   C CB  . VAL A 80  ? 0.8508 0.5772 0.4232 0.1868  0.0227  0.1579  80  VAL A CB  
625   C CG1 . VAL A 80  ? 0.8690 0.5590 0.4223 0.1546  0.0287  0.1593  80  VAL A CG1 
626   C CG2 . VAL A 80  ? 0.8278 0.5825 0.4242 0.2088  0.0208  0.1535  80  VAL A CG2 
627   N N   . GLU A 81  ? 0.7982 0.5786 0.4102 0.1300  0.0332  0.1585  81  GLU A N   
628   C CA  . GLU A 81  ? 0.8156 0.5883 0.4095 0.1104  0.0366  0.1629  81  GLU A CA  
629   C C   . GLU A 81  ? 0.8229 0.5890 0.4094 0.0800  0.0441  0.1645  81  GLU A C   
630   O O   . GLU A 81  ? 0.7890 0.5819 0.4060 0.0734  0.0480  0.1593  81  GLU A O   
631   C CB  . GLU A 81  ? 0.7729 0.5959 0.4024 0.1111  0.0372  0.1588  81  GLU A CB  
632   C CG  . GLU A 81  ? 0.7894 0.6115 0.4011 0.0968  0.0405  0.1631  81  GLU A CG  
633   C CD  . GLU A 81  ? 0.7525 0.6191 0.3939 0.0995  0.0408  0.1579  81  GLU A CD  
634   O OE1 . GLU A 81  ? 0.7145 0.6128 0.3881 0.0993  0.0425  0.1509  81  GLU A OE1 
635   O OE2 . GLU A 81  ? 0.7668 0.6314 0.3939 0.1024  0.0388  0.1609  81  GLU A OE2 
636   N N   . LYS A 82  ? 0.8696 0.6032 0.4143 0.0595  0.0456  0.1723  82  LYS A N   
637   C CA  . LYS A 82  ? 0.8802 0.6173 0.4152 0.0249  0.0522  0.1758  82  LYS A CA  
638   C C   . LYS A 82  ? 0.8311 0.6382 0.4083 0.0138  0.0601  0.1720  82  LYS A C   
639   O O   . LYS A 82  ? 0.7998 0.6392 0.4030 0.0307  0.0596  0.1675  82  LYS A O   
640   C CB  . LYS A 82  ? 0.9520 0.6334 0.4228 0.0017  0.0503  0.1867  82  LYS A CB  
641   C CG  . LYS A 82  ? 1.0166 0.6175 0.4312 0.0051  0.0430  0.1906  82  LYS A CG  
642   C CD  . LYS A 82  ? 1.0992 0.6342 0.4391 -0.0215 0.0393  0.2020  82  LYS A CD  
643   C CE  . LYS A 82  ? 1.1739 0.6216 0.4478 -0.0262 0.0320  0.2059  82  LYS A CE  
644   N NZ  . LYS A 82  ? 1.2044 0.6006 0.4517 0.0203  0.0232  0.2026  82  LYS A NZ  
645   N N   . ALA A 83  ? 0.8297 0.6597 0.4094 -0.0134 0.0666  0.1740  83  ALA A N   
646   C CA  . ALA A 83  ? 0.7909 0.6905 0.4040 -0.0207 0.0744  0.1707  83  ALA A CA  
647   C C   . ALA A 83  ? 0.8089 0.7252 0.4051 -0.0290 0.0769  0.1764  83  ALA A C   
648   O O   . ALA A 83  ? 0.7774 0.7403 0.3993 -0.0152 0.0800  0.1713  83  ALA A O   
649   C CB  . ALA A 83  ? 0.7875 0.7141 0.4050 -0.0476 0.0804  0.1725  83  ALA A CB  
650   N N   . ASN A 84  ? 0.8658 0.7393 0.4134 -0.0510 0.0748  0.1871  84  ASN A N   
651   C CA  . ASN A 84  ? 0.8889 0.7752 0.4152 -0.0627 0.0771  0.1940  84  ASN A CA  
652   C C   . ASN A 84  ? 0.9473 0.7601 0.4222 -0.0619 0.0692  0.2013  84  ASN A C   
653   O O   . ASN A 84  ? 1.0036 0.7843 0.4292 -0.0930 0.0685  0.2122  84  ASN A O   
654   C CB  . ASN A 84  ? 0.9047 0.8329 0.4185 -0.1025 0.0846  0.2023  84  ASN A CB  
655   C CG  . ASN A 84  ? 0.8519 0.8581 0.4131 -0.0993 0.0925  0.1952  84  ASN A CG  
656   O OD1 . ASN A 84  ? 0.8112 0.8658 0.4061 -0.0734 0.0958  0.1872  84  ASN A OD1 
657   N ND2 . ASN A 84  ? 0.8580 0.8725 0.4167 -0.1246 0.0945  0.1981  84  ASN A ND2 
658   N N   . PRO A 85  ? 0.9384 0.7255 0.4211 -0.0272 0.0626  0.1959  85  PRO A N   
659   C CA  . PRO A 85  ? 0.9949 0.7138 0.4279 -0.0191 0.0544  0.2020  85  PRO A CA  
660   C C   . PRO A 85  ? 1.0273 0.7457 0.4301 -0.0359 0.0559  0.2102  85  PRO A C   
661   O O   . PRO A 85  ? 0.9906 0.7638 0.4244 -0.0297 0.0606  0.2071  85  PRO A O   
662   C CB  . PRO A 85  ? 0.9620 0.6854 0.4244 0.0220  0.0485  0.1937  85  PRO A CB  
663   C CG  . PRO A 85  ? 0.9006 0.6733 0.4178 0.0306  0.0520  0.1841  85  PRO A CG  
664   C CD  . PRO A 85  ? 0.8802 0.7022 0.4139 0.0049  0.0615  0.1845  85  PRO A CD  
665   N N   . VAL A 86  ? 1.1015 0.7540 0.4390 -0.0566 0.0513  0.2206  86  VAL A N   
666   C CA  . VAL A 86  ? 1.1410 0.7874 0.4419 -0.0781 0.0523  0.2301  86  VAL A CA  
667   C C   . VAL A 86  ? 1.1381 0.7759 0.4399 -0.0466 0.0477  0.2280  86  VAL A C   
668   O O   . VAL A 86  ? 1.1324 0.8048 0.4385 -0.0539 0.0518  0.2308  86  VAL A O   
669   C CB  . VAL A 86  ? 1.2334 0.8004 0.4524 -0.1137 0.0468  0.2430  86  VAL A CB  
670   C CG1 . VAL A 86  ? 1.2403 0.8218 0.4548 -0.1531 0.0510  0.2469  86  VAL A CG1 
671   C CG2 . VAL A 86  ? 1.2920 0.7620 0.4588 -0.0869 0.0347  0.2431  86  VAL A CG2 
672   N N   . ASN A 87  ? 1.1440 0.7404 0.4407 -0.0113 0.0392  0.2235  87  ASN A N   
673   C CA  . ASN A 87  ? 1.1434 0.7331 0.4393 0.0192  0.0335  0.2220  87  ASN A CA  
674   C C   . ASN A 87  ? 1.0654 0.7258 0.4298 0.0431  0.0359  0.2115  87  ASN A C   
675   O O   . ASN A 87  ? 1.0429 0.7059 0.4291 0.0731  0.0301  0.2053  87  ASN A O   
676   C CB  . ASN A 87  ? 1.1932 0.7119 0.4466 0.0482  0.0225  0.2229  87  ASN A CB  
677   C CG  . ASN A 87  ? 1.2894 0.7196 0.4563 0.0295  0.0169  0.2339  87  ASN A CG  
678   O OD1 . ASN A 87  ? 1.3209 0.7437 0.4580 -0.0026 0.0198  0.2421  87  ASN A OD1 
679   N ND2 . ASN A 87  ? 1.3428 0.7028 0.4633 0.0505  0.0081  0.2343  87  ASN A ND2 
680   N N   . ASP A 88  ? 1.0302 0.7474 0.4228 0.0291  0.0438  0.2100  88  ASP A N   
681   C CA  . ASP A 88  ? 0.9693 0.7433 0.4138 0.0488  0.0452  0.2004  88  ASP A CA  
682   C C   . ASP A 88  ? 0.9790 0.7558 0.4123 0.0589  0.0423  0.2022  88  ASP A C   
683   O O   . ASP A 88  ? 1.0090 0.7465 0.4167 0.0740  0.0342  0.2054  88  ASP A O   
684   C CB  . ASP A 88  ? 0.9304 0.7618 0.4077 0.0335  0.0550  0.1962  88  ASP A CB  
685   C CG  . ASP A 88  ? 0.8770 0.7530 0.3995 0.0555  0.0546  0.1850  88  ASP A CG  
686   O OD1 . ASP A 88  ? 0.8659 0.7310 0.3985 0.0775  0.0464  0.1808  88  ASP A OD1 
687   O OD2 . ASP A 88  ? 0.8509 0.7730 0.3946 0.0503  0.0619  0.1809  88  ASP A OD2 
688   N N   . LEU A 89  ? 0.9570 0.7801 0.4062 0.0532  0.0487  0.2002  89  LEU A N   
689   C CA  . LEU A 89  ? 0.9686 0.7951 0.4046 0.0608  0.0467  0.2020  89  LEU A CA  
690   C C   . LEU A 89  ? 1.0201 0.8226 0.4101 0.0360  0.0501  0.2137  89  LEU A C   
691   O O   . LEU A 89  ? 1.0210 0.8587 0.4088 0.0133  0.0593  0.2173  89  LEU A O   
692   C CB  . LEU A 89  ? 0.9309 0.8128 0.3961 0.0687  0.0515  0.1943  89  LEU A CB  
693   C CG  . LEU A 89  ? 0.8991 0.7912 0.3905 0.0944  0.0439  0.1844  89  LEU A CG  
694   C CD1 . LEU A 89  ? 0.8889 0.7577 0.3932 0.1056  0.0352  0.1821  89  LEU A CD1 
695   C CD2 . LEU A 89  ? 0.8670 0.8026 0.3831 0.0994  0.0491  0.1755  89  LEU A CD2 
696   N N   . CYS A 90  ? 1.0664 0.8109 0.4166 0.0405  0.0423  0.2200  90  CYS A N   
697   C CA  . CYS A 90  ? 1.1276 0.8345 0.4230 0.0157  0.0431  0.2320  90  CYS A CA  
698   C C   . CYS A 90  ? 1.1237 0.8716 0.4192 0.0070  0.0492  0.2345  90  CYS A C   
699   O O   . CYS A 90  ? 1.1423 0.9113 0.4207 -0.0239 0.0570  0.2418  90  CYS A O   
700   C CB  . CYS A 90  ? 1.1826 0.8148 0.4307 0.0309  0.0319  0.2369  90  CYS A CB  
701   S SG  . CYS A 90  ? 1.1595 0.7974 0.4288 0.0747  0.0222  0.2300  90  CYS A SG  
702   N N   . TYR A 91  ? 1.0485 0.6681 0.5739 -0.0530 0.1036  0.2416  91  TYR A N   
703   C CA  . TYR A 91  ? 1.0439 0.7098 0.5716 -0.0647 0.1285  0.2449  91  TYR A CA  
704   C C   . TYR A 91  ? 0.9679 0.7061 0.5608 -0.0661 0.1371  0.2224  91  TYR A C   
705   O O   . TYR A 91  ? 0.9144 0.6738 0.5312 -0.0428 0.1225  0.2037  91  TYR A O   
706   C CB  . TYR A 91  ? 1.0590 0.7206 0.5421 -0.0380 0.1245  0.2471  91  TYR A CB  
707   C CG  . TYR A 91  ? 1.0863 0.7723 0.5458 -0.0486 0.1497  0.2558  91  TYR A CG  
708   C CD1 . TYR A 91  ? 1.0379 0.7888 0.5301 -0.0437 0.1633  0.2384  91  TYR A CD1 
709   C CD2 . TYR A 91  ? 1.1680 0.8085 0.5670 -0.0618 0.1598  0.2815  91  TYR A CD2 
710   C CE1 . TYR A 91  ? 1.0702 0.8427 0.5349 -0.0484 0.1876  0.2448  91  TYR A CE1 
711   C CE2 . TYR A 91  ? 1.1999 0.8632 0.5713 -0.0694 0.1857  0.2903  91  TYR A CE2 
712   C CZ  . TYR A 91  ? 1.1507 0.8815 0.5549 -0.0610 0.2003  0.2711  91  TYR A CZ  
713   O OH  . TYR A 91  ? 1.1891 0.9419 0.5605 -0.0636 0.2271  0.2782  91  TYR A OH  
714   N N   . PRO A 92  ? 0.9664 0.7443 0.5886 -0.0930 0.1607  0.2252  92  PRO A N   
715   C CA  . PRO A 92  ? 0.9001 0.7420 0.5860 -0.0938 0.1658  0.2032  92  PRO A CA  
716   C C   . PRO A 92  ? 0.8552 0.7365 0.5459 -0.0648 0.1632  0.1836  92  PRO A C   
717   O O   . PRO A 92  ? 0.8808 0.7546 0.5279 -0.0504 0.1665  0.1886  92  PRO A O   
718   C CB  . PRO A 92  ? 0.9206 0.8016 0.6288 -0.1245 0.1949  0.2140  92  PRO A CB  
719   C CG  . PRO A 92  ? 0.9987 0.8290 0.6585 -0.1465 0.2029  0.2441  92  PRO A CG  
720   C CD  . PRO A 92  ? 1.0271 0.8007 0.6238 -0.1203 0.1856  0.2489  92  PRO A CD  
721   N N   . GLY A 93  ? 0.7954 0.7132 0.5353 -0.0572 0.1545  0.1617  93  GLY A N   
722   C CA  . GLY A 93  ? 0.7567 0.7072 0.5032 -0.0331 0.1480  0.1429  93  GLY A CA  
723   C C   . GLY A 93  ? 0.6983 0.6697 0.4914 -0.0250 0.1310  0.1225  93  GLY A C   
724   O O   . GLY A 93  ? 0.6829 0.6576 0.5114 -0.0391 0.1291  0.1189  93  GLY A O   
725   N N   . ASP A 94  ? 0.6715 0.6546 0.4620 -0.0034 0.1167  0.1101  94  ASP A N   
726   C CA  . ASP A 94  ? 0.6219 0.6205 0.4485 0.0052  0.0989  0.0934  94  ASP A CA  
727   C C   . ASP A 94  ? 0.6138 0.5935 0.4235 0.0229  0.0786  0.0968  94  ASP A C   
728   O O   . ASP A 94  ? 0.6416 0.6052 0.4149 0.0320  0.0759  0.1072  94  ASP A O   
729   C CB  . ASP A 94  ? 0.5981 0.6363 0.4452 0.0121  0.0996  0.0743  94  ASP A CB  
730   C CG  . ASP A 94  ? 0.6036 0.6739 0.4763 -0.0013 0.1208  0.0693  94  ASP A CG  
731   O OD1 . ASP A 94  ? 0.5877 0.6652 0.4977 -0.0151 0.1208  0.0666  94  ASP A OD1 
732   O OD2 . ASP A 94  ? 0.6277 0.7179 0.4832 0.0029  0.1370  0.0681  94  ASP A OD2 
733   N N   . PHE A 95  ? 0.5787 0.5628 0.4155 0.0278  0.0644  0.0890  95  PHE A N   
734   C CA  . PHE A 95  ? 0.5641 0.5455 0.3972 0.0439  0.0467  0.0919  95  PHE A CA  
735   C C   . PHE A 95  ? 0.5267 0.5372 0.3873 0.0469  0.0348  0.0769  95  PHE A C   
736   O O   . PHE A 95  ? 0.5030 0.5229 0.3916 0.0413  0.0336  0.0659  95  PHE A O   
737   C CB  . PHE A 95  ? 0.5652 0.5240 0.4004 0.0484  0.0421  0.0984  95  PHE A CB  
738   C CG  . PHE A 95  ? 0.5684 0.5232 0.3909 0.0673  0.0303  0.1086  95  PHE A CG  
739   C CD1 . PHE A 95  ? 0.5381 0.5227 0.3800 0.0756  0.0172  0.1058  95  PHE A CD1 
740   C CD2 . PHE A 95  ? 0.6056 0.5278 0.3983 0.0767  0.0309  0.1219  95  PHE A CD2 
741   C CE1 . PHE A 95  ? 0.5409 0.5322 0.3796 0.0918  0.0072  0.1171  95  PHE A CE1 
742   C CE2 . PHE A 95  ? 0.6096 0.5354 0.3956 0.0976  0.0202  0.1309  95  PHE A CE2 
743   C CZ  . PHE A 95  ? 0.5750 0.5402 0.3875 0.1047  0.0094  0.1290  95  PHE A CZ  
744   N N   . ASN A 96  ? 0.5277 0.5474 0.3771 0.0551  0.0229  0.0765  96  ASN A N   
745   C CA  . ASN A 96  ? 0.5044 0.5430 0.3719 0.0565  0.0081  0.0629  96  ASN A CA  
746   C C   . ASN A 96  ? 0.4753 0.5214 0.3672 0.0582  -0.0066 0.0656  96  ASN A C   
747   O O   . ASN A 96  ? 0.4771 0.5227 0.3658 0.0647  -0.0123 0.0797  96  ASN A O   
748   C CB  . ASN A 96  ? 0.5261 0.5641 0.3682 0.0635  -0.0040 0.0623  96  ASN A CB  
749   C CG  . ASN A 96  ? 0.5186 0.5659 0.3689 0.0648  -0.0185 0.0449  96  ASN A CG  
750   O OD1 . ASN A 96  ? 0.5214 0.5755 0.3750 0.0647  -0.0080 0.0303  96  ASN A OD1 
751   N ND2 . ASN A 96  ? 0.5131 0.5612 0.3676 0.0661  -0.0442 0.0469  96  ASN A ND2 
752   N N   . ASP A 97  ? 0.4525 0.5072 0.3677 0.0538  -0.0124 0.0527  97  ASP A N   
753   C CA  . ASP A 97  ? 0.4295 0.4899 0.3649 0.0536  -0.0238 0.0556  97  ASP A CA  
754   C C   . ASP A 97  ? 0.4292 0.4819 0.3634 0.0588  -0.0144 0.0681  97  ASP A C   
755   O O   . ASP A 97  ? 0.4243 0.4867 0.3630 0.0654  -0.0204 0.0802  97  ASP A O   
756   C CB  . ASP A 97  ? 0.4273 0.4991 0.3654 0.0540  -0.0449 0.0619  97  ASP A CB  
757   C CG  . ASP A 97  ? 0.4313 0.5009 0.3689 0.0502  -0.0609 0.0464  97  ASP A CG  
758   O OD1 . ASP A 97  ? 0.4288 0.4947 0.3716 0.0497  -0.0558 0.0300  97  ASP A OD1 
759   O OD2 . ASP A 97  ? 0.4420 0.5124 0.3739 0.0487  -0.0812 0.0503  97  ASP A OD2 
760   N N   . TYR A 98  ? 0.4392 0.4747 0.3669 0.0563  -0.0002 0.0653  98  TYR A N   
761   C CA  . TYR A 98  ? 0.4522 0.4678 0.3691 0.0631  0.0067  0.0746  98  TYR A CA  
762   C C   . TYR A 98  ? 0.4386 0.4538 0.3671 0.0682  0.0014  0.0723  98  TYR A C   
763   O O   . TYR A 98  ? 0.4474 0.4581 0.3665 0.0819  0.0025  0.0824  98  TYR A O   
764   C CB  . TYR A 98  ? 0.4737 0.4662 0.3815 0.0536  0.0188  0.0715  98  TYR A CB  
765   C CG  . TYR A 98  ? 0.5019 0.4600 0.3896 0.0594  0.0224  0.0799  98  TYR A CG  
766   C CD1 . TYR A 98  ? 0.5205 0.4679 0.3860 0.0764  0.0211  0.0933  98  TYR A CD1 
767   C CD2 . TYR A 98  ? 0.5161 0.4500 0.4060 0.0487  0.0247  0.0740  98  TYR A CD2 
768   C CE1 . TYR A 98  ? 0.5556 0.4643 0.3962 0.0859  0.0221  0.0990  98  TYR A CE1 
769   C CE2 . TYR A 98  ? 0.5524 0.4445 0.4172 0.0543  0.0236  0.0805  98  TYR A CE2 
770   C CZ  . TYR A 98  ? 0.5738 0.4509 0.4112 0.0744  0.0226  0.0923  98  TYR A CZ  
771   O OH  . TYR A 98  ? 0.6181 0.4471 0.4248 0.0839  0.0192  0.0969  98  TYR A OH  
772   N N   . GLU A 99  ? 0.4213 0.4413 0.3673 0.0596  -0.0042 0.0588  99  GLU A N   
773   C CA  . GLU A 99  ? 0.4145 0.4291 0.3660 0.0633  -0.0101 0.0555  99  GLU A CA  
774   C C   . GLU A 99  ? 0.4024 0.4393 0.3592 0.0691  -0.0173 0.0664  99  GLU A C   
775   O O   . GLU A 99  ? 0.4072 0.4429 0.3584 0.0791  -0.0155 0.0734  99  GLU A O   
776   C CB  . GLU A 99  ? 0.4043 0.4165 0.3725 0.0530  -0.0172 0.0379  99  GLU A CB  
777   C CG  . GLU A 99  ? 0.4172 0.4126 0.3888 0.0449  -0.0112 0.0289  99  GLU A CG  
778   C CD  . GLU A 99  ? 0.4220 0.4288 0.3966 0.0365  -0.0005 0.0291  99  GLU A CD  
779   O OE1 . GLU A 99  ? 0.4113 0.4395 0.3906 0.0365  -0.0020 0.0261  99  GLU A OE1 
780   O OE2 . GLU A 99  ? 0.4424 0.4334 0.4111 0.0296  0.0085  0.0328  99  GLU A OE2 
781   N N   . GLU A 100 ? 0.3915 0.4485 0.3577 0.0626  -0.0260 0.0684  100 GLU A N   
782   C CA  . GLU A 100 ? 0.3841 0.4653 0.3598 0.0628  -0.0354 0.0823  100 GLU A CA  
783   C C   . GLU A 100 ? 0.3920 0.4887 0.3639 0.0762  -0.0272 0.1007  100 GLU A C   
784   O O   . GLU A 100 ? 0.3890 0.5094 0.3711 0.0808  -0.0278 0.1148  100 GLU A O   
785   C CB  . GLU A 100 ? 0.3804 0.4709 0.3626 0.0520  -0.0515 0.0792  100 GLU A CB  
786   C CG  . GLU A 100 ? 0.3763 0.4557 0.3637 0.0429  -0.0646 0.0633  100 GLU A CG  
787   C CD  . GLU A 100 ? 0.3732 0.4563 0.3686 0.0377  -0.0746 0.0710  100 GLU A CD  
788   O OE1 . GLU A 100 ? 0.3738 0.4778 0.3774 0.0336  -0.0804 0.0897  100 GLU A OE1 
789   O OE2 . GLU A 100 ? 0.3732 0.4398 0.3674 0.0368  -0.0771 0.0596  100 GLU A OE2 
790   N N   . LEU A 101 ? 0.4058 0.4905 0.3628 0.0831  -0.0195 0.1014  101 LEU A N   
791   C CA  . LEU A 101 ? 0.4197 0.5138 0.3695 0.1002  -0.0135 0.1168  101 LEU A CA  
792   C C   . LEU A 101 ? 0.4332 0.5133 0.3708 0.1168  -0.0023 0.1181  101 LEU A C   
793   O O   . LEU A 101 ? 0.4377 0.5411 0.3794 0.1333  0.0017  0.1311  101 LEU A O   
794   C CB  . LEU A 101 ? 0.4400 0.5152 0.3693 0.1032  -0.0105 0.1172  101 LEU A CB  
795   C CG  . LEU A 101 ? 0.4606 0.5408 0.3791 0.1235  -0.0082 0.1320  101 LEU A CG  
796   C CD1 . LEU A 101 ? 0.4468 0.5749 0.3924 0.1284  -0.0176 0.1468  101 LEU A CD1 
797   C CD2 . LEU A 101 ? 0.4854 0.5422 0.3790 0.1227  -0.0086 0.1327  101 LEU A CD2 
798   N N   . LYS A 102 ? 0.4438 0.4868 0.3660 0.1135  0.0018  0.1045  102 LYS A N   
799   C CA  . LYS A 102 ? 0.4652 0.4833 0.3685 0.1286  0.0079  0.1019  102 LYS A CA  
800   C C   . LYS A 102 ? 0.4550 0.4958 0.3680 0.1337  0.0078  0.1061  102 LYS A C   
801   O O   . LYS A 102 ? 0.4760 0.5147 0.3729 0.1554  0.0154  0.1118  102 LYS A O   
802   C CB  . LYS A 102 ? 0.4773 0.4539 0.3696 0.1172  0.0063  0.0860  102 LYS A CB  
803   C CG  . LYS A 102 ? 0.5105 0.4499 0.3789 0.1195  0.0099  0.0863  102 LYS A CG  
804   C CD  . LYS A 102 ? 0.5180 0.4287 0.3882 0.0997  0.0070  0.0731  102 LYS A CD  
805   C CE  . LYS A 102 ? 0.5658 0.4230 0.4045 0.1056  0.0054  0.0724  102 LYS A CE  
806   N NZ  . LYS A 102 ? 0.5726 0.4072 0.4206 0.0854  -0.0013 0.0598  102 LYS A NZ  
807   N N   . HIS A 103 ? 0.4296 0.4892 0.3643 0.1151  -0.0008 0.1035  103 HIS A N   
808   C CA  . HIS A 103 ? 0.4241 0.5046 0.3667 0.1154  -0.0019 0.1110  103 HIS A CA  
809   C C   . HIS A 103 ? 0.4232 0.5505 0.3803 0.1258  0.0041  0.1332  103 HIS A C   
810   O O   . HIS A 103 ? 0.4336 0.5788 0.3876 0.1381  0.0131  0.1439  103 HIS A O   
811   C CB  . HIS A 103 ? 0.4039 0.4880 0.3637 0.0922  -0.0167 0.1040  103 HIS A CB  
812   C CG  . HIS A 103 ? 0.4041 0.5047 0.3687 0.0884  -0.0197 0.1145  103 HIS A CG  
813   N ND1 . HIS A 103 ? 0.4200 0.4969 0.3650 0.0943  -0.0178 0.1085  103 HIS A ND1 
814   C CD2 . HIS A 103 ? 0.3962 0.5332 0.3809 0.0779  -0.0252 0.1326  103 HIS A CD2 
815   C CE1 . HIS A 103 ? 0.4227 0.5203 0.3727 0.0881  -0.0197 0.1231  103 HIS A CE1 
816   N NE2 . HIS A 103 ? 0.4077 0.5433 0.3842 0.0764  -0.0241 0.1388  103 HIS A NE2 
817   N N   . LEU A 104 ? 0.4147 0.5638 0.3877 0.1214  -0.0008 0.1406  104 LEU A N   
818   C CA  . LEU A 104 ? 0.4141 0.6135 0.4085 0.1302  0.0015  0.1621  104 LEU A CA  
819   C C   . LEU A 104 ? 0.4395 0.6435 0.4174 0.1633  0.0184  0.1687  104 LEU A C   
820   O O   . LEU A 104 ? 0.4420 0.6929 0.4366 0.1762  0.0270  0.1863  104 LEU A O   
821   C CB  . LEU A 104 ? 0.4071 0.6178 0.4144 0.1216  -0.0109 0.1653  104 LEU A CB  
822   C CG  . LEU A 104 ? 0.3937 0.6516 0.4363 0.1054  -0.0259 0.1822  104 LEU A CG  
823   C CD1 . LEU A 104 ? 0.3828 0.6347 0.4343 0.0793  -0.0391 0.1784  104 LEU A CD1 
824   C CD2 . LEU A 104 ? 0.3969 0.6528 0.4401 0.1017  -0.0400 0.1817  104 LEU A CD2 
825   N N   . LEU A 105 ? 0.4634 0.6184 0.4080 0.1770  0.0226  0.1550  105 LEU A N   
826   C CA  . LEU A 105 ? 0.4998 0.6415 0.4170 0.2116  0.0347  0.1568  105 LEU A CA  
827   C C   . LEU A 105 ? 0.5191 0.6612 0.4202 0.2290  0.0465  0.1573  105 LEU A C   
828   O O   . LEU A 105 ? 0.5503 0.6988 0.4333 0.2629  0.0582  0.1628  105 LEU A O   
829   C CB  . LEU A 105 ? 0.5276 0.6039 0.4081 0.2160  0.0317  0.1415  105 LEU A CB  
830   C CG  . LEU A 105 ? 0.5352 0.6026 0.4122 0.2158  0.0260  0.1447  105 LEU A CG  
831   C CD1 . LEU A 105 ? 0.5656 0.5652 0.4067 0.2115  0.0234  0.1314  105 LEU A CD1 
832   C CD2 . LEU A 105 ? 0.5561 0.6513 0.4323 0.2483  0.0303  0.1587  105 LEU A CD2 
833   N N   . SER A 106 ? 0.5081 0.6396 0.4103 0.2093  0.0429  0.1507  106 SER A N   
834   C CA  . SER A 106 ? 0.5308 0.6618 0.4134 0.2241  0.0533  0.1526  106 SER A CA  
835   C C   . SER A 106 ? 0.5253 0.7284 0.4348 0.2332  0.0668  0.1773  106 SER A C   
836   O O   . SER A 106 ? 0.5535 0.7662 0.4427 0.2560  0.0822  0.1833  106 SER A O   
837   C CB  . SER A 106 ? 0.5225 0.6237 0.3998 0.1998  0.0428  0.1404  106 SER A CB  
838   O OG  . SER A 106 ? 0.4889 0.6262 0.4026 0.1707  0.0343  0.1499  106 SER A OG  
839   N N   . ARG A 107 ? 0.4941 0.7480 0.4484 0.2149  0.0606  0.1923  107 ARG A N   
840   C CA  . ARG A 107 ? 0.4881 0.8199 0.4792 0.2193  0.0711  0.2192  107 ARG A CA  
841   C C   . ARG A 107 ? 0.4963 0.8655 0.5003 0.2489  0.0785  0.2289  107 ARG A C   
842   O O   . ARG A 107 ? 0.4883 0.9314 0.5331 0.2516  0.0852  0.2522  107 ARG A O   
843   C CB  . ARG A 107 ? 0.4555 0.8220 0.4912 0.1786  0.0543  0.2320  107 ARG A CB  
844   C CG  . ARG A 107 ? 0.4546 0.8152 0.4890 0.1535  0.0509  0.2359  107 ARG A CG  
845   C CD  . ARG A 107 ? 0.4388 0.8576 0.5214 0.1230  0.0407  0.2616  107 ARG A CD  
846   N NE  . ARG A 107 ? 0.4339 0.8214 0.5139 0.0883  0.0211  0.2573  107 ARG A NE  
847   C CZ  . ARG A 107 ? 0.4478 0.8445 0.5265 0.0725  0.0233  0.2720  107 ARG A CZ  
848   N NH1 . ARG A 107 ? 0.4674 0.9101 0.5483 0.0869  0.0481  0.2941  107 ARG A NH1 
849   N NH2 . ARG A 107 ? 0.4473 0.8055 0.5194 0.0432  0.0004  0.2649  107 ARG A NH2 
850   N N   . ILE A 108 ? 0.5154 0.8347 0.4864 0.2702  0.0759  0.2126  108 ILE A N   
851   C CA  . ILE A 108 ? 0.5275 0.8709 0.5064 0.2977  0.0771  0.2196  108 ILE A CA  
852   C C   . ILE A 108 ? 0.5777 0.8851 0.5079 0.3450  0.0898  0.2100  108 ILE A C   
853   O O   . ILE A 108 ? 0.6034 0.8342 0.4852 0.3490  0.0859  0.1902  108 ILE A O   
854   C CB  . ILE A 108 ? 0.5132 0.8277 0.4959 0.2786  0.0568  0.2121  108 ILE A CB  
855   C CG1 . ILE A 108 ? 0.4723 0.8244 0.5002 0.2383  0.0417  0.2219  108 ILE A CG1 
856   C CG2 . ILE A 108 ? 0.5354 0.8636 0.5173 0.3097  0.0554  0.2181  108 ILE A CG2 
857   C CD1 . ILE A 108 ? 0.4628 0.7794 0.4855 0.2177  0.0226  0.2117  108 ILE A CD1 
858   N N   . ASN A 109 ? 0.5952 0.9587 0.5393 0.3813  0.1030  0.2243  109 ASN A N   
859   C CA  . ASN A 109 ? 0.6516 0.9854 0.5480 0.4340  0.1140  0.2158  109 ASN A CA  
860   C C   . ASN A 109 ? 0.6740 0.9980 0.5644 0.4607  0.1039  0.2148  109 ASN A C   
861   O O   . ASN A 109 ? 0.7287 0.9930 0.5646 0.4979  0.1035  0.2013  109 ASN A O   
862   C CB  . ASN A 109 ? 0.6699 1.0721 0.5762 0.4667  0.1402  0.2308  109 ASN A CB  
863   C CG  . ASN A 109 ? 0.6947 1.0571 0.5562 0.4704  0.1520  0.2210  109 ASN A CG  
864   O OD1 . ASN A 109 ? 0.7522 1.0788 0.5595 0.5148  0.1627  0.2102  109 ASN A OD1 
865   N ND2 . ASN A 109 ? 0.6586 1.0210 0.5374 0.4258  0.1474  0.2235  109 ASN A ND2 
866   N N   . HIS A 110 ? 0.6392 1.0158 0.5804 0.4433  0.0931  0.2289  110 HIS A N   
867   C CA  . HIS A 110 ? 0.6634 1.0279 0.5969 0.4677  0.0803  0.2286  110 HIS A CA  
868   C C   . HIS A 110 ? 0.6276 1.0065 0.5964 0.4324  0.0590  0.2354  110 HIS A C   
869   O O   . HIS A 110 ? 0.5843 1.0316 0.6099 0.4046  0.0554  0.2508  110 HIS A O   
870   C CB  . HIS A 110 ? 0.6895 1.1243 0.6426 0.5190  0.0937  0.2417  110 HIS A CB  
871   C CG  . HIS A 110 ? 0.7363 1.1365 0.6597 0.5583  0.0812  0.2360  110 HIS A CG  
872   N ND1 . HIS A 110 ? 0.7450 1.2187 0.7064 0.5924  0.0808  0.2505  110 HIS A ND1 
873   C CD2 . HIS A 110 ? 0.7811 1.0796 0.6404 0.5677  0.0666  0.2186  110 HIS A CD2 
874   C CE1 . HIS A 110 ? 0.7952 1.2094 0.7127 0.6242  0.0658  0.2407  110 HIS A CE1 
875   N NE2 . HIS A 110 ? 0.8194 1.1249 0.6730 0.6084  0.0571  0.2223  110 HIS A NE2 
876   N N   . PHE A 111 ? 0.6538 0.9628 0.5832 0.4344  0.0435  0.2244  111 PHE A N   
877   C CA  . PHE A 111 ? 0.6386 0.9514 0.5861 0.4128  0.0228  0.2299  111 PHE A CA  
878   C C   . PHE A 111 ? 0.6779 1.0026 0.6202 0.4548  0.0144  0.2365  111 PHE A C   
879   O O   . PHE A 111 ? 0.7292 1.0124 0.6271 0.4956  0.0197  0.2287  111 PHE A O   
880   C CB  . PHE A 111 ? 0.6466 0.8714 0.5495 0.3840  0.0124  0.2148  111 PHE A CB  
881   C CG  . PHE A 111 ? 0.6011 0.8248 0.5213 0.3370  0.0121  0.2098  111 PHE A CG  
882   C CD1 . PHE A 111 ? 0.5566 0.8455 0.5302 0.3112  0.0061  0.2212  111 PHE A CD1 
883   C CD2 . PHE A 111 ? 0.6078 0.7627 0.4908 0.3184  0.0148  0.1938  111 PHE A CD2 
884   C CE1 . PHE A 111 ? 0.5231 0.8033 0.5065 0.2718  0.0029  0.2149  111 PHE A CE1 
885   C CE2 . PHE A 111 ? 0.5697 0.7249 0.4689 0.2797  0.0135  0.1878  111 PHE A CE2 
886   C CZ  . PHE A 111 ? 0.5289 0.7439 0.4754 0.2582  0.0074  0.1975  111 PHE A CZ  
887   N N   . GLU A 112 ? 0.6594 1.0366 0.6446 0.4461  -0.0016 0.2499  112 GLU A N   
888   C CA  . GLU A 112 ? 0.6988 1.0744 0.6747 0.4800  -0.0173 0.2546  112 GLU A CA  
889   C C   . GLU A 112 ? 0.6987 1.0322 0.6593 0.4497  -0.0413 0.2533  112 GLU A C   
890   O O   . GLU A 112 ? 0.6584 1.0281 0.6574 0.4132  -0.0518 0.2598  112 GLU A O   
891   C CB  . GLU A 112 ? 0.6865 1.1714 0.7297 0.5046  -0.0174 0.2737  112 GLU A CB  
892   C CG  . GLU A 112 ? 0.7377 1.2214 0.7669 0.5545  -0.0302 0.2760  112 GLU A CG  
893   C CD  . GLU A 112 ? 0.7211 1.3215 0.8285 0.5721  -0.0363 0.2965  112 GLU A CD  
894   O OE1 . GLU A 112 ? 0.6880 1.3753 0.8514 0.5691  -0.0170 0.3089  112 GLU A OE1 
895   O OE2 . GLU A 112 ? 0.7446 1.3508 0.8578 0.5885  -0.0608 0.3014  112 GLU A OE2 
896   N N   . LYS A 113 ? 0.7510 1.0037 0.6504 0.4653  -0.0508 0.2453  113 LYS A N   
897   C CA  . LYS A 113 ? 0.7620 0.9663 0.6345 0.4389  -0.0702 0.2442  113 LYS A CA  
898   C C   . LYS A 113 ? 0.7727 1.0211 0.6720 0.4535  -0.0945 0.2571  113 LYS A C   
899   O O   . LYS A 113 ? 0.8021 1.0783 0.7099 0.4971  -0.0990 0.2631  113 LYS A O   
900   C CB  . LYS A 113 ? 0.8211 0.9196 0.6153 0.4466  -0.0703 0.2339  113 LYS A CB  
901   C CG  . LYS A 113 ? 0.8338 0.8753 0.5920 0.4127  -0.0815 0.2323  113 LYS A CG  
902   C CD  . LYS A 113 ? 0.8533 0.8141 0.5612 0.3913  -0.0687 0.2212  113 LYS A CD  
903   C CE  . LYS A 113 ? 0.9233 0.8113 0.5736 0.4232  -0.0694 0.2180  113 LYS A CE  
904   N NZ  . LYS A 113 ? 0.9409 0.7557 0.5507 0.3965  -0.0592 0.2090  113 LYS A NZ  
905   N N   . ILE A 114 ? 0.7525 1.0075 0.6644 0.4193  -0.1118 0.2605  114 ILE A N   
906   C CA  . ILE A 114 ? 0.7701 1.0541 0.6992 0.4291  -0.1407 0.2714  114 ILE A CA  
907   C C   . ILE A 114 ? 0.7918 1.0123 0.6742 0.4015  -0.1584 0.2672  114 ILE A C   
908   O O   . ILE A 114 ? 0.7718 0.9589 0.6357 0.3661  -0.1487 0.2585  114 ILE A O   
909   C CB  . ILE A 114 ? 0.7230 1.1140 0.7381 0.4185  -0.1509 0.2854  114 ILE A CB  
910   C CG1 . ILE A 114 ? 0.6718 1.0762 0.7112 0.3694  -0.1457 0.2826  114 ILE A CG1 
911   C CG2 . ILE A 114 ? 0.7138 1.1805 0.7770 0.4545  -0.1347 0.2941  114 ILE A CG2 
912   C CD1 . ILE A 114 ? 0.6443 1.1224 0.7486 0.3464  -0.1705 0.2964  114 ILE A CD1 
913   N N   . GLN A 115 ? 0.8366 1.0428 0.6991 0.4207  -0.1844 0.2736  115 GLN A N   
914   C CA  . GLN A 115 ? 0.8688 1.0162 0.6810 0.4003  -0.2030 0.2715  115 GLN A CA  
915   C C   . GLN A 115 ? 0.8378 1.0396 0.6966 0.3744  -0.2267 0.2764  115 GLN A C   
916   O O   . GLN A 115 ? 0.8289 1.1007 0.7438 0.3879  -0.2476 0.2876  115 GLN A O   
917   C CB  . GLN A 115 ? 0.9417 1.0399 0.7024 0.4344  -0.2229 0.2764  115 GLN A CB  
918   C CG  . GLN A 115 ? 0.9861 1.0262 0.6905 0.4185  -0.2446 0.2770  115 GLN A CG  
919   C CD  . GLN A 115 ? 1.0664 1.0470 0.7106 0.4526  -0.2634 0.2827  115 GLN A CD  
920   O OE1 . GLN A 115 ? 1.1129 1.0152 0.6921 0.4593  -0.2499 0.2805  115 GLN A OE1 
921   N NE2 . GLN A 115 ? 1.0877 1.1029 0.7529 0.4732  -0.2974 0.2910  115 GLN A NE2 
922   N N   . ILE A 116 ? 0.8260 0.9954 0.6616 0.3380  -0.2249 0.2681  116 ILE A N   
923   C CA  . ILE A 116 ? 0.8107 1.0117 0.6747 0.3123  -0.2519 0.2700  116 ILE A CA  
924   C C   . ILE A 116 ? 0.8700 1.0077 0.6679 0.3102  -0.2762 0.2674  116 ILE A C   
925   O O   . ILE A 116 ? 0.8878 1.0479 0.7012 0.3106  -0.3121 0.2736  116 ILE A O   
926   C CB  . ILE A 116 ? 0.7590 0.9749 0.6477 0.2756  -0.2378 0.2616  116 ILE A CB  
927   C CG1 . ILE A 116 ? 0.7580 0.9123 0.5965 0.2654  -0.2047 0.2479  116 ILE A CG1 
928   C CG2 . ILE A 116 ? 0.7052 1.0048 0.6742 0.2732  -0.2299 0.2704  116 ILE A CG2 
929   C CD1 . ILE A 116 ? 0.7324 0.8759 0.5682 0.2313  -0.2008 0.2363  116 ILE A CD1 
930   N N   . ILE A 117 ? 0.9049 0.9646 0.6288 0.3074  -0.2573 0.2594  117 ILE A N   
931   C CA  . ILE A 117 ? 0.9730 0.9656 0.6216 0.3100  -0.2741 0.2590  117 ILE A CA  
932   C C   . ILE A 117 ? 1.0286 0.9674 0.6246 0.3382  -0.2666 0.2651  117 ILE A C   
933   O O   . ILE A 117 ? 1.0282 0.9322 0.6005 0.3360  -0.2361 0.2618  117 ILE A O   
934   C CB  . ILE A 117 ? 0.9782 0.9233 0.5784 0.2810  -0.2573 0.2470  117 ILE A CB  
935   C CG1 . ILE A 117 ? 0.9655 0.9347 0.5844 0.2613  -0.2832 0.2411  117 ILE A CG1 
936   C CG2 . ILE A 117 ? 1.0531 0.9159 0.5611 0.2868  -0.2518 0.2485  117 ILE A CG2 
937   C CD1 . ILE A 117 ? 0.8933 0.9259 0.5877 0.2417  -0.2784 0.2374  117 ILE A CD1 
938   N N   . PRO A 118 ? 1.0813 1.0101 0.6585 0.3649  -0.2976 0.2742  118 PRO A N   
939   C CA  . PRO A 118 ? 1.1479 1.0100 0.6616 0.3912  -0.2941 0.2799  118 PRO A CA  
940   C C   . PRO A 118 ? 1.2074 0.9791 0.6280 0.3743  -0.2825 0.2789  118 PRO A C   
941   O O   . PRO A 118 ? 1.2231 0.9807 0.6158 0.3565  -0.2928 0.2758  118 PRO A O   
942   C CB  . PRO A 118 ? 1.1879 1.0696 0.7111 0.4244  -0.3350 0.2894  118 PRO A CB  
943   C CG  . PRO A 118 ? 1.1278 1.1050 0.7407 0.4162  -0.3543 0.2903  118 PRO A CG  
944   C CD  . PRO A 118 ? 1.0807 1.0649 0.7037 0.3747  -0.3382 0.2807  118 PRO A CD  
945   N N   . LYS A 119 ? 1.2456 0.9561 0.6171 0.3799  -0.2614 0.2821  119 LYS A N   
946   C CA  . LYS A 119 ? 1.3050 0.9336 0.5914 0.3610  -0.2454 0.2852  119 LYS A CA  
947   C C   . LYS A 119 ? 1.3912 0.9670 0.6067 0.3753  -0.2747 0.2946  119 LYS A C   
948   O O   . LYS A 119 ? 1.4310 0.9648 0.5869 0.3565  -0.2690 0.2957  119 LYS A O   
949   C CB  . LYS A 119 ? 1.3321 0.9068 0.5871 0.3626  -0.2215 0.2894  119 LYS A CB  
950   C CG  . LYS A 119 ? 1.3678 0.8803 0.5610 0.3304  -0.1937 0.2928  119 LYS A CG  
951   C CD  . LYS A 119 ? 1.3878 0.8541 0.5639 0.3277  -0.1741 0.2966  119 LYS A CD  
952   C CE  . LYS A 119 ? 1.4494 0.8432 0.5538 0.2982  -0.1529 0.3073  119 LYS A CE  
953   N NZ  . LYS A 119 ? 1.4944 0.8255 0.5693 0.2985  -0.1456 0.3150  119 LYS A NZ  
954   N N   . SER A 120 ? 1.4238 1.0030 0.6445 0.4111  -0.3060 0.3012  120 SER A N   
955   C CA  . SER A 120 ? 1.5061 1.0405 0.6658 0.4300  -0.3415 0.3098  120 SER A CA  
956   C C   . SER A 120 ? 1.4945 1.0612 0.6652 0.4172  -0.3644 0.3043  120 SER A C   
957   O O   . SER A 120 ? 1.5677 1.0798 0.6650 0.4189  -0.3831 0.3087  120 SER A O   
958   C CB  . SER A 120 ? 1.5293 1.0807 0.7133 0.4742  -0.3730 0.3156  120 SER A CB  
959   O OG  . SER A 120 ? 1.4493 1.1045 0.7370 0.4823  -0.3835 0.3099  120 SER A OG  
960   N N   . SER A 121 ? 1.4096 1.0600 0.6672 0.4042  -0.3642 0.2950  121 SER A N   
961   C CA  . SER A 121 ? 1.3961 1.0810 0.6746 0.3916  -0.3917 0.2890  121 SER A CA  
962   C C   . SER A 121 ? 1.4337 1.0642 0.6381 0.3672  -0.3809 0.2825  121 SER A C   
963   O O   . SER A 121 ? 1.4563 1.0873 0.6467 0.3639  -0.4115 0.2779  121 SER A O   
964   C CB  . SER A 121 ? 1.2983 1.0797 0.6852 0.3786  -0.3895 0.2826  121 SER A CB  
965   O OG  . SER A 121 ? 1.2646 1.0531 0.6549 0.3464  -0.3768 0.2713  121 SER A OG  
966   N N   . TRP A 122 ? 1.4464 1.0306 0.6026 0.3516  -0.3392 0.2824  122 TRP A N   
967   C CA  . TRP A 122 ? 1.4855 1.0244 0.5716 0.3316  -0.3223 0.2774  122 TRP A CA  
968   C C   . TRP A 122 ? 1.5968 1.0558 0.5788 0.3465  -0.3392 0.2883  122 TRP A C   
969   O O   . TRP A 122 ? 1.6509 1.0495 0.5651 0.3416  -0.3121 0.2985  122 TRP A O   
970   C CB  . TRP A 122 ? 1.4556 0.9858 0.5388 0.3078  -0.2704 0.2752  122 TRP A CB  
971   C CG  . TRP A 122 ? 1.3545 0.9560 0.5299 0.2928  -0.2547 0.2634  122 TRP A CG  
972   C CD1 . TRP A 122 ? 1.3007 0.9314 0.5323 0.2931  -0.2366 0.2647  122 TRP A CD1 
973   C CD2 . TRP A 122 ? 1.3031 0.9501 0.5193 0.2768  -0.2585 0.2484  122 TRP A CD2 
974   N NE1 . TRP A 122 ? 1.2178 0.9110 0.5225 0.2773  -0.2270 0.2525  122 TRP A NE1 
975   C CE2 . TRP A 122 ? 1.2174 0.9211 0.5152 0.2664  -0.2408 0.2428  122 TRP A CE2 
976   C CE3 . TRP A 122 ? 1.3288 0.9677 0.5145 0.2718  -0.2770 0.2387  122 TRP A CE3 
977   C CZ2 . TRP A 122 ? 1.1561 0.9082 0.5069 0.2492  -0.2411 0.2293  122 TRP A CZ2 
978   C CZ3 . TRP A 122 ? 1.2694 0.9543 0.5075 0.2559  -0.2789 0.2239  122 TRP A CZ3 
979   C CH2 . TRP A 122 ? 1.1835 0.9243 0.5041 0.2439  -0.2611 0.2201  122 TRP A CH2 
980   N N   . SER A 123 ? 1.2858 1.2453 0.5209 0.2392  -0.2405 0.3090  123 SER A N   
981   C CA  . SER A 123 ? 1.3620 1.2885 0.5353 0.2376  -0.2614 0.3280  123 SER A CA  
982   C C   . SER A 123 ? 1.3936 1.3064 0.5149 0.2042  -0.2464 0.3258  123 SER A C   
983   O O   . SER A 123 ? 1.4644 1.3341 0.5224 0.1951  -0.2540 0.3435  123 SER A O   
984   C CB  . SER A 123 ? 1.3668 1.3275 0.5550 0.2571  -0.2931 0.3304  123 SER A CB  
985   O OG  . SER A 123 ? 1.3205 1.3343 0.5385 0.2457  -0.2883 0.3114  123 SER A OG  
986   N N   . SER A 124 ? 1.3449 1.2940 0.4925 0.1859  -0.2256 0.3036  124 SER A N   
987   C CA  . SER A 124 ? 1.3682 1.3131 0.4750 0.1546  -0.2089 0.2954  124 SER A CA  
988   C C   . SER A 124 ? 1.3654 1.2838 0.4625 0.1338  -0.1763 0.2898  124 SER A C   
989   O O   . SER A 124 ? 1.3896 1.3014 0.4508 0.1069  -0.1593 0.2828  124 SER A O   
990   C CB  . SER A 124 ? 1.3206 1.3199 0.4628 0.1470  -0.2068 0.2722  124 SER A CB  
991   O OG  . SER A 124 ? 1.3446 1.3431 0.4490 0.1185  -0.1918 0.2613  124 SER A OG  
992   N N   . HIS A 125 ? 1.3380 1.2434 0.4676 0.1458  -0.1678 0.2914  125 HIS A N   
993   C CA  . HIS A 125 ? 1.3330 1.2144 0.4597 0.1281  -0.1388 0.2859  125 HIS A CA  
994   C C   . HIS A 125 ? 1.3689 1.2003 0.4782 0.1398  -0.1427 0.3059  125 HIS A C   
995   O O   . HIS A 125 ? 1.3846 1.2061 0.4982 0.1658  -0.1668 0.3202  125 HIS A O   
996   C CB  . HIS A 125 ? 1.2536 1.1723 0.4459 0.1282  -0.1212 0.2624  125 HIS A CB  
997   C CG  . HIS A 125 ? 1.2210 1.1826 0.4317 0.1135  -0.1142 0.2406  125 HIS A CG  
998   N ND1 . HIS A 125 ? 1.1955 1.1967 0.4326 0.1249  -0.1325 0.2347  125 HIS A ND1 
999   C CD2 . HIS A 125 ? 1.2117 1.1828 0.4200 0.0885  -0.0914 0.2218  125 HIS A CD2 
1000  C CE1 . HIS A 125 ? 1.1735 1.2036 0.4220 0.1075  -0.1222 0.2139  125 HIS A CE1 
1001  N NE2 . HIS A 125 ? 1.1824 1.1955 0.4148 0.0862  -0.0972 0.2050  125 HIS A NE2 
1002  N N   . GLU A 126 ? 1.3857 1.1859 0.4766 0.1204  -0.1195 0.3058  126 GLU A N   
1003  C CA  . GLU A 126 ? 1.4171 1.1680 0.4950 0.1287  -0.1204 0.3222  126 GLU A CA  
1004  C C   . GLU A 126 ? 1.3529 1.1198 0.4925 0.1407  -0.1084 0.3078  126 GLU A C   
1005  O O   . GLU A 126 ? 1.3076 1.0998 0.4770 0.1256  -0.0858 0.2876  126 GLU A O   
1006  C CB  . GLU A 126 ? 1.4746 1.1817 0.4968 0.0986  -0.1021 0.3309  126 GLU A CB  
1007  C CG  . GLU A 126 ? 1.5194 1.1678 0.5191 0.1040  -0.1055 0.3507  126 GLU A CG  
1008  C CD  . GLU A 126 ? 1.5747 1.1897 0.5447 0.1280  -0.1396 0.3760  126 GLU A CD  
1009  O OE1 . GLU A 126 ? 1.6337 1.2332 0.5495 0.1194  -0.1535 0.3911  126 GLU A OE1 
1010  O OE2 . GLU A 126 ? 1.5615 1.1654 0.5622 0.1558  -0.1530 0.3800  126 GLU A OE2 
1011  N N   . ALA A 127 ? 1.3518 1.1044 0.5105 0.1684  -0.1244 0.3171  127 ALA A N   
1012  C CA  . ALA A 127 ? 1.2912 1.0631 0.5082 0.1832  -0.1164 0.3036  127 ALA A CA  
1013  C C   . ALA A 127 ? 1.3139 1.0388 0.5263 0.1905  -0.1130 0.3121  127 ALA A C   
1014  O O   . ALA A 127 ? 1.2686 1.0047 0.5227 0.1966  -0.1018 0.2994  127 ALA A O   
1015  C CB  . ALA A 127 ? 1.2549 1.0677 0.5135 0.2114  -0.1364 0.2999  127 ALA A CB  
1016  N N   . SER A 128 ? 1.3860 1.0570 0.5468 0.1890  -0.1233 0.3334  128 SER A N   
1017  C CA  . SER A 128 ? 1.4162 1.0373 0.5706 0.1992  -0.1257 0.3433  128 SER A CA  
1018  C C   . SER A 128 ? 1.4424 1.0248 0.5693 0.1695  -0.1022 0.3448  128 SER A C   
1019  O O   . SER A 128 ? 1.4663 1.0062 0.5891 0.1743  -0.1018 0.3513  128 SER A O   
1020  C CB  . SER A 128 ? 1.4841 1.0644 0.6025 0.2195  -0.1559 0.3670  128 SER A CB  
1021  O OG  . SER A 128 ? 1.4561 1.0709 0.6126 0.2524  -0.1773 0.3629  128 SER A OG  
1022  N N   . LEU A 129 ? 1.4394 1.0375 0.5494 0.1389  -0.0826 0.3374  129 LEU A N   
1023  C CA  . LEU A 129 ? 1.4642 1.0328 0.5501 0.1077  -0.0582 0.3368  129 LEU A CA  
1024  C C   . LEU A 129 ? 1.3960 1.0030 0.5313 0.0952  -0.0322 0.3102  129 LEU A C   
1025  O O   . LEU A 129 ? 1.4079 1.0022 0.5327 0.0681  -0.0096 0.3045  129 LEU A O   
1026  C CB  . LEU A 129 ? 1.5221 1.0763 0.5472 0.0793  -0.0532 0.3478  129 LEU A CB  
1027  C CG  . LEU A 129 ? 1.6107 1.1074 0.5718 0.0816  -0.0752 0.3785  129 LEU A CG  
1028  C CD1 . LEU A 129 ? 1.6167 1.1266 0.5771 0.1109  -0.1073 0.3880  129 LEU A CD1 
1029  C CD2 . LEU A 129 ? 1.6707 1.1478 0.5694 0.0440  -0.0607 0.3874  129 LEU A CD2 
1030  N N   . GLY A 130 ? 1.3287 0.9823 0.5181 0.1144  -0.0361 0.2942  130 GLY A N   
1031  C CA  . GLY A 130 ? 1.2638 0.9538 0.5021 0.1054  -0.0160 0.2698  130 GLY A CA  
1032  C C   . GLY A 130 ? 1.2448 0.9164 0.5114 0.1129  -0.0098 0.2649  130 GLY A C   
1033  O O   . GLY A 130 ? 1.1938 0.8916 0.5057 0.1321  -0.0144 0.2544  130 GLY A O   
1034  N N   . VAL A 131 ? 1.2879 0.9147 0.5265 0.0961  0.0008  0.2723  131 VAL A N   
1035  C CA  . VAL A 131 ? 1.2798 0.8823 0.5393 0.1007  0.0063  0.2683  131 VAL A CA  
1036  C C   . VAL A 131 ? 1.2810 0.8767 0.5414 0.0692  0.0320  0.2572  131 VAL A C   
1037  O O   . VAL A 131 ? 1.2926 0.9015 0.5357 0.0443  0.0460  0.2528  131 VAL A O   
1038  C CB  . VAL A 131 ? 1.3394 0.8845 0.5666 0.1156  -0.0104 0.2899  131 VAL A CB  
1039  C CG1 . VAL A 131 ? 1.3439 0.8971 0.5702 0.1469  -0.0368 0.3004  131 VAL A CG1 
1040  C CG2 . VAL A 131 ? 1.4141 0.9101 0.5826 0.0897  -0.0050 0.3078  131 VAL A CG2 
1041  N N   . SER A 132 ? 1.2711 0.8483 0.5531 0.0705  0.0380  0.2511  132 SER A N   
1042  C CA  . SER A 132 ? 1.2702 0.8420 0.5597 0.0422  0.0611  0.2391  132 SER A CA  
1043  C C   . SER A 132 ? 1.2897 0.8182 0.5815 0.0450  0.0607  0.2426  132 SER A C   
1044  O O   . SER A 132 ? 1.2811 0.7982 0.5865 0.0721  0.0450  0.2458  132 SER A O   
1045  C CB  . SER A 132 ? 1.2009 0.8273 0.5429 0.0379  0.0731  0.2128  132 SER A CB  
1046  O OG  . SER A 132 ? 1.1951 0.8176 0.5553 0.0165  0.0921  0.1989  132 SER A OG  
1047  N N   . SER A 133 ? 1.3160 0.8224 0.5958 0.0161  0.0788  0.2404  133 SER A N   
1048  C CA  . SER A 133 ? 1.3357 0.8011 0.6189 0.0137  0.0806  0.2415  133 SER A CA  
1049  C C   . SER A 133 ? 1.2707 0.7649 0.6110 0.0244  0.0836  0.2188  133 SER A C   
1050  O O   . SER A 133 ? 1.2798 0.7444 0.6287 0.0309  0.0800  0.2178  133 SER A O   
1051  C CB  . SER A 133 ? 1.3838 0.8219 0.6393 -0.0239 0.1005  0.2449  133 SER A CB  
1052  O OG  . SER A 133 ? 1.3452 0.8294 0.6296 -0.0463 0.1223  0.2230  133 SER A OG  
1053  N N   . ALA A 134 ? 1.2083 0.7580 0.5856 0.0256  0.0891  0.2008  134 ALA A N   
1054  C CA  . ALA A 134 ? 1.1473 0.7265 0.5767 0.0360  0.0895  0.1806  134 ALA A CA  
1055  C C   . ALA A 134 ? 1.1273 0.7053 0.5692 0.0699  0.0699  0.1843  134 ALA A C   
1056  O O   . ALA A 134 ? 1.1025 0.6817 0.5730 0.0787  0.0682  0.1733  134 ALA A O   
1057  C CB  . ALA A 134 ? 1.0946 0.7294 0.5571 0.0282  0.0980  0.1622  134 ALA A CB  
1058  N N   . CYS A 135 ? 1.1390 0.7167 0.5598 0.0884  0.0554  0.1987  135 CYS A N   
1059  C CA  . CYS A 135 ? 1.1294 0.7051 0.5589 0.1209  0.0373  0.2030  135 CYS A CA  
1060  C C   . CYS A 135 ? 1.1928 0.7146 0.5821 0.1320  0.0243  0.2232  135 CYS A C   
1061  O O   . CYS A 135 ? 1.2148 0.7343 0.5807 0.1432  0.0119  0.2374  135 CYS A O   
1062  C CB  . CYS A 135 ? 1.0909 0.7139 0.5356 0.1366  0.0282  0.2016  135 CYS A CB  
1063  S SG  . CYS A 135 ? 1.0239 0.7062 0.5109 0.1229  0.0399  0.1806  135 CYS A SG  
1064  N N   . PRO A 136 ? 1.2243 0.7011 0.6059 0.1289  0.0256  0.2244  136 PRO A N   
1065  C CA  . PRO A 136 ? 1.2897 0.7092 0.6345 0.1398  0.0115  0.2432  136 PRO A CA  
1066  C C   . PRO A 136 ? 1.2857 0.7011 0.6446 0.1769  -0.0074 0.2422  136 PRO A C   
1067  O O   . PRO A 136 ? 1.2438 0.6825 0.6384 0.1888  -0.0056 0.2252  136 PRO A O   
1068  C CB  . PRO A 136 ? 1.3237 0.6993 0.6589 0.1175  0.0226  0.2418  136 PRO A CB  
1069  C CG  . PRO A 136 ? 1.2648 0.6766 0.6456 0.1126  0.0347  0.2181  136 PRO A CG  
1070  C CD  . PRO A 136 ? 1.2087 0.6818 0.6122 0.1106  0.0405  0.2091  136 PRO A CD  
1071  N N   . TYR A 137 ? 1.3317 0.7181 0.6621 0.1946  -0.0257 0.2597  137 TYR A N   
1072  C CA  . TYR A 137 ? 1.3397 0.7169 0.6814 0.2308  -0.0448 0.2588  137 TYR A CA  
1073  C C   . TYR A 137 ? 1.4198 0.7269 0.7220 0.2379  -0.0611 0.2778  137 TYR A C   
1074  O O   . TYR A 137 ? 1.4630 0.7490 0.7286 0.2319  -0.0697 0.2975  137 TYR A O   
1075  C CB  . TYR A 137 ? 1.3060 0.7334 0.6639 0.2533  -0.0558 0.2584  137 TYR A CB  
1076  C CG  . TYR A 137 ? 1.3194 0.7418 0.6891 0.2914  -0.0760 0.2574  137 TYR A CG  
1077  C CD1 . TYR A 137 ? 1.2911 0.7277 0.6947 0.3094  -0.0744 0.2389  137 TYR A CD1 
1078  C CD2 . TYR A 137 ? 1.3616 0.7674 0.7095 0.3098  -0.0970 0.2737  137 TYR A CD2 
1079  C CE1 . TYR A 137 ? 1.3041 0.7403 0.7208 0.3446  -0.0912 0.2350  137 TYR A CE1 
1080  C CE2 . TYR A 137 ? 1.3739 0.7787 0.7376 0.3461  -0.1158 0.2703  137 TYR A CE2 
1081  C CZ  . TYR A 137 ? 1.3445 0.7658 0.7435 0.3634  -0.1118 0.2501  137 TYR A CZ  
1082  O OH  . TYR A 137 ? 1.3579 0.7818 0.7745 0.3997  -0.1289 0.2440  137 TYR A OH  
1083  N N   . GLN A 138 ? 1.4420 0.7119 0.7508 0.2504  -0.0664 0.2716  138 GLN A N   
1084  C CA  . GLN A 138 ? 1.5220 0.7183 0.7963 0.2577  -0.0832 0.2879  138 GLN A CA  
1085  C C   . GLN A 138 ? 1.5780 0.7268 0.8055 0.2220  -0.0765 0.3082  138 GLN A C   
1086  O O   . GLN A 138 ? 1.6449 0.7460 0.8319 0.2242  -0.0931 0.3306  138 GLN A O   
1087  C CB  . GLN A 138 ? 1.5485 0.7402 0.8166 0.2925  -0.1093 0.2981  138 GLN A CB  
1088  C CG  . GLN A 138 ? 1.4921 0.7401 0.8067 0.3256  -0.1140 0.2782  138 GLN A CG  
1089  C CD  . GLN A 138 ? 1.5317 0.7565 0.8489 0.3649  -0.1402 0.2806  138 GLN A CD  
1090  O OE1 . GLN A 138 ? 1.5868 0.7768 0.8734 0.3723  -0.1596 0.3008  138 GLN A OE1 
1091  N NE2 . GLN A 138 ? 1.5060 0.7509 0.8598 0.3907  -0.1414 0.2591  138 GLN A NE2 
1092  N N   . GLY A 139 ? 1.5519 0.7154 0.7854 0.1888  -0.0525 0.2998  139 GLY A N   
1093  C CA  . GLY A 139 ? 1.6013 0.7266 0.7946 0.1505  -0.0410 0.3153  139 GLY A CA  
1094  C C   . GLY A 139 ? 1.6069 0.7535 0.7714 0.1328  -0.0363 0.3293  139 GLY A C   
1095  O O   . GLY A 139 ? 1.6507 0.7697 0.7783 0.0995  -0.0255 0.3424  139 GLY A O   
1096  N N   . LYS A 140 ? 1.5637 0.7609 0.7448 0.1534  -0.0438 0.3256  140 LYS A N   
1097  C CA  . LYS A 140 ? 1.5680 0.7886 0.7233 0.1408  -0.0425 0.3371  140 LYS A CA  
1098  C C   . LYS A 140 ? 1.4855 0.7823 0.6809 0.1371  -0.0268 0.3164  140 LYS A C   
1099  O O   . LYS A 140 ? 1.4271 0.7598 0.6689 0.1551  -0.0255 0.2974  140 LYS A O   
1100  C CB  . LYS A 140 ? 1.6034 0.8091 0.7376 0.1701  -0.0711 0.3543  140 LYS A CB  
1101  C CG  . LYS A 140 ? 1.6976 0.8230 0.7816 0.1692  -0.0890 0.3796  140 LYS A CG  
1102  C CD  . LYS A 140 ? 1.7211 0.8240 0.8128 0.2120  -0.1196 0.3845  140 LYS A CD  
1103  C CE  . LYS A 140 ? 1.8165 0.8322 0.8635 0.2118  -0.1383 0.4073  140 LYS A CE  
1104  N NZ  . LYS A 140 ? 1.8848 0.8679 0.8743 0.2018  -0.1539 0.4362  140 LYS A NZ  
1105  N N   . SER A 141 ? 1.4849 0.8044 0.6607 0.1132  -0.0155 0.3201  141 SER A N   
1106  C CA  . SER A 141 ? 1.4135 0.8012 0.6245 0.1070  -0.0012 0.3009  141 SER A CA  
1107  C C   . SER A 141 ? 1.3726 0.8024 0.6082 0.1388  -0.0182 0.2973  141 SER A C   
1108  O O   . SER A 141 ? 1.4076 0.8243 0.6170 0.1540  -0.0376 0.3136  141 SER A O   
1109  C CB  . SER A 141 ? 1.4318 0.8302 0.6122 0.0739  0.0141  0.3050  141 SER A CB  
1110  O OG  . SER A 141 ? 1.4609 0.8321 0.6270 0.0416  0.0341  0.3040  141 SER A OG  
1111  N N   . SER A 142 ? 1.3012 0.7811 0.5868 0.1476  -0.0114 0.2763  142 SER A N   
1112  C CA  . SER A 142 ? 1.2580 0.7818 0.5728 0.1756  -0.0250 0.2707  142 SER A CA  
1113  C C   . SER A 142 ? 1.1903 0.7744 0.5411 0.1650  -0.0115 0.2522  142 SER A C   
1114  O O   . SER A 142 ? 1.1834 0.7747 0.5314 0.1374  0.0062  0.2452  142 SER A O   
1115  C CB  . SER A 142 ? 1.2477 0.7631 0.5888 0.2043  -0.0355 0.2648  142 SER A CB  
1116  O OG  . SER A 142 ? 1.2150 0.7709 0.5814 0.2315  -0.0491 0.2610  142 SER A OG  
1117  N N   . PHE A 143 ? 1.1432 0.7704 0.5283 0.1864  -0.0201 0.2438  143 PHE A N   
1118  C CA  . PHE A 143 ? 1.0808 0.7623 0.5020 0.1784  -0.0104 0.2269  143 PHE A CA  
1119  C C   . PHE A 143 ? 1.0351 0.7517 0.4963 0.2028  -0.0187 0.2176  143 PHE A C   
1120  O O   . PHE A 143 ? 1.0516 0.7557 0.5123 0.2270  -0.0319 0.2234  143 PHE A O   
1121  C CB  . PHE A 143 ? 1.0816 0.7879 0.4875 0.1680  -0.0118 0.2308  143 PHE A CB  
1122  C CG  . PHE A 143 ? 1.0326 0.7811 0.4664 0.1502  0.0018  0.2133  143 PHE A CG  
1123  C CD1 . PHE A 143 ? 1.0282 0.7695 0.4665 0.1260  0.0207  0.2024  143 PHE A CD1 
1124  C CD2 . PHE A 143 ? 0.9931 0.7883 0.4505 0.1576  -0.0049 0.2070  143 PHE A CD2 
1125  C CE1 . PHE A 143 ? 0.9856 0.7649 0.4526 0.1116  0.0315  0.1848  143 PHE A CE1 
1126  C CE2 . PHE A 143 ? 0.9521 0.7821 0.4358 0.1419  0.0055  0.1906  143 PHE A CE2 
1127  C CZ  . PHE A 143 ? 0.9485 0.7703 0.4375 0.1199  0.0233  0.1791  143 PHE A CZ  
1128  N N   . PHE A 144 ? 0.9808 0.7406 0.4763 0.1958  -0.0111 0.2028  144 PHE A N   
1129  C CA  . PHE A 144 ? 0.9378 0.7367 0.4688 0.2143  -0.0180 0.1950  144 PHE A CA  
1130  C C   . PHE A 144 ? 0.9507 0.7636 0.4752 0.2356  -0.0351 0.2055  144 PHE A C   
1131  O O   . PHE A 144 ? 0.9543 0.7832 0.4679 0.2299  -0.0397 0.2107  144 PHE A O   
1132  C CB  . PHE A 144 ? 0.8861 0.7286 0.4476 0.2004  -0.0108 0.1817  144 PHE A CB  
1133  C CG  . PHE A 144 ? 0.8722 0.7064 0.4444 0.1791  0.0042  0.1698  144 PHE A CG  
1134  C CD1 . PHE A 144 ? 0.8581 0.6842 0.4489 0.1821  0.0081  0.1612  144 PHE A CD1 
1135  C CD2 . PHE A 144 ? 0.8741 0.7110 0.4391 0.1563  0.0141  0.1654  144 PHE A CD2 
1136  C CE1 . PHE A 144 ? 0.8458 0.6662 0.4493 0.1631  0.0200  0.1495  144 PHE A CE1 
1137  C CE2 . PHE A 144 ? 0.8610 0.6943 0.4409 0.1377  0.0276  0.1523  144 PHE A CE2 
1138  C CZ  . PHE A 144 ? 0.8465 0.6714 0.4465 0.1412  0.0297  0.1447  144 PHE A CZ  
1139  N N   . ARG A 145 ? 0.9590 0.7675 0.4916 0.2603  -0.0447 0.2069  145 ARG A N   
1140  C CA  . ARG A 145 ? 0.9780 0.7962 0.5062 0.2834  -0.0624 0.2161  145 ARG A CA  
1141  C C   . ARG A 145 ? 0.9399 0.8149 0.4932 0.2872  -0.0681 0.2124  145 ARG A C   
1142  O O   . ARG A 145 ? 0.9571 0.8426 0.5033 0.2999  -0.0827 0.2208  145 ARG A O   
1143  C CB  . ARG A 145 ? 0.9916 0.7976 0.5302 0.3101  -0.0699 0.2138  145 ARG A CB  
1144  C CG  . ARG A 145 ? 1.0365 0.7826 0.5505 0.3099  -0.0681 0.2181  145 ARG A CG  
1145  C CD  . ARG A 145 ? 1.0646 0.7950 0.5827 0.3410  -0.0818 0.2183  145 ARG A CD  
1146  N NE  . ARG A 145 ? 1.1053 0.7783 0.6044 0.3409  -0.0800 0.2198  145 ARG A NE  
1147  C CZ  . ARG A 145 ? 1.1621 0.7801 0.6229 0.3344  -0.0861 0.2350  145 ARG A CZ  
1148  N NH1 . ARG A 145 ? 1.1868 0.7992 0.6210 0.3275  -0.0944 0.2506  145 ARG A NH1 
1149  N NH2 . ARG A 145 ? 1.1975 0.7645 0.6447 0.3335  -0.0843 0.2350  145 ARG A NH2 
1150  N N   . ASN A 146 ? 0.8916 0.8020 0.4745 0.2763  -0.0581 0.2001  146 ASN A N   
1151  C CA  . ASN A 146 ? 0.8555 0.8192 0.4652 0.2789  -0.0634 0.1961  146 ASN A CA  
1152  C C   . ASN A 146 ? 0.8499 0.8286 0.4512 0.2607  -0.0641 0.1982  146 ASN A C   
1153  O O   . ASN A 146 ? 0.8301 0.8482 0.4479 0.2636  -0.0720 0.1974  146 ASN A O   
1154  C CB  . ASN A 146 ? 0.8105 0.8040 0.4544 0.2756  -0.0549 0.1835  146 ASN A CB  
1155  C CG  . ASN A 146 ? 0.8139 0.8087 0.4703 0.2973  -0.0566 0.1798  146 ASN A CG  
1156  O OD1 . ASN A 146 ? 0.8300 0.8351 0.4889 0.3186  -0.0675 0.1835  146 ASN A OD1 
1157  N ND2 . ASN A 146 ? 0.8008 0.7861 0.4659 0.2924  -0.0465 0.1710  146 ASN A ND2 
1158  N N   . VAL A 147 ? 0.8693 0.8179 0.4455 0.2415  -0.0554 0.1996  147 VAL A N   
1159  C CA  . VAL A 147 ? 0.8697 0.8302 0.4344 0.2236  -0.0545 0.1993  147 VAL A CA  
1160  C C   . VAL A 147 ? 0.9236 0.8448 0.4421 0.2164  -0.0556 0.2111  147 VAL A C   
1161  O O   . VAL A 147 ? 0.9557 0.8349 0.4526 0.2158  -0.0509 0.2168  147 VAL A O   
1162  C CB  . VAL A 147 ? 0.8342 0.8083 0.4189 0.2016  -0.0402 0.1848  147 VAL A CB  
1163  C CG1 . VAL A 147 ? 0.7861 0.8021 0.4120 0.2055  -0.0428 0.1759  147 VAL A CG1 
1164  C CG2 . VAL A 147 ? 0.8422 0.7823 0.4214 0.1918  -0.0262 0.1804  147 VAL A CG2 
1165  N N   . VAL A 148 ? 0.9364 0.8708 0.4383 0.2095  -0.0623 0.2148  148 VAL A N   
1166  C CA  . VAL A 148 ? 0.9927 0.8930 0.4456 0.2020  -0.0657 0.2278  148 VAL A CA  
1167  C C   . VAL A 148 ? 0.9962 0.8941 0.4335 0.1729  -0.0493 0.2196  148 VAL A C   
1168  O O   . VAL A 148 ? 0.9670 0.8998 0.4213 0.1630  -0.0471 0.2081  148 VAL A O   
1169  C CB  . VAL A 148 ? 1.0130 0.9290 0.4525 0.2148  -0.0865 0.2380  148 VAL A CB  
1170  C CG1 . VAL A 148 ? 1.0806 0.9530 0.4647 0.2112  -0.0941 0.2555  148 VAL A CG1 
1171  C CG2 . VAL A 148 ? 0.9973 0.9333 0.4662 0.2435  -0.1018 0.2403  148 VAL A CG2 
1172  N N   . TRP A 149 ? 1.0341 0.8911 0.4401 0.1588  -0.0377 0.2245  149 TRP A N   
1173  C CA  . TRP A 149 ? 1.0475 0.9013 0.4341 0.1305  -0.0210 0.2169  149 TRP A CA  
1174  C C   . TRP A 149 ? 1.0962 0.9418 0.4355 0.1240  -0.0299 0.2291  149 TRP A C   
1175  O O   . TRP A 149 ? 1.1529 0.9578 0.4481 0.1241  -0.0357 0.2472  149 TRP A O   
1176  C CB  . TRP A 149 ? 1.0708 0.8864 0.4437 0.1159  -0.0041 0.2172  149 TRP A CB  
1177  C CG  . TRP A 149 ? 1.0754 0.8952 0.4407 0.0861  0.0172  0.2040  149 TRP A CG  
1178  C CD1 . TRP A 149 ? 1.0684 0.9178 0.4316 0.0717  0.0223  0.1927  149 TRP A CD1 
1179  C CD2 . TRP A 149 ? 1.0906 0.8857 0.4508 0.0670  0.0365  0.1991  149 TRP A CD2 
1180  N NE1 . TRP A 149 ? 1.0767 0.9234 0.4354 0.0459  0.0444  0.1798  149 TRP A NE1 
1181  C CE2 . TRP A 149 ? 1.0900 0.9046 0.4474 0.0419  0.0536  0.1839  149 TRP A CE2 
1182  C CE3 . TRP A 149 ? 1.1057 0.8653 0.4650 0.0685  0.0409  0.2047  149 TRP A CE3 
1183  C CZ2 . TRP A 149 ? 1.1026 0.9055 0.4586 0.0182  0.0756  0.1740  149 TRP A CZ2 
1184  C CZ3 . TRP A 149 ? 1.1185 0.8640 0.4751 0.0440  0.0618  0.1961  149 TRP A CZ3 
1185  C CH2 . TRP A 149 ? 1.1169 0.8855 0.4728 0.0191  0.0793  0.1809  149 TRP A CH2 
1186  N N   . LEU A 150 ? 1.0767 0.9595 0.4242 0.1180  -0.0324 0.2192  150 LEU A N   
1187  C CA  . LEU A 150 ? 1.1200 1.0010 0.4247 0.1130  -0.0432 0.2288  150 LEU A CA  
1188  C C   . LEU A 150 ? 1.1548 1.0230 0.4219 0.0830  -0.0246 0.2238  150 LEU A C   
1189  O O   . LEU A 150 ? 1.1253 1.0109 0.4158 0.0663  -0.0049 0.2039  150 LEU A O   
1190  C CB  . LEU A 150 ? 1.0857 1.0136 0.4168 0.1210  -0.0563 0.2198  150 LEU A CB  
1191  C CG  . LEU A 150 ? 1.0601 1.0072 0.4226 0.1493  -0.0768 0.2261  150 LEU A CG  
1192  C CD1 . LEU A 150 ? 1.0264 1.0213 0.4159 0.1507  -0.0864 0.2150  150 LEU A CD1 
1193  C CD2 . LEU A 150 ? 1.1117 1.0287 0.4394 0.1669  -0.0966 0.2487  150 LEU A CD2 
1194  N N   . ILE A 151 ? 1.2201 1.0584 0.4289 0.0764  -0.0317 0.2417  151 ILE A N   
1195  C CA  . ILE A 151 ? 1.2637 1.0904 0.4275 0.0464  -0.0147 0.2390  151 ILE A CA  
1196  C C   . ILE A 151 ? 1.3107 1.1383 0.4264 0.0434  -0.0305 0.2499  151 ILE A C   
1197  O O   . ILE A 151 ? 1.3180 1.1465 0.4307 0.0655  -0.0565 0.2633  151 ILE A O   
1198  C CB  . ILE A 151 ? 1.3122 1.0889 0.4406 0.0320  -0.0015 0.2524  151 ILE A CB  
1199  C CG1 . ILE A 151 ? 1.3730 1.1033 0.4564 0.0462  -0.0242 0.2828  151 ILE A CG1 
1200  C CG2 . ILE A 151 ? 1.2666 1.0427 0.4428 0.0350  0.0125  0.2409  151 ILE A CG2 
1201  C CD1 . ILE A 151 ? 1.4226 1.0985 0.4733 0.0341  -0.0148 0.2980  151 ILE A CD1 
1202  N N   . LYS A 152 ? 1.3440 1.1729 0.4225 0.0156  -0.0146 0.2426  152 LYS A N   
1203  C CA  . LYS A 152 ? 1.3935 1.2242 0.4207 0.0078  -0.0268 0.2501  152 LYS A CA  
1204  C C   . LYS A 152 ? 1.4645 1.2478 0.4343 0.0163  -0.0492 0.2832  152 LYS A C   
1205  O O   . LYS A 152 ? 1.4962 1.2356 0.4462 0.0146  -0.0457 0.2997  152 LYS A O   
1206  C CB  . LYS A 152 ? 1.4218 1.2593 0.4167 -0.0265 -0.0006 0.2350  152 LYS A CB  
1207  C CG  . LYS A 152 ? 1.4773 1.2708 0.4270 -0.0493 0.0179  0.2480  152 LYS A CG  
1208  C CD  . LYS A 152 ? 1.4863 1.2982 0.4256 -0.0829 0.0504  0.2251  152 LYS A CD  
1209  C CE  . LYS A 152 ? 1.5614 1.3289 0.4378 -0.1101 0.0660  0.2426  152 LYS A CE  
1210  N NZ  . LYS A 152 ? 1.5826 1.3719 0.4386 -0.1448 0.0968  0.2208  152 LYS A NZ  
1211  N N   . LYS A 153 ? 1.4915 1.2827 0.4353 0.0253  -0.0737 0.2924  153 LYS A N   
1212  C CA  . LYS A 153 ? 1.5669 1.3136 0.4516 0.0326  -0.0986 0.3236  153 LYS A CA  
1213  C C   . LYS A 153 ? 1.6367 1.3734 0.4492 0.0056  -0.0965 0.3293  153 LYS A C   
1214  O O   . LYS A 153 ? 1.6241 1.3994 0.4379 -0.0004 -0.0979 0.3133  153 LYS A O   
1215  C CB  . LYS A 153 ? 1.5502 1.3113 0.4606 0.0672  -0.1333 0.3324  153 LYS A CB  
1216  C CG  . LYS A 153 ? 1.6141 1.3231 0.4857 0.0845  -0.1602 0.3641  153 LYS A CG  
1217  C CD  . LYS A 153 ? 1.6337 1.3535 0.4992 0.1088  -0.1978 0.3758  153 LYS A CD  
1218  C CE  . LYS A 153 ? 1.5946 1.3231 0.5163 0.1464  -0.2177 0.3785  153 LYS A CE  
1219  N NZ  . LYS A 153 ? 1.5027 1.2871 0.5021 0.1575  -0.2066 0.3531  153 LYS A NZ  
1220  N N   . ASN A 154 ? 1.7134 1.3972 0.4616 -0.0112 -0.0937 0.3522  154 ASN A N   
1221  C CA  . ASN A 154 ? 1.7909 1.4586 0.4609 -0.0416 -0.0884 0.3602  154 ASN A CA  
1222  C C   . ASN A 154 ? 1.7657 1.4767 0.4435 -0.0701 -0.0559 0.3285  154 ASN A C   
1223  O O   . ASN A 154 ? 1.7958 1.5253 0.4367 -0.0841 -0.0579 0.3219  154 ASN A O   
1224  C CB  . ASN A 154 ? 1.8380 1.5010 0.4675 -0.0283 -0.1249 0.3777  154 ASN A CB  
1225  C CG  . ASN A 154 ? 1.9408 1.5645 0.4743 -0.0566 -0.1267 0.3986  154 ASN A CG  
1226  O OD1 . ASN A 154 ? 1.9906 1.5724 0.4823 -0.0798 -0.1092 0.4119  154 ASN A OD1 
1227  N ND2 . ASN A 154 ? 1.9761 1.6127 0.4726 -0.0563 -0.1484 0.4020  154 ASN A ND2 
1228  N N   . SER A 155 ? 1.7115 1.4386 0.4392 -0.0774 -0.0271 0.3077  155 SER A N   
1229  C CA  . SER A 155 ? 1.6869 1.4528 0.4293 -0.1035 0.0057  0.2756  155 SER A CA  
1230  C C   . SER A 155 ? 1.6320 1.4546 0.4170 -0.0933 -0.0001 0.2482  155 SER A C   
1231  O O   . SER A 155 ? 1.6433 1.4932 0.4121 -0.1149 0.0158  0.2269  155 SER A O   
1232  C CB  . SER A 155 ? 1.7717 1.5164 0.4336 -0.1409 0.0232  0.2824  155 SER A CB  
1233  O OG  . SER A 155 ? 1.7526 1.5237 0.4322 -0.1679 0.0614  0.2538  155 SER A OG  
1234  N N   . THR A 156 ? 1.5762 1.4163 0.4148 -0.0614 -0.0230 0.2482  156 THR A N   
1235  C CA  . THR A 156 ? 1.5198 1.4121 0.4061 -0.0512 -0.0297 0.2230  156 THR A CA  
1236  C C   . THR A 156 ? 1.4420 1.3524 0.4055 -0.0229 -0.0389 0.2179  156 THR A C   
1237  O O   . THR A 156 ? 1.4437 1.3325 0.4121 -0.0001 -0.0594 0.2399  156 THR A O   
1238  C CB  . THR A 156 ? 1.5552 1.4553 0.4060 -0.0433 -0.0592 0.2325  156 THR A CB  
1239  O OG1 . THR A 156 ? 1.5381 1.4316 0.4124 -0.0113 -0.0902 0.2516  156 THR A OG1 
1240  C CG2 . THR A 156 ? 1.6507 1.5163 0.4102 -0.0654 -0.0607 0.2515  156 THR A CG2 
1241  N N   . TYR A 157 ? 1.3782 1.3272 0.4005 -0.0245 -0.0242 0.1887  157 TYR A N   
1242  C CA  . TYR A 157 ? 1.3054 1.2756 0.3995 -0.0006 -0.0327 0.1823  157 TYR A CA  
1243  C C   . TYR A 157 ? 1.2702 1.2842 0.3968 0.0073  -0.0473 0.1654  157 TYR A C   
1244  O O   . TYR A 157 ? 1.2356 1.2795 0.3949 -0.0031 -0.0335 0.1378  157 TYR A O   
1245  C CB  . TYR A 157 ? 1.2597 1.2350 0.3993 -0.0079 -0.0070 0.1644  157 TYR A CB  
1246  C CG  . TYR A 157 ? 1.1979 1.1810 0.3988 0.0157  -0.0151 0.1655  157 TYR A CG  
1247  C CD1 . TYR A 157 ? 1.1416 1.1630 0.3956 0.0285  -0.0258 0.1510  157 TYR A CD1 
1248  C CD2 . TYR A 157 ? 1.1993 1.1507 0.4031 0.0239  -0.0120 0.1810  157 TYR A CD2 
1249  C CE1 . TYR A 157 ? 1.0899 1.1189 0.3956 0.0476  -0.0320 0.1526  157 TYR A CE1 
1250  C CE2 . TYR A 157 ? 1.1466 1.1061 0.4030 0.0445  -0.0184 0.1809  157 TYR A CE2 
1251  C CZ  . TYR A 157 ? 1.0925 1.0915 0.3985 0.0559  -0.0280 0.1670  157 TYR A CZ  
1252  O OH  . TYR A 157 ? 1.0444 1.0520 0.3987 0.0742  -0.0334 0.1675  157 TYR A OH  
1253  N N   . PRO A 158 ? 1.2820 1.2996 0.4006 0.0257  -0.0763 0.1811  158 PRO A N   
1254  C CA  . PRO A 158 ? 1.2494 1.3085 0.4010 0.0329  -0.0918 0.1662  158 PRO A CA  
1255  C C   . PRO A 158 ? 1.1743 1.2606 0.4014 0.0463  -0.0906 0.1532  158 PRO A C   
1256  O O   . PRO A 158 ? 1.1497 1.2222 0.4015 0.0581  -0.0868 0.1625  158 PRO A O   
1257  C CB  . PRO A 158 ? 1.2836 1.3363 0.4080 0.0502  -0.1234 0.1894  158 PRO A CB  
1258  C CG  . PRO A 158 ? 1.3135 1.3238 0.4135 0.0608  -0.1267 0.2160  158 PRO A CG  
1259  C CD  . PRO A 158 ? 1.3315 1.3146 0.4083 0.0392  -0.0970 0.2125  158 PRO A CD  
1260  N N   . THR A 159 ? 1.1425 1.2655 0.4037 0.0434  -0.0944 0.1319  159 THR A N   
1261  C CA  . THR A 159 ? 1.0765 1.2249 0.4063 0.0528  -0.0944 0.1195  159 THR A CA  
1262  C C   . THR A 159 ? 1.0575 1.2095 0.4115 0.0773  -0.1143 0.1391  159 THR A C   
1263  O O   . THR A 159 ? 1.0830 1.2384 0.4169 0.0880  -0.1360 0.1531  159 THR A O   
1264  C CB  . THR A 159 ? 1.0535 1.2376 0.4110 0.0450  -0.0996 0.0951  159 THR A CB  
1265  O OG1 . THR A 159 ? 1.0792 1.2621 0.4112 0.0232  -0.0819 0.0748  159 THR A OG1 
1266  C CG2 . THR A 159 ? 0.9892 1.1940 0.4145 0.0508  -0.0977 0.0825  159 THR A CG2 
1267  N N   . ILE A 160 ? 1.0152 1.1676 0.4125 0.0860  -0.1067 0.1388  160 ILE A N   
1268  C CA  . ILE A 160 ? 0.9929 1.1523 0.4190 0.1086  -0.1213 0.1537  160 ILE A CA  
1269  C C   . ILE A 160 ? 0.9452 1.1446 0.4254 0.1118  -0.1301 0.1412  160 ILE A C   
1270  O O   . ILE A 160 ? 0.9124 1.1219 0.4234 0.1010  -0.1182 0.1237  160 ILE A O   
1271  C CB  . ILE A 160 ? 0.9763 1.1119 0.4155 0.1154  -0.1076 0.1606  160 ILE A CB  
1272  C CG1 . ILE A 160 ? 1.0294 1.1219 0.4149 0.1123  -0.1009 0.1756  160 ILE A CG1 
1273  C CG2 . ILE A 160 ? 0.9467 1.0961 0.4216 0.1380  -0.1205 0.1709  160 ILE A CG2 
1274  C CD1 . ILE A 160 ? 1.0190 1.0848 0.4125 0.1117  -0.0829 0.1775  160 ILE A CD1 
1275  N N   . LYS A 161 ? 0.9454 1.1671 0.4374 0.1260  -0.1516 0.1503  161 LYS A N   
1276  C CA  . LYS A 161 ? 0.9021 1.1617 0.4467 0.1293  -0.1604 0.1421  161 LYS A CA  
1277  C C   . LYS A 161 ? 0.8916 1.1626 0.4584 0.1511  -0.1720 0.1576  161 LYS A C   
1278  O O   . LYS A 161 ? 0.9161 1.1952 0.4697 0.1635  -0.1904 0.1687  161 LYS A O   
1279  C CB  . LYS A 161 ? 0.9110 1.1972 0.4545 0.1209  -0.1756 0.1321  161 LYS A CB  
1280  C CG  . LYS A 161 ? 0.9241 1.2036 0.4493 0.0997  -0.1641 0.1127  161 LYS A CG  
1281  C CD  . LYS A 161 ? 0.9253 1.2340 0.4599 0.0914  -0.1793 0.0992  161 LYS A CD  
1282  C CE  . LYS A 161 ? 0.9409 1.2435 0.4581 0.0714  -0.1671 0.0767  161 LYS A CE  
1283  N NZ  . LYS A 161 ? 0.9591 1.2837 0.4688 0.0635  -0.1834 0.0647  161 LYS A NZ  
1284  N N   . ARG A 162 ? 0.8588 1.1314 0.4596 0.1560  -0.1617 0.1571  162 ARG A N   
1285  C CA  . ARG A 162 ? 0.8496 1.1333 0.4722 0.1764  -0.1689 0.1691  162 ARG A CA  
1286  C C   . ARG A 162 ? 0.8055 1.1213 0.4803 0.1749  -0.1668 0.1621  162 ARG A C   
1287  O O   . ARG A 162 ? 0.7801 1.0916 0.4717 0.1617  -0.1540 0.1517  162 ARG A O   
1288  C CB  . ARG A 162 ? 0.8649 1.1112 0.4668 0.1869  -0.1584 0.1797  162 ARG A CB  
1289  C CG  . ARG A 162 ? 0.9184 1.1345 0.4714 0.1952  -0.1669 0.1936  162 ARG A CG  
1290  C CD  . ARG A 162 ? 0.9363 1.1741 0.4903 0.2128  -0.1916 0.2034  162 ARG A CD  
1291  N NE  . ARG A 162 ? 0.9593 1.1762 0.5036 0.2353  -0.1984 0.2180  162 ARG A NE  
1292  C CZ  . ARG A 162 ? 1.0085 1.1811 0.5054 0.2384  -0.2005 0.2305  162 ARG A CZ  
1293  N NH1 . ARG A 162 ? 1.0396 1.1871 0.4929 0.2190  -0.1943 0.2306  162 ARG A NH1 
1294  N NH2 . ARG A 162 ? 1.0297 1.1826 0.5223 0.2602  -0.2086 0.2427  162 ARG A NH2 
1295  N N   . SER A 163 ? 0.8017 1.1501 0.5017 0.1880  -0.1803 0.1678  163 SER A N   
1296  C CA  . SER A 163 ? 0.7667 1.1493 0.5136 0.1855  -0.1796 0.1633  163 SER A CA  
1297  C C   . SER A 163 ? 0.7680 1.1656 0.5328 0.2063  -0.1817 0.1726  163 SER A C   
1298  O O   . SER A 163 ? 0.7929 1.1947 0.5466 0.2235  -0.1942 0.1806  163 SER A O   
1299  C CB  . SER A 163 ? 0.7590 1.1784 0.5257 0.1756  -0.1944 0.1570  163 SER A CB  
1300  O OG  . SER A 163 ? 0.7243 1.1761 0.5347 0.1703  -0.1939 0.1542  163 SER A OG  
1301  N N   . TYR A 164 ? 0.7477 1.1527 0.5395 0.2052  -0.1702 0.1706  164 TYR A N   
1302  C CA  . TYR A 164 ? 0.7480 1.1752 0.5621 0.2231  -0.1706 0.1758  164 TYR A CA  
1303  C C   . TYR A 164 ? 0.7253 1.1950 0.5816 0.2135  -0.1693 0.1715  164 TYR A C   
1304  O O   . TYR A 164 ? 0.7032 1.1670 0.5695 0.1964  -0.1600 0.1667  164 TYR A O   
1305  C CB  . TYR A 164 ? 0.7500 1.1439 0.5516 0.2334  -0.1566 0.1788  164 TYR A CB  
1306  C CG  . TYR A 164 ? 0.7359 1.1571 0.5654 0.2487  -0.1543 0.1800  164 TYR A CG  
1307  C CD1 . TYR A 164 ? 0.7553 1.1905 0.5876 0.2724  -0.1650 0.1845  164 TYR A CD1 
1308  C CD2 . TYR A 164 ? 0.7061 1.1413 0.5597 0.2393  -0.1424 0.1757  164 TYR A CD2 
1309  C CE1 . TYR A 164 ? 0.7436 1.2083 0.6042 0.2869  -0.1618 0.1825  164 TYR A CE1 
1310  C CE2 . TYR A 164 ? 0.6962 1.1596 0.5735 0.2517  -0.1387 0.1753  164 TYR A CE2 
1311  C CZ  . TYR A 164 ? 0.7140 1.1937 0.5960 0.2757  -0.1474 0.1776  164 TYR A CZ  
1312  O OH  . TYR A 164 ? 0.7051 1.2163 0.6128 0.2886  -0.1423 0.1743  164 TYR A OH  
1313  N N   . ASN A 165 ? 0.7388 1.2508 0.6198 0.2245  -0.1791 0.1735  165 ASN A N   
1314  C CA  . ASN A 165 ? 0.7265 1.2836 0.6474 0.2150  -0.1775 0.1707  165 ASN A CA  
1315  C C   . ASN A 165 ? 0.7047 1.2736 0.6408 0.2281  -0.1659 0.1719  165 ASN A C   
1316  O O   . ASN A 165 ? 0.7194 1.2956 0.6557 0.2513  -0.1694 0.1738  165 ASN A O   
1317  C CB  . ASN A 165 ? 0.7568 1.3597 0.6993 0.2170  -0.1946 0.1701  165 ASN A CB  
1318  C CG  . ASN A 165 ? 0.7666 1.4138 0.7476 0.1986  -0.1940 0.1670  165 ASN A CG  
1319  O OD1 . ASN A 165 ? 0.7465 1.3941 0.7391 0.1878  -0.1808 0.1669  165 ASN A OD1 
1320  N ND2 . ASN A 165 ? 0.8152 1.4992 0.8150 0.1939  -0.2093 0.1651  165 ASN A ND2 
1321  N N   . ASN A 166 ? 0.6697 1.2402 0.6182 0.2134  -0.1532 0.1703  166 ASN A N   
1322  C CA  . ASN A 166 ? 0.6518 1.2341 0.6123 0.2227  -0.1408 0.1701  166 ASN A CA  
1323  C C   . ASN A 166 ? 0.6352 1.2782 0.6316 0.2257  -0.1432 0.1685  166 ASN A C   
1324  O O   . ASN A 166 ? 0.6167 1.2881 0.6347 0.2059  -0.1395 0.1683  166 ASN A O   
1325  C CB  . ASN A 166 ? 0.6345 1.1953 0.5919 0.2047  -0.1277 0.1695  166 ASN A CB  
1326  C CG  . ASN A 166 ? 0.6319 1.1933 0.5909 0.2154  -0.1142 0.1686  166 ASN A CG  
1327  O OD1 . ASN A 166 ? 0.6452 1.2072 0.6003 0.2389  -0.1131 0.1675  166 ASN A OD1 
1328  N ND2 . ASN A 166 ? 0.6169 1.1761 0.5807 0.1985  -0.1050 0.1688  166 ASN A ND2 
1329  N N   . THR A 167 ? 0.6410 1.3033 0.6443 0.2504  -0.1498 0.1673  167 THR A N   
1330  C CA  . THR A 167 ? 0.6291 1.3536 0.6702 0.2569  -0.1523 0.1634  167 THR A CA  
1331  C C   . THR A 167 ? 0.6167 1.3611 0.6720 0.2650  -0.1357 0.1587  167 THR A C   
1332  O O   . THR A 167 ? 0.6102 1.4107 0.6990 0.2665  -0.1332 0.1538  167 THR A O   
1333  C CB  . THR A 167 ? 0.6496 1.3895 0.6961 0.2820  -0.1694 0.1624  167 THR A CB  
1334  O OG1 . THR A 167 ? 0.6713 1.3708 0.6929 0.3072  -0.1688 0.1634  167 THR A OG1 
1335  C CG2 . THR A 167 ? 0.6577 1.3883 0.6923 0.2722  -0.1868 0.1659  167 THR A CG2 
1336  N N   . ASN A 168 ? 0.6131 1.3135 0.6434 0.2696  -0.1241 0.1591  168 ASN A N   
1337  C CA  . ASN A 168 ? 0.6038 1.3182 0.6424 0.2749  -0.1076 0.1537  168 ASN A CA  
1338  C C   . ASN A 168 ? 0.5790 1.3158 0.6293 0.2449  -0.0977 0.1557  168 ASN A C   
1339  O O   . ASN A 168 ? 0.5700 1.2849 0.6103 0.2224  -0.1017 0.1616  168 ASN A O   
1340  C CB  . ASN A 168 ? 0.6143 1.2721 0.6214 0.2855  -0.0991 0.1536  168 ASN A CB  
1341  C CG  . ASN A 168 ? 0.6365 1.2490 0.6180 0.3036  -0.1105 0.1570  168 ASN A CG  
1342  O OD1 . ASN A 168 ? 0.6568 1.2658 0.6380 0.3304  -0.1146 0.1537  168 ASN A OD1 
1343  N ND2 . ASN A 168 ? 0.6361 1.2127 0.5954 0.2885  -0.1159 0.1632  168 ASN A ND2 
1344  N N   . GLN A 169 ? 0.5693 1.3485 0.6397 0.2439  -0.0853 0.1505  169 GLN A N   
1345  C CA  . GLN A 169 ? 0.5527 1.3479 0.6281 0.2139  -0.0754 0.1543  169 GLN A CA  
1346  C C   . GLN A 169 ? 0.5512 1.3029 0.5988 0.2099  -0.0633 0.1552  169 GLN A C   
1347  O O   . GLN A 169 ? 0.5524 1.3239 0.6023 0.2051  -0.0494 0.1521  169 GLN A O   
1348  C CB  . GLN A 169 ? 0.5492 1.4157 0.6588 0.2081  -0.0676 0.1493  169 GLN A CB  
1349  C CG  . GLN A 169 ? 0.5588 1.4545 0.6793 0.2321  -0.0549 0.1373  169 GLN A CG  
1350  C CD  . GLN A 169 ? 0.5558 1.5139 0.7005 0.2151  -0.0399 0.1332  169 GLN A CD  
1351  O OE1 . GLN A 169 ? 0.5612 1.5699 0.7321 0.2320  -0.0329 0.1210  169 GLN A OE1 
1352  N NE2 . GLN A 169 ? 0.5492 1.5043 0.6855 0.1811  -0.0354 0.1432  169 GLN A NE2 
1353  N N   . GLU A 170 ? 0.5490 1.2425 0.5701 0.2114  -0.0689 0.1589  170 GLU A N   
1354  C CA  . GLU A 170 ? 0.5482 1.1952 0.5432 0.2084  -0.0605 0.1594  170 GLU A CA  
1355  C C   . GLU A 170 ? 0.5406 1.1395 0.5181 0.1947  -0.0690 0.1650  170 GLU A C   
1356  O O   . GLU A 170 ? 0.5400 1.1337 0.5188 0.1957  -0.0804 0.1666  170 GLU A O   
1357  C CB  . GLU A 170 ? 0.5629 1.1866 0.5441 0.2375  -0.0555 0.1523  170 GLU A CB  
1358  C CG  . GLU A 170 ? 0.5704 1.2322 0.5648 0.2520  -0.0437 0.1431  170 GLU A CG  
1359  C CD  . GLU A 170 ? 0.5793 1.2773 0.5962 0.2775  -0.0493 0.1363  170 GLU A CD  
1360  O OE1 . GLU A 170 ? 0.5768 1.2861 0.6046 0.2779  -0.0628 0.1405  170 GLU A OE1 
1361  O OE2 . GLU A 170 ? 0.5904 1.3061 0.6149 0.2979  -0.0413 0.1257  170 GLU A OE2 
1362  N N   . ASP A 171 ? 0.5355 1.1012 0.4972 0.1817  -0.0638 0.1668  171 ASP A N   
1363  C CA  . ASP A 171 ? 0.5314 1.0471 0.4760 0.1745  -0.0694 0.1683  171 ASP A CA  
1364  C C   . ASP A 171 ? 0.5420 1.0249 0.4684 0.1981  -0.0681 0.1643  171 ASP A C   
1365  O O   . ASP A 171 ? 0.5520 1.0388 0.4748 0.2171  -0.0612 0.1603  171 ASP A O   
1366  C CB  . ASP A 171 ? 0.5282 1.0176 0.4628 0.1578  -0.0650 0.1699  171 ASP A CB  
1367  C CG  . ASP A 171 ? 0.5211 1.0325 0.4693 0.1312  -0.0692 0.1764  171 ASP A CG  
1368  O OD1 . ASP A 171 ? 0.5160 1.0520 0.4808 0.1215  -0.0775 0.1792  171 ASP A OD1 
1369  O OD2 . ASP A 171 ? 0.5237 1.0252 0.4646 0.1190  -0.0653 0.1791  171 ASP A OD2 
1370  N N   . LEU A 172 ? 0.5418 0.9925 0.4562 0.1961  -0.0748 0.1648  172 LEU A N   
1371  C CA  . LEU A 172 ? 0.5567 0.9735 0.4505 0.2145  -0.0744 0.1631  172 LEU A CA  
1372  C C   . LEU A 172 ? 0.5558 0.9248 0.4315 0.2048  -0.0721 0.1615  172 LEU A C   
1373  O O   . LEU A 172 ? 0.5470 0.9094 0.4254 0.1884  -0.0772 0.1611  172 LEU A O   
1374  C CB  . LEU A 172 ? 0.5664 0.9951 0.4606 0.2239  -0.0851 0.1652  172 LEU A CB  
1375  C CG  . LEU A 172 ? 0.5913 0.9889 0.4630 0.2452  -0.0864 0.1659  172 LEU A CG  
1376  C CD1 . LEU A 172 ? 0.6030 1.0213 0.4830 0.2690  -0.0852 0.1641  172 LEU A CD1 
1377  C CD2 . LEU A 172 ? 0.6037 0.9957 0.4648 0.2454  -0.0981 0.1692  172 LEU A CD2 
1378  N N   . LEU A 173 ? 0.5656 0.9025 0.4247 0.2152  -0.0645 0.1590  173 LEU A N   
1379  C CA  . LEU A 173 ? 0.5677 0.8605 0.4109 0.2074  -0.0612 0.1563  173 LEU A CA  
1380  C C   . LEU A 173 ? 0.5858 0.8549 0.4099 0.2148  -0.0641 0.1577  173 LEU A C   
1381  O O   . LEU A 173 ? 0.6068 0.8613 0.4163 0.2324  -0.0630 0.1597  173 LEU A O   
1382  C CB  . LEU A 173 ? 0.5738 0.8420 0.4074 0.2133  -0.0521 0.1528  173 LEU A CB  
1383  C CG  . LEU A 173 ? 0.5797 0.8030 0.3983 0.2068  -0.0479 0.1490  173 LEU A CG  
1384  C CD1 . LEU A 173 ? 0.5615 0.7817 0.3916 0.1852  -0.0506 0.1458  173 LEU A CD1 
1385  C CD2 . LEU A 173 ? 0.5903 0.7907 0.3990 0.2156  -0.0403 0.1454  173 LEU A CD2 
1386  N N   . VAL A 174 ? 0.5805 0.8443 0.4036 0.2006  -0.0682 0.1563  174 VAL A N   
1387  C CA  . VAL A 174 ? 0.6002 0.8419 0.4015 0.2029  -0.0701 0.1574  174 VAL A CA  
1388  C C   . VAL A 174 ? 0.6040 0.8074 0.3923 0.1922  -0.0616 0.1518  174 VAL A C   
1389  O O   . VAL A 174 ? 0.5857 0.7884 0.3882 0.1770  -0.0598 0.1451  174 VAL A O   
1390  C CB  . VAL A 174 ? 0.5963 0.8602 0.4035 0.1938  -0.0798 0.1573  174 VAL A CB  
1391  C CG1 . VAL A 174 ? 0.6240 0.8681 0.4036 0.1980  -0.0827 0.1599  174 VAL A CG1 
1392  C CG2 . VAL A 174 ? 0.5865 0.8946 0.4147 0.1996  -0.0882 0.1612  174 VAL A CG2 
1393  N N   . LEU A 175 ? 0.6297 0.8014 0.3924 0.1999  -0.0572 0.1543  175 LEU A N   
1394  C CA  . LEU A 175 ? 0.6381 0.7748 0.3872 0.1890  -0.0480 0.1489  175 LEU A CA  
1395  C C   . LEU A 175 ? 0.6630 0.7853 0.3870 0.1843  -0.0483 0.1508  175 LEU A C   
1396  O O   . LEU A 175 ? 0.6862 0.8076 0.3921 0.1961  -0.0549 0.1598  175 LEU A O   
1397  C CB  . LEU A 175 ? 0.6532 0.7603 0.3902 0.1989  -0.0408 0.1504  175 LEU A CB  
1398  C CG  . LEU A 175 ? 0.6364 0.7538 0.3912 0.2053  -0.0394 0.1483  175 LEU A CG  
1399  C CD1 . LEU A 175 ? 0.6586 0.7445 0.3975 0.2173  -0.0338 0.1492  175 LEU A CD1 
1400  C CD2 . LEU A 175 ? 0.6101 0.7329 0.3852 0.1885  -0.0371 0.1400  175 LEU A CD2 
1401  N N   . TRP A 176 ? 0.6605 0.7721 0.3833 0.1671  -0.0417 0.1417  176 TRP A N   
1402  C CA  . TRP A 176 ? 0.6886 0.7835 0.3832 0.1594  -0.0383 0.1419  176 TRP A CA  
1403  C C   . TRP A 176 ? 0.6896 0.7639 0.3837 0.1429  -0.0249 0.1303  176 TRP A C   
1404  O O   . TRP A 176 ? 0.6673 0.7405 0.3848 0.1388  -0.0206 0.1223  176 TRP A O   
1405  C CB  . TRP A 176 ? 0.6859 0.8074 0.3823 0.1543  -0.0475 0.1401  176 TRP A CB  
1406  C CG  . TRP A 176 ? 0.6565 0.7977 0.3820 0.1398  -0.0477 0.1262  176 TRP A CG  
1407  C CD1 . TRP A 176 ? 0.6586 0.7961 0.3837 0.1238  -0.0416 0.1128  176 TRP A CD1 
1408  C CD2 . TRP A 176 ? 0.6242 0.7911 0.3836 0.1399  -0.0552 0.1239  176 TRP A CD2 
1409  N NE1 . TRP A 176 ? 0.6297 0.7869 0.3883 0.1158  -0.0465 0.1018  176 TRP A NE1 
1410  C CE2 . TRP A 176 ? 0.6094 0.7831 0.3877 0.1244  -0.0553 0.1097  176 TRP A CE2 
1411  C CE3 . TRP A 176 ? 0.6093 0.7942 0.3842 0.1507  -0.0616 0.1319  176 TRP A CE3 
1412  C CZ2 . TRP A 176 ? 0.5824 0.7757 0.3930 0.1192  -0.0635 0.1057  176 TRP A CZ2 
1413  C CZ3 . TRP A 176 ? 0.5822 0.7895 0.3873 0.1436  -0.0676 0.1282  176 TRP A CZ3 
1414  C CH2 . TRP A 176 ? 0.5701 0.7791 0.3918 0.1278  -0.0694 0.1162  176 TRP A CH2 
1415  N N   . GLY A 177 ? 0.7179 0.7771 0.3852 0.1329  -0.0184 0.1290  177 GLY A N   
1416  C CA  . GLY A 177 ? 0.7230 0.7654 0.3896 0.1164  -0.0037 0.1168  177 GLY A CA  
1417  C C   . GLY A 177 ? 0.7431 0.7881 0.3914 0.1009  0.0024  0.1090  177 GLY A C   
1418  O O   . GLY A 177 ? 0.7619 0.8143 0.3882 0.1031  -0.0049 0.1159  177 GLY A O   
1419  N N   . ILE A 178 ? 0.7402 0.7808 0.3989 0.0852  0.0159  0.0931  178 ILE A N   
1420  C CA  . ILE A 178 ? 0.7636 0.8053 0.4039 0.0681  0.0267  0.0824  178 ILE A CA  
1421  C C   . ILE A 178 ? 0.7892 0.8035 0.4123 0.0565  0.0443  0.0810  178 ILE A C   
1422  O O   . ILE A 178 ? 0.7736 0.7778 0.4178 0.0578  0.0486  0.0778  178 ILE A O   
1423  C CB  . ILE A 178 ? 0.7354 0.8047 0.4119 0.0584  0.0272  0.0592  178 ILE A CB  
1424  C CG1 . ILE A 178 ? 0.7623 0.8395 0.4162 0.0433  0.0358  0.0479  178 ILE A CG1 
1425  C CG2 . ILE A 178 ? 0.7102 0.7777 0.4240 0.0534  0.0346  0.0444  178 ILE A CG2 
1426  C CD1 . ILE A 178 ? 0.7495 0.8422 0.4332 0.0288  0.0467  0.0199  178 ILE A CD1 
1427  N N   . HIS A 179 ? 0.8311 0.8334 0.4147 0.0438  0.0541  0.0837  179 HIS A N   
1428  C CA  . HIS A 179 ? 0.8604 0.8382 0.4257 0.0283  0.0725  0.0820  179 HIS A CA  
1429  C C   . HIS A 179 ? 0.8596 0.8559 0.4388 0.0071  0.0897  0.0569  179 HIS A C   
1430  O O   . HIS A 179 ? 0.8679 0.8838 0.4378 0.0000  0.0905  0.0478  179 HIS A O   
1431  C CB  . HIS A 179 ? 0.9161 0.8632 0.4235 0.0256  0.0733  0.1034  179 HIS A CB  
1432  C CG  . HIS A 179 ? 0.9525 0.8743 0.4366 0.0054  0.0931  0.1026  179 HIS A CG  
1433  N ND1 . HIS A 179 ? 0.9985 0.9141 0.4410 -0.0147 0.1055  0.1031  179 HIS A ND1 
1434  C CD2 . HIS A 179 ? 0.9515 0.8539 0.4482 0.0004  0.1031  0.1007  179 HIS A CD2 
1435  C CE1 . HIS A 179 ? 1.0247 0.9184 0.4552 -0.0321 0.1231  0.1024  179 HIS A CE1 
1436  N NE2 . HIS A 179 ? 0.9963 0.8814 0.4604 -0.0230 0.1215  0.1006  179 HIS A NE2 
1437  N N   . HIS A 180 ? 0.8513 0.8426 0.4538 -0.0023 0.1032  0.0445  180 HIS A N   
1438  C CA  . HIS A 180 ? 0.8520 0.8616 0.4725 -0.0223 0.1214  0.0186  180 HIS A CA  
1439  C C   . HIS A 180 ? 0.9004 0.8871 0.4824 -0.0423 0.1417  0.0237  180 HIS A C   
1440  O O   . HIS A 180 ? 0.9069 0.8700 0.4897 -0.0441 0.1467  0.0308  180 HIS A O   
1441  C CB  . HIS A 180 ? 0.8091 0.8322 0.4878 -0.0196 0.1211  -0.0005 180 HIS A CB  
1442  C CG  . HIS A 180 ? 0.7661 0.8081 0.4814 -0.0025 0.1010  -0.0040 180 HIS A CG  
1443  N ND1 . HIS A 180 ? 0.7409 0.8114 0.4954 -0.0051 0.0985  -0.0281 180 HIS A ND1 
1444  C CD2 . HIS A 180 ? 0.7468 0.7831 0.4655 0.0162  0.0826  0.0131  180 HIS A CD2 
1445  C CE1 . HIS A 180 ? 0.7093 0.7882 0.4876 0.0100  0.0787  -0.0236 180 HIS A CE1 
1446  N NE2 . HIS A 180 ? 0.7117 0.7721 0.4687 0.0225  0.0699  0.0010  180 HIS A NE2 
1447  N N   . PRO A 181 ? 0.9378 0.9305 0.4837 -0.0589 0.1532  0.0203  181 PRO A N   
1448  C CA  . PRO A 181 ? 0.9912 0.9612 0.4936 -0.0811 0.1728  0.0275  181 PRO A CA  
1449  C C   . PRO A 181 ? 0.9874 0.9740 0.5200 -0.1023 0.1968  0.0011  181 PRO A C   
1450  O O   . PRO A 181 ? 0.9474 0.9670 0.5319 -0.1003 0.1982  -0.0258 181 PRO A O   
1451  C CB  . PRO A 181 ? 1.0311 1.0064 0.4846 -0.0903 0.1741  0.0323  181 PRO A CB  
1452  C CG  . PRO A 181 ? 0.9920 1.0070 0.4824 -0.0823 0.1666  0.0098  181 PRO A CG  
1453  C CD  . PRO A 181 ? 0.9356 0.9561 0.4777 -0.0590 0.1484  0.0093  181 PRO A CD  
1454  N N   . ASN A 182 ? 1.0313 0.9946 0.5324 -0.1228 0.2146  0.0089  182 ASN A N   
1455  C CA  . ASN A 182 ? 1.0327 1.0116 0.5615 -0.1452 0.2391  -0.0150 182 ASN A CA  
1456  C C   . ASN A 182 ? 1.0416 1.0600 0.5762 -0.1642 0.2584  -0.0438 182 ASN A C   
1457  O O   . ASN A 182 ? 1.0106 1.0619 0.5997 -0.1686 0.2683  -0.0749 182 ASN A O   
1458  C CB  . ASN A 182 ? 1.0835 1.0246 0.5724 -0.1644 0.2529  0.0034  182 ASN A CB  
1459  C CG  . ASN A 182 ? 1.0688 0.9766 0.5700 -0.1482 0.2385  0.0209  182 ASN A CG  
1460  O OD1 . ASN A 182 ? 1.0316 0.9506 0.5845 -0.1444 0.2393  0.0049  182 ASN A OD1 
1461  N ND2 . ASN A 182 ? 1.0996 0.9667 0.5541 -0.1378 0.2241  0.0525  182 ASN A ND2 
1462  N N   . ASP A 183 ? 1.0861 1.1011 0.5647 -0.1747 0.2626  -0.0342 183 ASP A N   
1463  C CA  . ASP A 183 ? 1.1042 1.1553 0.5782 -0.1944 0.2824  -0.0610 183 ASP A CA  
1464  C C   . ASP A 183 ? 1.1301 1.1821 0.5557 -0.1908 0.2717  -0.0506 183 ASP A C   
1465  O O   . ASP A 183 ? 1.1384 1.1617 0.5313 -0.1745 0.2499  -0.0208 183 ASP A O   
1466  C CB  . ASP A 183 ? 1.1543 1.2026 0.6019 -0.2287 0.3139  -0.0661 183 ASP A CB  
1467  C CG  . ASP A 183 ? 1.2138 1.2110 0.5908 -0.2397 0.3136  -0.0274 183 ASP A CG  
1468  O OD1 . ASP A 183 ? 1.2410 1.2152 0.5666 -0.2309 0.2971  -0.0021 183 ASP A OD1 
1469  O OD2 . ASP A 183 ? 1.2357 1.2148 0.6096 -0.2574 0.3289  -0.0226 183 ASP A OD2 
1470  N N   . ALA A 184 ? 1.1440 1.2307 0.5669 -0.2056 0.2870  -0.0772 184 ALA A N   
1471  C CA  . ALA A 184 ? 1.1707 1.2632 0.5493 -0.2046 0.2782  -0.0726 184 ALA A CA  
1472  C C   . ALA A 184 ? 1.2388 1.2918 0.5329 -0.2163 0.2768  -0.0367 184 ALA A C   
1473  O O   . ALA A 184 ? 1.2542 1.2973 0.5117 -0.2052 0.2570  -0.0195 184 ALA A O   
1474  C CB  . ALA A 184 ? 1.1792 1.3160 0.5695 -0.2217 0.2989  -0.1113 184 ALA A CB  
1475  N N   . ALA A 185 ? 1.2815 1.3114 0.5459 -0.2392 0.2965  -0.0255 185 ALA A N   
1476  C CA  . ALA A 185 ? 1.3526 1.3380 0.5359 -0.2521 0.2944  0.0108  185 ALA A CA  
1477  C C   . ALA A 185 ? 1.3445 1.2872 0.5170 -0.2248 0.2635  0.0466  185 ALA A C   
1478  O O   . ALA A 185 ? 1.3883 1.3022 0.5023 -0.2210 0.2473  0.0746  185 ALA A O   
1479  C CB  . ALA A 185 ? 1.3991 1.3699 0.5590 -0.2849 0.3234  0.0128  185 ALA A CB  
1480  N N   . GLU A 186 ? 1.2909 1.2305 0.5201 -0.2055 0.2549  0.0445  186 GLU A N   
1481  C CA  . GLU A 186 ? 1.2782 1.1828 0.5054 -0.1780 0.2271  0.0737  186 GLU A CA  
1482  C C   . GLU A 186 ? 1.2443 1.1655 0.4840 -0.1505 0.2005  0.0755  186 GLU A C   
1483  O O   . GLU A 186 ? 1.2598 1.1535 0.4705 -0.1330 0.1776  0.1031  186 GLU A O   
1484  C CB  . GLU A 186 ? 1.2330 1.1320 0.5159 -0.1675 0.2273  0.0685  186 GLU A CB  
1485  C CG  . GLU A 186 ? 1.2259 1.0877 0.5046 -0.1412 0.2019  0.0970  186 GLU A CG  
1486  C CD  . GLU A 186 ? 1.2079 1.0512 0.5195 -0.1394 0.2065  0.0971  186 GLU A CD  
1487  O OE1 . GLU A 186 ? 1.1488 1.0186 0.5222 -0.1286 0.2058  0.0762  186 GLU A OE1 
1488  O OE2 . GLU A 186 ? 1.2547 1.0548 0.5291 -0.1490 0.2093  0.1184  186 GLU A OE2 
1489  N N   . GLN A 187 ? 1.1998 1.1658 0.4849 -0.1467 0.2029  0.0455  187 GLN A N   
1490  C CA  . GLN A 187 ? 1.1708 1.1565 0.4686 -0.1251 0.1797  0.0440  187 GLN A CA  
1491  C C   . GLN A 187 ? 1.2273 1.1997 0.4570 -0.1295 0.1700  0.0632  187 GLN A C   
1492  O O   . GLN A 187 ? 1.2254 1.1857 0.4426 -0.1085 0.1443  0.0839  187 GLN A O   
1493  C CB  . GLN A 187 ? 1.1274 1.1606 0.4778 -0.1267 0.1870  0.0063  187 GLN A CB  
1494  C CG  . GLN A 187 ? 1.1068 1.1622 0.4650 -0.1109 0.1660  0.0014  187 GLN A CG  
1495  C CD  . GLN A 187 ? 1.0700 1.1148 0.4492 -0.0821 0.1379  0.0216  187 GLN A CD  
1496  O OE1 . GLN A 187 ? 1.0283 1.0700 0.4518 -0.0701 0.1344  0.0212  187 GLN A OE1 
1497  N NE2 . GLN A 187 ? 1.0868 1.1278 0.4345 -0.0714 0.1179  0.0385  187 GLN A NE2 
1498  N N   . THR A 188 ? 1.2797 1.2557 0.4657 -0.1573 0.1905  0.0557  188 THR A N   
1499  C CA  . THR A 188 ? 1.3420 1.3042 0.4567 -0.1654 0.1825  0.0733  188 THR A CA  
1500  C C   . THR A 188 ? 1.3925 1.3011 0.4532 -0.1620 0.1690  0.1140  188 THR A C   
1501  O O   . THR A 188 ? 1.4198 1.3124 0.4424 -0.1497 0.1453  0.1360  188 THR A O   
1502  C CB  . THR A 188 ? 1.3912 1.3702 0.4683 -0.1993 0.2105  0.0546  188 THR A CB  
1503  O OG1 . THR A 188 ? 1.4160 1.3794 0.4857 -0.2224 0.2366  0.0550  188 THR A OG1 
1504  C CG2 . THR A 188 ? 1.3488 1.3808 0.4756 -0.2004 0.2205  0.0128  188 THR A CG2 
1505  N N   . LYS A 189 ? 1.4065 1.2871 0.4660 -0.1722 0.1826  0.1233  189 LYS A N   
1506  C CA  . LYS A 189 ? 1.4567 1.2820 0.4685 -0.1689 0.1696  0.1607  189 LYS A CA  
1507  C C   . LYS A 189 ? 1.4277 1.2391 0.4579 -0.1321 0.1361  0.1797  189 LYS A C   
1508  O O   . LYS A 189 ? 1.4745 1.2511 0.4565 -0.1236 0.1156  0.2087  189 LYS A O   
1509  C CB  . LYS A 189 ? 1.4649 1.2657 0.4863 -0.1840 0.1891  0.1630  189 LYS A CB  
1510  C CG  . LYS A 189 ? 1.5103 1.2508 0.4928 -0.1772 0.1736  0.1997  189 LYS A CG  
1511  C CD  . LYS A 189 ? 1.5439 1.2564 0.5147 -0.2037 0.1969  0.2033  189 LYS A CD  
1512  C CE  . LYS A 189 ? 1.5911 1.2396 0.5252 -0.1959 0.1795  0.2390  189 LYS A CE  
1513  N NZ  . LYS A 189 ? 1.5372 1.1775 0.5283 -0.1708 0.1698  0.2370  189 LYS A NZ  
1514  N N   . LEU A 190 ? 1.3536 1.1928 0.4535 -0.1108 0.1306  0.1628  190 LEU A N   
1515  C CA  . LEU A 190 ? 1.3207 1.1530 0.4459 -0.0769 0.1025  0.1772  190 LEU A CA  
1516  C C   . LEU A 190 ? 1.3053 1.1648 0.4317 -0.0608 0.0812  0.1757  190 LEU A C   
1517  O O   . LEU A 190 ? 1.3240 1.1657 0.4286 -0.0419 0.0565  0.1982  190 LEU A O   
1518  C CB  . LEU A 190 ? 1.2519 1.1014 0.4482 -0.0633 0.1061  0.1608  190 LEU A CB  
1519  C CG  . LEU A 190 ? 1.2627 1.0763 0.4626 -0.0658 0.1142  0.1708  190 LEU A CG  
1520  C CD1 . LEU A 190 ? 1.2067 1.0449 0.4689 -0.0690 0.1301  0.1449  190 LEU A CD1 
1521  C CD2 . LEU A 190 ? 1.2660 1.0492 0.4625 -0.0379 0.0894  0.1954  190 LEU A CD2 
1522  N N   . TYR A 191 ? 1.2711 1.1743 0.4264 -0.0679 0.0901  0.1477  191 TYR A N   
1523  C CA  . TYR A 191 ? 1.2465 1.1807 0.4153 -0.0532 0.0707  0.1414  191 TYR A CA  
1524  C C   . TYR A 191 ? 1.2805 1.2348 0.4137 -0.0729 0.0778  0.1278  191 TYR A C   
1525  O O   . TYR A 191 ? 1.2730 1.2487 0.4069 -0.0632 0.0602  0.1247  191 TYR A O   
1526  C CB  . TYR A 191 ? 1.1689 1.1379 0.4131 -0.0389 0.0690  0.1193  191 TYR A CB  
1527  C CG  . TYR A 191 ? 1.1350 1.0883 0.4164 -0.0270 0.0708  0.1247  191 TYR A CG  
1528  C CD1 . TYR A 191 ? 1.1266 1.0620 0.4125 -0.0026 0.0503  0.1466  191 TYR A CD1 
1529  C CD2 . TYR A 191 ? 1.1141 1.0712 0.4259 -0.0401 0.0930  0.1066  191 TYR A CD2 
1530  C CE1 . TYR A 191 ? 1.0988 1.0200 0.4161 0.0078  0.0522  0.1499  191 TYR A CE1 
1531  C CE2 . TYR A 191 ? 1.0862 1.0283 0.4296 -0.0299 0.0935  0.1111  191 TYR A CE2 
1532  C CZ  . TYR A 191 ? 1.0793 1.0029 0.4237 -0.0062 0.0734  0.1327  191 TYR A CZ  
1533  O OH  . TYR A 191 ? 1.0545 0.9635 0.4280 0.0037  0.0741  0.1357  191 TYR A OH  
1534  N N   . GLN A 192 ? 1.3181 1.2673 0.4215 -0.1013 0.1039  0.1185  192 GLN A N   
1535  C CA  . GLN A 192 ? 1.3593 1.3262 0.4220 -0.1239 0.1151  0.1044  192 GLN A CA  
1536  C C   . GLN A 192 ? 1.3128 1.3291 0.4240 -0.1251 0.1220  0.0668  192 GLN A C   
1537  O O   . GLN A 192 ? 1.3265 1.3624 0.4347 -0.1480 0.1471  0.0416  192 GLN A O   
1538  C CB  . GLN A 192 ? 1.4147 1.3636 0.4140 -0.1203 0.0922  0.1289  192 GLN A CB  
1539  C CG  . GLN A 192 ? 1.4880 1.4321 0.4177 -0.1512 0.1084  0.1270  192 GLN A CG  
1540  C CD  . GLN A 192 ? 1.5535 1.4694 0.4126 -0.1488 0.0842  0.1571  192 GLN A CD  
1541  O OE1 . GLN A 192 ? 1.6219 1.4978 0.4181 -0.1644 0.0876  0.1815  192 GLN A OE1 
1542  N NE2 . GLN A 192 ? 1.5357 1.4712 0.4049 -0.1295 0.0580  0.1562  192 GLN A NE2 
1543  N N   . ASN A 193 ? 1.2610 1.2972 0.4168 -0.1012 0.1000  0.0624  193 ASN A N   
1544  C CA  . ASN A 193 ? 1.2182 1.2969 0.4218 -0.1004 0.1021  0.0284  193 ASN A CA  
1545  C C   . ASN A 193 ? 1.1772 1.2712 0.4362 -0.1073 0.1246  0.0021  193 ASN A C   
1546  O O   . ASN A 193 ? 1.1411 1.2232 0.4364 -0.0954 0.1228  0.0102  193 ASN A O   
1547  C CB  . ASN A 193 ? 1.1719 1.2646 0.4140 -0.0741 0.0730  0.0329  193 ASN A CB  
1548  C CG  . ASN A 193 ? 1.2076 1.2845 0.4029 -0.0634 0.0478  0.0613  193 ASN A CG  
1549  O OD1 . ASN A 193 ? 1.2653 1.3123 0.4006 -0.0716 0.0488  0.0834  193 ASN A OD1 
1550  N ND2 . ASN A 193 ? 1.1759 1.2724 0.3993 -0.0453 0.0239  0.0612  193 ASN A ND2 
1551  N N   . PRO A 194 ? 1.1846 1.3057 0.4506 -0.1261 0.1455  -0.0306 194 PRO A N   
1552  C CA  . PRO A 194 ? 1.1529 1.2895 0.4702 -0.1340 0.1677  -0.0570 194 PRO A CA  
1553  C C   . PRO A 194 ? 1.0814 1.2347 0.4755 -0.1128 0.1536  -0.0706 194 PRO A C   
1554  O O   . PRO A 194 ? 1.0497 1.1975 0.4834 -0.1087 0.1597  -0.0723 194 PRO A O   
1555  C CB  . PRO A 194 ? 1.1818 1.3480 0.4872 -0.1564 0.1895  -0.0907 194 PRO A CB  
1556  C CG  . PRO A 194 ? 1.2017 1.3772 0.4762 -0.1520 0.1712  -0.0897 194 PRO A CG  
1557  C CD  . PRO A 194 ? 1.2195 1.3618 0.4527 -0.1386 0.1474  -0.0476 194 PRO A CD  
1558  N N   . THR A 195 ? 1.0599 1.2321 0.4723 -0.1006 0.1341  -0.0793 195 THR A N   
1559  C CA  . THR A 195 ? 0.9985 1.1854 0.4787 -0.0824 0.1183  -0.0907 195 THR A CA  
1560  C C   . THR A 195 ? 0.9821 1.1564 0.4579 -0.0618 0.0902  -0.0610 195 THR A C   
1561  O O   . THR A 195 ? 1.0059 1.1822 0.4474 -0.0597 0.0764  -0.0514 195 THR A O   
1562  C CB  . THR A 195 ? 0.9872 1.2069 0.4980 -0.0858 0.1174  -0.1267 195 THR A CB  
1563  O OG1 . THR A 195 ? 1.0173 1.2515 0.5171 -0.1070 0.1449  -0.1543 195 THR A OG1 
1564  C CG2 . THR A 195 ? 0.9288 1.1602 0.5136 -0.0714 0.1055  -0.1421 195 THR A CG2 
1565  N N   . THR A 196 ? 0.9436 1.1063 0.4536 -0.0470 0.0821  -0.0474 196 THR A N   
1566  C CA  . THR A 196 ? 0.9286 1.0809 0.4365 -0.0275 0.0583  -0.0195 196 THR A CA  
1567  C C   . THR A 196 ? 0.8716 1.0348 0.4411 -0.0126 0.0449  -0.0242 196 THR A C   
1568  O O   . THR A 196 ? 0.8446 1.0156 0.4568 -0.0159 0.0536  -0.0445 196 THR A O   
1569  C CB  . THR A 196 ? 0.9519 1.0713 0.4241 -0.0235 0.0605  0.0106  196 THR A CB  
1570  O OG1 . THR A 196 ? 0.9346 1.0431 0.4322 -0.0269 0.0759  0.0057  196 THR A OG1 
1571  C CG2 . THR A 196 ? 1.0154 1.1188 0.4196 -0.0381 0.0691  0.0212  196 THR A CG2 
1572  N N   . TYR A 197 ? 0.8563 1.0207 0.4296 0.0032  0.0232  -0.0053 197 TYR A N   
1573  C CA  . TYR A 197 ? 0.8075 0.9822 0.4328 0.0159  0.0092  -0.0060 197 TYR A CA  
1574  C C   . TYR A 197 ? 0.7995 0.9662 0.4180 0.0329  -0.0065 0.0226  197 TYR A C   
1575  O O   . TYR A 197 ? 0.8313 0.9870 0.4076 0.0368  -0.0106 0.0414  197 TYR A O   
1576  C CB  . TYR A 197 ? 0.7923 0.9926 0.4447 0.0141  -0.0031 -0.0250 197 TYR A CB  
1577  C CG  . TYR A 197 ? 0.8128 1.0225 0.4362 0.0175  -0.0191 -0.0141 197 TYR A CG  
1578  C CD1 . TYR A 197 ? 0.8551 1.0675 0.4360 0.0063  -0.0138 -0.0214 197 TYR A CD1 
1579  C CD2 . TYR A 197 ? 0.7920 1.0096 0.4302 0.0312  -0.0396 0.0029  197 TYR A CD2 
1580  C CE1 . TYR A 197 ? 0.8761 1.0971 0.4300 0.0096  -0.0305 -0.0115 197 TYR A CE1 
1581  C CE2 . TYR A 197 ? 0.8108 1.0397 0.4260 0.0345  -0.0553 0.0120  197 TYR A CE2 
1582  C CZ  . TYR A 197 ? 0.8529 1.0825 0.4259 0.0242  -0.0517 0.0049  197 TYR A CZ  
1583  O OH  . TYR A 197 ? 0.8737 1.1143 0.4234 0.0276  -0.0693 0.0136  197 TYR A OH  
1584  N N   . ILE A 198 ? 0.7593 0.9320 0.4199 0.0430  -0.0157 0.0250  198 ILE A N   
1585  C CA  . ILE A 198 ? 0.7463 0.9205 0.4100 0.0591  -0.0312 0.0474  198 ILE A CA  
1586  C C   . ILE A 198 ? 0.7085 0.9048 0.4178 0.0625  -0.0454 0.0409  198 ILE A C   
1587  O O   . ILE A 198 ? 0.6813 0.8766 0.4255 0.0608  -0.0428 0.0317  198 ILE A O   
1588  C CB  . ILE A 198 ? 0.7409 0.8933 0.4034 0.0681  -0.0248 0.0623  198 ILE A CB  
1589  C CG1 . ILE A 198 ? 0.7785 0.9046 0.4011 0.0606  -0.0084 0.0659  198 ILE A CG1 
1590  C CG2 . ILE A 198 ? 0.7358 0.8918 0.3959 0.0856  -0.0396 0.0840  198 ILE A CG2 
1591  C CD1 . ILE A 198 ? 0.7806 0.8816 0.3968 0.0696  -0.0038 0.0815  198 ILE A CD1 
1592  N N   . SER A 199 ? 0.7097 0.9250 0.4178 0.0663  -0.0615 0.0462  199 SER A N   
1593  C CA  . SER A 199 ? 0.6789 0.9147 0.4272 0.0676  -0.0760 0.0428  199 SER A CA  
1594  C C   . SER A 199 ? 0.6661 0.9098 0.4202 0.0814  -0.0864 0.0646  199 SER A C   
1595  O O   . SER A 199 ? 0.6853 0.9321 0.4135 0.0901  -0.0920 0.0786  199 SER A O   
1596  C CB  . SER A 199 ? 0.6881 0.9430 0.4379 0.0596  -0.0869 0.0299  199 SER A CB  
1597  O OG  . SER A 199 ? 0.7170 0.9770 0.4302 0.0635  -0.0932 0.0409  199 SER A OG  
1598  N N   . VAL A 200 ? 0.6362 0.8837 0.4241 0.0835  -0.0892 0.0665  200 VAL A N   
1599  C CA  . VAL A 200 ? 0.6225 0.8814 0.4201 0.0951  -0.0967 0.0842  200 VAL A CA  
1600  C C   . VAL A 200 ? 0.5988 0.8801 0.4325 0.0893  -0.1097 0.0817  200 VAL A C   
1601  O O   . VAL A 200 ? 0.5838 0.8598 0.4421 0.0799  -0.1099 0.0705  200 VAL A O   
1602  C CB  . VAL A 200 ? 0.6134 0.8535 0.4124 0.1024  -0.0862 0.0916  200 VAL A CB  
1603  C CG1 . VAL A 200 ? 0.6096 0.8611 0.4081 0.1170  -0.0914 0.1092  200 VAL A CG1 
1604  C CG2 . VAL A 200 ? 0.6363 0.8486 0.4056 0.1020  -0.0715 0.0893  200 VAL A CG2 
1605  N N   . GLY A 201 ? 0.5979 0.9039 0.4355 0.0943  -0.1214 0.0923  201 GLY A N   
1606  C CA  . GLY A 201 ? 0.5801 0.9091 0.4497 0.0864  -0.1341 0.0917  201 GLY A CA  
1607  C C   . GLY A 201 ? 0.5689 0.9196 0.4500 0.0948  -0.1382 0.1078  201 GLY A C   
1608  O O   . GLY A 201 ? 0.5796 0.9374 0.4440 0.1086  -0.1371 0.1180  201 GLY A O   
1609  N N   . THR A 202 ? 0.5501 0.9106 0.4596 0.0862  -0.1428 0.1096  202 THR A N   
1610  C CA  . THR A 202 ? 0.5401 0.9295 0.4650 0.0890  -0.1474 0.1225  202 THR A CA  
1611  C C   . THR A 202 ? 0.5315 0.9366 0.4843 0.0713  -0.1599 0.1197  202 THR A C   
1612  O O   . THR A 202 ? 0.5376 0.9333 0.4947 0.0608  -0.1668 0.1075  202 THR A O   
1613  C CB  . THR A 202 ? 0.5299 0.9115 0.4559 0.0959  -0.1370 0.1309  202 THR A CB  
1614  O OG1 . THR A 202 ? 0.5184 0.8849 0.4605 0.0827  -0.1375 0.1274  202 THR A OG1 
1615  C CG2 . THR A 202 ? 0.5406 0.8964 0.4398 0.1105  -0.1248 0.1311  202 THR A CG2 
1616  N N   . SER A 203 ? 0.5212 0.9496 0.4923 0.0670  -0.1628 0.1301  203 SER A N   
1617  C CA  . SER A 203 ? 0.5158 0.9534 0.5122 0.0474  -0.1743 0.1300  203 SER A CA  
1618  C C   . SER A 203 ? 0.5123 0.9155 0.5148 0.0375  -0.1748 0.1234  203 SER A C   
1619  O O   . SER A 203 ? 0.5155 0.9114 0.5340 0.0227  -0.1867 0.1164  203 SER A O   
1620  C CB  . SER A 203 ? 0.5089 0.9781 0.5204 0.0431  -0.1743 0.1437  203 SER A CB  
1621  O OG  . SER A 203 ? 0.5033 0.9642 0.5065 0.0515  -0.1618 0.1507  203 SER A OG  
1622  N N   . THR A 204 ? 0.5079 0.8891 0.4987 0.0461  -0.1631 0.1247  204 THR A N   
1623  C CA  . THR A 204 ? 0.5050 0.8546 0.5030 0.0388  -0.1642 0.1184  204 THR A CA  
1624  C C   . THR A 204 ? 0.5092 0.8323 0.4952 0.0460  -0.1569 0.1035  204 THR A C   
1625  O O   . THR A 204 ? 0.5113 0.8152 0.5097 0.0380  -0.1627 0.0904  204 THR A O   
1626  C CB  . THR A 204 ? 0.4986 0.8423 0.4947 0.0405  -0.1575 0.1298  204 THR A CB  
1627  O OG1 . THR A 204 ? 0.4979 0.8405 0.4733 0.0580  -0.1428 0.1325  204 THR A OG1 
1628  C CG2 . THR A 204 ? 0.4973 0.8688 0.5045 0.0302  -0.1629 0.1440  204 THR A CG2 
1629  N N   . LEU A 205 ? 0.5132 0.8351 0.4759 0.0605  -0.1443 0.1049  205 LEU A N   
1630  C CA  . LEU A 205 ? 0.5198 0.8166 0.4682 0.0655  -0.1344 0.0926  205 LEU A CA  
1631  C C   . LEU A 205 ? 0.5314 0.8284 0.4772 0.0603  -0.1383 0.0773  205 LEU A C   
1632  O O   . LEU A 205 ? 0.5401 0.8569 0.4789 0.0609  -0.1440 0.0795  205 LEU A O   
1633  C CB  . LEU A 205 ? 0.5261 0.8187 0.4478 0.0809  -0.1209 0.1004  205 LEU A CB  
1634  C CG  . LEU A 205 ? 0.5336 0.7979 0.4397 0.0846  -0.1081 0.0911  205 LEU A CG  
1635  C CD1 . LEU A 205 ? 0.5225 0.7675 0.4470 0.0784  -0.1070 0.0843  205 LEU A CD1 
1636  C CD2 . LEU A 205 ? 0.5436 0.8018 0.4234 0.0992  -0.0974 0.1016  205 LEU A CD2 
1637  N N   . ASN A 206 ? 0.5333 0.8097 0.4861 0.0551  -0.1355 0.0605  206 ASN A N   
1638  C CA  . ASN A 206 ? 0.5466 0.8216 0.4950 0.0503  -0.1358 0.0420  206 ASN A CA  
1639  C C   . ASN A 206 ? 0.5527 0.8068 0.4914 0.0522  -0.1207 0.0285  206 ASN A C   
1640  O O   . ASN A 206 ? 0.5495 0.7918 0.5095 0.0462  -0.1217 0.0115  206 ASN A O   
1641  C CB  . ASN A 206 ? 0.5446 0.8217 0.5227 0.0382  -0.1517 0.0296  206 ASN A CB  
1642  C CG  . ASN A 206 ? 0.5608 0.8398 0.5345 0.0334  -0.1525 0.0084  206 ASN A CG  
1643  O OD1 . ASN A 206 ? 0.5752 0.8606 0.5201 0.0376  -0.1442 0.0074  206 ASN A OD1 
1644  N ND2 . ASN A 206 ? 0.5618 0.8341 0.5631 0.0246  -0.1634 -0.0089 206 ASN A ND2 
1645  N N   . GLN A 207 ? 0.5637 0.8138 0.4713 0.0603  -0.1075 0.0358  207 GLN A N   
1646  C CA  . GLN A 207 ? 0.5713 0.8018 0.4668 0.0613  -0.0912 0.0272  207 GLN A CA  
1647  C C   . GLN A 207 ? 0.5965 0.8270 0.4641 0.0580  -0.0821 0.0166  207 GLN A C   
1648  O O   . GLN A 207 ? 0.6109 0.8530 0.4562 0.0602  -0.0866 0.0241  207 GLN A O   
1649  C CB  . GLN A 207 ? 0.5692 0.7896 0.4485 0.0716  -0.0828 0.0451  207 GLN A CB  
1650  C CG  . GLN A 207 ? 0.5805 0.7797 0.4434 0.0722  -0.0657 0.0396  207 GLN A CG  
1651  C CD  . GLN A 207 ? 0.5787 0.7658 0.4297 0.0824  -0.0599 0.0561  207 GLN A CD  
1652  O OE1 . GLN A 207 ? 0.5978 0.7765 0.4179 0.0890  -0.0525 0.0660  207 GLN A OE1 
1653  N NE2 . GLN A 207 ? 0.5591 0.7436 0.4331 0.0838  -0.0646 0.0593  207 GLN A NE2 
1654  N N   . ARG A 208 ? 0.6036 0.8225 0.4728 0.0519  -0.0695 -0.0013 208 ARG A N   
1655  C CA  . ARG A 208 ? 0.6320 0.8488 0.4695 0.0468  -0.0563 -0.0107 208 ARG A CA  
1656  C C   . ARG A 208 ? 0.6372 0.8375 0.4721 0.0431  -0.0376 -0.0199 208 ARG A C   
1657  O O   . ARG A 208 ? 0.6267 0.8263 0.4924 0.0375  -0.0346 -0.0402 208 ARG A O   
1658  C CB  . ARG A 208 ? 0.6418 0.8724 0.4874 0.0377  -0.0615 -0.0328 208 ARG A CB  
1659  C CG  . ARG A 208 ? 0.6766 0.9102 0.4793 0.0327  -0.0524 -0.0362 208 ARG A CG  
1660  C CD  . ARG A 208 ? 0.6895 0.9341 0.5006 0.0219  -0.0509 -0.0655 208 ARG A CD  
1661  N NE  . ARG A 208 ? 0.7268 0.9753 0.4919 0.0159  -0.0435 -0.0675 208 ARG A NE  
1662  C CZ  . ARG A 208 ? 0.7426 1.0009 0.4835 0.0178  -0.0563 -0.0571 208 ARG A CZ  
1663  N NH1 . ARG A 208 ? 0.7226 0.9906 0.4836 0.0250  -0.0760 -0.0445 208 ARG A NH1 
1664  N NH2 . ARG A 208 ? 0.7810 1.0403 0.4766 0.0113  -0.0495 -0.0593 208 ARG A NH2 
1665  N N   . LEU A 209 ? 0.6555 0.8421 0.4551 0.0462  -0.0261 -0.0052 209 LEU A N   
1666  C CA  . LEU A 209 ? 0.6628 0.8324 0.4575 0.0418  -0.0082 -0.0104 209 LEU A CA  
1667  C C   . LEU A 209 ? 0.6974 0.8655 0.4602 0.0300  0.0079  -0.0216 209 LEU A C   
1668  O O   . LEU A 209 ? 0.7230 0.8932 0.4491 0.0293  0.0061  -0.0126 209 LEU A O   
1669  C CB  . LEU A 209 ? 0.6649 0.8164 0.4404 0.0518  -0.0060 0.0134  209 LEU A CB  
1670  C CG  . LEU A 209 ? 0.6367 0.7906 0.4353 0.0636  -0.0200 0.0270  209 LEU A CG  
1671  C CD1 . LEU A 209 ? 0.6459 0.7827 0.4204 0.0742  -0.0167 0.0482  209 LEU A CD1 
1672  C CD2 . LEU A 209 ? 0.6100 0.7638 0.4512 0.0605  -0.0224 0.0134  209 LEU A CD2 
1673  N N   . VAL A 210 ? 0.7001 0.8660 0.4771 0.0200  0.0236  -0.0416 210 VAL A N   
1674  C CA  . VAL A 210 ? 0.7359 0.9007 0.4818 0.0058  0.0434  -0.0527 210 VAL A CA  
1675  C C   . VAL A 210 ? 0.7439 0.8908 0.4853 0.0004  0.0611  -0.0505 210 VAL A C   
1676  O O   . VAL A 210 ? 0.7170 0.8612 0.4964 0.0038  0.0602  -0.0568 210 VAL A O   
1677  C CB  . VAL A 210 ? 0.7375 0.9241 0.5062 -0.0046 0.0483  -0.0858 210 VAL A CB  
1678  C CG1 . VAL A 210 ? 0.7302 0.9323 0.5063 0.0003  0.0289  -0.0884 210 VAL A CG1 
1679  C CG2 . VAL A 210 ? 0.7108 0.9026 0.5332 -0.0058 0.0517  -0.1086 210 VAL A CG2 
1680  N N   . PRO A 211 ? 0.7840 0.9166 0.4774 -0.0088 0.0759  -0.0407 211 PRO A N   
1681  C CA  . PRO A 211 ? 0.7956 0.9100 0.4838 -0.0166 0.0933  -0.0388 211 PRO A CA  
1682  C C   . PRO A 211 ? 0.7891 0.9193 0.5124 -0.0302 0.1100  -0.0702 211 PRO A C   
1683  O O   . PRO A 211 ? 0.8052 0.9545 0.5253 -0.0422 0.1202  -0.0915 211 PRO A O   
1684  C CB  . PRO A 211 ? 0.8467 0.9429 0.4719 -0.0262 0.1038  -0.0218 211 PRO A CB  
1685  C CG  . PRO A 211 ? 0.8554 0.9550 0.4544 -0.0162 0.0860  -0.0066 211 PRO A CG  
1686  C CD  . PRO A 211 ? 0.8224 0.9511 0.4623 -0.0118 0.0745  -0.0268 211 PRO A CD  
1687  N N   . ARG A 212 ? 0.7665 0.8904 0.5245 -0.0276 0.1120  -0.0743 212 ARG A N   
1688  C CA  . ARG A 212 ? 0.7611 0.8990 0.5559 -0.0395 0.1275  -0.1031 212 ARG A CA  
1689  C C   . ARG A 212 ? 0.7948 0.9174 0.5604 -0.0555 0.1505  -0.0982 212 ARG A C   
1690  O O   . ARG A 212 ? 0.7977 0.8945 0.5498 -0.0513 0.1489  -0.0772 212 ARG A O   
1691  C CB  . ARG A 212 ? 0.7192 0.8589 0.5702 -0.0281 0.1141  -0.1107 212 ARG A CB  
1692  C CG  . ARG A 212 ? 0.6893 0.8375 0.5655 -0.0129 0.0893  -0.1092 212 ARG A CG  
1693  C CD  . ARG A 212 ? 0.6549 0.8059 0.5868 -0.0053 0.0766  -0.1208 212 ARG A CD  
1694  N NE  . ARG A 212 ? 0.6478 0.7779 0.5789 -0.0006 0.0758  -0.1043 212 ARG A NE  
1695  C CZ  . ARG A 212 ? 0.6397 0.7533 0.5535 0.0113  0.0629  -0.0776 212 ARG A CZ  
1696  N NH1 . ARG A 212 ? 0.6363 0.7530 0.5335 0.0198  0.0494  -0.0630 212 ARG A NH1 
1697  N NH2 . ARG A 212 ? 0.6362 0.7315 0.5503 0.0146  0.0637  -0.0669 212 ARG A NH2 
1698  N N   . ILE A 213 ? 0.8232 0.9616 0.5784 -0.0748 0.1720  -0.1182 213 ILE A N   
1699  C CA  . ILE A 213 ? 0.8610 0.9870 0.5867 -0.0946 0.1961  -0.1149 213 ILE A CA  
1700  C C   . ILE A 213 ? 0.8437 0.9836 0.6216 -0.1026 0.2088  -0.1401 213 ILE A C   
1701  O O   . ILE A 213 ? 0.8200 0.9900 0.6475 -0.1016 0.2090  -0.1710 213 ILE A O   
1702  C CB  . ILE A 213 ? 0.9085 1.0443 0.5871 -0.1146 0.2147  -0.1210 213 ILE A CB  
1703  C CG1 . ILE A 213 ? 0.9314 1.0490 0.5543 -0.1066 0.2000  -0.0926 213 ILE A CG1 
1704  C CG2 . ILE A 213 ? 0.9497 1.0748 0.6004 -0.1392 0.2416  -0.1196 213 ILE A CG2 
1705  C CD1 . ILE A 213 ? 0.9747 1.1051 0.5531 -0.1229 0.2120  -0.1000 213 ILE A CD1 
1706  N N   . ALA A 214 ? 0.8574 0.9746 0.6252 -0.1098 0.2177  -0.1271 214 ALA A N   
1707  C CA  . ALA A 214 ? 0.8465 0.9755 0.6603 -0.1196 0.2306  -0.1491 214 ALA A CA  
1708  C C   . ALA A 214 ? 0.8806 0.9809 0.6616 -0.1348 0.2456  -0.1311 214 ALA A C   
1709  O O   . ALA A 214 ? 0.9011 0.9663 0.6347 -0.1298 0.2380  -0.0990 214 ALA A O   
1710  C CB  . ALA A 214 ? 0.7969 0.9289 0.6681 -0.0992 0.2086  -0.1554 214 ALA A CB  
1711  N N   . THR A 215 ? 0.8889 1.0046 0.6970 -0.1536 0.2663  -0.1528 215 THR A N   
1712  C CA  . THR A 215 ? 0.9194 1.0088 0.7052 -0.1701 0.2804  -0.1388 215 THR A CA  
1713  C C   . THR A 215 ? 0.8858 0.9583 0.7081 -0.1536 0.2626  -0.1328 215 THR A C   
1714  O O   . THR A 215 ? 0.8486 0.9453 0.7320 -0.1468 0.2567  -0.1571 215 THR A O   
1715  C CB  . THR A 215 ? 0.9428 1.0593 0.7449 -0.1995 0.3114  -0.1659 215 THR A CB  
1716  O OG1 . THR A 215 ? 0.9652 1.1091 0.7474 -0.2121 0.3267  -0.1811 215 THR A OG1 
1717  C CG2 . THR A 215 ? 0.9886 1.0728 0.7501 -0.2217 0.3278  -0.1459 215 THR A CG2 
1718  N N   . ARG A 216 ? 0.9015 0.9321 0.6860 -0.1467 0.2529  -0.1012 216 ARG A N   
1719  C CA  . ARG A 216 ? 0.8721 0.8846 0.6834 -0.1287 0.2339  -0.0932 216 ARG A CA  
1720  C C   . ARG A 216 ? 0.9038 0.8819 0.6942 -0.1411 0.2424  -0.0787 216 ARG A C   
1721  O O   . ARG A 216 ? 0.9517 0.9080 0.6923 -0.1586 0.2571  -0.0636 216 ARG A O   
1722  C CB  . ARG A 216 ? 0.8543 0.8502 0.6462 -0.1023 0.2088  -0.0702 216 ARG A CB  
1723  C CG  . ARG A 216 ? 0.8233 0.8502 0.6374 -0.0898 0.1973  -0.0830 216 ARG A CG  
1724  C CD  . ARG A 216 ? 0.8143 0.8257 0.6018 -0.0679 0.1758  -0.0581 216 ARG A CD  
1725  N NE  . ARG A 216 ? 0.8519 0.8523 0.5825 -0.0730 0.1810  -0.0407 216 ARG A NE  
1726  C CZ  . ARG A 216 ? 0.8536 0.8750 0.5740 -0.0732 0.1801  -0.0467 216 ARG A CZ  
1727  N NH1 . ARG A 216 ? 0.8200 0.8742 0.5842 -0.0685 0.1745  -0.0704 216 ARG A NH1 
1728  N NH2 . ARG A 216 ? 0.8924 0.9001 0.5573 -0.0782 0.1832  -0.0288 216 ARG A NH2 
1729  N N   . SER A 217 ? 0.8801 0.8515 0.7074 -0.1324 0.2319  -0.0832 217 SER A N   
1730  C CA  . SER A 217 ? 0.9073 0.8440 0.7196 -0.1414 0.2363  -0.0707 217 SER A CA  
1731  C C   . SER A 217 ? 0.9335 0.8254 0.6903 -0.1282 0.2240  -0.0363 217 SER A C   
1732  O O   . SER A 217 ? 0.9136 0.8048 0.6616 -0.1055 0.2059  -0.0249 217 SER A O   
1733  C CB  . SER A 217 ? 0.8722 0.8143 0.7382 -0.1325 0.2243  -0.0849 217 SER A CB  
1734  O OG  . SER A 217 ? 0.8439 0.8297 0.7673 -0.1383 0.2296  -0.1175 217 SER A OG  
1735  N N   . LYS A 218 ? 0.9812 0.8363 0.7023 -0.1430 0.2334  -0.0206 218 LYS A N   
1736  C CA  . LYS A 218 ? 1.0118 0.8205 0.6827 -0.1300 0.2208  0.0106  218 LYS A CA  
1737  C C   . LYS A 218 ? 0.9800 0.7747 0.6732 -0.1051 0.1994  0.0144  218 LYS A C   
1738  O O   . LYS A 218 ? 0.9710 0.7622 0.6949 -0.1096 0.2000  0.0031  218 LYS A O   
1739  C CB  . LYS A 218 ? 1.0766 0.8452 0.7043 -0.1536 0.2352  0.0259  218 LYS A CB  
1740  C CG  . LYS A 218 ? 1.1272 0.8866 0.6992 -0.1688 0.2465  0.0410  218 LYS A CG  
1741  C CD  . LYS A 218 ? 1.1879 0.9256 0.7320 -0.2037 0.2690  0.0451  218 LYS A CD  
1742  C CE  . LYS A 218 ? 1.2437 0.9728 0.7283 -0.2210 0.2802  0.0603  218 LYS A CE  
1743  N NZ  . LYS A 218 ? 1.2715 1.0257 0.7585 -0.2583 0.3105  0.0428  218 LYS A NZ  
1744  N N   . VAL A 219 ? 0.9638 0.7530 0.6420 -0.0796 0.1809  0.0292  219 VAL A N   
1745  C CA  . VAL A 219 ? 0.9432 0.7155 0.6305 -0.0558 0.1616  0.0368  219 VAL A CA  
1746  C C   . VAL A 219 ? 0.9809 0.7134 0.6160 -0.0443 0.1535  0.0644  219 VAL A C   
1747  O O   . VAL A 219 ? 0.9925 0.7283 0.5987 -0.0400 0.1514  0.0762  219 VAL A O   
1748  C CB  . VAL A 219 ? 0.8893 0.6966 0.6116 -0.0354 0.1462  0.0274  219 VAL A CB  
1749  C CG1 . VAL A 219 ? 0.8744 0.6655 0.5982 -0.0111 0.1272  0.0373  219 VAL A CG1 
1750  C CG2 . VAL A 219 ? 0.8557 0.6983 0.6313 -0.0456 0.1513  -0.0002 219 VAL A CG2 
1751  N N   . ASN A 220 ? 1.0028 0.6969 0.6263 -0.0393 0.1481  0.0737  220 ASN A N   
1752  C CA  . ASN A 220 ? 1.0476 0.6976 0.6226 -0.0294 0.1402  0.0988  220 ASN A CA  
1753  C C   . ASN A 220 ? 1.0979 0.7308 0.6271 -0.0489 0.1518  0.1128  220 ASN A C   
1754  O O   . ASN A 220 ? 1.1239 0.7389 0.6151 -0.0373 0.1422  0.1325  220 ASN A O   
1755  C CB  . ASN A 220 ? 1.0246 0.6824 0.5966 0.0019  0.1206  0.1084  220 ASN A CB  
1756  C CG  . ASN A 220 ? 0.9971 0.6532 0.5958 0.0217  0.1079  0.1021  220 ASN A CG  
1757  O OD1 . ASN A 220 ? 0.9793 0.6416 0.6091 0.0135  0.1118  0.0862  220 ASN A OD1 
1758  N ND2 . ASN A 220 ? 0.9951 0.6446 0.5819 0.0477  0.0925  0.1137  220 ASN A ND2 
1759  N N   . GLY A 221 ? 1.1135 0.7534 0.6466 -0.0791 0.1721  0.1021  221 GLY A N   
1760  C CA  . GLY A 221 ? 1.1668 0.7905 0.6541 -0.1031 0.1862  0.1145  221 GLY A CA  
1761  C C   . GLY A 221 ? 1.1589 0.8146 0.6325 -0.1037 0.1889  0.1142  221 GLY A C   
1762  O O   . GLY A 221 ? 1.2076 0.8472 0.6344 -0.1199 0.1967  0.1281  221 GLY A O   
1763  N N   . GLN A 222 ? 1.1009 0.8003 0.6133 -0.0873 0.1817  0.0987  222 GLN A N   
1764  C CA  . GLN A 222 ? 1.0897 0.8213 0.5938 -0.0859 0.1821  0.0960  222 GLN A CA  
1765  C C   . GLN A 222 ? 1.0348 0.8185 0.5934 -0.0890 0.1888  0.0665  222 GLN A C   
1766  O O   . GLN A 222 ? 0.9907 0.7883 0.5944 -0.0758 0.1802  0.0541  222 GLN A O   
1767  C CB  . GLN A 222 ? 1.0804 0.8068 0.5692 -0.0561 0.1590  0.1130  222 GLN A CB  
1768  C CG  . GLN A 222 ? 1.1364 0.8123 0.5723 -0.0491 0.1488  0.1419  222 GLN A CG  
1769  C CD  . GLN A 222 ? 1.1998 0.8555 0.5820 -0.0735 0.1605  0.1550  222 GLN A CD  
1770  O OE1 . GLN A 222 ? 1.1989 0.8842 0.5743 -0.0861 0.1700  0.1470  222 GLN A OE1 
1771  N NE2 . GLN A 222 ? 1.2586 0.8621 0.6004 -0.0807 0.1593  0.1754  222 GLN A NE2 
1772  N N   . SER A 223 ? 1.0410 0.8522 0.5941 -0.1066 0.2035  0.0549  223 SER A N   
1773  C CA  . SER A 223 ? 0.9943 0.8550 0.5982 -0.1090 0.2091  0.0252  223 SER A CA  
1774  C C   . SER A 223 ? 0.9659 0.8519 0.5723 -0.0910 0.1950  0.0246  223 SER A C   
1775  O O   . SER A 223 ? 0.9262 0.8499 0.5757 -0.0881 0.1942  0.0017  223 SER A O   
1776  C CB  . SER A 223 ? 1.0191 0.8992 0.6231 -0.1406 0.2362  0.0068  223 SER A CB  
1777  O OG  . SER A 223 ? 1.0274 0.8980 0.6517 -0.1565 0.2486  -0.0015 223 SER A OG  
1778  N N   . GLY A 224 ? 0.9879 0.8525 0.5495 -0.0791 0.1826  0.0493  224 GLY A N   
1779  C CA  . GLY A 224 ? 0.9618 0.8475 0.5257 -0.0604 0.1662  0.0515  224 GLY A CA  
1780  C C   . GLY A 224 ? 0.9132 0.8044 0.5142 -0.0348 0.1464  0.0523  224 GLY A C   
1781  O O   . GLY A 224 ? 0.9106 0.7789 0.5187 -0.0276 0.1421  0.0592  224 GLY A O   
1782  N N   . ARG A 225 ? 0.8773 0.7982 0.5002 -0.0222 0.1344  0.0451  225 ARG A N   
1783  C CA  . ARG A 225 ? 0.8318 0.7626 0.4904 -0.0009 0.1164  0.0447  225 ARG A CA  
1784  C C   . ARG A 225 ? 0.8236 0.7614 0.4679 0.0175  0.0986  0.0595  225 ARG A C   
1785  O O   . ARG A 225 ? 0.8378 0.7871 0.4612 0.0137  0.0985  0.0609  225 ARG A O   
1786  C CB  . ARG A 225 ? 0.7906 0.7535 0.5032 -0.0046 0.1173  0.0182  225 ARG A CB  
1787  C CG  . ARG A 225 ? 0.7906 0.7513 0.5289 -0.0196 0.1316  0.0013  225 ARG A CG  
1788  C CD  . ARG A 225 ? 0.7819 0.7199 0.5308 -0.0101 0.1242  0.0092  225 ARG A CD  
1789  N NE  . ARG A 225 ? 0.7821 0.7193 0.5580 -0.0248 0.1364  -0.0076 225 ARG A NE  
1790  C CZ  . ARG A 225 ? 0.8181 0.7343 0.5726 -0.0418 0.1528  -0.0050 225 ARG A CZ  
1791  N NH1 . ARG A 225 ? 0.8608 0.7507 0.5630 -0.0465 0.1585  0.0153  225 ARG A NH1 
1792  N NH2 . ARG A 225 ? 0.8139 0.7347 0.6002 -0.0549 0.1625  -0.0226 225 ARG A NH2 
1793  N N   . MET A 226 ? 0.8021 0.7343 0.4580 0.0370  0.0838  0.0696  226 MET A N   
1794  C CA  . MET A 226 ? 0.7885 0.7330 0.4403 0.0551  0.0667  0.0814  226 MET A CA  
1795  C C   . MET A 226 ? 0.7407 0.7086 0.4372 0.0644  0.0560  0.0718  226 MET A C   
1796  O O   . MET A 226 ? 0.7271 0.6860 0.4420 0.0691  0.0545  0.0702  226 MET A O   
1797  C CB  . MET A 226 ? 0.8134 0.7300 0.4349 0.0706  0.0587  0.1037  226 MET A CB  
1798  C CG  . MET A 226 ? 0.8655 0.7566 0.4373 0.0644  0.0631  0.1183  226 MET A CG  
1799  S SD  . MET A 226 ? 0.8769 0.7872 0.4247 0.0701  0.0515  0.1272  226 MET A SD  
1800  C CE  . MET A 226 ? 0.9467 0.8148 0.4321 0.0627  0.0553  0.1475  226 MET A CE  
1801  N N   . GLU A 227 ? 0.7186 0.7149 0.4307 0.0660  0.0477  0.0658  227 GLU A N   
1802  C CA  . GLU A 227 ? 0.6780 0.6950 0.4296 0.0727  0.0359  0.0585  227 GLU A CA  
1803  C C   . GLU A 227 ? 0.6690 0.6972 0.4141 0.0884  0.0210  0.0738  227 GLU A C   
1804  O O   . GLU A 227 ? 0.6783 0.7183 0.4079 0.0892  0.0168  0.0784  227 GLU A O   
1805  C CB  . GLU A 227 ? 0.6615 0.7017 0.4412 0.0611  0.0371  0.0378  227 GLU A CB  
1806  C CG  . GLU A 227 ? 0.6259 0.6803 0.4487 0.0645  0.0251  0.0284  227 GLU A CG  
1807  C CD  . GLU A 227 ? 0.6141 0.6863 0.4682 0.0535  0.0260  0.0050  227 GLU A CD  
1808  O OE1 . GLU A 227 ? 0.6319 0.7097 0.4742 0.0432  0.0374  -0.0053 227 GLU A OE1 
1809  O OE2 . GLU A 227 ? 0.5897 0.6698 0.4799 0.0553  0.0148  -0.0034 227 GLU A OE2 
1810  N N   . PHE A 228 ? 0.6523 0.6787 0.4094 0.1002  0.0133  0.0808  228 PHE A N   
1811  C CA  . PHE A 228 ? 0.6466 0.6848 0.3980 0.1155  0.0014  0.0951  228 PHE A CA  
1812  C C   . PHE A 228 ? 0.6135 0.6788 0.3965 0.1164  -0.0101 0.0913  228 PHE A C   
1813  O O   . PHE A 228 ? 0.5946 0.6605 0.4029 0.1116  -0.0116 0.0826  228 PHE A O   
1814  C CB  . PHE A 228 ? 0.6586 0.6766 0.3963 0.1288  0.0019  0.1062  228 PHE A CB  
1815  C CG  . PHE A 228 ? 0.6970 0.6858 0.3993 0.1298  0.0094  0.1144  228 PHE A CG  
1816  C CD1 . PHE A 228 ? 0.7201 0.7078 0.3959 0.1394  0.0036  0.1277  228 PHE A CD1 
1817  C CD2 . PHE A 228 ? 0.7132 0.6747 0.4084 0.1201  0.0211  0.1093  228 PHE A CD2 
1818  C CE1 . PHE A 228 ? 0.7613 0.7177 0.4015 0.1397  0.0081  0.1372  228 PHE A CE1 
1819  C CE2 . PHE A 228 ? 0.7536 0.6849 0.4138 0.1187  0.0275  0.1186  228 PHE A CE2 
1820  C CZ  . PHE A 228 ? 0.7791 0.7061 0.4103 0.1285  0.0204  0.1333  228 PHE A CZ  
1821  N N   . PHE A 229 ? 0.6098 0.6965 0.3903 0.1217  -0.0193 0.0984  229 PHE A N   
1822  C CA  . PHE A 229 ? 0.5837 0.6964 0.3910 0.1203  -0.0310 0.0968  229 PHE A CA  
1823  C C   . PHE A 229 ? 0.5811 0.7101 0.3846 0.1338  -0.0388 0.1110  229 PHE A C   
1824  O O   . PHE A 229 ? 0.6002 0.7235 0.3808 0.1453  -0.0373 0.1207  229 PHE A O   
1825  C CB  . PHE A 229 ? 0.5813 0.7100 0.3955 0.1104  -0.0352 0.0882  229 PHE A CB  
1826  C CG  . PHE A 229 ? 0.5819 0.7014 0.4065 0.0971  -0.0276 0.0704  229 PHE A CG  
1827  C CD1 . PHE A 229 ? 0.6059 0.7092 0.4071 0.0922  -0.0143 0.0662  229 PHE A CD1 
1828  C CD2 . PHE A 229 ? 0.5613 0.6885 0.4195 0.0892  -0.0341 0.0575  229 PHE A CD2 
1829  C CE1 . PHE A 229 ? 0.6071 0.7067 0.4204 0.0793  -0.0053 0.0476  229 PHE A CE1 
1830  C CE2 . PHE A 229 ? 0.5623 0.6840 0.4348 0.0787  -0.0274 0.0384  229 PHE A CE2 
1831  C CZ  . PHE A 229 ? 0.5841 0.6944 0.4352 0.0736  -0.0119 0.0325  229 PHE A CZ  
1832  N N   . TRP A 230 ? 0.5596 0.7089 0.3862 0.1320  -0.0475 0.1119  230 TRP A N   
1833  C CA  . TRP A 230 ? 0.5555 0.7262 0.3832 0.1426  -0.0534 0.1232  230 TRP A CA  
1834  C C   . TRP A 230 ? 0.5375 0.7369 0.3880 0.1344  -0.0643 0.1239  230 TRP A C   
1835  O O   . TRP A 230 ? 0.5269 0.7253 0.3943 0.1213  -0.0689 0.1157  230 TRP A O   
1836  C CB  . TRP A 230 ? 0.5547 0.7156 0.3812 0.1505  -0.0490 0.1266  230 TRP A CB  
1837  C CG  . TRP A 230 ? 0.5398 0.6943 0.3843 0.1399  -0.0506 0.1204  230 TRP A CG  
1838  C CD1 . TRP A 230 ? 0.5409 0.6703 0.3880 0.1335  -0.0458 0.1111  230 TRP A CD1 
1839  C CD2 . TRP A 230 ? 0.5248 0.6978 0.3868 0.1341  -0.0586 0.1236  230 TRP A CD2 
1840  N NE1 . TRP A 230 ? 0.5274 0.6577 0.3931 0.1255  -0.0523 0.1081  230 TRP A NE1 
1841  C CE2 . TRP A 230 ? 0.5191 0.6742 0.3919 0.1251  -0.0602 0.1166  230 TRP A CE2 
1842  C CE3 . TRP A 230 ? 0.5182 0.7217 0.3876 0.1343  -0.0648 0.1318  230 TRP A CE3 
1843  C CZ2 . TRP A 230 ? 0.5098 0.6728 0.3969 0.1166  -0.0692 0.1193  230 TRP A CZ2 
1844  C CZ3 . TRP A 230 ? 0.5087 0.7214 0.3921 0.1240  -0.0716 0.1345  230 TRP A CZ3 
1845  C CH2 . TRP A 230 ? 0.5059 0.6965 0.3962 0.1153  -0.0745 0.1290  230 TRP A CH2 
1846  N N   . THR A 231 ? 0.5364 0.7616 0.3885 0.1422  -0.0689 0.1332  231 THR A N   
1847  C CA  . THR A 231 ? 0.5219 0.7760 0.3952 0.1335  -0.0784 0.1361  231 THR A CA  
1848  C C   . THR A 231 ? 0.5220 0.8015 0.3968 0.1438  -0.0779 0.1454  231 THR A C   
1849  O O   . THR A 231 ? 0.5341 0.8103 0.3945 0.1599  -0.0723 0.1485  231 THR A O   
1850  C CB  . THR A 231 ? 0.5224 0.7925 0.4010 0.1267  -0.0869 0.1336  231 THR A CB  
1851  O OG1 . THR A 231 ? 0.5093 0.8017 0.4106 0.1145  -0.0968 0.1353  231 THR A OG1 
1852  C CG2 . THR A 231 ? 0.5358 0.8214 0.4001 0.1402  -0.0880 0.1399  231 THR A CG2 
1853  N N   . ILE A 232 ? 0.5114 0.8158 0.4042 0.1339  -0.0838 0.1492  232 ILE A N   
1854  C CA  . ILE A 232 ? 0.5116 0.8500 0.4101 0.1407  -0.0830 0.1565  232 ILE A CA  
1855  C C   . ILE A 232 ? 0.5098 0.8792 0.4209 0.1361  -0.0922 0.1587  232 ILE A C   
1856  O O   . ILE A 232 ? 0.5021 0.8780 0.4275 0.1191  -0.1006 0.1582  232 ILE A O   
1857  C CB  . ILE A 232 ? 0.5053 0.8523 0.4120 0.1308  -0.0815 0.1602  232 ILE A CB  
1858  C CG1 . ILE A 232 ? 0.5128 0.8464 0.4053 0.1440  -0.0709 0.1592  232 ILE A CG1 
1859  C CG2 . ILE A 232 ? 0.5017 0.8930 0.4236 0.1252  -0.0844 0.1668  232 ILE A CG2 
1860  C CD1 . ILE A 232 ? 0.5191 0.8109 0.3965 0.1503  -0.0664 0.1529  232 ILE A CD1 
1861  N N   . LEU A 233 ? 0.5198 0.9064 0.4261 0.1518  -0.0923 0.1607  233 LEU A N   
1862  C CA  . LEU A 233 ? 0.5205 0.9389 0.4387 0.1496  -0.1021 0.1623  233 LEU A CA  
1863  C C   . LEU A 233 ? 0.5153 0.9781 0.4536 0.1487  -0.1020 0.1672  233 LEU A C   
1864  O O   . LEU A 233 ? 0.5207 0.9983 0.4580 0.1651  -0.0957 0.1683  233 LEU A O   
1865  C CB  . LEU A 233 ? 0.5370 0.9500 0.4388 0.1670  -0.1046 0.1621  233 LEU A CB  
1866  C CG  . LEU A 233 ? 0.5409 0.9824 0.4510 0.1662  -0.1169 0.1628  233 LEU A CG  
1867  C CD1 . LEU A 233 ? 0.5352 0.9704 0.4503 0.1460  -0.1243 0.1578  233 LEU A CD1 
1868  C CD2 . LEU A 233 ? 0.5633 0.9934 0.4517 0.1852  -0.1202 0.1645  233 LEU A CD2 
1869  N N   . LYS A 234 ? 0.5077 0.9915 0.4646 0.1289  -0.1087 0.1692  234 LYS A N   
1870  C CA  . LYS A 234 ? 0.5047 1.0328 0.4813 0.1227  -0.1075 0.1741  234 LYS A CA  
1871  C C   . LYS A 234 ? 0.5099 1.0786 0.4993 0.1350  -0.1121 0.1738  234 LYS A C   
1872  O O   . LYS A 234 ? 0.5164 1.0772 0.4991 0.1436  -0.1200 0.1712  234 LYS A O   
1873  C CB  . LYS A 234 ? 0.4985 1.0322 0.4899 0.0952  -0.1149 0.1777  234 LYS A CB  
1874  C CG  . LYS A 234 ? 0.4975 0.9997 0.4803 0.0835  -0.1113 0.1798  234 LYS A CG  
1875  C CD  . LYS A 234 ? 0.4965 0.9943 0.4921 0.0572  -0.1227 0.1836  234 LYS A CD  
1876  C CE  . LYS A 234 ? 0.4999 0.9739 0.4881 0.0454  -0.1207 0.1883  234 LYS A CE  
1877  N NZ  . LYS A 234 ? 0.5040 0.9681 0.5037 0.0201  -0.1345 0.1932  234 LYS A NZ  
1878  N N   . PRO A 235 ? 0.5097 1.1234 0.5172 0.1359  -0.1073 0.1758  235 PRO A N   
1879  C CA  . PRO A 235 ? 0.5146 1.1705 0.5389 0.1496  -0.1124 0.1739  235 PRO A CA  
1880  C C   . PRO A 235 ? 0.5137 1.1874 0.5526 0.1355  -0.1271 0.1744  235 PRO A C   
1881  O O   . PRO A 235 ? 0.5077 1.1781 0.5536 0.1109  -0.1311 0.1771  235 PRO A O   
1882  C CB  . PRO A 235 ? 0.5116 1.2148 0.5559 0.1480  -0.1020 0.1742  235 PRO A CB  
1883  C CG  . PRO A 235 ? 0.5099 1.1886 0.5396 0.1382  -0.0904 0.1765  235 PRO A CG  
1884  C CD  . PRO A 235 ? 0.5064 1.1370 0.5207 0.1229  -0.0975 0.1794  235 PRO A CD  
1885  N N   . ASN A 236 ? 0.5231 1.2129 0.5658 0.1513  -0.1366 0.1718  236 ASN A N   
1886  C CA  . ASN A 236 ? 0.5253 1.2357 0.5819 0.1402  -0.1520 0.1709  236 ASN A CA  
1887  C C   . ASN A 236 ? 0.5281 1.1947 0.5650 0.1287  -0.1598 0.1690  236 ASN A C   
1888  O O   . ASN A 236 ? 0.5308 1.2084 0.5769 0.1162  -0.1725 0.1668  236 ASN A O   
1889  C CB  . ASN A 236 ? 0.5171 1.2729 0.6050 0.1171  -0.1524 0.1733  236 ASN A CB  
1890  C CG  . ASN A 236 ? 0.5211 1.3309 0.6369 0.1207  -0.1629 0.1709  236 ASN A CG  
1891  O OD1 . ASN A 236 ? 0.5340 1.3429 0.6447 0.1360  -0.1749 0.1677  236 ASN A OD1 
1892  N ND2 . ASN A 236 ? 0.5153 1.3733 0.6604 0.1055  -0.1588 0.1725  236 ASN A ND2 
1893  N N   . ASP A 237 ? 0.5295 1.1482 0.5406 0.1330  -0.1519 0.1683  237 ASP A N   
1894  C CA  . ASP A 237 ? 0.5324 1.1102 0.5256 0.1235  -0.1564 0.1640  237 ASP A CA  
1895  C C   . ASP A 237 ? 0.5483 1.0967 0.5121 0.1430  -0.1557 0.1621  237 ASP A C   
1896  O O   . ASP A 237 ? 0.5546 1.0988 0.5086 0.1624  -0.1488 0.1651  237 ASP A O   
1897  C CB  . ASP A 237 ? 0.5228 1.0695 0.5125 0.1096  -0.1482 0.1639  237 ASP A CB  
1898  C CG  . ASP A 237 ? 0.5252 1.0361 0.5050 0.0977  -0.1535 0.1565  237 ASP A CG  
1899  O OD1 . ASP A 237 ? 0.5307 1.0497 0.5145 0.0909  -0.1650 0.1517  237 ASP A OD1 
1900  O OD2 . ASP A 237 ? 0.5221 0.9982 0.4917 0.0953  -0.1464 0.1540  237 ASP A OD2 
1901  N N   . ALA A 238 ? 0.5575 1.0849 0.5064 0.1369  -0.1628 0.1568  238 ALA A N   
1902  C CA  . ALA A 238 ? 0.5784 1.0781 0.4955 0.1512  -0.1631 0.1560  238 ALA A CA  
1903  C C   . ALA A 238 ? 0.5803 1.0348 0.4763 0.1434  -0.1543 0.1502  238 ALA A C   
1904  O O   . ALA A 238 ? 0.5691 1.0162 0.4761 0.1257  -0.1543 0.1436  238 ALA A O   
1905  C CB  . ALA A 238 ? 0.5942 1.1107 0.5070 0.1513  -0.1786 0.1539  238 ALA A CB  
1906  N N   . ILE A 239 ? 0.5965 1.0209 0.4637 0.1566  -0.1473 0.1523  239 ILE A N   
1907  C CA  . ILE A 239 ? 0.6029 0.9870 0.4484 0.1494  -0.1383 0.1457  239 ILE A CA  
1908  C C   . ILE A 239 ? 0.6306 1.0019 0.4462 0.1503  -0.1436 0.1433  239 ILE A C   
1909  O O   . ILE A 239 ? 0.6517 1.0274 0.4507 0.1645  -0.1504 0.1511  239 ILE A O   
1910  C CB  . ILE A 239 ? 0.6032 0.9586 0.4368 0.1587  -0.1244 0.1492  239 ILE A CB  
1911  C CG1 . ILE A 239 ? 0.6058 0.9256 0.4257 0.1476  -0.1146 0.1403  239 ILE A CG1 
1912  C CG2 . ILE A 239 ? 0.6269 0.9739 0.4380 0.1795  -0.1249 0.1580  239 ILE A CG2 
1913  C CD1 . ILE A 239 ? 0.5972 0.8941 0.4179 0.1502  -0.1022 0.1408  239 ILE A CD1 
1914  N N   . ASN A 240 ? 0.6330 0.9889 0.4417 0.1351  -0.1412 0.1320  240 ASN A N   
1915  C CA  . ASN A 240 ? 0.6613 1.0072 0.4399 0.1320  -0.1452 0.1274  240 ASN A CA  
1916  C C   . ASN A 240 ? 0.6749 0.9842 0.4274 0.1261  -0.1305 0.1207  240 ASN A C   
1917  O O   . ASN A 240 ? 0.6588 0.9587 0.4263 0.1144  -0.1223 0.1090  240 ASN A O   
1918  C CB  . ASN A 240 ? 0.6573 1.0239 0.4510 0.1174  -0.1562 0.1161  240 ASN A CB  
1919  C CG  . ASN A 240 ? 0.6467 1.0520 0.4664 0.1202  -0.1713 0.1219  240 ASN A CG  
1920  O OD1 . ASN A 240 ? 0.6594 1.0794 0.4715 0.1342  -0.1791 0.1322  240 ASN A OD1 
1921  N ND2 . ASN A 240 ? 0.6256 1.0479 0.4776 0.1063  -0.1764 0.1151  240 ASN A ND2 
1922  N N   . PHE A 241 ? 0.7068 0.9958 0.4211 0.1337  -0.1280 0.1280  241 PHE A N   
1923  C CA  . PHE A 241 ? 0.7261 0.9819 0.4116 0.1262  -0.1131 0.1227  241 PHE A CA  
1924  C C   . PHE A 241 ? 0.7587 1.0113 0.4116 0.1165  -0.1161 0.1164  241 PHE A C   
1925  O O   . PHE A 241 ? 0.7820 1.0439 0.4157 0.1232  -0.1298 0.1250  241 PHE A O   
1926  C CB  . PHE A 241 ? 0.7449 0.9738 0.4064 0.1394  -0.1066 0.1370  241 PHE A CB  
1927  C CG  . PHE A 241 ? 0.7173 0.9431 0.4049 0.1467  -0.0998 0.1400  241 PHE A CG  
1928  C CD1 . PHE A 241 ? 0.7042 0.9110 0.3998 0.1376  -0.0850 0.1312  241 PHE A CD1 
1929  C CD2 . PHE A 241 ? 0.7058 0.9498 0.4108 0.1626  -0.1084 0.1502  241 PHE A CD2 
1930  C CE1 . PHE A 241 ? 0.6818 0.8850 0.3986 0.1438  -0.0799 0.1337  241 PHE A CE1 
1931  C CE2 . PHE A 241 ? 0.6836 0.9256 0.4094 0.1685  -0.1014 0.1518  241 PHE A CE2 
1932  C CZ  . PHE A 241 ? 0.6722 0.8925 0.4024 0.1589  -0.0877 0.1441  241 PHE A CZ  
1933  N N   . GLU A 242 ? 0.7616 1.0028 0.4091 0.1009  -0.1036 0.1003  242 GLU A N   
1934  C CA  . GLU A 242 ? 0.7986 1.0325 0.4081 0.0900  -0.1012 0.0929  242 GLU A CA  
1935  C C   . GLU A 242 ? 0.8115 1.0190 0.4030 0.0789  -0.0796 0.0843  242 GLU A C   
1936  O O   . GLU A 242 ? 0.7847 0.9922 0.4066 0.0720  -0.0691 0.0698  242 GLU A O   
1937  C CB  . GLU A 242 ? 0.7918 1.0506 0.4178 0.0790  -0.1100 0.0751  242 GLU A CB  
1938  C CG  . GLU A 242 ? 0.8337 1.0890 0.4182 0.0678  -0.1089 0.0661  242 GLU A CG  
1939  C CD  . GLU A 242 ? 0.8272 1.1058 0.4306 0.0568  -0.1171 0.0450  242 GLU A CD  
1940  O OE1 . GLU A 242 ? 0.8108 1.1124 0.4387 0.0616  -0.1351 0.0478  242 GLU A OE1 
1941  O OE2 . GLU A 242 ? 0.8402 1.1148 0.4348 0.0430  -0.1055 0.0243  242 GLU A OE2 
1942  N N   . SER A 243 ? 0.8545 1.0394 0.3971 0.0767  -0.0738 0.0936  243 SER A N   
1943  C CA  . SER A 243 ? 0.8726 1.0339 0.3947 0.0635  -0.0520 0.0861  243 SER A CA  
1944  C C   . SER A 243 ? 0.9295 1.0741 0.3920 0.0536  -0.0480 0.0917  243 SER A C   
1945  O O   . SER A 243 ? 0.9604 1.0960 0.3901 0.0629  -0.0619 0.1114  243 SER A O   
1946  C CB  . SER A 243 ? 0.8617 0.9999 0.3912 0.0717  -0.0433 0.0980  243 SER A CB  
1947  O OG  . SER A 243 ? 0.8814 0.9975 0.3919 0.0576  -0.0224 0.0913  243 SER A OG  
1948  N N   . ASN A 244 ? 0.9453 1.0862 0.3945 0.0346  -0.0292 0.0739  244 ASN A N   
1949  C CA  . ASN A 244 ? 1.0036 1.1265 0.3925 0.0204  -0.0201 0.0780  244 ASN A CA  
1950  C C   . ASN A 244 ? 1.0229 1.1156 0.3925 0.0113  0.0010  0.0836  244 ASN A C   
1951  O O   . ASN A 244 ? 1.0720 1.1490 0.3932 -0.0051 0.0134  0.0850  244 ASN A O   
1952  C CB  . ASN A 244 ? 1.0165 1.1607 0.3985 0.0027  -0.0129 0.0520  244 ASN A CB  
1953  C CG  . ASN A 244 ? 0.9815 1.1399 0.4089 -0.0069 0.0049  0.0232  244 ASN A CG  
1954  O OD1 . ASN A 244 ? 0.9362 1.0968 0.4113 0.0023  0.0043  0.0215  244 ASN A OD1 
1955  N ND2 . ASN A 244 ? 1.0043 1.1730 0.4175 -0.0253 0.0202  -0.0002 244 ASN A ND2 
1956  N N   . GLY A 245 ? 0.9867 1.0715 0.3927 0.0205  0.0051  0.0867  245 GLY A N   
1957  C CA  . GLY A 245 ? 1.0034 1.0585 0.3948 0.0133  0.0228  0.0933  245 GLY A CA  
1958  C C   . GLY A 245 ? 0.9570 1.0097 0.3968 0.0224  0.0270  0.0903  245 GLY A C   
1959  O O   . GLY A 245 ? 0.9094 0.9861 0.3982 0.0294  0.0211  0.0773  245 GLY A O   
1960  N N   . ASN A 246 ? 0.9755 0.9968 0.3986 0.0213  0.0362  0.1031  246 ASN A N   
1961  C CA  . ASN A 246 ? 0.9411 0.9547 0.4023 0.0266  0.0430  0.0999  246 ASN A CA  
1962  C C   . ASN A 246 ? 0.9013 0.9221 0.3965 0.0502  0.0253  0.1091  246 ASN A C   
1963  O O   . ASN A 246 ? 0.8644 0.8889 0.3990 0.0542  0.0286  0.1013  246 ASN A O   
1964  C CB  . ASN A 246 ? 0.9123 0.9462 0.4122 0.0121  0.0595  0.0713  246 ASN A CB  
1965  C CG  . ASN A 246 ? 0.9505 0.9838 0.4208 -0.0121 0.0798  0.0584  246 ASN A CG  
1966  O OD1 . ASN A 246 ? 0.9710 1.0188 0.4190 -0.0197 0.0786  0.0521  246 ASN A OD1 
1967  N ND2 . ASN A 246 ? 0.9613 0.9797 0.4317 -0.0256 0.0992  0.0532  246 ASN A ND2 
1968  N N   . PHE A 247 ? 0.9120 0.9348 0.3908 0.0651  0.0066  0.1255  247 PHE A N   
1969  C CA  . PHE A 247 ? 0.8759 0.9137 0.3874 0.0862  -0.0097 0.1322  247 PHE A CA  
1970  C C   . PHE A 247 ? 0.8885 0.8990 0.3895 0.1023  -0.0144 0.1512  247 PHE A C   
1971  O O   . PHE A 247 ? 0.9335 0.9177 0.3931 0.1058  -0.0188 0.1677  247 PHE A O   
1972  C CB  . PHE A 247 ? 0.8773 0.9400 0.3848 0.0936  -0.0280 0.1360  247 PHE A CB  
1973  C CG  . PHE A 247 ? 0.8433 0.9270 0.3845 0.1131  -0.0440 0.1423  247 PHE A CG  
1974  C CD1 . PHE A 247 ? 0.7964 0.8969 0.3839 0.1149  -0.0418 0.1321  247 PHE A CD1 
1975  C CD2 . PHE A 247 ? 0.8609 0.9493 0.3872 0.1288  -0.0619 0.1579  247 PHE A CD2 
1976  C CE1 . PHE A 247 ? 0.7690 0.8907 0.3847 0.1300  -0.0548 0.1379  247 PHE A CE1 
1977  C CE2 . PHE A 247 ? 0.8307 0.9433 0.3900 0.1454  -0.0748 0.1619  247 PHE A CE2 
1978  C CZ  . PHE A 247 ? 0.7852 0.9149 0.3880 0.1450  -0.0701 0.1520  247 PHE A CZ  
1979  N N   . ILE A 248 ? 0.8515 0.8670 0.3895 0.1121  -0.0142 0.1481  248 ILE A N   
1980  C CA  . ILE A 248 ? 0.8582 0.8534 0.3935 0.1301  -0.0200 0.1625  248 ILE A CA  
1981  C C   . ILE A 248 ? 0.8329 0.8575 0.3925 0.1491  -0.0370 0.1671  248 ILE A C   
1982  O O   . ILE A 248 ? 0.7909 0.8402 0.3891 0.1513  -0.0377 0.1582  248 ILE A O   
1983  C CB  . ILE A 248 ? 0.8386 0.8195 0.3958 0.1275  -0.0077 0.1555  248 ILE A CB  
1984  C CG1 . ILE A 248 ? 0.8511 0.8172 0.3991 0.1046  0.0108  0.1441  248 ILE A CG1 
1985  C CG2 . ILE A 248 ? 0.8603 0.8111 0.4035 0.1436  -0.0117 0.1698  248 ILE A CG2 
1986  C CD1 . ILE A 248 ? 0.9067 0.8428 0.4043 0.0940  0.0167  0.1546  248 ILE A CD1 
1987  N N   . ALA A 249 ? 0.8617 0.8838 0.3979 0.1619  -0.0513 0.1812  249 ALA A N   
1988  C CA  . ALA A 249 ? 0.8424 0.8975 0.4008 0.1785  -0.0679 0.1846  249 ALA A CA  
1989  C C   . ALA A 249 ? 0.8271 0.8830 0.4078 0.1982  -0.0711 0.1890  249 ALA A C   
1990  O O   . ALA A 249 ? 0.8490 0.8714 0.4142 0.2048  -0.0668 0.1953  249 ALA A O   
1991  C CB  . ALA A 249 ? 0.8811 0.9347 0.4082 0.1857  -0.0836 0.1969  249 ALA A CB  
1992  N N   . PRO A 250 ? 0.7920 0.8864 0.4085 0.2066  -0.0783 0.1851  250 PRO A N   
1993  C CA  . PRO A 250 ? 0.7810 0.8822 0.4175 0.2258  -0.0814 0.1881  250 PRO A CA  
1994  C C   . PRO A 250 ? 0.8124 0.9113 0.4356 0.2482  -0.0966 0.2001  250 PRO A C   
1995  O O   . PRO A 250 ? 0.8145 0.9403 0.4416 0.2530  -0.1099 0.2029  250 PRO A O   
1996  C CB  . PRO A 250 ? 0.7365 0.8830 0.4132 0.2228  -0.0834 0.1799  250 PRO A CB  
1997  C CG  . PRO A 250 ? 0.7332 0.8994 0.4088 0.2095  -0.0894 0.1766  250 PRO A CG  
1998  C CD  . PRO A 250 ? 0.7610 0.8937 0.4025 0.1959  -0.0820 0.1758  250 PRO A CD  
1999  N N   . GLU A 251 ? 0.8388 0.9049 0.4478 0.2622  -0.0960 0.2062  251 GLU A N   
2000  C CA  . GLU A 251 ? 0.8651 0.9310 0.4715 0.2880  -0.1115 0.2149  251 GLU A CA  
2001  C C   . GLU A 251 ? 0.8309 0.9377 0.4792 0.3026  -0.1125 0.2073  251 GLU A C   
2002  O O   . GLU A 251 ? 0.8240 0.9685 0.4913 0.3142  -0.1248 0.2077  251 GLU A O   
2003  C CB  . GLU A 251 ? 0.9096 0.9217 0.4859 0.2977  -0.1114 0.2234  251 GLU A CB  
2004  C CG  . GLU A 251 ? 0.9646 0.9468 0.5018 0.3042  -0.1270 0.2385  251 GLU A CG  
2005  C CD  . GLU A 251 ? 0.9902 0.9713 0.5336 0.3352  -0.1457 0.2448  251 GLU A CD  
2006  O OE1 . GLU A 251 ? 1.0034 0.9587 0.5492 0.3491  -0.1436 0.2440  251 GLU A OE1 
2007  O OE2 . GLU A 251 ? 0.9992 1.0050 0.5462 0.3463  -0.1634 0.2492  251 GLU A OE2 
2008  N N   . TYR A 252 ? 0.8111 0.9118 0.4734 0.3005  -0.0990 0.1997  252 TYR A N   
2009  C CA  . TYR A 252 ? 0.7830 0.9191 0.4803 0.3121  -0.0968 0.1919  252 TYR A CA  
2010  C C   . TYR A 252 ? 0.7396 0.9012 0.4602 0.2923  -0.0853 0.1829  252 TYR A C   
2011  O O   . TYR A 252 ? 0.7323 0.8720 0.4437 0.2736  -0.0757 0.1801  252 TYR A O   
2012  C CB  . TYR A 252 ? 0.8018 0.9092 0.4947 0.3289  -0.0928 0.1900  252 TYR A CB  
2013  C CG  . TYR A 252 ? 0.8479 0.9290 0.5220 0.3517  -0.1067 0.1984  252 TYR A CG  
2014  C CD1 . TYR A 252 ? 0.8535 0.9656 0.5480 0.3759  -0.1194 0.1973  252 TYR A CD1 
2015  C CD2 . TYR A 252 ? 0.8889 0.9138 0.5254 0.3486  -0.1079 0.2075  252 TYR A CD2 
2016  C CE1 . TYR A 252 ? 0.8989 0.9848 0.5780 0.3987  -0.1352 0.2047  252 TYR A CE1 
2017  C CE2 . TYR A 252 ? 0.9367 0.9323 0.5537 0.3691  -0.1232 0.2169  252 TYR A CE2 
2018  C CZ  . TYR A 252 ? 0.9418 0.9670 0.5806 0.3953  -0.1379 0.2154  252 TYR A CZ  
2019  O OH  . TYR A 252 ? 0.9920 0.9862 0.6134 0.4175  -0.1560 0.2245  252 TYR A OH  
2020  N N   . ALA A 253 ? 0.7137 0.9219 0.4653 0.2964  -0.0871 0.1785  253 ALA A N   
2021  C CA  . ALA A 253 ? 0.6771 0.9095 0.4511 0.2794  -0.0785 0.1717  253 ALA A CA  
2022  C C   . ALA A 253 ? 0.6670 0.9246 0.4619 0.2917  -0.0740 0.1665  253 ALA A C   
2023  O O   . ALA A 253 ? 0.6757 0.9590 0.4824 0.3104  -0.0803 0.1665  253 ALA A O   
2024  C CB  . ALA A 253 ? 0.6572 0.9256 0.4470 0.2657  -0.0853 0.1721  253 ALA A CB  
2025  N N   . TYR A 254 ? 0.6510 0.9022 0.4505 0.2813  -0.0634 0.1612  254 TYR A N   
2026  C CA  . TYR A 254 ? 0.6448 0.9172 0.4590 0.2905  -0.0571 0.1552  254 TYR A CA  
2027  C C   . TYR A 254 ? 0.6210 0.9481 0.4623 0.2827  -0.0580 0.1542  254 TYR A C   
2028  O O   . TYR A 254 ? 0.6024 0.9421 0.4514 0.2628  -0.0604 0.1569  254 TYR A O   
2029  C CB  . TYR A 254 ? 0.6404 0.8843 0.4462 0.2811  -0.0469 0.1503  254 TYR A CB  
2030  C CG  . TYR A 254 ? 0.6674 0.8609 0.4497 0.2911  -0.0445 0.1496  254 TYR A CG  
2031  C CD1 . TYR A 254 ? 0.6884 0.8728 0.4672 0.3122  -0.0426 0.1449  254 TYR A CD1 
2032  C CD2 . TYR A 254 ? 0.6744 0.8299 0.4387 0.2788  -0.0439 0.1527  254 TYR A CD2 
2033  C CE1 . TYR A 254 ? 0.7167 0.8518 0.4738 0.3202  -0.0416 0.1447  254 TYR A CE1 
2034  C CE2 . TYR A 254 ? 0.7021 0.8113 0.4445 0.2852  -0.0412 0.1529  254 TYR A CE2 
2035  C CZ  . TYR A 254 ? 0.7238 0.8211 0.4622 0.3057  -0.0408 0.1497  254 TYR A CZ  
2036  O OH  . TYR A 254 ? 0.7550 0.8030 0.4713 0.3110  -0.0393 0.1504  254 TYR A OH  
2037  N N   . LYS A 255 ? 0.6244 0.9839 0.4807 0.2982  -0.0557 0.1495  255 LYS A N   
2038  C CA  . LYS A 255 ? 0.6062 1.0222 0.4891 0.2914  -0.0549 0.1481  255 LYS A CA  
2039  C C   . LYS A 255 ? 0.5988 1.0248 0.4848 0.2846  -0.0425 0.1424  255 LYS A C   
2040  O O   . LYS A 255 ? 0.6137 1.0242 0.4913 0.2998  -0.0362 0.1355  255 LYS A O   
2041  C CB  . LYS A 255 ? 0.6183 1.0696 0.5185 0.3145  -0.0610 0.1452  255 LYS A CB  
2042  C CG  . LYS A 255 ? 0.6038 1.1072 0.5295 0.3063  -0.0679 0.1477  255 LYS A CG  
2043  C CD  . LYS A 255 ? 0.6208 1.1447 0.5586 0.3310  -0.0798 0.1463  255 LYS A CD  
2044  C CE  . LYS A 255 ? 0.6183 1.2028 0.5894 0.3433  -0.0764 0.1373  255 LYS A CE  
2045  N NZ  . LYS A 255 ? 0.6316 1.2406 0.6195 0.3634  -0.0920 0.1368  255 LYS A NZ  
2046  N N   . ILE A 256 ? 0.5793 1.0293 0.4755 0.2613  -0.0402 0.1453  256 ILE A N   
2047  C CA  . ILE A 256 ? 0.5758 1.0319 0.4696 0.2504  -0.0299 0.1421  256 ILE A CA  
2048  C C   . ILE A 256 ? 0.5756 1.0895 0.4896 0.2541  -0.0233 0.1375  256 ILE A C   
2049  O O   . ILE A 256 ? 0.5631 1.1138 0.4924 0.2359  -0.0240 0.1422  256 ILE A O   
2050  C CB  . ILE A 256 ? 0.5605 1.0044 0.4510 0.2214  -0.0324 0.1489  256 ILE A CB  
2051  C CG1 . ILE A 256 ? 0.5561 0.9615 0.4383 0.2156  -0.0412 0.1528  256 ILE A CG1 
2052  C CG2 . ILE A 256 ? 0.5654 0.9907 0.4417 0.2141  -0.0246 0.1459  256 ILE A CG2 
2053  C CD1 . ILE A 256 ? 0.5440 0.9316 0.4249 0.1907  -0.0450 0.1566  256 ILE A CD1 
2054  N N   . VAL A 257 ? 0.5915 1.1140 0.5066 0.2775  -0.0167 0.1272  257 VAL A N   
2055  C CA  . VAL A 257 ? 0.5938 1.1757 0.5314 0.2842  -0.0090 0.1193  257 VAL A CA  
2056  C C   . VAL A 257 ? 0.5937 1.1955 0.5261 0.2662  0.0042  0.1166  257 VAL A C   
2057  O O   . VAL A 257 ? 0.5886 1.2431 0.5386 0.2540  0.0101  0.1166  257 VAL A O   
2058  C CB  . VAL A 257 ? 0.6136 1.2017 0.5591 0.3187  -0.0082 0.1068  257 VAL A CB  
2059  C CG1 . VAL A 257 ? 0.6172 1.1971 0.5703 0.3344  -0.0235 0.1114  257 VAL A CG1 
2060  C CG2 . VAL A 257 ? 0.6321 1.1731 0.5540 0.3323  -0.0031 0.0992  257 VAL A CG2 
2061  N N   . LYS A 258 ? 0.6017 1.1619 0.5092 0.2633  0.0085  0.1148  258 LYS A N   
2062  C CA  . LYS A 258 ? 0.6066 1.1787 0.5027 0.2458  0.0194  0.1130  258 LYS A CA  
2063  C C   . LYS A 258 ? 0.6004 1.1303 0.4759 0.2218  0.0138  0.1236  258 LYS A C   
2064  O O   . LYS A 258 ? 0.6016 1.0807 0.4629 0.2273  0.0080  0.1239  258 LYS A O   
2065  C CB  . LYS A 258 ? 0.6280 1.1972 0.5140 0.2659  0.0306  0.0970  258 LYS A CB  
2066  C CG  . LYS A 258 ? 0.6370 1.2691 0.5383 0.2692  0.0444  0.0858  258 LYS A CG  
2067  C CD  . LYS A 258 ? 0.6558 1.2863 0.5353 0.2643  0.0575  0.0762  258 LYS A CD  
2068  C CE  . LYS A 258 ? 0.6751 1.2692 0.5428 0.2922  0.0591  0.0610  258 LYS A CE  
2069  N NZ  . LYS A 258 ? 0.6971 1.3161 0.5550 0.2953  0.0750  0.0444  258 LYS A NZ  
2070  N N   . LYS A 259 ? 0.5963 1.1481 0.4714 0.1947  0.0150  0.1320  259 LYS A N   
2071  C CA  . LYS A 259 ? 0.5954 1.1115 0.4520 0.1715  0.0087  0.1412  259 LYS A CA  
2072  C C   . LYS A 259 ? 0.6137 1.1406 0.4516 0.1610  0.0188  0.1381  259 LYS A C   
2073  O O   . LYS A 259 ? 0.6199 1.1925 0.4623 0.1478  0.0267  0.1402  259 LYS A O   
2074  C CB  . LYS A 259 ? 0.5818 1.1074 0.4499 0.1465  -0.0016 0.1553  259 LYS A CB  
2075  C CG  . LYS A 259 ? 0.5658 1.0719 0.4467 0.1522  -0.0134 0.1585  259 LYS A CG  
2076  C CD  . LYS A 259 ? 0.5550 1.0767 0.4502 0.1285  -0.0233 0.1700  259 LYS A CD  
2077  C CE  . LYS A 259 ? 0.5418 1.0464 0.4480 0.1347  -0.0343 0.1709  259 LYS A CE  
2078  N NZ  . LYS A 259 ? 0.5329 1.0562 0.4557 0.1137  -0.0443 0.1797  259 LYS A NZ  
2079  N N   . GLY A 260 ? 0.7385 1.4449 0.4617 -0.1275 -0.0950 0.1389  260 GLY A N   
2080  C CA  . GLY A 260 ? 0.7181 1.4090 0.4613 -0.1243 -0.0892 0.1353  260 GLY A CA  
2081  C C   . GLY A 260 ? 0.7151 1.2525 0.4531 -0.1033 -0.0803 0.1273  260 GLY A C   
2082  O O   . GLY A 260 ? 0.7334 1.1772 0.4473 -0.0952 -0.0791 0.1245  260 GLY A O   
2083  N N   . ASP A 261 ? 0.6931 1.2139 0.4531 -0.0930 -0.0740 0.1245  261 ASP A N   
2084  C CA  . ASP A 261 ? 0.6852 1.0813 0.4470 -0.0696 -0.0649 0.1187  261 ASP A CA  
2085  C C   . ASP A 261 ? 0.6524 1.0315 0.4520 -0.0020 -0.0537 0.1265  261 ASP A C   
2086  O O   . ASP A 261 ? 0.6291 1.0741 0.4612 0.0374  -0.0489 0.1338  261 ASP A O   
2087  C CB  . ASP A 261 ? 0.6748 1.0619 0.4461 -0.0826 -0.0624 0.1134  261 ASP A CB  
2088  C CG  . ASP A 261 ? 0.7242 1.0723 0.4396 -0.1521 -0.0725 0.1043  261 ASP A CG  
2089  O OD1 . ASP A 261 ? 0.7755 1.0728 0.4350 -0.1866 -0.0809 0.1006  261 ASP A OD1 
2090  O OD2 . ASP A 261 ? 0.7210 1.0804 0.4398 -0.1723 -0.0725 0.1010  261 ASP A OD2 
2091  N N   . SER A 262 ? 0.6610 0.9489 0.4467 0.0109  -0.0499 0.1259  262 SER A N   
2092  C CA  . SER A 262 ? 0.6415 0.9001 0.4522 0.0633  -0.0403 0.1345  262 SER A CA  
2093  C C   . SER A 262 ? 0.6481 0.8038 0.4448 0.0647  -0.0352 0.1316  262 SER A C   
2094  O O   . SER A 262 ? 0.6723 0.7792 0.4355 0.0337  -0.0390 0.1224  262 SER A O   
2095  C CB  . SER A 262 ? 0.6477 0.9531 0.4571 0.0825  -0.0424 0.1432  262 SER A CB  
2096  O OG  . SER A 262 ? 0.6413 0.9039 0.4625 0.1261  -0.0340 0.1525  262 SER A OG  
2097  N N   . THR A 263 ? 0.6351 0.7591 0.4498 0.1008  -0.0269 0.1403  263 THR A N   
2098  C CA  . THR A 263 ? 0.6385 0.6896 0.4439 0.1047  -0.0215 0.1409  263 THR A CA  
2099  C C   . THR A 263 ? 0.6346 0.6738 0.4521 0.1358  -0.0151 0.1546  263 THR A C   
2100  O O   . THR A 263 ? 0.6317 0.6912 0.4635 0.1583  -0.0129 0.1625  263 THR A O   
2101  C CB  . THR A 263 ? 0.6269 0.6422 0.4413 0.0982  -0.0174 0.1355  263 THR A CB  
2102  O OG1 . THR A 263 ? 0.6387 0.5989 0.4324 0.0958  -0.0145 0.1335  263 THR A OG1 
2103  C CG2 . THR A 263 ? 0.6101 0.6235 0.4527 0.1226  -0.0110 0.1435  263 THR A CG2 
2104  N N   . ILE A 264 ? 0.6440 0.6482 0.4471 0.1384  -0.0124 0.1581  264 ILE A N   
2105  C CA  . ILE A 264 ? 0.6440 0.6365 0.4552 0.1594  -0.0062 0.1728  264 ILE A CA  
2106  C C   . ILE A 264 ? 0.6356 0.5961 0.4570 0.1572  0.0000  0.1765  264 ILE A C   
2107  O O   . ILE A 264 ? 0.6358 0.5796 0.4477 0.1515  0.0020  0.1735  264 ILE A O   
2108  C CB  . ILE A 264 ? 0.6592 0.6492 0.4503 0.1653  -0.0064 0.1773  264 ILE A CB  
2109  C CG1 . ILE A 264 ? 0.6713 0.6958 0.4500 0.1630  -0.0138 0.1736  264 ILE A CG1 
2110  C CG2 . ILE A 264 ? 0.6604 0.6454 0.4596 0.1816  0.0000  0.1948  264 ILE A CG2 
2111  C CD1 . ILE A 264 ? 0.6956 0.7084 0.4421 0.1632  -0.0164 0.1726  264 ILE A CD1 
2112  N N   . MET A 265 ? 0.6365 0.5879 0.4695 0.1638  0.0023  0.1833  265 MET A N   
2113  C CA  . MET A 265 ? 0.6352 0.5574 0.4741 0.1554  0.0065  0.1873  265 MET A CA  
2114  C C   . MET A 265 ? 0.6520 0.5615 0.4830 0.1550  0.0106  0.2049  265 MET A C   
2115  O O   . MET A 265 ? 0.6735 0.5778 0.4923 0.1662  0.0103  0.2153  265 MET A O   
2116  C CB  . MET A 265 ? 0.6439 0.5519 0.4843 0.1615  0.0055  0.1851  265 MET A CB  
2117  C CG  . MET A 265 ? 0.6456 0.5209 0.4885 0.1484  0.0080  0.1851  265 MET A CG  
2118  S SD  . MET A 265 ? 0.6657 0.5214 0.4995 0.1641  0.0061  0.1800  265 MET A SD  
2119  C CE  . MET A 265 ? 0.6289 0.5395 0.4852 0.1601  0.0027  0.1624  265 MET A CE  
2120  N N   . LYS A 266 ? 0.6458 0.5563 0.4806 0.1416  0.0143  0.2093  266 LYS A N   
2121  C CA  . LYS A 266 ? 0.6625 0.5779 0.4900 0.1325  0.0178  0.2281  266 LYS A CA  
2122  C C   . LYS A 266 ? 0.6869 0.5681 0.5053 0.1115  0.0178  0.2364  266 LYS A C   
2123  O O   . LYS A 266 ? 0.6750 0.5558 0.5029 0.0982  0.0185  0.2310  266 LYS A O   
2124  C CB  . LYS A 266 ? 0.6473 0.6024 0.4790 0.1328  0.0218  0.2308  266 LYS A CB  
2125  C CG  . LYS A 266 ? 0.6462 0.6209 0.4677 0.1543  0.0215  0.2272  266 LYS A CG  
2126  C CD  . LYS A 266 ? 0.6624 0.6480 0.4767 0.1584  0.0222  0.2429  266 LYS A CD  
2127  C CE  . LYS A 266 ? 0.6651 0.6760 0.4658 0.1795  0.0230  0.2422  266 LYS A CE  
2128  N NZ  . LYS A 266 ? 0.6797 0.7081 0.4750 0.1825  0.0246  0.2599  266 LYS A NZ  
2129  N N   . SER A 267 ? 0.7309 0.5753 0.5220 0.1083  0.0165  0.2495  267 SER A N   
2130  C CA  . SER A 267 ? 0.7787 0.5663 0.5394 0.0864  0.0146  0.2574  267 SER A CA  
2131  C C   . SER A 267 ? 0.8435 0.5875 0.5580 0.0751  0.0134  0.2774  267 SER A C   
2132  O O   . SER A 267 ? 0.8564 0.5964 0.5597 0.0987  0.0132  0.2807  267 SER A O   
2133  C CB  . SER A 267 ? 0.7903 0.5351 0.5419 0.1058  0.0118  0.2430  267 SER A CB  
2134  O OG  . SER A 267 ? 0.8511 0.5244 0.5592 0.0885  0.0092  0.2494  267 SER A OG  
2135  N N   . GLU A 268 ? 0.8912 0.6006 0.5731 0.0354  0.0117  0.2912  268 GLU A N   
2136  C CA  . GLU A 268 ? 0.9743 0.6219 0.5939 0.0135  0.0090  0.3116  268 GLU A CA  
2137  C C   . GLU A 268 ? 1.0570 0.5906 0.6098 0.0285  0.0042  0.3084  268 GLU A C   
2138  O O   . GLU A 268 ? 1.1452 0.6010 0.6277 0.0214  0.0012  0.3231  268 GLU A O   
2139  C CB  . GLU A 268 ? 1.0009 0.6666 0.6046 -0.0463 0.0079  0.3306  268 GLU A CB  
2140  C CG  . GLU A 268 ? 0.9263 0.7147 0.5900 -0.0547 0.0132  0.3348  268 GLU A CG  
2141  C CD  . GLU A 268 ? 0.8967 0.7378 0.5812 -0.0264 0.0173  0.3394  268 GLU A CD  
2142  O OE1 . GLU A 268 ? 0.9491 0.7583 0.5942 -0.0372 0.0159  0.3558  268 GLU A OE1 
2143  O OE2 . GLU A 268 ? 0.8293 0.7358 0.5617 0.0059  0.0215  0.3265  268 GLU A OE2 
2144  N N   . LEU A 269 ? 1.0374 0.5578 0.6041 0.0520  0.0036  0.2899  269 LEU A N   
2145  C CA  . LEU A 269 ? 1.1192 0.5365 0.6185 0.0760  -0.0002 0.2855  269 LEU A CA  
2146  C C   . LEU A 269 ? 1.1453 0.5451 0.6210 0.1317  0.0004  0.2841  269 LEU A C   
2147  O O   . LEU A 269 ? 1.0775 0.5591 0.6071 0.1538  0.0036  0.2800  269 LEU A O   
2148  C CB  . LEU A 269 ? 1.0836 0.5094 0.6102 0.0882  -0.0003 0.2666  269 LEU A CB  
2149  C CG  . LEU A 269 ? 1.0853 0.5023 0.6130 0.0373  -0.0023 0.2680  269 LEU A CG  
2150  C CD1 . LEU A 269 ? 1.0244 0.4776 0.5996 0.0530  -0.0009 0.2480  269 LEU A CD1 
2151  C CD2 . LEU A 269 ? 1.2106 0.5015 0.6375 0.0083  -0.0088 0.2800  269 LEU A CD2 
2152  N N   . GLU A 270 ? 1.2528 0.5427 0.6397 0.1562  -0.0029 0.2876  270 GLU A N   
2153  C CA  . GLU A 270 ? 1.2983 0.5643 0.6456 0.2157  -0.0023 0.2891  270 GLU A CA  
2154  C C   . GLU A 270 ? 1.2790 0.5715 0.6393 0.2740  -0.0013 0.2715  270 GLU A C   
2155  O O   . GLU A 270 ? 1.1741 0.5759 0.6209 0.2781  0.0010  0.2581  270 GLU A O   
2156  C CB  . GLU A 270 ? 1.4456 0.5710 0.6709 0.2136  -0.0063 0.3073  270 GLU A CB  
2157  C CG  . GLU A 270 ? 1.5494 0.5507 0.6894 0.1683  -0.0122 0.3137  270 GLU A CG  
2158  C CD  . GLU A 270 ? 1.7159 0.5595 0.7156 0.1629  -0.0175 0.3320  270 GLU A CD  
2159  O OE1 . GLU A 270 ? 1.7496 0.5805 0.7196 0.1993  -0.0158 0.3403  270 GLU A OE1 
2160  O OE2 . GLU A 270 ? 1.8224 0.5475 0.7330 0.1193  -0.0242 0.3385  270 GLU A OE2 
2161  N N   . TYR A 271 ? 1.3862 0.5803 0.6548 0.3185  -0.0035 0.2722  271 TYR A N   
2162  C CA  . TYR A 271 ? 1.3748 0.6105 0.6501 0.3834  -0.0019 0.2587  271 TYR A CA  
2163  C C   . TYR A 271 ? 1.4841 0.5997 0.6655 0.4068  -0.0048 0.2557  271 TYR A C   
2164  O O   . TYR A 271 ? 1.6223 0.5969 0.6855 0.4202  -0.0081 0.2668  271 TYR A O   
2165  C CB  . TYR A 271 ? 1.3966 0.6667 0.6521 0.4463  0.0000  0.2636  271 TYR A CB  
2166  C CG  . TYR A 271 ? 1.3733 0.7263 0.6465 0.5132  0.0019  0.2523  271 TYR A CG  
2167  C CD1 . TYR A 271 ? 1.2501 0.7425 0.6272 0.4994  0.0032  0.2387  271 TYR A CD1 
2168  C CD2 . TYR A 271 ? 1.4832 0.7776 0.6612 0.5913  0.0022  0.2565  271 TYR A CD2 
2169  C CE1 . TYR A 271 ? 1.2301 0.8143 0.6233 0.5529  0.0044  0.2308  271 TYR A CE1 
2170  C CE2 . TYR A 271 ? 1.4614 0.8541 0.6568 0.6553  0.0044  0.2483  271 TYR A CE2 
2171  C CZ  . TYR A 271 ? 1.3311 0.8755 0.6380 0.6317  0.0053  0.2361  271 TYR A CZ  
2172  O OH  . TYR A 271 ? 1.3120 0.9678 0.6349 0.6884  0.0069  0.2303  271 TYR A OH  
2173  N N   . GLY A 272 ? 1.4312 0.5949 0.6564 0.4113  -0.0041 0.2409  272 GLY A N   
2174  C CA  . GLY A 272 ? 1.5283 0.5853 0.6694 0.4342  -0.0068 0.2361  272 GLY A CA  
2175  C C   . GLY A 272 ? 1.6018 0.6450 0.6769 0.5284  -0.0052 0.2329  272 GLY A C   
2176  O O   . GLY A 272 ? 1.7157 0.6437 0.6911 0.5608  -0.0077 0.2310  272 GLY A O   
2177  N N   . ASN A 273 ? 1.5433 0.7064 0.6678 0.5740  -0.0013 0.2328  273 ASN A N   
2178  C CA  . ASN A 273 ? 1.5941 0.7906 0.6727 0.6688  0.0012  0.2308  273 ASN A CA  
2179  C C   . ASN A 273 ? 1.5664 0.8130 0.6674 0.6916  0.0023  0.2172  273 ASN A C   
2180  O O   . ASN A 273 ? 1.6625 0.8641 0.6787 0.7669  0.0031  0.2162  273 ASN A O   
2181  C CB  . ASN A 273 ? 1.7747 0.8048 0.6959 0.7275  -0.0005 0.2426  273 ASN A CB  
2182  C CG  . ASN A 273 ? 1.8073 0.9065 0.6989 0.8216  0.0032  0.2476  273 ASN A CG  
2183  O OD1 . ASN A 273 ? 1.8735 0.9191 0.7077 0.8420  0.0030  0.2600  273 ASN A OD1 
2184  N ND2 . ASN A 273 ? 1.7598 0.9895 0.6915 0.8781  0.0066  0.2392  273 ASN A ND2 
2185  N N   . CYS A 274 ? 1.4380 0.7792 0.6501 0.6289  0.0026  0.2073  274 CYS A N   
2186  C CA  . CYS A 274 ? 1.3935 0.7905 0.6429 0.6325  0.0035  0.1944  274 CYS A CA  
2187  C C   . CYS A 274 ? 1.2629 0.8548 0.6245 0.6295  0.0060  0.1881  274 CYS A C   
2188  O O   . CYS A 274 ? 1.2153 0.8869 0.6183 0.6244  0.0064  0.1933  274 CYS A O   
2189  C CB  . CYS A 274 ? 1.3634 0.6970 0.6392 0.5540  0.0009  0.1888  274 CYS A CB  
2190  S SG  . CYS A 274 ? 1.2836 0.6338 0.6294 0.4673  -0.0001 0.1954  274 CYS A SG  
2191  N N   . ASN A 275 ? 1.2131 0.8769 0.6166 0.6287  0.0069  0.1775  275 ASN A N   
2192  C CA  . ASN A 275 ? 1.0976 0.9358 0.6000 0.6084  0.0077  0.1715  275 ASN A CA  
2193  C C   . ASN A 275 ? 1.0226 0.8741 0.5877 0.5442  0.0069  0.1601  275 ASN A C   
2194  O O   . ASN A 275 ? 1.0636 0.8235 0.5933 0.5416  0.0068  0.1555  275 ASN A O   
2195  C CB  . ASN A 275 ? 1.1191 1.0672 0.6042 0.6841  0.0099  0.1727  275 ASN A CB  
2196  C CG  . ASN A 275 ? 1.0130 1.1509 0.5898 0.6565  0.0092  0.1697  275 ASN A CG  
2197  O OD1 . ASN A 275 ? 0.9601 1.1573 0.5819 0.6205  0.0071  0.1727  275 ASN A OD1 
2198  N ND2 . ASN A 275 ? 0.9893 1.2203 0.5872 0.6700  0.0101  0.1645  275 ASN A ND2 
2199  N N   . THR A 276 ? 0.9229 0.8797 0.5715 0.4925  0.0058  0.1556  276 THR A N   
2200  C CA  . THR A 276 ? 0.8570 0.8279 0.5591 0.4351  0.0052  0.1450  276 THR A CA  
2201  C C   . THR A 276 ? 0.7760 0.8865 0.5449 0.4024  0.0033  0.1402  276 THR A C   
2202  O O   . THR A 276 ? 0.7645 0.9649 0.5443 0.4151  0.0019  0.1455  276 THR A O   
2203  C CB  . THR A 276 ? 0.8437 0.7189 0.5550 0.3789  0.0045  0.1448  276 THR A CB  
2204  O OG1 . THR A 276 ? 0.7975 0.6733 0.5456 0.3365  0.0044  0.1349  276 THR A OG1 
2205  C CG2 . THR A 276 ? 0.8003 0.7118 0.5462 0.3474  0.0033  0.1491  276 THR A CG2 
2206  N N   . LYS A 277 ? 0.7292 0.8529 0.5350 0.3578  0.0027  0.1308  277 LYS A N   
2207  C CA  . LYS A 277 ? 0.6669 0.8940 0.5219 0.3115  -0.0004 0.1259  277 LYS A CA  
2208  C C   . LYS A 277 ? 0.6296 0.8033 0.5089 0.2497  -0.0018 0.1203  277 LYS A C   
2209  O O   . LYS A 277 ? 0.5952 0.8235 0.4981 0.2067  -0.0054 0.1159  277 LYS A O   
2210  C CB  . LYS A 277 ? 0.6535 0.9524 0.5214 0.3137  -0.0002 0.1203  277 LYS A CB  
2211  C CG  . LYS A 277 ? 0.6646 1.0974 0.5284 0.3562  -0.0006 0.1266  277 LYS A CG  
2212  C CD  . LYS A 277 ? 0.6295 1.1709 0.5231 0.3251  -0.0026 0.1224  277 LYS A CD  
2213  C CE  . LYS A 277 ? 0.5858 1.1620 0.5104 0.2437  -0.0086 0.1183  277 LYS A CE  
2214  N NZ  . LYS A 277 ? 0.5674 1.2847 0.5090 0.2149  -0.0125 0.1196  277 LYS A NZ  
2215  N N   . CYS A 278 ? 0.6461 0.7134 0.5107 0.2460  0.0004  0.1215  278 CYS A N   
2216  C CA  . CYS A 278 ? 0.6184 0.6396 0.4999 0.1999  0.0002  0.1183  278 CYS A CA  
2217  C C   . CYS A 278 ? 0.6474 0.5879 0.5069 0.2071  0.0021  0.1270  278 CYS A C   
2218  O O   . CYS A 278 ? 0.6885 0.5622 0.5182 0.2247  0.0036  0.1303  278 CYS A O   
2219  C CB  . CYS A 278 ? 0.6011 0.5946 0.4942 0.1760  0.0014  0.1094  278 CYS A CB  
2220  S SG  . CYS A 278 ? 0.5787 0.5165 0.4825 0.1334  0.0024  0.1068  278 CYS A SG  
2221  N N   . GLN A 279 ? 0.6343 0.5779 0.5010 0.1907  0.0014  0.1312  279 GLN A N   
2222  C CA  . GLN A 279 ? 0.6625 0.5453 0.5081 0.1950  0.0030  0.1420  279 GLN A CA  
2223  C C   . GLN A 279 ? 0.6381 0.5001 0.4988 0.1600  0.0042  0.1426  279 GLN A C   
2224  O O   . GLN A 279 ? 0.6063 0.5028 0.4853 0.1412  0.0031  0.1363  279 GLN A O   
2225  C CB  . GLN A 279 ? 0.6790 0.5904 0.5125 0.2195  0.0018  0.1500  279 GLN A CB  
2226  C CG  . GLN A 279 ? 0.7181 0.5654 0.5221 0.2250  0.0032  0.1630  279 GLN A CG  
2227  C CD  . GLN A 279 ? 0.7867 0.5556 0.5392 0.2497  0.0038  0.1691  279 GLN A CD  
2228  O OE1 . GLN A 279 ? 0.8228 0.5975 0.5475 0.2919  0.0034  0.1687  279 GLN A OE1 
2229  N NE2 . GLN A 279 ? 0.8147 0.5100 0.5456 0.2241  0.0042  0.1755  279 GLN A NE2 
2230  N N   . THR A 280 ? 0.6635 0.4683 0.5072 0.1521  0.0060  0.1512  280 THR A N   
2231  C CA  . THR A 280 ? 0.6476 0.4473 0.5015 0.1261  0.0079  0.1561  280 THR A CA  
2232  C C   . THR A 280 ? 0.6831 0.4548 0.5132 0.1268  0.0085  0.1720  280 THR A C   
2233  O O   . THR A 280 ? 0.7308 0.4625 0.5270 0.1442  0.0071  0.1786  280 THR A O   
2234  C CB  . THR A 280 ? 0.6417 0.4193 0.5007 0.1041  0.0094  0.1536  280 THR A CB  
2235  O OG1 . THR A 280 ? 0.6880 0.4122 0.5164 0.0953  0.0088  0.1647  280 THR A OG1 
2236  C CG2 . THR A 280 ? 0.6262 0.4117 0.4962 0.1077  0.0086  0.1399  280 THR A CG2 
2237  N N   . PRO A 281 ? 0.6678 0.4585 0.5082 0.1106  0.0105  0.1790  281 PRO A N   
2238  C CA  . PRO A 281 ? 0.7013 0.4728 0.5197 0.1025  0.0112  0.1964  281 PRO A CA  
2239  C C   . PRO A 281 ? 0.7513 0.4678 0.5372 0.0793  0.0100  0.2069  281 PRO A C   
2240  O O   . PRO A 281 ? 0.7997 0.4822 0.5507 0.0696  0.0089  0.2222  281 PRO A O   
2241  C CB  . PRO A 281 ? 0.6682 0.4878 0.5075 0.0921  0.0142  0.2001  281 PRO A CB  
2242  C CG  . PRO A 281 ? 0.6294 0.4775 0.4901 0.0994  0.0144  0.1837  281 PRO A CG  
2243  C CD  . PRO A 281 ? 0.6268 0.4597 0.4907 0.1055  0.0118  0.1709  281 PRO A CD  
2244  N N   . MET A 282 ? 0.7472 0.4513 0.5380 0.0665  0.0095  0.1992  282 MET A N   
2245  C CA  . MET A 282 ? 0.8031 0.4479 0.5550 0.0396  0.0066  0.2069  282 MET A CA  
2246  C C   . MET A 282 ? 0.8659 0.4319 0.5679 0.0628  0.0031  0.2033  282 MET A C   
2247  O O   . MET A 282 ? 0.9451 0.4313 0.5855 0.0464  -0.0007 0.2130  282 MET A O   
2248  C CB  . MET A 282 ? 0.7722 0.4406 0.5495 0.0194  0.0074  0.1992  282 MET A CB  
2249  C CG  . MET A 282 ? 0.7176 0.4648 0.5363 0.0090  0.0117  0.2010  282 MET A CG  
2250  S SD  . MET A 282 ? 0.7466 0.5201 0.5501 -0.0376 0.0113  0.2230  282 MET A SD  
2251  C CE  . MET A 282 ? 0.7625 0.5085 0.5559 -0.0652 0.0080  0.2173  282 MET A CE  
2252  N N   . GLY A 283 ? 0.8385 0.4273 0.5594 0.1008  0.0040  0.1898  283 GLY A N   
2253  C CA  . GLY A 283 ? 0.8932 0.4274 0.5697 0.1354  0.0019  0.1850  283 GLY A CA  
2254  C C   . GLY A 283 ? 0.8401 0.4358 0.5570 0.1629  0.0034  0.1691  283 GLY A C   
2255  O O   . GLY A 283 ? 0.7695 0.4355 0.5411 0.1501  0.0052  0.1618  283 GLY A O   
2256  N N   . ALA A 284 ? 0.8838 0.4509 0.5651 0.2007  0.0023  0.1646  284 ALA A N   
2257  C CA  . ALA A 284 ? 0.8406 0.4793 0.5554 0.2270  0.0034  0.1522  284 ALA A CA  
2258  C C   . ALA A 284 ? 0.8271 0.4573 0.5525 0.2145  0.0034  0.1418  284 ALA A C   
2259  O O   . ALA A 284 ? 0.8707 0.4250 0.5612 0.1973  0.0019  0.1439  284 ALA A O   
2260  C CB  . ALA A 284 ? 0.8939 0.5308 0.5657 0.2845  0.0031  0.1545  284 ALA A CB  
2261  N N   . ILE A 285 ? 0.7714 0.4804 0.5404 0.2192  0.0045  0.1312  285 ILE A N   
2262  C CA  . ILE A 285 ? 0.7502 0.4639 0.5355 0.2072  0.0049  0.1207  285 ILE A CA  
2263  C C   . ILE A 285 ? 0.7607 0.5177 0.5383 0.2478  0.0052  0.1147  285 ILE A C   
2264  O O   . ILE A 285 ? 0.7389 0.5773 0.5342 0.2664  0.0052  0.1149  285 ILE A O   
2265  C CB  . ILE A 285 ? 0.6780 0.4433 0.5176 0.1670  0.0059  0.1141  285 ILE A CB  
2266  C CG1 . ILE A 285 ? 0.6766 0.3952 0.5167 0.1327  0.0065  0.1181  285 ILE A CG1 
2267  C CG2 . ILE A 285 ? 0.6484 0.4545 0.5102 0.1643  0.0063  0.1026  285 ILE A CG2 
2268  C CD1 . ILE A 285 ? 0.6247 0.3844 0.5007 0.1062  0.0081  0.1158  285 ILE A CD1 
2269  N N   . ASN A 286 ? 0.7973 0.5053 0.5456 0.2604  0.0050  0.1102  286 ASN A N   
2270  C CA  . ASN A 286 ? 0.8086 0.5609 0.5481 0.3006  0.0060  0.1045  286 ASN A CA  
2271  C C   . ASN A 286 ? 0.7891 0.5284 0.5435 0.2789  0.0063  0.0948  286 ASN A C   
2272  O O   . ASN A 286 ? 0.8459 0.4974 0.5537 0.2865  0.0051  0.0936  286 ASN A O   
2273  C CB  . ASN A 286 ? 0.9063 0.5932 0.5663 0.3614  0.0055  0.1100  286 ASN A CB  
2274  C CG  . ASN A 286 ? 0.9268 0.6656 0.5702 0.4141  0.0072  0.1051  286 ASN A CG  
2275  O OD1 . ASN A 286 ? 0.8620 0.7218 0.5603 0.4095  0.0087  0.1013  286 ASN A OD1 
2276  N ND2 . ASN A 286 ? 1.0267 0.6724 0.5859 0.4637  0.0066  0.1061  286 ASN A ND2 
2277  N N   . SER A 287 ? 0.7169 0.5357 0.5284 0.2487  0.0072  0.0882  287 SER A N   
2278  C CA  . SER A 287 ? 0.6957 0.5099 0.5230 0.2292  0.0079  0.0792  287 SER A CA  
2279  C C   . SER A 287 ? 0.6373 0.5516 0.5098 0.2111  0.0085  0.0733  287 SER A C   
2280  O O   . SER A 287 ? 0.6075 0.5869 0.5027 0.1968  0.0074  0.0757  287 SER A O   
2281  C CB  . SER A 287 ? 0.6841 0.4335 0.5191 0.1856  0.0075  0.0785  287 SER A CB  
2282  O OG  . SER A 287 ? 0.6271 0.4201 0.5045 0.1496  0.0082  0.0773  287 SER A OG  
2283  N N   . SER A 288 ? 0.6289 0.5491 0.5074 0.2076  0.0095  0.0659  288 SER A N   
2284  C CA  . SER A 288 ? 0.5842 0.5878 0.4963 0.1832  0.0095  0.0608  288 SER A CA  
2285  C C   . SER A 288 ? 0.5504 0.5202 0.4829 0.1343  0.0096  0.0549  288 SER A C   
2286  O O   . SER A 288 ? 0.5253 0.5401 0.4741 0.1074  0.0091  0.0503  288 SER A O   
2287  C CB  . SER A 288 ? 0.6007 0.6420 0.5028 0.2154  0.0111  0.0575  288 SER A CB  
2288  O OG  . SER A 288 ? 0.6491 0.5982 0.5134 0.2438  0.0118  0.0553  288 SER A OG  
2289  N N   . MET A 289 ? 0.5562 0.4503 0.4818 0.1232  0.0100  0.0562  289 MET A N   
2290  C CA  . MET A 289 ? 0.5313 0.3976 0.4701 0.0877  0.0108  0.0520  289 MET A CA  
2291  C C   . MET A 289 ? 0.5094 0.4092 0.4573 0.0609  0.0096  0.0517  289 MET A C   
2292  O O   . MET A 289 ? 0.5123 0.4398 0.4583 0.0648  0.0078  0.0567  289 MET A O   
2293  C CB  . MET A 289 ? 0.5453 0.3471 0.4740 0.0823  0.0113  0.0570  289 MET A CB  
2294  C CG  . MET A 289 ? 0.5856 0.3313 0.4878 0.0975  0.0104  0.0582  289 MET A CG  
2295  S SD  . MET A 289 ? 0.5811 0.3145 0.4863 0.0905  0.0112  0.0484  289 MET A SD  
2296  C CE  . MET A 289 ? 0.6327 0.2809 0.5003 0.0818  0.0083  0.0536  289 MET A CE  
2297  N N   . PRO A 290 ? 0.4970 0.3864 0.4454 0.0345  0.0100  0.0458  290 PRO A N   
2298  C CA  . PRO A 290 ? 0.4988 0.3909 0.4340 0.0090  0.0079  0.0450  290 PRO A CA  
2299  C C   . PRO A 290 ? 0.5035 0.3560 0.4299 0.0114  0.0090  0.0496  290 PRO A C   
2300  O O   . PRO A 290 ? 0.5157 0.3660 0.4233 -0.0009 0.0067  0.0503  290 PRO A O   
2301  C CB  . PRO A 290 ? 0.5018 0.3754 0.4252 -0.0125 0.0084  0.0375  290 PRO A CB  
2302  C CG  . PRO A 290 ? 0.4916 0.3406 0.4295 0.0031  0.0121  0.0356  290 PRO A CG  
2303  C CD  . PRO A 290 ? 0.4916 0.3613 0.4427 0.0289  0.0120  0.0392  290 PRO A CD  
2304  N N   . PHE A 291 ? 0.4999 0.3235 0.4345 0.0248  0.0120  0.0534  291 PHE A N   
2305  C CA  . PHE A 291 ? 0.5030 0.3043 0.4316 0.0268  0.0137  0.0598  291 PHE A CA  
2306  C C   . PHE A 291 ? 0.5081 0.3011 0.4429 0.0385  0.0139  0.0692  291 PHE A C   
2307  O O   . PHE A 291 ? 0.5184 0.3023 0.4538 0.0473  0.0130  0.0694  291 PHE A O   
2308  C CB  . PHE A 291 ? 0.5021 0.2829 0.4262 0.0228  0.0168  0.0579  291 PHE A CB  
2309  C CG  . PHE A 291 ? 0.5147 0.2815 0.4141 0.0146  0.0170  0.0503  291 PHE A CG  
2310  C CD1 . PHE A 291 ? 0.5384 0.2880 0.4061 0.0157  0.0164  0.0512  291 PHE A CD1 
2311  C CD2 . PHE A 291 ? 0.5144 0.2747 0.4117 0.0065  0.0173  0.0425  291 PHE A CD2 
2312  C CE1 . PHE A 291 ? 0.5722 0.2862 0.3959 0.0087  0.0156  0.0442  291 PHE A CE1 
2313  C CE2 . PHE A 291 ? 0.5411 0.2734 0.4014 -0.0028 0.0169  0.0362  291 PHE A CE2 
2314  C CZ  . PHE A 291 ? 0.5758 0.2787 0.3940 -0.0018 0.0158  0.0370  291 PHE A CZ  
2315  N N   . HIS A 292 ? 0.5103 0.3001 0.4406 0.0390  0.0148  0.0774  292 HIS A N   
2316  C CA  . HIS A 292 ? 0.5239 0.2996 0.4516 0.0408  0.0148  0.0885  292 HIS A CA  
2317  C C   . HIS A 292 ? 0.5200 0.3069 0.4462 0.0349  0.0173  0.0969  292 HIS A C   
2318  O O   . HIS A 292 ? 0.5122 0.3107 0.4334 0.0389  0.0192  0.0933  292 HIS A O   
2319  C CB  . HIS A 292 ? 0.5391 0.3151 0.4598 0.0544  0.0126  0.0934  292 HIS A CB  
2320  C CG  . HIS A 292 ? 0.5316 0.3291 0.4521 0.0567  0.0125  0.0966  292 HIS A CG  
2321  N ND1 . HIS A 292 ? 0.5416 0.3357 0.4562 0.0579  0.0132  0.1080  292 HIS A ND1 
2322  C CD2 . HIS A 292 ? 0.5226 0.3416 0.4414 0.0546  0.0112  0.0901  292 HIS A CD2 
2323  C CE1 . HIS A 292 ? 0.5355 0.3486 0.4478 0.0617  0.0128  0.1076  292 HIS A CE1 
2324  N NE2 . HIS A 292 ? 0.5278 0.3521 0.4390 0.0580  0.0110  0.0966  292 HIS A NE2 
2325  N N   . ASN A 293 ? 0.5350 0.3171 0.4568 0.0258  0.0170  0.1090  293 ASN A N   
2326  C CA  . ASN A 293 ? 0.5322 0.3450 0.4540 0.0201  0.0197  0.1202  293 ASN A CA  
2327  C C   . ASN A 293 ? 0.5533 0.3655 0.4656 0.0130  0.0183  0.1350  293 ASN A C   
2328  O O   . ASN A 293 ? 0.5606 0.4025 0.4707 -0.0014 0.0195  0.1482  293 ASN A O   
2329  C CB  . ASN A 293 ? 0.5302 0.3608 0.4556 0.0043  0.0208  0.1231  293 ASN A CB  
2330  C CG  . ASN A 293 ? 0.5604 0.3612 0.4732 -0.0212 0.0164  0.1296  293 ASN A CG  
2331  O OD1 . ASN A 293 ? 0.5864 0.3385 0.4830 -0.0187 0.0130  0.1277  293 ASN A OD1 
2332  N ND2 . ASN A 293 ? 0.5669 0.3952 0.4782 -0.0452 0.0160  0.1378  293 ASN A ND2 
2333  N N   . ILE A 294 ? 0.5667 0.3520 0.4708 0.0235  0.0160  0.1339  294 ILE A N   
2334  C CA  . ILE A 294 ? 0.5968 0.3670 0.4833 0.0189  0.0143  0.1475  294 ILE A CA  
2335  C C   . ILE A 294 ? 0.5822 0.3927 0.4757 0.0258  0.0170  0.1553  294 ILE A C   
2336  O O   . ILE A 294 ? 0.5942 0.4262 0.4820 0.0106  0.0179  0.1701  294 ILE A O   
2337  C CB  . ILE A 294 ? 0.6221 0.3524 0.4913 0.0377  0.0113  0.1438  294 ILE A CB  
2338  C CG1 . ILE A 294 ? 0.6446 0.3339 0.4989 0.0401  0.0090  0.1357  294 ILE A CG1 
2339  C CG2 . ILE A 294 ? 0.6659 0.3671 0.5055 0.0349  0.0095  0.1584  294 ILE A CG2 
2340  C CD1 . ILE A 294 ? 0.6794 0.3330 0.5104 0.0110  0.0067  0.1422  294 ILE A CD1 
2341  N N   . HIS A 295 ? 0.5628 0.3846 0.4634 0.0461  0.0177  0.1460  295 HIS A N   
2342  C CA  . HIS A 295 ? 0.5583 0.4064 0.4562 0.0571  0.0195  0.1515  295 HIS A CA  
2343  C C   . HIS A 295 ? 0.5474 0.3958 0.4409 0.0714  0.0188  0.1375  295 HIS A C   
2344  O O   . HIS A 295 ? 0.5450 0.3807 0.4404 0.0715  0.0157  0.1276  295 HIS A O   
2345  C CB  . HIS A 295 ? 0.5792 0.4153 0.4678 0.0592  0.0176  0.1618  295 HIS A CB  
2346  C CG  . HIS A 295 ? 0.5802 0.4461 0.4650 0.0647  0.0198  0.1727  295 HIS A CG  
2347  N ND1 . HIS A 295 ? 0.5717 0.4505 0.4529 0.0827  0.0200  0.1666  295 HIS A ND1 
2348  C CD2 . HIS A 295 ? 0.5944 0.4806 0.4735 0.0525  0.0214  0.1902  295 HIS A CD2 
2349  C CE1 . HIS A 295 ? 0.5779 0.4827 0.4531 0.0879  0.0223  0.1788  295 HIS A CE1 
2350  N NE2 . HIS A 295 ? 0.5885 0.5046 0.4655 0.0693  0.0235  0.1940  295 HIS A NE2 
2351  N N   . PRO A 296 ? 0.5505 0.4124 0.4291 0.0829  0.0212  0.1374  296 PRO A N   
2352  C CA  . PRO A 296 ? 0.5624 0.4037 0.4158 0.0903  0.0190  0.1243  296 PRO A CA  
2353  C C   . PRO A 296 ? 0.5692 0.4058 0.4168 0.0877  0.0140  0.1208  296 PRO A C   
2354  O O   . PRO A 296 ? 0.5750 0.4003 0.4126 0.0773  0.0097  0.1098  296 PRO A O   
2355  C CB  . PRO A 296 ? 0.5822 0.4298 0.4061 0.1111  0.0227  0.1282  296 PRO A CB  
2356  C CG  . PRO A 296 ? 0.5714 0.4627 0.4151 0.1134  0.0265  0.1457  296 PRO A CG  
2357  C CD  . PRO A 296 ? 0.5538 0.4499 0.4283 0.0901  0.0258  0.1502  296 PRO A CD  
2358  N N   . LEU A 297 ? 0.5708 0.4231 0.4231 0.0948  0.0143  0.1314  297 LEU A N   
2359  C CA  . LEU A 297 ? 0.5781 0.4358 0.4246 0.0952  0.0098  0.1300  297 LEU A CA  
2360  C C   . LEU A 297 ? 0.5680 0.4373 0.4359 0.0925  0.0074  0.1302  297 LEU A C   
2361  O O   . LEU A 297 ? 0.5706 0.4392 0.4479 0.0994  0.0090  0.1407  297 LEU A O   
2362  C CB  . LEU A 297 ? 0.5862 0.4566 0.4268 0.1077  0.0115  0.1419  297 LEU A CB  
2363  C CG  . LEU A 297 ? 0.6031 0.4707 0.4169 0.1215  0.0148  0.1440  297 LEU A CG  
2364  C CD1 . LEU A 297 ? 0.6053 0.4989 0.4219 0.1333  0.0177  0.1593  297 LEU A CD1 
2365  C CD2 . LEU A 297 ? 0.6364 0.4704 0.4044 0.1229  0.0103  0.1307  297 LEU A CD2 
2366  N N   . THR A 298 ? 0.5662 0.4448 0.4331 0.0833  0.0034  0.1195  298 THR A N   
2367  C CA  . THR A 298 ? 0.5614 0.4646 0.4431 0.0896  0.0015  0.1197  298 THR A CA  
2368  C C   . THR A 298 ? 0.5664 0.5121 0.4410 0.0841  -0.0042 0.1159  298 THR A C   
2369  O O   . THR A 298 ? 0.5782 0.5211 0.4310 0.0661  -0.0080 0.1106  298 THR A O   
2370  C CB  . THR A 298 ? 0.5523 0.4501 0.4446 0.0844  0.0023  0.1128  298 THR A CB  
2371  O OG1 . THR A 298 ? 0.5507 0.4613 0.4346 0.0640  -0.0011 0.1017  298 THR A OG1 
2372  C CG2 . THR A 298 ? 0.5494 0.4113 0.4452 0.0819  0.0068  0.1155  298 THR A CG2 
2373  N N   . ILE A 299 ? 0.5666 0.5506 0.4515 0.1007  -0.0053 0.1193  299 ILE A N   
2374  C CA  . ILE A 299 ? 0.5700 0.6191 0.4523 0.0965  -0.0109 0.1180  299 ILE A CA  
2375  C C   . ILE A 299 ? 0.5655 0.6625 0.4599 0.1083  -0.0111 0.1161  299 ILE A C   
2376  O O   . ILE A 299 ? 0.5718 0.6460 0.4692 0.1373  -0.0068 0.1198  299 ILE A O   
2377  C CB  . ILE A 299 ? 0.5802 0.6487 0.4583 0.1180  -0.0114 0.1278  299 ILE A CB  
2378  C CG1 . ILE A 299 ? 0.5828 0.7379 0.4604 0.1172  -0.0173 0.1282  299 ILE A CG1 
2379  C CG2 . ILE A 299 ? 0.5931 0.6289 0.4711 0.1536  -0.0062 0.1378  299 ILE A CG2 
2380  C CD1 . ILE A 299 ? 0.5919 0.7645 0.4508 0.0792  -0.0245 0.1234  299 ILE A CD1 
2381  N N   . GLY A 300 ? 0.5633 0.7245 0.4569 0.0837  -0.0166 0.1110  300 GLY A N   
2382  C CA  . GLY A 300 ? 0.5590 0.7906 0.4641 0.0953  -0.0170 0.1106  300 GLY A CA  
2383  C C   . GLY A 300 ? 0.5516 0.7719 0.4593 0.0667  -0.0173 0.1018  300 GLY A C   
2384  O O   . GLY A 300 ? 0.5558 0.7201 0.4496 0.0329  -0.0187 0.0953  300 GLY A O   
2385  N N   . GLU A 301 ? 0.5475 0.8197 0.4669 0.0854  -0.0157 0.1020  301 GLU A N   
2386  C CA  . GLU A 301 ? 0.5403 0.8105 0.4636 0.0618  -0.0156 0.0945  301 GLU A CA  
2387  C C   . GLU A 301 ? 0.5376 0.7139 0.4641 0.0798  -0.0094 0.0911  301 GLU A C   
2388  O O   . GLU A 301 ? 0.5449 0.7116 0.4735 0.1193  -0.0053 0.0937  301 GLU A O   
2389  C CB  . GLU A 301 ? 0.5377 0.9152 0.4716 0.0779  -0.0163 0.0973  301 GLU A CB  
2390  C CG  . GLU A 301 ? 0.5310 0.9278 0.4680 0.0447  -0.0174 0.0908  301 GLU A CG  
2391  C CD  . GLU A 301 ? 0.5417 0.9643 0.4603 -0.0239 -0.0256 0.0880  301 GLU A CD  
2392  O OE1 . GLU A 301 ? 0.5560 0.9836 0.4581 -0.0462 -0.0310 0.0904  301 GLU A OE1 
2393  O OE2 . GLU A 301 ? 0.5449 0.9757 0.4574 -0.0577 -0.0273 0.0834  301 GLU A OE2 
2394  N N   . CYS A 302 ? 0.5361 0.6425 0.4546 0.0515  -0.0091 0.0858  302 CYS A N   
2395  C CA  . CYS A 302 ? 0.5337 0.5619 0.4548 0.0634  -0.0038 0.0846  302 CYS A CA  
2396  C C   . CYS A 302 ? 0.5272 0.5249 0.4455 0.0379  -0.0031 0.0760  302 CYS A C   
2397  O O   . CYS A 302 ? 0.5348 0.5425 0.4369 0.0051  -0.0071 0.0708  302 CYS A O   
2398  C CB  . CYS A 302 ? 0.5401 0.5189 0.4528 0.0645  -0.0025 0.0894  302 CYS A CB  
2399  S SG  . CYS A 302 ? 0.5535 0.5486 0.4649 0.0969  -0.0023 0.1009  302 CYS A SG  
2400  N N   . PRO A 303 ? 0.5216 0.4759 0.4475 0.0508  0.0011  0.0748  303 PRO A N   
2401  C CA  . PRO A 303 ? 0.5172 0.4351 0.4385 0.0310  0.0026  0.0677  303 PRO A CA  
2402  C C   . PRO A 303 ? 0.5259 0.4004 0.4287 0.0210  0.0032  0.0683  303 PRO A C   
2403  O O   . PRO A 303 ? 0.5307 0.4025 0.4304 0.0300  0.0032  0.0748  303 PRO A O   
2404  C CB  . PRO A 303 ? 0.5136 0.4027 0.4462 0.0491  0.0064  0.0683  303 PRO A CB  
2405  C CG  . PRO A 303 ? 0.5277 0.4084 0.4583 0.0746  0.0069  0.0770  303 PRO A CG  
2406  C CD  . PRO A 303 ? 0.5306 0.4624 0.4598 0.0824  0.0040  0.0803  303 PRO A CD  
2407  N N   . LYS A 304 ? 0.5334 0.3746 0.4186 0.0073  0.0041  0.0620  304 LYS A N   
2408  C CA  . LYS A 304 ? 0.5539 0.3539 0.4088 0.0074  0.0052  0.0623  304 LYS A CA  
2409  C C   . LYS A 304 ? 0.5390 0.3282 0.4097 0.0274  0.0107  0.0694  304 LYS A C   
2410  O O   . LYS A 304 ? 0.5231 0.3145 0.4153 0.0306  0.0132  0.0699  304 LYS A O   
2411  C CB  . LYS A 304 ? 0.5853 0.3460 0.3994 -0.0092 0.0039  0.0536  304 LYS A CB  
2412  C CG  . LYS A 304 ? 0.6106 0.3818 0.3987 -0.0421 -0.0029 0.0481  304 LYS A CG  
2413  C CD  . LYS A 304 ? 0.6461 0.4083 0.3968 -0.0554 -0.0087 0.0496  304 LYS A CD  
2414  C CE  . LYS A 304 ? 0.6416 0.4700 0.4037 -0.0815 -0.0152 0.0511  304 LYS A CE  
2415  N NZ  . LYS A 304 ? 0.6998 0.5039 0.3998 -0.1176 -0.0240 0.0489  304 LYS A NZ  
2416  N N   . TYR A 305 ? 0.5481 0.3299 0.4047 0.0380  0.0119  0.0756  305 TYR A N   
2417  C CA  . TYR A 305 ? 0.5368 0.3260 0.4067 0.0516  0.0166  0.0852  305 TYR A CA  
2418  C C   . TYR A 305 ? 0.5472 0.3232 0.3967 0.0604  0.0204  0.0830  305 TYR A C   
2419  O O   . TYR A 305 ? 0.5798 0.3250 0.3856 0.0670  0.0199  0.0770  305 TYR A O   
2420  C CB  . TYR A 305 ? 0.5435 0.3435 0.4077 0.0620  0.0170  0.0948  305 TYR A CB  
2421  C CG  . TYR A 305 ? 0.5375 0.3587 0.4111 0.0707  0.0216  0.1071  305 TYR A CG  
2422  C CD1 . TYR A 305 ? 0.5261 0.3608 0.4246 0.0605  0.0218  0.1164  305 TYR A CD1 
2423  C CD2 . TYR A 305 ? 0.5532 0.3815 0.4019 0.0887  0.0252  0.1104  305 TYR A CD2 
2424  C CE1 . TYR A 305 ? 0.5266 0.3901 0.4297 0.0575  0.0248  0.1297  305 TYR A CE1 
2425  C CE2 . TYR A 305 ? 0.5468 0.4176 0.4061 0.0950  0.0295  0.1239  305 TYR A CE2 
2426  C CZ  . TYR A 305 ? 0.5312 0.4239 0.4203 0.0741  0.0289  0.1341  305 TYR A CZ  
2427  O OH  . TYR A 305 ? 0.5301 0.4737 0.4260 0.0696  0.0318  0.1496  305 TYR A OH  
2428  N N   . VAL A 306 ? 0.5285 0.3242 0.4008 0.0608  0.0236  0.0883  306 VAL A N   
2429  C CA  . VAL A 306 ? 0.5358 0.3400 0.3930 0.0747  0.0281  0.0897  306 VAL A CA  
2430  C C   . VAL A 306 ? 0.5204 0.3741 0.4011 0.0735  0.0309  0.1046  306 VAL A C   
2431  O O   . VAL A 306 ? 0.5095 0.3706 0.4138 0.0551  0.0285  0.1111  306 VAL A O   
2432  C CB  . VAL A 306 ? 0.5332 0.3205 0.3896 0.0684  0.0284  0.0798  306 VAL A CB  
2433  C CG1 . VAL A 306 ? 0.5632 0.3019 0.3794 0.0668  0.0257  0.0674  306 VAL A CG1 
2434  C CG2 . VAL A 306 ? 0.5079 0.3021 0.4014 0.0480  0.0260  0.0788  306 VAL A CG2 
2435  N N   . LYS A 307 ? 0.5289 0.4163 0.3947 0.0932  0.0355  0.1109  307 LYS A N   
2436  C CA  . LYS A 307 ? 0.5177 0.4725 0.4029 0.0868  0.0379  0.1275  307 LYS A CA  
2437  C C   . LYS A 307 ? 0.5037 0.4826 0.4097 0.0647  0.0373  0.1292  307 LYS A C   
2438  O O   . LYS A 307 ? 0.5007 0.5434 0.4176 0.0519  0.0383  0.1437  307 LYS A O   
2439  C CB  . LYS A 307 ? 0.5359 0.5380 0.3941 0.1233  0.0436  0.1358  307 LYS A CB  
2440  C CG  . LYS A 307 ? 0.5535 0.5476 0.3905 0.1426  0.0441  0.1395  307 LYS A CG  
2441  C CD  . LYS A 307 ? 0.5730 0.6326 0.3850 0.1815  0.0504  0.1517  307 LYS A CD  
2442  C CE  . LYS A 307 ? 0.6062 0.6374 0.3775 0.2131  0.0512  0.1508  307 LYS A CE  
2443  N NZ  . LYS A 307 ? 0.6323 0.7317 0.3722 0.2609  0.0581  0.1632  307 LYS A NZ  
2444  N N   . SER A 308 ? 0.4982 0.4322 0.4075 0.0570  0.0352  0.1154  308 SER A N   
2445  C CA  . SER A 308 ? 0.4891 0.4394 0.4131 0.0381  0.0343  0.1152  308 SER A CA  
2446  C C   . SER A 308 ? 0.4925 0.4396 0.4308 0.0004  0.0292  0.1236  308 SER A C   
2447  O O   . SER A 308 ? 0.5011 0.4098 0.4377 -0.0070 0.0260  0.1238  308 SER A O   
2448  C CB  . SER A 308 ? 0.4862 0.3865 0.4065 0.0413  0.0335  0.0982  308 SER A CB  
2449  O OG  . SER A 308 ? 0.5012 0.3724 0.3919 0.0680  0.0359  0.0893  308 SER A OG  
2450  N N   . ASN A 309 ? 0.4954 0.4793 0.4386 -0.0230 0.0278  0.1309  309 ASN A N   
2451  C CA  . ASN A 309 ? 0.5190 0.4755 0.4566 -0.0643 0.0212  0.1365  309 ASN A CA  
2452  C C   . ASN A 309 ? 0.5233 0.4189 0.4582 -0.0681 0.0182  0.1214  309 ASN A C   
2453  O O   . ASN A 309 ? 0.5562 0.3956 0.4726 -0.0895 0.0124  0.1212  309 ASN A O   
2454  C CB  . ASN A 309 ? 0.5309 0.5593 0.4666 -0.0981 0.0194  0.1533  309 ASN A CB  
2455  C CG  . ASN A 309 ? 0.5367 0.6279 0.4708 -0.1052 0.0207  0.1724  309 ASN A CG  
2456  O OD1 . ASN A 309 ? 0.5539 0.6053 0.4775 -0.1116 0.0185  0.1767  309 ASN A OD1 
2457  N ND2 . ASN A 309 ? 0.5246 0.7215 0.4673 -0.1013 0.0246  0.1850  309 ASN A ND2 
2458  N N   . ARG A 310 ? 0.4991 0.4005 0.4441 -0.0450 0.0220  0.1091  310 ARG A N   
2459  C CA  . ARG A 310 ? 0.5001 0.3598 0.4449 -0.0488 0.0199  0.0960  310 ARG A CA  
2460  C C   . ARG A 310 ? 0.4777 0.3269 0.4277 -0.0196 0.0243  0.0817  310 ARG A C   
2461  O O   . ARG A 310 ? 0.4685 0.3510 0.4156 -0.0016 0.0289  0.0818  310 ARG A O   
2462  C CB  . ARG A 310 ? 0.5092 0.4005 0.4524 -0.0752 0.0176  0.1011  310 ARG A CB  
2463  C CG  . ARG A 310 ? 0.5245 0.3639 0.4593 -0.0869 0.0134  0.0900  310 ARG A CG  
2464  C CD  . ARG A 310 ? 0.5352 0.4114 0.4661 -0.1160 0.0105  0.0953  310 ARG A CD  
2465  N NE  . ARG A 310 ? 0.5337 0.3772 0.4643 -0.1113 0.0097  0.0812  310 ARG A NE  
2466  C CZ  . ARG A 310 ? 0.5702 0.3441 0.4766 -0.1253 0.0037  0.0745  310 ARG A CZ  
2467  N NH1 . ARG A 310 ? 0.6213 0.3378 0.4927 -0.1447 -0.0025 0.0804  310 ARG A NH1 
2468  N NH2 . ARG A 310 ? 0.5643 0.3199 0.4732 -0.1166 0.0041  0.0621  310 ARG A NH2 
2469  N N   . LEU A 311 ? 0.4775 0.2808 0.4270 -0.0146 0.0225  0.0706  311 LEU A N   
2470  C CA  . LEU A 311 ? 0.4654 0.2560 0.4139 0.0003  0.0250  0.0578  311 LEU A CA  
2471  C C   . LEU A 311 ? 0.4670 0.2309 0.4194 -0.0053 0.0224  0.0484  311 LEU A C   
2472  O O   . LEU A 311 ? 0.4749 0.2187 0.4260 -0.0019 0.0200  0.0458  311 LEU A O   
2473  C CB  . LEU A 311 ? 0.4659 0.2451 0.4060 0.0123  0.0256  0.0549  311 LEU A CB  
2474  C CG  . LEU A 311 ? 0.4726 0.2661 0.3972 0.0257  0.0283  0.0611  311 LEU A CG  
2475  C CD1 . LEU A 311 ? 0.4813 0.2539 0.3923 0.0295  0.0267  0.0573  311 LEU A CD1 
2476  C CD2 . LEU A 311 ? 0.4821 0.2818 0.3854 0.0417  0.0325  0.0589  311 LEU A CD2 
2477  N N   . VAL A 312 ? 0.4624 0.2311 0.4168 -0.0094 0.0233  0.0438  312 VAL A N   
2478  C CA  . VAL A 312 ? 0.4666 0.2122 0.4217 -0.0123 0.0212  0.0349  312 VAL A CA  
2479  C C   . VAL A 312 ? 0.4528 0.2035 0.4090 -0.0053 0.0245  0.0255  312 VAL A C   
2480  O O   . VAL A 312 ? 0.4487 0.2160 0.4014 -0.0029 0.0274  0.0264  312 VAL A O   
2481  C CB  . VAL A 312 ? 0.4866 0.2228 0.4346 -0.0309 0.0173  0.0385  312 VAL A CB  
2482  C CG1 . VAL A 312 ? 0.5018 0.2038 0.4411 -0.0283 0.0148  0.0287  312 VAL A CG1 
2483  C CG2 . VAL A 312 ? 0.5148 0.2365 0.4480 -0.0454 0.0132  0.0499  312 VAL A CG2 
2484  N N   . LEU A 313 ? 0.4507 0.1913 0.4073 -0.0012 0.0241  0.0176  313 LEU A N   
2485  C CA  . LEU A 313 ? 0.4459 0.1863 0.3974 -0.0010 0.0264  0.0093  313 LEU A CA  
2486  C C   . LEU A 313 ? 0.4451 0.1816 0.4035 -0.0022 0.0255  0.0033  313 LEU A C   
2487  O O   . LEU A 313 ? 0.4540 0.1830 0.4143 0.0018  0.0228  0.0021  313 LEU A O   
2488  C CB  . LEU A 313 ? 0.4480 0.1933 0.3932 -0.0036 0.0257  0.0060  313 LEU A CB  
2489  C CG  . LEU A 313 ? 0.4606 0.1974 0.3839 -0.0071 0.0260  0.0088  313 LEU A CG  
2490  C CD1 . LEU A 313 ? 0.4659 0.2186 0.3843 -0.0183 0.0232  0.0077  313 LEU A CD1 
2491  C CD2 . LEU A 313 ? 0.4809 0.1912 0.3722 -0.0064 0.0288  0.0057  313 LEU A CD2 
2492  N N   . ALA A 314 ? 0.4421 0.1795 0.3966 -0.0035 0.0279  -0.0005 314 ALA A N   
2493  C CA  . ALA A 314 ? 0.4417 0.1758 0.4006 -0.0046 0.0274  -0.0074 314 ALA A CA  
2494  C C   . ALA A 314 ? 0.4404 0.1805 0.3988 -0.0029 0.0278  -0.0133 314 ALA A C   
2495  O O   . ALA A 314 ? 0.4429 0.1858 0.3896 -0.0091 0.0294  -0.0139 314 ALA A O   
2496  C CB  . ALA A 314 ? 0.4392 0.1783 0.3928 -0.0044 0.0303  -0.0093 314 ALA A CB  
2497  N N   . THR A 315 ? 0.4460 0.1880 0.4091 0.0047  0.0258  -0.0166 315 THR A N   
2498  C CA  . THR A 315 ? 0.4441 0.2117 0.4088 0.0087  0.0266  -0.0212 315 THR A CA  
2499  C C   . THR A 315 ? 0.4454 0.2080 0.4097 0.0111  0.0275  -0.0280 315 THR A C   
2500  O O   . THR A 315 ? 0.4392 0.2200 0.4028 0.0037  0.0298  -0.0313 315 THR A O   
2501  C CB  . THR A 315 ? 0.4554 0.2409 0.4196 0.0276  0.0246  -0.0193 315 THR A CB  
2502  O OG1 . THR A 315 ? 0.4814 0.2258 0.4318 0.0416  0.0216  -0.0188 315 THR A OG1 
2503  C CG2 . THR A 315 ? 0.4505 0.2575 0.4171 0.0229  0.0240  -0.0130 315 THR A CG2 
2504  N N   . GLY A 316 ? 0.4604 0.1947 0.4193 0.0174  0.0251  -0.0296 316 GLY A N   
2505  C CA  . GLY A 316 ? 0.4667 0.1917 0.4217 0.0192  0.0250  -0.0364 316 GLY A CA  
2506  C C   . GLY A 316 ? 0.4547 0.1779 0.4137 0.0048  0.0268  -0.0367 316 GLY A C   
2507  O O   . GLY A 316 ? 0.4440 0.1744 0.4045 -0.0016 0.0292  -0.0322 316 GLY A O   
2508  N N   . LEU A 317 ? 0.4635 0.1766 0.4181 0.0039  0.0256  -0.0418 317 LEU A N   
2509  C CA  . LEU A 317 ? 0.4543 0.1766 0.4114 -0.0042 0.0276  -0.0422 317 LEU A CA  
2510  C C   . LEU A 317 ? 0.4697 0.1862 0.4212 -0.0175 0.0229  -0.0385 317 LEU A C   
2511  O O   . LEU A 317 ? 0.4960 0.1856 0.4340 -0.0241 0.0174  -0.0365 317 LEU A O   
2512  C CB  . LEU A 317 ? 0.4510 0.1779 0.4073 0.0004  0.0300  -0.0501 317 LEU A CB  
2513  C CG  . LEU A 317 ? 0.4689 0.1816 0.4180 0.0089  0.0268  -0.0570 317 LEU A CG  
2514  C CD1 . LEU A 317 ? 0.4901 0.1808 0.4266 -0.0010 0.0216  -0.0589 317 LEU A CD1 
2515  C CD2 . LEU A 317 ? 0.4596 0.1920 0.4120 0.0162  0.0308  -0.0626 317 LEU A CD2 
2516  N N   . ARG A 318 ? 0.4618 0.2045 0.4167 -0.0225 0.0247  -0.0363 318 ARG A N   
2517  C CA  . ARG A 318 ? 0.4757 0.2361 0.4264 -0.0419 0.0200  -0.0303 318 ARG A CA  
2518  C C   . ARG A 318 ? 0.5111 0.2360 0.4428 -0.0573 0.0126  -0.0359 318 ARG A C   
2519  O O   . ARG A 318 ? 0.5125 0.2286 0.4417 -0.0501 0.0132  -0.0446 318 ARG A O   
2520  C CB  . ARG A 318 ? 0.4599 0.2695 0.4160 -0.0362 0.0242  -0.0273 318 ARG A CB  
2521  C CG  . ARG A 318 ? 0.4698 0.3249 0.4242 -0.0595 0.0192  -0.0189 318 ARG A CG  
2522  C CD  . ARG A 318 ? 0.4557 0.3710 0.4134 -0.0429 0.0245  -0.0158 318 ARG A CD  
2523  N NE  . ARG A 318 ? 0.4465 0.3912 0.4017 -0.0155 0.0314  -0.0082 318 ARG A NE  
2524  C CZ  . ARG A 318 ? 0.4461 0.4564 0.4029 -0.0161 0.0316  0.0047  318 ARG A CZ  
2525  N NH1 . ARG A 318 ? 0.4528 0.5136 0.4160 -0.0517 0.0245  0.0131  318 ARG A NH1 
2526  N NH2 . ARG A 318 ? 0.4468 0.4724 0.3916 0.0177  0.0384  0.0103  318 ARG A NH2 
2527  N N   . ASN A 319 ? 0.5505 0.2475 0.4599 -0.0792 0.0051  -0.0306 319 ASN A N   
2528  C CA  . ASN A 319 ? 0.6094 0.2463 0.4783 -0.0943 -0.0035 -0.0358 319 ASN A CA  
2529  C C   . ASN A 319 ? 0.6327 0.2909 0.4880 -0.1299 -0.0099 -0.0328 319 ASN A C   
2530  O O   . ASN A 319 ? 0.6205 0.3365 0.4878 -0.1531 -0.0107 -0.0215 319 ASN A O   
2531  C CB  . ASN A 319 ? 0.6590 0.2369 0.4919 -0.1019 -0.0095 -0.0311 319 ASN A CB  
2532  C CG  . ASN A 319 ? 0.7385 0.2261 0.5086 -0.1043 -0.0181 -0.0382 319 ASN A CG  
2533  O OD1 . ASN A 319 ? 0.7511 0.2227 0.5091 -0.0971 -0.0191 -0.0476 319 ASN A OD1 
2534  N ND2 . ASN A 319 ? 0.8020 0.2221 0.5227 -0.1114 -0.0244 -0.0336 319 ASN A ND2 
2535  N N   . SER A 320 ? 0.6708 0.2891 0.4986 -0.1338 -0.0146 -0.0422 320 SER A N   
2536  C CA  . SER A 320 ? 0.6922 0.3361 0.5071 -0.1679 -0.0210 -0.0410 320 SER A CA  
2537  C C   . SER A 320 ? 0.7726 0.3727 0.5303 -0.2211 -0.0346 -0.0336 320 SER A C   
2538  O O   . SER A 320 ? 0.8347 0.3463 0.5435 -0.2237 -0.0403 -0.0345 320 SER A O   
2539  C CB  . SER A 320 ? 0.7019 0.3165 0.5060 -0.1510 -0.0209 -0.0548 320 SER A CB  
2540  O OG  . SER A 320 ? 0.6387 0.2930 0.4883 -0.1107 -0.0092 -0.0599 320 SER A OG  
2541  N N   . PRO A 321 ? 0.7804 0.4442 0.5374 -0.2649 -0.0403 -0.0250 321 PRO A N   
2542  C CA  . PRO A 321 ? 0.8663 0.4934 0.5598 -0.3299 -0.0554 -0.0169 321 PRO A CA  
2543  C C   . PRO A 321 ? 0.9403 0.4932 0.5732 -0.3533 -0.0660 -0.0275 321 PRO A C   
2544  O O   . PRO A 321 ? 1.0090 0.4403 0.5839 -0.3369 -0.0703 -0.0384 321 PRO A O   
2545  C CB  . PRO A 321 ? 0.8251 0.5890 0.5567 -0.3626 -0.0549 -0.0006 321 PRO A CB  
2546  C CG  . PRO A 321 ? 0.7448 0.5905 0.5365 -0.3164 -0.0430 -0.0066 321 PRO A CG  
2547  C CD  . PRO A 321 ? 0.7103 0.4954 0.5232 -0.2554 -0.0325 -0.0197 321 PRO A CD  
2548  N N   . GLY B 1   ? 0.2086 0.3384 0.2793 0.0228  0.0184  -0.0673 1   GLY B N   
2549  C CA  . GLY B 1   ? 0.2129 0.2951 0.2721 0.0299  0.0134  -0.0472 1   GLY B CA  
2550  C C   . GLY B 1   ? 0.2307 0.2969 0.2649 0.0552  0.0035  -0.0414 1   GLY B C   
2551  O O   . GLY B 1   ? 0.2392 0.3247 0.2645 0.0716  -0.0001 -0.0493 1   GLY B O   
2552  N N   . LEU B 2   ? 0.2435 0.2700 0.2599 0.0577  0.0003  -0.0281 2   LEU B N   
2553  C CA  . LEU B 2   ? 0.2779 0.2709 0.2545 0.0790  -0.0062 -0.0225 2   LEU B CA  
2554  C C   . LEU B 2   ? 0.2935 0.2661 0.2532 0.0836  -0.0062 -0.0174 2   LEU B C   
2555  O O   . LEU B 2   ? 0.3287 0.2831 0.2510 0.1080  -0.0106 -0.0186 2   LEU B O   
2556  C CB  . LEU B 2   ? 0.2940 0.2426 0.2513 0.0705  -0.0063 -0.0100 2   LEU B CB  
2557  C CG  . LEU B 2   ? 0.2958 0.2507 0.2508 0.0763  -0.0089 -0.0140 2   LEU B CG  
2558  C CD1 . LEU B 2   ? 0.3146 0.2236 0.2483 0.0641  -0.0081 -0.0018 2   LEU B CD1 
2559  C CD2 . LEU B 2   ? 0.3228 0.2891 0.2496 0.1100  -0.0154 -0.0246 2   LEU B CD2 
2560  N N   . PHE B 3   ? 0.2730 0.2469 0.2553 0.0632  -0.0009 -0.0118 3   PHE B N   
2561  C CA  . PHE B 3   ? 0.2870 0.2414 0.2543 0.0632  0.0000  -0.0058 3   PHE B CA  
2562  C C   . PHE B 3   ? 0.2734 0.2623 0.2577 0.0699  0.0005  -0.0157 3   PHE B C   
2563  O O   . PHE B 3   ? 0.2851 0.2619 0.2568 0.0729  0.0008  -0.0122 3   PHE B O   
2564  C CB  . PHE B 3   ? 0.2797 0.2173 0.2542 0.0394  0.0046  0.0060  3   PHE B CB  
2565  C CG  . PHE B 3   ? 0.3025 0.2066 0.2517 0.0308  0.0044  0.0138  3   PHE B CG  
2566  C CD1 . PHE B 3   ? 0.3490 0.2059 0.2495 0.0302  0.0050  0.0191  3   PHE B CD1 
2567  C CD2 . PHE B 3   ? 0.2857 0.1998 0.2522 0.0232  0.0046  0.0144  3   PHE B CD2 
2568  C CE1 . PHE B 3   ? 0.3792 0.1997 0.2488 0.0182  0.0067  0.0241  3   PHE B CE1 
2569  C CE2 . PHE B 3   ? 0.3085 0.1937 0.2504 0.0145  0.0044  0.0199  3   PHE B CE2 
2570  C CZ  . PHE B 3   ? 0.3559 0.1943 0.2491 0.0105  0.0058  0.0241  3   PHE B CZ  
2571  N N   . GLY B 4   ? 0.2527 0.2851 0.2628 0.0691  0.0017  -0.0294 4   GLY B N   
2572  C CA  . GLY B 4   ? 0.2466 0.3204 0.2671 0.0760  0.0021  -0.0441 4   GLY B CA  
2573  C C   . GLY B 4   ? 0.2317 0.3101 0.2720 0.0589  0.0089  -0.0441 4   GLY B C   
2574  O O   . GLY B 4   ? 0.2294 0.3394 0.2756 0.0626  0.0097  -0.0563 4   GLY B O   
2575  N N   . ALA B 5   ? 0.2250 0.2761 0.2734 0.0426  0.0139  -0.0317 5   ALA B N   
2576  C CA  . ALA B 5   ? 0.2180 0.2677 0.2781 0.0320  0.0204  -0.0301 5   ALA B CA  
2577  C C   . ALA B 5   ? 0.2137 0.2699 0.2870 0.0157  0.0301  -0.0383 5   ALA B C   
2578  O O   . ALA B 5   ? 0.2159 0.2894 0.2934 0.0085  0.0359  -0.0513 5   ALA B O   
2579  C CB  . ALA B 5   ? 0.2199 0.2430 0.2749 0.0284  0.0205  -0.0136 5   ALA B CB  
2580  N N   . ILE B 6   ? 0.2149 0.2530 0.2888 0.0086  0.0331  -0.0312 6   ILE B N   
2581  C CA  . ILE B 6   ? 0.2251 0.2531 0.2984 -0.0064 0.0445  -0.0370 6   ILE B CA  
2582  C C   . ILE B 6   ? 0.2292 0.2868 0.3048 -0.0180 0.0482  -0.0566 6   ILE B C   
2583  O O   . ILE B 6   ? 0.2227 0.3020 0.3018 -0.0122 0.0415  -0.0603 6   ILE B O   
2584  C CB  . ILE B 6   ? 0.2282 0.2312 0.2972 -0.0069 0.0460  -0.0243 6   ILE B CB  
2585  C CG1 . ILE B 6   ? 0.2285 0.2165 0.2948 0.0023  0.0449  -0.0093 6   ILE B CG1 
2586  C CG2 . ILE B 6   ? 0.2490 0.2333 0.3066 -0.0216 0.0588  -0.0312 6   ILE B CG2 
2587  C CD1 . ILE B 6   ? 0.2305 0.2070 0.2932 0.0057  0.0444  0.0023  6   ILE B CD1 
2588  N N   . ALA B 7   ? 0.2456 0.3062 0.3160 -0.0355 0.0598  -0.0705 7   ALA B N   
2589  C CA  . ALA B 7   ? 0.2520 0.3546 0.3242 -0.0534 0.0654  -0.0942 7   ALA B CA  
2590  C C   . ALA B 7   ? 0.2341 0.3940 0.3190 -0.0344 0.0521  -0.1035 7   ALA B C   
2591  O O   . ALA B 7   ? 0.2313 0.4387 0.3208 -0.0368 0.0505  -0.1193 7   ALA B O   
2592  C CB  . ALA B 7   ? 0.2618 0.3586 0.3281 -0.0691 0.0719  -0.0979 7   ALA B CB  
2593  N N   . GLY B 8   ? 0.2274 0.3826 0.3131 -0.0132 0.0432  -0.0939 8   GLY B N   
2594  C CA  . GLY B 8   ? 0.2228 0.4159 0.3077 0.0128  0.0307  -0.0987 8   GLY B CA  
2595  C C   . GLY B 8   ? 0.2251 0.4363 0.3105 0.0173  0.0305  -0.1056 8   GLY B C   
2596  O O   . GLY B 8   ? 0.2284 0.4789 0.3198 0.0005  0.0379  -0.1260 8   GLY B O   
2597  N N   . PHE B 9   ? 0.2278 0.4107 0.3043 0.0365  0.0235  -0.0899 9   PHE B N   
2598  C CA  . PHE B 9   ? 0.2306 0.4245 0.3067 0.0408  0.0238  -0.0940 9   PHE B CA  
2599  C C   . PHE B 9   ? 0.2322 0.3952 0.3142 0.0188  0.0348  -0.0894 9   PHE B C   
2600  O O   . PHE B 9   ? 0.2362 0.4113 0.3196 0.0148  0.0385  -0.0973 9   PHE B O   
2601  C CB  . PHE B 9   ? 0.2406 0.4157 0.2972 0.0692  0.0136  -0.0809 9   PHE B CB  
2602  C CG  . PHE B 9   ? 0.2434 0.3625 0.2919 0.0658  0.0139  -0.0583 9   PHE B CG  
2603  C CD1 . PHE B 9   ? 0.2406 0.3451 0.2930 0.0585  0.0180  -0.0517 9   PHE B CD1 
2604  C CD2 . PHE B 9   ? 0.2514 0.3387 0.2863 0.0695  0.0104  -0.0455 9   PHE B CD2 
2605  C CE1 . PHE B 9   ? 0.2435 0.3123 0.2892 0.0543  0.0185  -0.0340 9   PHE B CE1 
2606  C CE2 . PHE B 9   ? 0.2561 0.3041 0.2829 0.0618  0.0116  -0.0282 9   PHE B CE2 
2607  C CZ  . PHE B 9   ? 0.2511 0.2947 0.2844 0.0540  0.0156  -0.0231 9   PHE B CZ  
2608  N N   . ILE B 10  ? 0.2350 0.3585 0.3163 0.0080  0.0400  -0.0772 10  ILE B N   
2609  C CA  . ILE B 10  ? 0.2482 0.3396 0.3250 -0.0083 0.0522  -0.0752 10  ILE B CA  
2610  C C   . ILE B 10  ? 0.2652 0.3534 0.3357 -0.0318 0.0640  -0.0882 10  ILE B C   
2611  O O   . ILE B 10  ? 0.2681 0.3341 0.3349 -0.0345 0.0655  -0.0802 10  ILE B O   
2612  C CB  . ILE B 10  ? 0.2473 0.2994 0.3202 0.0003  0.0508  -0.0532 10  ILE B CB  
2613  C CG1 . ILE B 10  ? 0.2367 0.2938 0.3114 0.0166  0.0408  -0.0420 10  ILE B CG1 
2614  C CG2 . ILE B 10  ? 0.2686 0.2876 0.3285 -0.0061 0.0628  -0.0513 10  ILE B CG2 
2615  C CD1 . ILE B 10  ? 0.2345 0.2709 0.3068 0.0210  0.0385  -0.0238 10  ILE B CD1 
2616  N N   . GLU B 11  ? 0.2809 0.3921 0.3471 -0.0517 0.0734  -0.1097 11  GLU B N   
2617  C CA  . GLU B 11  ? 0.3032 0.4219 0.3593 -0.0817 0.0864  -0.1279 11  GLU B CA  
2618  C C   . GLU B 11  ? 0.3340 0.3865 0.3653 -0.0951 0.0993  -0.1182 11  GLU B C   
2619  O O   . GLU B 11  ? 0.3450 0.3990 0.3698 -0.1122 0.1055  -0.1254 11  GLU B O   
2620  C CB  . GLU B 11  ? 0.3259 0.4700 0.3728 -0.1085 0.0986  -0.1532 11  GLU B CB  
2621  C CG  . GLU B 11  ? 0.3047 0.5372 0.3722 -0.1044 0.0898  -0.1741 11  GLU B CG  
2622  C CD  . GLU B 11  ? 0.3319 0.5963 0.3882 -0.1409 0.1052  -0.2037 11  GLU B CD  
2623  O OE1 . GLU B 11  ? 0.3530 0.5793 0.3940 -0.1489 0.1136  -0.2028 11  GLU B OE1 
2624  O OE2 . GLU B 11  ? 0.3357 0.6650 0.3960 -0.1634 0.1098  -0.2291 11  GLU B OE2 
2625  N N   . GLY B 12  ? 0.3528 0.3493 0.3663 -0.0852 0.1040  -0.1031 12  GLY B N   
2626  C CA  . GLY B 12  ? 0.3951 0.3228 0.3735 -0.0910 0.1176  -0.0944 12  GLY B CA  
2627  C C   . GLY B 12  ? 0.3998 0.2873 0.3688 -0.0614 0.1139  -0.0718 12  GLY B C   
2628  O O   . GLY B 12  ? 0.3758 0.2835 0.3621 -0.0433 0.1042  -0.0650 12  GLY B O   
2629  N N   . GLY B 13  ? 0.4338 0.2686 0.3728 -0.0557 0.1221  -0.0611 13  GLY B N   
2630  C CA  . GLY B 13  ? 0.4455 0.2497 0.3701 -0.0241 0.1197  -0.0417 13  GLY B CA  
2631  C C   . GLY B 13  ? 0.5008 0.2512 0.3811 -0.0187 0.1338  -0.0438 13  GLY B C   
2632  O O   . GLY B 13  ? 0.5343 0.2638 0.3922 -0.0446 0.1471  -0.0607 13  GLY B O   
2633  N N   . TRP B 14  ? 0.5149 0.2455 0.3791 0.0153  0.1315  -0.0280 14  TRP B N   
2634  C CA  . TRP B 14  ? 0.5700 0.2494 0.3882 0.0311  0.1431  -0.0275 14  TRP B CA  
2635  C C   . TRP B 14  ? 0.6422 0.2467 0.3965 0.0552  0.1559  -0.0175 14  TRP B C   
2636  O O   . TRP B 14  ? 0.6319 0.2534 0.3901 0.0902  0.1468  -0.0022 14  TRP B O   
2637  C CB  . TRP B 14  ? 0.5311 0.2594 0.3798 0.0582  0.1292  -0.0189 14  TRP B CB  
2638  C CG  . TRP B 14  ? 0.4783 0.2634 0.3734 0.0399  0.1195  -0.0281 14  TRP B CG  
2639  C CD1 . TRP B 14  ? 0.4775 0.2677 0.3780 0.0081  0.1249  -0.0458 14  TRP B CD1 
2640  C CD2 . TRP B 14  ? 0.4260 0.2713 0.3624 0.0533  0.1037  -0.0210 14  TRP B CD2 
2641  N NE1 . TRP B 14  ? 0.4280 0.2765 0.3699 0.0069  0.1122  -0.0489 14  TRP B NE1 
2642  C CE2 . TRP B 14  ? 0.3988 0.2750 0.3604 0.0328  0.1000  -0.0332 14  TRP B CE2 
2643  C CE3 . TRP B 14  ? 0.4043 0.2833 0.3552 0.0788  0.0935  -0.0071 14  TRP B CE3 
2644  C CZ2 . TRP B 14  ? 0.3563 0.2822 0.3510 0.0389  0.0871  -0.0297 14  TRP B CZ2 
2645  C CZ3 . TRP B 14  ? 0.3609 0.2927 0.3465 0.0779  0.0819  -0.0054 14  TRP B CZ3 
2646  C CH2 . TRP B 14  ? 0.3401 0.2882 0.3444 0.0590  0.0791  -0.0155 14  TRP B CH2 
2647  N N   . GLN B 15  ? 0.7221 0.2431 0.4116 0.0362  0.1781  -0.0275 15  GLN B N   
2648  C CA  . GLN B 15  ? 0.8172 0.2424 0.4228 0.0632  0.1947  -0.0188 15  GLN B CA  
2649  C C   . GLN B 15  ? 0.8375 0.2569 0.4218 0.1145  0.1904  -0.0071 15  GLN B C   
2650  O O   . GLN B 15  ? 0.8877 0.2685 0.4247 0.1580  0.1932  0.0061  15  GLN B O   
2651  C CB  . GLN B 15  ? 0.9137 0.2395 0.4420 0.0273  0.2228  -0.0345 15  GLN B CB  
2652  C CG  . GLN B 15  ? 0.9102 0.2388 0.4465 -0.0267 0.2316  -0.0497 15  GLN B CG  
2653  C CD  . GLN B 15  ? 0.9650 0.2314 0.4520 -0.0223 0.2423  -0.0413 15  GLN B CD  
2654  O OE1 . GLN B 15  ? 0.9179 0.2313 0.4465 -0.0420 0.2350  -0.0430 15  GLN B OE1 
2655  N NE2 . GLN B 15  ? 1.0715 0.2285 0.4641 0.0061  0.2600  -0.0322 15  GLN B NE2 
2656  N N   . GLY B 16  ? 0.8005 0.2627 0.4180 0.1117  0.1834  -0.0129 16  GLY B N   
2657  C CA  . GLY B 16  ? 0.8166 0.2832 0.4176 0.1570  0.1795  -0.0047 16  GLY B CA  
2658  C C   . GLY B 16  ? 0.7526 0.3080 0.4038 0.1949  0.1582  0.0094  16  GLY B C   
2659  O O   . GLY B 16  ? 0.7719 0.3379 0.4047 0.2368  0.1555  0.0157  16  GLY B O   
2660  N N   . MET B 17  ? 0.6803 0.3025 0.3917 0.1794  0.1440  0.0129  17  MET B N   
2661  C CA  . MET B 17  ? 0.6262 0.3328 0.3803 0.2068  0.1261  0.0240  17  MET B CA  
2662  C C   . MET B 17  ? 0.6498 0.3444 0.3804 0.2297  0.1264  0.0338  17  MET B C   
2663  O O   . MET B 17  ? 0.6203 0.3242 0.3756 0.2047  0.1232  0.0337  17  MET B O   
2664  C CB  . MET B 17  ? 0.5358 0.3238 0.3674 0.1741  0.1103  0.0210  17  MET B CB  
2665  C CG  . MET B 17  ? 0.4872 0.3616 0.3580 0.1924  0.0947  0.0291  17  MET B CG  
2666  S SD  . MET B 17  ? 0.4051 0.3495 0.3452 0.1535  0.0803  0.0254  17  MET B SD  
2667  C CE  . MET B 17  ? 0.3951 0.3097 0.3431 0.1237  0.0816  0.0227  17  MET B CE  
2668  N N   . VAL B 18  ? 0.7045 0.3826 0.3858 0.2811  0.1297  0.0417  18  VAL B N   
2669  C CA  . VAL B 18  ? 0.7460 0.4008 0.3884 0.3120  0.1323  0.0509  18  VAL B CA  
2670  C C   . VAL B 18  ? 0.6984 0.4583 0.3796 0.3425  0.1151  0.0580  18  VAL B C   
2671  O O   . VAL B 18  ? 0.7107 0.4750 0.3789 0.3597  0.1135  0.0643  18  VAL B O   
2672  C CB  . VAL B 18  ? 0.8652 0.4115 0.4033 0.3553  0.1512  0.0547  18  VAL B CB  
2673  C CG1 . VAL B 18  ? 0.9216 0.3632 0.4142 0.3181  0.1711  0.0447  18  VAL B CG1 
2674  C CG2 . VAL B 18  ? 0.8901 0.4705 0.4056 0.4128  0.1467  0.0585  18  VAL B CG2 
2675  N N   . ASP B 19  ? 0.6468 0.4940 0.3738 0.3459  0.1032  0.0554  19  ASP B N   
2676  C CA  . ASP B 19  ? 0.6094 0.5659 0.3680 0.3714  0.0892  0.0583  19  ASP B CA  
2677  C C   . ASP B 19  ? 0.5233 0.5591 0.3562 0.3254  0.0761  0.0558  19  ASP B C   
2678  O O   . ASP B 19  ? 0.4869 0.6209 0.3516 0.3317  0.0655  0.0547  19  ASP B O   
2679  C CB  . ASP B 19  ? 0.6143 0.6258 0.3705 0.4038  0.0857  0.0556  19  ASP B CB  
2680  C CG  . ASP B 19  ? 0.5764 0.5909 0.3678 0.3662  0.0850  0.0488  19  ASP B CG  
2681  O OD1 . ASP B 19  ? 0.5541 0.5230 0.3652 0.3200  0.0880  0.0457  19  ASP B OD1 
2682  O OD2 . ASP B 19  ? 0.5714 0.6382 0.3690 0.3854  0.0815  0.0459  19  ASP B OD2 
2683  N N   . GLY B 20  ? 0.4973 0.4913 0.3522 0.2792  0.0779  0.0535  20  GLY B N   
2684  C CA  . GLY B 20  ? 0.4300 0.4810 0.3420 0.2390  0.0671  0.0515  20  GLY B CA  
2685  C C   . GLY B 20  ? 0.4156 0.4128 0.3393 0.1994  0.0701  0.0489  20  GLY B C   
2686  O O   . GLY B 20  ? 0.4516 0.3748 0.3456 0.1945  0.0811  0.0461  20  GLY B O   
2687  N N   . TRP B 21  ? 0.3678 0.4045 0.3310 0.1701  0.0613  0.0482  21  TRP B N   
2688  C CA  . TRP B 21  ? 0.3506 0.3513 0.3276 0.1363  0.0620  0.0447  21  TRP B CA  
2689  C C   . TRP B 21  ? 0.3233 0.3271 0.3237 0.1107  0.0596  0.0379  21  TRP B C   
2690  O O   . TRP B 21  ? 0.3273 0.2920 0.3253 0.0931  0.0642  0.0317  21  TRP B O   
2691  C CB  . TRP B 21  ? 0.3219 0.3547 0.3212 0.1216  0.0542  0.0471  21  TRP B CB  
2692  C CG  . TRP B 21  ? 0.3487 0.3485 0.3248 0.1330  0.0588  0.0512  21  TRP B CG  
2693  C CD1 . TRP B 21  ? 0.3928 0.3218 0.3324 0.1388  0.0707  0.0508  21  TRP B CD1 
2694  C CD2 . TRP B 21  ? 0.3379 0.3713 0.3217 0.1359  0.0531  0.0553  21  TRP B CD2 
2695  N NE1 . TRP B 21  ? 0.4107 0.3250 0.3336 0.1478  0.0725  0.0557  21  TRP B NE1 
2696  C CE2 . TRP B 21  ? 0.3745 0.3550 0.3267 0.1480  0.0610  0.0587  21  TRP B CE2 
2697  C CE3 . TRP B 21  ? 0.3059 0.4077 0.3162 0.1265  0.0435  0.0553  21  TRP B CE3 
2698  C CZ2 . TRP B 21  ? 0.3750 0.3721 0.3252 0.1552  0.0579  0.0631  21  TRP B CZ2 
2699  C CZ3 . TRP B 21  ? 0.3062 0.4274 0.3153 0.1310  0.0407  0.0583  21  TRP B CZ3 
2700  C CH2 . TRP B 21  ? 0.3380 0.4086 0.3193 0.1474  0.0470  0.0627  21  TRP B CH2 
2701  N N   . TYR B 22  ? 0.2985 0.3532 0.3192 0.1081  0.0528  0.0380  22  TYR B N   
2702  C CA  . TYR B 22  ? 0.2783 0.3364 0.3156 0.0884  0.0504  0.0328  22  TYR B CA  
2703  C C   . TYR B 22  ? 0.2843 0.3692 0.3190 0.1032  0.0511  0.0325  22  TYR B C   
2704  O O   . TYR B 22  ? 0.2894 0.4163 0.3204 0.1222  0.0496  0.0357  22  TYR B O   
2705  C CB  . TYR B 22  ? 0.2482 0.3339 0.3066 0.0635  0.0423  0.0331  22  TYR B CB  
2706  C CG  . TYR B 22  ? 0.2425 0.3264 0.3030 0.0559  0.0396  0.0358  22  TYR B CG  
2707  C CD1 . TYR B 22  ? 0.2451 0.2899 0.3026 0.0496  0.0414  0.0334  22  TYR B CD1 
2708  C CD2 . TYR B 22  ? 0.2356 0.3631 0.3007 0.0530  0.0357  0.0391  22  TYR B CD2 
2709  C CE1 . TYR B 22  ? 0.2406 0.2843 0.2997 0.0436  0.0389  0.0359  22  TYR B CE1 
2710  C CE2 . TYR B 22  ? 0.2321 0.3580 0.2981 0.0454  0.0333  0.0410  22  TYR B CE2 
2711  C CZ  . TYR B 22  ? 0.2342 0.3155 0.2973 0.0422  0.0346  0.0403  22  TYR B CZ  
2712  O OH  . TYR B 22  ? 0.2312 0.3112 0.2948 0.0356  0.0323  0.0422  22  TYR B OH  
2713  N N   . GLY B 23  ? 0.2842 0.3523 0.3209 0.0956  0.0530  0.0273  23  GLY B N   
2714  C CA  . GLY B 23  ? 0.2895 0.3821 0.3243 0.1082  0.0537  0.0264  23  GLY B CA  
2715  C C   . GLY B 23  ? 0.2877 0.3599 0.3258 0.0969  0.0555  0.0198  23  GLY B C   
2716  O O   . GLY B 23  ? 0.2747 0.3297 0.3222 0.0769  0.0538  0.0155  23  GLY B O   
2717  N N   . TYR B 24  ? 0.3038 0.3820 0.3321 0.1131  0.0589  0.0183  24  TYR B N   
2718  C CA  . TYR B 24  ? 0.3013 0.3716 0.3337 0.1044  0.0600  0.0118  24  TYR B CA  
2719  C C   . TYR B 24  ? 0.3410 0.3657 0.3448 0.1190  0.0703  0.0063  24  TYR B C   
2720  O O   . TYR B 24  ? 0.3760 0.3820 0.3513 0.1445  0.0762  0.0096  24  TYR B O   
2721  C CB  . TYR B 24  ? 0.2856 0.4072 0.3306 0.1055  0.0553  0.0138  24  TYR B CB  
2722  C CG  . TYR B 24  ? 0.2642 0.4305 0.3245 0.0903  0.0488  0.0185  24  TYR B CG  
2723  C CD1 . TYR B 24  ? 0.2668 0.4710 0.3260 0.1016  0.0477  0.0224  24  TYR B CD1 
2724  C CD2 . TYR B 24  ? 0.2495 0.4182 0.3183 0.0647  0.0448  0.0181  24  TYR B CD2 
2725  C CE1 . TYR B 24  ? 0.2522 0.4999 0.3220 0.0811  0.0436  0.0239  24  TYR B CE1 
2726  C CE2 . TYR B 24  ? 0.2432 0.4405 0.3143 0.0456  0.0419  0.0213  24  TYR B CE2 
2727  C CZ  . TYR B 24  ? 0.2429 0.4820 0.3164 0.0504  0.0417  0.0233  24  TYR B CZ  
2728  O OH  . TYR B 24  ? 0.2411 0.5119 0.3141 0.0252  0.0405  0.0237  24  TYR B OH  
2729  N N   . HIS B 25  ? 0.3432 0.3482 0.3484 0.1036  0.0732  -0.0029 25  HIS B N   
2730  C CA  . HIS B 25  ? 0.3844 0.3495 0.3603 0.1114  0.0840  -0.0105 25  HIS B CA  
2731  C C   . HIS B 25  ? 0.3684 0.3593 0.3595 0.1062  0.0808  -0.0158 25  HIS B C   
2732  O O   . HIS B 25  ? 0.3415 0.3499 0.3547 0.0864  0.0756  -0.0212 25  HIS B O   
2733  C CB  . HIS B 25  ? 0.4134 0.3260 0.3682 0.0921  0.0945  -0.0212 25  HIS B CB  
2734  C CG  . HIS B 25  ? 0.4695 0.3290 0.3819 0.0952  0.1090  -0.0303 25  HIS B CG  
2735  N ND1 . HIS B 25  ? 0.4690 0.3304 0.3848 0.0775  0.1124  -0.0436 25  HIS B ND1 
2736  C CD2 . HIS B 25  ? 0.5339 0.3323 0.3924 0.1156  0.1219  -0.0282 25  HIS B CD2 
2737  C CE1 . HIS B 25  ? 0.5308 0.3332 0.3976 0.0817  0.1275  -0.0504 25  HIS B CE1 
2738  N NE2 . HIS B 25  ? 0.5752 0.3328 0.4027 0.1061  0.1340  -0.0406 25  HIS B NE2 
2739  N N   . HIS B 26  ? 0.3896 0.3836 0.3653 0.1279  0.0838  -0.0143 26  HIS B N   
2740  C CA  . HIS B 26  ? 0.3777 0.3963 0.3650 0.1258  0.0814  -0.0188 26  HIS B CA  
2741  C C   . HIS B 26  ? 0.4210 0.3913 0.3767 0.1271  0.0932  -0.0299 26  HIS B C   
2742  O O   . HIS B 26  ? 0.4715 0.3875 0.3862 0.1387  0.1043  -0.0312 26  HIS B O   
2743  C CB  . HIS B 26  ? 0.3679 0.4361 0.3624 0.1467  0.0761  -0.0107 26  HIS B CB  
2744  C CG  . HIS B 26  ? 0.4130 0.4632 0.3719 0.1816  0.0833  -0.0091 26  HIS B CG  
2745  N ND1 . HIS B 26  ? 0.4352 0.4829 0.3750 0.2058  0.0845  -0.0023 26  HIS B ND1 
2746  C CD2 . HIS B 26  ? 0.4463 0.4782 0.3795 0.2007  0.0897  -0.0137 26  HIS B CD2 
2747  C CE1 . HIS B 26  ? 0.4834 0.5101 0.3834 0.2421  0.0913  -0.0023 26  HIS B CE1 
2748  N NE2 . HIS B 26  ? 0.4918 0.5062 0.3865 0.2388  0.0949  -0.0092 26  HIS B NE2 
2749  N N   . SER B 27  ? 0.4088 0.3940 0.3773 0.1144  0.0919  -0.0385 27  SER B N   
2750  C CA  . SER B 27  ? 0.4509 0.3983 0.3892 0.1144  0.1031  -0.0503 27  SER B CA  
2751  C C   . SER B 27  ? 0.4284 0.4163 0.3864 0.1165  0.0973  -0.0527 27  SER B C   
2752  O O   . SER B 27  ? 0.3878 0.4157 0.3778 0.1021  0.0882  -0.0539 27  SER B O   
2753  C CB  . SER B 27  ? 0.4716 0.3838 0.3968 0.0842  0.1125  -0.0663 27  SER B CB  
2754  O OG  . SER B 27  ? 0.4283 0.3875 0.3902 0.0637  0.1038  -0.0738 27  SER B OG  
2755  N N   . ASN B 28  ? 0.4611 0.4351 0.3942 0.1379  0.1030  -0.0530 28  ASN B N   
2756  C CA  . ASN B 28  ? 0.4451 0.4551 0.3924 0.1424  0.0988  -0.0553 28  ASN B CA  
2757  C C   . ASN B 28  ? 0.5015 0.4668 0.4060 0.1577  0.1109  -0.0633 28  ASN B C   
2758  O O   . ASN B 28  ? 0.5580 0.4561 0.4176 0.1587  0.1239  -0.0688 28  ASN B O   
2759  C CB  . ASN B 28  ? 0.4097 0.4807 0.3829 0.1571  0.0880  -0.0420 28  ASN B CB  
2760  C CG  . ASN B 28  ? 0.4347 0.5071 0.3864 0.1891  0.0902  -0.0336 28  ASN B CG  
2761  O OD1 . ASN B 28  ? 0.4877 0.5066 0.3968 0.2089  0.1003  -0.0363 28  ASN B OD1 
2762  N ND2 . ASN B 28  ? 0.4038 0.5375 0.3789 0.1947  0.0817  -0.0245 28  ASN B ND2 
2763  N N   . GLU B 29  ? 0.4951 0.4903 0.4065 0.1684  0.1081  -0.0643 29  GLU B N   
2764  C CA  . GLU B 29  ? 0.5518 0.5029 0.4195 0.1841  0.1196  -0.0725 29  GLU B CA  
2765  C C   . GLU B 29  ? 0.6101 0.5160 0.4273 0.2220  0.1277  -0.0657 29  GLU B C   
2766  O O   . GLU B 29  ? 0.6820 0.5120 0.4405 0.2307  0.1425  -0.0734 29  GLU B O   
2767  C CB  . GLU B 29  ? 0.5301 0.5307 0.4177 0.1927  0.1136  -0.0732 29  GLU B CB  
2768  C CG  . GLU B 29  ? 0.4910 0.5244 0.4130 0.1626  0.1080  -0.0818 29  GLU B CG  
2769  C CD  . GLU B 29  ? 0.4862 0.5493 0.4134 0.1712  0.1061  -0.0852 29  GLU B CD  
2770  O OE1 . GLU B 29  ? 0.5027 0.5760 0.4162 0.1999  0.1068  -0.0793 29  GLU B OE1 
2771  O OE2 . GLU B 29  ? 0.4681 0.5489 0.4120 0.1513  0.1037  -0.0948 29  GLU B OE2 
2772  N N   . GLN B 30  ? 0.5856 0.5373 0.4197 0.2452  0.1187  -0.0522 30  GLN B N   
2773  C CA  . GLN B 30  ? 0.6386 0.5644 0.4260 0.2902  0.1239  -0.0452 30  GLN B CA  
2774  C C   . GLN B 30  ? 0.6885 0.5349 0.4317 0.2902  0.1343  -0.0443 30  GLN B C   
2775  O O   . GLN B 30  ? 0.7642 0.5489 0.4421 0.3270  0.1448  -0.0422 30  GLN B O   
2776  C CB  . GLN B 30  ? 0.5939 0.6124 0.4176 0.3114  0.1106  -0.0341 30  GLN B CB  
2777  C CG  . GLN B 30  ? 0.5619 0.6552 0.4140 0.3177  0.1034  -0.0352 30  GLN B CG  
2778  C CD  . GLN B 30  ? 0.4903 0.6717 0.4021 0.2913  0.0908  -0.0299 30  GLN B CD  
2779  O OE1 . GLN B 30  ? 0.4530 0.6372 0.3961 0.2530  0.0871  -0.0318 30  GLN B OE1 
2780  N NE2 . GLN B 30  ? 0.4782 0.7318 0.4001 0.3119  0.0851  -0.0246 30  GLN B NE2 
2781  N N   . GLY B 31  ? 0.6516 0.4974 0.4246 0.2517  0.1319  -0.0458 31  GLY B N   
2782  C CA  . GLY B 31  ? 0.6961 0.4697 0.4298 0.2451  0.1424  -0.0459 31  GLY B CA  
2783  C C   . GLY B 31  ? 0.6352 0.4459 0.4180 0.2152  0.1332  -0.0424 31  GLY B C   
2784  O O   . GLY B 31  ? 0.5661 0.4433 0.4070 0.1931  0.1209  -0.0425 31  GLY B O   
2785  N N   . SER B 32  ? 0.6681 0.4292 0.4203 0.2169  0.1400  -0.0391 32  SER B N   
2786  C CA  . SER B 32  ? 0.6182 0.4083 0.4100 0.1929  0.1322  -0.0353 32  SER B CA  
2787  C C   . SER B 32  ? 0.6447 0.4157 0.4100 0.2212  0.1332  -0.0237 32  SER B C   
2788  O O   . SER B 32  ? 0.7173 0.4303 0.4197 0.2564  0.1437  -0.0207 32  SER B O   
2789  C CB  . SER B 32  ? 0.6292 0.3777 0.4151 0.1487  0.1416  -0.0493 32  SER B CB  
2790  O OG  . SER B 32  ? 0.7193 0.3707 0.4311 0.1482  0.1621  -0.0569 32  SER B OG  
2791  N N   . GLY B 33  ? 0.5913 0.4080 0.3990 0.2087  0.1225  -0.0172 33  GLY B N   
2792  C CA  . GLY B 33  ? 0.6114 0.4189 0.3986 0.2339  0.1223  -0.0069 33  GLY B CA  
2793  C C   . GLY B 33  ? 0.5492 0.4113 0.3865 0.2155  0.1101  -0.0010 33  GLY B C   
2794  O O   . GLY B 33  ? 0.4866 0.4055 0.3767 0.1897  0.0994  -0.0024 33  GLY B O   
2795  N N   . TYR B 34  ? 0.5748 0.4130 0.3878 0.2312  0.1128  0.0057  34  TYR B N   
2796  C CA  . TYR B 34  ? 0.5259 0.4087 0.3779 0.2172  0.1026  0.0114  34  TYR B CA  
2797  C C   . TYR B 34  ? 0.5038 0.4623 0.3725 0.2469  0.0921  0.0199  34  TYR B C   
2798  O O   . TYR B 34  ? 0.5484 0.5028 0.3785 0.2903  0.0955  0.0236  34  TYR B O   
2799  C CB  . TYR B 34  ? 0.5675 0.3831 0.3834 0.2137  0.1122  0.0126  34  TYR B CB  
2800  C CG  . TYR B 34  ? 0.5940 0.3427 0.3903 0.1780  0.1248  0.0010  34  TYR B CG  
2801  C CD1 . TYR B 34  ? 0.5436 0.3181 0.3838 0.1373  0.1195  -0.0057 34  TYR B CD1 
2802  C CD2 . TYR B 34  ? 0.6765 0.3370 0.4045 0.1849  0.1432  -0.0048 34  TYR B CD2 
2803  C CE1 . TYR B 34  ? 0.5672 0.2977 0.3911 0.1035  0.1311  -0.0198 34  TYR B CE1 
2804  C CE2 . TYR B 34  ? 0.7050 0.3114 0.4126 0.1447  0.1568  -0.0189 34  TYR B CE2 
2805  C CZ  . TYR B 34  ? 0.6464 0.2961 0.4058 0.1037  0.1502  -0.0272 34  TYR B CZ  
2806  O OH  . TYR B 34  ? 0.6738 0.2873 0.4154 0.0628  0.1635  -0.0444 34  TYR B OH  
2807  N N   . ALA B 35  ? 0.4414 0.4694 0.3621 0.2233  0.0801  0.0215  35  ALA B N   
2808  C CA  . ALA B 35  ? 0.4192 0.5278 0.3582 0.2392  0.0712  0.0264  35  ALA B CA  
2809  C C   . ALA B 35  ? 0.3844 0.5122 0.3514 0.2120  0.0650  0.0291  35  ALA B C   
2810  O O   . ALA B 35  ? 0.3487 0.4781 0.3450 0.1752  0.0611  0.0268  35  ALA B O   
2811  C CB  . ALA B 35  ? 0.3860 0.5667 0.3544 0.2319  0.0648  0.0233  35  ALA B CB  
2812  N N   . ALA B 36  ? 0.4009 0.5400 0.3535 0.2337  0.0644  0.0338  36  ALA B N   
2813  C CA  . ALA B 36  ? 0.3716 0.5313 0.3477 0.2106  0.0587  0.0362  36  ALA B CA  
2814  C C   . ALA B 36  ? 0.3287 0.5760 0.3418 0.1885  0.0499  0.0340  36  ALA B C   
2815  O O   . ALA B 36  ? 0.3292 0.6433 0.3441 0.2058  0.0478  0.0317  36  ALA B O   
2816  C CB  . ALA B 36  ? 0.4047 0.5555 0.3517 0.2426  0.0609  0.0413  36  ALA B CB  
2817  N N   . ASP B 37  ? 0.2991 0.5439 0.3359 0.1495  0.0461  0.0335  37  ASP B N   
2818  C CA  . ASP B 37  ? 0.2724 0.5831 0.3317 0.1212  0.0407  0.0310  37  ASP B CA  
2819  C C   . ASP B 37  ? 0.2731 0.6315 0.3331 0.1278  0.0379  0.0318  37  ASP B C   
2820  O O   . ASP B 37  ? 0.2710 0.5965 0.3305 0.1193  0.0372  0.0348  37  ASP B O   
2821  C CB  . ASP B 37  ? 0.2550 0.5283 0.3253 0.0818  0.0392  0.0306  37  ASP B CB  
2822  C CG  . ASP B 37  ? 0.2440 0.5648 0.3223 0.0484  0.0373  0.0275  37  ASP B CG  
2823  O OD1 . ASP B 37  ? 0.2434 0.5843 0.3225 0.0383  0.0386  0.0246  37  ASP B OD1 
2824  O OD2 . ASP B 37  ? 0.2414 0.5756 0.3206 0.0297  0.0358  0.0275  37  ASP B OD2 
2825  N N   . LYS B 38  ? 0.2764 0.7193 0.3376 0.1442  0.0364  0.0277  38  LYS B N   
2826  C CA  . LYS B 38  ? 0.2800 0.7848 0.3404 0.1575  0.0335  0.0262  38  LYS B CA  
2827  C C   . LYS B 38  ? 0.2598 0.7849 0.3362 0.1116  0.0312  0.0232  38  LYS B C   
2828  O O   . LYS B 38  ? 0.2619 0.7813 0.3355 0.1164  0.0295  0.0257  38  LYS B O   
2829  C CB  . LYS B 38  ? 0.2867 0.8974 0.3464 0.1840  0.0319  0.0189  38  LYS B CB  
2830  C CG  . LYS B 38  ? 0.3241 0.9202 0.3530 0.2481  0.0337  0.0226  38  LYS B CG  
2831  C CD  . LYS B 38  ? 0.3336 1.0504 0.3592 0.2835  0.0305  0.0143  38  LYS B CD  
2832  C CE  . LYS B 38  ? 0.3229 1.0964 0.3610 0.2743  0.0310  0.0065  38  LYS B CE  
2833  N NZ  . LYS B 38  ? 0.3235 1.2408 0.3666 0.2963  0.0275  -0.0057 38  LYS B NZ  
2834  N N   . GLU B 39  ? 0.2477 0.7902 0.3343 0.0675  0.0323  0.0180  39  GLU B N   
2835  C CA  . GLU B 39  ? 0.2427 0.7976 0.3323 0.0202  0.0328  0.0138  39  GLU B CA  
2836  C C   . GLU B 39  ? 0.2407 0.7103 0.3257 0.0106  0.0316  0.0209  39  GLU B C   
2837  O O   . GLU B 39  ? 0.2407 0.7247 0.3256 0.0019  0.0302  0.0200  39  GLU B O   
2838  C CB  . GLU B 39  ? 0.2479 0.8112 0.3335 -0.0250 0.0372  0.0079  39  GLU B CB  
2839  C CG  . GLU B 39  ? 0.2611 0.7781 0.3318 -0.0735 0.0403  0.0071  39  GLU B CG  
2840  C CD  . GLU B 39  ? 0.2824 0.8282 0.3362 -0.1230 0.0479  -0.0018 39  GLU B CD  
2841  O OE1 . GLU B 39  ? 0.2843 0.8457 0.3381 -0.1224 0.0504  -0.0036 39  GLU B OE1 
2842  O OE2 . GLU B 39  ? 0.3034 0.8532 0.3393 -0.1649 0.0527  -0.0077 39  GLU B OE2 
2843  N N   . SER B 40  ? 0.2393 0.6282 0.3204 0.0118  0.0322  0.0264  40  SER B N   
2844  C CA  . SER B 40  ? 0.2382 0.5556 0.3151 0.0039  0.0310  0.0310  40  SER B CA  
2845  C C   . SER B 40  ? 0.2386 0.5443 0.3158 0.0340  0.0298  0.0352  40  SER B C   
2846  O O   . SER B 40  ? 0.2377 0.5215 0.3136 0.0244  0.0283  0.0369  40  SER B O   
2847  C CB  . SER B 40  ? 0.2387 0.4887 0.3119 0.0025  0.0318  0.0330  40  SER B CB  
2848  O OG  . SER B 40  ? 0.2398 0.4784 0.3150 0.0322  0.0334  0.0341  40  SER B OG  
2849  N N   . THR B 41  ? 0.2469 0.5621 0.3189 0.0713  0.0314  0.0370  41  THR B N   
2850  C CA  . THR B 41  ? 0.2623 0.5561 0.3210 0.1035  0.0326  0.0417  41  THR B CA  
2851  C C   . THR B 41  ? 0.2603 0.6157 0.3213 0.1075  0.0293  0.0406  41  THR B C   
2852  O O   . THR B 41  ? 0.2638 0.5926 0.3200 0.1097  0.0288  0.0440  41  THR B O   
2853  C CB  . THR B 41  ? 0.2893 0.5719 0.3271 0.1460  0.0370  0.0437  41  THR B CB  
2854  O OG1 . THR B 41  ? 0.2920 0.5189 0.3272 0.1389  0.0409  0.0430  41  THR B OG1 
2855  C CG2 . THR B 41  ? 0.3225 0.5647 0.3314 0.1800  0.0410  0.0493  41  THR B CG2 
2856  N N   . GLN B 42  ? 0.2549 0.6991 0.3231 0.1074  0.0272  0.0342  42  GLN B N   
2857  C CA  . GLN B 42  ? 0.2534 0.7755 0.3247 0.1109  0.0241  0.0298  42  GLN B CA  
2858  C C   . GLN B 42  ? 0.2399 0.7522 0.3201 0.0659  0.0229  0.0274  42  GLN B C   
2859  O O   . GLN B 42  ? 0.2414 0.7725 0.3202 0.0712  0.0208  0.0275  42  GLN B O   
2860  C CB  . GLN B 42  ? 0.2503 0.8840 0.3292 0.1121  0.0230  0.0193  42  GLN B CB  
2861  C CG  . GLN B 42  ? 0.2515 0.9858 0.3330 0.1214  0.0196  0.0115  42  GLN B CG  
2862  C CD  . GLN B 42  ? 0.2747 0.9948 0.3354 0.1804  0.0177  0.0192  42  GLN B CD  
2863  O OE1 . GLN B 42  ? 0.2754 0.9929 0.3341 0.1798  0.0158  0.0208  42  GLN B OE1 
2864  N NE2 . GLN B 42  ? 0.3011 1.0034 0.3394 0.2326  0.0192  0.0241  42  GLN B NE2 
2865  N N   . LYS B 43  ? 0.2327 0.7113 0.3163 0.0243  0.0247  0.0254  43  LYS B N   
2866  C CA  . LYS B 43  ? 0.2323 0.6806 0.3125 -0.0167 0.0251  0.0238  43  LYS B CA  
2867  C C   . LYS B 43  ? 0.2303 0.6071 0.3076 -0.0033 0.0232  0.0317  43  LYS B C   
2868  O O   . LYS B 43  ? 0.2313 0.6079 0.3063 -0.0182 0.0220  0.0307  43  LYS B O   
2869  C CB  . LYS B 43  ? 0.2400 0.6451 0.3110 -0.0524 0.0285  0.0222  43  LYS B CB  
2870  C CG  . LYS B 43  ? 0.2585 0.6754 0.3130 -0.1029 0.0326  0.0144  43  LYS B CG  
2871  C CD  . LYS B 43  ? 0.2739 0.7066 0.3164 -0.1313 0.0384  0.0085  43  LYS B CD  
2872  C CE  . LYS B 43  ? 0.3115 0.7019 0.3179 -0.1839 0.0458  0.0036  43  LYS B CE  
2873  N NZ  . LYS B 43  ? 0.3328 0.6932 0.3188 -0.2017 0.0517  0.0030  43  LYS B NZ  
2874  N N   . ALA B 44  ? 0.2299 0.5485 0.3052 0.0218  0.0241  0.0380  44  ALA B N   
2875  C CA  . ALA B 44  ? 0.2316 0.4876 0.3024 0.0330  0.0242  0.0435  44  ALA B CA  
2876  C C   . ALA B 44  ? 0.2402 0.5186 0.3048 0.0611  0.0239  0.0466  44  ALA B C   
2877  O O   . ALA B 44  ? 0.2406 0.4959 0.3031 0.0569  0.0230  0.0487  44  ALA B O   
2878  C CB  . ALA B 44  ? 0.2369 0.4343 0.3029 0.0475  0.0276  0.0460  44  ALA B CB  
2879  N N   . ILE B 45  ? 0.2512 0.5742 0.3089 0.0934  0.0246  0.0468  45  ILE B N   
2880  C CA  . ILE B 45  ? 0.2691 0.6162 0.3121 0.1289  0.0243  0.0499  45  ILE B CA  
2881  C C   . ILE B 45  ? 0.2552 0.6668 0.3100 0.1103  0.0196  0.0449  45  ILE B C   
2882  O O   . ILE B 45  ? 0.2633 0.6635 0.3098 0.1226  0.0189  0.0484  45  ILE B O   
2883  C CB  . ILE B 45  ? 0.2922 0.6808 0.3183 0.1740  0.0256  0.0501  45  ILE B CB  
2884  C CG1 . ILE B 45  ? 0.3239 0.6250 0.3221 0.2001  0.0329  0.0567  45  ILE B CG1 
2885  C CG2 . ILE B 45  ? 0.3110 0.7571 0.3219 0.2113  0.0231  0.0505  45  ILE B CG2 
2886  C CD1 . ILE B 45  ? 0.3503 0.6762 0.3282 0.2401  0.0351  0.0563  45  ILE B CD1 
2887  N N   . ASP B 46  ? 0.2388 0.7156 0.3090 0.0776  0.0177  0.0356  46  ASP B N   
2888  C CA  . ASP B 46  ? 0.2314 0.7709 0.3088 0.0502  0.0153  0.0276  46  ASP B CA  
2889  C C   . ASP B 46  ? 0.2276 0.7007 0.3037 0.0213  0.0152  0.0305  46  ASP B C   
2890  O O   . ASP B 46  ? 0.2289 0.7200 0.3038 0.0225  0.0132  0.0298  46  ASP B O   
2891  C CB  . ASP B 46  ? 0.2258 0.8368 0.3112 0.0109  0.0168  0.0151  46  ASP B CB  
2892  C CG  . ASP B 46  ? 0.2278 0.9285 0.3166 0.0396  0.0162  0.0092  46  ASP B CG  
2893  O OD1 . ASP B 46  ? 0.2383 0.9532 0.3190 0.0944  0.0138  0.0145  46  ASP B OD1 
2894  O OD2 . ASP B 46  ? 0.2250 0.9796 0.3192 0.0085  0.0188  -0.0009 46  ASP B OD2 
2895  N N   . GLY B 47  ? 0.2253 0.6245 0.2995 -0.0007 0.0171  0.0333  47  GLY B N   
2896  C CA  . GLY B 47  ? 0.2264 0.5629 0.2952 -0.0240 0.0168  0.0352  47  GLY B CA  
2897  C C   . GLY B 47  ? 0.2266 0.5247 0.2939 0.0017  0.0156  0.0423  47  GLY B C   
2898  O O   . GLY B 47  ? 0.2278 0.5191 0.2927 -0.0104 0.0140  0.0416  47  GLY B O   
2899  N N   . VAL B 48  ? 0.2320 0.5007 0.2954 0.0352  0.0178  0.0485  48  VAL B N   
2900  C CA  . VAL B 48  ? 0.2427 0.4654 0.2957 0.0574  0.0199  0.0548  48  VAL B CA  
2901  C C   . VAL B 48  ? 0.2538 0.5222 0.2987 0.0821  0.0185  0.0566  48  VAL B C   
2902  O O   . VAL B 48  ? 0.2600 0.5040 0.2982 0.0860  0.0188  0.0598  48  VAL B O   
2903  C CB  . VAL B 48  ? 0.2589 0.4277 0.2987 0.0799  0.0260  0.0589  48  VAL B CB  
2904  C CG1 . VAL B 48  ? 0.2853 0.4077 0.3020 0.1029  0.0316  0.0647  48  VAL B CG1 
2905  C CG2 . VAL B 48  ? 0.2471 0.3716 0.2956 0.0558  0.0268  0.0558  48  VAL B CG2 
2906  N N   . THR B 49  ? 0.2581 0.5977 0.3023 0.1009  0.0169  0.0537  49  THR B N   
2907  C CA  . THR B 49  ? 0.2704 0.6693 0.3056 0.1291  0.0145  0.0535  49  THR B CA  
2908  C C   . THR B 49  ? 0.2548 0.6908 0.3037 0.0965  0.0104  0.0473  49  THR B C   
2909  O O   . THR B 49  ? 0.2631 0.6903 0.3036 0.1095  0.0096  0.0509  49  THR B O   
2910  C CB  . THR B 49  ? 0.2761 0.7645 0.3100 0.1548  0.0125  0.0480  49  THR B CB  
2911  O OG1 . THR B 49  ? 0.2998 0.7450 0.3129 0.1907  0.0170  0.0544  49  THR B OG1 
2912  C CG2 . THR B 49  ? 0.2895 0.8545 0.3133 0.1876  0.0088  0.0456  49  THR B CG2 
2913  N N   . ASN B 50  ? 0.2392 0.7103 0.3034 0.0527  0.0092  0.0379  50  ASN B N   
2914  C CA  . ASN B 50  ? 0.2342 0.7323 0.3030 0.0144  0.0075  0.0300  50  ASN B CA  
2915  C C   . ASN B 50  ? 0.2355 0.6531 0.2994 0.0063  0.0075  0.0365  50  ASN B C   
2916  O O   . ASN B 50  ? 0.2371 0.6717 0.2994 0.0008  0.0056  0.0345  50  ASN B O   
2917  C CB  . ASN B 50  ? 0.2328 0.7467 0.3035 -0.0358 0.0101  0.0198  50  ASN B CB  
2918  C CG  . ASN B 50  ? 0.2319 0.8471 0.3088 -0.0385 0.0108  0.0092  50  ASN B CG  
2919  O OD1 . ASN B 50  ? 0.2317 0.9386 0.3129 -0.0236 0.0083  0.0021  50  ASN B OD1 
2920  N ND2 . ASN B 50  ? 0.2327 0.8378 0.3091 -0.0563 0.0141  0.0069  50  ASN B ND2 
2921  N N   . LYS B 51  ? 0.2358 0.5727 0.2973 0.0058  0.0096  0.0427  51  LYS B N   
2922  C CA  . LYS B 51  ? 0.2372 0.5027 0.2945 0.0005  0.0099  0.0472  51  LYS B CA  
2923  C C   . LYS B 51  ? 0.2459 0.5017 0.2965 0.0303  0.0103  0.0536  51  LYS B C   
2924  O O   . LYS B 51  ? 0.2458 0.4863 0.2947 0.0211  0.0090  0.0537  51  LYS B O   
2925  C CB  . LYS B 51  ? 0.2360 0.4371 0.2926 0.0016  0.0124  0.0504  51  LYS B CB  
2926  C CG  . LYS B 51  ? 0.2370 0.3759 0.2900 0.0012  0.0133  0.0530  51  LYS B CG  
2927  C CD  . LYS B 51  ? 0.2359 0.3311 0.2895 0.0019  0.0159  0.0528  51  LYS B CD  
2928  C CE  . LYS B 51  ? 0.2348 0.2940 0.2855 -0.0166 0.0136  0.0488  51  LYS B CE  
2929  N NZ  . LYS B 51  ? 0.2344 0.2726 0.2847 -0.0195 0.0142  0.0462  51  LYS B NZ  
2930  N N   . VAL B 52  ? 0.2613 0.5185 0.3015 0.0671  0.0133  0.0592  52  VAL B N   
2931  C CA  . VAL B 52  ? 0.2846 0.5206 0.3051 0.0989  0.0161  0.0663  52  VAL B CA  
2932  C C   . VAL B 52  ? 0.2852 0.5895 0.3070 0.1053  0.0112  0.0634  52  VAL B C   
2933  O O   . VAL B 52  ? 0.2921 0.5765 0.3063 0.1090  0.0114  0.0666  52  VAL B O   
2934  C CB  . VAL B 52  ? 0.3163 0.5297 0.3105 0.1400  0.0223  0.0727  52  VAL B CB  
2935  C CG1 . VAL B 52  ? 0.3550 0.5465 0.3146 0.1779  0.0266  0.0804  52  VAL B CG1 
2936  C CG2 . VAL B 52  ? 0.3211 0.4604 0.3107 0.1295  0.0288  0.0741  52  VAL B CG2 
2937  N N   . ASN B 53  ? 0.2793 0.6699 0.3108 0.1045  0.0072  0.0559  53  ASN B N   
2938  C CA  . ASN B 53  ? 0.2793 0.7542 0.3142 0.1064  0.0025  0.0491  53  ASN B CA  
2939  C C   . ASN B 53  ? 0.2656 0.7364 0.3126 0.0599  0.0005  0.0426  53  ASN B C   
2940  O O   . ASN B 53  ? 0.2687 0.7617 0.3126 0.0636  -0.0016 0.0416  53  ASN B O   
2941  C CB  . ASN B 53  ? 0.2747 0.8558 0.3184 0.1091  -0.0002 0.0384  53  ASN B CB  
2942  C CG  . ASN B 53  ? 0.2961 0.8874 0.3224 0.1617  0.0012  0.0441  53  ASN B CG  
2943  O OD1 . ASN B 53  ? 0.3253 0.8519 0.3240 0.2027  0.0048  0.0560  53  ASN B OD1 
2944  N ND2 . ASN B 53  ? 0.2889 0.9577 0.3255 0.1599  -0.0002 0.0350  53  ASN B ND2 
2945  N N   . SER B 54  ? 0.2576 0.6952 0.3124 0.0188  0.0018  0.0383  54  SER B N   
2946  C CA  . SER B 54  ? 0.2580 0.6697 0.3118 -0.0227 0.0015  0.0329  54  SER B CA  
2947  C C   . SER B 54  ? 0.2622 0.6100 0.3107 -0.0102 0.0012  0.0410  54  SER B C   
2948  O O   . SER B 54  ? 0.2646 0.6225 0.3104 -0.0227 -0.0005 0.0377  54  SER B O   
2949  C CB  . SER B 54  ? 0.2599 0.6239 0.3096 -0.0576 0.0042  0.0297  54  SER B CB  
2950  O OG  . SER B 54  ? 0.2651 0.6894 0.3135 -0.0863 0.0062  0.0186  54  SER B OG  
2951  N N   . ILE B 55  ? 0.2671 0.5517 0.3126 0.0112  0.0038  0.0501  55  ILE B N   
2952  C CA  . ILE B 55  ? 0.2746 0.5003 0.3135 0.0213  0.0055  0.0565  55  ILE B CA  
2953  C C   . ILE B 55  ? 0.2890 0.5418 0.3186 0.0472  0.0051  0.0603  55  ILE B C   
2954  O O   . ILE B 55  ? 0.2897 0.5297 0.3177 0.0393  0.0038  0.0602  55  ILE B O   
2955  C CB  . ILE B 55  ? 0.2808 0.4449 0.3140 0.0361  0.0109  0.0624  55  ILE B CB  
2956  C CG1 . ILE B 55  ? 0.2701 0.3978 0.3108 0.0100  0.0103  0.0580  55  ILE B CG1 
2957  C CG2 . ILE B 55  ? 0.2964 0.4149 0.3153 0.0519  0.0158  0.0683  55  ILE B CG2 
2958  C CD1 . ILE B 55  ? 0.2731 0.3602 0.3121 0.0189  0.0152  0.0599  55  ILE B CD1 
2959  N N   . ILE B 56  ? 0.3065 0.5966 0.3263 0.0815  0.0060  0.0637  56  ILE B N   
2960  C CA  . ILE B 56  ? 0.3287 0.6452 0.3313 0.1150  0.0057  0.0680  56  ILE B CA  
2961  C C   . ILE B 56  ? 0.3183 0.7052 0.3339 0.0955  -0.0005 0.0590  56  ILE B C   
2962  O O   . ILE B 56  ? 0.3249 0.7008 0.3336 0.0996  -0.0011 0.0614  56  ILE B O   
2963  C CB  . ILE B 56  ? 0.3537 0.7058 0.3363 0.1615  0.0071  0.0717  56  ILE B CB  
2964  C CG1 . ILE B 56  ? 0.3821 0.6475 0.3384 0.1833  0.0161  0.0814  56  ILE B CG1 
2965  C CG2 . ILE B 56  ? 0.3778 0.7754 0.3393 0.2004  0.0052  0.0742  56  ILE B CG2 
2966  C CD1 . ILE B 56  ? 0.4079 0.6975 0.3432 0.2239  0.0179  0.0837  56  ILE B CD1 
2967  N N   . ASP B 57  ? 0.3079 0.7661 0.3393 0.0707  -0.0040 0.0474  57  ASP B N   
2968  C CA  . ASP B 57  ? 0.3047 0.8396 0.3441 0.0454  -0.0080 0.0350  57  ASP B CA  
2969  C C   . ASP B 57  ? 0.3041 0.7902 0.3439 0.0096  -0.0080 0.0329  57  ASP B C   
2970  O O   . ASP B 57  ? 0.3077 0.8298 0.3457 0.0056  -0.0104 0.0282  57  ASP B O   
2971  C CB  . ASP B 57  ? 0.2973 0.9075 0.3476 0.0138  -0.0083 0.0206  57  ASP B CB  
2972  C CG  . ASP B 57  ? 0.3025 1.0112 0.3536 0.0506  -0.0106 0.0166  57  ASP B CG  
2973  O OD1 . ASP B 57  ? 0.3113 1.0847 0.3568 0.0806  -0.0141 0.0146  57  ASP B OD1 
2974  O OD2 . ASP B 57  ? 0.3001 1.0251 0.3553 0.0525  -0.0092 0.0149  57  ASP B OD2 
2975  N N   . LYS B 58  ? 0.3051 0.7120 0.3444 -0.0131 -0.0055 0.0355  58  LYS B N   
2976  C CA  . LYS B 58  ? 0.3112 0.6661 0.3446 -0.0400 -0.0056 0.0337  58  LYS B CA  
2977  C C   . LYS B 58  ? 0.3180 0.6420 0.3477 -0.0149 -0.0062 0.0421  58  LYS B C   
2978  O O   . LYS B 58  ? 0.3217 0.6416 0.3473 -0.0300 -0.0078 0.0384  58  LYS B O   
2979  C CB  . LYS B 58  ? 0.3124 0.5935 0.3409 -0.0605 -0.0033 0.0344  58  LYS B CB  
2980  C CG  . LYS B 58  ? 0.3287 0.6066 0.3420 -0.1054 -0.0016 0.0232  58  LYS B CG  
2981  C CD  . LYS B 58  ? 0.3329 0.6985 0.3474 -0.1265 -0.0004 0.0116  58  LYS B CD  
2982  C CE  . LYS B 58  ? 0.3631 0.7126 0.3506 -0.1788 0.0050  -0.0007 58  LYS B CE  
2983  N NZ  . LYS B 58  ? 0.3695 0.8170 0.3580 -0.2060 0.0079  -0.0155 58  LYS B NZ  
2984  N N   . MET B 59  ? 0.3283 0.6274 0.3538 0.0216  -0.0035 0.0527  59  MET B N   
2985  C CA  . MET B 59  ? 0.3432 0.6072 0.3571 0.0445  -0.0013 0.0609  59  MET B CA  
2986  C C   . MET B 59  ? 0.3596 0.6835 0.3639 0.0727  -0.0034 0.0622  59  MET B C   
2987  O O   . MET B 59  ? 0.3694 0.6769 0.3631 0.0839  -0.0026 0.0664  59  MET B O   
2988  C CB  . MET B 59  ? 0.3571 0.5567 0.3584 0.0660  0.0058  0.0703  59  MET B CB  
2989  C CG  . MET B 59  ? 0.3449 0.4975 0.3564 0.0426  0.0074  0.0675  59  MET B CG  
2990  S SD  . MET B 59  ? 0.3364 0.4567 0.3544 0.0129  0.0045  0.0617  59  MET B SD  
2991  C CE  . MET B 59  ? 0.3497 0.4211 0.3543 0.0276  0.0117  0.0676  59  MET B CE  
2992  N N   . ASN B 60  ? 0.3654 0.7639 0.3722 0.0857  -0.0061 0.0577  60  ASN B N   
2993  C CA  . ASN B 60  ? 0.3836 0.8566 0.3795 0.1198  -0.0091 0.0569  60  ASN B CA  
2994  C C   . ASN B 60  ? 0.3836 0.8830 0.3816 0.1073  -0.0126 0.0521  60  ASN B C   
2995  O O   . ASN B 60  ? 0.4030 0.9091 0.3820 0.1432  -0.0126 0.0585  60  ASN B O   
2996  C CB  . ASN B 60  ? 0.3779 0.9526 0.3841 0.1223  -0.0130 0.0460  60  ASN B CB  
2997  C CG  . ASN B 60  ? 0.3829 1.0667 0.3893 0.1348  -0.0185 0.0360  60  ASN B CG  
2998  O OD1 . ASN B 60  ? 0.3721 1.0852 0.3893 0.0990  -0.0208 0.0259  60  ASN B OD1 
2999  N ND2 . ASN B 60  ? 0.4033 1.1504 0.3939 0.1873  -0.0204 0.0375  60  ASN B ND2 
3000  N N   . THR B 61  ? 0.3698 0.8783 0.3842 0.0578  -0.0148 0.0408  61  THR B N   
3001  C CA  . THR B 61  ? 0.3719 0.8965 0.3859 0.0412  -0.0174 0.0353  61  THR B CA  
3002  C C   . THR B 61  ? 0.3706 0.7981 0.3815 0.0248  -0.0148 0.0415  61  THR B C   
3003  O O   . THR B 61  ? 0.3659 0.7487 0.3809 -0.0077 -0.0136 0.0377  61  THR B O   
3004  C CB  . THR B 61  ? 0.3680 0.9734 0.3909 -0.0023 -0.0199 0.0161  61  THR B CB  
3005  O OG1 . THR B 61  ? 0.3732 0.9398 0.3914 -0.0369 -0.0196 0.0112  61  THR B OG1 
3006  C CG2 . THR B 61  ? 0.3641 0.9830 0.3933 -0.0349 -0.0175 0.0072  61  THR B CG2 
3007  N N   . GLN B 62  ? 0.3801 0.7780 0.3795 0.0507  -0.0136 0.0506  62  GLN B N   
3008  C CA  . GLN B 62  ? 0.3808 0.6945 0.3756 0.0443  -0.0101 0.0571  62  GLN B CA  
3009  C C   . GLN B 62  ? 0.3928 0.7018 0.3735 0.0660  -0.0093 0.0629  62  GLN B C   
3010  O O   . GLN B 62  ? 0.4097 0.7656 0.3782 0.0974  -0.0102 0.0660  62  GLN B O   
3011  C CB  . GLN B 62  ? 0.3880 0.6396 0.3775 0.0575  -0.0039 0.0658  62  GLN B CB  
3012  C CG  . GLN B 62  ? 0.4102 0.5967 0.3810 0.0753  0.0034  0.0757  62  GLN B CG  
3013  C CD  . GLN B 62  ? 0.4238 0.5547 0.3859 0.0812  0.0113  0.0809  62  GLN B CD  
3014  O OE1 . GLN B 62  ? 0.4137 0.5521 0.3880 0.0729  0.0098  0.0778  62  GLN B OE1 
3015  N NE2 . GLN B 62  ? 0.4522 0.5260 0.3899 0.0924  0.0210  0.0877  62  GLN B NE2 
3016  N N   . PHE B 63  ? 0.3869 0.6421 0.3664 0.0522  -0.0074 0.0641  63  PHE B N   
3017  C CA  . PHE B 63  ? 0.3956 0.6442 0.3624 0.0654  -0.0064 0.0682  63  PHE B CA  
3018  C C   . PHE B 63  ? 0.4253 0.6597 0.3633 0.1083  0.0000  0.0808  63  PHE B C   
3019  O O   . PHE B 63  ? 0.4442 0.6308 0.3665 0.1226  0.0076  0.0883  63  PHE B O   
3020  C CB  . PHE B 63  ? 0.3898 0.5786 0.3584 0.0462  -0.0038 0.0675  63  PHE B CB  
3021  C CG  . PHE B 63  ? 0.3990 0.5848 0.3569 0.0533  -0.0032 0.0697  63  PHE B CG  
3022  C CD1 . PHE B 63  ? 0.3903 0.6171 0.3548 0.0390  -0.0101 0.0614  63  PHE B CD1 
3023  C CD2 . PHE B 63  ? 0.4218 0.5614 0.3583 0.0715  0.0056  0.0791  63  PHE B CD2 
3024  C CE1 . PHE B 63  ? 0.3988 0.6246 0.3538 0.0465  -0.0098 0.0634  63  PHE B CE1 
3025  C CE2 . PHE B 63  ? 0.4334 0.5696 0.3579 0.0774  0.0069  0.0813  63  PHE B CE2 
3026  C CZ  . PHE B 63  ? 0.4184 0.5999 0.3546 0.0669  -0.0016 0.0739  63  PHE B CZ  
3027  N N   . GLU B 64  ? 0.4350 0.7063 0.3598 0.1291  -0.0022 0.0824  64  GLU B N   
3028  C CA  . GLU B 64  ? 0.4768 0.7252 0.3611 0.1743  0.0047  0.0950  64  GLU B CA  
3029  C C   . GLU B 64  ? 0.4881 0.7089 0.3571 0.1753  0.0076  0.0987  64  GLU B C   
3030  O O   . GLU B 64  ? 0.4694 0.7421 0.3546 0.1644  -0.0001 0.0913  64  GLU B O   
3031  C CB  . GLU B 64  ? 0.4904 0.8210 0.3647 0.2110  -0.0011 0.0939  64  GLU B CB  
3032  C CG  . GLU B 64  ? 0.4764 0.8526 0.3671 0.2107  -0.0048 0.0883  64  GLU B CG  
3033  C CD  . GLU B 64  ? 0.4902 0.9652 0.3715 0.2495  -0.0110 0.0843  64  GLU B CD  
3034  O OE1 . GLU B 64  ? 0.5136 1.0191 0.3727 0.2812  -0.0126 0.0869  64  GLU B OE1 
3035  O OE2 . GLU B 64  ? 0.4786 1.0064 0.3739 0.2497  -0.0144 0.0777  64  GLU B OE2 
3036  N N   . ALA B 65  ? 0.5209 0.6601 0.3551 0.1859  0.0202  0.1091  65  ALA B N   
3037  C CA  . ALA B 65  ? 0.5362 0.6431 0.3510 0.1854  0.0253  0.1128  65  ALA B CA  
3038  C C   . ALA B 65  ? 0.5663 0.7074 0.3492 0.2276  0.0235  0.1192  65  ALA B C   
3039  O O   . ALA B 65  ? 0.5979 0.7553 0.3521 0.2686  0.0242  0.1252  65  ALA B O   
3040  C CB  . ALA B 65  ? 0.5758 0.5874 0.3554 0.1797  0.0420  0.1200  65  ALA B CB  
3041  N N   . VAL B 66  ? 0.5567 0.7115 0.3428 0.2205  0.0209  0.1172  66  VAL B N   
3042  C CA  . VAL B 66  ? 0.5860 0.7741 0.3411 0.2602  0.0191  0.1226  66  VAL B CA  
3043  C C   . VAL B 66  ? 0.6169 0.7382 0.3389 0.2591  0.0297  0.1301  66  VAL B C   
3044  O O   . VAL B 66  ? 0.5894 0.6867 0.3362 0.2192  0.0310  0.1244  66  VAL B O   
3045  C CB  . VAL B 66  ? 0.5417 0.8396 0.3376 0.2504  0.0032  0.1089  66  VAL B CB  
3046  C CG1 . VAL B 66  ? 0.5755 0.9196 0.3397 0.2949  0.0007  0.1129  66  VAL B CG1 
3047  C CG2 . VAL B 66  ? 0.5105 0.8767 0.3376 0.2424  -0.0051 0.0989  66  VAL B CG2 
3048  N N   . GLY B 67  ? 0.6783 0.7695 0.3393 0.3052  0.0378  0.1427  67  GLY B N   
3049  C CA  . GLY B 67  ? 0.7203 0.7440 0.3384 0.3070  0.0501  0.1508  67  GLY B CA  
3050  C C   . GLY B 67  ? 0.6868 0.7744 0.3308 0.3014  0.0393  0.1445  67  GLY B C   
3051  O O   . GLY B 67  ? 0.6860 0.8498 0.3302 0.3335  0.0288  0.1428  67  GLY B O   
3052  N N   . ARG B 68  ? 0.6593 0.7217 0.3242 0.2612  0.0420  0.1395  68  ARG B N   
3053  C CA  . ARG B 68  ? 0.6301 0.7418 0.3170 0.2518  0.0332  0.1330  68  ARG B CA  
3054  C C   . ARG B 68  ? 0.6675 0.7068 0.3175 0.2441  0.0475  0.1398  68  ARG B C   
3055  O O   . ARG B 68  ? 0.6755 0.6510 0.3199 0.2151  0.0595  0.1395  68  ARG B O   
3056  C CB  . ARG B 68  ? 0.5561 0.7204 0.3105 0.2063  0.0202  0.1163  68  ARG B CB  
3057  C CG  . ARG B 68  ? 0.5195 0.7763 0.3077 0.2085  0.0051  0.1060  68  ARG B CG  
3058  C CD  . ARG B 68  ? 0.4644 0.7462 0.3029 0.1605  -0.0036 0.0904  68  ARG B CD  
3059  N NE  . ARG B 68  ? 0.4416 0.7657 0.3023 0.1531  -0.0099 0.0834  68  ARG B NE  
3060  C CZ  . ARG B 68  ? 0.4311 0.7189 0.3021 0.1392  -0.0067 0.0839  68  ARG B CZ  
3061  N NH1 . ARG B 68  ? 0.4375 0.6506 0.3019 0.1282  0.0023  0.0891  68  ARG B NH1 
3062  N NH2 . ARG B 68  ? 0.4138 0.7477 0.3026 0.1338  -0.0125 0.0772  68  ARG B NH2 
3063  N N   . GLU B 69  ? 0.6905 0.7462 0.3151 0.2682  0.0466  0.1443  69  GLU B N   
3064  C CA  . GLU B 69  ? 0.7372 0.7239 0.3168 0.2651  0.0617  0.1518  69  GLU B CA  
3065  C C   . GLU B 69  ? 0.6866 0.7165 0.3084 0.2355  0.0530  0.1410  69  GLU B C   
3066  O O   . GLU B 69  ? 0.6459 0.7570 0.3033 0.2398  0.0368  0.1329  69  GLU B O   
3067  C CB  . GLU B 69  ? 0.8182 0.7776 0.3230 0.3213  0.0693  0.1671  69  GLU B CB  
3068  C CG  . GLU B 69  ? 0.8879 0.7849 0.3308 0.3583  0.0810  0.1796  69  GLU B CG  
3069  C CD  . GLU B 69  ? 0.9781 0.7429 0.3409 0.3520  0.1080  0.1912  69  GLU B CD  
3070  O OE1 . GLU B 69  ? 0.9617 0.6902 0.3435 0.2990  0.1172  0.1842  69  GLU B OE1 
3071  O OE2 . GLU B 69  ? 1.0735 0.7707 0.3483 0.4005  0.1210  0.2063  69  GLU B OE2 
3072  N N   . PHE B 70  ? 0.6929 0.6701 0.3070 0.2044  0.0649  0.1395  70  PHE B N   
3073  C CA  . PHE B 70  ? 0.6535 0.6632 0.3004 0.1787  0.0587  0.1295  70  PHE B CA  
3074  C C   . PHE B 70  ? 0.7082 0.6564 0.3039 0.1760  0.0764  0.1367  70  PHE B C   
3075  O O   . PHE B 70  ? 0.7634 0.6342 0.3109 0.1699  0.0961  0.1436  70  PHE B O   
3076  C CB  . PHE B 70  ? 0.5944 0.6203 0.2965 0.1363  0.0528  0.1146  70  PHE B CB  
3077  C CG  . PHE B 70  ? 0.5498 0.6178 0.2924 0.1335  0.0393  0.1081  70  PHE B CG  
3078  C CD1 . PHE B 70  ? 0.5580 0.5941 0.2947 0.1330  0.0454  0.1115  70  PHE B CD1 
3079  C CD2 . PHE B 70  ? 0.5053 0.6415 0.2868 0.1285  0.0222  0.0978  70  PHE B CD2 
3080  C CE1 . PHE B 70  ? 0.5193 0.5939 0.2914 0.1293  0.0338  0.1054  70  PHE B CE1 
3081  C CE2 . PHE B 70  ? 0.4726 0.6431 0.2846 0.1209  0.0122  0.0908  70  PHE B CE2 
3082  C CZ  . PHE B 70  ? 0.4778 0.6189 0.2865 0.1223  0.0176  0.0951  70  PHE B CZ  
3083  N N   . ASN B 71  ? 0.6972 0.6774 0.2994 0.1773  0.0709  0.1339  71  ASN B N   
3084  C CA  . ASN B 71  ? 0.7504 0.6765 0.3032 0.1733  0.0879  0.1401  71  ASN B CA  
3085  C C   . ASN B 71  ? 0.7284 0.6400 0.3035 0.1249  0.0960  0.1279  71  ASN B C   
3086  O O   . ASN B 71  ? 0.6772 0.6137 0.3004 0.1001  0.0890  0.1162  71  ASN B O   
3087  C CB  . ASN B 71  ? 0.7565 0.7220 0.3002 0.1989  0.0799  0.1432  71  ASN B CB  
3088  C CG  . ASN B 71  ? 0.6855 0.7236 0.2931 0.1748  0.0630  0.1273  71  ASN B CG  
3089  O OD1 . ASN B 71  ? 0.6589 0.6925 0.2924 0.1391  0.0655  0.1169  71  ASN B OD1 
3090  N ND2 . ASN B 71  ? 0.6609 0.7675 0.2886 0.1954  0.0466  0.1242  71  ASN B ND2 
3091  N N   . ASN B 72  ? 0.7703 0.6456 0.3073 0.1136  0.1111  0.1299  72  ASN B N   
3092  C CA  . ASN B 72  ? 0.7650 0.6276 0.3104 0.0686  0.1232  0.1176  72  ASN B CA  
3093  C C   . ASN B 72  ? 0.6867 0.6256 0.3023 0.0484  0.1058  0.0999  72  ASN B C   
3094  O O   . ASN B 72  ? 0.6679 0.6169 0.3042 0.0158  0.1108  0.0862  72  ASN B O   
3095  C CB  . ASN B 72  ? 0.8428 0.6443 0.3191 0.0610  0.1464  0.1245  72  ASN B CB  
3096  C CG  . ASN B 72  ? 0.8604 0.6383 0.3272 0.0106  0.1661  0.1117  72  ASN B CG  
3097  O OD1 . ASN B 72  ? 0.8638 0.6211 0.3318 -0.0110 0.1743  0.1062  72  ASN B OD1 
3098  N ND2 . ASN B 72  ? 0.8721 0.6599 0.3297 -0.0096 0.1741  0.1052  72  ASN B ND2 
3099  N N   . LEU B 73  ? 0.6477 0.6402 0.2938 0.0688  0.0863  0.0988  73  LEU B N   
3100  C CA  . LEU B 73  ? 0.5855 0.6383 0.2869 0.0546  0.0697  0.0827  73  LEU B CA  
3101  C C   . LEU B 73  ? 0.5369 0.6274 0.2804 0.0616  0.0508  0.0776  73  LEU B C   
3102  O O   . LEU B 73  ? 0.5020 0.6358 0.2756 0.0612  0.0354  0.0683  73  LEU B O   
3103  C CB  . LEU B 73  ? 0.5874 0.6664 0.2845 0.0638  0.0647  0.0822  73  LEU B CB  
3104  C CG  . LEU B 73  ? 0.6271 0.6783 0.2903 0.0480  0.0827  0.0822  73  LEU B CG  
3105  C CD1 . LEU B 73  ? 0.6405 0.7083 0.2883 0.0652  0.0790  0.0867  73  LEU B CD1 
3106  C CD2 . LEU B 73  ? 0.5969 0.6737 0.2910 0.0165  0.0838  0.0640  73  LEU B CD2 
3107  N N   . GLU B 74  ? 0.5422 0.6103 0.2813 0.0658  0.0538  0.0833  74  GLU B N   
3108  C CA  . GLU B 74  ? 0.5015 0.5985 0.2765 0.0666  0.0393  0.0780  74  GLU B CA  
3109  C C   . GLU B 74  ? 0.4958 0.5664 0.2787 0.0496  0.0462  0.0746  74  GLU B C   
3110  O O   . GLU B 74  ? 0.4885 0.5558 0.2779 0.0561  0.0429  0.0781  74  GLU B O   
3111  C CB  . GLU B 74  ? 0.5138 0.6235 0.2757 0.0950  0.0343  0.0885  74  GLU B CB  
3112  C CG  . GLU B 74  ? 0.5128 0.6664 0.2730 0.1117  0.0248  0.0885  74  GLU B CG  
3113  C CD  . GLU B 74  ? 0.5215 0.7076 0.2730 0.1407  0.0184  0.0949  74  GLU B CD  
3114  O OE1 . GLU B 74  ? 0.5602 0.7114 0.2767 0.1637  0.0281  0.1077  74  GLU B OE1 
3115  O OE2 . GLU B 74  ? 0.4946 0.7423 0.2702 0.1400  0.0045  0.0857  74  GLU B OE2 
3116  N N   . ARG B 75  ? 0.4992 0.5583 0.2817 0.0274  0.0557  0.0664  75  ARG B N   
3117  C CA  . ARG B 75  ? 0.5004 0.5394 0.2858 0.0088  0.0649  0.0614  75  ARG B CA  
3118  C C   . ARG B 75  ? 0.4531 0.5221 0.2803 0.0047  0.0502  0.0506  75  ARG B C   
3119  O O   . ARG B 75  ? 0.4498 0.5046 0.2816 -0.0007 0.0532  0.0504  75  ARG B O   
3120  C CB  . ARG B 75  ? 0.5203 0.5536 0.2925 -0.0168 0.0802  0.0520  75  ARG B CB  
3121  C CG  . ARG B 75  ? 0.5855 0.5666 0.3011 -0.0212 0.1018  0.0627  75  ARG B CG  
3122  C CD  . ARG B 75  ? 0.6301 0.5523 0.3089 -0.0281 0.1187  0.0701  75  ARG B CD  
3123  N NE  . ARG B 75  ? 0.7107 0.5629 0.3179 -0.0263 0.1407  0.0832  75  ARG B NE  
3124  C CZ  . ARG B 75  ? 0.7573 0.5599 0.3194 0.0058  0.1443  0.1015  75  ARG B CZ  
3125  N NH1 . ARG B 75  ? 0.7253 0.5518 0.3128 0.0368  0.1268  0.1081  75  ARG B NH1 
3126  N NH2 . ARG B 75  ? 0.8434 0.5714 0.3284 0.0083  0.1666  0.1128  75  ARG B NH2 
3127  N N   . ARG B 76  ? 0.4239 0.5275 0.2746 0.0078  0.0354  0.0416  76  ARG B N   
3128  C CA  . ARG B 76  ? 0.3934 0.5129 0.2705 0.0062  0.0226  0.0317  76  ARG B CA  
3129  C C   . ARG B 76  ? 0.3859 0.4991 0.2685 0.0135  0.0163  0.0390  76  ARG B C   
3130  O O   . ARG B 76  ? 0.3743 0.4804 0.2680 0.0088  0.0152  0.0361  76  ARG B O   
3131  C CB  . ARG B 76  ? 0.3811 0.5235 0.2664 0.0098  0.0101  0.0217  76  ARG B CB  
3132  C CG  . ARG B 76  ? 0.3832 0.5422 0.2679 0.0054  0.0134  0.0104  76  ARG B CG  
3133  C CD  . ARG B 76  ? 0.3810 0.5539 0.2644 0.0136  0.0018  0.0029  76  ARG B CD  
3134  N NE  . ARG B 76  ? 0.3891 0.5640 0.2632 0.0176  0.0008  0.0119  76  ARG B NE  
3135  C CZ  . ARG B 76  ? 0.3898 0.5728 0.2603 0.0215  -0.0093 0.0080  76  ARG B CZ  
3136  N NH1 . ARG B 76  ? 0.3907 0.5678 0.2587 0.0219  -0.0184 -0.0036 76  ARG B NH1 
3137  N NH2 . ARG B 76  ? 0.3968 0.5911 0.2598 0.0257  -0.0094 0.0155  76  ARG B NH2 
3138  N N   . ILE B 77  ? 0.3930 0.5158 0.2677 0.0255  0.0124  0.0472  77  ILE B N   
3139  C CA  . ILE B 77  ? 0.3874 0.5190 0.2671 0.0326  0.0066  0.0521  77  ILE B CA  
3140  C C   . ILE B 77  ? 0.4063 0.5113 0.2712 0.0415  0.0172  0.0635  77  ILE B C   
3141  O O   . ILE B 77  ? 0.3973 0.5058 0.2709 0.0438  0.0137  0.0650  77  ILE B O   
3142  C CB  . ILE B 77  ? 0.3892 0.5564 0.2656 0.0429  -0.0014 0.0537  77  ILE B CB  
3143  C CG1 . ILE B 77  ? 0.4172 0.5824 0.2680 0.0620  0.0060  0.0647  77  ILE B CG1 
3144  C CG2 . ILE B 77  ? 0.3772 0.5624 0.2631 0.0296  -0.0113 0.0406  77  ILE B CG2 
3145  C CD1 . ILE B 77  ? 0.4208 0.6324 0.2675 0.0780  -0.0018 0.0663  77  ILE B CD1 
3146  N N   . GLU B 78  ? 0.4393 0.5129 0.2761 0.0452  0.0314  0.0711  78  GLU B N   
3147  C CA  . GLU B 78  ? 0.4717 0.5027 0.2821 0.0501  0.0450  0.0805  78  GLU B CA  
3148  C C   . GLU B 78  ? 0.4538 0.4745 0.2834 0.0296  0.0473  0.0720  78  GLU B C   
3149  O O   . GLU B 78  ? 0.4601 0.4630 0.2855 0.0335  0.0503  0.0765  78  GLU B O   
3150  C CB  . GLU B 78  ? 0.5243 0.5108 0.2889 0.0509  0.0631  0.0881  78  GLU B CB  
3151  C CG  . GLU B 78  ? 0.5780 0.5028 0.2967 0.0567  0.0807  0.0988  78  GLU B CG  
3152  C CD  . GLU B 78  ? 0.6475 0.5164 0.3046 0.0598  0.1003  0.1078  78  GLU B CD  
3153  O OE1 . GLU B 78  ? 0.6527 0.5179 0.3076 0.0331  0.1090  0.0995  78  GLU B OE1 
3154  O OE2 . GLU B 78  ? 0.7026 0.5306 0.3085 0.0904  0.1077  0.1227  78  GLU B OE2 
3155  N N   . ASN B 79  ? 0.4340 0.4703 0.2829 0.0109  0.0456  0.0590  79  ASN B N   
3156  C CA  . ASN B 79  ? 0.4171 0.4556 0.2845 -0.0052 0.0465  0.0483  79  ASN B CA  
3157  C C   . ASN B 79  ? 0.3853 0.4417 0.2796 -0.0002 0.0315  0.0448  79  ASN B C   
3158  O O   . ASN B 79  ? 0.3784 0.4262 0.2804 -0.0050 0.0330  0.0430  79  ASN B O   
3159  C CB  . ASN B 79  ? 0.4083 0.4706 0.2854 -0.0195 0.0476  0.0338  79  ASN B CB  
3160  C CG  . ASN B 79  ? 0.3959 0.4705 0.2879 -0.0334 0.0501  0.0209  79  ASN B CG  
3161  O OD1 . ASN B 79  ? 0.4140 0.4669 0.2939 -0.0459 0.0629  0.0220  79  ASN B OD1 
3162  N ND2 . ASN B 79  ? 0.3716 0.4798 0.2843 -0.0297 0.0385  0.0077  79  ASN B ND2 
3163  N N   . LEU B 80  ? 0.3717 0.4503 0.2758 0.0067  0.0185  0.0430  80  LEU B N   
3164  C CA  . LEU B 80  ? 0.3539 0.4427 0.2728 0.0068  0.0065  0.0392  80  LEU B CA  
3165  C C   . LEU B 80  ? 0.3581 0.4423 0.2752 0.0136  0.0083  0.0490  80  LEU B C   
3166  O O   . LEU B 80  ? 0.3475 0.4270 0.2746 0.0094  0.0059  0.0469  80  LEU B O   
3167  C CB  . LEU B 80  ? 0.3513 0.4599 0.2696 0.0078  -0.0037 0.0352  80  LEU B CB  
3168  C CG  . LEU B 80  ? 0.3457 0.4561 0.2673 -0.0003 -0.0139 0.0270  80  LEU B CG  
3169  C CD1 . LEU B 80  ? 0.3547 0.4767 0.2663 -0.0044 -0.0204 0.0205  80  LEU B CD1 
3170  C CD2 . LEU B 80  ? 0.3416 0.4616 0.2679 -0.0023 -0.0155 0.0318  80  LEU B CD2 
3171  N N   . ASN B 81  ? 0.3783 0.4647 0.2788 0.0276  0.0127  0.0595  81  ASN B N   
3172  C CA  . ASN B 81  ? 0.3904 0.4764 0.2821 0.0424  0.0148  0.0691  81  ASN B CA  
3173  C C   . ASN B 81  ? 0.4035 0.4522 0.2876 0.0397  0.0252  0.0725  81  ASN B C   
3174  O O   . ASN B 81  ? 0.3966 0.4486 0.2877 0.0433  0.0227  0.0742  81  ASN B O   
3175  C CB  . ASN B 81  ? 0.4204 0.5093 0.2843 0.0657  0.0193  0.0799  81  ASN B CB  
3176  C CG  . ASN B 81  ? 0.4383 0.5319 0.2865 0.0900  0.0207  0.0893  81  ASN B CG  
3177  O OD1 . ASN B 81  ? 0.4177 0.5548 0.2847 0.0918  0.0107  0.0853  81  ASN B OD1 
3178  N ND2 . ASN B 81  ? 0.4841 0.5310 0.2916 0.1088  0.0344  0.1011  81  ASN B ND2 
3179  N N   . LYS B 82  ? 0.4261 0.4421 0.2943 0.0301  0.0378  0.0720  82  LYS B N   
3180  C CA  . LYS B 82  ? 0.4459 0.4255 0.3018 0.0213  0.0502  0.0726  82  LYS B CA  
3181  C C   . LYS B 82  ? 0.4125 0.4086 0.3008 0.0077  0.0426  0.0621  82  LYS B C   
3182  O O   . LYS B 82  ? 0.4139 0.3968 0.3023 0.0091  0.0449  0.0647  82  LYS B O   
3183  C CB  . LYS B 82  ? 0.4787 0.4274 0.3089 0.0044  0.0670  0.0697  82  LYS B CB  
3184  C CG  . LYS B 82  ? 0.4985 0.4154 0.3163 -0.0141 0.0811  0.0654  82  LYS B CG  
3185  C CD  . LYS B 82  ? 0.5533 0.4270 0.3266 -0.0337 0.1037  0.0643  82  LYS B CD  
3186  C CE  . LYS B 82  ? 0.5349 0.4440 0.3288 -0.0635 0.1066  0.0459  82  LYS B CE  
3187  N NZ  . LYS B 82  ? 0.5922 0.4648 0.3396 -0.0891 0.1303  0.0428  82  LYS B NZ  
3188  N N   . LYS B 83  ? 0.3892 0.4111 0.2997 -0.0019 0.0339  0.0505  83  LYS B N   
3189  C CA  . LYS B 83  ? 0.3666 0.4000 0.2992 -0.0093 0.0267  0.0403  83  LYS B CA  
3190  C C   . LYS B 83  ? 0.3532 0.3926 0.2963 -0.0029 0.0164  0.0436  83  LYS B C   
3191  O O   . LYS B 83  ? 0.3448 0.3789 0.2966 -0.0062 0.0154  0.0410  83  LYS B O   
3192  C CB  . LYS B 83  ? 0.3554 0.4101 0.2977 -0.0127 0.0196  0.0276  83  LYS B CB  
3193  C CG  . LYS B 83  ? 0.3612 0.4264 0.3034 -0.0240 0.0287  0.0165  83  LYS B CG  
3194  C CD  . LYS B 83  ? 0.3905 0.4353 0.3113 -0.0361 0.0466  0.0218  83  LYS B CD  
3195  C CE  . LYS B 83  ? 0.3989 0.4604 0.3183 -0.0567 0.0583  0.0072  83  LYS B CE  
3196  N NZ  . LYS B 83  ? 0.4069 0.4915 0.3206 -0.0639 0.0623  -0.0006 83  LYS B NZ  
3197  N N   . MET B 84  ? 0.3540 0.4090 0.2952 0.0040  0.0096  0.0479  84  MET B N   
3198  C CA  . MET B 84  ? 0.3461 0.4159 0.2942 0.0049  0.0018  0.0491  84  MET B CA  
3199  C C   . MET B 84  ? 0.3529 0.4153 0.2976 0.0139  0.0076  0.0577  84  MET B C   
3200  O O   . MET B 84  ? 0.3423 0.4042 0.2967 0.0091  0.0049  0.0556  84  MET B O   
3201  C CB  . MET B 84  ? 0.3491 0.4489 0.2935 0.0081  -0.0043 0.0498  84  MET B CB  
3202  C CG  . MET B 84  ? 0.3429 0.4662 0.2930 -0.0024 -0.0123 0.0443  84  MET B CG  
3203  S SD  . MET B 84  ? 0.3489 0.5272 0.2962 0.0089  -0.0148 0.0485  84  MET B SD  
3204  C CE  . MET B 84  ? 0.3553 0.5238 0.2992 0.0314  -0.0077 0.0604  84  MET B CE  
3205  N N   . GLU B 85  ? 0.3775 0.4278 0.3021 0.0288  0.0166  0.0675  85  GLU B N   
3206  C CA  . GLU B 85  ? 0.3968 0.4316 0.3066 0.0436  0.0233  0.0766  85  GLU B CA  
3207  C C   . GLU B 85  ? 0.3989 0.3994 0.3092 0.0316  0.0314  0.0739  85  GLU B C   
3208  O O   . GLU B 85  ? 0.3940 0.3938 0.3096 0.0346  0.0305  0.0753  85  GLU B O   
3209  C CB  . GLU B 85  ? 0.4391 0.4551 0.3118 0.0674  0.0325  0.0883  85  GLU B CB  
3210  C CG  . GLU B 85  ? 0.4386 0.4994 0.3108 0.0830  0.0238  0.0900  85  GLU B CG  
3211  C CD  . GLU B 85  ? 0.4752 0.5434 0.3157 0.1199  0.0267  0.1012  85  GLU B CD  
3212  O OE1 . GLU B 85  ? 0.5248 0.5458 0.3215 0.1389  0.0390  0.1113  85  GLU B OE1 
3213  O OE2 . GLU B 85  ? 0.4617 0.5844 0.3159 0.1309  0.0172  0.0989  85  GLU B OE2 
3214  N N   . ASP B 86  ? 0.4059 0.3854 0.3114 0.0166  0.0395  0.0684  86  ASP B N   
3215  C CA  . ASP B 86  ? 0.4058 0.3664 0.3144 0.0006  0.0471  0.0615  86  ASP B CA  
3216  C C   . ASP B 86  ? 0.3691 0.3535 0.3086 -0.0060 0.0355  0.0526  86  ASP B C   
3217  O O   . ASP B 86  ? 0.3672 0.3419 0.3105 -0.0104 0.0386  0.0507  86  ASP B O   
3218  C CB  . ASP B 86  ? 0.4189 0.3720 0.3192 -0.0175 0.0572  0.0528  86  ASP B CB  
3219  C CG  . ASP B 86  ? 0.4722 0.3773 0.3290 -0.0226 0.0772  0.0588  86  ASP B CG  
3220  O OD1 . ASP B 86  ? 0.4987 0.3696 0.3352 -0.0210 0.0862  0.0635  86  ASP B OD1 
3221  O OD2 . ASP B 86  ? 0.4959 0.3915 0.3329 -0.0289 0.0852  0.0585  86  ASP B OD2 
3222  N N   . GLY B 87  ? 0.3471 0.3563 0.3019 -0.0066 0.0234  0.0471  87  GLY B N   
3223  C CA  . GLY B 87  ? 0.3270 0.3460 0.2975 -0.0107 0.0136  0.0391  87  GLY B CA  
3224  C C   . GLY B 87  ? 0.3203 0.3396 0.2956 -0.0081 0.0098  0.0439  87  GLY B C   
3225  O O   . GLY B 87  ? 0.3135 0.3271 0.2957 -0.0117 0.0085  0.0397  87  GLY B O   
3226  N N   . PHE B 88  ? 0.3233 0.3557 0.2943 -0.0006 0.0080  0.0517  88  PHE B N   
3227  C CA  . PHE B 88  ? 0.3176 0.3630 0.2931 0.0018  0.0048  0.0549  88  PHE B CA  
3228  C C   . PHE B 88  ? 0.3263 0.3526 0.2970 0.0099  0.0132  0.0608  88  PHE B C   
3229  O O   . PHE B 88  ? 0.3180 0.3472 0.2966 0.0077  0.0111  0.0599  88  PHE B O   
3230  C CB  . PHE B 88  ? 0.3208 0.4013 0.2925 0.0097  0.0007  0.0588  88  PHE B CB  
3231  C CG  . PHE B 88  ? 0.3150 0.4168 0.2896 -0.0058 -0.0075 0.0504  88  PHE B CG  
3232  C CD1 . PHE B 88  ? 0.3121 0.4112 0.2883 -0.0237 -0.0119 0.0429  88  PHE B CD1 
3233  C CD2 . PHE B 88  ? 0.3203 0.4385 0.2892 -0.0043 -0.0096 0.0495  88  PHE B CD2 
3234  C CE1 . PHE B 88  ? 0.3217 0.4266 0.2876 -0.0421 -0.0166 0.0342  88  PHE B CE1 
3235  C CE2 . PHE B 88  ? 0.3229 0.4551 0.2881 -0.0220 -0.0156 0.0404  88  PHE B CE2 
3236  C CZ  . PHE B 88  ? 0.3271 0.4490 0.2878 -0.0423 -0.0184 0.0325  88  PHE B CZ  
3237  N N   . LEU B 89  ? 0.3494 0.3507 0.3014 0.0176  0.0242  0.0663  89  LEU B N   
3238  C CA  . LEU B 89  ? 0.3705 0.3400 0.3070 0.0219  0.0351  0.0705  89  LEU B CA  
3239  C C   . LEU B 89  ? 0.3549 0.3167 0.3068 0.0045  0.0361  0.0610  89  LEU B C   
3240  O O   . LEU B 89  ? 0.3558 0.3082 0.3079 0.0060  0.0386  0.0621  89  LEU B O   
3241  C CB  . LEU B 89  ? 0.4132 0.3425 0.3140 0.0265  0.0501  0.0761  89  LEU B CB  
3242  C CG  . LEU B 89  ? 0.4441 0.3703 0.3164 0.0522  0.0520  0.0875  89  LEU B CG  
3243  C CD1 . LEU B 89  ? 0.5004 0.3672 0.3245 0.0534  0.0705  0.0929  89  LEU B CD1 
3244  C CD2 . LEU B 89  ? 0.4498 0.3938 0.3164 0.0782  0.0475  0.0949  89  LEU B CD2 
3245  N N   . ASP B 90  ? 0.3424 0.3125 0.3053 -0.0087 0.0340  0.0510  90  ASP B N   
3246  C CA  . ASP B 90  ? 0.3292 0.3037 0.3054 -0.0201 0.0336  0.0398  90  ASP B CA  
3247  C C   . ASP B 90  ? 0.3076 0.2940 0.2990 -0.0169 0.0221  0.0383  90  ASP B C   
3248  O O   . ASP B 90  ? 0.3037 0.2871 0.3010 -0.0198 0.0231  0.0344  90  ASP B O   
3249  C CB  . ASP B 90  ? 0.3246 0.3160 0.3057 -0.0280 0.0325  0.0283  90  ASP B CB  
3250  C CG  . ASP B 90  ? 0.3495 0.3301 0.3132 -0.0387 0.0466  0.0267  90  ASP B CG  
3251  O OD1 . ASP B 90  ? 0.3778 0.3268 0.3197 -0.0431 0.0599  0.0326  90  ASP B OD1 
3252  O OD2 . ASP B 90  ? 0.3478 0.3475 0.3138 -0.0430 0.0456  0.0191  90  ASP B OD2 
3253  N N   . VAL B 91  ? 0.2992 0.2971 0.2927 -0.0137 0.0124  0.0403  91  VAL B N   
3254  C CA  . VAL B 91  ? 0.2904 0.2917 0.2879 -0.0160 0.0041  0.0386  91  VAL B CA  
3255  C C   . VAL B 91  ? 0.2876 0.2914 0.2885 -0.0132 0.0065  0.0452  91  VAL B C   
3256  O O   . VAL B 91  ? 0.2830 0.2814 0.2882 -0.0161 0.0051  0.0425  91  VAL B O   
3257  C CB  . VAL B 91  ? 0.2944 0.3048 0.2850 -0.0202 -0.0032 0.0380  91  VAL B CB  
3258  C CG1 . VAL B 91  ? 0.2977 0.3078 0.2838 -0.0294 -0.0078 0.0364  91  VAL B CG1 
3259  C CG2 . VAL B 91  ? 0.3014 0.3027 0.2834 -0.0203 -0.0067 0.0302  91  VAL B CG2 
3260  N N   . TRP B 92  ? 0.2938 0.3064 0.2893 -0.0038 0.0101  0.0536  92  TRP B N   
3261  C CA  . TRP B 92  ? 0.2957 0.3163 0.2905 0.0050  0.0120  0.0596  92  TRP B CA  
3262  C C   . TRP B 92  ? 0.3054 0.2968 0.2937 0.0089  0.0215  0.0614  92  TRP B C   
3263  O O   . TRP B 92  ? 0.3031 0.2964 0.2943 0.0123  0.0217  0.0629  92  TRP B O   
3264  C CB  . TRP B 92  ? 0.3072 0.3525 0.2920 0.0215  0.0120  0.0669  92  TRP B CB  
3265  C CG  . TRP B 92  ? 0.2964 0.3844 0.2896 0.0125  0.0028  0.0624  92  TRP B CG  
3266  C CD1 . TRP B 92  ? 0.2985 0.4055 0.2888 0.0103  -0.0005 0.0607  92  TRP B CD1 
3267  C CD2 . TRP B 92  ? 0.2869 0.4026 0.2885 -0.0008 -0.0023 0.0572  92  TRP B CD2 
3268  N NE1 . TRP B 92  ? 0.2930 0.4382 0.2880 -0.0056 -0.0069 0.0536  92  TRP B NE1 
3269  C CE2 . TRP B 92  ? 0.2876 0.4378 0.2880 -0.0142 -0.0075 0.0512  92  TRP B CE2 
3270  C CE3 . TRP B 92  ? 0.2819 0.3962 0.2891 -0.0052 -0.0019 0.0561  92  TRP B CE3 
3271  C CZ2 . TRP B 92  ? 0.2880 0.4697 0.2890 -0.0362 -0.0106 0.0430  92  TRP B CZ2 
3272  C CZ3 . TRP B 92  ? 0.2794 0.4251 0.2891 -0.0240 -0.0059 0.0494  92  TRP B CZ3 
3273  C CH2 . TRP B 92  ? 0.2848 0.4629 0.2895 -0.0414 -0.0095 0.0424  92  TRP B CH2 
3274  N N   . THR B 93  ? 0.3191 0.2848 0.2963 0.0051  0.0305  0.0596  93  THR B N   
3275  C CA  . THR B 93  ? 0.3349 0.2712 0.3013 0.0000  0.0418  0.0576  93  THR B CA  
3276  C C   . THR B 93  ? 0.3111 0.2588 0.2985 -0.0113 0.0367  0.0478  93  THR B C   
3277  O O   . THR B 93  ? 0.3136 0.2523 0.3007 -0.0112 0.0400  0.0478  93  THR B O   
3278  C CB  . THR B 93  ? 0.3605 0.2713 0.3068 -0.0105 0.0546  0.0540  93  THR B CB  
3279  O OG1 . THR B 93  ? 0.3930 0.2823 0.3101 0.0036  0.0610  0.0646  93  THR B OG1 
3280  C CG2 . THR B 93  ? 0.3827 0.2650 0.3140 -0.0244 0.0683  0.0481  93  THR B CG2 
3281  N N   . TYR B 94  ? 0.2928 0.2584 0.2935 -0.0176 0.0287  0.0397  94  TYR B N   
3282  C CA  . TYR B 94  ? 0.2781 0.2533 0.2907 -0.0215 0.0230  0.0304  94  TYR B CA  
3283  C C   . TYR B 94  ? 0.2702 0.2457 0.2875 -0.0177 0.0166  0.0348  94  TYR B C   
3284  O O   . TYR B 94  ? 0.2663 0.2395 0.2880 -0.0188 0.0175  0.0314  94  TYR B O   
3285  C CB  . TYR B 94  ? 0.2726 0.2602 0.2866 -0.0204 0.0150  0.0226  94  TYR B CB  
3286  C CG  . TYR B 94  ? 0.2688 0.2589 0.2828 -0.0151 0.0070  0.0152  94  TYR B CG  
3287  C CD1 . TYR B 94  ? 0.2737 0.2500 0.2785 -0.0130 -0.0005 0.0191  94  TYR B CD1 
3288  C CD2 . TYR B 94  ? 0.2675 0.2739 0.2845 -0.0124 0.0080  0.0030  94  TYR B CD2 
3289  C CE1 . TYR B 94  ? 0.2844 0.2489 0.2761 -0.0059 -0.0061 0.0134  94  TYR B CE1 
3290  C CE2 . TYR B 94  ? 0.2722 0.2785 0.2815 -0.0002 0.0004  -0.0031 94  TYR B CE2 
3291  C CZ  . TYR B 94  ? 0.2839 0.2620 0.2772 0.0041  -0.0062 0.0031  94  TYR B CZ  
3292  O OH  . TYR B 94  ? 0.3020 0.2665 0.2754 0.0182  -0.0119 -0.0020 94  TYR B OH  
3293  N N   . ASN B 95  ? 0.2691 0.2523 0.2845 -0.0157 0.0109  0.0409  95  ASN B N   
3294  C CA  . ASN B 95  ? 0.2653 0.2561 0.2826 -0.0174 0.0065  0.0437  95  ASN B CA  
3295  C C   . ASN B 95  ? 0.2653 0.2557 0.2855 -0.0111 0.0121  0.0484  95  ASN B C   
3296  O O   . ASN B 95  ? 0.2606 0.2502 0.2849 -0.0139 0.0105  0.0466  95  ASN B O   
3297  C CB  . ASN B 95  ? 0.2678 0.2801 0.2816 -0.0203 0.0023  0.0471  95  ASN B CB  
3298  C CG  . ASN B 95  ? 0.2755 0.2809 0.2793 -0.0306 -0.0031 0.0413  95  ASN B CG  
3299  O OD1 . ASN B 95  ? 0.2809 0.2642 0.2780 -0.0301 -0.0048 0.0355  95  ASN B OD1 
3300  N ND2 . ASN B 95  ? 0.2806 0.3069 0.2793 -0.0384 -0.0058 0.0415  95  ASN B ND2 
3301  N N   . ALA B 96  ? 0.2773 0.2626 0.2890 -0.0006 0.0194  0.0547  96  ALA B N   
3302  C CA  . ALA B 96  ? 0.2899 0.2649 0.2929 0.0104  0.0264  0.0600  96  ALA B CA  
3303  C C   . ALA B 96  ? 0.2906 0.2429 0.2947 0.0021  0.0323  0.0540  96  ALA B C   
3304  O O   . ALA B 96  ? 0.2867 0.2403 0.2950 0.0039  0.0320  0.0541  96  ALA B O   
3305  C CB  . ALA B 96  ? 0.3199 0.2770 0.2980 0.0264  0.0351  0.0678  96  ALA B CB  
3306  N N   . GLU B 97  ? 0.2956 0.2342 0.2963 -0.0082 0.0379  0.0471  97  GLU B N   
3307  C CA  . GLU B 97  ? 0.2997 0.2274 0.3001 -0.0196 0.0451  0.0380  97  GLU B CA  
3308  C C   . GLU B 97  ? 0.2743 0.2230 0.2945 -0.0225 0.0357  0.0304  97  GLU B C   
3309  O O   . GLU B 97  ? 0.2751 0.2212 0.2974 -0.0260 0.0392  0.0257  97  GLU B O   
3310  C CB  . GLU B 97  ? 0.3135 0.2354 0.3050 -0.0338 0.0540  0.0292  97  GLU B CB  
3311  C CG  . GLU B 97  ? 0.3529 0.2384 0.3122 -0.0330 0.0674  0.0364  97  GLU B CG  
3312  C CD  . GLU B 97  ? 0.3736 0.2518 0.3192 -0.0543 0.0794  0.0258  97  GLU B CD  
3313  O OE1 . GLU B 97  ? 0.3512 0.2663 0.3183 -0.0663 0.0748  0.0122  97  GLU B OE1 
3314  O OE2 . GLU B 97  ? 0.4188 0.2544 0.3270 -0.0583 0.0942  0.0304  97  GLU B OE2 
3315  N N   . LEU B 98  ? 0.2592 0.2230 0.2872 -0.0202 0.0249  0.0291  98  LEU B N   
3316  C CA  . LEU B 98  ? 0.2490 0.2200 0.2822 -0.0186 0.0167  0.0232  98  LEU B CA  
3317  C C   . LEU B 98  ? 0.2456 0.2131 0.2798 -0.0168 0.0142  0.0298  98  LEU B C   
3318  O O   . LEU B 98  ? 0.2432 0.2099 0.2800 -0.0162 0.0138  0.0261  98  LEU B O   
3319  C CB  . LEU B 98  ? 0.2511 0.2232 0.2773 -0.0153 0.0081  0.0208  98  LEU B CB  
3320  C CG  . LEU B 98  ? 0.2585 0.2239 0.2741 -0.0082 0.0011  0.0148  98  LEU B CG  
3321  C CD1 . LEU B 98  ? 0.2560 0.2406 0.2762 -0.0013 0.0023  0.0024  98  LEU B CD1 
3322  C CD2 . LEU B 98  ? 0.2763 0.2249 0.2706 -0.0047 -0.0054 0.0147  98  LEU B CD2 
3323  N N   . LEU B 99  ? 0.2458 0.2181 0.2780 -0.0162 0.0125  0.0382  99  LEU B N   
3324  C CA  . LEU B 99  ? 0.2434 0.2246 0.2769 -0.0167 0.0106  0.0427  99  LEU B CA  
3325  C C   . LEU B 99  ? 0.2431 0.2198 0.2800 -0.0107 0.0169  0.0441  99  LEU B C   
3326  O O   . LEU B 99  ? 0.2390 0.2181 0.2789 -0.0122 0.0153  0.0432  99  LEU B O   
3327  C CB  . LEU B 99  ? 0.2453 0.2494 0.2772 -0.0155 0.0092  0.0488  99  LEU B CB  
3328  C CG  . LEU B 99  ? 0.2441 0.2743 0.2776 -0.0194 0.0071  0.0504  99  LEU B CG  
3329  C CD1 . LEU B 99  ? 0.2499 0.2696 0.2750 -0.0373 0.0032  0.0450  99  LEU B CD1 
3330  C CD2 . LEU B 99  ? 0.2461 0.3157 0.2791 -0.0161 0.0057  0.0533  99  LEU B CD2 
3331  N N   . VAL B 100 ? 0.2539 0.2178 0.2841 -0.0048 0.0254  0.0461  100 VAL B N   
3332  C CA  . VAL B 100 ? 0.2660 0.2134 0.2889 -0.0005 0.0340  0.0466  100 VAL B CA  
3333  C C   . VAL B 100 ? 0.2577 0.2026 0.2889 -0.0107 0.0346  0.0364  100 VAL B C   
3334  O O   . VAL B 100 ? 0.2547 0.2005 0.2891 -0.0090 0.0345  0.0360  100 VAL B O   
3335  C CB  . VAL B 100 ? 0.2971 0.2149 0.2957 0.0052  0.0462  0.0502  100 VAL B CB  
3336  C CG1 . VAL B 100 ? 0.3223 0.2083 0.3031 0.0026  0.0583  0.0472  100 VAL B CG1 
3337  C CG2 . VAL B 100 ? 0.3102 0.2350 0.2959 0.0254  0.0451  0.0612  100 VAL B CG2 
3338  N N   . LEU B 101 ? 0.2544 0.2029 0.2885 -0.0192 0.0347  0.0272  101 LEU B N   
3339  C CA  . LEU B 101 ? 0.2469 0.2079 0.2886 -0.0247 0.0337  0.0148  101 LEU B CA  
3340  C C   . LEU B 101 ? 0.2353 0.2041 0.2828 -0.0178 0.0237  0.0153  101 LEU B C   
3341  O O   . LEU B 101 ? 0.2335 0.2060 0.2841 -0.0177 0.0248  0.0105  101 LEU B O   
3342  C CB  . LEU B 101 ? 0.2448 0.2232 0.2885 -0.0289 0.0323  0.0042  101 LEU B CB  
3343  C CG  . LEU B 101 ? 0.2571 0.2445 0.2969 -0.0447 0.0443  -0.0087 101 LEU B CG  
3344  C CD1 . LEU B 101 ? 0.2849 0.2362 0.3050 -0.0550 0.0591  -0.0029 101 LEU B CD1 
3345  C CD2 . LEU B 101 ? 0.2542 0.2653 0.2960 -0.0467 0.0419  -0.0170 101 LEU B CD2 
3346  N N   . MET B 102 ? 0.2336 0.2006 0.2769 -0.0141 0.0154  0.0202  102 MET B N   
3347  C CA  . MET B 102 ? 0.2372 0.1983 0.2726 -0.0108 0.0084  0.0204  102 MET B CA  
3348  C C   . MET B 102 ? 0.2346 0.1953 0.2729 -0.0136 0.0098  0.0269  102 MET B C   
3349  O O   . MET B 102 ? 0.2371 0.1942 0.2722 -0.0117 0.0083  0.0245  102 MET B O   
3350  C CB  . MET B 102 ? 0.2500 0.1986 0.2690 -0.0121 0.0024  0.0231  102 MET B CB  
3351  C CG  . MET B 102 ? 0.2573 0.2053 0.2684 -0.0044 -0.0004 0.0160  102 MET B CG  
3352  S SD  . MET B 102 ? 0.2880 0.2049 0.2652 -0.0038 -0.0064 0.0176  102 MET B SD  
3353  C CE  . MET B 102 ? 0.2795 0.2057 0.2662 -0.0222 -0.0039 0.0266  102 MET B CE  
3354  N N   . GLU B 103 ? 0.2317 0.2002 0.2743 -0.0154 0.0126  0.0345  103 GLU B N   
3355  C CA  . GLU B 103 ? 0.2299 0.2094 0.2749 -0.0152 0.0135  0.0396  103 GLU B CA  
3356  C C   . GLU B 103 ? 0.2291 0.2045 0.2788 -0.0084 0.0198  0.0389  103 GLU B C   
3357  O O   . GLU B 103 ? 0.2273 0.2093 0.2789 -0.0075 0.0195  0.0400  103 GLU B O   
3358  C CB  . GLU B 103 ? 0.2310 0.2320 0.2759 -0.0141 0.0134  0.0460  103 GLU B CB  
3359  C CG  . GLU B 103 ? 0.2361 0.2450 0.2730 -0.0279 0.0082  0.0450  103 GLU B CG  
3360  C CD  . GLU B 103 ? 0.2468 0.2502 0.2717 -0.0428 0.0062  0.0422  103 GLU B CD  
3361  O OE1 . GLU B 103 ? 0.2433 0.2544 0.2725 -0.0415 0.0077  0.0427  103 GLU B OE1 
3362  O OE2 . GLU B 103 ? 0.2657 0.2509 0.2705 -0.0565 0.0042  0.0393  103 GLU B OE2 
3363  N N   . ASN B 104 ? 0.2355 0.1978 0.2828 -0.0064 0.0268  0.0360  104 ASN B N   
3364  C CA  . ASN B 104 ? 0.2445 0.1940 0.2882 -0.0059 0.0350  0.0320  104 ASN B CA  
3365  C C   . ASN B 104 ? 0.2346 0.1922 0.2866 -0.0103 0.0314  0.0237  104 ASN B C   
3366  O O   . ASN B 104 ? 0.2357 0.1919 0.2883 -0.0085 0.0339  0.0230  104 ASN B O   
3367  C CB  . ASN B 104 ? 0.2623 0.1925 0.2943 -0.0128 0.0455  0.0264  104 ASN B CB  
3368  C CG  . ASN B 104 ? 0.2888 0.1944 0.2988 -0.0038 0.0538  0.0354  104 ASN B CG  
3369  O OD1 . ASN B 104 ? 0.2919 0.2024 0.2975 0.0120  0.0513  0.0449  104 ASN B OD1 
3370  N ND2 . ASN B 104 ? 0.3132 0.1939 0.3048 -0.0129 0.0644  0.0313  104 ASN B ND2 
3371  N N   . GLU B 105 ? 0.1750 0.2363 0.2623 0.0117  -0.0218 -0.0147 105 GLU B N   
3372  C CA  . GLU B 105 ? 0.1591 0.2435 0.2654 0.0260  -0.0207 -0.0235 105 GLU B CA  
3373  C C   . GLU B 105 ? 0.1535 0.1946 0.2613 0.0325  -0.0346 -0.0237 105 GLU B C   
3374  O O   . GLU B 105 ? 0.1342 0.1813 0.2614 0.0327  -0.0354 -0.0231 105 GLU B O   
3375  C CB  . GLU B 105 ? 0.1823 0.2979 0.2728 0.0540  -0.0145 -0.0372 105 GLU B CB  
3376  C CG  . GLU B 105 ? 0.1694 0.3321 0.2820 0.0706  -0.0112 -0.0456 105 GLU B CG  
3377  C CD  . GLU B 105 ? 0.1940 0.4104 0.2957 0.1018  -0.0021 -0.0595 105 GLU B CD  
3378  O OE1 . GLU B 105 ? 0.2340 0.4131 0.2965 0.1296  -0.0066 -0.0676 105 GLU B OE1 
3379  O OE2 . GLU B 105 ? 0.1794 0.4778 0.3101 0.0981  0.0093  -0.0634 105 GLU B OE2 
3380  N N   . ARG B 106 ? 0.1762 0.1749 0.2607 0.0345  -0.0454 -0.0247 106 ARG B N   
3381  C CA  . ARG B 106 ? 0.1789 0.1395 0.2634 0.0305  -0.0568 -0.0234 106 ARG B CA  
3382  C C   . ARG B 106 ? 0.1458 0.1134 0.2615 0.0114  -0.0582 -0.0120 106 ARG B C   
3383  O O   . ARG B 106 ? 0.1371 0.0954 0.2641 0.0088  -0.0600 -0.0099 106 ARG B O   
3384  C CB  . ARG B 106 ? 0.2193 0.1374 0.2710 0.0283  -0.0692 -0.0285 106 ARG B CB  
3385  C CG  . ARG B 106 ? 0.2691 0.1591 0.2769 0.0529  -0.0701 -0.0423 106 ARG B CG  
3386  C CD  . ARG B 106 ? 0.3216 0.1457 0.2915 0.0448  -0.0851 -0.0480 106 ARG B CD  
3387  N NE  . ARG B 106 ? 0.3483 0.1307 0.3010 0.0512  -0.0869 -0.0489 106 ARG B NE  
3388  C CZ  . ARG B 106 ? 0.3827 0.1137 0.3172 0.0277  -0.0965 -0.0466 106 ARG B CZ  
3389  N NH1 . ARG B 106 ? 0.3866 0.1153 0.3274 -0.0045 -0.1067 -0.0451 106 ARG B NH1 
3390  N NH2 . ARG B 106 ? 0.4193 0.1035 0.3271 0.0347  -0.0962 -0.0455 106 ARG B NH2 
3391  N N   . THR B 107 ? 0.1365 0.1163 0.2592 0.0016  -0.0566 -0.0046 107 THR B N   
3392  C CA  . THR B 107 ? 0.1175 0.0994 0.2613 -0.0075 -0.0584 0.0047  107 THR B CA  
3393  C C   . THR B 107 ? 0.0967 0.0911 0.2585 -0.0086 -0.0496 0.0054  107 THR B C   
3394  O O   . THR B 107 ? 0.0842 0.0758 0.2611 -0.0094 -0.0512 0.0081  107 THR B O   
3395  C CB  . THR B 107 ? 0.1313 0.1094 0.2636 -0.0114 -0.0598 0.0130  107 THR B CB  
3396  O OG1 . THR B 107 ? 0.1512 0.1212 0.2678 -0.0096 -0.0721 0.0118  107 THR B OG1 
3397  C CG2 . THR B 107 ? 0.1251 0.0984 0.2703 -0.0116 -0.0615 0.0211  107 THR B CG2 
3398  N N   . LEU B 108 ? 0.0961 0.1103 0.2560 -0.0097 -0.0404 0.0019  108 LEU B N   
3399  C CA  . LEU B 108 ? 0.0820 0.1128 0.2573 -0.0139 -0.0349 0.0000  108 LEU B CA  
3400  C C   . LEU B 108 ? 0.0724 0.1038 0.2546 -0.0003 -0.0384 -0.0054 108 LEU B C   
3401  O O   . LEU B 108 ? 0.0628 0.0912 0.2550 -0.0020 -0.0386 -0.0041 108 LEU B O   
3402  C CB  . LEU B 108 ? 0.0872 0.1546 0.2626 -0.0227 -0.0250 -0.0045 108 LEU B CB  
3403  C CG  . LEU B 108 ? 0.1101 0.1704 0.2689 -0.0427 -0.0181 0.0032  108 LEU B CG  
3404  C CD1 . LEU B 108 ? 0.1172 0.2246 0.2815 -0.0611 -0.0059 -0.0013 108 LEU B CD1 
3405  C CD2 . LEU B 108 ? 0.1248 0.1399 0.2729 -0.0527 -0.0219 0.0131  108 LEU B CD2 
3406  N N   . ASP B 109 ? 0.0857 0.1124 0.2537 0.0149  -0.0413 -0.0113 109 ASP B N   
3407  C CA  . ASP B 109 ? 0.0959 0.1053 0.2546 0.0296  -0.0455 -0.0144 109 ASP B CA  
3408  C C   . ASP B 109 ? 0.0982 0.0744 0.2564 0.0191  -0.0496 -0.0069 109 ASP B C   
3409  O O   . ASP B 109 ? 0.1038 0.0680 0.2582 0.0227  -0.0494 -0.0051 109 ASP B O   
3410  C CB  . ASP B 109 ? 0.1294 0.1242 0.2585 0.0515  -0.0486 -0.0227 109 ASP B CB  
3411  C CG  . ASP B 109 ? 0.1292 0.1747 0.2622 0.0693  -0.0429 -0.0321 109 ASP B CG  
3412  O OD1 . ASP B 109 ? 0.1072 0.1973 0.2643 0.0658  -0.0392 -0.0336 109 ASP B OD1 
3413  O OD2 . ASP B 109 ? 0.1563 0.2008 0.2667 0.0870  -0.0424 -0.0396 109 ASP B OD2 
3414  N N   . PHE B 110 ? 0.0983 0.0659 0.2592 0.0060  -0.0532 -0.0026 110 PHE B N   
3415  C CA  . PHE B 110 ? 0.0986 0.0566 0.2679 -0.0072 -0.0564 0.0035  110 PHE B CA  
3416  C C   . PHE B 110 ? 0.0754 0.0524 0.2673 -0.0082 -0.0502 0.0085  110 PHE B C   
3417  O O   . PHE B 110 ? 0.0790 0.0526 0.2735 -0.0119 -0.0473 0.0119  110 PHE B O   
3418  C CB  . PHE B 110 ? 0.1026 0.0651 0.2747 -0.0172 -0.0640 0.0051  110 PHE B CB  
3419  C CG  . PHE B 110 ? 0.1012 0.0770 0.2910 -0.0316 -0.0681 0.0100  110 PHE B CG  
3420  C CD1 . PHE B 110 ? 0.1234 0.0832 0.3048 -0.0470 -0.0688 0.0104  110 PHE B CD1 
3421  C CD2 . PHE B 110 ? 0.0867 0.0924 0.2975 -0.0298 -0.0713 0.0143  110 PHE B CD2 
3422  C CE1 . PHE B 110 ? 0.1231 0.1119 0.3262 -0.0658 -0.0706 0.0145  110 PHE B CE1 
3423  C CE2 . PHE B 110 ? 0.0851 0.1224 0.3182 -0.0392 -0.0751 0.0172  110 PHE B CE2 
3424  C CZ  . PHE B 110 ? 0.0995 0.1360 0.3333 -0.0601 -0.0738 0.0170  110 PHE B CZ  
3425  N N   . HIS B 111 ? 0.0617 0.0525 0.2624 -0.0059 -0.0475 0.0088  111 HIS B N   
3426  C CA  . HIS B 111 ? 0.0533 0.0498 0.2639 -0.0041 -0.0428 0.0106  111 HIS B CA  
3427  C C   . HIS B 111 ? 0.0524 0.0497 0.2591 0.0007  -0.0390 0.0064  111 HIS B C   
3428  O O   . HIS B 111 ? 0.0527 0.0494 0.2620 0.0032  -0.0355 0.0080  111 HIS B O   
3429  C CB  . HIS B 111 ? 0.0588 0.0515 0.2642 -0.0068 -0.0415 0.0110  111 HIS B CB  
3430  C CG  . HIS B 111 ? 0.0700 0.0552 0.2718 -0.0049 -0.0463 0.0171  111 HIS B CG  
3431  N ND1 . HIS B 111 ? 0.0724 0.0629 0.2833 0.0047  -0.0491 0.0208  111 HIS B ND1 
3432  C CD2 . HIS B 111 ? 0.0846 0.0613 0.2718 -0.0079 -0.0492 0.0201  111 HIS B CD2 
3433  C CE1 . HIS B 111 ? 0.0882 0.0744 0.2908 0.0104  -0.0561 0.0254  111 HIS B CE1 
3434  N NE2 . HIS B 111 ? 0.0975 0.0699 0.2826 0.0017  -0.0563 0.0258  111 HIS B NE2 
3435  N N   . ASP B 112 ? 0.0556 0.0589 0.2540 0.0058  -0.0402 0.0005  112 ASP B N   
3436  C CA  . ASP B 112 ? 0.0603 0.0701 0.2521 0.0161  -0.0403 -0.0043 112 ASP B CA  
3437  C C   . ASP B 112 ? 0.0790 0.0621 0.2545 0.0222  -0.0405 0.0006  112 ASP B C   
3438  O O   . ASP B 112 ? 0.0856 0.0656 0.2544 0.0270  -0.0385 0.0015  112 ASP B O   
3439  C CB  . ASP B 112 ? 0.0644 0.0977 0.2519 0.0268  -0.0426 -0.0125 112 ASP B CB  
3440  C CG  . ASP B 112 ? 0.0682 0.1265 0.2542 0.0394  -0.0456 -0.0198 112 ASP B CG  
3441  O OD1 . ASP B 112 ? 0.0678 0.1207 0.2537 0.0364  -0.0458 -0.0189 112 ASP B OD1 
3442  O OD2 . ASP B 112 ? 0.0753 0.1635 0.2589 0.0555  -0.0484 -0.0276 112 ASP B OD2 
3443  N N   . SER B 113 ? 0.0960 0.0556 0.2593 0.0185  -0.0428 0.0038  113 SER B N   
3444  C CA  . SER B 113 ? 0.1282 0.0524 0.2683 0.0138  -0.0420 0.0101  113 SER B CA  
3445  C C   . SER B 113 ? 0.1196 0.0558 0.2761 -0.0013 -0.0344 0.0179  113 SER B C   
3446  O O   . SER B 113 ? 0.1430 0.0627 0.2817 -0.0028 -0.0290 0.0234  113 SER B O   
3447  C CB  . SER B 113 ? 0.1553 0.0495 0.2770 0.0047  -0.0475 0.0098  113 SER B CB  
3448  O OG  . SER B 113 ? 0.1925 0.0518 0.2928 -0.0135 -0.0459 0.0171  113 SER B OG  
3449  N N   . ASN B 114 ? 0.0936 0.0590 0.2795 -0.0092 -0.0335 0.0185  114 ASN B N   
3450  C CA  . ASN B 114 ? 0.0870 0.0768 0.2915 -0.0160 -0.0260 0.0238  114 ASN B CA  
3451  C C   . ASN B 114 ? 0.0853 0.0799 0.2864 -0.0035 -0.0188 0.0226  114 ASN B C   
3452  O O   . ASN B 114 ? 0.0964 0.0997 0.2960 -0.0069 -0.0094 0.0276  114 ASN B O   
3453  C CB  . ASN B 114 ? 0.0673 0.0864 0.2979 -0.0154 -0.0296 0.0231  114 ASN B CB  
3454  C CG  . ASN B 114 ? 0.0737 0.0967 0.3085 -0.0300 -0.0379 0.0240  114 ASN B CG  
3455  O OD1 . ASN B 114 ? 0.0965 0.1066 0.3199 -0.0482 -0.0383 0.0262  114 ASN B OD1 
3456  N ND2 . ASN B 114 ? 0.0639 0.0980 0.3076 -0.0239 -0.0454 0.0222  114 ASN B ND2 
3457  N N   . VAL B 115 ? 0.0769 0.0683 0.2747 0.0077  -0.0228 0.0154  115 VAL B N   
3458  C CA  . VAL B 115 ? 0.0831 0.0745 0.2717 0.0175  -0.0196 0.0110  115 VAL B CA  
3459  C C   . VAL B 115 ? 0.1067 0.0827 0.2699 0.0225  -0.0180 0.0135  115 VAL B C   
3460  O O   . VAL B 115 ? 0.1219 0.0968 0.2728 0.0270  -0.0110 0.0153  115 VAL B O   
3461  C CB  . VAL B 115 ? 0.0767 0.0701 0.2652 0.0193  -0.0263 0.0014  115 VAL B CB  
3462  C CG1 . VAL B 115 ? 0.0908 0.0824 0.2645 0.0255  -0.0267 -0.0057 115 VAL B CG1 
3463  C CG2 . VAL B 115 ? 0.0721 0.0636 0.2705 0.0146  -0.0270 0.0011  115 VAL B CG2 
3464  N N   . LYS B 116 ? 0.1190 0.0787 0.2673 0.0257  -0.0247 0.0135  116 LYS B N   
3465  C CA  . LYS B 116 ? 0.1566 0.0882 0.2683 0.0367  -0.0261 0.0169  116 LYS B CA  
3466  C C   . LYS B 116 ? 0.1881 0.0952 0.2805 0.0226  -0.0153 0.0296  116 LYS B C   
3467  O O   . LYS B 116 ? 0.2188 0.1096 0.2824 0.0283  -0.0101 0.0347  116 LYS B O   
3468  C CB  . LYS B 116 ? 0.1749 0.0865 0.2685 0.0479  -0.0355 0.0141  116 LYS B CB  
3469  C CG  . LYS B 116 ? 0.2002 0.1088 0.2668 0.0759  -0.0444 0.0084  116 LYS B CG  
3470  C CD  . LYS B 116 ? 0.2551 0.1164 0.2730 0.0845  -0.0423 0.0183  116 LYS B CD  
3471  C CE  . LYS B 116 ? 0.2785 0.1488 0.2720 0.1177  -0.0537 0.0116  116 LYS B CE  
3472  N NZ  . LYS B 116 ? 0.3088 0.1655 0.2786 0.1468  -0.0651 0.0062  116 LYS B NZ  
3473  N N   . ASN B 117 ? 0.1858 0.0935 0.2922 0.0016  -0.0119 0.0347  117 ASN B N   
3474  C CA  . ASN B 117 ? 0.2195 0.1141 0.3118 -0.0220 -0.0009 0.0465  117 ASN B CA  
3475  C C   . ASN B 117 ? 0.2072 0.1427 0.3183 -0.0247 0.0134  0.0497  117 ASN B C   
3476  O O   . ASN B 117 ? 0.2447 0.1699 0.3316 -0.0365 0.0262  0.0596  117 ASN B O   
3477  C CB  . ASN B 117 ? 0.2192 0.1175 0.3272 -0.0473 -0.0039 0.0479  117 ASN B CB  
3478  C CG  . ASN B 117 ? 0.2532 0.0964 0.3264 -0.0445 -0.0161 0.0448  117 ASN B CG  
3479  O OD1 . ASN B 117 ? 0.2903 0.0870 0.3205 -0.0245 -0.0204 0.0447  117 ASN B OD1 
3480  N ND2 . ASN B 117 ? 0.2479 0.0960 0.3350 -0.0605 -0.0230 0.0413  117 ASN B ND2 
3481  N N   . LEU B 118 ? 0.1650 0.1416 0.3120 -0.0123 0.0122  0.0412  118 LEU B N   
3482  C CA  . LEU B 118 ? 0.1601 0.1711 0.3186 -0.0041 0.0245  0.0405  118 LEU B CA  
3483  C C   . LEU B 118 ? 0.1838 0.1721 0.3075 0.0122  0.0270  0.0385  118 LEU B C   
3484  O O   . LEU B 118 ? 0.2058 0.2052 0.3162 0.0133  0.0414  0.0431  118 LEU B O   
3485  C CB  . LEU B 118 ? 0.1274 0.1662 0.3167 0.0104  0.0193  0.0310  118 LEU B CB  
3486  C CG  . LEU B 118 ? 0.1319 0.1988 0.3266 0.0283  0.0300  0.0270  118 LEU B CG  
3487  C CD1 . LEU B 118 ? 0.1431 0.2563 0.3515 0.0175  0.0471  0.0356  118 LEU B CD1 
3488  C CD2 . LEU B 118 ? 0.1174 0.1910 0.3288 0.0447  0.0219  0.0189  118 LEU B CD2 
3489  N N   . TYR B 119 ? 0.1822 0.1458 0.2911 0.0253  0.0129  0.0310  119 TYR B N   
3490  C CA  . TYR B 119 ? 0.2074 0.1549 0.2828 0.0417  0.0103  0.0272  119 TYR B CA  
3491  C C   . TYR B 119 ? 0.2581 0.1723 0.2893 0.0386  0.0176  0.0406  119 TYR B C   
3492  O O   . TYR B 119 ? 0.2880 0.1979 0.2912 0.0455  0.0264  0.0435  119 TYR B O   
3493  C CB  . TYR B 119 ? 0.1961 0.1403 0.2706 0.0539  -0.0078 0.0158  119 TYR B CB  
3494  C CG  . TYR B 119 ? 0.2251 0.1614 0.2658 0.0715  -0.0150 0.0104  119 TYR B CG  
3495  C CD1 . TYR B 119 ? 0.2278 0.1766 0.2651 0.0769  -0.0157 -0.0006 119 TYR B CD1 
3496  C CD2 . TYR B 119 ? 0.2597 0.1715 0.2648 0.0858  -0.0231 0.0152  119 TYR B CD2 
3497  C CE1 . TYR B 119 ? 0.2580 0.2035 0.2626 0.0921  -0.0252 -0.0074 119 TYR B CE1 
3498  C CE2 . TYR B 119 ? 0.2906 0.2006 0.2626 0.1062  -0.0327 0.0098  119 TYR B CE2 
3499  C CZ  . TYR B 119 ? 0.2865 0.2177 0.2611 0.1073  -0.0341 -0.0018 119 TYR B CZ  
3500  O OH  . TYR B 119 ? 0.3200 0.2535 0.2608 0.1261  -0.0463 -0.0090 119 TYR B OH  
3501  N N   . ASP B 120 ? 0.2791 0.1609 0.2951 0.0283  0.0139  0.0488  120 ASP B N   
3502  C CA  . ASP B 120 ? 0.3463 0.1756 0.3059 0.0227  0.0199  0.0634  120 ASP B CA  
3503  C C   . ASP B 120 ? 0.3684 0.2106 0.3258 -0.0051 0.0429  0.0765  120 ASP B C   
3504  O O   . ASP B 120 ? 0.4244 0.2370 0.3335 -0.0073 0.0538  0.0880  120 ASP B O   
3505  C CB  . ASP B 120 ? 0.3770 0.1561 0.3128 0.0173  0.0100  0.0674  120 ASP B CB  
3506  C CG  . ASP B 120 ? 0.3715 0.1417 0.2990 0.0513  -0.0102 0.0555  120 ASP B CG  
3507  O OD1 . ASP B 120 ? 0.3753 0.1567 0.2898 0.0779  -0.0177 0.0494  120 ASP B OD1 
3508  O OD2 . ASP B 120 ? 0.3679 0.1252 0.3010 0.0517  -0.0188 0.0513  120 ASP B OD2 
3509  N N   . LYS B 121 ? 0.3291 0.2209 0.3376 -0.0254 0.0503  0.0749  121 LYS B N   
3510  C CA  . LYS B 121 ? 0.3422 0.2739 0.3631 -0.0517 0.0729  0.0846  121 LYS B CA  
3511  C C   . LYS B 121 ? 0.3546 0.3076 0.3604 -0.0335 0.0872  0.0843  121 LYS B C   
3512  O O   . LYS B 121 ? 0.4034 0.3539 0.3787 -0.0506 0.1069  0.0976  121 LYS B O   
3513  C CB  . LYS B 121 ? 0.2880 0.2880 0.3743 -0.0608 0.0731  0.0775  121 LYS B CB  
3514  C CG  . LYS B 121 ? 0.2967 0.3608 0.4086 -0.0887 0.0943  0.0854  121 LYS B CG  
3515  C CD  . LYS B 121 ? 0.2441 0.3790 0.4197 -0.0861 0.0884  0.0760  121 LYS B CD  
3516  C CE  . LYS B 121 ? 0.2542 0.4620 0.4624 -0.1230 0.1032  0.0831  121 LYS B CE  
3517  N NZ  . LYS B 121 ? 0.2554 0.5408 0.4828 -0.1111 0.1264  0.0835  121 LYS B NZ  
3518  N N   . VAL B 122 ? 0.3193 0.2888 0.3408 -0.0014 0.0775  0.0689  122 VAL B N   
3519  C CA  . VAL B 122 ? 0.3369 0.3166 0.3364 0.0204  0.0866  0.0640  122 VAL B CA  
3520  C C   . VAL B 122 ? 0.3937 0.3169 0.3276 0.0289  0.0833  0.0711  122 VAL B C   
3521  O O   . VAL B 122 ? 0.4402 0.3601 0.3364 0.0278  0.1010  0.0801  122 VAL B O   
3522  C CB  . VAL B 122 ? 0.2986 0.2939 0.3217 0.0475  0.0732  0.0439  122 VAL B CB  
3523  C CG1 . VAL B 122 ? 0.3296 0.3172 0.3159 0.0711  0.0766  0.0352  122 VAL B CG1 
3524  C CG2 . VAL B 122 ? 0.2625 0.3086 0.3362 0.0471  0.0792  0.0390  122 VAL B CG2 
3525  N N   . ARG B 123 ? 0.3954 0.2781 0.3131 0.0402  0.0611  0.0673  123 ARG B N   
3526  C CA  . ARG B 123 ? 0.4540 0.2845 0.3072 0.0571  0.0528  0.0729  123 ARG B CA  
3527  C C   . ARG B 123 ? 0.5289 0.3150 0.3267 0.0362  0.0714  0.0961  123 ARG B C   
3528  O O   . ARG B 123 ? 0.5869 0.3458 0.3275 0.0472  0.0780  0.1038  123 ARG B O   
3529  C CB  . ARG B 123 ? 0.4472 0.2507 0.2969 0.0725  0.0275  0.0667  123 ARG B CB  
3530  C CG  . ARG B 123 ? 0.5032 0.2667 0.2914 0.1027  0.0125  0.0675  123 ARG B CG  
3531  C CD  . ARG B 123 ? 0.4981 0.2495 0.2875 0.1235  -0.0111 0.0600  123 ARG B CD  
3532  N NE  . ARG B 123 ? 0.5066 0.2235 0.2975 0.1057  -0.0077 0.0692  123 ARG B NE  
3533  C CZ  . ARG B 123 ? 0.5843 0.2261 0.3132 0.0973  -0.0015 0.0873  123 ARG B CZ  
3534  N NH1 . ARG B 123 ? 0.6626 0.2534 0.3200 0.1059  0.0039  0.1012  123 ARG B NH1 
3535  N NH2 . ARG B 123 ? 0.5936 0.2036 0.3247 0.0778  -0.0008 0.0916  123 ARG B NH2 
3536  N N   . LEU B 124 ? 0.5359 0.3116 0.3459 0.0028  0.0795  0.1071  124 LEU B N   
3537  C CA  . LEU B 124 ? 0.6191 0.3434 0.3725 -0.0293 0.0974  0.1301  124 LEU B CA  
3538  C C   . LEU B 124 ? 0.6401 0.4094 0.3922 -0.0505 0.1285  0.1400  124 LEU B C   
3539  O O   . LEU B 124 ? 0.7238 0.4465 0.4109 -0.0710 0.1454  0.1599  124 LEU B O   
3540  C CB  . LEU B 124 ? 0.6235 0.3279 0.3920 -0.0659 0.0958  0.1357  124 LEU B CB  
3541  C CG  . LEU B 124 ? 0.6342 0.2756 0.3808 -0.0457 0.0691  0.1296  124 LEU B CG  
3542  C CD1 . LEU B 124 ? 0.6146 0.2592 0.3956 -0.0776 0.0653  0.1272  124 LEU B CD1 
3543  C CD2 . LEU B 124 ? 0.7428 0.2770 0.3885 -0.0332 0.0638  0.1443  124 LEU B CD2 
3544  N N   . GLN B 125 ? 0.5740 0.4308 0.3920 -0.0440 0.1368  0.1265  125 GLN B N   
3545  C CA  . GLN B 125 ? 0.5907 0.5046 0.4113 -0.0521 0.1665  0.1315  125 GLN B CA  
3546  C C   . GLN B 125 ? 0.6300 0.5193 0.3951 -0.0182 0.1680  0.1292  125 GLN B C   
3547  O O   . GLN B 125 ? 0.6977 0.5744 0.4102 -0.0302 0.1910  0.1449  125 GLN B O   
3548  C CB  . GLN B 125 ? 0.5171 0.5262 0.4171 -0.0423 0.1715  0.1151  125 GLN B CB  
3549  C CG  . GLN B 125 ? 0.4831 0.5399 0.4417 -0.0762 0.1737  0.1173  125 GLN B CG  
3550  C CD  . GLN B 125 ? 0.4219 0.5708 0.4498 -0.0559 0.1770  0.1014  125 GLN B CD  
3551  O OE1 . GLN B 125 ? 0.4323 0.6480 0.4714 -0.0493 0.2006  0.1009  125 GLN B OE1 
3552  N NE2 . GLN B 125 ? 0.3666 0.5179 0.4357 -0.0421 0.1539  0.0884  125 GLN B NE2 
3553  N N   . LEU B 126 ? 0.5932 0.4773 0.3678 0.0208  0.1436  0.1092  126 LEU B N   
3554  C CA  . LEU B 126 ? 0.6264 0.4960 0.3540 0.0538  0.1404  0.1013  126 LEU B CA  
3555  C C   . LEU B 126 ? 0.7089 0.5010 0.3514 0.0597  0.1339  0.1168  126 LEU B C   
3556  O O   . LEU B 126 ? 0.7672 0.5456 0.3526 0.0716  0.1454  0.1222  126 LEU B O   
3557  C CB  . LEU B 126 ? 0.5725 0.4556 0.3312 0.0851  0.1135  0.0746  126 LEU B CB  
3558  C CG  . LEU B 126 ? 0.5077 0.4490 0.3353 0.0868  0.1166  0.0587  126 LEU B CG  
3559  C CD1 . LEU B 126 ? 0.4865 0.4239 0.3191 0.1140  0.0940  0.0337  126 LEU B CD1 
3560  C CD2 . LEU B 126 ? 0.5216 0.5158 0.3577 0.0833  0.1487  0.0629  126 LEU B CD2 
3561  N N   . ARG B 127 ? 0.7239 0.4619 0.3512 0.0552  0.1154  0.1240  127 ARG B N   
3562  C CA  . ARG B 127 ? 0.8152 0.4685 0.3528 0.0686  0.1057  0.1393  127 ARG B CA  
3563  C C   . ARG B 127 ? 0.8338 0.4864 0.3353 0.1127  0.0876  0.1257  127 ARG B C   
3564  O O   . ARG B 127 ? 0.7704 0.4642 0.3190 0.1343  0.0652  0.1015  127 ARG B O   
3565  C CB  . ARG B 127 ? 0.9058 0.5136 0.3806 0.0321  0.1364  0.1688  127 ARG B CB  
3566  C CG  . ARG B 127 ? 0.9126 0.4963 0.4040 -0.0126 0.1438  0.1817  127 ARG B CG  
3567  C CD  . ARG B 127 ? 0.9429 0.5571 0.4386 -0.0678 0.1819  0.1998  127 ARG B CD  
3568  N NE  . ARG B 127 ? 1.0548 0.6191 0.4605 -0.0880 0.2082  0.2254  127 ARG B NE  
3569  C CZ  . ARG B 127 ? 1.1641 0.6181 0.4617 -0.0739 0.2009  0.2428  127 ARG B CZ  
3570  N NH1 . ARG B 127 ? 1.1821 0.5630 0.4432 -0.0330 0.1659  0.2369  127 ARG B NH1 
3571  N NH2 . ARG B 127 ? 1.2661 0.6838 0.4856 -0.0998 0.2303  0.2676  127 ARG B NH2 
3572  N N   . ASP B 128 ? 0.9243 0.5320 0.3411 0.1227  0.0966  0.1404  128 ASP B N   
3573  C CA  . ASP B 128 ? 0.9516 0.5574 0.3266 0.1647  0.0761  0.1268  128 ASP B CA  
3574  C C   . ASP B 128 ? 0.9363 0.5961 0.3224 0.1685  0.0925  0.1132  128 ASP B C   
3575  O O   . ASP B 128 ? 0.9803 0.6311 0.3146 0.1975  0.0813  0.1048  128 ASP B O   
3576  C CB  . ASP B 128 ? 1.0708 0.5893 0.3345 0.1837  0.0708  0.1488  128 ASP B CB  
3577  C CG  . ASP B 128 ? 1.1561 0.6371 0.3542 0.1543  0.1094  0.1770  128 ASP B CG  
3578  O OD1 . ASP B 128 ? 1.1185 0.6518 0.3659 0.1178  0.1409  0.1793  128 ASP B OD1 
3579  O OD2 . ASP B 128 ? 1.2678 0.6697 0.3622 0.1686  0.1085  0.1971  128 ASP B OD2 
3580  N N   . ASN B 129 ? 0.8816 0.5970 0.3304 0.1434  0.1174  0.1095  129 ASN B N   
3581  C CA  . ASN B 129 ? 0.8688 0.6353 0.3300 0.1541  0.1326  0.0931  129 ASN B CA  
3582  C C   . ASN B 129 ? 0.8011 0.6021 0.3151 0.1742  0.1069  0.0602  129 ASN B C   
3583  O O   . ASN B 129 ? 0.7991 0.6294 0.3170 0.1870  0.1158  0.0431  129 ASN B O   
3584  C CB  . ASN B 129 ? 0.8540 0.6715 0.3530 0.1248  0.1721  0.1038  129 ASN B CB  
3585  C CG  . ASN B 129 ? 0.9422 0.7392 0.3743 0.1038  0.2061  0.1322  129 ASN B CG  
3586  O OD1 . ASN B 129 ? 1.0209 0.7466 0.3727 0.1073  0.2000  0.1493  129 ASN B OD1 
3587  N ND2 . ASN B 129 ? 0.9366 0.7988 0.3989 0.0825  0.2428  0.1378  129 ASN B ND2 
3588  N N   . ALA B 130 ? 0.7559 0.5499 0.3036 0.1766  0.0762  0.0512  130 ALA B N   
3589  C CA  . ALA B 130 ? 0.7034 0.5239 0.2939 0.1874  0.0508  0.0219  130 ALA B CA  
3590  C C   . ALA B 130 ? 0.6932 0.5033 0.2849 0.1978  0.0151  0.0146  130 ALA B C   
3591  O O   . ALA B 130 ? 0.7059 0.4908 0.2856 0.1971  0.0107  0.0317  130 ALA B O   
3592  C CB  . ALA B 130 ? 0.6328 0.4889 0.2990 0.1695  0.0603  0.0161  130 ALA B CB  
3593  N N   . LYS B 131 ? 0.6778 0.5084 0.2812 0.2073  -0.0102 -0.0118 131 LYS B N   
3594  C CA  . LYS B 131 ? 0.6616 0.5077 0.2791 0.2155  -0.0442 -0.0231 131 LYS B CA  
3595  C C   . LYS B 131 ? 0.5869 0.4593 0.2790 0.1956  -0.0482 -0.0269 131 LYS B C   
3596  O O   . LYS B 131 ? 0.5489 0.4366 0.2808 0.1789  -0.0423 -0.0390 131 LYS B O   
3597  C CB  . LYS B 131 ? 0.6808 0.5474 0.2830 0.2237  -0.0697 -0.0516 131 LYS B CB  
3598  C CG  . LYS B 131 ? 0.7600 0.6034 0.2834 0.2463  -0.0714 -0.0529 131 LYS B CG  
3599  C CD  . LYS B 131 ? 0.7792 0.6381 0.2913 0.2448  -0.0923 -0.0854 131 LYS B CD  
3600  C CE  . LYS B 131 ? 0.8573 0.7072 0.2935 0.2709  -0.1112 -0.0925 131 LYS B CE  
3601  N NZ  . LYS B 131 ? 0.8656 0.7427 0.2976 0.2894  -0.1430 -0.0909 131 LYS B NZ  
3602  N N   . GLU B 132 ? 0.5753 0.4470 0.2783 0.2009  -0.0584 -0.0168 132 GLU B N   
3603  C CA  . GLU B 132 ? 0.5112 0.4111 0.2788 0.1856  -0.0645 -0.0220 132 GLU B CA  
3604  C C   . GLU B 132 ? 0.4917 0.4410 0.2850 0.1864  -0.0926 -0.0472 132 GLU B C   
3605  O O   . GLU B 132 ? 0.5117 0.4831 0.2902 0.2081  -0.1149 -0.0521 132 GLU B O   
3606  C CB  . GLU B 132 ? 0.5185 0.3947 0.2793 0.1941  -0.0643 -0.0036 132 GLU B CB  
3607  C CG  . GLU B 132 ? 0.4579 0.3597 0.2796 0.1796  -0.0672 -0.0076 132 GLU B CG  
3608  C CD  . GLU B 132 ? 0.4755 0.3380 0.2821 0.1850  -0.0625 0.0104  132 GLU B CD  
3609  O OE1 . GLU B 132 ? 0.5422 0.3580 0.2866 0.2070  -0.0655 0.0234  132 GLU B OE1 
3610  O OE2 . GLU B 132 ? 0.4325 0.3031 0.2820 0.1673  -0.0567 0.0114  132 GLU B OE2 
3611  N N   . LEU B 133 ? 0.4607 0.4276 0.2892 0.1624  -0.0916 -0.0633 133 LEU B N   
3612  C CA  . LEU B 133 ? 0.4565 0.4659 0.3024 0.1508  -0.1160 -0.0886 133 LEU B CA  
3613  C C   . LEU B 133 ? 0.4173 0.4802 0.3114 0.1445  -0.1308 -0.0935 133 LEU B C   
3614  O O   . LEU B 133 ? 0.4229 0.5390 0.3271 0.1405  -0.1541 -0.1122 133 LEU B O   
3615  C CB  . LEU B 133 ? 0.4546 0.4461 0.3084 0.1245  -0.1093 -0.1030 133 LEU B CB  
3616  C CG  . LEU B 133 ? 0.5126 0.4756 0.3130 0.1303  -0.1119 -0.1172 133 LEU B CG  
3617  C CD1 . LEU B 133 ? 0.5538 0.4958 0.3020 0.1610  -0.1034 -0.1033 133 LEU B CD1 
3618  C CD2 . LEU B 133 ? 0.5196 0.4411 0.3174 0.1178  -0.0950 -0.1228 133 LEU B CD2 
3619  N N   . GLY B 134 ? 0.3819 0.4369 0.3050 0.1429  -0.1174 -0.0780 134 GLY B N   
3620  C CA  . GLY B 134 ? 0.3482 0.4528 0.3136 0.1407  -0.1273 -0.0818 134 GLY B CA  
3621  C C   . GLY B 134 ? 0.3067 0.4261 0.3196 0.1046  -0.1200 -0.0880 134 GLY B C   
3622  O O   . GLY B 134 ? 0.2785 0.4423 0.3272 0.0990  -0.1246 -0.0910 134 GLY B O   
3623  N N   . ASN B 135 ? 0.3115 0.3911 0.3187 0.0837  -0.1080 -0.0893 135 ASN B N   
3624  C CA  . ASN B 135 ? 0.2913 0.3687 0.3277 0.0509  -0.1028 -0.0949 135 ASN B CA  
3625  C C   . ASN B 135 ? 0.2738 0.3037 0.3149 0.0492  -0.0816 -0.0800 135 ASN B C   
3626  O O   . ASN B 135 ? 0.2705 0.2821 0.3219 0.0283  -0.0768 -0.0830 135 ASN B O   
3627  C CB  . ASN B 135 ? 0.3313 0.4006 0.3483 0.0269  -0.1133 -0.1153 135 ASN B CB  
3628  C CG  . ASN B 135 ? 0.3759 0.3924 0.3460 0.0417  -0.1073 -0.1170 135 ASN B CG  
3629  O OD1 . ASN B 135 ? 0.3729 0.3653 0.3302 0.0659  -0.0921 -0.1013 135 ASN B OD1 
3630  N ND2 . ASN B 135 ? 0.4271 0.4262 0.3679 0.0250  -0.1186 -0.1368 135 ASN B ND2 
3631  N N   . GLY B 136 ? 0.2698 0.2803 0.2999 0.0702  -0.0697 -0.0637 136 GLY B N   
3632  C CA  . GLY B 136 ? 0.2567 0.2380 0.2937 0.0690  -0.0505 -0.0508 136 GLY B CA  
3633  C C   . GLY B 136 ? 0.2880 0.2429 0.2936 0.0801  -0.0390 -0.0506 136 GLY B C   
3634  O O   . GLY B 136 ? 0.2814 0.2272 0.2935 0.0835  -0.0220 -0.0401 136 GLY B O   
3635  N N   . CYS B 137 ? 0.3243 0.2742 0.2960 0.0866  -0.0483 -0.0635 137 CYS B N   
3636  C CA  . CYS B 137 ? 0.3637 0.2886 0.2979 0.1005  -0.0371 -0.0662 137 CYS B CA  
3637  C C   . CYS B 137 ? 0.3906 0.3148 0.2900 0.1185  -0.0324 -0.0562 137 CYS B C   
3638  O O   . CYS B 137 ? 0.3952 0.3311 0.2857 0.1242  -0.0462 -0.0540 137 CYS B O   
3639  C CB  . CYS B 137 ? 0.4041 0.3090 0.3101 0.0945  -0.0503 -0.0895 137 CYS B CB  
3640  S SG  . CYS B 137 ? 0.4000 0.2815 0.3255 0.0700  -0.0546 -0.0997 137 CYS B SG  
3641  N N   . PHE B 138 ? 0.4151 0.3263 0.2912 0.1298  -0.0118 -0.0496 138 PHE B N   
3642  C CA  . PHE B 138 ? 0.4562 0.3588 0.2871 0.1443  -0.0027 -0.0391 138 PHE B CA  
3643  C C   . PHE B 138 ? 0.5060 0.3940 0.2931 0.1591  0.0018  -0.0536 138 PHE B C   
3644  O O   . PHE B 138 ? 0.5093 0.3955 0.3022 0.1637  0.0168  -0.0587 138 PHE B O   
3645  C CB  . PHE B 138 ? 0.4487 0.3559 0.2892 0.1389  0.0230  -0.0154 138 PHE B CB  
3646  C CG  . PHE B 138 ? 0.4151 0.3237 0.2855 0.1248  0.0185  -0.0016 138 PHE B CG  
3647  C CD1 . PHE B 138 ? 0.4430 0.3290 0.2808 0.1300  0.0107  0.0100  138 PHE B CD1 
3648  C CD2 . PHE B 138 ? 0.3655 0.2914 0.2884 0.1101  0.0208  -0.0010 138 PHE B CD2 
3649  C CE1 . PHE B 138 ? 0.4252 0.3019 0.2806 0.1212  0.0061  0.0205  138 PHE B CE1 
3650  C CE2 . PHE B 138 ? 0.3421 0.2650 0.2860 0.0983  0.0161  0.0096  138 PHE B CE2 
3651  C CZ  . PHE B 138 ? 0.3732 0.2696 0.2826 0.1040  0.0090  0.0195  138 PHE B CZ  
3652  N N   . GLU B 139 ? 0.5513 0.4288 0.2904 0.1706  -0.0121 -0.0613 139 GLU B N   
3653  C CA  . GLU B 139 ? 0.6097 0.4681 0.2963 0.1860  -0.0105 -0.0776 139 GLU B CA  
3654  C C   . GLU B 139 ? 0.6546 0.5070 0.2940 0.2024  0.0123  -0.0602 139 GLU B C   
3655  O O   . GLU B 139 ? 0.6751 0.5215 0.2870 0.2068  0.0069  -0.0461 139 GLU B O   
3656  C CB  . GLU B 139 ? 0.6381 0.4933 0.2989 0.1849  -0.0436 -0.0998 139 GLU B CB  
3657  C CG  . GLU B 139 ? 0.7090 0.5368 0.3074 0.1985  -0.0475 -0.1210 139 GLU B CG  
3658  C CD  . GLU B 139 ? 0.7402 0.5751 0.3142 0.1930  -0.0834 -0.1426 139 GLU B CD  
3659  O OE1 . GLU B 139 ? 0.7135 0.5645 0.3245 0.1679  -0.1043 -0.1567 139 GLU B OE1 
3660  O OE2 . GLU B 139 ? 0.7947 0.6246 0.3122 0.2121  -0.0908 -0.1450 139 GLU B OE2 
3661  N N   . PHE B 140 ? 0.6786 0.5316 0.3034 0.2133  0.0384  -0.0611 140 PHE B N   
3662  C CA  . PHE B 140 ? 0.7201 0.5787 0.3067 0.2226  0.0680  -0.0421 140 PHE B CA  
3663  C C   . PHE B 140 ? 0.7971 0.6300 0.3040 0.2425  0.0616  -0.0495 140 PHE B C   
3664  O O   . PHE B 140 ? 0.8271 0.6420 0.3057 0.2543  0.0420  -0.0761 140 PHE B O   
3665  C CB  . PHE B 140 ? 0.7177 0.6046 0.3225 0.2307  0.0999  -0.0422 140 PHE B CB  
3666  C CG  . PHE B 140 ? 0.6504 0.5706 0.3288 0.2128  0.1088  -0.0312 140 PHE B CG  
3667  C CD1 . PHE B 140 ? 0.6129 0.5298 0.3315 0.2133  0.0936  -0.0473 140 PHE B CD1 
3668  C CD2 . PHE B 140 ? 0.6345 0.5847 0.3354 0.1927  0.1315  -0.0047 140 PHE B CD2 
3669  C CE1 . PHE B 140 ? 0.5564 0.5041 0.3378 0.1996  0.0999  -0.0374 140 PHE B CE1 
3670  C CE2 . PHE B 140 ? 0.5771 0.5611 0.3440 0.1748  0.1368  0.0033  140 PHE B CE2 
3671  C CZ  . PHE B 140 ? 0.5360 0.5211 0.3438 0.1811  0.1205  -0.0131 140 PHE B CZ  
3672  N N   . TYR B 141 ? 0.8393 0.6647 0.3033 0.2440  0.0775  -0.0258 141 TYR B N   
3673  C CA  . TYR B 141 ? 0.9237 0.7242 0.3025 0.2657  0.0766  -0.0290 141 TYR B CA  
3674  C C   . TYR B 141 ? 0.9656 0.7788 0.3155 0.2817  0.1079  -0.0369 141 TYR B C   
3675  O O   . TYR B 141 ? 1.0269 0.8199 0.3162 0.3045  0.1004  -0.0566 141 TYR B O   
3676  C CB  . TYR B 141 ? 0.9692 0.7452 0.2994 0.2626  0.0841  0.0018  141 TYR B CB  
3677  C CG  . TYR B 141 ? 0.9489 0.7074 0.2909 0.2603  0.0504  0.0064  141 TYR B CG  
3678  C CD1 . TYR B 141 ? 0.9593 0.7158 0.2853 0.2777  0.0104  -0.0161 141 TYR B CD1 
3679  C CD2 . TYR B 141 ? 0.9243 0.6727 0.2931 0.2414  0.0577  0.0313  141 TYR B CD2 
3680  C CE1 . TYR B 141 ? 0.9415 0.6976 0.2822 0.2815  -0.0196 -0.0136 141 TYR B CE1 
3681  C CE2 . TYR B 141 ? 0.9130 0.6454 0.2881 0.2472  0.0275  0.0336  141 TYR B CE2 
3682  C CZ  . TYR B 141 ? 0.9195 0.6614 0.2830 0.2698  -0.0103 0.0113  141 TYR B CZ  
3683  O OH  . TYR B 141 ? 0.9098 0.6508 0.2829 0.2813  -0.0395 0.0122  141 TYR B OH  
3684  N N   . HIS B 142 ? 0.9370 0.7887 0.3297 0.2713  0.1422  -0.0227 142 HIS B N   
3685  C CA  . HIS B 142 ? 0.9692 0.8516 0.3482 0.2912  0.1747  -0.0311 142 HIS B CA  
3686  C C   . HIS B 142 ? 0.9348 0.8250 0.3574 0.3054  0.1650  -0.0583 142 HIS B C   
3687  O O   . HIS B 142 ? 0.8721 0.7590 0.3524 0.2891  0.1438  -0.0616 142 HIS B O   
3688  C CB  . HIS B 142 ? 0.9631 0.8988 0.3666 0.2723  0.2179  -0.0019 142 HIS B CB  
3689  C CG  . HIS B 142 ? 0.8842 0.8497 0.3715 0.2414  0.2175  0.0119  142 HIS B CG  
3690  N ND1 . HIS B 142 ? 0.8350 0.8556 0.3891 0.2445  0.2298  0.0041  142 HIS B ND1 
3691  C CD2 . HIS B 142 ? 0.8542 0.7988 0.3632 0.2104  0.2047  0.0319  142 HIS B CD2 
3692  C CE1 . HIS B 142 ? 0.7745 0.8099 0.3897 0.2131  0.2242  0.0188  142 HIS B CE1 
3693  N NE2 . HIS B 142 ? 0.7860 0.7733 0.3741 0.1915  0.2097  0.0352  142 HIS B NE2 
3694  N N   . LYS B 143 ? 0.9870 0.8815 0.3734 0.3383  0.1812  -0.0774 143 LYS B N   
3695  C CA  . LYS B 143 ? 0.9765 0.8689 0.3893 0.3593  0.1770  -0.1013 143 LYS B CA  
3696  C C   . LYS B 143 ? 0.9120 0.8727 0.4052 0.3496  0.2006  -0.0835 143 LYS B C   
3697  O O   . LYS B 143 ? 0.9150 0.9387 0.4193 0.3463  0.2360  -0.0638 143 LYS B O   
3698  C CB  . LYS B 143 ? 1.0629 0.9415 0.4066 0.4042  0.1923  -0.1251 143 LYS B CB  
3699  C CG  . LYS B 143 ? 1.0854 0.9243 0.4238 0.4326  0.1785  -0.1558 143 LYS B CG  
3700  C CD  . LYS B 143 ? 1.1857 1.0047 0.4442 0.4831  0.1953  -0.1801 143 LYS B CD  
3701  C CE  . LYS B 143 ? 1.2144 1.0113 0.4724 0.5229  0.1962  -0.2031 143 LYS B CE  
3702  N NZ  . LYS B 143 ? 1.1652 1.0569 0.4935 0.5393  0.2292  -0.1861 143 LYS B NZ  
3703  N N   . CYS B 144 ? 0.8591 0.8103 0.4062 0.3416  0.1806  -0.0902 144 CYS B N   
3704  C CA  . CYS B 144 ? 0.7952 0.8099 0.4205 0.3300  0.1955  -0.0743 144 CYS B CA  
3705  C C   . CYS B 144 ? 0.8043 0.8224 0.4431 0.3672  0.1958  -0.0946 144 CYS B C   
3706  O O   . CYS B 144 ? 0.7955 0.7582 0.4385 0.3674  0.1680  -0.1088 144 CYS B O   
3707  C CB  . CYS B 144 ? 0.7266 0.7278 0.4021 0.2885  0.1719  -0.0600 144 CYS B CB  
3708  S SG  . CYS B 144 ? 0.6524 0.7287 0.4180 0.2634  0.1872  -0.0374 144 CYS B SG  
3709  N N   . ASP B 145 ? 0.8307 0.9141 0.4714 0.4003  0.2281  -0.0956 145 ASP B N   
3710  C CA  . ASP B 145 ? 0.8531 0.9447 0.4994 0.4482  0.2304  -0.1146 145 ASP B CA  
3711  C C   . ASP B 145 ? 0.7798 0.9171 0.5082 0.4338  0.2242  -0.1026 145 ASP B C   
3712  O O   . ASP B 145 ? 0.7133 0.8700 0.4910 0.3850  0.2178  -0.0817 145 ASP B O   
3713  C CB  . ASP B 145 ? 0.9097 1.0701 0.5311 0.4957  0.2678  -0.1214 145 ASP B CB  
3714  C CG  . ASP B 145 ? 0.8654 1.1543 0.5492 0.4727  0.3039  -0.0948 145 ASP B CG  
3715  O OD1 . ASP B 145 ? 0.7951 1.1119 0.5389 0.4216  0.2987  -0.0721 145 ASP B OD1 
3716  O OD2 . ASP B 145 ? 0.9083 1.2715 0.5779 0.5042  0.3386  -0.0975 145 ASP B OD2 
3717  N N   . ASN B 146 ? 0.8009 0.9505 0.5370 0.4800  0.2248  -0.1166 146 ASN B N   
3718  C CA  . ASN B 146 ? 0.7422 0.9306 0.5477 0.4735  0.2154  -0.1075 146 ASN B CA  
3719  C C   . ASN B 146 ? 0.6790 0.9981 0.5640 0.4464  0.2398  -0.0838 146 ASN B C   
3720  O O   . ASN B 146 ? 0.6174 0.9622 0.5618 0.4168  0.2279  -0.0710 146 ASN B O   
3721  C CB  . ASN B 146 ? 0.7966 0.9622 0.5788 0.5384  0.2094  -0.1281 146 ASN B CB  
3722  C CG  . ASN B 146 ? 0.8640 0.8819 0.5678 0.5513  0.1798  -0.1498 146 ASN B CG  
3723  O OD1 . ASN B 146 ? 0.8520 0.7989 0.5368 0.5059  0.1599  -0.1488 146 ASN B OD1 
3724  N ND2 . ASN B 146 ? 0.9438 0.9154 0.5986 0.6136  0.1761  -0.1701 146 ASN B ND2 
3725  N N   . GLU B 147 ? 0.7020 1.1024 0.5844 0.4524  0.2740  -0.0783 147 GLU B N   
3726  C CA  . GLU B 147 ? 0.6549 1.1756 0.6045 0.4120  0.2993  -0.0545 147 GLU B CA  
3727  C C   . GLU B 147 ? 0.6201 1.0978 0.5720 0.3418  0.2915  -0.0322 147 GLU B C   
3728  O O   . GLU B 147 ? 0.5672 1.0874 0.5759 0.2963  0.2899  -0.0142 147 GLU B O   
3729  C CB  . GLU B 147 ? 0.7000 1.3206 0.6393 0.4342  0.3416  -0.0542 147 GLU B CB  
3730  C CG  . GLU B 147 ? 0.7459 1.4220 0.6795 0.5134  0.3531  -0.0775 147 GLU B CG  
3731  C CD  . GLU B 147 ? 0.8316 1.4059 0.6692 0.5687  0.3480  -0.1029 147 GLU B CD  
3732  O OE1 . GLU B 147 ? 0.8473 1.2926 0.6425 0.5771  0.3131  -0.1163 147 GLU B OE1 
3733  O OE2 . GLU B 147 ? 0.8894 1.5126 0.6905 0.6005  0.3793  -0.1099 147 GLU B OE2 
3734  N N   . CYS B 148 ? 0.6593 1.0501 0.5436 0.3368  0.2850  -0.0349 148 CYS B N   
3735  C CA  . CYS B 148 ? 0.6414 0.9756 0.5130 0.2838  0.2726  -0.0168 148 CYS B CA  
3736  C C   . CYS B 148 ? 0.5851 0.8716 0.4942 0.2608  0.2384  -0.0155 148 CYS B C   
3737  O O   . CYS B 148 ? 0.5499 0.8388 0.4866 0.2151  0.2344  0.0036  148 CYS B O   
3738  C CB  . CYS B 148 ? 0.6981 0.9493 0.4870 0.2959  0.2653  -0.0256 148 CYS B CB  
3739  S SG  . CYS B 148 ? 0.6838 0.8499 0.4468 0.2508  0.2381  -0.0111 148 CYS B SG  
3740  N N   . MET B 149 ? 0.5883 0.8264 0.4915 0.2921  0.2149  -0.0360 149 MET B N   
3741  C CA  . MET B 149 ? 0.5411 0.7396 0.4779 0.2728  0.1854  -0.0354 149 MET B CA  
3742  C C   . MET B 149 ? 0.4945 0.7719 0.5036 0.2575  0.1917  -0.0227 149 MET B C   
3743  O O   . MET B 149 ? 0.4485 0.7144 0.4900 0.2214  0.1768  -0.0115 149 MET B O   
3744  C CB  . MET B 149 ? 0.5682 0.6965 0.4746 0.3075  0.1629  -0.0589 149 MET B CB  
3745  C CG  . MET B 149 ? 0.6207 0.6645 0.4558 0.3151  0.1494  -0.0753 149 MET B CG  
3746  S SD  . MET B 149 ? 0.5876 0.5838 0.4181 0.2661  0.1256  -0.0662 149 MET B SD  
3747  C CE  . MET B 149 ? 0.6603 0.5696 0.4114 0.2828  0.1049  -0.0939 149 MET B CE  
3748  N N   . GLU B 150 ? 0.5134 0.8757 0.5463 0.2873  0.2131  -0.0261 150 GLU B N   
3749  C CA  . GLU B 150 ? 0.4760 0.9310 0.5801 0.2754  0.2181  -0.0167 150 GLU B CA  
3750  C C   . GLU B 150 ? 0.4537 0.9567 0.5901 0.2131  0.2317  0.0067  150 GLU B C   
3751  O O   . GLU B 150 ? 0.4141 0.9507 0.6008 0.1833  0.2225  0.0155  150 GLU B O   
3752  C CB  . GLU B 150 ? 0.5033 1.0549 0.6251 0.3267  0.2390  -0.0274 150 GLU B CB  
3753  C CG  . GLU B 150 ? 0.4632 1.1301 0.6622 0.3209  0.2421  -0.0209 150 GLU B CG  
3754  C CD  . GLU B 150 ? 0.4295 1.0509 0.6504 0.3221  0.2088  -0.0232 150 GLU B CD  
3755  O OE1 . GLU B 150 ? 0.4549 0.9751 0.6308 0.3541  0.1877  -0.0361 150 GLU B OE1 
3756  O OE2 . GLU B 150 ? 0.3853 1.0701 0.6643 0.2879  0.2038  -0.0122 150 GLU B OE2 
3757  N N   . SER B 151 ? 0.4942 0.9917 0.5933 0.1930  0.2526  0.0166  151 SER B N   
3758  C CA  . SER B 151 ? 0.4966 1.0165 0.6065 0.1314  0.2665  0.0404  151 SER B CA  
3759  C C   . SER B 151 ? 0.4791 0.9075 0.5797 0.0957  0.2386  0.0491  151 SER B C   
3760  O O   . SER B 151 ? 0.4675 0.9092 0.5918 0.0477  0.2392  0.0648  151 SER B O   
3761  C CB  . SER B 151 ? 0.5546 1.0744 0.6108 0.1225  0.2956  0.0503  151 SER B CB  
3762  O OG  . SER B 151 ? 0.5825 0.9957 0.5710 0.1385  0.2801  0.0448  151 SER B OG  
3763  N N   . VAL B 152 ? 0.4873 0.8251 0.5508 0.1189  0.2142  0.0375  152 VAL B N   
3764  C CA  . VAL B 152 ? 0.4699 0.7318 0.5271 0.0954  0.1869  0.0419  152 VAL B CA  
3765  C C   . VAL B 152 ? 0.4272 0.7121 0.5413 0.0887  0.1701  0.0390  152 VAL B C   
3766  O O   . VAL B 152 ? 0.4080 0.6755 0.5370 0.0538  0.1600  0.0496  152 VAL B O   
3767  C CB  . VAL B 152 ? 0.4814 0.6618 0.4924 0.1213  0.1651  0.0274  152 VAL B CB  
3768  C CG1 . VAL B 152 ? 0.4560 0.5772 0.4666 0.1001  0.1388  0.0312  152 VAL B CG1 
3769  C CG2 . VAL B 152 ? 0.5378 0.6954 0.4870 0.1316  0.1788  0.0286  152 VAL B CG2 
3770  N N   . ARG B 153 ? 0.4268 0.7440 0.5643 0.1255  0.1665  0.0243  153 ARG B N   
3771  C CA  . ARG B 153 ? 0.3975 0.7436 0.5845 0.1257  0.1518  0.0219  153 ARG B CA  
3772  C C   . ARG B 153 ? 0.3975 0.8386 0.6354 0.0950  0.1664  0.0339  153 ARG B C   
3773  O O   . ARG B 153 ? 0.3671 0.8152 0.6372 0.0689  0.1523  0.0389  153 ARG B O   
3774  C CB  . ARG B 153 ? 0.4049 0.7529 0.5900 0.1788  0.1448  0.0041  153 ARG B CB  
3775  C CG  . ARG B 153 ? 0.4120 0.6593 0.5566 0.1934  0.1216  -0.0076 153 ARG B CG  
3776  C CD  . ARG B 153 ? 0.4395 0.6671 0.5693 0.2418  0.1131  -0.0236 153 ARG B CD  
3777  N NE  . ARG B 153 ? 0.4960 0.6697 0.5661 0.2723  0.1164  -0.0388 153 ARG B NE  
3778  C CZ  . ARG B 153 ? 0.5401 0.7463 0.5901 0.3142  0.1343  -0.0483 153 ARG B CZ  
3779  N NH1 . ARG B 153 ? 0.5304 0.8377 0.6220 0.3329  0.1522  -0.0441 153 ARG B NH1 
3780  N NH2 . ARG B 153 ? 0.6001 0.7413 0.5865 0.3384  0.1338  -0.0639 153 ARG B NH2 
3781  N N   . ASN B 154 ? 0.4465 0.9640 0.6897 0.0965  0.1949  0.0375  154 ASN B N   
3782  C CA  . ASN B 154 ? 0.4601 1.0803 0.7497 0.0569  0.2134  0.0495  154 ASN B CA  
3783  C C   . ASN B 154 ? 0.4485 1.0288 0.7324 -0.0087 0.2091  0.0667  154 ASN B C   
3784  O O   . ASN B 154 ? 0.4336 1.0716 0.7608 -0.0453 0.2069  0.0720  154 ASN B O   
3785  C CB  . ASN B 154 ? 0.5317 1.2226 0.8101 0.0589  0.2495  0.0538  154 ASN B CB  
3786  C CG  . ASN B 154 ? 0.5796 1.3845 0.8962 0.1088  0.2630  0.0400  154 ASN B CG  
3787  O OD1 . ASN B 154 ? 0.5590 1.3951 0.9123 0.1410  0.2447  0.0286  154 ASN B OD1 
3788  N ND2 . ASN B 154 ? 0.6838 1.5525 0.9868 0.1190  0.2962  0.0412  154 ASN B ND2 
3789  N N   . GLY B 155 ? 0.4601 0.9396 0.6849 -0.0211 0.2063  0.0741  155 GLY B N   
3790  C CA  . GLY B 155 ? 0.4796 0.9107 0.6754 -0.0778 0.2098  0.0926  155 GLY B CA  
3791  C C   . GLY B 155 ? 0.5262 0.9878 0.6917 -0.1036 0.2440  0.1072  155 GLY B C   
3792  O O   . GLY B 155 ? 0.5723 1.0005 0.7078 -0.1568 0.2532  0.1253  155 GLY B O   
3793  N N   . THR B 156 ? 0.5239 1.0401 0.6883 -0.0650 0.2634  0.0995  156 THR B N   
3794  C CA  . THR B 156 ? 0.5682 1.1441 0.7140 -0.0847 0.3014  0.1115  156 THR B CA  
3795  C C   . THR B 156 ? 0.6112 1.1123 0.6793 -0.0588 0.3103  0.1137  156 THR B C   
3796  O O   . THR B 156 ? 0.6608 1.2037 0.7025 -0.0667 0.3429  0.1228  156 THR B O   
3797  C CB  . THR B 156 ? 0.5458 1.2671 0.7535 -0.0560 0.3209  0.0993  156 THR B CB  
3798  O OG1 . THR B 156 ? 0.5062 1.3078 0.7852 -0.0835 0.3119  0.0982  156 THR B OG1 
3799  C CG2 . THR B 156 ? 0.5997 1.4019 0.7926 -0.0723 0.3645  0.1100  156 THR B CG2 
3800  N N   . TYR B 157 ? 0.5953 0.9921 0.6260 -0.0301 0.2814  0.1055  157 TYR B N   
3801  C CA  . TYR B 157 ? 0.6361 0.9654 0.5940 -0.0019 0.2835  0.1040  157 TYR B CA  
3802  C C   . TYR B 157 ? 0.7111 1.0124 0.6067 -0.0412 0.3091  0.1289  157 TYR B C   
3803  O O   . TYR B 157 ? 0.7384 0.9728 0.6055 -0.0815 0.3014  0.1463  157 TYR B O   
3804  C CB  . TYR B 157 ? 0.6158 0.8435 0.5467 0.0195  0.2461  0.0943  157 TYR B CB  
3805  C CG  . TYR B 157 ? 0.6633 0.8266 0.5199 0.0467  0.2431  0.0911  157 TYR B CG  
3806  C CD1 . TYR B 157 ? 0.6683 0.8457 0.5117 0.0925  0.2442  0.0707  157 TYR B CD1 
3807  C CD2 . TYR B 157 ? 0.7135 0.7976 0.5060 0.0291  0.2376  0.1077  157 TYR B CD2 
3808  C CE1 . TYR B 157 ? 0.7177 0.8386 0.4907 0.1155  0.2389  0.0657  157 TYR B CE1 
3809  C CE2 . TYR B 157 ? 0.7622 0.7937 0.4854 0.0567  0.2319  0.1042  157 TYR B CE2 
3810  C CZ  . TYR B 157 ? 0.7607 0.8144 0.4768 0.0975  0.2323  0.0827  157 TYR B CZ  
3811  O OH  . TYR B 157 ? 0.8129 0.8159 0.4577 0.1228  0.2241  0.0773  157 TYR B OH  
3812  N N   . ASP B 158 ? 0.7542 1.0990 0.6203 -0.0275 0.3396  0.1306  158 ASP B N   
3813  C CA  . ASP B 158 ? 0.8370 1.1615 0.6389 -0.0671 0.3694  0.1565  158 ASP B CA  
3814  C C   . ASP B 158 ? 0.8929 1.0962 0.6009 -0.0471 0.3541  0.1617  158 ASP B C   
3815  O O   . ASP B 158 ? 0.9242 1.1226 0.5884 -0.0076 0.3611  0.1526  158 ASP B O   
3816  C CB  . ASP B 158 ? 0.8661 1.3026 0.6768 -0.0632 0.4130  0.1574  158 ASP B CB  
3817  C CG  . ASP B 158 ? 0.9489 1.3938 0.7153 -0.1267 0.4502  0.1884  158 ASP B CG  
3818  O OD1 . ASP B 158 ? 0.9564 1.3966 0.7412 -0.1885 0.4508  0.2051  158 ASP B OD1 
3819  O OD2 . ASP B 158 ? 1.0157 1.4672 0.7230 -0.1176 0.4793  0.1960  158 ASP B OD2 
3820  N N   . TYR B 159 ? 0.9104 1.0171 0.5849 -0.0714 0.3316  0.1750  159 TYR B N   
3821  C CA  . TYR B 159 ? 0.9687 0.9624 0.5532 -0.0512 0.3132  0.1816  159 TYR B CA  
3822  C C   . TYR B 159 ? 1.0696 1.0446 0.5676 -0.0575 0.3449  0.2006  159 TYR B C   
3823  O O   . TYR B 159 ? 1.0995 1.0400 0.5433 -0.0145 0.3363  0.1918  159 TYR B O   
3824  C CB  . TYR B 159 ? 0.9869 0.8863 0.5463 -0.0769 0.2889  0.1952  159 TYR B CB  
3825  C CG  . TYR B 159 ? 1.0648 0.8496 0.5240 -0.0556 0.2713  0.2059  159 TYR B CG  
3826  C CD1 . TYR B 159 ? 1.0305 0.7790 0.4855 -0.0059 0.2332  0.1863  159 TYR B CD1 
3827  C CD2 . TYR B 159 ? 1.1802 0.8947 0.5453 -0.0856 0.2923  0.2359  159 TYR B CD2 
3828  C CE1 . TYR B 159 ? 1.1038 0.7608 0.4701 0.0193  0.2143  0.1945  159 TYR B CE1 
3829  C CE2 . TYR B 159 ? 1.2624 0.8684 0.5281 -0.0584 0.2738  0.2462  159 TYR B CE2 
3830  C CZ  . TYR B 159 ? 1.2214 0.8045 0.4911 -0.0029 0.2336  0.2245  159 TYR B CZ  
3831  O OH  . TYR B 159 ? 1.3055 0.7935 0.4790 0.0291  0.2127  0.2335  159 TYR B OH  
3832  N N   . PRO B 160 ? 1.1283 1.1279 0.6104 -0.1139 0.3818  0.2262  160 PRO B N   
3833  C CA  . PRO B 160 ? 1.2342 1.2157 0.6279 -0.1254 0.4163  0.2474  160 PRO B CA  
3834  C C   . PRO B 160 ? 1.2306 1.2877 0.6235 -0.0792 0.4363  0.2302  160 PRO B C   
3835  O O   . PRO B 160 ? 1.3184 1.3322 0.6210 -0.0673 0.4513  0.2416  160 PRO B O   
3836  C CB  . PRO B 160 ? 1.2772 1.3057 0.6832 -0.2029 0.4546  0.2730  160 PRO B CB  
3837  C CG  . PRO B 160 ? 1.2301 1.2317 0.6867 -0.2342 0.4283  0.2720  160 PRO B CG  
3838  C CD  . PRO B 160 ? 1.1123 1.1485 0.6471 -0.1759 0.3923  0.2383  160 PRO B CD  
3839  N N   . GLN B 161 ? 1.1430 1.3041 0.6258 -0.0508 0.4362  0.2033  161 GLN B N   
3840  C CA  . GLN B 161 ? 1.1470 1.3716 0.6245 0.0003  0.4528  0.1827  161 GLN B CA  
3841  C C   . GLN B 161 ? 1.1552 1.2951 0.5781 0.0580  0.4174  0.1623  161 GLN B C   
3842  O O   . GLN B 161 ? 1.2194 1.3468 0.5729 0.0872  0.4304  0.1587  161 GLN B O   
3843  C CB  . GLN B 161 ? 1.0630 1.4098 0.6435 0.0213  0.4588  0.1588  161 GLN B CB  
3844  C CG  . GLN B 161 ? 1.0745 1.4784 0.6450 0.0825  0.4739  0.1339  161 GLN B CG  
3845  C CD  . GLN B 161 ? 0.9992 1.4966 0.6598 0.1172  0.4693  0.1074  161 GLN B CD  
3846  O OE1 . GLN B 161 ? 0.9306 1.4502 0.6642 0.0970  0.4514  0.1068  161 GLN B OE1 
3847  N NE2 . GLN B 161 ? 1.0207 1.5664 0.6684 0.1740  0.4843  0.0849  161 GLN B NE2 
3848  N N   . TYR B 162 ? 1.0936 1.1818 0.5481 0.0719  0.3731  0.1479  162 TYR B N   
3849  C CA  . TYR B 162 ? 1.0928 1.1162 0.5103 0.1200  0.3358  0.1251  162 TYR B CA  
3850  C C   . TYR B 162 ? 1.1534 1.0706 0.4906 0.1166  0.3118  0.1408  162 TYR B C   
3851  O O   . TYR B 162 ? 1.1529 1.0231 0.4639 0.1516  0.2763  0.1223  162 TYR B O   
3852  C CB  . TYR B 162 ? 0.9972 1.0327 0.4931 0.1381  0.3018  0.0989  162 TYR B CB  
3853  C CG  . TYR B 162 ? 0.9473 1.0758 0.5140 0.1527  0.3192  0.0817  162 TYR B CG  
3854  C CD1 . TYR B 162 ? 0.9692 1.1215 0.5159 0.1995  0.3264  0.0573  162 TYR B CD1 
3855  C CD2 . TYR B 162 ? 0.8870 1.0766 0.5347 0.1238  0.3264  0.0885  162 TYR B CD2 
3856  C CE1 . TYR B 162 ? 0.9364 1.1680 0.5394 0.2225  0.3408  0.0410  162 TYR B CE1 
3857  C CE2 . TYR B 162 ? 0.8475 1.1262 0.5574 0.1445  0.3395  0.0727  162 TYR B CE2 
3858  C CZ  . TYR B 162 ? 0.8740 1.1721 0.5603 0.1966  0.3469  0.0494  162 TYR B CZ  
3859  O OH  . TYR B 162 ? 0.8470 1.2283 0.5871 0.2262  0.3588  0.0333  162 TYR B OH  
3860  N N   . SER B 163 ? 1.2153 1.0943 0.5096 0.0750  0.3300  0.1741  163 SER B N   
3861  C CA  . SER B 163 ? 1.2899 1.0590 0.4959 0.0773  0.3079  0.1918  163 SER B CA  
3862  C C   . SER B 163 ? 1.3948 1.1289 0.4946 0.0975  0.3236  0.2014  163 SER B C   
3863  O O   . SER B 163 ? 1.4848 1.1273 0.4919 0.0982  0.3145  0.2226  163 SER B O   
3864  C CB  . SER B 163 ? 1.3280 1.0462 0.5193 0.0245  0.3170  0.2234  163 SER B CB  
3865  O OG  . SER B 163 ? 1.4179 1.1396 0.5553 -0.0167 0.3624  0.2524  163 SER B OG  
3866  N N   . ASP C 1   ? 0.4303 0.3388 0.4005 -0.1666 0.0109  0.1538  1   ASP C N   
3867  C CA  . ASP C 1   ? 0.4569 0.3286 0.4026 -0.1572 0.0065  0.1535  1   ASP C CA  
3868  C C   . ASP C 1   ? 0.4153 0.3190 0.3950 -0.1378 0.0038  0.1489  1   ASP C C   
3869  O O   . ASP C 1   ? 0.3827 0.3190 0.3875 -0.1238 0.0042  0.1476  1   ASP C O   
3870  C CB  . ASP C 1   ? 0.5108 0.3272 0.4057 -0.1406 0.0036  0.1588  1   ASP C CB  
3871  C CG  . ASP C 1   ? 0.5612 0.3363 0.4137 -0.1609 0.0069  0.1637  1   ASP C CG  
3872  O OD1 . ASP C 1   ? 0.5493 0.3467 0.4162 -0.1895 0.0113  0.1625  1   ASP C OD1 
3873  O OD2 . ASP C 1   ? 0.6171 0.3377 0.4185 -0.1473 0.0052  0.1687  1   ASP C OD2 
3874  N N   . GLN C 2   ? 0.4196 0.3128 0.3970 -0.1396 0.0016  0.1462  2   GLN C N   
3875  C CA  . GLN C 2   ? 0.3841 0.3045 0.3905 -0.1239 -0.0005 0.1417  2   GLN C CA  
3876  C C   . GLN C 2   ? 0.4082 0.2964 0.3926 -0.1166 -0.0046 0.1406  2   GLN C C   
3877  O O   . GLN C 2   ? 0.4479 0.2967 0.3998 -0.1311 -0.0048 0.1420  2   GLN C O   
3878  C CB  . GLN C 2   ? 0.3425 0.3076 0.3885 -0.1358 0.0028  0.1375  2   GLN C CB  
3879  C CG  . GLN C 2   ? 0.3539 0.3181 0.3963 -0.1588 0.0039  0.1363  2   GLN C CG  
3880  C CD  . GLN C 2   ? 0.3153 0.3261 0.3944 -0.1615 0.0063  0.1320  2   GLN C CD  
3881  O OE1 . GLN C 2   ? 0.3167 0.3342 0.3986 -0.1704 0.0052  0.1294  2   GLN C OE1 
3882  N NE2 . GLN C 2   ? 0.2854 0.3265 0.3884 -0.1528 0.0097  0.1310  2   GLN C NE2 
3883  N N   . ILE C 3   ? 0.3863 0.2913 0.3861 -0.0958 -0.0073 0.1378  3   ILE C N   
3884  C CA  . ILE C 3   ? 0.4002 0.2846 0.3874 -0.0875 -0.0108 0.1356  3   ILE C CA  
3885  C C   . ILE C 3   ? 0.3533 0.2793 0.3812 -0.0876 -0.0104 0.1302  3   ILE C C   
3886  O O   . ILE C 3   ? 0.3186 0.2817 0.3741 -0.0812 -0.0087 0.1282  3   ILE C O   
3887  C CB  . ILE C 3   ? 0.4297 0.2903 0.3873 -0.0582 -0.0148 0.1374  3   ILE C CB  
3888  C CG1 . ILE C 3   ? 0.4568 0.2844 0.3912 -0.0508 -0.0180 0.1356  3   ILE C CG1 
3889  C CG2 . ILE C 3   ? 0.3919 0.3019 0.3788 -0.0395 -0.0154 0.1349  3   ILE C CG2 
3890  C CD1 . ILE C 3   ? 0.5095 0.2935 0.3950 -0.0226 -0.0213 0.1388  3   ILE C CD1 
3891  N N   . CYS C 4   ? 0.3571 0.2737 0.3841 -0.0965 -0.0116 0.1278  4   CYS C N   
3892  C CA  . CYS C 4   ? 0.3192 0.2696 0.3793 -0.0966 -0.0111 0.1232  4   CYS C CA  
3893  C C   . CYS C 4   ? 0.3255 0.2614 0.3766 -0.0835 -0.0151 0.1207  4   CYS C C   
3894  O O   . CYS C 4   ? 0.3652 0.2599 0.3818 -0.0802 -0.0178 0.1223  4   CYS C O   
3895  C CB  . CYS C 4   ? 0.3127 0.2777 0.3851 -0.1183 -0.0089 0.1219  4   CYS C CB  
3896  S SG  . CYS C 4   ? 0.3082 0.2943 0.3893 -0.1342 -0.0039 0.1244  4   CYS C SG  
3897  N N   . ILE C 5   ? 0.2904 0.2561 0.3679 -0.0759 -0.0148 0.1167  5   ILE C N   
3898  C CA  . ILE C 5   ? 0.2918 0.2500 0.3655 -0.0661 -0.0180 0.1137  5   ILE C CA  
3899  C C   . ILE C 5   ? 0.2739 0.2447 0.3652 -0.0792 -0.0173 0.1109  5   ILE C C   
3900  O O   . ILE C 5   ? 0.2475 0.2467 0.3622 -0.0856 -0.0138 0.1099  5   ILE C O   
3901  C CB  . ILE C 5   ? 0.2711 0.2556 0.3578 -0.0489 -0.0182 0.1107  5   ILE C CB  
3902  C CG1 . ILE C 5   ? 0.2845 0.2700 0.3569 -0.0349 -0.0189 0.1132  5   ILE C CG1 
3903  C CG2 . ILE C 5   ? 0.2764 0.2543 0.3575 -0.0380 -0.0215 0.1075  5   ILE C CG2 
3904  C CD1 . ILE C 5   ? 0.3279 0.2756 0.3627 -0.0182 -0.0231 0.1158  5   ILE C CD1 
3905  N N   . GLY C 6   ? 0.2927 0.2407 0.3685 -0.0818 -0.0204 0.1097  6   GLY C N   
3906  C CA  . GLY C 6   ? 0.2806 0.2424 0.3698 -0.0944 -0.0204 0.1071  6   GLY C CA  
3907  C C   . GLY C 6   ? 0.2967 0.2368 0.3712 -0.0911 -0.0241 0.1046  6   GLY C C   
3908  O O   . GLY C 6   ? 0.3191 0.2315 0.3713 -0.0770 -0.0265 0.1049  6   GLY C O   
3909  N N   . TYR C 7   ? 0.2870 0.2418 0.3724 -0.1023 -0.0246 0.1021  7   TYR C N   
3910  C CA  . TYR C 7   ? 0.2974 0.2377 0.3736 -0.0998 -0.0279 0.0991  7   TYR C CA  
3911  C C   . TYR C 7   ? 0.3154 0.2536 0.3817 -0.1229 -0.0288 0.0977  7   TYR C C   
3912  O O   . TYR C 7   ? 0.3090 0.2717 0.3845 -0.1395 -0.0268 0.0984  7   TYR C O   
3913  C CB  . TYR C 7   ? 0.2627 0.2313 0.3656 -0.0860 -0.0276 0.0962  7   TYR C CB  
3914  C CG  . TYR C 7   ? 0.2323 0.2393 0.3623 -0.0901 -0.0246 0.0956  7   TYR C CG  
3915  C CD1 . TYR C 7   ? 0.2139 0.2383 0.3572 -0.0854 -0.0205 0.0971  7   TYR C CD1 
3916  C CD2 . TYR C 7   ? 0.2265 0.2514 0.3648 -0.0966 -0.0256 0.0935  7   TYR C CD2 
3917  C CE1 . TYR C 7   ? 0.1953 0.2478 0.3555 -0.0850 -0.0171 0.0968  7   TYR C CE1 
3918  C CE2 . TYR C 7   ? 0.2055 0.2645 0.3630 -0.0943 -0.0228 0.0933  7   TYR C CE2 
3919  C CZ  . TYR C 7   ? 0.1921 0.2617 0.3585 -0.0874 -0.0183 0.0950  7   TYR C CZ  
3920  O OH  . TYR C 7   ? 0.1797 0.2766 0.3576 -0.0814 -0.0149 0.0949  7   TYR C OH  
3921  N N   . HIS C 8   ? 0.3398 0.2515 0.3859 -0.1242 -0.0318 0.0953  8   HIS C N   
3922  C CA  . HIS C 8   ? 0.3667 0.2704 0.3949 -0.1493 -0.0329 0.0931  8   HIS C CA  
3923  C C   . HIS C 8   ? 0.3343 0.2938 0.3955 -0.1579 -0.0329 0.0905  8   HIS C C   
3924  O O   . HIS C 8   ? 0.3008 0.2872 0.3894 -0.1401 -0.0332 0.0894  8   HIS C O   
3925  C CB  . HIS C 8   ? 0.3993 0.2594 0.3972 -0.1441 -0.0359 0.0907  8   HIS C CB  
3926  C CG  . HIS C 8   ? 0.4368 0.2783 0.4063 -0.1727 -0.0368 0.0879  8   HIS C CG  
3927  N ND1 . HIS C 8   ? 0.4861 0.2915 0.4149 -0.1988 -0.0348 0.0888  8   HIS C ND1 
3928  C CD2 . HIS C 8   ? 0.4367 0.2890 0.4083 -0.1817 -0.0390 0.0837  8   HIS C CD2 
3929  C CE1 . HIS C 8   ? 0.5155 0.3116 0.4219 -0.2254 -0.0355 0.0849  8   HIS C CE1 
3930  N NE2 . HIS C 8   ? 0.4847 0.3108 0.4181 -0.2145 -0.0384 0.0817  8   HIS C NE2 
3931  N N   . ALA C 9   ? 0.3491 0.3267 0.4040 -0.1850 -0.0321 0.0894  9   ALA C N   
3932  C CA  . ALA C 9   ? 0.3295 0.3611 0.4071 -0.1938 -0.0330 0.0862  9   ALA C CA  
3933  C C   . ALA C 9   ? 0.3710 0.3902 0.4181 -0.2263 -0.0344 0.0827  9   ALA C C   
3934  O O   . ALA C 9   ? 0.4169 0.3834 0.4235 -0.2432 -0.0335 0.0834  9   ALA C O   
3935  C CB  . ALA C 9   ? 0.3017 0.3888 0.4068 -0.1945 -0.0300 0.0875  9   ALA C CB  
3936  N N   . ASN C 10  ? 0.3612 0.4260 0.4227 -0.2353 -0.0363 0.0789  10  ASN C N   
3937  C CA  . ASN C 10  ? 0.4014 0.4641 0.4342 -0.2713 -0.0373 0.0745  10  ASN C CA  
3938  C C   . ASN C 10  ? 0.3796 0.5211 0.4395 -0.2792 -0.0389 0.0705  10  ASN C C   
3939  O O   . ASN C 10  ? 0.3370 0.5308 0.4344 -0.2548 -0.0388 0.0719  10  ASN C O   
3940  C CB  . ASN C 10  ? 0.4400 0.4335 0.4351 -0.2726 -0.0395 0.0728  10  ASN C CB  
3941  C CG  . ASN C 10  ? 0.4116 0.4164 0.4291 -0.2468 -0.0430 0.0712  10  ASN C CG  
3942  O OD1 . ASN C 10  ? 0.3682 0.4307 0.4250 -0.2310 -0.0439 0.0710  10  ASN C OD1 
3943  N ND2 . ASN C 10  ? 0.4410 0.3873 0.4291 -0.2410 -0.0446 0.0701  10  ASN C ND2 
3944  N N   . ASN C 11  ? 0.4150 0.5637 0.4513 -0.3130 -0.0402 0.0655  11  ASN C N   
3945  C CA  . ASN C 11  ? 0.4001 0.6321 0.4585 -0.3240 -0.0420 0.0610  11  ASN C CA  
3946  C C   . ASN C 11  ? 0.3834 0.6257 0.4553 -0.3043 -0.0464 0.0588  11  ASN C C   
3947  O O   . ASN C 11  ? 0.3767 0.6825 0.4601 -0.3145 -0.0487 0.0546  11  ASN C O   
3948  C CB  . ASN C 11  ? 0.4460 0.6935 0.4716 -0.3771 -0.0406 0.0557  11  ASN C CB  
3949  C CG  . ASN C 11  ? 0.5032 0.6735 0.4767 -0.4034 -0.0413 0.0525  11  ASN C CG  
3950  O OD1 . ASN C 11  ? 0.5053 0.6210 0.4719 -0.3792 -0.0436 0.0538  11  ASN C OD1 
3951  N ND2 . ASN C 11  ? 0.5552 0.7193 0.4873 -0.4542 -0.0387 0.0480  11  ASN C ND2 
3952  N N   . SER C 12  ? 0.3780 0.5625 0.4482 -0.2762 -0.0476 0.0614  12  SER C N   
3953  C CA  . SER C 12  ? 0.3648 0.5505 0.4449 -0.2570 -0.0513 0.0596  12  SER C CA  
3954  C C   . SER C 12  ? 0.3220 0.5772 0.4421 -0.2290 -0.0522 0.0605  12  SER C C   
3955  O O   . SER C 12  ? 0.2983 0.5724 0.4389 -0.2082 -0.0495 0.0643  12  SER C O   
3956  C CB  . SER C 12  ? 0.3666 0.4812 0.4368 -0.2321 -0.0514 0.0623  12  SER C CB  
3957  O OG  . SER C 12  ? 0.3527 0.4690 0.4325 -0.2138 -0.0546 0.0605  12  SER C OG  
3958  N N   . THR C 13  ? 0.3189 0.6077 0.4450 -0.2277 -0.0558 0.0570  13  THR C N   
3959  C CA  . THR C 13  ? 0.2869 0.6319 0.4421 -0.1964 -0.0570 0.0580  13  THR C CA  
3960  C C   . THR C 13  ? 0.2794 0.5912 0.4358 -0.1715 -0.0592 0.0583  13  THR C C   
3961  O O   . THR C 13  ? 0.2618 0.6090 0.4338 -0.1458 -0.0602 0.0589  13  THR C O   
3962  C CB  . THR C 13  ? 0.2879 0.7178 0.4508 -0.2120 -0.0595 0.0536  13  THR C CB  
3963  O OG1 . THR C 13  ? 0.3163 0.7351 0.4570 -0.2447 -0.0626 0.0481  13  THR C OG1 
3964  C CG2 . THR C 13  ? 0.2891 0.7702 0.4571 -0.2304 -0.0566 0.0533  13  THR C CG2 
3965  N N   . GLU C 14  ? 0.2974 0.5409 0.4340 -0.1774 -0.0596 0.0579  14  GLU C N   
3966  C CA  . GLU C 14  ? 0.2911 0.5031 0.4280 -0.1555 -0.0613 0.0578  14  GLU C CA  
3967  C C   . GLU C 14  ? 0.2630 0.4706 0.4173 -0.1211 -0.0582 0.0621  14  GLU C C   
3968  O O   . GLU C 14  ? 0.2571 0.4476 0.4141 -0.1158 -0.0546 0.0653  14  GLU C O   
3969  C CB  . GLU C 14  ? 0.3196 0.4614 0.4297 -0.1653 -0.0617 0.0566  14  GLU C CB  
3970  C CG  . GLU C 14  ? 0.3593 0.4891 0.4408 -0.1990 -0.0641 0.0517  14  GLU C CG  
3971  C CD  . GLU C 14  ? 0.3804 0.4633 0.4421 -0.1951 -0.0664 0.0489  14  GLU C CD  
3972  O OE1 . GLU C 14  ? 0.3603 0.4629 0.4386 -0.1764 -0.0686 0.0482  14  GLU C OE1 
3973  O OE2 . GLU C 14  ? 0.4222 0.4458 0.4481 -0.2092 -0.0658 0.0475  14  GLU C OE2 
3974  N N   . GLN C 15  ? 0.2502 0.4703 0.4120 -0.0997 -0.0593 0.0620  15  GLN C N   
3975  C CA  . GLN C 15  ? 0.2337 0.4447 0.4029 -0.0699 -0.0556 0.0654  15  GLN C CA  
3976  C C   . GLN C 15  ? 0.2332 0.4022 0.3947 -0.0590 -0.0558 0.0646  15  GLN C C   
3977  O O   . GLN C 15  ? 0.2410 0.4030 0.3957 -0.0668 -0.0596 0.0614  15  GLN C O   
3978  C CB  . GLN C 15  ? 0.2280 0.4897 0.4052 -0.0504 -0.0555 0.0665  15  GLN C CB  
3979  C CG  . GLN C 15  ? 0.2278 0.5471 0.4140 -0.0600 -0.0559 0.0664  15  GLN C CG  
3980  C CD  . GLN C 15  ? 0.2251 0.5973 0.4164 -0.0328 -0.0555 0.0677  15  GLN C CD  
3981  O OE1 . GLN C 15  ? 0.2229 0.6271 0.4195 -0.0228 -0.0526 0.0697  15  GLN C OE1 
3982  N NE2 . GLN C 15  ? 0.2296 0.6109 0.4163 -0.0182 -0.0583 0.0666  15  GLN C NE2 
3983  N N   . VAL C 16  ? 0.2248 0.3675 0.3857 -0.0428 -0.0513 0.0670  16  VAL C N   
3984  C CA  . VAL C 16  ? 0.2248 0.3352 0.3782 -0.0328 -0.0503 0.0659  16  VAL C CA  
3985  C C   . VAL C 16  ? 0.2234 0.3302 0.3723 -0.0120 -0.0452 0.0683  16  VAL C C   
3986  O O   . VAL C 16  ? 0.2219 0.3394 0.3722 -0.0050 -0.0417 0.0710  16  VAL C O   
3987  C CB  . VAL C 16  ? 0.2260 0.3000 0.3744 -0.0394 -0.0492 0.0651  16  VAL C CB  
3988  C CG1 . VAL C 16  ? 0.2393 0.3036 0.3807 -0.0577 -0.0533 0.0631  16  VAL C CG1 
3989  C CG2 . VAL C 16  ? 0.2190 0.2869 0.3707 -0.0360 -0.0442 0.0680  16  VAL C CG2 
3990  N N   . ASP C 17  ? 0.2293 0.3169 0.3681 -0.0030 -0.0444 0.0671  17  ASP C N   
3991  C CA  . ASP C 17  ? 0.2394 0.3092 0.3628 0.0133  -0.0383 0.0689  17  ASP C CA  
3992  C C   . ASP C 17  ? 0.2398 0.2769 0.3560 0.0075  -0.0335 0.0679  17  ASP C C   
3993  O O   . ASP C 17  ? 0.2324 0.2620 0.3542 -0.0029 -0.0357 0.0652  17  ASP C O   
3994  C CB  . ASP C 17  ? 0.2525 0.3206 0.3629 0.0259  -0.0395 0.0683  17  ASP C CB  
3995  C CG  . ASP C 17  ? 0.2559 0.3641 0.3702 0.0370  -0.0435 0.0695  17  ASP C CG  
3996  O OD1 . ASP C 17  ? 0.2554 0.3885 0.3746 0.0428  -0.0425 0.0718  17  ASP C OD1 
3997  O OD2 . ASP C 17  ? 0.2610 0.3804 0.3730 0.0404  -0.0477 0.0680  17  ASP C OD2 
3998  N N   . THR C 18  ? 0.2521 0.2715 0.3524 0.0147  -0.0265 0.0697  18  THR C N   
3999  C CA  . THR C 18  ? 0.2589 0.2513 0.3464 0.0074  -0.0205 0.0680  18  THR C CA  
4000  C C   . THR C 18  ? 0.2898 0.2531 0.3445 0.0172  -0.0139 0.0686  18  THR C C   
4001  O O   . THR C 18  ? 0.3051 0.2692 0.3482 0.0336  -0.0145 0.0709  18  THR C O   
4002  C CB  . THR C 18  ? 0.2510 0.2441 0.3443 0.0003  -0.0171 0.0691  18  THR C CB  
4003  O OG1 . THR C 18  ? 0.2636 0.2526 0.3447 0.0111  -0.0128 0.0724  18  THR C OG1 
4004  C CG2 . THR C 18  ? 0.2302 0.2452 0.3483 -0.0075 -0.0232 0.0693  18  THR C CG2 
4005  N N   . ILE C 19  ? 0.3059 0.2434 0.3411 0.0070  -0.0072 0.0665  19  ILE C N   
4006  C CA  . ILE C 19  ? 0.3465 0.2447 0.3397 0.0116  0.0007  0.0667  19  ILE C CA  
4007  C C   . ILE C 19  ? 0.3737 0.2539 0.3439 0.0270  0.0057  0.0708  19  ILE C C   
4008  O O   . ILE C 19  ? 0.4051 0.2625 0.3446 0.0457  0.0083  0.0732  19  ILE C O   
4009  C CB  . ILE C 19  ? 0.3593 0.2372 0.3337 -0.0095 0.0078  0.0625  19  ILE C CB  
4010  C CG1 . ILE C 19  ? 0.3399 0.2379 0.3324 -0.0205 0.0035  0.0581  19  ILE C CG1 
4011  C CG2 . ILE C 19  ? 0.4105 0.2374 0.3310 -0.0095 0.0176  0.0626  19  ILE C CG2 
4012  C CD1 . ILE C 19  ? 0.3567 0.2396 0.3322 -0.0147 0.0027  0.0573  19  ILE C CD1 
4013  N N   . MET C 20  ? 0.3654 0.2555 0.3479 0.0215  0.0073  0.0717  20  MET C N   
4014  C CA  . MET C 20  ? 0.3943 0.2656 0.3526 0.0351  0.0131  0.0750  20  MET C CA  
4015  C C   . MET C 20  ? 0.3850 0.2920 0.3641 0.0557  0.0075  0.0787  20  MET C C   
4016  O O   . MET C 20  ? 0.4103 0.3052 0.3658 0.0748  0.0119  0.0817  20  MET C O   
4017  C CB  . MET C 20  ? 0.3891 0.2552 0.3489 0.0180  0.0180  0.0739  20  MET C CB  
4018  C CG  . MET C 20  ? 0.4113 0.2449 0.3422 -0.0039 0.0257  0.0698  20  MET C CG  
4019  S SD  . MET C 20  ? 0.4138 0.2424 0.3396 -0.0206 0.0323  0.0689  20  MET C SD  
4020  C CE  . MET C 20  ? 0.4466 0.2439 0.3335 -0.0501 0.0414  0.0628  20  MET C CE  
4021  N N   . GLU C 21  ? 0.3543 0.3057 0.3738 0.0509  -0.0015 0.0781  21  GLU C N   
4022  C CA  . GLU C 21  ? 0.3451 0.3394 0.3860 0.0630  -0.0067 0.0805  21  GLU C CA  
4023  C C   . GLU C 21  ? 0.3291 0.3594 0.3958 0.0594  -0.0158 0.0790  21  GLU C C   
4024  O O   . GLU C 21  ? 0.3116 0.3418 0.3942 0.0416  -0.0195 0.0762  21  GLU C O   
4025  C CB  . GLU C 21  ? 0.3247 0.3371 0.3876 0.0511  -0.0067 0.0811  21  GLU C CB  
4026  C CG  . GLU C 21  ? 0.3228 0.3724 0.3949 0.0653  -0.0081 0.0838  21  GLU C CG  
4027  C CD  . GLU C 21  ? 0.3055 0.3698 0.3968 0.0518  -0.0076 0.0845  21  GLU C CD  
4028  O OE1 . GLU C 21  ? 0.3015 0.3412 0.3929 0.0360  -0.0049 0.0834  21  GLU C OE1 
4029  O OE2 . GLU C 21  ? 0.2968 0.4011 0.4023 0.0570  -0.0099 0.0859  21  GLU C OE2 
4030  N N   . LYS C 22  ? 0.3416 0.4045 0.4094 0.0774  -0.0191 0.0806  22  LYS C N   
4031  C CA  . LYS C 22  ? 0.3322 0.4341 0.4210 0.0726  -0.0274 0.0788  22  LYS C CA  
4032  C C   . LYS C 22  ? 0.3200 0.4745 0.4351 0.0645  -0.0318 0.0788  22  LYS C C   
4033  O O   . LYS C 22  ? 0.3232 0.4914 0.4373 0.0731  -0.0286 0.0810  22  LYS C O   
4034  C CB  . LYS C 22  ? 0.3550 0.4622 0.4233 0.0975  -0.0282 0.0798  22  LYS C CB  
4035  C CG  . LYS C 22  ? 0.3670 0.4370 0.4192 0.0951  -0.0279 0.0781  22  LYS C CG  
4036  C CD  . LYS C 22  ? 0.4106 0.4329 0.4172 0.1179  -0.0202 0.0806  22  LYS C CD  
4037  C CE  . LYS C 22  ? 0.4335 0.4800 0.4237 0.1497  -0.0225 0.0830  22  LYS C CE  
4038  N NZ  . LYS C 22  ? 0.4327 0.4872 0.4245 0.1497  -0.0280 0.0812  22  LYS C NZ  
4039  N N   . ASN C 23  ? 0.3155 0.4970 0.4501 0.0460  -0.0387 0.0760  23  ASN C N   
4040  C CA  . ASN C 23  ? 0.3123 0.5440 0.4667 0.0316  -0.0428 0.0751  23  ASN C CA  
4041  C C   . ASN C 23  ? 0.2883 0.5125 0.4511 0.0178  -0.0399 0.0763  23  ASN C C   
4042  O O   . ASN C 23  ? 0.2837 0.5456 0.4541 0.0185  -0.0392 0.0774  23  ASN C O   
4043  C CB  . ASN C 23  ? 0.3421 0.6301 0.4958 0.0527  -0.0441 0.0761  23  ASN C CB  
4044  C CG  . ASN C 23  ? 0.3822 0.6882 0.5301 0.0635  -0.0485 0.0746  23  ASN C CG  
4045  O OD1 . ASN C 23  ? 0.3832 0.6699 0.5334 0.0473  -0.0520 0.0719  23  ASN C OD1 
4046  N ND2 . ASN C 23  ? 0.4377 0.7814 0.5759 0.0932  -0.0484 0.0763  23  ASN C ND2 
4047  N N   . VAL C 24  ? 0.2705 0.4497 0.4313 0.0060  -0.0381 0.0759  24  VAL C N   
4048  C CA  . VAL C 24  ? 0.2531 0.4214 0.4203 -0.0075 -0.0359 0.0770  24  VAL C CA  
4049  C C   . VAL C 24  ? 0.2418 0.4233 0.4179 -0.0331 -0.0408 0.0750  24  VAL C C   
4050  O O   . VAL C 24  ? 0.2438 0.4048 0.4158 -0.0440 -0.0442 0.0726  24  VAL C O   
4051  C CB  . VAL C 24  ? 0.2525 0.3734 0.4116 -0.0085 -0.0322 0.0770  24  VAL C CB  
4052  C CG1 . VAL C 24  ? 0.2457 0.3582 0.4108 -0.0216 -0.0308 0.0780  24  VAL C CG1 
4053  C CG2 . VAL C 24  ? 0.2640 0.3637 0.4056 0.0104  -0.0259 0.0784  24  VAL C CG2 
4054  N N   . THR C 25  ? 0.2317 0.4439 0.4150 -0.0433 -0.0407 0.0758  25  THR C N   
4055  C CA  . THR C 25  ? 0.2328 0.4518 0.4159 -0.0717 -0.0442 0.0738  25  THR C CA  
4056  C C   . THR C 25  ? 0.2339 0.4036 0.4085 -0.0824 -0.0431 0.0746  25  THR C C   
4057  O O   . THR C 25  ? 0.2270 0.3832 0.4037 -0.0754 -0.0392 0.0772  25  THR C O   
4058  C CB  . THR C 25  ? 0.2316 0.5002 0.4224 -0.0824 -0.0435 0.0742  25  THR C CB  
4059  O OG1 . THR C 25  ? 0.2263 0.5464 0.4247 -0.0629 -0.0435 0.0742  25  THR C OG1 
4060  C CG2 . THR C 25  ? 0.2471 0.5259 0.4304 -0.1163 -0.0470 0.0709  25  THR C CG2 
4061  N N   . VAL C 26  ? 0.2443 0.3871 0.4059 -0.0976 -0.0466 0.0721  26  VAL C N   
4062  C CA  . VAL C 26  ? 0.2532 0.3477 0.4006 -0.1024 -0.0460 0.0728  26  VAL C CA  
4063  C C   . VAL C 26  ? 0.2798 0.3579 0.4063 -0.1289 -0.0479 0.0714  26  VAL C C   
4064  O O   . VAL C 26  ? 0.2917 0.3911 0.4130 -0.1470 -0.0503 0.0686  26  VAL C O   
4065  C CB  . VAL C 26  ? 0.2538 0.3161 0.3944 -0.0896 -0.0472 0.0711  26  VAL C CB  
4066  C CG1 . VAL C 26  ? 0.2326 0.3008 0.3857 -0.0683 -0.0438 0.0724  26  VAL C CG1 
4067  C CG2 . VAL C 26  ? 0.2648 0.3292 0.3980 -0.0964 -0.0513 0.0675  26  VAL C CG2 
4068  N N   . THR C 27  ? 0.2935 0.3322 0.4038 -0.1316 -0.0465 0.0733  27  THR C N   
4069  C CA  . THR C 27  ? 0.3306 0.3394 0.4102 -0.1565 -0.0471 0.0726  27  THR C CA  
4070  C C   . THR C 27  ? 0.3618 0.3324 0.4128 -0.1638 -0.0500 0.0691  27  THR C C   
4071  O O   . THR C 27  ? 0.3983 0.3555 0.4224 -0.1911 -0.0508 0.0666  27  THR C O   
4072  C CB  . THR C 27  ? 0.3442 0.3158 0.4086 -0.1525 -0.0446 0.0761  27  THR C CB  
4073  O OG1 . THR C 27  ? 0.3444 0.2829 0.4022 -0.1292 -0.0451 0.0766  27  THR C OG1 
4074  C CG2 . THR C 27  ? 0.3148 0.3216 0.4052 -0.1468 -0.0413 0.0794  27  THR C CG2 
4075  N N   . HIS C 28  ? 0.3520 0.3038 0.4053 -0.1412 -0.0512 0.0684  28  HIS C N   
4076  C CA  . HIS C 28  ? 0.3804 0.2958 0.4068 -0.1433 -0.0538 0.0650  28  HIS C CA  
4077  C C   . HIS C 28  ? 0.3510 0.2859 0.3998 -0.1231 -0.0554 0.0633  28  HIS C C   
4078  O O   . HIS C 28  ? 0.3192 0.2731 0.3926 -0.1031 -0.0536 0.0652  28  HIS C O   
4079  C CB  . HIS C 28  ? 0.4181 0.2717 0.4077 -0.1341 -0.0531 0.0660  28  HIS C CB  
4080  C CG  . HIS C 28  ? 0.4528 0.2774 0.4138 -0.1516 -0.0509 0.0684  28  HIS C CG  
4081  N ND1 . HIS C 28  ? 0.4334 0.2738 0.4107 -0.1464 -0.0484 0.0725  28  HIS C ND1 
4082  C CD2 . HIS C 28  ? 0.5099 0.2875 0.4229 -0.1762 -0.0503 0.0671  28  HIS C CD2 
4083  C CE1 . HIS C 28  ? 0.4749 0.2812 0.4176 -0.1659 -0.0467 0.0739  28  HIS C CE1 
4084  N NE2 . HIS C 28  ? 0.5241 0.2897 0.4252 -0.1851 -0.0475 0.0706  28  HIS C NE2 
4085  N N   . ALA C 29  ? 0.3666 0.2935 0.4025 -0.1305 -0.0582 0.0595  29  ALA C N   
4086  C CA  . ALA C 29  ? 0.3445 0.2864 0.3969 -0.1138 -0.0598 0.0575  29  ALA C CA  
4087  C C   . ALA C 29  ? 0.3788 0.2834 0.4010 -0.1187 -0.0623 0.0535  29  ALA C C   
4088  O O   . ALA C 29  ? 0.4223 0.2897 0.4088 -0.1372 -0.0626 0.0520  29  ALA C O   
4089  C CB  . ALA C 29  ? 0.3161 0.3129 0.3962 -0.1168 -0.0607 0.0573  29  ALA C CB  
4090  N N   . GLN C 30  ? 0.3644 0.2743 0.3962 -0.1028 -0.0636 0.0515  30  GLN C N   
4091  C CA  . GLN C 30  ? 0.3955 0.2728 0.3999 -0.1054 -0.0660 0.0473  30  GLN C CA  
4092  C C   . GLN C 30  ? 0.3715 0.2804 0.3960 -0.1005 -0.0682 0.0450  30  GLN C C   
4093  O O   . GLN C 30  ? 0.3442 0.2669 0.3881 -0.0801 -0.0671 0.0457  30  GLN C O   
4094  C CB  . GLN C 30  ? 0.4165 0.2502 0.3985 -0.0841 -0.0648 0.0471  30  GLN C CB  
4095  C CG  . GLN C 30  ? 0.4588 0.2500 0.4038 -0.0851 -0.0667 0.0427  30  GLN C CG  
4096  C CD  . GLN C 30  ? 0.4923 0.2364 0.4048 -0.0621 -0.0654 0.0426  30  GLN C CD  
4097  O OE1 . GLN C 30  ? 0.4989 0.2318 0.4053 -0.0521 -0.0634 0.0458  30  GLN C OE1 
4098  N NE2 . GLN C 30  ? 0.5169 0.2348 0.4063 -0.0516 -0.0666 0.0387  30  GLN C NE2 
4099  N N   . ASP C 31  ? 0.3847 0.3055 0.4014 -0.1212 -0.0710 0.0420  31  ASP C N   
4100  C CA  . ASP C 31  ? 0.3703 0.3161 0.3991 -0.1171 -0.0737 0.0394  31  ASP C CA  
4101  C C   . ASP C 31  ? 0.3903 0.2942 0.3972 -0.1059 -0.0743 0.0363  31  ASP C C   
4102  O O   . ASP C 31  ? 0.4323 0.2880 0.4024 -0.1138 -0.0742 0.0340  31  ASP C O   
4103  C CB  . ASP C 31  ? 0.3838 0.3578 0.4072 -0.1440 -0.0767 0.0364  31  ASP C CB  
4104  C CG  . ASP C 31  ? 0.3615 0.3784 0.4052 -0.1363 -0.0796 0.0350  31  ASP C CG  
4105  O OD1 . ASP C 31  ? 0.3458 0.3553 0.3985 -0.1136 -0.0793 0.0355  31  ASP C OD1 
4106  O OD2 . ASP C 31  ? 0.3623 0.4231 0.4112 -0.1533 -0.0821 0.0332  31  ASP C OD2 
4107  N N   . ILE C 32  ? 0.3640 0.2839 0.3894 -0.0866 -0.0744 0.0360  32  ILE C N   
4108  C CA  . ILE C 32  ? 0.3781 0.2683 0.3871 -0.0736 -0.0747 0.0328  32  ILE C CA  
4109  C C   . ILE C 32  ? 0.3729 0.2803 0.3864 -0.0756 -0.0776 0.0297  32  ILE C C   
4110  O O   . ILE C 32  ? 0.3820 0.2708 0.3848 -0.0647 -0.0779 0.0268  32  ILE C O   
4111  C CB  . ILE C 32  ? 0.3570 0.2483 0.3788 -0.0493 -0.0713 0.0345  32  ILE C CB  
4112  C CG1 . ILE C 32  ? 0.3174 0.2496 0.3717 -0.0428 -0.0693 0.0375  32  ILE C CG1 
4113  C CG2 . ILE C 32  ? 0.3707 0.2389 0.3803 -0.0447 -0.0690 0.0367  32  ILE C CG2 
4114  C CD1 . ILE C 32  ? 0.3016 0.2376 0.3639 -0.0251 -0.0658 0.0373  32  ILE C CD1 
4115  N N   . LEU C 33  ? 0.3600 0.3059 0.3882 -0.0881 -0.0799 0.0302  33  LEU C N   
4116  C CA  . LEU C 33  ? 0.3554 0.3238 0.3882 -0.0891 -0.0831 0.0277  33  LEU C CA  
4117  C C   . LEU C 33  ? 0.3852 0.3550 0.3978 -0.1164 -0.0867 0.0235  33  LEU C C   
4118  O O   . LEU C 33  ? 0.3869 0.3845 0.4030 -0.1350 -0.0876 0.0239  33  LEU C O   
4119  C CB  . LEU C 33  ? 0.3222 0.3392 0.3836 -0.0782 -0.0829 0.0313  33  LEU C CB  
4120  C CG  . LEU C 33  ? 0.3163 0.3592 0.3825 -0.0726 -0.0859 0.0299  33  LEU C CG  
4121  C CD1 . LEU C 33  ? 0.3157 0.3319 0.3764 -0.0572 -0.0845 0.0285  33  LEU C CD1 
4122  C CD2 . LEU C 33  ? 0.2947 0.3821 0.3804 -0.0598 -0.0854 0.0341  33  LEU C CD2 
4123  N N   . GLU C 34  ? 0.4109 0.3533 0.4007 -0.1208 -0.0886 0.0188  34  GLU C N   
4124  C CA  . GLU C 34  ? 0.4423 0.3870 0.4096 -0.1496 -0.0919 0.0138  34  GLU C CA  
4125  C C   . GLU C 34  ? 0.4177 0.4256 0.4094 -0.1509 -0.0957 0.0135  34  GLU C C   
4126  O O   . GLU C 34  ? 0.4012 0.4181 0.4041 -0.1322 -0.0968 0.0136  34  GLU C O   
4127  C CB  . GLU C 34  ? 0.4836 0.3719 0.4128 -0.1526 -0.0921 0.0087  34  GLU C CB  
4128  C CG  . GLU C 34  ? 0.5245 0.4073 0.4224 -0.1869 -0.0947 0.0028  34  GLU C CG  
4129  C CD  . GLU C 34  ? 0.5454 0.4368 0.4303 -0.2190 -0.0939 0.0024  34  GLU C CD  
4130  O OE1 . GLU C 34  ? 0.5761 0.4167 0.4333 -0.2236 -0.0904 0.0034  34  GLU C OE1 
4131  O OE2 . GLU C 34  ? 0.5320 0.4848 0.4339 -0.2385 -0.0967 0.0011  34  GLU C OE2 
4132  N N   . LYS C 35  ? 0.4186 0.4721 0.4159 -0.1726 -0.0975 0.0128  35  LYS C N   
4133  C CA  . LYS C 35  ? 0.3957 0.5203 0.4167 -0.1694 -0.1012 0.0130  35  LYS C CA  
4134  C C   . LYS C 35  ? 0.4221 0.5700 0.4252 -0.1982 -0.1056 0.0064  35  LYS C C   
4135  O O   . LYS C 35  ? 0.4061 0.6120 0.4257 -0.1917 -0.1094 0.0059  35  LYS C O   
4136  C CB  . LYS C 35  ? 0.3729 0.5512 0.4175 -0.1679 -0.1004 0.0169  35  LYS C CB  
4137  C CG  . LYS C 35  ? 0.3389 0.5217 0.4085 -0.1318 -0.0974 0.0236  35  LYS C CG  
4138  C CD  . LYS C 35  ? 0.3231 0.5485 0.4101 -0.1307 -0.0958 0.0273  35  LYS C CD  
4139  C CE  . LYS C 35  ? 0.3228 0.5057 0.4076 -0.1312 -0.0911 0.0302  35  LYS C CE  
4140  N NZ  . LYS C 35  ? 0.3558 0.4863 0.4122 -0.1574 -0.0904 0.0266  35  LYS C NZ  
4141  N N   . THR C 36  ? 0.4674 0.5681 0.4325 -0.2291 -0.1048 0.0011  36  THR C N   
4142  C CA  . THR C 36  ? 0.5008 0.6216 0.4421 -0.2652 -0.1080 -0.0060 36  THR C CA  
4143  C C   . THR C 36  ? 0.5372 0.5992 0.4441 -0.2707 -0.1085 -0.0111 36  THR C C   
4144  O O   . THR C 36  ? 0.5491 0.5428 0.4402 -0.2525 -0.1056 -0.0099 36  THR C O   
4145  C CB  . THR C 36  ? 0.5382 0.6555 0.4517 -0.3087 -0.1060 -0.0096 36  THR C CB  
4146  O OG1 . THR C 36  ? 0.5788 0.6037 0.4526 -0.3145 -0.1013 -0.0097 36  THR C OG1 
4147  C CG2 . THR C 36  ? 0.5048 0.6878 0.4516 -0.3059 -0.1055 -0.0054 36  THR C CG2 
4148  N N   . HIS C 37  ? 0.5559 0.6509 0.4510 -0.2956 -0.1123 -0.0172 37  HIS C N   
4149  C CA  . HIS C 37  ? 0.5993 0.6425 0.4549 -0.3096 -0.1129 -0.0235 37  HIS C CA  
4150  C C   . HIS C 37  ? 0.6393 0.7137 0.4667 -0.3603 -0.1149 -0.0315 37  HIS C C   
4151  O O   . HIS C 37  ? 0.6212 0.7744 0.4706 -0.3766 -0.1169 -0.0317 37  HIS C O   
4152  C CB  . HIS C 37  ? 0.5688 0.6289 0.4478 -0.2772 -0.1161 -0.0223 37  HIS C CB  
4153  C CG  . HIS C 37  ? 0.5318 0.6865 0.4474 -0.2711 -0.1212 -0.0212 37  HIS C CG  
4154  N ND1 . HIS C 37  ? 0.5461 0.7407 0.4527 -0.2911 -0.1259 -0.0272 37  HIS C ND1 
4155  C CD2 . HIS C 37  ? 0.4860 0.7023 0.4428 -0.2449 -0.1223 -0.0149 37  HIS C CD2 
4156  C CE1 . HIS C 37  ? 0.5094 0.7898 0.4514 -0.2751 -0.1299 -0.0244 37  HIS C CE1 
4157  N NE2 . HIS C 37  ? 0.4748 0.7667 0.4456 -0.2461 -0.1277 -0.0169 37  HIS C NE2 
4158  N N   . ASN C 38  ? 0.6966 0.7122 0.4732 -0.3859 -0.1141 -0.0385 38  ASN C N   
4159  C CA  . ASN C 38  ? 0.7440 0.7827 0.4849 -0.4411 -0.1151 -0.0474 38  ASN C CA  
4160  C C   . ASN C 38  ? 0.7192 0.8487 0.4864 -0.4466 -0.1216 -0.0510 38  ASN C C   
4161  O O   . ASN C 38  ? 0.7417 0.9269 0.4958 -0.4905 -0.1234 -0.0577 38  ASN C O   
4162  C CB  . ASN C 38  ? 0.8280 0.7590 0.4921 -0.4714 -0.1105 -0.0541 38  ASN C CB  
4163  C CG  . ASN C 38  ? 0.8389 0.7179 0.4879 -0.4468 -0.1115 -0.0558 38  ASN C CG  
4164  O OD1 . ASN C 38  ? 0.7868 0.7163 0.4807 -0.4155 -0.1160 -0.0532 38  ASN C OD1 
4165  N ND2 . ASN C 38  ? 0.9122 0.6862 0.4929 -0.4600 -0.1067 -0.0602 38  ASN C ND2 
4166  N N   . GLY C 39  ? 0.6770 0.8221 0.4781 -0.4032 -0.1249 -0.0470 39  GLY C N   
4167  C CA  . GLY C 39  ? 0.6492 0.8810 0.4781 -0.3981 -0.1314 -0.0488 39  GLY C CA  
4168  C C   . GLY C 39  ? 0.6881 0.8892 0.4818 -0.4167 -0.1332 -0.0563 39  GLY C C   
4169  O O   . GLY C 39  ? 0.6771 0.9498 0.4838 -0.4231 -0.1387 -0.0596 39  GLY C O   
4170  N N   . LYS C 40  ? 0.7352 0.8304 0.4827 -0.4220 -0.1286 -0.0588 40  LYS C N   
4171  C CA  . LYS C 40  ? 0.7873 0.8372 0.4880 -0.4458 -0.1290 -0.0670 40  LYS C CA  
4172  C C   . LYS C 40  ? 0.7909 0.7614 0.4810 -0.4078 -0.1269 -0.0649 40  LYS C C   
4173  O O   . LYS C 40  ? 0.7756 0.7001 0.4751 -0.3746 -0.1233 -0.0587 40  LYS C O   
4174  C CB  . LYS C 40  ? 0.8672 0.8563 0.4996 -0.5011 -0.1241 -0.0749 40  LYS C CB  
4175  C CG  . LYS C 40  ? 0.8792 0.9522 0.5093 -0.5531 -0.1263 -0.0809 40  LYS C CG  
4176  C CD  . LYS C 40  ? 0.9401 0.9589 0.5182 -0.5976 -0.1198 -0.0842 40  LYS C CD  
4177  C CE  . LYS C 40  ? 0.9609 1.0643 0.5292 -0.6576 -0.1212 -0.0921 40  LYS C CE  
4178  N NZ  . LYS C 40  ? 1.0168 1.0741 0.5376 -0.7014 -0.1144 -0.0945 40  LYS C NZ  
4179  N N   . LEU C 41  ? 0.8125 0.7724 0.4827 -0.4138 -0.1293 -0.0705 41  LEU C N   
4180  C CA  . LEU C 41  ? 0.8291 0.7111 0.4781 -0.3854 -0.1269 -0.0706 41  LEU C CA  
4181  C C   . LEU C 41  ? 0.9159 0.6935 0.4865 -0.4151 -0.1211 -0.0775 41  LEU C C   
4182  O O   . LEU C 41  ? 0.9704 0.7410 0.4963 -0.4632 -0.1211 -0.0859 41  LEU C O   
4183  C CB  . LEU C 41  ? 0.8125 0.7334 0.4758 -0.3768 -0.1320 -0.0733 41  LEU C CB  
4184  C CG  . LEU C 41  ? 0.7372 0.7372 0.4664 -0.3363 -0.1367 -0.0658 41  LEU C CG  
4185  C CD1 . LEU C 41  ? 0.7227 0.6821 0.4579 -0.2964 -0.1355 -0.0633 41  LEU C CD1 
4186  C CD2 . LEU C 41  ? 0.6880 0.7313 0.4616 -0.3159 -0.1361 -0.0573 41  LEU C CD2 
4187  N N   . CYS C 42  ? 0.9329 0.6295 0.4830 -0.3861 -0.1159 -0.0742 42  CYS C N   
4188  C CA  . CYS C 42  ? 1.0199 0.6101 0.4913 -0.4067 -0.1094 -0.0788 42  CYS C CA  
4189  C C   . CYS C 42  ? 1.0590 0.5614 0.4898 -0.3754 -0.1059 -0.0805 42  CYS C C   
4190  O O   . CYS C 42  ? 1.0095 0.5337 0.4807 -0.3329 -0.1077 -0.0768 42  CYS C O   
4191  C CB  . CYS C 42  ? 1.0182 0.5864 0.4910 -0.4004 -0.1054 -0.0729 42  CYS C CB  
4192  S SG  . CYS C 42  ? 0.9926 0.6432 0.4950 -0.4410 -0.1072 -0.0715 42  CYS C SG  
4193  N N   . ASP C 43  ? 1.1538 0.5545 0.4992 -0.3968 -0.1002 -0.0864 43  ASP C N   
4194  C CA  . ASP C 43  ? 1.2042 0.5097 0.4995 -0.3621 -0.0955 -0.0876 43  ASP C CA  
4195  C C   . ASP C 43  ? 1.1681 0.4645 0.4923 -0.3126 -0.0932 -0.0791 43  ASP C C   
4196  O O   . ASP C 43  ? 1.1608 0.4620 0.4928 -0.3199 -0.0917 -0.0748 43  ASP C O   
4197  C CB  . ASP C 43  ? 1.3256 0.5146 0.5126 -0.3955 -0.0890 -0.0951 43  ASP C CB  
4198  C CG  . ASP C 43  ? 1.3741 0.5603 0.5206 -0.4457 -0.0903 -0.1050 43  ASP C CG  
4199  O OD1 . ASP C 43  ? 1.3118 0.5881 0.5156 -0.4503 -0.0968 -0.1059 43  ASP C OD1 
4200  O OD2 . ASP C 43  ? 1.4798 0.5708 0.5321 -0.4815 -0.0845 -0.1120 43  ASP C OD2 
4201  N N   . LEU C 44  ? 1.1462 0.4338 0.4859 -0.2642 -0.0928 -0.0772 44  LEU C N   
4202  C CA  . LEU C 44  ? 1.1168 0.3984 0.4798 -0.2166 -0.0903 -0.0703 44  LEU C CA  
4203  C C   . LEU C 44  ? 1.2064 0.3775 0.4870 -0.1941 -0.0839 -0.0729 44  LEU C C   
4204  O O   . LEU C 44  ? 1.2484 0.3746 0.4896 -0.1787 -0.0823 -0.0780 44  LEU C O   
4205  C CB  . LEU C 44  ? 1.0358 0.3861 0.4682 -0.1772 -0.0934 -0.0667 44  LEU C CB  
4206  C CG  . LEU C 44  ? 0.9887 0.3600 0.4604 -0.1348 -0.0915 -0.0595 44  LEU C CG  
4207  C CD1 . LEU C 44  ? 0.9248 0.3646 0.4557 -0.1473 -0.0940 -0.0530 44  LEU C CD1 
4208  C CD2 . LEU C 44  ? 0.9424 0.3503 0.4517 -0.0963 -0.0921 -0.0588 44  LEU C CD2 
4209  N N   . ASP C 45  ? 1.2392 0.3658 0.4910 -0.1901 -0.0800 -0.0693 45  ASP C N   
4210  C CA  . ASP C 45  ? 1.3327 0.3494 0.4987 -0.1648 -0.0735 -0.0708 45  ASP C CA  
4211  C C   . ASP C 45  ? 1.4407 0.3619 0.5102 -0.1961 -0.0700 -0.0796 45  ASP C C   
4212  O O   . ASP C 45  ? 1.5157 0.3516 0.5154 -0.1667 -0.0654 -0.0829 45  ASP C O   
4213  C CB  . ASP C 45  ? 1.3063 0.3330 0.4927 -0.1022 -0.0728 -0.0688 45  ASP C CB  
4214  C CG  . ASP C 45  ? 1.3745 0.3200 0.4982 -0.0628 -0.0670 -0.0667 45  ASP C CG  
4215  O OD1 . ASP C 45  ? 1.3512 0.3126 0.4966 -0.0545 -0.0665 -0.0605 45  ASP C OD1 
4216  O OD2 . ASP C 45  ? 1.4538 0.3202 0.5047 -0.0378 -0.0630 -0.0712 45  ASP C OD2 
4217  N N   . GLY C 46  ? 1.4506 0.3892 0.5144 -0.2555 -0.0719 -0.0838 46  GLY C N   
4218  C CA  . GLY C 46  ? 1.5498 0.4086 0.5251 -0.2960 -0.0687 -0.0932 46  GLY C CA  
4219  C C   . GLY C 46  ? 1.5291 0.4202 0.5220 -0.2959 -0.0723 -0.0988 46  GLY C C   
4220  O O   . GLY C 46  ? 1.5887 0.4466 0.5298 -0.3409 -0.0715 -0.1068 46  GLY C O   
4221  N N   . VAL C 47  ? 1.4464 0.4033 0.5105 -0.2482 -0.0761 -0.0948 47  VAL C N   
4222  C CA  . VAL C 47  ? 1.4265 0.4103 0.5068 -0.2398 -0.0791 -0.0994 47  VAL C CA  
4223  C C   . VAL C 47  ? 1.3415 0.4384 0.5006 -0.2714 -0.0866 -0.0990 47  VAL C C   
4224  O O   . VAL C 47  ? 1.2486 0.4347 0.4913 -0.2566 -0.0907 -0.0920 47  VAL C O   
4225  C CB  . VAL C 47  ? 1.3825 0.3848 0.4980 -0.1747 -0.0789 -0.0957 47  VAL C CB  
4226  C CG1 . VAL C 47  ? 1.3663 0.3938 0.4952 -0.1678 -0.0815 -0.1007 47  VAL C CG1 
4227  C CG2 . VAL C 47  ? 1.4653 0.3654 0.5040 -0.1359 -0.0718 -0.0958 47  VAL C CG2 
4228  N N   . LYS C 48  ? 1.3781 0.4694 0.5062 -0.3132 -0.0882 -0.1068 48  LYS C N   
4229  C CA  . LYS C 48  ? 1.3131 0.5085 0.5028 -0.3475 -0.0953 -0.1074 48  LYS C CA  
4230  C C   . LYS C 48  ? 1.2181 0.5003 0.4901 -0.3106 -0.1009 -0.1032 48  LYS C C   
4231  O O   . LYS C 48  ? 1.2262 0.4790 0.4870 -0.2772 -0.0995 -0.1048 48  LYS C O   
4232  C CB  . LYS C 48  ? 1.3850 0.5500 0.5132 -0.4009 -0.0952 -0.1179 48  LYS C CB  
4233  C CG  . LYS C 48  ? 1.3469 0.6078 0.5151 -0.4511 -0.1010 -0.1196 48  LYS C CG  
4234  C CD  . LYS C 48  ? 1.3682 0.6506 0.5193 -0.4832 -0.1044 -0.1283 48  LYS C CD  
4235  C CE  . LYS C 48  ? 1.3343 0.7192 0.5220 -0.5317 -0.1101 -0.1304 48  LYS C CE  
4236  N NZ  . LYS C 48  ? 1.3008 0.7590 0.5200 -0.5391 -0.1168 -0.1342 48  LYS C NZ  
4237  N N   . PRO C 49  ? 1.1323 0.5196 0.4828 -0.3160 -0.1067 -0.0979 49  PRO C N   
4238  C CA  . PRO C 49  ? 1.0551 0.5177 0.4723 -0.2874 -0.1116 -0.0945 49  PRO C CA  
4239  C C   . PRO C 49  ? 1.0712 0.5506 0.4748 -0.3097 -0.1154 -0.1016 49  PRO C C   
4240  O O   . PRO C 49  ? 1.1193 0.5907 0.4839 -0.3570 -0.1162 -0.1083 49  PRO C O   
4241  C CB  . PRO C 49  ? 0.9780 0.5363 0.4666 -0.2912 -0.1162 -0.0874 49  PRO C CB  
4242  C CG  . PRO C 49  ? 1.0186 0.5713 0.4762 -0.3391 -0.1157 -0.0906 49  PRO C CG  
4243  C CD  . PRO C 49  ? 1.1036 0.5428 0.4837 -0.3424 -0.1085 -0.0941 49  PRO C CD  
4244  N N   . LEU C 50  ? 1.0323 0.5370 0.4667 -0.2777 -0.1173 -0.1003 50  LEU C N   
4245  C CA  . LEU C 50  ? 1.0304 0.5694 0.4670 -0.2937 -0.1220 -0.1054 50  LEU C CA  
4246  C C   . LEU C 50  ? 0.9612 0.6078 0.4626 -0.3040 -0.1290 -0.1008 50  LEU C C   
4247  O O   . LEU C 50  ? 0.8936 0.5927 0.4529 -0.2707 -0.1309 -0.0932 50  LEU C O   
4248  C CB  . LEU C 50  ? 1.0159 0.5416 0.4604 -0.2541 -0.1210 -0.1054 50  LEU C CB  
4249  C CG  . LEU C 50  ? 0.9944 0.5693 0.4578 -0.2593 -0.1263 -0.1082 50  LEU C CG  
4250  C CD1 . LEU C 50  ? 1.0541 0.6142 0.4682 -0.3081 -0.1284 -0.1175 50  LEU C CD1 
4251  C CD2 . LEU C 50  ? 0.9940 0.5394 0.4526 -0.2218 -0.1236 -0.1092 50  LEU C CD2 
4252  N N   . ILE C 51  ? 0.9833 0.6621 0.4702 -0.3500 -0.1323 -0.1056 51  ILE C N   
4253  C CA  . ILE C 51  ? 0.9255 0.7123 0.4679 -0.3588 -0.1392 -0.1021 51  ILE C CA  
4254  C C   . ILE C 51  ? 0.9246 0.7529 0.4686 -0.3681 -0.1446 -0.1069 51  ILE C C   
4255  O O   . ILE C 51  ? 0.9796 0.7933 0.4778 -0.4096 -0.1453 -0.1161 51  ILE C O   
4256  C CB  . ILE C 51  ? 0.9439 0.7612 0.4762 -0.4030 -0.1399 -0.1044 51  ILE C CB  
4257  C CG1 . ILE C 51  ? 0.9609 0.7180 0.4770 -0.3974 -0.1336 -0.1008 51  ILE C CG1 
4258  C CG2 . ILE C 51  ? 0.8783 0.8144 0.4730 -0.4005 -0.1467 -0.0994 51  ILE C CG2 
4259  C CD1 . ILE C 51  ? 0.9566 0.7593 0.4822 -0.4293 -0.1342 -0.0999 51  ILE C CD1 
4260  N N   . LEU C 52  ? 0.8661 0.7443 0.4594 -0.3309 -0.1481 -0.1008 52  LEU C N   
4261  C CA  . LEU C 52  ? 0.8618 0.7778 0.4587 -0.3323 -0.1533 -0.1041 52  LEU C CA  
4262  C C   . LEU C 52  ? 0.8486 0.8613 0.4640 -0.3609 -0.1606 -0.1059 52  LEU C C   
4263  O O   . LEU C 52  ? 0.8553 0.9032 0.4659 -0.3710 -0.1655 -0.1103 52  LEU C O   
4264  C CB  . LEU C 52  ? 0.8098 0.7409 0.4470 -0.2830 -0.1537 -0.0966 52  LEU C CB  
4265  C CG  . LEU C 52  ? 0.8178 0.6704 0.4417 -0.2525 -0.1467 -0.0952 52  LEU C CG  
4266  C CD1 . LEU C 52  ? 0.7649 0.6445 0.4305 -0.2103 -0.1468 -0.0878 52  LEU C CD1 
4267  C CD2 . LEU C 52  ? 0.8815 0.6611 0.4475 -0.2661 -0.1438 -0.1047 52  LEU C CD2 
4268  N N   . ARG C 53  ? 0.8308 0.8897 0.4668 -0.3728 -0.1615 -0.1028 53  ARG C N   
4269  C CA  . ARG C 53  ? 0.8171 0.9788 0.4727 -0.3976 -0.1682 -0.1045 53  ARG C CA  
4270  C C   . ARG C 53  ? 0.7638 1.0034 0.4657 -0.3594 -0.1745 -0.0980 53  ARG C C   
4271  O O   . ARG C 53  ? 0.7178 0.9695 0.4578 -0.3171 -0.1738 -0.0881 53  ARG C O   
4272  C CB  . ARG C 53  ? 0.8806 1.0402 0.4851 -0.4564 -0.1692 -0.1170 53  ARG C CB  
4273  C CG  . ARG C 53  ? 0.8746 1.1423 0.4932 -0.4920 -0.1747 -0.1203 53  ARG C CG  
4274  C CD  . ARG C 53  ? 0.9406 1.2108 0.5057 -0.5550 -0.1755 -0.1337 53  ARG C CD  
4275  N NE  . ARG C 53  ? 0.9965 1.2211 0.5154 -0.6053 -0.1695 -0.1399 53  ARG C NE  
4276  C CZ  . ARG C 53  ? 1.0654 1.1666 0.5197 -0.6264 -0.1617 -0.1451 53  ARG C CZ  
4277  N NH1 . ARG C 53  ? 1.0868 1.0990 0.5157 -0.6011 -0.1587 -0.1454 53  ARG C NH1 
4278  N NH2 . ARG C 53  ? 1.1183 1.1834 0.5285 -0.6727 -0.1563 -0.1501 53  ARG C NH2 
4279  N N   . ASP C 54  ? 0.7750 1.0622 0.4693 -0.3735 -0.1803 -0.1034 54  ASP C N   
4280  C CA  . ASP C 54  ? 0.7334 1.0890 0.4632 -0.3361 -0.1864 -0.0973 54  ASP C CA  
4281  C C   . ASP C 54  ? 0.7347 1.0332 0.4559 -0.3085 -0.1849 -0.0962 54  ASP C C   
4282  O O   . ASP C 54  ? 0.7059 1.0450 0.4504 -0.2752 -0.1888 -0.0906 54  ASP C O   
4283  C CB  . ASP C 54  ? 0.7404 1.1986 0.4713 -0.3631 -0.1945 -0.1030 54  ASP C CB  
4284  C CG  . ASP C 54  ? 0.7260 1.2675 0.4772 -0.3791 -0.1968 -0.1022 54  ASP C CG  
4285  O OD1 . ASP C 54  ? 0.6838 1.2560 0.4716 -0.3407 -0.1969 -0.0924 54  ASP C OD1 
4286  O OD2 . ASP C 54  ? 0.7602 1.3370 0.4878 -0.4315 -0.1983 -0.1118 54  ASP C OD2 
4287  N N   . CYS C 55  ? 0.7722 0.9765 0.4564 -0.3212 -0.1790 -0.1017 55  CYS C N   
4288  C CA  . CYS C 55  ? 0.7738 0.9220 0.4496 -0.2940 -0.1765 -0.1009 55  CYS C CA  
4289  C C   . CYS C 55  ? 0.7356 0.8498 0.4386 -0.2495 -0.1713 -0.0913 55  CYS C C   
4290  O O   . CYS C 55  ? 0.7250 0.8232 0.4378 -0.2466 -0.1676 -0.0876 55  CYS C O   
4291  C CB  . CYS C 55  ? 0.8346 0.8967 0.4555 -0.3214 -0.1719 -0.1110 55  CYS C CB  
4292  S SG  . CYS C 55  ? 0.8862 0.9753 0.4669 -0.3709 -0.1772 -0.1234 55  CYS C SG  
4293  N N   . SER C 56  ? 0.7168 0.8222 0.4300 -0.2174 -0.1709 -0.0875 56  SER C N   
4294  C CA  . SER C 56  ? 0.6878 0.7577 0.4198 -0.1801 -0.1651 -0.0799 56  SER C CA  
4295  C C   . SER C 56  ? 0.7159 0.7039 0.4184 -0.1784 -0.1586 -0.0851 56  SER C C   
4296  O O   . SER C 56  ? 0.7599 0.7136 0.4250 -0.2033 -0.1586 -0.0940 56  SER C O   
4297  C CB  . SER C 56  ? 0.6580 0.7633 0.4123 -0.1474 -0.1674 -0.0729 56  SER C CB  
4298  O OG  . SER C 56  ? 0.6759 0.7547 0.4109 -0.1442 -0.1672 -0.0772 56  SER C OG  
4299  N N   . VAL C 57  ? 0.6936 0.6518 0.4100 -0.1486 -0.1528 -0.0799 57  VAL C N   
4300  C CA  . VAL C 57  ? 0.7169 0.6076 0.4083 -0.1397 -0.1464 -0.0843 57  VAL C CA  
4301  C C   . VAL C 57  ? 0.7324 0.6154 0.4070 -0.1362 -0.1476 -0.0889 57  VAL C C   
4302  O O   . VAL C 57  ? 0.7726 0.6049 0.4109 -0.1435 -0.1449 -0.0966 57  VAL C O   
4303  C CB  . VAL C 57  ? 0.6862 0.5624 0.3999 -0.1093 -0.1401 -0.0778 57  VAL C CB  
4304  C CG1 . VAL C 57  ? 0.7096 0.5299 0.3989 -0.0959 -0.1338 -0.0827 57  VAL C CG1 
4305  C CG2 . VAL C 57  ? 0.6737 0.5526 0.4012 -0.1132 -0.1386 -0.0737 57  VAL C CG2 
4306  N N   . ALA C 58  ? 0.7044 0.6345 0.4015 -0.1234 -0.1513 -0.0840 58  ALA C N   
4307  C CA  . ALA C 58  ? 0.7170 0.6475 0.4002 -0.1207 -0.1532 -0.0876 58  ALA C CA  
4308  C C   . ALA C 58  ? 0.7559 0.6885 0.4092 -0.1534 -0.1583 -0.0965 58  ALA C C   
4309  O O   . ALA C 58  ? 0.7903 0.6825 0.4119 -0.1599 -0.1566 -0.1040 58  ALA C O   
4310  C CB  . ALA C 58  ? 0.6852 0.6652 0.3937 -0.1008 -0.1564 -0.0797 58  ALA C CB  
4311  N N   . GLY C 59  ? 0.7526 0.7342 0.4141 -0.1747 -0.1643 -0.0962 59  GLY C N   
4312  C CA  . GLY C 59  ? 0.7911 0.7838 0.4233 -0.2125 -0.1690 -0.1052 59  GLY C CA  
4313  C C   . GLY C 59  ? 0.8453 0.7603 0.4300 -0.2356 -0.1638 -0.1144 59  GLY C C   
4314  O O   . GLY C 59  ? 0.8888 0.7776 0.4357 -0.2560 -0.1644 -0.1231 59  GLY C O   
4315  N N   . TRP C 60  ? 0.8472 0.7220 0.4297 -0.2310 -0.1583 -0.1124 60  TRP C N   
4316  C CA  . TRP C 60  ? 0.9050 0.6961 0.4361 -0.2457 -0.1523 -0.1199 60  TRP C CA  
4317  C C   . TRP C 60  ? 0.9272 0.6609 0.4336 -0.2224 -0.1474 -0.1235 60  TRP C C   
4318  O O   . TRP C 60  ? 0.9854 0.6683 0.4406 -0.2402 -0.1459 -0.1326 60  TRP C O   
4319  C CB  . TRP C 60  ? 0.8982 0.6641 0.4357 -0.2391 -0.1477 -0.1155 60  TRP C CB  
4320  C CG  . TRP C 60  ? 0.9506 0.6240 0.4394 -0.2340 -0.1400 -0.1203 60  TRP C CG  
4321  C CD1 . TRP C 60  ? 1.0245 0.6289 0.4482 -0.2554 -0.1373 -0.1300 60  TRP C CD1 
4322  C CD2 . TRP C 60  ? 0.9387 0.5780 0.4352 -0.2039 -0.1340 -0.1155 60  TRP C CD2 
4323  N NE1 . TRP C 60  ? 1.0618 0.5885 0.4499 -0.2362 -0.1298 -0.1312 60  TRP C NE1 
4324  C CE2 . TRP C 60  ? 1.0078 0.5589 0.4420 -0.2044 -0.1280 -0.1224 60  TRP C CE2 
4325  C CE3 . TRP C 60  ? 0.8800 0.5542 0.4267 -0.1763 -0.1329 -0.1063 60  TRP C CE3 
4326  C CZ2 . TRP C 60  ? 1.0174 0.5211 0.4408 -0.1752 -0.1216 -0.1202 60  TRP C CZ2 
4327  C CZ3 . TRP C 60  ? 0.8870 0.5161 0.4251 -0.1519 -0.1264 -0.1045 60  TRP C CZ3 
4328  C CH2 . TRP C 60  ? 0.9537 0.5018 0.4321 -0.1501 -0.1211 -0.1113 60  TRP C CH2 
4329  N N   . LEU C 61  ? 0.8844 0.6277 0.4243 -0.1841 -0.1446 -0.1169 61  LEU C N   
4330  C CA  . LEU C 61  ? 0.9017 0.5978 0.4217 -0.1590 -0.1390 -0.1202 61  LEU C CA  
4331  C C   . LEU C 61  ? 0.9168 0.6200 0.4223 -0.1634 -0.1419 -0.1253 61  LEU C C   
4332  O O   . LEU C 61  ? 0.9620 0.6108 0.4256 -0.1605 -0.1381 -0.1327 61  LEU C O   
4333  C CB  . LEU C 61  ? 0.8520 0.5650 0.4116 -0.1220 -0.1349 -0.1123 61  LEU C CB  
4334  C CG  . LEU C 61  ? 0.8448 0.5368 0.4111 -0.1109 -0.1301 -0.1086 61  LEU C CG  
4335  C CD1 . LEU C 61  ? 0.8010 0.5122 0.4015 -0.0775 -0.1256 -0.1025 61  LEU C CD1 
4336  C CD2 . LEU C 61  ? 0.9077 0.5240 0.4193 -0.1142 -0.1253 -0.1159 61  LEU C CD2 
4337  N N   . LEU C 62  ? 0.8825 0.6511 0.4192 -0.1680 -0.1485 -0.1213 62  LEU C N   
4338  C CA  . LEU C 62  ? 0.8968 0.6780 0.4200 -0.1744 -0.1521 -0.1259 62  LEU C CA  
4339  C C   . LEU C 62  ? 0.9525 0.7158 0.4311 -0.2145 -0.1554 -0.1358 62  LEU C C   
4340  O O   . LEU C 62  ? 0.9814 0.7318 0.4335 -0.2224 -0.1566 -0.1422 62  LEU C O   
4341  C CB  . LEU C 62  ? 0.8483 0.7036 0.4134 -0.1640 -0.1582 -0.1182 62  LEU C CB  
4342  C CG  . LEU C 62  ? 0.8061 0.6698 0.4027 -0.1275 -0.1540 -0.1098 62  LEU C CG  
4343  C CD1 . LEU C 62  ? 0.7677 0.6958 0.3977 -0.1174 -0.1595 -0.1009 62  LEU C CD1 
4344  C CD2 . LEU C 62  ? 0.8213 0.6513 0.3997 -0.1122 -0.1494 -0.1140 62  LEU C CD2 
4345  N N   . GLY C 63  ? 0.9712 0.7323 0.4384 -0.2422 -0.1563 -0.1374 63  GLY C N   
4346  C CA  . GLY C 63  ? 1.0314 0.7728 0.4500 -0.2873 -0.1583 -0.1475 63  GLY C CA  
4347  C C   . GLY C 63  ? 1.0138 0.8404 0.4524 -0.3118 -0.1674 -0.1479 63  GLY C C   
4348  O O   . GLY C 63  ? 1.0508 0.8773 0.4578 -0.3372 -0.1702 -0.1560 63  GLY C O   
4349  N N   . ASN C 64  ? 0.9597 0.8608 0.4489 -0.3024 -0.1720 -0.1392 64  ASN C N   
4350  C CA  . ASN C 64  ? 0.9428 0.9356 0.4522 -0.3220 -0.1809 -0.1391 64  ASN C CA  
4351  C C   . ASN C 64  ? 0.9980 0.9893 0.4650 -0.3781 -0.1822 -0.1497 64  ASN C C   
4352  O O   . ASN C 64  ? 1.0257 0.9718 0.4699 -0.3970 -0.1774 -0.1520 64  ASN C O   
4353  C CB  . ASN C 64  ? 0.8817 0.9428 0.4463 -0.2968 -0.1839 -0.1276 64  ASN C CB  
4354  C CG  . ASN C 64  ? 0.8675 1.0294 0.4511 -0.3161 -0.1927 -0.1274 64  ASN C CG  
4355  O OD1 . ASN C 64  ? 0.9043 1.0856 0.4610 -0.3609 -0.1953 -0.1364 64  ASN C OD1 
4356  N ND2 . ASN C 64  ? 0.8178 1.0451 0.4448 -0.2819 -0.1968 -0.1173 64  ASN C ND2 
4357  N N   . PRO C 65  ? 1.0187 1.0578 0.4710 -0.4067 -0.1884 -0.1566 65  PRO C N   
4358  C CA  . PRO C 65  ? 1.0803 1.1166 0.4839 -0.4671 -0.1891 -0.1685 65  PRO C CA  
4359  C C   . PRO C 65  ? 1.0786 1.1589 0.4904 -0.4973 -0.1900 -0.1684 65  PRO C C   
4360  O O   . PRO C 65  ? 1.1403 1.1860 0.5008 -0.5483 -0.1869 -0.1781 65  PRO C O   
4361  C CB  . PRO C 65  ? 1.0798 1.1926 0.4862 -0.4826 -0.1974 -0.1731 65  PRO C CB  
4362  C CG  . PRO C 65  ? 1.0120 1.1825 0.4752 -0.4289 -0.2022 -0.1617 65  PRO C CG  
4363  C CD  . PRO C 65  ? 0.9899 1.0860 0.4661 -0.3850 -0.1948 -0.1539 65  PRO C CD  
4364  N N   . MET C 66  ? 1.0144 1.1667 0.4851 -0.4674 -0.1936 -0.1578 66  MET C N   
4365  C CA  . MET C 66  ? 1.0063 1.2025 0.4903 -0.4895 -0.1940 -0.1565 66  MET C CA  
4366  C C   . MET C 66  ? 1.0258 1.1279 0.4900 -0.4870 -0.1850 -0.1548 66  MET C C   
4367  O O   . MET C 66  ? 1.0409 1.1506 0.4959 -0.5169 -0.1833 -0.1565 66  MET C O   
4368  C CB  . MET C 66  ? 0.9335 1.2316 0.4841 -0.4514 -0.2002 -0.1451 66  MET C CB  
4369  C CG  . MET C 66  ? 0.9106 1.3076 0.4839 -0.4419 -0.2095 -0.1445 66  MET C CG  
4370  S SD  . MET C 66  ? 0.9549 1.4351 0.4985 -0.5101 -0.2156 -0.1582 66  MET C SD  
4371  C CE  . MET C 66  ? 0.8997 1.5280 0.4958 -0.4749 -0.2273 -0.1512 66  MET C CE  
4372  N N   . CYS C 67  ? 1.0261 1.0439 0.4833 -0.4505 -0.1793 -0.1514 67  CYS C N   
4373  C CA  . CYS C 67  ? 1.0423 0.9727 0.4822 -0.4385 -0.1709 -0.1489 67  CYS C CA  
4374  C C   . CYS C 67  ? 1.1280 0.9471 0.4900 -0.4646 -0.1639 -0.1593 67  CYS C C   
4375  O O   . CYS C 67  ? 1.1458 0.8791 0.4873 -0.4376 -0.1569 -0.1577 67  CYS C O   
4376  C CB  . CYS C 67  ? 0.9868 0.9053 0.4699 -0.3787 -0.1688 -0.1384 67  CYS C CB  
4377  S SG  . CYS C 67  ? 0.9012 0.9363 0.4614 -0.3457 -0.1763 -0.1264 67  CYS C SG  
4378  N N   . ASP C 68  ? 1.1850 1.0073 0.5002 -0.5171 -0.1656 -0.1702 68  ASP C N   
4379  C CA  . ASP C 68  ? 1.2814 0.9936 0.5096 -0.5500 -0.1585 -0.1812 68  ASP C CA  
4380  C C   . ASP C 68  ? 1.3271 0.9615 0.5150 -0.5636 -0.1507 -0.1815 68  ASP C C   
4381  O O   . ASP C 68  ? 1.4058 0.9257 0.5208 -0.5703 -0.1429 -0.1874 68  ASP C O   
4382  C CB  . ASP C 68  ? 1.3340 1.0763 0.5201 -0.6115 -0.1619 -0.1932 68  ASP C CB  
4383  C CG  . ASP C 68  ? 1.3236 1.0958 0.5171 -0.6012 -0.1669 -0.1962 68  ASP C CG  
4384  O OD1 . ASP C 68  ? 1.2738 1.0472 0.5069 -0.5472 -0.1678 -0.1887 68  ASP C OD1 
4385  O OD2 . ASP C 68  ? 1.3680 1.1635 0.5255 -0.6497 -0.1697 -0.2065 68  ASP C OD2 
4386  N N   . GLU C 69  ? 1.2828 0.9768 0.5136 -0.5664 -0.1527 -0.1751 69  GLU C N   
4387  C CA  . GLU C 69  ? 1.3165 0.9424 0.5172 -0.5730 -0.1457 -0.1736 69  GLU C CA  
4388  C C   . GLU C 69  ? 1.3156 0.8542 0.5108 -0.5178 -0.1393 -0.1677 69  GLU C C   
4389  O O   . GLU C 69  ? 1.3807 0.8196 0.5162 -0.5224 -0.1315 -0.1700 69  GLU C O   
4390  C CB  . GLU C 69  ? 1.2534 0.9719 0.5147 -0.5759 -0.1497 -0.1662 69  GLU C CB  
4391  C CG  . GLU C 69  ? 1.2874 0.9444 0.5190 -0.5879 -0.1430 -0.1648 69  GLU C CG  
4392  C CD  . GLU C 69  ? 1.2262 0.9790 0.5170 -0.5925 -0.1469 -0.1581 69  GLU C CD  
4393  O OE1 . GLU C 69  ? 1.1690 1.0379 0.5146 -0.5940 -0.1549 -0.1562 69  GLU C OE1 
4394  O OE2 . GLU C 69  ? 1.2380 0.9492 0.5182 -0.5924 -0.1419 -0.1547 69  GLU C OE2 
4395  N N   . PHE C 70  ? 1.2469 0.8237 0.4999 -0.4665 -0.1423 -0.1605 70  PHE C N   
4396  C CA  . PHE C 70  ? 1.2275 0.7517 0.4925 -0.4119 -0.1372 -0.1538 70  PHE C CA  
4397  C C   . PHE C 70  ? 1.2629 0.7205 0.4920 -0.3858 -0.1335 -0.1582 70  PHE C C   
4398  O O   . PHE C 70  ? 1.2235 0.6771 0.4832 -0.3367 -0.1316 -0.1524 70  PHE C O   
4399  C CB  . PHE C 70  ? 1.1265 0.7390 0.4803 -0.3732 -0.1416 -0.1420 70  PHE C CB  
4400  C CG  . PHE C 70  ? 1.0894 0.7774 0.4810 -0.3954 -0.1458 -0.1378 70  PHE C CG  
4401  C CD1 . PHE C 70  ? 1.1128 0.7657 0.4852 -0.4100 -0.1416 -0.1368 70  PHE C CD1 
4402  C CD2 . PHE C 70  ? 1.0360 0.8301 0.4780 -0.4008 -0.1539 -0.1351 70  PHE C CD2 
4403  C CE1 . PHE C 70  ? 1.0800 0.8053 0.4864 -0.4307 -0.1451 -0.1334 70  PHE C CE1 
4404  C CE2 . PHE C 70  ? 1.0049 0.8730 0.4795 -0.4181 -0.1576 -0.1316 70  PHE C CE2 
4405  C CZ  . PHE C 70  ? 1.0255 0.8606 0.4837 -0.4343 -0.1532 -0.1310 70  PHE C CZ  
4406  N N   . ILE C 71  ? 1.3400 0.7470 0.5019 -0.4201 -0.1321 -0.1689 71  ILE C N   
4407  C CA  . ILE C 71  ? 1.3963 0.7176 0.5042 -0.3984 -0.1267 -0.1746 71  ILE C CA  
4408  C C   . ILE C 71  ? 1.4791 0.6822 0.5123 -0.3924 -0.1173 -0.1773 71  ILE C C   
4409  O O   . ILE C 71  ? 1.5409 0.7010 0.5220 -0.4346 -0.1146 -0.1816 71  ILE C O   
4410  C CB  . ILE C 71  ? 1.4479 0.7610 0.5111 -0.4358 -0.1290 -0.1853 71  ILE C CB  
4411  C CG1 . ILE C 71  ? 1.5332 0.7319 0.5163 -0.4210 -0.1213 -0.1929 71  ILE C CG1 
4412  C CG2 . ILE C 71  ? 1.4983 0.8193 0.5219 -0.5037 -0.1305 -0.1926 71  ILE C CG2 
4413  C CD1 . ILE C 71  ? 1.5638 0.7646 0.5193 -0.4422 -0.1239 -0.2017 71  ILE C CD1 
4414  N N   . ASN C 72  ? 1.4831 0.6365 0.5088 -0.3397 -0.1122 -0.1747 72  ASN C N   
4415  C CA  . ASN C 72  ? 1.5574 0.6030 0.5153 -0.3203 -0.1033 -0.1758 72  ASN C CA  
4416  C C   . ASN C 72  ? 1.5491 0.5959 0.5168 -0.3317 -0.1022 -0.1701 72  ASN C C   
4417  O O   . ASN C 72  ? 1.6373 0.6004 0.5284 -0.3602 -0.0969 -0.1747 72  ASN C O   
4418  C CB  . ASN C 72  ? 1.6838 0.6140 0.5285 -0.3482 -0.0972 -0.1875 72  ASN C CB  
4419  C CG  . ASN C 72  ? 1.7045 0.6112 0.5278 -0.3237 -0.0961 -0.1930 72  ASN C CG  
4420  O OD1 . ASN C 72  ? 1.6251 0.6011 0.5176 -0.2860 -0.0996 -0.1881 72  ASN C OD1 
4421  N ND2 . ASN C 72  ? 1.8168 0.6215 0.5392 -0.3466 -0.0905 -0.2035 72  ASN C ND2 
4422  N N   . VAL C 73  ? 1.4488 0.5862 0.5063 -0.3098 -0.1067 -0.1602 73  VAL C N   
4423  C CA  . VAL C 73  ? 1.4303 0.5795 0.5063 -0.3181 -0.1061 -0.1541 73  VAL C CA  
4424  C C   . VAL C 73  ? 1.4853 0.5408 0.5097 -0.2862 -0.0980 -0.1525 73  VAL C C   
4425  O O   . VAL C 73  ? 1.4941 0.5152 0.5074 -0.2384 -0.0943 -0.1522 73  VAL C O   
4426  C CB  . VAL C 73  ? 1.3130 0.5762 0.4941 -0.2975 -0.1122 -0.1436 73  VAL C CB  
4427  C CG1 . VAL C 73  ? 1.2669 0.6238 0.4926 -0.3330 -0.1204 -0.1441 73  VAL C CG1 
4428  C CG2 . VAL C 73  ? 1.2580 0.5441 0.4838 -0.2407 -0.1115 -0.1384 73  VAL C CG2 
4429  N N   . PRO C 74  ? 1.5238 0.5415 0.5156 -0.3115 -0.0952 -0.1516 74  PRO C N   
4430  C CA  . PRO C 74  ? 1.5684 0.5066 0.5178 -0.2777 -0.0881 -0.1486 74  PRO C CA  
4431  C C   . PRO C 74  ? 1.4693 0.4814 0.5056 -0.2322 -0.0904 -0.1380 74  PRO C C   
4432  O O   . PRO C 74  ? 1.3741 0.4909 0.4963 -0.2360 -0.0969 -0.1328 74  PRO C O   
4433  C CB  . PRO C 74  ? 1.6338 0.5220 0.5278 -0.3277 -0.0853 -0.1508 74  PRO C CB  
4434  C CG  . PRO C 74  ? 1.5670 0.5618 0.5253 -0.3739 -0.0929 -0.1501 74  PRO C CG  
4435  C CD  . PRO C 74  ? 1.5225 0.5798 0.5203 -0.3705 -0.0986 -0.1529 74  PRO C CD  
4436  N N   . GLU C 75  ? 1.4957 0.4527 0.5054 -0.1894 -0.0847 -0.1349 75  GLU C N   
4437  C CA  . GLU C 75  ? 1.4088 0.4326 0.4945 -0.1473 -0.0860 -0.1257 75  GLU C CA  
4438  C C   . GLU C 75  ? 1.3506 0.4359 0.4906 -0.1742 -0.0897 -0.1192 75  GLU C C   
4439  O O   . GLU C 75  ? 1.3984 0.4480 0.4981 -0.2160 -0.0888 -0.1213 75  GLU C O   
4440  C CB  . GLU C 75  ? 1.4567 0.4116 0.4971 -0.0965 -0.0792 -0.1244 75  GLU C CB  
4441  C CG  . GLU C 75  ? 1.5116 0.4021 0.5042 -0.1040 -0.0751 -0.1219 75  GLU C CG  
4442  C CD  . GLU C 75  ? 1.5504 0.3874 0.5060 -0.0459 -0.0692 -0.1197 75  GLU C CD  
4443  O OE1 . GLU C 75  ? 1.6316 0.3902 0.5132 -0.0198 -0.0642 -0.1254 75  GLU C OE1 
4444  O OE2 . GLU C 75  ? 1.5017 0.3771 0.5008 -0.0248 -0.0694 -0.1124 75  GLU C OE2 
4445  N N   . TRP C 76  ? 1.2511 0.4271 0.4787 -0.1506 -0.0933 -0.1116 76  TRP C N   
4446  C CA  . TRP C 76  ? 1.1861 0.4327 0.4741 -0.1712 -0.0974 -0.1050 76  TRP C CA  
4447  C C   . TRP C 76  ? 1.1406 0.4071 0.4670 -0.1333 -0.0952 -0.0970 76  TRP C C   
4448  O O   . TRP C 76  ? 1.1240 0.3927 0.4621 -0.0900 -0.0928 -0.0957 76  TRP C O   
4449  C CB  . TRP C 76  ? 1.1086 0.4530 0.4666 -0.1836 -0.1043 -0.1031 76  TRP C CB  
4450  C CG  . TRP C 76  ? 1.0538 0.4398 0.4571 -0.1428 -0.1048 -0.1005 76  TRP C CG  
4451  C CD1 . TRP C 76  ? 0.9818 0.4243 0.4473 -0.1129 -0.1050 -0.0930 76  TRP C CD1 
4452  C CD2 . TRP C 76  ? 1.0713 0.4437 0.4567 -0.1302 -0.1046 -0.1059 76  TRP C CD2 
4453  N NE1 . TRP C 76  ? 0.9549 0.4205 0.4409 -0.0850 -0.1045 -0.0935 76  TRP C NE1 
4454  C CE2 . TRP C 76  ? 1.0068 0.4319 0.4465 -0.0936 -0.1045 -0.1013 76  TRP C CE2 
4455  C CE3 . TRP C 76  ? 1.1383 0.4580 0.4644 -0.1481 -0.1040 -0.1146 76  TRP C CE3 
4456  C CZ2 . TRP C 76  ? 1.0051 0.4349 0.4436 -0.0744 -0.1039 -0.1049 76  TRP C CZ2 
4457  C CZ3 . TRP C 76  ? 1.1351 0.4585 0.4613 -0.1264 -0.1037 -0.1180 76  TRP C CZ3 
4458  C CH2 . TRP C 76  ? 1.0678 0.4474 0.4509 -0.0898 -0.1037 -0.1131 76  TRP C CH2 
4459  N N   . SER C 77  ? 1.1218 0.4065 0.4668 -0.1511 -0.0959 -0.0922 77  SER C N   
4460  C CA  . SER C 77  ? 1.0697 0.3859 0.4594 -0.1210 -0.0947 -0.0844 77  SER C CA  
4461  C C   . SER C 77  ? 0.9718 0.3869 0.4473 -0.1093 -0.0990 -0.0789 77  SER C C   
4462  O O   . SER C 77  ? 0.9300 0.3719 0.4396 -0.0733 -0.0973 -0.0750 77  SER C O   
4463  C CB  . SER C 77  ? 1.0845 0.3874 0.4640 -0.1471 -0.0940 -0.0813 77  SER C CB  
4464  O OG  . SER C 77  ? 1.0795 0.4169 0.4675 -0.1953 -0.0982 -0.0834 77  SER C OG  
4465  N N   . TYR C 78  ? 0.9408 0.4092 0.4459 -0.1407 -0.1043 -0.0790 78  TYR C N   
4466  C CA  . TYR C 78  ? 0.8608 0.4142 0.4355 -0.1312 -0.1084 -0.0741 78  TYR C CA  
4467  C C   . TYR C 78  ? 0.8592 0.4479 0.4378 -0.1612 -0.1139 -0.0778 78  TYR C C   
4468  O O   . TYR C 78  ? 0.9135 0.4691 0.4467 -0.1946 -0.1146 -0.0839 78  TYR C O   
4469  C CB  . TYR C 78  ? 0.8062 0.4086 0.4298 -0.1290 -0.1091 -0.0661 78  TYR C CB  
4470  C CG  . TYR C 78  ? 0.8200 0.4310 0.4359 -0.1666 -0.1113 -0.0661 78  TYR C CG  
4471  C CD1 . TYR C 78  ? 0.8754 0.4246 0.4435 -0.1809 -0.1077 -0.0679 78  TYR C CD1 
4472  C CD2 . TYR C 78  ? 0.7814 0.4637 0.4345 -0.1869 -0.1167 -0.0643 78  TYR C CD2 
4473  C CE1 . TYR C 78  ? 0.8905 0.4504 0.4496 -0.2193 -0.1091 -0.0684 78  TYR C CE1 
4474  C CE2 . TYR C 78  ? 0.7935 0.4943 0.4408 -0.2220 -0.1186 -0.0649 78  TYR C CE2 
4475  C CZ  . TYR C 78  ? 0.8472 0.4875 0.4482 -0.2404 -0.1146 -0.0672 78  TYR C CZ  
4476  O OH  . TYR C 78  ? 0.8610 0.5228 0.4546 -0.2791 -0.1160 -0.0684 78  TYR C OH  
4477  N N   . ILE C 79  ? 0.8016 0.4559 0.4302 -0.1499 -0.1175 -0.0742 79  ILE C N   
4478  C CA  . ILE C 79  ? 0.7960 0.4926 0.4320 -0.1719 -0.1232 -0.0770 79  ILE C CA  
4479  C C   . ILE C 79  ? 0.7462 0.5197 0.4297 -0.1812 -0.1279 -0.0711 79  ILE C C   
4480  O O   . ILE C 79  ? 0.7007 0.5022 0.4230 -0.1594 -0.1267 -0.0637 79  ILE C O   
4481  C CB  . ILE C 79  ? 0.7787 0.4870 0.4259 -0.1495 -0.1238 -0.0780 79  ILE C CB  
4482  C CG1 . ILE C 79  ? 0.8337 0.4694 0.4297 -0.1400 -0.1193 -0.0849 79  ILE C CG1 
4483  C CG2 . ILE C 79  ? 0.7688 0.5274 0.4269 -0.1689 -0.1302 -0.0798 79  ILE C CG2 
4484  C CD1 . ILE C 79  ? 0.8139 0.4581 0.4230 -0.1108 -0.1179 -0.0852 79  ILE C CD1 
4485  N N   . VAL C 80  ? 0.7587 0.5679 0.4364 -0.2133 -0.1329 -0.0746 80  VAL C N   
4486  C CA  . VAL C 80  ? 0.7167 0.6068 0.4357 -0.2199 -0.1379 -0.0697 80  VAL C CA  
4487  C C   . VAL C 80  ? 0.7035 0.6497 0.4360 -0.2220 -0.1439 -0.0711 80  VAL C C   
4488  O O   . VAL C 80  ? 0.7413 0.6817 0.4427 -0.2491 -0.1464 -0.0788 80  VAL C O   
4489  C CB  . VAL C 80  ? 0.7413 0.6422 0.4445 -0.2580 -0.1387 -0.0724 80  VAL C CB  
4490  C CG1 . VAL C 80  ? 0.6948 0.6870 0.4430 -0.2588 -0.1435 -0.0672 80  VAL C CG1 
4491  C CG2 . VAL C 80  ? 0.7629 0.6008 0.4457 -0.2561 -0.1325 -0.0711 80  VAL C CG2 
4492  N N   . GLU C 81  ? 0.6550 0.6523 0.4293 -0.1934 -0.1460 -0.0636 81  GLU C N   
4493  C CA  . GLU C 81  ? 0.6411 0.6913 0.4286 -0.1867 -0.1516 -0.0632 81  GLU C CA  
4494  C C   . GLU C 81  ? 0.6047 0.7311 0.4282 -0.1756 -0.1555 -0.0562 81  GLU C C   
4495  O O   . GLU C 81  ? 0.5788 0.7062 0.4240 -0.1567 -0.1524 -0.0494 81  GLU C O   
4496  C CB  . GLU C 81  ? 0.6283 0.6509 0.4203 -0.1549 -0.1489 -0.0606 81  GLU C CB  
4497  C CG  . GLU C 81  ? 0.6215 0.6849 0.4187 -0.1470 -0.1540 -0.0605 81  GLU C CG  
4498  C CD  . GLU C 81  ? 0.6091 0.6459 0.4102 -0.1167 -0.1504 -0.0573 81  GLU C CD  
4499  O OE1 . GLU C 81  ? 0.5864 0.6077 0.4036 -0.0944 -0.1453 -0.0514 81  GLU C OE1 
4500  O OE2 . GLU C 81  ? 0.6237 0.6572 0.4106 -0.1174 -0.1524 -0.0612 81  GLU C OE2 
4501  N N   . LYS C 82  ? 0.6065 0.7982 0.4338 -0.1856 -0.1622 -0.0580 82  LYS C N   
4502  C CA  . LYS C 82  ? 0.5771 0.8470 0.4344 -0.1689 -0.1663 -0.0515 82  LYS C CA  
4503  C C   . LYS C 82  ? 0.5520 0.8223 0.4264 -0.1239 -0.1651 -0.0427 82  LYS C C   
4504  O O   . LYS C 82  ? 0.5561 0.7776 0.4208 -0.1104 -0.1621 -0.0426 82  LYS C O   
4505  C CB  . LYS C 82  ? 0.5887 0.9360 0.4423 -0.1914 -0.1741 -0.0567 82  LYS C CB  
4506  C CG  . LYS C 82  ? 0.6105 0.9816 0.4522 -0.2367 -0.1750 -0.0636 82  LYS C CG  
4507  C CD  . LYS C 82  ? 0.6220 1.0810 0.4604 -0.2615 -0.1826 -0.0696 82  LYS C CD  
4508  C CE  . LYS C 82  ? 0.6372 1.1408 0.4700 -0.3043 -0.1833 -0.0751 82  LYS C CE  
4509  N NZ  . LYS C 82  ? 0.6866 1.1161 0.4762 -0.3517 -0.1787 -0.0843 82  LYS C NZ  
4510  N N   . ALA C 83  ? 0.5317 0.8554 0.4271 -0.1014 -0.1670 -0.0355 83  ALA C N   
4511  C CA  . ALA C 83  ? 0.5185 0.8387 0.4208 -0.0595 -0.1653 -0.0268 83  ALA C CA  
4512  C C   . ALA C 83  ? 0.5314 0.8736 0.4222 -0.0477 -0.1701 -0.0274 83  ALA C C   
4513  O O   . ALA C 83  ? 0.5345 0.8375 0.4169 -0.0246 -0.1668 -0.0236 83  ALA C O   
4514  C CB  . ALA C 83  ? 0.5011 0.8691 0.4206 -0.0370 -0.1659 -0.0193 83  ALA C CB  
4515  N N   . ASN C 84  ? 0.5429 0.9491 0.4315 -0.0657 -0.1776 -0.0326 84  ASN C N   
4516  C CA  . ASN C 84  ? 0.5556 0.9918 0.4332 -0.0556 -0.1831 -0.0336 84  ASN C CA  
4517  C C   . ASN C 84  ? 0.5767 1.0366 0.4414 -0.0968 -0.1882 -0.0446 84  ASN C C   
4518  O O   . ASN C 84  ? 0.5810 1.1212 0.4480 -0.1051 -0.1954 -0.0473 84  ASN C O   
4519  C CB  . ASN C 84  ? 0.5496 1.0610 0.4354 -0.0222 -0.1881 -0.0266 84  ASN C CB  
4520  C CG  . ASN C 84  ? 0.5401 1.0202 0.4290 0.0184  -0.1824 -0.0159 84  ASN C CG  
4521  O OD1 . ASN C 84  ? 0.5458 0.9627 0.4220 0.0376  -0.1771 -0.0117 84  ASN C OD1 
4522  N ND2 . ASN C 84  ? 0.5291 1.0527 0.4320 0.0294  -0.1828 -0.0118 84  ASN C ND2 
4523  N N   . PRO C 85  ? 0.5938 0.9844 0.4413 -0.1221 -0.1841 -0.0513 85  PRO C N   
4524  C CA  . PRO C 85  ? 0.6234 1.0217 0.4493 -0.1642 -0.1876 -0.0623 85  PRO C CA  
4525  C C   . PRO C 85  ? 0.6327 1.0758 0.4509 -0.1592 -0.1943 -0.0644 85  PRO C C   
4526  O O   . PRO C 85  ? 0.6289 1.0441 0.4446 -0.1299 -0.1932 -0.0601 85  PRO C O   
4527  C CB  . PRO C 85  ? 0.6429 0.9435 0.4468 -0.1765 -0.1807 -0.0668 85  PRO C CB  
4528  C CG  . PRO C 85  ? 0.6195 0.8771 0.4394 -0.1502 -0.1740 -0.0591 85  PRO C CG  
4529  C CD  . PRO C 85  ? 0.5911 0.8942 0.4340 -0.1119 -0.1759 -0.0493 85  PRO C CD  
4530  N N   . VAL C 86  ? 0.6469 1.1612 0.4599 -0.1893 -0.2009 -0.0713 86  VAL C N   
4531  C CA  . VAL C 86  ? 0.6554 1.2260 0.4619 -0.1860 -0.2082 -0.0738 86  VAL C CA  
4532  C C   . VAL C 86  ? 0.6819 1.1905 0.4604 -0.2024 -0.2068 -0.0808 86  VAL C C   
4533  O O   . VAL C 86  ? 0.6833 1.2023 0.4582 -0.1809 -0.2099 -0.0788 86  VAL C O   
4534  C CB  . VAL C 86  ? 0.6641 1.3408 0.4728 -0.2169 -0.2158 -0.0803 86  VAL C CB  
4535  C CG1 . VAL C 86  ? 0.6369 1.3872 0.4737 -0.1940 -0.2178 -0.0731 86  VAL C CG1 
4536  C CG2 . VAL C 86  ? 0.6983 1.3523 0.4813 -0.2789 -0.2139 -0.0925 86  VAL C CG2 
4537  N N   . ASN C 87  ? 0.7076 1.1497 0.4622 -0.2388 -0.2018 -0.0887 87  ASN C N   
4538  C CA  . ASN C 87  ? 0.7391 1.1168 0.4612 -0.2551 -0.1997 -0.0963 87  ASN C CA  
4539  C C   . ASN C 87  ? 0.7286 1.0214 0.4507 -0.2224 -0.1926 -0.0912 87  ASN C C   
4540  O O   . ASN C 87  ? 0.7476 0.9639 0.4508 -0.2332 -0.1859 -0.0947 87  ASN C O   
4541  C CB  . ASN C 87  ? 0.7853 1.1246 0.4704 -0.3086 -0.1972 -0.1078 87  ASN C CB  
4542  C CG  . ASN C 87  ? 0.8061 1.2278 0.4808 -0.3511 -0.2040 -0.1160 87  ASN C CG  
4543  O OD1 . ASN C 87  ? 0.7939 1.2938 0.4816 -0.3421 -0.2114 -0.1154 87  ASN C OD1 
4544  N ND2 . ASN C 87  ? 0.8418 1.2466 0.4893 -0.3988 -0.2014 -0.1239 87  ASN C ND2 
4545  N N   . ASP C 88  ? 0.7019 1.0102 0.4416 -0.1821 -0.1937 -0.0830 88  ASP C N   
4546  C CA  . ASP C 88  ? 0.6915 0.9318 0.4313 -0.1527 -0.1869 -0.0784 88  ASP C CA  
4547  C C   . ASP C 88  ? 0.7111 0.9311 0.4295 -0.1528 -0.1881 -0.0831 88  ASP C C   
4548  O O   . ASP C 88  ? 0.7441 0.9392 0.4353 -0.1836 -0.1884 -0.0930 88  ASP C O   
4549  C CB  . ASP C 88  ? 0.6575 0.9185 0.4234 -0.1117 -0.1858 -0.0663 88  ASP C CB  
4550  C CG  . ASP C 88  ? 0.6480 0.8408 0.4142 -0.0875 -0.1773 -0.0617 88  ASP C CG  
4551  O OD1 . ASP C 88  ? 0.6625 0.7970 0.4136 -0.0993 -0.1723 -0.0676 88  ASP C OD1 
4552  O OD2 . ASP C 88  ? 0.6299 0.8282 0.4078 -0.0564 -0.1753 -0.0526 88  ASP C OD2 
4553  N N   . LEU C 89  ? 0.6958 0.9222 0.4215 -0.1197 -0.1883 -0.0763 89  LEU C N   
4554  C CA  . LEU C 89  ? 0.7125 0.9258 0.4193 -0.1175 -0.1898 -0.0799 89  LEU C CA  
4555  C C   . LEU C 89  ? 0.7202 1.0093 0.4244 -0.1272 -0.1995 -0.0822 89  LEU C C   
4556  O O   . LEU C 89  ? 0.7051 1.0460 0.4219 -0.1000 -0.2038 -0.0744 89  LEU C O   
4557  C CB  . LEU C 89  ? 0.6983 0.8839 0.4092 -0.0801 -0.1851 -0.0717 89  LEU C CB  
4558  C CG  . LEU C 89  ? 0.7008 0.8121 0.4034 -0.0744 -0.1758 -0.0733 89  LEU C CG  
4559  C CD1 . LEU C 89  ? 0.7087 0.7795 0.4069 -0.0951 -0.1713 -0.0794 89  LEU C CD1 
4560  C CD2 . LEU C 89  ? 0.6805 0.7765 0.3943 -0.0426 -0.1700 -0.0633 89  LEU C CD2 
4561  N N   . CYS C 90  ? 0.7481 1.0430 0.4318 -0.1657 -0.2026 -0.0931 90  CYS C N   
4562  C CA  . CYS C 90  ? 0.7588 1.1322 0.4381 -0.1822 -0.2119 -0.0972 90  CYS C CA  
4563  C C   . CYS C 90  ? 0.7562 1.1473 0.4325 -0.1535 -0.2155 -0.0931 90  CYS C C   
4564  O O   . CYS C 90  ? 0.7452 1.2090 0.4332 -0.1331 -0.2222 -0.0875 90  CYS C O   
4565  C CB  . CYS C 90  ? 0.7992 1.1602 0.4479 -0.2338 -0.2129 -0.1108 90  CYS C CB  
4566  S SG  . CYS C 90  ? 0.8365 1.0862 0.4471 -0.2459 -0.2050 -0.1190 90  CYS C SG  
4567  N N   . TYR C 91  ? 0.7691 1.0937 0.4272 -0.1501 -0.2107 -0.0958 91  TYR C N   
4568  C CA  . TYR C 91  ? 0.7668 1.0919 0.4205 -0.1198 -0.2119 -0.0906 91  TYR C CA  
4569  C C   . TYR C 91  ? 0.7426 1.0371 0.4108 -0.0799 -0.2058 -0.0789 91  TYR C C   
4570  O O   . TYR C 91  ? 0.7361 0.9703 0.4069 -0.0796 -0.1976 -0.0787 91  TYR C O   
4571  C CB  . TYR C 91  ? 0.7924 1.0597 0.4199 -0.1333 -0.2086 -0.0987 91  TYR C CB  
4572  C CG  . TYR C 91  ? 0.7979 1.0791 0.4160 -0.1119 -0.2117 -0.0957 91  TYR C CG  
4573  C CD1 . TYR C 91  ? 0.7871 1.0322 0.4068 -0.0769 -0.2063 -0.0871 91  TYR C CD1 
4574  C CD2 . TYR C 91  ? 0.8173 1.1479 0.4218 -0.1287 -0.2199 -0.1017 91  TYR C CD2 
4575  C CE1 . TYR C 91  ? 0.7974 1.0501 0.4035 -0.0583 -0.2087 -0.0841 91  TYR C CE1 
4576  C CE2 . TYR C 91  ? 0.8243 1.1669 0.4184 -0.1079 -0.2229 -0.0986 91  TYR C CE2 
4577  C CZ  . TYR C 91  ? 0.8151 1.1162 0.4092 -0.0721 -0.2172 -0.0896 91  TYR C CZ  
4578  O OH  . TYR C 91  ? 0.8270 1.1349 0.4059 -0.0524 -0.2197 -0.0864 91  TYR C OH  
4579  N N   . PRO C 92  ? 0.7344 1.0679 0.4070 -0.0459 -0.2094 -0.0693 92  PRO C N   
4580  C CA  . PRO C 92  ? 0.7194 1.0227 0.3989 -0.0113 -0.2031 -0.0581 92  PRO C CA  
4581  C C   . PRO C 92  ? 0.7225 0.9471 0.3908 -0.0043 -0.1935 -0.0575 92  PRO C C   
4582  O O   . PRO C 92  ? 0.7381 0.9396 0.3902 -0.0135 -0.1930 -0.0632 92  PRO C O   
4583  C CB  . PRO C 92  ? 0.7269 1.0781 0.3983 0.0235  -0.2089 -0.0493 92  PRO C CB  
4584  C CG  . PRO C 92  ? 0.7369 1.1617 0.4066 0.0066  -0.2194 -0.0558 92  PRO C CG  
4585  C CD  . PRO C 92  ? 0.7464 1.1430 0.4100 -0.0357 -0.2183 -0.0684 92  PRO C CD  
4586  N N   . GLY C 93  ? 0.7087 0.8968 0.3846 0.0109  -0.1859 -0.0510 93  GLY C N   
4587  C CA  . GLY C 93  ? 0.7109 0.8341 0.3770 0.0164  -0.1762 -0.0505 93  GLY C CA  
4588  C C   . GLY C 93  ? 0.6938 0.7846 0.3725 0.0224  -0.1680 -0.0462 93  GLY C C   
4589  O O   . GLY C 93  ? 0.6817 0.7953 0.3733 0.0317  -0.1694 -0.0404 93  GLY C O   
4590  N N   . ASP C 94  ? 0.6935 0.7351 0.3677 0.0176  -0.1595 -0.0493 94  ASP C N   
4591  C CA  . ASP C 94  ? 0.6779 0.6900 0.3634 0.0200  -0.1512 -0.0469 94  ASP C CA  
4592  C C   . ASP C 94  ? 0.6746 0.6610 0.3650 0.0013  -0.1475 -0.0562 94  ASP C C   
4593  O O   . ASP C 94  ? 0.6895 0.6673 0.3677 -0.0099 -0.1489 -0.0641 94  ASP C O   
4594  C CB  . ASP C 94  ? 0.6863 0.6652 0.3558 0.0359  -0.1427 -0.0409 94  ASP C CB  
4595  C CG  . ASP C 94  ? 0.7010 0.6905 0.3542 0.0588  -0.1448 -0.0308 94  ASP C CG  
4596  O OD1 . ASP C 94  ? 0.6936 0.6990 0.3555 0.0696  -0.1464 -0.0246 94  ASP C OD1 
4597  O OD2 . ASP C 94  ? 0.7241 0.7034 0.3522 0.0678  -0.1447 -0.0289 94  ASP C OD2 
4598  N N   . PHE C 95  ? 0.6584 0.6310 0.3634 0.0002  -0.1425 -0.0553 95  PHE C N   
4599  C CA  . PHE C 95  ? 0.6585 0.6020 0.3641 -0.0100 -0.1375 -0.0627 95  PHE C CA  
4600  C C   . PHE C 95  ? 0.6483 0.5703 0.3567 0.0013  -0.1277 -0.0596 95  PHE C C   
4601  O O   . PHE C 95  ? 0.6335 0.5589 0.3533 0.0084  -0.1249 -0.0528 95  PHE C O   
4602  C CB  . PHE C 95  ? 0.6522 0.6014 0.3698 -0.0225 -0.1404 -0.0647 95  PHE C CB  
4603  C CG  . PHE C 95  ? 0.6691 0.5863 0.3743 -0.0349 -0.1381 -0.0740 95  PHE C CG  
4604  C CD1 . PHE C 95  ? 0.6689 0.5559 0.3711 -0.0258 -0.1299 -0.0765 95  PHE C CD1 
4605  C CD2 . PHE C 95  ? 0.6910 0.6078 0.3824 -0.0555 -0.1437 -0.0806 95  PHE C CD2 
4606  C CE1 . PHE C 95  ? 0.6918 0.5461 0.3762 -0.0312 -0.1276 -0.0848 95  PHE C CE1 
4607  C CE2 . PHE C 95  ? 0.7182 0.5937 0.3875 -0.0652 -0.1408 -0.0890 95  PHE C CE2 
4608  C CZ  . PHE C 95  ? 0.7195 0.5621 0.3845 -0.0501 -0.1329 -0.0908 95  PHE C CZ  
4609  N N   . ASN C 96  ? 0.6581 0.5609 0.3541 0.0019  -0.1223 -0.0650 96  ASN C N   
4610  C CA  . ASN C 96  ? 0.6521 0.5431 0.3474 0.0089  -0.1126 -0.0632 96  ASN C CA  
4611  C C   . ASN C 96  ? 0.6379 0.5226 0.3475 0.0088  -0.1076 -0.0653 96  ASN C C   
4612  O O   . ASN C 96  ? 0.6442 0.5195 0.3526 0.0057  -0.1087 -0.0721 96  ASN C O   
4613  C CB  . ASN C 96  ? 0.6684 0.5499 0.3459 0.0090  -0.1085 -0.0691 96  ASN C CB  
4614  C CG  . ASN C 96  ? 0.6679 0.5450 0.3390 0.0119  -0.0988 -0.0664 96  ASN C CG  
4615  O OD1 . ASN C 96  ? 0.6739 0.5477 0.3349 0.0144  -0.0975 -0.0589 96  ASN C OD1 
4616  N ND2 . ASN C 96  ? 0.6657 0.5426 0.3381 0.0116  -0.0915 -0.0727 96  ASN C ND2 
4617  N N   . ASP C 97  ? 0.6239 0.5102 0.3418 0.0126  -0.1017 -0.0595 97  ASP C N   
4618  C CA  . ASP C 97  ? 0.6083 0.4939 0.3413 0.0134  -0.0971 -0.0603 97  ASP C CA  
4619  C C   . ASP C 97  ? 0.6028 0.4874 0.3466 0.0101  -0.1034 -0.0616 97  ASP C C   
4620  O O   . ASP C 97  ? 0.6055 0.4801 0.3499 0.0110  -0.1015 -0.0670 97  ASP C O   
4621  C CB  . ASP C 97  ? 0.6130 0.4973 0.3410 0.0160  -0.0896 -0.0676 97  ASP C CB  
4622  C CG  . ASP C 97  ? 0.6156 0.5059 0.3347 0.0140  -0.0811 -0.0660 97  ASP C CG  
4623  O OD1 . ASP C 97  ? 0.6163 0.5027 0.3316 0.0112  -0.0794 -0.0584 97  ASP C OD1 
4624  O OD2 . ASP C 97  ? 0.6225 0.5205 0.3344 0.0150  -0.0754 -0.0726 97  ASP C OD2 
4625  N N   . TYR C 98  ? 0.5988 0.4944 0.3473 0.0068  -0.1105 -0.0568 98  TYR C N   
4626  C CA  . TYR C 98  ? 0.5974 0.4968 0.3531 -0.0017 -0.1168 -0.0582 98  TYR C CA  
4627  C C   . TYR C 98  ? 0.5805 0.4769 0.3521 -0.0002 -0.1134 -0.0556 98  TYR C C   
4628  O O   . TYR C 98  ? 0.5870 0.4712 0.3574 -0.0065 -0.1146 -0.0598 98  TYR C O   
4629  C CB  . TYR C 98  ? 0.5964 0.5219 0.3548 -0.0042 -0.1247 -0.0533 98  TYR C CB  
4630  C CG  . TYR C 98  ? 0.5985 0.5384 0.3622 -0.0182 -0.1316 -0.0553 98  TYR C CG  
4631  C CD1 . TYR C 98  ? 0.6191 0.5397 0.3688 -0.0334 -0.1332 -0.0638 98  TYR C CD1 
4632  C CD2 . TYR C 98  ? 0.5857 0.5581 0.3632 -0.0170 -0.1362 -0.0489 98  TYR C CD2 
4633  C CE1 . TYR C 98  ? 0.6280 0.5592 0.3762 -0.0519 -0.1387 -0.0662 98  TYR C CE1 
4634  C CE2 . TYR C 98  ? 0.5888 0.5816 0.3704 -0.0334 -0.1422 -0.0514 98  TYR C CE2 
4635  C CZ  . TYR C 98  ? 0.6106 0.5820 0.3769 -0.0534 -0.1432 -0.0601 98  TYR C CZ  
4636  O OH  . TYR C 98  ? 0.6200 0.6092 0.3847 -0.0751 -0.1483 -0.0630 98  TYR C OH  
4637  N N   . GLU C 99  ? 0.5637 0.4667 0.3453 0.0073  -0.1087 -0.0489 99  GLU C N   
4638  C CA  . GLU C 99  ? 0.5466 0.4495 0.3439 0.0088  -0.1054 -0.0458 99  GLU C CA  
4639  C C   . GLU C 99  ? 0.5463 0.4366 0.3429 0.0117  -0.0990 -0.0513 99  GLU C C   
4640  O O   . GLU C 99  ? 0.5413 0.4265 0.3457 0.0116  -0.0985 -0.0521 99  GLU C O   
4641  C CB  . GLU C 99  ? 0.5366 0.4454 0.3377 0.0153  -0.1014 -0.0374 99  GLU C CB  
4642  C CG  . GLU C 99  ? 0.5375 0.4617 0.3390 0.0194  -0.1076 -0.0308 99  GLU C CG  
4643  C CD  . GLU C 99  ? 0.5546 0.4834 0.3390 0.0229  -0.1115 -0.0306 99  GLU C CD  
4644  O OE1 . GLU C 99  ? 0.5662 0.4801 0.3349 0.0243  -0.1067 -0.0323 99  GLU C OE1 
4645  O OE2 . GLU C 99  ? 0.5571 0.5083 0.3429 0.0238  -0.1194 -0.0290 99  GLU C OE2 
4646  N N   . GLU C 100 ? 0.5534 0.4415 0.3391 0.0155  -0.0940 -0.0553 100 GLU C N   
4647  C CA  . GLU C 100 ? 0.5566 0.4417 0.3390 0.0220  -0.0883 -0.0616 100 GLU C CA  
4648  C C   . GLU C 100 ? 0.5773 0.4420 0.3465 0.0242  -0.0921 -0.0684 100 GLU C C   
4649  O O   . GLU C 100 ? 0.5828 0.4396 0.3491 0.0329  -0.0890 -0.0718 100 GLU C O   
4650  C CB  . GLU C 100 ? 0.5624 0.4565 0.3343 0.0243  -0.0822 -0.0650 100 GLU C CB  
4651  C CG  . GLU C 100 ? 0.5506 0.4579 0.3269 0.0199  -0.0751 -0.0601 100 GLU C CG  
4652  C CD  . GLU C 100 ? 0.5368 0.4583 0.3255 0.0224  -0.0691 -0.0608 100 GLU C CD  
4653  O OE1 . GLU C 100 ? 0.5403 0.4712 0.3283 0.0313  -0.0668 -0.0675 100 GLU C OE1 
4654  O OE2 . GLU C 100 ? 0.5253 0.4488 0.3220 0.0171  -0.0667 -0.0548 100 GLU C OE2 
4655  N N   . LEU C 101 ? 0.5939 0.4480 0.3503 0.0165  -0.0984 -0.0704 101 LEU C N   
4656  C CA  . LEU C 101 ? 0.6237 0.4493 0.3583 0.0137  -0.1017 -0.0770 101 LEU C CA  
4657  C C   . LEU C 101 ? 0.6236 0.4389 0.3626 0.0058  -0.1047 -0.0745 101 LEU C C   
4658  O O   . LEU C 101 ? 0.6459 0.4327 0.3676 0.0099  -0.1031 -0.0786 101 LEU C O   
4659  C CB  . LEU C 101 ? 0.6436 0.4635 0.3615 0.0027  -0.1074 -0.0802 101 LEU C CB  
4660  C CG  . LEU C 101 ? 0.6849 0.4678 0.3703 -0.0046 -0.1101 -0.0880 101 LEU C CG  
4661  C CD1 . LEU C 101 ? 0.7092 0.4636 0.3726 0.0134  -0.1038 -0.0944 101 LEU C CD1 
4662  C CD2 . LEU C 101 ? 0.7027 0.4865 0.3726 -0.0162 -0.1150 -0.0916 101 LEU C CD2 
4663  N N   . LYS C 102 ? 0.6023 0.4399 0.3610 -0.0039 -0.1088 -0.0679 102 LYS C N   
4664  C CA  . LYS C 102 ? 0.5975 0.4340 0.3646 -0.0124 -0.1112 -0.0648 102 LYS C CA  
4665  C C   . LYS C 102 ? 0.5870 0.4159 0.3627 -0.0006 -0.1053 -0.0633 102 LYS C C   
4666  O O   . LYS C 102 ? 0.5994 0.4086 0.3675 -0.0045 -0.1058 -0.0643 102 LYS C O   
4667  C CB  . LYS C 102 ? 0.5732 0.4441 0.3623 -0.0185 -0.1155 -0.0574 102 LYS C CB  
4668  C CG  . LYS C 102 ? 0.5871 0.4717 0.3682 -0.0352 -0.1233 -0.0590 102 LYS C CG  
4669  C CD  . LYS C 102 ? 0.5646 0.4903 0.3655 -0.0324 -0.1271 -0.0514 102 LYS C CD  
4670  C CE  . LYS C 102 ? 0.5685 0.5207 0.3726 -0.0498 -0.1340 -0.0514 102 LYS C CE  
4671  N NZ  . LYS C 102 ? 0.5455 0.5389 0.3700 -0.0398 -0.1365 -0.0431 102 LYS C NZ  
4672  N N   . HIS C 103 ? 0.5670 0.4122 0.3558 0.0119  -0.0996 -0.0612 103 HIS C N   
4673  C CA  . HIS C 103 ? 0.5573 0.4035 0.3541 0.0231  -0.0938 -0.0607 103 HIS C CA  
4674  C C   . HIS C 103 ? 0.5881 0.4075 0.3600 0.0352  -0.0915 -0.0680 103 HIS C C   
4675  O O   . HIS C 103 ? 0.5939 0.4015 0.3627 0.0428  -0.0895 -0.0681 103 HIS C O   
4676  C CB  . HIS C 103 ? 0.5347 0.4073 0.3456 0.0293  -0.0875 -0.0581 103 HIS C CB  
4677  C CG  . HIS C 103 ? 0.5238 0.4067 0.3434 0.0389  -0.0814 -0.0584 103 HIS C CG  
4678  N ND1 . HIS C 103 ? 0.5049 0.3945 0.3417 0.0361  -0.0808 -0.0528 103 HIS C ND1 
4679  C CD2 . HIS C 103 ? 0.5301 0.4224 0.3430 0.0524  -0.0759 -0.0638 103 HIS C CD2 
4680  C CE1 . HIS C 103 ? 0.4996 0.4017 0.3402 0.0461  -0.0752 -0.0547 103 HIS C CE1 
4681  N NE2 . HIS C 103 ? 0.5144 0.4213 0.3410 0.0568  -0.0723 -0.0614 103 HIS C NE2 
4682  N N   . LEU C 104 ? 0.6120 0.4199 0.3628 0.0390  -0.0915 -0.0740 104 LEU C N   
4683  C CA  . LEU C 104 ? 0.6507 0.4279 0.3695 0.0544  -0.0891 -0.0814 104 LEU C CA  
4684  C C   . LEU C 104 ? 0.6870 0.4182 0.3786 0.0474  -0.0924 -0.0829 104 LEU C C   
4685  O O   . LEU C 104 ? 0.7171 0.4184 0.3835 0.0635  -0.0894 -0.0861 104 LEU C O   
4686  C CB  . LEU C 104 ? 0.6717 0.4429 0.3706 0.0572  -0.0890 -0.0875 104 LEU C CB  
4687  C CG  . LEU C 104 ? 0.6854 0.4637 0.3706 0.0816  -0.0827 -0.0937 104 LEU C CG  
4688  C CD1 . LEU C 104 ? 0.6467 0.4760 0.3628 0.0876  -0.0771 -0.0907 104 LEU C CD1 
4689  C CD2 . LEU C 104 ? 0.7070 0.4766 0.3719 0.0808  -0.0836 -0.0993 104 LEU C CD2 
4690  N N   . LEU C 105 ? 0.8270 0.4051 0.3959 -0.0515 -0.0927 -0.0632 105 LEU C N   
4691  C CA  . LEU C 105 ? 0.8550 0.4080 0.4033 -0.0605 -0.0948 -0.0539 105 LEU C CA  
4692  C C   . LEU C 105 ? 0.8721 0.4197 0.4048 -0.0598 -0.0951 -0.0481 105 LEU C C   
4693  O O   . LEU C 105 ? 0.9026 0.4240 0.4139 -0.0631 -0.0979 -0.0395 105 LEU C O   
4694  C CB  . LEU C 105 ? 0.8465 0.4069 0.4039 -0.0769 -0.0883 -0.0486 105 LEU C CB  
4695  C CG  . LEU C 105 ? 0.8470 0.4033 0.4081 -0.0824 -0.0907 -0.0507 105 LEU C CG  
4696  C CD1 . LEU C 105 ? 0.8347 0.4092 0.4096 -0.0975 -0.0846 -0.0450 105 LEU C CD1 
4697  C CD2 . LEU C 105 ? 0.8830 0.4030 0.4212 -0.0838 -0.0978 -0.0502 105 LEU C CD2 
4698  N N   . SER C 106 ? 0.8561 0.4277 0.3985 -0.0564 -0.0914 -0.0528 106 SER C N   
4699  C CA  . SER C 106 ? 0.8742 0.4450 0.3995 -0.0546 -0.0924 -0.0491 106 SER C CA  
4700  C C   . SER C 106 ? 0.9003 0.4558 0.4065 -0.0396 -0.1041 -0.0479 106 SER C C   
4701  O O   . SER C 106 ? 0.9259 0.4729 0.4102 -0.0372 -0.1072 -0.0405 106 SER C O   
4702  C CB  . SER C 106 ? 0.8524 0.4535 0.3932 -0.0553 -0.0855 -0.0579 106 SER C CB  
4703  O OG  . SER C 106 ? 0.8376 0.4550 0.3926 -0.0444 -0.0895 -0.0696 106 SER C OG  
4704  N N   . ARG C 107 ? 0.8963 0.4497 0.4107 -0.0285 -0.1101 -0.0544 107 ARG C N   
4705  C CA  . ARG C 107 ? 0.9225 0.4607 0.4221 -0.0119 -0.1208 -0.0526 107 ARG C CA  
4706  C C   . ARG C 107 ? 0.9511 0.4504 0.4350 -0.0109 -0.1237 -0.0453 107 ARG C C   
4707  O O   . ARG C 107 ? 0.9739 0.4569 0.4479 0.0045  -0.1312 -0.0439 107 ARG C O   
4708  C CB  . ARG C 107 ? 0.9036 0.4646 0.4234 0.0014  -0.1247 -0.0653 107 ARG C CB  
4709  C CG  . ARG C 107 ? 0.8924 0.4862 0.4212 0.0062  -0.1269 -0.0730 107 ARG C CG  
4710  C CD  . ARG C 107 ? 0.8926 0.5007 0.4318 0.0239  -0.1354 -0.0810 107 ARG C CD  
4711  N NE  . ARG C 107 ? 0.8668 0.5131 0.4302 0.0227  -0.1330 -0.0947 107 ARG C NE  
4712  C CZ  . ARG C 107 ? 0.8721 0.5429 0.4355 0.0283  -0.1398 -0.1003 107 ARG C CZ  
4713  N NH1 . ARG C 107 ? 0.9030 0.5670 0.4418 0.0382  -0.1508 -0.0916 107 ARG C NH1 
4714  N NH2 . ARG C 107 ? 0.8485 0.5519 0.4370 0.0238  -0.1356 -0.1149 107 ARG C NH2 
4715  N N   . ILE C 108 ? 0.9520 0.4371 0.4349 -0.0271 -0.1174 -0.0413 108 ILE C N   
4716  C CA  . ILE C 108 ? 0.9786 0.4278 0.4500 -0.0296 -0.1190 -0.0384 108 ILE C CA  
4717  C C   . ILE C 108 ? 1.0077 0.4300 0.4607 -0.0445 -0.1152 -0.0256 108 ILE C C   
4718  O O   . ILE C 108 ? 0.9939 0.4303 0.4530 -0.0604 -0.1082 -0.0223 108 ILE C O   
4719  C CB  . ILE C 108 ? 0.9564 0.4142 0.4454 -0.0364 -0.1161 -0.0485 108 ILE C CB  
4720  C CG1 . ILE C 108 ? 0.9345 0.4138 0.4395 -0.0209 -0.1187 -0.0600 108 ILE C CG1 
4721  C CG2 . ILE C 108 ? 0.9875 0.4083 0.4631 -0.0423 -0.1174 -0.0482 108 ILE C CG2 
4722  C CD1 . ILE C 108 ? 0.9099 0.4054 0.4324 -0.0265 -0.1147 -0.0687 108 ILE C CD1 
4723  N N   . ASN C 109 ? 1.0501 0.4327 0.4817 -0.0388 -0.1186 -0.0181 109 ASN C N   
4724  C CA  . ASN C 109 ? 1.0858 0.4362 0.4986 -0.0527 -0.1140 -0.0049 109 ASN C CA  
4725  C C   . ASN C 109 ? 1.1077 0.4255 0.5185 -0.0650 -0.1120 -0.0081 109 ASN C C   
4726  O O   . ASN C 109 ? 1.1263 0.4274 0.5308 -0.0840 -0.1061 -0.0007 109 ASN C O   
4727  C CB  . ASN C 109 ? 1.1267 0.4518 0.5138 -0.0387 -0.1177 0.0093  109 ASN C CB  
4728  C CG  . ASN C 109 ? 1.1218 0.4698 0.5010 -0.0404 -0.1154 0.0183  109 ASN C CG  
4729  O OD1 . ASN C 109 ? 1.1503 0.4801 0.5115 -0.0506 -0.1098 0.0325  109 ASN C OD1 
4730  N ND2 . ASN C 109 ? 1.0883 0.4762 0.4805 -0.0316 -0.1188 0.0095  109 ASN C ND2 
4731  N N   . HIS C 110 ? 1.1080 0.4173 0.5239 -0.0552 -0.1163 -0.0200 110 HIS C N   
4732  C CA  . HIS C 110 ? 1.1309 0.4105 0.5438 -0.0676 -0.1146 -0.0267 110 HIS C CA  
4733  C C   . HIS C 110 ? 1.1117 0.4041 0.5377 -0.0621 -0.1175 -0.0442 110 HIS C C   
4734  O O   . HIS C 110 ? 1.1048 0.4034 0.5338 -0.0412 -0.1214 -0.0501 110 HIS C O   
4735  C CB  . HIS C 110 ? 1.1886 0.4128 0.5779 -0.0619 -0.1143 -0.0186 110 HIS C CB  
4736  C CG  . HIS C 110 ? 1.2204 0.4093 0.6042 -0.0817 -0.1102 -0.0237 110 HIS C CG  
4737  N ND1 . HIS C 110 ? 1.2688 0.4071 0.6377 -0.0752 -0.1097 -0.0266 110 HIS C ND1 
4738  C CD2 . HIS C 110 ? 1.2121 0.4107 0.6049 -0.1082 -0.1063 -0.0278 110 HIS C CD2 
4739  C CE1 . HIS C 110 ? 1.2902 0.4069 0.6581 -0.0987 -0.1055 -0.0335 110 HIS C CE1 
4740  N NE2 . HIS C 110 ? 1.2556 0.4104 0.6383 -0.1191 -0.1042 -0.0341 110 HIS C NE2 
4741  N N   . PHE C 111 ? 1.1050 0.4034 0.5387 -0.0814 -0.1153 -0.0521 111 PHE C N   
4742  C CA  . PHE C 111 ? 1.0978 0.4024 0.5381 -0.0798 -0.1174 -0.0684 111 PHE C CA  
4743  C C   . PHE C 111 ? 1.1463 0.4048 0.5707 -0.0895 -0.1168 -0.0752 111 PHE C C   
4744  O O   . PHE C 111 ? 1.1722 0.4080 0.5891 -0.1079 -0.1138 -0.0686 111 PHE C O   
4745  C CB  . PHE C 111 ? 1.0583 0.4063 0.5177 -0.0946 -0.1163 -0.0729 111 PHE C CB  
4746  C CG  . PHE C 111 ? 1.0117 0.4037 0.4896 -0.0825 -0.1158 -0.0727 111 PHE C CG  
4747  C CD1 . PHE C 111 ? 1.0031 0.4006 0.4834 -0.0610 -0.1178 -0.0786 111 PHE C CD1 
4748  C CD2 . PHE C 111 ? 0.9782 0.4065 0.4730 -0.0933 -0.1124 -0.0671 111 PHE C CD2 
4749  C CE1 . PHE C 111 ? 0.9631 0.3998 0.4620 -0.0526 -0.1161 -0.0793 111 PHE C CE1 
4750  C CE2 . PHE C 111 ? 0.9399 0.4043 0.4523 -0.0833 -0.1103 -0.0675 111 PHE C CE2 
4751  C CZ  . PHE C 111 ? 0.9327 0.4007 0.4470 -0.0639 -0.1121 -0.0738 111 PHE C CZ  
4752  N N   . GLU C 112 ? 1.1608 0.4052 0.5807 -0.0778 -0.1185 -0.0892 112 GLU C N   
4753  C CA  . GLU C 112 ? 1.2039 0.4102 0.6110 -0.0894 -0.1173 -0.1016 112 GLU C CA  
4754  C C   . GLU C 112 ? 1.1841 0.4187 0.5989 -0.0936 -0.1192 -0.1193 112 GLU C C   
4755  O O   . GLU C 112 ? 1.1633 0.4182 0.5839 -0.0751 -0.1202 -0.1256 112 GLU C O   
4756  C CB  . GLU C 112 ? 1.2515 0.4067 0.6419 -0.0705 -0.1158 -0.1034 112 GLU C CB  
4757  C CG  . GLU C 112 ? 1.3068 0.4110 0.6818 -0.0858 -0.1123 -0.1138 112 GLU C CG  
4758  C CD  . GLU C 112 ? 1.3544 0.4090 0.7150 -0.0642 -0.1095 -0.1190 112 GLU C CD  
4759  O OE1 . GLU C 112 ? 1.3609 0.4050 0.7187 -0.0414 -0.1099 -0.1048 112 GLU C OE1 
4760  O OE2 . GLU C 112 ? 1.3874 0.4145 0.7396 -0.0695 -0.1069 -0.1377 112 GLU C OE2 
4761  N N   . LYS C 113 ? 1.1924 0.4306 0.6071 -0.1184 -0.1198 -0.1269 113 LYS C N   
4762  C CA  . LYS C 113 ? 1.1760 0.4456 0.5957 -0.1241 -0.1226 -0.1420 113 LYS C CA  
4763  C C   . LYS C 113 ? 1.2168 0.4526 0.6196 -0.1183 -0.1219 -0.1618 113 LYS C C   
4764  O O   . LYS C 113 ? 1.2663 0.4517 0.6541 -0.1248 -0.1195 -0.1670 113 LYS C O   
4765  C CB  . LYS C 113 ? 1.1703 0.4623 0.5974 -0.1528 -0.1249 -0.1423 113 LYS C CB  
4766  C CG  . LYS C 113 ? 1.1446 0.4828 0.5798 -0.1578 -0.1291 -0.1521 113 LYS C CG  
4767  C CD  . LYS C 113 ? 1.1076 0.4930 0.5630 -0.1720 -0.1308 -0.1399 113 LYS C CD  
4768  C CE  . LYS C 113 ? 1.1307 0.5058 0.5874 -0.1999 -0.1315 -0.1383 113 LYS C CE  
4769  N NZ  . LYS C 113 ? 1.0932 0.5174 0.5727 -0.2105 -0.1321 -0.1252 113 LYS C NZ  
4770  N N   . ILE C 114 ? 1.1990 0.4609 0.6038 -0.1057 -0.1226 -0.1727 114 ILE C N   
4771  C CA  . ILE C 114 ? 1.2365 0.4728 0.6249 -0.1007 -0.1210 -0.1939 114 ILE C CA  
4772  C C   . ILE C 114 ? 1.2169 0.4960 0.6067 -0.1052 -0.1234 -0.2064 114 ILE C C   
4773  O O   . ILE C 114 ? 1.1702 0.4979 0.5756 -0.1013 -0.1248 -0.1966 114 ILE C O   
4774  C CB  . ILE C 114 ? 1.2492 0.4615 0.6336 -0.0706 -0.1166 -0.1955 114 ILE C CB  
4775  C CG1 . ILE C 114 ? 1.1974 0.4554 0.6001 -0.0510 -0.1167 -0.1849 114 ILE C CG1 
4776  C CG2 . ILE C 114 ? 1.2853 0.4459 0.6620 -0.0651 -0.1142 -0.1855 114 ILE C CG2 
4777  C CD1 . ILE C 114 ? 1.2053 0.4576 0.6069 -0.0239 -0.1126 -0.1935 114 ILE C CD1 
4778  N N   . GLN C 115 ? 1.2567 0.5159 0.6287 -0.1133 -0.1231 -0.2279 115 GLN C N   
4779  C CA  . GLN C 115 ? 1.2482 0.5446 0.6153 -0.1172 -0.1255 -0.2414 115 GLN C CA  
4780  C C   . GLN C 115 ? 1.2440 0.5452 0.6078 -0.0901 -0.1196 -0.2483 115 GLN C C   
4781  O O   . GLN C 115 ? 1.2804 0.5395 0.6326 -0.0766 -0.1141 -0.2593 115 GLN C O   
4782  C CB  . GLN C 115 ? 1.2972 0.5715 0.6448 -0.1402 -0.1281 -0.2638 115 GLN C CB  
4783  C CG  . GLN C 115 ? 1.2992 0.6084 0.6354 -0.1438 -0.1309 -0.2806 115 GLN C CG  
4784  C CD  . GLN C 115 ? 1.3488 0.6399 0.6660 -0.1701 -0.1350 -0.3042 115 GLN C CD  
4785  O OE1 . GLN C 115 ? 1.3444 0.6579 0.6677 -0.1951 -0.1428 -0.3020 115 GLN C OE1 
4786  N NE2 . GLN C 115 ? 1.3977 0.6498 0.6929 -0.1648 -0.1295 -0.3280 115 GLN C NE2 
4787  N N   . ILE C 116 ? 1.2017 0.5539 0.5769 -0.0820 -0.1195 -0.2412 116 ILE C N   
4788  C CA  . ILE C 116 ? 1.1957 0.5602 0.5697 -0.0586 -0.1128 -0.2474 116 ILE C CA  
4789  C C   . ILE C 116 ? 1.2091 0.5980 0.5669 -0.0646 -0.1127 -0.2637 116 ILE C C   
4790  O O   . ILE C 116 ? 1.2370 0.6118 0.5801 -0.0522 -0.1064 -0.2805 116 ILE C O   
4791  C CB  . ILE C 116 ? 1.1429 0.5437 0.5417 -0.0422 -0.1100 -0.2280 116 ILE C CB  
4792  C CG1 . ILE C 116 ? 1.1027 0.5431 0.5174 -0.0567 -0.1149 -0.2108 116 ILE C CG1 
4793  C CG2 . ILE C 116 ? 1.1423 0.5151 0.5509 -0.0265 -0.1080 -0.2190 116 ILE C CG2 
4794  C CD1 . ILE C 116 ? 1.0574 0.5414 0.4918 -0.0438 -0.1102 -0.1980 116 ILE C CD1 
4795  N N   . ILE C 117 ? 1.1917 0.6185 0.5516 -0.0826 -0.1194 -0.2584 117 ILE C N   
4796  C CA  . ILE C 117 ? 1.2095 0.6617 0.5508 -0.0918 -0.1220 -0.2730 117 ILE C CA  
4797  C C   . ILE C 117 ? 1.2402 0.6817 0.5700 -0.1204 -0.1314 -0.2838 117 ILE C C   
4798  O O   . ILE C 117 ? 1.2177 0.6779 0.5630 -0.1353 -0.1381 -0.2693 117 ILE C O   
4799  C CB  . ILE C 117 ? 1.1659 0.6780 0.5196 -0.0876 -0.1224 -0.2564 117 ILE C CB  
4800  C CG1 . ILE C 117 ? 1.1554 0.6801 0.5093 -0.0633 -0.1115 -0.2565 117 ILE C CG1 
4801  C CG2 . ILE C 117 ? 1.1788 0.7248 0.5179 -0.1063 -0.1309 -0.2629 117 ILE C CG2 
4802  C CD1 . ILE C 117 ? 1.1235 0.6407 0.5018 -0.0447 -0.1048 -0.2419 117 ILE C CD1 
4803  N N   . PRO C 118 ? 1.2936 0.7050 0.5976 -0.1287 -0.1312 -0.3103 118 PRO C N   
4804  C CA  . PRO C 118 ? 1.3240 0.7319 0.6181 -0.1589 -0.1406 -0.3230 118 PRO C CA  
4805  C C   . PRO C 118 ? 1.3090 0.7786 0.6003 -0.1718 -0.1501 -0.3214 118 PRO C C   
4806  O O   . PRO C 118 ? 1.3014 0.8027 0.5830 -0.1587 -0.1476 -0.3228 118 PRO C O   
4807  C CB  . PRO C 118 ? 1.3883 0.7455 0.6548 -0.1620 -0.1359 -0.3540 118 PRO C CB  
4808  C CG  . PRO C 118 ? 1.3901 0.7154 0.6571 -0.1322 -0.1237 -0.3531 118 PRO C CG  
4809  C CD  . PRO C 118 ? 1.3321 0.7047 0.6180 -0.1121 -0.1215 -0.3302 118 PRO C CD  
4810  N N   . LYS C 119 ? 1.3064 0.7942 0.6068 -0.1966 -0.1604 -0.3172 119 LYS C N   
4811  C CA  . LYS C 119 ? 1.2924 0.8424 0.5935 -0.2089 -0.1711 -0.3130 119 LYS C CA  
4812  C C   . LYS C 119 ? 1.3399 0.8978 0.6086 -0.2186 -0.1756 -0.3414 119 LYS C C   
4813  O O   . LYS C 119 ? 1.3311 0.9396 0.5911 -0.2147 -0.1801 -0.3385 119 LYS C O   
4814  C CB  . LYS C 119 ? 1.2826 0.8484 0.6036 -0.2340 -0.1808 -0.3037 119 LYS C CB  
4815  C CG  . LYS C 119 ? 1.2510 0.8877 0.5852 -0.2396 -0.1908 -0.2876 119 LYS C CG  
4816  C CD  . LYS C 119 ? 1.2379 0.8885 0.5972 -0.2614 -0.1979 -0.2764 119 LYS C CD  
4817  C CE  . LYS C 119 ? 1.2216 0.9430 0.5912 -0.2717 -0.2105 -0.2670 119 LYS C CE  
4818  N NZ  . LYS C 119 ? 1.2213 0.9557 0.6128 -0.2978 -0.2181 -0.2634 119 LYS C NZ  
4819  N N   . SER C 120 ? 1.3937 0.9002 0.6435 -0.2311 -0.1736 -0.3688 120 SER C N   
4820  C CA  . SER C 120 ? 1.4470 0.9508 0.6629 -0.2404 -0.1757 -0.4011 120 SER C CA  
4821  C C   . SER C 120 ? 1.4479 0.9592 0.6454 -0.2132 -0.1659 -0.4052 120 SER C C   
4822  O O   . SER C 120 ? 1.4748 1.0128 0.6459 -0.2168 -0.1692 -0.4225 120 SER C O   
4823  C CB  . SER C 120 ? 1.5057 0.9407 0.7079 -0.2555 -0.1713 -0.4288 120 SER C CB  
4824  O OG  . SER C 120 ? 1.5065 0.8862 0.7133 -0.2327 -0.1573 -0.4241 120 SER C OG  
4825  N N   . SER C 121 ? 1.4204 0.9104 0.6319 -0.1865 -0.1538 -0.3894 121 SER C N   
4826  C CA  . SER C 121 ? 1.4213 0.9145 0.6197 -0.1599 -0.1421 -0.3930 121 SER C CA  
4827  C C   . SER C 121 ? 1.3971 0.9553 0.5896 -0.1524 -0.1444 -0.3812 121 SER C C   
4828  O O   . SER C 121 ? 1.4094 0.9737 0.5842 -0.1353 -0.1349 -0.3893 121 SER C O   
4829  C CB  . SER C 121 ? 1.3881 0.8567 0.6100 -0.1344 -0.1307 -0.3742 121 SER C CB  
4830  O OG  . SER C 121 ? 1.4147 0.8212 0.6395 -0.1361 -0.1269 -0.3830 121 SER C OG  
4831  N N   . TRP C 122 ? 1.3639 0.9701 0.5721 -0.1634 -0.1557 -0.3605 122 TRP C N   
4832  C CA  . TRP C 122 ? 1.3428 1.0108 0.5467 -0.1556 -0.1581 -0.3452 122 TRP C CA  
4833  C C   . TRP C 122 ? 1.3903 1.0836 0.5585 -0.1711 -0.1670 -0.3690 122 TRP C C   
4834  O O   . TRP C 122 ? 1.3903 1.1246 0.5589 -0.1894 -0.1818 -0.3650 122 TRP C O   
4835  C CB  . TRP C 122 ? 1.2926 1.0013 0.5280 -0.1596 -0.1661 -0.3135 122 TRP C CB  
4836  C CG  . TRP C 122 ? 1.2474 0.9362 0.5153 -0.1439 -0.1569 -0.2908 122 TRP C CG  
4837  C CD1 . TRP C 122 ? 1.2297 0.8940 0.5218 -0.1524 -0.1594 -0.2824 122 TRP C CD1 
4838  C CD2 . TRP C 122 ? 1.2171 0.9101 0.4962 -0.1180 -0.1434 -0.2748 122 TRP C CD2 
4839  N NE1 . TRP C 122 ? 1.1907 0.8449 0.5064 -0.1330 -0.1493 -0.2628 122 TRP C NE1 
4840  C CE2 . TRP C 122 ? 1.1817 0.8533 0.4915 -0.1124 -0.1396 -0.2584 122 TRP C CE2 
4841  C CE3 . TRP C 122 ? 1.2183 0.9324 0.4845 -0.1000 -0.1336 -0.2729 122 TRP C CE3 
4842  C CZ2 . TRP C 122 ? 1.1474 0.8192 0.4763 -0.0904 -0.1276 -0.2420 122 TRP C CZ2 
4843  C CZ3 . TRP C 122 ? 1.1836 0.8967 0.4707 -0.0784 -0.1205 -0.2555 122 TRP C CZ3 
4844  C CH2 . TRP C 122 ? 1.1486 0.8411 0.4672 -0.0743 -0.1182 -0.2412 122 TRP C CH2 
4845  N N   . SER C 123 ? 1.4326 1.1032 0.5703 -0.1631 -0.1578 -0.3942 123 SER C N   
4846  C CA  . SER C 123 ? 1.4871 1.1742 0.5855 -0.1779 -0.1646 -0.4231 123 SER C CA  
4847  C C   . SER C 123 ? 1.4793 1.2326 0.5616 -0.1696 -0.1676 -0.4093 123 SER C C   
4848  O O   . SER C 123 ? 1.5132 1.3007 0.5689 -0.1860 -0.1799 -0.4239 123 SER C O   
4849  C CB  . SER C 123 ? 1.5386 1.1733 0.6097 -0.1709 -0.1513 -0.4565 123 SER C CB  
4850  O OG  . SER C 123 ? 1.5213 1.1535 0.5937 -0.1410 -0.1342 -0.4463 123 SER C OG  
4851  N N   . SER C 124 ? 1.4383 1.2094 0.5363 -0.1447 -0.1563 -0.3812 124 SER C N   
4852  C CA  . SER C 124 ? 1.4306 1.2602 0.5152 -0.1335 -0.1557 -0.3632 124 SER C CA  
4853  C C   . SER C 124 ? 1.3862 1.2658 0.4981 -0.1362 -0.1669 -0.3278 124 SER C C   
4854  O O   . SER C 124 ? 1.3815 1.3123 0.4834 -0.1282 -0.1684 -0.3094 124 SER C O   
4855  C CB  . SER C 124 ? 1.4161 1.2363 0.5024 -0.1052 -0.1345 -0.3532 124 SER C CB  
4856  O OG  . SER C 124 ? 1.4142 1.2866 0.4851 -0.0942 -0.1313 -0.3356 124 SER C OG  
4857  N N   . HIS C 125 ? 1.3569 1.2211 0.5025 -0.1464 -0.1737 -0.3177 125 HIS C N   
4858  C CA  . HIS C 125 ? 1.3156 1.2228 0.4908 -0.1487 -0.1831 -0.2856 125 HIS C CA  
4859  C C   . HIS C 125 ? 1.3243 1.2339 0.5102 -0.1761 -0.2006 -0.2948 125 HIS C C   
4860  O O   . HIS C 125 ? 1.3556 1.2231 0.5322 -0.1923 -0.2029 -0.3231 125 HIS C O   
4861  C CB  . HIS C 125 ? 1.2613 1.1515 0.4750 -0.1307 -0.1705 -0.2580 125 HIS C CB  
4862  C CG  . HIS C 125 ? 1.2476 1.1445 0.4584 -0.1053 -0.1534 -0.2438 125 HIS C CG  
4863  N ND1 . HIS C 125 ? 1.2625 1.1213 0.4614 -0.0928 -0.1386 -0.2604 125 HIS C ND1 
4864  C CD2 . HIS C 125 ? 1.2227 1.1598 0.4425 -0.0903 -0.1477 -0.2142 125 HIS C CD2 
4865  C CE1 . HIS C 125 ? 1.2463 1.1238 0.4477 -0.0726 -0.1247 -0.2424 125 HIS C CE1 
4866  N NE2 . HIS C 125 ? 1.2230 1.1459 0.4364 -0.0710 -0.1295 -0.2140 125 HIS C NE2 
4867  N N   . GLU C 126 ? 1.2990 1.2579 0.5059 -0.1808 -0.2118 -0.2704 126 GLU C N   
4868  C CA  . GLU C 126 ? 1.3003 1.2683 0.5251 -0.2060 -0.2273 -0.2745 126 GLU C CA  
4869  C C   . GLU C 126 ? 1.2561 1.1965 0.5222 -0.2023 -0.2205 -0.2549 126 GLU C C   
4870  O O   . GLU C 126 ? 1.2149 1.1703 0.5042 -0.1831 -0.2124 -0.2251 126 GLU C O   
4871  C CB  . GLU C 126 ? 1.2989 1.3407 0.5251 -0.2125 -0.2438 -0.2590 126 GLU C CB  
4872  C CG  . GLU C 126 ? 1.3045 1.3656 0.5483 -0.2408 -0.2613 -0.2660 126 GLU C CG  
4873  C CD  . GLU C 126 ? 1.3586 1.3918 0.5762 -0.2681 -0.2692 -0.3079 126 GLU C CD  
4874  O OE1 . GLU C 126 ? 1.4016 1.4545 0.5815 -0.2731 -0.2757 -0.3289 126 GLU C OE1 
4875  O OE2 . GLU C 126 ? 1.3608 1.3515 0.5949 -0.2850 -0.2682 -0.3197 126 GLU C OE2 
4876  N N   . ALA C 127 ? 1.2685 1.1675 0.5427 -0.2211 -0.2229 -0.2719 127 ALA C N   
4877  C CA  . ALA C 127 ? 1.2332 1.0979 0.5407 -0.2180 -0.2151 -0.2570 127 ALA C CA  
4878  C C   . ALA C 127 ? 1.2263 1.1028 0.5592 -0.2415 -0.2260 -0.2529 127 ALA C C   
4879  O O   . ALA C 127 ? 1.1928 1.0543 0.5551 -0.2381 -0.2201 -0.2353 127 ALA C O   
4880  C CB  . ALA C 127 ? 1.2519 1.0466 0.5485 -0.2135 -0.2032 -0.2761 127 ALA C CB  
4881  N N   . SER C 128 ? 1.2586 1.1643 0.5807 -0.2657 -0.2413 -0.2694 128 SER C N   
4882  C CA  . SER C 128 ? 1.2599 1.1743 0.6051 -0.2922 -0.2512 -0.2709 128 SER C CA  
4883  C C   . SER C 128 ? 1.2311 1.2182 0.6026 -0.2943 -0.2625 -0.2462 128 SER C C   
4884  O O   . SER C 128 ? 1.2263 1.2285 0.6224 -0.3146 -0.2698 -0.2439 128 SER C O   
4885  C CB  . SER C 128 ? 1.3174 1.2152 0.6387 -0.3218 -0.2607 -0.3076 128 SER C CB  
4886  O OG  . SER C 128 ? 1.3440 1.1663 0.6508 -0.3227 -0.2489 -0.3279 128 SER C OG  
4887  N N   . LEU C 129 ? 1.2139 1.2457 0.5815 -0.2728 -0.2629 -0.2268 129 LEU C N   
4888  C CA  . LEU C 129 ? 1.1899 1.2919 0.5817 -0.2702 -0.2729 -0.2009 129 LEU C CA  
4889  C C   . LEU C 129 ? 1.1390 1.2444 0.5617 -0.2448 -0.2598 -0.1657 129 LEU C C   
4890  O O   . LEU C 129 ? 1.1179 1.2774 0.5621 -0.2364 -0.2645 -0.1404 129 LEU C O   
4891  C CB  . LEU C 129 ? 1.2141 1.3708 0.5784 -0.2655 -0.2844 -0.2025 129 LEU C CB  
4892  C CG  . LEU C 129 ? 1.2638 1.4436 0.6045 -0.2945 -0.3029 -0.2338 129 LEU C CG  
4893  C CD1 . LEU C 129 ? 1.3071 1.4269 0.6110 -0.3041 -0.2973 -0.2707 129 LEU C CD1 
4894  C CD2 . LEU C 129 ? 1.2776 1.5309 0.6014 -0.2878 -0.3169 -0.2244 129 LEU C CD2 
4895  N N   . GLY C 130 ? 1.1233 1.1716 0.5490 -0.2324 -0.2433 -0.1646 130 GLY C N   
4896  C CA  . GLY C 130 ? 1.0781 1.1234 0.5315 -0.2100 -0.2296 -0.1355 130 GLY C CA  
4897  C C   . GLY C 130 ? 1.0520 1.0948 0.5420 -0.2192 -0.2282 -0.1236 130 GLY C C   
4898  O O   . GLY C 130 ? 1.0367 1.0323 0.5363 -0.2160 -0.2167 -0.1233 130 GLY C O   
4899  N N   . VAL C 131 ? 1.0481 1.1445 0.5585 -0.2299 -0.2398 -0.1132 131 VAL C N   
4900  C CA  . VAL C 131 ? 1.0261 1.1291 0.5727 -0.2401 -0.2386 -0.1018 131 VAL C CA  
4901  C C   . VAL C 131 ? 0.9970 1.1583 0.5746 -0.2254 -0.2390 -0.0710 131 VAL C C   
4902  O O   . VAL C 131 ? 0.9978 1.1941 0.5676 -0.2084 -0.2412 -0.0579 131 VAL C O   
4903  C CB  . VAL C 131 ? 1.0546 1.1637 0.6021 -0.2734 -0.2520 -0.1228 131 VAL C CB  
4904  C CG1 . VAL C 131 ? 1.0915 1.1414 0.6066 -0.2874 -0.2511 -0.1541 131 VAL C CG1 
4905  C CG2 . VAL C 131 ? 1.0708 1.2506 0.6186 -0.2834 -0.2706 -0.1230 131 VAL C CG2 
4906  N N   . SER C 132 ? 0.9755 1.1460 0.5879 -0.2311 -0.2356 -0.0587 132 SER C N   
4907  C CA  . SER C 132 ? 0.9486 1.1712 0.5948 -0.2168 -0.2341 -0.0296 132 SER C CA  
4908  C C   . SER C 132 ? 0.9377 1.1815 0.6184 -0.2345 -0.2367 -0.0259 132 SER C C   
4909  O O   . SER C 132 ? 0.9426 1.1471 0.6241 -0.2526 -0.2330 -0.0403 132 SER C O   
4910  C CB  . SER C 132 ? 0.9188 1.1172 0.5756 -0.1889 -0.2149 -0.0092 132 SER C CB  
4911  O OG  . SER C 132 ? 0.8938 1.1311 0.5877 -0.1766 -0.2099 0.0172  132 SER C OG  
4912  N N   . SER C 133 ? 0.9238 1.2304 0.6336 -0.2279 -0.2421 -0.0049 133 SER C N   
4913  C CA  . SER C 133 ? 0.9098 1.2461 0.6577 -0.2414 -0.2430 0.0019  133 SER C CA  
4914  C C   . SER C 133 ? 0.8773 1.1791 0.6487 -0.2303 -0.2224 0.0152  133 SER C C   
4915  O O   . SER C 133 ? 0.8697 1.1793 0.6679 -0.2439 -0.2192 0.0167  133 SER C O   
4916  C CB  . SER C 133 ? 0.9059 1.3232 0.6796 -0.2336 -0.2545 0.0222  133 SER C CB  
4917  O OG  . SER C 133 ? 0.8850 1.3138 0.6683 -0.2007 -0.2438 0.0495  133 SER C OG  
4918  N N   . ALA C 134 ? 0.8591 1.1249 0.6204 -0.2064 -0.2081 0.0239  134 ALA C N   
4919  C CA  . ALA C 134 ? 0.8314 1.0614 0.6100 -0.1955 -0.1885 0.0334  134 ALA C CA  
4920  C C   . ALA C 134 ? 0.8375 1.0103 0.6027 -0.2141 -0.1837 0.0137  134 ALA C C   
4921  O O   . ALA C 134 ? 0.8226 0.9796 0.6068 -0.2155 -0.1717 0.0192  134 ALA C O   
4922  C CB  . ALA C 134 ? 0.8166 1.0249 0.5872 -0.1674 -0.1756 0.0455  134 ALA C CB  
4923  N N   . CYS C 135 ? 0.8613 1.0031 0.5931 -0.2273 -0.1921 -0.0084 135 CYS C N   
4924  C CA  . CYS C 135 ? 0.8754 0.9633 0.5925 -0.2460 -0.1892 -0.0270 135 CYS C CA  
4925  C C   . CYS C 135 ? 0.9046 1.0066 0.6174 -0.2768 -0.2039 -0.0447 135 CYS C C   
4926  O O   . CYS C 135 ? 0.9327 1.0164 0.6161 -0.2866 -0.2130 -0.0647 135 CYS C O   
4927  C CB  . CYS C 135 ? 0.8851 0.9173 0.5679 -0.2361 -0.1848 -0.0399 135 CYS C CB  
4928  S SG  . CYS C 135 ? 0.8545 0.8727 0.5402 -0.2023 -0.1692 -0.0229 135 CYS C SG  
4929  N N   . PRO C 136 ? 0.8990 1.0347 0.6422 -0.2928 -0.2054 -0.0385 136 PRO C N   
4930  C CA  . PRO C 136 ? 0.9282 1.0800 0.6720 -0.3249 -0.2184 -0.0557 136 PRO C CA  
4931  C C   . PRO C 136 ? 0.9501 1.0423 0.6820 -0.3472 -0.2121 -0.0719 136 PRO C C   
4932  O O   . PRO C 136 ? 0.9358 0.9956 0.6756 -0.3418 -0.1973 -0.0627 136 PRO C O   
4933  C CB  . PRO C 136 ? 0.9112 1.1289 0.6979 -0.3295 -0.2206 -0.0389 136 PRO C CB  
4934  C CG  . PRO C 136 ? 0.8779 1.0834 0.6843 -0.3077 -0.2021 -0.0179 136 PRO C CG  
4935  C CD  . PRO C 136 ? 0.8675 1.0376 0.6488 -0.2809 -0.1956 -0.0149 136 PRO C CD  
4936  N N   . TYR C 137 ? 0.9875 1.0657 0.6997 -0.3719 -0.2229 -0.0956 137 TYR C N   
4937  C CA  . TYR C 137 ? 1.0170 1.0403 0.7190 -0.3963 -0.2176 -0.1112 137 TYR C CA  
4938  C C   . TYR C 137 ? 1.0494 1.1015 0.7599 -0.4320 -0.2305 -0.1286 137 TYR C C   
4939  O O   . TYR C 137 ? 1.0726 1.1436 0.7664 -0.4402 -0.2451 -0.1457 137 TYR C O   
4940  C CB  . TYR C 137 ? 1.0397 0.9936 0.7013 -0.3887 -0.2141 -0.1273 137 TYR C CB  
4941  C CG  . TYR C 137 ? 1.0796 0.9727 0.7268 -0.4128 -0.2093 -0.1442 137 TYR C CG  
4942  C CD1 . TYR C 137 ? 1.0756 0.9331 0.7323 -0.4158 -0.1950 -0.1331 137 TYR C CD1 
4943  C CD2 . TYR C 137 ? 1.1252 0.9943 0.7475 -0.4322 -0.2179 -0.1711 137 TYR C CD2 
4944  C CE1 . TYR C 137 ? 1.1160 0.9154 0.7587 -0.4367 -0.1894 -0.1459 137 TYR C CE1 
4945  C CE2 . TYR C 137 ? 1.1662 0.9748 0.7757 -0.4536 -0.2118 -0.1858 137 TYR C CE2 
4946  C CZ  . TYR C 137 ? 1.1615 0.9351 0.7816 -0.4554 -0.1975 -0.1718 137 TYR C CZ  
4947  O OH  . TYR C 137 ? 1.2060 0.9177 0.8127 -0.4757 -0.1904 -0.1838 137 TYR C OH  
4948  N N   . GLN C 138 ? 1.0528 1.1088 0.7887 -0.4539 -0.2246 -0.1249 138 GLN C N   
4949  C CA  . GLN C 138 ? 1.0829 1.1696 0.8340 -0.4910 -0.2352 -0.1404 138 GLN C CA  
4950  C C   . GLN C 138 ? 1.0744 1.2473 0.8437 -0.4929 -0.2539 -0.1398 138 GLN C C   
4951  O O   . GLN C 138 ? 1.1080 1.3013 0.8700 -0.5176 -0.2691 -0.1618 138 GLN C O   
4952  C CB  . GLN C 138 ? 1.1350 1.1622 0.8535 -0.5148 -0.2379 -0.1698 138 GLN C CB  
4953  C CG  . GLN C 138 ? 1.1473 1.0873 0.8432 -0.5084 -0.2207 -0.1695 138 GLN C CG  
4954  C CD  . GLN C 138 ? 1.2017 1.0881 0.8847 -0.5419 -0.2179 -0.1917 138 GLN C CD  
4955  O OE1 . GLN C 138 ? 1.2386 1.1281 0.9087 -0.5630 -0.2298 -0.2169 138 GLN C OE1 
4956  N NE2 . GLN C 138 ? 1.2103 1.0458 0.8952 -0.5470 -0.2016 -0.1825 138 GLN C NE2 
4957  N N   . GLY C 139 ? 1.0320 1.2546 0.8244 -0.4663 -0.2526 -0.1146 139 GLY C N   
4958  C CA  . GLY C 139 ? 1.0213 1.3300 0.8344 -0.4628 -0.2693 -0.1076 139 GLY C CA  
4959  C C   . GLY C 139 ? 1.0288 1.3503 0.8107 -0.4467 -0.2827 -0.1146 139 GLY C C   
4960  O O   . GLY C 139 ? 1.0247 1.4175 0.8186 -0.4423 -0.2978 -0.1082 139 GLY C O   
4961  N N   . LYS C 140 ? 1.0411 1.2955 0.7828 -0.4370 -0.2769 -0.1266 140 LYS C N   
4962  C CA  . LYS C 140 ? 1.0533 1.3113 0.7606 -0.4230 -0.2870 -0.1358 140 LYS C CA  
4963  C C   . LYS C 140 ? 1.0251 1.2461 0.7173 -0.3865 -0.2730 -0.1195 140 LYS C C   
4964  O O   . LYS C 140 ? 1.0085 1.1803 0.7049 -0.3782 -0.2564 -0.1115 140 LYS C O   
4965  C CB  . LYS C 140 ? 1.1027 1.3153 0.7745 -0.4481 -0.2932 -0.1705 140 LYS C CB  
4966  C CG  . LYS C 140 ? 1.1364 1.3941 0.8186 -0.4850 -0.3104 -0.1908 140 LYS C CG  
4967  C CD  . LYS C 140 ? 1.1792 1.3754 0.8490 -0.5184 -0.3059 -0.2187 140 LYS C CD  
4968  C CE  . LYS C 140 ? 1.2099 1.4540 0.8993 -0.5584 -0.3209 -0.2370 140 LYS C CE  
4969  N NZ  . LYS C 140 ? 1.2482 1.5200 0.9098 -0.5712 -0.3402 -0.2640 140 LYS C NZ  
4970  N N   . SER C 141 ? 1.0220 1.2685 0.6963 -0.3656 -0.2798 -0.1147 141 SER C N   
4971  C CA  . SER C 141 ? 0.9970 1.2151 0.6587 -0.3318 -0.2669 -0.0993 141 SER C CA  
4972  C C   . SER C 141 ? 1.0144 1.1532 0.6418 -0.3311 -0.2574 -0.1182 141 SER C C   
4973  O O   . SER C 141 ? 1.0524 1.1704 0.6510 -0.3472 -0.2653 -0.1443 141 SER C O   
4974  C CB  . SER C 141 ? 0.9958 1.2627 0.6456 -0.3119 -0.2763 -0.0895 141 SER C CB  
4975  O OG  . SER C 141 ? 0.9768 1.3157 0.6606 -0.3058 -0.2830 -0.0666 141 SER C OG  
4976  N N   . SER C 142 ? 0.9883 1.0846 0.6198 -0.3119 -0.2406 -0.1055 142 SER C N   
4977  C CA  . SER C 142 ? 1.0013 1.0244 0.6057 -0.3083 -0.2306 -0.1197 142 SER C CA  
4978  C C   . SER C 142 ? 0.9709 0.9773 0.5724 -0.2757 -0.2178 -0.1033 142 SER C C   
4979  O O   . SER C 142 ? 0.9473 0.9963 0.5615 -0.2574 -0.2177 -0.0842 142 SER C O   
4980  C CB  . SER C 142 ? 1.0077 0.9883 0.6225 -0.3261 -0.2227 -0.1240 142 SER C CB  
4981  O OG  . SER C 142 ? 1.0276 0.9384 0.6155 -0.3240 -0.2150 -0.1385 142 SER C OG  
4982  N N   . PHE C 143 ? 0.9739 0.9189 0.5594 -0.2686 -0.2071 -0.1106 143 PHE C N   
4983  C CA  . PHE C 143 ? 0.9466 0.8735 0.5314 -0.2403 -0.1945 -0.0974 143 PHE C CA  
4984  C C   . PHE C 143 ? 0.9470 0.8123 0.5261 -0.2381 -0.1833 -0.1020 143 PHE C C   
4985  O O   . PHE C 143 ? 0.9729 0.8050 0.5439 -0.2569 -0.1850 -0.1156 143 PHE C O   
4986  C CB  . PHE C 143 ? 0.9576 0.8877 0.5160 -0.2259 -0.1969 -0.1046 143 PHE C CB  
4987  C CG  . PHE C 143 ? 0.9267 0.8624 0.4922 -0.1977 -0.1856 -0.0862 143 PHE C CG  
4988  C CD1 . PHE C 143 ? 0.8982 0.8785 0.4904 -0.1866 -0.1831 -0.0620 143 PHE C CD1 
4989  C CD2 . PHE C 143 ? 0.9285 0.8249 0.4755 -0.1825 -0.1768 -0.0932 143 PHE C CD2 
4990  C CE1 . PHE C 143 ? 0.8740 0.8560 0.4735 -0.1622 -0.1711 -0.0456 143 PHE C CE1 
4991  C CE2 . PHE C 143 ? 0.9022 0.8045 0.4577 -0.1590 -0.1657 -0.0772 143 PHE C CE2 
4992  C CZ  . PHE C 143 ? 0.8758 0.8191 0.4572 -0.1496 -0.1625 -0.0537 143 PHE C CZ  
4993  N N   . PHE C 144 ? 0.9207 0.7717 0.5045 -0.2152 -0.1718 -0.0900 144 PHE C N   
4994  C CA  . PHE C 144 ? 0.9220 0.7185 0.4973 -0.2090 -0.1623 -0.0942 144 PHE C CA  
4995  C C   . PHE C 144 ? 0.9614 0.7152 0.5060 -0.2162 -0.1665 -0.1173 144 PHE C C   
4996  O O   . PHE C 144 ? 0.9723 0.7269 0.4984 -0.2072 -0.1687 -0.1269 144 PHE C O   
4997  C CB  . PHE C 144 ? 0.8935 0.6861 0.4735 -0.1828 -0.1517 -0.0831 144 PHE C CB  
4998  C CG  . PHE C 144 ? 0.8586 0.6897 0.4678 -0.1730 -0.1455 -0.0615 144 PHE C CG  
4999  C CD1 . PHE C 144 ? 0.8423 0.6710 0.4721 -0.1766 -0.1388 -0.0511 144 PHE C CD1 
5000  C CD2 . PHE C 144 ? 0.8452 0.7130 0.4602 -0.1593 -0.1450 -0.0512 144 PHE C CD2 
5001  C CE1 . PHE C 144 ? 0.8135 0.6749 0.4704 -0.1665 -0.1315 -0.0326 144 PHE C CE1 
5002  C CE2 . PHE C 144 ? 0.8171 0.7162 0.4597 -0.1488 -0.1378 -0.0308 144 PHE C CE2 
5003  C CZ  . PHE C 144 ? 0.8012 0.6965 0.4653 -0.1523 -0.1308 -0.0224 144 PHE C CZ  
5004  N N   . ARG C 145 ? 0.9853 0.7007 0.5244 -0.2320 -0.1661 -0.1258 145 ARG C N   
5005  C CA  . ARG C 145 ? 1.0296 0.7013 0.5414 -0.2416 -0.1693 -0.1483 145 ARG C CA  
5006  C C   . ARG C 145 ? 1.0371 0.6699 0.5291 -0.2203 -0.1631 -0.1558 145 ARG C C   
5007  O O   . ARG C 145 ? 1.0727 0.6789 0.5413 -0.2232 -0.1656 -0.1754 145 ARG C O   
5008  C CB  . ARG C 145 ? 1.0546 0.6892 0.5672 -0.2619 -0.1676 -0.1519 145 ARG C CB  
5009  C CG  . ARG C 145 ? 1.0544 0.7243 0.5871 -0.2866 -0.1731 -0.1475 145 ARG C CG  
5010  C CD  . ARG C 145 ? 1.0949 0.7228 0.6210 -0.3112 -0.1721 -0.1582 145 ARG C CD  
5011  N NE  . ARG C 145 ? 1.0920 0.7544 0.6420 -0.3350 -0.1752 -0.1519 145 ARG C NE  
5012  C CZ  . ARG C 145 ? 1.1031 0.8074 0.6603 -0.3548 -0.1863 -0.1614 145 ARG C CZ  
5013  N NH1 . ARG C 145 ? 1.1193 0.8363 0.6585 -0.3540 -0.1958 -0.1780 145 ARG C NH1 
5014  N NH2 . ARG C 145 ? 1.0990 0.8359 0.6817 -0.3756 -0.1880 -0.1543 145 ARG C NH2 
5015  N N   . ASN C 146 ? 1.0063 0.6362 0.5086 -0.1995 -0.1547 -0.1415 146 ASN C N   
5016  C CA  . ASN C 146 ? 1.0118 0.6073 0.5000 -0.1793 -0.1486 -0.1475 146 ASN C CA  
5017  C C   . ASN C 146 ? 1.0036 0.6218 0.4846 -0.1629 -0.1478 -0.1514 146 ASN C C   
5018  O O   . ASN C 146 ? 1.0154 0.6075 0.4825 -0.1484 -0.1435 -0.1608 146 ASN C O   
5019  C CB  . ASN C 146 ? 0.9864 0.5682 0.4882 -0.1659 -0.1406 -0.1326 146 ASN C CB  
5020  C CG  . ASN C 146 ? 1.0067 0.5515 0.5061 -0.1782 -0.1395 -0.1311 146 ASN C CG  
5021  O OD1 . ASN C 146 ? 1.0464 0.5514 0.5276 -0.1862 -0.1412 -0.1442 146 ASN C OD1 
5022  N ND2 . ASN C 146 ? 0.9830 0.5392 0.5002 -0.1798 -0.1354 -0.1150 146 ASN C ND2 
5023  N N   . VAL C 147 ? 0.9856 0.6531 0.4763 -0.1646 -0.1513 -0.1432 147 VAL C N   
5024  C CA  . VAL C 147 ? 0.9811 0.6731 0.4635 -0.1501 -0.1498 -0.1445 147 VAL C CA  
5025  C C   . VAL C 147 ? 0.9998 0.7273 0.4713 -0.1629 -0.1599 -0.1513 147 VAL C C   
5026  O O   . VAL C 147 ? 0.9997 0.7514 0.4819 -0.1800 -0.1677 -0.1470 147 VAL C O   
5027  C CB  . VAL C 147 ? 0.9391 0.6589 0.4439 -0.1322 -0.1414 -0.1235 147 VAL C CB  
5028  C CG1 . VAL C 147 ? 0.9259 0.6136 0.4365 -0.1174 -0.1319 -0.1215 147 VAL C CG1 
5029  C CG2 . VAL C 147 ? 0.9146 0.6680 0.4447 -0.1402 -0.1431 -0.1055 147 VAL C CG2 
5030  N N   . VAL C 148 ? 1.0171 0.7505 0.4675 -0.1544 -0.1597 -0.1619 148 VAL C N   
5031  C CA  . VAL C 148 ? 1.0420 0.8079 0.4752 -0.1656 -0.1699 -0.1717 148 VAL C CA  
5032  C C   . VAL C 148 ? 1.0198 0.8372 0.4596 -0.1519 -0.1686 -0.1531 148 VAL C C   
5033  O O   . VAL C 148 ? 1.0090 0.8248 0.4456 -0.1322 -0.1585 -0.1477 148 VAL C O   
5034  C CB  . VAL C 148 ? 1.0854 0.8218 0.4848 -0.1664 -0.1700 -0.1988 148 VAL C CB  
5035  C CG1 . VAL C 148 ? 1.1185 0.8843 0.4979 -0.1841 -0.1826 -0.2136 148 VAL C CG1 
5036  C CG2 . VAL C 148 ? 1.1081 0.7844 0.5017 -0.1724 -0.1669 -0.2141 148 VAL C CG2 
5037  N N   . TRP C 149 ? 1.0152 0.8786 0.4652 -0.1621 -0.1783 -0.1426 149 TRP C N   
5038  C CA  . TRP C 149 ? 1.0027 0.9168 0.4561 -0.1496 -0.1784 -0.1240 149 TRP C CA  
5039  C C   . TRP C 149 ? 1.0403 0.9709 0.4587 -0.1521 -0.1854 -0.1404 149 TRP C C   
5040  O O   . TRP C 149 ? 1.0666 1.0186 0.4731 -0.1707 -0.1996 -0.1529 149 TRP C O   
5041  C CB  . TRP C 149 ? 0.9849 0.9440 0.4648 -0.1576 -0.1863 -0.1051 149 TRP C CB  
5042  C CG  . TRP C 149 ? 0.9679 0.9759 0.4583 -0.1409 -0.1841 -0.0795 149 TRP C CG  
5043  C CD1 . TRP C 149 ? 0.9712 0.9887 0.4467 -0.1225 -0.1766 -0.0724 149 TRP C CD1 
5044  C CD2 . TRP C 149 ? 0.9486 1.0023 0.4672 -0.1406 -0.1884 -0.0564 149 TRP C CD2 
5045  N NE1 . TRP C 149 ? 0.9562 1.0193 0.4480 -0.1107 -0.1757 -0.0452 149 TRP C NE1 
5046  C CE2 . TRP C 149 ? 0.9421 1.0285 0.4609 -0.1205 -0.1831 -0.0351 149 TRP C CE2 
5047  C CE3 . TRP C 149 ? 0.9380 1.0082 0.4827 -0.1547 -0.1950 -0.0510 149 TRP C CE3 
5048  C CZ2 . TRP C 149 ? 0.9265 1.0596 0.4707 -0.1126 -0.1846 -0.0081 149 TRP C CZ2 
5049  C CZ3 . TRP C 149 ? 0.9204 1.0401 0.4916 -0.1470 -0.1966 -0.0255 149 TRP C CZ3 
5050  C CH2 . TRP C 149 ? 0.9158 1.0656 0.4866 -0.1254 -0.1916 -0.0042 149 TRP C CH2 
5051  N N   . LEU C 150 ? 1.0441 0.9664 0.4464 -0.1341 -0.1750 -0.1412 150 LEU C N   
5052  C CA  . LEU C 150 ? 1.0825 1.0156 0.4481 -0.1344 -0.1787 -0.1584 150 LEU C CA  
5053  C C   . LEU C 150 ? 1.0825 1.0747 0.4430 -0.1268 -0.1830 -0.1393 150 LEU C C   
5054  O O   . LEU C 150 ? 1.0517 1.0638 0.4335 -0.1106 -0.1746 -0.1115 150 LEU C O   
5055  C CB  . LEU C 150 ? 1.0904 0.9865 0.4403 -0.1183 -0.1640 -0.1694 150 LEU C CB  
5056  C CG  . LEU C 150 ? 1.1031 0.9399 0.4495 -0.1230 -0.1601 -0.1917 150 LEU C CG  
5057  C CD1 . LEU C 150 ? 1.1067 0.9180 0.4428 -0.1031 -0.1450 -0.1980 150 LEU C CD1 
5058  C CD2 . LEU C 150 ? 1.1481 0.9695 0.4701 -0.1452 -0.1719 -0.2205 150 LEU C CD2 
5059  N N   . ILE C 151 ? 1.1205 1.1397 0.4518 -0.1385 -0.1959 -0.1546 151 ILE C N   
5060  C CA  . ILE C 151 ? 1.1300 1.2075 0.4488 -0.1312 -0.2018 -0.1383 151 ILE C CA  
5061  C C   . ILE C 151 ? 1.1765 1.2590 0.4490 -0.1322 -0.2038 -0.1609 151 ILE C C   
5062  O O   . ILE C 151 ? 1.2047 1.2479 0.4562 -0.1423 -0.2032 -0.1923 151 ILE C O   
5063  C CB  . ILE C 151 ? 1.1286 1.2558 0.4626 -0.1461 -0.2203 -0.1286 151 ILE C CB  
5064  C CG1 . ILE C 151 ? 1.1679 1.2928 0.4817 -0.1742 -0.2370 -0.1617 151 ILE C CG1 
5065  C CG2 . ILE C 151 ? 1.0845 1.2065 0.4639 -0.1447 -0.2165 -0.1072 151 ILE C CG2 
5066  C CD1 . ILE C 151 ? 1.1662 1.3394 0.4995 -0.1921 -0.2555 -0.1554 151 ILE C CD1 
5067  N N   . LYS C 152 ? 1.1869 1.3176 0.4433 -0.1208 -0.2053 -0.1442 152 LYS C N   
5068  C CA  . LYS C 152 ? 1.2326 1.3762 0.4424 -0.1194 -0.2061 -0.1619 152 LYS C CA  
5069  C C   . LYS C 152 ? 1.2776 1.4280 0.4596 -0.1454 -0.2247 -0.1966 152 LYS C C   
5070  O O   . LYS C 152 ? 1.2749 1.4487 0.4725 -0.1635 -0.2415 -0.1972 152 LYS C O   
5071  C CB  . LYS C 152 ? 1.2355 1.4365 0.4354 -0.1030 -0.2062 -0.1319 152 LYS C CB  
5072  C CG  . LYS C 152 ? 1.2382 1.4991 0.4461 -0.1127 -0.2273 -0.1176 152 LYS C CG  
5073  C CD  . LYS C 152 ? 1.2308 1.5419 0.4414 -0.0911 -0.2241 -0.0779 152 LYS C CD  
5074  C CE  . LYS C 152 ? 1.2491 1.6279 0.4548 -0.1000 -0.2477 -0.0690 152 LYS C CE  
5075  N NZ  . LYS C 152 ? 1.2555 1.6844 0.4530 -0.0774 -0.2450 -0.0320 152 LYS C NZ  
5076  N N   . LYS C 153 ? 1.3207 1.4511 0.4626 -0.1475 -0.2207 -0.2261 153 LYS C N   
5077  C CA  . LYS C 153 ? 1.3723 1.5088 0.4818 -0.1721 -0.2366 -0.2623 153 LYS C CA  
5078  C C   . LYS C 153 ? 1.4134 1.6004 0.4790 -0.1678 -0.2424 -0.2652 153 LYS C C   
5079  O O   . LYS C 153 ? 1.4249 1.6051 0.4670 -0.1491 -0.2268 -0.2630 153 LYS C O   
5080  C CB  . LYS C 153 ? 1.3983 1.4666 0.4938 -0.1802 -0.2274 -0.2995 153 LYS C CB  
5081  C CG  . LYS C 153 ? 1.4412 1.5005 0.5215 -0.2116 -0.2436 -0.3359 153 LYS C CG  
5082  C CD  . LYS C 153 ? 1.4915 1.5001 0.5362 -0.2158 -0.2343 -0.3763 153 LYS C CD  
5083  C CE  . LYS C 153 ? 1.4742 1.4100 0.5389 -0.2066 -0.2168 -0.3811 153 LYS C CE  
5084  N NZ  . LYS C 153 ? 1.4673 1.3647 0.5591 -0.2266 -0.2225 -0.3894 153 LYS C NZ  
5085  N N   . ASN C 154 ? 1.4373 1.6767 0.4920 -0.1856 -0.2647 -0.2702 154 ASN C N   
5086  C CA  . ASN C 154 ? 1.4782 1.7764 0.4910 -0.1830 -0.2744 -0.2701 154 ASN C CA  
5087  C C   . ASN C 154 ? 1.4574 1.7871 0.4700 -0.1523 -0.2621 -0.2285 154 ASN C C   
5088  O O   . ASN C 154 ? 1.4905 1.8358 0.4626 -0.1407 -0.2551 -0.2308 154 ASN C O   
5089  C CB  . ASN C 154 ? 1.5387 1.8128 0.5003 -0.1929 -0.2716 -0.3142 154 ASN C CB  
5090  C CG  . ASN C 154 ? 1.5909 1.9296 0.5077 -0.2019 -0.2895 -0.3249 154 ASN C CG  
5091  O OD1 . ASN C 154 ? 1.5884 1.9861 0.5151 -0.2116 -0.3107 -0.3110 154 ASN C OD1 
5092  N ND2 . ASN C 154 ? 1.6409 1.9710 0.5081 -0.1985 -0.2811 -0.3501 154 ASN C ND2 
5093  N N   . SER C 155 ? 1.4051 1.7420 0.4631 -0.1398 -0.2582 -0.1910 155 SER C N   
5094  C CA  . SER C 155 ? 1.3840 1.7501 0.4494 -0.1121 -0.2467 -0.1479 155 SER C CA  
5095  C C   . SER C 155 ? 1.3796 1.7037 0.4349 -0.0916 -0.2193 -0.1450 155 SER C C   
5096  O O   . SER C 155 ? 1.3917 1.7419 0.4274 -0.0728 -0.2094 -0.1230 155 SER C O   
5097  C CB  . SER C 155 ? 1.4208 1.8607 0.4531 -0.1092 -0.2622 -0.1349 155 SER C CB  
5098  O OG  . SER C 155 ? 1.3952 1.8712 0.4486 -0.0862 -0.2571 -0.0867 155 SER C OG  
5099  N N   . THR C 156 ? 1.3648 1.6255 0.4337 -0.0953 -0.2071 -0.1665 156 THR C N   
5100  C CA  . THR C 156 ? 1.3554 1.5762 0.4231 -0.0764 -0.1813 -0.1641 156 THR C CA  
5101  C C   . THR C 156 ? 1.3146 1.4778 0.4228 -0.0773 -0.1717 -0.1688 156 THR C C   
5102  O O   . THR C 156 ? 1.3211 1.4531 0.4329 -0.0954 -0.1805 -0.1965 156 THR C O   
5103  C CB  . THR C 156 ? 1.4063 1.6101 0.4254 -0.0781 -0.1743 -0.1989 156 THR C CB  
5104  O OG1 . THR C 156 ? 1.4141 1.5637 0.4357 -0.0928 -0.1748 -0.2359 156 THR C OG1 
5105  C CG2 . THR C 156 ? 1.4590 1.7154 0.4306 -0.0872 -0.1905 -0.2098 156 THR C CG2 
5106  N N   . TYR C 157 ? 1.2760 1.4254 0.4140 -0.0585 -0.1537 -0.1418 157 TYR C N   
5107  C CA  . TYR C 157 ? 1.2390 1.3363 0.4129 -0.0569 -0.1433 -0.1454 157 TYR C CA  
5108  C C   . TYR C 157 ? 1.2435 1.3087 0.4094 -0.0413 -0.1209 -0.1532 157 TYR C C   
5109  O O   . TYR C 157 ? 1.2209 1.2919 0.4031 -0.0239 -0.1044 -0.1278 157 TYR C O   
5110  C CB  . TYR C 157 ? 1.1892 1.2957 0.4091 -0.0497 -0.1409 -0.1107 157 TYR C CB  
5111  C CG  . TYR C 157 ? 1.1533 1.2132 0.4093 -0.0540 -0.1372 -0.1165 157 TYR C CG  
5112  C CD1 . TYR C 157 ? 1.1365 1.1564 0.4051 -0.0423 -0.1189 -0.1200 157 TYR C CD1 
5113  C CD2 . TYR C 157 ? 1.1379 1.1967 0.4155 -0.0699 -0.1520 -0.1180 157 TYR C CD2 
5114  C CE1 . TYR C 157 ? 1.1069 1.0877 0.4059 -0.0454 -0.1167 -0.1244 157 TYR C CE1 
5115  C CE2 . TYR C 157 ? 1.1088 1.1263 0.4161 -0.0734 -0.1482 -0.1220 157 TYR C CE2 
5116  C CZ  . TYR C 157 ? 1.0939 1.0726 0.4106 -0.0608 -0.1311 -0.1250 157 TYR C CZ  
5117  O OH  . TYR C 157 ? 1.0676 1.0083 0.4115 -0.0637 -0.1284 -0.1282 157 TYR C OH  
5118  N N   . PRO C 158 ? 1.2755 1.3071 0.4174 -0.0475 -0.1193 -0.1889 158 PRO C N   
5119  C CA  . PRO C 158 ? 1.2805 1.2829 0.4179 -0.0321 -0.0980 -0.1979 158 PRO C CA  
5120  C C   . PRO C 158 ? 1.2360 1.2017 0.4172 -0.0241 -0.0871 -0.1886 158 PRO C C   
5121  O O   . PRO C 158 ? 1.2108 1.1595 0.4182 -0.0339 -0.0971 -0.1872 158 PRO C O   
5122  C CB  . PRO C 158 ? 1.3278 1.3023 0.4306 -0.0423 -0.1015 -0.2399 158 PRO C CB  
5123  C CG  . PRO C 158 ? 1.3360 1.3083 0.4387 -0.0653 -0.1236 -0.2535 158 PRO C CG  
5124  C CD  . PRO C 158 ? 1.3132 1.3354 0.4299 -0.0687 -0.1361 -0.2226 158 PRO C CD  
5125  N N   . THR C 159 ? 1.2287 1.1853 0.4175 -0.0068 -0.0665 -0.1826 159 THR C N   
5126  C CA  . THR C 159 ? 1.1891 1.1163 0.4186 0.0016  -0.0557 -0.1742 159 THR C CA  
5127  C C   . THR C 159 ? 1.1944 1.0748 0.4292 -0.0058 -0.0619 -0.2013 159 THR C C   
5128  O O   . THR C 159 ? 1.2332 1.0944 0.4395 -0.0088 -0.0626 -0.2302 159 THR C O   
5129  C CB  . THR C 159 ? 1.1858 1.1141 0.4205 0.0200  -0.0322 -0.1675 159 THR C CB  
5130  O OG1 . THR C 159 ? 1.1913 1.1608 0.4156 0.0269  -0.0249 -0.1424 159 THR C OG1 
5131  C CG2 . THR C 159 ? 1.1413 1.0480 0.4214 0.0275  -0.0226 -0.1561 159 THR C CG2 
5132  N N   . ILE C 160 ? 1.1589 1.0206 0.4294 -0.0085 -0.0657 -0.1913 160 ILE C N   
5133  C CA  . ILE C 160 ? 1.1614 0.9780 0.4406 -0.0143 -0.0710 -0.2111 160 ILE C CA  
5134  C C   . ILE C 160 ? 1.1459 0.9385 0.4468 0.0021  -0.0554 -0.2119 160 ILE C C   
5135  O O   . ILE C 160 ? 1.1107 0.9167 0.4400 0.0110  -0.0464 -0.1902 160 ILE C O   
5136  C CB  . ILE C 160 ? 1.1320 0.9440 0.4364 -0.0273 -0.0844 -0.1991 160 ILE C CB  
5137  C CG1 . ILE C 160 ? 1.1505 0.9883 0.4365 -0.0451 -0.1013 -0.2006 160 ILE C CG1 
5138  C CG2 . ILE C 160 ? 1.1316 0.8954 0.4467 -0.0307 -0.0871 -0.2150 160 ILE C CG2 
5139  C CD1 . ILE C 160 ? 1.1188 0.9677 0.4324 -0.0557 -0.1121 -0.1820 160 ILE C CD1 
5140  N N   . LYS C 161 ? 1.1754 0.9335 0.4640 0.0062  -0.0520 -0.2373 161 LYS C N   
5141  C CA  . LYS C 161 ? 1.1627 0.8972 0.4744 0.0217  -0.0401 -0.2398 161 LYS C CA  
5142  C C   . LYS C 161 ? 1.1793 0.8672 0.4919 0.0175  -0.0480 -0.2580 161 LYS C C   
5143  O O   . LYS C 161 ? 1.2220 0.8852 0.5085 0.0161  -0.0485 -0.2829 161 LYS C O   
5144  C CB  . LYS C 161 ? 1.1853 0.9271 0.4832 0.0374  -0.0230 -0.2505 161 LYS C CB  
5145  C CG  . LYS C 161 ? 1.1751 0.9607 0.4719 0.0428  -0.0122 -0.2305 161 LYS C CG  
5146  C CD  . LYS C 161 ? 1.1916 0.9838 0.4831 0.0595  0.0077  -0.2385 161 LYS C CD  
5147  C CE  . LYS C 161 ? 1.1849 1.0191 0.4747 0.0641  0.0201  -0.2162 161 LYS C CE  
5148  N NZ  . LYS C 161 ? 1.2134 1.0580 0.4865 0.0773  0.0394  -0.2268 161 LYS C NZ  
5149  N N   . ARG C 162 ? 1.1503 0.8249 0.4919 0.0155  -0.0534 -0.2454 162 ARG C N   
5150  C CA  . ARG C 162 ? 1.1663 0.7967 0.5095 0.0110  -0.0611 -0.2577 162 ARG C CA  
5151  C C   . ARG C 162 ? 1.1434 0.7586 0.5175 0.0250  -0.0559 -0.2493 162 ARG C C   
5152  O O   . ARG C 162 ? 1.1028 0.7412 0.5036 0.0285  -0.0530 -0.2293 162 ARG C O   
5153  C CB  . ARG C 162 ? 1.1621 0.7895 0.5037 -0.0104 -0.0767 -0.2526 162 ARG C CB  
5154  C CG  . ARG C 162 ? 1.2014 0.8303 0.5102 -0.0270 -0.0853 -0.2697 162 ARG C CG  
5155  C CD  . ARG C 162 ? 1.2523 0.8405 0.5353 -0.0252 -0.0822 -0.2997 162 ARG C CD  
5156  N NE  . ARG C 162 ? 1.2792 0.8360 0.5515 -0.0452 -0.0939 -0.3130 162 ARG C NE  
5157  C CZ  . ARG C 162 ? 1.2991 0.8718 0.5524 -0.0662 -0.1047 -0.3212 162 ARG C CZ  
5158  N NH1 . ARG C 162 ? 1.2958 0.9161 0.5367 -0.0682 -0.1064 -0.3160 162 ARG C NH1 
5159  N NH2 . ARG C 162 ? 1.3243 0.8666 0.5713 -0.0855 -0.1139 -0.3338 162 ARG C NH2 
5160  N N   . SER C 163 ? 1.1751 0.7512 0.5450 0.0333  -0.0547 -0.2652 163 SER C N   
5161  C CA  . SER C 163 ? 1.1622 0.7237 0.5582 0.0483  -0.0512 -0.2595 163 SER C CA  
5162  C C   . SER C 163 ? 1.1916 0.7061 0.5829 0.0442  -0.0600 -0.2666 163 SER C C   
5163  O O   . SER C 163 ? 1.2351 0.7188 0.6014 0.0390  -0.0618 -0.2851 163 SER C O   
5164  C CB  . SER C 163 ? 1.1742 0.7390 0.5726 0.0697  -0.0372 -0.2701 163 SER C CB  
5165  O OG  . SER C 163 ? 1.1578 0.7136 0.5830 0.0850  -0.0350 -0.2649 163 SER C OG  
5166  N N   . TYR C 164 ? 1.1749 0.6832 0.5891 0.0460  -0.0647 -0.2519 164 TYR C N   
5167  C CA  . TYR C 164 ? 1.2057 0.6690 0.6170 0.0457  -0.0711 -0.2552 164 TYR C CA  
5168  C C   . TYR C 164 ? 1.2055 0.6620 0.6388 0.0668  -0.0679 -0.2491 164 TYR C C   
5169  O O   . TYR C 164 ? 1.1645 0.6507 0.6223 0.0708  -0.0674 -0.2342 164 TYR C O   
5170  C CB  . TYR C 164 ? 1.1906 0.6489 0.6041 0.0252  -0.0820 -0.2428 164 TYR C CB  
5171  C CG  . TYR C 164 ? 1.2079 0.6231 0.6222 0.0274  -0.0867 -0.2409 164 TYR C CG  
5172  C CD1 . TYR C 164 ? 1.2578 0.6261 0.6500 0.0223  -0.0881 -0.2559 164 TYR C CD1 
5173  C CD2 . TYR C 164 ? 1.1790 0.5991 0.6151 0.0352  -0.0888 -0.2244 164 TYR C CD2 
5174  C CE1 . TYR C 164 ? 1.2785 0.6045 0.6706 0.0256  -0.0909 -0.2518 164 TYR C CE1 
5175  C CE2 . TYR C 164 ? 1.1986 0.5803 0.6329 0.0387  -0.0929 -0.2206 164 TYR C CE2 
5176  C CZ  . TYR C 164 ? 1.2485 0.5824 0.6609 0.0344  -0.0936 -0.2330 164 TYR C CZ  
5177  O OH  . TYR C 164 ? 1.2717 0.5651 0.6816 0.0387  -0.0964 -0.2267 164 TYR C OH  
5178  N N   . ASN C 165 ? 1.2597 0.6767 0.6842 0.0797  -0.0662 -0.2607 165 ASN C N   
5179  C CA  . ASN C 165 ? 1.2718 0.6806 0.7153 0.1015  -0.0648 -0.2552 165 ASN C CA  
5180  C C   . ASN C 165 ? 1.2678 0.6431 0.7110 0.0972  -0.0744 -0.2445 165 ASN C C   
5181  O O   . ASN C 165 ? 1.3073 0.6390 0.7299 0.0893  -0.0769 -0.2519 165 ASN C O   
5182  C CB  . ASN C 165 ? 1.3390 0.7256 0.7743 0.1223  -0.0557 -0.2729 165 ASN C CB  
5183  C CG  . ASN C 165 ? 1.3655 0.7607 0.8259 0.1484  -0.0528 -0.2672 165 ASN C CG  
5184  O OD1 . ASN C 165 ? 1.3338 0.7430 0.8140 0.1503  -0.0596 -0.2511 165 ASN C OD1 
5185  N ND2 . ASN C 165 ? 1.4406 0.8293 0.9002 0.1689  -0.0427 -0.2816 165 ASN C ND2 
5186  N N   . ASN C 166 ? 1.2202 0.6153 0.6854 0.1017  -0.0789 -0.2278 166 ASN C N   
5187  C CA  . ASN C 166 ? 1.2164 0.5846 0.6808 0.0986  -0.0874 -0.2154 166 ASN C CA  
5188  C C   . ASN C 166 ? 1.2460 0.5781 0.7079 0.1212  -0.0869 -0.2175 166 ASN C C   
5189  O O   . ASN C 166 ? 1.2309 0.5805 0.7118 0.1404  -0.0879 -0.2104 166 ASN C O   
5190  C CB  . ASN C 166 ? 1.1675 0.5717 0.6542 0.0951  -0.0920 -0.1982 166 ASN C CB  
5191  C CG  . ASN C 166 ? 1.1722 0.5527 0.6536 0.0865  -0.1003 -0.1847 166 ASN C CG  
5192  O OD1 . ASN C 166 ? 1.2046 0.5459 0.6660 0.0756  -0.1025 -0.1865 166 ASN C OD1 
5193  N ND2 . ASN C 166 ? 1.1410 0.5455 0.6399 0.0904  -0.1042 -0.1718 166 ASN C ND2 
5194  N N   . THR C 167 ? 1.2868 0.5690 0.7259 0.1187  -0.0854 -0.2274 167 THR C N   
5195  C CA  . THR C 167 ? 1.3254 0.5651 0.7596 0.1408  -0.0835 -0.2291 167 THR C CA  
5196  C C   . THR C 167 ? 1.3316 0.5426 0.7631 0.1402  -0.0913 -0.2107 167 THR C C   
5197  O O   . THR C 167 ? 1.3664 0.5456 0.7962 0.1613  -0.0908 -0.2066 167 THR C O   
5198  C CB  . THR C 167 ? 1.3808 0.5733 0.7908 0.1388  -0.0762 -0.2494 167 THR C CB  
5199  O OG1 . THR C 167 ? 1.3943 0.5632 0.7855 0.1095  -0.0799 -0.2514 167 THR C OG1 
5200  C CG2 . THR C 167 ? 1.3769 0.5960 0.7869 0.1443  -0.0672 -0.2681 167 THR C CG2 
5201  N N   . ASN C 168 ? 1.2986 0.5209 0.7292 0.1174  -0.0977 -0.1989 168 ASN C N   
5202  C CA  . ASN C 168 ? 1.3008 0.5025 0.7285 0.1155  -0.1043 -0.1800 168 ASN C CA  
5203  C C   . ASN C 168 ? 1.2652 0.5027 0.7138 0.1358  -0.1090 -0.1671 168 ASN C C   
5204  O O   . ASN C 168 ? 1.2226 0.5090 0.6903 0.1387  -0.1082 -0.1704 168 ASN C O   
5205  C CB  . ASN C 168 ? 1.2786 0.4890 0.7021 0.0857  -0.1086 -0.1715 168 ASN C CB  
5206  C CG  . ASN C 168 ? 1.2851 0.4917 0.6973 0.0621  -0.1056 -0.1864 168 ASN C CG  
5207  O OD1 . ASN C 168 ? 1.3254 0.4896 0.7198 0.0478  -0.1046 -0.1912 168 ASN C OD1 
5208  N ND2 . ASN C 168 ? 1.2476 0.4996 0.6701 0.0575  -0.1042 -0.1933 168 ASN C ND2 
5209  N N   . GLN C 169 ? 1.2829 0.4971 0.7276 0.1493  -0.1137 -0.1525 169 GLN C N   
5210  C CA  . GLN C 169 ? 1.2516 0.5035 0.7146 0.1660  -0.1204 -0.1400 169 GLN C CA  
5211  C C   . GLN C 169 ? 1.2143 0.4891 0.6787 0.1461  -0.1265 -0.1264 169 GLN C C   
5212  O O   . GLN C 169 ? 1.2238 0.4917 0.6830 0.1512  -0.1327 -0.1104 169 GLN C O   
5213  C CB  . GLN C 169 ? 1.2929 0.5175 0.7527 0.1948  -0.1232 -0.1305 169 GLN C CB  
5214  C CG  . GLN C 169 ? 1.3412 0.5089 0.7767 0.1917  -0.1246 -0.1162 169 GLN C CG  
5215  C CD  . GLN C 169 ? 1.3663 0.5275 0.8024 0.2196  -0.1312 -0.0983 169 GLN C CD  
5216  O OE1 . GLN C 169 ? 1.3354 0.5450 0.7898 0.2333  -0.1385 -0.0929 169 GLN C OE1 
5217  N NE2 . GLN C 169 ? 1.4246 0.5264 0.8407 0.2277  -0.1287 -0.0885 169 GLN C NE2 
5218  N N   . GLU C 170 ? 1.1730 0.4754 0.6437 0.1244  -0.1239 -0.1328 170 GLU C N   
5219  C CA  . GLU C 170 ? 1.1362 0.4622 0.6104 0.1045  -0.1272 -0.1227 170 GLU C CA  
5220  C C   . GLU C 170 ? 1.0853 0.4590 0.5787 0.0946  -0.1237 -0.1309 170 GLU C C   
5221  O O   . GLU C 170 ? 1.0830 0.4629 0.5797 0.0963  -0.1181 -0.1439 170 GLU C O   
5222  C CB  . GLU C 170 ? 1.1570 0.4476 0.6113 0.0811  -0.1262 -0.1182 170 GLU C CB  
5223  C CG  . GLU C 170 ? 1.2010 0.4466 0.6365 0.0851  -0.1289 -0.1045 170 GLU C CG  
5224  C CD  . GLU C 170 ? 1.2562 0.4458 0.6740 0.0894  -0.1245 -0.1112 170 GLU C CD  
5225  O OE1 . GLU C 170 ? 1.2640 0.4511 0.6848 0.0982  -0.1204 -0.1274 170 GLU C OE1 
5226  O OE2 . GLU C 170 ? 1.2950 0.4412 0.6953 0.0837  -0.1240 -0.1006 170 GLU C OE2 
5227  N N   . ASP C 171 ? 1.0467 0.4528 0.5519 0.0851  -0.1259 -0.1229 171 ASP C N   
5228  C CA  . ASP C 171 ? 1.0033 0.4466 0.5240 0.0710  -0.1212 -0.1271 171 ASP C CA  
5229  C C   . ASP C 171 ? 1.0093 0.4342 0.5159 0.0496  -0.1189 -0.1283 171 ASP C C   
5230  O O   . ASP C 171 ? 1.0357 0.4273 0.5251 0.0405  -0.1215 -0.1224 171 ASP C O   
5231  C CB  . ASP C 171 ? 0.9697 0.4454 0.5049 0.0651  -0.1230 -0.1186 171 ASP C CB  
5232  C CG  . ASP C 171 ? 0.9577 0.4613 0.5105 0.0833  -0.1259 -0.1199 171 ASP C CG  
5233  O OD1 . ASP C 171 ? 0.9619 0.4731 0.5240 0.0992  -0.1242 -0.1284 171 ASP C OD1 
5234  O OD2 . ASP C 171 ? 0.9448 0.4652 0.5028 0.0810  -0.1297 -0.1133 171 ASP C OD2 
5235  N N   . LEU C 172 ? 0.9860 0.4339 0.5002 0.0413  -0.1139 -0.1354 172 LEU C N   
5236  C CA  . LEU C 172 ? 0.9912 0.4298 0.4940 0.0215  -0.1130 -0.1377 172 LEU C CA  
5237  C C   . LEU C 172 ? 0.9503 0.4278 0.4685 0.0085  -0.1100 -0.1328 172 LEU C C   
5238  O O   . LEU C 172 ? 0.9254 0.4336 0.4588 0.0152  -0.1051 -0.1355 172 LEU C O   
5239  C CB  . LEU C 172 ? 1.0167 0.4405 0.5074 0.0253  -0.1102 -0.1525 172 LEU C CB  
5240  C CG  . LEU C 172 ? 1.0359 0.4440 0.5103 0.0044  -0.1114 -0.1576 172 LEU C CG  
5241  C CD1 . LEU C 172 ? 1.0799 0.4380 0.5354 -0.0004 -0.1144 -0.1579 172 LEU C CD1 
5242  C CD2 . LEU C 172 ? 1.0454 0.4614 0.5127 0.0056  -0.1076 -0.1726 172 LEU C CD2 
5243  N N   . LEU C 173 ? 0.9451 0.4208 0.4603 -0.0094 -0.1118 -0.1249 173 LEU C N   
5244  C CA  . LEU C 173 ? 0.9114 0.4214 0.4411 -0.0215 -0.1087 -0.1191 173 LEU C CA  
5245  C C   . LEU C 173 ? 0.9178 0.4343 0.4403 -0.0312 -0.1084 -0.1257 173 LEU C C   
5246  O O   . LEU C 173 ? 0.9407 0.4387 0.4492 -0.0452 -0.1124 -0.1280 173 LEU C O   
5247  C CB  . LEU C 173 ? 0.9049 0.4138 0.4365 -0.0356 -0.1101 -0.1076 173 LEU C CB  
5248  C CG  . LEU C 173 ? 0.8756 0.4178 0.4227 -0.0480 -0.1064 -0.1007 173 LEU C CG  
5249  C CD1 . LEU C 173 ? 0.8419 0.4157 0.4106 -0.0383 -0.1000 -0.0980 173 LEU C CD1 
5250  C CD2 . LEU C 173 ? 0.8767 0.4141 0.4236 -0.0625 -0.1072 -0.0908 173 LEU C CD2 
5251  N N   . VAL C 174 ? 0.8989 0.4432 0.4308 -0.0245 -0.1035 -0.1286 174 VAL C N   
5252  C CA  . VAL C 174 ? 0.9043 0.4618 0.4285 -0.0318 -0.1032 -0.1338 174 VAL C CA  
5253  C C   . VAL C 174 ? 0.8735 0.4671 0.4140 -0.0406 -0.1006 -0.1215 174 VAL C C   
5254  O O   . VAL C 174 ? 0.8452 0.4599 0.4054 -0.0337 -0.0944 -0.1136 174 VAL C O   
5255  C CB  . VAL C 174 ? 0.9093 0.4745 0.4306 -0.0172 -0.0979 -0.1438 174 VAL C CB  
5256  C CG1 . VAL C 174 ? 0.9256 0.4998 0.4313 -0.0251 -0.0988 -0.1511 174 VAL C CG1 
5257  C CG2 . VAL C 174 ? 0.9350 0.4685 0.4468 -0.0034 -0.0985 -0.1541 174 VAL C CG2 
5258  N N   . LEU C 175 ? 0.8815 0.4821 0.4148 -0.0558 -0.1052 -0.1205 175 LEU C N   
5259  C CA  . LEU C 175 ? 0.8572 0.4935 0.4055 -0.0629 -0.1035 -0.1081 175 LEU C CA  
5260  C C   . LEU C 175 ? 0.8670 0.5243 0.4050 -0.0649 -0.1050 -0.1120 175 LEU C C   
5261  O O   . LEU C 175 ? 0.8970 0.5393 0.4137 -0.0711 -0.1109 -0.1251 175 LEU C O   
5262  C CB  . LEU C 175 ? 0.8581 0.4928 0.4098 -0.0797 -0.1085 -0.1014 175 LEU C CB  
5263  C CG  . LEU C 175 ? 0.8546 0.4681 0.4115 -0.0806 -0.1076 -0.0968 175 LEU C CG  
5264  C CD1 . LEU C 175 ? 0.8624 0.4737 0.4195 -0.0992 -0.1118 -0.0915 175 LEU C CD1 
5265  C CD2 . LEU C 175 ? 0.8226 0.4542 0.4009 -0.0703 -0.0995 -0.0873 175 LEU C CD2 
5266  N N   . TRP C 176 ? 0.8447 0.5358 0.3967 -0.0597 -0.0991 -0.1007 176 TRP C N   
5267  C CA  . TRP C 176 ? 0.8535 0.5712 0.3960 -0.0616 -0.1009 -0.0999 176 TRP C CA  
5268  C C   . TRP C 176 ? 0.8283 0.5825 0.3918 -0.0606 -0.0963 -0.0803 176 TRP C C   
5269  O O   . TRP C 176 ? 0.8045 0.5605 0.3900 -0.0585 -0.0906 -0.0696 176 TRP C O   
5270  C CB  . TRP C 176 ? 0.8658 0.5816 0.3949 -0.0487 -0.0953 -0.1095 176 TRP C CB  
5271  C CG  . TRP C 176 ? 0.8415 0.5685 0.3897 -0.0339 -0.0827 -0.1008 176 TRP C CG  
5272  C CD1 . TRP C 176 ? 0.8294 0.5861 0.3867 -0.0272 -0.0741 -0.0884 176 TRP C CD1 
5273  C CD2 . TRP C 176 ? 0.8293 0.5386 0.3905 -0.0247 -0.0770 -0.1038 176 TRP C CD2 
5274  N NE1 . TRP C 176 ? 0.8107 0.5671 0.3871 -0.0160 -0.0624 -0.0846 176 TRP C NE1 
5275  C CE2 . TRP C 176 ? 0.8094 0.5394 0.3889 -0.0145 -0.0648 -0.0948 176 TRP C CE2 
5276  C CE3 . TRP C 176 ? 0.8355 0.5145 0.3946 -0.0239 -0.0811 -0.1126 176 TRP C CE3 
5277  C CZ2 . TRP C 176 ? 0.7947 0.5184 0.3917 -0.0055 -0.0574 -0.0966 176 TRP C CZ2 
5278  C CZ3 . TRP C 176 ? 0.8208 0.4955 0.3957 -0.0129 -0.0749 -0.1129 176 TRP C CZ3 
5279  C CH2 . TRP C 176 ? 0.7999 0.4982 0.3943 -0.0047 -0.0636 -0.1061 176 TRP C CH2 
5280  N N   . GLY C 177 ? 0.8366 0.6196 0.3925 -0.0613 -0.0986 -0.0755 177 GLY C N   
5281  C CA  . GLY C 177 ? 0.8180 0.6362 0.3931 -0.0587 -0.0946 -0.0548 177 GLY C CA  
5282  C C   . GLY C 177 ? 0.8269 0.6738 0.3927 -0.0505 -0.0915 -0.0475 177 GLY C C   
5283  O O   . GLY C 177 ? 0.8507 0.6946 0.3914 -0.0497 -0.0946 -0.0603 177 GLY C O   
5284  N N   . ILE C 178 ? 0.8103 0.6842 0.3962 -0.0435 -0.0843 -0.0261 178 ILE C N   
5285  C CA  . ILE C 178 ? 0.8200 0.7257 0.3987 -0.0353 -0.0814 -0.0129 178 ILE C CA  
5286  C C   . ILE C 178 ? 0.8161 0.7559 0.4075 -0.0394 -0.0881 0.0047  178 ILE C C   
5287  O O   . ILE C 178 ? 0.7964 0.7351 0.4126 -0.0422 -0.0864 0.0127  178 ILE C O   
5288  C CB  . ILE C 178 ? 0.8072 0.7125 0.4007 -0.0196 -0.0628 -0.0002 178 ILE C CB  
5289  C CG1 . ILE C 178 ? 0.8260 0.7581 0.4029 -0.0107 -0.0589 0.0103  178 ILE C CG1 
5290  C CG2 . ILE C 178 ? 0.7814 0.6891 0.4091 -0.0160 -0.0532 0.0170  178 ILE C CG2 
5291  C CD1 . ILE C 178 ? 0.8158 0.7621 0.4134 0.0027  -0.0420 0.0350  178 ILE C CD1 
5292  N N   . HIS C 179 ? 0.8363 0.8087 0.4109 -0.0393 -0.0960 0.0103  179 HIS C N   
5293  C CA  . HIS C 179 ? 0.8349 0.8468 0.4225 -0.0408 -0.1032 0.0290  179 HIS C CA  
5294  C C   . HIS C 179 ? 0.8323 0.8699 0.4311 -0.0228 -0.0913 0.0564  179 HIS C C   
5295  O O   . HIS C 179 ? 0.8481 0.8907 0.4281 -0.0136 -0.0855 0.0592  179 HIS C O   
5296  C CB  . HIS C 179 ? 0.8618 0.8992 0.4247 -0.0538 -0.1223 0.0183  179 HIS C CB  
5297  C CG  . HIS C 179 ? 0.8625 0.9485 0.4385 -0.0538 -0.1311 0.0382  179 HIS C CG  
5298  N ND1 . HIS C 179 ? 0.8851 1.0121 0.4429 -0.0489 -0.1388 0.0477  179 HIS C ND1 
5299  C CD2 . HIS C 179 ? 0.8445 0.9475 0.4510 -0.0567 -0.1331 0.0513  179 HIS C CD2 
5300  C CE1 . HIS C 179 ? 0.8807 1.0491 0.4582 -0.0485 -0.1464 0.0663  179 HIS C CE1 
5301  N NE2 . HIS C 179 ? 0.8557 1.0102 0.4640 -0.0531 -0.1425 0.0686  179 HIS C NE2 
5302  N N   . HIS C 180 ? 0.8154 0.8685 0.4449 -0.0177 -0.0866 0.0770  180 HIS C N   
5303  C CA  . HIS C 180 ? 0.8156 0.8922 0.4595 -0.0001 -0.0748 0.1061  180 HIS C CA  
5304  C C   . HIS C 180 ? 0.8284 0.9547 0.4726 0.0001  -0.0890 0.1221  180 HIS C C   
5305  O O   . HIS C 180 ? 0.8169 0.9573 0.4827 -0.0059 -0.0957 0.1257  180 HIS C O   
5306  C CB  . HIS C 180 ? 0.7908 0.8486 0.4712 0.0073  -0.0577 0.1180  180 HIS C CB  
5307  C CG  . HIS C 180 ? 0.7785 0.7928 0.4616 0.0064  -0.0451 0.1023  180 HIS C CG  
5308  N ND1 . HIS C 180 ? 0.7758 0.7762 0.4693 0.0186  -0.0255 0.1123  180 HIS C ND1 
5309  C CD2 . HIS C 180 ? 0.7700 0.7538 0.4478 -0.0052 -0.0494 0.0781  180 HIS C CD2 
5310  C CE1 . HIS C 180 ? 0.7645 0.7310 0.4600 0.0141  -0.0193 0.0936  180 HIS C CE1 
5311  N NE2 . HIS C 180 ? 0.7611 0.7171 0.4464 0.0008  -0.0339 0.0736  180 HIS C NE2 
5312  N N   . PRO C 181 ? 0.8537 1.0093 0.4737 0.0074  -0.0937 0.1316  181 PRO C N   
5313  C CA  . PRO C 181 ? 0.8695 1.0781 0.4867 0.0080  -0.1095 0.1463  181 PRO C CA  
5314  C C   . PRO C 181 ? 0.8634 1.0975 0.5110 0.0272  -0.0994 0.1821  181 PRO C C   
5315  O O   . PRO C 181 ? 0.8536 1.0632 0.5179 0.0411  -0.0782 0.1963  181 PRO C O   
5316  C CB  . PRO C 181 ? 0.9019 1.1280 0.4776 0.0099  -0.1162 0.1419  181 PRO C CB  
5317  C CG  . PRO C 181 ? 0.9004 1.0914 0.4702 0.0214  -0.0949 0.1439  181 PRO C CG  
5318  C CD  . PRO C 181 ? 0.8707 1.0145 0.4644 0.0156  -0.0841 0.1296  181 PRO C CD  
5319  N N   . ASN C 182 ? 0.8717 1.1551 0.5271 0.0278  -0.1142 0.1960  182 ASN C N   
5320  C CA  . ASN C 182 ? 0.8689 1.1807 0.5553 0.0474  -0.1063 0.2311  182 ASN C CA  
5321  C C   . ASN C 182 ? 0.8911 1.2156 0.5657 0.0698  -0.0947 0.2597  182 ASN C C   
5322  O O   . ASN C 182 ? 0.8853 1.1966 0.5854 0.0878  -0.0744 0.2841  182 ASN C O   
5323  C CB  . ASN C 182 ? 0.8734 1.2407 0.5718 0.0419  -0.1274 0.2375  182 ASN C CB  
5324  C CG  . ASN C 182 ? 0.8492 1.2050 0.5728 0.0244  -0.1320 0.2195  182 ASN C CG  
5325  O OD1 . ASN C 182 ? 0.8284 1.1679 0.5864 0.0318  -0.1173 0.2298  182 ASN C OD1 
5326  N ND2 . ASN C 182 ? 0.8549 1.2172 0.5607 0.0007  -0.1512 0.1922  182 ASN C ND2 
5327  N N   . ASP C 183 ? 0.9196 1.2685 0.5550 0.0684  -0.1067 0.2563  183 ASP C N   
5328  C CA  . ASP C 183 ? 0.9468 1.3126 0.5648 0.0890  -0.0971 0.2844  183 ASP C CA  
5329  C C   . ASP C 183 ? 0.9725 1.3356 0.5417 0.0822  -0.1021 0.2664  183 ASP C C   
5330  O O   . ASP C 183 ? 0.9712 1.3226 0.5203 0.0620  -0.1149 0.2320  183 ASP C O   
5331  C CB  . ASP C 183 ? 0.9648 1.3922 0.5913 0.1035  -0.1091 0.3164  183 ASP C CB  
5332  C CG  . ASP C 183 ? 0.9732 1.4489 0.5867 0.0861  -0.1398 0.2994  183 ASP C CG  
5333  O OD1 . ASP C 183 ? 0.9876 1.4626 0.5640 0.0689  -0.1530 0.2708  183 ASP C OD1 
5334  O OD2 . ASP C 183 ? 0.9674 1.4827 0.6091 0.0896  -0.1502 0.3141  183 ASP C OD2 
5335  N N   . ALA C 184 ? 0.9987 1.3714 0.5491 0.0999  -0.0904 0.2903  184 ALA C N   
5336  C CA  . ALA C 184 ? 1.0271 1.3994 0.5305 0.0966  -0.0914 0.2767  184 ALA C CA  
5337  C C   . ALA C 184 ? 1.0520 1.4676 0.5197 0.0826  -0.1200 0.2577  184 ALA C C   
5338  O O   . ALA C 184 ? 1.0677 1.4717 0.4994 0.0706  -0.1245 0.2294  184 ALA C O   
5339  C CB  . ALA C 184 ? 1.0537 1.4345 0.5454 0.1194  -0.0730 0.3116  184 ALA C CB  
5340  N N   . ALA C 185 ? 1.0573 1.5236 0.5363 0.0841  -0.1387 0.2723  185 ALA C N   
5341  C CA  . ALA C 185 ? 1.0813 1.5943 0.5315 0.0686  -0.1676 0.2537  185 ALA C CA  
5342  C C   . ALA C 185 ? 1.0647 1.5521 0.5161 0.0403  -0.1800 0.2104  185 ALA C C   
5343  O O   . ALA C 185 ? 1.0885 1.5854 0.5040 0.0234  -0.1956 0.1816  185 ALA C O   
5344  C CB  . ALA C 185 ? 1.0885 1.6650 0.5575 0.0779  -0.1838 0.2819  185 ALA C CB  
5345  N N   . GLU C 186 ? 1.0277 1.4812 0.5192 0.0353  -0.1722 0.2060  186 GLU C N   
5346  C CA  . GLU C 186 ? 1.0124 1.4360 0.5075 0.0099  -0.1810 0.1686  186 GLU C CA  
5347  C C   . GLU C 186 ? 1.0144 1.3826 0.4846 0.0030  -0.1695 0.1406  186 GLU C C   
5348  O O   . GLU C 186 ? 1.0234 1.3762 0.4742 -0.0173 -0.1809 0.1067  186 GLU C O   
5349  C CB  . GLU C 186 ? 0.9744 1.3803 0.5183 0.0082  -0.1748 0.1747  186 GLU C CB  
5350  C CG  . GLU C 186 ? 0.9615 1.3411 0.5100 -0.0177 -0.1846 0.1402  186 GLU C CG  
5351  C CD  . GLU C 186 ? 0.9325 1.3173 0.5260 -0.0215 -0.1849 0.1484  186 GLU C CD  
5352  O OE1 . GLU C 186 ? 0.9059 1.2554 0.5265 -0.0120 -0.1658 0.1580  186 GLU C OE1 
5353  O OE2 . GLU C 186 ? 0.9381 1.3633 0.5399 -0.0350 -0.2038 0.1441  186 GLU C OE2 
5354  N N   . GLN C 187 ? 1.0080 1.3463 0.4809 0.0199  -0.1463 0.1550  187 GLN C N   
5355  C CA  . GLN C 187 ? 1.0119 1.3041 0.4628 0.0169  -0.1338 0.1320  187 GLN C CA  
5356  C C   . GLN C 187 ? 1.0522 1.3620 0.4535 0.0090  -0.1459 0.1113  187 GLN C C   
5357  O O   . GLN C 187 ? 1.0588 1.3393 0.4414 -0.0058 -0.1499 0.0773  187 GLN C O   
5358  C CB  . GLN C 187 ? 1.0043 1.2746 0.4660 0.0373  -0.1072 0.1553  187 GLN C CB  
5359  C CG  . GLN C 187 ? 1.0132 1.2473 0.4511 0.0373  -0.0933 0.1361  187 GLN C CG  
5360  C CD  . GLN C 187 ? 0.9937 1.1823 0.4377 0.0218  -0.0945 0.1019  187 GLN C CD  
5361  O OE1 . GLN C 187 ? 0.9620 1.1276 0.4399 0.0184  -0.0912 0.1016  187 GLN C OE1 
5362  N NE2 . GLN C 187 ? 1.0151 1.1904 0.4255 0.0135  -0.0986 0.0734  187 GLN C NE2 
5363  N N   . THR C 188 ? 1.0822 1.4398 0.4616 0.0199  -0.1513 0.1322  188 THR C N   
5364  C CA  . THR C 188 ? 1.1255 1.5065 0.4547 0.0134  -0.1630 0.1141  188 THR C CA  
5365  C C   . THR C 188 ? 1.1389 1.5400 0.4567 -0.0108 -0.1897 0.0847  188 THR C C   
5366  O O   . THR C 188 ? 1.1645 1.5530 0.4480 -0.0251 -0.1964 0.0512  188 THR C O   
5367  C CB  . THR C 188 ? 1.1567 1.5890 0.4642 0.0317  -0.1633 0.1468  188 THR C CB  
5368  O OG1 . THR C 188 ? 1.1500 1.6283 0.4829 0.0367  -0.1767 0.1732  188 THR C OG1 
5369  C CG2 . THR C 188 ? 1.1531 1.5622 0.4654 0.0537  -0.1347 0.1734  188 THR C CG2 
5370  N N   . LYS C 189 ? 1.1235 1.5549 0.4716 -0.0159 -0.2038 0.0964  189 LYS C N   
5371  C CA  . LYS C 189 ? 1.1351 1.5879 0.4789 -0.0410 -0.2285 0.0699  189 LYS C CA  
5372  C C   . LYS C 189 ? 1.1281 1.5238 0.4703 -0.0620 -0.2270 0.0305  189 LYS C C   
5373  O O   . LYS C 189 ? 1.1565 1.5547 0.4720 -0.0825 -0.2420 -0.0014 189 LYS C O   
5374  C CB  . LYS C 189 ? 1.1123 1.6027 0.4983 -0.0417 -0.2395 0.0911  189 LYS C CB  
5375  C CG  . LYS C 189 ? 1.1186 1.6273 0.5091 -0.0700 -0.2626 0.0638  189 LYS C CG  
5376  C CD  . LYS C 189 ? 1.1083 1.6772 0.5329 -0.0682 -0.2770 0.0880  189 LYS C CD  
5377  C CE  . LYS C 189 ? 1.1144 1.7026 0.5473 -0.0987 -0.2988 0.0603  189 LYS C CE  
5378  N NZ  . LYS C 189 ? 1.0767 1.6267 0.5512 -0.1088 -0.2908 0.0551  189 LYS C NZ  
5379  N N   . LEU C 190 ? 1.0937 1.4382 0.4640 -0.0564 -0.2089 0.0332  190 LEU C N   
5380  C CA  . LEU C 190 ? 1.0853 1.3743 0.4582 -0.0731 -0.2064 0.0011  190 LEU C CA  
5381  C C   . LEU C 190 ? 1.1039 1.3524 0.4434 -0.0706 -0.1949 -0.0214 190 LEU C C   
5382  O O   . LEU C 190 ? 1.1257 1.3504 0.4432 -0.0876 -0.2020 -0.0551 190 LEU C O   
5383  C CB  . LEU C 190 ? 1.0421 1.2975 0.4591 -0.0678 -0.1930 0.0140  190 LEU C CB  
5384  C CG  . LEU C 190 ? 1.0243 1.3016 0.4758 -0.0792 -0.2048 0.0210  190 LEU C CG  
5385  C CD1 . LEU C 190 ? 0.9857 1.2541 0.4795 -0.0636 -0.1893 0.0492  190 LEU C CD1 
5386  C CD2 . LEU C 190 ? 1.0285 1.2731 0.4791 -0.1044 -0.2133 -0.0114 190 LEU C CD2 
5387  N N   . TYR C 191 ? 1.0961 1.3359 0.4340 -0.0493 -0.1758 -0.0025 191 TYR C N   
5388  C CA  . TYR C 191 ? 1.1074 1.3077 0.4221 -0.0438 -0.1607 -0.0205 191 TYR C CA  
5389  C C   . TYR C 191 ? 1.1388 1.3658 0.4183 -0.0299 -0.1538 -0.0109 191 TYR C C   
5390  O O   . TYR C 191 ? 1.1558 1.3574 0.4113 -0.0263 -0.1423 -0.0280 191 TYR C O   
5391  C CB  . TYR C 191 ? 1.0687 1.2260 0.4168 -0.0329 -0.1405 -0.0109 191 TYR C CB  
5392  C CG  . TYR C 191 ? 1.0339 1.1757 0.4210 -0.0417 -0.1450 -0.0084 191 TYR C CG  
5393  C CD1 . TYR C 191 ? 1.0329 1.1407 0.4208 -0.0592 -0.1527 -0.0365 191 TYR C CD1 
5394  C CD2 . TYR C 191 ? 1.0056 1.1661 0.4278 -0.0321 -0.1404 0.0226  191 TYR C CD2 
5395  C CE1 . TYR C 191 ? 1.0040 1.0986 0.4252 -0.0674 -0.1558 -0.0332 191 TYR C CE1 
5396  C CE2 . TYR C 191 ? 0.9764 1.1240 0.4326 -0.0400 -0.1433 0.0241  191 TYR C CE2 
5397  C CZ  . TYR C 191 ? 0.9754 1.0912 0.4302 -0.0579 -0.1511 -0.0035 191 TYR C CZ  
5398  O OH  . TYR C 191 ? 0.9491 1.0530 0.4355 -0.0659 -0.1529 -0.0012 191 TYR C OH  
5399  N N   . GLN C 192 ? 1.1475 1.4262 0.4244 -0.0210 -0.1599 0.0175  192 GLN C N   
5400  C CA  . GLN C 192 ? 1.1815 1.4928 0.4228 -0.0074 -0.1549 0.0315  192 GLN C CA  
5401  C C   . GLN C 192 ? 1.1706 1.4617 0.4193 0.0135  -0.1275 0.0538  192 GLN C C   
5402  O O   . GLN C 192 ? 1.1784 1.5003 0.4265 0.0300  -0.1205 0.0878  192 GLN C O   
5403  C CB  . GLN C 192 ? 1.2270 1.5419 0.4181 -0.0195 -0.1642 -0.0032 192 GLN C CB  
5404  C CG  . GLN C 192 ? 1.2693 1.6410 0.4212 -0.0124 -0.1720 0.0106  192 GLN C CG  
5405  C CD  . GLN C 192 ? 1.3173 1.6980 0.4198 -0.0282 -0.1852 -0.0271 192 GLN C CD  
5406  O OE1 . GLN C 192 ? 1.3428 1.7677 0.4278 -0.0404 -0.2081 -0.0339 192 GLN C OE1 
5407  N NE2 . GLN C 192 ? 1.3319 1.6714 0.4127 -0.0283 -0.1706 -0.0533 192 GLN C NE2 
5408  N N   . ASN C 193 ? 1.1547 1.3957 0.4114 0.0130  -0.1121 0.0353  193 ASN C N   
5409  C CA  . ASN C 193 ? 1.1444 1.3652 0.4112 0.0301  -0.0855 0.0524  193 ASN C CA  
5410  C C   . ASN C 193 ? 1.1097 1.3321 0.4211 0.0413  -0.0756 0.0881  193 ASN C C   
5411  O O   . ASN C 193 ? 1.0763 1.2803 0.4223 0.0345  -0.0803 0.0853  193 ASN C O   
5412  C CB  . ASN C 193 ? 1.1318 1.3014 0.4043 0.0261  -0.0736 0.0237  193 ASN C CB  
5413  C CG  . ASN C 193 ? 1.1651 1.3255 0.3985 0.0139  -0.0837 -0.0149 193 ASN C CG  
5414  O OD1 . ASN C 193 ? 1.1932 1.3818 0.3993 0.0035  -0.1028 -0.0252 193 ASN C OD1 
5415  N ND2 . ASN C 193 ? 1.1640 1.2855 0.3957 0.0151  -0.0708 -0.0373 193 ASN C ND2 
5416  N N   . PRO C 194 ? 1.1207 1.3638 0.4305 0.0588  -0.0609 0.1218  194 PRO C N   
5417  C CA  . PRO C 194 ? 1.0952 1.3407 0.4457 0.0704  -0.0510 0.1569  194 PRO C CA  
5418  C C   . PRO C 194 ? 1.0569 1.2547 0.4474 0.0708  -0.0325 0.1531  194 PRO C C   
5419  O O   . PRO C 194 ? 1.0269 1.2153 0.4547 0.0699  -0.0334 0.1624  194 PRO C O   
5420  C CB  . PRO C 194 ? 1.1258 1.3985 0.4580 0.0887  -0.0369 0.1907  194 PRO C CB  
5421  C CG  . PRO C 194 ? 1.1548 1.4210 0.4471 0.0876  -0.0288 0.1708  194 PRO C CG  
5422  C CD  . PRO C 194 ? 1.1591 1.4186 0.4302 0.0690  -0.0493 0.1284  194 PRO C CD  
5423  N N   . THR C 195 ? 1.0597 1.2302 0.4418 0.0722  -0.0159 0.1388  195 THR C N   
5424  C CA  . THR C 195 ? 1.0273 1.1565 0.4447 0.0722  0.0013  0.1329  195 THR C CA  
5425  C C   . THR C 195 ? 1.0186 1.1191 0.4285 0.0592  -0.0070 0.0932  195 THR C C   
5426  O O   . THR C 195 ? 1.0439 1.1447 0.4206 0.0574  -0.0076 0.0735  195 THR C O   
5427  C CB  . THR C 195 ? 1.0379 1.1601 0.4571 0.0846  0.0288  0.1493  195 THR C CB  
5428  O OG1 . THR C 195 ? 1.0602 1.2127 0.4725 0.0977  0.0353  0.1861  195 THR C OG1 
5429  C CG2 . THR C 195 ? 1.0041 1.0910 0.4677 0.0849  0.0467  0.1502  195 THR C CG2 
5430  N N   . THR C 196 ? 0.9857 1.0613 0.4257 0.0509  -0.0126 0.0821  196 THR C N   
5431  C CA  . THR C 196 ? 0.9789 1.0259 0.4134 0.0392  -0.0220 0.0473  196 THR C CA  
5432  C C   . THR C 196 ? 0.9452 0.9566 0.4157 0.0388  -0.0110 0.0411  196 THR C C   
5433  O O   . THR C 196 ? 0.9240 0.9329 0.4264 0.0442  0.0004  0.0615  196 THR C O   
5434  C CB  . THR C 196 ? 0.9802 1.0348 0.4069 0.0251  -0.0466 0.0345  196 THR C CB  
5435  O OG1 . THR C 196 ? 0.9537 1.0147 0.4136 0.0243  -0.0499 0.0537  196 THR C OG1 
5436  C CG2 . THR C 196 ? 1.0172 1.1088 0.4052 0.0227  -0.0601 0.0343  196 THR C CG2 
5437  N N   . TYR C 197 ? 0.9436 0.9278 0.4080 0.0328  -0.0146 0.0124  197 TYR C N   
5438  C CA  . TYR C 197 ? 0.9153 0.8682 0.4098 0.0325  -0.0067 0.0035  197 TYR C CA  
5439  C C   . TYR C 197 ? 0.9148 0.8416 0.4017 0.0226  -0.0210 -0.0248 197 TYR C C   
5440  O O   . TYR C 197 ? 0.9395 0.8686 0.3964 0.0161  -0.0340 -0.0407 197 TYR C O   
5441  C CB  . TYR C 197 ? 0.9178 0.8644 0.4174 0.0423  0.0139  0.0025  197 TYR C CB  
5442  C CG  . TYR C 197 ? 0.9455 0.8883 0.4130 0.0438  0.0134  -0.0202 197 TYR C CG  
5443  C CD1 . TYR C 197 ? 0.9785 0.9455 0.4128 0.0482  0.0163  -0.0155 197 TYR C CD1 
5444  C CD2 . TYR C 197 ? 0.9418 0.8571 0.4112 0.0419  0.0106  -0.0462 197 TYR C CD2 
5445  C CE1 . TYR C 197 ? 1.0071 0.9701 0.4109 0.0499  0.0172  -0.0382 197 TYR C CE1 
5446  C CE2 . TYR C 197 ? 0.9701 0.8800 0.4113 0.0449  0.0117  -0.0677 197 TYR C CE2 
5447  C CZ  . TYR C 197 ? 1.0027 0.9361 0.4111 0.0484  0.0155  -0.0646 197 TYR C CZ  
5448  O OH  . TYR C 197 ? 1.0336 0.9613 0.4130 0.0515  0.0179  -0.0876 197 TYR C OH  
5449  N N   . ILE C 198 ? 0.8895 0.7910 0.4032 0.0215  -0.0180 -0.0310 198 ILE C N   
5450  C CA  . ILE C 198 ? 0.8903 0.7625 0.3991 0.0154  -0.0278 -0.0558 198 ILE C CA  
5451  C C   . ILE C 198 ? 0.8735 0.7265 0.4048 0.0225  -0.0156 -0.0622 198 ILE C C   
5452  O O   . ILE C 198 ? 0.8471 0.6972 0.4085 0.0230  -0.0096 -0.0515 198 ILE C O   
5453  C CB  . ILE C 198 ? 0.8767 0.7394 0.3952 0.0036  -0.0425 -0.0562 198 ILE C CB  
5454  C CG1 . ILE C 198 ? 0.8875 0.7779 0.3938 -0.0034 -0.0536 -0.0449 198 ILE C CG1 
5455  C CG2 . ILE C 198 ? 0.8873 0.7184 0.3938 -0.0027 -0.0526 -0.0808 198 ILE C CG2 
5456  C CD1 . ILE C 198 ? 0.8784 0.7628 0.3928 -0.0166 -0.0681 -0.0471 198 ILE C CD1 
5457  N N   . SER C 199 ? 0.8906 0.7321 0.4079 0.0281  -0.0119 -0.0805 199 SER C N   
5458  C CA  . SER C 199 ? 0.8771 0.7045 0.4161 0.0355  -0.0021 -0.0884 199 SER C CA  
5459  C C   . SER C 199 ? 0.8808 0.6784 0.4156 0.0330  -0.0140 -0.1084 199 SER C C   
5460  O O   . SER C 199 ? 0.9074 0.6926 0.4149 0.0309  -0.0224 -0.1241 199 SER C O   
5461  C CB  . SER C 199 ? 0.8931 0.7316 0.4251 0.0461  0.0133  -0.0925 199 SER C CB  
5462  O OG  . SER C 199 ? 0.9267 0.7625 0.4232 0.0471  0.0083  -0.1083 199 SER C OG  
5463  N N   . VAL C 200 ? 0.8571 0.6428 0.4184 0.0331  -0.0143 -0.1076 200 VAL C N   
5464  C CA  . VAL C 200 ? 0.8607 0.6180 0.4202 0.0324  -0.0248 -0.1226 200 VAL C CA  
5465  C C   . VAL C 200 ? 0.8498 0.6039 0.4316 0.0430  -0.0167 -0.1288 200 VAL C C   
5466  O O   . VAL C 200 ? 0.8259 0.5940 0.4352 0.0440  -0.0079 -0.1189 200 VAL C O   
5467  C CB  . VAL C 200 ? 0.8446 0.5919 0.4128 0.0214  -0.0358 -0.1154 200 VAL C CB  
5468  C CG1 . VAL C 200 ? 0.8594 0.5751 0.4153 0.0191  -0.0478 -0.1299 200 VAL C CG1 
5469  C CG2 . VAL C 200 ? 0.8468 0.6098 0.4050 0.0113  -0.0410 -0.1035 200 VAL C CG2 
5470  N N   . GLY C 201 ? 0.8697 0.6061 0.4409 0.0510  -0.0194 -0.1457 201 GLY C N   
5471  C CA  . GLY C 201 ? 0.8628 0.6004 0.4551 0.0629  -0.0128 -0.1526 201 GLY C CA  
5472  C C   . GLY C 201 ? 0.8732 0.5829 0.4622 0.0676  -0.0241 -0.1640 201 GLY C C   
5473  O O   . GLY C 201 ? 0.8985 0.5834 0.4622 0.0653  -0.0329 -0.1725 201 GLY C O   
5474  N N   . THR C 202 ? 0.8559 0.5697 0.4706 0.0735  -0.0237 -0.1636 202 THR C N   
5475  C CA  . THR C 202 ? 0.8681 0.5605 0.4827 0.0830  -0.0323 -0.1731 202 THR C CA  
5476  C C   . THR C 202 ? 0.8569 0.5717 0.4998 0.0960  -0.0241 -0.1771 202 THR C C   
5477  O O   . THR C 202 ? 0.8487 0.5897 0.5052 0.0973  -0.0108 -0.1753 202 THR C O   
5478  C CB  . THR C 202 ? 0.8585 0.5343 0.4744 0.0747  -0.0449 -0.1664 202 THR C CB  
5479  O OG1 . THR C 202 ? 0.8284 0.5261 0.4729 0.0722  -0.0421 -0.1587 202 THR C OG1 
5480  C CG2 . THR C 202 ? 0.8624 0.5263 0.4586 0.0588  -0.0508 -0.1598 202 THR C CG2 
5481  N N   . SER C 203 ? 0.8591 0.5654 0.5115 0.1057  -0.0318 -0.1817 203 SER C N   
5482  C CA  . SER C 203 ? 0.8450 0.5783 0.5288 0.1162  -0.0265 -0.1849 203 SER C CA  
5483  C C   . SER C 203 ? 0.8117 0.5712 0.5218 0.1042  -0.0218 -0.1760 203 SER C C   
5484  O O   . SER C 203 ? 0.7989 0.5877 0.5358 0.1067  -0.0109 -0.1777 203 SER C O   
5485  C CB  . SER C 203 ? 0.8560 0.5766 0.5433 0.1291  -0.0383 -0.1895 203 SER C CB  
5486  O OG  . SER C 203 ? 0.8514 0.5534 0.5296 0.1198  -0.0508 -0.1818 203 SER C OG  
5487  N N   . THR C 204 ? 0.8000 0.5482 0.5032 0.0906  -0.0286 -0.1670 204 THR C N   
5488  C CA  . THR C 204 ? 0.7724 0.5399 0.4988 0.0790  -0.0238 -0.1593 204 THR C CA  
5489  C C   . THR C 204 ? 0.7650 0.5354 0.4856 0.0671  -0.0148 -0.1485 204 THR C C   
5490  O O   . THR C 204 ? 0.7499 0.5412 0.4924 0.0621  -0.0022 -0.1434 204 THR C O   
5491  C CB  . THR C 204 ? 0.7647 0.5210 0.4909 0.0733  -0.0365 -0.1564 204 THR C CB  
5492  O OG1 . THR C 204 ? 0.7757 0.5040 0.4738 0.0667  -0.0449 -0.1509 204 THR C OG1 
5493  C CG2 . THR C 204 ? 0.7733 0.5303 0.5057 0.0863  -0.0461 -0.1645 204 THR C CG2 
5494  N N   . LEU C 205 ? 0.7777 0.5281 0.4702 0.0625  -0.0210 -0.1447 205 LEU C N   
5495  C CA  . LEU C 205 ? 0.7716 0.5269 0.4583 0.0518  -0.0155 -0.1327 205 LEU C CA  
5496  C C   . LEU C 205 ? 0.7785 0.5514 0.4643 0.0555  -0.0014 -0.1304 205 LEU C C   
5497  O O   . LEU C 205 ? 0.7991 0.5696 0.4705 0.0644  0.0000  -0.1396 205 LEU C O   
5498  C CB  . LEU C 205 ? 0.7850 0.5183 0.4433 0.0449  -0.0274 -0.1305 205 LEU C CB  
5499  C CG  . LEU C 205 ? 0.7767 0.5170 0.4317 0.0334  -0.0257 -0.1165 205 LEU C CG  
5500  C CD1 . LEU C 205 ? 0.7514 0.5016 0.4324 0.0272  -0.0208 -0.1070 205 LEU C CD1 
5501  C CD2 . LEU C 205 ? 0.7915 0.5124 0.4212 0.0256  -0.0388 -0.1169 205 LEU C CD2 
5502  N N   . ASN C 206 ? 0.7644 0.5538 0.4654 0.0493  0.0101  -0.1177 206 ASN C N   
5503  C CA  . ASN C 206 ? 0.7721 0.5783 0.4705 0.0517  0.0246  -0.1107 206 ASN C CA  
5504  C C   . ASN C 206 ? 0.7665 0.5776 0.4623 0.0434  0.0281  -0.0926 206 ASN C C   
5505  O O   . ASN C 206 ? 0.7536 0.5761 0.4726 0.0403  0.0409  -0.0813 206 ASN C O   
5506  C CB  . ASN C 206 ? 0.7639 0.5897 0.4921 0.0558  0.0407  -0.1125 206 ASN C CB  
5507  C CG  . ASN C 206 ? 0.7765 0.6188 0.5002 0.0591  0.0575  -0.1047 206 ASN C CG  
5508  O OD1 . ASN C 206 ? 0.7958 0.6359 0.4897 0.0617  0.0554  -0.1031 206 ASN C OD1 
5509  N ND2 . ASN C 206 ? 0.7682 0.6277 0.5208 0.0581  0.0747  -0.1003 206 ASN C ND2 
5510  N N   . GLN C 207 ? 0.7785 0.5813 0.4470 0.0401  0.0170  -0.0901 207 GLN C N   
5511  C CA  . GLN C 207 ? 0.7740 0.5828 0.4398 0.0330  0.0162  -0.0731 207 GLN C CA  
5512  C C   . GLN C 207 ? 0.7939 0.6172 0.4371 0.0354  0.0202  -0.0647 207 GLN C C   
5513  O O   . GLN C 207 ? 0.8151 0.6365 0.4341 0.0393  0.0168  -0.0760 207 GLN C O   
5514  C CB  . GLN C 207 ? 0.7722 0.5646 0.4269 0.0253  -0.0009 -0.0762 207 GLN C CB  
5515  C CG  . GLN C 207 ? 0.7693 0.5702 0.4208 0.0182  -0.0043 -0.0602 207 GLN C CG  
5516  C CD  . GLN C 207 ? 0.7664 0.5523 0.4118 0.0094  -0.0194 -0.0639 207 GLN C CD  
5517  O OE1 . GLN C 207 ? 0.7815 0.5654 0.4049 0.0040  -0.0305 -0.0660 207 GLN C OE1 
5518  N NE2 . GLN C 207 ? 0.7492 0.5253 0.4136 0.0070  -0.0194 -0.0655 207 GLN C NE2 
5519  N N   . ARG C 208 ? 0.7897 0.6276 0.4406 0.0337  0.0280  -0.0446 208 ARG C N   
5520  C CA  . ARG C 208 ? 0.8098 0.6647 0.4374 0.0357  0.0290  -0.0329 208 ARG C CA  
5521  C C   . ARG C 208 ? 0.8022 0.6672 0.4376 0.0319  0.0273  -0.0118 208 ARG C C   
5522  O O   . ARG C 208 ? 0.7909 0.6606 0.4514 0.0339  0.0410  0.0038  208 ARG C O   
5523  C CB  . ARG C 208 ? 0.8219 0.6915 0.4504 0.0438  0.0477  -0.0263 208 ARG C CB  
5524  C CG  . ARG C 208 ? 0.8510 0.7367 0.4446 0.0472  0.0462  -0.0221 208 ARG C CG  
5525  C CD  . ARG C 208 ? 0.8633 0.7669 0.4594 0.0546  0.0671  -0.0061 208 ARG C CD  
5526  N NE  . ARG C 208 ? 0.8948 0.8155 0.4533 0.0584  0.0654  -0.0039 208 ARG C NE  
5527  C CZ  . ARG C 208 ? 0.9165 0.8364 0.4496 0.0615  0.0643  -0.0231 208 ARG C CZ  
5528  N NH1 . ARG C 208 ? 0.9096 0.8125 0.4525 0.0628  0.0647  -0.0449 208 ARG C NH1 
5529  N NH2 . ARG C 208 ? 0.9478 0.8850 0.4448 0.0641  0.0630  -0.0208 208 ARG C NH2 
5530  N N   . LEU C 209 ? 0.8105 0.6790 0.4259 0.0264  0.0110  -0.0122 209 LEU C N   
5531  C CA  . LEU C 209 ? 0.8035 0.6843 0.4274 0.0231  0.0068  0.0062  209 LEU C CA  
5532  C C   . LEU C 209 ? 0.8248 0.7328 0.4295 0.0276  0.0073  0.0227  209 LEU C C   
5533  O O   . LEU C 209 ? 0.8475 0.7627 0.4220 0.0277  0.0009  0.0131  209 LEU C O   
5534  C CB  . LEU C 209 ? 0.7992 0.6704 0.4166 0.0126  -0.0118 -0.0041 209 LEU C CB  
5535  C CG  . LEU C 209 ? 0.7839 0.6281 0.4133 0.0081  -0.0154 -0.0205 209 LEU C CG  
5536  C CD1 . LEU C 209 ? 0.7871 0.6220 0.4047 -0.0027 -0.0330 -0.0292 209 LEU C CD1 
5537  C CD2 . LEU C 209 ? 0.7604 0.6005 0.4235 0.0097  -0.0032 -0.0111 209 LEU C CD2 
5538  N N   . VAL C 210 ? 0.8203 0.7434 0.4419 0.0319  0.0151  0.0475  210 VAL C N   
5539  C CA  . VAL C 210 ? 0.8413 0.7941 0.4462 0.0375  0.0136  0.0675  210 VAL C CA  
5540  C C   . VAL C 210 ? 0.8329 0.8002 0.4510 0.0351  0.0042  0.0830  210 VAL C C   
5541  O O   . VAL C 210 ? 0.8116 0.7668 0.4599 0.0345  0.0103  0.0886  210 VAL C O   
5542  C CB  . VAL C 210 ? 0.8519 0.8132 0.4634 0.0492  0.0355  0.0885  210 VAL C CB  
5543  C CG1 . VAL C 210 ? 0.8589 0.8082 0.4620 0.0510  0.0463  0.0726  210 VAL C CG1 
5544  C CG2 . VAL C 210 ? 0.8341 0.7864 0.4841 0.0531  0.0513  0.1068  210 VAL C CG2 
5545  N N   . PRO C 211 ? 0.8511 0.8462 0.4472 0.0335  -0.0107 0.0886  211 PRO C N   
5546  C CA  . PRO C 211 ? 0.8439 0.8587 0.4552 0.0321  -0.0197 0.1042  211 PRO C CA  
5547  C C   . PRO C 211 ? 0.8416 0.8680 0.4781 0.0458  -0.0035 0.1360  211 PRO C C   
5548  O O   . PRO C 211 ? 0.8610 0.9015 0.4875 0.0569  0.0066  0.1538  211 PRO C O   
5549  C CB  . PRO C 211 ? 0.8686 0.9157 0.4484 0.0278  -0.0388 0.1024  211 PRO C CB  
5550  C CG  . PRO C 211 ? 0.8850 0.9180 0.4332 0.0222  -0.0428 0.0766  211 PRO C CG  
5551  C CD  . PRO C 211 ? 0.8792 0.8891 0.4359 0.0310  -0.0217 0.0768  211 PRO C CD  
5552  N N   . ARG C 212 ? 0.8209 0.8393 0.4894 0.0452  0.0001  0.1427  212 ARG C N   
5553  C CA  . ARG C 212 ? 0.8207 0.8476 0.5162 0.0583  0.0150  0.1722  212 ARG C CA  
5554  C C   . ARG C 212 ? 0.8279 0.8925 0.5249 0.0614  0.0009  0.1897  212 ARG C C   
5555  O O   . ARG C 212 ? 0.8151 0.8847 0.5193 0.0513  -0.0129 0.1793  212 ARG C O   
5556  C CB  . ARG C 212 ? 0.7967 0.7933 0.5272 0.0564  0.0287  0.1680  212 ARG C CB  
5557  C CG  . ARG C 212 ? 0.7873 0.7506 0.5189 0.0508  0.0388  0.1467  212 ARG C CG  
5558  C CD  . ARG C 212 ? 0.7693 0.7070 0.5356 0.0503  0.0548  0.1455  212 ARG C CD  
5559  N NE  . ARG C 212 ? 0.7528 0.6884 0.5319 0.0430  0.0449  0.1383  212 ARG C NE  
5560  C CZ  . ARG C 212 ? 0.7406 0.6639 0.5110 0.0305  0.0315  0.1142  212 ARG C CZ  
5561  N NH1 . ARG C 212 ? 0.7424 0.6535 0.4921 0.0248  0.0254  0.0941  212 ARG C NH1 
5562  N NH2 . ARG C 212 ? 0.7285 0.6515 0.5113 0.0245  0.0250  0.1110  212 ARG C NH2 
5563  N N   . ILE C 213 ? 0.8504 0.9431 0.5409 0.0755  0.0047  0.2170  213 ILE C N   
5564  C CA  . ILE C 213 ? 0.8605 0.9959 0.5531 0.0810  -0.0091 0.2366  213 ILE C CA  
5565  C C   . ILE C 213 ? 0.8530 0.9885 0.5853 0.0945  0.0055  0.2628  213 ILE C C   
5566  O O   . ILE C 213 ? 0.8568 0.9708 0.6049 0.1062  0.0286  0.2786  213 ILE C O   
5567  C CB  . ILE C 213 ? 0.8932 1.0648 0.5536 0.0901  -0.0156 0.2531  213 ILE C CB  
5568  C CG1 . ILE C 213 ? 0.9039 1.0769 0.5242 0.0756  -0.0314 0.2237  213 ILE C CG1 
5569  C CG2 . ILE C 213 ? 0.9045 1.1253 0.5708 0.0983  -0.0296 0.2767  213 ILE C CG2 
5570  C CD1 . ILE C 213 ? 0.9387 1.1391 0.5222 0.0837  -0.0335 0.2346  213 ILE C CD1 
5571  N N   . ALA C 214 ? 0.8442 1.0031 0.5938 0.0921  -0.0069 0.2662  214 ALA C N   
5572  C CA  . ALA C 214 ? 0.8398 1.0037 0.6276 0.1060  0.0054  0.2907  214 ALA C CA  
5573  C C   . ALA C 214 ? 0.8377 1.0457 0.6358 0.1041  -0.0141 0.2966  214 ALA C C   
5574  O O   . ALA C 214 ? 0.8317 1.0534 0.6140 0.0865  -0.0351 0.2744  214 ALA C O   
5575  C CB  . ALA C 214 ? 0.8167 0.9352 0.6322 0.1010  0.0229  0.2769  214 ALA C CB  
5576  N N   . THR C 215 ? 0.8452 1.0754 0.6713 0.1225  -0.0064 0.3269  215 THR C N   
5577  C CA  . THR C 215 ? 0.8415 1.1160 0.6860 0.1228  -0.0221 0.3348  215 THR C CA  
5578  C C   . THR C 215 ? 0.8149 1.0644 0.6903 0.1136  -0.0147 0.3192  215 THR C C   
5579  O O   . THR C 215 ? 0.8091 1.0267 0.7104 0.1237  0.0083  0.3269  215 THR C O   
5580  C CB  . THR C 215 ? 0.8621 1.1733 0.7259 0.1493  -0.0164 0.3759  215 THR C CB  
5581  O OG1 . THR C 215 ? 0.8903 1.2124 0.7250 0.1609  -0.0155 0.3937  215 THR C OG1 
5582  C CG2 . THR C 215 ? 0.8622 1.2332 0.7385 0.1484  -0.0387 0.3831  215 THR C CG2 
5583  N N   . ARG C 216 ? 0.8018 1.0647 0.6734 0.0936  -0.0335 0.2967  216 ARG C N   
5584  C CA  . ARG C 216 ? 0.7785 1.0154 0.6721 0.0818  -0.0273 0.2784  216 ARG C CA  
5585  C C   . ARG C 216 ? 0.7733 1.0532 0.6893 0.0770  -0.0406 0.2820  216 ARG C C   
5586  O O   . ARG C 216 ? 0.7846 1.1130 0.6916 0.0745  -0.0609 0.2881  216 ARG C O   
5587  C CB  . ARG C 216 ? 0.7674 0.9679 0.6343 0.0593  -0.0339 0.2439  216 ARG C CB  
5588  C CG  . ARG C 216 ? 0.7709 0.9301 0.6192 0.0627  -0.0204 0.2375  216 ARG C CG  
5589  C CD  . ARG C 216 ? 0.7645 0.8962 0.5842 0.0426  -0.0305 0.2052  216 ARG C CD  
5590  N NE  . ARG C 216 ? 0.7820 0.9361 0.5672 0.0361  -0.0492 0.1988  216 ARG C NE  
5591  C CZ  . ARG C 216 ? 0.7965 0.9421 0.5554 0.0408  -0.0465 0.1980  216 ARG C CZ  
5592  N NH1 . ARG C 216 ? 0.7951 0.9110 0.5596 0.0516  -0.0258 0.2042  216 ARG C NH1 
5593  N NH2 . ARG C 216 ? 0.8145 0.9825 0.5414 0.0339  -0.0641 0.1899  216 ARG C NH2 
5594  N N   . SER C 217 ? 0.7579 1.0215 0.7033 0.0753  -0.0285 0.2775  217 SER C N   
5595  C CA  . SER C 217 ? 0.7514 1.0527 0.7216 0.0692  -0.0379 0.2787  217 SER C CA  
5596  C C   . SER C 217 ? 0.7481 1.0567 0.6959 0.0412  -0.0601 0.2517  217 SER C C   
5597  O O   . SER C 217 ? 0.7445 1.0134 0.6649 0.0266  -0.0618 0.2282  217 SER C O   
5598  C CB  . SER C 217 ? 0.7367 1.0127 0.7401 0.0733  -0.0168 0.2775  217 SER C CB  
5599  O OG  . SER C 217 ? 0.7438 0.9992 0.7648 0.0968  0.0067  0.2974  217 SER C OG  
5600  N N   . LYS C 218 ? 0.7524 1.1124 0.7132 0.0340  -0.0767 0.2554  218 LYS C N   
5601  C CA  . LYS C 218 ? 0.7531 1.1212 0.6970 0.0057  -0.0966 0.2303  218 LYS C CA  
5602  C C   . LYS C 218 ? 0.7348 1.0651 0.6881 -0.0094 -0.0868 0.2110  218 LYS C C   
5603  O O   . LYS C 218 ? 0.7246 1.0626 0.7113 -0.0035 -0.0746 0.2197  218 LYS C O   
5604  C CB  . LYS C 218 ? 0.7642 1.2014 0.7239 0.0006  -0.1163 0.2394  218 LYS C CB  
5605  C CG  . LYS C 218 ? 0.7890 1.2614 0.7195 -0.0015 -0.1377 0.2407  218 LYS C CG  
5606  C CD  . LYS C 218 ? 0.8026 1.3514 0.7568 0.0070  -0.1520 0.2626  218 LYS C CD  
5607  C CE  . LYS C 218 ? 0.8318 1.4179 0.7535 0.0055  -0.1736 0.2639  218 LYS C CE  
5608  N NZ  . LYS C 218 ? 0.8477 1.4850 0.7845 0.0342  -0.1745 0.2999  218 LYS C NZ  
5609  N N   . VAL C 219 ? 0.7330 1.0221 0.6557 -0.0277 -0.0914 0.1854  219 VAL C N   
5610  C CA  . VAL C 219 ? 0.7211 0.9771 0.6453 -0.0453 -0.0865 0.1659  219 VAL C CA  
5611  C C   . VAL C 219 ? 0.7316 0.9962 0.6341 -0.0715 -0.1076 0.1459  219 VAL C C   
5612  O O   . VAL C 219 ? 0.7447 1.0018 0.6157 -0.0768 -0.1194 0.1357  219 VAL C O   
5613  C CB  . VAL C 219 ? 0.7138 0.9085 0.6216 -0.0418 -0.0714 0.1541  219 VAL C CB  
5614  C CG1 . VAL C 219 ? 0.7072 0.8679 0.6094 -0.0606 -0.0692 0.1335  219 VAL C CG1 
5615  C CG2 . VAL C 219 ? 0.7061 0.8915 0.6378 -0.0182 -0.0493 0.1721  219 VAL C CG2 
5616  N N   . ASN C 220 ? 0.7284 1.0091 0.6482 -0.0882 -0.1114 0.1403  220 ASN C N   
5617  C CA  . ASN C 220 ? 0.7425 1.0366 0.6477 -0.1150 -0.1308 0.1228  220 ASN C CA  
5618  C C   . ASN C 220 ? 0.7593 1.1002 0.6534 -0.1157 -0.1508 0.1264  220 ASN C C   
5619  O O   . ASN C 220 ? 0.7768 1.1098 0.6416 -0.1334 -0.1656 0.1073  220 ASN C O   
5620  C CB  . ASN C 220 ? 0.7493 0.9839 0.6203 -0.1309 -0.1313 0.0979  220 ASN C CB  
5621  C CG  . ASN C 220 ? 0.7396 0.9395 0.6199 -0.1394 -0.1180 0.0911  220 ASN C CG  
5622  O OD1 . ASN C 220 ? 0.7249 0.9326 0.6334 -0.1283 -0.1033 0.1041  220 ASN C OD1 
5623  N ND2 . ASN C 220 ? 0.7510 0.9113 0.6064 -0.1585 -0.1224 0.0707  220 ASN C ND2 
5624  N N   . GLY C 221 ? 0.7565 1.1457 0.6735 -0.0957 -0.1506 0.1510  221 GLY C N   
5625  C CA  . GLY C 221 ? 0.7744 1.2168 0.6829 -0.0939 -0.1700 0.1581  221 GLY C CA  
5626  C C   . GLY C 221 ? 0.7884 1.2123 0.6583 -0.0847 -0.1737 0.1556  221 GLY C C   
5627  O O   . GLY C 221 ? 0.8080 1.2709 0.6614 -0.0873 -0.1914 0.1559  221 GLY C O   
5628  N N   . GLN C 222 ? 0.7798 1.1471 0.6356 -0.0742 -0.1570 0.1527  222 GLN C N   
5629  C CA  . GLN C 222 ? 0.7926 1.1386 0.6131 -0.0654 -0.1573 0.1497  222 GLN C CA  
5630  C C   . GLN C 222 ? 0.7789 1.0966 0.6082 -0.0399 -0.1350 0.1675  222 GLN C C   
5631  O O   . GLN C 222 ? 0.7608 1.0440 0.6077 -0.0373 -0.1184 0.1663  222 GLN C O   
5632  C CB  . GLN C 222 ? 0.8020 1.0997 0.5884 -0.0855 -0.1619 0.1186  222 GLN C CB  
5633  C CG  . GLN C 222 ? 0.8221 1.1397 0.5957 -0.1128 -0.1828 0.0977  222 GLN C CG  
5634  C CD  . GLN C 222 ? 0.8479 1.2208 0.6076 -0.1128 -0.2016 0.1023  222 GLN C CD  
5635  O OE1 . GLN C 222 ? 0.8594 1.2370 0.5989 -0.0965 -0.2005 0.1113  222 GLN C OE1 
5636  N NE2 . GLN C 222 ? 0.8581 1.2749 0.6282 -0.1319 -0.2189 0.0958  222 GLN C NE2 
5637  N N   . SER C 223 ? 0.7901 1.1232 0.6063 -0.0222 -0.1343 0.1836  223 SER C N   
5638  C CA  . SER C 223 ? 0.7829 1.0883 0.6054 0.0007  -0.1125 0.2007  223 SER C CA  
5639  C C   . SER C 223 ? 0.7871 1.0468 0.5755 -0.0011 -0.1071 0.1845  223 SER C C   
5640  O O   . SER C 223 ? 0.7818 1.0117 0.5742 0.0135  -0.0881 0.1933  223 SER C O   
5641  C CB  . SER C 223 ? 0.7962 1.1464 0.6298 0.0242  -0.1114 0.2337  223 SER C CB  
5642  O OG  . SER C 223 ? 0.7874 1.1697 0.6613 0.0328  -0.1082 0.2524  223 SER C OG  
5643  N N   . GLY C 224 ? 0.7980 1.0524 0.5546 -0.0195 -0.1229 0.1602  224 GLY C N   
5644  C CA  . GLY C 224 ? 0.8020 1.0122 0.5280 -0.0229 -0.1182 0.1411  224 GLY C CA  
5645  C C   . GLY C 224 ? 0.7815 0.9407 0.5156 -0.0313 -0.1077 0.1238  224 GLY C C   
5646  O O   . GLY C 224 ? 0.7692 0.9275 0.5228 -0.0416 -0.1094 0.1193  224 GLY C O   
5647  N N   . ARG C 225 ? 0.7790 0.8983 0.4980 -0.0267 -0.0968 0.1143  225 ARG C N   
5648  C CA  . ARG C 225 ? 0.7614 0.8341 0.4869 -0.0320 -0.0866 0.0992  225 ARG C CA  
5649  C C   . ARG C 225 ? 0.7704 0.8094 0.4649 -0.0414 -0.0915 0.0737  225 ARG C C   
5650  O O   . ARG C 225 ? 0.7873 0.8301 0.4574 -0.0376 -0.0944 0.0703  225 ARG C O   
5651  C CB  . ARG C 225 ? 0.7471 0.8021 0.4942 -0.0151 -0.0646 0.1135  225 ARG C CB  
5652  C CG  . ARG C 225 ? 0.7379 0.8165 0.5194 -0.0046 -0.0559 0.1370  225 ARG C CG  
5653  C CD  . ARG C 225 ? 0.7227 0.7944 0.5242 -0.0153 -0.0561 0.1295  225 ARG C CD  
5654  N NE  . ARG C 225 ? 0.7154 0.8096 0.5513 -0.0039 -0.0461 0.1510  225 ARG C NE  
5655  C CZ  . ARG C 225 ? 0.7200 0.8593 0.5699 -0.0024 -0.0554 0.1657  225 ARG C CZ  
5656  N NH1 . ARG C 225 ? 0.7325 0.9015 0.5641 -0.0136 -0.0761 0.1603  225 ARG C NH1 
5657  N NH2 . ARG C 225 ? 0.7138 0.8698 0.5973 0.0105  -0.0435 0.1852  225 ARG C NH2 
5658  N N   . MET C 226 ? 0.7612 0.7678 0.4566 -0.0529 -0.0919 0.0567  226 MET C N   
5659  C CA  . MET C 226 ? 0.7694 0.7394 0.4398 -0.0594 -0.0946 0.0338  226 MET C CA  
5660  C C   . MET C 226 ? 0.7507 0.6856 0.4337 -0.0537 -0.0805 0.0303  226 MET C C   
5661  O O   . MET C 226 ? 0.7370 0.6645 0.4387 -0.0578 -0.0767 0.0322  226 MET C O   
5662  C CB  . MET C 226 ? 0.7827 0.7447 0.4394 -0.0793 -0.1097 0.0160  226 MET C CB  
5663  C CG  . MET C 226 ? 0.8068 0.7989 0.4447 -0.0884 -0.1255 0.0117  226 MET C CG  
5664  S SD  . MET C 226 ? 0.8341 0.8096 0.4324 -0.0867 -0.1295 -0.0071 226 MET C SD  
5665  C CE  . MET C 226 ? 0.8631 0.8787 0.4435 -0.1022 -0.1497 -0.0135 226 MET C CE  
5666  N N   . GLU C 227 ? 0.7516 0.6675 0.4244 -0.0448 -0.0726 0.0245  227 GLU C N   
5667  C CA  . GLU C 227 ? 0.7359 0.6225 0.4203 -0.0398 -0.0604 0.0193  227 GLU C CA  
5668  C C   . GLU C 227 ? 0.7449 0.6005 0.4076 -0.0454 -0.0667 -0.0026 227 GLU C C   
5669  O O   . GLU C 227 ? 0.7604 0.6134 0.4022 -0.0428 -0.0698 -0.0112 227 GLU C O   
5670  C CB  . GLU C 227 ? 0.7306 0.6216 0.4259 -0.0249 -0.0447 0.0308  227 GLU C CB  
5671  C CG  . GLU C 227 ? 0.7139 0.5826 0.4291 -0.0208 -0.0306 0.0281  227 GLU C CG  
5672  C CD  . GLU C 227 ? 0.7107 0.5848 0.4418 -0.0083 -0.0132 0.0414  227 GLU C CD  
5673  O OE1 . GLU C 227 ? 0.7220 0.6162 0.4465 -0.0013 -0.0115 0.0544  227 GLU C OE1 
5674  O OE2 . GLU C 227 ? 0.6992 0.5575 0.4492 -0.0060 -0.0007 0.0389  227 GLU C OE2 
5675  N N   . PHE C 228 ? 0.7374 0.5700 0.4046 -0.0521 -0.0679 -0.0111 228 PHE C N   
5676  C CA  . PHE C 228 ? 0.7499 0.5519 0.3968 -0.0572 -0.0750 -0.0298 228 PHE C CA  
5677  C C   . PHE C 228 ? 0.7401 0.5204 0.3927 -0.0483 -0.0663 -0.0365 228 PHE C C   
5678  O O   . PHE C 228 ? 0.7224 0.5027 0.3954 -0.0452 -0.0572 -0.0304 228 PHE C O   
5679  C CB  . PHE C 228 ? 0.7559 0.5470 0.3994 -0.0717 -0.0842 -0.0342 228 PHE C CB  
5680  C CG  . PHE C 228 ? 0.7704 0.5818 0.4056 -0.0833 -0.0952 -0.0329 228 PHE C CG  
5681  C CD1 . PHE C 228 ? 0.7962 0.5978 0.4056 -0.0901 -0.1054 -0.0473 228 PHE C CD1 
5682  C CD2 . PHE C 228 ? 0.7601 0.6025 0.4144 -0.0872 -0.0953 -0.0182 228 PHE C CD2 
5683  C CE1 . PHE C 228 ? 0.8120 0.6349 0.4139 -0.1027 -0.1164 -0.0485 228 PHE C CE1 
5684  C CE2 . PHE C 228 ? 0.7739 0.6408 0.4227 -0.0985 -0.1068 -0.0175 228 PHE C CE2 
5685  C CZ  . PHE C 228 ? 0.8001 0.6577 0.4222 -0.1073 -0.1178 -0.0334 228 PHE C CZ  
5686  N N   . PHE C 229 ? 0.7538 0.5171 0.3885 -0.0442 -0.0691 -0.0500 229 PHE C N   
5687  C CA  . PHE C 229 ? 0.7475 0.4949 0.3874 -0.0350 -0.0625 -0.0577 229 PHE C CA  
5688  C C   . PHE C 229 ? 0.7643 0.4821 0.3861 -0.0370 -0.0714 -0.0726 229 PHE C C   
5689  O O   . PHE C 229 ? 0.7848 0.4919 0.3871 -0.0447 -0.0809 -0.0789 229 PHE C O   
5690  C CB  . PHE C 229 ? 0.7490 0.5078 0.3887 -0.0241 -0.0542 -0.0579 229 PHE C CB  
5691  C CG  . PHE C 229 ? 0.7357 0.5197 0.3939 -0.0200 -0.0430 -0.0413 229 PHE C CG  
5692  C CD1 . PHE C 229 ? 0.7424 0.5481 0.3950 -0.0225 -0.0459 -0.0298 229 PHE C CD1 
5693  C CD2 . PHE C 229 ? 0.7194 0.5054 0.4009 -0.0137 -0.0294 -0.0368 229 PHE C CD2 
5694  C CE1 . PHE C 229 ? 0.7338 0.5613 0.4033 -0.0165 -0.0350 -0.0117 229 PHE C CE1 
5695  C CE2 . PHE C 229 ? 0.7116 0.5161 0.4107 -0.0095 -0.0172 -0.0205 229 PHE C CE2 
5696  C CZ  . PHE C 229 ? 0.7192 0.5436 0.4120 -0.0098 -0.0198 -0.0067 229 PHE C CZ  
5697  N N   . TRP C 230 ? 0.7576 0.4624 0.3865 -0.0301 -0.0680 -0.0781 230 TRP C N   
5698  C CA  . TRP C 230 ? 0.7748 0.4513 0.3885 -0.0287 -0.0756 -0.0895 230 TRP C CA  
5699  C C   . TRP C 230 ? 0.7719 0.4444 0.3920 -0.0154 -0.0714 -0.0972 230 TRP C C   
5700  O O   . TRP C 230 ? 0.7536 0.4445 0.3930 -0.0098 -0.0620 -0.0942 230 TRP C O   
5701  C CB  . TRP C 230 ? 0.7739 0.4372 0.3882 -0.0375 -0.0802 -0.0856 230 TRP C CB  
5702  C CG  . TRP C 230 ? 0.7509 0.4254 0.3864 -0.0358 -0.0729 -0.0795 230 TRP C CG  
5703  C CD1 . TRP C 230 ? 0.7328 0.4270 0.3860 -0.0406 -0.0659 -0.0689 230 TRP C CD1 
5704  C CD2 . TRP C 230 ? 0.7467 0.4139 0.3878 -0.0288 -0.0718 -0.0845 230 TRP C CD2 
5705  N NE1 . TRP C 230 ? 0.7187 0.4155 0.3874 -0.0380 -0.0594 -0.0687 230 TRP C NE1 
5706  C CE2 . TRP C 230 ? 0.7266 0.4088 0.3878 -0.0314 -0.0637 -0.0785 230 TRP C CE2 
5707  C CE3 . TRP C 230 ? 0.7600 0.4107 0.3916 -0.0198 -0.0771 -0.0936 230 TRP C CE3 
5708  C CZ2 . TRP C 230 ? 0.7199 0.4023 0.3902 -0.0274 -0.0615 -0.0832 230 TRP C CZ2 
5709  C CZ3 . TRP C 230 ? 0.7519 0.4058 0.3938 -0.0145 -0.0759 -0.0961 230 TRP C CZ3 
5710  C CH2 . TRP C 230 ? 0.7322 0.4023 0.3924 -0.0193 -0.0685 -0.0919 230 TRP C CH2 
5711  N N   . THR C 231 ? 0.7925 0.4409 0.3973 -0.0105 -0.0781 -0.1072 231 THR C N   
5712  C CA  . THR C 231 ? 0.7921 0.4374 0.4039 0.0028  -0.0764 -0.1143 231 THR C CA  
5713  C C   . THR C 231 ? 0.8156 0.4305 0.4115 0.0058  -0.0857 -0.1194 231 THR C C   
5714  O O   . THR C 231 ? 0.8358 0.4290 0.4133 -0.0025 -0.0918 -0.1193 231 THR C O   
5715  C CB  . THR C 231 ? 0.7977 0.4525 0.4094 0.0135  -0.0705 -0.1219 231 THR C CB  
5716  O OG1 . THR C 231 ? 0.7917 0.4522 0.4179 0.0259  -0.0676 -0.1276 231 THR C OG1 
5717  C CG2 . THR C 231 ? 0.8293 0.4620 0.4150 0.0147  -0.0760 -0.1313 231 THR C CG2 
5718  N N   . ILE C 232 ? 0.8151 0.4294 0.4189 0.0176  -0.0865 -0.1231 232 ILE C N   
5719  C CA  . ILE C 232 ? 0.8420 0.4281 0.4308 0.0257  -0.0945 -0.1269 232 ILE C CA  
5720  C C   . ILE C 232 ? 0.8568 0.4408 0.4443 0.0412  -0.0924 -0.1374 232 ILE C C   
5721  O O   . ILE C 232 ? 0.8417 0.4494 0.4480 0.0511  -0.0875 -0.1409 232 ILE C O   
5722  C CB  . ILE C 232 ? 0.8353 0.4241 0.4318 0.0295  -0.0986 -0.1225 232 ILE C CB  
5723  C CG1 . ILE C 232 ? 0.8433 0.4140 0.4265 0.0167  -0.1032 -0.1135 232 ILE C CG1 
5724  C CG2 . ILE C 232 ? 0.8566 0.4325 0.4484 0.0471  -0.1042 -0.1274 232 ILE C CG2 
5725  C CD1 . ILE C 232 ? 0.8267 0.4087 0.4141 0.0000  -0.0986 -0.1075 232 ILE C CD1 
5726  N N   . LEU C 233 ? 0.8887 0.4446 0.4547 0.0424  -0.0952 -0.1435 233 LEU C N   
5727  C CA  . LEU C 233 ? 0.9088 0.4584 0.4708 0.0577  -0.0922 -0.1549 233 LEU C CA  
5728  C C   . LEU C 233 ? 0.9324 0.4592 0.4906 0.0733  -0.0979 -0.1563 233 LEU C C   
5729  O O   . LEU C 233 ? 0.9599 0.4516 0.4996 0.0705  -0.1038 -0.1539 233 LEU C O   
5730  C CB  . LEU C 233 ? 0.9346 0.4652 0.4743 0.0506  -0.0912 -0.1630 233 LEU C CB  
5731  C CG  . LEU C 233 ? 0.9582 0.4824 0.4904 0.0648  -0.0857 -0.1770 233 LEU C CG  
5732  C CD1 . LEU C 233 ? 0.9331 0.4965 0.4850 0.0727  -0.0761 -0.1784 233 LEU C CD1 
5733  C CD2 . LEU C 233 ? 0.9874 0.4909 0.4941 0.0539  -0.0862 -0.1862 233 LEU C CD2 
5734  N N   . LYS C 234 ? 1.2024 0.6789 0.5030 0.1684  -0.1888 -0.1988 234 LYS C N   
5735  C CA  . LYS C 234 ? 1.2226 0.7078 0.5179 0.1951  -0.1892 -0.1951 234 LYS C CA  
5736  C C   . LYS C 234 ? 1.2670 0.7071 0.5316 0.2089  -0.1774 -0.1890 234 LYS C C   
5737  O O   . LYS C 234 ? 1.2766 0.6888 0.5308 0.1972  -0.1697 -0.1923 234 LYS C O   
5738  C CB  . LYS C 234 ? 1.1981 0.7423 0.5310 0.2071  -0.1919 -0.2063 234 LYS C CB  
5739  C CG  . LYS C 234 ? 1.1644 0.7542 0.5252 0.1975  -0.2014 -0.2137 234 LYS C CG  
5740  C CD  . LYS C 234 ? 1.1402 0.7904 0.5430 0.2020  -0.2008 -0.2313 234 LYS C CD  
5741  C CE  . LYS C 234 ? 1.1156 0.8140 0.5423 0.1961  -0.2097 -0.2408 234 LYS C CE  
5742  N NZ  . LYS C 234 ? 1.0939 0.8558 0.5650 0.1962  -0.2071 -0.2633 234 LYS C NZ  
5743  N N   . PRO C 235 ? 1.2982 0.7304 0.5464 0.2352  -0.1740 -0.1794 235 PRO C N   
5744  C CA  . PRO C 235 ? 1.3464 0.7289 0.5640 0.2492  -0.1579 -0.1725 235 PRO C CA  
5745  C C   . PRO C 235 ? 1.3476 0.7412 0.5779 0.2584  -0.1511 -0.1798 235 PRO C C   
5746  O O   . PRO C 235 ? 1.3181 0.7663 0.5819 0.2664  -0.1580 -0.1874 235 PRO C O   
5747  C CB  . PRO C 235 ? 1.3762 0.7586 0.5785 0.2814  -0.1545 -0.1581 235 PRO C CB  
5748  C CG  . PRO C 235 ? 1.3455 0.7712 0.5644 0.2790  -0.1705 -0.1577 235 PRO C CG  
5749  C CD  . PRO C 235 ? 1.2938 0.7641 0.5500 0.2557  -0.1825 -0.1741 235 PRO C CD  
5750  N N   . ASN C 236 ? 1.3833 0.7261 0.5881 0.2555  -0.1361 -0.1794 236 ASN C N   
5751  C CA  . ASN C 236 ? 1.3917 0.7362 0.6033 0.2652  -0.1267 -0.1850 236 ASN C CA  
5752  C C   . ASN C 236 ? 1.3529 0.7249 0.5906 0.2439  -0.1322 -0.1980 236 ASN C C   
5753  O O   . ASN C 236 ? 1.3541 0.7351 0.6033 0.2509  -0.1248 -0.2037 236 ASN C O   
5754  C CB  . ASN C 236 ? 1.3971 0.7804 0.6250 0.3008  -0.1259 -0.1801 236 ASN C CB  
5755  C CG  . ASN C 236 ? 1.4455 0.7920 0.6517 0.3242  -0.1064 -0.1735 236 ASN C CG  
5756  O OD1 . ASN C 236 ? 1.4719 0.7710 0.6582 0.3112  -0.0934 -0.1776 236 ASN C OD1 
5757  N ND2 . ASN C 236 ? 1.4627 0.8336 0.6720 0.3604  -0.1036 -0.1631 236 ASN C ND2 
5758  N N   . ASP C 237 ? 1.3228 0.7058 0.5686 0.2197  -0.1427 -0.2011 237 ASP C N   
5759  C CA  . ASP C 237 ? 1.2900 0.6954 0.5578 0.2014  -0.1446 -0.2097 237 ASP C CA  
5760  C C   . ASP C 237 ? 1.3011 0.6710 0.5425 0.1784  -0.1426 -0.2098 237 ASP C C   
5761  O O   . ASP C 237 ? 1.3190 0.6605 0.5359 0.1696  -0.1447 -0.2060 237 ASP C O   
5762  C CB  . ASP C 237 ? 1.2476 0.7010 0.5494 0.1944  -0.1559 -0.2129 237 ASP C CB  
5763  C CG  . ASP C 237 ? 1.2188 0.6951 0.5474 0.1801  -0.1517 -0.2206 237 ASP C CG  
5764  O OD1 . ASP C 237 ? 1.2263 0.6981 0.5583 0.1840  -0.1407 -0.2248 237 ASP C OD1 
5765  O OD2 . ASP C 237 ? 1.1915 0.6881 0.5372 0.1660  -0.1568 -0.2215 237 ASP C OD2 
5766  N N   . ALA C 238 ? 1.2919 0.6668 0.5389 0.1691  -0.1376 -0.2149 238 ALA C N   
5767  C CA  . ALA C 238 ? 1.3045 0.6565 0.5263 0.1502  -0.1360 -0.2163 238 ALA C CA  
5768  C C   . ALA C 238 ? 1.2710 0.6521 0.5102 0.1361  -0.1416 -0.2145 238 ALA C C   
5769  O O   . ALA C 238 ? 1.2436 0.6553 0.5148 0.1408  -0.1392 -0.2149 238 ALA C O   
5770  C CB  . ALA C 238 ? 1.3320 0.6623 0.5369 0.1544  -0.1229 -0.2215 238 ALA C CB  
5771  N N   . ILE C 239 ? 1.2759 0.6484 0.4950 0.1190  -0.1467 -0.2132 239 ILE C N   
5772  C CA  . ILE C 239 ? 1.2518 0.6499 0.4815 0.1086  -0.1495 -0.2087 239 ILE C CA  
5773  C C   . ILE C 239 ? 1.2717 0.6643 0.4786 0.1043  -0.1429 -0.2107 239 ILE C C   
5774  O O   . ILE C 239 ? 1.3033 0.6725 0.4796 0.0975  -0.1425 -0.2177 239 ILE C O   
5775  C CB  . ILE C 239 ? 1.2388 0.6444 0.4670 0.0948  -0.1614 -0.2042 239 ILE C CB  
5776  C CG1 . ILE C 239 ? 1.2129 0.6484 0.4576 0.0893  -0.1616 -0.1966 239 ILE C CG1 
5777  C CG2 . ILE C 239 ? 1.2690 0.6500 0.4632 0.0811  -0.1650 -0.2093 239 ILE C CG2 
5778  C CD1 . ILE C 239 ? 1.1908 0.6404 0.4479 0.0805  -0.1712 -0.1910 239 ILE C CD1 
5779  N N   . ASN C 240 ? 1.2565 0.6708 0.4780 0.1085  -0.1356 -0.2051 240 ASN C N   
5780  C CA  . ASN C 240 ? 1.2762 0.6908 0.4762 0.1093  -0.1279 -0.2047 240 ASN C CA  
5781  C C   . ASN C 240 ? 1.2643 0.7061 0.4636 0.1050  -0.1295 -0.1939 240 ASN C C   
5782  O O   . ASN C 240 ? 1.2397 0.6990 0.4663 0.1101  -0.1233 -0.1844 240 ASN C O   
5783  C CB  . ASN C 240 ? 1.2784 0.6912 0.4924 0.1240  -0.1115 -0.2050 240 ASN C CB  
5784  C CG  . ASN C 240 ? 1.2926 0.6830 0.5071 0.1320  -0.1083 -0.2143 240 ASN C CG  
5785  O OD1 . ASN C 240 ? 1.3216 0.6864 0.5078 0.1285  -0.1108 -0.2211 240 ASN C OD1 
5786  N ND2 . ASN C 240 ? 1.2752 0.6767 0.5229 0.1430  -0.1007 -0.2154 240 ASN C ND2 
5787  N N   . PHE C 241 ? 1.2846 0.7319 0.4528 0.0962  -0.1360 -0.1964 241 PHE C N   
5788  C CA  . PHE C 241 ? 1.2791 0.7587 0.4417 0.0956  -0.1382 -0.1851 241 PHE C CA  
5789  C C   . PHE C 241 ? 1.3032 0.7934 0.4428 0.1056  -0.1283 -0.1823 241 PHE C C   
5790  O O   . PHE C 241 ? 1.3319 0.8080 0.4454 0.1022  -0.1281 -0.1954 241 PHE C O   
5791  C CB  . PHE C 241 ? 1.2842 0.7752 0.4301 0.0779  -0.1547 -0.1910 241 PHE C CB  
5792  C CG  . PHE C 241 ? 1.2599 0.7460 0.4272 0.0697  -0.1635 -0.1894 241 PHE C CG  
5793  C CD1 . PHE C 241 ? 1.2324 0.7425 0.4217 0.0721  -0.1647 -0.1750 241 PHE C CD1 
5794  C CD2 . PHE C 241 ? 1.2681 0.7241 0.4320 0.0614  -0.1681 -0.2010 241 PHE C CD2 
5795  C CE1 . PHE C 241 ? 1.2115 0.7178 0.4192 0.0645  -0.1724 -0.1741 241 PHE C CE1 
5796  C CE2 . PHE C 241 ? 1.2486 0.7012 0.4295 0.0560  -0.1755 -0.1982 241 PHE C CE2 
5797  C CZ  . PHE C 241 ? 1.2192 0.6980 0.4221 0.0567  -0.1786 -0.1857 241 PHE C CZ  
5798  N N   . GLU C 242 ? 1.2950 0.8082 0.4432 0.1192  -0.1177 -0.1648 242 GLU C N   
5799  C CA  . GLU C 242 ? 1.3206 0.8519 0.4426 0.1318  -0.1088 -0.1577 242 GLU C CA  
5800  C C   . GLU C 242 ? 1.3144 0.8844 0.4357 0.1403  -0.1084 -0.1378 242 GLU C C   
5801  O O   . GLU C 242 ? 1.2924 0.8637 0.4423 0.1477  -0.0979 -0.1227 242 GLU C O   
5802  C CB  . GLU C 242 ? 1.3279 0.8401 0.4594 0.1487  -0.0858 -0.1527 242 GLU C CB  
5803  C CG  . GLU C 242 ? 1.3600 0.8868 0.4605 0.1640  -0.0746 -0.1450 242 GLU C CG  
5804  C CD  . GLU C 242 ? 1.3676 0.8732 0.4805 0.1809  -0.0483 -0.1387 242 GLU C CD  
5805  O OE1 . GLU C 242 ? 1.3664 0.8432 0.4906 0.1767  -0.0449 -0.1526 242 GLU C OE1 
5806  O OE2 . GLU C 242 ? 1.3774 0.8953 0.4885 0.1997  -0.0291 -0.1192 242 GLU C OE2 
5807  N N   . SER C 243 ? 1.3359 0.9397 0.4248 0.1396  -0.1186 -0.1389 243 SER C N   
5808  C CA  . SER C 243 ? 1.3348 0.9833 0.4192 0.1518  -0.1187 -0.1185 243 SER C CA  
5809  C C   . SER C 243 ? 1.3689 1.0596 0.4131 0.1609  -0.1230 -0.1183 243 SER C C   
5810  O O   . SER C 243 ? 1.3890 1.0845 0.4083 0.1449  -0.1363 -0.1419 243 SER C O   
5811  C CB  . SER C 243 ? 1.3120 0.9769 0.4098 0.1349  -0.1369 -0.1211 243 SER C CB  
5812  O OG  . SER C 243 ? 1.3125 1.0242 0.4061 0.1483  -0.1371 -0.1007 243 SER C OG  
5813  N N   . ASN C 244 ? 1.3782 1.1003 0.4161 0.1873  -0.1096 -0.0918 244 ASN C N   
5814  C CA  . ASN C 244 ? 1.4108 1.1873 0.4103 0.2016  -0.1143 -0.0868 244 ASN C CA  
5815  C C   . ASN C 244 ? 1.4048 1.2402 0.4026 0.2053  -0.1278 -0.0746 244 ASN C C   
5816  O O   . ASN C 244 ? 1.4304 1.3231 0.3994 0.2228  -0.1309 -0.0653 244 ASN C O   
5817  C CB  . ASN C 244 ? 1.4355 1.2091 0.4221 0.2353  -0.0866 -0.0627 244 ASN C CB  
5818  C CG  . ASN C 244 ? 1.4215 1.1814 0.4368 0.2574  -0.0609 -0.0305 244 ASN C CG  
5819  O OD1 . ASN C 244 ? 1.3891 1.1234 0.4403 0.2443  -0.0606 -0.0312 244 ASN C OD1 
5820  N ND2 . ASN C 244 ? 1.4495 1.2251 0.4482 0.2915  -0.0367 -0.0025 244 ASN C ND2 
5821  N N   . GLY C 245 ? 1.3721 1.1973 0.4003 0.1903  -0.1356 -0.0744 245 GLY C N   
5822  C CA  . GLY C 245 ? 1.3640 1.2432 0.3942 0.1905  -0.1495 -0.0654 245 GLY C CA  
5823  C C   . GLY C 245 ? 1.3273 1.1846 0.3947 0.1779  -0.1516 -0.0606 245 GLY C C   
5824  O O   . GLY C 245 ? 1.3079 1.1129 0.4022 0.1769  -0.1370 -0.0563 245 GLY C O   
5825  N N   . ASN C 246 ? 1.3194 1.2218 0.3880 0.1679  -0.1699 -0.0630 246 ASN C N   
5826  C CA  . ASN C 246 ? 1.2879 1.1817 0.3882 0.1587  -0.1726 -0.0554 246 ASN C CA  
5827  C C   . ASN C 246 ? 1.2639 1.1018 0.3859 0.1291  -0.1798 -0.0777 246 ASN C C   
5828  O O   . ASN C 246 ? 1.2377 1.0547 0.3881 0.1253  -0.1759 -0.0694 246 ASN C O   
5829  C CB  . ASN C 246 ? 1.2805 1.1653 0.4003 0.1880  -0.1461 -0.0197 246 ASN C CB  
5830  C CG  . ASN C 246 ? 1.3094 1.2463 0.4058 0.2236  -0.1342 0.0079  246 ASN C CG  
5831  O OD1 . ASN C 246 ? 1.3356 1.2725 0.4089 0.2402  -0.1236 0.0114  246 ASN C OD1 
5832  N ND2 . ASN C 246 ? 1.3068 1.2890 0.4085 0.2378  -0.1345 0.0293  246 ASN C ND2 
5833  N N   . PHE C 247 ? 1.2762 1.0922 0.3830 0.1095  -0.1895 -0.1056 247 PHE C N   
5834  C CA  . PHE C 247 ? 1.2610 1.0214 0.3835 0.0877  -0.1927 -0.1241 247 PHE C CA  
5835  C C   . PHE C 247 ? 1.2574 1.0250 0.3801 0.0593  -0.2117 -0.1446 247 PHE C C   
5836  O O   . PHE C 247 ? 1.2792 1.0787 0.3801 0.0456  -0.2234 -0.1629 247 PHE C O   
5837  C CB  . PHE C 247 ? 1.2806 1.0053 0.3872 0.0860  -0.1868 -0.1400 247 PHE C CB  
5838  C CG  . PHE C 247 ? 1.2710 0.9411 0.3904 0.0690  -0.1883 -0.1569 247 PHE C CG  
5839  C CD1 . PHE C 247 ? 1.2423 0.8842 0.3928 0.0713  -0.1825 -0.1476 247 PHE C CD1 
5840  C CD2 . PHE C 247 ? 1.2948 0.9428 0.3938 0.0525  -0.1933 -0.1820 247 PHE C CD2 
5841  C CE1 . PHE C 247 ? 1.2364 0.8356 0.3963 0.0602  -0.1842 -0.1612 247 PHE C CE1 
5842  C CE2 . PHE C 247 ? 1.2909 0.8892 0.3994 0.0421  -0.1920 -0.1937 247 PHE C CE2 
5843  C CZ  . PHE C 247 ? 1.2614 0.8380 0.3997 0.0474  -0.1885 -0.1824 247 PHE C CZ  
5844  N N   . ILE C 248 ? 1.2322 0.9710 0.3801 0.0499  -0.2128 -0.1427 248 ILE C N   
5845  C CA  . ILE C 248 ? 1.2303 0.9623 0.3804 0.0233  -0.2262 -0.1613 248 ILE C CA  
5846  C C   . ILE C 248 ? 1.2356 0.9077 0.3853 0.0124  -0.2228 -0.1776 248 ILE C C   
5847  O O   . ILE C 248 ? 1.2155 0.8537 0.3855 0.0180  -0.2169 -0.1698 248 ILE C O   
5848  C CB  . ILE C 248 ? 1.2023 0.9443 0.3779 0.0217  -0.2293 -0.1471 248 ILE C CB  
5849  C CG1 . ILE C 248 ? 1.1958 0.9889 0.3762 0.0426  -0.2255 -0.1222 248 ILE C CG1 
5850  C CG2 . ILE C 248 ? 1.2069 0.9547 0.3805 -0.0053 -0.2425 -0.1660 248 ILE C CG2 
5851  C CD1 . ILE C 248 ? 1.2192 1.0742 0.3758 0.0443  -0.2347 -0.1268 248 ILE C CD1 
5852  N N   . ALA C 249 ? 1.2657 0.9277 0.3916 -0.0019 -0.2252 -0.2008 249 ALA C N   
5853  C CA  . ALA C 249 ? 1.2792 0.8846 0.3998 -0.0073 -0.2183 -0.2144 249 ALA C CA  
5854  C C   . ALA C 249 ? 1.2765 0.8490 0.4058 -0.0243 -0.2210 -0.2229 249 ALA C C   
5855  O O   . ALA C 249 ? 1.2776 0.8705 0.4077 -0.0413 -0.2286 -0.2296 249 ALA C O   
5856  C CB  . ALA C 249 ? 1.3176 0.9207 0.4083 -0.0164 -0.2158 -0.2362 249 ALA C CB  
5857  N N   . PRO C 250 ? 1.2749 0.7991 0.4108 -0.0182 -0.2137 -0.2222 250 PRO C N   
5858  C CA  . PRO C 250 ? 1.2810 0.7698 0.4194 -0.0305 -0.2132 -0.2291 250 PRO C CA  
5859  C C   . PRO C 250 ? 1.3246 0.7854 0.4380 -0.0501 -0.2068 -0.2532 250 PRO C C   
5860  O O   . PRO C 250 ? 1.3493 0.7832 0.4473 -0.0457 -0.1974 -0.2618 250 PRO C O   
5861  C CB  . PRO C 250 ? 1.2680 0.7236 0.4198 -0.0119 -0.2067 -0.2190 250 PRO C CB  
5862  C CG  . PRO C 250 ? 1.2705 0.7302 0.4188 0.0033  -0.2005 -0.2168 250 PRO C CG  
5863  C CD  . PRO C 250 ? 1.2660 0.7716 0.4100 0.0029  -0.2049 -0.2125 250 PRO C CD  
5864  N N   . GLU C 251 ? 1.3364 0.8025 0.4469 -0.0725 -0.2094 -0.2649 251 GLU C N   
5865  C CA  . GLU C 251 ? 1.3811 0.8089 0.4720 -0.0937 -0.1974 -0.2887 251 GLU C CA  
5866  C C   . GLU C 251 ? 1.3888 0.7576 0.4823 -0.0855 -0.1863 -0.2813 251 GLU C C   
5867  O O   . GLU C 251 ? 1.4192 0.7421 0.4978 -0.0799 -0.1717 -0.2873 251 GLU C O   
5868  C CB  . GLU C 251 ? 1.3931 0.8503 0.4830 -0.1226 -0.2016 -0.3063 251 GLU C CB  
5869  C CG  . GLU C 251 ? 1.4302 0.9090 0.4994 -0.1444 -0.1983 -0.3358 251 GLU C CG  
5870  C CD  . GLU C 251 ? 1.4804 0.9091 0.5348 -0.1707 -0.1786 -0.3633 251 GLU C CD  
5871  O OE1 . GLU C 251 ? 1.4865 0.9098 0.5493 -0.1898 -0.1753 -0.3707 251 GLU C OE1 
5872  O OE2 . GLU C 251 ? 1.5169 0.9094 0.5514 -0.1726 -0.1636 -0.3779 251 GLU C OE2 
5873  N N   . TYR C 252 ? 1.3626 0.7356 0.4741 -0.0825 -0.1926 -0.2669 252 TYR C N   
5874  C CA  . TYR C 252 ? 1.3696 0.6956 0.4829 -0.0726 -0.1836 -0.2577 252 TYR C CA  
5875  C C   . TYR C 252 ? 1.3288 0.6667 0.4631 -0.0468 -0.1923 -0.2349 252 TYR C C   
5876  O O   . TYR C 252 ? 1.2912 0.6721 0.4442 -0.0431 -0.2047 -0.2247 252 TYR C O   
5877  C CB  . TYR C 252 ? 1.3807 0.6968 0.4953 -0.0924 -0.1804 -0.2629 252 TYR C CB  
5878  C CG  . TYR C 252 ? 1.4268 0.7264 0.5234 -0.1215 -0.1671 -0.2898 252 TYR C CG  
5879  C CD1 . TYR C 252 ? 1.4773 0.7142 0.5538 -0.1249 -0.1433 -0.3005 252 TYR C CD1 
5880  C CD2 . TYR C 252 ? 1.4233 0.7722 0.5234 -0.1454 -0.1763 -0.3057 252 TYR C CD2 
5881  C CE1 . TYR C 252 ? 1.5241 0.7431 0.5856 -0.1549 -0.1268 -0.3289 252 TYR C CE1 
5882  C CE2 . TYR C 252 ? 1.4670 0.8072 0.5532 -0.1756 -0.1634 -0.3356 252 TYR C CE2 
5883  C CZ  . TYR C 252 ? 1.5181 0.7907 0.5854 -0.1820 -0.1375 -0.3486 252 TYR C CZ  
5884  O OH  . TYR C 252 ? 1.5658 0.8268 0.6208 -0.2152 -0.1204 -0.3818 252 TYR C OH  
5885  N N   . ALA C 253 ? 1.3399 0.6411 0.4710 -0.0288 -0.1836 -0.2278 253 ALA C N   
5886  C CA  . ALA C 253 ? 1.3069 0.6202 0.4579 -0.0062 -0.1903 -0.2107 253 ALA C CA  
5887  C C   . ALA C 253 ? 1.3239 0.6038 0.4693 0.0016  -0.1833 -0.2039 253 ALA C C   
5888  O O   . ALA C 253 ? 1.3674 0.6022 0.4912 0.0027  -0.1675 -0.2088 253 ALA C O   
5889  C CB  . ALA C 253 ? 1.3030 0.6176 0.4571 0.0139  -0.1878 -0.2086 253 ALA C CB  
5890  N N   . TYR C 254 ? 1.2935 0.5940 0.4570 0.0083  -0.1925 -0.1922 254 TYR C N   
5891  C CA  . TYR C 254 ? 1.3088 0.5838 0.4658 0.0179  -0.1868 -0.1837 254 TYR C CA  
5892  C C   . TYR C 254 ? 1.3182 0.5824 0.4724 0.0476  -0.1821 -0.1758 254 TYR C C   
5893  O O   . TYR C 254 ? 1.2924 0.5862 0.4633 0.0607  -0.1894 -0.1746 254 TYR C O   
5894  C CB  . TYR C 254 ? 1.2742 0.5787 0.4507 0.0137  -0.1985 -0.1754 254 TYR C CB  
5895  C CG  . TYR C 254 ? 1.2728 0.5839 0.4498 -0.0130 -0.2006 -0.1811 254 TYR C CG  
5896  C CD1 . TYR C 254 ? 1.3034 0.5821 0.4662 -0.0247 -0.1904 -0.1831 254 TYR C CD1 
5897  C CD2 . TYR C 254 ? 1.2436 0.5954 0.4359 -0.0253 -0.2110 -0.1839 254 TYR C CD2 
5898  C CE1 . TYR C 254 ? 1.3020 0.5925 0.4686 -0.0505 -0.1922 -0.1906 254 TYR C CE1 
5899  C CE2 . TYR C 254 ? 1.2426 0.6092 0.4368 -0.0477 -0.2139 -0.1890 254 TYR C CE2 
5900  C CZ  . TYR C 254 ? 1.2705 0.6083 0.4532 -0.0616 -0.2054 -0.1937 254 TYR C CZ  
5901  O OH  . TYR C 254 ? 1.2696 0.6273 0.4573 -0.0853 -0.2080 -0.2011 254 TYR C OH  
5902  N N   . LYS C 255 ? 1.3582 0.5813 0.4916 0.0589  -0.1680 -0.1702 255 LYS C N   
5903  C CA  . LYS C 255 ? 1.3759 0.5888 0.5022 0.0911  -0.1613 -0.1606 255 LYS C CA  
5904  C C   . LYS C 255 ? 1.3676 0.5935 0.4978 0.1073  -0.1662 -0.1473 255 LYS C C   
5905  O O   . LYS C 255 ? 1.3837 0.5869 0.5032 0.0976  -0.1603 -0.1434 255 LYS C O   
5906  C CB  . LYS C 255 ? 1.4368 0.5896 0.5323 0.0963  -0.1367 -0.1616 255 LYS C CB  
5907  C CG  . LYS C 255 ? 1.4552 0.6001 0.5443 0.1226  -0.1287 -0.1587 255 LYS C CG  
5908  C CD  . LYS C 255 ? 1.5118 0.5975 0.5733 0.1157  -0.1033 -0.1665 255 LYS C CD  
5909  C CE  . LYS C 255 ? 1.5699 0.6028 0.6049 0.1408  -0.0774 -0.1525 255 LYS C CE  
5910  N NZ  . LYS C 255 ? 1.6243 0.6030 0.6360 0.1405  -0.0505 -0.1600 255 LYS C NZ  
5911  N N   . ILE C 256 ? 1.3443 0.6090 0.4901 0.1310  -0.1763 -0.1420 256 ILE C N   
5912  C CA  . ILE C 256 ? 1.3328 0.6222 0.4842 0.1465  -0.1837 -0.1321 256 ILE C CA  
5913  C C   . ILE C 256 ? 1.3787 0.6436 0.5050 0.1805  -0.1700 -0.1181 256 ILE C C   
5914  O O   . ILE C 256 ? 1.3777 0.6702 0.5093 0.2076  -0.1730 -0.1152 256 ILE C O   
5915  C CB  . ILE C 256 ? 1.2824 0.6366 0.4676 0.1510  -0.2019 -0.1378 256 ILE C CB  
5916  C CG1 . ILE C 256 ? 1.2475 0.6204 0.4552 0.1268  -0.2085 -0.1501 256 ILE C CG1 
5917  C CG2 . ILE C 256 ? 1.2638 0.6441 0.4576 0.1510  -0.2109 -0.1334 256 ILE C CG2 
5918  C CD1 . ILE C 256 ? 1.2018 0.6308 0.4445 0.1262  -0.2203 -0.1571 256 ILE C CD1 
5919  N N   . VAL C 257 ? 1.4221 0.6356 0.5210 0.1803  -0.1527 -0.1089 257 VAL C N   
5920  C CA  . VAL C 257 ? 1.4766 0.6565 0.5465 0.2152  -0.1332 -0.0920 257 VAL C CA  
5921  C C   . VAL C 257 ? 1.4716 0.6888 0.5411 0.2445  -0.1419 -0.0777 257 VAL C C   
5922  O O   . VAL C 257 ? 1.4958 0.7248 0.5540 0.2828  -0.1370 -0.0653 257 VAL C O   
5923  C CB  . VAL C 257 ? 1.5358 0.6378 0.5745 0.2050  -0.1039 -0.0879 257 VAL C CB  
5924  C CG1 . VAL C 257 ? 1.5509 0.6194 0.5861 0.1825  -0.0925 -0.1035 257 VAL C CG1 
5925  C CG2 . VAL C 257 ? 1.5289 0.6201 0.5686 0.1790  -0.1047 -0.0894 257 VAL C CG2 
5926  N N   . LYS C 258 ? 1.4419 0.6811 0.5232 0.2277  -0.1544 -0.0797 258 LYS C N   
5927  C CA  . LYS C 258 ? 1.4357 0.7146 0.5167 0.2518  -0.1638 -0.0692 258 LYS C CA  
5928  C C   . LYS C 258 ? 1.3726 0.7202 0.4898 0.2363  -0.1898 -0.0834 258 LYS C C   
5929  O O   . LYS C 258 ? 1.3405 0.6884 0.4753 0.2023  -0.1967 -0.0939 258 LYS C O   
5930  C CB  . LYS C 258 ? 1.4719 0.7066 0.5271 0.2519  -0.1484 -0.0551 258 LYS C CB  
5931  C CG  . LYS C 258 ? 1.5328 0.7414 0.5526 0.2961  -0.1283 -0.0315 258 LYS C CG  
5932  C CD  . LYS C 258 ? 1.5416 0.7635 0.5492 0.3108  -0.1297 -0.0179 258 LYS C CD  
5933  C CE  . LYS C 258 ? 1.5587 0.7248 0.5557 0.2821  -0.1145 -0.0164 258 LYS C CE  
5934  N NZ  . LYS C 258 ? 1.6004 0.7503 0.5684 0.3102  -0.1005 0.0057  258 LYS C NZ  
5935  N N   . LYS C 259 ? 1.3584 0.7657 0.4869 0.2622  -0.2021 -0.0842 259 LYS C N   
5936  C CA  . LYS C 259 ? 1.3071 0.7808 0.4685 0.2506  -0.2223 -0.0988 259 LYS C CA  
5937  C C   . LYS C 259 ? 1.3191 0.8204 0.4679 0.2724  -0.2263 -0.0893 259 LYS C C   
5938  O O   . LYS C 259 ? 1.3464 0.8718 0.4797 0.3101  -0.2252 -0.0796 259 LYS C O   
5939  C CB  . LYS C 259 ? 1.2800 0.8105 0.4697 0.2588  -0.2330 -0.1138 259 LYS C CB  
5940  C CG  . LYS C 259 ? 1.2592 0.7734 0.4669 0.2344  -0.2313 -0.1258 259 LYS C CG  
5941  C CD  . LYS C 259 ? 1.2409 0.8058 0.4738 0.2463  -0.2375 -0.1389 259 LYS C CD  
5942  C CE  . LYS C 259 ? 1.2252 0.7697 0.4721 0.2245  -0.2334 -0.1485 259 LYS C CE  
5943  N NZ  . LYS C 259 ? 1.2139 0.7998 0.4831 0.2374  -0.2356 -0.1601 259 LYS C NZ  
5944  N N   . GLY C 260 ? 1.3006 0.8011 0.4550 0.2507  -0.2305 -0.0914 260 GLY C N   
5945  C CA  . GLY C 260 ? 1.3107 0.8380 0.4530 0.2684  -0.2344 -0.0838 260 GLY C CA  
5946  C C   . GLY C 260 ? 1.2669 0.8279 0.4360 0.2403  -0.2465 -0.0984 260 GLY C C   
5947  O O   . GLY C 260 ? 1.2276 0.7963 0.4269 0.2098  -0.2516 -0.1139 260 GLY C O   
5948  N N   . ASP C 261 ? 1.2771 0.8570 0.4335 0.2525  -0.2488 -0.0922 261 ASP C N   
5949  C CA  . ASP C 261 ? 1.2424 0.8476 0.4202 0.2268  -0.2568 -0.1043 261 ASP C CA  
5950  C C   . ASP C 261 ? 1.2421 0.7863 0.4151 0.1980  -0.2471 -0.0964 261 ASP C C   
5951  O O   . ASP C 261 ? 1.2810 0.7738 0.4230 0.2064  -0.2339 -0.0780 261 ASP C O   
5952  C CB  . ASP C 261 ? 1.2568 0.9039 0.4202 0.2499  -0.2621 -0.1010 261 ASP C CB  
5953  C CG  . ASP C 261 ? 1.2422 0.9734 0.4239 0.2678  -0.2762 -0.1192 261 ASP C CG  
5954  O OD1 . ASP C 261 ? 1.2139 0.9705 0.4261 0.2558  -0.2814 -0.1371 261 ASP C OD1 
5955  O OD2 . ASP C 261 ? 1.2606 1.0356 0.4265 0.2937  -0.2815 -0.1166 261 ASP C OD2 
5956  N N   . SER C 262 ? 1.2005 0.7523 0.4053 0.1648  -0.2517 -0.1105 262 SER C N   
5957  C CA  . SER C 262 ? 1.1945 0.7028 0.4008 0.1363  -0.2448 -0.1056 262 SER C CA  
5958  C C   . SER C 262 ? 1.1495 0.6914 0.3907 0.1106  -0.2515 -0.1198 262 SER C C   
5959  O O   . SER C 262 ? 1.1263 0.7188 0.3902 0.1127  -0.2587 -0.1350 262 SER C O   
5960  C CB  . SER C 262 ? 1.2023 0.6689 0.4055 0.1250  -0.2380 -0.1038 262 SER C CB  
5961  O OG  . SER C 262 ? 1.1923 0.6307 0.4022 0.0959  -0.2336 -0.1029 262 SER C OG  
5962  N N   . THR C 263 ? 1.1402 0.6549 0.3865 0.0864  -0.2467 -0.1154 263 THR C N   
5963  C CA  . THR C 263 ? 1.1023 0.6423 0.3801 0.0637  -0.2488 -0.1252 263 THR C CA  
5964  C C   . THR C 263 ? 1.0952 0.6039 0.3782 0.0399  -0.2434 -0.1185 263 THR C C   
5965  O O   . THR C 263 ? 1.1207 0.5909 0.3821 0.0378  -0.2377 -0.1077 263 THR C O   
5966  C CB  . THR C 263 ? 1.0991 0.6649 0.3782 0.0668  -0.2503 -0.1277 263 THR C CB  
5967  O OG1 . THR C 263 ? 1.0640 0.6634 0.3775 0.0493  -0.2503 -0.1424 263 THR C OG1 
5968  C CG2 . THR C 263 ? 1.1174 0.6472 0.3775 0.0609  -0.2438 -0.1128 263 THR C CG2 
5969  N N   . ILE C 264 ? 1.0636 0.5909 0.3756 0.0228  -0.2432 -0.1255 264 ILE C N   
5970  C CA  . ILE C 264 ? 1.0545 0.5658 0.3745 0.0024  -0.2391 -0.1189 264 ILE C CA  
5971  C C   . ILE C 264 ? 1.0423 0.5643 0.3741 -0.0070 -0.2358 -0.1166 264 ILE C C   
5972  O O   . ILE C 264 ? 1.0193 0.5690 0.3751 -0.0113 -0.2333 -0.1242 264 ILE C O   
5973  C CB  . ILE C 264 ? 1.0326 0.5566 0.3738 -0.0065 -0.2382 -0.1234 264 ILE C CB  
5974  C CG1 . ILE C 264 ? 1.0475 0.5591 0.3752 0.0028  -0.2408 -0.1262 264 ILE C CG1 
5975  C CG2 . ILE C 264 ? 1.0254 0.5419 0.3732 -0.0239 -0.2349 -0.1153 264 ILE C CG2 
5976  C CD1 . ILE C 264 ? 1.0283 0.5573 0.3757 0.0000  -0.2394 -0.1323 264 ILE C CD1 
5977  N N   . MET C 265 ? 0.7292 0.6324 0.4383 -0.1118 -0.1268 -0.1299 265 MET C N   
5978  C CA  . MET C 265 ? 0.6911 0.6115 0.4379 -0.1262 -0.1360 -0.1226 265 MET C CA  
5979  C C   . MET C 265 ? 0.6998 0.6187 0.4408 -0.1373 -0.1546 -0.1252 265 MET C C   
5980  O O   . MET C 265 ? 0.7351 0.6313 0.4505 -0.1432 -0.1642 -0.1343 265 MET C O   
5981  C CB  . MET C 265 ? 0.6955 0.5984 0.4506 -0.1305 -0.1381 -0.1250 265 MET C CB  
5982  C CG  . MET C 265 ? 0.6525 0.5858 0.4505 -0.1426 -0.1427 -0.1176 265 MET C CG  
5983  S SD  . MET C 265 ? 0.6752 0.5763 0.4659 -0.1537 -0.1424 -0.1198 265 MET C SD  
5984  C CE  . MET C 265 ? 0.6758 0.5677 0.4593 -0.1209 -0.1235 -0.1168 265 MET C CE  
5985  N N   . LYS C 266 ? 0.6770 0.6178 0.4337 -0.1368 -0.1611 -0.1181 266 LYS C N   
5986  C CA  . LYS C 266 ? 0.6914 0.6381 0.4377 -0.1351 -0.1811 -0.1217 266 LYS C CA  
5987  C C   . LYS C 266 ? 0.6680 0.6562 0.4505 -0.1394 -0.1928 -0.1241 266 LYS C C   
5988  O O   . LYS C 266 ? 0.6377 0.6475 0.4466 -0.1338 -0.1900 -0.1173 266 LYS C O   
5989  C CB  . LYS C 266 ? 0.7052 0.6367 0.4233 -0.1246 -0.1845 -0.1140 266 LYS C CB  
5990  C CG  . LYS C 266 ? 0.7437 0.6408 0.4141 -0.1292 -0.1770 -0.1131 266 LYS C CG  
5991  C CD  . LYS C 266 ? 0.7794 0.6607 0.4219 -0.1264 -0.1905 -0.1233 266 LYS C CD  
5992  C CE  . LYS C 266 ? 0.8263 0.6701 0.4117 -0.1306 -0.1866 -0.1213 266 LYS C CE  
5993  N NZ  . LYS C 266 ? 0.8647 0.6893 0.4188 -0.1250 -0.2030 -0.1308 266 LYS C NZ  
5994  N N   . SER C 267 ? 0.6868 0.6913 0.4673 -0.1530 -0.2057 -0.1341 267 SER C N   
5995  C CA  . SER C 267 ? 0.6704 0.7327 0.4832 -0.1674 -0.2159 -0.1381 267 SER C CA  
5996  C C   . SER C 267 ? 0.6990 0.7973 0.5007 -0.1826 -0.2351 -0.1500 267 SER C C   
5997  O O   . SER C 267 ? 0.7381 0.7959 0.5048 -0.1949 -0.2373 -0.1557 267 SER C O   
5998  C CB  . SER C 267 ? 0.6669 0.7124 0.4904 -0.1921 -0.2037 -0.1359 267 SER C CB  
5999  O OG  . SER C 267 ? 0.6572 0.7615 0.5063 -0.2165 -0.2121 -0.1392 267 SER C OG  
6000  N N   . GLU C 268 ? 0.6827 0.8652 0.5126 -0.1804 -0.2494 -0.1547 268 GLU C N   
6001  C CA  . GLU C 268 ? 0.7056 0.9538 0.5328 -0.1987 -0.2689 -0.1673 268 GLU C CA  
6002  C C   . GLU C 268 ? 0.7195 0.9921 0.5523 -0.2564 -0.2675 -0.1712 268 GLU C C   
6003  O O   . GLU C 268 ? 0.7499 1.0701 0.5712 -0.2894 -0.2819 -0.1814 268 GLU C O   
6004  C CB  . GLU C 268 ? 0.6890 1.0357 0.5388 -0.1628 -0.2867 -0.1731 268 GLU C CB  
6005  C CG  . GLU C 268 ? 0.6980 1.0005 0.5209 -0.1052 -0.2910 -0.1683 268 GLU C CG  
6006  C CD  . GLU C 268 ? 0.7400 0.9674 0.5125 -0.0977 -0.2948 -0.1691 268 GLU C CD  
6007  O OE1 . GLU C 268 ? 0.7651 1.0253 0.5256 -0.1074 -0.3099 -0.1800 268 GLU C OE1 
6008  O OE2 . GLU C 268 ? 0.7503 0.8916 0.4933 -0.0856 -0.2826 -0.1591 268 GLU C OE2 
6009  N N   . LEU C 269 ? 0.7076 0.9438 0.5491 -0.2719 -0.2512 -0.1630 269 LEU C N   
6010  C CA  . LEU C 269 ? 0.7380 0.9761 0.5672 -0.3301 -0.2499 -0.1649 269 LEU C CA  
6011  C C   . LEU C 269 ? 0.8131 0.9532 0.5746 -0.3640 -0.2508 -0.1689 269 LEU C C   
6012  O O   . LEU C 269 ? 0.8299 0.8918 0.5620 -0.3352 -0.2456 -0.1680 269 LEU C O   
6013  C CB  . LEU C 269 ? 0.7138 0.9253 0.5604 -0.3306 -0.2333 -0.1547 269 LEU C CB  
6014  C CG  . LEU C 269 ? 0.6535 0.9650 0.5589 -0.3107 -0.2333 -0.1519 269 LEU C CG  
6015  C CD1 . LEU C 269 ? 0.6283 0.8935 0.5470 -0.3000 -0.2157 -0.1404 269 LEU C CD1 
6016  C CD2 . LEU C 269 ? 0.6600 1.0858 0.5831 -0.3559 -0.2446 -0.1604 269 LEU C CD2 
6017  N N   . GLU C 270 ? 0.8682 1.0108 0.5964 -0.4275 -0.2578 -0.1736 270 GLU C N   
6018  C CA  . GLU C 270 ? 0.9645 1.0021 0.6076 -0.4666 -0.2630 -0.1787 270 GLU C CA  
6019  C C   . GLU C 270 ? 1.0239 0.9357 0.6075 -0.4797 -0.2509 -0.1725 270 GLU C C   
6020  O O   . GLU C 270 ? 1.0004 0.8548 0.5902 -0.4274 -0.2364 -0.1663 270 GLU C O   
6021  C CB  . GLU C 270 ? 1.0130 1.1188 0.6330 -0.5342 -0.2826 -0.1891 270 GLU C CB  
6022  C CG  . GLU C 270 ? 0.9761 1.2296 0.6490 -0.5729 -0.2880 -0.1909 270 GLU C CG  
6023  C CD  . GLU C 270 ? 1.0291 1.3678 0.6768 -0.6470 -0.3072 -0.2022 270 GLU C CD  
6024  O OE1 . GLU C 270 ? 1.0989 1.3702 0.6834 -0.6710 -0.3177 -0.2082 270 GLU C OE1 
6025  O OE2 . GLU C 270 ? 1.0031 1.4858 0.6931 -0.6830 -0.3119 -0.2058 270 GLU C OE2 
6026  N N   . TYR C 271 ? 1.1087 0.9781 0.6280 -0.5487 -0.2575 -0.1743 271 TYR C N   
6027  C CA  . TYR C 271 ? 1.1976 0.9184 0.6303 -0.5584 -0.2506 -0.1700 271 TYR C CA  
6028  C C   . TYR C 271 ? 1.2416 0.9727 0.6481 -0.6299 -0.2531 -0.1666 271 TYR C C   
6029  O O   . TYR C 271 ? 1.2944 1.0666 0.6691 -0.7068 -0.2666 -0.1719 271 TYR C O   
6030  C CB  . TYR C 271 ? 1.3221 0.9000 0.6384 -0.5702 -0.2598 -0.1774 271 TYR C CB  
6031  C CG  . TYR C 271 ? 1.4352 0.8385 0.6407 -0.5600 -0.2555 -0.1754 271 TYR C CG  
6032  C CD1 . TYR C 271 ? 1.3976 0.7633 0.6229 -0.4827 -0.2395 -0.1709 271 TYR C CD1 
6033  C CD2 . TYR C 271 ? 1.5928 0.8653 0.6621 -0.6270 -0.2691 -0.1790 271 TYR C CD2 
6034  C CE1 . TYR C 271 ? 1.5084 0.7205 0.6269 -0.4613 -0.2378 -0.1712 271 TYR C CE1 
6035  C CE2 . TYR C 271 ? 1.7178 0.8120 0.6655 -0.6082 -0.2684 -0.1783 271 TYR C CE2 
6036  C CZ  . TYR C 271 ? 1.6727 0.7414 0.6480 -0.5196 -0.2530 -0.1751 271 TYR C CZ  
6037  O OH  . TYR C 271 ? 1.8046 0.7018 0.6533 -0.4902 -0.2545 -0.1765 271 TYR C OH  
6038  N N   . GLY C 272 ? 1.2235 0.9227 0.6405 -0.6086 -0.2402 -0.1579 272 GLY C N   
6039  C CA  . GLY C 272 ? 1.2640 0.9696 0.6557 -0.6739 -0.2404 -0.1533 272 GLY C CA  
6040  C C   . GLY C 272 ? 1.4337 0.9573 0.6720 -0.7274 -0.2476 -0.1532 272 GLY C C   
6041  O O   . GLY C 272 ? 1.4966 1.0131 0.6887 -0.8024 -0.2510 -0.1501 272 GLY C O   
6042  N N   . ASN C 273 ? 1.5196 0.8916 0.6682 -0.6887 -0.2508 -0.1572 273 ASN C N   
6043  C CA  . ASN C 273 ? 1.7048 0.8681 0.6822 -0.7191 -0.2598 -0.1582 273 ASN C CA  
6044  C C   . ASN C 273 ? 1.7349 0.8268 0.6803 -0.7071 -0.2513 -0.1494 273 ASN C C   
6045  O O   . ASN C 273 ? 1.8820 0.8440 0.6974 -0.7690 -0.2603 -0.1473 273 ASN C O   
6046  C CB  . ASN C 273 ? 1.8311 0.9590 0.7086 -0.8322 -0.2784 -0.1627 273 ASN C CB  
6047  C CG  . ASN C 273 ? 2.0285 0.9302 0.7204 -0.8435 -0.2932 -0.1689 273 ASN C CG  
6048  O OD1 . ASN C 273 ? 2.0843 0.9705 0.7302 -0.8792 -0.3064 -0.1768 273 ASN C OD1 
6049  N ND2 . ASN C 273 ? 2.1427 0.8635 0.7200 -0.8069 -0.2924 -0.1663 273 ASN C ND2 
6050  N N   . CYS C 274 ? 1.6025 0.7744 0.6593 -0.6284 -0.2349 -0.1442 274 CYS C N   
6051  C CA  . CYS C 274 ? 1.5993 0.7350 0.6542 -0.6039 -0.2252 -0.1358 274 CYS C CA  
6052  C C   . CYS C 274 ? 1.6143 0.6585 0.6402 -0.5029 -0.2184 -0.1378 274 CYS C C   
6053  O O   . CYS C 274 ? 1.6265 0.6428 0.6355 -0.4576 -0.2203 -0.1457 274 CYS C O   
6054  C CB  . CYS C 274 ? 1.4274 0.7539 0.6425 -0.5979 -0.2120 -0.1286 274 CYS C CB  
6055  S SG  . CYS C 274 ? 1.2639 0.7586 0.6249 -0.5452 -0.2065 -0.1325 274 CYS C SG  
6056  N N   . ASN C 275 ? 1.6147 0.6228 0.6347 -0.4677 -0.2107 -0.1316 275 ASN C N   
6057  C CA  . ASN C 275 ? 1.6116 0.5731 0.6224 -0.3679 -0.2029 -0.1340 275 ASN C CA  
6058  C C   . ASN C 275 ? 1.4681 0.5530 0.6058 -0.3305 -0.1866 -0.1248 275 ASN C C   
6059  O O   . ASN C 275 ? 1.4309 0.5650 0.6079 -0.3780 -0.1839 -0.1165 275 ASN C O   
6060  C CB  . ASN C 275 ? 1.8078 0.5570 0.6372 -0.3503 -0.2149 -0.1381 275 ASN C CB  
6061  C CG  . ASN C 275 ? 1.8222 0.5314 0.6289 -0.2378 -0.2095 -0.1447 275 ASN C CG  
6062  O OD1 . ASN C 275 ? 1.7791 0.5356 0.6211 -0.1861 -0.2050 -0.1525 275 ASN C OD1 
6063  N ND2 . ASN C 275 ? 1.8862 0.5165 0.6322 -0.1991 -0.2101 -0.1424 275 ASN C ND2 
6064  N N   . THR C 276 ? 1.3921 0.5316 0.5900 -0.2497 -0.1756 -0.1268 276 THR C N   
6065  C CA  . THR C 276 ? 1.2674 0.5161 0.5742 -0.2153 -0.1610 -0.1183 276 THR C CA  
6066  C C   . THR C 276 ? 1.2616 0.5091 0.5658 -0.1260 -0.1529 -0.1228 276 THR C C   
6067  O O   . THR C 276 ? 1.3414 0.5203 0.5709 -0.0836 -0.1573 -0.1335 276 THR C O   
6068  C CB  . THR C 276 ? 1.1123 0.5255 0.5602 -0.2368 -0.1530 -0.1129 276 THR C CB  
6069  O OG1 . THR C 276 ? 1.0145 0.5115 0.5478 -0.2170 -0.1414 -0.1037 276 THR C OG1 
6070  C CG2 . THR C 276 ? 1.0643 0.5299 0.5499 -0.2011 -0.1496 -0.1190 276 THR C CG2 
6071  N N   . LYS C 277 ? 1.1714 0.5020 0.5544 -0.0986 -0.1415 -0.1154 277 LYS C N   
6072  C CA  . LYS C 277 ? 1.1416 0.5180 0.5464 -0.0213 -0.1319 -0.1190 277 LYS C CA  
6073  C C   . LYS C 277 ? 0.9906 0.5257 0.5270 -0.0176 -0.1178 -0.1131 277 LYS C C   
6074  O O   . LYS C 277 ? 0.9554 0.5556 0.5199 0.0336  -0.1084 -0.1158 277 LYS C O   
6075  C CB  . LYS C 277 ? 1.1865 0.5153 0.5516 0.0102  -0.1323 -0.1161 277 LYS C CB  
6076  C CG  . LYS C 277 ? 1.3681 0.5223 0.5707 0.0439  -0.1470 -0.1262 277 LYS C CG  
6077  C CD  . LYS C 277 ? 1.4137 0.5668 0.5738 0.1441  -0.1453 -0.1372 277 LYS C CD  
6078  C CE  . LYS C 277 ? 1.3474 0.5791 0.5678 0.1761  -0.1372 -0.1308 277 LYS C CE  
6079  N NZ  . LYS C 277 ? 1.3306 0.6502 0.5669 0.2652  -0.1302 -0.1413 277 LYS C NZ  
6080  N N   . CYS C 278 ? 0.9139 0.5096 0.5200 -0.0724 -0.1177 -0.1058 278 CYS C N   
6081  C CA  . CYS C 278 ? 0.7959 0.5132 0.5030 -0.0745 -0.1082 -0.0997 278 CYS C CA  
6082  C C   . CYS C 278 ? 0.7680 0.5109 0.5025 -0.1208 -0.1150 -0.0995 278 CYS C C   
6083  O O   . CYS C 278 ? 0.7746 0.5083 0.5099 -0.1645 -0.1220 -0.0967 278 CYS C O   
6084  C CB  . CYS C 278 ? 0.7262 0.5006 0.4945 -0.0791 -0.1014 -0.0887 278 CYS C CB  
6085  S SG  . CYS C 278 ? 0.6091 0.5021 0.4750 -0.0896 -0.0936 -0.0800 278 CYS C SG  
6086  N N   . GLN C 279 ? 0.7409 0.5234 0.4950 -0.1113 -0.1134 -0.1030 279 GLN C N   
6087  C CA  . GLN C 279 ? 0.7264 0.5301 0.4961 -0.1459 -0.1224 -0.1050 279 GLN C CA  
6088  C C   . GLN C 279 ? 0.6443 0.5329 0.4807 -0.1431 -0.1186 -0.0993 279 GLN C C   
6089  O O   . GLN C 279 ? 0.6184 0.5367 0.4690 -0.1172 -0.1089 -0.0971 279 GLN C O   
6090  C CB  . GLN C 279 ? 0.7979 0.5426 0.5040 -0.1410 -0.1287 -0.1158 279 GLN C CB  
6091  C CG  . GLN C 279 ? 0.7946 0.5582 0.5079 -0.1777 -0.1402 -0.1193 279 GLN C CG  
6092  C CD  . GLN C 279 ? 0.8308 0.5740 0.5236 -0.2293 -0.1516 -0.1199 279 GLN C CD  
6093  O OE1 . GLN C 279 ? 0.9208 0.5733 0.5374 -0.2449 -0.1565 -0.1234 279 GLN C OE1 
6094  N NE2 . GLN C 279 ? 0.7724 0.5994 0.5231 -0.2561 -0.1568 -0.1172 279 GLN C NE2 
6095  N N   . THR C 280 ? 0.6159 0.5427 0.4827 -0.1704 -0.1275 -0.0978 280 THR C N   
6096  C CA  . THR C 280 ? 0.5666 0.5497 0.4712 -0.1646 -0.1294 -0.0943 280 THR C CA  
6097  C C   . THR C 280 ? 0.5855 0.5788 0.4794 -0.1801 -0.1434 -0.1020 280 THR C C   
6098  O O   . THR C 280 ? 0.6247 0.5986 0.4943 -0.2059 -0.1515 -0.1086 280 THR C O   
6099  C CB  . THR C 280 ? 0.5167 0.5470 0.4657 -0.1673 -0.1293 -0.0861 280 THR C CB  
6100  O OG1 . THR C 280 ? 0.5149 0.5800 0.4770 -0.1891 -0.1411 -0.0901 280 THR C OG1 
6101  C CG2 . THR C 280 ? 0.5087 0.5259 0.4653 -0.1631 -0.1190 -0.0800 280 THR C CG2 
6102  N N   . PRO C 281 ? 0.5679 0.5874 0.4707 -0.1671 -0.1476 -0.1012 281 PRO C N   
6103  C CA  . PRO C 281 ? 0.5829 0.6236 0.4783 -0.1745 -0.1633 -0.1086 281 PRO C CA  
6104  C C   . PRO C 281 ? 0.5690 0.6709 0.4920 -0.1899 -0.1753 -0.1117 281 PRO C C   
6105  O O   . PRO C 281 ? 0.5866 0.7201 0.5033 -0.2017 -0.1892 -0.1203 281 PRO C O   
6106  C CB  . PRO C 281 ? 0.5745 0.6178 0.4627 -0.1515 -0.1651 -0.1049 281 PRO C CB  
6107  C CG  . PRO C 281 ? 0.5607 0.5854 0.4486 -0.1421 -0.1488 -0.0959 281 PRO C CG  
6108  C CD  . PRO C 281 ? 0.5508 0.5696 0.4538 -0.1472 -0.1379 -0.0942 281 PRO C CD  
6109  N N   . MET C 282 ? 0.5394 0.6677 0.4924 -0.1891 -0.1698 -0.1054 282 MET C N   
6110  C CA  . MET C 282 ? 0.5253 0.7264 0.5067 -0.2035 -0.1781 -0.1086 282 MET C CA  
6111  C C   . MET C 282 ? 0.5539 0.7471 0.5235 -0.2497 -0.1765 -0.1116 282 MET C C   
6112  O O   . MET C 282 ? 0.5606 0.8209 0.5402 -0.2794 -0.1855 -0.1180 282 MET C O   
6113  C CB  . MET C 282 ? 0.4887 0.7140 0.4996 -0.1828 -0.1721 -0.1003 282 MET C CB  
6114  C CG  . MET C 282 ? 0.4825 0.6899 0.4838 -0.1437 -0.1739 -0.0952 282 MET C CG  
6115  S SD  . MET C 282 ? 0.4917 0.7666 0.4922 -0.1096 -0.1945 -0.1030 282 MET C SD  
6116  C CE  . MET C 282 ? 0.4585 0.7936 0.4967 -0.1061 -0.1903 -0.1001 282 MET C CE  
6117  N N   . GLY C 283 ? 0.5806 0.6922 0.5202 -0.2557 -0.1656 -0.1075 283 GLY C N   
6118  C CA  . GLY C 283 ? 0.6319 0.7003 0.5350 -0.2969 -0.1646 -0.1087 283 GLY C CA  
6119  C C   . GLY C 283 ? 0.6507 0.6372 0.5275 -0.2789 -0.1520 -0.1022 283 GLY C C   
6120  O O   . GLY C 283 ? 0.6162 0.5975 0.5114 -0.2388 -0.1432 -0.0975 283 GLY C O   
6121  N N   . ALA C 284 ? 0.7148 0.6380 0.5405 -0.3101 -0.1523 -0.1025 284 ALA C N   
6122  C CA  . ALA C 284 ? 0.7528 0.5895 0.5371 -0.2863 -0.1437 -0.0986 284 ALA C CA  
6123  C C   . ALA C 284 ? 0.7153 0.5771 0.5333 -0.2852 -0.1359 -0.0897 284 ALA C C   
6124  O O   . ALA C 284 ? 0.6824 0.6121 0.5378 -0.3153 -0.1378 -0.0874 284 ALA C O   
6125  C CB  . ALA C 284 ? 0.8720 0.5938 0.5542 -0.3139 -0.1513 -0.1044 284 ALA C CB  
6126  N N   . ILE C 285 ? 0.7235 0.5376 0.5261 -0.2479 -0.1273 -0.0857 285 ILE C N   
6127  C CA  . ILE C 285 ? 0.6900 0.5213 0.5212 -0.2405 -0.1197 -0.0770 285 ILE C CA  
6128  C C   . ILE C 285 ? 0.7797 0.5055 0.5316 -0.2382 -0.1202 -0.0768 285 ILE C C   
6129  O O   . ILE C 285 ? 0.8440 0.4942 0.5341 -0.2051 -0.1216 -0.0823 285 ILE C O   
6130  C CB  . ILE C 285 ? 0.6108 0.4997 0.5019 -0.1959 -0.1099 -0.0714 285 ILE C CB  
6131  C CG1 . ILE C 285 ? 0.5345 0.5131 0.4928 -0.2043 -0.1108 -0.0676 285 ILE C CG1 
6132  C CG2 . ILE C 285 ? 0.6086 0.4794 0.4985 -0.1742 -0.1022 -0.0649 285 ILE C CG2 
6133  C CD1 . ILE C 285 ? 0.4838 0.4998 0.4752 -0.1728 -0.1055 -0.0638 285 ILE C CD1 
6134  N N   . ASN C 286 ? 0.7915 0.5115 0.5385 -0.2703 -0.1199 -0.0711 286 ASN C N   
6135  C CA  . ASN C 286 ? 0.8825 0.4960 0.5481 -0.2688 -0.1214 -0.0692 286 ASN C CA  
6136  C C   . ASN C 286 ? 0.8263 0.4856 0.5415 -0.2661 -0.1135 -0.0596 286 ASN C C   
6137  O O   . ASN C 286 ? 0.8235 0.5094 0.5484 -0.3150 -0.1137 -0.0555 286 ASN C O   
6138  C CB  . ASN C 286 ? 0.9995 0.5232 0.5689 -0.3326 -0.1325 -0.0724 286 ASN C CB  
6139  C CG  . ASN C 286 ? 1.1196 0.5074 0.5803 -0.3346 -0.1368 -0.0699 286 ASN C CG  
6140  O OD1 . ASN C 286 ? 1.1441 0.4779 0.5759 -0.2714 -0.1351 -0.0705 286 ASN C OD1 
6141  N ND2 . ASN C 286 ? 1.2038 0.5381 0.5968 -0.4082 -0.1432 -0.0677 286 ASN C ND2 
6142  N N   . SER C 287 ? 0.7821 0.4609 0.5289 -0.2112 -0.1062 -0.0564 287 SER C N   
6143  C CA  . SER C 287 ? 0.7348 0.4494 0.5224 -0.2054 -0.0994 -0.0474 287 SER C CA  
6144  C C   . SER C 287 ? 0.7363 0.4350 0.5158 -0.1460 -0.0952 -0.0465 287 SER C C   
6145  O O   . SER C 287 ? 0.7443 0.4432 0.5130 -0.1043 -0.0948 -0.0528 287 SER C O   
6146  C CB  . SER C 287 ? 0.6230 0.4572 0.5098 -0.2163 -0.0937 -0.0424 287 SER C CB  
6147  O OG  . SER C 287 ? 0.5595 0.4470 0.4944 -0.1763 -0.0886 -0.0416 287 SER C OG  
6148  N N   . SER C 288 ? 0.7288 0.4252 0.5145 -0.1429 -0.0920 -0.0392 288 SER C N   
6149  C CA  . SER C 288 ? 0.7253 0.4255 0.5096 -0.0887 -0.0888 -0.0381 288 SER C CA  
6150  C C   . SER C 288 ? 0.6108 0.4257 0.4920 -0.0814 -0.0795 -0.0307 288 SER C C   
6151  O O   . SER C 288 ? 0.5944 0.4381 0.4875 -0.0454 -0.0761 -0.0289 288 SER C O   
6152  C CB  . SER C 288 ? 0.8085 0.4168 0.5209 -0.0881 -0.0936 -0.0350 288 SER C CB  
6153  O OG  . SER C 288 ? 0.8131 0.4090 0.5258 -0.1506 -0.0936 -0.0287 288 SER C OG  
6154  N N   . MET C 289 ? 0.5426 0.4201 0.4831 -0.1142 -0.0769 -0.0274 289 MET C N   
6155  C CA  . MET C 289 ? 0.4570 0.4186 0.4671 -0.1113 -0.0709 -0.0204 289 MET C CA  
6156  C C   . MET C 289 ? 0.4337 0.4394 0.4580 -0.0805 -0.0672 -0.0228 289 MET C C   
6157  O O   . MET C 289 ? 0.4637 0.4554 0.4626 -0.0671 -0.0688 -0.0309 289 MET C O   
6158  C CB  . MET C 289 ? 0.4134 0.4187 0.4626 -0.1414 -0.0724 -0.0193 289 MET C CB  
6159  C CG  . MET C 289 ? 0.4274 0.4254 0.4727 -0.1769 -0.0749 -0.0185 289 MET C CG  
6160  S SD  . MET C 289 ? 0.4078 0.4168 0.4709 -0.1804 -0.0697 -0.0089 289 MET C SD  
6161  C CE  . MET C 289 ? 0.3863 0.4538 0.4767 -0.2173 -0.0715 -0.0105 289 MET C CE  
6162  N N   . PRO C 290 ? 0.3858 0.4480 0.4458 -0.0736 -0.0621 -0.0161 290 PRO C N   
6163  C CA  . PRO C 290 ? 0.3642 0.4856 0.4375 -0.0593 -0.0577 -0.0176 290 PRO C CA  
6164  C C   . PRO C 290 ? 0.3374 0.4814 0.4269 -0.0822 -0.0583 -0.0169 290 PRO C C   
6165  O O   . PRO C 290 ? 0.3364 0.5175 0.4233 -0.0770 -0.0550 -0.0200 290 PRO C O   
6166  C CB  . PRO C 290 ? 0.3328 0.5014 0.4304 -0.0591 -0.0538 -0.0093 290 PRO C CB  
6167  C CG  . PRO C 290 ? 0.3179 0.4562 0.4282 -0.0808 -0.0561 -0.0018 290 PRO C CG  
6168  C CD  . PRO C 290 ? 0.3595 0.4331 0.4410 -0.0821 -0.0602 -0.0070 290 PRO C CD  
6169  N N   . PHE C 291 ? 0.3220 0.4480 0.4230 -0.1048 -0.0629 -0.0138 291 PHE C N   
6170  C CA  . PHE C 291 ? 0.3079 0.4455 0.4137 -0.1194 -0.0666 -0.0133 291 PHE C CA  
6171  C C   . PHE C 291 ? 0.3170 0.4329 0.4194 -0.1286 -0.0738 -0.0192 291 PHE C C   
6172  O O   . PHE C 291 ? 0.3295 0.4264 0.4298 -0.1356 -0.0754 -0.0211 291 PHE C O   
6173  C CB  . PHE C 291 ? 0.2878 0.4366 0.4035 -0.1304 -0.0682 -0.0042 291 PHE C CB  
6174  C CG  . PHE C 291 ? 0.2834 0.4593 0.3956 -0.1352 -0.0630 0.0024  291 PHE C CG  
6175  C CD1 . PHE C 291 ? 0.2960 0.4903 0.3894 -0.1468 -0.0616 0.0028  291 PHE C CD1 
6176  C CD2 . PHE C 291 ? 0.2720 0.4590 0.3955 -0.1339 -0.0598 0.0086  291 PHE C CD2 
6177  C CE1 . PHE C 291 ? 0.2985 0.5298 0.3837 -0.1629 -0.0568 0.0090  291 PHE C CE1 
6178  C CE2 . PHE C 291 ? 0.2707 0.4938 0.3894 -0.1448 -0.0560 0.0145  291 PHE C CE2 
6179  C CZ  . PHE C 291 ? 0.2850 0.5340 0.3841 -0.1623 -0.0543 0.0146  291 PHE C CZ  
6180  N N   . HIS C 292 ? 0.3161 0.4378 0.4127 -0.1323 -0.0788 -0.0219 292 HIS C N   
6181  C CA  . HIS C 292 ? 0.3206 0.4423 0.4178 -0.1399 -0.0877 -0.0278 292 HIS C CA  
6182  C C   . HIS C 292 ? 0.3198 0.4484 0.4070 -0.1352 -0.0951 -0.0270 292 HIS C C   
6183  O O   . HIS C 292 ? 0.3252 0.4455 0.3956 -0.1345 -0.0926 -0.0216 292 HIS C O   
6184  C CB  . HIS C 292 ? 0.3502 0.4506 0.4288 -0.1444 -0.0896 -0.0369 292 HIS C CB  
6185  C CG  . HIS C 292 ? 0.3617 0.4577 0.4230 -0.1360 -0.0892 -0.0404 292 HIS C CG  
6186  N ND1 . HIS C 292 ? 0.3709 0.4689 0.4231 -0.1398 -0.0974 -0.0457 292 HIS C ND1 
6187  C CD2 . HIS C 292 ? 0.3674 0.4666 0.4178 -0.1241 -0.0814 -0.0398 292 HIS C CD2 
6188  C CE1 . HIS C 292 ? 0.3837 0.4758 0.4175 -0.1334 -0.0941 -0.0474 292 HIS C CE1 
6189  N NE2 . HIS C 292 ? 0.3806 0.4801 0.4146 -0.1247 -0.0838 -0.0442 292 HIS C NE2 
6190  N N   . ASN C 293 ? 0.3231 0.4670 0.4118 -0.1329 -0.1052 -0.0328 293 ASN C N   
6191  C CA  . ASN C 293 ? 0.3403 0.4786 0.4040 -0.1184 -0.1160 -0.0337 293 ASN C CA  
6192  C C   . ASN C 293 ? 0.3550 0.5090 0.4125 -0.1150 -0.1265 -0.0441 293 ASN C C   
6193  O O   . ASN C 293 ? 0.3736 0.5358 0.4123 -0.0950 -0.1393 -0.0480 293 ASN C O   
6194  C CB  . ASN C 293 ? 0.3399 0.4886 0.4014 -0.1020 -0.1220 -0.0308 293 ASN C CB  
6195  C CG  . ASN C 293 ? 0.3237 0.5304 0.4161 -0.0995 -0.1258 -0.0384 293 ASN C CG  
6196  O OD1 . ASN C 293 ? 0.3131 0.5424 0.4279 -0.1219 -0.1215 -0.0428 293 ASN C OD1 
6197  N ND2 . ASN C 293 ? 0.3327 0.5632 0.4168 -0.0734 -0.1346 -0.0406 293 ASN C ND2 
6198  N N   . ILE C 294 ? 0.3564 0.5095 0.4207 -0.1312 -0.1227 -0.0494 294 ILE C N   
6199  C CA  . ILE C 294 ? 0.3725 0.5429 0.4312 -0.1356 -0.1326 -0.0597 294 ILE C CA  
6200  C C   . ILE C 294 ? 0.3963 0.5396 0.4224 -0.1234 -0.1387 -0.0613 294 ILE C C   
6201  O O   . ILE C 294 ? 0.4131 0.5710 0.4244 -0.1073 -0.1523 -0.0665 294 ILE C O   
6202  C CB  . ILE C 294 ? 0.3860 0.5431 0.4438 -0.1608 -0.1279 -0.0645 294 ILE C CB  
6203  C CG1 . ILE C 294 ? 0.3794 0.5466 0.4529 -0.1793 -0.1225 -0.0620 294 ILE C CG1 
6204  C CG2 . ILE C 294 ? 0.4085 0.5856 0.4564 -0.1730 -0.1393 -0.0751 294 ILE C CG2 
6205  C CD1 . ILE C 294 ? 0.3600 0.5940 0.4595 -0.1815 -0.1284 -0.0637 294 ILE C CD1 
6206  N N   . HIS C 295 ? 0.4035 0.5122 0.4141 -0.1289 -0.1290 -0.0577 295 HIS C N   
6207  C CA  . HIS C 295 ? 0.4311 0.5142 0.4065 -0.1254 -0.1322 -0.0590 295 HIS C CA  
6208  C C   . HIS C 295 ? 0.4329 0.5013 0.3967 -0.1331 -0.1178 -0.0531 295 HIS C C   
6209  O O   . HIS C 295 ? 0.4198 0.4973 0.4013 -0.1349 -0.1072 -0.0539 295 HIS C O   
6210  C CB  . HIS C 295 ? 0.4469 0.5337 0.4179 -0.1301 -0.1387 -0.0698 295 HIS C CB  
6211  C CG  . HIS C 295 ? 0.4787 0.5452 0.4128 -0.1228 -0.1475 -0.0729 295 HIS C CG  
6212  N ND1 . HIS C 295 ? 0.4980 0.5367 0.4039 -0.1278 -0.1393 -0.0704 295 HIS C ND1 
6213  C CD2 . HIS C 295 ? 0.5001 0.5737 0.4165 -0.1095 -0.1643 -0.0789 295 HIS C CD2 
6214  C CE1 . HIS C 295 ? 0.5323 0.5502 0.4011 -0.1223 -0.1503 -0.0736 295 HIS C CE1 
6215  N NE2 . HIS C 295 ? 0.5354 0.5707 0.4086 -0.1079 -0.1665 -0.0789 295 HIS C NE2 
6216  N N   . PRO C 296 ? 0.4589 0.5062 0.3844 -0.1380 -0.1181 -0.0478 296 PRO C N   
6217  C CA  . PRO C 296 ? 0.4623 0.5203 0.3770 -0.1526 -0.1037 -0.0427 296 PRO C CA  
6218  C C   . PRO C 296 ? 0.4637 0.5418 0.3835 -0.1490 -0.0944 -0.0507 296 PRO C C   
6219  O O   . PRO C 296 ? 0.4506 0.5618 0.3855 -0.1454 -0.0818 -0.0510 296 PRO C O   
6220  C CB  . PRO C 296 ? 0.5103 0.5312 0.3652 -0.1682 -0.1095 -0.0364 296 PRO C CB  
6221  C CG  . PRO C 296 ? 0.5373 0.5217 0.3679 -0.1507 -0.1276 -0.0416 296 PRO C CG  
6222  C CD  . PRO C 296 ? 0.4987 0.5103 0.3783 -0.1313 -0.1330 -0.0464 296 PRO C CD  
6223  N N   . LEU C 297 ? 0.4862 0.5449 0.3876 -0.1452 -0.1017 -0.0583 297 LEU C N   
6224  C CA  . LEU C 297 ? 0.5009 0.5673 0.3940 -0.1383 -0.0947 -0.0671 297 LEU C CA  
6225  C C   . LEU C 297 ? 0.4976 0.5549 0.4079 -0.1238 -0.0952 -0.0748 297 LEU C C   
6226  O O   . LEU C 297 ? 0.5078 0.5417 0.4166 -0.1267 -0.1066 -0.0802 297 LEU C O   
6227  C CB  . LEU C 297 ? 0.5341 0.5745 0.3930 -0.1419 -0.1037 -0.0721 297 LEU C CB  
6228  C CG  . LEU C 297 ? 0.5633 0.5862 0.3804 -0.1590 -0.1067 -0.0645 297 LEU C CG  
6229  C CD1 . LEU C 297 ? 0.6003 0.5866 0.3812 -0.1560 -0.1205 -0.0700 297 LEU C CD1 
6230  C CD2 . LEU C 297 ? 0.5738 0.6315 0.3741 -0.1770 -0.0899 -0.0606 297 LEU C CD2 
6231  N N   . THR C 298 ? 0.4945 0.5689 0.4115 -0.1098 -0.0840 -0.0758 298 THR C N   
6232  C CA  . THR C 298 ? 0.5175 0.5590 0.4253 -0.0945 -0.0857 -0.0830 298 THR C CA  
6233  C C   . THR C 298 ? 0.5560 0.5981 0.4315 -0.0651 -0.0774 -0.0923 298 THR C C   
6234  O O   . THR C 298 ? 0.5492 0.6431 0.4248 -0.0578 -0.0673 -0.0924 298 THR C O   
6235  C CB  . THR C 298 ? 0.4963 0.5395 0.4274 -0.0936 -0.0840 -0.0769 298 THR C CB  
6236  O OG1 . THR C 298 ? 0.4847 0.5693 0.4235 -0.0755 -0.0720 -0.0742 298 THR C OG1 
6237  C CG2 . THR C 298 ? 0.4583 0.5153 0.4204 -0.1151 -0.0902 -0.0682 298 THR C CG2 
6238  N N   . ILE C 299 ? 0.6072 0.5899 0.4456 -0.0492 -0.0827 -0.1006 299 ILE C N   
6239  C CA  . ILE C 299 ? 0.6650 0.6303 0.4552 -0.0083 -0.0781 -0.1119 299 ILE C CA  
6240  C C   . ILE C 299 ? 0.7128 0.6185 0.4680 0.0134  -0.0820 -0.1145 299 ILE C C   
6241  O O   . ILE C 299 ? 0.7286 0.5755 0.4737 -0.0140 -0.0917 -0.1113 299 ILE C O   
6242  C CB  . ILE C 299 ? 0.7182 0.6350 0.4612 -0.0074 -0.0848 -0.1221 299 ILE C CB  
6243  C CG1 . ILE C 299 ? 0.7981 0.6775 0.4732 0.0438  -0.0826 -0.1360 299 ILE C CG1 
6244  C CG2 . ILE C 299 ? 0.7411 0.5897 0.4685 -0.0434 -0.1001 -0.1220 299 ILE C CG2 
6245  C CD1 . ILE C 299 ? 0.7866 0.7519 0.4685 0.0741  -0.0687 -0.1416 299 ILE C CD1 
6246  N N   . GLY C 300 ? 0.7411 0.6682 0.4737 0.0623  -0.0749 -0.1206 300 GLY C N   
6247  C CA  . GLY C 300 ? 0.8079 0.6656 0.4874 0.0951  -0.0803 -0.1246 300 GLY C CA  
6248  C C   . GLY C 300 ? 0.7584 0.6751 0.4836 0.1020  -0.0739 -0.1161 300 GLY C C   
6249  O O   . GLY C 300 ? 0.6798 0.7004 0.4715 0.0885  -0.0637 -0.1090 300 GLY C O   
6250  N N   . GLU C 301 ? 0.8164 0.6571 0.4952 0.1196  -0.0811 -0.1167 301 GLU C N   
6251  C CA  . GLU C 301 ? 0.7804 0.6634 0.4934 0.1286  -0.0769 -0.1092 301 GLU C CA  
6252  C C   . GLU C 301 ? 0.7137 0.6006 0.4844 0.0668  -0.0779 -0.0947 301 GLU C C   
6253  O O   . GLU C 301 ? 0.7531 0.5552 0.4913 0.0407  -0.0866 -0.0921 301 GLU C O   
6254  C CB  . GLU C 301 ? 0.8850 0.6715 0.5097 0.1769  -0.0860 -0.1163 301 GLU C CB  
6255  C CG  . GLU C 301 ? 0.8571 0.6959 0.5092 0.2017  -0.0821 -0.1113 301 GLU C CG  
6256  C CD  . GLU C 301 ? 0.8222 0.7964 0.5083 0.2525  -0.0718 -0.1181 301 GLU C CD  
6257  O OE1 . GLU C 301 ? 0.8230 0.8512 0.5086 0.2704  -0.0665 -0.1272 301 GLU C OE1 
6258  O OE2 . GLU C 301 ? 0.7962 0.8308 0.5084 0.2723  -0.0689 -0.1148 301 GLU C OE2 
6259  N N   . CYS C 302 ? 0.6234 0.6082 0.4704 0.0430  -0.0693 -0.0860 302 CYS C N   
6260  C CA  . CYS C 302 ? 0.5650 0.5594 0.4617 -0.0068 -0.0709 -0.0743 302 CYS C CA  
6261  C C   . CYS C 302 ? 0.5062 0.5640 0.4522 -0.0117 -0.0644 -0.0639 302 CYS C C   
6262  O O   . CYS C 302 ? 0.4910 0.6164 0.4492 0.0108  -0.0567 -0.0647 302 CYS C O   
6263  C CB  . CYS C 302 ? 0.5310 0.5560 0.4531 -0.0346 -0.0712 -0.0733 302 CYS C CB  
6264  S SG  . CYS C 302 ? 0.5937 0.5472 0.4643 -0.0406 -0.0808 -0.0841 302 CYS C SG  
6265  N N   . PRO C 303 ? 0.4759 0.5199 0.4484 -0.0430 -0.0677 -0.0550 303 PRO C N   
6266  C CA  . PRO C 303 ? 0.4209 0.5197 0.4374 -0.0540 -0.0627 -0.0445 303 PRO C CA  
6267  C C   . PRO C 303 ? 0.3843 0.5343 0.4241 -0.0740 -0.0598 -0.0403 303 PRO C C   
6268  O O   . PRO C 303 ? 0.3960 0.5363 0.4237 -0.0804 -0.0625 -0.0451 303 PRO C O   
6269  C CB  . PRO C 303 ? 0.4104 0.4750 0.4389 -0.0791 -0.0680 -0.0385 303 PRO C CB  
6270  C CG  . PRO C 303 ? 0.4441 0.4613 0.4480 -0.0952 -0.0756 -0.0449 303 PRO C CG  
6271  C CD  . PRO C 303 ? 0.4986 0.4820 0.4559 -0.0706 -0.0763 -0.0551 303 PRO C CD  
6272  N N   . LYS C 304 ? 0.3521 0.5460 0.4140 -0.0865 -0.0556 -0.0314 304 LYS C N   
6273  C CA  . LYS C 304 ? 0.3411 0.5648 0.4020 -0.1114 -0.0542 -0.0264 304 LYS C CA  
6274  C C   . LYS C 304 ? 0.3358 0.5172 0.3943 -0.1307 -0.0637 -0.0218 304 LYS C C   
6275  O O   . LYS C 304 ? 0.3237 0.4844 0.3959 -0.1310 -0.0681 -0.0184 304 LYS C O   
6276  C CB  . LYS C 304 ? 0.3279 0.6074 0.3964 -0.1244 -0.0478 -0.0186 304 LYS C CB  
6277  C CG  . LYS C 304 ? 0.3327 0.6803 0.4058 -0.0984 -0.0392 -0.0250 304 LYS C CG  
6278  C CD  . LYS C 304 ? 0.3513 0.7481 0.4086 -0.0948 -0.0332 -0.0331 304 LYS C CD  
6279  C CE  . LYS C 304 ? 0.3763 0.7948 0.4239 -0.0419 -0.0304 -0.0468 304 LYS C CE  
6280  N NZ  . LYS C 304 ? 0.3860 0.9074 0.4279 -0.0335 -0.0206 -0.0544 304 LYS C NZ  
6281  N N   . TYR C 305 ? 0.3508 0.5228 0.3870 -0.1431 -0.0673 -0.0226 305 TYR C N   
6282  C CA  . TYR C 305 ? 0.3588 0.4921 0.3816 -0.1499 -0.0789 -0.0206 305 TYR C CA  
6283  C C   . TYR C 305 ? 0.3705 0.4890 0.3697 -0.1659 -0.0820 -0.0102 305 TYR C C   
6284  O O   . TYR C 305 ? 0.3883 0.5194 0.3624 -0.1877 -0.0768 -0.0046 305 TYR C O   
6285  C CB  . TYR C 305 ? 0.3847 0.5008 0.3807 -0.1519 -0.0843 -0.0264 305 TYR C CB  
6286  C CG  . TYR C 305 ? 0.4049 0.4844 0.3768 -0.1500 -0.0988 -0.0256 305 TYR C CG  
6287  C CD1 . TYR C 305 ? 0.3935 0.4744 0.3859 -0.1356 -0.1078 -0.0316 305 TYR C CD1 
6288  C CD2 . TYR C 305 ? 0.4471 0.4912 0.3658 -0.1622 -0.1046 -0.0196 305 TYR C CD2 
6289  C CE1 . TYR C 305 ? 0.4160 0.4797 0.3849 -0.1229 -0.1224 -0.0334 305 TYR C CE1 
6290  C CE2 . TYR C 305 ? 0.4827 0.4831 0.3638 -0.1481 -0.1208 -0.0205 305 TYR C CE2 
6291  C CZ  . TYR C 305 ? 0.4629 0.4812 0.3738 -0.1232 -0.1297 -0.0283 305 TYR C CZ  
6292  O OH  . TYR C 305 ? 0.5012 0.4925 0.3743 -0.0987 -0.1470 -0.0317 305 TYR C OH  
6293  N N   . VAL C 306 ? 0.3685 0.4619 0.3688 -0.1567 -0.0909 -0.0082 306 VAL C N   
6294  C CA  . VAL C 306 ? 0.4008 0.4557 0.3586 -0.1641 -0.0983 0.0000  306 VAL C CA  
6295  C C   . VAL C 306 ? 0.4254 0.4467 0.3604 -0.1402 -0.1137 -0.0046 306 VAL C C   
6296  O O   . VAL C 306 ? 0.3998 0.4495 0.3707 -0.1233 -0.1164 -0.0132 306 VAL C O   
6297  C CB  . VAL C 306 ? 0.3801 0.4467 0.3567 -0.1676 -0.0932 0.0072  306 VAL C CB  
6298  C CG1 . VAL C 306 ? 0.3713 0.4765 0.3540 -0.1911 -0.0812 0.0122  306 VAL C CG1 
6299  C CG2 . VAL C 306 ? 0.3369 0.4308 0.3672 -0.1483 -0.0908 0.0025  306 VAL C CG2 
6300  N N   . LYS C 307 ? 0.4860 0.4466 0.3520 -0.1387 -0.1250 0.0001  307 LYS C N   
6301  C CA  . LYS C 307 ? 0.5257 0.4533 0.3550 -0.1032 -0.1426 -0.0058 307 LYS C CA  
6302  C C   . LYS C 307 ? 0.5120 0.4552 0.3594 -0.0759 -0.1466 -0.0069 307 LYS C C   
6303  O O   . LYS C 307 ? 0.5516 0.4773 0.3631 -0.0380 -0.1619 -0.0130 307 LYS C O   
6304  C CB  . LYS C 307 ? 0.6238 0.4561 0.3452 -0.1061 -0.1564 -0.0010 307 LYS C CB  
6305  C CG  . LYS C 307 ? 0.6530 0.4659 0.3429 -0.1244 -0.1571 -0.0026 307 LYS C CG  
6306  C CD  . LYS C 307 ? 0.7707 0.4711 0.3357 -0.1201 -0.1757 0.0007  307 LYS C CD  
6307  C CE  . LYS C 307 ? 0.8132 0.4835 0.3310 -0.1562 -0.1733 0.0032  307 LYS C CE  
6308  N NZ  . LYS C 307 ? 0.9492 0.4882 0.3243 -0.1561 -0.1934 0.0073  307 LYS C NZ  
6309  N N   . SER C 308 ? 0.4621 0.4415 0.3603 -0.0906 -0.1337 -0.0020 308 SER C N   
6310  C CA  . SER C 308 ? 0.4513 0.4458 0.3638 -0.0692 -0.1357 -0.0021 308 SER C CA  
6311  C C   . SER C 308 ? 0.4144 0.4805 0.3789 -0.0462 -0.1379 -0.0137 308 SER C C   
6312  O O   . SER C 308 ? 0.3803 0.4885 0.3870 -0.0598 -0.1329 -0.0193 308 SER C O   
6313  C CB  . SER C 308 ? 0.4103 0.4239 0.3611 -0.0935 -0.1214 0.0063  308 SER C CB  
6314  O OG  . SER C 308 ? 0.4293 0.4133 0.3512 -0.1256 -0.1160 0.0152  308 SER C OG  
6315  N N   . ASN C 309 ? 0.4295 0.5113 0.3837 -0.0134 -0.1459 -0.0179 309 ASN C N   
6316  C CA  . ASN C 309 ? 0.3918 0.5656 0.3999 -0.0003 -0.1454 -0.0283 309 ASN C CA  
6317  C C   . ASN C 309 ? 0.3429 0.5543 0.4037 -0.0247 -0.1305 -0.0234 309 ASN C C   
6318  O O   . ASN C 309 ? 0.3099 0.5938 0.4179 -0.0377 -0.1255 -0.0296 309 ASN C O   
6319  C CB  . ASN C 309 ? 0.4361 0.6284 0.4058 0.0542  -0.1615 -0.0378 309 ASN C CB  
6320  C CG  . ASN C 309 ? 0.4870 0.6613 0.4083 0.0857  -0.1789 -0.0468 309 ASN C CG  
6321  O OD1 . ASN C 309 ? 0.4623 0.6772 0.4153 0.0690  -0.1783 -0.0525 309 ASN C OD1 
6322  N ND2 . ASN C 309 ? 0.5703 0.6733 0.4031 0.1334  -0.1961 -0.0484 309 ASN C ND2 
6323  N N   . ARG C 310 ? 0.3468 0.5069 0.3922 -0.0352 -0.1243 -0.0120 310 ARG C N   
6324  C CA  . ARG C 310 ? 0.3114 0.4967 0.3948 -0.0509 -0.1125 -0.0070 310 ARG C CA  
6325  C C   . ARG C 310 ? 0.3076 0.4419 0.3819 -0.0737 -0.1044 0.0054  310 ARG C C   
6326  O O   . ARG C 310 ? 0.3464 0.4244 0.3699 -0.0696 -0.1100 0.0117  310 ARG C O   
6327  C CB  . ARG C 310 ? 0.3281 0.5378 0.3990 -0.0183 -0.1179 -0.0105 310 ARG C CB  
6328  C CG  . ARG C 310 ? 0.2923 0.5489 0.4068 -0.0340 -0.1062 -0.0083 310 ARG C CG  
6329  C CD  . ARG C 310 ? 0.3132 0.5977 0.4104 0.0029  -0.1112 -0.0125 310 ARG C CD  
6330  N NE  . ARG C 310 ? 0.2927 0.5803 0.4102 -0.0137 -0.0999 -0.0050 310 ARG C NE  
6331  C CZ  . ARG C 310 ? 0.2604 0.6148 0.4231 -0.0379 -0.0893 -0.0070 310 ARG C CZ  
6332  N NH1 . ARG C 310 ? 0.2458 0.6759 0.4387 -0.0545 -0.0881 -0.0165 310 ARG C NH1 
6333  N NH2 . ARG C 310 ? 0.2508 0.5928 0.4211 -0.0507 -0.0804 0.0007  310 ARG C NH2 
6334  N N   . LEU C 311 ? 0.2713 0.4240 0.3853 -0.0980 -0.0927 0.0082  311 LEU C N   
6335  C CA  . LEU C 311 ? 0.2632 0.3929 0.3771 -0.1135 -0.0850 0.0180  311 LEU C CA  
6336  C C   . LEU C 311 ? 0.2374 0.3881 0.3842 -0.1212 -0.0763 0.0198  311 LEU C C   
6337  O O   . LEU C 311 ? 0.2288 0.3888 0.3938 -0.1318 -0.0714 0.0165  311 LEU C O   
6338  C CB  . LEU C 311 ? 0.2620 0.3856 0.3744 -0.1277 -0.0812 0.0186  311 LEU C CB  
6339  C CG  . LEU C 311 ? 0.2942 0.3906 0.3652 -0.1314 -0.0877 0.0193  311 LEU C CG  
6340  C CD1 . LEU C 311 ? 0.2862 0.3993 0.3662 -0.1446 -0.0810 0.0179  311 LEU C CD1 
6341  C CD2 . LEU C 311 ? 0.3311 0.3867 0.3535 -0.1397 -0.0922 0.0284  311 LEU C CD2 
6342  N N   . VAL C 312 ? 0.2373 0.3835 0.3797 -0.1158 -0.0757 0.0251  312 VAL C N   
6343  C CA  . VAL C 312 ? 0.2209 0.3806 0.3860 -0.1237 -0.0680 0.0277  312 VAL C CA  
6344  C C   . VAL C 312 ? 0.2209 0.3575 0.3765 -0.1264 -0.0653 0.0375  312 VAL C C   
6345  O O   . VAL C 312 ? 0.2383 0.3543 0.3672 -0.1201 -0.0702 0.0420  312 VAL C O   
6346  C CB  . VAL C 312 ? 0.2203 0.4154 0.3935 -0.1153 -0.0688 0.0231  312 VAL C CB  
6347  C CG1 . VAL C 312 ? 0.2122 0.4176 0.4018 -0.1322 -0.0601 0.0262  312 VAL C CG1 
6348  C CG2 . VAL C 312 ? 0.2215 0.4589 0.4037 -0.1133 -0.0732 0.0122  312 VAL C CG2 
6349  N N   . LEU C 313 ? 0.2119 0.3472 0.3801 -0.1341 -0.0593 0.0402  313 LEU C N   
6350  C CA  . LEU C 313 ? 0.2105 0.3388 0.3742 -0.1356 -0.0572 0.0483  313 LEU C CA  
6351  C C   . LEU C 313 ? 0.2089 0.3327 0.3788 -0.1355 -0.0536 0.0514  313 LEU C C   
6352  O O   . LEU C 313 ? 0.2138 0.3359 0.3900 -0.1404 -0.0500 0.0480  313 LEU C O   
6353  C CB  . LEU C 313 ? 0.2103 0.3477 0.3777 -0.1333 -0.0545 0.0475  313 LEU C CB  
6354  C CG  . LEU C 313 ? 0.2116 0.3693 0.3716 -0.1374 -0.0561 0.0466  313 LEU C CG  
6355  C CD1 . LEU C 313 ? 0.2155 0.3950 0.3798 -0.1236 -0.0532 0.0415  313 LEU C CD1 
6356  C CD2 . LEU C 313 ? 0.2183 0.3831 0.3608 -0.1529 -0.0585 0.0548  313 LEU C CD2 
6357  N N   . ALA C 314 ? 0.2118 0.3273 0.3708 -0.1344 -0.0548 0.0582  314 ALA C N   
6358  C CA  . ALA C 314 ? 0.2119 0.3225 0.3744 -0.1345 -0.0509 0.0623  314 ALA C CA  
6359  C C   . ALA C 314 ? 0.2149 0.3192 0.3798 -0.1346 -0.0483 0.0649  314 ALA C C   
6360  O O   . ALA C 314 ? 0.2134 0.3290 0.3758 -0.1319 -0.0506 0.0670  314 ALA C O   
6361  C CB  . ALA C 314 ? 0.2225 0.3183 0.3641 -0.1315 -0.0543 0.0686  314 ALA C CB  
6362  N N   . THR C 315 ? 0.2289 0.3170 0.3908 -0.1376 -0.0445 0.0638  315 THR C N   
6363  C CA  . THR C 315 ? 0.2516 0.3153 0.3975 -0.1294 -0.0446 0.0662  315 THR C CA  
6364  C C   . THR C 315 ? 0.2583 0.3088 0.3974 -0.1333 -0.0423 0.0729  315 THR C C   
6365  O O   . THR C 315 ? 0.2634 0.3106 0.3954 -0.1223 -0.0447 0.0776  315 THR C O   
6366  C CB  . THR C 315 ? 0.2917 0.3163 0.4114 -0.1314 -0.0445 0.0605  315 THR C CB  
6367  O OG1 . THR C 315 ? 0.2989 0.3219 0.4178 -0.1574 -0.0408 0.0580  315 THR C OG1 
6368  C CG2 . THR C 315 ? 0.2937 0.3257 0.4125 -0.1182 -0.0478 0.0538  315 THR C CG2 
6369  N N   . GLY C 316 ? 0.2595 0.3125 0.4008 -0.1485 -0.0377 0.0725  316 GLY C N   
6370  C CA  . GLY C 316 ? 0.2674 0.3129 0.4014 -0.1537 -0.0341 0.0781  316 GLY C CA  
6371  C C   . GLY C 316 ? 0.2463 0.3116 0.3894 -0.1447 -0.0358 0.0818  316 GLY C C   
6372  O O   . GLY C 316 ? 0.2343 0.3078 0.3800 -0.1376 -0.0411 0.0817  316 GLY C O   
6373  N N   . LEU C 317 ? 0.2538 0.3191 0.3907 -0.1474 -0.0318 0.0850  317 LEU C N   
6374  C CA  . LEU C 317 ? 0.2527 0.3181 0.3808 -0.1361 -0.0347 0.0886  317 LEU C CA  
6375  C C   . LEU C 317 ? 0.2552 0.3515 0.3834 -0.1268 -0.0321 0.0822  317 LEU C C   
6376  O O   . LEU C 317 ? 0.2504 0.3838 0.3937 -0.1351 -0.0268 0.0753  317 LEU C O   
6377  C CB  . LEU C 317 ? 0.2651 0.3073 0.3795 -0.1377 -0.0338 0.0966  317 LEU C CB  
6378  C CG  . LEU C 317 ? 0.2819 0.3168 0.3904 -0.1500 -0.0258 0.0977  317 LEU C CG  
6379  C CD1 . LEU C 317 ? 0.2841 0.3498 0.3925 -0.1506 -0.0188 0.0948  317 LEU C CD1 
6380  C CD2 . LEU C 317 ? 0.2996 0.2993 0.3900 -0.1479 -0.0285 0.1055  317 LEU C CD2 
6381  N N   . ARG C 318 ? 0.2726 0.3543 0.3760 -0.1084 -0.0373 0.0835  318 ARG C N   
6382  C CA  . ARG C 318 ? 0.2887 0.3988 0.3798 -0.0838 -0.0377 0.0754  318 ARG C CA  
6383  C C   . ARG C 318 ? 0.2850 0.4479 0.3938 -0.0900 -0.0262 0.0719  318 ARG C C   
6384  O O   . ARG C 318 ? 0.2923 0.4391 0.3940 -0.0986 -0.0214 0.0782  318 ARG C O   
6385  C CB  . ARG C 318 ? 0.3298 0.3879 0.3681 -0.0603 -0.0473 0.0783  318 ARG C CB  
6386  C CG  . ARG C 318 ? 0.3632 0.4401 0.3710 -0.0191 -0.0507 0.0682  318 ARG C CG  
6387  C CD  . ARG C 318 ? 0.4272 0.4234 0.3599 0.0036  -0.0624 0.0719  318 ARG C CD  
6388  N NE  . ARG C 318 ? 0.4672 0.3915 0.3498 0.0002  -0.0762 0.0748  318 ARG C NE  
6389  C CZ  . ARG C 318 ? 0.5230 0.4126 0.3485 0.0349  -0.0883 0.0670  318 ARG C CZ  
6390  N NH1 . ARG C 318 ? 0.5411 0.4748 0.3575 0.0848  -0.0890 0.0540  318 ARG C NH1 
6391  N NH2 . ARG C 318 ? 0.5688 0.3823 0.3394 0.0204  -0.1006 0.0715  318 ARG C NH2 
6392  N N   . ASN C 319 ? 0.2788 0.5106 0.4079 -0.0894 -0.0220 0.0615  319 ASN C N   
6393  C CA  . ASN C 319 ? 0.2794 0.5805 0.4248 -0.1086 -0.0100 0.0572  319 ASN C CA  
6394  C C   . ASN C 319 ? 0.2984 0.6530 0.4299 -0.0720 -0.0084 0.0497  319 ASN C C   
6395  O O   . ASN C 319 ? 0.3146 0.6800 0.4276 -0.0272 -0.0176 0.0415  319 ASN C O   
6396  C CB  . ASN C 319 ? 0.2676 0.6302 0.4382 -0.1341 -0.0066 0.0490  319 ASN C CB  
6397  C CG  . ASN C 319 ? 0.2773 0.7026 0.4551 -0.1767 0.0062  0.0469  319 ASN C CG  
6398  O OD1 . ASN C 319 ? 0.2911 0.7074 0.4561 -0.1883 0.0134  0.0524  319 ASN C OD1 
6399  N ND2 . ASN C 319 ? 0.2768 0.7653 0.4691 -0.2061 0.0088  0.0390  319 ASN C ND2 
6400  N N   . SER C 320 ? 0.3085 0.6918 0.4399 -0.0880 0.0023  0.0518  320 SER C N   
6401  C CA  . SER C 320 ? 0.3315 0.7621 0.4446 -0.0500 0.0049  0.0451  320 SER C CA  
6402  C C   . SER C 320 ? 0.3309 0.9013 0.4646 -0.0371 0.0111  0.0286  320 SER C C   
6403  O O   . SER C 320 ? 0.3145 0.9519 0.4793 -0.0811 0.0182  0.0251  320 SER C O   
6404  C CB  . SER C 320 ? 0.3412 0.7502 0.4449 -0.0745 0.0149  0.0542  320 SER C CB  
6405  O OG  . SER C 320 ? 0.3452 0.6418 0.4306 -0.0820 0.0078  0.0679  320 SER C OG  
6406  N N   . PRO C 321 ? 0.3595 0.9759 0.4683 0.0250  0.0070  0.0173  321 PRO C N   
6407  C CA  . PRO C 321 ? 0.3614 1.1361 0.4881 0.0481  0.0130  -0.0008 321 PRO C CA  
6408  C C   . PRO C 321 ? 0.3659 1.2261 0.5002 0.0279  0.0300  -0.0024 321 PRO C C   
6409  O O   . PRO C 321 ? 0.3496 1.2475 0.5106 -0.0448 0.0437  0.0033  321 PRO C O   
6410  C CB  . PRO C 321 ? 0.4064 1.1625 0.4829 0.1392  -0.0033 -0.0124 321 PRO C CB  
6411  C CG  . PRO C 321 ? 0.4407 1.0428 0.4634 0.1540  -0.0110 0.0008  321 PRO C CG  
6412  C CD  . PRO C 321 ? 0.4031 0.9180 0.4530 0.0824  -0.0069 0.0194  321 PRO C CD  
6413  N N   . GLY D 1   ? 0.3459 0.2347 0.2826 0.0460  0.0402  0.0648  1   GLY D N   
6414  C CA  . GLY D 1   ? 0.3165 0.2173 0.2759 0.0177  0.0245  0.0511  1   GLY D CA  
6415  C C   . GLY D 1   ? 0.3492 0.2054 0.2686 -0.0049 0.0230  0.0411  1   GLY D C   
6416  O O   . GLY D 1   ? 0.3920 0.2037 0.2679 -0.0044 0.0313  0.0424  1   GLY D O   
6417  N N   . LEU D 2   ? 0.3321 0.2043 0.2640 -0.0266 0.0121  0.0323  2   LEU D N   
6418  C CA  . LEU D 2   ? 0.3644 0.2095 0.2585 -0.0552 0.0090  0.0255  2   LEU D CA  
6419  C C   . LEU D 2   ? 0.3689 0.2137 0.2575 -0.0689 0.0042  0.0238  2   LEU D C   
6420  O O   . LEU D 2   ? 0.4180 0.2214 0.2546 -0.0908 0.0064  0.0219  2   LEU D O   
6421  C CB  . LEU D 2   ? 0.3361 0.2219 0.2558 -0.0733 -0.0024 0.0197  2   LEU D CB  
6422  C CG  . LEU D 2   ? 0.3500 0.2219 0.2548 -0.0724 0.0019  0.0193  2   LEU D CG  
6423  C CD1 . LEU D 2   ? 0.3195 0.2404 0.2529 -0.0895 -0.0096 0.0145  2   LEU D CD1 
6424  C CD2 . LEU D 2   ? 0.4252 0.2222 0.2525 -0.0841 0.0133  0.0199  2   LEU D CD2 
6425  N N   . PHE D 3   ? 0.3251 0.2110 0.2604 -0.0585 -0.0025 0.0248  3   PHE D N   
6426  C CA  . PHE D 3   ? 0.3237 0.2182 0.2599 -0.0699 -0.0088 0.0232  3   PHE D CA  
6427  C C   . PHE D 3   ? 0.3442 0.2074 0.2629 -0.0567 0.0000  0.0282  3   PHE D C   
6428  O O   . PHE D 3   ? 0.3500 0.2114 0.2622 -0.0658 -0.0036 0.0273  3   PHE D O   
6429  C CB  . PHE D 3   ? 0.2756 0.2270 0.2610 -0.0674 -0.0217 0.0210  3   PHE D CB  
6430  C CG  . PHE D 3   ? 0.2643 0.2493 0.2588 -0.0796 -0.0290 0.0177  3   PHE D CG  
6431  C CD1 . PHE D 3   ? 0.2771 0.2839 0.2569 -0.1032 -0.0353 0.0173  3   PHE D CD1 
6432  C CD2 . PHE D 3   ? 0.2455 0.2434 0.2593 -0.0698 -0.0292 0.0167  3   PHE D CD2 
6433  C CE1 . PHE D 3   ? 0.2685 0.3171 0.2566 -0.1148 -0.0412 0.0171  3   PHE D CE1 
6434  C CE2 . PHE D 3   ? 0.2379 0.2676 0.2579 -0.0797 -0.0345 0.0146  3   PHE D CE2 
6435  C CZ  . PHE D 3   ? 0.2488 0.3067 0.2569 -0.1015 -0.0402 0.0153  3   PHE D CZ  
6436  N N   . GLY D 4   ? 0.3572 0.2011 0.2674 -0.0333 0.0123  0.0350  4   GLY D N   
6437  C CA  . GLY D 4   ? 0.3929 0.2006 0.2713 -0.0164 0.0255  0.0423  4   GLY D CA  
6438  C C   . GLY D 4   ? 0.3621 0.2027 0.2764 -0.0064 0.0228  0.0472  4   GLY D C   
6439  O O   . GLY D 4   ? 0.3909 0.2071 0.2802 0.0068  0.0335  0.0537  4   GLY D O   
6440  N N   . ALA D 5   ? 0.3131 0.2030 0.2782 -0.0121 0.0096  0.0448  5   ALA D N   
6441  C CA  . ALA D 5   ? 0.2916 0.2056 0.2830 -0.0087 0.0053  0.0489  5   ALA D CA  
6442  C C   . ALA D 5   ? 0.2750 0.2222 0.2914 0.0049  0.0088  0.0601  5   ALA D C   
6443  O O   . ALA D 5   ? 0.2856 0.2386 0.2973 0.0177  0.0179  0.0711  5   ALA D O   
6444  C CB  . ALA D 5   ? 0.2654 0.2009 0.2807 -0.0222 -0.0100 0.0410  5   ALA D CB  
6445  N N   . ILE D 6   ? 0.2525 0.2259 0.2933 0.0009  0.0013  0.0588  6   ILE D N   
6446  C CA  . ILE D 6   ? 0.2389 0.2520 0.3024 0.0062  0.0017  0.0706  6   ILE D CA  
6447  C C   . ILE D 6   ? 0.2594 0.2776 0.3079 0.0295  0.0179  0.0833  6   ILE D C   
6448  O O   . ILE D 6   ? 0.2778 0.2700 0.3047 0.0379  0.0244  0.0797  6   ILE D O   
6449  C CB  . ILE D 6   ? 0.2183 0.2488 0.3016 -0.0051 -0.0100 0.0654  6   ILE D CB  
6450  C CG1 . ILE D 6   ? 0.2115 0.2346 0.3000 -0.0202 -0.0235 0.0568  6   ILE D CG1 
6451  C CG2 . ILE D 6   ? 0.2103 0.2836 0.3104 -0.0035 -0.0093 0.0791  6   ILE D CG2 
6452  C CD1 . ILE D 6   ? 0.2041 0.2299 0.2989 -0.0276 -0.0337 0.0504  6   ILE D CD1 
6453  N N   . ALA D 7   ? 0.2629 0.3155 0.3183 0.0415  0.0252  0.0997  7   ALA D N   
6454  C CA  . ALA D 7   ? 0.2902 0.3529 0.3258 0.0738  0.0439  0.1159  7   ALA D CA  
6455  C C   . ALA D 7   ? 0.3390 0.3292 0.3202 0.0908  0.0580  0.1097  7   ALA D C   
6456  O O   . ALA D 7   ? 0.3754 0.3424 0.3219 0.1168  0.0728  0.1161  7   ALA D O   
6457  C CB  . ALA D 7   ? 0.2810 0.3781 0.3296 0.0821  0.0445  0.1232  7   ALA D CB  
6458  N N   . GLY D 8   ? 0.3479 0.2981 0.3146 0.0746  0.0533  0.0978  8   GLY D N   
6459  C CA  . GLY D 8   ? 0.4015 0.2764 0.3090 0.0782  0.0629  0.0902  8   GLY D CA  
6460  C C   . GLY D 8   ? 0.4237 0.2795 0.3118 0.0829  0.0690  0.0935  8   GLY D C   
6461  O O   . GLY D 8   ? 0.4449 0.3129 0.3209 0.1121  0.0841  0.1093  8   GLY D O   
6462  N N   . PHE D 9   ? 0.4206 0.2527 0.3058 0.0565  0.0578  0.0805  9   PHE D N   
6463  C CA  . PHE D 9   ? 0.4368 0.2541 0.3080 0.0577  0.0612  0.0828  9   PHE D CA  
6464  C C   . PHE D 9   ? 0.3892 0.2700 0.3156 0.0534  0.0523  0.0892  9   PHE D C   
6465  O O   . PHE D 9   ? 0.3994 0.2824 0.3208 0.0601  0.0575  0.0960  9   PHE D O   
6466  C CB  . PHE D 9   ? 0.4601 0.2281 0.2988 0.0312  0.0536  0.0688  9   PHE D CB  
6467  C CG  . PHE D 9   ? 0.4114 0.2157 0.2942 0.0037  0.0328  0.0583  9   PHE D CG  
6468  C CD1 . PHE D 9   ? 0.3875 0.2146 0.2957 -0.0021 0.0247  0.0582  9   PHE D CD1 
6469  C CD2 . PHE D 9   ? 0.3974 0.2100 0.2890 -0.0132 0.0227  0.0496  9   PHE D CD2 
6470  C CE1 . PHE D 9   ? 0.3549 0.2089 0.2928 -0.0193 0.0081  0.0502  9   PHE D CE1 
6471  C CE2 . PHE D 9   ? 0.3605 0.2087 0.2866 -0.0301 0.0062  0.0424  9   PHE D CE2 
6472  C CZ  . PHE D 9   ? 0.3419 0.2083 0.2885 -0.0308 -0.0005 0.0429  9   PHE D CZ  
6473  N N   . ILE D 10  ? 0.3468 0.2729 0.3179 0.0405  0.0391  0.0874  10  ILE D N   
6474  C CA  . ILE D 10  ? 0.3160 0.2964 0.3266 0.0332  0.0315  0.0960  10  ILE D CA  
6475  C C   . ILE D 10  ? 0.3097 0.3404 0.3370 0.0476  0.0382  0.1120  10  ILE D C   
6476  O O   . ILE D 10  ? 0.2910 0.3399 0.3364 0.0396  0.0305  0.1092  10  ILE D O   
6477  C CB  . ILE D 10  ? 0.2878 0.2740 0.3224 0.0075  0.0120  0.0840  10  ILE D CB  
6478  C CG1 . ILE D 10  ? 0.2960 0.2438 0.3143 -0.0019 0.0059  0.0705  10  ILE D CG1 
6479  C CG2 . ILE D 10  ? 0.2746 0.2969 0.3305 -0.0056 0.0044  0.0926  10  ILE D CG2 
6480  C CD1 . ILE D 10  ? 0.2780 0.2287 0.3106 -0.0163 -0.0097 0.0597  10  ILE D CD1 
6481  N N   . GLU D 11  ? 0.3283 0.3860 0.3480 0.0706  0.0531  0.1303  11  GLU D N   
6482  C CA  . GLU D 11  ? 0.3311 0.4441 0.3599 0.0936  0.0636  0.1500  11  GLU D CA  
6483  C C   . GLU D 11  ? 0.2951 0.4738 0.3661 0.0704  0.0491  0.1561  11  GLU D C   
6484  O O   . GLU D 11  ? 0.2926 0.5035 0.3705 0.0832  0.0529  0.1649  11  GLU D O   
6485  C CB  . GLU D 11  ? 0.3527 0.5049 0.3730 0.1212  0.0806  0.1727  11  GLU D CB  
6486  C CG  . GLU D 11  ? 0.4094 0.5017 0.3722 0.1618  0.1035  0.1755  11  GLU D CG  
6487  C CD  . GLU D 11  ? 0.4320 0.5791 0.3878 0.1985  0.1229  0.2029  11  GLU D CD  
6488  O OE1 . GLU D 11  ? 0.4151 0.6021 0.3937 0.1836  0.1183  0.2100  11  GLU D OE1 
6489  O OE2 . GLU D 11  ? 0.4703 0.6229 0.3952 0.2441  0.1433  0.2189  11  GLU D OE2 
6490  N N   . GLY D 12  ? 0.2762 0.4700 0.3675 0.0363  0.0330  0.1525  12  GLY D N   
6491  C CA  . GLY D 12  ? 0.2574 0.5043 0.3748 0.0077  0.0186  0.1597  12  GLY D CA  
6492  C C   . GLY D 12  ? 0.2540 0.4690 0.3706 -0.0302 -0.0005 0.1454  12  GLY D C   
6493  O O   . GLY D 12  ? 0.2615 0.4293 0.3643 -0.0336 -0.0026 0.1336  12  GLY D O   
6494  N N   . GLY D 13  ? 0.2500 0.4868 0.3745 -0.0572 -0.0139 0.1471  13  GLY D N   
6495  C CA  . GLY D 13  ? 0.2637 0.4603 0.3722 -0.0913 -0.0310 0.1354  13  GLY D CA  
6496  C C   . GLY D 13  ? 0.2833 0.5038 0.3828 -0.1212 -0.0369 0.1486  13  GLY D C   
6497  O O   . GLY D 13  ? 0.2801 0.5623 0.3935 -0.1160 -0.0280 0.1685  13  GLY D O   
6498  N N   . TRP D 14  ? 0.3113 0.4804 0.3811 -0.1513 -0.0511 0.1386  14  TRP D N   
6499  C CA  . TRP D 14  ? 0.3426 0.5138 0.3896 -0.1859 -0.0583 0.1484  14  TRP D CA  
6500  C C   . TRP D 14  ? 0.3789 0.5507 0.3976 -0.2332 -0.0740 0.1546  14  TRP D C   
6501  O O   . TRP D 14  ? 0.4116 0.5090 0.3917 -0.2453 -0.0841 0.1391  14  TRP D O   
6502  C CB  . TRP D 14  ? 0.3650 0.4568 0.3819 -0.1818 -0.0607 0.1319  14  TRP D CB  
6503  C CG  . TRP D 14  ? 0.3404 0.4309 0.3759 -0.1466 -0.0475 0.1281  14  TRP D CG  
6504  C CD1 . TRP D 14  ? 0.3173 0.4638 0.3803 -0.1254 -0.0333 0.1417  14  TRP D CD1 
6505  C CD2 . TRP D 14  ? 0.3458 0.3736 0.3657 -0.1289 -0.0470 0.1111  14  TRP D CD2 
6506  N NE1 . TRP D 14  ? 0.3130 0.4252 0.3733 -0.0992 -0.0245 0.1323  14  TRP D NE1 
6507  C CE2 . TRP D 14  ? 0.3257 0.3715 0.3636 -0.1033 -0.0337 0.1140  14  TRP D CE2 
6508  C CE3 . TRP D 14  ? 0.3711 0.3311 0.3590 -0.1297 -0.0558 0.0952  14  TRP D CE3 
6509  C CZ2 . TRP D 14  ? 0.3267 0.3287 0.3545 -0.0859 -0.0311 0.1014  14  TRP D CZ2 
6510  C CZ3 . TRP D 14  ? 0.3676 0.2951 0.3510 -0.1071 -0.0523 0.0845  14  TRP D CZ3 
6511  C CH2 . TRP D 14  ? 0.3439 0.2943 0.3486 -0.0892 -0.0412 0.0874  14  TRP D CH2 
6512  N N   . GLN D 15  ? 0.3797 0.6367 0.4119 -0.2601 -0.0757 0.1790  15  GLN D N   
6513  C CA  . GLN D 15  ? 0.4265 0.6902 0.4225 -0.3188 -0.0924 0.1893  15  GLN D CA  
6514  C C   . GLN D 15  ? 0.4897 0.6627 0.4216 -0.3533 -0.1029 0.1799  15  GLN D C   
6515  O O   . GLN D 15  ? 0.5497 0.6656 0.4241 -0.3953 -0.1172 0.1761  15  GLN D O   
6516  C CB  . GLN D 15  ? 0.4171 0.8062 0.4406 -0.3438 -0.0916 0.2221  15  GLN D CB  
6517  C CG  . GLN D 15  ? 0.3672 0.8537 0.4450 -0.3089 -0.0804 0.2370  15  GLN D CG  
6518  C CD  . GLN D 15  ? 0.3773 0.8898 0.4499 -0.3369 -0.0925 0.2420  15  GLN D CD  
6519  O OE1 . GLN D 15  ? 0.3471 0.8668 0.4449 -0.3018 -0.0861 0.2361  15  GLN D OE1 
6520  N NE2 . GLN D 15  ? 0.4267 0.9504 0.4611 -0.4035 -0.1103 0.2536  15  GLN D NE2 
6521  N N   . GLY D 16  ? 0.4838 0.6372 0.4182 -0.3348 -0.0951 0.1766  16  GLY D N   
6522  C CA  . GLY D 16  ? 0.5453 0.6131 0.4178 -0.3612 -0.1027 0.1690  16  GLY D CA  
6523  C C   . GLY D 16  ? 0.5822 0.5278 0.4052 -0.3425 -0.1062 0.1431  16  GLY D C   
6524  O O   . GLY D 16  ? 0.6490 0.5118 0.4061 -0.3636 -0.1127 0.1374  16  GLY D O   
6525  N N   . MET D 17  ? 0.5445 0.4791 0.3944 -0.3013 -0.1011 0.1288  17  MET D N   
6526  C CA  . MET D 17  ? 0.5786 0.4136 0.3843 -0.2787 -0.1033 0.1075  17  MET D CA  
6527  C C   . MET D 17  ? 0.6126 0.4138 0.3844 -0.2944 -0.1119 0.1029  17  MET D C   
6528  O O   . MET D 17  ? 0.5655 0.4069 0.3799 -0.2737 -0.1086 0.1002  17  MET D O   
6529  C CB  . MET D 17  ? 0.5195 0.3649 0.3727 -0.2233 -0.0919 0.0951  17  MET D CB  
6530  C CG  . MET D 17  ? 0.5528 0.3140 0.3646 -0.1953 -0.0929 0.0774  17  MET D CG  
6531  S SD  . MET D 17  ? 0.4881 0.2765 0.3532 -0.1422 -0.0817 0.0670  17  MET D SD  
6532  C CE  . MET D 17  ? 0.4266 0.2867 0.3506 -0.1354 -0.0774 0.0697  17  MET D CE  
6533  N N   . VAL D 18  ? 0.7030 0.4209 0.3895 -0.3312 -0.1226 0.1018  18  VAL D N   
6534  C CA  . VAL D 18  ? 0.7543 0.4305 0.3918 -0.3566 -0.1320 0.0996  18  VAL D CA  
6535  C C   . VAL D 18  ? 0.8139 0.3749 0.3841 -0.3254 -0.1311 0.0807  18  VAL D C   
6536  O O   . VAL D 18  ? 0.8441 0.3724 0.3834 -0.3305 -0.1355 0.0761  18  VAL D O   
6537  C CB  . VAL D 18  ? 0.8331 0.4932 0.4054 -0.4303 -0.1459 0.1146  18  VAL D CB  
6538  C CG1 . VAL D 18  ? 0.7771 0.5649 0.4154 -0.4579 -0.1457 0.1374  18  VAL D CG1 
6539  C CG2 . VAL D 18  ? 0.9395 0.4750 0.4077 -0.4493 -0.1502 0.1086  18  VAL D CG2 
6540  N N   . ASP D 19  ? 0.8324 0.3367 0.3789 -0.2899 -0.1246 0.0712  19  ASP D N   
6541  C CA  . ASP D 19  ? 0.9018 0.2982 0.3741 -0.2542 -0.1219 0.0570  19  ASP D CA  
6542  C C   . ASP D 19  ? 0.8307 0.2654 0.3629 -0.1919 -0.1119 0.0468  19  ASP D C   
6543  O O   . ASP D 19  ? 0.8754 0.2437 0.3595 -0.1512 -0.1070 0.0378  19  ASP D O   
6544  C CB  . ASP D 19  ? 0.9820 0.2874 0.3772 -0.2505 -0.1207 0.0550  19  ASP D CB  
6545  C CG  . ASP D 19  ? 0.9122 0.2819 0.3748 -0.2314 -0.1143 0.0579  19  ASP D CG  
6546  O OD1 . ASP D 19  ? 0.8109 0.2893 0.3718 -0.2257 -0.1106 0.0624  19  ASP D OD1 
6547  O OD2 . ASP D 19  ? 0.9670 0.2712 0.3762 -0.2211 -0.1122 0.0560  19  ASP D OD2 
6548  N N   . GLY D 20  ? 0.7278 0.2690 0.3580 -0.1842 -0.1083 0.0499  20  GLY D N   
6549  C CA  . GLY D 20  ? 0.6649 0.2458 0.3485 -0.1356 -0.1002 0.0416  20  GLY D CA  
6550  C C   . GLY D 20  ? 0.5712 0.2534 0.3447 -0.1365 -0.0968 0.0460  20  GLY D C   
6551  O O   . GLY D 20  ? 0.5469 0.2798 0.3498 -0.1668 -0.0988 0.0570  20  GLY D O   
6552  N N   . TRP D 21  ? 0.5249 0.2369 0.3367 -0.1017 -0.0910 0.0389  21  TRP D N   
6553  C CA  . TRP D 21  ? 0.4482 0.2405 0.3324 -0.0977 -0.0862 0.0417  21  TRP D CA  
6554  C C   . TRP D 21  ? 0.4010 0.2344 0.3282 -0.0835 -0.0788 0.0433  21  TRP D C   
6555  O O   . TRP D 21  ? 0.3601 0.2464 0.3290 -0.0904 -0.0743 0.0506  21  TRP D O   
6556  C CB  . TRP D 21  ? 0.4289 0.2302 0.3267 -0.0738 -0.0839 0.0338  21  TRP D CB  
6557  C CG  . TRP D 21  ? 0.4393 0.2416 0.3298 -0.0926 -0.0888 0.0357  21  TRP D CG  
6558  C CD1 . TRP D 21  ? 0.4350 0.2675 0.3360 -0.1264 -0.0933 0.0462  21  TRP D CD1 
6559  C CD2 . TRP D 21  ? 0.4551 0.2352 0.3273 -0.0779 -0.0895 0.0285  21  TRP D CD2 
6560  N NE1 . TRP D 21  ? 0.4481 0.2751 0.3371 -0.1361 -0.0979 0.0453  21  TRP D NE1 
6561  C CE2 . TRP D 21  ? 0.4613 0.2516 0.3314 -0.1064 -0.0953 0.0336  21  TRP D CE2 
6562  C CE3 . TRP D 21  ? 0.4660 0.2255 0.3231 -0.0424 -0.0854 0.0202  21  TRP D CE3 
6563  C CZ2 . TRP D 21  ? 0.4792 0.2497 0.3303 -0.1013 -0.0973 0.0286  21  TRP D CZ2 
6564  C CZ3 . TRP D 21  ? 0.4835 0.2271 0.3225 -0.0347 -0.0863 0.0161  21  TRP D CZ3 
6565  C CH2 . TRP D 21  ? 0.4905 0.2347 0.3257 -0.0645 -0.0922 0.0193  21  TRP D CH2 
6566  N N   . TYR D 22  ? 0.4130 0.2204 0.3243 -0.0612 -0.0769 0.0375  22  TYR D N   
6567  C CA  . TYR D 22  ? 0.3791 0.2159 0.3205 -0.0505 -0.0711 0.0385  22  TYR D CA  
6568  C C   . TYR D 22  ? 0.4201 0.2143 0.3240 -0.0495 -0.0729 0.0390  22  TYR D C   
6569  O O   . TYR D 22  ? 0.4745 0.2122 0.3261 -0.0420 -0.0767 0.0357  22  TYR D O   
6570  C CB  . TYR D 22  ? 0.3477 0.2107 0.3125 -0.0245 -0.0671 0.0320  22  TYR D CB  
6571  C CG  . TYR D 22  ? 0.3323 0.2116 0.3091 -0.0191 -0.0674 0.0284  22  TYR D CG  
6572  C CD1 . TYR D 22  ? 0.2994 0.2121 0.3078 -0.0308 -0.0646 0.0314  22  TYR D CD1 
6573  C CD2 . TYR D 22  ? 0.3550 0.2166 0.3080 0.0016  -0.0692 0.0234  22  TYR D CD2 
6574  C CE1 . TYR D 22  ? 0.2873 0.2129 0.3051 -0.0263 -0.0648 0.0280  22  TYR D CE1 
6575  C CE2 . TYR D 22  ? 0.3421 0.2200 0.3056 0.0067  -0.0690 0.0205  22  TYR D CE2 
6576  C CZ  . TYR D 22  ? 0.3070 0.2156 0.3038 -0.0094 -0.0674 0.0222  22  TYR D CZ  
6577  O OH  . TYR D 22  ? 0.2960 0.2188 0.3016 -0.0049 -0.0672 0.0193  22  TYR D OH  
6578  N N   . GLY D 23  ? 0.4015 0.2165 0.3252 -0.0543 -0.0692 0.0435  23  GLY D N   
6579  C CA  . GLY D 23  ? 0.4381 0.2155 0.3286 -0.0532 -0.0705 0.0442  23  GLY D CA  
6580  C C   . GLY D 23  ? 0.4120 0.2187 0.3295 -0.0576 -0.0652 0.0494  23  GLY D C   
6581  O O   . GLY D 23  ? 0.3684 0.2187 0.3255 -0.0528 -0.0591 0.0505  23  GLY D O   
6582  N N   . TYR D 24  ? 0.4486 0.2228 0.3355 -0.0666 -0.0670 0.0527  24  TYR D N   
6583  C CA  . TYR D 24  ? 0.4338 0.2258 0.3367 -0.0674 -0.0619 0.0571  24  TYR D CA  
6584  C C   . TYR D 24  ? 0.4525 0.2474 0.3461 -0.0969 -0.0622 0.0683  24  TYR D C   
6585  O O   . TYR D 24  ? 0.4959 0.2582 0.3519 -0.1199 -0.0691 0.0713  24  TYR D O   
6586  C CB  . TYR D 24  ? 0.4595 0.2168 0.3347 -0.0482 -0.0632 0.0521  24  TYR D CB  
6587  C CG  . TYR D 24  ? 0.4581 0.2152 0.3302 -0.0195 -0.0647 0.0446  24  TYR D CG  
6588  C CD1 . TYR D 24  ? 0.4992 0.2171 0.3325 -0.0082 -0.0687 0.0413  24  TYR D CD1 
6589  C CD2 . TYR D 24  ? 0.4231 0.2201 0.3248 -0.0046 -0.0618 0.0424  24  TYR D CD2 
6590  C CE1 . TYR D 24  ? 0.4992 0.2281 0.3300 0.0227  -0.0685 0.0374  24  TYR D CE1 
6591  C CE2 . TYR D 24  ? 0.4213 0.2346 0.3222 0.0186  -0.0637 0.0389  24  TYR D CE2 
6592  C CZ  . TYR D 24  ? 0.4564 0.2409 0.3252 0.0352  -0.0664 0.0371  24  TYR D CZ  
6593  O OH  . TYR D 24  ? 0.4562 0.2674 0.3244 0.0632  -0.0668 0.0365  24  TYR D OH  
6594  N N   . HIS D 25  ? 0.4268 0.2601 0.3489 -0.0974 -0.0545 0.0756  25  HIS D N   
6595  C CA  . HIS D 25  ? 0.4458 0.2905 0.3595 -0.1215 -0.0535 0.0883  25  HIS D CA  
6596  C C   . HIS D 25  ? 0.4461 0.2828 0.3586 -0.1098 -0.0479 0.0882  25  HIS D C   
6597  O O   . HIS D 25  ? 0.4158 0.2760 0.3544 -0.0899 -0.0393 0.0869  25  HIS D O   
6598  C CB  . HIS D 25  ? 0.4176 0.3311 0.3664 -0.1317 -0.0472 0.1028  25  HIS D CB  
6599  C CG  . HIS D 25  ? 0.4377 0.3795 0.3790 -0.1594 -0.0468 0.1195  25  HIS D CG  
6600  N ND1 . HIS D 25  ? 0.4246 0.3983 0.3816 -0.1499 -0.0362 0.1291  25  HIS D ND1 
6601  C CD2 . HIS D 25  ? 0.4742 0.4173 0.3886 -0.1994 -0.0560 0.1295  25  HIS D CD2 
6602  C CE1 . HIS D 25  ? 0.4462 0.4501 0.3933 -0.1808 -0.0384 0.1454  25  HIS D CE1 
6603  N NE2 . HIS D 25  ? 0.4778 0.4643 0.3980 -0.2146 -0.0512 0.1461  25  HIS D NE2 
6604  N N   . HIS D 26  ? 0.4900 0.2862 0.3641 -0.1241 -0.0527 0.0897  26  HIS D N   
6605  C CA  . HIS D 26  ? 0.4963 0.2799 0.3637 -0.1153 -0.0485 0.0900  26  HIS D CA  
6606  C C   . HIS D 26  ? 0.5057 0.3186 0.3743 -0.1395 -0.0445 0.1055  26  HIS D C   
6607  O O   . HIS D 26  ? 0.5255 0.3525 0.3830 -0.1703 -0.0491 0.1155  26  HIS D O   
6608  C CB  . HIS D 26  ? 0.5435 0.2581 0.3616 -0.1080 -0.0557 0.0812  26  HIS D CB  
6609  C CG  . HIS D 26  ? 0.6072 0.2718 0.3700 -0.1378 -0.0628 0.0860  26  HIS D CG  
6610  N ND1 . HIS D 26  ? 0.6485 0.2727 0.3726 -0.1509 -0.0703 0.0834  26  HIS D ND1 
6611  C CD2 . HIS D 26  ? 0.6458 0.2873 0.3765 -0.1604 -0.0637 0.0935  26  HIS D CD2 
6612  C CE1 . HIS D 26  ? 0.7160 0.2882 0.3803 -0.1830 -0.0759 0.0889  26  HIS D CE1 
6613  N NE2 . HIS D 26  ? 0.7138 0.2983 0.3831 -0.1902 -0.0722 0.0954  26  HIS D NE2 
6614  N N   . SER D 27  ? 0.4948 0.3212 0.3750 -0.1274 -0.0359 0.1088  27  SER D N   
6615  C CA  . SER D 27  ? 0.5098 0.3617 0.3858 -0.1471 -0.0315 0.1241  27  SER D CA  
6616  C C   . SER D 27  ? 0.5215 0.3432 0.3833 -0.1337 -0.0275 0.1203  27  SER D C   
6617  O O   . SER D 27  ? 0.4985 0.3195 0.3753 -0.1065 -0.0210 0.1133  27  SER D O   
6618  C CB  . SER D 27  ? 0.4771 0.4084 0.3924 -0.1431 -0.0196 0.1402  27  SER D CB  
6619  O OG  . SER D 27  ? 0.4520 0.3915 0.3864 -0.1084 -0.0070 0.1367  27  SER D OG  
6620  N N   . ASN D 28  ? 0.5645 0.3564 0.3908 -0.1563 -0.0323 0.1249  28  ASN D N   
6621  C CA  . ASN D 28  ? 0.5819 0.3420 0.3896 -0.1467 -0.0297 0.1223  28  ASN D CA  
6622  C C   . ASN D 28  ? 0.6202 0.3824 0.4022 -0.1796 -0.0303 0.1363  28  ASN D C   
6623  O O   . ASN D 28  ? 0.6264 0.4302 0.4122 -0.2097 -0.0315 0.1502  28  ASN D O   
6624  C CB  . ASN D 28  ? 0.6059 0.2985 0.3813 -0.1292 -0.0380 0.1064  28  ASN D CB  
6625  C CG  . ASN D 28  ? 0.6614 0.2959 0.3848 -0.1477 -0.0490 0.1037  28  ASN D CG  
6626  O OD1 . ASN D 28  ? 0.6922 0.3256 0.3938 -0.1835 -0.0523 0.1135  28  ASN D OD1 
6627  N ND2 . ASN D 28  ? 0.6822 0.2672 0.3786 -0.1234 -0.0542 0.0919  28  ASN D ND2 
6628  N N   . GLU D 29  ? 0.6484 0.3716 0.4033 -0.1767 -0.0298 0.1343  29  GLU D N   
6629  C CA  . GLU D 29  ? 0.6882 0.4119 0.4154 -0.2098 -0.0300 0.1479  29  GLU D CA  
6630  C C   . GLU D 29  ? 0.7476 0.4299 0.4223 -0.2528 -0.0425 0.1513  29  GLU D C   
6631  O O   . GLU D 29  ? 0.7711 0.4859 0.4340 -0.2939 -0.0437 0.1679  29  GLU D O   
6632  C CB  . GLU D 29  ? 0.7137 0.3901 0.4143 -0.1971 -0.0283 0.1429  29  GLU D CB  
6633  C CG  . GLU D 29  ? 0.6722 0.3832 0.4103 -0.1647 -0.0158 0.1426  29  GLU D CG  
6634  C CD  . GLU D 29  ? 0.6999 0.3763 0.4110 -0.1617 -0.0136 0.1426  29  GLU D CD  
6635  O OE1 . GLU D 29  ? 0.7514 0.3680 0.4136 -0.1774 -0.0224 0.1398  29  GLU D OE1 
6636  O OE2 . GLU D 29  ? 0.6774 0.3797 0.4094 -0.1423 -0.0024 0.1454  29  GLU D OE2 
6637  N N   . GLN D 30  ? 0.7785 0.3888 0.4156 -0.2441 -0.0514 0.1367  30  GLN D N   
6638  C CA  . GLN D 30  ? 0.8543 0.3986 0.4211 -0.2819 -0.0628 0.1374  30  GLN D CA  
6639  C C   . GLN D 30  ? 0.8424 0.4360 0.4255 -0.3139 -0.0671 0.1463  30  GLN D C   
6640  O O   . GLN D 30  ? 0.9068 0.4710 0.4350 -0.3635 -0.0760 0.1545  30  GLN D O   
6641  C CB  . GLN D 30  ? 0.9000 0.3481 0.4143 -0.2518 -0.0680 0.1202  30  GLN D CB  
6642  C CG  . GLN D 30  ? 0.9329 0.3227 0.4118 -0.2262 -0.0659 0.1142  30  GLN D CG  
6643  C CD  . GLN D 30  ? 0.9031 0.2855 0.4021 -0.1702 -0.0637 0.1008  30  GLN D CD  
6644  O OE1 . GLN D 30  ? 0.8314 0.2797 0.3968 -0.1463 -0.0578 0.0990  30  GLN D OE1 
6645  N NE2 . GLN D 30  ? 0.9664 0.2680 0.4011 -0.1492 -0.0680 0.0928  30  GLN D NE2 
6646  N N   . GLY D 31  ? 0.7669 0.4314 0.4186 -0.2882 -0.0614 0.1453  31  GLY D N   
6647  C CA  . GLY D 31  ? 0.7491 0.4704 0.4228 -0.3132 -0.0648 0.1547  31  GLY D CA  
6648  C C   . GLY D 31  ? 0.6860 0.4391 0.4118 -0.2747 -0.0606 0.1452  31  GLY D C   
6649  O O   . GLY D 31  ? 0.6459 0.3982 0.4015 -0.2315 -0.0534 0.1346  31  GLY D O   
6650  N N   . SER D 32  ? 0.6817 0.4625 0.4139 -0.2947 -0.0659 0.1497  32  SER D N   
6651  C CA  . SER D 32  ? 0.6295 0.4365 0.4046 -0.2634 -0.0630 0.1412  32  SER D CA  
6652  C C   . SER D 32  ? 0.6664 0.4332 0.4046 -0.2857 -0.0744 0.1363  32  SER D C   
6653  O O   . SER D 32  ? 0.7290 0.4663 0.4135 -0.3329 -0.0840 0.1440  32  SER D O   
6654  C CB  . SER D 32  ? 0.5682 0.4828 0.4090 -0.2547 -0.0523 0.1566  32  SER D CB  
6655  O OG  . SER D 32  ? 0.5852 0.5609 0.4235 -0.2989 -0.0559 0.1783  32  SER D OG  
6656  N N   . GLY D 33  ? 0.6341 0.3961 0.3947 -0.2546 -0.0734 0.1240  33  GLY D N   
6657  C CA  . GLY D 33  ? 0.6692 0.3912 0.3945 -0.2704 -0.0829 0.1187  33  GLY D CA  
6658  C C   . GLY D 33  ? 0.6295 0.3519 0.3837 -0.2319 -0.0805 0.1053  33  GLY D C   
6659  O O   . GLY D 33  ? 0.5859 0.3198 0.3748 -0.1917 -0.0731 0.0967  33  GLY D O   
6660  N N   . TYR D 34  ? 0.6502 0.3594 0.3850 -0.2489 -0.0875 0.1042  34  TYR D N   
6661  C CA  . TYR D 34  ? 0.6205 0.3287 0.3763 -0.2178 -0.0863 0.0927  34  TYR D CA  
6662  C C   . TYR D 34  ? 0.6835 0.2936 0.3722 -0.2007 -0.0907 0.0789  34  TYR D C   
6663  O O   . TYR D 34  ? 0.7667 0.3014 0.3782 -0.2279 -0.0978 0.0798  34  TYR D O   
6664  C CB  . TYR D 34  ? 0.6067 0.3622 0.3811 -0.2428 -0.0904 0.1006  34  TYR D CB  
6665  C CG  . TYR D 34  ? 0.5501 0.4105 0.3871 -0.2522 -0.0843 0.1176  34  TYR D CG  
6666  C CD1 . TYR D 34  ? 0.4814 0.4003 0.3811 -0.2155 -0.0735 0.1165  34  TYR D CD1 
6667  C CD2 . TYR D 34  ? 0.5734 0.4745 0.3999 -0.2971 -0.0886 0.1366  34  TYR D CD2 
6668  C CE1 . TYR D 34  ? 0.4419 0.4495 0.3877 -0.2153 -0.0651 0.1337  34  TYR D CE1 
6669  C CE2 . TYR D 34  ? 0.5249 0.5324 0.4073 -0.2981 -0.0809 0.1557  34  TYR D CE2 
6670  C CZ  . TYR D 34  ? 0.4614 0.5181 0.4012 -0.2531 -0.0683 0.1540  34  TYR D CZ  
6671  O OH  . TYR D 34  ? 0.4253 0.5801 0.4100 -0.2453 -0.0580 0.1743  34  TYR D OH  
6672  N N   . ALA D 35  ? 0.6515 0.2623 0.3632 -0.1554 -0.0857 0.0678  35  ALA D N   
6673  C CA  . ALA D 35  ? 0.7053 0.2412 0.3605 -0.1279 -0.0873 0.0574  35  ALA D CA  
6674  C C   . ALA D 35  ? 0.6578 0.2323 0.3545 -0.1011 -0.0848 0.0510  35  ALA D C   
6675  O O   . ALA D 35  ? 0.5888 0.2266 0.3484 -0.0796 -0.0794 0.0492  35  ALA D O   
6676  C CB  . ALA D 35  ? 0.7222 0.2271 0.3577 -0.0945 -0.0833 0.0533  35  ALA D CB  
6677  N N   . ALA D 36  ? 0.7019 0.2334 0.3566 -0.1059 -0.0889 0.0478  36  ALA D N   
6678  C CA  . ALA D 36  ? 0.6649 0.2272 0.3514 -0.0810 -0.0867 0.0420  36  ALA D CA  
6679  C C   . ALA D 36  ? 0.6693 0.2200 0.3471 -0.0303 -0.0814 0.0355  36  ALA D C   
6680  O O   . ALA D 36  ? 0.7384 0.2202 0.3501 -0.0116 -0.0807 0.0344  36  ALA D O   
6681  C CB  . ALA D 36  ? 0.7199 0.2327 0.3552 -0.1003 -0.0924 0.0410  36  ALA D CB  
6682  N N   . ASP D 37  ? 0.6007 0.2216 0.3416 -0.0089 -0.0776 0.0330  37  ASP D N   
6683  C CA  . ASP D 37  ? 0.5990 0.2324 0.3390 0.0355  -0.0735 0.0299  37  ASP D CA  
6684  C C   . ASP D 37  ? 0.6408 0.2397 0.3409 0.0555  -0.0730 0.0268  37  ASP D C   
6685  O O   . ASP D 37  ? 0.6041 0.2384 0.3382 0.0476  -0.0736 0.0248  37  ASP D O   
6686  C CB  . ASP D 37  ? 0.5167 0.2387 0.3328 0.0405  -0.0707 0.0299  37  ASP D CB  
6687  C CG  . ASP D 37  ? 0.5125 0.2660 0.3314 0.0788  -0.0680 0.0304  37  ASP D CG  
6688  O OD1 . ASP D 37  ? 0.5196 0.2769 0.3319 0.0907  -0.0672 0.0333  37  ASP D OD1 
6689  O OD2 . ASP D 37  ? 0.5023 0.2836 0.3304 0.0964  -0.0667 0.0294  37  ASP D OD2 
6690  N N   . LYS D 38  ? 0.7252 0.2490 0.3464 0.0838  -0.0709 0.0268  38  LYS D N   
6691  C CA  . LYS D 38  ? 0.7879 0.2572 0.3496 0.1064  -0.0688 0.0245  38  LYS D CA  
6692  C C   . LYS D 38  ? 0.7400 0.2818 0.3465 0.1419  -0.0640 0.0246  38  LYS D C   
6693  O O   . LYS D 38  ? 0.7401 0.2799 0.3457 0.1389  -0.0643 0.0218  38  LYS D O   
6694  C CB  . LYS D 38  ? 0.9028 0.2664 0.3565 0.1385  -0.0646 0.0260  38  LYS D CB  
6695  C CG  . LYS D 38  ? 0.9890 0.2458 0.3618 0.0966  -0.0702 0.0250  38  LYS D CG  
6696  C CD  . LYS D 38  ? 1.1270 0.2542 0.3689 0.1313  -0.0644 0.0255  38  LYS D CD  
6697  C CE  . LYS D 38  ? 1.1547 0.2632 0.3714 0.1585  -0.0601 0.0296  38  LYS D CE  
6698  N NZ  . LYS D 38  ? 1.2900 0.2802 0.3786 0.2113  -0.0507 0.0318  38  LYS D NZ  
6699  N N   . GLU D 39  ? 0.7020 0.3108 0.3455 0.1718  -0.0603 0.0289  39  GLU D N   
6700  C CA  . GLU D 39  ? 0.6626 0.3509 0.3445 0.2037  -0.0562 0.0321  39  GLU D CA  
6701  C C   . GLU D 39  ? 0.5841 0.3370 0.3370 0.1722  -0.0594 0.0282  39  GLU D C   
6702  O O   . GLU D 39  ? 0.5857 0.3498 0.3371 0.1850  -0.0573 0.0274  39  GLU D O   
6703  C CB  . GLU D 39  ? 0.6353 0.3962 0.3468 0.2294  -0.0541 0.0398  39  GLU D CB  
6704  C CG  . GLU D 39  ? 0.5686 0.4415 0.3456 0.2349  -0.0538 0.0442  39  GLU D CG  
6705  C CD  . GLU D 39  ? 0.5698 0.5135 0.3516 0.2726  -0.0509 0.0563  39  GLU D CD  
6706  O OE1 . GLU D 39  ? 0.5869 0.5168 0.3538 0.2775  -0.0517 0.0594  39  GLU D OE1 
6707  O OE2 . GLU D 39  ? 0.5556 0.5750 0.3556 0.2968  -0.0481 0.0641  39  GLU D OE2 
6708  N N   . SER D 40  ? 0.5219 0.3134 0.3306 0.1348  -0.0632 0.0266  40  SER D N   
6709  C CA  . SER D 40  ? 0.4576 0.3021 0.3243 0.1086  -0.0646 0.0239  40  SER D CA  
6710  C C   . SER D 40  ? 0.4741 0.2752 0.3239 0.0895  -0.0668 0.0199  40  SER D C   
6711  O O   . SER D 40  ? 0.4460 0.2782 0.3214 0.0864  -0.0664 0.0180  40  SER D O   
6712  C CB  . SER D 40  ? 0.4064 0.2860 0.3201 0.0783  -0.0659 0.0242  40  SER D CB  
6713  O OG  . SER D 40  ? 0.4259 0.2584 0.3223 0.0568  -0.0677 0.0243  40  SER D OG  
6714  N N   . THR D 41  ? 0.5236 0.2538 0.3264 0.0737  -0.0698 0.0195  41  THR D N   
6715  C CA  . THR D 41  ? 0.5503 0.2380 0.3276 0.0487  -0.0738 0.0176  41  THR D CA  
6716  C C   . THR D 41  ? 0.5980 0.2485 0.3287 0.0755  -0.0716 0.0148  41  THR D C   
6717  O O   . THR D 41  ? 0.5812 0.2449 0.3270 0.0643  -0.0731 0.0127  41  THR D O   
6718  C CB  . THR D 41  ? 0.6084 0.2264 0.3328 0.0199  -0.0788 0.0197  41  THR D CB  
6719  O OG1 . THR D 41  ? 0.5627 0.2213 0.3318 -0.0026 -0.0796 0.0238  41  THR D OG1 
6720  C CG2 . THR D 41  ? 0.6406 0.2230 0.3362 -0.0146 -0.0850 0.0200  41  THR D CG2 
6721  N N   . GLN D 42  ? 0.6619 0.2647 0.3319 0.1146  -0.0670 0.0158  42  GLN D N   
6722  C CA  . GLN D 42  ? 0.7227 0.2808 0.3345 0.1492  -0.0621 0.0148  42  GLN D CA  
6723  C C   . GLN D 42  ? 0.6594 0.3052 0.3307 0.1698  -0.0583 0.0156  42  GLN D C   
6724  O O   . GLN D 42  ? 0.6786 0.3086 0.3310 0.1771  -0.0568 0.0134  42  GLN D O   
6725  C CB  . GLN D 42  ? 0.8087 0.3039 0.3403 0.1977  -0.0549 0.0185  42  GLN D CB  
6726  C CG  . GLN D 42  ? 0.8956 0.3238 0.3450 0.2399  -0.0473 0.0188  42  GLN D CG  
6727  C CD  . GLN D 42  ? 0.9606 0.2930 0.3462 0.2038  -0.0528 0.0126  42  GLN D CD  
6728  O OE1 . GLN D 42  ? 0.9566 0.2952 0.3449 0.2049  -0.0521 0.0101  42  GLN D OE1 
6729  N NE2 . GLN D 42  ? 1.0227 0.2689 0.3491 0.1671  -0.0590 0.0111  42  GLN D NE2 
6730  N N   . LYS D 43  ? 0.5896 0.3253 0.3274 0.1755  -0.0571 0.0192  43  LYS D N   
6731  C CA  . LYS D 43  ? 0.5279 0.3546 0.3240 0.1841  -0.0548 0.0212  43  LYS D CA  
6732  C C   . LYS D 43  ? 0.4814 0.3237 0.3178 0.1464  -0.0589 0.0157  43  LYS D C   
6733  O O   . LYS D 43  ? 0.4674 0.3394 0.3167 0.1553  -0.0568 0.0153  43  LYS D O   
6734  C CB  . LYS D 43  ? 0.4720 0.3815 0.3227 0.1817  -0.0552 0.0262  43  LYS D CB  
6735  C CG  . LYS D 43  ? 0.4550 0.4494 0.3258 0.2133  -0.0509 0.0346  43  LYS D CG  
6736  C CD  . LYS D 43  ? 0.4594 0.4928 0.3301 0.2334  -0.0500 0.0433  43  LYS D CD  
6737  C CE  . LYS D 43  ? 0.4189 0.5685 0.3323 0.2412  -0.0496 0.0538  43  LYS D CE  
6738  N NZ  . LYS D 43  ? 0.4038 0.5959 0.3335 0.2348  -0.0528 0.0602  43  LYS D NZ  
6739  N N   . ALA D 44  ? 0.4593 0.2858 0.3142 0.1071  -0.0641 0.0132  44  ALA D N   
6740  C CA  . ALA D 44  ? 0.4220 0.2631 0.3102 0.0746  -0.0673 0.0107  44  ALA D CA  
6741  C C   . ALA D 44  ? 0.4712 0.2543 0.3125 0.0714  -0.0696 0.0080  44  ALA D C   
6742  O O   . ALA D 44  ? 0.4485 0.2535 0.3103 0.0646  -0.0699 0.0062  44  ALA D O   
6743  C CB  . ALA D 44  ? 0.3964 0.2407 0.3095 0.0406  -0.0705 0.0124  44  ALA D CB  
6744  N N   . ILE D 45  ? 0.5462 0.2484 0.3169 0.0740  -0.0714 0.0077  45  ILE D N   
6745  C CA  . ILE D 45  ? 0.6138 0.2429 0.3199 0.0675  -0.0740 0.0052  45  ILE D CA  
6746  C C   . ILE D 45  ? 0.6320 0.2628 0.3195 0.1074  -0.0673 0.0035  45  ILE D C   
6747  O O   . ILE D 45  ? 0.6406 0.2586 0.3190 0.0972  -0.0692 0.0009  45  ILE D O   
6748  C CB  . ILE D 45  ? 0.7110 0.2367 0.3258 0.0614  -0.0765 0.0055  45  ILE D CB  
6749  C CG1 . ILE D 45  ? 0.6995 0.2242 0.3275 0.0077  -0.0855 0.0088  45  ILE D CG1 
6750  C CG2 . ILE D 45  ? 0.8076 0.2388 0.3298 0.0690  -0.0763 0.0025  45  ILE D CG2 
6751  C CD1 . ILE D 45  ? 0.7835 0.2216 0.3331 -0.0040 -0.0882 0.0104  45  ILE D CD1 
6752  N N   . ASP D 46  ? 0.6373 0.2914 0.3203 0.1531  -0.0594 0.0066  46  ASP D N   
6753  C CA  . ASP D 46  ? 0.6524 0.3260 0.3216 0.1965  -0.0513 0.0084  46  ASP D CA  
6754  C C   . ASP D 46  ? 0.5699 0.3321 0.3163 0.1821  -0.0523 0.0076  46  ASP D C   
6755  O O   . ASP D 46  ? 0.5845 0.3388 0.3166 0.1909  -0.0501 0.0059  46  ASP D O   
6756  C CB  . ASP D 46  ? 0.6680 0.3734 0.3256 0.2482  -0.0427 0.0162  46  ASP D CB  
6757  C CG  . ASP D 46  ? 0.7669 0.3719 0.3318 0.2731  -0.0392 0.0177  46  ASP D CG  
6758  O OD1 . ASP D 46  ? 0.8380 0.3377 0.3334 0.2514  -0.0429 0.0123  46  ASP D OD1 
6759  O OD2 . ASP D 46  ? 0.7793 0.4099 0.3356 0.3126  -0.0330 0.0253  46  ASP D OD2 
6760  N N   . GLY D 47  ? 0.4922 0.3299 0.3118 0.1597  -0.0550 0.0088  47  GLY D N   
6761  C CA  . GLY D 47  ? 0.4241 0.3369 0.3073 0.1438  -0.0553 0.0084  47  GLY D CA  
6762  C C   . GLY D 47  ? 0.4165 0.3055 0.3053 0.1144  -0.0596 0.0034  47  GLY D C   
6763  O O   . GLY D 47  ? 0.4002 0.3171 0.3039 0.1184  -0.0577 0.0025  47  GLY D O   
6764  N N   . VAL D 48  ? 0.4302 0.2736 0.3063 0.0843  -0.0657 0.0018  48  VAL D N   
6765  C CA  . VAL D 48  ? 0.4250 0.2548 0.3061 0.0535  -0.0710 0.0002  48  VAL D CA  
6766  C C   . VAL D 48  ? 0.4922 0.2575 0.3099 0.0620  -0.0720 -0.0026 48  VAL D C   
6767  O O   . VAL D 48  ? 0.4817 0.2553 0.3090 0.0502  -0.0739 -0.0040 48  VAL D O   
6768  C CB  . VAL D 48  ? 0.4211 0.2375 0.3078 0.0177  -0.0772 0.0033  48  VAL D CB  
6769  C CG1 . VAL D 48  ? 0.4317 0.2341 0.3102 -0.0136 -0.0839 0.0050  48  VAL D CG1 
6770  C CG2 . VAL D 48  ? 0.3555 0.2347 0.3041 0.0100  -0.0745 0.0062  48  VAL D CG2 
6771  N N   . THR D 49  ? 0.5692 0.2638 0.3149 0.0839  -0.0699 -0.0031 49  THR D N   
6772  C CA  . THR D 49  ? 0.6521 0.2683 0.3193 0.0970  -0.0689 -0.0058 49  THR D CA  
6773  C C   . THR D 49  ? 0.6347 0.2927 0.3189 0.1313  -0.0611 -0.0062 49  THR D C   
6774  O O   . THR D 49  ? 0.6459 0.2885 0.3183 0.1215  -0.0629 -0.0089 49  THR D O   
6775  C CB  . THR D 49  ? 0.7516 0.2738 0.3247 0.1234  -0.0649 -0.0054 49  THR D CB  
6776  O OG1 . THR D 49  ? 0.7762 0.2542 0.3265 0.0844  -0.0732 -0.0047 49  THR D OG1 
6777  C CG2 . THR D 49  ? 0.8530 0.2794 0.3286 0.1421  -0.0615 -0.0081 49  THR D CG2 
6778  N N   . ASN D 50  ? 0.6076 0.3256 0.3203 0.1690  -0.0529 -0.0021 50  ASN D N   
6779  C CA  . ASN D 50  ? 0.5882 0.3642 0.3213 0.2012  -0.0451 0.0005  50  ASN D CA  
6780  C C   . ASN D 50  ? 0.5194 0.3530 0.3169 0.1693  -0.0493 -0.0021 50  ASN D C   
6781  O O   . ASN D 50  ? 0.5275 0.3657 0.3170 0.1803  -0.0461 -0.0030 50  ASN D O   
6782  C CB  . ASN D 50  ? 0.5554 0.4122 0.3229 0.2332  -0.0384 0.0085  50  ASN D CB  
6783  C CG  . ASN D 50  ? 0.6314 0.4398 0.3298 0.2802  -0.0310 0.0139  50  ASN D CG  
6784  O OD1 . ASN D 50  ? 0.7151 0.4517 0.3350 0.3150  -0.0241 0.0144  50  ASN D OD1 
6785  N ND2 . ASN D 50  ? 0.6104 0.4525 0.3305 0.2836  -0.0315 0.0185  50  ASN D ND2 
6786  N N   . LYS D 51  ? 0.4589 0.3319 0.3142 0.1328  -0.0552 -0.0028 51  LYS D N   
6787  C CA  . LYS D 51  ? 0.4010 0.3206 0.3108 0.1036  -0.0581 -0.0044 51  LYS D CA  
6788  C C   . LYS D 51  ? 0.4278 0.3017 0.3129 0.0851  -0.0630 -0.0078 51  LYS D C   
6789  O O   . LYS D 51  ? 0.4070 0.3071 0.3110 0.0832  -0.0618 -0.0090 51  LYS D O   
6790  C CB  . LYS D 51  ? 0.3535 0.3000 0.3078 0.0738  -0.0619 -0.0032 51  LYS D CB  
6791  C CG  . LYS D 51  ? 0.3071 0.2856 0.3040 0.0468  -0.0636 -0.0034 51  LYS D CG  
6792  C CD  . LYS D 51  ? 0.2757 0.2713 0.3026 0.0268  -0.0645 -0.0006 51  LYS D CD  
6793  C CE  . LYS D 51  ? 0.2332 0.2773 0.2980 0.0199  -0.0600 0.0002  51  LYS D CE  
6794  N NZ  . LYS D 51  ? 0.2172 0.2727 0.2969 0.0116  -0.0583 0.0027  51  LYS D NZ  
6795  N N   . VAL D 52  ? 0.4778 0.2851 0.3182 0.0674  -0.0692 -0.0086 52  VAL D N   
6796  C CA  . VAL D 52  ? 0.5126 0.2763 0.3217 0.0425  -0.0760 -0.0101 52  VAL D CA  
6797  C C   . VAL D 52  ? 0.5702 0.2907 0.3251 0.0702  -0.0713 -0.0135 52  VAL D C   
6798  O O   . VAL D 52  ? 0.5637 0.2904 0.3242 0.0599  -0.0732 -0.0150 52  VAL D O   
6799  C CB  . VAL D 52  ? 0.5648 0.2660 0.3264 0.0113  -0.0848 -0.0083 52  VAL D CB  
6800  C CG1 . VAL D 52  ? 0.6196 0.2672 0.3298 -0.0173 -0.0931 -0.0086 52  VAL D CG1 
6801  C CG2 . VAL D 52  ? 0.5051 0.2609 0.3256 -0.0166 -0.0888 -0.0028 52  VAL D CG2 
6802  N N   . ASN D 53  ? 0.6311 0.3088 0.3311 0.1092  -0.0639 -0.0136 53  ASN D N   
6803  C CA  . ASN D 53  ? 0.6969 0.3313 0.3363 0.1467  -0.0559 -0.0149 53  ASN D CA  
6804  C C   . ASN D 53  ? 0.6370 0.3596 0.3351 0.1685  -0.0488 -0.0130 53  ASN D C   
6805  O O   . ASN D 53  ? 0.6586 0.3666 0.3350 0.1771  -0.0463 -0.0148 53  ASN D O   
6806  C CB  . ASN D 53  ? 0.7781 0.3523 0.3422 0.1933  -0.0468 -0.0125 53  ASN D CB  
6807  C CG  . ASN D 53  ? 0.8568 0.3283 0.3459 0.1706  -0.0533 -0.0145 53  ASN D CG  
6808  O OD1 . ASN D 53  ? 0.8732 0.3046 0.3464 0.1205  -0.0648 -0.0172 53  ASN D OD1 
6809  N ND2 . ASN D 53  ? 0.9100 0.3423 0.3501 0.2062  -0.0461 -0.0115 53  ASN D ND2 
6810  N N   . SER D 54  ? 0.5681 0.3796 0.3352 0.1736  -0.0461 -0.0089 54  SER D N   
6811  C CA  . SER D 54  ? 0.5116 0.4128 0.3349 0.1826  -0.0410 -0.0058 54  SER D CA  
6812  C C   . SER D 54  ? 0.4766 0.3891 0.3325 0.1475  -0.0468 -0.0101 54  SER D C   
6813  O O   . SER D 54  ? 0.4749 0.4079 0.3327 0.1583  -0.0428 -0.0101 54  SER D O   
6814  C CB  . SER D 54  ? 0.4483 0.4332 0.3327 0.1778  -0.0402 -0.0008 54  SER D CB  
6815  O OG  . SER D 54  ? 0.4751 0.4813 0.3382 0.2194  -0.0327 0.0065  54  SER D OG  
6816  N N   . ILE D 55  ? 0.4527 0.3558 0.3327 0.1084  -0.0554 -0.0122 55  ILE D N   
6817  C CA  . ILE D 55  ? 0.4235 0.3388 0.3322 0.0772  -0.0608 -0.0139 55  ILE D CA  
6818  C C   . ILE D 55  ? 0.4792 0.3380 0.3373 0.0769  -0.0633 -0.0169 55  ILE D C   
6819  O O   . ILE D 55  ? 0.4623 0.3437 0.3363 0.0749  -0.0622 -0.0179 55  ILE D O   
6820  C CB  . ILE D 55  ? 0.3971 0.3138 0.3313 0.0426  -0.0682 -0.0119 55  ILE D CB  
6821  C CG1 . ILE D 55  ? 0.3380 0.3161 0.3277 0.0389  -0.0644 -0.0094 55  ILE D CG1 
6822  C CG2 . ILE D 55  ? 0.3909 0.3040 0.3316 0.0150  -0.0746 -0.0109 55  ILE D CG2 
6823  C CD1 . ILE D 55  ? 0.3197 0.2994 0.3282 0.0169  -0.0682 -0.0060 55  ILE D CD1 
6824  N N   . ILE D 56  ? 0.5551 0.3341 0.3450 0.0768  -0.0669 -0.0184 56  ILE D N   
6825  C CA  . ILE D 56  ? 0.6260 0.3345 0.3502 0.0722  -0.0700 -0.0214 56  ILE D CA  
6826  C C   . ILE D 56  ? 0.6505 0.3617 0.3539 0.1136  -0.0592 -0.0227 56  ILE D C   
6827  O O   . ILE D 56  ? 0.6504 0.3625 0.3531 0.1065  -0.0603 -0.0245 56  ILE D O   
6828  C CB  . ILE D 56  ? 0.7206 0.3268 0.3552 0.0650  -0.0745 -0.0225 56  ILE D CB  
6829  C CG1 . ILE D 56  ? 0.7036 0.3131 0.3562 0.0149  -0.0870 -0.0191 56  ILE D CG1 
6830  C CG2 . ILE D 56  ? 0.8132 0.3295 0.3584 0.0661  -0.0754 -0.0260 56  ILE D CG2 
6831  C CD1 . ILE D 56  ? 0.7863 0.3090 0.3611 0.0047  -0.0909 -0.0189 56  ILE D CD1 
6832  N N   . ASP D 57  ? 0.6733 0.3928 0.3605 0.1582  -0.0483 -0.0200 57  ASP D N   
6833  C CA  . ASP D 57  ? 0.7048 0.4348 0.3662 0.2055  -0.0359 -0.0176 57  ASP D CA  
6834  C C   . ASP D 57  ? 0.6331 0.4546 0.3648 0.2006  -0.0336 -0.0160 57  ASP D C   
6835  O O   . ASP D 57  ? 0.6589 0.4735 0.3669 0.2188  -0.0281 -0.0162 57  ASP D O   
6836  C CB  . ASP D 57  ? 0.7288 0.4771 0.3716 0.2558  -0.0244 -0.0107 57  ASP D CB  
6837  C CG  . ASP D 57  ? 0.8439 0.4749 0.3791 0.2825  -0.0205 -0.0116 57  ASP D CG  
6838  O OD1 . ASP D 57  ? 0.9290 0.4757 0.3834 0.2972  -0.0168 -0.0145 57  ASP D OD1 
6839  O OD2 . ASP D 57  ? 0.8582 0.4739 0.3815 0.2889  -0.0206 -0.0094 57  ASP D OD2 
6840  N N   . LYS D 58  ? 0.5536 0.4536 0.3635 0.1756  -0.0373 -0.0143 58  LYS D N   
6841  C CA  . LYS D 58  ? 0.4950 0.4710 0.3621 0.1644  -0.0356 -0.0129 58  LYS D CA  
6842  C C   . LYS D 58  ? 0.4974 0.4449 0.3626 0.1378  -0.0417 -0.0180 58  LYS D C   
6843  O O   . LYS D 58  ? 0.4841 0.4636 0.3624 0.1425  -0.0377 -0.0175 58  LYS D O   
6844  C CB  . LYS D 58  ? 0.4251 0.4709 0.3581 0.1405  -0.0379 -0.0102 58  LYS D CB  
6845  C CG  . LYS D 58  ? 0.4012 0.5307 0.3603 0.1603  -0.0301 -0.0021 58  LYS D CG  
6846  C CD  . LYS D 58  ? 0.4528 0.5797 0.3677 0.2112  -0.0211 0.0041  58  LYS D CD  
6847  C CE  . LYS D 58  ? 0.4264 0.6576 0.3718 0.2291  -0.0141 0.0162  58  LYS D CE  
6848  N NZ  . LYS D 58  ? 0.4825 0.7170 0.3809 0.2883  -0.0031 0.0255  58  LYS D NZ  
6849  N N   . MET D 59  ? 0.5188 0.4111 0.3659 0.1092  -0.0515 -0.0213 59  MET D N   
6850  C CA  . MET D 59  ? 0.5248 0.3949 0.3672 0.0821  -0.0588 -0.0237 59  MET D CA  
6851  C C   . MET D 59  ? 0.6083 0.4013 0.3732 0.0952  -0.0585 -0.0270 59  MET D C   
6852  O O   . MET D 59  ? 0.6146 0.3978 0.3725 0.0819  -0.0618 -0.0286 59  MET D O   
6853  C CB  . MET D 59  ? 0.5094 0.3704 0.3673 0.0433  -0.0699 -0.0220 59  MET D CB  
6854  C CG  . MET D 59  ? 0.4435 0.3660 0.3649 0.0339  -0.0687 -0.0185 59  MET D CG  
6855  S SD  . MET D 59  ? 0.3863 0.3770 0.3628 0.0331  -0.0626 -0.0175 59  MET D SD  
6856  C CE  . MET D 59  ? 0.3747 0.3632 0.3611 0.0049  -0.0702 -0.0145 59  MET D CE  
6857  N N   . ASN D 60  ? 0.6811 0.4137 0.3809 0.1228  -0.0537 -0.0275 60  ASN D N   
6858  C CA  . ASN D 60  ? 0.7842 0.4210 0.3877 0.1398  -0.0512 -0.0305 60  ASN D CA  
6859  C C   . ASN D 60  ? 0.7894 0.4397 0.3883 0.1575  -0.0449 -0.0315 60  ASN D C   
6860  O O   . ASN D 60  ? 0.8445 0.4287 0.3883 0.1426  -0.0498 -0.0350 60  ASN D O   
6861  C CB  . ASN D 60  ? 0.8597 0.4404 0.3937 0.1852  -0.0409 -0.0289 60  ASN D CB  
6862  C CG  . ASN D 60  ? 0.9584 0.4653 0.3999 0.2288  -0.0295 -0.0295 60  ASN D CG  
6863  O OD1 . ASN D 60  ? 0.9369 0.4971 0.4009 0.2595  -0.0195 -0.0266 60  ASN D OD1 
6864  N ND2 . ASN D 60  ? 1.0755 0.4550 0.4049 0.2321  -0.0301 -0.0325 60  ASN D ND2 
6865  N N   . THR D 61  ? 0.7360 0.4726 0.3891 0.1855  -0.0345 -0.0275 61  THR D N   
6866  C CA  . THR D 61  ? 0.7326 0.4953 0.3896 0.2001  -0.0282 -0.0272 61  THR D CA  
6867  C C   . THR D 61  ? 0.6424 0.4820 0.3835 0.1631  -0.0347 -0.0274 61  THR D C   
6868  O O   . THR D 61  ? 0.5758 0.4944 0.3817 0.1584  -0.0327 -0.0236 61  THR D O   
6869  C CB  . THR D 61  ? 0.7510 0.5556 0.3954 0.2582  -0.0109 -0.0199 61  THR D CB  
6870  O OG1 . THR D 61  ? 0.6942 0.5836 0.3945 0.2562  -0.0069 -0.0168 61  THR D OG1 
6871  C CG2 . THR D 61  ? 0.7306 0.5854 0.3988 0.2811  -0.0054 -0.0129 61  THR D CG2 
6872  N N   . GLN D 62  ? 0.6505 0.4590 0.3803 0.1366  -0.0424 -0.0311 62  GLN D N   
6873  C CA  . GLN D 62  ? 0.5812 0.4413 0.3743 0.1010  -0.0495 -0.0308 62  GLN D CA  
6874  C C   . GLN D 62  ? 0.6077 0.4333 0.3723 0.0876  -0.0542 -0.0335 62  GLN D C   
6875  O O   . GLN D 62  ? 0.6856 0.4338 0.3767 0.0936  -0.0558 -0.0364 62  GLN D O   
6876  C CB  . GLN D 62  ? 0.5534 0.4162 0.3742 0.0677  -0.0600 -0.0294 62  GLN D CB  
6877  C CG  . GLN D 62  ? 0.5402 0.4024 0.3752 0.0299  -0.0714 -0.0278 62  GLN D CG  
6878  C CD  . GLN D 62  ? 0.5167 0.3925 0.3777 0.0035  -0.0796 -0.0231 62  GLN D CD  
6879  O OE1 . GLN D 62  ? 0.5062 0.3909 0.3797 0.0114  -0.0767 -0.0226 62  GLN D OE1 
6880  N NE2 . GLN D 62  ? 0.5109 0.3947 0.3801 -0.0267 -0.0896 -0.0180 62  GLN D NE2 
6881  N N   . PHE D 63  ? 0.5503 0.4264 0.3653 0.0690  -0.0563 -0.0321 63  PHE D N   
6882  C CA  . PHE D 63  ? 0.5652 0.4231 0.3623 0.0586  -0.0598 -0.0337 63  PHE D CA  
6883  C C   . PHE D 63  ? 0.6216 0.4099 0.3641 0.0321  -0.0727 -0.0346 63  PHE D C   
6884  O O   . PHE D 63  ? 0.6178 0.4019 0.3668 0.0051  -0.0827 -0.0314 63  PHE D O   
6885  C CB  . PHE D 63  ? 0.4992 0.4184 0.3574 0.0400  -0.0609 -0.0307 63  PHE D CB  
6886  C CG  . PHE D 63  ? 0.5109 0.4208 0.3556 0.0339  -0.0627 -0.0316 63  PHE D CG  
6887  C CD1 . PHE D 63  ? 0.5197 0.4390 0.3539 0.0572  -0.0527 -0.0337 63  PHE D CD1 
6888  C CD2 . PHE D 63  ? 0.5146 0.4131 0.3564 0.0050  -0.0746 -0.0286 63  PHE D CD2 
6889  C CE1 . PHE D 63  ? 0.5331 0.4413 0.3530 0.0516  -0.0542 -0.0348 63  PHE D CE1 
6890  C CE2 . PHE D 63  ? 0.5274 0.4188 0.3557 -0.0007 -0.0768 -0.0288 63  PHE D CE2 
6891  C CZ  . PHE D 63  ? 0.5368 0.4281 0.3531 0.0225  -0.0665 -0.0330 63  PHE D CZ  
6892  N N   . GLU D 64  ? 0.6769 0.4130 0.3621 0.0378  -0.0725 -0.0379 64  GLU D N   
6893  C CA  . GLU D 64  ? 0.7407 0.4080 0.3636 0.0056  -0.0859 -0.0382 64  GLU D CA  
6894  C C   . GLU D 64  ? 0.7315 0.4120 0.3598 -0.0084 -0.0901 -0.0376 64  GLU D C   
6895  O O   . GLU D 64  ? 0.7423 0.4190 0.3585 0.0187  -0.0800 -0.0411 64  GLU D O   
6896  C CB  . GLU D 64  ? 0.8484 0.4111 0.3679 0.0247  -0.0819 -0.0433 64  GLU D CB  
6897  C CG  . GLU D 64  ? 0.8701 0.4091 0.3706 0.0465  -0.0758 -0.0437 64  GLU D CG  
6898  C CD  . GLU D 64  ? 0.9941 0.4154 0.3760 0.0719  -0.0695 -0.0478 64  GLU D CD  
6899  O OE1 . GLU D 64  ? 1.0680 0.4195 0.3776 0.0692  -0.0705 -0.0509 64  GLU D OE1 
6900  O OE2 . GLU D 64  ? 1.0248 0.4178 0.3794 0.0968  -0.0627 -0.0476 64  GLU D OE2 
6901  N N   . ALA D 65  ? 0.7129 0.4138 0.3580 -0.0497 -0.1047 -0.0314 65  ALA D N   
6902  C CA  . ALA D 65  ? 0.7032 0.4219 0.3545 -0.0649 -0.1101 -0.0289 65  ALA D CA  
6903  C C   . ALA D 65  ? 0.7955 0.4254 0.3542 -0.0717 -0.1141 -0.0338 65  ALA D C   
6904  O O   . ALA D 65  ? 0.8757 0.4253 0.3574 -0.0843 -0.1195 -0.0361 65  ALA D O   
6905  C CB  . ALA D 65  ? 0.6660 0.4403 0.3577 -0.1033 -0.1241 -0.0173 65  ALA D CB  
6906  N N   . VAL D 66  ? 0.7905 0.4275 0.3492 -0.0636 -0.1110 -0.0355 66  VAL D N   
6907  C CA  . VAL D 66  ? 0.8800 0.4323 0.3490 -0.0700 -0.1142 -0.0400 66  VAL D CA  
6908  C C   . VAL D 66  ? 0.8585 0.4465 0.3468 -0.0997 -0.1254 -0.0344 66  VAL D C   
6909  O O   . VAL D 66  ? 0.7788 0.4478 0.3441 -0.0908 -0.1213 -0.0305 66  VAL D O   
6910  C CB  . VAL D 66  ? 0.9124 0.4280 0.3470 -0.0174 -0.0950 -0.0480 66  VAL D CB  
6911  C CG1 . VAL D 66  ? 1.0202 0.4355 0.3499 -0.0202 -0.0967 -0.0526 66  VAL D CG1 
6912  C CG2 . VAL D 66  ? 0.9281 0.4232 0.3482 0.0181  -0.0828 -0.0506 66  VAL D CG2 
6913  N N   . GLY D 67  ? 0.9370 0.4599 0.3476 -0.1366 -0.1395 -0.0332 67  GLY D N   
6914  C CA  . GLY D 67  ? 0.9281 0.4822 0.3462 -0.1681 -0.1519 -0.0263 67  GLY D CA  
6915  C C   . GLY D 67  ? 0.9377 0.4708 0.3393 -0.1389 -0.1411 -0.0334 67  GLY D C   
6916  O O   . GLY D 67  ? 1.0227 0.4629 0.3394 -0.1220 -0.1343 -0.0422 67  GLY D O   
6917  N N   . ARG D 68  ? 0.8559 0.4716 0.3324 -0.1309 -0.1384 -0.0287 68  ARG D N   
6918  C CA  . ARG D 68  ? 0.8553 0.4644 0.3255 -0.1069 -0.1287 -0.0339 68  ARG D CA  
6919  C C   . ARG D 68  ? 0.8302 0.4876 0.3248 -0.1363 -0.1414 -0.0245 68  ARG D C   
6920  O O   . ARG D 68  ? 0.7662 0.5032 0.3266 -0.1493 -0.1475 -0.0135 68  ARG D O   
6921  C CB  . ARG D 68  ? 0.7832 0.4464 0.3196 -0.0619 -0.1090 -0.0375 68  ARG D CB  
6922  C CG  . ARG D 68  ? 0.8214 0.4361 0.3185 -0.0217 -0.0928 -0.0461 68  ARG D CG  
6923  C CD  . ARG D 68  ? 0.7536 0.4344 0.3143 0.0154  -0.0750 -0.0469 68  ARG D CD  
6924  N NE  . ARG D 68  ? 0.6793 0.4257 0.3124 0.0081  -0.0762 -0.0423 68  ARG D NE  
6925  C CZ  . ARG D 68  ? 0.6750 0.4193 0.3132 0.0167  -0.0736 -0.0428 68  ARG D CZ  
6926  N NH1 . ARG D 68  ? 0.7425 0.4213 0.3159 0.0354  -0.0691 -0.0472 68  ARG D NH1 
6927  N NH2 . ARG D 68  ? 0.6099 0.4124 0.3118 0.0086  -0.0746 -0.0384 68  ARG D NH2 
6928  N N   . GLU D 69  ? 0.8848 0.4933 0.3222 -0.1431 -0.1444 -0.0278 69  GLU D N   
6929  C CA  . GLU D 69  ? 0.8760 0.5229 0.3227 -0.1736 -0.1583 -0.0180 69  GLU D CA  
6930  C C   . GLU D 69  ? 0.8318 0.5097 0.3140 -0.1429 -0.1457 -0.0209 69  GLU D C   
6931  O O   . GLU D 69  ? 0.8551 0.4882 0.3092 -0.1108 -0.1309 -0.0317 69  GLU D O   
6932  C CB  . GLU D 69  ? 0.9843 0.5471 0.3290 -0.2138 -0.1739 -0.0186 69  GLU D CB  
6933  C CG  . GLU D 69  ? 1.0402 0.5681 0.3365 -0.2575 -0.1898 -0.0137 69  GLU D CG  
6934  C CD  . GLU D 69  ? 1.0258 0.6289 0.3454 -0.3124 -0.2128 0.0050  69  GLU D CD  
6935  O OE1 . GLU D 69  ? 0.9362 0.6493 0.3477 -0.3019 -0.2120 0.0166  69  GLU D OE1 
6936  O OE2 . GLU D 69  ? 1.1133 0.6646 0.3524 -0.3663 -0.2314 0.0097  69  GLU D OE2 
6937  N N   . PHE D 70  ? 0.7719 0.5277 0.3114 -0.1515 -0.1510 -0.0096 70  PHE D N   
6938  C CA  . PHE D 70  ? 0.7352 0.5194 0.3045 -0.1276 -0.1405 -0.0107 70  PHE D CA  
6939  C C   . PHE D 70  ? 0.7408 0.5583 0.3075 -0.1542 -0.1552 0.0015  70  PHE D C   
6940  O O   . PHE D 70  ? 0.7328 0.5978 0.3142 -0.1829 -0.1704 0.0159  70  PHE D O   
6941  C CB  . PHE D 70  ? 0.6546 0.5018 0.2999 -0.0995 -0.1265 -0.0086 70  PHE D CB  
6942  C CG  . PHE D 70  ? 0.6398 0.4725 0.2960 -0.0784 -0.1144 -0.0172 70  PHE D CG  
6943  C CD1 . PHE D 70  ? 0.6240 0.4719 0.2982 -0.0888 -0.1198 -0.0130 70  PHE D CD1 
6944  C CD2 . PHE D 70  ? 0.6420 0.4537 0.2909 -0.0482 -0.0977 -0.0275 70  PHE D CD2 
6945  C CE1 . PHE D 70  ? 0.6115 0.4483 0.2953 -0.0689 -0.1091 -0.0202 70  PHE D CE1 
6946  C CE2 . PHE D 70  ? 0.6292 0.4390 0.2891 -0.0281 -0.0870 -0.0327 70  PHE D CE2 
6947  C CZ  . PHE D 70  ? 0.6141 0.4336 0.2909 -0.0384 -0.0929 -0.0296 70  PHE D CZ  
6948  N N   . ASN D 71  ? 0.7545 0.5547 0.3030 -0.1442 -0.1506 -0.0024 71  ASN D N   
6949  C CA  . ASN D 71  ? 0.7630 0.5954 0.3063 -0.1672 -0.1642 0.0095  71  ASN D CA  
6950  C C   . ASN D 71  ? 0.6917 0.6106 0.3059 -0.1495 -0.1594 0.0225  71  ASN D C   
6951  O O   . ASN D 71  ? 0.6407 0.5880 0.3026 -0.1252 -0.1470 0.0220  71  ASN D O   
6952  C CB  . ASN D 71  ? 0.8189 0.5897 0.3037 -0.1662 -0.1626 0.0004  71  ASN D CB  
6953  C CG  . ASN D 71  ? 0.7833 0.5604 0.2966 -0.1259 -0.1423 -0.0073 71  ASN D CG  
6954  O OD1 . ASN D 71  ? 0.7256 0.5631 0.2953 -0.1112 -0.1362 -0.0001 71  ASN D OD1 
6955  N ND2 . ASN D 71  ? 0.8267 0.5384 0.2929 -0.1081 -0.1312 -0.0207 71  ASN D ND2 
6956  N N   . ASN D 72  ? 0.6965 0.6512 0.3093 -0.1609 -0.1688 0.0347  72  ASN D N   
6957  C CA  . ASN D 72  ? 0.6466 0.6805 0.3116 -0.1433 -0.1657 0.0513  72  ASN D CA  
6958  C C   . ASN D 72  ? 0.6127 0.6398 0.3031 -0.1030 -0.1443 0.0440  72  ASN D C   
6959  O O   . ASN D 72  ? 0.5782 0.6511 0.3044 -0.0813 -0.1366 0.0551  72  ASN D O   
6960  C CB  . ASN D 72  ? 0.6705 0.7475 0.3200 -0.1664 -0.1826 0.0685  72  ASN D CB  
6961  C CG  . ASN D 72  ? 0.6308 0.8018 0.3275 -0.1487 -0.1822 0.0921  72  ASN D CG  
6962  O OD1 . ASN D 72  ? 0.6019 0.8198 0.3320 -0.1432 -0.1816 0.1024  72  ASN D OD1 
6963  N ND2 . ASN D 72  ? 0.6341 0.8319 0.3297 -0.1360 -0.1816 0.1019  72  ASN D ND2 
6964  N N   . LEU D 73  ? 0.6304 0.5987 0.2950 -0.0937 -0.1341 0.0269  73  LEU D N   
6965  C CA  . LEU D 73  ? 0.6057 0.5661 0.2877 -0.0640 -0.1145 0.0198  73  LEU D CA  
6966  C C   . LEU D 73  ? 0.5916 0.5249 0.2816 -0.0513 -0.1010 0.0058  73  LEU D C   
6967  O O   . LEU D 73  ? 0.5902 0.5050 0.2768 -0.0361 -0.0867 -0.0033 73  LEU D O   
6968  C CB  . LEU D 73  ? 0.6342 0.5672 0.2853 -0.0619 -0.1121 0.0151  73  LEU D CB  
6969  C CG  . LEU D 73  ? 0.6407 0.6100 0.2906 -0.0667 -0.1216 0.0307  73  LEU D CG  
6970  C CD1 . LEU D 73  ? 0.6789 0.6129 0.2888 -0.0725 -0.1235 0.0248  73  LEU D CD1 
6971  C CD2 . LEU D 73  ? 0.6101 0.6129 0.2905 -0.0405 -0.1094 0.0404  73  LEU D CD2 
6972  N N   . GLU D 74  ? 0.5823 0.5206 0.2829 -0.0590 -0.1061 0.0061  74  GLU D N   
6973  C CA  . GLU D 74  ? 0.5647 0.4899 0.2785 -0.0463 -0.0946 -0.0037 74  GLU D CA  
6974  C C   . GLU D 74  ? 0.5276 0.4906 0.2804 -0.0456 -0.0953 0.0043  74  GLU D C   
6975  O O   . GLU D 74  ? 0.5221 0.4777 0.2800 -0.0478 -0.0958 0.0002  74  GLU D O   
6976  C CB  . GLU D 74  ? 0.6061 0.4823 0.2787 -0.0533 -0.0989 -0.0132 74  GLU D CB  
6977  C CG  . GLU D 74  ? 0.6500 0.4806 0.2766 -0.0457 -0.0938 -0.0221 74  GLU D CG  
6978  C CD  . GLU D 74  ? 0.7048 0.4743 0.2776 -0.0439 -0.0943 -0.0309 74  GLU D CD  
6979  O OE1 . GLU D 74  ? 0.7354 0.4812 0.2815 -0.0672 -0.1086 -0.0284 74  GLU D OE1 
6980  O OE2 . GLU D 74  ? 0.7233 0.4688 0.2757 -0.0182 -0.0798 -0.0389 74  GLU D OE2 
6981  N N   . ARG D 75  ? 0.5078 0.5082 0.2827 -0.0393 -0.0945 0.0168  75  ARG D N   
6982  C CA  . ARG D 75  ? 0.4812 0.5190 0.2864 -0.0349 -0.0949 0.0277  75  ARG D CA  
6983  C C   . ARG D 75  ? 0.4572 0.4851 0.2805 -0.0204 -0.0800 0.0204  75  ARG D C   
6984  O O   . ARG D 75  ? 0.4393 0.4826 0.2820 -0.0204 -0.0808 0.0236  75  ARG D O   
6985  C CB  . ARG D 75  ? 0.4793 0.5574 0.2924 -0.0236 -0.0956 0.0457  75  ARG D CB  
6986  C CG  . ARG D 75  ? 0.4976 0.6113 0.3013 -0.0422 -0.1138 0.0594  75  ARG D CG  
6987  C CD  . ARG D 75  ? 0.4897 0.6469 0.3094 -0.0594 -0.1266 0.0711  75  ARG D CD  
6988  N NE  . ARG D 75  ? 0.5150 0.7076 0.3187 -0.0896 -0.1469 0.0843  75  ARG D NE  
6989  C CZ  . ARG D 75  ? 0.5467 0.7143 0.3209 -0.1272 -0.1625 0.0789  75  ARG D CZ  
6990  N NH1 . ARG D 75  ? 0.5573 0.6626 0.3147 -0.1329 -0.1589 0.0604  75  ARG D NH1 
6991  N NH2 . ARG D 75  ? 0.5760 0.7793 0.3300 -0.1603 -0.1818 0.0934  75  ARG D NH2 
6992  N N   . ARG D 76  ? 0.4595 0.4646 0.2744 -0.0115 -0.0669 0.0117  76  ARG D N   
6993  C CA  . ARG D 76  ? 0.4440 0.4424 0.2699 -0.0052 -0.0537 0.0058  76  ARG D CA  
6994  C C   . ARG D 76  ? 0.4334 0.4294 0.2689 -0.0098 -0.0552 -0.0028 76  ARG D C   
6995  O O   . ARG D 76  ? 0.4148 0.4202 0.2684 -0.0084 -0.0524 -0.0019 76  ARG D O   
6996  C CB  . ARG D 76  ? 0.4556 0.4365 0.2651 -0.0032 -0.0414 0.0000  76  ARG D CB  
6997  C CG  . ARG D 76  ? 0.4733 0.4446 0.2654 0.0039  -0.0358 0.0081  76  ARG D CG  
6998  C CD  . ARG D 76  ? 0.4914 0.4432 0.2614 -0.0007 -0.0258 0.0017  76  ARG D CD  
6999  N NE  . ARG D 76  ? 0.4972 0.4501 0.2610 -0.0036 -0.0312 -0.0040 76  ARG D NE  
7000  C CZ  . ARG D 76  ? 0.5066 0.4553 0.2583 -0.0072 -0.0236 -0.0110 76  ARG D CZ  
7001  N NH1 . ARG D 76  ? 0.5095 0.4596 0.2561 -0.0147 -0.0117 -0.0126 76  ARG D NH1 
7002  N NH2 . ARG D 76  ? 0.5190 0.4627 0.2587 -0.0050 -0.0280 -0.0153 76  ARG D NH2 
7003  N N   . ILE D 77  ? 0.4520 0.4304 0.2688 -0.0122 -0.0587 -0.0106 77  ILE D N   
7004  C CA  . ILE D 77  ? 0.4553 0.4233 0.2692 -0.0100 -0.0586 -0.0178 77  ILE D CA  
7005  C C   . ILE D 77  ? 0.4592 0.4241 0.2738 -0.0209 -0.0716 -0.0140 77  ILE D C   
7006  O O   . ILE D 77  ? 0.4537 0.4148 0.2738 -0.0184 -0.0705 -0.0175 77  ILE D O   
7007  C CB  . ILE D 77  ? 0.4882 0.4291 0.2686 -0.0014 -0.0549 -0.0261 77  ILE D CB  
7008  C CG1 . ILE D 77  ? 0.5275 0.4370 0.2713 -0.0112 -0.0666 -0.0255 77  ILE D CG1 
7009  C CG2 . ILE D 77  ? 0.4811 0.4388 0.2657 0.0077  -0.0409 -0.0283 77  ILE D CG2 
7010  C CD1 . ILE D 77  ? 0.5755 0.4420 0.2717 0.0004  -0.0627 -0.0336 77  ILE D CD1 
7011  N N   . GLU D 78  ? 0.4711 0.4424 0.2788 -0.0349 -0.0842 -0.0055 78  GLU D N   
7012  C CA  . GLU D 78  ? 0.4742 0.4572 0.2850 -0.0516 -0.0976 0.0020  78  GLU D CA  
7013  C C   . GLU D 78  ? 0.4353 0.4540 0.2859 -0.0437 -0.0923 0.0087  78  GLU D C   
7014  O O   . GLU D 78  ? 0.4304 0.4520 0.2883 -0.0504 -0.0967 0.0094  78  GLU D O   
7015  C CB  . GLU D 78  ? 0.4926 0.4950 0.2914 -0.0705 -0.1122 0.0141  78  GLU D CB  
7016  C CG  . GLU D 78  ? 0.5031 0.5265 0.2993 -0.0965 -0.1283 0.0247  78  GLU D CG  
7017  C CD  . GLU D 78  ? 0.5313 0.5779 0.3072 -0.1223 -0.1449 0.0376  78  GLU D CD  
7018  O OE1 . GLU D 78  ? 0.5134 0.6045 0.3097 -0.1111 -0.1431 0.0491  78  GLU D OE1 
7019  O OE2 . GLU D 78  ? 0.5785 0.5960 0.3115 -0.1547 -0.1597 0.0371  78  GLU D OE2 
7020  N N   . ASN D 79  ? 0.4168 0.4545 0.2849 -0.0291 -0.0823 0.0135  79  ASN D N   
7021  C CA  . ASN D 79  ? 0.3933 0.4520 0.2861 -0.0181 -0.0748 0.0200  79  ASN D CA  
7022  C C   . ASN D 79  ? 0.3804 0.4228 0.2814 -0.0139 -0.0651 0.0090  79  ASN D C   
7023  O O   . ASN D 79  ? 0.3647 0.4177 0.2823 -0.0126 -0.0641 0.0116  79  ASN D O   
7024  C CB  . ASN D 79  ? 0.3972 0.4612 0.2863 -0.0023 -0.0652 0.0279  79  ASN D CB  
7025  C CG  . ASN D 79  ? 0.3891 0.4636 0.2885 0.0127  -0.0565 0.0368  79  ASN D CG  
7026  O OD1 . ASN D 79  ? 0.3797 0.4861 0.2950 0.0139  -0.0626 0.0475  79  ASN D OD1 
7027  N ND2 . ASN D 79  ? 0.4007 0.4458 0.2842 0.0226  -0.0421 0.0334  79  ASN D ND2 
7028  N N   . LEU D 80  ? 0.3885 0.4119 0.2776 -0.0117 -0.0578 -0.0014 80  LEU D N   
7029  C CA  . LEU D 80  ? 0.3790 0.4002 0.2749 -0.0088 -0.0493 -0.0096 80  LEU D CA  
7030  C C   . LEU D 80  ? 0.3802 0.3967 0.2779 -0.0105 -0.0564 -0.0128 80  LEU D C   
7031  O O   . LEU D 80  ? 0.3639 0.3891 0.2774 -0.0090 -0.0536 -0.0134 80  LEU D O   
7032  C CB  . LEU D 80  ? 0.3911 0.4068 0.2720 -0.0052 -0.0416 -0.0168 80  LEU D CB  
7033  C CG  . LEU D 80  ? 0.3816 0.4146 0.2697 -0.0032 -0.0307 -0.0210 80  LEU D CG  
7034  C CD1 . LEU D 80  ? 0.3955 0.4356 0.2687 -0.0011 -0.0231 -0.0235 80  LEU D CD1 
7035  C CD2 . LEU D 80  ? 0.3785 0.4161 0.2715 0.0050  -0.0324 -0.0246 80  LEU D CD2 
7036  N N   . ASN D 81  ? 0.4085 0.4040 0.2817 -0.0154 -0.0658 -0.0146 81  ASN D N   
7037  C CA  . ASN D 81  ? 0.4286 0.4023 0.2855 -0.0197 -0.0731 -0.0175 81  ASN D CA  
7038  C C   . ASN D 81  ? 0.4125 0.4053 0.2907 -0.0311 -0.0808 -0.0097 81  ASN D C   
7039  O O   . ASN D 81  ? 0.4105 0.3965 0.2912 -0.0296 -0.0805 -0.0125 81  ASN D O   
7040  C CB  . ASN D 81  ? 0.4765 0.4117 0.2881 -0.0297 -0.0831 -0.0193 81  ASN D CB  
7041  C CG  . ASN D 81  ? 0.5158 0.4092 0.2910 -0.0369 -0.0902 -0.0227 81  ASN D CG  
7042  O OD1 . ASN D 81  ? 0.5285 0.4008 0.2899 -0.0183 -0.0817 -0.0295 81  ASN D OD1 
7043  N ND2 . ASN D 81  ? 0.5414 0.4237 0.2958 -0.0646 -0.1058 -0.0165 81  ASN D ND2 
7044  N N   . LYS D 82  ? 0.4042 0.4252 0.2965 -0.0395 -0.0867 0.0014  82  LYS D N   
7045  C CA  . LYS D 82  ? 0.3901 0.4416 0.3035 -0.0474 -0.0928 0.0124  82  LYS D CA  
7046  C C   . LYS D 82  ? 0.3617 0.4247 0.3022 -0.0330 -0.0813 0.0113  82  LYS D C   
7047  O O   . LYS D 82  ? 0.3540 0.4214 0.3041 -0.0370 -0.0840 0.0123  82  LYS D O   
7048  C CB  . LYS D 82  ? 0.3870 0.4796 0.3099 -0.0512 -0.0987 0.0285  82  LYS D CB  
7049  C CG  . LYS D 82  ? 0.3688 0.5068 0.3168 -0.0517 -0.1016 0.0433  82  LYS D CG  
7050  C CD  . LYS D 82  ? 0.3743 0.5673 0.3268 -0.0586 -0.1112 0.0635  82  LYS D CD  
7051  C CE  . LYS D 82  ? 0.3633 0.5836 0.3284 -0.0276 -0.0985 0.0750  82  LYS D CE  
7052  N NZ  . LYS D 82  ? 0.3710 0.6543 0.3390 -0.0284 -0.1070 0.0973  82  LYS D NZ  
7053  N N   . LYS D 83  ? 0.3542 0.4172 0.3005 -0.0195 -0.0690 0.0094  83  LYS D N   
7054  C CA  . LYS D 83  ? 0.3394 0.4048 0.2998 -0.0109 -0.0581 0.0087  83  LYS D CA  
7055  C C   . LYS D 83  ? 0.3335 0.3894 0.2973 -0.0122 -0.0556 -0.0015 83  LYS D C   
7056  O O   . LYS D 83  ? 0.3201 0.3821 0.2973 -0.0113 -0.0531 -0.0006 83  LYS D O   
7057  C CB  . LYS D 83  ? 0.3480 0.4030 0.2974 -0.0034 -0.0462 0.0088  83  LYS D CB  
7058  C CG  . LYS D 83  ? 0.3584 0.4192 0.3025 0.0088  -0.0421 0.0221  83  LYS D CG  
7059  C CD  . LYS D 83  ? 0.3582 0.4517 0.3106 0.0097  -0.0536 0.0347  83  LYS D CD  
7060  C CE  . LYS D 83  ? 0.3679 0.4811 0.3171 0.0306  -0.0477 0.0521  83  LYS D CE  
7061  N NZ  . LYS D 83  ? 0.3902 0.5006 0.3189 0.0428  -0.0442 0.0590  83  LYS D NZ  
7062  N N   . MET D 84  ? 0.3482 0.3908 0.2971 -0.0111 -0.0555 -0.0098 84  MET D N   
7063  C CA  . MET D 84  ? 0.3499 0.3888 0.2970 -0.0053 -0.0524 -0.0169 84  MET D CA  
7064  C C   . MET D 84  ? 0.3560 0.3838 0.3011 -0.0092 -0.0610 -0.0161 84  MET D C   
7065  O O   . MET D 84  ? 0.3417 0.3774 0.3001 -0.0060 -0.0581 -0.0170 84  MET D O   
7066  C CB  . MET D 84  ? 0.3746 0.4003 0.2973 0.0039  -0.0496 -0.0231 84  MET D CB  
7067  C CG  . MET D 84  ? 0.3760 0.4143 0.2976 0.0187  -0.0412 -0.0270 84  MET D CG  
7068  S SD  . MET D 84  ? 0.4276 0.4268 0.3025 0.0388  -0.0417 -0.0320 84  MET D SD  
7069  C CE  . MET D 84  ? 0.4444 0.4058 0.3057 0.0278  -0.0539 -0.0318 84  MET D CE  
7070  N N   . GLU D 85  ? 0.3811 0.3905 0.3060 -0.0199 -0.0724 -0.0136 85  GLU D N   
7071  C CA  . GLU D 85  ? 0.3994 0.3915 0.3110 -0.0310 -0.0820 -0.0121 85  GLU D CA  
7072  C C   . GLU D 85  ? 0.3683 0.3936 0.3130 -0.0378 -0.0840 -0.0033 85  GLU D C   
7073  O O   . GLU D 85  ? 0.3654 0.3860 0.3138 -0.0380 -0.0844 -0.0045 85  GLU D O   
7074  C CB  . GLU D 85  ? 0.4449 0.4071 0.3164 -0.0503 -0.0952 -0.0102 85  GLU D CB  
7075  C CG  . GLU D 85  ? 0.4889 0.4061 0.3161 -0.0403 -0.0921 -0.0191 85  GLU D CG  
7076  C CD  . GLU D 85  ? 0.5603 0.4122 0.3217 -0.0542 -0.1018 -0.0223 85  GLU D CD  
7077  O OE1 . GLU D 85  ? 0.5896 0.4315 0.3270 -0.0840 -0.1158 -0.0163 85  GLU D OE1 
7078  O OE2 . GLU D 85  ? 0.5966 0.4046 0.3227 -0.0352 -0.0950 -0.0296 85  GLU D OE2 
7079  N N   . ASP D 86  ? 0.3494 0.4070 0.3142 -0.0390 -0.0837 0.0064  86  ASP D N   
7080  C CA  . ASP D 86  ? 0.3250 0.4151 0.3166 -0.0367 -0.0818 0.0168  86  ASP D CA  
7081  C C   . ASP D 86  ? 0.3044 0.3910 0.3108 -0.0237 -0.0698 0.0114  86  ASP D C   
7082  O O   . ASP D 86  ? 0.2926 0.3898 0.3125 -0.0236 -0.0694 0.0154  86  ASP D O   
7083  C CB  . ASP D 86  ? 0.3202 0.4413 0.3205 -0.0300 -0.0798 0.0297  86  ASP D CB  
7084  C CG  . ASP D 86  ? 0.3303 0.4865 0.3303 -0.0457 -0.0933 0.0442  86  ASP D CG  
7085  O OD1 . ASP D 86  ? 0.3307 0.5035 0.3366 -0.0591 -0.1008 0.0501  86  ASP D OD1 
7086  O OD2 . ASP D 86  ? 0.3412 0.5132 0.3341 -0.0470 -0.0969 0.0512  86  ASP D OD2 
7087  N N   . GLY D 87  ? 0.3029 0.3775 0.3043 -0.0160 -0.0605 0.0037  87  GLY D N   
7088  C CA  . GLY D 87  ? 0.2913 0.3652 0.3000 -0.0113 -0.0502 -0.0002 87  GLY D CA  
7089  C C   . GLY D 87  ? 0.2841 0.3569 0.2986 -0.0117 -0.0519 -0.0056 87  GLY D C   
7090  O O   . GLY D 87  ? 0.2733 0.3517 0.2988 -0.0115 -0.0482 -0.0041 87  GLY D O   
7091  N N   . PHE D 88  ? 0.2975 0.3574 0.2977 -0.0098 -0.0566 -0.0113 88  PHE D N   
7092  C CA  . PHE D 88  ? 0.3011 0.3535 0.2972 -0.0045 -0.0573 -0.0156 88  PHE D CA  
7093  C C   . PHE D 88  ? 0.3013 0.3473 0.3008 -0.0135 -0.0654 -0.0111 88  PHE D C   
7094  O O   . PHE D 88  ? 0.2934 0.3413 0.3003 -0.0104 -0.0638 -0.0122 88  PHE D O   
7095  C CB  . PHE D 88  ? 0.3329 0.3607 0.2975 0.0064  -0.0579 -0.0215 88  PHE D CB  
7096  C CG  . PHE D 88  ? 0.3298 0.3782 0.2946 0.0204  -0.0476 -0.0244 88  PHE D CG  
7097  C CD1 . PHE D 88  ? 0.3112 0.3929 0.2932 0.0267  -0.0402 -0.0238 88  PHE D CD1 
7098  C CD2 . PHE D 88  ? 0.3471 0.3882 0.2942 0.0250  -0.0458 -0.0262 88  PHE D CD2 
7099  C CE1 . PHE D 88  ? 0.3096 0.4255 0.2927 0.0353  -0.0315 -0.0232 88  PHE D CE1 
7100  C CE2 . PHE D 88  ? 0.3452 0.4150 0.2933 0.0368  -0.0361 -0.0267 88  PHE D CE2 
7101  C CZ  . PHE D 88  ? 0.3262 0.4379 0.2931 0.0410  -0.0290 -0.0244 88  PHE D CZ  
7102  N N   . LEU D 89  ? 0.3110 0.3558 0.3049 -0.0266 -0.0745 -0.0046 89  LEU D N   
7103  C CA  . LEU D 89  ? 0.3116 0.3637 0.3103 -0.0398 -0.0826 0.0029  89  LEU D CA  
7104  C C   . LEU D 89  ? 0.2797 0.3606 0.3094 -0.0334 -0.0757 0.0089  89  LEU D C   
7105  O O   . LEU D 89  ? 0.2750 0.3577 0.3108 -0.0367 -0.0776 0.0106  89  LEU D O   
7106  C CB  . LEU D 89  ? 0.3264 0.3917 0.3168 -0.0583 -0.0938 0.0130  89  LEU D CB  
7107  C CG  . LEU D 89  ? 0.3731 0.3996 0.3197 -0.0734 -0.1037 0.0087  89  LEU D CG  
7108  C CD1 . LEU D 89  ? 0.3846 0.4396 0.3270 -0.0987 -0.1164 0.0223  89  LEU D CD1 
7109  C CD2 . LEU D 89  ? 0.4127 0.3876 0.3206 -0.0784 -0.1073 0.0011  89  LEU D CD2 
7110  N N   . ASP D 90  ? 0.2661 0.3616 0.3071 -0.0238 -0.0671 0.0120  90  ASP D N   
7111  C CA  . ASP D 90  ? 0.2521 0.3591 0.3066 -0.0150 -0.0583 0.0176  90  ASP D CA  
7112  C C   . ASP D 90  ? 0.2440 0.3384 0.3007 -0.0131 -0.0522 0.0089  90  ASP D C   
7113  O O   . ASP D 90  ? 0.2377 0.3355 0.3023 -0.0114 -0.0495 0.0121  90  ASP D O   
7114  C CB  . ASP D 90  ? 0.2589 0.3654 0.3060 -0.0044 -0.0491 0.0224  90  ASP D CB  
7115  C CG  . ASP D 90  ? 0.2657 0.3964 0.3131 -0.0015 -0.0539 0.0350  90  ASP D CG  
7116  O OD1 . ASP D 90  ? 0.2628 0.4207 0.3198 -0.0106 -0.0640 0.0435  90  ASP D OD1 
7117  O OD2 . ASP D 90  ? 0.2778 0.4028 0.3129 0.0078  -0.0480 0.0376  90  ASP D OD2 
7118  N N   . VAL D 91  ? 0.2461 0.3321 0.2952 -0.0128 -0.0498 -0.0002 91  VAL D N   
7119  C CA  . VAL D 91  ? 0.2393 0.3282 0.2912 -0.0120 -0.0452 -0.0061 91  VAL D CA  
7120  C C   . VAL D 91  ? 0.2374 0.3232 0.2929 -0.0103 -0.0509 -0.0073 91  VAL D C   
7121  O O   . VAL D 91  ? 0.2288 0.3197 0.2928 -0.0108 -0.0483 -0.0067 91  VAL D O   
7122  C CB  . VAL D 91  ? 0.2448 0.3415 0.2886 -0.0093 -0.0417 -0.0120 91  VAL D CB  
7123  C CG1 . VAL D 91  ? 0.2395 0.3553 0.2880 -0.0061 -0.0387 -0.0146 91  VAL D CG1 
7124  C CG2 . VAL D 91  ? 0.2498 0.3475 0.2860 -0.0162 -0.0350 -0.0109 91  VAL D CG2 
7125  N N   . TRP D 92  ? 0.2535 0.3234 0.2946 -0.0100 -0.0586 -0.0089 92  TRP D N   
7126  C CA  . TRP D 92  ? 0.2668 0.3195 0.2968 -0.0094 -0.0639 -0.0104 92  TRP D CA  
7127  C C   . TRP D 92  ? 0.2594 0.3170 0.3001 -0.0216 -0.0694 -0.0029 92  TRP D C   
7128  O O   . TRP D 92  ? 0.2616 0.3120 0.3012 -0.0218 -0.0708 -0.0034 92  TRP D O   
7129  C CB  . TRP D 92  ? 0.3066 0.3233 0.2989 -0.0067 -0.0694 -0.0146 92  TRP D CB  
7130  C CG  . TRP D 92  ? 0.3188 0.3339 0.2971 0.0146  -0.0616 -0.0204 92  TRP D CG  
7131  C CD1 . TRP D 92  ? 0.3318 0.3447 0.2964 0.0226  -0.0584 -0.0228 92  TRP D CD1 
7132  C CD2 . TRP D 92  ? 0.3189 0.3450 0.2967 0.0331  -0.0551 -0.0220 92  TRP D CD2 
7133  N NE1 . TRP D 92  ? 0.3406 0.3665 0.2965 0.0462  -0.0498 -0.0248 92  TRP D NE1 
7134  C CE2 . TRP D 92  ? 0.3326 0.3701 0.2969 0.0535  -0.0477 -0.0236 92  TRP D CE2 
7135  C CE3 . TRP D 92  ? 0.3101 0.3426 0.2974 0.0356  -0.0546 -0.0208 92  TRP D CE3 
7136  C CZ2 . TRP D 92  ? 0.3375 0.4014 0.2988 0.0779  -0.0398 -0.0220 92  TRP D CZ2 
7137  C CZ3 . TRP D 92  ? 0.3149 0.3675 0.2984 0.0582  -0.0476 -0.0206 92  TRP D CZ3 
7138  C CH2 . TRP D 92  ? 0.3285 0.4008 0.2996 0.0799  -0.0401 -0.0203 92  TRP D CH2 
7139  N N   . THR D 93  ? 0.2521 0.3274 0.3024 -0.0297 -0.0719 0.0055  93  THR D N   
7140  C CA  . THR D 93  ? 0.2433 0.3401 0.3072 -0.0374 -0.0751 0.0164  93  THR D CA  
7141  C C   . THR D 93  ? 0.2233 0.3290 0.3045 -0.0264 -0.0652 0.0172  93  THR D C   
7142  O O   . THR D 93  ? 0.2198 0.3294 0.3072 -0.0292 -0.0665 0.0203  93  THR D O   
7143  C CB  . THR D 93  ? 0.2410 0.3687 0.3118 -0.0416 -0.0779 0.0292  93  THR D CB  
7144  O OG1 . THR D 93  ? 0.2651 0.3836 0.3150 -0.0585 -0.0892 0.0292  93  THR D OG1 
7145  C CG2 . THR D 93  ? 0.2318 0.3969 0.3186 -0.0442 -0.0790 0.0442  93  THR D CG2 
7146  N N   . TYR D 94  ? 0.2175 0.3214 0.2998 -0.0170 -0.0555 0.0145  94  TYR D N   
7147  C CA  . TYR D 94  ? 0.2128 0.3126 0.2970 -0.0111 -0.0458 0.0148  94  TYR D CA  
7148  C C   . TYR D 94  ? 0.2076 0.3021 0.2950 -0.0140 -0.0467 0.0075  94  TYR D C   
7149  O O   . TYR D 94  ? 0.2032 0.2977 0.2952 -0.0134 -0.0443 0.0103  94  TYR D O   
7150  C CB  . TYR D 94  ? 0.2226 0.3099 0.2924 -0.0085 -0.0368 0.0121  94  TYR D CB  
7151  C CG  . TYR D 94  ? 0.2315 0.3023 0.2882 -0.0117 -0.0281 0.0097  94  TYR D CG  
7152  C CD1 . TYR D 94  ? 0.2273 0.3035 0.2844 -0.0219 -0.0286 0.0018  94  TYR D CD1 
7153  C CD2 . TYR D 94  ? 0.2518 0.3019 0.2890 -0.0041 -0.0189 0.0168  94  TYR D CD2 
7154  C CE1 . TYR D 94  ? 0.2410 0.3053 0.2815 -0.0325 -0.0224 0.0009  94  TYR D CE1 
7155  C CE2 . TYR D 94  ? 0.2735 0.2960 0.2855 -0.0118 -0.0113 0.0142  94  TYR D CE2 
7156  C CZ  . TYR D 94  ? 0.2667 0.2979 0.2815 -0.0300 -0.0143 0.0061  94  TYR D CZ  
7157  O OH  . TYR D 94  ? 0.2935 0.3006 0.2791 -0.0450 -0.0086 0.0048  94  TYR D OH  
7158  N N   . ASN D 95  ? 0.2112 0.3031 0.2935 -0.0138 -0.0492 -0.0004 95  ASN D N   
7159  C CA  . ASN D 95  ? 0.2108 0.3040 0.2931 -0.0105 -0.0498 -0.0052 95  ASN D CA  
7160  C C   . ASN D 95  ? 0.2139 0.2969 0.2963 -0.0117 -0.0557 -0.0030 95  ASN D C   
7161  O O   . ASN D 95  ? 0.2076 0.2938 0.2957 -0.0107 -0.0538 -0.0030 95  ASN D O   
7162  C CB  . ASN D 95  ? 0.2239 0.3174 0.2938 -0.0013 -0.0507 -0.0107 95  ASN D CB  
7163  C CG  . ASN D 95  ? 0.2207 0.3359 0.2921 -0.0021 -0.0442 -0.0121 95  ASN D CG  
7164  O OD1 . ASN D 95  ? 0.2158 0.3361 0.2908 -0.0133 -0.0395 -0.0101 95  ASN D OD1 
7165  N ND2 . ASN D 95  ? 0.2322 0.3566 0.2935 0.0096  -0.0432 -0.0147 95  ASN D ND2 
7166  N N   . ALA D 96  ? 0.2278 0.2980 0.2998 -0.0177 -0.0635 -0.0004 96  ALA D N   
7167  C CA  . ALA D 96  ? 0.2405 0.2977 0.3038 -0.0263 -0.0707 0.0027  96  ALA D CA  
7168  C C   . ALA D 96  ? 0.2201 0.2993 0.3048 -0.0305 -0.0684 0.0112  96  ALA D C   
7169  O O   . ALA D 96  ? 0.2192 0.2936 0.3052 -0.0307 -0.0685 0.0111  96  ALA D O   
7170  C CB  . ALA D 96  ? 0.2679 0.3097 0.3089 -0.0413 -0.0807 0.0059  96  ALA D CB  
7171  N N   . GLU D 97  ? 0.2080 0.3102 0.3054 -0.0299 -0.0651 0.0194  97  GLU D N   
7172  C CA  . GLU D 97  ? 0.1974 0.3217 0.3085 -0.0269 -0.0606 0.0304  97  GLU D CA  
7173  C C   . GLU D 97  ? 0.1893 0.3027 0.3023 -0.0168 -0.0505 0.0266  97  GLU D C   
7174  O O   . GLU D 97  ? 0.1868 0.3059 0.3049 -0.0149 -0.0480 0.0320  97  GLU D O   
7175  C CB  . GLU D 97  ? 0.1972 0.3481 0.3132 -0.0202 -0.0571 0.0423  97  GLU D CB  
7176  C CG  . GLU D 97  ? 0.2059 0.3794 0.3205 -0.0358 -0.0687 0.0500  97  GLU D CG  
7177  C CD  . GLU D 97  ? 0.2050 0.4187 0.3269 -0.0258 -0.0652 0.0655  97  GLU D CD  
7178  O OE1 . GLU D 97  ? 0.2054 0.4154 0.3256 -0.0026 -0.0520 0.0683  97  GLU D OE1 
7179  O OE2 . GLU D 97  ? 0.2121 0.4589 0.3349 -0.0417 -0.0755 0.0760  97  GLU D OE2 
7180  N N   . LEU D 98  ? 0.1887 0.2880 0.2943 -0.0136 -0.0452 0.0182  98  LEU D N   
7181  C CA  . LEU D 98  ? 0.1898 0.2772 0.2886 -0.0125 -0.0374 0.0148  98  LEU D CA  
7182  C C   . LEU D 98  ? 0.1821 0.2703 0.2866 -0.0160 -0.0418 0.0096  98  LEU D C   
7183  O O   . LEU D 98  ? 0.1820 0.2661 0.2862 -0.0162 -0.0386 0.0115  98  LEU D O   
7184  C CB  . LEU D 98  ? 0.1986 0.2773 0.2835 -0.0165 -0.0323 0.0090  98  LEU D CB  
7185  C CG  . LEU D 98  ? 0.2131 0.2765 0.2797 -0.0248 -0.0253 0.0069  98  LEU D CG  
7186  C CD1 . LEU D 98  ? 0.2381 0.2721 0.2810 -0.0175 -0.0156 0.0142  98  LEU D CD1 
7187  C CD2 . LEU D 98  ? 0.2236 0.2889 0.2760 -0.0377 -0.0234 0.0020  98  LEU D CD2 
7188  N N   . LEU D 99  ? 0.1815 0.2715 0.2853 -0.0156 -0.0480 0.0037  99  LEU D N   
7189  C CA  . LEU D 99  ? 0.1830 0.2713 0.2849 -0.0122 -0.0511 0.0000  99  LEU D CA  
7190  C C   . LEU D 99  ? 0.1838 0.2633 0.2876 -0.0154 -0.0547 0.0044  99  LEU D C   
7191  O O   . LEU D 99  ? 0.1813 0.2603 0.2868 -0.0141 -0.0535 0.0039  99  LEU D O   
7192  C CB  . LEU D 99  ? 0.1988 0.2793 0.2864 -0.0035 -0.0554 -0.0047 99  LEU D CB  
7193  C CG  . LEU D 99  ? 0.2123 0.2884 0.2880 0.0093  -0.0562 -0.0072 99  LEU D CG  
7194  C CD1 . LEU D 99  ? 0.1973 0.3083 0.2855 0.0118  -0.0508 -0.0069 99  LEU D CD1 
7195  C CD2 . LEU D 99  ? 0.2434 0.2992 0.2905 0.0250  -0.0577 -0.0104 99  LEU D CD2 
7196  N N   . VAL D 100 ? 0.1881 0.2660 0.2911 -0.0222 -0.0596 0.0102  100 VAL D N   
7197  C CA  . VAL D 100 ? 0.1911 0.2702 0.2956 -0.0302 -0.0636 0.0172  100 VAL D CA  
7198  C C   . VAL D 100 ? 0.1764 0.2699 0.2948 -0.0252 -0.0552 0.0233  100 VAL D C   
7199  O O   . VAL D 100 ? 0.1762 0.2650 0.2952 -0.0258 -0.0550 0.0236  100 VAL D O   
7200  C CB  . VAL D 100 ? 0.2025 0.2905 0.3019 -0.0447 -0.0716 0.0255  100 VAL D CB  
7201  C CG1 . VAL D 100 ? 0.2024 0.3118 0.3089 -0.0560 -0.0744 0.0376  100 VAL D CG1 
7202  C CG2 . VAL D 100 ? 0.2347 0.2875 0.3027 -0.0530 -0.0805 0.0187  100 VAL D CG2 
7203  N N   . LEU D 101 ? 0.1719 0.2752 0.2936 -0.0180 -0.0475 0.0281  101 LEU D N   
7204  C CA  . LEU D 101 ? 0.1746 0.2755 0.2930 -0.0084 -0.0367 0.0337  101 LEU D CA  
7205  C C   . LEU D 101 ? 0.1774 0.2580 0.2875 -0.0105 -0.0332 0.0256  101 LEU D C   
7206  O O   . LEU D 101 ? 0.1810 0.2570 0.2889 -0.0082 -0.0296 0.0291  101 LEU D O   
7207  C CB  . LEU D 101 ? 0.1866 0.2820 0.2922 0.0024  -0.0273 0.0378  101 LEU D CB  
7208  C CG  . LEU D 101 ? 0.1943 0.3128 0.3000 0.0181  -0.0211 0.0542  101 LEU D CG  
7209  C CD1 . LEU D 101 ? 0.1804 0.3429 0.3083 0.0086  -0.0321 0.0636  101 LEU D CD1 
7210  C CD2 . LEU D 101 ? 0.2115 0.3178 0.2987 0.0301  -0.0135 0.0563  101 LEU D CD2 
7211  N N   . MET D 102 ? 0.1772 0.2518 0.2819 -0.0159 -0.0344 0.0164  102 MET D N   
7212  C CA  . MET D 102 ? 0.1818 0.2500 0.2777 -0.0224 -0.0322 0.0112  102 MET D CA  
7213  C C   . MET D 102 ? 0.1728 0.2487 0.2786 -0.0218 -0.0383 0.0092  102 MET D C   
7214  O O   . MET D 102 ? 0.1768 0.2475 0.2777 -0.0249 -0.0360 0.0096  102 MET D O   
7215  C CB  . MET D 102 ? 0.1845 0.2618 0.2743 -0.0301 -0.0327 0.0053  102 MET D CB  
7216  C CG  . MET D 102 ? 0.2030 0.2630 0.2728 -0.0344 -0.0258 0.0066  102 MET D CG  
7217  S SD  . MET D 102 ? 0.2130 0.2877 0.2698 -0.0527 -0.0260 0.0016  102 MET D SD  
7218  C CE  . MET D 102 ? 0.1867 0.2991 0.2719 -0.0397 -0.0341 -0.0014 102 MET D CE  
7219  N N   . GLU D 103 ? 0.1687 0.2496 0.2805 -0.0176 -0.0457 0.0071  103 GLU D N   
7220  C CA  . GLU D 103 ? 0.1727 0.2498 0.2820 -0.0136 -0.0507 0.0052  103 GLU D CA  
7221  C C   . GLU D 103 ? 0.1749 0.2417 0.2856 -0.0173 -0.0524 0.0106  103 GLU D C   
7222  O O   . GLU D 103 ? 0.1786 0.2396 0.2859 -0.0158 -0.0537 0.0099  103 GLU D O   
7223  C CB  . GLU D 103 ? 0.1864 0.2561 0.2837 -0.0051 -0.0560 0.0013  103 GLU D CB  
7224  C CG  . GLU D 103 ? 0.1852 0.2765 0.2814 0.0035  -0.0534 -0.0021 103 GLU D CG  
7225  C CD  . GLU D 103 ? 0.1805 0.2990 0.2805 0.0068  -0.0510 -0.0014 103 GLU D CD  
7226  O OE1 . GLU D 103 ? 0.1842 0.2950 0.2816 0.0096  -0.0524 -0.0003 103 GLU D OE1 
7227  O OE2 . GLU D 103 ? 0.1751 0.3273 0.2793 0.0039  -0.0484 -0.0008 103 GLU D OE2 
7228  N N   . ASN D 104 ? 0.1735 0.2447 0.2892 -0.0221 -0.0525 0.0176  104 ASN D N   
7229  C CA  . ASN D 104 ? 0.1741 0.2512 0.2944 -0.0265 -0.0525 0.0265  104 ASN D CA  
7230  C C   . ASN D 104 ? 0.1712 0.2464 0.2927 -0.0206 -0.0439 0.0281  104 ASN D C   
7231  O O   . ASN D 104 ? 0.1733 0.2456 0.2946 -0.0224 -0.0446 0.0306  104 ASN D O   
7232  C CB  . ASN D 104 ? 0.1715 0.2728 0.2996 -0.0291 -0.0518 0.0380  104 ASN D CB  
7233  C CG  . ASN D 104 ? 0.1831 0.2869 0.3042 -0.0446 -0.0630 0.0402  104 ASN D CG  
7234  O OD1 . ASN D 104 ? 0.2011 0.2765 0.3035 -0.0522 -0.0703 0.0332  104 ASN D OD1 
7235  N ND2 . ASN D 104 ? 0.1807 0.3157 0.3095 -0.0491 -0.0639 0.0512  104 ASN D ND2 
7236  N N   . GLU D 105 ? 0.2145 0.1946 0.2605 0.0158  0.0199  -0.0250 105 GLU D N   
7237  C CA  . GLU D 105 ? 0.2288 0.1724 0.2630 0.0216  0.0285  -0.0200 105 GLU D CA  
7238  C C   . GLU D 105 ? 0.1997 0.1473 0.2588 0.0008  0.0342  -0.0341 105 GLU D C   
7239  O O   . GLU D 105 ? 0.1873 0.1302 0.2589 0.0042  0.0349  -0.0343 105 GLU D O   
7240  C CB  . GLU D 105 ? 0.2952 0.1775 0.2685 0.0237  0.0390  -0.0091 105 GLU D CB  
7241  C CG  . GLU D 105 ? 0.3327 0.1635 0.2768 0.0385  0.0470  -0.0011 105 GLU D CG  
7242  C CD  . GLU D 105 ? 0.4208 0.1745 0.2890 0.0487  0.0564  0.0133  105 GLU D CD  
7243  O OE1 . GLU D 105 ? 0.4545 0.1770 0.2881 0.0196  0.0647  0.0106  105 GLU D OE1 
7244  O OE2 . GLU D 105 ? 0.4636 0.1876 0.3033 0.0869  0.0567  0.0277  105 GLU D OE2 
7245  N N   . ARG D 106 ? 0.1932 0.1546 0.2583 -0.0184 0.0384  -0.0455 106 ARG D N   
7246  C CA  . ARG D 106 ? 0.1676 0.1490 0.2610 -0.0319 0.0417  -0.0578 106 ARG D CA  
7247  C C   . ARG D 106 ? 0.1280 0.1359 0.2609 -0.0214 0.0317  -0.0631 106 ARG D C   
7248  O O   . ARG D 106 ? 0.1123 0.1266 0.2632 -0.0231 0.0309  -0.0662 106 ARG D O   
7249  C CB  . ARG D 106 ? 0.1739 0.1769 0.2675 -0.0487 0.0503  -0.0688 106 ARG D CB  
7250  C CG  . ARG D 106 ? 0.2206 0.1967 0.2717 -0.0709 0.0632  -0.0647 106 ARG D CG  
7251  C CD  . ARG D 106 ? 0.2175 0.2363 0.2843 -0.0941 0.0737  -0.0776 106 ARG D CD  
7252  N NE  . ARG D 106 ? 0.2201 0.2463 0.2920 -0.1131 0.0764  -0.0796 106 ARG D NE  
7253  C CZ  . ARG D 106 ? 0.1981 0.2867 0.3067 -0.1228 0.0781  -0.0905 106 ARG D CZ  
7254  N NH1 . ARG D 106 ? 0.1741 0.3169 0.3170 -0.1088 0.0796  -0.1009 106 ARG D NH1 
7255  N NH2 . ARG D 106 ? 0.2067 0.3053 0.3146 -0.1449 0.0782  -0.0914 106 ARG D NH2 
7256  N N   . THR D 107 ? 0.1207 0.1408 0.2604 -0.0141 0.0238  -0.0638 107 THR D N   
7257  C CA  . THR D 107 ? 0.0999 0.1322 0.2639 -0.0109 0.0156  -0.0684 107 THR D CA  
7258  C C   . THR D 107 ? 0.0885 0.1189 0.2617 -0.0046 0.0120  -0.0591 107 THR D C   
7259  O O   . THR D 107 ? 0.0764 0.1063 0.2648 -0.0055 0.0098  -0.0618 107 THR D O   
7260  C CB  . THR D 107 ? 0.1087 0.1508 0.2674 -0.0143 0.0083  -0.0721 107 THR D CB  
7261  O OG1 . THR D 107 ? 0.1240 0.1635 0.2714 -0.0191 0.0138  -0.0843 107 THR D OG1 
7262  C CG2 . THR D 107 ? 0.1038 0.1459 0.2752 -0.0187 0.0012  -0.0759 107 THR D CG2 
7263  N N   . LEU D 108 ? 0.0990 0.1273 0.2592 0.0048  0.0123  -0.0475 108 LEU D N   
7264  C CA  . LEU D 108 ? 0.0943 0.1243 0.2607 0.0146  0.0125  -0.0396 108 LEU D CA  
7265  C C   . LEU D 108 ? 0.0973 0.1007 0.2576 0.0109  0.0197  -0.0417 108 LEU D C   
7266  O O   . LEU D 108 ? 0.0861 0.0929 0.2586 0.0103  0.0185  -0.0416 108 LEU D O   
7267  C CB  . LEU D 108 ? 0.1161 0.1500 0.2656 0.0352  0.0136  -0.0265 108 LEU D CB  
7268  C CG  . LEU D 108 ? 0.1158 0.1921 0.2722 0.0390  0.0032  -0.0221 108 LEU D CG  
7269  C CD1 . LEU D 108 ? 0.1395 0.2317 0.2843 0.0693  0.0035  -0.0064 108 LEU D CD1 
7270  C CD2 . LEU D 108 ? 0.0919 0.2064 0.2770 0.0209  -0.0052 -0.0288 108 LEU D CD2 
7271  N N   . ASP D 109 ? 0.1184 0.0966 0.2555 0.0035  0.0269  -0.0436 109 ASP D N   
7272  C CA  . ASP D 109 ? 0.1283 0.0870 0.2550 -0.0088 0.0325  -0.0472 109 ASP D CA  
7273  C C   . ASP D 109 ? 0.0989 0.0872 0.2564 -0.0183 0.0264  -0.0560 109 ASP D C   
7274  O O   . ASP D 109 ? 0.0993 0.0860 0.2577 -0.0243 0.0255  -0.0570 109 ASP D O   
7275  C CB  . ASP D 109 ? 0.1673 0.0956 0.2572 -0.0240 0.0422  -0.0480 109 ASP D CB  
7276  C CG  . ASP D 109 ? 0.2186 0.0954 0.2611 -0.0100 0.0498  -0.0370 109 ASP D CG  
7277  O OD1 . ASP D 109 ? 0.2284 0.0917 0.2649 0.0111  0.0507  -0.0306 109 ASP D OD1 
7278  O OD2 . ASP D 109 ? 0.2582 0.1059 0.2649 -0.0185 0.0563  -0.0343 109 ASP D OD2 
7279  N N   . PHE D 110 ? 0.0820 0.0944 0.2589 -0.0170 0.0225  -0.0622 110 PHE D N   
7280  C CA  . PHE D 110 ? 0.0662 0.1014 0.2670 -0.0148 0.0172  -0.0692 110 PHE D CA  
7281  C C   . PHE D 110 ? 0.0589 0.0861 0.2679 -0.0075 0.0097  -0.0645 110 PHE D C   
7282  O O   . PHE D 110 ? 0.0577 0.0906 0.2735 -0.0062 0.0054  -0.0643 110 PHE D O   
7283  C CB  . PHE D 110 ? 0.0663 0.1135 0.2739 -0.0093 0.0177  -0.0774 110 PHE D CB  
7284  C CG  . PHE D 110 ? 0.0661 0.1259 0.2900 0.0032  0.0140  -0.0843 110 PHE D CG  
7285  C CD1 . PHE D 110 ? 0.0630 0.1545 0.3017 0.0062  0.0141  -0.0869 110 PHE D CD1 
7286  C CD2 . PHE D 110 ? 0.0792 0.1183 0.2980 0.0126  0.0104  -0.0882 110 PHE D CD2 
7287  C CE1 . PHE D 110 ? 0.0717 0.1762 0.3228 0.0281  0.0103  -0.0912 110 PHE D CE1 
7288  C CE2 . PHE D 110 ? 0.0971 0.1310 0.3184 0.0309  0.0087  -0.0937 110 PHE D CE2 
7289  C CZ  . PHE D 110 ? 0.0927 0.1607 0.3317 0.0435  0.0085  -0.0943 110 PHE D CZ  
7290  N N   . HIS D 111 ? 0.0583 0.0776 0.2647 -0.0048 0.0078  -0.0599 111 HIS D N   
7291  C CA  . HIS D 111 ? 0.0576 0.0715 0.2670 -0.0047 0.0035  -0.0547 111 HIS D CA  
7292  C C   . HIS D 111 ? 0.0595 0.0671 0.2619 -0.0049 0.0069  -0.0489 111 HIS D C   
7293  O O   . HIS D 111 ? 0.0630 0.0653 0.2653 -0.0066 0.0034  -0.0464 111 HIS D O   
7294  C CB  . HIS D 111 ? 0.0586 0.0828 0.2683 -0.0077 0.0022  -0.0511 111 HIS D CB  
7295  C CG  . HIS D 111 ? 0.0687 0.0904 0.2763 -0.0146 -0.0023 -0.0584 111 HIS D CG  
7296  N ND1 . HIS D 111 ? 0.0876 0.0846 0.2881 -0.0186 -0.0058 -0.0631 111 HIS D ND1 
7297  C CD2 . HIS D 111 ? 0.0737 0.1064 0.2764 -0.0184 -0.0036 -0.0619 111 HIS D CD2 
7298  C CE1 . HIS D 111 ? 0.1075 0.0946 0.2959 -0.0257 -0.0074 -0.0712 111 HIS D CE1 
7299  N NE2 . HIS D 111 ? 0.0957 0.1092 0.2875 -0.0276 -0.0068 -0.0710 111 HIS D NE2 
7300  N N   . ASP D 112 ? 0.0683 0.0676 0.2557 -0.0031 0.0144  -0.0468 112 ASP D N   
7301  C CA  . ASP D 112 ? 0.0848 0.0651 0.2530 -0.0036 0.0206  -0.0439 112 ASP D CA  
7302  C C   . ASP D 112 ? 0.0884 0.0679 0.2541 -0.0166 0.0167  -0.0488 112 ASP D C   
7303  O O   . ASP D 112 ? 0.0971 0.0699 0.2542 -0.0202 0.0156  -0.0471 112 ASP D O   
7304  C CB  . ASP D 112 ? 0.1130 0.0667 0.2519 0.0029  0.0310  -0.0414 112 ASP D CB  
7305  C CG  . ASP D 112 ? 0.1452 0.0672 0.2539 0.0090  0.0408  -0.0389 112 ASP D CG  
7306  O OD1 . ASP D 112 ? 0.1387 0.0686 0.2538 0.0075  0.0397  -0.0386 112 ASP D OD1 
7307  O OD2 . ASP D 112 ? 0.1872 0.0683 0.2577 0.0156  0.0510  -0.0373 112 ASP D OD2 
7308  N N   . SER D 113 ? 0.0843 0.0788 0.2572 -0.0242 0.0146  -0.0547 113 SER D N   
7309  C CA  . SER D 113 ? 0.0860 0.1028 0.2643 -0.0359 0.0092  -0.0592 113 SER D CA  
7310  C C   . SER D 113 ? 0.0756 0.1100 0.2729 -0.0243 -0.0025 -0.0564 113 SER D C   
7311  O O   . SER D 113 ? 0.0846 0.1294 0.2775 -0.0299 -0.0090 -0.0549 113 SER D O   
7312  C CB  . SER D 113 ? 0.0825 0.1276 0.2711 -0.0435 0.0115  -0.0661 113 SER D CB  
7313  O OG  . SER D 113 ? 0.0783 0.1694 0.2850 -0.0484 0.0042  -0.0700 113 SER D OG  
7314  N N   . ASN D 114 ? 0.0673 0.0991 0.2778 -0.0095 -0.0054 -0.0554 114 ASN D N   
7315  C CA  . ASN D 114 ? 0.0756 0.1040 0.2903 0.0032  -0.0150 -0.0514 114 ASN D CA  
7316  C C   . ASN D 114 ? 0.0873 0.0943 0.2859 -0.0016 -0.0172 -0.0430 114 ASN D C   
7317  O O   . ASN D 114 ? 0.1031 0.1098 0.2958 0.0038  -0.0262 -0.0378 114 ASN D O   
7318  C CB  . ASN D 114 ? 0.0818 0.0921 0.2980 0.0133  -0.0147 -0.0537 114 ASN D CB  
7319  C CG  . ASN D 114 ? 0.0795 0.1097 0.3075 0.0227  -0.0120 -0.0631 114 ASN D CG  
7320  O OD1 . ASN D 114 ? 0.0762 0.1425 0.3173 0.0282  -0.0132 -0.0664 114 ASN D OD1 
7321  N ND2 . ASN D 114 ? 0.0849 0.0983 0.3075 0.0226  -0.0080 -0.0681 114 ASN D ND2 
7322  N N   . VAL D 115 ? 0.0846 0.0778 0.2747 -0.0093 -0.0086 -0.0408 115 VAL D N   
7323  C CA  . VAL D 115 ? 0.0976 0.0771 0.2719 -0.0147 -0.0062 -0.0341 115 VAL D CA  
7324  C C   . VAL D 115 ? 0.1108 0.0902 0.2686 -0.0220 -0.0071 -0.0348 115 VAL D C   
7325  O O   . VAL D 115 ? 0.1280 0.1005 0.2714 -0.0249 -0.0122 -0.0293 115 VAL D O   
7326  C CB  . VAL D 115 ? 0.0933 0.0736 0.2660 -0.0155 0.0055  -0.0326 115 VAL D CB  
7327  C CG1 . VAL D 115 ? 0.1097 0.0837 0.2654 -0.0194 0.0123  -0.0275 115 VAL D CG1 
7328  C CG2 . VAL D 115 ? 0.0861 0.0752 0.2721 -0.0165 0.0041  -0.0318 115 VAL D CG2 
7329  N N   . LYS D 116 ? 0.1116 0.0940 0.2642 -0.0288 -0.0019 -0.0415 116 LYS D N   
7330  C CA  . LYS D 116 ? 0.1351 0.1132 0.2634 -0.0448 -0.0019 -0.0452 116 LYS D CA  
7331  C C   . LYS D 116 ? 0.1361 0.1478 0.2742 -0.0482 -0.0182 -0.0438 116 LYS D C   
7332  O O   . LYS D 116 ? 0.1574 0.1686 0.2753 -0.0578 -0.0240 -0.0417 116 LYS D O   
7333  C CB  . LYS D 116 ? 0.1471 0.1158 0.2618 -0.0574 0.0068  -0.0529 116 LYS D CB  
7334  C CG  . LYS D 116 ? 0.1923 0.1166 0.2593 -0.0714 0.0187  -0.0570 116 LYS D CG  
7335  C CD  . LYS D 116 ? 0.2180 0.1503 0.2638 -0.0957 0.0107  -0.0610 116 LYS D CD  
7336  C CE  . LYS D 116 ? 0.2751 0.1481 0.2624 -0.1076 0.0246  -0.0662 116 LYS D CE  
7337  N NZ  . LYS D 116 ? 0.3203 0.1493 0.2670 -0.1266 0.0369  -0.0741 116 LYS D NZ  
7338  N N   . ASN D 117 ? 0.1179 0.1624 0.2850 -0.0374 -0.0255 -0.0450 117 ASN D N   
7339  C CA  . ASN D 117 ? 0.1216 0.2109 0.3030 -0.0307 -0.0410 -0.0427 117 ASN D CA  
7340  C C   . ASN D 117 ? 0.1387 0.2116 0.3111 -0.0129 -0.0519 -0.0311 117 ASN D C   
7341  O O   . ASN D 117 ? 0.1567 0.2553 0.3231 -0.0110 -0.0658 -0.0255 117 ASN D O   
7342  C CB  . ASN D 117 ? 0.1044 0.2319 0.3173 -0.0158 -0.0420 -0.0475 117 ASN D CB  
7343  C CG  . ASN D 117 ? 0.0978 0.2487 0.3143 -0.0394 -0.0323 -0.0577 117 ASN D CG  
7344  O OD1 . ASN D 117 ? 0.1147 0.2567 0.3070 -0.0687 -0.0281 -0.0613 117 ASN D OD1 
7345  N ND2 . ASN D 117 ? 0.0838 0.2574 0.3224 -0.0288 -0.0274 -0.0629 117 ASN D ND2 
7346  N N   . LEU D 118 ? 0.1401 0.1711 0.3072 -0.0030 -0.0459 -0.0267 118 LEU D N   
7347  C CA  . LEU D 118 ? 0.1692 0.1689 0.3156 0.0064  -0.0527 -0.0148 118 LEU D CA  
7348  C C   . LEU D 118 ? 0.1867 0.1736 0.3051 -0.0117 -0.0511 -0.0105 118 LEU D C   
7349  O O   . LEU D 118 ? 0.2172 0.1971 0.3143 -0.0077 -0.0621 -0.0004 118 LEU D O   
7350  C CB  . LEU D 118 ? 0.1730 0.1327 0.3155 0.0090  -0.0443 -0.0133 118 LEU D CB  
7351  C CG  . LEU D 118 ? 0.2154 0.1296 0.3265 0.0103  -0.0479 -0.0011 118 LEU D CG  
7352  C CD1 . LEU D 118 ? 0.2536 0.1595 0.3508 0.0363  -0.0638 0.0078  118 LEU D CD1 
7353  C CD2 . LEU D 118 ? 0.2236 0.1051 0.3297 0.0027  -0.0391 -0.0028 118 LEU D CD2 
7354  N N   . TYR D 119 ? 0.1762 0.1561 0.2889 -0.0284 -0.0366 -0.0179 119 TYR D N   
7355  C CA  . TYR D 119 ? 0.2002 0.1637 0.2809 -0.0434 -0.0307 -0.0171 119 TYR D CA  
7356  C C   . TYR D 119 ? 0.2208 0.2063 0.2856 -0.0551 -0.0435 -0.0186 119 TYR D C   
7357  O O   . TYR D 119 ? 0.2512 0.2287 0.2878 -0.0610 -0.0499 -0.0121 119 TYR D O   
7358  C CB  . TYR D 119 ? 0.1960 0.1430 0.2688 -0.0503 -0.0108 -0.0257 119 TYR D CB  
7359  C CG  . TYR D 119 ? 0.2312 0.1553 0.2639 -0.0621 -0.0009 -0.0279 119 TYR D CG  
7360  C CD1 . TYR D 119 ? 0.2469 0.1585 0.2645 -0.0606 0.0074  -0.0212 119 TYR D CD1 
7361  C CD2 . TYR D 119 ? 0.2579 0.1700 0.2613 -0.0784 0.0017  -0.0378 119 TYR D CD2 
7362  C CE1 . TYR D 119 ? 0.2847 0.1753 0.2620 -0.0692 0.0192  -0.0247 119 TYR D CE1 
7363  C CE2 . TYR D 119 ? 0.3025 0.1830 0.2591 -0.0891 0.0128  -0.0423 119 TYR D CE2 
7364  C CZ  . TYR D 119 ? 0.3139 0.1853 0.2591 -0.0815 0.0219  -0.0358 119 TYR D CZ  
7365  O OH  . TYR D 119 ? 0.3628 0.2034 0.2587 -0.0897 0.0356  -0.0414 119 TYR D OH  
7366  N N   . ASP D 120 ? 0.2092 0.2268 0.2897 -0.0626 -0.0473 -0.0273 120 ASP D N   
7367  C CA  . ASP D 120 ? 0.2303 0.2842 0.2983 -0.0817 -0.0604 -0.0305 120 ASP D CA  
7368  C C   . ASP D 120 ? 0.2382 0.3326 0.3180 -0.0626 -0.0836 -0.0179 120 ASP D C   
7369  O O   . ASP D 120 ? 0.2672 0.3817 0.3242 -0.0744 -0.0971 -0.0141 120 ASP D O   
7370  C CB  . ASP D 120 ? 0.2194 0.3060 0.3027 -0.0994 -0.0576 -0.0424 120 ASP D CB  
7371  C CG  . ASP D 120 ? 0.2362 0.2700 0.2890 -0.1196 -0.0361 -0.0533 120 ASP D CG  
7372  O OD1 . ASP D 120 ? 0.2695 0.2543 0.2804 -0.1282 -0.0260 -0.0553 120 ASP D OD1 
7373  O OD2 . ASP D 120 ? 0.2247 0.2628 0.2900 -0.1246 -0.0283 -0.0596 120 ASP D OD2 
7374  N N   . LYS D 121 ? 0.2221 0.3237 0.3309 -0.0312 -0.0880 -0.0112 121 LYS D N   
7375  C CA  . LYS D 121 ? 0.2436 0.3685 0.3562 -0.0010 -0.1080 0.0027  121 LYS D CA  
7376  C C   . LYS D 121 ? 0.2855 0.3709 0.3551 -0.0021 -0.1149 0.0162  121 LYS D C   
7377  O O   . LYS D 121 ? 0.3155 0.4323 0.3720 0.0055  -0.1348 0.0264  121 LYS D O   
7378  C CB  . LYS D 121 ? 0.2374 0.3396 0.3687 0.0326  -0.1045 0.0060  121 LYS D CB  
7379  C CG  . LYS D 121 ? 0.2724 0.3876 0.4026 0.0745  -0.1223 0.0198  121 LYS D CG  
7380  C CD  . LYS D 121 ? 0.2804 0.3510 0.4150 0.1032  -0.1137 0.0192  121 LYS D CD  
7381  C CE  . LYS D 121 ? 0.3164 0.4103 0.4564 0.1542  -0.1272 0.0275  121 LYS D CE  
7382  N NZ  . LYS D 121 ? 0.3870 0.4205 0.4778 0.1810  -0.1395 0.0478  121 LYS D NZ  
7383  N N   . VAL D 122 ? 0.2905 0.3140 0.3382 -0.0124 -0.0984 0.0168  122 VAL D N   
7384  C CA  . VAL D 122 ? 0.3323 0.3160 0.3355 -0.0201 -0.0992 0.0282  122 VAL D CA  
7385  C C   . VAL D 122 ? 0.3498 0.3510 0.3261 -0.0483 -0.1011 0.0223  122 VAL D C   
7386  O O   . VAL D 122 ? 0.3897 0.3964 0.3346 -0.0497 -0.1166 0.0330  122 VAL D O   
7387  C CB  . VAL D 122 ? 0.3302 0.2605 0.3229 -0.0283 -0.0778 0.0282  122 VAL D CB  
7388  C CG1 . VAL D 122 ? 0.3719 0.2696 0.3179 -0.0447 -0.0726 0.0368  122 VAL D CG1 
7389  C CG2 . VAL D 122 ? 0.3365 0.2381 0.3381 -0.0072 -0.0791 0.0355  122 VAL D CG2 
7390  N N   . ARG D 123 ? 0.3309 0.3339 0.3116 -0.0707 -0.0853 0.0053  123 ARG D N   
7391  C CA  . ARG D 123 ? 0.3617 0.3647 0.3049 -0.1013 -0.0833 -0.0041 123 ARG D CA  
7392  C C   . ARG D 123 ? 0.3835 0.4449 0.3223 -0.1098 -0.1101 -0.0006 123 ARG D C   
7393  O O   . ARG D 123 ? 0.4267 0.4858 0.3226 -0.1278 -0.1184 0.0017  123 ARG D O   
7394  C CB  . ARG D 123 ? 0.3492 0.3387 0.2939 -0.1196 -0.0640 -0.0226 123 ARG D CB  
7395  C CG  . ARG D 123 ? 0.3985 0.3585 0.2876 -0.1519 -0.0545 -0.0352 123 ARG D CG  
7396  C CD  . ARG D 123 ? 0.4042 0.3334 0.2829 -0.1662 -0.0347 -0.0518 123 ARG D CD  
7397  N NE  . ARG D 123 ? 0.3740 0.3482 0.2914 -0.1713 -0.0441 -0.0552 123 ARG D NE  
7398  C CZ  . ARG D 123 ? 0.3875 0.4130 0.3042 -0.1992 -0.0608 -0.0600 123 ARG D CZ  
7399  N NH1 . ARG D 123 ? 0.4325 0.4704 0.3097 -0.2264 -0.0733 -0.0621 123 ARG D NH1 
7400  N NH2 . ARG D 123 ? 0.3584 0.4308 0.3139 -0.2023 -0.0651 -0.0631 123 ARG D NH2 
7401  N N   . LEU D 124 ? 0.3568 0.4779 0.3401 -0.0966 -0.1234 -0.0004 124 LEU D N   
7402  C CA  . LEU D 124 ? 0.3726 0.5754 0.3641 -0.1023 -0.1498 0.0027  124 LEU D CA  
7403  C C   . LEU D 124 ? 0.4075 0.6257 0.3846 -0.0730 -0.1740 0.0247  124 LEU D C   
7404  O O   . LEU D 124 ? 0.4358 0.7149 0.4011 -0.0830 -0.1971 0.0293  124 LEU D O   
7405  C CB  . LEU D 124 ? 0.3339 0.6064 0.3814 -0.0913 -0.1539 -0.0028 124 LEU D CB  
7406  C CG  . LEU D 124 ? 0.3158 0.5843 0.3688 -0.1278 -0.1346 -0.0232 124 LEU D CG  
7407  C CD1 . LEU D 124 ? 0.2748 0.5931 0.3826 -0.1092 -0.1320 -0.0266 124 LEU D CD1 
7408  C CD2 . LEU D 124 ? 0.3522 0.6551 0.3733 -0.1804 -0.1413 -0.0350 124 LEU D CD2 
7409  N N   . GLN D 125 ? 0.4147 0.5765 0.3873 -0.0391 -0.1693 0.0388  125 GLN D N   
7410  C CA  . GLN D 125 ? 0.4657 0.6139 0.4075 -0.0112 -0.1888 0.0620  125 GLN D CA  
7411  C C   . GLN D 125 ? 0.5106 0.6176 0.3924 -0.0403 -0.1869 0.0656  125 GLN D C   
7412  O O   . GLN D 125 ? 0.5548 0.6916 0.4066 -0.0401 -0.2100 0.0777  125 GLN D O   
7413  C CB  . GLN D 125 ? 0.4759 0.5560 0.4155 0.0244  -0.1804 0.0745  125 GLN D CB  
7414  C CG  . GLN D 125 ? 0.4538 0.5634 0.4394 0.0632  -0.1841 0.0742  125 GLN D CG  
7415  C CD  . GLN D 125 ? 0.4838 0.5084 0.4499 0.0919  -0.1751 0.0850  125 GLN D CD  
7416  O OE1 . GLN D 125 ? 0.5502 0.5298 0.4724 0.1168  -0.1871 0.1057  125 GLN D OE1 
7417  N NE2 . GLN D 125 ? 0.4459 0.4429 0.4368 0.0858  -0.1544 0.0716  125 GLN D NE2 
7418  N N   . LEU D 126 ? 0.5035 0.5469 0.3672 -0.0627 -0.1590 0.0554  126 LEU D N   
7419  C CA  . LEU D 126 ? 0.5498 0.5479 0.3547 -0.0867 -0.1506 0.0577  126 LEU D CA  
7420  C C   . LEU D 126 ? 0.5753 0.6054 0.3506 -0.1231 -0.1572 0.0447  126 LEU D C   
7421  O O   . LEU D 126 ? 0.6285 0.6488 0.3516 -0.1362 -0.1666 0.0525  126 LEU D O   
7422  C CB  . LEU D 126 ? 0.5341 0.4720 0.3340 -0.0970 -0.1168 0.0490  126 LEU D CB  
7423  C CG  . LEU D 126 ? 0.5187 0.4216 0.3397 -0.0733 -0.1082 0.0596  126 LEU D CG  
7424  C CD1 . LEU D 126 ? 0.5175 0.3781 0.3249 -0.0894 -0.0778 0.0542  126 LEU D CD1 
7425  C CD2 . LEU D 126 ? 0.5691 0.4509 0.3625 -0.0496 -0.1290 0.0845  126 LEU D CD2 
7426  N N   . ARG D 127 ? 0.5483 0.6115 0.3491 -0.1432 -0.1523 0.0248  127 ARG D N   
7427  C CA  . ARG D 127 ? 0.5849 0.6696 0.3488 -0.1867 -0.1570 0.0092  127 ARG D CA  
7428  C C   . ARG D 127 ? 0.6372 0.6498 0.3327 -0.2102 -0.1360 0.0017  127 ARG D C   
7429  O O   . ARG D 127 ? 0.6246 0.5790 0.3181 -0.2029 -0.1062 -0.0046 127 ARG D O   
7430  C CB  . ARG D 127 ? 0.6076 0.7797 0.3741 -0.1885 -0.1951 0.0204  127 ARG D CB  
7431  C CG  . ARG D 127 ? 0.5618 0.8198 0.3951 -0.1750 -0.2094 0.0191  127 ARG D CG  
7432  C CD  . ARG D 127 ? 0.5671 0.9053 0.4285 -0.1340 -0.2436 0.0424  127 ARG D CD  
7433  N NE  . ARG D 127 ? 0.6192 1.0216 0.4482 -0.1465 -0.2756 0.0529  127 ARG D NE  
7434  C CZ  . ARG D 127 ? 0.6547 1.0913 0.4471 -0.2022 -0.2837 0.0385  127 ARG D CZ  
7435  N NH1 . ARG D 127 ? 0.6543 1.0558 0.4278 -0.2544 -0.2602 0.0115  127 ARG D NH1 
7436  N NH2 . ARG D 127 ? 0.7025 1.2063 0.4690 -0.2062 -0.3171 0.0521  127 ARG D NH2 
7437  N N   . ASP D 128 ? 0.6980 0.7196 0.3378 -0.2359 -0.1508 0.0026  128 ASP D N   
7438  C CA  . ASP D 128 ? 0.7566 0.7101 0.3249 -0.2586 -0.1287 -0.0068 128 ASP D CA  
7439  C C   . ASP D 128 ? 0.7813 0.7045 0.3231 -0.2383 -0.1280 0.0146  128 ASP D C   
7440  O O   . ASP D 128 ? 0.8389 0.7205 0.3160 -0.2577 -0.1150 0.0102  128 ASP D O   
7441  C CB  . ASP D 128 ? 0.8231 0.7899 0.3301 -0.3068 -0.1408 -0.0219 128 ASP D CB  
7442  C CG  . ASP D 128 ? 0.8508 0.8901 0.3484 -0.3097 -0.1826 -0.0030 128 ASP D CG  
7443  O OD1 . ASP D 128 ? 0.8213 0.8972 0.3609 -0.2686 -0.2023 0.0221  128 ASP D OD1 
7444  O OD2 . ASP D 128 ? 0.9117 0.9687 0.3542 -0.3523 -0.1961 -0.0133 128 ASP D OD2 
7445  N N   . ASN D 129 ? 0.7489 0.6861 0.3324 -0.2017 -0.1400 0.0371  129 ASN D N   
7446  C CA  . ASN D 129 ? 0.7809 0.6766 0.3341 -0.1861 -0.1366 0.0588  129 ASN D CA  
7447  C C   . ASN D 129 ? 0.7585 0.6019 0.3210 -0.1811 -0.0990 0.0540  129 ASN D C   
7448  O O   . ASN D 129 ? 0.7879 0.5967 0.3247 -0.1759 -0.0918 0.0706  129 ASN D O   
7449  C CB  . ASN D 129 ? 0.7808 0.6997 0.3574 -0.1494 -0.1664 0.0863  129 ASN D CB  
7450  C CG  . ASN D 129 ? 0.8314 0.7996 0.3774 -0.1485 -0.2048 0.1010  129 ASN D CG  
7451  O OD1 . ASN D 129 ? 0.8562 0.8568 0.3742 -0.1815 -0.2131 0.0877  129 ASN D OD1 
7452  N ND2 . ASN D 129 ? 0.8570 0.8286 0.4023 -0.1098 -0.2288 0.1291  129 ASN D ND2 
7453  N N   . ALA D 130 ? 0.7134 0.5542 0.3091 -0.1840 -0.0757 0.0326  130 ALA D N   
7454  C CA  . ALA D 130 ? 0.6920 0.5013 0.3006 -0.1777 -0.0408 0.0267  130 ALA D CA  
7455  C C   . ALA D 130 ? 0.6843 0.4804 0.2909 -0.1861 -0.0148 0.0006  130 ALA D C   
7456  O O   . ALA D 130 ? 0.6791 0.4868 0.2902 -0.1958 -0.0242 -0.0123 130 ALA D O   
7457  C CB  . ALA D 130 ? 0.6379 0.4565 0.3064 -0.1533 -0.0432 0.0372  130 ALA D CB  
7458  N N   . LYS D 131 ? 0.6922 0.4641 0.2880 -0.1817 0.0187  -0.0061 131 LYS D N   
7459  C CA  . LYS D 131 ? 0.6967 0.4464 0.2855 -0.1777 0.0471  -0.0286 131 LYS D CA  
7460  C C   . LYS D 131 ? 0.6303 0.3978 0.2856 -0.1552 0.0516  -0.0302 131 LYS D C   
7461  O O   . LYS D 131 ? 0.5911 0.3801 0.2883 -0.1407 0.0559  -0.0186 131 LYS D O   
7462  C CB  . LYS D 131 ? 0.7360 0.4656 0.2901 -0.1729 0.0827  -0.0339 131 LYS D CB  
7463  C CG  . LYS D 131 ? 0.8112 0.5174 0.2906 -0.1954 0.0851  -0.0343 131 LYS D CG  
7464  C CD  . LYS D 131 ? 0.8386 0.5442 0.2993 -0.1881 0.1205  -0.0340 131 LYS D CD  
7465  C CE  . LYS D 131 ? 0.9269 0.5957 0.3013 -0.2055 0.1374  -0.0458 131 LYS D CE  
7466  N NZ  . LYS D 131 ? 0.9733 0.5945 0.3044 -0.2015 0.1557  -0.0731 131 LYS D NZ  
7467  N N   . GLU D 132 ? 0.6255 0.3811 0.2838 -0.1568 0.0508  -0.0447 132 GLU D N   
7468  C CA  . GLU D 132 ? 0.5744 0.3396 0.2844 -0.1358 0.0580  -0.0474 132 GLU D CA  
7469  C C   . GLU D 132 ? 0.5943 0.3357 0.2918 -0.1138 0.0934  -0.0566 132 GLU D C   
7470  O O   . GLU D 132 ? 0.6498 0.3426 0.2962 -0.1139 0.1115  -0.0727 132 GLU D O   
7471  C CB  . GLU D 132 ? 0.5728 0.3313 0.2828 -0.1493 0.0452  -0.0581 132 GLU D CB  
7472  C CG  . GLU D 132 ? 0.5227 0.2908 0.2826 -0.1298 0.0495  -0.0590 132 GLU D CG  
7473  C CD  . GLU D 132 ? 0.5170 0.2917 0.2829 -0.1487 0.0338  -0.0660 132 GLU D CD  
7474  O OE1 . GLU D 132 ? 0.5658 0.3254 0.2854 -0.1800 0.0268  -0.0757 132 GLU D OE1 
7475  O OE2 . GLU D 132 ? 0.4670 0.2660 0.2823 -0.1359 0.0289  -0.0623 132 GLU D OE2 
7476  N N   . LEU D 133 ? 0.5576 0.3337 0.2977 -0.0947 0.1036  -0.0464 133 LEU D N   
7477  C CA  . LEU D 133 ? 0.5761 0.3545 0.3115 -0.0696 0.1369  -0.0520 133 LEU D CA  
7478  C C   . LEU D 133 ? 0.5762 0.3369 0.3207 -0.0413 0.1506  -0.0616 133 LEU D C   
7479  O O   . LEU D 133 ? 0.6182 0.3618 0.3360 -0.0148 0.1794  -0.0700 133 LEU D O   
7480  C CB  . LEU D 133 ? 0.5382 0.3741 0.3184 -0.0656 0.1418  -0.0376 133 LEU D CB  
7481  C CG  . LEU D 133 ? 0.5758 0.4200 0.3232 -0.0821 0.1530  -0.0317 133 LEU D CG  
7482  C CD1 . LEU D 133 ? 0.6236 0.4249 0.3122 -0.1071 0.1384  -0.0330 133 LEU D CD1 
7483  C CD2 . LEU D 133 ? 0.5416 0.4297 0.3281 -0.0958 0.1453  -0.0143 133 LEU D CD2 
7484  N N   . GLY D 134 ? 0.5375 0.3012 0.3153 -0.0437 0.1314  -0.0596 134 GLY D N   
7485  C CA  . GLY D 134 ? 0.5428 0.2840 0.3240 -0.0194 0.1416  -0.0658 134 GLY D CA  
7486  C C   . GLY D 134 ? 0.4843 0.2818 0.3313 0.0047  0.1410  -0.0554 134 GLY D C   
7487  O O   . GLY D 134 ? 0.4869 0.2714 0.3389 0.0280  0.1473  -0.0574 134 GLY D O   
7488  N N   . ASN D 135 ? 0.4413 0.2965 0.3316 -0.0040 0.1328  -0.0440 135 ASN D N   
7489  C CA  . ASN D 135 ? 0.3936 0.3084 0.3412 0.0105  0.1327  -0.0352 135 ASN D CA  
7490  C C   . ASN D 135 ? 0.3387 0.2771 0.3270 -0.0111 0.1071  -0.0264 135 ASN D C   
7491  O O   . ASN D 135 ? 0.3059 0.2909 0.3345 -0.0100 0.1052  -0.0196 135 ASN D O   
7492  C CB  . ASN D 135 ? 0.4077 0.3735 0.3637 0.0183  0.1533  -0.0311 135 ASN D CB  
7493  C CG  . ASN D 135 ? 0.4241 0.3918 0.3631 -0.0136 0.1493  -0.0255 135 ASN D CG  
7494  O OD1 . ASN D 135 ? 0.4235 0.3579 0.3482 -0.0369 0.1284  -0.0229 135 ASN D OD1 
7495  N ND2 . ASN D 135 ? 0.4467 0.4568 0.3849 -0.0133 0.1700  -0.0229 135 ASN D ND2 
7496  N N   . GLY D 136 ? 0.3354 0.2433 0.3099 -0.0302 0.0878  -0.0269 136 GLY D N   
7497  C CA  . GLY D 136 ? 0.2997 0.2208 0.3026 -0.0439 0.0652  -0.0187 136 GLY D CA  
7498  C C   . GLY D 136 ? 0.3175 0.2332 0.3015 -0.0624 0.0573  -0.0092 136 GLY D C   
7499  O O   . GLY D 136 ? 0.3082 0.2194 0.3014 -0.0693 0.0385  -0.0015 136 GLY D O   
7500  N N   . CYS D 137 ? 0.3515 0.2623 0.3027 -0.0678 0.0727  -0.0093 137 CYS D N   
7501  C CA  . CYS D 137 ? 0.3810 0.2817 0.3043 -0.0871 0.0676  0.0014  137 CYS D CA  
7502  C C   . CYS D 137 ? 0.4183 0.2880 0.2954 -0.0957 0.0588  -0.0008 137 CYS D C   
7503  O O   . CYS D 137 ? 0.4352 0.2896 0.2905 -0.0919 0.0667  -0.0136 137 CYS D O   
7504  C CB  . CYS D 137 ? 0.3999 0.3263 0.3165 -0.0937 0.0918  0.0044  137 CYS D CB  
7505  S SG  . CYS D 137 ? 0.3614 0.3432 0.3315 -0.0930 0.1001  0.0078  137 CYS D SG  
7506  N N   . PHE D 138 ? 0.4403 0.2965 0.2960 -0.1084 0.0416  0.0123  138 PHE D N   
7507  C CA  . PHE D 138 ? 0.4827 0.3190 0.2911 -0.1192 0.0299  0.0139  138 PHE D CA  
7508  C C   . PHE D 138 ? 0.5304 0.3525 0.2973 -0.1345 0.0377  0.0262  138 PHE D C   
7509  O O   . PHE D 138 ? 0.5382 0.3525 0.3072 -0.1392 0.0317  0.0414  138 PHE D O   
7510  C CB  . PHE D 138 ? 0.4752 0.3142 0.2929 -0.1146 -0.0021 0.0221  138 PHE D CB  
7511  C CG  . PHE D 138 ? 0.4333 0.2924 0.2883 -0.1053 -0.0096 0.0102  138 PHE D CG  
7512  C CD1 . PHE D 138 ? 0.4470 0.3084 0.2823 -0.1165 -0.0123 -0.0028 138 PHE D CD1 
7513  C CD2 . PHE D 138 ? 0.3885 0.2608 0.2912 -0.0906 -0.0126 0.0113  138 PHE D CD2 
7514  C CE1 . PHE D 138 ? 0.4173 0.2952 0.2808 -0.1148 -0.0172 -0.0132 138 PHE D CE1 
7515  C CE2 . PHE D 138 ? 0.3549 0.2461 0.2879 -0.0845 -0.0176 0.0008  138 PHE D CE2 
7516  C CZ  . PHE D 138 ? 0.3693 0.2642 0.2832 -0.0975 -0.0195 -0.0107 138 PHE D CZ  
7517  N N   . GLU D 139 ? 0.5726 0.3839 0.2937 -0.1444 0.0525  0.0189  139 GLU D N   
7518  C CA  . GLU D 139 ? 0.6251 0.4240 0.2995 -0.1618 0.0632  0.0293  139 GLU D CA  
7519  C C   . GLU D 139 ? 0.6751 0.4492 0.2972 -0.1733 0.0384  0.0389  139 GLU D C   
7520  O O   . GLU D 139 ? 0.6927 0.4621 0.2895 -0.1772 0.0324  0.0268  139 GLU D O   
7521  C CB  . GLU D 139 ? 0.6476 0.4544 0.3015 -0.1618 0.0988  0.0144  139 GLU D CB  
7522  C CG  . GLU D 139 ? 0.7045 0.5068 0.3096 -0.1818 0.1163  0.0227  139 GLU D CG  
7523  C CD  . GLU D 139 ? 0.7335 0.5459 0.3156 -0.1745 0.1533  0.0048  139 GLU D CD  
7524  O OE1 . GLU D 139 ? 0.7007 0.5487 0.3253 -0.1539 0.1755  -0.0042 139 GLU D OE1 
7525  O OE2 . GLU D 139 ? 0.7954 0.5800 0.3135 -0.1863 0.1602  -0.0001 139 GLU D OE2 
7526  N N   . PHE D 140 ? 0.7076 0.4629 0.3069 -0.1801 0.0238  0.0610  140 PHE D N   
7527  C CA  . PHE D 140 ? 0.7573 0.4940 0.3100 -0.1830 -0.0057 0.0755  140 PHE D CA  
7528  C C   . PHE D 140 ? 0.8251 0.5458 0.3072 -0.2048 0.0042  0.0746  140 PHE D C   
7529  O O   . PHE D 140 ? 0.8491 0.5625 0.3087 -0.2190 0.0343  0.0725  140 PHE D O   
7530  C CB  . PHE D 140 ? 0.7847 0.4913 0.3262 -0.1763 -0.0240 0.1019  140 PHE D CB  
7531  C CG  . PHE D 140 ? 0.7339 0.4485 0.3324 -0.1524 -0.0379 0.1030  140 PHE D CG  
7532  C CD1 . PHE D 140 ? 0.6991 0.4128 0.3353 -0.1545 -0.0191 0.0988  140 PHE D CD1 
7533  C CD2 . PHE D 140 ? 0.7248 0.4552 0.3385 -0.1284 -0.0693 0.1077  140 PHE D CD2 
7534  C CE1 . PHE D 140 ? 0.6600 0.3763 0.3415 -0.1340 -0.0308 0.0983  140 PHE D CE1 
7535  C CE2 . PHE D 140 ? 0.6835 0.4223 0.3469 -0.1043 -0.0791 0.1074  140 PHE D CE2 
7536  C CZ  . PHE D 140 ? 0.6532 0.3786 0.3471 -0.1075 -0.0594 0.1022  140 PHE D CZ  
7537  N N   . TYR D 141 ? 0.8594 0.5819 0.3062 -0.2088 -0.0207 0.0756  141 TYR D N   
7538  C CA  . TYR D 141 ? 0.9362 0.6394 0.3053 -0.2314 -0.0169 0.0769  141 TYR D CA  
7539  C C   . TYR D 141 ? 0.9978 0.6696 0.3188 -0.2358 -0.0286 0.1072  141 TYR D C   
7540  O O   . TYR D 141 ? 1.0579 0.7057 0.3197 -0.2570 -0.0099 0.1115  141 TYR D O   
7541  C CB  . TYR D 141 ? 0.9578 0.6787 0.3013 -0.2403 -0.0423 0.0673  141 TYR D CB  
7542  C CG  . TYR D 141 ? 0.9257 0.6570 0.2921 -0.2451 -0.0267 0.0366  141 TYR D CG  
7543  C CD1 . TYR D 141 ? 0.9488 0.6532 0.2867 -0.2542 0.0124  0.0152  141 TYR D CD1 
7544  C CD2 . TYR D 141 ? 0.8818 0.6463 0.2932 -0.2390 -0.0489 0.0293  141 TYR D CD2 
7545  C CE1 . TYR D 141 ? 0.9376 0.6330 0.2829 -0.2548 0.0280  -0.0114 141 TYR D CE1 
7546  C CE2 . TYR D 141 ? 0.8667 0.6269 0.2874 -0.2475 -0.0333 0.0026  141 TYR D CE2 
7547  C CZ  . TYR D 141 ? 0.8991 0.6172 0.2825 -0.2543 0.0046  -0.0171 141 TYR D CZ  
7548  O OH  . TYR D 141 ? 0.9019 0.5982 0.2814 -0.2591 0.0210  -0.0422 141 TYR D OH  
7549  N N   . HIS D 142 ? 0.9923 0.6592 0.3332 -0.2141 -0.0580 0.1281  142 HIS D N   
7550  C CA  . HIS D 142 ? 1.0626 0.6810 0.3522 -0.2125 -0.0697 0.1595  142 HIS D CA  
7551  C C   . HIS D 142 ? 1.0511 0.6393 0.3617 -0.2168 -0.0459 0.1652  142 HIS D C   
7552  O O   . HIS D 142 ? 0.9780 0.5923 0.3567 -0.2091 -0.0329 0.1491  142 HIS D O   
7553  C CB  . HIS D 142 ? 1.0816 0.7028 0.3703 -0.1798 -0.1139 0.1806  142 HIS D CB  
7554  C CG  . HIS D 142 ? 1.0064 0.6593 0.3748 -0.1499 -0.1246 0.1726  142 HIS D CG  
7555  N ND1 . HIS D 142 ? 1.0074 0.6225 0.3929 -0.1278 -0.1265 0.1864  142 HIS D ND1 
7556  C CD2 . HIS D 142 ? 0.9369 0.6511 0.3657 -0.1418 -0.1323 0.1514  142 HIS D CD2 
7557  C CE1 . HIS D 142 ? 0.9368 0.5937 0.3931 -0.1041 -0.1348 0.1737  142 HIS D CE1 
7558  N NE2 . HIS D 142 ? 0.8917 0.6112 0.3767 -0.1130 -0.1383 0.1533  142 HIS D NE2 
7559  N N   . LYS D 143 ? 1.1321 0.6639 0.3779 -0.2332 -0.0408 0.1885  143 LYS D N   
7560  C CA  . LYS D 143 ? 1.1431 0.6377 0.3938 -0.2458 -0.0223 0.1971  143 LYS D CA  
7561  C C   . LYS D 143 ? 1.1291 0.5988 0.4099 -0.2111 -0.0485 0.2071  143 LYS D C   
7562  O O   . LYS D 143 ? 1.1760 0.6180 0.4243 -0.1821 -0.0810 0.2264  143 LYS D O   
7563  C CB  . LYS D 143 ? 1.2528 0.6814 0.4108 -0.2766 -0.0128 0.2220  143 LYS D CB  
7564  C CG  . LYS D 143 ? 1.2737 0.6731 0.4273 -0.3097 0.0155  0.2262  143 LYS D CG  
7565  C CD  . LYS D 143 ? 1.3971 0.7241 0.4471 -0.3460 0.0246  0.2525  143 LYS D CD  
7566  C CE  . LYS D 143 ? 1.4491 0.7161 0.4742 -0.3774 0.0395  0.2649  143 LYS D CE  
7567  N NZ  . LYS D 143 ? 1.4919 0.6752 0.4957 -0.3449 0.0095  0.2830  143 LYS D NZ  
7568  N N   . CYS D 144 ? 1.0690 0.5532 0.4106 -0.2110 -0.0342 0.1938  144 CYS D N   
7569  C CA  . CYS D 144 ? 1.0500 0.5152 0.4249 -0.1772 -0.0545 0.1975  144 CYS D CA  
7570  C C   . CYS D 144 ? 1.0992 0.4954 0.4471 -0.1964 -0.0411 0.2080  144 CYS D C   
7571  O O   . CYS D 144 ? 1.0524 0.4761 0.4422 -0.2210 -0.0170 0.1924  144 CYS D O   
7572  C CB  . CYS D 144 ? 0.9392 0.4800 0.4066 -0.1603 -0.0526 0.1703  144 CYS D CB  
7573  S SG  . CYS D 144 ? 0.9073 0.4456 0.4222 -0.1140 -0.0780 0.1705  144 CYS D SG  
7574  N N   . ASP D 145 ? 1.2038 0.5078 0.4751 -0.1859 -0.0572 0.2351  145 ASP D N   
7575  C CA  . ASP D 145 ? 1.2793 0.4930 0.5025 -0.2085 -0.0455 0.2466  145 ASP D CA  
7576  C C   . ASP D 145 ? 1.2372 0.4448 0.5116 -0.1808 -0.0521 0.2349  145 ASP D C   
7577  O O   . ASP D 145 ? 1.1440 0.4244 0.4946 -0.1459 -0.0639 0.2185  145 ASP D O   
7578  C CB  . ASP D 145 ? 1.4263 0.5234 0.5338 -0.2039 -0.0593 0.2809  145 ASP D CB  
7579  C CG  . ASP D 145 ? 1.4599 0.5279 0.5523 -0.1352 -0.0965 0.2971  145 ASP D CG  
7580  O OD1 . ASP D 145 ? 1.3694 0.5081 0.5423 -0.0954 -0.1105 0.2809  145 ASP D OD1 
7581  O OD2 . ASP D 145 ? 1.5836 0.5603 0.5808 -0.1196 -0.1116 0.3273  145 ASP D OD2 
7582  N N   . ASN D 146 ? 1.3137 0.4310 0.5397 -0.2007 -0.0432 0.2423  146 ASN D N   
7583  C CA  . ASN D 146 ? 1.2872 0.3888 0.5504 -0.1807 -0.0459 0.2294  146 ASN D CA  
7584  C C   . ASN D 146 ? 1.3023 0.3790 0.5678 -0.1085 -0.0750 0.2368  146 ASN D C   
7585  O O   . ASN D 146 ? 1.2392 0.3496 0.5655 -0.0815 -0.0788 0.2200  146 ASN D O   
7586  C CB  . ASN D 146 ? 1.3865 0.3842 0.5803 -0.2262 -0.0288 0.2350  146 ASN D CB  
7587  C CG  . ASN D 146 ? 1.3528 0.4077 0.5681 -0.2986 0.0012  0.2225  146 ASN D CG  
7588  O OD1 . ASN D 146 ? 1.2432 0.4178 0.5369 -0.3054 0.0110  0.2060  146 ASN D OD1 
7589  N ND2 . ASN D 146 ? 1.4559 0.4250 0.5974 -0.3530 0.0170  0.2301  146 ASN D ND2 
7590  N N   . GLU D 147 ? 1.3885 0.4147 0.5886 -0.0758 -0.0955 0.2625  147 GLU D N   
7591  C CA  . GLU D 147 ? 1.3989 0.4304 0.6093 -0.0011 -0.1250 0.2711  147 GLU D CA  
7592  C C   . GLU D 147 ? 1.2672 0.4449 0.5774 0.0178  -0.1370 0.2533  147 GLU D C   
7593  O O   . GLU D 147 ? 1.2116 0.4425 0.5823 0.0610  -0.1494 0.2424  147 GLU D O   
7594  C CB  . GLU D 147 ? 1.5350 0.4789 0.6438 0.0307  -0.1455 0.3064  147 GLU D CB  
7595  C CG  . GLU D 147 ? 1.6956 0.4711 0.6836 0.0125  -0.1344 0.3276  147 GLU D CG  
7596  C CD  . GLU D 147 ? 1.7470 0.4847 0.6730 -0.0616 -0.1135 0.3367  147 GLU D CD  
7597  O OE1 . GLU D 147 ? 1.6733 0.4638 0.6463 -0.1230 -0.0871 0.3146  147 GLU D OE1 
7598  O OE2 . GLU D 147 ? 1.8639 0.5254 0.6940 -0.0570 -0.1235 0.3665  147 GLU D OE2 
7599  N N   . CYS D 148 ? 1.2292 0.4665 0.5492 -0.0173 -0.1313 0.2498  148 CYS D N   
7600  C CA  . CYS D 148 ? 1.1186 0.4792 0.5184 -0.0133 -0.1377 0.2303  148 CYS D CA  
7601  C C   . CYS D 148 ? 1.0115 0.4331 0.4999 -0.0216 -0.1218 0.2008  148 CYS D C   
7602  O O   . CYS D 148 ? 0.9395 0.4373 0.4921 0.0043  -0.1336 0.1873  148 CYS D O   
7603  C CB  . CYS D 148 ? 1.1147 0.5042 0.4923 -0.0559 -0.1268 0.2293  148 CYS D CB  
7604  S SG  . CYS D 148 ? 0.9933 0.5073 0.4519 -0.0682 -0.1227 0.1994  148 CYS D SG  
7605  N N   . MET D 149 ? 1.0085 0.3999 0.4974 -0.0599 -0.0956 0.1917  149 MET D N   
7606  C CA  . MET D 149 ? 0.9191 0.3615 0.4837 -0.0669 -0.0816 0.1667  149 MET D CA  
7607  C C   . MET D 149 ? 0.9257 0.3473 0.5095 -0.0243 -0.0948 0.1646  149 MET D C   
7608  O O   . MET D 149 ? 0.8427 0.3306 0.4967 -0.0096 -0.0955 0.1459  149 MET D O   
7609  C CB  . MET D 149 ? 0.9253 0.3445 0.4800 -0.1170 -0.0538 0.1606  149 MET D CB  
7610  C CG  . MET D 149 ? 0.9144 0.3707 0.4609 -0.1579 -0.0342 0.1586  149 MET D CG  
7611  S SD  . MET D 149 ? 0.7987 0.3678 0.4233 -0.1515 -0.0273 0.1345  149 MET D SD  
7612  C CE  . MET D 149 ? 0.8152 0.4070 0.4161 -0.1988 0.0041  0.1327  149 MET D CE  
7613  N N   . GLU D 150 ? 1.0376 0.3608 0.5519 -0.0034 -0.1035 0.1839  150 GLU D N   
7614  C CA  . GLU D 150 ? 1.0665 0.3562 0.5855 0.0433  -0.1133 0.1825  150 GLU D CA  
7615  C C   . GLU D 150 ? 1.0241 0.3964 0.5940 0.0983  -0.1366 0.1814  150 GLU D C   
7616  O O   . GLU D 150 ? 0.9885 0.3906 0.6042 0.1291  -0.1387 0.1686  150 GLU D O   
7617  C CB  . GLU D 150 ? 1.2159 0.3636 0.6309 0.0578  -0.1161 0.2053  150 GLU D CB  
7618  C CG  . GLU D 150 ? 1.2663 0.3574 0.6684 0.1113  -0.1224 0.2039  150 GLU D CG  
7619  C CD  . GLU D 150 ? 1.2059 0.3141 0.6577 0.0904  -0.1050 0.1768  150 GLU D CD  
7620  O OE1 . GLU D 150 ? 1.1837 0.2903 0.6392 0.0282  -0.0857 0.1663  150 GLU D OE1 
7621  O OE2 . GLU D 150 ? 1.1847 0.3150 0.6721 0.1366  -0.1105 0.1663  150 GLU D OE2 
7622  N N   . SER D 151 ? 1.0356 0.4503 0.5959 0.1069  -0.1536 0.1942  151 SER D N   
7623  C CA  . SER D 151 ? 0.9990 0.5090 0.6073 0.1501  -0.1774 0.1936  151 SER D CA  
7624  C C   . SER D 151 ? 0.8802 0.4992 0.5792 0.1298  -0.1697 0.1654  151 SER D C   
7625  O O   . SER D 151 ? 0.8386 0.5313 0.5899 0.1616  -0.1814 0.1575  151 SER D O   
7626  C CB  . SER D 151 ? 1.0421 0.5729 0.6110 0.1547  -0.1986 0.2137  151 SER D CB  
7627  O OG  . SER D 151 ? 0.9977 0.5608 0.5719 0.0997  -0.1864 0.2040  151 SER D OG  
7628  N N   . VAL D 152 ? 0.8374 0.4656 0.5507 0.0780  -0.1488 0.1512  152 VAL D N   
7629  C CA  . VAL D 152 ? 0.7415 0.4496 0.5260 0.0580  -0.1380 0.1258  152 VAL D CA  
7630  C C   . VAL D 152 ? 0.7168 0.4194 0.5404 0.0716  -0.1282 0.1125  152 VAL D C   
7631  O O   . VAL D 152 ? 0.6556 0.4257 0.5354 0.0832  -0.1307 0.0979  152 VAL D O   
7632  C CB  . VAL D 152 ? 0.7101 0.4197 0.4921 0.0087  -0.1157 0.1157  152 VAL D CB  
7633  C CG1 . VAL D 152 ? 0.6218 0.3986 0.4659 -0.0048 -0.1045 0.0915  152 VAL D CG1 
7634  C CG2 . VAL D 152 ? 0.7516 0.4602 0.4866 -0.0065 -0.1226 0.1272  152 VAL D CG2 
7635  N N   . ARG D 153 ? 0.7765 0.3964 0.5640 0.0652  -0.1165 0.1172  153 ARG D N   
7636  C CA  . ARG D 153 ? 0.7756 0.3751 0.5844 0.0774  -0.1082 0.1054  153 ARG D CA  
7637  C C   . ARG D 153 ? 0.8246 0.4234 0.6345 0.1355  -0.1245 0.1106  153 ARG D C   
7638  O O   . ARG D 153 ? 0.7813 0.4182 0.6370 0.1527  -0.1213 0.0955  153 ARG D O   
7639  C CB  . ARG D 153 ? 0.8339 0.3391 0.5904 0.0486  -0.0926 0.1091  153 ARG D CB  
7640  C CG  . ARG D 153 ? 0.7754 0.3109 0.5569 -0.0036 -0.0723 0.0967  153 ARG D CG  
7641  C CD  . ARG D 153 ? 0.8344 0.2947 0.5698 -0.0395 -0.0575 0.0985  153 ARG D CD  
7642  N NE  . ARG D 153 ? 0.8730 0.3131 0.5667 -0.0797 -0.0478 0.1101  153 ARG D NE  
7643  C CZ  . ARG D 153 ? 0.9776 0.3282 0.5900 -0.0881 -0.0501 0.1300  153 ARG D CZ  
7644  N NH1 . ARG D 153 ? 1.0642 0.3252 0.6213 -0.0539 -0.0623 0.1420  153 ARG D NH1 
7645  N NH2 . ARG D 153 ? 1.0049 0.3520 0.5855 -0.1297 -0.0382 0.1385  153 ARG D NH2 
7646  N N   . ASN D 154 ? 0.9316 0.4890 0.6885 0.1681  -0.1411 0.1329  154 ASN D N   
7647  C CA  . ASN D 154 ? 0.9914 0.5610 0.7473 0.2344  -0.1589 0.1419  154 ASN D CA  
7648  C C   . ASN D 154 ? 0.8921 0.5965 0.7295 0.2527  -0.1690 0.1289  154 ASN D C   
7649  O O   . ASN D 154 ? 0.8930 0.6270 0.7568 0.2976  -0.1719 0.1237  154 ASN D O   
7650  C CB  . ASN D 154 ? 1.1140 0.6460 0.8060 0.2643  -0.1796 0.1708  154 ASN D CB  
7651  C CG  . ASN D 154 ? 1.2931 0.6762 0.8898 0.2866  -0.1761 0.1892  154 ASN D CG  
7652  O OD1 . ASN D 154 ? 1.3286 0.6358 0.9055 0.2825  -0.1590 0.1788  154 ASN D OD1 
7653  N ND2 . ASN D 154 ? 1.4479 0.7819 0.9760 0.3087  -0.1927 0.2172  154 ASN D ND2 
7654  N N   . GLY D 155 ? 0.8124 0.5947 0.6830 0.2156  -0.1726 0.1231  155 GLY D N   
7655  C CA  . GLY D 155 ? 0.7447 0.6515 0.6725 0.2252  -0.1873 0.1164  155 GLY D CA  
7656  C C   . GLY D 155 ? 0.7892 0.7279 0.6884 0.2520  -0.2147 0.1386  155 GLY D C   
7657  O O   . GLY D 155 ? 0.7636 0.8126 0.7034 0.2660  -0.2322 0.1373  155 GLY D O   
7658  N N   . THR D 156 ? 0.8600 0.7057 0.6864 0.2548  -0.2186 0.1596  156 THR D N   
7659  C CA  . THR D 156 ? 0.9285 0.7805 0.7105 0.2907  -0.2460 0.1864  156 THR D CA  
7660  C C   . THR D 156 ? 0.9295 0.7819 0.6760 0.2440  -0.2517 0.1935  156 THR D C   
7661  O O   . THR D 156 ? 0.9997 0.8473 0.6982 0.2658  -0.2743 0.2173  156 THR D O   
7662  C CB  . THR D 156 ? 1.0454 0.7698 0.7514 0.3385  -0.2468 0.2091  156 THR D CB  
7663  O OG1 . THR D 156 ? 1.0499 0.7744 0.7825 0.3885  -0.2417 0.2014  156 THR D OG1 
7664  C CG2 . THR D 156 ? 1.1429 0.8573 0.7896 0.3821  -0.2757 0.2414  156 THR D CG2 
7665  N N   . TYR D 157 ? 0.8573 0.7155 0.6235 0.1835  -0.2312 0.1733  157 TYR D N   
7666  C CA  . TYR D 157 ? 0.8643 0.7140 0.5915 0.1388  -0.2305 0.1766  157 TYR D CA  
7667  C C   . TYR D 157 ? 0.8787 0.8147 0.6021 0.1470  -0.2610 0.1861  157 TYR D C   
7668  O O   . TYR D 157 ? 0.8203 0.8599 0.5986 0.1397  -0.2697 0.1708  157 TYR D O   
7669  C CB  . TYR D 157 ? 0.7850 0.6506 0.5449 0.0838  -0.2042 0.1498  157 TYR D CB  
7670  C CG  . TYR D 157 ? 0.8005 0.6577 0.5184 0.0412  -0.1995 0.1497  157 TYR D CG  
7671  C CD1 . TYR D 157 ? 0.8533 0.6267 0.5115 0.0224  -0.1851 0.1615  157 TYR D CD1 
7672  C CD2 . TYR D 157 ? 0.7718 0.7027 0.5030 0.0164  -0.2079 0.1369  157 TYR D CD2 
7673  C CE1 . TYR D 157 ? 0.8735 0.6416 0.4908 -0.0143 -0.1779 0.1603  157 TYR D CE1 
7674  C CE2 . TYR D 157 ? 0.7983 0.7136 0.4825 -0.0212 -0.2016 0.1347  157 TYR D CE2 
7675  C CZ  . TYR D 157 ? 0.8466 0.6828 0.4758 -0.0337 -0.1860 0.1464  157 TYR D CZ  
7676  O OH  . TYR D 157 ? 0.8767 0.7002 0.4574 -0.0693 -0.1770 0.1429  157 TYR D OH  
7677  N N   . ASP D 158 ? 0.9618 0.8556 0.6157 0.1579  -0.2774 0.2118  158 ASP D N   
7678  C CA  . ASP D 158 ? 0.9898 0.9667 0.6323 0.1693  -0.3108 0.2248  158 ASP D CA  
7679  C C   . ASP D 158 ? 0.9652 0.9747 0.5943 0.1058  -0.3063 0.2097  158 ASP D C   
7680  O O   . ASP D 158 ? 1.0218 0.9698 0.5832 0.0823  -0.3028 0.2208  158 ASP D O   
7681  C CB  . ASP D 158 ? 1.1045 1.0195 0.6703 0.2152  -0.3333 0.2619  158 ASP D CB  
7682  C CG  . ASP D 158 ? 1.1349 1.1587 0.7058 0.2516  -0.3743 0.2788  158 ASP D CG  
7683  O OD1 . ASP D 158 ? 1.0883 1.2187 0.7288 0.2826  -0.3870 0.2708  158 ASP D OD1 
7684  O OD2 . ASP D 158 ? 1.2084 1.2187 0.7138 0.2487  -0.3941 0.3005  158 ASP D OD2 
7685  N N   . TYR D 159 ? 0.8894 0.9893 0.5764 0.0771  -0.3044 0.1839  159 TYR D N   
7686  C CA  . TYR D 159 ? 0.8747 1.0014 0.5440 0.0173  -0.2991 0.1656  159 TYR D CA  
7687  C C   . TYR D 159 ? 0.9486 1.1016 0.5572 0.0111  -0.3286 0.1840  159 TYR D C   
7688  O O   . TYR D 159 ? 0.9844 1.0849 0.5341 -0.0269 -0.3172 0.1815  159 TYR D O   
7689  C CB  . TYR D 159 ? 0.8025 1.0194 0.5351 -0.0092 -0.2965 0.1377  159 TYR D CB  
7690  C CG  . TYR D 159 ? 0.8083 1.0503 0.5119 -0.0704 -0.2943 0.1180  159 TYR D CG  
7691  C CD1 . TYR D 159 ? 0.7894 0.9642 0.4751 -0.1114 -0.2597 0.0954  159 TYR D CD1 
7692  C CD2 . TYR D 159 ? 0.8409 1.1740 0.5304 -0.0863 -0.3268 0.1216  159 TYR D CD2 
7693  C CE1 . TYR D 159 ? 0.8123 0.9926 0.4587 -0.1645 -0.2547 0.0758  159 TYR D CE1 
7694  C CE2 . TYR D 159 ? 0.8612 1.2054 0.5119 -0.1480 -0.3239 0.1012  159 TYR D CE2 
7695  C CZ  . TYR D 159 ? 0.8515 1.1107 0.4769 -0.1860 -0.2864 0.0777  159 TYR D CZ  
7696  O OH  . TYR D 159 ? 0.8889 1.1432 0.4639 -0.2444 -0.2809 0.0560  159 TYR D OH  
7697  N N   . PRO D 160 ? 0.9763 1.2148 0.5972 0.0509  -0.3664 0.2030  160 PRO D N   
7698  C CA  . PRO D 160 ? 1.0512 1.3253 0.6135 0.0473  -0.3989 0.2227  160 PRO D CA  
7699  C C   . PRO D 160 ? 1.1396 1.2992 0.6117 0.0549  -0.3962 0.2485  160 PRO D C   
7700  O O   . PRO D 160 ? 1.1976 1.3646 0.6087 0.0286  -0.4117 0.2565  160 PRO D O   
7701  C CB  . PRO D 160 ? 1.0644 1.4480 0.6658 0.1079  -0.4374 0.2430  160 PRO D CB  
7702  C CG  . PRO D 160 ? 0.9772 1.4228 0.6679 0.1140  -0.4239 0.2203  160 PRO D CG  
7703  C CD  . PRO D 160 ? 0.9399 1.2628 0.6317 0.0997  -0.3811 0.2054  160 PRO D CD  
7704  N N   . GLN D 161 ? 1.1590 1.2131 0.6165 0.0859  -0.3767 0.2612  161 GLN D N   
7705  C CA  . GLN D 161 ? 1.2509 1.1877 0.6175 0.0860  -0.3700 0.2858  161 GLN D CA  
7706  C C   . GLN D 161 ? 1.2413 1.1245 0.5731 0.0190  -0.3367 0.2661  161 GLN D C   
7707  O O   . GLN D 161 ? 1.3143 1.1593 0.5688 -0.0027 -0.3402 0.2794  161 GLN D O   
7708  C CB  . GLN D 161 ? 1.2832 1.1166 0.6379 0.1289  -0.3559 0.3021  161 GLN D CB  
7709  C CG  . GLN D 161 ? 1.3871 1.0885 0.6414 0.1210  -0.3451 0.3274  161 GLN D CG  
7710  C CD  . GLN D 161 ? 1.4193 1.0073 0.6575 0.1440  -0.3239 0.3359  161 GLN D CD  
7711  O OE1 . GLN D 161 ? 1.3580 0.9634 0.6619 0.1652  -0.3149 0.3206  161 GLN D OE1 
7712  N NE2 . GLN D 161 ? 1.5240 0.9914 0.6675 0.1348  -0.3148 0.3598  161 GLN D NE2 
7713  N N   . TYR D 162 ? 1.1572 1.0392 0.5438 -0.0096 -0.3038 0.2351  162 TYR D N   
7714  C CA  . TYR D 162 ? 1.1467 0.9811 0.5079 -0.0627 -0.2676 0.2152  162 TYR D CA  
7715  C C   . TYR D 162 ? 1.1211 1.0179 0.4872 -0.1070 -0.2659 0.1875  162 TYR D C   
7716  O O   . TYR D 162 ? 1.1142 0.9759 0.4620 -0.1453 -0.2335 0.1670  162 TYR D O   
7717  C CB  . TYR D 162 ? 1.0827 0.8748 0.4920 -0.0658 -0.2317 0.1990  162 TYR D CB  
7718  C CG  . TYR D 162 ? 1.1197 0.8362 0.5140 -0.0331 -0.2289 0.2219  162 TYR D CG  
7719  C CD1 . TYR D 162 ? 1.1971 0.8235 0.5172 -0.0480 -0.2148 0.2405  162 TYR D CD1 
7720  C CD2 . TYR D 162 ? 1.0877 0.8169 0.5342 0.0090  -0.2383 0.2239  162 TYR D CD2 
7721  C CE1 . TYR D 162 ? 1.2485 0.7914 0.5415 -0.0257 -0.2110 0.2605  162 TYR D CE1 
7722  C CE2 . TYR D 162 ? 1.1379 0.7826 0.5579 0.0367  -0.2341 0.2426  162 TYR D CE2 
7723  C CZ  . TYR D 162 ? 1.2217 0.7690 0.5622 0.0172  -0.2209 0.2609  162 TYR D CZ  
7724  O OH  . TYR D 162 ? 1.2877 0.7377 0.5893 0.0376  -0.2156 0.2786  162 TYR D OH  
7725  N N   . SER D 163 ? 1.1174 1.1059 0.5037 -0.1023 -0.2995 0.1864  163 SER D N   
7726  C CA  . SER D 163 ? 1.1082 1.1505 0.4881 -0.1515 -0.3002 0.1594  163 SER D CA  
7727  C C   . SER D 163 ? 1.1952 1.2272 0.4863 -0.1789 -0.3145 0.1689  163 SER D C   
7728  O O   . SER D 163 ? 1.2131 1.2927 0.4812 -0.2197 -0.3246 0.1511  163 SER D O   
7729  C CB  . SER D 163 ? 1.0658 1.2226 0.5082 -0.1459 -0.3283 0.1511  163 SER D CB  
7730  O OG  . SER D 163 ? 1.1184 1.3485 0.5420 -0.1243 -0.3730 0.1759  163 SER D OG  
7731  N N   . ASP E 1   ? 0.2066 0.6597 0.3979 0.0194  -0.1018 -0.1149 1   ASP E N   
7732  C CA  . ASP E 1   ? 0.2128 0.6693 0.4007 -0.0028 -0.0999 -0.1186 1   ASP E CA  
7733  C C   . ASP E 1   ? 0.2130 0.6144 0.3943 -0.0020 -0.0960 -0.1177 1   ASP E C   
7734  O O   . ASP E 1   ? 0.2158 0.5745 0.3879 0.0030  -0.0960 -0.1167 1   ASP E O   
7735  C CB  . ASP E 1   ? 0.2337 0.6970 0.4049 -0.0355 -0.1034 -0.1252 1   ASP E CB  
7736  C CG  . ASP E 1   ? 0.2342 0.7586 0.4116 -0.0399 -0.1078 -0.1259 1   ASP E CG  
7737  O OD1 . ASP E 1   ? 0.2179 0.7784 0.4124 -0.0134 -0.1078 -0.1210 1   ASP E OD1 
7738  O OD2 . ASP E 1   ? 0.2558 0.7903 0.4169 -0.0701 -0.1113 -0.1311 1   ASP E OD2 
7739  N N   . GLN E 2   ? 0.2100 0.6176 0.3963 -0.0061 -0.0927 -0.1176 2   GLN E N   
7740  C CA  . GLN E 2   ? 0.2096 0.5713 0.3908 -0.0051 -0.0889 -0.1164 2   GLN E CA  
7741  C C   . GLN E 2   ? 0.2158 0.5818 0.3940 -0.0239 -0.0864 -0.1193 2   GLN E C   
7742  O O   . GLN E 2   ? 0.2145 0.6280 0.4008 -0.0316 -0.0866 -0.1204 2   GLN E O   
7743  C CB  . GLN E 2   ? 0.1962 0.5485 0.3873 0.0211  -0.0865 -0.1102 2   GLN E CB  
7744  C CG  . GLN E 2   ? 0.1906 0.5822 0.3929 0.0350  -0.0848 -0.1080 2   GLN E CG  
7745  C CD  . GLN E 2   ? 0.1888 0.5548 0.3896 0.0571  -0.0819 -0.1026 2   GLN E CD  
7746  O OE1 . GLN E 2   ? 0.1900 0.5655 0.3926 0.0649  -0.0788 -0.1014 2   GLN E OE1 
7747  N NE2 . GLN E 2   ? 0.1897 0.5224 0.3840 0.0660  -0.0830 -0.0989 2   GLN E NE2 
7748  N N   . ILE E 3   ? 0.2235 0.5430 0.3893 -0.0304 -0.0838 -0.1199 3   ILE E N   
7749  C CA  . ILE E 3   ? 0.2293 0.5442 0.3914 -0.0448 -0.0806 -0.1216 3   ILE E CA  
7750  C C   . ILE E 3   ? 0.2178 0.5040 0.3856 -0.0285 -0.0767 -0.1173 3   ILE E C   
7751  O O   . ILE E 3   ? 0.2165 0.4693 0.3790 -0.0175 -0.0765 -0.1145 3   ILE E O   
7752  C CB  . ILE E 3   ? 0.2595 0.5418 0.3928 -0.0723 -0.0809 -0.1268 3   ILE E CB  
7753  C CG1 . ILE E 3   ? 0.2678 0.5542 0.3969 -0.0908 -0.0780 -0.1284 3   ILE E CG1 
7754  C CG2 . ILE E 3   ? 0.2722 0.4956 0.3855 -0.0641 -0.0797 -0.1260 3   ILE E CG2 
7755  C CD1 . ILE E 3   ? 0.3055 0.5729 0.4020 -0.1246 -0.0793 -0.1339 3   ILE E CD1 
7756  N N   . CYS E 4   ? 0.2108 0.5142 0.3885 -0.0274 -0.0738 -0.1164 4   CYS E N   
7757  C CA  . CYS E 4   ? 0.2023 0.4817 0.3840 -0.0139 -0.0704 -0.1125 4   CYS E CA  
7758  C C   . CYS E 4   ? 0.2077 0.4718 0.3824 -0.0290 -0.0671 -0.1145 4   CYS E C   
7759  O O   . CYS E 4   ? 0.2167 0.5009 0.3877 -0.0479 -0.0670 -0.1181 4   CYS E O   
7760  C CB  . CYS E 4   ? 0.1936 0.4996 0.3884 0.0062  -0.0693 -0.1091 4   CYS E CB  
7761  S SG  . CYS E 4   ? 0.1932 0.5169 0.3918 0.0264  -0.0728 -0.1063 4   CYS E SG  
7762  N N   . ILE E 5   ? 0.2032 0.4336 0.3744 -0.0222 -0.0645 -0.1116 5   ILE E N   
7763  C CA  . ILE E 5   ? 0.2071 0.4234 0.3730 -0.0323 -0.0608 -0.1125 5   ILE E CA  
7764  C C   . ILE E 5   ? 0.1928 0.4197 0.3718 -0.0187 -0.0584 -0.1093 5   ILE E C   
7765  O O   . ILE E 5   ? 0.1857 0.4039 0.3679 -0.0024 -0.0590 -0.1053 5   ILE E O   
7766  C CB  . ILE E 5   ? 0.2181 0.3895 0.3667 -0.0337 -0.0593 -0.1113 5   ILE E CB  
7767  C CG1 . ILE E 5   ? 0.2387 0.3915 0.3668 -0.0419 -0.0614 -0.1142 5   ILE E CG1 
7768  C CG2 . ILE E 5   ? 0.2266 0.3824 0.3671 -0.0439 -0.0554 -0.1121 5   ILE E CG2 
7769  C CD1 . ILE E 5   ? 0.2633 0.4144 0.3735 -0.0666 -0.0615 -0.1198 5   ILE E CD1 
7770  N N   . GLY E 6   ? 0.1929 0.4367 0.3751 -0.0266 -0.0558 -0.1110 6   GLY E N   
7771  C CA  . GLY E 6   ? 0.1849 0.4383 0.3751 -0.0128 -0.0532 -0.1086 6   GLY E CA  
7772  C C   . GLY E 6   ? 0.1870 0.4462 0.3770 -0.0246 -0.0496 -0.1103 6   GLY E C   
7773  O O   . GLY E 6   ? 0.1966 0.4500 0.3785 -0.0452 -0.0492 -0.1131 6   GLY E O   
7774  N N   . TYR E 7   ? 0.1827 0.4496 0.3774 -0.0115 -0.0469 -0.1084 7   TYR E N   
7775  C CA  . TYR E 7   ? 0.1843 0.4533 0.3788 -0.0199 -0.0432 -0.1092 7   TYR E CA  
7776  C C   . TYR E 7   ? 0.1837 0.4931 0.3852 -0.0069 -0.0409 -0.1087 7   TYR E C   
7777  O O   . TYR E 7   ? 0.1844 0.5090 0.3868 0.0140  -0.0416 -0.1069 7   TYR E O   
7778  C CB  . TYR E 7   ? 0.1839 0.4092 0.3714 -0.0169 -0.0413 -0.1069 7   TYR E CB  
7779  C CG  . TYR E 7   ? 0.1831 0.3903 0.3672 0.0027  -0.0418 -0.1033 7   TYR E CG  
7780  C CD1 . TYR E 7   ? 0.1823 0.3707 0.3624 0.0077  -0.0449 -0.1009 7   TYR E CD1 
7781  C CD2 . TYR E 7   ? 0.1885 0.3946 0.3687 0.0149  -0.0391 -0.1021 7   TYR E CD2 
7782  C CE1 . TYR E 7   ? 0.1887 0.3571 0.3597 0.0209  -0.0457 -0.0972 7   TYR E CE1 
7783  C CE2 . TYR E 7   ? 0.1984 0.3786 0.3660 0.0297  -0.0397 -0.0990 7   TYR E CE2 
7784  C CZ  . TYR E 7   ? 0.1991 0.3602 0.3617 0.0309  -0.0431 -0.0964 7   TYR E CZ  
7785  O OH  . TYR E 7   ? 0.2152 0.3476 0.3598 0.0413  -0.0439 -0.0929 7   TYR E OH  
7786  N N   . HIS E 8   ? 0.1860 0.5117 0.3893 -0.0180 -0.0378 -0.1098 8   HIS E N   
7787  C CA  . HIS E 8   ? 0.1870 0.5598 0.3965 -0.0070 -0.0350 -0.1090 8   HIS E CA  
7788  C C   . HIS E 8   ? 0.1931 0.5475 0.3957 0.0220  -0.0324 -0.1064 8   HIS E C   
7789  O O   . HIS E 8   ? 0.1961 0.5024 0.3901 0.0234  -0.0316 -0.1056 8   HIS E O   
7790  C CB  . HIS E 8   ? 0.1889 0.5761 0.3995 -0.0292 -0.0322 -0.1104 8   HIS E CB  
7791  C CG  . HIS E 8   ? 0.1890 0.6348 0.4068 -0.0210 -0.0292 -0.1091 8   HIS E CG  
7792  N ND1 . HIS E 8   ? 0.1882 0.7001 0.4142 -0.0214 -0.0304 -0.1084 8   HIS E ND1 
7793  C CD2 . HIS E 8   ? 0.1908 0.6437 0.4081 -0.0118 -0.0248 -0.1080 8   HIS E CD2 
7794  C CE1 . HIS E 8   ? 0.1891 0.7499 0.4198 -0.0109 -0.0267 -0.1064 8   HIS E CE1 
7795  N NE2 . HIS E 8   ? 0.1913 0.7150 0.4162 -0.0046 -0.0231 -0.1063 8   HIS E NE2 
7796  N N   . ALA E 9   ? 0.2002 0.5925 0.4023 0.0456  -0.0311 -0.1047 9   ALA E N   
7797  C CA  . ALA E 9   ? 0.2165 0.5930 0.4038 0.0741  -0.0275 -0.1025 9   ALA E CA  
7798  C C   . ALA E 9   ? 0.2208 0.6607 0.4130 0.0863  -0.0238 -0.1016 9   ALA E C   
7799  O O   . ALA E 9   ? 0.2108 0.7096 0.4183 0.0726  -0.0249 -0.1019 9   ALA E O   
7800  C CB  . ALA E 9   ? 0.2320 0.5803 0.4023 0.0997  -0.0290 -0.1003 9   ALA E CB  
7801  N N   . ASN E 10  ? 0.2393 0.6686 0.4159 0.1107  -0.0194 -0.1000 10  ASN E N   
7802  C CA  . ASN E 10  ? 0.2467 0.7395 0.4251 0.1288  -0.0152 -0.0981 10  ASN E CA  
7803  C C   . ASN E 10  ? 0.2792 0.7431 0.4283 0.1671  -0.0105 -0.0961 10  ASN E C   
7804  O O   . ASN E 10  ? 0.2983 0.6916 0.4235 0.1773  -0.0112 -0.0962 10  ASN E O   
7805  C CB  . ASN E 10  ? 0.2300 0.7606 0.4270 0.0987  -0.0137 -0.0995 10  ASN E CB  
7806  C CG  . ASN E 10  ? 0.2319 0.7097 0.4216 0.0890  -0.0114 -0.1011 10  ASN E CG  
7807  O OD1 . ASN E 10  ? 0.2470 0.6657 0.4171 0.1057  -0.0105 -0.1009 10  ASN E OD1 
7808  N ND2 . ASN E 10  ? 0.2198 0.7183 0.4225 0.0601  -0.0105 -0.1023 10  ASN E ND2 
7809  N N   . ASN E 11  ? 0.2905 0.8087 0.4379 0.1875  -0.0057 -0.0940 11  ASN E N   
7810  C CA  . ASN E 11  ? 0.3295 0.8227 0.4425 0.2292  -0.0004 -0.0919 11  ASN E CA  
7811  C C   . ASN E 11  ? 0.3375 0.7890 0.4399 0.2226  0.0027  -0.0937 11  ASN E C   
7812  O O   . ASN E 11  ? 0.3702 0.8056 0.4427 0.2552  0.0076  -0.0923 11  ASN E O   
7813  C CB  . ASN E 11  ? 0.3417 0.9195 0.4534 0.2633  0.0036  -0.0877 11  ASN E CB  
7814  C CG  . ASN E 11  ? 0.3170 0.9788 0.4585 0.2429  0.0056  -0.0870 11  ASN E CG  
7815  O OD1 . ASN E 11  ? 0.2976 0.9447 0.4554 0.2064  0.0046  -0.0899 11  ASN E OD1 
7816  N ND2 . ASN E 11  ? 0.3205 1.0735 0.4671 0.2664  0.0084  -0.0824 11  ASN E ND2 
7817  N N   . SER E 12  ? 0.3118 0.7434 0.4349 0.1825  0.0001  -0.0966 12  SER E N   
7818  C CA  . SER E 12  ? 0.3156 0.7109 0.4321 0.1723  0.0026  -0.0982 12  SER E CA  
7819  C C   . SER E 12  ? 0.3500 0.6596 0.4287 0.1881  0.0029  -0.0987 12  SER E C   
7820  O O   . SER E 12  ? 0.3590 0.6229 0.4257 0.1862  -0.0008 -0.0986 12  SER E O   
7821  C CB  . SER E 12  ? 0.2837 0.6727 0.4266 0.1278  -0.0003 -0.1007 12  SER E CB  
7822  O OG  . SER E 12  ? 0.2863 0.6409 0.4229 0.1184  0.0020  -0.1018 12  SER E OG  
7823  N N   . THR E 13  ? 0.3732 0.6619 0.4306 0.2018  0.0074  -0.0989 13  THR E N   
7824  C CA  . THR E 13  ? 0.4110 0.6151 0.4273 0.2104  0.0076  -0.0996 13  THR E CA  
7825  C C   . THR E 13  ? 0.3994 0.5750 0.4226 0.1825  0.0076  -0.1016 13  THR E C   
7826  O O   . THR E 13  ? 0.4301 0.5413 0.4196 0.1850  0.0079  -0.1022 13  THR E O   
7827  C CB  . THR E 13  ? 0.4625 0.6507 0.4334 0.2557  0.0132  -0.0982 13  THR E CB  
7828  O OG1 . THR E 13  ? 0.4536 0.7041 0.4386 0.2670  0.0185  -0.0976 13  THR E OG1 
7829  C CG2 . THR E 13  ? 0.4867 0.6826 0.4380 0.2879  0.0132  -0.0956 13  THR E CG2 
7830  N N   . GLU E 14  ? 0.3601 0.5812 0.4226 0.1550  0.0072  -0.1024 14  GLU E N   
7831  C CA  . GLU E 14  ? 0.3486 0.5461 0.4186 0.1292  0.0073  -0.1038 14  GLU E CA  
7832  C C   . GLU E 14  ? 0.3481 0.4862 0.4102 0.1094  0.0025  -0.1040 14  GLU E C   
7833  O O   . GLU E 14  ? 0.3340 0.4720 0.4076 0.0991  -0.0016 -0.1034 14  GLU E O   
7834  C CB  . GLU E 14  ? 0.3129 0.5648 0.4206 0.1030  0.0076  -0.1043 14  GLU E CB  
7835  C CG  . GLU E 14  ? 0.3130 0.6305 0.4297 0.1155  0.0124  -0.1034 14  GLU E CG  
7836  C CD  . GLU E 14  ? 0.2991 0.6333 0.4308 0.0926  0.0149  -0.1040 14  GLU E CD  
7837  O OE1 . GLU E 14  ? 0.3095 0.5995 0.4272 0.0912  0.0163  -0.1049 14  GLU E OE1 
7838  O OE2 . GLU E 14  ? 0.2814 0.6720 0.4362 0.0742  0.0153  -0.1033 14  GLU E OE2 
7839  N N   . GLN E 15  ? 0.3642 0.4564 0.4060 0.1037  0.0031  -0.1043 15  GLN E N   
7840  C CA  . GLN E 15  ? 0.3677 0.4100 0.3988 0.0844  -0.0011 -0.1034 15  GLN E CA  
7841  C C   . GLN E 15  ? 0.3445 0.3876 0.3931 0.0590  -0.0011 -0.1034 15  GLN E C   
7842  O O   . GLN E 15  ? 0.3402 0.4011 0.3948 0.0596  0.0027  -0.1046 15  GLN E O   
7843  C CB  . GLN E 15  ? 0.4176 0.3983 0.3994 0.0979  -0.0012 -0.1031 15  GLN E CB  
7844  C CG  . GLN E 15  ? 0.4525 0.4226 0.4055 0.1293  0.0000  -0.1027 15  GLN E CG  
7845  C CD  . GLN E 15  ? 0.5134 0.4083 0.4067 0.1401  -0.0001 -0.1024 15  GLN E CD  
7846  O OE1 . GLN E 15  ? 0.5437 0.4053 0.4083 0.1502  -0.0022 -0.1010 15  GLN E OE1 
7847  N NE2 . GLN E 15  ? 0.5367 0.4004 0.4066 0.1367  0.0019  -0.1036 15  GLN E NE2 
7848  N N   . VAL E 16  ? 0.3312 0.3572 0.3863 0.0384  -0.0053 -0.1016 16  VAL E N   
7849  C CA  . VAL E 16  ? 0.3149 0.3380 0.3809 0.0174  -0.0054 -0.1006 16  VAL E CA  
7850  C C   . VAL E 16  ? 0.3300 0.3143 0.3757 0.0053  -0.0093 -0.0978 16  VAL E C   
7851  O O   . VAL E 16  ? 0.3444 0.3095 0.3754 0.0075  -0.0127 -0.0963 16  VAL E O   
7852  C CB  . VAL E 16  ? 0.2809 0.3362 0.3786 0.0030  -0.0059 -0.1002 16  VAL E CB  
7853  C CG1 . VAL E 16  ? 0.2700 0.3666 0.3848 0.0085  -0.0026 -0.1026 16  VAL E CG1 
7854  C CG2 . VAL E 16  ? 0.2726 0.3243 0.3754 -0.0018 -0.0104 -0.0983 16  VAL E CG2 
7855  N N   . ASP E 17  ? 0.3289 0.3047 0.3725 -0.0084 -0.0089 -0.0964 17  ASP E N   
7856  C CA  . ASP E 17  ? 0.3408 0.2917 0.3676 -0.0246 -0.0129 -0.0926 17  ASP E CA  
7857  C C   . ASP E 17  ? 0.3108 0.2866 0.3626 -0.0385 -0.0148 -0.0890 17  ASP E C   
7858  O O   . ASP E 17  ? 0.2869 0.2877 0.3621 -0.0384 -0.0122 -0.0898 17  ASP E O   
7859  C CB  . ASP E 17  ? 0.3630 0.2906 0.3671 -0.0311 -0.0117 -0.0928 17  ASP E CB  
7860  C CG  . ASP E 17  ? 0.4068 0.2961 0.3725 -0.0166 -0.0102 -0.0958 17  ASP E CG  
7861  O OD1 . ASP E 17  ? 0.4316 0.2986 0.3764 -0.0072 -0.0119 -0.0959 17  ASP E OD1 
7862  O OD2 . ASP E 17  ? 0.4217 0.3002 0.3743 -0.0131 -0.0070 -0.0978 17  ASP E OD2 
7863  N N   . THR E 18  ? 0.3175 0.2848 0.3596 -0.0500 -0.0193 -0.0846 18  THR E N   
7864  C CA  . THR E 18  ? 0.2968 0.2873 0.3550 -0.0608 -0.0211 -0.0796 18  THR E CA  
7865  C C   . THR E 18  ? 0.3157 0.2970 0.3531 -0.0781 -0.0245 -0.0744 18  THR E C   
7866  O O   . THR E 18  ? 0.3473 0.2979 0.3559 -0.0834 -0.0255 -0.0756 18  THR E O   
7867  C CB  . THR E 18  ? 0.2835 0.2864 0.3534 -0.0576 -0.0239 -0.0780 18  THR E CB  
7868  O OG1 . THR E 18  ? 0.3049 0.2875 0.3531 -0.0625 -0.0280 -0.0759 18  THR E OG1 
7869  C CG2 . THR E 18  ? 0.2715 0.2838 0.3576 -0.0440 -0.0214 -0.0830 18  THR E CG2 
7870  N N   . ILE E 19  ? 0.3028 0.3105 0.3505 -0.0867 -0.0261 -0.0685 19  ILE E N   
7871  C CA  . ILE E 19  ? 0.3189 0.3310 0.3489 -0.1059 -0.0297 -0.0622 19  ILE E CA  
7872  C C   . ILE E 19  ? 0.3486 0.3391 0.3525 -0.1185 -0.0348 -0.0601 19  ILE E C   
7873  O O   . ILE E 19  ? 0.3807 0.3466 0.3530 -0.1354 -0.0373 -0.0590 19  ILE E O   
7874  C CB  . ILE E 19  ? 0.2963 0.3515 0.3434 -0.1078 -0.0300 -0.0550 19  ILE E CB  
7875  C CG1 . ILE E 19  ? 0.2795 0.3476 0.3429 -0.0965 -0.0248 -0.0564 19  ILE E CG1 
7876  C CG2 . ILE E 19  ? 0.3102 0.3823 0.3400 -0.1297 -0.0343 -0.0472 19  ILE E CG2 
7877  C CD1 . ILE E 19  ? 0.2898 0.3536 0.3424 -0.1054 -0.0234 -0.0562 19  ILE E CD1 
7878  N N   . MET E 20  ? 0.3431 0.3394 0.3565 -0.1114 -0.0364 -0.0596 20  MET E N   
7879  C CA  . MET E 20  ? 0.3710 0.3495 0.3601 -0.1237 -0.0413 -0.0565 20  MET E CA  
7880  C C   . MET E 20  ? 0.4072 0.3363 0.3703 -0.1151 -0.0409 -0.0623 20  MET E C   
7881  O O   . MET E 20  ? 0.4408 0.3403 0.3711 -0.1272 -0.0447 -0.0601 20  MET E O   
7882  C CB  . MET E 20  ? 0.3466 0.3561 0.3568 -0.1190 -0.0431 -0.0526 20  MET E CB  
7883  C CG  . MET E 20  ? 0.3240 0.3824 0.3506 -0.1254 -0.0439 -0.0448 20  MET E CG  
7884  S SD  . MET E 20  ? 0.3075 0.3954 0.3477 -0.1206 -0.0467 -0.0396 20  MET E SD  
7885  C CE  . MET E 20  ? 0.2889 0.4363 0.3417 -0.1231 -0.0464 -0.0297 20  MET E CE  
7886  N N   . GLU E 21  ? 0.4052 0.3269 0.3801 -0.0936 -0.0363 -0.0691 21  GLU E N   
7887  C CA  . GLU E 21  ? 0.4399 0.3234 0.3917 -0.0783 -0.0352 -0.0740 21  GLU E CA  
7888  C C   . GLU E 21  ? 0.4476 0.3243 0.4016 -0.0609 -0.0298 -0.0800 21  GLU E C   
7889  O O   . GLU E 21  ? 0.4126 0.3230 0.4002 -0.0542 -0.0266 -0.0819 21  GLU E O   
7890  C CB  . GLU E 21  ? 0.4227 0.3208 0.3931 -0.0645 -0.0358 -0.0746 21  GLU E CB  
7891  C CG  . GLU E 21  ? 0.4617 0.3190 0.3988 -0.0524 -0.0364 -0.0766 21  GLU E CG  
7892  C CD  . GLU E 21  ? 0.4436 0.3197 0.4005 -0.0393 -0.0373 -0.0769 21  GLU E CD  
7893  O OE1 . GLU E 21  ? 0.4062 0.3214 0.3972 -0.0443 -0.0385 -0.0748 21  GLU E OE1 
7894  O OE2 . GLU E 21  ? 0.4698 0.3203 0.4049 -0.0224 -0.0367 -0.0790 21  GLU E OE2 
7895  N N   . LYS E 22  ? 0.5016 0.3322 0.4150 -0.0532 -0.0288 -0.0828 22  LYS E N   
7896  C CA  . LYS E 22  ? 0.5179 0.3416 0.4273 -0.0336 -0.0235 -0.0880 22  LYS E CA  
7897  C C   . LYS E 22  ? 0.5388 0.3551 0.4406 -0.0054 -0.0211 -0.0912 22  LYS E C   
7898  O O   . LYS E 22  ? 0.5603 0.3545 0.4421 -0.0023 -0.0237 -0.0897 22  LYS E O   
7899  C CB  . LYS E 22  ? 0.5671 0.3432 0.4301 -0.0421 -0.0233 -0.0886 22  LYS E CB  
7900  C CG  . LYS E 22  ? 0.5485 0.3450 0.4272 -0.0586 -0.0226 -0.0877 22  LYS E CG  
7901  C CD  . LYS E 22  ? 0.5776 0.3520 0.4262 -0.0898 -0.0277 -0.0830 22  LYS E CD  
7902  C CE  . LYS E 22  ? 0.6466 0.3539 0.4323 -0.0922 -0.0277 -0.0854 22  LYS E CE  
7903  N NZ  . LYS E 22  ? 0.6508 0.3551 0.4329 -0.0892 -0.0239 -0.0886 22  LYS E NZ  
7904  N N   . ASN E 23  ? 0.5383 0.3773 0.4558 0.0148  -0.0160 -0.0950 23  ASN E N   
7905  C CA  . ASN E 23  ? 0.5606 0.4036 0.4712 0.0449  -0.0129 -0.0974 23  ASN E CA  
7906  C C   . ASN E 23  ? 0.5193 0.3917 0.4557 0.0485  -0.0153 -0.0962 23  ASN E C   
7907  O O   . ASN E 23  ? 0.5439 0.3977 0.4573 0.0660  -0.0157 -0.0960 23  ASN E O   
7908  C CB  . ASN E 23  ? 0.6519 0.4305 0.4994 0.0611  -0.0119 -0.0981 23  ASN E CB  
7909  C CG  . ASN E 23  ? 0.7146 0.4653 0.5340 0.0637  -0.0086 -0.1003 23  ASN E CG  
7910  O OD1 . ASN E 23  ? 0.6829 0.4718 0.5341 0.0620  -0.0056 -0.1018 23  ASN E OD1 
7911  N ND2 . ASN E 23  ? 0.8295 0.5089 0.5840 0.0673  -0.0089 -0.1005 23  ASN E ND2 
7912  N N   . VAL E 24  ? 0.4574 0.3724 0.4376 0.0329  -0.0167 -0.0954 24  VAL E N   
7913  C CA  . VAL E 24  ? 0.4204 0.3664 0.4275 0.0345  -0.0188 -0.0948 24  VAL E CA  
7914  C C   . VAL E 24  ? 0.3963 0.3852 0.4247 0.0530  -0.0151 -0.0978 24  VAL E C   
7915  O O   . VAL E 24  ? 0.3728 0.3923 0.4237 0.0484  -0.0123 -0.0994 24  VAL E O   
7916  C CB  . VAL E 24  ? 0.3823 0.3522 0.4207 0.0120  -0.0214 -0.0927 24  VAL E CB  
7917  C CG1 . VAL E 24  ? 0.3576 0.3572 0.4207 0.0144  -0.0231 -0.0928 24  VAL E CG1 
7918  C CG2 . VAL E 24  ? 0.3956 0.3372 0.4155 -0.0067 -0.0252 -0.0884 24  VAL E CG2 
7919  N N   . THR E 25  ? 0.4008 0.3941 0.4204 0.0729  -0.0152 -0.0979 25  THR E N   
7920  C CA  . THR E 25  ? 0.3819 0.4250 0.4203 0.0904  -0.0121 -0.0998 25  THR E CA  
7921  C C   . THR E 25  ? 0.3350 0.4239 0.4141 0.0730  -0.0140 -0.1003 25  THR E C   
7922  O O   . THR E 25  ? 0.3236 0.4070 0.4098 0.0633  -0.0180 -0.0991 25  THR E O   
7923  C CB  . THR E 25  ? 0.4097 0.4483 0.4250 0.1192  -0.0117 -0.0990 25  THR E CB  
7924  O OG1 . THR E 25  ? 0.4608 0.4377 0.4262 0.1330  -0.0108 -0.0981 25  THR E OG1 
7925  C CG2 . THR E 25  ? 0.4032 0.4986 0.4318 0.1409  -0.0075 -0.1000 25  THR E CG2 
7926  N N   . VAL E 26  ? 0.3102 0.4417 0.4115 0.0683  -0.0110 -0.1020 26  VAL E N   
7927  C CA  . VAL E 26  ? 0.2765 0.4435 0.4075 0.0486  -0.0125 -0.1029 26  VAL E CA  
7928  C C   . VAL E 26  ? 0.2674 0.4923 0.4126 0.0558  -0.0105 -0.1039 26  VAL E C   
7929  O O   . VAL E 26  ? 0.2805 0.5259 0.4177 0.0752  -0.0068 -0.1037 26  VAL E O   
7930  C CB  . VAL E 26  ? 0.2618 0.4223 0.4029 0.0261  -0.0113 -0.1033 26  VAL E CB  
7931  C CG1 . VAL E 26  ? 0.2639 0.3804 0.3950 0.0166  -0.0140 -0.1012 26  VAL E CG1 
7932  C CG2 . VAL E 26  ? 0.2683 0.4394 0.4058 0.0308  -0.0066 -0.1041 26  VAL E CG2 
7933  N N   . THR E 27  ? 0.2472 0.5001 0.4111 0.0397  -0.0129 -0.1046 27  THR E N   
7934  C CA  . THR E 27  ? 0.2395 0.5540 0.4169 0.0405  -0.0121 -0.1050 27  THR E CA  
7935  C C   . THR E 27  ? 0.2339 0.5816 0.4197 0.0273  -0.0084 -0.1056 27  THR E C   
7936  O O   . THR E 27  ? 0.2368 0.6393 0.4277 0.0366  -0.0060 -0.1047 27  THR E O   
7937  C CB  . THR E 27  ? 0.2266 0.5566 0.4164 0.0222  -0.0163 -0.1060 27  THR E CB  
7938  O OG1 . THR E 27  ? 0.2194 0.5272 0.4124 -0.0057 -0.0171 -0.1073 27  THR E OG1 
7939  C CG2 . THR E 27  ? 0.2301 0.5315 0.4126 0.0349  -0.0200 -0.1050 27  THR E CG2 
7940  N N   . HIS E 28  ? 0.2277 0.5455 0.4139 0.0062  -0.0079 -0.1065 28  HIS E N   
7941  C CA  . HIS E 28  ? 0.2251 0.5656 0.4159 -0.0086 -0.0044 -0.1068 28  HIS E CA  
7942  C C   . HIS E 28  ? 0.2277 0.5209 0.4097 -0.0119 -0.0025 -0.1068 28  HIS E C   
7943  O O   . HIS E 28  ? 0.2275 0.4750 0.4035 -0.0151 -0.0048 -0.1065 28  HIS E O   
7944  C CB  . HIS E 28  ? 0.2203 0.5808 0.4182 -0.0402 -0.0059 -0.1079 28  HIS E CB  
7945  C CG  . HIS E 28  ? 0.2179 0.6260 0.4236 -0.0424 -0.0086 -0.1079 28  HIS E CG  
7946  N ND1 . HIS E 28  ? 0.2152 0.6074 0.4206 -0.0383 -0.0128 -0.1085 28  HIS E ND1 
7947  C CD2 . HIS E 28  ? 0.2178 0.6940 0.4317 -0.0486 -0.0077 -0.1070 28  HIS E CD2 
7948  C CE1 . HIS E 28  ? 0.2138 0.6595 0.4269 -0.0416 -0.0145 -0.1082 28  HIS E CE1 
7949  N NE2 . HIS E 28  ? 0.2153 0.7151 0.4337 -0.0485 -0.0116 -0.1071 28  HIS E NE2 
7950  N N   . ALA E 29  ? 0.2308 0.5402 0.4123 -0.0111 0.0016  -0.1065 29  ALA E N   
7951  C CA  . ALA E 29  ? 0.2341 0.5048 0.4073 -0.0142 0.0037  -0.1064 29  ALA E CA  
7952  C C   . ALA E 29  ? 0.2338 0.5334 0.4117 -0.0275 0.0078  -0.1063 29  ALA E C   
7953  O O   . ALA E 29  ? 0.2326 0.5851 0.4190 -0.0329 0.0090  -0.1060 29  ALA E O   
7954  C CB  . ALA E 29  ? 0.2476 0.4917 0.4053 0.0117  0.0047  -0.1060 29  ALA E CB  
7955  N N   . GLN E 30  ? 0.2361 0.5044 0.4078 -0.0343 0.0098  -0.1061 30  GLN E N   
7956  C CA  . GLN E 30  ? 0.2382 0.5288 0.4118 -0.0467 0.0140  -0.1057 30  GLN E CA  
7957  C C   . GLN E 30  ? 0.2434 0.5064 0.4079 -0.0359 0.0169  -0.1054 30  GLN E C   
7958  O O   . GLN E 30  ? 0.2434 0.4629 0.4011 -0.0418 0.0159  -0.1051 30  GLN E O   
7959  C CB  . GLN E 30  ? 0.2404 0.5202 0.4124 -0.0774 0.0135  -0.1056 30  GLN E CB  
7960  C CG  . GLN E 30  ? 0.2472 0.5520 0.4183 -0.0945 0.0177  -0.1048 30  GLN E CG  
7961  C CD  . GLN E 30  ? 0.2602 0.5540 0.4211 -0.1270 0.0172  -0.1047 30  GLN E CD  
7962  O OE1 . GLN E 30  ? 0.2656 0.5504 0.4223 -0.1374 0.0138  -0.1056 30  GLN E OE1 
7963  N NE2 . GLN E 30  ? 0.2710 0.5617 0.4233 -0.1435 0.0208  -0.1036 30  GLN E NE2 
7964  N N   . ASP E 31  ? 0.2495 0.5410 0.4122 -0.0189 0.0205  -0.1053 31  ASP E N   
7965  C CA  . ASP E 31  ? 0.2581 0.5275 0.4099 -0.0101 0.0237  -0.1053 31  ASP E CA  
7966  C C   . ASP E 31  ? 0.2526 0.5260 0.4093 -0.0344 0.0262  -0.1045 31  ASP E C   
7967  O O   . ASP E 31  ? 0.2492 0.5637 0.4148 -0.0504 0.0278  -0.1037 31  ASP E O   
7968  C CB  . ASP E 31  ? 0.2719 0.5721 0.4163 0.0172  0.0275  -0.1052 31  ASP E CB  
7969  C CG  . ASP E 31  ? 0.2898 0.5522 0.4141 0.0318  0.0300  -0.1060 31  ASP E CG  
7970  O OD1 . ASP E 31  ? 0.2871 0.5136 0.4090 0.0162  0.0294  -0.1061 31  ASP E OD1 
7971  O OD2 . ASP E 31  ? 0.3115 0.5796 0.4192 0.0603  0.0327  -0.1062 31  ASP E OD2 
7972  N N   . ILE E 32  ? 0.2542 0.4849 0.4024 -0.0385 0.0265  -0.1044 32  ILE E N   
7973  C CA  . ILE E 32  ? 0.2535 0.4790 0.4015 -0.0585 0.0292  -0.1032 32  ILE E CA  
7974  C C   . ILE E 32  ? 0.2596 0.4778 0.4001 -0.0496 0.0330  -0.1031 32  ILE E C   
7975  O O   . ILE E 32  ? 0.2610 0.4711 0.3993 -0.0636 0.0354  -0.1020 32  ILE E O   
7976  C CB  . ILE E 32  ? 0.2520 0.4358 0.3949 -0.0727 0.0265  -0.1022 32  ILE E CB  
7977  C CG1 . ILE E 32  ? 0.2515 0.3989 0.3874 -0.0595 0.0235  -0.1019 32  ILE E CG1 
7978  C CG2 . ILE E 32  ? 0.2506 0.4415 0.3970 -0.0855 0.0238  -0.1024 32  ILE E CG2 
7979  C CD1 . ILE E 32  ? 0.2516 0.3663 0.3811 -0.0693 0.0222  -0.0995 32  ILE E CD1 
7980  N N   . LEU E 33  ? 0.2678 0.4852 0.4001 -0.0256 0.0336  -0.1043 33  LEU E N   
7981  C CA  . LEU E 33  ? 0.2792 0.4849 0.3992 -0.0148 0.0370  -0.1048 33  LEU E CA  
7982  C C   . LEU E 33  ? 0.2868 0.5393 0.4071 0.0013  0.0417  -0.1048 33  LEU E C   
7983  O O   . LEU E 33  ? 0.2956 0.5651 0.4108 0.0234  0.0417  -0.1054 33  LEU E O   
7984  C CB  . LEU E 33  ? 0.2945 0.4532 0.3937 0.0003  0.0343  -0.1061 33  LEU E CB  
7985  C CG  . LEU E 33  ? 0.3128 0.4469 0.3919 0.0092  0.0369  -0.1070 33  LEU E CG  
7986  C CD1 . LEU E 33  ? 0.3027 0.4243 0.3873 -0.0112 0.0374  -0.1054 33  LEU E CD1 
7987  C CD2 . LEU E 33  ? 0.3380 0.4245 0.3886 0.0222  0.0338  -0.1084 33  LEU E CD2 
7988  N N   . GLU E 34  ? 0.2856 0.5608 0.4103 -0.0078 0.0459  -0.1037 34  GLU E N   
7989  C CA  . GLU E 34  ? 0.2940 0.6173 0.4176 0.0093  0.0509  -0.1029 34  GLU E CA  
7990  C C   . GLU E 34  ? 0.3174 0.6084 0.4160 0.0375  0.0530  -0.1048 34  GLU E C   
7991  O O   . GLU E 34  ? 0.3228 0.5764 0.4114 0.0315  0.0535  -0.1056 34  GLU E O   
7992  C CB  . GLU E 34  ? 0.2867 0.6459 0.4215 -0.0127 0.0547  -0.1006 34  GLU E CB  
7993  C CG  . GLU E 34  ? 0.2938 0.7140 0.4294 0.0038  0.0602  -0.0988 34  GLU E CG  
7994  C CD  . GLU E 34  ? 0.2958 0.7659 0.4354 0.0245  0.0600  -0.0978 34  GLU E CD  
7995  O OE1 . GLU E 34  ? 0.2837 0.7891 0.4388 0.0052  0.0576  -0.0963 34  GLU E OE1 
7996  O OE2 . GLU E 34  ? 0.3138 0.7841 0.4370 0.0609  0.0623  -0.0985 34  GLU E OE2 
7997  N N   . LYS E 35  ? 0.3360 0.6401 0.4204 0.0688  0.0544  -0.1053 35  LYS E N   
7998  C CA  . LYS E 35  ? 0.3705 0.6311 0.4197 0.0980  0.0562  -0.1074 35  LYS E CA  
7999  C C   . LYS E 35  ? 0.3887 0.6868 0.4265 0.1235  0.0630  -0.1065 35  LYS E C   
8000  O O   . LYS E 35  ? 0.4220 0.6784 0.4259 0.1453  0.0652  -0.1085 35  LYS E O   
8001  C CB  . LYS E 35  ? 0.3921 0.6220 0.4195 0.1203  0.0533  -0.1087 35  LYS E CB  
8002  C CG  . LYS E 35  ? 0.3936 0.5580 0.4118 0.1033  0.0471  -0.1103 35  LYS E CG  
8003  C CD  . LYS E 35  ? 0.4132 0.5535 0.4124 0.1212  0.0441  -0.1109 35  LYS E CD  
8004  C CE  . LYS E 35  ? 0.3813 0.5447 0.4111 0.1026  0.0396  -0.1096 35  LYS E CE  
8005  N NZ  . LYS E 35  ? 0.3511 0.5884 0.4160 0.0933  0.0416  -0.1076 35  LYS E NZ  
8006  N N   . THR E 36  ? 0.3707 0.7466 0.4334 0.1194  0.0663  -0.1032 36  THR E N   
8007  C CA  . THR E 36  ? 0.3872 0.8143 0.4409 0.1471  0.0730  -0.1011 36  THR E CA  
8008  C C   . THR E 36  ? 0.3716 0.8387 0.4436 0.1252  0.0767  -0.0989 36  THR E C   
8009  O O   . THR E 36  ? 0.3461 0.8180 0.4416 0.0866  0.0743  -0.0980 36  THR E O   
8010  C CB  . THR E 36  ? 0.3859 0.8889 0.4488 0.1679  0.0749  -0.0975 36  THR E CB  
8011  O OG1 . THR E 36  ? 0.3511 0.9118 0.4510 0.1316  0.0726  -0.0947 36  THR E OG1 
8012  C CG2 . THR E 36  ? 0.4069 0.8712 0.4477 0.1943  0.0720  -0.0993 36  THR E CG2 
8013  N N   . HIS E 37  ? 0.3927 0.8850 0.4487 0.1524  0.0829  -0.0977 37  HIS E N   
8014  C CA  . HIS E 37  ? 0.3821 0.9250 0.4526 0.1381  0.0875  -0.0947 37  HIS E CA  
8015  C C   . HIS E 37  ? 0.4020 1.0144 0.4618 0.1777  0.0942  -0.0912 37  HIS E C   
8016  O O   . HIS E 37  ? 0.4309 1.0307 0.4638 0.2192  0.0956  -0.0920 37  HIS E O   
8017  C CB  . HIS E 37  ? 0.3904 0.8696 0.4465 0.1290  0.0880  -0.0977 37  HIS E CB  
8018  C CG  . HIS E 37  ? 0.4305 0.8503 0.4446 0.1661  0.0897  -0.1014 37  HIS E CG  
8019  N ND1 . HIS E 37  ? 0.4562 0.8897 0.4485 0.1938  0.0960  -0.1010 37  HIS E ND1 
8020  C CD2 . HIS E 37  ? 0.4553 0.7988 0.4397 0.1788  0.0859  -0.1055 37  HIS E CD2 
8021  C CE1 . HIS E 37  ? 0.4984 0.8608 0.4462 0.2222  0.0961  -0.1051 37  HIS E CE1 
8022  N NE2 . HIS E 37  ? 0.4994 0.8062 0.4411 0.2119  0.0898  -0.1078 37  HIS E NE2 
8023  N N   . ASN E 38  ? 0.3907 1.0764 0.4680 0.1663  0.0987  -0.0866 38  ASN E N   
8024  C CA  . ASN E 38  ? 0.4078 1.1745 0.4771 0.2045  0.1056  -0.0819 38  ASN E CA  
8025  C C   . ASN E 38  ? 0.4459 1.1752 0.4772 0.2459  0.1113  -0.0840 38  ASN E C   
8026  O O   . ASN E 38  ? 0.4725 1.2475 0.4839 0.2916  0.1171  -0.0810 38  ASN E O   
8027  C CB  . ASN E 38  ? 0.3827 1.2551 0.4843 0.1750  0.1082  -0.0750 38  ASN E CB  
8028  C CG  . ASN E 38  ? 0.3725 1.2301 0.4819 0.1412  0.1096  -0.0750 38  ASN E CG  
8029  O OD1 . ASN E 38  ? 0.3848 1.1643 0.4756 0.1467  0.1097  -0.0796 38  ASN E OD1 
8030  N ND2 . ASN E 38  ? 0.3534 1.2864 0.4876 0.1043  0.1105  -0.0694 38  ASN E ND2 
8031  N N   . GLY E 39  ? 0.4517 1.1000 0.4705 0.2307  0.1097  -0.0888 39  GLY E N   
8032  C CA  . GLY E 39  ? 0.4926 1.0883 0.4695 0.2650  0.1140  -0.0920 39  GLY E CA  
8033  C C   . GLY E 39  ? 0.4898 1.1325 0.4733 0.2622  0.1199  -0.0890 39  GLY E C   
8034  O O   . GLY E 39  ? 0.5260 1.1434 0.4741 0.2961  0.1249  -0.0906 39  GLY E O   
8035  N N   . LYS E 40  ? 0.4512 1.1568 0.4756 0.2205  0.1195  -0.0846 40  LYS E N   
8036  C CA  . LYS E 40  ? 0.4460 1.2146 0.4807 0.2143  0.1253  -0.0801 40  LYS E CA  
8037  C C   . LYS E 40  ? 0.4202 1.1658 0.4765 0.1621  0.1228  -0.0804 40  LYS E C   
8038  O O   . LYS E 40  ? 0.3992 1.1130 0.4726 0.1255  0.1168  -0.0817 40  LYS E O   
8039  C CB  . LYS E 40  ? 0.4326 1.3245 0.4907 0.2169  0.1288  -0.0721 40  LYS E CB  
8040  C CG  . LYS E 40  ? 0.4641 1.4004 0.4970 0.2781  0.1342  -0.0697 40  LYS E CG  
8041  C CD  . LYS E 40  ? 0.4474 1.4854 0.5046 0.2775  0.1338  -0.0631 40  LYS E CD  
8042  C CE  . LYS E 40  ? 0.4810 1.5764 0.5121 0.3429  0.1404  -0.0591 40  LYS E CE  
8043  N NZ  . LYS E 40  ? 0.4661 1.6579 0.5191 0.3452  0.1394  -0.0528 40  LYS E NZ  
8044  N N   . LEU E 41  ? 0.4259 1.1873 0.4782 0.1616  0.1277  -0.0787 41  LEU E N   
8045  C CA  . LEU E 41  ? 0.4055 1.1597 0.4761 0.1150  0.1269  -0.0773 41  LEU E CA  
8046  C C   . LEU E 41  ? 0.3867 1.2436 0.4847 0.0868  0.1292  -0.0694 41  LEU E C   
8047  O O   . LEU E 41  ? 0.3944 1.3348 0.4928 0.1088  0.1350  -0.0643 41  LEU E O   
8048  C CB  . LEU E 41  ? 0.4231 1.1435 0.4737 0.1279  0.1311  -0.0792 41  LEU E CB  
8049  C CG  . LEU E 41  ? 0.4428 1.0551 0.4648 0.1404  0.1279  -0.0868 41  LEU E CG  
8050  C CD1 . LEU E 41  ? 0.4293 0.9964 0.4587 0.1033  0.1259  -0.0877 41  LEU E CD1 
8051  C CD2 . LEU E 41  ? 0.4470 1.0024 0.4600 0.1471  0.1216  -0.0913 41  LEU E CD2 
8052  N N   . CYS E 42  ? 0.3668 1.2172 0.4836 0.0380  0.1247  -0.0680 42  CYS E N   
8053  C CA  . CYS E 42  ? 0.3548 1.2938 0.4923 0.0044  0.1251  -0.0610 42  CYS E CA  
8054  C C   . CYS E 42  ? 0.3502 1.2829 0.4928 -0.0473 0.1252  -0.0578 42  CYS E C   
8055  O O   . CYS E 42  ? 0.3518 1.2037 0.4854 -0.0597 0.1237  -0.0615 42  CYS E O   
8056  C CB  . CYS E 42  ? 0.3446 1.2843 0.4926 -0.0089 0.1191  -0.0618 42  CYS E CB  
8057  S SG  . CYS E 42  ? 0.3513 1.3159 0.4943 0.0452  0.1187  -0.0635 42  CYS E SG  
8058  N N   . ASP E 43  ? 0.3480 1.3678 0.5020 -0.0781 0.1269  -0.0505 43  ASP E N   
8059  C CA  . ASP E 43  ? 0.3520 1.3640 0.5046 -0.1344 0.1263  -0.0469 43  ASP E CA  
8060  C C   . ASP E 43  ? 0.3512 1.2873 0.4996 -0.1645 0.1196  -0.0507 43  ASP E C   
8061  O O   . ASP E 43  ? 0.3444 1.2895 0.4998 -0.1597 0.1155  -0.0522 43  ASP E O   
8062  C CB  . ASP E 43  ? 0.3550 1.4812 0.5168 -0.1650 0.1286  -0.0378 43  ASP E CB  
8063  C CG  . ASP E 43  ? 0.3576 1.5673 0.5227 -0.1396 0.1359  -0.0325 43  ASP E CG  
8064  O OD1 . ASP E 43  ? 0.3598 1.5313 0.5170 -0.0997 0.1394  -0.0364 43  ASP E OD1 
8065  O OD2 . ASP E 43  ? 0.3594 1.6759 0.5331 -0.1602 0.1383  -0.0242 43  ASP E OD2 
8066  N N   . LEU E 44  ? 0.3608 1.2225 0.4955 -0.1926 0.1187  -0.0519 44  LEU E N   
8067  C CA  . LEU E 44  ? 0.3666 1.1538 0.4916 -0.2203 0.1132  -0.0546 44  LEU E CA  
8068  C C   . LEU E 44  ? 0.3875 1.1954 0.5003 -0.2768 0.1128  -0.0490 44  LEU E C   
8069  O O   . LEU E 44  ? 0.4045 1.2108 0.5038 -0.3020 0.1163  -0.0451 44  LEU E O   
8070  C CB  . LEU E 44  ? 0.3699 1.0577 0.4815 -0.2124 0.1126  -0.0590 44  LEU E CB  
8071  C CG  . LEU E 44  ? 0.3745 0.9823 0.4755 -0.2268 0.1071  -0.0623 44  LEU E CG  
8072  C CD1 . LEU E 44  ? 0.3568 0.9487 0.4696 -0.1933 0.1028  -0.0677 44  LEU E CD1 
8073  C CD2 . LEU E 44  ? 0.3855 0.9123 0.4684 -0.2315 0.1077  -0.0633 44  LEU E CD2 
8074  N N   . ASP E 45  ? 0.3908 1.2150 0.5044 -0.2981 0.1084  -0.0486 45  ASP E N   
8075  C CA  . ASP E 45  ? 0.4184 1.2582 0.5134 -0.3558 0.1072  -0.0436 45  ASP E CA  
8076  C C   . ASP E 45  ? 0.4254 1.3644 0.5237 -0.3775 0.1118  -0.0357 45  ASP E C   
8077  O O   . ASP E 45  ? 0.4558 1.3911 0.5302 -0.4265 0.1128  -0.0309 45  ASP E O   
8078  C CB  . ASP E 45  ? 0.4482 1.1820 0.5101 -0.3836 0.1065  -0.0448 45  ASP E CB  
8079  C CG  . ASP E 45  ? 0.4849 1.1971 0.5173 -0.4374 0.1032  -0.0425 45  ASP E CG  
8080  O OD1 . ASP E 45  ? 0.4827 1.1731 0.5159 -0.4365 0.0982  -0.0460 45  ASP E OD1 
8081  O OD2 . ASP E 45  ? 0.5203 1.2332 0.5251 -0.4813 0.1054  -0.0372 45  ASP E OD2 
8082  N N   . GLY E 46  ? 0.4013 1.4277 0.5254 -0.3399 0.1148  -0.0341 46  GLY E N   
8083  C CA  . GLY E 46  ? 0.4041 1.5366 0.5348 -0.3509 0.1198  -0.0260 46  GLY E CA  
8084  C C   . GLY E 46  ? 0.4058 1.5217 0.5318 -0.3364 0.1257  -0.0251 46  GLY E C   
8085  O O   . GLY E 46  ? 0.4017 1.6074 0.5379 -0.3263 0.1307  -0.0194 46  GLY E O   
8086  N N   . VAL E 47  ? 0.4119 1.4172 0.5222 -0.3336 0.1251  -0.0303 47  VAL E N   
8087  C CA  . VAL E 47  ? 0.4168 1.3949 0.5189 -0.3256 0.1301  -0.0296 47  VAL E CA  
8088  C C   . VAL E 47  ? 0.3940 1.3661 0.5111 -0.2632 0.1325  -0.0347 47  VAL E C   
8089  O O   . VAL E 47  ? 0.3842 1.2863 0.5021 -0.2352 0.1292  -0.0417 47  VAL E O   
8090  C CB  . VAL E 47  ? 0.4382 1.3019 0.5128 -0.3510 0.1286  -0.0320 47  VAL E CB  
8091  C CG1 . VAL E 47  ? 0.4440 1.2842 0.5103 -0.3428 0.1338  -0.0308 47  VAL E CG1 
8092  C CG2 . VAL E 47  ? 0.4724 1.3253 0.5206 -0.4124 0.1263  -0.0275 47  VAL E CG2 
8093  N N   . LYS E 48  ? 0.3906 1.4334 0.5151 -0.2432 0.1383  -0.0308 48  LYS E N   
8094  C CA  . LYS E 48  ? 0.3782 1.4240 0.5097 -0.1828 0.1413  -0.0350 48  LYS E CA  
8095  C C   . LYS E 48  ? 0.3797 1.3211 0.4984 -0.1657 0.1411  -0.0415 48  LYS E C   
8096  O O   . LYS E 48  ? 0.3902 1.2928 0.4973 -0.1940 0.1424  -0.0398 48  LYS E O   
8097  C CB  . LYS E 48  ? 0.3805 1.5292 0.5182 -0.1670 0.1483  -0.0284 48  LYS E CB  
8098  C CG  . LYS E 48  ? 0.3757 1.5577 0.5171 -0.1018 0.1514  -0.0310 48  LYS E CG  
8099  C CD  . LYS E 48  ? 0.3838 1.6073 0.5198 -0.0743 0.1589  -0.0281 48  LYS E CD  
8100  C CE  . LYS E 48  ? 0.3900 1.6336 0.5189 -0.0044 0.1624  -0.0312 48  LYS E CE  
8101  N NZ  . LYS E 48  ? 0.3914 1.7656 0.5297 0.0172  0.1669  -0.0232 48  LYS E NZ  
8102  N N   . PRO E 49  ? 0.3723 1.2683 0.4901 -0.1205 0.1394  -0.0485 49  PRO E N   
8103  C CA  . PRO E 49  ? 0.3756 1.1867 0.4804 -0.1037 0.1395  -0.0540 49  PRO E CA  
8104  C C   . PRO E 49  ? 0.3832 1.2230 0.4818 -0.0839 0.1460  -0.0522 49  PRO E C   
8105  O O   . PRO E 49  ? 0.3851 1.3064 0.4885 -0.0626 0.1506  -0.0486 49  PRO E O   
8106  C CB  . PRO E 49  ? 0.3721 1.1398 0.4736 -0.0633 0.1359  -0.0611 49  PRO E CB  
8107  C CG  . PRO E 49  ? 0.3702 1.2189 0.4809 -0.0415 0.1374  -0.0587 49  PRO E CG  
8108  C CD  . PRO E 49  ? 0.3649 1.2771 0.4892 -0.0867 0.1369  -0.0518 49  PRO E CD  
8109  N N   . LEU E 50  ? 0.3882 1.1634 0.4751 -0.0891 0.1465  -0.0543 50  LEU E N   
8110  C CA  . LEU E 50  ? 0.3968 1.1814 0.4747 -0.0653 0.1520  -0.0544 50  LEU E CA  
8111  C C   . LEU E 50  ? 0.4036 1.1495 0.4688 -0.0160 0.1512  -0.0617 50  LEU E C   
8112  O O   . LEU E 50  ? 0.4051 1.0692 0.4601 -0.0118 0.1469  -0.0676 50  LEU E O   
8113  C CB  . LEU E 50  ? 0.4019 1.1298 0.4701 -0.0901 0.1525  -0.0539 50  LEU E CB  
8114  C CG  . LEU E 50  ? 0.4113 1.1234 0.4670 -0.0657 0.1568  -0.0557 50  LEU E CG  
8115  C CD1 . LEU E 50  ? 0.4173 1.2173 0.4753 -0.0457 0.1636  -0.0515 50  LEU E CD1 
8116  C CD2 . LEU E 50  ? 0.4161 1.0834 0.4640 -0.0961 0.1574  -0.0534 50  LEU E CD2 
8117  N N   . ILE E 51  ? 0.4123 1.2171 0.4741 0.0209  0.1553  -0.0609 51  ILE E N   
8118  C CA  . ILE E 51  ? 0.4311 1.1949 0.4702 0.0699  0.1554  -0.0676 51  ILE E CA  
8119  C C   . ILE E 51  ? 0.4509 1.2100 0.4703 0.0933  0.1610  -0.0684 51  ILE E C   
8120  O O   . ILE E 51  ? 0.4577 1.2932 0.4780 0.1091  0.1676  -0.0634 51  ILE E O   
8121  C CB  . ILE E 51  ? 0.4378 1.2582 0.4761 0.1042  0.1568  -0.0665 51  ILE E CB  
8122  C CG1 . ILE E 51  ? 0.4164 1.2573 0.4778 0.0752  0.1516  -0.0644 51  ILE E CG1 
8123  C CG2 . ILE E 51  ? 0.4663 1.2219 0.4715 0.1519  0.1560  -0.0740 51  ILE E CG2 
8124  C CD1 . ILE E 51  ? 0.4228 1.2927 0.4809 0.1093  0.1509  -0.0651 51  ILE E CD1 
8125  N N   . LEU E 52  ? 0.4614 1.1341 0.4623 0.0953  0.1585  -0.0745 52  LEU E N   
8126  C CA  . LEU E 52  ? 0.4816 1.1385 0.4613 0.1132  0.1630  -0.0760 52  LEU E CA  
8127  C C   . LEU E 52  ? 0.5177 1.1729 0.4640 0.1681  0.1670  -0.0798 52  LEU E C   
8128  O O   . LEU E 52  ? 0.5397 1.1946 0.4651 0.1892  0.1720  -0.0805 52  LEU E O   
8129  C CB  . LEU E 52  ? 0.4821 1.0501 0.4516 0.0946  0.1584  -0.0809 52  LEU E CB  
8130  C CG  . LEU E 52  ? 0.4554 1.0135 0.4489 0.0463  0.1552  -0.0770 52  LEU E CG  
8131  C CD1 . LEU E 52  ? 0.4582 0.9330 0.4392 0.0357  0.1506  -0.0815 52  LEU E CD1 
8132  C CD2 . LEU E 52  ? 0.4482 1.0678 0.4552 0.0243  0.1610  -0.0695 52  LEU E CD2 
8133  N N   . ARG E 53  ? 0.5281 1.1782 0.4655 0.1922  0.1649  -0.0822 53  ARG E N   
8134  C CA  . ARG E 53  ? 0.5714 1.2103 0.4687 0.2476  0.1686  -0.0856 53  ARG E CA  
8135  C C   . ARG E 53  ? 0.6083 1.1449 0.4620 0.2614  0.1668  -0.0939 53  ARG E C   
8136  O O   . ARG E 53  ? 0.6094 1.0688 0.4552 0.2445  0.1597  -0.0992 53  ARG E O   
8137  C CB  . ARG E 53  ? 0.5807 1.3190 0.4787 0.2772  0.1776  -0.0789 53  ARG E CB  
8138  C CG  . ARG E 53  ? 0.6265 1.3691 0.4837 0.3397  0.1822  -0.0805 53  ARG E CG  
8139  C CD  . ARG E 53  ? 0.6378 1.4844 0.4936 0.3730  0.1918  -0.0730 53  ARG E CD  
8140  N NE  . ARG E 53  ? 0.6179 1.5699 0.5017 0.3783  0.1935  -0.0651 53  ARG E NE  
8141  C CZ  . ARG E 53  ? 0.5754 1.6241 0.5067 0.3377  0.1937  -0.0566 53  ARG E CZ  
8142  N NH1 . ARG E 53  ? 0.5489 1.6009 0.5048 0.2891  0.1927  -0.0545 53  ARG E NH1 
8143  N NH2 . ARG E 53  ? 0.5633 1.7061 0.5140 0.3451  0.1949  -0.0497 53  ARG E NH2 
8144  N N   . ASP E 54  ? 0.6402 1.1774 0.4644 0.2896  0.1730  -0.0947 54  ASP E N   
8145  C CA  . ASP E 54  ? 0.6807 1.1218 0.4585 0.3002  0.1713  -0.1025 54  ASP E CA  
8146  C C   . ASP E 54  ? 0.6596 1.0851 0.4533 0.2635  0.1701  -0.1022 54  ASP E C   
8147  O O   . ASP E 54  ? 0.6885 1.0383 0.4483 0.2642  0.1679  -0.1082 54  ASP E O   
8148  C CB  . ASP E 54  ? 0.7399 1.1751 0.4641 0.3573  0.1786  -0.1046 54  ASP E CB  
8149  C CG  . ASP E 54  ? 0.7772 1.1963 0.4680 0.3991  0.1791  -0.1066 54  ASP E CG  
8150  O OD1 . ASP E 54  ? 0.7934 1.1321 0.4631 0.3920  0.1724  -0.1123 54  ASP E OD1 
8151  O OD2 . ASP E 54  ? 0.7925 1.2816 0.4765 0.4400  0.1865  -0.1018 54  ASP E OD2 
8152  N N   . CYS E 55  ? 0.6140 1.1087 0.4551 0.2308  0.1716  -0.0950 55  CYS E N   
8153  C CA  . CYS E 55  ? 0.5936 1.0728 0.4504 0.1946  0.1705  -0.0938 55  CYS E CA  
8154  C C   . CYS E 55  ? 0.5699 0.9913 0.4417 0.1568  0.1619  -0.0959 55  CYS E C   
8155  O O   . CYS E 55  ? 0.5530 0.9762 0.4411 0.1472  0.1577  -0.0955 55  CYS E O   
8156  C CB  . CYS E 55  ? 0.5634 1.1326 0.4566 0.1734  0.1758  -0.0848 55  CYS E CB  
8157  S SG  . CYS E 55  ? 0.5891 1.2282 0.4656 0.2114  0.1864  -0.0811 55  CYS E SG  
8158  N N   . SER E 56  ? 0.5698 0.9433 0.4347 0.1375  0.1595  -0.0979 56  SER E N   
8159  C CA  . SER E 56  ? 0.5470 0.8760 0.4267 0.1028  0.1523  -0.0984 56  SER E CA  
8160  C C   . SER E 56  ? 0.5123 0.8817 0.4272 0.0680  0.1539  -0.0910 56  SER E C   
8161  O O   . SER E 56  ? 0.5067 0.9364 0.4335 0.0675  0.1602  -0.0858 56  SER E O   
8162  C CB  . SER E 56  ? 0.5707 0.8274 0.4195 0.1015  0.1484  -0.1040 56  SER E CB  
8163  O OG  . SER E 56  ? 0.5671 0.8343 0.4189 0.0903  0.1519  -0.1014 56  SER E OG  
8164  N N   . VAL E 57  ? 0.4935 0.8285 0.4208 0.0393  0.1484  -0.0901 57  VAL E N   
8165  C CA  . VAL E 57  ? 0.4706 0.8271 0.4211 0.0068  0.1498  -0.0833 57  VAL E CA  
8166  C C   . VAL E 57  ? 0.4788 0.8361 0.4205 0.0037  0.1541  -0.0813 57  VAL E C   
8167  O O   . VAL E 57  ? 0.4712 0.8685 0.4251 -0.0124 0.1589  -0.0751 57  VAL E O   
8168  C CB  . VAL E 57  ? 0.4559 0.7689 0.4143 -0.0165 0.1433  -0.0828 57  VAL E CB  
8169  C CG1 . VAL E 57  ? 0.4445 0.7664 0.4151 -0.0463 0.1453  -0.0757 57  VAL E CG1 
8170  C CG2 . VAL E 57  ? 0.4466 0.7622 0.4153 -0.0152 0.1393  -0.0842 57  VAL E CG2 
8171  N N   . ALA E 58  ? 0.4971 0.8090 0.4147 0.0173  0.1521  -0.0867 58  ALA E N   
8172  C CA  . ALA E 58  ? 0.5079 0.8177 0.4137 0.0180  0.1559  -0.0858 58  ALA E CA  
8173  C C   . ALA E 58  ? 0.5186 0.8825 0.4214 0.0373  0.1638  -0.0841 58  ALA E C   
8174  O O   . ALA E 58  ? 0.5128 0.9106 0.4246 0.0253  0.1689  -0.0786 58  ALA E O   
8175  C CB  . ALA E 58  ? 0.5308 0.7816 0.4068 0.0286  0.1515  -0.0925 58  ALA E CB  
8176  N N   . GLY E 59  ? 0.5369 0.9096 0.4244 0.0683  0.1650  -0.0884 59  GLY E N   
8177  C CA  . GLY E 59  ? 0.5497 0.9805 0.4321 0.0935  0.1728  -0.0864 59  GLY E CA  
8178  C C   . GLY E 59  ? 0.5243 1.0334 0.4393 0.0734  0.1773  -0.0774 59  GLY E C   
8179  O O   . GLY E 59  ? 0.5270 1.0847 0.4445 0.0744  0.1837  -0.0727 59  GLY E O   
8180  N N   . TRP E 60  ? 0.5026 1.0232 0.4398 0.0528  0.1737  -0.0748 60  TRP E N   
8181  C CA  . TRP E 60  ? 0.4833 1.0710 0.4468 0.0257  0.1768  -0.0663 60  TRP E CA  
8182  C C   . TRP E 60  ? 0.4771 1.0580 0.4461 -0.0085 0.1785  -0.0609 60  TRP E C   
8183  O O   . TRP E 60  ? 0.4780 1.1155 0.4528 -0.0189 0.1844  -0.0544 60  TRP E O   
8184  C CB  . TRP E 60  ? 0.4668 1.0547 0.4471 0.0099  0.1717  -0.0658 60  TRP E CB  
8185  C CG  . TRP E 60  ? 0.4521 1.0791 0.4524 -0.0309 0.1725  -0.0578 60  TRP E CG  
8186  C CD1 . TRP E 60  ? 0.4525 1.1508 0.4610 -0.0471 0.1783  -0.0501 60  TRP E CD1 
8187  C CD2 . TRP E 60  ? 0.4410 1.0356 0.4501 -0.0618 0.1673  -0.0567 60  TRP E CD2 
8188  N NE1 . TRP E 60  ? 0.4462 1.1527 0.4645 -0.0894 0.1768  -0.0445 60  TRP E NE1 
8189  C CE2 . TRP E 60  ? 0.4401 1.0814 0.4578 -0.0972 0.1702  -0.0486 60  TRP E CE2 
8190  C CE3 . TRP E 60  ? 0.4351 0.9654 0.4425 -0.0633 0.1605  -0.0614 60  TRP E CE3 
8191  C CZ2 . TRP E 60  ? 0.4382 1.0559 0.4584 -0.1327 0.1666  -0.0457 60  TRP E CZ2 
8192  C CZ3 . TRP E 60  ? 0.4284 0.9418 0.4426 -0.0955 0.1572  -0.0582 60  TRP E CZ3 
8193  C CH2 . TRP E 60  ? 0.4322 0.9851 0.4505 -0.1291 0.1604  -0.0507 60  TRP E CH2 
8194  N N   . LEU E 61  ? 0.4736 0.9871 0.4384 -0.0248 0.1735  -0.0629 61  LEU E N   
8195  C CA  . LEU E 61  ? 0.4718 0.9707 0.4376 -0.0561 0.1748  -0.0573 61  LEU E CA  
8196  C C   . LEU E 61  ? 0.4837 0.9887 0.4377 -0.0487 0.1799  -0.0561 61  LEU E C   
8197  O O   . LEU E 61  ? 0.4860 1.0161 0.4421 -0.0711 0.1843  -0.0491 61  LEU E O   
8198  C CB  . LEU E 61  ? 0.4671 0.8965 0.4292 -0.0696 0.1684  -0.0591 61  LEU E CB  
8199  C CG  . LEU E 61  ? 0.4563 0.8767 0.4295 -0.0861 0.1639  -0.0582 61  LEU E CG  
8200  C CD1 . LEU E 61  ? 0.4551 0.8111 0.4215 -0.0968 0.1588  -0.0587 61  LEU E CD1 
8201  C CD2 . LEU E 61  ? 0.4569 0.9223 0.4384 -0.1152 0.1675  -0.0506 61  LEU E CD2 
8202  N N   . LEU E 62  ? 0.4955 0.9744 0.4331 -0.0189 0.1792  -0.0629 62  LEU E N   
8203  C CA  . LEU E 62  ? 0.5094 0.9948 0.4333 -0.0082 0.1841  -0.0626 62  LEU E CA  
8204  C C   . LEU E 62  ? 0.5157 1.0767 0.4427 0.0063  0.1917  -0.0590 62  LEU E C   
8205  O O   . LEU E 62  ? 0.5238 1.1065 0.4449 0.0071  0.1970  -0.0559 62  LEU E O   
8206  C CB  . LEU E 62  ? 0.5269 0.9570 0.4260 0.0171  0.1807  -0.0713 62  LEU E CB  
8207  C CG  . LEU E 62  ? 0.5224 0.8882 0.4169 0.0009  0.1740  -0.0733 62  LEU E CG  
8208  C CD1 . LEU E 62  ? 0.5434 0.8580 0.4109 0.0222  0.1693  -0.0822 62  LEU E CD1 
8209  C CD2 . LEU E 62  ? 0.5199 0.8811 0.4154 -0.0193 0.1764  -0.0677 62  LEU E CD2 
8210  N N   . GLY E 63  ? 0.5124 1.1178 0.4484 0.0184  0.1923  -0.0587 63  GLY E N   
8211  C CA  . GLY E 63  ? 0.5180 1.2076 0.4581 0.0342  0.1995  -0.0540 63  GLY E CA  
8212  C C   . GLY E 63  ? 0.5441 1.2308 0.4583 0.0824  0.2026  -0.0600 63  GLY E C   
8213  O O   . GLY E 63  ? 0.5559 1.2859 0.4627 0.0970  0.2093  -0.0570 63  GLY E O   
8214  N N   . ASN E 64  ? 0.5579 1.1897 0.4539 0.1071  0.1979  -0.0683 64  ASN E N   
8215  C CA  . ASN E 64  ? 0.5940 1.2113 0.4551 0.1553  0.2007  -0.0745 64  ASN E CA  
8216  C C   . ASN E 64  ? 0.6002 1.3102 0.4656 0.1832  0.2081  -0.0691 64  ASN E C   
8217  O O   . ASN E 64  ? 0.5802 1.3427 0.4703 0.1729  0.2075  -0.0643 64  ASN E O   
8218  C CB  . ASN E 64  ? 0.6100 1.1493 0.4489 0.1692  0.1936  -0.0834 64  ASN E CB  
8219  C CG  . ASN E 64  ? 0.6561 1.1758 0.4512 0.2208  0.1964  -0.0895 64  ASN E CG  
8220  O OD1 . ASN E 64  ? 0.6684 1.2525 0.4590 0.2518  0.2034  -0.0860 64  ASN E OD1 
8221  N ND2 . ASN E 64  ? 0.6862 1.1157 0.4449 0.2303  0.1909  -0.0984 64  ASN E ND2 
8222  N N   . PRO E 65  ? 0.6295 1.3640 0.4699 0.2189  0.2151  -0.0692 65  PRO E N   
8223  C CA  . PRO E 65  ? 0.6368 1.4720 0.4805 0.2484  0.2232  -0.0625 65  PRO E CA  
8224  C C   . PRO E 65  ? 0.6465 1.5073 0.4850 0.2799  0.2229  -0.0631 65  PRO E C   
8225  O O   . PRO E 65  ? 0.6390 1.6004 0.4940 0.2910  0.2282  -0.0551 65  PRO E O   
8226  C CB  . PRO E 65  ? 0.6768 1.5010 0.4812 0.2895  0.2296  -0.0656 65  PRO E CB  
8227  C CG  . PRO E 65  ? 0.6980 1.4055 0.4715 0.2868  0.2238  -0.0758 65  PRO E CG  
8228  C CD  . PRO E 65  ? 0.6589 1.3311 0.4651 0.2331  0.2159  -0.0753 65  PRO E CD  
8229  N N   . MET E 66  ? 0.6652 1.4393 0.4796 0.2933  0.2169  -0.0720 66  MET E N   
8230  C CA  . MET E 66  ? 0.6754 1.4617 0.4830 0.3209  0.2158  -0.0730 66  MET E CA  
8231  C C   . MET E 66  ? 0.6292 1.4574 0.4841 0.2793  0.2111  -0.0677 66  MET E C   
8232  O O   . MET E 66  ? 0.6274 1.4995 0.4886 0.2961  0.2113  -0.0654 66  MET E O   
8233  C CB  . MET E 66  ? 0.7140 1.3856 0.4766 0.3432  0.2104  -0.0841 66  MET E CB  
8234  C CG  . MET E 66  ? 0.7704 1.3783 0.4753 0.3807  0.2138  -0.0909 66  MET E CG  
8235  S SD  . MET E 66  ? 0.8165 1.4962 0.4862 0.4499  0.2256  -0.0870 66  MET E SD  
8236  C CE  . MET E 66  ? 0.9009 1.4493 0.4826 0.4944  0.2255  -0.0994 66  MET E CE  
8237  N N   . CYS E 67  ? 0.5963 1.4073 0.4801 0.2264  0.2068  -0.0658 67  CYS E N   
8238  C CA  . CYS E 67  ? 0.5591 1.3931 0.4805 0.1830  0.2019  -0.0615 67  CYS E CA  
8239  C C   . CYS E 67  ? 0.5359 1.4695 0.4887 0.1510  0.2064  -0.0505 67  CYS E C   
8240  O O   . CYS E 67  ? 0.5116 1.4440 0.4881 0.1018  0.2029  -0.0467 67  CYS E O   
8241  C CB  . CYS E 67  ? 0.5461 1.2877 0.4708 0.1475  0.1942  -0.0665 67  CYS E CB  
8242  S SG  . CYS E 67  ? 0.5791 1.2064 0.4619 0.1785  0.1888  -0.0787 67  CYS E SG  
8243  N N   . ASP E 68  ? 0.5487 1.5673 0.4968 0.1797  0.2143  -0.0450 68  ASP E N   
8244  C CA  . ASP E 68  ? 0.5315 1.6599 0.5061 0.1516  0.2191  -0.0334 68  ASP E CA  
8245  C C   . ASP E 68  ? 0.5099 1.6978 0.5115 0.1249  0.2160  -0.0279 68  ASP E C   
8246  O O   . ASP E 68  ? 0.4947 1.7510 0.5182 0.0816  0.2171  -0.0189 68  ASP E O   
8247  C CB  . ASP E 68  ? 0.5522 1.7668 0.5138 0.1960  0.2284  -0.0285 68  ASP E CB  
8248  C CG  . ASP E 68  ? 0.5687 1.7535 0.5112 0.2052  0.2327  -0.0302 68  ASP E CG  
8249  O OD1 . ASP E 68  ? 0.5645 1.6612 0.5031 0.1792  0.2284  -0.0354 68  ASP E OD1 
8250  O OD2 . ASP E 68  ? 0.5870 1.8404 0.5175 0.2402  0.2407  -0.0259 68  ASP E OD2 
8251  N N   . GLU E 69  ? 0.5126 1.6739 0.5093 0.1491  0.2120  -0.0331 69  GLU E N   
8252  C CA  . GLU E 69  ? 0.4922 1.6972 0.5132 0.1228  0.2080  -0.0291 69  GLU E CA  
8253  C C   . GLU E 69  ? 0.4716 1.6301 0.5098 0.0589  0.2019  -0.0283 69  GLU E C   
8254  O O   . GLU E 69  ? 0.4577 1.6733 0.5159 0.0198  0.2004  -0.0215 69  GLU E O   
8255  C CB  . GLU E 69  ? 0.5012 1.6632 0.5096 0.1607  0.2042  -0.0362 69  GLU E CB  
8256  C CG  . GLU E 69  ? 0.4818 1.6931 0.5138 0.1398  0.2002  -0.0323 69  GLU E CG  
8257  C CD  . GLU E 69  ? 0.4932 1.6631 0.5107 0.1801  0.1970  -0.0390 69  GLU E CD  
8258  O OE1 . GLU E 69  ? 0.5227 1.6370 0.5070 0.2290  0.1989  -0.0456 69  GLU E OE1 
8259  O OE2 . GLU E 69  ? 0.4767 1.6664 0.5122 0.1616  0.1924  -0.0375 69  GLU E OE2 
8260  N N   . PHE E 70  ? 0.4741 1.5301 0.5006 0.0492  0.1986  -0.0349 70  PHE E N   
8261  C CA  . PHE E 70  ? 0.4608 1.4542 0.4959 -0.0003 0.1926  -0.0355 70  PHE E CA  
8262  C C   . PHE E 70  ? 0.4627 1.4487 0.4969 -0.0392 0.1950  -0.0304 70  PHE E C   
8263  O O   . PHE E 70  ? 0.4608 1.3693 0.4904 -0.0657 0.1910  -0.0327 70  PHE E O   
8264  C CB  . PHE E 70  ? 0.4625 1.3472 0.4847 0.0152  0.1862  -0.0457 70  PHE E CB  
8265  C CG  . PHE E 70  ? 0.4683 1.3497 0.4836 0.0562  0.1843  -0.0510 70  PHE E CG  
8266  C CD1 . PHE E 70  ? 0.4558 1.3777 0.4874 0.0477  0.1816  -0.0486 70  PHE E CD1 
8267  C CD2 . PHE E 70  ? 0.4914 1.3280 0.4793 0.1030  0.1854  -0.0581 70  PHE E CD2 
8268  C CE1 . PHE E 70  ? 0.4639 1.3823 0.4869 0.0869  0.1801  -0.0529 70  PHE E CE1 
8269  C CE2 . PHE E 70  ? 0.5051 1.3316 0.4791 0.1412  0.1840  -0.0626 70  PHE E CE2 
8270  C CZ  . PHE E 70  ? 0.4901 1.3588 0.4828 0.1343  0.1815  -0.0598 70  PHE E CZ  
8271  N N   . ILE E 71  ? 0.4687 1.5371 0.5054 -0.0410 0.2018  -0.0229 71  ILE E N   
8272  C CA  . ILE E 71  ? 0.4732 1.5509 0.5091 -0.0854 0.2045  -0.0158 71  ILE E CA  
8273  C C   . ILE E 71  ? 0.4707 1.5974 0.5175 -0.1374 0.2028  -0.0077 71  ILE E C   
8274  O O   . ILE E 71  ? 0.4661 1.6820 0.5256 -0.1345 0.2039  -0.0031 71  ILE E O   
8275  C CB  . ILE E 71  ? 0.4832 1.6273 0.5146 -0.0678 0.2126  -0.0108 71  ILE E CB  
8276  C CG1 . ILE E 71  ? 0.4895 1.6683 0.5214 -0.1204 0.2157  -0.0009 71  ILE E CG1 
8277  C CG2 . ILE E 71  ? 0.4839 1.7336 0.5224 -0.0307 0.2173  -0.0073 71  ILE E CG2 
8278  C CD1 . ILE E 71  ? 0.4993 1.7133 0.5236 -0.1065 0.2229  0.0026  71  ILE E CD1 
8279  N N   . ASN E 72  ? 0.4784 1.5451 0.5161 -0.1841 0.2000  -0.0059 72  ASN E N   
8280  C CA  . ASN E 72  ? 0.4859 1.5749 0.5233 -0.2386 0.1976  0.0007  72  ASN E CA  
8281  C C   . ASN E 72  ? 0.4733 1.5783 0.5236 -0.2347 0.1924  -0.0019 72  ASN E C   
8282  O O   . ASN E 72  ? 0.4732 1.6660 0.5329 -0.2548 0.1930  0.0046  72  ASN E O   
8283  C CB  . ASN E 72  ? 0.4977 1.6904 0.5359 -0.2699 0.2033  0.0122  72  ASN E CB  
8284  C CG  . ASN E 72  ? 0.5156 1.6825 0.5367 -0.2895 0.2077  0.0162  72  ASN E CG  
8285  O OD1 . ASN E 72  ? 0.5194 1.5914 0.5279 -0.2799 0.2066  0.0107  72  ASN E OD1 
8286  N ND2 . ASN E 72  ? 0.5278 1.7834 0.5475 -0.3178 0.2128  0.0266  72  ASN E ND2 
8287  N N   . VAL E 73  ? 0.4633 1.4865 0.5133 -0.2102 0.1873  -0.0111 73  VAL E N   
8288  C CA  . VAL E 73  ? 0.4513 1.4804 0.5125 -0.2032 0.1821  -0.0144 73  VAL E CA  
8289  C C   . VAL E 73  ? 0.4612 1.4852 0.5175 -0.2584 0.1782  -0.0099 73  VAL E C   
8290  O O   . VAL E 73  ? 0.4805 1.4454 0.5174 -0.2960 0.1777  -0.0077 73  VAL E O   
8291  C CB  . VAL E 73  ? 0.4414 1.3789 0.5005 -0.1683 0.1771  -0.0249 73  VAL E CB  
8292  C CG1 . VAL E 73  ? 0.4381 1.3858 0.4969 -0.1116 0.1801  -0.0300 73  VAL E CG1 
8293  C CG2 . VAL E 73  ? 0.4494 1.2839 0.4926 -0.1876 0.1744  -0.0277 73  VAL E CG2 
8294  N N   . PRO E 74  ? 0.4528 1.5354 0.5222 -0.2624 0.1757  -0.0084 74  PRO E N   
8295  C CA  . PRO E 74  ? 0.4654 1.5330 0.5263 -0.3129 0.1711  -0.0056 74  PRO E CA  
8296  C C   . PRO E 74  ? 0.4631 1.4195 0.5161 -0.3072 0.1650  -0.0138 74  PRO E C   
8297  O O   . PRO E 74  ? 0.4470 1.3565 0.5066 -0.2630 0.1638  -0.0213 74  PRO E O   
8298  C CB  . PRO E 74  ? 0.4536 1.6265 0.5341 -0.3090 0.1704  -0.0021 74  PRO E CB  
8299  C CG  . PRO E 74  ? 0.4323 1.6261 0.5290 -0.2426 0.1721  -0.0076 74  PRO E CG  
8300  C CD  . PRO E 74  ? 0.4355 1.5934 0.5240 -0.2172 0.1767  -0.0097 74  PRO E CD  
8301  N N   . GLU E 75  ? 0.4826 1.3974 0.5183 -0.3520 0.1613  -0.0120 75  GLU E N   
8302  C CA  . GLU E 75  ? 0.4834 1.2961 0.5091 -0.3476 0.1559  -0.0187 75  GLU E CA  
8303  C C   . GLU E 75  ? 0.4552 1.2792 0.5039 -0.3106 0.1517  -0.0251 75  GLU E C   
8304  O O   . GLU E 75  ? 0.4433 1.3524 0.5097 -0.3042 0.1518  -0.0230 75  GLU E O   
8305  C CB  . GLU E 75  ? 0.5183 1.2843 0.5140 -0.4016 0.1532  -0.0151 75  GLU E CB  
8306  C CG  . GLU E 75  ? 0.5203 1.3298 0.5207 -0.4253 0.1491  -0.0139 75  GLU E CG  
8307  C CD  . GLU E 75  ? 0.5635 1.3065 0.5248 -0.4769 0.1463  -0.0116 75  GLU E CD  
8308  O OE1 . GLU E 75  ? 0.6019 1.3432 0.5331 -0.5205 0.1492  -0.0048 75  GLU E OE1 
8309  O OE2 . GLU E 75  ? 0.5635 1.2528 0.5203 -0.4735 0.1413  -0.0164 75  GLU E OE2 
8310  N N   . TRP E 76  ? 0.4465 1.1861 0.4930 -0.2866 0.1480  -0.0322 76  TRP E N   
8311  C CA  . TRP E 76  ? 0.4232 1.1591 0.4871 -0.2488 0.1441  -0.0388 76  TRP E CA  
8312  C C   . TRP E 76  ? 0.4263 1.0902 0.4819 -0.2618 0.1381  -0.0423 76  TRP E C   
8313  O O   . TRP E 76  ? 0.4446 1.0381 0.4790 -0.2829 0.1373  -0.0417 76  TRP E O   
8314  C CB  . TRP E 76  ? 0.4111 1.1170 0.4786 -0.2022 0.1455  -0.0444 76  TRP E CB  
8315  C CG  . TRP E 76  ? 0.4197 1.0387 0.4707 -0.2057 0.1449  -0.0465 76  TRP E CG  
8316  C CD1 . TRP E 76  ? 0.4171 0.9582 0.4620 -0.1992 0.1400  -0.0512 76  TRP E CD1 
8317  C CD2 . TRP E 76  ? 0.4329 1.0401 0.4712 -0.2160 0.1494  -0.0431 76  TRP E CD2 
8318  N NE1 . TRP E 76  ? 0.4278 0.9131 0.4569 -0.2034 0.1413  -0.0506 76  TRP E NE1 
8319  C CE2 . TRP E 76  ? 0.4378 0.9594 0.4623 -0.2136 0.1470  -0.0459 76  TRP E CE2 
8320  C CE3 . TRP E 76  ? 0.4414 1.1058 0.4784 -0.2266 0.1554  -0.0374 76  TRP E CE3 
8321  C CZ2 . TRP E 76  ? 0.4514 0.9412 0.4604 -0.2202 0.1504  -0.0434 76  TRP E CZ2 
8322  C CZ3 . TRP E 76  ? 0.4549 1.0838 0.4763 -0.2347 0.1587  -0.0352 76  TRP E CZ3 
8323  C CH2 . TRP E 76  ? 0.4600 1.0015 0.4674 -0.2309 0.1562  -0.0383 76  TRP E CH2 
8324  N N   . SER E 77  ? 0.4109 1.0933 0.4810 -0.2465 0.1341  -0.0455 77  SER E N   
8325  C CA  . SER E 77  ? 0.4098 1.0267 0.4749 -0.2506 0.1282  -0.0496 77  SER E CA  
8326  C C   . SER E 77  ? 0.3990 0.9457 0.4632 -0.2167 0.1263  -0.0557 77  SER E C   
8327  O O   . SER E 77  ? 0.4068 0.8815 0.4572 -0.2251 0.1236  -0.0571 77  SER E O   
8328  C CB  . SER E 77  ? 0.3965 1.0615 0.4781 -0.2438 0.1248  -0.0509 77  SER E CB  
8329  O OG  . SER E 77  ? 0.3801 1.1052 0.4792 -0.2046 0.1271  -0.0521 77  SER E OG  
8330  N N   . TYR E 78  ? 0.3849 0.9544 0.4601 -0.1783 0.1278  -0.0590 78  TYR E N   
8331  C CA  . TYR E 78  ? 0.3792 0.8889 0.4498 -0.1486 0.1261  -0.0645 78  TYR E CA  
8332  C C   . TYR E 78  ? 0.3792 0.9197 0.4503 -0.1173 0.1305  -0.0658 78  TYR E C   
8333  O O   . TYR E 78  ? 0.3800 0.9924 0.4580 -0.1129 0.1346  -0.0626 78  TYR E O   
8334  C CB  . TYR E 78  ? 0.3683 0.8477 0.4440 -0.1312 0.1202  -0.0697 78  TYR E CB  
8335  C CG  . TYR E 78  ? 0.3607 0.8961 0.4482 -0.1085 0.1201  -0.0710 78  TYR E CG  
8336  C CD1 . TYR E 78  ? 0.3575 0.9485 0.4556 -0.1269 0.1197  -0.0675 78  TYR E CD1 
8337  C CD2 . TYR E 78  ? 0.3618 0.8928 0.4451 -0.0683 0.1205  -0.0754 78  TYR E CD2 
8338  C CE1 . TYR E 78  ? 0.3515 0.9992 0.4597 -0.1030 0.1198  -0.0680 78  TYR E CE1 
8339  C CE2 . TYR E 78  ? 0.3613 0.9398 0.4495 -0.0427 0.1211  -0.0761 78  TYR E CE2 
8340  C CZ  . TYR E 78  ? 0.3539 0.9943 0.4566 -0.0587 0.1208  -0.0721 78  TYR E CZ  
8341  O OH  . TYR E 78  ? 0.3540 1.0464 0.4610 -0.0302 0.1216  -0.0721 78  TYR E OH  
8342  N N   . ILE E 79  ? 0.3813 0.8693 0.4426 -0.0960 0.1296  -0.0702 79  ILE E N   
8343  C CA  . ILE E 79  ? 0.3888 0.8912 0.4426 -0.0659 0.1335  -0.0722 79  ILE E CA  
8344  C C   . ILE E 79  ? 0.3933 0.8698 0.4387 -0.0299 0.1306  -0.0787 79  ILE E C   
8345  O O   . ILE E 79  ? 0.3899 0.8147 0.4326 -0.0307 0.1249  -0.0822 79  ILE E O   
8346  C CB  . ILE E 79  ? 0.3958 0.8567 0.4376 -0.0716 0.1352  -0.0721 79  ILE E CB  
8347  C CG1 . ILE E 79  ? 0.3991 0.8837 0.4428 -0.1055 0.1391  -0.0652 79  ILE E CG1 
8348  C CG2 . ILE E 79  ? 0.4075 0.8743 0.4370 -0.0395 0.1388  -0.0752 79  ILE E CG2 
8349  C CD1 . ILE E 79  ? 0.4067 0.8406 0.4374 -0.1164 0.1398  -0.0641 79  ILE E CD1 
8350  N N   . VAL E 80  ? 0.4059 0.9169 0.4430 0.0021  0.1347  -0.0799 80  VAL E N   
8351  C CA  . VAL E 80  ? 0.4226 0.9015 0.4405 0.0388  0.1328  -0.0859 80  VAL E CA  
8352  C C   . VAL E 80  ? 0.4479 0.9022 0.4394 0.0645  0.1362  -0.0891 80  VAL E C   
8353  O O   . VAL E 80  ? 0.4558 0.9591 0.4451 0.0770  0.1426  -0.0863 80  VAL E O   
8354  C CB  . VAL E 80  ? 0.4254 0.9614 0.4473 0.0624  0.1345  -0.0848 80  VAL E CB  
8355  C CG1 . VAL E 80  ? 0.4502 0.9397 0.4443 0.1004  0.1324  -0.0910 80  VAL E CG1 
8356  C CG2 . VAL E 80  ? 0.4024 0.9671 0.4496 0.0341  0.1310  -0.0815 80  VAL E CG2 
8357  N N   . GLU E 81  ? 0.4631 0.8429 0.4326 0.0710  0.1319  -0.0948 81  GLU E N   
8358  C CA  . GLU E 81  ? 0.4928 0.8349 0.4309 0.0908  0.1339  -0.0988 81  GLU E CA  
8359  C C   . GLU E 81  ? 0.5259 0.8088 0.4287 0.1167  0.1302  -0.1054 81  GLU E C   
8360  O O   . GLU E 81  ? 0.5196 0.7689 0.4251 0.1063  0.1241  -0.1072 81  GLU E O   
8361  C CB  . GLU E 81  ? 0.4839 0.7878 0.4245 0.0633  0.1315  -0.0985 81  GLU E CB  
8362  C CG  . GLU E 81  ? 0.5123 0.7829 0.4225 0.0777  0.1336  -0.1020 81  GLU E CG  
8363  C CD  . GLU E 81  ? 0.5035 0.7379 0.4158 0.0512  0.1305  -0.1014 81  GLU E CD  
8364  O OE1 . GLU E 81  ? 0.4897 0.6936 0.4103 0.0318  0.1245  -0.1014 81  GLU E OE1 
8365  O OE2 . GLU E 81  ? 0.5114 0.7506 0.4162 0.0516  0.1344  -0.1006 81  GLU E OE2 
8366  N N   . LYS E 82  ? 0.5666 0.8334 0.4320 0.1501  0.1341  -0.1088 82  LYS E N   
8367  C CA  . LYS E 82  ? 0.6117 0.8098 0.4308 0.1743  0.1311  -0.1152 82  LYS E CA  
8368  C C   . LYS E 82  ? 0.6244 0.7462 0.4234 0.1518  0.1246  -0.1195 82  LYS E C   
8369  O O   . LYS E 82  ? 0.6011 0.7257 0.4192 0.1246  0.1236  -0.1175 82  LYS E O   
8370  C CB  . LYS E 82  ? 0.6607 0.8582 0.4365 0.2193  0.1379  -0.1175 82  LYS E CB  
8371  C CG  . LYS E 82  ? 0.6629 0.9242 0.4445 0.2518  0.1430  -0.1141 82  LYS E CG  
8372  C CD  . LYS E 82  ? 0.7170 0.9766 0.4502 0.3020  0.1504  -0.1157 82  LYS E CD  
8373  C CE  . LYS E 82  ? 0.7309 1.0393 0.4577 0.3416  0.1546  -0.1129 82  LYS E CE  
8374  N NZ  . LYS E 82  ? 0.6838 1.1090 0.4637 0.3342  0.1590  -0.1044 82  LYS E NZ  
8375  N N   . ALA E 83  ? 0.6646 0.7200 0.4225 0.1627  0.1203  -0.1248 83  ALA E N   
8376  C CA  . ALA E 83  ? 0.6837 0.6692 0.4163 0.1401  0.1135  -0.1285 83  ALA E CA  
8377  C C   . ALA E 83  ? 0.7188 0.6749 0.4168 0.1450  0.1161  -0.1314 83  ALA E C   
8378  O O   . ALA E 83  ? 0.7098 0.6465 0.4116 0.1170  0.1122  -0.1313 83  ALA E O   
8379  C CB  . ALA E 83  ? 0.7241 0.6456 0.4154 0.1485  0.1084  -0.1330 83  ALA E CB  
8380  N N   . ASN E 84  ? 0.7605 0.7161 0.4236 0.1820  0.1227  -0.1336 84  ASN E N   
8381  C CA  . ASN E 84  ? 0.8002 0.7253 0.4245 0.1911  0.1258  -0.1369 84  ASN E CA  
8382  C C   . ASN E 84  ? 0.8012 0.7856 0.4313 0.2225  0.1355  -0.1342 84  ASN E C   
8383  O O   . ASN E 84  ? 0.8574 0.8161 0.4362 0.2611  0.1404  -0.1376 84  ASN E O   
8384  C CB  . ASN E 84  ? 0.8788 0.7092 0.4252 0.2066  0.1229  -0.1443 84  ASN E CB  
8385  C CG  . ASN E 84  ? 0.8826 0.6578 0.4195 0.1725  0.1130  -0.1463 84  ASN E CG  
8386  O OD1 . ASN E 84  ? 0.8571 0.6305 0.4139 0.1361  0.1079  -0.1451 84  ASN E OD1 
8387  N ND2 . ASN E 84  ? 0.9161 0.6495 0.4215 0.1850  0.1104  -0.1488 84  ASN E ND2 
8388  N N   . PRO E 85  ? 0.7438 0.8065 0.4322 0.2061  0.1386  -0.1277 85  PRO E N   
8389  C CA  . PRO E 85  ? 0.7408 0.8718 0.4392 0.2314  0.1477  -0.1238 85  PRO E CA  
8390  C C   . PRO E 85  ? 0.7840 0.8859 0.4400 0.2493  0.1520  -0.1272 85  PRO E C   
8391  O O   . PRO E 85  ? 0.7823 0.8500 0.4350 0.2235  0.1487  -0.1289 85  PRO E O   
8392  C CB  . PRO E 85  ? 0.6757 0.8774 0.4384 0.1965  0.1482  -0.1165 85  PRO E CB  
8393  C CG  . PRO E 85  ? 0.6454 0.8231 0.4326 0.1637  0.1402  -0.1163 85  PRO E CG  
8394  C CD  . PRO E 85  ? 0.6849 0.7742 0.4271 0.1633  0.1341  -0.1232 85  PRO E CD  
8395  N N   . VAL E 86  ? 0.8244 0.9417 0.4467 0.2949  0.1594  -0.1278 86  VAL E N   
8396  C CA  . VAL E 86  ? 0.8739 0.9595 0.4479 0.3183  0.1642  -0.1314 86  VAL E CA  
8397  C C   . VAL E 86  ? 0.8369 0.9831 0.4477 0.3018  0.1685  -0.1265 86  VAL E C   
8398  O O   . VAL E 86  ? 0.8601 0.9665 0.4449 0.2965  0.1686  -0.1298 86  VAL E O   
8399  C CB  . VAL E 86  ? 0.9349 1.0195 0.4560 0.3784  0.1719  -0.1329 86  VAL E CB  
8400  C CG1 . VAL E 86  ? 0.9854 0.9931 0.4561 0.3968  0.1678  -0.1383 86  VAL E CG1 
8401  C CG2 . VAL E 86  ? 0.8995 1.0990 0.4635 0.3997  0.1795  -0.1244 86  VAL E CG2 
8402  N N   . ASN E 87  ? 0.7830 1.0235 0.4510 0.2920  0.1721  -0.1184 87  ASN E N   
8403  C CA  . ASN E 87  ? 0.7496 1.0516 0.4519 0.2745  0.1766  -0.1126 87  ASN E CA  
8404  C C   . ASN E 87  ? 0.7039 0.9942 0.4446 0.2224  0.1705  -0.1107 87  ASN E C   
8405  O O   . ASN E 87  ? 0.6568 1.0037 0.4461 0.1954  0.1704  -0.1041 87  ASN E O   
8406  C CB  . ASN E 87  ? 0.7213 1.1316 0.4603 0.2852  0.1835  -0.1040 87  ASN E CB  
8407  C CG  . ASN E 87  ? 0.7667 1.2065 0.4681 0.3413  0.1917  -0.1039 87  ASN E CG  
8408  O OD1 . ASN E 87  ? 0.8186 1.2055 0.4680 0.3703  0.1944  -0.1094 87  ASN E OD1 
8409  N ND2 . ASN E 87  ? 0.7506 1.2774 0.4755 0.3576  0.1961  -0.0973 87  ASN E ND2 
8410  N N   . ASP E 88  ? 0.7230 0.9388 0.4373 0.2090  0.1655  -0.1162 88  ASP E N   
8411  C CA  . ASP E 88  ? 0.6868 0.8882 0.4299 0.1654  0.1599  -0.1143 88  ASP E CA  
8412  C C   . ASP E 88  ? 0.6866 0.9014 0.4293 0.1588  0.1641  -0.1123 88  ASP E C   
8413  O O   . ASP E 88  ? 0.6724 0.9528 0.4350 0.1650  0.1712  -0.1068 88  ASP E O   
8414  C CB  . ASP E 88  ? 0.7058 0.8265 0.4227 0.1525  0.1510  -0.1204 88  ASP E CB  
8415  C CG  . ASP E 88  ? 0.6660 0.7806 0.4157 0.1109  0.1449  -0.1172 88  ASP E CG  
8416  O OD1 . ASP E 88  ? 0.6251 0.7903 0.4164 0.0924  0.1475  -0.1104 88  ASP E OD1 
8417  O OD2 . ASP E 88  ? 0.6802 0.7384 0.4099 0.0969  0.1377  -0.1210 88  ASP E OD2 
8418  N N   . LEU E 89  ? 0.7035 0.8605 0.4227 0.1454  0.1597  -0.1164 89  LEU E N   
8419  C CA  . LEU E 89  ? 0.7078 0.8709 0.4214 0.1407  0.1632  -0.1153 89  LEU E CA  
8420  C C   . LEU E 89  ? 0.7625 0.9045 0.4251 0.1788  0.1682  -0.1208 89  LEU E C   
8421  O O   . LEU E 89  ? 0.8098 0.8798 0.4222 0.1869  0.1643  -0.1283 89  LEU E O   
8422  C CB  . LEU E 89  ? 0.7039 0.8189 0.4130 0.1102  0.1561  -0.1169 89  LEU E CB  
8423  C CG  . LEU E 89  ? 0.6544 0.7985 0.4092 0.0756  0.1543  -0.1094 89  LEU E CG  
8424  C CD1 . LEU E 89  ? 0.6158 0.8144 0.4132 0.0681  0.1569  -0.1028 89  LEU E CD1 
8425  C CD2 . LEU E 89  ? 0.6514 0.7484 0.4012 0.0518  0.1453  -0.1111 89  LEU E CD2 
8426  N N   . CYS E 90  ? 0.7601 0.9648 0.4319 0.2016  0.1769  -0.1166 90  CYS E N   
8427  C CA  . CYS E 90  ? 0.8135 1.0072 0.4364 0.2439  0.1832  -0.1207 90  CYS E CA  
8428  C C   . CYS E 90  ? 0.8450 0.9845 0.4317 0.2386  0.1820  -0.1256 90  CYS E C   
8429  O O   . CYS E 90  ? 0.9055 0.9742 0.4314 0.2591  0.1805  -0.1336 90  CYS E O   
8430  C CB  . CYS E 90  ? 0.7984 1.0853 0.4450 0.2655  0.1930  -0.1134 90  CYS E CB  
8431  S SG  . CYS E 90  ? 0.7386 1.1036 0.4460 0.2264  0.1961  -0.1031 90  CYS E SG  
8432  N N   . TYR E 91  ? 0.8084 0.9777 0.4283 0.2102  0.1825  -0.1208 91  TYR E N   
8433  C CA  . TYR E 91  ? 0.8290 0.9498 0.4226 0.1965  0.1797  -0.1246 91  TYR E CA  
8434  C C   . TYR E 91  ? 0.8185 0.8865 0.4143 0.1623  0.1693  -0.1271 91  TYR E C   
8435  O O   . TYR E 91  ? 0.7691 0.8660 0.4120 0.1357  0.1663  -0.1215 91  TYR E O   
8436  C CB  . TYR E 91  ? 0.7953 0.9709 0.4230 0.1809  0.1845  -0.1176 91  TYR E CB  
8437  C CG  . TYR E 91  ? 0.8251 0.9610 0.4196 0.1778  0.1840  -0.1215 91  TYR E CG  
8438  C CD1 . TYR E 91  ? 0.8166 0.9129 0.4119 0.1450  0.1763  -0.1227 91  TYR E CD1 
8439  C CD2 . TYR E 91  ? 0.8634 1.0046 0.4240 0.2089  0.1911  -0.1238 91  TYR E CD2 
8440  C CE1 . TYR E 91  ? 0.8444 0.9083 0.4088 0.1406  0.1754  -0.1261 91  TYR E CE1 
8441  C CE2 . TYR E 91  ? 0.8927 0.9961 0.4207 0.2053  0.1904  -0.1277 91  TYR E CE2 
8442  C CZ  . TYR E 91  ? 0.8826 0.9477 0.4131 0.1698  0.1824  -0.1289 91  TYR E CZ  
8443  O OH  . TYR E 91  ? 0.9121 0.9438 0.4102 0.1647  0.1814  -0.1326 91  TYR E OH  
8444  N N   . PRO E 92  ? 0.8681 0.8594 0.4102 0.1618  0.1638  -0.1352 92  PRO E N   
8445  C CA  . PRO E 92  ? 0.8630 0.8092 0.4032 0.1303  0.1536  -0.1372 92  PRO E CA  
8446  C C   . PRO E 92  ? 0.8120 0.7872 0.3971 0.0937  0.1501  -0.1308 92  PRO E C   
8447  O O   . PRO E 92  ? 0.7983 0.8037 0.3972 0.0902  0.1544  -0.1272 92  PRO E O   
8448  C CB  . PRO E 92  ? 0.9343 0.7984 0.4016 0.1339  0.1494  -0.1464 92  PRO E CB  
8449  C CG  . PRO E 92  ? 0.9820 0.8394 0.4082 0.1748  0.1578  -0.1500 92  PRO E CG  
8450  C CD  . PRO E 92  ? 0.9323 0.8769 0.4119 0.1849  0.1664  -0.1420 92  PRO E CD  
8451  N N   . GLY E 93  ? 0.7873 0.7527 0.3920 0.0687  0.1427  -0.1291 93  GLY E N   
8452  C CA  . GLY E 93  ? 0.7446 0.7342 0.3863 0.0381  0.1394  -0.1226 93  GLY E CA  
8453  C C   . GLY E 93  ? 0.7128 0.7055 0.3828 0.0191  0.1333  -0.1193 93  GLY E C   
8454  O O   . GLY E 93  ? 0.7296 0.6920 0.3828 0.0227  0.1291  -0.1236 93  GLY E O   
8455  N N   . ASP E 94  ? 0.6704 0.6972 0.3796 0.0000  0.1330  -0.1115 94  ASP E N   
8456  C CA  . ASP E 94  ? 0.6380 0.6733 0.3763 -0.0160 0.1283  -0.1071 94  ASP E CA  
8457  C C   . ASP E 94  ? 0.5982 0.6799 0.3788 -0.0179 0.1341  -0.0992 94  ASP E C   
8458  O O   . ASP E 94  ? 0.5931 0.7015 0.3819 -0.0140 0.1407  -0.0958 94  ASP E O   
8459  C CB  . ASP E 94  ? 0.6344 0.6589 0.3695 -0.0390 0.1214  -0.1044 94  ASP E CB  
8460  C CG  . ASP E 94  ? 0.6777 0.6559 0.3669 -0.0455 0.1145  -0.1116 94  ASP E CG  
8461  O OD1 . ASP E 94  ? 0.6956 0.6439 0.3675 -0.0452 0.1099  -0.1162 94  ASP E OD1 
8462  O OD2 . ASP E 94  ? 0.6974 0.6673 0.3650 -0.0528 0.1134  -0.1125 94  ASP E OD2 
8463  N N   . PHE E 95  ? 0.5739 0.6625 0.3777 -0.0253 0.1315  -0.0964 95  PHE E N   
8464  C CA  . PHE E 95  ? 0.5423 0.6645 0.3796 -0.0330 0.1356  -0.0888 95  PHE E CA  
8465  C C   . PHE E 95  ? 0.5256 0.6392 0.3732 -0.0500 0.1304  -0.0837 95  PHE E C   
8466  O O   . PHE E 95  ? 0.5233 0.6196 0.3696 -0.0542 0.1240  -0.0856 95  PHE E O   
8467  C CB  . PHE E 95  ? 0.5331 0.6717 0.3849 -0.0250 0.1373  -0.0898 95  PHE E CB  
8468  C CG  . PHE E 95  ? 0.5132 0.6914 0.3904 -0.0317 0.1436  -0.0830 95  PHE E CG  
8469  C CD1 . PHE E 95  ? 0.4961 0.6762 0.3888 -0.0501 0.1433  -0.0759 95  PHE E CD1 
8470  C CD2 . PHE E 95  ? 0.5167 0.7302 0.3977 -0.0198 0.1498  -0.0831 95  PHE E CD2 
8471  C CE1 . PHE E 95  ? 0.4873 0.6955 0.3948 -0.0605 0.1488  -0.0697 95  PHE E CE1 
8472  C CE2 . PHE E 95  ? 0.5024 0.7550 0.4036 -0.0316 0.1551  -0.0764 95  PHE E CE2 
8473  C CZ  . PHE E 95  ? 0.4897 0.7357 0.4022 -0.0540 0.1544  -0.0699 95  PHE E CZ  
8474  N N   . ASN E 96  ? 0.5169 0.6428 0.3717 -0.0581 0.1334  -0.0768 96  ASN E N   
8475  C CA  . ASN E 96  ? 0.5069 0.6272 0.3658 -0.0687 0.1295  -0.0710 96  ASN E CA  
8476  C C   . ASN E 96  ? 0.4891 0.6123 0.3663 -0.0737 0.1294  -0.0665 96  ASN E C   
8477  O O   . ASN E 96  ? 0.4840 0.6195 0.3718 -0.0753 0.1349  -0.0635 96  ASN E O   
8478  C CB  . ASN E 96  ? 0.5102 0.6398 0.3651 -0.0716 0.1335  -0.0646 96  ASN E CB  
8479  C CG  . ASN E 96  ? 0.5080 0.6344 0.3587 -0.0770 0.1289  -0.0592 96  ASN E CG  
8480  O OD1 . ASN E 96  ? 0.5153 0.6363 0.3538 -0.0802 0.1226  -0.0624 96  ASN E OD1 
8481  N ND2 . ASN E 96  ? 0.5023 0.6324 0.3591 -0.0783 0.1321  -0.0506 96  ASN E ND2 
8482  N N   . ASP E 97  ? 0.4821 0.5949 0.3604 -0.0776 0.1229  -0.0656 97  ASP E N   
8483  C CA  . ASP E 97  ? 0.4682 0.5792 0.3602 -0.0807 0.1219  -0.0622 97  ASP E CA  
8484  C C   . ASP E 97  ? 0.4620 0.5784 0.3654 -0.0788 0.1243  -0.0660 97  ASP E C   
8485  O O   . ASP E 97  ? 0.4564 0.5784 0.3694 -0.0839 0.1279  -0.0619 97  ASP E O   
8486  C CB  . ASP E 97  ? 0.4687 0.5803 0.3607 -0.0836 0.1259  -0.0528 97  ASP E CB  
8487  C CG  . ASP E 97  ? 0.4718 0.5835 0.3542 -0.0819 0.1225  -0.0475 97  ASP E CG  
8488  O OD1 . ASP E 97  ? 0.4696 0.5835 0.3494 -0.0831 0.1157  -0.0505 97  ASP E OD1 
8489  O OD2 . ASP E 97  ? 0.4801 0.5906 0.3547 -0.0795 0.1267  -0.0398 97  ASP E OD2 
8490  N N   . TYR E 98  ? 0.4674 0.5809 0.3653 -0.0714 0.1223  -0.0736 98  TYR E N   
8491  C CA  . TYR E 98  ? 0.4646 0.5895 0.3707 -0.0648 0.1247  -0.0774 98  TYR E CA  
8492  C C   . TYR E 98  ? 0.4505 0.5723 0.3703 -0.0691 0.1213  -0.0767 98  TYR E C   
8493  O O   . TYR E 98  ? 0.4426 0.5820 0.3756 -0.0710 0.1245  -0.0753 98  TYR E O   
8494  C CB  . TYR E 98  ? 0.4837 0.5971 0.3710 -0.0511 0.1231  -0.0855 98  TYR E CB  
8495  C CG  . TYR E 98  ? 0.4872 0.6160 0.3775 -0.0372 0.1263  -0.0893 98  TYR E CG  
8496  C CD1 . TYR E 98  ? 0.4781 0.6447 0.3842 -0.0364 0.1331  -0.0857 98  TYR E CD1 
8497  C CD2 . TYR E 98  ? 0.5041 0.6109 0.3773 -0.0245 0.1225  -0.0961 98  TYR E CD2 
8498  C CE1 . TYR E 98  ? 0.4814 0.6724 0.3904 -0.0220 0.1360  -0.0882 98  TYR E CE1 
8499  C CE2 . TYR E 98  ? 0.5105 0.6339 0.3834 -0.0069 0.1258  -0.0989 98  TYR E CE2 
8500  C CZ  . TYR E 98  ? 0.4971 0.6671 0.3899 -0.0049 0.1326  -0.0947 98  TYR E CZ  
8501  O OH  . TYR E 98  ? 0.5033 0.6997 0.3963 0.0139  0.1359  -0.0966 98  TYR E OH  
8502  N N   . GLU E 99  ? 0.4480 0.5506 0.3638 -0.0723 0.1146  -0.0771 99  GLU E N   
8503  C CA  . GLU E 99  ? 0.4359 0.5335 0.3628 -0.0754 0.1107  -0.0767 99  GLU E CA  
8504  C C   . GLU E 99  ? 0.4257 0.5280 0.3634 -0.0838 0.1133  -0.0693 99  GLU E C   
8505  O O   . GLU E 99  ? 0.4187 0.5236 0.3669 -0.0868 0.1134  -0.0688 99  GLU E O   
8506  C CB  . GLU E 99  ? 0.4391 0.5185 0.3563 -0.0780 0.1028  -0.0784 99  GLU E CB  
8507  C CG  . GLU E 99  ? 0.4584 0.5198 0.3562 -0.0722 0.0993  -0.0863 99  GLU E CG  
8508  C CD  . GLU E 99  ? 0.4794 0.5339 0.3558 -0.0698 0.1008  -0.0890 99  GLU E CD  
8509  O OE1 . GLU E 99  ? 0.4777 0.5390 0.3525 -0.0768 0.1010  -0.0845 99  GLU E OE1 
8510  O OE2 . GLU E 99  ? 0.5007 0.5418 0.3589 -0.0590 0.1020  -0.0954 99  GLU E OE2 
8511  N N   . GLU E 100 ? 0.4301 0.5299 0.3605 -0.0868 0.1154  -0.0635 100 GLU E N   
8512  C CA  . GLU E 100 ? 0.4324 0.5268 0.3617 -0.0925 0.1191  -0.0561 100 GLU E CA  
8513  C C   . GLU E 100 ? 0.4368 0.5414 0.3694 -0.1002 0.1255  -0.0552 100 GLU E C   
8514  O O   . GLU E 100 ? 0.4422 0.5385 0.3730 -0.1088 0.1274  -0.0514 100 GLU E O   
8515  C CB  . GLU E 100 ? 0.4423 0.5311 0.3578 -0.0903 0.1206  -0.0498 100 GLU E CB  
8516  C CG  . GLU E 100 ? 0.4387 0.5248 0.3504 -0.0854 0.1146  -0.0474 100 GLU E CG  
8517  C CD  . GLU E 100 ? 0.4383 0.5129 0.3499 -0.0838 0.1134  -0.0429 100 GLU E CD  
8518  O OE1 . GLU E 100 ? 0.4525 0.5119 0.3539 -0.0847 0.1185  -0.0378 100 GLU E OE1 
8519  O OE2 . GLU E 100 ? 0.4281 0.5059 0.3459 -0.0822 0.1073  -0.0445 100 GLU E OE2 
8520  N N   . LEU E 101 ? 0.4380 0.5614 0.3722 -0.0979 0.1289  -0.0583 101 LEU E N   
8521  C CA  . LEU E 101 ? 0.4416 0.5867 0.3801 -0.1064 0.1348  -0.0570 101 LEU E CA  
8522  C C   . LEU E 101 ? 0.4313 0.5921 0.3836 -0.1072 0.1330  -0.0607 101 LEU E C   
8523  O O   . LEU E 101 ? 0.4341 0.6043 0.3891 -0.1210 0.1355  -0.0575 101 LEU E O   
8524  C CB  . LEU E 101 ? 0.4462 0.6134 0.3825 -0.1002 0.1390  -0.0590 101 LEU E CB  
8525  C CG  . LEU E 101 ? 0.4508 0.6513 0.3914 -0.1096 0.1455  -0.0564 101 LEU E CG  
8526  C CD1 . LEU E 101 ? 0.4641 0.6529 0.3953 -0.1308 0.1490  -0.0486 101 LEU E CD1 
8527  C CD2 . LEU E 101 ? 0.4571 0.6776 0.3930 -0.1008 0.1498  -0.0576 101 LEU E CD2 
8528  N N   . LYS E 102 ? 0.4232 0.5850 0.3804 -0.0933 0.1286  -0.0672 102 LYS E N   
8529  C CA  . LYS E 102 ? 0.4146 0.5885 0.3831 -0.0901 0.1263  -0.0707 102 LYS E CA  
8530  C C   . LYS E 102 ? 0.4088 0.5670 0.3820 -0.1017 0.1233  -0.0677 102 LYS E C   
8531  O O   . LYS E 102 ? 0.4044 0.5788 0.3867 -0.1081 0.1237  -0.0677 102 LYS E O   
8532  C CB  . LYS E 102 ? 0.4158 0.5783 0.3794 -0.0729 0.1215  -0.0777 102 LYS E CB  
8533  C CG  . LYS E 102 ? 0.4264 0.6093 0.3838 -0.0565 0.1249  -0.0821 102 LYS E CG  
8534  C CD  . LYS E 102 ? 0.4407 0.5947 0.3798 -0.0408 0.1202  -0.0889 102 LYS E CD  
8535  C CE  . LYS E 102 ? 0.4525 0.6206 0.3852 -0.0200 0.1220  -0.0936 102 LYS E CE  
8536  N NZ  . LYS E 102 ? 0.4725 0.5997 0.3816 -0.0083 0.1164  -0.0999 102 LYS E NZ  
8537  N N   . HIS E 103 ? 0.4105 0.5395 0.3757 -0.1032 0.1204  -0.0649 103 HIS E N   
8538  C CA  . HIS E 103 ? 0.4105 0.5208 0.3747 -0.1109 0.1183  -0.0615 103 HIS E CA  
8539  C C   . HIS E 103 ? 0.4263 0.5347 0.3817 -0.1276 0.1236  -0.0560 103 HIS E C   
8540  O O   . HIS E 103 ? 0.4298 0.5320 0.3848 -0.1374 0.1229  -0.0549 103 HIS E O   
8541  C CB  . HIS E 103 ? 0.4123 0.4982 0.3667 -0.1053 0.1148  -0.0584 103 HIS E CB  
8542  C CG  . HIS E 103 ? 0.4165 0.4819 0.3653 -0.1086 0.1133  -0.0543 103 HIS E CG  
8543  N ND1 . HIS E 103 ? 0.4047 0.4679 0.3631 -0.1062 0.1081  -0.0571 103 HIS E ND1 
8544  C CD2 . HIS E 103 ? 0.4362 0.4784 0.3661 -0.1126 0.1165  -0.0476 103 HIS E CD2 
8545  C CE1 . HIS E 103 ? 0.4151 0.4572 0.3627 -0.1083 0.1082  -0.0524 103 HIS E CE1 
8546  N NE2 . HIS E 103 ? 0.4367 0.4632 0.3645 -0.1114 0.1134  -0.0467 103 HIS E NE2 
8547  N N   . LEU E 104 ? 0.4399 0.5512 0.3848 -0.1324 0.1288  -0.0525 104 LEU E N   
8548  C CA  . LEU E 104 ? 0.4632 0.5688 0.3926 -0.1519 0.1343  -0.0469 104 LEU E CA  
8549  C C   . LEU E 104 ? 0.4602 0.6003 0.4013 -0.1661 0.1356  -0.0485 104 LEU E C   
8550  O O   . LEU E 104 ? 0.4786 0.6092 0.4068 -0.1867 0.1372  -0.0448 104 LEU E O   
8551  C CB  . LEU E 104 ? 0.4770 0.5843 0.3941 -0.1536 0.1396  -0.0432 104 LEU E CB  
8552  C CG  . LEU E 104 ? 0.5099 0.5781 0.3956 -0.1633 0.1436  -0.0354 104 LEU E CG  
8553  C CD1 . LEU E 104 ? 0.5146 0.5469 0.3883 -0.1482 0.1403  -0.0332 104 LEU E CD1 
8554  C CD2 . LEU E 104 ? 0.5198 0.5966 0.3970 -0.1639 0.1488  -0.0325 104 LEU E CD2 
8555  N N   . LEU E 105 ? 0.4593 0.8217 0.4275 -0.1655 0.1304  -0.0416 105 LEU E N   
8556  C CA  . LEU E 105 ? 0.4575 0.8475 0.4333 -0.1720 0.1276  -0.0478 105 LEU E CA  
8557  C C   . LEU E 105 ? 0.4622 0.8593 0.4347 -0.1742 0.1242  -0.0506 105 LEU E C   
8558  O O   . LEU E 105 ? 0.4670 0.8824 0.4419 -0.1834 0.1220  -0.0568 105 LEU E O   
8559  C CB  . LEU E 105 ? 0.4423 0.8546 0.4330 -0.1623 0.1215  -0.0460 105 LEU E CB  
8560  C CG  . LEU E 105 ? 0.4421 0.8599 0.4360 -0.1618 0.1249  -0.0470 105 LEU E CG  
8561  C CD1 . LEU E 105 ? 0.4308 0.8649 0.4365 -0.1482 0.1176  -0.0457 105 LEU E CD1 
8562  C CD2 . LEU E 105 ? 0.4505 0.8851 0.4462 -0.1762 0.1306  -0.0525 105 LEU E CD2 
8563  N N   . SER E 106 ? 0.4624 0.8472 0.4299 -0.1655 0.1233  -0.0455 106 SER E N   
8564  C CA  . SER E 106 ? 0.4714 0.8600 0.4308 -0.1661 0.1213  -0.0479 106 SER E CA  
8565  C C   . SER E 106 ? 0.4957 0.8678 0.4370 -0.1783 0.1262  -0.0566 106 SER E C   
8566  O O   . SER E 106 ? 0.5080 0.8850 0.4400 -0.1823 0.1233  -0.0622 106 SER E O   
8567  C CB  . SER E 106 ? 0.4673 0.8478 0.4257 -0.1531 0.1213  -0.0385 106 SER E CB  
8568  O OG  . SER E 106 ? 0.4766 0.8306 0.4252 -0.1508 0.1287  -0.0355 106 SER E OG  
8569  N N   . ARG E 107 ? 0.5060 0.8564 0.4408 -0.1842 0.1327  -0.0577 107 ARG E N   
8570  C CA  . ARG E 107 ? 0.5328 0.8633 0.4507 -0.1972 0.1366  -0.0659 107 ARG E CA  
8571  C C   . ARG E 107 ? 0.5374 0.8798 0.4616 -0.2138 0.1356  -0.0713 107 ARG E C   
8572  O O   . ARG E 107 ? 0.5605 0.8847 0.4727 -0.2270 0.1381  -0.0769 107 ARG E O   
8573  C CB  . ARG E 107 ? 0.5460 0.8422 0.4517 -0.1938 0.1445  -0.0627 107 ARG E CB  
8574  C CG  . ARG E 107 ? 0.5571 0.8353 0.4495 -0.1820 0.1477  -0.0606 107 ARG E CG  
8575  C CD  . ARG E 107 ? 0.5840 0.8257 0.4581 -0.1842 0.1550  -0.0630 107 ARG E CD  
8576  N NE  . ARG E 107 ? 0.5857 0.8122 0.4560 -0.1681 0.1605  -0.0552 107 ARG E NE  
8577  C CZ  . ARG E 107 ? 0.6067 0.8174 0.4599 -0.1601 0.1650  -0.0577 107 ARG E CZ  
8578  N NH1 . ARG E 107 ? 0.6314 0.8349 0.4656 -0.1666 0.1636  -0.0694 107 ARG E NH1 
8579  N NH2 . ARG E 107 ? 0.6049 0.8074 0.4600 -0.1448 0.1708  -0.0482 107 ARG E NH2 
8580  N N   . ILE E 108 ? 0.5177 0.8904 0.4610 -0.2130 0.1322  -0.0690 108 ILE E N   
8581  C CA  . ILE E 108 ? 0.5200 0.9089 0.4731 -0.2268 0.1335  -0.0713 108 ILE E CA  
8582  C C   . ILE E 108 ? 0.5124 0.9390 0.4809 -0.2313 0.1259  -0.0747 108 ILE E C   
8583  O O   . ILE E 108 ? 0.4942 0.9417 0.4739 -0.2189 0.1209  -0.0718 108 ILE E O   
8584  C CB  . ILE E 108 ? 0.5078 0.8984 0.4692 -0.2210 0.1389  -0.0649 108 ILE E CB  
8585  C CG1 . ILE E 108 ? 0.5190 0.8727 0.4651 -0.2190 0.1455  -0.0613 108 ILE E CG1 
8586  C CG2 . ILE E 108 ? 0.5103 0.9233 0.4832 -0.2337 0.1417  -0.0658 108 ILE E CG2 
8587  C CD1 . ILE E 108 ? 0.5092 0.8604 0.4592 -0.2104 0.1491  -0.0546 108 ILE E CD1 
8588  N N   . ASN E 109 ? 0.5282 0.9629 0.4981 -0.2495 0.1243  -0.0801 109 ASN E N   
8589  C CA  . ASN E 109 ? 0.5240 0.9967 0.5105 -0.2564 0.1164  -0.0829 109 ASN E CA  
8590  C C   . ASN E 109 ? 0.5177 1.0199 0.5254 -0.2647 0.1200  -0.0799 109 ASN E C   
8591  O O   . ASN E 109 ? 0.5063 1.0465 0.5335 -0.2634 0.1149  -0.0795 109 ASN E O   
8592  C CB  . ASN E 109 ? 0.5489 1.0142 0.5234 -0.2718 0.1090  -0.0913 109 ASN E CB  
8593  C CG  . ASN E 109 ? 0.5498 1.0139 0.5130 -0.2613 0.1013  -0.0943 109 ASN E CG  
8594  O OD1 . ASN E 109 ? 0.5494 1.0408 0.5206 -0.2640 0.0916  -0.0969 109 ASN E OD1 
8595  N ND2 . ASN E 109 ? 0.5521 0.9867 0.4974 -0.2488 0.1058  -0.0928 109 ASN E ND2 
8596  N N   . HIS E 110 ? 0.5267 1.0129 0.5307 -0.2726 0.1293  -0.0770 110 HIS E N   
8597  C CA  . HIS E 110 ? 0.5229 1.0381 0.5460 -0.2797 0.1350  -0.0725 110 HIS E CA  
8598  C C   . HIS E 110 ? 0.5256 1.0222 0.5418 -0.2773 0.1467  -0.0665 110 HIS E C   
8599  O O   . HIS E 110 ? 0.5418 1.0017 0.5401 -0.2837 0.1507  -0.0662 110 HIS E O   
8600  C CB  . HIS E 110 ? 0.5411 1.0719 0.5735 -0.3041 0.1315  -0.0749 110 HIS E CB  
8601  C CG  . HIS E 110 ? 0.5340 1.1090 0.5931 -0.3100 0.1357  -0.0694 110 HIS E CG  
8602  N ND1 . HIS E 110 ? 0.5514 1.1366 0.6205 -0.3330 0.1386  -0.0665 110 HIS E ND1 
8603  C CD2 . HIS E 110 ? 0.5134 1.1253 0.5915 -0.2950 0.1380  -0.0657 110 HIS E CD2 
8604  C CE1 . HIS E 110 ? 0.5401 1.1704 0.6348 -0.3318 0.1436  -0.0604 110 HIS E CE1 
8605  N NE2 . HIS E 110 ? 0.5177 1.1640 0.6172 -0.3080 0.1435  -0.0605 110 HIS E NE2 
8606  N N   . PHE E 111 ? 0.5117 1.0343 0.5413 -0.2669 0.1518  -0.0619 111 PHE E N   
8607  C CA  . PHE E 111 ? 0.5168 1.0303 0.5412 -0.2652 0.1630  -0.0558 111 PHE E CA  
8608  C C   . PHE E 111 ? 0.5244 1.0720 0.5666 -0.2796 0.1697  -0.0516 111 PHE E C   
8609  O O   . PHE E 111 ? 0.5158 1.1036 0.5794 -0.2807 0.1660  -0.0525 111 PHE E O   
8610  C CB  . PHE E 111 ? 0.5003 1.0172 0.5238 -0.2414 0.1644  -0.0539 111 PHE E CB  
8611  C CG  . PHE E 111 ? 0.4970 0.9757 0.5022 -0.2288 0.1613  -0.0540 111 PHE E CG  
8612  C CD1 . PHE E 111 ? 0.5117 0.9526 0.4988 -0.2358 0.1648  -0.0522 111 PHE E CD1 
8613  C CD2 . PHE E 111 ? 0.4807 0.9618 0.4881 -0.2095 0.1547  -0.0548 111 PHE E CD2 
8614  C CE1 . PHE E 111 ? 0.5085 0.9186 0.4821 -0.2236 0.1621  -0.0510 111 PHE E CE1 
8615  C CE2 . PHE E 111 ? 0.4781 0.9275 0.4723 -0.1991 0.1515  -0.0531 111 PHE E CE2 
8616  C CZ  . PHE E 111 ? 0.4911 0.9069 0.4694 -0.2059 0.1554  -0.0511 111 PHE E CZ  
8617  N N   . GLU E 112 ? 0.5415 1.0744 0.5758 -0.2903 0.1795  -0.0457 112 GLU E N   
8618  C CA  . GLU E 112 ? 0.5486 1.1150 0.5993 -0.3007 0.1892  -0.0385 112 GLU E CA  
8619  C C   . GLU E 112 ? 0.5510 1.1094 0.5897 -0.2875 0.2009  -0.0322 112 GLU E C   
8620  O O   . GLU E 112 ? 0.5625 1.0814 0.5794 -0.2875 0.2039  -0.0300 112 GLU E O   
8621  C CB  . GLU E 112 ? 0.5726 1.1313 0.6256 -0.3294 0.1903  -0.0351 112 GLU E CB  
8622  C CG  . GLU E 112 ? 0.5779 1.1826 0.6563 -0.3432 0.1980  -0.0268 112 GLU E CG  
8623  C CD  . GLU E 112 ? 0.6059 1.1977 0.6849 -0.3725 0.2004  -0.0207 112 GLU E CD  
8624  O OE1 . GLU E 112 ? 0.6202 1.1813 0.6894 -0.3864 0.1901  -0.0270 112 GLU E OE1 
8625  O OE2 . GLU E 112 ? 0.6160 1.2275 0.7045 -0.3813 0.2125  -0.0095 112 GLU E OE2 
8626  N N   . LYS E 113 ? 0.5426 1.1384 0.5944 -0.2751 0.2071  -0.0296 113 LYS E N   
8627  C CA  . LYS E 113 ? 0.5478 1.1374 0.5854 -0.2598 0.2175  -0.0251 113 LYS E CA  
8628  C C   . LYS E 113 ? 0.5697 1.1638 0.6056 -0.2759 0.2312  -0.0145 113 LYS E C   
8629  O O   . LYS E 113 ? 0.5753 1.2024 0.6326 -0.2934 0.2355  -0.0094 113 LYS E O   
8630  C CB  . LYS E 113 ? 0.5347 1.1606 0.5842 -0.2381 0.2190  -0.0275 113 LYS E CB  
8631  C CG  . LYS E 113 ? 0.5408 1.1533 0.5700 -0.2169 0.2255  -0.0266 113 LYS E CG  
8632  C CD  . LYS E 113 ? 0.5262 1.1412 0.5552 -0.1916 0.2166  -0.0345 113 LYS E CD  
8633  C CE  . LYS E 113 ? 0.5168 1.1817 0.5718 -0.1838 0.2173  -0.0363 113 LYS E CE  
8634  N NZ  . LYS E 113 ? 0.5055 1.1666 0.5588 -0.1595 0.2070  -0.0438 113 LYS E NZ  
8635  N N   . ILE E 114 ? 0.5835 1.1449 0.5944 -0.2708 0.2375  -0.0101 114 ILE E N   
8636  C CA  . ILE E 114 ? 0.6067 1.1708 0.6124 -0.2832 0.2516  0.0015  114 ILE E CA  
8637  C C   . ILE E 114 ? 0.6160 1.1678 0.5978 -0.2635 0.2598  0.0048  114 ILE E C   
8638  O O   . ILE E 114 ? 0.6093 1.1328 0.5732 -0.2455 0.2522  -0.0015 114 ILE E O   
8639  C CB  . ILE E 114 ? 0.6265 1.1528 0.6219 -0.3065 0.2503  0.0062  114 ILE E CB  
8640  C CG1 . ILE E 114 ? 0.6257 1.0996 0.5962 -0.2969 0.2413  0.0005  114 ILE E CG1 
8641  C CG2 . ILE E 114 ? 0.6270 1.1683 0.6449 -0.3299 0.2437  0.0044  114 ILE E CG2 
8642  C CD1 . ILE E 114 ? 0.6519 1.0843 0.6038 -0.3115 0.2446  0.0078  114 ILE E CD1 
8643  N N   . GLN E 115 ? 0.6335 1.2073 0.6154 -0.2677 0.2750  0.0154  115 GLN E N   
8644  C CA  . GLN E 115 ? 0.6487 1.2123 0.6048 -0.2504 0.2842  0.0194  115 GLN E CA  
8645  C C   . GLN E 115 ? 0.6708 1.1882 0.6013 -0.2606 0.2857  0.0270  115 GLN E C   
8646  O O   . GLN E 115 ? 0.6868 1.2015 0.6227 -0.2839 0.2915  0.0369  115 GLN E O   
8647  C CB  . GLN E 115 ? 0.6599 1.2715 0.6266 -0.2487 0.3015  0.0283  115 GLN E CB  
8648  C CG  . GLN E 115 ? 0.6822 1.2850 0.6191 -0.2322 0.3131  0.0337  115 GLN E CG  
8649  C CD  . GLN E 115 ? 0.6936 1.3484 0.6415 -0.2272 0.3316  0.0420  115 GLN E CD  
8650  O OE1 . GLN E 115 ? 0.6839 1.3694 0.6401 -0.2067 0.3331  0.0348  115 GLN E OE1 
8651  N NE2 . GLN E 115 ? 0.7161 1.3809 0.6641 -0.2453 0.3463  0.0580  115 GLN E NE2 
8652  N N   . ILE E 116 ? 0.6734 1.1545 0.5773 -0.2433 0.2794  0.0229  116 ILE E N   
8653  C CA  . ILE E 116 ? 0.6957 1.1329 0.5735 -0.2488 0.2802  0.0305  116 ILE E CA  
8654  C C   . ILE E 116 ? 0.7193 1.1560 0.5713 -0.2355 0.2910  0.0378  116 ILE E C   
8655  O O   . ILE E 116 ? 0.7450 1.1684 0.5830 -0.2468 0.3002  0.0504  116 ILE E O   
8656  C CB  . ILE E 116 ? 0.6855 1.0786 0.5516 -0.2416 0.2643  0.0229  116 ILE E CB  
8657  C CG1 . ILE E 116 ? 0.6632 1.0619 0.5307 -0.2186 0.2536  0.0108  116 ILE E CG1 
8658  C CG2 . ILE E 116 ? 0.6787 1.0588 0.5599 -0.2607 0.2576  0.0206  116 ILE E CG2 
8659  C CD1 . ILE E 116 ? 0.6618 1.0188 0.5105 -0.2065 0.2413  0.0077  116 ILE E CD1 
8660  N N   . ILE E 117 ? 0.7139 1.1632 0.5577 -0.2113 0.2894  0.0300  117 ILE E N   
8661  C CA  . ILE E 117 ? 0.7387 1.1930 0.5568 -0.1959 0.3000  0.0347  117 ILE E CA  
8662  C C   . ILE E 117 ? 0.7359 1.2427 0.5702 -0.1870 0.3117  0.0331  117 ILE E C   
8663  O O   . ILE E 117 ? 0.7161 1.2382 0.5630 -0.1727 0.3040  0.0212  117 ILE E O   
8664  C CB  . ILE E 117 ? 0.7420 1.1621 0.5316 -0.1726 0.2871  0.0260  117 ILE E CB  
8665  C CG1 . ILE E 117 ? 0.7603 1.1343 0.5248 -0.1785 0.2825  0.0336  117 ILE E CG1 
8666  C CG2 . ILE E 117 ? 0.7597 1.1966 0.5289 -0.1492 0.2942  0.0226  117 ILE E CG2 
8667  C CD1 . ILE E 117 ? 0.7427 1.0879 0.5196 -0.1907 0.2696  0.0316  117 ILE E CD1 
8668  N N   . PRO E 118 ? 0.7569 1.2925 0.5923 -0.1953 0.3307  0.0461  118 PRO E N   
8669  C CA  . PRO E 118 ? 0.7572 1.3448 0.6063 -0.1827 0.3434  0.0453  118 PRO E CA  
8670  C C   . PRO E 118 ? 0.7730 1.3552 0.5908 -0.1507 0.3445  0.0370  118 PRO E C   
8671  O O   . PRO E 118 ? 0.7964 1.3440 0.5782 -0.1429 0.3436  0.0392  118 PRO E O   
8672  C CB  . PRO E 118 ? 0.7786 1.3957 0.6362 -0.2019 0.3639  0.0642  118 PRO E CB  
8673  C CG  . PRO E 118 ? 0.7836 1.3657 0.6407 -0.2290 0.3588  0.0730  118 PRO E CG  
8674  C CD  . PRO E 118 ? 0.7790 1.3058 0.6105 -0.2189 0.3411  0.0630  118 PRO E CD  
8675  N N   . LYS E 119 ? 0.7629 1.3775 0.5938 -0.1320 0.3453  0.0273  119 LYS E N   
8676  C CA  . LYS E 119 ? 0.7803 1.3887 0.5820 -0.0999 0.3447  0.0169  119 LYS E CA  
8677  C C   . LYS E 119 ? 0.8187 1.4424 0.5937 -0.0912 0.3658  0.0271  119 LYS E C   
8678  O O   . LYS E 119 ? 0.8454 1.4419 0.5800 -0.0711 0.3640  0.0222  119 LYS E O   
8679  C CB  . LYS E 119 ? 0.7623 1.4039 0.5872 -0.0826 0.3418  0.0052  119 LYS E CB  
8680  C CG  . LYS E 119 ? 0.7750 1.3950 0.5714 -0.0503 0.3321  -0.0101 119 LYS E CG  
8681  C CD  . LYS E 119 ? 0.7554 1.4040 0.5783 -0.0356 0.3267  -0.0210 119 LYS E CD  
8682  C CE  . LYS E 119 ? 0.7779 1.4134 0.5720 -0.0010 0.3223  -0.0351 119 LYS E CE  
8683  N NZ  . LYS E 119 ? 0.7657 1.4377 0.5862 0.0151  0.3225  -0.0429 119 LYS E NZ  
8684  N N   . SER E 120 ? 0.8234 1.4914 0.6212 -0.1068 0.3854  0.0420  120 SER E N   
8685  C CA  . SER E 120 ? 0.8600 1.5478 0.6366 -0.1026 0.4082  0.0558  120 SER E CA  
8686  C C   . SER E 120 ? 0.8859 1.5274 0.6256 -0.1113 0.4070  0.0648  120 SER E C   
8687  O O   . SER E 120 ? 0.9218 1.5606 0.6258 -0.0975 0.4194  0.0704  120 SER E O   
8688  C CB  . SER E 120 ? 0.8560 1.5998 0.6718 -0.1243 0.4272  0.0728  120 SER E CB  
8689  O OG  . SER E 120 ? 0.8400 1.5695 0.6787 -0.1582 0.4198  0.0815  120 SER E OG  
8690  N N   . SER E 121 ? 0.8701 1.4753 0.6172 -0.1330 0.3921  0.0663  121 SER E N   
8691  C CA  . SER E 121 ? 0.8932 1.4544 0.6102 -0.1436 0.3900  0.0765  121 SER E CA  
8692  C C   . SER E 121 ? 0.9180 1.4387 0.5862 -0.1192 0.3814  0.0685  121 SER E C   
8693  O O   . SER E 121 ? 0.9446 1.4361 0.5833 -0.1241 0.3833  0.0791  121 SER E O   
8694  C CB  . SER E 121 ? 0.8702 1.3975 0.6045 -0.1665 0.3732  0.0760  121 SER E CB  
8695  O OG  . SER E 121 ? 0.8535 1.4106 0.6284 -0.1920 0.3790  0.0837  121 SER E OG  
8696  N N   . TRP E 122 ? 0.9109 1.4274 0.5707 -0.0941 0.3701  0.0503  122 TRP E N   
8697  C CA  . TRP E 122 ? 0.9364 1.4138 0.5506 -0.0709 0.3589  0.0410  122 TRP E CA  
8698  C C   . TRP E 122 ? 0.9795 1.4755 0.5591 -0.0520 0.3781  0.0456  122 TRP E C   
8699  O O   . TRP E 122 ? 0.9905 1.4999 0.5577 -0.0260 0.3797  0.0329  122 TRP E O   
8700  C CB  . TRP E 122 ? 0.9162 1.3800 0.5346 -0.0523 0.3385  0.0202  122 TRP E CB  
8701  C CG  . TRP E 122 ? 0.8781 1.3214 0.5255 -0.0688 0.3198  0.0162  122 TRP E CG  
8702  C CD1 . TRP E 122 ? 0.8418 1.3079 0.5300 -0.0762 0.3155  0.0106  122 TRP E CD1 
8703  C CD2 . TRP E 122 ? 0.8749 1.2719 0.5119 -0.0789 0.3034  0.0184  122 TRP E CD2 
8704  N NE1 . TRP E 122 ? 0.8172 1.2533 0.5189 -0.0899 0.2981  0.0086  122 TRP E NE1 
8705  C CE2 . TRP E 122 ? 0.8362 1.2306 0.5084 -0.0915 0.2909  0.0135  122 TRP E CE2 
8706  C CE3 . TRP E 122 ? 0.9023 1.2608 0.5036 -0.0777 0.2981  0.0244  122 TRP E CE3 
8707  C CZ2 . TRP E 122 ? 0.8241 1.1801 0.4973 -0.1019 0.2748  0.0144  122 TRP E CZ2 
8708  C CZ3 . TRP E 122 ? 0.8890 1.2100 0.4936 -0.0884 0.2810  0.0256  122 TRP E CZ3 
8709  C CH2 . TRP E 122 ? 0.8502 1.1707 0.4908 -0.1000 0.2703  0.0207  122 TRP E CH2 
8710  N N   . SER E 123 ? 1.0067 1.5022 0.5698 -0.0646 0.3929  0.0642  123 SER E N   
8711  C CA  . SER E 123 ? 1.0501 1.5679 0.5812 -0.0498 0.4151  0.0729  123 SER E CA  
8712  C C   . SER E 123 ? 1.0891 1.5664 0.5623 -0.0245 0.4053  0.0638  123 SER E C   
8713  O O   . SER E 123 ? 1.1249 1.6181 0.5668 -0.0014 0.4190  0.0618  123 SER E O   
8714  C CB  . SER E 123 ? 1.0663 1.5981 0.6020 -0.0749 0.4343  0.0985  123 SER E CB  
8715  O OG  . SER E 123 ? 1.0727 1.5554 0.5915 -0.0898 0.4212  0.1057  123 SER E OG  
8716  N N   . SER E 124 ? 1.0844 1.5102 0.5435 -0.0285 0.3815  0.0586  124 SER E N   
8717  C CA  . SER E 124 ? 1.1208 1.5040 0.5268 -0.0077 0.3675  0.0503  124 SER E CA  
8718  C C   . SER E 124 ? 1.1126 1.4762 0.5121 0.0148  0.3454  0.0258  124 SER E C   
8719  O O   . SER E 124 ? 1.1448 1.4741 0.5004 0.0340  0.3318  0.0162  124 SER E O   
8720  C CB  . SER E 124 ? 1.1239 1.4631 0.5184 -0.0248 0.3536  0.0607  124 SER E CB  
8721  O OG  . SER E 124 ? 1.1612 1.4605 0.5048 -0.0065 0.3392  0.0546  124 SER E OG  
8722  N N   . HIS E 125 ? 1.0723 1.4564 0.5149 0.0118  0.3407  0.0163  125 HIS E N   
8723  C CA  . HIS E 125 ? 1.0626 1.4298 0.5048 0.0310  0.3199  -0.0053 125 HIS E CA  
8724  C C   . HIS E 125 ? 1.0516 1.4634 0.5184 0.0440  0.3323  -0.0137 125 HIS E C   
8725  O O   . HIS E 125 ? 1.0401 1.4977 0.5351 0.0330  0.3542  -0.0021 125 HIS E O   
8726  C CB  . HIS E 125 ? 1.0208 1.3610 0.4930 0.0146  0.2961  -0.0089 125 HIS E CB  
8727  C CG  . HIS E 125 ? 1.0320 1.3263 0.4812 0.0064  0.2801  -0.0032 125 HIS E CG  
8728  N ND1 . HIS E 125 ? 1.0305 1.3206 0.4846 -0.0158 0.2879  0.0148  125 HIS E ND1 
8729  C CD2 . HIS E 125 ? 1.0465 1.2975 0.4688 0.0174  0.2558  -0.0126 125 HIS E CD2 
8730  C CE1 . HIS E 125 ? 1.0433 1.2905 0.4744 -0.0166 0.2699  0.0164  125 HIS E CE1 
8731  N NE2 . HIS E 125 ? 1.0523 1.2766 0.4649 0.0027  0.2500  0.0001  125 HIS E NE2 
8732  N N   . GLU E 126 ? 1.0576 1.4551 0.5142 0.0671  0.3172  -0.0331 126 GLU E N   
8733  C CA  . GLU E 126 ? 1.0462 1.4812 0.5275 0.0816  0.3251  -0.0427 126 GLU E CA  
8734  C C   . GLU E 126 ? 0.9959 1.4326 0.5257 0.0667  0.3093  -0.0469 126 GLU E C   
8735  O O   . GLU E 126 ? 0.9849 1.3811 0.5127 0.0642  0.2845  -0.0547 126 GLU E O   
8736  C CB  . GLU E 126 ? 1.0854 1.5011 0.5264 0.1166  0.3173  -0.0617 126 GLU E CB  
8737  C CG  . GLU E 126 ? 1.0818 1.5359 0.5421 0.1368  0.3276  -0.0715 126 GLU E CG  
8738  C CD  . GLU E 126 ? 1.0897 1.6033 0.5626 0.1373  0.3613  -0.0580 126 GLU E CD  
8739  O OE1 . GLU E 126 ? 1.1332 1.6507 0.5666 0.1493  0.3780  -0.0527 126 GLU E OE1 
8740  O OE2 . GLU E 126 ? 1.0536 1.6115 0.5762 0.1257  0.3708  -0.0520 126 GLU E OE2 
8741  N N   . ALA E 127 ? 0.9675 1.4522 0.5409 0.0566  0.3237  -0.0410 127 ALA E N   
8742  C CA  . ALA E 127 ? 0.9194 1.4103 0.5397 0.0393  0.3113  -0.0423 127 ALA E CA  
8743  C C   . ALA E 127 ? 0.9032 1.4269 0.5518 0.0538  0.3119  -0.0525 127 ALA E C   
8744  O O   . ALA E 127 ? 0.8681 1.3903 0.5487 0.0448  0.2977  -0.0566 127 ALA E O   
8745  C CB  . ALA E 127 ? 0.8954 1.4085 0.5467 0.0072  0.3230  -0.0246 127 ALA E CB  
8746  N N   . SER E 128 ? 0.9303 1.4834 0.5663 0.0774  0.3283  -0.0562 128 SER E N   
8747  C CA  . SER E 128 ? 0.9170 1.5090 0.5826 0.0919  0.3326  -0.0632 128 SER E CA  
8748  C C   . SER E 128 ? 0.9360 1.5001 0.5793 0.1232  0.3163  -0.0833 128 SER E C   
8749  O O   . SER E 128 ? 0.9265 1.5167 0.5927 0.1376  0.3168  -0.0903 128 SER E O   
8750  C CB  . SER E 128 ? 0.9333 1.5833 0.6068 0.0986  0.3629  -0.0532 128 SER E CB  
8751  O OG  . SER E 128 ? 0.9084 1.5919 0.6171 0.0670  0.3755  -0.0348 128 SER E OG  
8752  N N   . LEU E 129 ? 0.9649 1.4753 0.5642 0.1335  0.3006  -0.0922 129 LEU E N   
8753  C CA  . LEU E 129 ? 0.9902 1.4666 0.5637 0.1620  0.2826  -0.1115 129 LEU E CA  
8754  C C   . LEU E 129 ? 0.9681 1.3987 0.5499 0.1516  0.2518  -0.1180 129 LEU E C   
8755  O O   . LEU E 129 ? 0.9904 1.3843 0.5507 0.1708  0.2324  -0.1329 129 LEU E O   
8756  C CB  . LEU E 129 ? 1.0478 1.4962 0.5613 0.1849  0.2858  -0.1187 129 LEU E CB  
8757  C CG  . LEU E 129 ? 1.0823 1.5717 0.5792 0.2082  0.3144  -0.1180 129 LEU E CG  
8758  C CD1 . LEU E 129 ? 1.0740 1.6061 0.5843 0.1876  0.3414  -0.0967 129 LEU E CD1 
8759  C CD2 . LEU E 129 ? 1.1441 1.5942 0.5769 0.2379  0.3098  -0.1321 129 LEU E CD2 
8760  N N   . GLY E 130 ? 0.9280 1.3609 0.5412 0.1213  0.2473  -0.1064 130 GLY E N   
8761  C CA  . GLY E 130 ? 0.9041 1.2993 0.5291 0.1096  0.2208  -0.1096 130 GLY E CA  
8762  C C   . GLY E 130 ? 0.8728 1.2830 0.5362 0.1109  0.2114  -0.1146 130 GLY E C   
8763  O O   . GLY E 130 ? 0.8320 1.2557 0.5320 0.0887  0.2090  -0.1065 130 GLY E O   
8764  N N   . VAL E 131 ? 0.8948 1.3001 0.5473 0.1380  0.2056  -0.1281 131 VAL E N   
8765  C CA  . VAL E 131 ? 0.8716 1.2900 0.5570 0.1435  0.1964  -0.1332 131 VAL E CA  
8766  C C   . VAL E 131 ? 0.8938 1.2634 0.5589 0.1616  0.1703  -0.1474 131 VAL E C   
8767  O O   . VAL E 131 ? 0.9296 1.2573 0.5551 0.1703  0.1596  -0.1541 131 VAL E O   
8768  C CB  . VAL E 131 ? 0.8752 1.3459 0.5767 0.1601  0.2172  -0.1343 131 VAL E CB  
8769  C CG1 . VAL E 131 ? 0.8592 1.3783 0.5795 0.1417  0.2428  -0.1193 131 VAL E CG1 
8770  C CG2 . VAL E 131 ? 0.9265 1.3853 0.5882 0.1951  0.2210  -0.1479 131 VAL E CG2 
8771  N N   . SER E 132 ? 0.8755 1.2502 0.5681 0.1664  0.1593  -0.1512 132 SER E N   
8772  C CA  . SER E 132 ? 0.8953 1.2248 0.5741 0.1818  0.1337  -0.1631 132 SER E CA  
8773  C C   . SER E 132 ? 0.8856 1.2350 0.5907 0.1965  0.1310  -0.1679 132 SER E C   
8774  O O   . SER E 132 ? 0.8508 1.2460 0.5935 0.1867  0.1431  -0.1595 132 SER E O   
8775  C CB  . SER E 132 ? 0.8748 1.1683 0.5622 0.1595  0.1114  -0.1574 132 SER E CB  
8776  O OG  . SER E 132 ? 0.8869 1.1443 0.5730 0.1700  0.0865  -0.1656 132 SER E OG  
8777  N N   . SER E 133 ? 0.9189 1.2317 0.6031 0.2198  0.1136  -0.1813 133 SER E N   
8778  C CA  . SER E 133 ? 0.9149 1.2375 0.6202 0.2363  0.1074  -0.1864 133 SER E CA  
8779  C C   . SER E 133 ? 0.8718 1.1905 0.6145 0.2155  0.0906  -0.1774 133 SER E C   
8780  O O   . SER E 133 ? 0.8588 1.1967 0.6280 0.2229  0.0883  -0.1770 133 SER E O   
8781  C CB  . SER E 133 ? 0.9693 1.2462 0.6376 0.2672  0.0917  -0.2037 133 SER E CB  
8782  O OG  . SER E 133 ? 0.9832 1.2018 0.6323 0.2586  0.0649  -0.2068 133 SER E OG  
8783  N N   . ALA E 134 ? 0.8508 1.1456 0.5950 0.1908  0.0794  -0.1698 134 ALA E N   
8784  C CA  . ALA E 134 ? 0.8104 1.1029 0.5881 0.1699  0.0658  -0.1597 134 ALA E CA  
8785  C C   . ALA E 134 ? 0.7639 1.1105 0.5803 0.1529  0.0829  -0.1483 134 ALA E C   
8786  O O   . ALA E 134 ? 0.7378 1.0941 0.5836 0.1455  0.0749  -0.1426 134 ALA E O   
8787  C CB  . ALA E 134 ? 0.8051 1.0607 0.5734 0.1499  0.0514  -0.1542 134 ALA E CB  
8788  N N   . CYS E 135 ? 0.7560 1.1364 0.5713 0.1464  0.1056  -0.1444 135 CYS E N   
8789  C CA  . CYS E 135 ? 0.7189 1.1523 0.5690 0.1312  0.1224  -0.1347 135 CYS E CA  
8790  C C   . CYS E 135 ? 0.7307 1.2079 0.5849 0.1502  0.1418  -0.1384 135 CYS E C   
8791  O O   . CYS E 135 ? 0.7374 1.2380 0.5829 0.1479  0.1614  -0.1357 135 CYS E O   
8792  C CB  . CYS E 135 ? 0.7001 1.1404 0.5512 0.1047  0.1331  -0.1248 135 CYS E CB  
8793  S SG  . CYS E 135 ? 0.6899 1.0809 0.5330 0.0847  0.1136  -0.1198 135 CYS E SG  
8794  N N   . PRO E 136 ? 0.7340 1.2234 0.6020 0.1698  0.1367  -0.1435 136 PRO E N   
8795  C CA  . PRO E 136 ? 0.7459 1.2803 0.6214 0.1901  0.1549  -0.1464 136 PRO E CA  
8796  C C   . PRO E 136 ? 0.7088 1.3042 0.6269 0.1741  0.1689  -0.1351 136 PRO E C   
8797  O O   . PRO E 136 ? 0.6775 1.2783 0.6225 0.1572  0.1584  -0.1289 136 PRO E O   
8798  C CB  . PRO E 136 ? 0.7690 1.2835 0.6406 0.2183  0.1399  -0.1567 136 PRO E CB  
8799  C CG  . PRO E 136 ? 0.7466 1.2316 0.6325 0.2026  0.1170  -0.1525 136 PRO E CG  
8800  C CD  . PRO E 136 ? 0.7359 1.1923 0.6082 0.1777  0.1129  -0.1475 136 PRO E CD  
8801  N N   . TYR E 137 ? 0.7148 1.3558 0.6379 0.1797  0.1919  -0.1324 137 TYR E N   
8802  C CA  . TYR E 137 ? 0.6858 1.3894 0.6503 0.1669  0.2055  -0.1220 137 TYR E CA  
8803  C C   . TYR E 137 ? 0.7063 1.4551 0.6780 0.1942  0.2226  -0.1245 137 TYR E C   
8804  O O   . TYR E 137 ? 0.7342 1.4886 0.6824 0.2071  0.2392  -0.1267 137 TYR E O   
8805  C CB  . TYR E 137 ? 0.6677 1.3881 0.6379 0.1359  0.2188  -0.1109 137 TYR E CB  
8806  C CG  . TYR E 137 ? 0.6444 1.4294 0.6553 0.1209  0.2333  -0.0998 137 TYR E CG  
8807  C CD1 . TYR E 137 ? 0.6132 1.4181 0.6591 0.1062  0.2227  -0.0951 137 TYR E CD1 
8808  C CD2 . TYR E 137 ? 0.6555 1.4820 0.6697 0.1205  0.2571  -0.0933 137 TYR E CD2 
8809  C CE1 . TYR E 137 ? 0.5945 1.4576 0.6776 0.0911  0.2335  -0.0853 137 TYR E CE1 
8810  C CE2 . TYR E 137 ? 0.6356 1.5222 0.6897 0.1046  0.2690  -0.0821 137 TYR E CE2 
8811  C CZ  . TYR E 137 ? 0.6054 1.5094 0.6938 0.0897  0.2563  -0.0786 137 TYR E CZ  
8812  O OH  . TYR E 137 ? 0.5882 1.5511 0.7161 0.0729  0.2658  -0.0678 137 TYR E OH  
8813  N N   . GLN E 138 ? 0.6935 1.4757 0.6975 0.2038  0.2189  -0.1234 138 GLN E N   
8814  C CA  . GLN E 138 ? 0.7117 1.5405 0.7281 0.2323  0.2338  -0.1251 138 GLN E CA  
8815  C C   . GLN E 138 ? 0.7595 1.5554 0.7349 0.2693  0.2355  -0.1393 138 GLN E C   
8816  O O   . GLN E 138 ? 0.7846 1.6117 0.7526 0.2895  0.2563  -0.1405 138 GLN E O   
8817  C CB  . GLN E 138 ? 0.7019 1.5941 0.7413 0.2191  0.2594  -0.1131 138 GLN E CB  
8818  C CG  . GLN E 138 ? 0.6602 1.5787 0.7346 0.1800  0.2573  -0.1000 138 GLN E CG  
8819  C CD  . GLN E 138 ? 0.6478 1.6427 0.7635 0.1726  0.2757  -0.0879 138 GLN E CD  
8820  O OE1 . GLN E 138 ? 0.6678 1.6954 0.7802 0.1842  0.2977  -0.0846 138 GLN E OE1 
8821  N NE2 . GLN E 138 ? 0.6164 1.6408 0.7711 0.1527  0.2666  -0.0805 138 GLN E NE2 
8822  N N   . GLY E 139 ? 0.7742 1.5064 0.7223 0.2779  0.2132  -0.1499 139 GLY E N   
8823  C CA  . GLY E 139 ? 0.8238 1.5145 0.7298 0.3126  0.2093  -0.1654 139 GLY E CA  
8824  C C   . GLY E 139 ? 0.8523 1.5125 0.7135 0.3133  0.2175  -0.1704 139 GLY E C   
8825  O O   . GLY E 139 ? 0.8985 1.5221 0.7197 0.3417  0.2142  -0.1843 139 GLY E O   
8826  N N   . LYS E 140 ? 0.8278 1.5005 0.6936 0.2824  0.2270  -0.1594 140 LYS E N   
8827  C CA  . LYS E 140 ? 0.8526 1.5021 0.6783 0.2801  0.2364  -0.1612 140 LYS E CA  
8828  C C   . LYS E 140 ? 0.8318 1.4377 0.6488 0.2493  0.2202  -0.1572 140 LYS E C   
8829  O O   . LYS E 140 ? 0.7912 1.4038 0.6403 0.2241  0.2107  -0.1488 140 LYS E O   
8830  C CB  . LYS E 140 ? 0.8484 1.5580 0.6870 0.2733  0.2667  -0.1495 140 LYS E CB  
8831  C CG  . LYS E 140 ? 0.8790 1.6298 0.7170 0.3081  0.2863  -0.1538 140 LYS E CG  
8832  C CD  . LYS E 140 ? 0.8515 1.6821 0.7375 0.2969  0.3086  -0.1381 140 LYS E CD  
8833  C CE  . LYS E 140 ? 0.8788 1.7539 0.7717 0.3340  0.3259  -0.1419 140 LYS E CE  
8834  N NZ  . LYS E 140 ? 0.9207 1.8070 0.7787 0.3532  0.3505  -0.1429 140 LYS E NZ  
8835  N N   . SER E 141 ? 0.8618 1.4239 0.6347 0.2525  0.2170  -0.1632 141 SER E N   
8836  C CA  . SER E 141 ? 0.8474 1.3663 0.6091 0.2265  0.2014  -0.1596 141 SER E CA  
8837  C C   . SER E 141 ? 0.8125 1.3634 0.5967 0.1935  0.2158  -0.1435 141 SER E C   
8838  O O   . SER E 141 ? 0.8205 1.4071 0.6025 0.1928  0.2391  -0.1371 141 SER E O   
8839  C CB  . SER E 141 ? 0.8930 1.3600 0.6009 0.2400  0.1945  -0.1699 141 SER E CB  
8840  O OG  . SER E 141 ? 0.9269 1.3540 0.6125 0.2671  0.1761  -0.1855 141 SER E OG  
8841  N N   . SER E 142 ? 0.7764 1.3134 0.5815 0.1667  0.2019  -0.1367 142 SER E N   
8842  C CA  . SER E 142 ? 0.7437 1.3054 0.5713 0.1347  0.2122  -0.1224 142 SER E CA  
8843  C C   . SER E 142 ? 0.7311 1.2465 0.5486 0.1139  0.1954  -0.1197 142 SER E C   
8844  O O   . SER E 142 ? 0.7518 1.2194 0.5417 0.1242  0.1785  -0.1278 142 SER E O   
8845  C CB  . SER E 142 ? 0.7074 1.3156 0.5826 0.1233  0.2153  -0.1156 142 SER E CB  
8846  O OG  . SER E 142 ? 0.6818 1.3161 0.5778 0.0936  0.2265  -0.1027 142 SER E OG  
8847  N N   . PHE E 143 ? 0.6997 1.2291 0.5395 0.0850  0.1996  -0.1082 143 PHE E N   
8848  C CA  . PHE E 143 ? 0.6856 1.1763 0.5203 0.0653  0.1853  -0.1043 143 PHE E CA  
8849  C C   . PHE E 143 ? 0.6474 1.1604 0.5166 0.0377  0.1876  -0.0940 143 PHE E C   
8850  O O   . PHE E 143 ? 0.6342 1.1922 0.5290 0.0317  0.2006  -0.0895 143 PHE E O   
8851  C CB  . PHE E 143 ? 0.7096 1.1753 0.5097 0.0618  0.1910  -0.1019 143 PHE E CB  
8852  C CG  . PHE E 143 ? 0.7076 1.1244 0.4935 0.0522  0.1721  -0.1013 143 PHE E CG  
8853  C CD1 . PHE E 143 ? 0.7192 1.0988 0.4929 0.0660  0.1504  -0.1102 143 PHE E CD1 
8854  C CD2 . PHE E 143 ? 0.6963 1.1043 0.4819 0.0295  0.1756  -0.0912 143 PHE E CD2 
8855  C CE1 . PHE E 143 ? 0.7176 1.0560 0.4818 0.0566  0.1328  -0.1082 143 PHE E CE1 
8856  C CE2 . PHE E 143 ? 0.6950 1.0613 0.4699 0.0221  0.1587  -0.0897 143 PHE E CE2 
8857  C CZ  . PHE E 143 ? 0.7046 1.0381 0.4700 0.0352  0.1374  -0.0978 143 PHE E CZ  
8858  N N   . PHE E 144 ? 0.6321 1.1137 0.5016 0.0218  0.1745  -0.0906 144 PHE E N   
8859  C CA  . PHE E 144 ? 0.6022 1.0969 0.4967 -0.0041 0.1767  -0.0817 144 PHE E CA  
8860  C C   . PHE E 144 ? 0.6049 1.1294 0.5029 -0.0183 0.1976  -0.0739 144 PHE E C   
8861  O O   . PHE E 144 ? 0.6235 1.1326 0.4980 -0.0210 0.2050  -0.0706 144 PHE E O   
8862  C CB  . PHE E 144 ? 0.5948 1.0480 0.4803 -0.0169 0.1637  -0.0783 144 PHE E CB  
8863  C CG  . PHE E 144 ? 0.5951 1.0163 0.4765 -0.0054 0.1427  -0.0836 144 PHE E CG  
8864  C CD1 . PHE E 144 ? 0.5740 1.0033 0.4796 -0.0060 0.1325  -0.0839 144 PHE E CD1 
8865  C CD2 . PHE E 144 ? 0.6185 1.0009 0.4716 0.0047  0.1323  -0.0873 144 PHE E CD2 
8866  C CE1 . PHE E 144 ? 0.5762 0.9758 0.4792 0.0030  0.1132  -0.0867 144 PHE E CE1 
8867  C CE2 . PHE E 144 ? 0.6208 0.9733 0.4721 0.0131  0.1117  -0.0909 144 PHE E CE2 
8868  C CZ  . PHE E 144 ? 0.5994 0.9606 0.4764 0.0120  0.1026  -0.0901 144 PHE E CZ  
8869  N N   . ARG E 145 ? 0.5880 1.1551 0.5159 -0.0280 0.2061  -0.0701 145 ARG E N   
8870  C CA  . ARG E 145 ? 0.5924 1.1939 0.5287 -0.0415 0.2257  -0.0617 145 ARG E CA  
8871  C C   . ARG E 145 ? 0.5912 1.1745 0.5212 -0.0665 0.2298  -0.0530 145 ARG E C   
8872  O O   . ARG E 145 ? 0.6043 1.2039 0.5308 -0.0757 0.2458  -0.0453 145 ARG E O   
8873  C CB  . ARG E 145 ? 0.5736 1.2243 0.5470 -0.0487 0.2302  -0.0592 145 ARG E CB  
8874  C CG  . ARG E 145 ? 0.5762 1.2521 0.5599 -0.0238 0.2284  -0.0663 145 ARG E CG  
8875  C CD  . ARG E 145 ? 0.5650 1.2989 0.5841 -0.0308 0.2385  -0.0609 145 ARG E CD  
8876  N NE  . ARG E 145 ? 0.5652 1.3230 0.5978 -0.0069 0.2346  -0.0672 145 ARG E NE  
8877  C CZ  . ARG E 145 ? 0.5879 1.3596 0.6099 0.0193  0.2439  -0.0714 145 ARG E CZ  
8878  N NH1 . ARG E 145 ? 0.6129 1.3782 0.6090 0.0255  0.2581  -0.0701 145 ARG E NH1 
8879  N NH2 . ARG E 145 ? 0.5882 1.3795 0.6240 0.0410  0.2390  -0.0771 145 ARG E NH2 
8880  N N   . ASN E 146 ? 0.5775 1.1280 0.5067 -0.0772 0.2161  -0.0533 146 ASN E N   
8881  C CA  . ASN E 146 ? 0.5766 1.1087 0.5019 -0.1002 0.2191  -0.0455 146 ASN E CA  
8882  C C   . ASN E 146 ? 0.5981 1.0930 0.4910 -0.0973 0.2200  -0.0428 146 ASN E C   
8883  O O   . ASN E 146 ? 0.6040 1.0862 0.4907 -0.1144 0.2258  -0.0349 146 ASN E O   
8884  C CB  . ASN E 146 ? 0.5540 1.0706 0.4936 -0.1124 0.2057  -0.0464 146 ASN E CB  
8885  C CG  . ASN E 146 ? 0.5364 1.0902 0.5068 -0.1229 0.2066  -0.0465 146 ASN E CG  
8886  O OD1 . ASN E 146 ? 0.5402 1.1241 0.5233 -0.1357 0.2185  -0.0414 146 ASN E OD1 
8887  N ND2 . ASN E 146 ? 0.5190 1.0714 0.5018 -0.1181 0.1933  -0.0514 146 ASN E ND2 
8888  N N   . VAL E 147 ? 0.6128 1.0888 0.4839 -0.0756 0.2133  -0.0492 147 VAL E N   
8889  C CA  . VAL E 147 ? 0.6367 1.0779 0.4748 -0.0709 0.2122  -0.0472 147 VAL E CA  
8890  C C   . VAL E 147 ? 0.6661 1.1136 0.4797 -0.0496 0.2196  -0.0515 147 VAL E C   
8891  O O   . VAL E 147 ? 0.6676 1.1331 0.4864 -0.0322 0.2186  -0.0595 147 VAL E O   
8892  C CB  . VAL E 147 ? 0.6312 1.0303 0.4604 -0.0672 0.1920  -0.0506 147 VAL E CB  
8893  C CG1 . VAL E 147 ? 0.6102 0.9984 0.4557 -0.0878 0.1881  -0.0445 147 VAL E CG1 
8894  C CG2 . VAL E 147 ? 0.6237 1.0219 0.4603 -0.0500 0.1779  -0.0603 147 VAL E CG2 
8895  N N   . VAL E 148 ? 0.6921 1.1233 0.4773 -0.0501 0.2270  -0.0462 148 VAL E N   
8896  C CA  . VAL E 148 ? 0.7256 1.1625 0.4823 -0.0305 0.2366  -0.0491 148 VAL E CA  
8897  C C   . VAL E 148 ? 0.7490 1.1411 0.4705 -0.0141 0.2205  -0.0565 148 VAL E C   
8898  O O   . VAL E 148 ? 0.7540 1.1135 0.4608 -0.0231 0.2127  -0.0514 148 VAL E O   
8899  C CB  . VAL E 148 ? 0.7447 1.1966 0.4904 -0.0419 0.2574  -0.0365 148 VAL E CB  
8900  C CG1 . VAL E 148 ? 0.7780 1.2485 0.4995 -0.0207 0.2718  -0.0389 148 VAL E CG1 
8901  C CG2 . VAL E 148 ? 0.7220 1.2098 0.5038 -0.0651 0.2695  -0.0271 148 VAL E CG2 
8902  N N   . TRP E 149 ? 0.7657 1.1554 0.4737 0.0100  0.2145  -0.0685 149 TRP E N   
8903  C CA  . TRP E 149 ? 0.7959 1.1435 0.4670 0.0268  0.1987  -0.0767 149 TRP E CA  
8904  C C   . TRP E 149 ? 0.8372 1.1834 0.4693 0.0362  0.2130  -0.0742 149 TRP E C   
8905  O O   . TRP E 149 ? 0.8591 1.2286 0.4793 0.0538  0.2266  -0.0789 149 TRP E O   
8906  C CB  . TRP E 149 ? 0.8019 1.1436 0.4725 0.0490  0.1855  -0.0913 149 TRP E CB  
8907  C CG  . TRP E 149 ? 0.8299 1.1233 0.4679 0.0633  0.1632  -0.1007 149 TRP E CG  
8908  C CD1 . TRP E 149 ? 0.8524 1.1112 0.4598 0.0605  0.1550  -0.0980 149 TRP E CD1 
8909  C CD2 . TRP E 149 ? 0.8415 1.1152 0.4743 0.0824  0.1451  -0.1142 149 TRP E CD2 
8910  N NE1 . TRP E 149 ? 0.8766 1.0965 0.4612 0.0754  0.1320  -0.1091 149 TRP E NE1 
8911  C CE2 . TRP E 149 ? 0.8714 1.0981 0.4706 0.0887  0.1256  -0.1193 149 TRP E CE2 
8912  C CE3 . TRP E 149 ? 0.8316 1.1216 0.4850 0.0944  0.1425  -0.1220 149 TRP E CE3 
8913  C CZ2 . TRP E 149 ? 0.8927 1.0869 0.4785 0.1054  0.1031  -0.1321 149 TRP E CZ2 
8914  C CZ3 . TRP E 149 ? 0.8529 1.1098 0.4922 0.1121  0.1211  -0.1344 149 TRP E CZ3 
8915  C CH2 . TRP E 149 ? 0.8838 1.0924 0.4896 0.1168  0.1014  -0.1395 149 TRP E CH2 
8916  N N   . LEU E 150 ? 0.8494 1.1693 0.4614 0.0253  0.2103  -0.0660 150 LEU E N   
8917  C CA  . LEU E 150 ? 0.8889 1.2067 0.4633 0.0313  0.2243  -0.0606 150 LEU E CA  
8918  C C   . LEU E 150 ? 0.9313 1.2123 0.4599 0.0543  0.2097  -0.0722 150 LEU E C   
8919  O O   . LEU E 150 ? 0.9296 1.1739 0.4533 0.0558  0.1852  -0.0784 150 LEU E O   
8920  C CB  . LEU E 150 ? 0.8850 1.1915 0.4585 0.0085  0.2286  -0.0449 150 LEU E CB  
8921  C CG  . LEU E 150 ? 0.8559 1.1955 0.4659 -0.0154 0.2454  -0.0321 150 LEU E CG  
8922  C CD1 . LEU E 150 ? 0.8584 1.1756 0.4621 -0.0351 0.2455  -0.0183 150 LEU E CD1 
8923  C CD2 . LEU E 150 ? 0.8678 1.2530 0.4811 -0.0118 0.2711  -0.0274 150 LEU E CD2 
8924  N N   . ILE E 151 ? 0.9716 1.2634 0.4667 0.0720  0.2249  -0.0745 151 ILE E N   
8925  C CA  . ILE E 151 ? 1.0210 1.2776 0.4649 0.0950  0.2131  -0.0859 151 ILE E CA  
8926  C C   . ILE E 151 ? 1.0621 1.3214 0.4656 0.0989  0.2309  -0.0770 151 ILE E C   
8927  O O   . ILE E 151 ? 1.0539 1.3479 0.4710 0.0864  0.2551  -0.0625 151 ILE E O   
8928  C CB  . ILE E 151 ? 1.0397 1.3009 0.4745 0.1228  0.2104  -0.1038 151 ILE E CB  
8929  C CG1 . ILE E 151 ? 1.0506 1.3616 0.4878 0.1341  0.2409  -0.1011 151 ILE E CG1 
8930  C CG2 . ILE E 151 ? 1.0010 1.2593 0.4755 0.1186  0.1927  -0.1109 151 ILE E CG2 
8931  C CD1 . ILE E 151 ? 1.0664 1.3870 0.5000 0.1623  0.2407  -0.1177 151 ILE E CD1 
8932  N N   . LYS E 152 ? 1.1087 1.3303 0.4621 0.1160  0.2179  -0.0854 152 LYS E N   
8933  C CA  . LYS E 152 ? 1.1550 1.3724 0.4619 0.1223  0.2314  -0.0778 152 LYS E CA  
8934  C C   . LYS E 152 ? 1.1776 1.4389 0.4744 0.1369  0.2629  -0.0756 152 LYS E C   
8935  O O   . LYS E 152 ? 1.1770 1.4586 0.4831 0.1545  0.2681  -0.0876 152 LYS E O   
8936  C CB  . LYS E 152 ? 1.2038 1.3709 0.4570 0.1412  0.2079  -0.0911 152 LYS E CB  
8937  C CG  . LYS E 152 ? 1.2360 1.3955 0.4645 0.1717  0.2023  -0.1126 152 LYS E CG  
8938  C CD  . LYS E 152 ? 1.2760 1.3787 0.4618 0.1851  0.1703  -0.1275 152 LYS E CD  
8939  C CE  . LYS E 152 ? 1.3264 1.4183 0.4715 0.2190  0.1694  -0.1484 152 LYS E CE  
8940  N NZ  . LYS E 152 ? 1.3782 1.4128 0.4711 0.2324  0.1396  -0.1624 152 LYS E NZ  
8941  N N   . LYS E 153 ? 1.1991 1.4754 0.4775 0.1300  0.2840  -0.0593 153 LYS E N   
8942  C CA  . LYS E 153 ? 1.2275 1.5461 0.4916 0.1441  0.3154  -0.0542 153 LYS E CA  
8943  C C   . LYS E 153 ? 1.2942 1.5891 0.4898 0.1657  0.3184  -0.0569 153 LYS E C   
8944  O O   . LYS E 153 ? 1.3120 1.5798 0.4817 0.1552  0.3123  -0.0466 153 LYS E O   
8945  C CB  . LYS E 153 ? 1.2014 1.5631 0.5014 0.1179  0.3409  -0.0306 153 LYS E CB  
8946  C CG  . LYS E 153 ? 1.2085 1.6288 0.5213 0.1281  0.3725  -0.0255 153 LYS E CG  
8947  C CD  . LYS E 153 ? 1.2154 1.6674 0.5336 0.1087  0.3993  0.0000  153 LYS E CD  
8948  C CE  . LYS E 153 ? 1.1644 1.6289 0.5370 0.0722  0.3985  0.0148  153 LYS E CE  
8949  N NZ  . LYS E 153 ? 1.1216 1.6331 0.5515 0.0637  0.4071  0.0145  153 LYS E NZ  
8950  N N   . ASN E 154 ? 1.3331 1.6383 0.4989 0.1969  0.3279  -0.0707 154 ASN E N   
8951  C CA  . ASN E 154 ? 1.4033 1.6843 0.4983 0.2228  0.3298  -0.0774 154 ASN E CA  
8952  C C   . ASN E 154 ? 1.4272 1.6431 0.4835 0.2237  0.2952  -0.0873 154 ASN E C   
8953  O O   . ASN E 154 ? 1.4706 1.6640 0.4785 0.2267  0.2946  -0.0810 154 ASN E O   
8954  C CB  . ASN E 154 ? 1.4299 1.7424 0.5059 0.2178  0.3615  -0.0552 154 ASN E CB  
8955  C CG  . ASN E 154 ? 1.5041 1.8105 0.5110 0.2515  0.3736  -0.0631 154 ASN E CG  
8956  O OD1 . ASN E 154 ? 1.5314 1.8297 0.5154 0.2814  0.3689  -0.0847 154 ASN E OD1 
8957  N ND2 . ASN E 154 ? 1.5405 1.8494 0.5121 0.2475  0.3893  -0.0455 154 ASN E ND2 
8958  N N   . SER E 155 ? 1.3991 1.5867 0.4787 0.2206  0.2660  -0.1015 155 SER E N   
8959  C CA  . SER E 155 ? 1.4194 1.5473 0.4693 0.2219  0.2300  -0.1123 155 SER E CA  
8960  C C   . SER E 155 ? 1.4043 1.5143 0.4594 0.1947  0.2206  -0.0940 155 SER E C   
8961  O O   . SER E 155 ? 1.4428 1.5114 0.4544 0.1991  0.2010  -0.0965 155 SER E O   
8962  C CB  . SER E 155 ? 1.4956 1.5924 0.4720 0.2543  0.2240  -0.1290 155 SER E CB  
8963  O OG  . SER E 155 ? 1.5136 1.5551 0.4695 0.2605  0.1857  -0.1465 155 SER E OG  
8964  N N   . THR E 156 ? 1.3515 1.4918 0.4588 0.1676  0.2339  -0.0758 156 THR E N   
8965  C CA  . THR E 156 ? 1.3330 1.4566 0.4517 0.1417  0.2250  -0.0585 156 THR E CA  
8966  C C   . THR E 156 ? 1.2652 1.4101 0.4518 0.1154  0.2263  -0.0497 156 THR E C   
8967  O O   . THR E 156 ? 1.2390 1.4275 0.4592 0.1090  0.2499  -0.0437 156 THR E O   
8968  C CB  . THR E 156 ? 1.3617 1.4994 0.4537 0.1356  0.2491  -0.0379 156 THR E CB  
8969  O OG1 . THR E 156 ? 1.3251 1.5103 0.4617 0.1175  0.2771  -0.0217 156 THR E OG1 
8970  C CG2 . THR E 156 ? 1.4288 1.5655 0.4573 0.1641  0.2615  -0.0445 156 THR E CG2 
8971  N N   . TYR E 157 ? 1.2393 1.3547 0.4458 0.1006  0.2008  -0.0489 157 TYR E N   
8972  C CA  . TYR E 157 ? 1.1794 1.3102 0.4453 0.0758  0.2008  -0.0401 157 TYR E CA  
8973  C C   . TYR E 157 ? 1.1749 1.2922 0.4433 0.0547  0.2003  -0.0208 157 TYR E C   
8974  O O   . TYR E 157 ? 1.1724 1.2556 0.4386 0.0496  0.1760  -0.0205 157 TYR E O   
8975  C CB  . TYR E 157 ? 1.1498 1.2610 0.4424 0.0762  0.1735  -0.0538 157 TYR E CB  
8976  C CG  . TYR E 157 ? 1.0896 1.2245 0.4427 0.0563  0.1772  -0.0487 157 TYR E CG  
8977  C CD1 . TYR E 157 ? 1.0603 1.1900 0.4399 0.0330  0.1747  -0.0342 157 TYR E CD1 
8978  C CD2 . TYR E 157 ? 1.0651 1.2265 0.4470 0.0621  0.1828  -0.0587 157 TYR E CD2 
8979  C CE1 . TYR E 157 ? 1.0103 1.1595 0.4406 0.0161  0.1777  -0.0308 157 TYR E CE1 
8980  C CE2 . TYR E 157 ? 1.0136 1.1959 0.4475 0.0444  0.1852  -0.0543 157 TYR E CE2 
8981  C CZ  . TYR E 157 ? 0.9870 1.1627 0.4439 0.0214  0.1827  -0.0408 157 TYR E CZ  
8982  O OH  . TYR E 157 ? 0.9402 1.1349 0.4448 0.0050  0.1848  -0.0376 157 TYR E OH  
8983  N N   . PRO E 158 ? 1.1764 1.3206 0.4499 0.0425  0.2268  -0.0038 158 PRO E N   
8984  C CA  . PRO E 158 ? 1.1743 1.3043 0.4511 0.0224  0.2272  0.0151  158 PRO E CA  
8985  C C   . PRO E 158 ? 1.1226 1.2502 0.4509 0.0015  0.2172  0.0185  158 PRO E C   
8986  O O   . PRO E 158 ? 1.0847 1.2344 0.4514 -0.0021 0.2194  0.0108  158 PRO E O   
8987  C CB  . PRO E 158 ? 1.1886 1.3516 0.4615 0.0148  0.2594  0.0314  158 PRO E CB  
8988  C CG  . PRO E 158 ? 1.1774 1.3811 0.4672 0.0242  0.2764  0.0222  158 PRO E CG  
8989  C CD  . PRO E 158 ? 1.1861 1.3733 0.4594 0.0479  0.2571  -0.0005 158 PRO E CD  
8990  N N   . THR E 159 ? 1.1242 1.2248 0.4517 -0.0106 0.2063  0.0300  159 THR E N   
8991  C CA  . THR E 159 ? 1.0812 1.1760 0.4528 -0.0284 0.1967  0.0338  159 THR E CA  
8992  C C   . THR E 159 ? 1.0530 1.1810 0.4622 -0.0464 0.2192  0.0416  159 THR E C   
8993  O O   . THR E 159 ? 1.0714 1.2157 0.4710 -0.0534 0.2409  0.0541  159 THR E O   
8994  C CB  . THR E 159 ? 1.0927 1.1542 0.4538 -0.0367 0.1842  0.0470  159 THR E CB  
8995  O OG1 . THR E 159 ? 1.1261 1.1583 0.4493 -0.0205 0.1630  0.0410  159 THR E OG1 
8996  C CG2 . THR E 159 ? 1.0495 1.1033 0.4541 -0.0507 0.1725  0.0487  159 THR E CG2 
8997  N N   . ILE E 160 ? 1.0114 1.1491 0.4628 -0.0542 0.2132  0.0345  160 ILE E N   
8998  C CA  . ILE E 160 ? 0.9829 1.1497 0.4726 -0.0720 0.2300  0.0398  160 ILE E CA  
8999  C C   . ILE E 160 ? 0.9691 1.1166 0.4785 -0.0910 0.2256  0.0509  160 ILE E C   
9000  O O   . ILE E 160 ? 0.9548 1.0784 0.4724 -0.0896 0.2063  0.0473  160 ILE E O   
9001  C CB  . ILE E 160 ? 0.9458 1.1348 0.4687 -0.0684 0.2257  0.0250  160 ILE E CB  
9002  C CG1 . ILE E 160 ? 0.9629 1.1728 0.4682 -0.0483 0.2321  0.0138  160 ILE E CG1 
9003  C CG2 . ILE E 160 ? 0.9141 1.1295 0.4774 -0.0885 0.2389  0.0304  160 ILE E CG2 
9004  C CD1 . ILE E 160 ? 0.9350 1.1565 0.4642 -0.0390 0.2217  -0.0021 160 ILE E CD1 
9005  N N   . LYS E 161 ? 0.9772 1.1345 0.4938 -0.1082 0.2434  0.0648  161 LYS E N   
9006  C CA  . LYS E 161 ? 0.9660 1.1056 0.5031 -0.1267 0.2412  0.0743  161 LYS E CA  
9007  C C   . LYS E 161 ? 0.9499 1.1177 0.5190 -0.1453 0.2574  0.0773  161 LYS E C   
9008  O O   . LYS E 161 ? 0.9695 1.1543 0.5331 -0.1547 0.2758  0.0883  161 LYS E O   
9009  C CB  . LYS E 161 ? 1.0015 1.1126 0.5101 -0.1310 0.2429  0.0907  161 LYS E CB  
9010  C CG  . LYS E 161 ? 1.0224 1.1041 0.4997 -0.1140 0.2244  0.0889  161 LYS E CG  
9011  C CD  . LYS E 161 ? 1.0535 1.1046 0.5082 -0.1193 0.2233  0.1060  161 LYS E CD  
9012  C CE  . LYS E 161 ? 1.0756 1.0992 0.4999 -0.1025 0.2027  0.1041  161 LYS E CE  
9013  N NZ  . LYS E 161 ? 1.1177 1.1169 0.5085 -0.1035 0.2044  0.1216  161 LYS E NZ  
9014  N N   . ARG E 162 ? 0.9175 1.0914 0.5202 -0.1509 0.2500  0.0682  162 ARG E N   
9015  C CA  . ARG E 162 ? 0.9016 1.1027 0.5356 -0.1680 0.2619  0.0687  162 ARG E CA  
9016  C C   . ARG E 162 ? 0.8857 1.0687 0.5436 -0.1819 0.2542  0.0684  162 ARG E C   
9017  O O   . ARG E 162 ? 0.8672 1.0331 0.5313 -0.1739 0.2384  0.0607  162 ARG E O   
9018  C CB  . ARG E 162 ? 0.8763 1.1117 0.5284 -0.1584 0.2618  0.0547  162 ARG E CB  
9019  C CG  . ARG E 162 ? 0.8754 1.1527 0.5434 -0.1680 0.2808  0.0583  162 ARG E CG  
9020  C CD  . ARG E 162 ? 0.9103 1.1984 0.5557 -0.1702 0.2988  0.0719  162 ARG E CD  
9021  N NE  . ARG E 162 ? 0.9032 1.2398 0.5681 -0.1722 0.3143  0.0713  162 ARG E NE  
9022  C CZ  . ARG E 162 ? 0.9147 1.2794 0.5673 -0.1546 0.3238  0.0677  162 ARG E CZ  
9023  N NH1 . ARG E 162 ? 0.9395 1.2874 0.5546 -0.1330 0.3203  0.0640  162 ARG E NH1 
9024  N NH2 . ARG E 162 ? 0.9039 1.3152 0.5821 -0.1585 0.3374  0.0681  162 ARG E NH2 
9025  N N   . SER E 163 ? 0.8961 1.0850 0.5681 -0.2026 0.2655  0.0766  163 SER E N   
9026  C CA  . SER E 163 ? 0.8893 1.0591 0.5803 -0.2166 0.2599  0.0763  163 SER E CA  
9027  C C   . SER E 163 ? 0.8832 1.0819 0.6026 -0.2344 0.2687  0.0742  163 SER E C   
9028  O O   . SER E 163 ? 0.8972 1.1203 0.6183 -0.2445 0.2829  0.0820  163 SER E O   
9029  C CB  . SER E 163 ? 0.9192 1.0522 0.5924 -0.2257 0.2617  0.0907  163 SER E CB  
9030  O OG  . SER E 163 ? 0.9124 1.0232 0.6008 -0.2375 0.2566  0.0897  163 SER E OG  
9031  N N   . TYR E 164 ? 0.8676 1.0652 0.6094 -0.2382 0.2599  0.0641  164 TYR E N   
9032  C CA  . TYR E 164 ? 0.8668 1.0861 0.6345 -0.2569 0.2651  0.0618  164 TYR E CA  
9033  C C   . TYR E 164 ? 0.8810 1.0686 0.6550 -0.2700 0.2588  0.0612  164 TYR E C   
9034  O O   . TYR E 164 ? 0.8670 1.0332 0.6405 -0.2599 0.2474  0.0542  164 TYR E O   
9035  C CB  . TYR E 164 ? 0.8331 1.0883 0.6229 -0.2492 0.2611  0.0486  164 TYR E CB  
9036  C CG  . TYR E 164 ? 0.8216 1.0935 0.6377 -0.2682 0.2621  0.0452  164 TYR E CG  
9037  C CD1 . TYR E 164 ? 0.8311 1.1335 0.6604 -0.2850 0.2741  0.0520  164 TYR E CD1 
9038  C CD2 . TYR E 164 ? 0.8051 1.0616 0.6320 -0.2701 0.2509  0.0360  164 TYR E CD2 
9039  C CE1 . TYR E 164 ? 0.8239 1.1406 0.6773 -0.3040 0.2728  0.0490  164 TYR E CE1 
9040  C CE2 . TYR E 164 ? 0.7994 1.0684 0.6468 -0.2876 0.2503  0.0321  164 TYR E CE2 
9041  C CZ  . TYR E 164 ? 0.8089 1.1074 0.6697 -0.3050 0.2603  0.0383  164 TYR E CZ  
9042  O OH  . TYR E 164 ? 0.8057 1.1163 0.6869 -0.3235 0.2575  0.0343  164 TYR E OH  
9043  N N   . ASN E 165 ? 0.9159 1.1014 0.6963 -0.2925 0.2663  0.0686  165 ASN E N   
9044  C CA  . ASN E 165 ? 0.9412 1.0948 0.7255 -0.3064 0.2609  0.0671  165 ASN E CA  
9045  C C   . ASN E 165 ? 0.9096 1.0863 0.7195 -0.3179 0.2576  0.0563  165 ASN E C   
9046  O O   . ASN E 165 ? 0.9094 1.1196 0.7350 -0.3319 0.2646  0.0589  165 ASN E O   
9047  C CB  . ASN E 165 ? 1.0078 1.1383 0.7810 -0.3254 0.2691  0.0822  165 ASN E CB  
9048  C CG  . ASN E 165 ? 1.0638 1.1478 0.8314 -0.3342 0.2623  0.0814  165 ASN E CG  
9049  O OD1 . ASN E 165 ? 1.0466 1.1212 0.8220 -0.3297 0.2532  0.0689  165 ASN E OD1 
9050  N ND2 . ASN E 165 ? 1.1500 1.2035 0.9027 -0.3460 0.2673  0.0953  165 ASN E ND2 
9051  N N   . ASN E 166 ? 0.8811 1.0413 0.6952 -0.3120 0.2469  0.0451  166 ASN E N   
9052  C CA  . ASN E 166 ? 0.8546 1.0334 0.6894 -0.3213 0.2419  0.0340  166 ASN E CA  
9053  C C   . ASN E 166 ? 0.8740 1.0336 0.7110 -0.3465 0.2425  0.0363  166 ASN E C   
9054  O O   . ASN E 166 ? 0.8873 1.0084 0.7148 -0.3483 0.2364  0.0321  166 ASN E O   
9055  C CB  . ASN E 166 ? 0.8303 0.9985 0.6663 -0.3050 0.2310  0.0221  166 ASN E CB  
9056  C CG  . ASN E 166 ? 0.8094 1.0040 0.6654 -0.3104 0.2255  0.0106  166 ASN E CG  
9057  O OD1 . ASN E 166 ? 0.8029 1.0335 0.6752 -0.3211 0.2291  0.0107  166 ASN E OD1 
9058  N ND2 . ASN E 166 ? 0.7990 0.9777 0.6542 -0.3023 0.2170  0.0015  166 ASN E ND2 
9059  N N   . THR E 167 ? 0.8741 1.0610 0.7241 -0.3654 0.2497  0.0432  167 THR E N   
9060  C CA  . THR E 167 ? 0.8965 1.0681 0.7512 -0.3927 0.2493  0.0467  167 THR E CA  
9061  C C   . THR E 167 ? 0.8793 1.0661 0.7525 -0.4035 0.2400  0.0336  167 THR E C   
9062  O O   . THR E 167 ? 0.9051 1.0732 0.7803 -0.4257 0.2359  0.0333  167 THR E O   
9063  C CB  . THR E 167 ? 0.9142 1.1108 0.7773 -0.4109 0.2612  0.0624  167 THR E CB  
9064  O OG1 . THR E 167 ? 0.8867 1.1413 0.7715 -0.4067 0.2660  0.0611  167 THR E OG1 
9065  C CG2 . THR E 167 ? 0.9341 1.1093 0.7745 -0.4032 0.2701  0.0767  167 THR E CG2 
9066  N N   . ASN E 168 ? 0.8367 1.0555 0.7221 -0.3883 0.2357  0.0232  168 ASN E N   
9067  C CA  . ASN E 168 ? 0.8204 1.0530 0.7205 -0.3953 0.2256  0.0104  168 ASN E CA  
9068  C C   . ASN E 168 ? 0.8264 1.0116 0.7084 -0.3900 0.2166  0.0006  168 ASN E C   
9069  O O   . ASN E 168 ? 0.8242 0.9816 0.6889 -0.3718 0.2174  0.0013  168 ASN E O   
9070  C CB  . ASN E 168 ? 0.7809 1.0579 0.6972 -0.3780 0.2232  0.0029  168 ASN E CB  
9071  C CG  . ASN E 168 ? 0.7671 1.0824 0.6919 -0.3691 0.2337  0.0115  168 ASN E CG  
9072  O OD1 . ASN E 168 ? 0.7631 1.1208 0.7091 -0.3796 0.2381  0.0153  168 ASN E OD1 
9073  N ND2 . ASN E 168 ? 0.7614 1.0627 0.6695 -0.3488 0.2373  0.0145  168 ASN E ND2 
9074  N N   . GLN E 169 ? 0.8342 1.0104 0.7194 -0.4049 0.2078  -0.0084 169 GLN E N   
9075  C CA  . GLN E 169 ? 0.8418 0.9760 0.7083 -0.3970 0.1998  -0.0195 169 GLN E CA  
9076  C C   . GLN E 169 ? 0.8041 0.9618 0.6771 -0.3783 0.1936  -0.0309 169 GLN E C   
9077  O O   . GLN E 169 ? 0.8080 0.9637 0.6809 -0.3827 0.1848  -0.0421 169 GLN E O   
9078  C CB  . GLN E 169 ? 0.8816 0.9840 0.7407 -0.4207 0.1927  -0.0246 169 GLN E CB  
9079  C CG  . GLN E 169 ? 0.8814 1.0166 0.7606 -0.4413 0.1849  -0.0304 169 GLN E CG  
9080  C CD  . GLN E 169 ? 0.9177 1.0149 0.7827 -0.4556 0.1730  -0.0424 169 GLN E CD  
9081  O OE1 . GLN E 169 ? 0.9318 0.9865 0.7727 -0.4424 0.1700  -0.0510 169 GLN E OE1 
9082  N NE2 . GLN E 169 ? 0.9346 1.0474 0.8144 -0.4824 0.1658  -0.0432 169 GLN E NE2 
9083  N N   . GLU E 170 ? 0.7692 0.9476 0.6466 -0.3577 0.1979  -0.0272 170 GLU E N   
9084  C CA  . GLU E 170 ? 0.7331 0.9342 0.6177 -0.3389 0.1928  -0.0349 170 GLU E CA  
9085  C C   . GLU E 170 ? 0.7131 0.9067 0.5904 -0.3155 0.1962  -0.0299 170 GLU E C   
9086  O O   . GLU E 170 ? 0.7201 0.9057 0.5913 -0.3142 0.2029  -0.0202 170 GLU E O   
9087  C CB  . GLU E 170 ? 0.7085 0.9634 0.6177 -0.3424 0.1918  -0.0358 170 GLU E CB  
9088  C CG  . GLU E 170 ? 0.7176 0.9888 0.6385 -0.3618 0.1845  -0.0428 170 GLU E CG  
9089  C CD  . GLU E 170 ? 0.7354 1.0236 0.6696 -0.3864 0.1885  -0.0352 170 GLU E CD  
9090  O OE1 . GLU E 170 ? 0.7514 1.0249 0.6791 -0.3918 0.1974  -0.0247 170 GLU E OE1 
9091  O OE2 . GLU E 170 ? 0.7343 1.0523 0.6865 -0.4009 0.1825  -0.0388 170 GLU E OE2 
9092  N N   . ASP E 171 ? 0.6895 0.8855 0.5671 -0.2978 0.1908  -0.0357 171 ASP E N   
9093  C CA  . ASP E 171 ? 0.6654 0.8655 0.5429 -0.2766 0.1914  -0.0313 171 ASP E CA  
9094  C C   . ASP E 171 ? 0.6422 0.8839 0.5353 -0.2744 0.1932  -0.0291 171 ASP E C   
9095  O O   . ASP E 171 ? 0.6349 0.9074 0.5428 -0.2836 0.1918  -0.0331 171 ASP E O   
9096  C CB  . ASP E 171 ? 0.6488 0.8463 0.5268 -0.2605 0.1848  -0.0370 171 ASP E CB  
9097  C CG  . ASP E 171 ? 0.6701 0.8271 0.5313 -0.2572 0.1846  -0.0386 171 ASP E CG  
9098  O OD1 . ASP E 171 ? 0.6946 0.8205 0.5426 -0.2617 0.1889  -0.0336 171 ASP E OD1 
9099  O OD2 . ASP E 171 ? 0.6639 0.8202 0.5247 -0.2489 0.1805  -0.0444 171 ASP E OD2 
9100  N N   . LEU E 172 ? 0.6323 0.8745 0.5214 -0.2615 0.1959  -0.0227 172 LEU E N   
9101  C CA  . LEU E 172 ? 0.6158 0.8931 0.5153 -0.2563 0.1985  -0.0211 172 LEU E CA  
9102  C C   . LEU E 172 ? 0.5941 0.8744 0.4932 -0.2344 0.1929  -0.0218 172 LEU E C   
9103  O O   . LEU E 172 ? 0.5987 0.8530 0.4850 -0.2249 0.1914  -0.0174 172 LEU E O   
9104  C CB  . LEU E 172 ? 0.6350 0.9110 0.5266 -0.2642 0.2083  -0.0121 172 LEU E CB  
9105  C CG  . LEU E 172 ? 0.6261 0.9423 0.5284 -0.2610 0.2138  -0.0105 172 LEU E CG  
9106  C CD1 . LEU E 172 ? 0.6275 0.9752 0.5488 -0.2791 0.2170  -0.0118 172 LEU E CD1 
9107  C CD2 . LEU E 172 ? 0.6436 0.9526 0.5305 -0.2583 0.2227  -0.0010 172 LEU E CD2 
9108  N N   . LEU E 173 ? 0.5716 0.8832 0.4854 -0.2270 0.1887  -0.0268 173 LEU E N   
9109  C CA  . LEU E 173 ? 0.5541 0.8695 0.4687 -0.2074 0.1822  -0.0276 173 LEU E CA  
9110  C C   . LEU E 173 ? 0.5590 0.8851 0.4675 -0.2002 0.1871  -0.0244 173 LEU E C   
9111  O O   . LEU E 173 ? 0.5561 0.9134 0.4741 -0.2015 0.1916  -0.0262 173 LEU E O   
9112  C CB  . LEU E 173 ? 0.5328 0.8741 0.4643 -0.2015 0.1750  -0.0339 173 LEU E CB  
9113  C CG  . LEU E 173 ? 0.5183 0.8647 0.4525 -0.1822 0.1672  -0.0347 173 LEU E CG  
9114  C CD1 . LEU E 173 ? 0.5166 0.8330 0.4429 -0.1733 0.1603  -0.0312 173 LEU E CD1 
9115  C CD2 . LEU E 173 ? 0.5011 0.8757 0.4526 -0.1779 0.1612  -0.0400 173 LEU E CD2 
9116  N N   . VAL E 174 ? 0.5675 0.8684 0.4597 -0.1916 0.1858  -0.0197 174 VAL E N   
9117  C CA  . VAL E 174 ? 0.5770 0.8824 0.4573 -0.1824 0.1893  -0.0173 174 VAL E CA  
9118  C C   . VAL E 174 ? 0.5655 0.8690 0.4450 -0.1632 0.1779  -0.0211 174 VAL E C   
9119  O O   . VAL E 174 ? 0.5587 0.8414 0.4378 -0.1575 0.1682  -0.0202 174 VAL E O   
9120  C CB  . VAL E 174 ? 0.6002 0.8766 0.4594 -0.1858 0.1940  -0.0090 174 VAL E CB  
9121  C CG1 . VAL E 174 ? 0.6157 0.9000 0.4598 -0.1779 0.1997  -0.0063 174 VAL E CG1 
9122  C CG2 . VAL E 174 ? 0.6138 0.8822 0.4733 -0.2055 0.2025  -0.0045 174 VAL E CG2 
9123  N N   . LEU E 175 ? 0.5653 0.8906 0.4451 -0.1533 0.1792  -0.0250 175 LEU E N   
9124  C CA  . LEU E 175 ? 0.5609 0.8819 0.4372 -0.1349 0.1678  -0.0294 175 LEU E CA  
9125  C C   . LEU E 175 ? 0.5833 0.8971 0.4366 -0.1246 0.1707  -0.0287 175 LEU E C   
9126  O O   . LEU E 175 ? 0.5963 0.9269 0.4435 -0.1279 0.1836  -0.0271 175 LEU E O   
9127  C CB  . LEU E 175 ? 0.5454 0.8963 0.4398 -0.1284 0.1653  -0.0364 175 LEU E CB  
9128  C CG  . LEU E 175 ? 0.5250 0.8887 0.4410 -0.1374 0.1624  -0.0378 175 LEU E CG  
9129  C CD1 . LEU E 175 ? 0.5140 0.9104 0.4464 -0.1304 0.1610  -0.0436 175 LEU E CD1 
9130  C CD2 . LEU E 175 ? 0.5149 0.8545 0.4330 -0.1345 0.1505  -0.0360 175 LEU E CD2 
9131  N N   . TRP E 176 ? 0.5897 0.8791 0.4301 -0.1123 0.1582  -0.0294 176 TRP E N   
9132  C CA  . TRP E 176 ? 0.6142 0.8944 0.4294 -0.0994 0.1576  -0.0310 176 TRP E CA  
9133  C C   . TRP E 176 ? 0.6155 0.8778 0.4261 -0.0840 0.1391  -0.0363 176 TRP E C   
9134  O O   . TRP E 176 ? 0.5961 0.8547 0.4248 -0.0845 0.1280  -0.0368 176 TRP E O   
9135  C CB  . TRP E 176 ? 0.6353 0.8937 0.4289 -0.1056 0.1629  -0.0226 176 TRP E CB  
9136  C CG  . TRP E 176 ? 0.6329 0.8605 0.4248 -0.1075 0.1507  -0.0173 176 TRP E CG  
9137  C CD1 . TRP E 176 ? 0.6466 0.8487 0.4221 -0.0972 0.1369  -0.0164 176 TRP E CD1 
9138  C CD2 . TRP E 176 ? 0.6180 0.8379 0.4254 -0.1198 0.1510  -0.0119 176 TRP E CD2 
9139  N NE1 . TRP E 176 ? 0.6389 0.8214 0.4221 -0.1026 0.1291  -0.0096 176 TRP E NE1 
9140  C CE2 . TRP E 176 ? 0.6220 0.8143 0.4237 -0.1154 0.1383  -0.0069 176 TRP E CE2 
9141  C CE3 . TRP E 176 ? 0.6042 0.8373 0.4289 -0.1336 0.1602  -0.0110 176 TRP E CE3 
9142  C CZ2 . TRP E 176 ? 0.6121 0.7916 0.4255 -0.1226 0.1365  -0.0009 176 TRP E CZ2 
9143  C CZ3 . TRP E 176 ? 0.5970 0.8135 0.4297 -0.1408 0.1575  -0.0064 176 TRP E CZ3 
9144  C CH2 . TRP E 176 ? 0.6006 0.7914 0.4279 -0.1345 0.1467  -0.0012 176 TRP E CH2 
9145  N N   . GLY E 177 ? 0.6413 0.8919 0.4267 -0.0707 0.1355  -0.0399 177 GLY E N   
9146  C CA  . GLY E 177 ? 0.6488 0.8798 0.4274 -0.0563 0.1164  -0.0459 177 GLY E CA  
9147  C C   . GLY E 177 ? 0.6820 0.8860 0.4273 -0.0466 0.1088  -0.0466 177 GLY E C   
9148  O O   . GLY E 177 ? 0.7022 0.9061 0.4261 -0.0479 0.1207  -0.0433 177 GLY E O   
9149  N N   . ILE E 178 ? 0.6894 0.8700 0.4304 -0.0376 0.0881  -0.0503 178 ILE E N   
9150  C CA  . ILE E 178 ? 0.7246 0.8773 0.4327 -0.0263 0.0760  -0.0537 178 ILE E CA  
9151  C C   . ILE E 178 ? 0.7390 0.8852 0.4402 -0.0096 0.0631  -0.0661 178 ILE E C   
9152  O O   . ILE E 178 ? 0.7182 0.8703 0.4444 -0.0095 0.0551  -0.0682 178 ILE E O   
9153  C CB  . ILE E 178 ? 0.7253 0.8501 0.4344 -0.0327 0.0589  -0.0452 178 ILE E CB  
9154  C CG1 . ILE E 178 ? 0.7655 0.8632 0.4362 -0.0237 0.0493  -0.0469 178 ILE E CG1 
9155  C CG2 . ILE E 178 ? 0.7061 0.8240 0.4414 -0.0333 0.0400  -0.0452 178 ILE E CG2 
9156  C CD1 . ILE E 178 ? 0.7754 0.8432 0.4447 -0.0224 0.0227  -0.0446 178 ILE E CD1 
9157  N N   . HIS E 179 ? 0.7774 0.9103 0.4430 0.0052  0.0612  -0.0742 179 HIS E N   
9158  C CA  . HIS E 179 ? 0.7996 0.9193 0.4526 0.0231  0.0474  -0.0874 179 HIS E CA  
9159  C C   . HIS E 179 ? 0.8269 0.9053 0.4604 0.0278  0.0203  -0.0899 179 HIS E C   
9160  O O   . HIS E 179 ? 0.8506 0.9108 0.4580 0.0270  0.0169  -0.0867 179 HIS E O   
9161  C CB  . HIS E 179 ? 0.8291 0.9613 0.4535 0.0399  0.0628  -0.0970 179 HIS E CB  
9162  C CG  . HIS E 179 ? 0.8600 0.9728 0.4647 0.0612  0.0483  -0.1120 179 HIS E CG  
9163  N ND1 . HIS E 179 ? 0.9088 0.9972 0.4683 0.0779  0.0429  -0.1214 179 HIS E ND1 
9164  C CD2 . HIS E 179 ? 0.8525 0.9638 0.4747 0.0688  0.0370  -0.1192 179 HIS E CD2 
9165  C CE1 . HIS E 179 ? 0.9311 1.0025 0.4805 0.0954  0.0290  -0.1349 179 HIS E CE1 
9166  N NE2 . HIS E 179 ? 0.8974 0.9821 0.4852 0.0901  0.0251  -0.1334 179 HIS E NE2 
9167  N N   . HIS E 180 ? 0.8255 0.8895 0.4723 0.0321  0.0004  -0.0950 180 HIS E N   
9168  C CA  . HIS E 180 ? 0.8535 0.8781 0.4852 0.0360  -0.0282 -0.0981 180 HIS E CA  
9169  C C   . HIS E 180 ? 0.8960 0.9011 0.4960 0.0577  -0.0372 -0.1153 180 HIS E C   
9170  O O   . HIS E 180 ? 0.8901 0.9009 0.5042 0.0654  -0.0393 -0.1220 180 HIS E O   
9171  C CB  . HIS E 180 ? 0.8251 0.8452 0.4952 0.0244  -0.0455 -0.0900 180 HIS E CB  
9172  C CG  . HIS E 180 ? 0.7865 0.8247 0.4870 0.0057  -0.0367 -0.0741 180 HIS E CG  
9173  N ND1 . HIS E 180 ? 0.7846 0.8065 0.4933 -0.0045 -0.0520 -0.0633 180 HIS E ND1 
9174  C CD2 . HIS E 180 ? 0.7512 0.8216 0.4753 -0.0037 -0.0148 -0.0674 180 HIS E CD2 
9175  C CE1 . HIS E 180 ? 0.7502 0.7928 0.4851 -0.0179 -0.0387 -0.0510 180 HIS E CE1 
9176  N NE2 . HIS E 180 ? 0.7305 0.8010 0.4739 -0.0181 -0.0166 -0.0538 180 HIS E NE2 
9177  N N   . PRO E 181 ? 0.9418 0.9228 0.4971 0.0687  -0.0426 -0.1227 181 PRO E N   
9178  C CA  . PRO E 181 ? 0.9891 0.9488 0.5078 0.0917  -0.0500 -0.1405 181 PRO E CA  
9179  C C   . PRO E 181 ? 1.0139 0.9318 0.5287 0.0953  -0.0844 -0.1476 181 PRO E C   
9180  O O   . PRO E 181 ? 1.0002 0.9041 0.5351 0.0795  -0.1035 -0.1375 181 PRO E O   
9181  C CB  . PRO E 181 ? 1.0288 0.9786 0.5001 0.0999  -0.0426 -0.1435 181 PRO E CB  
9182  C CG  . PRO E 181 ? 1.0141 0.9570 0.4944 0.0806  -0.0501 -0.1286 181 PRO E CG  
9183  C CD  . PRO E 181 ? 0.9552 0.9260 0.4896 0.0613  -0.0425 -0.1147 181 PRO E CD  
9184  N N   . ASN E 182 ? 1.0525 0.9509 0.5419 0.1162  -0.0921 -0.1645 182 ASN E N   
9185  C CA  . ASN E 182 ? 1.0825 0.9376 0.5661 0.1207  -0.1255 -0.1729 182 ASN E CA  
9186  C C   . ASN E 182 ? 1.1259 0.9383 0.5757 0.1191  -0.1520 -0.1757 182 ASN E C   
9187  O O   . ASN E 182 ? 1.1258 0.9135 0.5927 0.1067  -0.1800 -0.1703 182 ASN E O   
9188  C CB  . ASN E 182 ? 1.1175 0.9608 0.5790 0.1460  -0.1254 -0.1915 182 ASN E CB  
9189  C CG  . ASN E 182 ? 1.0765 0.9539 0.5789 0.1461  -0.1104 -0.1880 182 ASN E CG  
9190  O OD1 . ASN E 182 ? 1.0536 0.9258 0.5908 0.1352  -0.1256 -0.1813 182 ASN E OD1 
9191  N ND2 . ASN E 182 ? 1.0680 0.9821 0.5672 0.1578  -0.0807 -0.1913 182 ASN E ND2 
9192  N N   . ASP E 183 ? 1.1644 0.9695 0.5668 0.1314  -0.1433 -0.1833 183 ASP E N   
9193  C CA  . ASP E 183 ? 1.2128 0.9768 0.5756 0.1323  -0.1682 -0.1876 183 ASP E CA  
9194  C C   . ASP E 183 ? 1.2273 1.0033 0.5561 0.1350  -0.1491 -0.1840 183 ASP E C   
9195  O O   . ASP E 183 ? 1.2040 1.0185 0.5377 0.1373  -0.1162 -0.1795 183 ASP E O   
9196  C CB  . ASP E 183 ? 1.2774 0.9945 0.5978 0.1537  -0.1917 -0.2095 183 ASP E CB  
9197  C CG  . ASP E 183 ? 1.3024 1.0303 0.5931 0.1807  -0.1683 -0.2256 183 ASP E CG  
9198  O OD1 . ASP E 183 ? 1.3009 1.0579 0.5735 0.1875  -0.1390 -0.2237 183 ASP E OD1 
9199  O OD2 . ASP E 183 ? 1.3254 1.0328 0.6116 0.1954  -0.1793 -0.2394 183 ASP E OD2 
9200  N N   . ALA E 184 ? 1.2677 1.0104 0.5626 0.1339  -0.1709 -0.1852 184 ALA E N   
9201  C CA  . ALA E 184 ? 1.2880 1.0363 0.5469 0.1360  -0.1569 -0.1806 184 ALA E CA  
9202  C C   . ALA E 184 ? 1.3253 1.0820 0.5377 0.1605  -0.1318 -0.1939 184 ALA E C   
9203  O O   . ALA E 184 ? 1.3217 1.1034 0.5205 0.1605  -0.1061 -0.1858 184 ALA E O   
9204  C CB  . ALA E 184 ? 1.3313 1.0379 0.5594 0.1326  -0.1898 -0.1814 184 ALA E CB  
9205  N N   . ALA E 185 ? 1.3631 1.0988 0.5518 0.1817  -0.1393 -0.2136 185 ALA E N   
9206  C CA  . ALA E 185 ? 1.4009 1.1460 0.5472 0.2082  -0.1152 -0.2273 185 ALA E CA  
9207  C C   . ALA E 185 ? 1.3511 1.1532 0.5336 0.2069  -0.0766 -0.2185 185 ALA E C   
9208  O O   . ALA E 185 ? 1.3641 1.1919 0.5227 0.2182  -0.0478 -0.2180 185 ALA E O   
9209  C CB  . ALA E 185 ? 1.4541 1.1597 0.5688 0.2320  -0.1347 -0.2509 185 ALA E CB  
9210  N N   . GLU E 186 ? 1.2965 1.1189 0.5364 0.1927  -0.0766 -0.2111 186 GLU E N   
9211  C CA  . GLU E 186 ? 1.2472 1.1232 0.5259 0.1886  -0.0437 -0.2022 186 GLU E CA  
9212  C C   . GLU E 186 ? 1.2086 1.1177 0.5070 0.1675  -0.0230 -0.1820 186 GLU E C   
9213  O O   . GLU E 186 ? 1.1916 1.1415 0.4973 0.1688  0.0082  -0.1762 186 GLU E O   
9214  C CB  . GLU E 186 ? 1.2043 1.0890 0.5352 0.1800  -0.0522 -0.2004 186 GLU E CB  
9215  C CG  . GLU E 186 ? 1.1585 1.0969 0.5275 0.1777  -0.0212 -0.1935 186 GLU E CG  
9216  C CD  . GLU E 186 ? 1.1358 1.0780 0.5410 0.1799  -0.0296 -0.1976 186 GLU E CD  
9217  O OE1 . GLU E 186 ? 1.0977 1.0374 0.5421 0.1600  -0.0439 -0.1876 186 GLU E OE1 
9218  O OE2 . GLU E 186 ? 1.1559 1.1048 0.5505 0.2021  -0.0212 -0.2101 186 GLU E OE2 
9219  N N   . GLN E 187 ? 1.1966 1.0880 0.5047 0.1483  -0.0411 -0.1709 187 GLN E N   
9220  C CA  . GLN E 187 ? 1.1686 1.0827 0.4898 0.1296  -0.0250 -0.1522 187 GLN E CA  
9221  C C   . GLN E 187 ? 1.2067 1.1289 0.4816 0.1414  -0.0035 -0.1524 187 GLN E C   
9222  O O   . GLN E 187 ? 1.1832 1.1425 0.4712 0.1343  0.0255  -0.1410 187 GLN E O   
9223  C CB  . GLN E 187 ? 1.1632 1.0502 0.4930 0.1125  -0.0516 -0.1425 187 GLN E CB  
9224  C CG  . GLN E 187 ? 1.1479 1.0483 0.4804 0.0969  -0.0390 -0.1245 187 GLN E CG  
9225  C CD  . GLN E 187 ? 1.0926 1.0365 0.4691 0.0819  -0.0111 -0.1112 187 GLN E CD  
9226  O OE1 . GLN E 187 ? 1.0497 1.0077 0.4710 0.0723  -0.0128 -0.1086 187 GLN E OE1 
9227  N NE2 . GLN E 187 ? 1.0959 1.0602 0.4586 0.0794  0.0140  -0.1023 187 GLN E NE2 
9228  N N   . THR E 188 ? 1.2684 1.1549 0.4883 0.1592  -0.0183 -0.1651 188 THR E N   
9229  C CA  . THR E 188 ? 1.3130 1.2036 0.4821 0.1731  0.0005  -0.1659 188 THR E CA  
9230  C C   . THR E 188 ? 1.3187 1.2440 0.4824 0.1912  0.0314  -0.1728 188 THR E C   
9231  O O   . THR E 188 ? 1.3214 1.2772 0.4746 0.1919  0.0604  -0.1633 188 THR E O   
9232  C CB  . THR E 188 ? 1.3832 1.2242 0.4905 0.1897  -0.0250 -0.1798 188 THR E CB  
9233  O OG1 . THR E 188 ? 1.4107 1.2254 0.5060 0.2077  -0.0434 -0.2006 188 THR E OG1 
9234  C CG2 . THR E 188 ? 1.3814 1.1929 0.4922 0.1715  -0.0540 -0.1703 188 THR E CG2 
9235  N N   . LYS E 189 ? 1.3218 1.2432 0.4939 0.2057  0.0250  -0.1880 189 LYS E N   
9236  C CA  . LYS E 189 ? 1.3268 1.2828 0.4981 0.2248  0.0527  -0.1948 189 LYS E CA  
9237  C C   . LYS E 189 ? 1.2706 1.2838 0.4901 0.2077  0.0841  -0.1771 189 LYS E C   
9238  O O   . LYS E 189 ? 1.2803 1.3287 0.4898 0.2175  0.1138  -0.1742 189 LYS E O   
9239  C CB  . LYS E 189 ? 1.3319 1.2730 0.5135 0.2404  0.0376  -0.2121 189 LYS E CB  
9240  C CG  . LYS E 189 ? 1.3284 1.3100 0.5199 0.2591  0.0654  -0.2176 189 LYS E CG  
9241  C CD  . LYS E 189 ? 1.3595 1.3139 0.5387 0.2836  0.0487  -0.2387 189 LYS E CD  
9242  C CE  . LYS E 189 ? 1.3548 1.3524 0.5474 0.3035  0.0764  -0.2431 189 LYS E CE  
9243  N NZ  . LYS E 189 ? 1.2931 1.3202 0.5500 0.2891  0.0779  -0.2357 189 LYS E NZ  
9244  N N   . LEU E 190 ? 1.2149 1.2369 0.4858 0.1821  0.0769  -0.1653 190 LEU E N   
9245  C CA  . LEU E 190 ? 1.1617 1.2332 0.4804 0.1639  0.1022  -0.1499 190 LEU E CA  
9246  C C   . LEU E 190 ? 1.1533 1.2377 0.4687 0.1459  0.1176  -0.1316 190 LEU E C   
9247  O O   . LEU E 190 ? 1.1442 1.2681 0.4676 0.1426  0.1466  -0.1222 190 LEU E O   
9248  C CB  . LEU E 190 ? 1.1093 1.1831 0.4820 0.1458  0.0878  -0.1460 190 LEU E CB  
9249  C CG  . LEU E 190 ? 1.1004 1.1839 0.4949 0.1589  0.0847  -0.1579 190 LEU E CG  
9250  C CD1 . LEU E 190 ? 1.0742 1.1336 0.4992 0.1477  0.0568  -0.1588 190 LEU E CD1 
9251  C CD2 . LEU E 190 ? 1.0655 1.2043 0.4961 0.1543  0.1137  -0.1505 190 LEU E CD2 
9252  N N   . TYR E 191 ? 1.1564 1.2078 0.4622 0.1337  0.0974  -0.1258 191 TYR E N   
9253  C CA  . TYR E 191 ? 1.1450 1.2032 0.4528 0.1144  0.1079  -0.1072 191 TYR E CA  
9254  C C   . TYR E 191 ? 1.1964 1.2221 0.4500 0.1216  0.0986  -0.1062 191 TYR E C   
9255  O O   . TYR E 191 ? 1.1971 1.2275 0.4446 0.1091  0.1092  -0.0906 191 TYR E O   
9256  C CB  . TYR E 191 ? 1.0948 1.1493 0.4493 0.0901  0.0945  -0.0969 191 TYR E CB  
9257  C CG  . TYR E 191 ? 1.0504 1.1244 0.4525 0.0858  0.0934  -0.1013 191 TYR E CG  
9258  C CD1 . TYR E 191 ? 1.0160 1.1336 0.4516 0.0775  0.1183  -0.0950 191 TYR E CD1 
9259  C CD2 . TYR E 191 ? 1.0454 1.0944 0.4584 0.0897  0.0666  -0.1113 191 TYR E CD2 
9260  C CE1 . TYR E 191 ? 0.9778 1.1134 0.4548 0.0740  0.1164  -0.0988 191 TYR E CE1 
9261  C CE2 . TYR E 191 ? 1.0074 1.0740 0.4621 0.0863  0.0656  -0.1142 191 TYR E CE2 
9262  C CZ  . TYR E 191 ? 0.9738 1.0837 0.4593 0.0790  0.0906  -0.1082 191 TYR E CZ  
9263  O OH  . TYR E 191 ? 0.9383 1.0658 0.4632 0.0760  0.0889  -0.1107 191 TYR E OH  
9264  N N   . GLN E 192 ? 1.2414 1.2320 0.4550 0.1414  0.0777  -0.1228 192 GLN E N   
9265  C CA  . GLN E 192 ? 1.2981 1.2545 0.4539 0.1515  0.0657  -0.1250 192 GLN E CA  
9266  C C   . GLN E 192 ? 1.2915 1.2184 0.4516 0.1343  0.0406  -0.1150 192 GLN E C   
9267  O O   . GLN E 192 ? 1.3283 1.2151 0.4578 0.1421  0.0117  -0.1243 192 GLN E O   
9268  C CB  . GLN E 192 ? 1.3281 1.3070 0.4496 0.1588  0.0960  -0.1167 192 GLN E CB  
9269  C CG  . GLN E 192 ? 1.4016 1.3489 0.4522 0.1823  0.0875  -0.1282 192 GLN E CG  
9270  C CD  . GLN E 192 ? 1.4339 1.4084 0.4503 0.1935  0.1207  -0.1212 192 GLN E CD  
9271  O OE1 . GLN E 192 ? 1.4729 1.4529 0.4561 0.2186  0.1321  -0.1346 192 GLN E OE1 
9272  N NE2 . GLN E 192 ? 1.4199 1.4119 0.4447 0.1753  0.1371  -0.0995 192 GLN E NE2 
9273  N N   . ASN E 193 ? 1.2473 1.1937 0.4450 0.1116  0.0508  -0.0961 193 ASN E N   
9274  C CA  . ASN E 193 ? 1.2385 1.1617 0.4447 0.0958  0.0298  -0.0845 193 ASN E CA  
9275  C C   . ASN E 193 ? 1.2193 1.1201 0.4528 0.0918  -0.0019 -0.0923 193 ASN E C   
9276  O O   . ASN E 193 ? 1.1762 1.0947 0.4537 0.0856  0.0007  -0.0944 193 ASN E O   
9277  C CB  . ASN E 193 ? 1.1943 1.1435 0.4388 0.0736  0.0490  -0.0639 193 ASN E CB  
9278  C CG  . ASN E 193 ? 1.2070 1.1837 0.4341 0.0745  0.0826  -0.0547 193 ASN E CG  
9279  O OD1 . ASN E 193 ? 1.2395 1.2255 0.4348 0.0919  0.0962  -0.0638 193 ASN E OD1 
9280  N ND2 . ASN E 193 ? 1.1836 1.1733 0.4317 0.0559  0.0963  -0.0361 193 ASN E ND2 
9281  N N   . PRO E 194 ? 1.2529 1.1153 0.4602 0.0950  -0.0326 -0.0958 194 PRO E N   
9282  C CA  . PRO E 194 ? 1.2423 1.0821 0.4728 0.0917  -0.0645 -0.1032 194 PRO E CA  
9283  C C   . PRO E 194 ? 1.1821 1.0369 0.4735 0.0696  -0.0680 -0.0882 194 PRO E C   
9284  O O   . PRO E 194 ? 1.1514 1.0106 0.4799 0.0654  -0.0765 -0.0923 194 PRO E O   
9285  C CB  . PRO E 194 ? 1.2967 1.0949 0.4827 0.0980  -0.0948 -0.1072 194 PRO E CB  
9286  C CG  . PRO E 194 ? 1.3147 1.1181 0.4731 0.0957  -0.0798 -0.0936 194 PRO E CG  
9287  C CD  . PRO E 194 ? 1.3008 1.1405 0.4596 0.0992  -0.0401 -0.0906 194 PRO E CD  
9288  N N   . THR E 195 ? 1.1682 1.0301 0.4679 0.0567  -0.0609 -0.0706 195 THR E N   
9289  C CA  . THR E 195 ? 1.1164 0.9916 0.4692 0.0376  -0.0623 -0.0556 195 THR E CA  
9290  C C   . THR E 195 ? 1.0825 0.9917 0.4559 0.0287  -0.0280 -0.0452 195 THR E C   
9291  O O   . THR E 195 ? 1.1021 1.0154 0.4491 0.0293  -0.0111 -0.0378 195 THR E O   
9292  C CB  . THR E 195 ? 1.1295 0.9839 0.4778 0.0301  -0.0833 -0.0429 195 THR E CB  
9293  O OG1 . THR E 195 ? 1.1754 0.9960 0.4905 0.0400  -0.1143 -0.0534 195 THR E OG1 
9294  C CG2 . THR E 195 ? 1.0807 0.9453 0.4853 0.0138  -0.0909 -0.0301 195 THR E CG2 
9295  N N   . THR E 196 ? 1.0343 0.9670 0.4537 0.0200  -0.0184 -0.0444 196 THR E N   
9296  C CA  . THR E 196 ? 1.0031 0.9678 0.4437 0.0109  0.0122  -0.0367 196 THR E CA  
9297  C C   . THR E 196 ? 0.9532 0.9306 0.4447 -0.0056 0.0129  -0.0261 196 THR E C   
9298  O O   . THR E 196 ? 0.9377 0.9052 0.4531 -0.0087 -0.0079 -0.0261 196 THR E O   
9299  C CB  . THR E 196 ? 0.9987 0.9866 0.4394 0.0198  0.0299  -0.0489 196 THR E CB  
9300  O OG1 . THR E 196 ? 0.9800 0.9662 0.4453 0.0229  0.0146  -0.0590 196 THR E OG1 
9301  C CG2 . THR E 196 ? 1.0499 1.0296 0.4383 0.0380  0.0349  -0.0585 196 THR E CG2 
9302  N N   . TYR E 197 ? 0.9310 0.9302 0.4382 -0.0163 0.0372  -0.0168 197 TYR E N   
9303  C CA  . TYR E 197 ? 0.8882 0.8989 0.4388 -0.0311 0.0410  -0.0073 197 TYR E CA  
9304  C C   . TYR E 197 ? 0.8646 0.9045 0.4326 -0.0395 0.0683  -0.0056 197 TYR E C   
9305  O O   . TYR E 197 ? 0.8820 0.9343 0.4289 -0.0357 0.0856  -0.0083 197 TYR E O   
9306  C CB  . TYR E 197 ? 0.8942 0.8884 0.4436 -0.0384 0.0353  0.0075  197 TYR E CB  
9307  C CG  . TYR E 197 ? 0.9168 0.9112 0.4400 -0.0414 0.0543  0.0163  197 TYR E CG  
9308  C CD1 . TYR E 197 ? 0.9619 0.9400 0.4400 -0.0317 0.0506  0.0160  197 TYR E CD1 
9309  C CD2 . TYR E 197 ? 0.8964 0.9059 0.4386 -0.0542 0.0756  0.0251  197 TYR E CD2 
9310  C CE1 . TYR E 197 ? 0.9848 0.9635 0.4385 -0.0347 0.0686  0.0260  197 TYR E CE1 
9311  C CE2 . TYR E 197 ? 0.9196 0.9278 0.4389 -0.0583 0.0926  0.0346  197 TYR E CE2 
9312  C CZ  . TYR E 197 ? 0.9631 0.9570 0.4388 -0.0486 0.0896  0.0358  197 TYR E CZ  
9313  O OH  . TYR E 197 ? 0.9880 0.9810 0.4405 -0.0530 0.1069  0.0471  197 TYR E OH  
9314  N N   . ILE E 198 ? 0.8269 0.8782 0.4332 -0.0511 0.0717  -0.0008 198 ILE E N   
9315  C CA  . ILE E 198 ? 0.8052 0.8804 0.4301 -0.0625 0.0948  0.0025  198 ILE E CA  
9316  C C   . ILE E 198 ? 0.7848 0.8542 0.4335 -0.0750 0.0953  0.0138  198 ILE E C   
9317  O O   . ILE E 198 ? 0.7605 0.8289 0.4359 -0.0766 0.0840  0.0138  198 ILE E O   
9318  C CB  . ILE E 198 ? 0.7783 0.8788 0.4277 -0.0617 0.0997  -0.0075 198 ILE E CB  
9319  C CG1 . ILE E 198 ? 0.7987 0.9008 0.4271 -0.0456 0.0945  -0.0202 198 ILE E CG1 
9320  C CG2 . ILE E 198 ? 0.7634 0.8896 0.4270 -0.0735 0.1232  -0.0044 198 ILE E CG2 
9321  C CD1 . ILE E 198 ? 0.7769 0.9052 0.4266 -0.0428 0.1009  -0.0296 198 ILE E CD1 
9322  N N   . SER E 199 ? 0.7972 0.8620 0.4355 -0.0832 0.1088  0.0239  199 SER E N   
9323  C CA  . SER E 199 ? 0.7832 0.8401 0.4408 -0.0939 0.1112  0.0340  199 SER E CA  
9324  C C   . SER E 199 ? 0.7662 0.8420 0.4410 -0.1067 0.1311  0.0341  199 SER E C   
9325  O O   . SER E 199 ? 0.7799 0.8666 0.4415 -0.1111 0.1467  0.0349  199 SER E O   
9326  C CB  . SER E 199 ? 0.8126 0.8453 0.4470 -0.0941 0.1093  0.0463  199 SER E CB  
9327  O OG  . SER E 199 ? 0.8403 0.8749 0.4465 -0.0956 0.1241  0.0494  199 SER E OG  
9328  N N   . VAL E 200 ? 0.7382 0.8184 0.4425 -0.1126 0.1299  0.0336  200 VAL E N   
9329  C CA  . VAL E 200 ? 0.7229 0.8185 0.4444 -0.1253 0.1454  0.0326  200 VAL E CA  
9330  C C   . VAL E 200 ? 0.7203 0.7982 0.4522 -0.1327 0.1465  0.0408  200 VAL E C   
9331  O O   . VAL E 200 ? 0.7090 0.7774 0.4537 -0.1273 0.1347  0.0428  200 VAL E O   
9332  C CB  . VAL E 200 ? 0.6930 0.8126 0.4391 -0.1245 0.1437  0.0220  200 VAL E CB  
9333  C CG1 . VAL E 200 ? 0.6841 0.8237 0.4421 -0.1375 0.1599  0.0198  200 VAL E CG1 
9334  C CG2 . VAL E 200 ? 0.6960 0.8262 0.4331 -0.1122 0.1364  0.0134  200 VAL E CG2 
9335  N N   . GLY E 201 ? 0.7329 0.8064 0.4597 -0.1447 0.1607  0.0460  201 GLY E N   
9336  C CA  . GLY E 201 ? 0.7377 0.7899 0.4698 -0.1508 0.1628  0.0532  201 GLY E CA  
9337  C C   . GLY E 201 ? 0.7322 0.7916 0.4762 -0.1654 0.1755  0.0503  201 GLY E C   
9338  O O   . GLY E 201 ? 0.7365 0.8127 0.4779 -0.1745 0.1861  0.0481  201 GLY E O   
9339  N N   . THR E 202 ? 0.7239 0.7715 0.4815 -0.1672 0.1741  0.0501  202 THR E N   
9340  C CA  . THR E 202 ? 0.7282 0.7716 0.4916 -0.1812 0.1842  0.0482  202 THR E CA  
9341  C C   . THR E 202 ? 0.7440 0.7547 0.5036 -0.1789 0.1827  0.0552  202 THR E C   
9342  O O   . THR E 202 ? 0.7547 0.7489 0.5055 -0.1687 0.1760  0.0634  202 THR E O   
9343  C CB  . THR E 202 ? 0.7006 0.7674 0.4854 -0.1841 0.1839  0.0368  202 THR E CB  
9344  O OG1 . THR E 202 ? 0.6852 0.7459 0.4823 -0.1739 0.1758  0.0354  202 THR E OG1 
9345  C CG2 . THR E 202 ? 0.6825 0.7815 0.4734 -0.1809 0.1824  0.0302  202 THR E CG2 
9346  N N   . SER E 203 ? 0.7482 0.7486 0.5136 -0.1875 0.1882  0.0517  203 SER E N   
9347  C CA  . SER E 203 ? 0.7626 0.7327 0.5257 -0.1821 0.1869  0.0562  203 SER E CA  
9348  C C   . SER E 203 ? 0.7402 0.7169 0.5179 -0.1653 0.1773  0.0557  203 SER E C   
9349  O O   . SER E 203 ? 0.7509 0.7080 0.5266 -0.1549 0.1733  0.0636  203 SER E O   
9350  C CB  . SER E 203 ? 0.7737 0.7313 0.5383 -0.1937 0.1938  0.0499  203 SER E CB  
9351  O OG  . SER E 203 ? 0.7480 0.7319 0.5283 -0.1964 0.1933  0.0383  203 SER E OG  
9352  N N   . THR E 204 ? 0.7102 0.7156 0.5037 -0.1629 0.1735  0.0475  204 THR E N   
9353  C CA  . THR E 204 ? 0.6882 0.7035 0.4984 -0.1492 0.1645  0.0479  204 THR E CA  
9354  C C   . THR E 204 ? 0.6742 0.7057 0.4879 -0.1415 0.1537  0.0501  204 THR E C   
9355  O O   . THR E 204 ? 0.6706 0.6986 0.4911 -0.1303 0.1441  0.0569  204 THR E O   
9356  C CB  . THR E 204 ? 0.6670 0.7003 0.4928 -0.1509 0.1666  0.0382  204 THR E CB  
9357  O OG1 . THR E 204 ? 0.6522 0.7107 0.4814 -0.1589 0.1674  0.0302  204 THR E OG1 
9358  C CG2 . THR E 204 ? 0.6849 0.6989 0.5047 -0.1574 0.1754  0.0345  204 THR E CG2 
9359  N N   . LEU E 205 ? 0.6688 0.7179 0.4780 -0.1471 0.1549  0.0442  205 LEU E N   
9360  C CA  . LEU E 205 ? 0.6580 0.7212 0.4688 -0.1391 0.1441  0.0434  205 LEU E CA  
9361  C C   . LEU E 205 ? 0.6799 0.7259 0.4728 -0.1332 0.1375  0.0521  205 LEU E C   
9362  O O   . LEU E 205 ? 0.7038 0.7359 0.4775 -0.1387 0.1449  0.0566  205 LEU E O   
9363  C CB  . LEU E 205 ? 0.6493 0.7359 0.4590 -0.1446 0.1484  0.0341  205 LEU E CB  
9364  C CG  . LEU E 205 ? 0.6362 0.7386 0.4499 -0.1353 0.1372  0.0298  205 LEU E CG  
9365  C CD1 . LEU E 205 ? 0.6140 0.7224 0.4495 -0.1280 0.1264  0.0297  205 LEU E CD1 
9366  C CD2 . LEU E 205 ? 0.6298 0.7559 0.4432 -0.1396 0.1437  0.0207  205 LEU E CD2 
9367  N N   . ASN E 206 ? 0.6735 0.7204 0.4729 -0.1225 0.1228  0.0552  206 ASN E N   
9368  C CA  . ASN E 206 ? 0.6943 0.7268 0.4766 -0.1159 0.1127  0.0624  206 ASN E CA  
9369  C C   . ASN E 206 ? 0.6852 0.7289 0.4709 -0.1085 0.0974  0.0578  206 ASN E C   
9370  O O   . ASN E 206 ? 0.6786 0.7204 0.4777 -0.1016 0.0828  0.0626  206 ASN E O   
9371  C CB  . ASN E 206 ? 0.7039 0.7178 0.4911 -0.1103 0.1070  0.0742  206 ASN E CB  
9372  C CG  . ASN E 206 ? 0.7286 0.7267 0.4965 -0.1042 0.0958  0.0825  206 ASN E CG  
9373  O OD1 . ASN E 206 ? 0.7459 0.7414 0.4898 -0.1057 0.0969  0.0802  206 ASN E OD1 
9374  N ND2 . ASN E 206 ? 0.7320 0.7207 0.5101 -0.0966 0.0851  0.0928  206 ASN E ND2 
9375  N N   . GLN E 207 ? 0.6876 0.7427 0.4613 -0.1098 0.1008  0.0489  207 GLN E N   
9376  C CA  . GLN E 207 ? 0.6810 0.7458 0.4567 -0.1027 0.0878  0.0417  207 GLN E CA  
9377  C C   . GLN E 207 ? 0.7095 0.7633 0.4551 -0.0965 0.0810  0.0407  207 GLN E C   
9378  O O   . GLN E 207 ? 0.7305 0.7791 0.4532 -0.0995 0.0923  0.0426  207 GLN E O   
9379  C CB  . GLN E 207 ? 0.6620 0.7500 0.4482 -0.1063 0.0967  0.0309  207 GLN E CB  
9380  C CG  . GLN E 207 ? 0.6578 0.7551 0.4441 -0.0983 0.0852  0.0221  207 GLN E CG  
9381  C CD  . GLN E 207 ? 0.6377 0.7591 0.4381 -0.1011 0.0938  0.0129  207 GLN E CD  
9382  O OE1 . GLN E 207 ? 0.6451 0.7777 0.4333 -0.0994 0.1005  0.0056  207 GLN E OE1 
9383  N NE2 . GLN E 207 ? 0.6134 0.7442 0.4394 -0.1048 0.0939  0.0139  207 GLN E NE2 
9384  N N   . ARG E 208 ? 0.7129 0.7621 0.4577 -0.0882 0.0621  0.0382  208 ARG E N   
9385  C CA  . ARG E 208 ? 0.7421 0.7808 0.4559 -0.0804 0.0536  0.0339  208 ARG E CA  
9386  C C   . ARG E 208 ? 0.7376 0.7792 0.4568 -0.0730 0.0369  0.0244  208 ARG E C   
9387  O O   . ARG E 208 ? 0.7318 0.7664 0.4670 -0.0710 0.0183  0.0282  208 ARG E O   
9388  C CB  . ARG E 208 ? 0.7684 0.7843 0.4646 -0.0773 0.0424  0.0442  208 ARG E CB  
9389  C CG  . ARG E 208 ? 0.8056 0.8098 0.4607 -0.0709 0.0412  0.0409  208 ARG E CG  
9390  C CD  . ARG E 208 ? 0.8326 0.8138 0.4708 -0.0655 0.0219  0.0489  208 ARG E CD  
9391  N NE  . ARG E 208 ? 0.8722 0.8414 0.4667 -0.0590 0.0223  0.0463  208 ARG E NE  
9392  C CZ  . ARG E 208 ? 0.8930 0.8584 0.4639 -0.0616 0.0387  0.0529  208 ARG E CZ  
9393  N NH1 . ARG E 208 ? 0.8792 0.8491 0.4659 -0.0714 0.0553  0.0620  208 ARG E NH1 
9394  N NH2 . ARG E 208 ? 0.9310 0.8866 0.4607 -0.0543 0.0385  0.0507  208 ARG E NH2 
9395  N N   . LEU E 209 ? 0.7420 0.7941 0.4490 -0.0688 0.0435  0.0129  209 LEU E N   
9396  C CA  . LEU E 209 ? 0.7399 0.7936 0.4510 -0.0610 0.0293  0.0026  209 LEU E CA  
9397  C C   . LEU E 209 ? 0.7782 0.8130 0.4530 -0.0498 0.0168  -0.0040 209 LEU E C   
9398  O O   . LEU E 209 ? 0.8026 0.8348 0.4472 -0.0467 0.0280  -0.0050 209 LEU E O   
9399  C CB  . LEU E 209 ? 0.7218 0.7998 0.4436 -0.0613 0.0442  -0.0065 209 LEU E CB  
9400  C CG  . LEU E 209 ? 0.6881 0.7860 0.4408 -0.0723 0.0580  -0.0021 209 LEU E CG  
9401  C CD1 . LEU E 209 ? 0.6762 0.7988 0.4349 -0.0721 0.0718  -0.0113 209 LEU E CD1 
9402  C CD2 . LEU E 209 ? 0.6656 0.7618 0.4483 -0.0747 0.0444  0.0033  209 LEU E CD2 
9403  N N   . VAL E 210 ? 0.7861 0.8069 0.4631 -0.0438 -0.0066 -0.0082 210 VAL E N   
9404  C CA  . VAL E 210 ? 0.8262 0.8259 0.4671 -0.0319 -0.0215 -0.0177 210 VAL E CA  
9405  C C   . VAL E 210 ? 0.8255 0.8252 0.4723 -0.0242 -0.0321 -0.0305 210 VAL E C   
9406  O O   . VAL E 210 ? 0.7987 0.8045 0.4795 -0.0293 -0.0405 -0.0278 210 VAL E O   
9407  C CB  . VAL E 210 ? 0.8492 0.8229 0.4798 -0.0318 -0.0456 -0.0105 210 VAL E CB  
9408  C CG1 . VAL E 210 ? 0.8498 0.8233 0.4771 -0.0386 -0.0354 0.0032  210 VAL E CG1 
9409  C CG2 . VAL E 210 ? 0.8307 0.8006 0.4961 -0.0367 -0.0678 -0.0057 210 VAL E CG2 
9410  N N   . PRO E 211 ? 0.8570 0.8497 0.4701 -0.0109 -0.0308 -0.0439 211 PRO E N   
9411  C CA  . PRO E 211 ? 0.8615 0.8504 0.4776 -0.0015 -0.0418 -0.0567 211 PRO E CA  
9412  C C   . PRO E 211 ? 0.8764 0.8370 0.4965 -0.0010 -0.0743 -0.0574 211 PRO E C   
9413  O O   . PRO E 211 ? 0.9100 0.8450 0.5038 0.0019  -0.0914 -0.0574 211 PRO E O   
9414  C CB  . PRO E 211 ? 0.8995 0.8841 0.4725 0.0145  -0.0328 -0.0702 211 PRO E CB  
9415  C CG  . PRO E 211 ? 0.9009 0.9005 0.4596 0.0104  -0.0090 -0.0627 211 PRO E CG  
9416  C CD  . PRO E 211 ? 0.8884 0.8802 0.4609 -0.0032 -0.0159 -0.0475 211 PRO E CD  
9417  N N   . ARG E 212 ? 0.8529 0.8186 0.5063 -0.0046 -0.0833 -0.0570 212 ARG E N   
9418  C CA  . ARG E 212 ? 0.8671 0.8077 0.5286 -0.0051 -0.1143 -0.0575 212 ARG E CA  
9419  C C   . ARG E 212 ? 0.8990 0.8215 0.5370 0.0100  -0.1244 -0.0751 212 ARG E C   
9420  O O   . ARG E 212 ? 0.8835 0.8225 0.5329 0.0150  -0.1122 -0.0812 212 ARG E O   
9421  C CB  . ARG E 212 ? 0.8255 0.7819 0.5373 -0.0179 -0.1181 -0.0449 212 ARG E CB  
9422  C CG  . ARG E 212 ? 0.7927 0.7701 0.5292 -0.0306 -0.1038 -0.0287 212 ARG E CG  
9423  C CD  . ARG E 212 ? 0.7598 0.7489 0.5423 -0.0415 -0.1114 -0.0155 212 ARG E CD  
9424  N NE  . ARG E 212 ? 0.7377 0.7429 0.5405 -0.0406 -0.1039 -0.0196 212 ARG E NE  
9425  C CZ  . ARG E 212 ? 0.7098 0.7420 0.5235 -0.0423 -0.0790 -0.0200 212 ARG E CZ  
9426  N NH1 . ARG E 212 ? 0.7005 0.7457 0.5073 -0.0458 -0.0584 -0.0167 212 ARG E NH1 
9427  N NH2 . ARG E 212 ? 0.6933 0.7385 0.5246 -0.0408 -0.0758 -0.0234 212 ARG E NH2 
9428  N N   . ILE E 213 ? 0.9463 0.8338 0.5505 0.0179  -0.1476 -0.0835 213 ILE E N   
9429  C CA  . ILE E 213 ? 0.9858 0.8489 0.5617 0.0343  -0.1597 -0.1018 213 ILE E CA  
9430  C C   . ILE E 213 ? 0.9891 0.8308 0.5890 0.0293  -0.1891 -0.1009 213 ILE E C   
9431  O O   . ILE E 213 ? 0.9875 0.8171 0.6048 0.0164  -0.2107 -0.0897 213 ILE E O   
9432  C CB  . ILE E 213 ? 1.0431 0.8762 0.5621 0.0477  -0.1688 -0.1137 213 ILE E CB  
9433  C CG1 . ILE E 213 ? 1.0424 0.8989 0.5375 0.0538  -0.1372 -0.1139 213 ILE E CG1 
9434  C CG2 . ILE E 213 ? 1.0896 0.8915 0.5772 0.0660  -0.1847 -0.1337 213 ILE E CG2 
9435  C CD1 . ILE E 213 ? 1.0946 0.9266 0.5356 0.0639  -0.1432 -0.1203 213 ILE E CD1 
9436  N N   . ALA E 214 ? 0.9945 0.8330 0.5968 0.0392  -0.1896 -0.1115 214 ALA E N   
9437  C CA  . ALA E 214 ? 1.0039 0.8189 0.6256 0.0359  -0.2173 -0.1116 214 ALA E CA  
9438  C C   . ALA E 214 ? 1.0285 0.8311 0.6329 0.0544  -0.2170 -0.1290 214 ALA E C   
9439  O O   . ALA E 214 ? 1.0192 0.8457 0.6145 0.0662  -0.1905 -0.1362 214 ALA E O   
9440  C CB  . ALA E 214 ? 0.9511 0.7931 0.6293 0.0176  -0.2143 -0.0924 214 ALA E CB  
9441  N N   . THR E 215 ? 1.0623 0.8271 0.6631 0.0569  -0.2471 -0.1352 215 THR E N   
9442  C CA  . THR E 215 ? 1.0873 0.8359 0.6754 0.0745  -0.2503 -0.1506 215 THR E CA  
9443  C C   . THR E 215 ? 1.0408 0.8163 0.6788 0.0656  -0.2429 -0.1387 215 THR E C   
9444  O O   . THR E 215 ? 1.0224 0.7949 0.6960 0.0481  -0.2597 -0.1237 215 THR E O   
9445  C CB  . THR E 215 ? 1.1480 0.8394 0.7093 0.0807  -0.2879 -0.1627 215 THR E CB  
9446  O OG1 . THR E 215 ? 1.1879 0.8542 0.7085 0.0829  -0.3001 -0.1692 215 THR E OG1 
9447  C CG2 . THR E 215 ? 1.1857 0.8562 0.7197 0.1053  -0.2878 -0.1829 215 THR E CG2 
9448  N N   . ARG E 216 ? 1.0229 0.8264 0.6639 0.0776  -0.2175 -0.1442 216 ARG E N   
9449  C CA  . ARG E 216 ? 0.9762 0.8113 0.6625 0.0694  -0.2065 -0.1323 216 ARG E CA  
9450  C C   . ARG E 216 ? 0.9948 0.8222 0.6760 0.0878  -0.2069 -0.1444 216 ARG E C   
9451  O O   . ARG E 216 ? 1.0343 0.8459 0.6772 0.1096  -0.2041 -0.1627 216 ARG E O   
9452  C CB  . ARG E 216 ? 0.9268 0.8126 0.6304 0.0624  -0.1730 -0.1235 216 ARG E CB  
9453  C CG  . ARG E 216 ? 0.9067 0.8015 0.6181 0.0448  -0.1707 -0.1102 216 ARG E CG  
9454  C CD  . ARG E 216 ? 0.8690 0.8071 0.5884 0.0406  -0.1378 -0.1049 216 ARG E CD  
9455  N NE  . ARG E 216 ? 0.8948 0.8330 0.5738 0.0534  -0.1233 -0.1167 216 ARG E NE  
9456  C CZ  . ARG E 216 ? 0.9064 0.8383 0.5642 0.0492  -0.1215 -0.1142 216 ARG E CZ  
9457  N NH1 . ARG E 216 ? 0.8943 0.8193 0.5678 0.0330  -0.1338 -0.1007 216 ARG E NH1 
9458  N NH2 . ARG E 216 ? 0.9317 0.8656 0.5523 0.0621  -0.1067 -0.1242 216 ARG E NH2 
9459  N N   . SER E 217 ? 0.9678 0.8070 0.6875 0.0801  -0.2100 -0.1336 217 SER E N   
9460  C CA  . SER E 217 ? 0.9806 0.8164 0.7017 0.0966  -0.2098 -0.1421 217 SER E CA  
9461  C C   . SER E 217 ? 0.9614 0.8392 0.6781 0.1100  -0.1770 -0.1487 217 SER E C   
9462  O O   . SER E 217 ? 0.9221 0.8389 0.6521 0.0993  -0.1543 -0.1403 217 SER E O   
9463  C CB  . SER E 217 ? 0.9526 0.7949 0.7176 0.0828  -0.2196 -0.1255 217 SER E CB  
9464  O OG  . SER E 217 ? 0.9629 0.7759 0.7398 0.0658  -0.2470 -0.1147 217 SER E OG  
9465  N N   . LYS E 218 ? 0.9920 0.8612 0.6904 0.1336  -0.1751 -0.1636 218 LYS E N   
9466  C CA  . LYS E 218 ? 0.9763 0.8878 0.6741 0.1475  -0.1452 -0.1693 218 LYS E CA  
9467  C C   . LYS E 218 ? 0.9232 0.8765 0.6665 0.1359  -0.1327 -0.1547 218 LYS E C   
9468  O O   . LYS E 218 ? 0.9219 0.8644 0.6859 0.1353  -0.1469 -0.1495 218 LYS E O   
9469  C CB  . LYS E 218 ? 1.0260 0.9176 0.6938 0.1781  -0.1473 -0.1886 218 LYS E CB  
9470  C CG  . LYS E 218 ? 1.0690 0.9484 0.6885 0.1956  -0.1394 -0.2049 218 LYS E CG  
9471  C CD  . LYS E 218 ? 1.1354 0.9703 0.7175 0.2242  -0.1550 -0.2250 218 LYS E CD  
9472  C CE  . LYS E 218 ? 1.1829 1.0043 0.7128 0.2426  -0.1472 -0.2412 218 LYS E CE  
9473  N NZ  . LYS E 218 ? 1.2511 1.0055 0.7399 0.2537  -0.1785 -0.2562 218 LYS E NZ  
9474  N N   . VAL E 219 ? 0.8820 0.8810 0.6392 0.1262  -0.1068 -0.1476 219 VAL E N   
9475  C CA  . VAL E 219 ? 0.8356 0.8781 0.6298 0.1178  -0.0916 -0.1367 219 VAL E CA  
9476  C C   . VAL E 219 ? 0.8315 0.9122 0.6180 0.1319  -0.0650 -0.1451 219 VAL E C   
9477  O O   . VAL E 219 ? 0.8362 0.9266 0.6026 0.1323  -0.0504 -0.1491 219 VAL E O   
9478  C CB  . VAL E 219 ? 0.7918 0.8540 0.6118 0.0910  -0.0860 -0.1197 219 VAL E CB  
9479  C CG1 . VAL E 219 ? 0.7479 0.8562 0.6006 0.0830  -0.0682 -0.1103 219 VAL E CG1 
9480  C CG2 . VAL E 219 ? 0.7958 0.8247 0.6273 0.0778  -0.1117 -0.1096 219 VAL E CG2 
9481  N N   . ASN E 220 ? 0.8251 0.9274 0.6275 0.1438  -0.0594 -0.1469 220 ASN E N   
9482  C CA  . ASN E 220 ? 0.8267 0.9660 0.6239 0.1602  -0.0362 -0.1549 220 ASN E CA  
9483  C C   . ASN E 220 ? 0.8733 0.9929 0.6278 0.1816  -0.0327 -0.1709 220 ASN E C   
9484  O O   . ASN E 220 ? 0.8716 1.0221 0.6165 0.1864  -0.0098 -0.1738 220 ASN E O   
9485  C CB  . ASN E 220 ? 0.7824 0.9716 0.6008 0.1421  -0.0121 -0.1448 220 ASN E CB  
9486  C CG  . ASN E 220 ? 0.7423 0.9614 0.6000 0.1294  -0.0103 -0.1329 220 ASN E CG  
9487  O OD1 . ASN E 220 ? 0.7408 0.9406 0.6123 0.1271  -0.0283 -0.1277 220 ASN E OD1 
9488  N ND2 . ASN E 220 ? 0.7121 0.9783 0.5874 0.1206  0.0110  -0.1280 220 ASN E ND2 
9489  N N   . GLY E 221 ? 0.9175 0.9850 0.6456 0.1940  -0.0557 -0.1807 221 GLY E N   
9490  C CA  . GLY E 221 ? 0.9702 1.0120 0.6525 0.2170  -0.0556 -0.1978 221 GLY E CA  
9491  C C   . GLY E 221 ? 0.9788 1.0121 0.6341 0.2077  -0.0505 -0.1982 221 GLY E C   
9492  O O   . GLY E 221 ? 1.0197 1.0409 0.6357 0.2265  -0.0448 -0.2112 221 GLY E O   
9493  N N   . GLN E 222 ? 0.9428 0.9820 0.6177 0.1800  -0.0525 -0.1838 222 GLN E N   
9494  C CA  . GLN E 222 ? 0.9480 0.9803 0.6007 0.1693  -0.0482 -0.1817 222 GLN E CA  
9495  C C   . GLN E 222 ? 0.9369 0.9391 0.5995 0.1476  -0.0711 -0.1717 222 GLN E C   
9496  O O   . GLN E 222 ? 0.8998 0.9127 0.5998 0.1309  -0.0765 -0.1589 222 GLN E O   
9497  C CB  . GLN E 222 ? 0.9105 0.9947 0.5793 0.1573  -0.0182 -0.1721 222 GLN E CB  
9498  C CG  . GLN E 222 ? 0.9204 1.0411 0.5821 0.1767  0.0066  -0.1795 222 GLN E CG  
9499  C CD  . GLN E 222 ? 0.9783 1.0763 0.5906 0.2015  0.0083  -0.1950 222 GLN E CD  
9500  O OE1 . GLN E 222 ? 1.0047 1.0737 0.5861 0.1983  0.0008  -0.1971 222 GLN E OE1 
9501  N NE2 . GLN E 222 ? 1.0012 1.1129 0.6049 0.2274  0.0183  -0.2058 222 GLN E NE2 
9502  N N   . SER E 223 ? 0.9705 0.9367 0.5993 0.1486  -0.0846 -0.1771 223 SER E N   
9503  C CA  . SER E 223 ? 0.9637 0.9032 0.6007 0.1284  -0.1066 -0.1671 223 SER E CA  
9504  C C   . SER E 223 ? 0.9371 0.8969 0.5764 0.1108  -0.0924 -0.1558 223 SER E C   
9505  O O   . SER E 223 ? 0.9245 0.8716 0.5766 0.0929  -0.1063 -0.1447 223 SER E O   
9506  C CB  . SER E 223 ? 1.0216 0.9045 0.6219 0.1391  -0.1357 -0.1794 223 SER E CB  
9507  O OG  . SER E 223 ? 1.0402 0.8976 0.6479 0.1480  -0.1554 -0.1850 223 SER E OG  
9508  N N   . GLY E 224 ? 0.9300 0.9216 0.5579 0.1162  -0.0649 -0.1577 224 GLY E N   
9509  C CA  . GLY E 224 ? 0.9034 0.9173 0.5363 0.0995  -0.0485 -0.1460 224 GLY E CA  
9510  C C   . GLY E 224 ? 0.8465 0.8951 0.5260 0.0800  -0.0374 -0.1311 224 GLY E C   
9511  O O   . GLY E 224 ? 0.8266 0.8938 0.5311 0.0825  -0.0340 -0.1311 224 GLY E O   
9512  N N   . ARG E 225 ? 0.8228 0.8791 0.5121 0.0616  -0.0320 -0.1187 225 ARG E N   
9513  C CA  . ARG E 225 ? 0.7733 0.8577 0.5031 0.0430  -0.0229 -0.1049 225 ARG E CA  
9514  C C   . ARG E 225 ? 0.7536 0.8664 0.4845 0.0326  0.0019  -0.0980 225 ARG E C   
9515  O O   . ARG E 225 ? 0.7745 0.8782 0.4784 0.0335  0.0068  -0.0985 225 ARG E O   
9516  C CB  . ARG E 225 ? 0.7617 0.8253 0.5102 0.0289  -0.0437 -0.0939 225 ARG E CB  
9517  C CG  . ARG E 225 ? 0.7754 0.8135 0.5315 0.0344  -0.0689 -0.0970 225 ARG E CG  
9518  C CD  . ARG E 225 ? 0.7479 0.8089 0.5351 0.0342  -0.0639 -0.0945 225 ARG E CD  
9519  N NE  . ARG E 225 ? 0.7632 0.7980 0.5581 0.0388  -0.0882 -0.0957 225 ARG E NE  
9520  C CZ  . ARG E 225 ? 0.7972 0.8117 0.5731 0.0569  -0.0983 -0.1092 225 ARG E CZ  
9521  N NH1 . ARG E 225 ? 0.8198 0.8396 0.5672 0.0742  -0.0849 -0.1231 225 ARG E NH1 
9522  N NH2 . ARG E 225 ? 0.8111 0.7993 0.5966 0.0583  -0.1217 -0.1082 225 ARG E NH2 
9523  N N   . MET E 226 ? 0.7158 0.8617 0.4773 0.0224  0.0167  -0.0914 226 MET E N   
9524  C CA  . MET E 226 ? 0.6955 0.8667 0.4632 0.0093  0.0382  -0.0838 226 MET E CA  
9525  C C   . MET E 226 ? 0.6604 0.8371 0.4589 -0.0084 0.0360  -0.0717 226 MET E C   
9526  O O   . MET E 226 ? 0.6388 0.8269 0.4629 -0.0107 0.0324  -0.0699 226 MET E O   
9527  C CB  . MET E 226 ? 0.6868 0.8951 0.4617 0.0135  0.0592  -0.0880 226 MET E CB  
9528  C CG  . MET E 226 ? 0.7210 0.9317 0.4650 0.0308  0.0684  -0.0979 226 MET E CG  
9529  S SD  . MET E 226 ? 0.7371 0.9509 0.4552 0.0241  0.0864  -0.0923 226 MET E SD  
9530  C CE  . MET E 226 ? 0.7761 0.9998 0.4626 0.0484  0.0980  -0.1045 226 MET E CE  
9531  N N   . GLU E 227 ? 0.6352 0.8596 0.3176 -0.0031 0.0632  -0.1061 227 GLU E N   
9532  C CA  . GLU E 227 ? 0.5818 0.8284 0.3225 -0.0187 0.0535  -0.0987 227 GLU E CA  
9533  C C   . GLU E 227 ? 0.5520 0.8388 0.3214 -0.0313 0.0745  -0.0949 227 GLU E C   
9534  O O   . GLU E 227 ? 0.5765 0.8512 0.3230 -0.0399 0.0796  -0.0898 227 GLU E O   
9535  C CB  . GLU E 227 ? 0.5991 0.8033 0.3339 -0.0313 0.0236  -0.0873 227 GLU E CB  
9536  C CG  . GLU E 227 ? 0.5512 0.7736 0.3445 -0.0406 0.0129  -0.0772 227 GLU E CG  
9537  C CD  . GLU E 227 ? 0.5699 0.7573 0.3629 -0.0506 -0.0184 -0.0619 227 GLU E CD  
9538  O OE1 . GLU E 227 ? 0.6220 0.7676 0.3661 -0.0536 -0.0348 -0.0599 227 GLU E OE1 
9539  O OE2 . GLU E 227 ? 0.5355 0.7379 0.3769 -0.0554 -0.0269 -0.0500 227 GLU E OE2 
9540  N N   . PHE E 228 ? 0.5047 0.8348 0.3198 -0.0334 0.0855  -0.0972 228 PHE E N   
9541  C CA  . PHE E 228 ? 0.4835 0.8501 0.3206 -0.0473 0.1048  -0.0949 228 PHE E CA  
9542  C C   . PHE E 228 ? 0.4576 0.8195 0.3262 -0.0629 0.0987  -0.0872 228 PHE E C   
9543  O O   . PHE E 228 ? 0.4337 0.7920 0.3285 -0.0594 0.0875  -0.0857 228 PHE E O   
9544  C CB  . PHE E 228 ? 0.4599 0.8780 0.3183 -0.0402 0.1224  -0.1019 228 PHE E CB  
9545  C CG  . PHE E 228 ? 0.4897 0.9191 0.3174 -0.0227 0.1364  -0.1057 228 PHE E CG  
9546  C CD1 . PHE E 228 ? 0.5106 0.9585 0.3230 -0.0284 0.1552  -0.1009 228 PHE E CD1 
9547  C CD2 . PHE E 228 ? 0.5031 0.9206 0.3136 0.0007  0.1321  -0.1126 228 PHE E CD2 
9548  C CE1 . PHE E 228 ? 0.5425 1.0015 0.3257 -0.0084 0.1719  -0.1016 228 PHE E CE1 
9549  C CE2 . PHE E 228 ? 0.5390 0.9611 0.3150 0.0215  0.1483  -0.1149 228 PHE E CE2 
9550  C CZ  . PHE E 228 ? 0.5582 1.0028 0.3216 0.0182  0.1693  -0.1088 228 PHE E CZ  
9551  N N   . PHE E 229 ? 0.4676 0.8268 0.3303 -0.0787 0.1077  -0.0810 229 PHE E N   
9552  C CA  . PHE E 229 ? 0.4561 0.8018 0.3379 -0.0914 0.1056  -0.0725 229 PHE E CA  
9553  C C   . PHE E 229 ? 0.4508 0.8198 0.3399 -0.1082 0.1241  -0.0739 229 PHE E C   
9554  O O   . PHE E 229 ? 0.4594 0.8555 0.3386 -0.1136 0.1373  -0.0775 229 PHE E O   
9555  C CB  . PHE E 229 ? 0.4858 0.7916 0.3455 -0.0958 0.0952  -0.0607 229 PHE E CB  
9556  C CG  . PHE E 229 ? 0.4960 0.7760 0.3493 -0.0849 0.0718  -0.0558 229 PHE E CG  
9557  C CD1 . PHE E 229 ? 0.5246 0.7920 0.3428 -0.0764 0.0647  -0.0620 229 PHE E CD1 
9558  C CD2 . PHE E 229 ? 0.4828 0.7493 0.3627 -0.0834 0.0566  -0.0434 229 PHE E CD2 
9559  C CE1 . PHE E 229 ? 0.5430 0.7798 0.3489 -0.0706 0.0394  -0.0574 229 PHE E CE1 
9560  C CE2 . PHE E 229 ? 0.4948 0.7408 0.3718 -0.0779 0.0318  -0.0360 229 PHE E CE2 
9561  C CZ  . PHE E 229 ? 0.5265 0.7551 0.3644 -0.0735 0.0213  -0.0437 229 PHE E CZ  
9562  N N   . TRP E 230 ? 0.4417 0.7980 0.3461 -0.1167 0.1249  -0.0695 230 TRP E N   
9563  C CA  . TRP E 230 ? 0.4457 0.8127 0.3503 -0.1361 0.1388  -0.0708 230 TRP E CA  
9564  C C   . TRP E 230 ? 0.4639 0.7894 0.3604 -0.1451 0.1406  -0.0618 230 TRP E C   
9565  O O   . TRP E 230 ? 0.4641 0.7615 0.3655 -0.1331 0.1320  -0.0530 230 TRP E O   
9566  C CB  . TRP E 230 ? 0.4183 0.8190 0.3467 -0.1353 0.1414  -0.0797 230 TRP E CB  
9567  C CG  . TRP E 230 ? 0.3976 0.7839 0.3455 -0.1217 0.1332  -0.0795 230 TRP E CG  
9568  C CD1 . TRP E 230 ? 0.3771 0.7693 0.3407 -0.1019 0.1226  -0.0812 230 TRP E CD1 
9569  C CD2 . TRP E 230 ? 0.4010 0.7619 0.3518 -0.1263 0.1365  -0.0762 230 TRP E CD2 
9570  N NE1 . TRP E 230 ? 0.3631 0.7412 0.3447 -0.0945 0.1194  -0.0777 230 TRP E NE1 
9571  C CE2 . TRP E 230 ? 0.3783 0.7364 0.3512 -0.1072 0.1290  -0.0746 230 TRP E CE2 
9572  C CE3 . TRP E 230 ? 0.4277 0.7629 0.3597 -0.1442 0.1457  -0.0737 230 TRP E CE3 
9573  C CZ2 . TRP E 230 ? 0.3799 0.7138 0.3584 -0.1028 0.1329  -0.0699 230 TRP E CZ2 
9574  C CZ3 . TRP E 230 ? 0.4344 0.7383 0.3656 -0.1394 0.1489  -0.0707 230 TRP E CZ3 
9575  C CH2 . TRP E 230 ? 0.4096 0.7149 0.3649 -0.1175 0.1437  -0.0684 230 TRP E CH2 
9576  N N   . THR E 231 ? 0.4838 0.8055 0.3668 -0.1666 0.1519  -0.0621 231 THR E N   
9577  C CA  . THR E 231 ? 0.5099 0.7861 0.3775 -0.1750 0.1568  -0.0551 231 THR E CA  
9578  C C   . THR E 231 ? 0.5271 0.8065 0.3832 -0.2001 0.1657  -0.0607 231 THR E C   
9579  O O   . THR E 231 ? 0.5192 0.8418 0.3821 -0.2136 0.1679  -0.0663 231 THR E O   
9580  C CB  . THR E 231 ? 0.5435 0.7839 0.3855 -0.1786 0.1583  -0.0436 231 THR E CB  
9581  O OG1 . THR E 231 ? 0.5701 0.7613 0.3975 -0.1789 0.1635  -0.0350 231 THR E OG1 
9582  C CG2 . THR E 231 ? 0.5673 0.8202 0.3878 -0.2011 0.1672  -0.0446 231 THR E CG2 
9583  N N   . ILE E 232 ? 0.5558 0.7884 0.3928 -0.2057 0.1705  -0.0576 232 ILE E N   
9584  C CA  . ILE E 232 ? 0.5906 0.8079 0.4024 -0.2347 0.1766  -0.0612 232 ILE E CA  
9585  C C   . ILE E 232 ? 0.6397 0.8107 0.4153 -0.2495 0.1838  -0.0520 232 ILE E C   
9586  O O   . ILE E 232 ? 0.6626 0.7824 0.4212 -0.2357 0.1874  -0.0436 232 ILE E O   
9587  C CB  . ILE E 232 ? 0.6015 0.7875 0.4042 -0.2316 0.1777  -0.0656 232 ILE E CB  
9588  C CG1 . ILE E 232 ? 0.5711 0.8075 0.3971 -0.2371 0.1712  -0.0765 232 ILE E CG1 
9589  C CG2 . ILE E 232 ? 0.6646 0.7902 0.4185 -0.2561 0.1849  -0.0641 232 ILE E CG2 
9590  C CD1 . ILE E 232 ? 0.5163 0.8104 0.3841 -0.2152 0.1648  -0.0795 232 ILE E CD1 
9591  N N   . LEU E 233 ? 0.6570 0.8492 0.4229 -0.2763 0.1867  -0.0515 233 LEU E N   
9592  C CA  . LEU E 233 ? 0.7069 0.8572 0.4366 -0.2940 0.1939  -0.0425 233 LEU E CA  
9593  C C   . LEU E 233 ? 0.7599 0.8651 0.4526 -0.3238 0.1974  -0.0439 233 LEU E C   
9594  O O   . LEU E 233 ? 0.7633 0.8995 0.4596 -0.3518 0.1941  -0.0484 233 LEU E O   
9595  C CB  . LEU E 233 ? 0.7016 0.8977 0.4388 -0.3072 0.1967  -0.0388 233 LEU E CB  
9596  C CG  . LEU E 233 ? 0.7496 0.9090 0.4516 -0.3240 0.2047  -0.0281 233 LEU E CG  
9597  C CD1 . LEU E 233 ? 0.7614 0.8721 0.4480 -0.2985 0.2043  -0.0203 233 LEU E CD1 
9598  C CD2 . LEU E 233 ? 0.7416 0.9558 0.4551 -0.3352 0.2097  -0.0241 233 LEU E CD2 
9599  N N   . LYS E 234 ? 0.8064 0.8366 0.4615 -0.3174 0.2034  -0.0388 234 LYS E N   
9600  C CA  . LYS E 234 ? 0.8718 0.8395 0.4778 -0.3428 0.2070  -0.0407 234 LYS E CA  
9601  C C   . LYS E 234 ? 0.9200 0.8762 0.4962 -0.3827 0.2093  -0.0354 234 LYS E C   
9602  O O   . LYS E 234 ? 0.9082 0.8919 0.4966 -0.3835 0.2121  -0.0280 234 LYS E O   
9603  C CB  . LYS E 234 ? 0.9125 0.7990 0.4834 -0.3176 0.2164  -0.0347 234 LYS E CB  
9604  C CG  . LYS E 234 ? 0.8808 0.7709 0.4738 -0.2854 0.2158  -0.0387 234 LYS E CG  
9605  C CD  . LYS E 234 ? 0.9154 0.7375 0.4839 -0.2535 0.2281  -0.0272 234 LYS E CD  
9606  C CE  . LYS E 234 ? 0.9004 0.7164 0.4803 -0.2272 0.2309  -0.0303 234 LYS E CE  
9607  N NZ  . LYS E 234 ? 0.9347 0.6906 0.4955 -0.1921 0.2461  -0.0151 234 LYS E NZ  
9608  N N   . PRO E 235 ? 0.9796 0.8930 0.5138 -0.4175 0.2075  -0.0384 235 PRO E N   
9609  C CA  . PRO E 235 ? 1.0281 0.9328 0.5358 -0.4605 0.2079  -0.0315 235 PRO E CA  
9610  C C   . PRO E 235 ? 1.0765 0.9174 0.5450 -0.4550 0.2195  -0.0206 235 PRO E C   
9611  O O   . PRO E 235 ? 1.1013 0.8766 0.5421 -0.4263 0.2269  -0.0188 235 PRO E O   
9612  C CB  . PRO E 235 ? 1.0907 0.9456 0.5525 -0.4968 0.2004  -0.0372 235 PRO E CB  
9613  C CG  . PRO E 235 ? 1.0630 0.9202 0.5368 -0.4726 0.1955  -0.0486 235 PRO E CG  
9614  C CD  . PRO E 235 ? 1.0139 0.8769 0.5161 -0.4200 0.2045  -0.0471 235 PRO E CD  
9615  N N   . ASN E 236 ? 1.0909 0.9539 0.5589 -0.4805 0.2221  -0.0115 236 ASN E N   
9616  C CA  . ASN E 236 ? 1.1420 0.9461 0.5701 -0.4800 0.2326  0.0000  236 ASN E CA  
9617  C C   . ASN E 236 ? 1.1007 0.9163 0.5523 -0.4342 0.2375  0.0052  236 ASN E C   
9618  O O   . ASN E 236 ? 1.1405 0.9053 0.5606 -0.4258 0.2454  0.0157  236 ASN E O   
9619  C CB  . ASN E 236 ? 1.2312 0.9233 0.5867 -0.4892 0.2375  0.0002  236 ASN E CB  
9620  C CG  . ASN E 236 ? 1.3108 0.9508 0.6141 -0.5299 0.2418  0.0099  236 ASN E CG  
9621  O OD1 . ASN E 236 ? 1.3038 0.9822 0.6231 -0.5421 0.2451  0.0196  236 ASN E OD1 
9622  N ND2 . ASN E 236 ? 1.3966 0.9430 0.6319 -0.5511 0.2424  0.0077  236 ASN E ND2 
9623  N N   . ASP E 237 ? 1.0263 0.9071 0.5312 -0.4064 0.2313  -0.0011 237 ASP E N   
9624  C CA  . ASP E 237 ? 0.9865 0.8827 0.5159 -0.3665 0.2309  0.0038  237 ASP E CA  
9625  C C   . ASP E 237 ? 0.9381 0.9134 0.5056 -0.3668 0.2278  0.0034  237 ASP E C   
9626  O O   . ASP E 237 ? 0.9132 0.9459 0.5054 -0.3854 0.2256  -0.0025 237 ASP E O   
9627  C CB  . ASP E 237 ? 0.9484 0.8461 0.5029 -0.3321 0.2258  -0.0018 237 ASP E CB  
9628  C CG  . ASP E 237 ? 0.9188 0.8226 0.4950 -0.2939 0.2224  0.0070  237 ASP E CG  
9629  O OD1 . ASP E 237 ? 0.9491 0.8226 0.5032 -0.2900 0.2260  0.0192  237 ASP E OD1 
9630  O OD2 . ASP E 237 ? 0.8679 0.8060 0.4826 -0.2694 0.2147  0.0029  237 ASP E OD2 
9631  N N   . ALA E 238 ? 0.9298 0.9057 0.4990 -0.3450 0.2279  0.0113  238 ALA E N   
9632  C CA  . ALA E 238 ? 0.8996 0.9349 0.4904 -0.3419 0.2275  0.0120  238 ALA E CA  
9633  C C   . ALA E 238 ? 0.8495 0.9124 0.4708 -0.3056 0.2168  0.0081  238 ALA E C   
9634  O O   . ALA E 238 ? 0.8476 0.8766 0.4686 -0.2824 0.2102  0.0120  238 ALA E O   
9635  C CB  . ALA E 238 ? 0.9442 0.9528 0.5010 -0.3515 0.2355  0.0247  238 ALA E CB  
9636  N N   . ILE E 239 ? 0.8135 0.9369 0.4599 -0.3010 0.2154  0.0024  239 ILE E N   
9637  C CA  . ILE E 239 ? 0.7772 0.9213 0.4430 -0.2699 0.2044  -0.0009 239 ILE E CA  
9638  C C   . ILE E 239 ? 0.7972 0.9437 0.4410 -0.2642 0.2066  0.0056  239 ILE E C   
9639  O O   . ILE E 239 ? 0.8146 0.9843 0.4480 -0.2808 0.2195  0.0083  239 ILE E O   
9640  C CB  . ILE E 239 ? 0.7279 0.9283 0.4314 -0.2621 0.2004  -0.0134 239 ILE E CB  
9641  C CG1 . ILE E 239 ? 0.6988 0.9057 0.4167 -0.2311 0.1865  -0.0166 239 ILE E CG1 
9642  C CG2 . ILE E 239 ? 0.7248 0.9801 0.4359 -0.2771 0.2118  -0.0148 239 ILE E CG2 
9643  C CD1 . ILE E 239 ? 0.6534 0.8959 0.4069 -0.2197 0.1802  -0.0278 239 ILE E CD1 
9644  N N   . ASN E 240 ? 0.7988 0.9207 0.4343 -0.2414 0.1937  0.0100  240 ASN E N   
9645  C CA  . ASN E 240 ? 0.8276 0.9385 0.4324 -0.2346 0.1927  0.0166  240 ASN E CA  
9646  C C   . ASN E 240 ? 0.8068 0.9347 0.4175 -0.2109 0.1784  0.0105  240 ASN E C   
9647  O O   . ASN E 240 ? 0.7869 0.9037 0.4141 -0.1954 0.1603  0.0106  240 ASN E O   
9648  C CB  . ASN E 240 ? 0.8658 0.9207 0.4431 -0.2321 0.1867  0.0309  240 ASN E CB  
9649  C CG  . ASN E 240 ? 0.9000 0.9243 0.4591 -0.2547 0.2015  0.0379  240 ASN E CG  
9650  O OD1 . ASN E 240 ? 0.9196 0.9571 0.4658 -0.2770 0.2169  0.0378  240 ASN E OD1 
9651  N ND2 . ASN E 240 ? 0.9127 0.8942 0.4691 -0.2487 0.1973  0.0458  240 ASN E ND2 
9652  N N   . PHE E 241 ? 0.8171 0.9690 0.4115 -0.2082 0.1871  0.0067  241 PHE E N   
9653  C CA  . PHE E 241 ? 0.8134 0.9702 0.3985 -0.1860 0.1754  0.0003  241 PHE E CA  
9654  C C   . PHE E 241 ? 0.8650 0.9848 0.3981 -0.1795 0.1716  0.0078  241 PHE E C   
9655  O O   . PHE E 241 ? 0.8990 1.0151 0.4050 -0.1900 0.1892  0.0145  241 PHE E O   
9656  C CB  . PHE E 241 ? 0.7939 1.0021 0.3932 -0.1815 0.1901  -0.0096 241 PHE E CB  
9657  C CG  . PHE E 241 ? 0.7436 0.9880 0.3910 -0.1835 0.1888  -0.0183 241 PHE E CG  
9658  C CD1 . PHE E 241 ? 0.7146 0.9600 0.3806 -0.1656 0.1715  -0.0265 241 PHE E CD1 
9659  C CD2 . PHE E 241 ? 0.7300 1.0047 0.4014 -0.2050 0.2032  -0.0174 241 PHE E CD2 
9660  C CE1 . PHE E 241 ? 0.6711 0.9477 0.3785 -0.1664 0.1708  -0.0341 241 PHE E CE1 
9661  C CE2 . PHE E 241 ? 0.6891 0.9936 0.3996 -0.2072 0.2004  -0.0254 241 PHE E CE2 
9662  C CZ  . PHE E 241 ? 0.6587 0.9643 0.3872 -0.1865 0.1852  -0.0339 241 PHE E CZ  
9663  N N   . GLU E 242 ? 0.8744 0.9654 0.3921 -0.1637 0.1473  0.0080  242 GLU E N   
9664  C CA  . GLU E 242 ? 0.9290 0.9823 0.3901 -0.1556 0.1396  0.0127  242 GLU E CA  
9665  C C   . GLU E 242 ? 0.9331 0.9771 0.3794 -0.1373 0.1201  0.0035  242 GLU E C   
9666  O O   . GLU E 242 ? 0.9056 0.9472 0.3802 -0.1330 0.0969  0.0028  242 GLU E O   
9667  C CB  . GLU E 242 ? 0.9580 0.9669 0.4014 -0.1608 0.1233  0.0284  242 GLU E CB  
9668  C CG  . GLU E 242 ? 1.0223 0.9880 0.4012 -0.1552 0.1144  0.0348  242 GLU E CG  
9669  C CD  . GLU E 242 ? 1.0496 0.9752 0.4153 -0.1592 0.0949  0.0526  242 GLU E CD  
9670  O OE1 . GLU E 242 ? 1.0476 0.9705 0.4260 -0.1701 0.1076  0.0622  242 GLU E OE1 
9671  O OE2 . GLU E 242 ? 1.0779 0.9725 0.4180 -0.1518 0.0659  0.0581  242 GLU E OE2 
9672  N N   . SER E 243 ? 0.9724 1.0085 0.3719 -0.1261 0.1307  -0.0023 243 SER E N   
9673  C CA  . SER E 243 ? 0.9924 1.0068 0.3626 -0.1083 0.1133  -0.0118 243 SER E CA  
9674  C C   . SER E 243 ? 1.0667 1.0421 0.3586 -0.0960 0.1210  -0.0129 243 SER E C   
9675  O O   . SER E 243 ? 1.0867 1.0783 0.3607 -0.0948 0.1522  -0.0106 243 SER E O   
9676  C CB  . SER E 243 ? 0.9468 1.0062 0.3554 -0.0987 0.1241  -0.0249 243 SER E CB  
9677  O OG  . SER E 243 ? 0.9741 1.0056 0.3478 -0.0809 0.1089  -0.0343 243 SER E OG  
9678  N N   . ASN E 244 ? 1.1115 1.0340 0.3555 -0.0874 0.0921  -0.0152 244 ASN E N   
9679  C CA  . ASN E 244 ? 1.1935 1.0656 0.3506 -0.0724 0.0958  -0.0187 244 ASN E CA  
9680  C C   . ASN E 244 ? 1.2102 1.0716 0.3417 -0.0514 0.0956  -0.0338 244 ASN E C   
9681  O O   . ASN E 244 ? 1.2876 1.0940 0.3379 -0.0361 0.0945  -0.0385 244 ASN E O   
9682  C CB  . ASN E 244 ? 1.2532 1.0588 0.3561 -0.0797 0.0609  -0.0094 244 ASN E CB  
9683  C CG  . ASN E 244 ? 1.2355 1.0246 0.3620 -0.0868 0.0167  -0.0078 244 ASN E CG  
9684  O OD1 . ASN E 244 ? 1.1649 0.9982 0.3638 -0.0910 0.0133  -0.0095 244 ASN E OD1 
9685  N ND2 . ASN E 244 ? 1.3026 1.0282 0.3677 -0.0894 -0.0178 -0.0030 244 ASN E ND2 
9686  N N   . GLY E 245 ? 1.1440 1.0522 0.3390 -0.0497 0.0972  -0.0412 245 GLY E N   
9687  C CA  . GLY E 245 ? 1.1558 1.0589 0.3320 -0.0284 0.1010  -0.0549 245 GLY E CA  
9688  C C   . GLY E 245 ? 1.0800 1.0306 0.3304 -0.0301 0.0949  -0.0611 245 GLY E C   
9689  O O   . GLY E 245 ? 1.0250 0.9983 0.3351 -0.0480 0.0779  -0.0552 245 GLY E O   
9690  N N   . ASN E 246 ? 1.0827 1.0458 0.3254 -0.0087 0.1109  -0.0720 246 ASN E N   
9691  C CA  . ASN E 246 ? 1.0240 1.0228 0.3230 -0.0052 0.1049  -0.0796 246 ASN E CA  
9692  C C   . ASN E 246 ? 0.9379 1.0149 0.3255 -0.0182 0.1210  -0.0760 246 ASN E C   
9693  O O   . ASN E 246 ? 0.8850 0.9869 0.3244 -0.0218 0.1092  -0.0795 246 ASN E O   
9694  C CB  . ASN E 246 ? 1.0278 0.9828 0.3248 -0.0147 0.0611  -0.0805 246 ASN E CB  
9695  C CG  . ASN E 246 ? 1.1213 0.9910 0.3250 -0.0072 0.0388  -0.0838 246 ASN E CG  
9696  O OD1 . ASN E 246 ? 1.1712 1.0009 0.3279 -0.0151 0.0300  -0.0766 246 ASN E OD1 
9697  N ND2 . ASN E 246 ? 1.1512 0.9875 0.3228 0.0072  0.0284  -0.0945 246 ASN E ND2 
9698  N N   . PHE E 247 ? 0.9299 1.0425 0.3302 -0.0256 0.1481  -0.0685 247 PHE E N   
9699  C CA  . PHE E 247 ? 0.8619 1.0372 0.3350 -0.0437 0.1602  -0.0638 247 PHE E CA  
9700  C C   . PHE E 247 ? 0.8319 1.0716 0.3386 -0.0334 0.1888  -0.0668 247 PHE E C   
9701  O O   . PHE E 247 ? 0.8657 1.1191 0.3442 -0.0185 0.2151  -0.0641 247 PHE E O   
9702  C CB  . PHE E 247 ? 0.8746 1.0481 0.3425 -0.0632 0.1695  -0.0518 247 PHE E CB  
9703  C CG  . PHE E 247 ? 0.8202 1.0447 0.3500 -0.0849 0.1809  -0.0466 247 PHE E CG  
9704  C CD1 . PHE E 247 ? 0.7685 1.0048 0.3485 -0.0947 0.1645  -0.0490 247 PHE E CD1 
9705  C CD2 . PHE E 247 ? 0.8281 1.0836 0.3610 -0.0968 0.2077  -0.0379 247 PHE E CD2 
9706  C CE1 . PHE E 247 ? 0.7309 1.0023 0.3558 -0.1147 0.1744  -0.0450 247 PHE E CE1 
9707  C CE2 . PHE E 247 ? 0.7889 1.0820 0.3701 -0.1204 0.2152  -0.0331 247 PHE E CE2 
9708  C CZ  . PHE E 247 ? 0.7430 1.0403 0.3665 -0.1290 0.1982  -0.0377 247 PHE E CZ  
9709  N N   . ILE E 248 ? 0.7709 1.0510 0.3381 -0.0403 0.1838  -0.0704 248 ILE E N   
9710  C CA  . ILE E 248 ? 0.7359 1.0844 0.3450 -0.0359 0.2069  -0.0706 248 ILE E CA  
9711  C C   . ILE E 248 ? 0.7011 1.0896 0.3552 -0.0653 0.2150  -0.0621 248 ILE E C   
9712  O O   . ILE E 248 ? 0.6619 1.0526 0.3526 -0.0813 0.2002  -0.0639 248 ILE E O   
9713  C CB  . ILE E 248 ? 0.6984 1.0622 0.3384 -0.0237 0.1955  -0.0805 248 ILE E CB  
9714  C CG1 . ILE E 248 ? 0.7374 1.0412 0.3287 -0.0023 0.1771  -0.0891 248 ILE E CG1 
9715  C CG2 . ILE E 248 ? 0.6777 1.1089 0.3481 -0.0118 0.2204  -0.0792 248 ILE E CG2 
9716  C CD1 . ILE E 248 ? 0.8059 1.0807 0.3301 0.0223  0.1934  -0.0899 248 ILE E CD1 
9717  N N   . ALA E 249 ? 0.7224 1.1378 0.3690 -0.0722 0.2392  -0.0518 249 ALA E N   
9718  C CA  . ALA E 249 ? 0.7060 1.1467 0.3818 -0.1038 0.2461  -0.0423 249 ALA E CA  
9719  C C   . ALA E 249 ? 0.6593 1.1664 0.3930 -0.1163 0.2529  -0.0413 249 ALA E C   
9720  O O   . ALA E 249 ? 0.6478 1.1994 0.3980 -0.0985 0.2638  -0.0422 249 ALA E O   
9721  C CB  . ALA E 249 ? 0.7499 1.1953 0.3960 -0.1089 0.2690  -0.0293 249 ALA E CB  
9722  N N   . PRO E 250 ? 0.6383 1.1486 0.3988 -0.1463 0.2459  -0.0386 250 PRO E N   
9723  C CA  . PRO E 250 ? 0.6048 1.1735 0.4129 -0.1640 0.2505  -0.0362 250 PRO E CA  
9724  C C   . PRO E 250 ? 0.6201 1.2456 0.4406 -0.1798 0.2735  -0.0204 250 PRO E C   
9725  O O   . PRO E 250 ? 0.6477 1.2576 0.4518 -0.2018 0.2801  -0.0107 250 PRO E O   
9726  C CB  . PRO E 250 ? 0.5939 1.1281 0.4100 -0.1903 0.2352  -0.0385 250 PRO E CB  
9727  C CG  . PRO E 250 ? 0.6286 1.1028 0.4049 -0.1933 0.2318  -0.0349 250 PRO E CG  
9728  C CD  . PRO E 250 ? 0.6486 1.1023 0.3929 -0.1630 0.2312  -0.0381 250 PRO E CD  
9729  N N   . GLU E 251 ? 0.6043 1.2967 0.4549 -0.1683 0.2859  -0.0156 251 GLU E N   
9730  C CA  . GLU E 251 ? 0.6098 1.3724 0.4892 -0.1883 0.3050  0.0033  251 GLU E CA  
9731  C C   . GLU E 251 ? 0.5863 1.3707 0.5019 -0.2273 0.2913  0.0050  251 GLU E C   
9732  O O   . GLU E 251 ? 0.6055 1.3898 0.5207 -0.2629 0.2934  0.0159  251 GLU E O   
9733  C CB  . GLU E 251 ? 0.6034 1.4345 0.5048 -0.1587 0.3237  0.0113  251 GLU E CB  
9734  C CG  . GLU E 251 ? 0.6434 1.5000 0.5262 -0.1441 0.3535  0.0289  251 GLU E CG  
9735  C CD  . GLU E 251 ? 0.6400 1.5874 0.5711 -0.1673 0.3713  0.0545  251 GLU E CD  
9736  O OE1 . GLU E 251 ? 0.6133 1.6308 0.5895 -0.1591 0.3747  0.0616  251 GLU E OE1 
9737  O OE2 . GLU E 251 ? 0.6661 1.6169 0.5912 -0.1942 0.3813  0.0694  251 GLU E OE2 
9738  N N   . TYR E 252 ? 0.5508 1.3474 0.4918 -0.2206 0.2767  -0.0059 252 TYR E N   
9739  C CA  . TYR E 252 ? 0.5333 1.3466 0.5027 -0.2541 0.2621  -0.0060 252 TYR E CA  
9740  C C   . TYR E 252 ? 0.5216 1.2665 0.4753 -0.2549 0.2410  -0.0240 252 TYR E C   
9741  O O   . TYR E 252 ? 0.5083 1.2194 0.4499 -0.2242 0.2346  -0.0365 252 TYR E O   
9742  C CB  . TYR E 252 ? 0.5048 1.3982 0.5202 -0.2476 0.2636  -0.0002 252 TYR E CB  
9743  C CG  . TYR E 252 ? 0.5153 1.4895 0.5566 -0.2481 0.2856  0.0227  252 TYR E CG  
9744  C CD1 . TYR E 252 ? 0.5288 1.5484 0.5940 -0.2909 0.2874  0.0421  252 TYR E CD1 
9745  C CD2 . TYR E 252 ? 0.5174 1.5209 0.5574 -0.2056 0.3053  0.0271  252 TYR E CD2 
9746  C CE1 . TYR E 252 ? 0.5382 1.6397 0.6336 -0.2915 0.3088  0.0676  252 TYR E CE1 
9747  C CE2 . TYR E 252 ? 0.5301 1.6104 0.5949 -0.2016 0.3295  0.0514  252 TYR E CE2 
9748  C CZ  . TYR E 252 ? 0.5375 1.6715 0.6342 -0.2448 0.3314  0.0729  252 TYR E CZ  
9749  O OH  . TYR E 252 ? 0.5495 1.7676 0.6774 -0.2411 0.3565  0.1014  252 TYR E OH  
9750  N N   . ALA E 253 ? 0.5321 1.2553 0.4839 -0.2906 0.2308  -0.0234 253 ALA E N   
9751  C CA  . ALA E 253 ? 0.5260 1.1892 0.4645 -0.2925 0.2141  -0.0372 253 ALA E CA  
9752  C C   . ALA E 253 ? 0.5225 1.2088 0.4798 -0.3211 0.2035  -0.0369 253 ALA E C   
9753  O O   . ALA E 253 ? 0.5438 1.2604 0.5081 -0.3560 0.2053  -0.0246 253 ALA E O   
9754  C CB  . ALA E 253 ? 0.5599 1.1492 0.4593 -0.3049 0.2132  -0.0370 253 ALA E CB  
9755  N N   . TYR E 254 ? 0.4997 1.1708 0.4634 -0.3077 0.1916  -0.0492 254 TYR E N   
9756  C CA  . TYR E 254 ? 0.4995 1.1877 0.4755 -0.3314 0.1796  -0.0504 254 TYR E CA  
9757  C C   . TYR E 254 ? 0.5418 1.1612 0.4805 -0.3637 0.1721  -0.0525 254 TYR E C   
9758  O O   . TYR E 254 ? 0.5574 1.1066 0.4651 -0.3538 0.1736  -0.0582 254 TYR E O   
9759  C CB  . TYR E 254 ? 0.4641 1.1578 0.4563 -0.3031 0.1712  -0.0624 254 TYR E CB  
9760  C CG  . TYR E 254 ? 0.4302 1.1956 0.4578 -0.2758 0.1772  -0.0593 254 TYR E CG  
9761  C CD1 . TYR E 254 ? 0.4201 1.2589 0.4810 -0.2878 0.1746  -0.0504 254 TYR E CD1 
9762  C CD2 . TYR E 254 ? 0.4143 1.1715 0.4390 -0.2379 0.1848  -0.0639 254 TYR E CD2 
9763  C CE1 . TYR E 254 ? 0.3936 1.2972 0.4856 -0.2586 0.1826  -0.0456 254 TYR E CE1 
9764  C CE2 . TYR E 254 ? 0.3934 1.2065 0.4416 -0.2103 0.1921  -0.0614 254 TYR E CE2 
9765  C CZ  . TYR E 254 ? 0.3824 1.2693 0.4650 -0.2187 0.1926  -0.0519 254 TYR E CZ  
9766  O OH  . TYR E 254 ? 0.3659 1.3080 0.4708 -0.1873 0.2024  -0.0473 254 TYR E OH  
9767  N N   . LYS E 255 ? 0.5653 1.2040 0.5055 -0.4022 0.1634  -0.0464 255 LYS E N   
9768  C CA  . LYS E 255 ? 0.6189 1.1881 0.5152 -0.4375 0.1556  -0.0478 255 LYS E CA  
9769  C C   . LYS E 255 ? 0.6219 1.1709 0.5098 -0.4407 0.1408  -0.0582 255 LYS E C   
9770  O O   . LYS E 255 ? 0.5991 1.2117 0.5196 -0.4449 0.1321  -0.0558 255 LYS E O   
9771  C CB  . LYS E 255 ? 0.6552 1.2562 0.5526 -0.4850 0.1541  -0.0314 255 LYS E CB  
9772  C CG  . LYS E 255 ? 0.7162 1.2401 0.5625 -0.5142 0.1565  -0.0282 255 LYS E CG  
9773  C CD  . LYS E 255 ? 0.7400 1.3094 0.5980 -0.5510 0.1615  -0.0083 255 LYS E CD  
9774  C CE  . LYS E 255 ? 0.7968 1.3514 0.6330 -0.6089 0.1445  -0.0007 255 LYS E CE  
9775  N NZ  . LYS E 255 ? 0.7801 1.4411 0.6699 -0.6350 0.1380  0.0178  255 LYS E NZ  
9776  N N   . ILE E 256 ? 0.6535 1.1138 0.4962 -0.4369 0.1392  -0.0681 256 ILE E N   
9777  C CA  . ILE E 256 ? 0.6621 1.0915 0.4886 -0.4338 0.1283  -0.0787 256 ILE E CA  
9778  C C   . ILE E 256 ? 0.7307 1.1185 0.5132 -0.4825 0.1155  -0.0768 256 ILE E C   
9779  O O   . ILE E 256 ? 0.7881 1.0855 0.5137 -0.4927 0.1181  -0.0803 256 ILE E O   
9780  C CB  . ILE E 256 ? 0.6613 1.0178 0.4631 -0.3971 0.1360  -0.0885 256 ILE E CB  
9781  C CG1 . ILE E 256 ? 0.6184 0.9906 0.4462 -0.3610 0.1479  -0.0864 256 ILE E CG1 
9782  C CG2 . ILE E 256 ? 0.6436 1.0011 0.4513 -0.3792 0.1285  -0.0979 256 ILE E CG2 
9783  C CD1 . ILE E 256 ? 0.6091 0.9280 0.4269 -0.3243 0.1533  -0.0916 256 ILE E CD1 
9784  N N   . VAL E 257 ? 0.7301 1.1823 0.5367 -0.5128 0.1011  -0.0698 257 VAL E N   
9785  C CA  . VAL E 257 ? 0.8009 1.2194 0.5664 -0.5666 0.0841  -0.0655 257 VAL E CA  
9786  C C   . VAL E 257 ? 0.8410 1.1920 0.5588 -0.5689 0.0713  -0.0787 257 VAL E C   
9787  O O   . VAL E 257 ? 0.9204 1.1838 0.5706 -0.5993 0.0643  -0.0818 257 VAL E O   
9788  C CB  . VAL E 257 ? 0.7919 1.3099 0.6035 -0.6046 0.0711  -0.0478 257 VAL E CB  
9789  C CG1 . VAL E 257 ? 0.7759 1.3410 0.6175 -0.6095 0.0861  -0.0326 257 VAL E CG1 
9790  C CG2 . VAL E 257 ? 0.7316 1.3401 0.6008 -0.5827 0.0644  -0.0466 257 VAL E CG2 
9791  N N   . LYS E 258 ? 0.7928 1.1784 0.5400 -0.5359 0.0693  -0.0862 258 LYS E N   
9792  C CA  . LYS E 258 ? 0.8278 1.1531 0.5312 -0.5325 0.0593  -0.0983 258 LYS E CA  
9793  C C   . LYS E 258 ? 0.7919 1.0843 0.4968 -0.4771 0.0752  -0.1096 258 LYS E C   
9794  O O   . LYS E 258 ? 0.7192 1.0767 0.4809 -0.4419 0.0826  -0.1091 258 LYS E O   
9795  C CB  . LYS E 258 ? 0.8169 1.2117 0.5479 -0.5525 0.0369  -0.0945 258 LYS E CB  
9796  C CG  . LYS E 258 ? 0.9035 1.2514 0.5775 -0.6084 0.0126  -0.0926 258 LYS E CG  
9797  C CD  . LYS E 258 ? 0.9190 1.2590 0.5748 -0.6076 -0.0053 -0.1003 258 LYS E CD  
9798  C CE  . LYS E 258 ? 0.8552 1.3201 0.5875 -0.6057 -0.0182 -0.0897 258 LYS E CE  
9799  N NZ  . LYS E 258 ? 0.9003 1.3575 0.6037 -0.6334 -0.0466 -0.0907 258 LYS E NZ  
9800  N N   . LYS E 259 ? 0.8491 1.0381 0.4887 -0.4699 0.0807  -0.1181 259 LYS E N   
9801  C CA  . LYS E 259 ? 0.8270 0.9801 0.4634 -0.4211 0.0946  -0.1259 259 LYS E CA  
9802  C C   . LYS E 259 ? 0.8680 0.9807 0.4632 -0.4248 0.0838  -0.1343 259 LYS E C   
9803  O O   . LYS E 259 ? 0.9540 0.9816 0.4752 -0.4503 0.0786  -0.1380 259 LYS E O   
9804  C CB  . LYS E 259 ? 0.8632 0.9286 0.4577 -0.4022 0.1144  -0.1254 259 LYS E CB  
9805  C CG  . LYS E 259 ? 0.8178 0.9182 0.4532 -0.3877 0.1265  -0.1175 259 LYS E CG  
9806  C CD  . LYS E 259 ? 0.8642 0.8763 0.4538 -0.3742 0.1436  -0.1143 259 LYS E CD  
9807  C CE  . LYS E 259 ? 0.8240 0.8701 0.4508 -0.3626 0.1527  -0.1057 259 LYS E CE  
9808  N NZ  . LYS E 259 ? 0.8743 0.8379 0.4563 -0.3535 0.1677  -0.0999 259 LYS E NZ  
9809  N N   . GLY E 260 ? 0.8132 0.9811 0.4503 -0.3992 0.0804  -0.1372 260 GLY E N   
9810  C CA  . GLY E 260 ? 0.8480 0.9819 0.4484 -0.3983 0.0707  -0.1448 260 GLY E CA  
9811  C C   . GLY E 260 ? 0.7907 0.9481 0.4263 -0.3495 0.0810  -0.1481 260 GLY E C   
9812  O O   . GLY E 260 ? 0.7294 0.9198 0.4129 -0.3165 0.0954  -0.1448 260 GLY E O   
9813  N N   . ASP E 261 ? 0.8158 0.9533 0.4243 -0.3468 0.0723  -0.1540 261 ASP E N   
9814  C CA  . ASP E 261 ? 0.7653 0.9282 0.4066 -0.3042 0.0800  -0.1561 261 ASP E CA  
9815  C C   . ASP E 261 ? 0.6878 0.9632 0.4051 -0.3005 0.0689  -0.1523 261 ASP E C   
9816  O O   . ASP E 261 ? 0.6937 1.0179 0.4200 -0.3306 0.0483  -0.1502 261 ASP E O   
9817  C CB  . ASP E 261 ? 0.8237 0.9251 0.4058 -0.3021 0.0751  -0.1630 261 ASP E CB  
9818  C CG  . ASP E 261 ? 0.8914 0.8797 0.4034 -0.2843 0.0960  -0.1653 261 ASP E CG  
9819  O OD1 . ASP E 261 ? 0.8791 0.8468 0.4012 -0.2661 0.1154  -0.1600 261 ASP E OD1 
9820  O OD2 . ASP E 261 ? 0.9607 0.8797 0.4057 -0.2866 0.0937  -0.1711 261 ASP E OD2 
9821  N N   . SER E 262 ? 0.6203 0.9347 0.3904 -0.2633 0.0824  -0.1498 262 SER E N   
9822  C CA  . SER E 262 ? 0.5518 0.9619 0.3881 -0.2512 0.0764  -0.1464 262 SER E CA  
9823  C C   . SER E 262 ? 0.5040 0.9175 0.3699 -0.2051 0.0898  -0.1472 262 SER E C   
9824  O O   . SER E 262 ? 0.5210 0.8714 0.3630 -0.1853 0.1036  -0.1478 262 SER E O   
9825  C CB  . SER E 262 ? 0.5255 0.9883 0.3968 -0.2661 0.0771  -0.1397 262 SER E CB  
9826  O OG  . SER E 262 ? 0.4643 1.0113 0.3944 -0.2471 0.0763  -0.1358 262 SER E OG  
9827  N N   . THR E 263 ? 0.4489 0.9350 0.3658 -0.1879 0.0862  -0.1453 263 THR E N   
9828  C CA  . THR E 263 ? 0.4062 0.8969 0.3511 -0.1480 0.0959  -0.1452 263 THR E CA  
9829  C C   . THR E 263 ? 0.3539 0.9210 0.3499 -0.1343 0.0933  -0.1424 263 THR E C   
9830  O O   . THR E 263 ? 0.3481 0.9733 0.3607 -0.1488 0.0833  -0.1402 263 THR E O   
9831  C CB  . THR E 263 ? 0.4190 0.8831 0.3457 -0.1317 0.0950  -0.1485 263 THR E CB  
9832  O OG1 . THR E 263 ? 0.3926 0.8372 0.3359 -0.0970 0.1078  -0.1458 263 THR E OG1 
9833  C CG2 . THR E 263 ? 0.4016 0.9272 0.3491 -0.1327 0.0806  -0.1493 263 THR E CG2 
9834  N N   . ILE E 264 ? 0.3211 0.8865 0.3399 -0.1063 0.1022  -0.1409 264 ILE E N   
9835  C CA  . ILE E 264 ? 0.2814 0.9036 0.3377 -0.0875 0.1012  -0.1394 264 ILE E CA  
9836  C C   . ILE E 264 ? 0.2650 0.8927 0.3314 -0.0616 0.0992  -0.1412 264 ILE E C   
9837  O O   . ILE E 264 ? 0.2582 0.8491 0.3241 -0.0416 0.1048  -0.1405 264 ILE E O   
9838  C CB  . ILE E 264 ? 0.2641 0.8772 0.3323 -0.0750 0.1087  -0.1369 264 ILE E CB  
9839  C CG1 . ILE E 264 ? 0.2833 0.8904 0.3392 -0.1007 0.1113  -0.1344 264 ILE E CG1 
9840  C CG2 . ILE E 264 ? 0.2356 0.8966 0.3307 -0.0540 0.1082  -0.1363 264 ILE E CG2 
9841  C CD1 . ILE E 264 ? 0.2784 0.8575 0.3345 -0.0919 0.1177  -0.1314 264 ILE E CD1 
9842  N N   . MET E 265 ? 0.5482 0.8054 0.4186 0.0217  0.1581  -0.0489 265 MET E N   
9843  C CA  . MET E 265 ? 0.5066 0.7841 0.4186 0.0283  0.1542  -0.0602 265 MET E CA  
9844  C C   . MET E 265 ? 0.5008 0.8003 0.4218 0.0287  0.1634  -0.0752 265 MET E C   
9845  O O   . MET E 265 ? 0.5140 0.8266 0.4314 0.0221  0.1760  -0.0783 265 MET E O   
9846  C CB  . MET E 265 ? 0.4941 0.7772 0.4313 0.0197  0.1581  -0.0597 265 MET E CB  
9847  C CG  . MET E 265 ? 0.4604 0.7530 0.4318 0.0318  0.1524  -0.0670 265 MET E CG  
9848  S SD  . MET E 265 ? 0.4499 0.7656 0.4471 0.0212  0.1555  -0.0645 265 MET E SD  
9849  C CE  . MET E 265 ? 0.4755 0.7405 0.4395 0.0071  0.1464  -0.0500 265 MET E CE  
9850  N N   . LYS E 266 ? 0.4910 0.7898 0.4147 0.0336  0.1588  -0.0853 266 LYS E N   
9851  C CA  . LYS E 266 ? 0.5073 0.8035 0.4189 0.0303  0.1702  -0.1011 266 LYS E CA  
9852  C C   . LYS E 266 ? 0.5073 0.7863 0.4314 0.0426  0.1777  -0.1087 266 LYS E C   
9853  O O   . LYS E 266 ? 0.4965 0.7603 0.4277 0.0463  0.1705  -0.1101 266 LYS E O   
9854  C CB  . LYS E 266 ? 0.5171 0.8180 0.4053 0.0187  0.1643  -0.1101 266 LYS E CB  
9855  C CG  . LYS E 266 ? 0.5284 0.8595 0.3959 0.0133  0.1600  -0.1054 266 LYS E CG  
9856  C CD  . LYS E 266 ? 0.5541 0.8834 0.4037 0.0055  0.1750  -0.1116 266 LYS E CD  
9857  C CE  . LYS E 266 ? 0.5709 0.9343 0.3935 -0.0022 0.1711  -0.1111 266 LYS E CE  
9858  N NZ  . LYS E 266 ? 0.5987 0.9581 0.4009 -0.0136 0.1868  -0.1201 266 LYS E NZ  
9859  N N   . SER E 267 ? 0.5247 0.8095 0.4473 0.0534  0.1927  -0.1133 267 SER E N   
9860  C CA  . SER E 267 ? 0.5355 0.8115 0.4624 0.0785  0.2012  -0.1187 267 SER E CA  
9861  C C   . SER E 267 ? 0.5751 0.8523 0.4790 0.0977  0.2208  -0.1276 267 SER E C   
9862  O O   . SER E 267 ? 0.5751 0.8861 0.4828 0.0898  0.2268  -0.1260 267 SER E O   
9863  C CB  . SER E 267 ? 0.5003 0.8176 0.4690 0.0844  0.1941  -0.1081 267 SER E CB  
9864  O OG  . SER E 267 ? 0.5105 0.8360 0.4844 0.1155  0.2012  -0.1123 267 SER E OG  
9865  N N   . GLU E 268 ? 0.6190 0.8526 0.4902 0.1257  0.2321  -0.1368 268 GLU E N   
9866  C CA  . GLU E 268 ? 0.6721 0.8977 0.5093 0.1583  0.2528  -0.1451 268 GLU E CA  
9867  C C   . GLU E 268 ? 0.6549 0.9540 0.5277 0.1954  0.2559  -0.1396 268 GLU E C   
9868  O O   . GLU E 268 ? 0.6903 1.0142 0.5454 0.2289  0.2720  -0.1447 268 GLU E O   
9869  C CB  . GLU E 268 ? 0.7548 0.8789 0.5152 0.1762  0.2674  -0.1577 268 GLU E CB  
9870  C CG  . GLU E 268 ? 0.7795 0.8412 0.4986 0.1300  0.2653  -0.1668 268 GLU E CG  
9871  C CD  . GLU E 268 ? 0.7732 0.8609 0.4906 0.0984  0.2668  -0.1704 268 GLU E CD  
9872  O OE1 . GLU E 268 ? 0.8132 0.8947 0.5029 0.1153  0.2836  -0.1762 268 GLU E OE1 
9873  O OE2 . GLU E 268 ? 0.7321 0.8493 0.4724 0.0610  0.2513  -0.1672 268 GLU E OE2 
9874  N N   . LEU E 269 ? 0.6045 0.9465 0.5247 0.1892  0.2410  -0.1301 269 LEU E N   
9875  C CA  . LEU E 269 ? 0.5864 1.0159 0.5420 0.2170  0.2425  -0.1263 269 LEU E CA  
9876  C C   . LEU E 269 ? 0.5620 1.0855 0.5493 0.1957  0.2465  -0.1245 269 LEU E C   
9877  O O   . LEU E 269 ? 0.5481 1.0613 0.5374 0.1538  0.2431  -0.1216 269 LEU E O   
9878  C CB  . LEU E 269 ? 0.5436 0.9894 0.5357 0.2070  0.2258  -0.1182 269 LEU E CB  
9879  C CG  . LEU E 269 ? 0.5720 0.9435 0.5342 0.2355  0.2237  -0.1199 269 LEU E CG  
9880  C CD1 . LEU E 269 ? 0.5234 0.9030 0.5229 0.2129  0.2051  -0.1118 269 LEU E CD1 
9881  C CD2 . LEU E 269 ? 0.6213 1.0090 0.5570 0.3006  0.2374  -0.1233 269 LEU E CD2 
9882  N N   . GLU E 270 ? 0.5634 1.1832 0.5702 0.2254  0.2544  -0.1264 270 GLU E N   
9883  C CA  . GLU E 270 ? 0.5499 1.2747 0.5813 0.2030  0.2617  -0.1278 270 GLU E CA  
9884  C C   . GLU E 270 ? 0.5073 1.3109 0.5819 0.1594  0.2514  -0.1218 270 GLU E C   
9885  O O   . GLU E 270 ? 0.4887 1.2365 0.5653 0.1139  0.2395  -0.1143 270 GLU E O   
9886  C CB  . GLU E 270 ? 0.5880 1.3854 0.6054 0.2604  0.2802  -0.1366 270 GLU E CB  
9887  C CG  . GLU E 270 ? 0.6235 1.4176 0.6201 0.3353  0.2845  -0.1385 270 GLU E CG  
9888  C CD  . GLU E 270 ? 0.6731 1.5428 0.6461 0.4034  0.3039  -0.1461 270 GLU E CD  
9889  O OE1 . GLU E 270 ? 0.6734 1.6069 0.6528 0.3888  0.3141  -0.1513 270 GLU E OE1 
9890  O OE2 . GLU E 270 ? 0.7193 1.5828 0.6610 0.4768  0.3098  -0.1465 270 GLU E OE2 
9891  N N   . TYR E 271 ? 0.5004 1.4328 0.6019 0.1729  0.2568  -0.1257 271 TYR E N   
9892  C CA  . TYR E 271 ? 0.4729 1.4887 0.6050 0.1176  0.2511  -0.1235 271 TYR E CA  
9893  C C   . TYR E 271 ? 0.4609 1.5912 0.6223 0.1526  0.2494  -0.1267 271 TYR E C   
9894  O O   . TYR E 271 ? 0.4756 1.7101 0.6422 0.2038  0.2603  -0.1337 271 TYR E O   
9895  C CB  . TYR E 271 ? 0.4830 1.5760 0.6136 0.0669  0.2633  -0.1280 271 TYR E CB  
9896  C CG  . TYR E 271 ? 0.4777 1.6325 0.6170 -0.0082 0.2618  -0.1276 271 TYR E CG  
9897  C CD1 . TYR E 271 ? 0.4813 1.5292 0.5999 -0.0574 0.2515  -0.1182 271 TYR E CD1 
9898  C CD2 . TYR E 271 ? 0.4802 1.8007 0.6388 -0.0318 0.2727  -0.1377 271 TYR E CD2 
9899  C CE1 . TYR E 271 ? 0.4986 1.5794 0.6047 -0.1297 0.2537  -0.1186 271 TYR E CE1 
9900  C CE2 . TYR E 271 ? 0.4909 1.8610 0.6434 -0.1133 0.2745  -0.1399 271 TYR E CE2 
9901  C CZ  . TYR E 271 ? 0.5058 1.7440 0.6266 -0.1632 0.2659  -0.1302 271 TYR E CZ  
9902  O OH  . TYR E 271 ? 0.5374 1.8041 0.6330 -0.2473 0.2711  -0.1333 271 TYR E OH  
9903  N N   . GLY E 272 ? 0.4382 1.5532 0.6151 0.1294  0.2360  -0.1214 272 GLY E N   
9904  C CA  . GLY E 272 ? 0.4256 1.6481 0.6299 0.1605  0.2322  -0.1237 272 GLY E CA  
9905  C C   . GLY E 272 ? 0.4148 1.8074 0.6469 0.1106  0.2371  -0.1311 272 GLY E C   
9906  O O   . GLY E 272 ? 0.4059 1.9280 0.6630 0.1411  0.2360  -0.1353 272 GLY E O   
9907  N N   . ASN E 273 ? 0.4239 1.8179 0.6441 0.0321  0.2436  -0.1334 273 ASN E N   
9908  C CA  . ASN E 273 ? 0.4290 1.9665 0.6594 -0.0399 0.2510  -0.1425 273 ASN E CA  
9909  C C   . ASN E 273 ? 0.4169 1.9735 0.6582 -0.0762 0.2403  -0.1415 273 ASN E C   
9910  O O   . ASN E 273 ? 0.4135 2.1338 0.6760 -0.1026 0.2439  -0.1515 273 ASN E O   
9911  C CB  . ASN E 273 ? 0.4294 2.1669 0.6853 -0.0033 0.2636  -0.1548 273 ASN E CB  
9912  C CG  . ASN E 273 ? 0.4504 2.3042 0.6982 -0.0905 0.2786  -0.1662 273 ASN E CG  
9913  O OD1 . ASN E 273 ? 0.4636 2.3766 0.7077 -0.0795 0.2918  -0.1724 273 ASN E OD1 
9914  N ND2 . ASN E 273 ? 0.4633 2.3414 0.6992 -0.1825 0.2785  -0.1700 273 ASN E ND2 
9915  N N   . CYS E 274 ? 0.4129 1.8064 0.6373 -0.0790 0.2276  -0.1304 274 CYS E N   
9916  C CA  . CYS E 274 ? 0.4042 1.7793 0.6327 -0.1064 0.2163  -0.1276 274 CYS E CA  
9917  C C   . CYS E 274 ? 0.4417 1.6899 0.6198 -0.1893 0.2175  -0.1226 274 CYS E C   
9918  O O   . CYS E 274 ? 0.4741 1.6546 0.6152 -0.2195 0.2265  -0.1206 274 CYS E O   
9919  C CB  . CYS E 274 ? 0.3777 1.6608 0.6197 -0.0312 0.2013  -0.1184 274 CYS E CB  
9920  S SG  . CYS E 274 ? 0.3844 1.5017 0.6010 0.0150  0.2003  -0.1102 274 CYS E SG  
9921  N N   . ASN E 275 ? 0.4466 1.6571 0.6150 -0.2216 0.2094  -0.1203 275 ASN E N   
9922  C CA  . ASN E 275 ? 0.4977 1.5628 0.6033 -0.2855 0.2106  -0.1138 275 ASN E CA  
9923  C C   . ASN E 275 ? 0.4784 1.4304 0.5863 -0.2520 0.1936  -0.1035 275 ASN E C   
9924  O O   . ASN E 275 ? 0.4349 1.4480 0.5882 -0.2118 0.1830  -0.1048 275 ASN E O   
9925  C CB  . ASN E 275 ? 0.5518 1.6834 0.6192 -0.3828 0.2240  -0.1246 275 ASN E CB  
9926  C CG  . ASN E 275 ? 0.6359 1.5955 0.6108 -0.4496 0.2312  -0.1179 275 ASN E CG  
9927  O OD1 . ASN E 275 ? 0.6746 1.5219 0.6025 -0.4507 0.2370  -0.1099 275 ASN E OD1 
9928  N ND2 . ASN E 275 ? 0.6745 1.6082 0.6142 -0.5021 0.2319  -0.1210 275 ASN E ND2 
9929  N N   . THR E 276 ? 0.5154 1.3071 0.5706 -0.2645 0.1913  -0.0930 276 THR E N   
9930  C CA  . THR E 276 ? 0.5022 1.1913 0.5547 -0.2353 0.1761  -0.0838 276 THR E CA  
9931  C C   . THR E 276 ? 0.5756 1.1145 0.5461 -0.2747 0.1795  -0.0751 276 THR E C   
9932  O O   . THR E 276 ? 0.6428 1.1370 0.5513 -0.3204 0.1941  -0.0745 276 THR E O   
9933  C CB  . THR E 276 ? 0.4498 1.1029 0.5401 -0.1567 0.1638  -0.0779 276 THR E CB  
9934  O OG1 . THR E 276 ? 0.4309 1.0175 0.5272 -0.1318 0.1492  -0.0720 276 THR E OG1 
9935  C CG2 . THR E 276 ? 0.4731 1.0409 0.5294 -0.1481 0.1677  -0.0717 276 THR E CG2 
9936  N N   . LYS E 277 ? 0.5717 1.0303 0.5346 -0.2534 0.1672  -0.0681 277 LYS E N   
9937  C CA  . LYS E 277 ? 0.6462 0.9526 0.5259 -0.2679 0.1689  -0.0577 277 LYS E CA  
9938  C C   . LYS E 277 ? 0.6165 0.8488 0.5060 -0.2008 0.1545  -0.0470 277 LYS E C   
9939  O O   . LYS E 277 ? 0.6752 0.7917 0.4977 -0.1942 0.1544  -0.0370 277 LYS E O   
9940  C CB  . LYS E 277 ? 0.6864 0.9581 0.5311 -0.3061 0.1693  -0.0596 277 LYS E CB  
9941  C CG  . LYS E 277 ? 0.7830 1.0414 0.5494 -0.3952 0.1902  -0.0671 277 LYS E CG  
9942  C CD  . LYS E 277 ? 0.8673 1.0051 0.5504 -0.4279 0.1940  -0.0642 277 LYS E CD  
9943  C CE  . LYS E 277 ? 0.9362 0.8971 0.5374 -0.3883 0.1929  -0.0481 277 LYS E CE  
9944  N NZ  . LYS E 277 ? 1.0704 0.8882 0.5456 -0.4373 0.2078  -0.0464 277 LYS E NZ  
9945  N N   . CYS E 278 ? 0.5362 0.8366 0.5001 -0.1516 0.1440  -0.0499 278 CYS E N   
9946  C CA  . CYS E 278 ? 0.5069 0.7602 0.4829 -0.0983 0.1318  -0.0438 278 CYS E CA  
9947  C C   . CYS E 278 ? 0.4563 0.7771 0.4833 -0.0672 0.1318  -0.0499 278 CYS E C   
9948  O O   . CYS E 278 ? 0.4162 0.8144 0.4914 -0.0542 0.1309  -0.0572 278 CYS E O   
9949  C CB  . CYS E 278 ? 0.4747 0.7138 0.4745 -0.0742 0.1175  -0.0426 278 CYS E CB  
9950  S SG  . CYS E 278 ? 0.4363 0.6458 0.4550 -0.0190 0.1033  -0.0396 278 CYS E SG  
9951  N N   . GLN E 279 ? 0.4679 0.7558 0.4757 -0.0523 0.1337  -0.0468 279 GLN E N   
9952  C CA  . GLN E 279 ? 0.4376 0.7748 0.4775 -0.0288 0.1374  -0.0535 279 GLN E CA  
9953  C C   . GLN E 279 ? 0.4206 0.7216 0.4624 0.0056  0.1286  -0.0531 279 GLN E C   
9954  O O   . GLN E 279 ? 0.4407 0.6884 0.4500 0.0094  0.1227  -0.0460 279 GLN E O   
9955  C CB  . GLN E 279 ? 0.4709 0.8212 0.4853 -0.0529 0.1513  -0.0540 279 GLN E CB  
9956  C CG  . GLN E 279 ? 0.4479 0.8505 0.4896 -0.0296 0.1578  -0.0619 279 GLN E CG  
9957  C CD  . GLN E 279 ? 0.4220 0.9167 0.5056 -0.0184 0.1627  -0.0709 279 GLN E CD  
9958  O OE1 . GLN E 279 ? 0.4316 0.9890 0.5197 -0.0492 0.1697  -0.0736 279 GLN E OE1 
9959  N NE2 . GLN E 279 ? 0.3999 0.9041 0.5051 0.0256  0.1607  -0.0760 279 GLN E NE2 
9960  N N   . THR E 280 ? 0.3946 0.7263 0.4655 0.0306  0.1294  -0.0614 280 THR E N   
9961  C CA  . THR E 280 ? 0.3911 0.6947 0.4548 0.0508  0.1257  -0.0653 280 THR E CA  
9962  C C   . THR E 280 ? 0.4031 0.7265 0.4640 0.0606  0.1382  -0.0735 280 THR E C   
9963  O O   . THR E 280 ? 0.4051 0.7737 0.4789 0.0631  0.1480  -0.0765 280 THR E O   
9964  C CB  . THR E 280 ? 0.3715 0.6626 0.4496 0.0682  0.1175  -0.0694 280 THR E CB  
9965  O OG1 . THR E 280 ? 0.3737 0.6830 0.4612 0.0886  0.1259  -0.0772 280 THR E OG1 
9966  C CG2 . THR E 280 ? 0.3586 0.6471 0.4487 0.0611  0.1080  -0.0630 280 THR E CG2 
9967  N N   . PRO E 281 ? 0.4157 0.7124 0.4562 0.0655  0.1386  -0.0784 281 PRO E N   
9968  C CA  . PRO E 281 ? 0.4380 0.7367 0.4644 0.0754  0.1519  -0.0881 281 PRO E CA  
9969  C C   . PRO E 281 ? 0.4527 0.7465 0.4783 0.1024  0.1599  -0.0962 281 PRO E C   
9970  O O   . PRO E 281 ? 0.4818 0.7770 0.4894 0.1188  0.1740  -0.1032 281 PRO E O   
9971  C CB  . PRO E 281 ? 0.4510 0.7205 0.4496 0.0666  0.1488  -0.0931 281 PRO E CB  
9972  C CG  . PRO E 281 ? 0.4341 0.7017 0.4353 0.0585  0.1336  -0.0842 281 PRO E CG  
9973  C CD  . PRO E 281 ? 0.4170 0.6892 0.4396 0.0593  0.1279  -0.0745 281 PRO E CD  
9974  N N   . MET E 282 ? 0.4427 0.7244 0.4789 0.1111  0.1519  -0.0947 282 MET E N   
9975  C CA  . MET E 282 ? 0.4671 0.7365 0.4930 0.1438  0.1590  -0.0995 282 MET E CA  
9976  C C   . MET E 282 ? 0.4500 0.7917 0.5083 0.1621  0.1612  -0.0952 282 MET E C   
9977  O O   . MET E 282 ? 0.4781 0.8340 0.5240 0.2012  0.1714  -0.0988 282 MET E O   
9978  C CB  . MET E 282 ? 0.4655 0.6942 0.4865 0.1428  0.1490  -0.0993 282 MET E CB  
9979  C CG  . MET E 282 ? 0.4795 0.6607 0.4720 0.1171  0.1452  -0.1053 282 MET E CG  
9980  S SD  . MET E 282 ? 0.5640 0.6605 0.4814 0.1241  0.1630  -0.1201 282 MET E SD  
9981  C CE  . MET E 282 ? 0.5771 0.6377 0.4862 0.1450  0.1594  -0.1178 282 MET E CE  
9982  N N   . GLY E 283 ? 0.4132 0.8006 0.5044 0.1341  0.1526  -0.0880 283 GLY E N   
9983  C CA  . GLY E 283 ? 0.3970 0.8668 0.5182 0.1354  0.1538  -0.0858 283 GLY E CA  
9984  C C   . GLY E 283 ? 0.3729 0.8509 0.5105 0.0956  0.1430  -0.0788 283 GLY E C   
9985  O O   . GLY E 283 ? 0.3709 0.7886 0.4947 0.0769  0.1348  -0.0742 283 GLY E O   
9986  N N   . ALA E 284 ? 0.3630 0.9178 0.5228 0.0836  0.1442  -0.0788 284 ALA E N   
9987  C CA  . ALA E 284 ? 0.3593 0.9139 0.5192 0.0384  0.1382  -0.0739 284 ALA E CA  
9988  C C   . ALA E 284 ? 0.3406 0.8850 0.5153 0.0469  0.1264  -0.0716 284 ALA E C   
9989  O O   . ALA E 284 ? 0.3296 0.8942 0.5195 0.0869  0.1243  -0.0740 284 ALA E O   
9990  C CB  . ALA E 284 ? 0.3702 1.0178 0.5365 0.0038  0.1484  -0.0779 284 ALA E CB  
9991  N N   . ILE E 285 ? 0.3475 0.8521 0.5079 0.0113  0.1201  -0.0666 285 ILE E N   
9992  C CA  . ILE E 285 ? 0.3326 0.8198 0.5029 0.0140  0.1087  -0.0642 285 ILE E CA  
9993  C C   . ILE E 285 ? 0.3469 0.8766 0.5135 -0.0310 0.1107  -0.0653 285 ILE E C   
9994  O O   . ILE E 285 ? 0.3857 0.8920 0.5160 -0.0763 0.1185  -0.0642 285 ILE E O   
9995  C CB  . ILE E 285 ? 0.3356 0.7256 0.4830 0.0187  0.0990  -0.0582 285 ILE E CB  
9996  C CG1 . ILE E 285 ? 0.3165 0.6838 0.4743 0.0586  0.0942  -0.0609 285 ILE E CG1 
9997  C CG2 . ILE E 285 ? 0.3394 0.7018 0.4792 0.0012  0.0907  -0.0545 285 ILE E CG2 
9998  C CD1 . ILE E 285 ? 0.3215 0.6237 0.4564 0.0613  0.0880  -0.0583 285 ILE E CD1 
9999  N N   . ASN E 286 ? 0.3251 0.9123 0.5203 -0.0205 0.1051  -0.0679 286 ASN E N   
10000 C CA  . ASN E 286 ? 0.3386 0.9717 0.5301 -0.0663 0.1058  -0.0709 286 ASN E CA  
10001 C C   . ASN E 286 ? 0.3179 0.9283 0.5232 -0.0493 0.0928  -0.0683 286 ASN E C   
10002 O O   . ASN E 286 ? 0.2909 0.9724 0.5303 -0.0167 0.0881  -0.0706 286 ASN E O   
10003 C CB  . ASN E 286 ? 0.3325 1.1127 0.5515 -0.0750 0.1142  -0.0797 286 ASN E CB  
10004 C CG  . ASN E 286 ? 0.3496 1.1970 0.5632 -0.1316 0.1159  -0.0859 286 ASN E CG  
10005 O OD1 . ASN E 286 ? 0.3901 1.1565 0.5589 -0.1835 0.1178  -0.0846 286 ASN E OD1 
10006 N ND2 . ASN E 286 ? 0.3286 1.3251 0.5799 -0.1205 0.1164  -0.0932 286 ASN E ND2 
10007 N N   . SER E 287 ? 0.3369 0.8469 0.5100 -0.0660 0.0876  -0.0630 287 SER E N   
10008 C CA  . SER E 287 ? 0.3205 0.8062 0.5032 -0.0545 0.0758  -0.0610 287 SER E CA  
10009 C C   . SER E 287 ? 0.3630 0.7554 0.4957 -0.0881 0.0751  -0.0572 287 SER E C   
10010 O O   . SER E 287 ? 0.4088 0.7293 0.4922 -0.1057 0.0823  -0.0535 287 SER E O   
10011 C CB  . SER E 287 ? 0.2870 0.7381 0.4906 0.0004  0.0664  -0.0579 287 SER E CB  
10012 O OG  . SER E 287 ? 0.2988 0.6594 0.4747 0.0057  0.0634  -0.0532 287 SER E OG  
10013 N N   . SER E 288 ? 0.3559 0.7452 0.4943 -0.0917 0.0672  -0.0576 288 SER E N   
10014 C CA  . SER E 288 ? 0.4033 0.6986 0.4886 -0.1150 0.0668  -0.0543 288 SER E CA  
10015 C C   . SER E 288 ? 0.3805 0.6114 0.4702 -0.0693 0.0544  -0.0481 288 SER E C   
10016 O O   . SER E 288 ? 0.4175 0.5731 0.4647 -0.0736 0.0526  -0.0447 288 SER E O   
10017 C CB  . SER E 288 ? 0.4178 0.7548 0.5001 -0.1557 0.0675  -0.0605 288 SER E CB  
10018 O OG  . SER E 288 ? 0.3577 0.8076 0.5062 -0.1326 0.0597  -0.0645 288 SER E OG  
10019 N N   . MET E 289 ? 0.3295 0.5890 0.4619 -0.0275 0.0477  -0.0478 289 MET E N   
10020 C CA  . MET E 289 ? 0.3086 0.5261 0.4456 0.0071  0.0373  -0.0450 289 MET E CA  
10021 C C   . MET E 289 ? 0.3461 0.4916 0.4348 0.0135  0.0389  -0.0395 289 MET E C   
10022 O O   . MET E 289 ? 0.3783 0.5070 0.4389 0.0027  0.0480  -0.0373 289 MET E O   
10023 C CB  . MET E 289 ? 0.2702 0.5210 0.4425 0.0389  0.0348  -0.0478 289 MET E CB  
10024 C CG  . MET E 289 ? 0.2465 0.5600 0.4538 0.0507  0.0344  -0.0514 289 MET E CG  
10025 S SD  . MET E 289 ? 0.2316 0.5453 0.4524 0.0563  0.0233  -0.0511 289 MET E SD  
10026 C CE  . MET E 289 ? 0.2190 0.5683 0.4590 0.0972  0.0244  -0.0531 289 MET E CE  
10027 N N   . PRO E 290 ? 0.3459 0.4544 0.4215 0.0350  0.0304  -0.0370 290 PRO E N   
10028 C CA  . PRO E 290 ? 0.3822 0.4401 0.4115 0.0561  0.0307  -0.0312 290 PRO E CA  
10029 C C   . PRO E 290 ? 0.3518 0.4429 0.4015 0.0775  0.0287  -0.0332 290 PRO E C   
10030 O O   . PRO E 290 ? 0.3843 0.4511 0.3968 0.0935  0.0307  -0.0284 290 PRO E O   
10031 C CB  . PRO E 290 ? 0.3861 0.4209 0.4035 0.0762  0.0216  -0.0299 290 PRO E CB  
10032 C CG  . PRO E 290 ? 0.3279 0.4139 0.4029 0.0712  0.0141  -0.0365 290 PRO E CG  
10033 C CD  . PRO E 290 ? 0.3197 0.4365 0.4168 0.0427  0.0207  -0.0390 290 PRO E CD  
10034 N N   . PHE E 291 ? 0.3011 0.4414 0.3990 0.0784  0.0259  -0.0402 291 PHE E N   
10035 C CA  . PHE E 291 ? 0.2818 0.4468 0.3904 0.0903  0.0259  -0.0450 291 PHE E CA  
10036 C C   . PHE E 291 ? 0.2652 0.4559 0.3973 0.0833  0.0336  -0.0500 291 PHE E C   
10037 O O   . PHE E 291 ? 0.2568 0.4645 0.4081 0.0768  0.0361  -0.0506 291 PHE E O   
10038 C CB  . PHE E 291 ? 0.2587 0.4408 0.3809 0.0994  0.0175  -0.0512 291 PHE E CB  
10039 C CG  . PHE E 291 ? 0.2713 0.4500 0.3715 0.1155  0.0097  -0.0484 291 PHE E CG  
10040 C CD1 . PHE E 291 ? 0.2884 0.4831 0.3645 0.1315  0.0089  -0.0474 291 PHE E CD1 
10041 C CD2 . PHE E 291 ? 0.2693 0.4367 0.3707 0.1192  0.0031  -0.0471 291 PHE E CD2 
10042 C CE1 . PHE E 291 ? 0.3055 0.5111 0.3573 0.1572  0.0018  -0.0446 291 PHE E CE1 
10043 C CE2 . PHE E 291 ? 0.2866 0.4560 0.3634 0.1417  -0.0032 -0.0448 291 PHE E CE2 
10044 C CZ  . PHE E 291 ? 0.3058 0.4976 0.3571 0.1638  -0.0038 -0.0434 291 PHE E CZ  
10045 N N   . HIS E 292 ? 0.2647 0.4635 0.3913 0.0878  0.0377  -0.0541 292 HIS E N   
10046 C CA  . HIS E 292 ? 0.2606 0.4725 0.3975 0.0888  0.0463  -0.0603 292 HIS E CA  
10047 C C   . HIS E 292 ? 0.2676 0.4753 0.3879 0.0889  0.0484  -0.0685 292 HIS E C   
10048 O O   . HIS E 292 ? 0.2681 0.4836 0.3762 0.0873  0.0425  -0.0691 292 HIS E O   
10049 C CB  . HIS E 292 ? 0.2716 0.4973 0.4080 0.0826  0.0557  -0.0573 292 HIS E CB  
10050 C CG  . HIS E 292 ? 0.2884 0.5050 0.4017 0.0796  0.0588  -0.0555 292 HIS E CG  
10051 N ND1 . HIS E 292 ? 0.2946 0.5194 0.4023 0.0816  0.0667  -0.0610 292 HIS E ND1 
10052 C CD2 . HIS E 292 ? 0.3094 0.5050 0.3955 0.0790  0.0558  -0.0482 292 HIS E CD2 
10053 C CE1 . HIS E 292 ? 0.3106 0.5299 0.3964 0.0796  0.0670  -0.0574 292 HIS E CE1 
10054 N NE2 . HIS E 292 ? 0.3227 0.5226 0.3923 0.0813  0.0606  -0.0489 292 HIS E NE2 
10055 N N   . ASN E 293 ? 0.2820 0.4794 0.3938 0.0914  0.0581  -0.0756 293 ASN E N   
10056 C CA  . ASN E 293 ? 0.3055 0.4882 0.3872 0.0809  0.0640  -0.0862 293 ASN E CA  
10057 C C   . ASN E 293 ? 0.3336 0.5031 0.3962 0.0842  0.0782  -0.0908 293 ASN E C   
10058 O O   . ASN E 293 ? 0.3728 0.5088 0.3969 0.0756  0.0881  -0.1014 293 ASN E O   
10059 C CB  . ASN E 293 ? 0.3244 0.4761 0.3858 0.0749  0.0648  -0.0939 293 ASN E CB  
10060 C CG  . ASN E 293 ? 0.3516 0.4664 0.4005 0.0952  0.0740  -0.0933 293 ASN E CG  
10061 O OD1 . ASN E 293 ? 0.3396 0.4758 0.4116 0.1156  0.0757  -0.0862 293 ASN E OD1 
10062 N ND2 . ASN E 293 ? 0.3980 0.4591 0.4023 0.0904  0.0814  -0.1012 293 ASN E ND2 
10063 N N   . ILE E 294 ? 0.3225 0.5145 0.4037 0.0928  0.0808  -0.0838 294 ILE E N   
10064 C CA  . ILE E 294 ? 0.3469 0.5362 0.4144 0.1007  0.0945  -0.0874 294 ILE E CA  
10065 C C   . ILE E 294 ? 0.3615 0.5492 0.4063 0.0848  0.0985  -0.0929 294 ILE E C   
10066 O O   . ILE E 294 ? 0.4005 0.5579 0.4094 0.0806  0.1098  -0.1032 294 ILE E O   
10067 C CB  . ILE E 294 ? 0.3305 0.5608 0.4260 0.1084  0.0967  -0.0796 294 ILE E CB  
10068 C CG1 . ILE E 294 ? 0.3153 0.5668 0.4347 0.1203  0.0922  -0.0753 294 ILE E CG1 
10069 C CG2 . ILE E 294 ? 0.3561 0.5945 0.4384 0.1210  0.1114  -0.0840 294 ILE E CG2 
10070 C CD1 . ILE E 294 ? 0.3406 0.5645 0.4416 0.1460  0.0968  -0.0798 294 ILE E CD1 
10071 N N   . HIS E 295 ? 0.3416 0.5564 0.3979 0.0771  0.0906  -0.0860 295 HIS E N   
10072 C CA  . HIS E 295 ? 0.3543 0.5811 0.3909 0.0670  0.0931  -0.0892 295 HIS E CA  
10073 C C   . HIS E 295 ? 0.3419 0.5910 0.3803 0.0698  0.0813  -0.0791 295 HIS E C   
10074 O O   . HIS E 295 ? 0.3364 0.5777 0.3839 0.0767  0.0778  -0.0682 295 HIS E O   
10075 C CB  . HIS E 295 ? 0.3692 0.5970 0.4024 0.0707  0.1055  -0.0890 295 HIS E CB  
10076 C CG  . HIS E 295 ? 0.3919 0.6232 0.3981 0.0595  0.1121  -0.0963 295 HIS E CG  
10077 N ND1 . HIS E 295 ? 0.3889 0.6459 0.3889 0.0553  0.1060  -0.0909 295 HIS E ND1 
10078 C CD2 . HIS E 295 ? 0.4272 0.6356 0.4028 0.0528  0.1253  -0.1088 295 HIS E CD2 
10079 C CE1 . HIS E 295 ? 0.4113 0.6746 0.3869 0.0436  0.1135  -0.1002 295 HIS E CE1 
10080 N NE2 . HIS E 295 ? 0.4363 0.6665 0.3953 0.0387  0.1259  -0.1119 295 HIS E NE2 
10081 N N   . PRO E 296 ? 0.3482 0.6248 0.3685 0.0655  0.0765  -0.0834 296 PRO E N   
10082 C CA  . PRO E 296 ? 0.3500 0.6487 0.3599 0.0824  0.0657  -0.0728 296 PRO E CA  
10083 C C   . PRO E 296 ? 0.3726 0.6501 0.3649 0.0938  0.0695  -0.0597 296 PRO E C   
10084 O O   . PRO E 296 ? 0.3898 0.6414 0.3654 0.1093  0.0652  -0.0472 296 PRO E O   
10085 C CB  . PRO E 296 ? 0.3558 0.7106 0.3488 0.0753  0.0622  -0.0830 296 PRO E CB  
10086 C CG  . PRO E 296 ? 0.3676 0.7131 0.3532 0.0473  0.0748  -0.0979 296 PRO E CG  
10087 C CD  . PRO E 296 ? 0.3644 0.6557 0.3639 0.0447  0.0818  -0.0992 296 PRO E CD  
10088 N N   . LEU E 297 ? 0.3838 0.6636 0.3696 0.0840  0.0793  -0.0630 297 LEU E N   
10089 C CA  . LEU E 297 ? 0.4132 0.6721 0.3750 0.0887  0.0850  -0.0520 297 LEU E CA  
10090 C C   . LEU E 297 ? 0.4165 0.6434 0.3887 0.0765  0.0931  -0.0473 297 LEU E C   
10091 O O   . LEU E 297 ? 0.4051 0.6435 0.3982 0.0645  0.1026  -0.0545 297 LEU E O   
10092 C CB  . LEU E 297 ? 0.4235 0.7045 0.3749 0.0803  0.0929  -0.0586 297 LEU E CB  
10093 C CG  . LEU E 297 ? 0.4239 0.7554 0.3629 0.0822  0.0866  -0.0669 297 LEU E CG  
10094 C CD1 . LEU E 297 ? 0.4348 0.7820 0.3649 0.0644  0.0971  -0.0774 297 LEU E CD1 
10095 C CD2 . LEU E 297 ? 0.4478 0.7979 0.3552 0.1124  0.0764  -0.0541 297 LEU E CD2 
10096 N N   . THR E 298 ? 0.4405 0.6305 0.3910 0.0796  0.0907  -0.0360 298 THR E N   
10097 C CA  . THR E 298 ? 0.4529 0.6222 0.4046 0.0574  0.0993  -0.0331 298 THR E CA  
10098 C C   . THR E 298 ? 0.5206 0.6342 0.4095 0.0493  0.1067  -0.0210 298 THR E C   
10099 O O   . THR E 298 ? 0.5606 0.6414 0.4016 0.0727  0.1033  -0.0120 298 THR E O   
10100 C CB  . THR E 298 ? 0.4327 0.5974 0.4065 0.0543  0.0932  -0.0338 298 THR E CB  
10101 O OG1 . THR E 298 ? 0.4693 0.5846 0.4010 0.0663  0.0871  -0.0239 298 THR E OG1 
10102 C CG2 . THR E 298 ? 0.3834 0.5837 0.4007 0.0657  0.0860  -0.0439 298 THR E CG2 
10103 N N   . ILE E 299 ? 0.5420 0.6476 0.4239 0.0160  0.1183  -0.0213 299 ILE E N   
10104 C CA  . ILE E 299 ? 0.6252 0.6630 0.4325 -0.0058 0.1299  -0.0117 299 ILE E CA  
10105 C C   . ILE E 299 ? 0.6473 0.6695 0.4454 -0.0439 0.1361  -0.0136 299 ILE E C   
10106 O O   . ILE E 299 ? 0.5936 0.6879 0.4523 -0.0605 0.1362  -0.0238 299 ILE E O   
10107 C CB  . ILE E 299 ? 0.6438 0.6984 0.4390 -0.0241 0.1425  -0.0133 299 ILE E CB  
10108 C CG1 . ILE E 299 ? 0.7430 0.7198 0.4501 -0.0593 0.1584  -0.0048 299 ILE E CG1 
10109 C CG2 . ILE E 299 ? 0.5825 0.7267 0.4478 -0.0410 0.1472  -0.0268 299 ILE E CG2 
10110 C CD1 . ILE E 299 ? 0.8244 0.7118 0.4436 -0.0303 0.1595  0.0099  299 ILE E CD1 
10111 N N   . GLY E 300 ? 0.7361 0.6622 0.4499 -0.0549 0.1421  -0.0040 300 GLY E N   
10112 C CA  . GLY E 300 ? 0.7796 0.6770 0.4637 -0.1020 0.1511  -0.0068 300 GLY E CA  
10113 C C   . GLY E 300 ? 0.7798 0.6408 0.4594 -0.0824 0.1406  -0.0042 300 GLY E C   
10114 O O   . GLY E 300 ? 0.7672 0.6083 0.4464 -0.0307 0.1282  0.0021  300 GLY E O   
10115 N N   . GLU E 301 ? 0.7956 0.6589 0.4715 -0.1261 0.1460  -0.0103 301 GLU E N   
10116 C CA  . GLU E 301 ? 0.7984 0.6285 0.4690 -0.1149 0.1376  -0.0092 301 GLU E CA  
10117 C C   . GLU E 301 ? 0.6785 0.6165 0.4612 -0.0881 0.1204  -0.0170 301 GLU E C   
10118 O O   . GLU E 301 ? 0.6307 0.6512 0.4696 -0.1151 0.1208  -0.0267 301 GLU E O   
10119 C CB  . GLU E 301 ? 0.8726 0.6614 0.4856 -0.1806 0.1521  -0.0142 301 GLU E CB  
10120 C CG  . GLU E 301 ? 0.9047 0.6288 0.4842 -0.1732 0.1473  -0.0120 301 GLU E CG  
10121 C CD  . GLU E 301 ? 1.0165 0.5900 0.4808 -0.1365 0.1521  0.0020  301 GLU E CD  
10122 O OE1 . GLU E 301 ? 1.0755 0.5912 0.4803 -0.1168 0.1593  0.0111  301 GLU E OE1 
10123 O OE2 . GLU E 301 ? 1.0519 0.5645 0.4800 -0.1224 0.1491  0.0045  301 GLU E OE2 
10124 N N   . CYS E 302 ? 0.6400 0.5783 0.4464 -0.0348 0.1063  -0.0128 302 CYS E N   
10125 C CA  . CYS E 302 ? 0.5430 0.5662 0.4387 -0.0106 0.0926  -0.0203 302 CYS E CA  
10126 C C   . CYS E 302 ? 0.5261 0.5315 0.4282 0.0175  0.0796  -0.0184 302 CYS E C   
10127 O O   . CYS E 302 ? 0.5821 0.5178 0.4233 0.0381  0.0786  -0.0100 302 CYS E O   
10128 C CB  . CYS E 302 ? 0.5073 0.5682 0.4307 0.0166  0.0894  -0.0217 302 CYS E CB  
10129 S SG  . CYS E 302 ? 0.5120 0.6121 0.4429 -0.0101 0.1037  -0.0260 302 CYS E SG  
10130 N N   . PRO E 303 ? 0.4561 0.5229 0.4253 0.0226  0.0706  -0.0259 303 PRO E N   
10131 C CA  . PRO E 303 ? 0.4315 0.4949 0.4139 0.0503  0.0578  -0.0257 303 PRO E CA  
10132 C C   . PRO E 303 ? 0.4153 0.4952 0.4003 0.0833  0.0513  -0.0256 303 PRO E C   
10133 O O   . PRO E 303 ? 0.4145 0.5119 0.4004 0.0835  0.0562  -0.0266 303 PRO E O   
10134 C CB  . PRO E 303 ? 0.3715 0.4934 0.4169 0.0436  0.0529  -0.0340 303 PRO E CB  
10135 C CG  . PRO E 303 ? 0.3552 0.5251 0.4270 0.0299  0.0615  -0.0388 303 PRO E CG  
10136 C CD  . PRO E 303 ? 0.4079 0.5484 0.4344 0.0066  0.0731  -0.0345 303 PRO E CD  
10137 N N   . LYS E 304 ? 0.4045 0.4881 0.3893 0.1081  0.0409  -0.0254 304 LYS E N   
10138 C CA  . LYS E 304 ? 0.3938 0.5127 0.3769 0.1345  0.0347  -0.0272 304 LYS E CA  
10139 C C   . LYS E 304 ? 0.3373 0.5140 0.3713 0.1227  0.0326  -0.0396 304 LYS E C   
10140 O O   . LYS E 304 ? 0.3073 0.4925 0.3735 0.1107  0.0308  -0.0453 304 LYS E O   
10141 C CB  . LYS E 304 ? 0.4114 0.5276 0.3698 0.1661  0.0254  -0.0236 304 LYS E CB  
10142 C CG  . LYS E 304 ? 0.4916 0.5263 0.3764 0.1854  0.0303  -0.0107 304 LYS E CG  
10143 C CD  . LYS E 304 ? 0.5522 0.5593 0.3777 0.2095  0.0363  -0.0015 304 LYS E CD  
10144 C CE  . LYS E 304 ? 0.6409 0.5405 0.3913 0.1953  0.0508  0.0085  304 LYS E CE  
10145 N NZ  . LYS E 304 ? 0.7370 0.5739 0.3927 0.2405  0.0560  0.0220  304 LYS E NZ  
10146 N N   . TYR E 305 ? 0.3342 0.5425 0.3645 0.1258  0.0342  -0.0438 305 TYR E N   
10147 C CA  . TYR E 305 ? 0.3045 0.5478 0.3610 0.1096  0.0362  -0.0568 305 TYR E CA  
10148 C C   . TYR E 305 ? 0.2900 0.5735 0.3499 0.1104  0.0278  -0.0653 305 TYR E C   
10149 O O   . TYR E 305 ? 0.2996 0.6187 0.3417 0.1293  0.0208  -0.0631 305 TYR E O   
10150 C CB  . TYR E 305 ? 0.3157 0.5750 0.3605 0.1044  0.0435  -0.0602 305 TYR E CB  
10151 C CG  . TYR E 305 ? 0.3070 0.5862 0.3584 0.0844  0.0484  -0.0752 305 TYR E CG  
10152 C CD1 . TYR E 305 ? 0.3068 0.5569 0.3684 0.0739  0.0578  -0.0805 305 TYR E CD1 
10153 C CD2 . TYR E 305 ? 0.3111 0.6376 0.3482 0.0760  0.0454  -0.0850 305 TYR E CD2 
10154 C CE1 . TYR E 305 ? 0.3242 0.5657 0.3690 0.0571  0.0660  -0.0941 305 TYR E CE1 
10155 C CE2 . TYR E 305 ? 0.3229 0.6519 0.3482 0.0471  0.0535  -0.1009 305 TYR E CE2 
10156 C CZ  . TYR E 305 ? 0.3359 0.6092 0.3590 0.0384  0.0648  -0.1049 305 TYR E CZ  
10157 O OH  . TYR E 305 ? 0.3719 0.6215 0.3613 0.0115  0.0764  -0.1204 305 TYR E OH  
10158 N N   . VAL E 306 ? 0.2743 0.5544 0.3504 0.0915  0.0297  -0.0751 306 VAL E N   
10159 C CA  . VAL E 306 ? 0.2693 0.5864 0.3412 0.0776  0.0256  -0.0870 306 VAL E CA  
10160 C C   . VAL E 306 ? 0.2861 0.5817 0.3449 0.0480  0.0370  -0.1005 306 VAL E C   
10161 O O   . VAL E 306 ? 0.2955 0.5444 0.3553 0.0498  0.0458  -0.0986 306 VAL E O   
10162 C CB  . VAL E 306 ? 0.2543 0.5674 0.3389 0.0840  0.0171  -0.0847 306 VAL E CB  
10163 C CG1 . VAL E 306 ? 0.2567 0.5899 0.3340 0.1152  0.0075  -0.0743 306 VAL E CG1 
10164 C CG2 . VAL E 306 ? 0.2477 0.5069 0.3493 0.0838  0.0202  -0.0794 306 VAL E CG2 
10165 N N   . LYS E 307 ? 0.3005 0.6303 0.3379 0.0208  0.0382  -0.1150 307 LYS E N   
10166 C CA  . LYS E 307 ? 0.3425 0.6314 0.3427 -0.0141 0.0526  -0.1299 307 LYS E CA  
10167 C C   . LYS E 307 ? 0.3619 0.5925 0.3479 -0.0234 0.0566  -0.1331 307 LYS E C   
10168 O O   . LYS E 307 ? 0.4180 0.5953 0.3533 -0.0524 0.0707  -0.1455 307 LYS E O   
10169 C CB  . LYS E 307 ? 0.3652 0.7158 0.3344 -0.0528 0.0553  -0.1471 307 LYS E CB  
10170 C CG  . LYS E 307 ? 0.3653 0.7624 0.3318 -0.0501 0.0563  -0.1475 307 LYS E CG  
10171 C CD  . LYS E 307 ? 0.4001 0.8557 0.3266 -0.1006 0.0628  -0.1689 307 LYS E CD  
10172 C CE  . LYS E 307 ? 0.3907 0.9296 0.3215 -0.0923 0.0584  -0.1686 307 LYS E CE  
10173 N NZ  . LYS E 307 ? 0.4260 1.0407 0.3171 -0.1487 0.0649  -0.1919 307 LYS E NZ  
10174 N N   . SER E 308 ? 0.3280 0.5590 0.3478 0.0001  0.0458  -0.1221 308 SER E N   
10175 C CA  . SER E 308 ? 0.3451 0.5281 0.3520 -0.0055 0.0479  -0.1240 308 SER E CA  
10176 C C   . SER E 308 ? 0.3798 0.4849 0.3669 0.0109  0.0600  -0.1202 308 SER E C   
10177 O O   . SER E 308 ? 0.3667 0.4719 0.3740 0.0352  0.0618  -0.1118 308 SER E O   
10178 C CB  . SER E 308 ? 0.2997 0.5089 0.3482 0.0163  0.0329  -0.1132 308 SER E CB  
10179 O OG  . SER E 308 ? 0.2711 0.5519 0.3374 0.0222  0.0218  -0.1119 308 SER E OG  
10180 N N   . ASN E 309 ? 0.4322 0.4728 0.3726 -0.0002 0.0692  -0.1264 309 ASN E N   
10181 C CA  . ASN E 309 ? 0.4730 0.4417 0.3881 0.0303  0.0793  -0.1204 309 ASN E CA  
10182 C C   . ASN E 309 ? 0.4321 0.4171 0.3905 0.0594  0.0673  -0.1080 309 ASN E C   
10183 O O   . ASN E 309 ? 0.4416 0.4093 0.4036 0.0956  0.0706  -0.0995 309 ASN E O   
10184 C CB  . ASN E 309 ? 0.5744 0.4438 0.3956 0.0092  0.0983  -0.1321 309 ASN E CB  
10185 C CG  . ASN E 309 ? 0.6374 0.4682 0.3992 -0.0160 0.1156  -0.1447 309 ASN E CG  
10186 O OD1 . ASN E 309 ? 0.6296 0.4688 0.4057 0.0083  0.1193  -0.1403 309 ASN E OD1 
10187 N ND2 . ASN E 309 ? 0.7066 0.4960 0.3961 -0.0705 0.1275  -0.1618 309 ASN E ND2 
10188 N N   . ARG E 310 ? 0.3895 0.4164 0.3785 0.0448  0.0537  -0.1076 310 ARG E N   
10189 C CA  . ARG E 310 ? 0.3601 0.3953 0.3800 0.0643  0.0433  -0.0983 310 ARG E CA  
10190 C C   . ARG E 310 ? 0.3010 0.3984 0.3665 0.0561  0.0272  -0.0957 310 ARG E C   
10191 O O   . ARG E 310 ? 0.3012 0.4218 0.3554 0.0311  0.0245  -0.1044 310 ARG E O   
10192 C CB  . ARG E 310 ? 0.4203 0.3867 0.3851 0.0582  0.0512  -0.1028 310 ARG E CB  
10193 C CG  . ARG E 310 ? 0.4064 0.3706 0.3920 0.0868  0.0436  -0.0923 310 ARG E CG  
10194 C CD  . ARG E 310 ? 0.4775 0.3636 0.3965 0.0808  0.0523  -0.0962 310 ARG E CD  
10195 N NE  . ARG E 310 ? 0.4460 0.3536 0.3959 0.0924  0.0399  -0.0889 310 ARG E NE  
10196 C CZ  . ARG E 310 ? 0.4429 0.3555 0.4078 0.1330  0.0366  -0.0777 310 ARG E CZ  
10197 N NH1 . ARG E 310 ? 0.4698 0.3745 0.4225 0.1716  0.0446  -0.0720 310 ARG E NH1 
10198 N NH2 . ARG E 310 ? 0.4141 0.3500 0.4054 0.1360  0.0251  -0.0729 310 ARG E NH2 
10199 N N   . LEU E 311 ? 0.2596 0.3851 0.3683 0.0767  0.0182  -0.0847 311 LEU E N   
10200 C CA  . LEU E 311 ? 0.2230 0.3835 0.3590 0.0764  0.0054  -0.0808 311 LEU E CA  
10201 C C   . LEU E 311 ? 0.2071 0.3642 0.3654 0.0892  -0.0004 -0.0727 311 LEU E C   
10202 O O   . LEU E 311 ? 0.1975 0.3662 0.3740 0.0981  -0.0001 -0.0659 311 LEU E O   
10203 C CB  . LEU E 311 ? 0.2073 0.3967 0.3550 0.0821  0.0023  -0.0764 311 LEU E CB  
10204 C CG  . LEU E 311 ? 0.2159 0.4315 0.3463 0.0730  0.0047  -0.0835 311 LEU E CG  
10205 C CD1 . LEU E 311 ? 0.2115 0.4421 0.3455 0.0884  0.0026  -0.0754 311 LEU E CD1 
10206 C CD2 . LEU E 311 ? 0.2145 0.4662 0.3351 0.0607  -0.0009 -0.0922 311 LEU E CD2 
10207 N N   . VAL E 312 ? 0.2075 0.3548 0.3613 0.0852  -0.0049 -0.0747 312 VAL E N   
10208 C CA  . VAL E 312 ? 0.1945 0.3437 0.3669 0.0951  -0.0109 -0.0682 312 VAL E CA  
10209 C C   . VAL E 312 ? 0.1759 0.3374 0.3567 0.0881  -0.0210 -0.0688 312 VAL E C   
10210 O O   . VAL E 312 ? 0.1824 0.3433 0.3481 0.0769  -0.0222 -0.0757 312 VAL E O   
10211 C CB  . VAL E 312 ? 0.2254 0.3418 0.3754 0.1057  -0.0056 -0.0683 312 VAL E CB  
10212 C CG1 . VAL E 312 ? 0.2109 0.3466 0.3831 0.1189  -0.0126 -0.0613 312 VAL E CG1 
10213 C CG2 . VAL E 312 ? 0.2586 0.3542 0.3860 0.1210  0.0066  -0.0684 312 VAL E CG2 
10214 N N   . LEU E 313 ? 0.1609 0.3331 0.3586 0.0916  -0.0265 -0.0627 313 LEU E N   
10215 C CA  . LEU E 313 ? 0.1537 0.3279 0.3517 0.0904  -0.0345 -0.0625 313 LEU E CA  
10216 C C   . LEU E 313 ? 0.1483 0.3197 0.3565 0.0887  -0.0389 -0.0607 313 LEU E C   
10217 O O   . LEU E 313 ? 0.1477 0.3278 0.3677 0.0898  -0.0376 -0.0566 313 LEU E O   
10218 C CB  . LEU E 313 ? 0.1644 0.3292 0.3533 0.0933  -0.0347 -0.0573 313 LEU E CB  
10219 C CG  . LEU E 313 ? 0.1784 0.3439 0.3462 0.1047  -0.0329 -0.0574 313 LEU E CG  
10220 C CD1 . LEU E 313 ? 0.2123 0.3426 0.3525 0.1076  -0.0286 -0.0505 313 LEU E CD1 
10221 C CD2 . LEU E 313 ? 0.1769 0.3645 0.3352 0.1164  -0.0390 -0.0620 313 LEU E CD2 
10222 N N   . ALA E 314 ? 0.1452 0.3155 0.3486 0.0859  -0.0442 -0.0644 314 ALA E N   
10223 C CA  . ALA E 314 ? 0.1413 0.3092 0.3522 0.0847  -0.0496 -0.0624 314 ALA E CA  
10224 C C   . ALA E 314 ? 0.1410 0.3094 0.3559 0.0816  -0.0531 -0.0588 314 ALA E C   
10225 O O   . ALA E 314 ? 0.1516 0.3090 0.3506 0.0850  -0.0536 -0.0594 314 ALA E O   
10226 C CB  . ALA E 314 ? 0.1426 0.3088 0.3428 0.0785  -0.0533 -0.0682 314 ALA E CB  
10227 N N   . THR E 315 ? 0.1403 0.3207 0.3668 0.0759  -0.0539 -0.0555 315 THR E N   
10228 C CA  . THR E 315 ? 0.1529 0.3281 0.3720 0.0610  -0.0556 -0.0547 315 THR E CA  
10229 C C   . THR E 315 ? 0.1458 0.3295 0.3722 0.0586  -0.0627 -0.0555 315 THR E C   
10230 O O   . THR E 315 ? 0.1582 0.3205 0.3688 0.0521  -0.0654 -0.0572 315 THR E O   
10231 C CB  . THR E 315 ? 0.1625 0.3626 0.3858 0.0440  -0.0501 -0.0531 315 THR E CB  
10232 O OG1 . THR E 315 ? 0.1450 0.3925 0.3935 0.0561  -0.0503 -0.0514 315 THR E OG1 
10233 C CG2 . THR E 315 ? 0.1824 0.3594 0.3861 0.0398  -0.0420 -0.0523 315 THR E CG2 
10234 N N   . GLY E 316 ? 0.1349 0.3438 0.3773 0.0682  -0.0649 -0.0536 316 GLY E N   
10235 C CA  . GLY E 316 ? 0.1324 0.3496 0.3784 0.0695  -0.0715 -0.0532 316 GLY E CA  
10236 C C   . GLY E 316 ? 0.1336 0.3220 0.3675 0.0754  -0.0738 -0.0560 316 GLY E C   
10237 O O   . GLY E 316 ? 0.1340 0.3067 0.3581 0.0749  -0.0712 -0.0599 316 GLY E O   
10238 N N   . LEU E 317 ? 0.1384 0.3277 0.3698 0.0791  -0.0783 -0.0547 317 LEU E N   
10239 C CA  . LEU E 317 ? 0.1469 0.3116 0.3610 0.0758  -0.0796 -0.0588 317 LEU E CA  
10240 C C   . LEU E 317 ? 0.1795 0.3144 0.3658 0.0864  -0.0739 -0.0567 317 LEU E C   
10241 O O   . LEU E 317 ? 0.1943 0.3300 0.3760 0.1060  -0.0700 -0.0508 317 LEU E O   
10242 C CB  . LEU E 317 ? 0.1408 0.3127 0.3589 0.0683  -0.0873 -0.0596 317 LEU E CB  
10243 C CG  . LEU E 317 ? 0.1415 0.3378 0.3697 0.0725  -0.0922 -0.0541 317 LEU E CG  
10244 C CD1 . LEU E 317 ? 0.1652 0.3460 0.3733 0.0896  -0.0918 -0.0493 317 LEU E CD1 
10245 C CD2 . LEU E 317 ? 0.1353 0.3399 0.3681 0.0567  -0.0982 -0.0572 317 LEU E CD2 
10246 N N   . ARG E 318 ? 0.2019 0.3081 0.3602 0.0733  -0.0715 -0.0622 318 ARG E N   
10247 C CA  . ARG E 318 ? 0.2593 0.3101 0.3662 0.0755  -0.0620 -0.0618 318 ARG E CA  
10248 C C   . ARG E 318 ? 0.2893 0.3244 0.3803 0.1037  -0.0635 -0.0515 318 ARG E C   
10249 O O   . ARG E 318 ? 0.2775 0.3297 0.3798 0.1034  -0.0717 -0.0492 318 ARG E O   
10250 C CB  . ARG E 318 ? 0.2818 0.3119 0.3564 0.0440  -0.0586 -0.0718 318 ARG E CB  
10251 C CG  . ARG E 318 ? 0.3636 0.3137 0.3617 0.0343  -0.0449 -0.0733 318 ARG E CG  
10252 C CD  . ARG E 318 ? 0.3870 0.3305 0.3526 -0.0089 -0.0411 -0.0856 318 ARG E CD  
10253 N NE  . ARG E 318 ? 0.3704 0.3573 0.3433 -0.0403 -0.0375 -0.0990 318 ARG E NE  
10254 C CZ  . ARG E 318 ? 0.4289 0.3769 0.3437 -0.0726 -0.0225 -0.1089 318 ARG E CZ  
10255 N NH1 . ARG E 318 ? 0.5211 0.3635 0.3540 -0.0763 -0.0074 -0.1064 318 ARG E NH1 
10256 N NH2 . ARG E 318 ? 0.4053 0.4181 0.3351 -0.1000 -0.0214 -0.1216 318 ARG E NH2 
10257 N N   . ASN E 319 ? 0.3341 0.3400 0.3948 0.1325  -0.0553 -0.0451 319 ASN E N   
10258 C CA  . ASN E 319 ? 0.3691 0.3750 0.4112 0.1737  -0.0563 -0.0338 319 ASN E CA  
10259 C C   . ASN E 319 ? 0.4589 0.3723 0.4180 0.1829  -0.0470 -0.0309 319 ASN E C   
10260 O O   . ASN E 319 ? 0.5206 0.3524 0.4170 0.1657  -0.0332 -0.0365 319 ASN E O   
10261 C CB  . ASN E 319 ? 0.3803 0.4069 0.4236 0.2098  -0.0508 -0.0280 319 ASN E CB  
10262 C CG  . ASN E 319 ? 0.3994 0.4701 0.4394 0.2592  -0.0546 -0.0167 319 ASN E CG  
10263 O OD1 . ASN E 319 ? 0.3966 0.4879 0.4400 0.2642  -0.0629 -0.0129 319 ASN E OD1 
10264 N ND2 . ASN E 319 ? 0.4202 0.5156 0.4528 0.2986  -0.0486 -0.0116 319 ASN E ND2 
10265 N N   . SER E 320 ? 0.4777 0.4010 0.4284 0.2070  -0.0535 -0.0226 320 SER E N   
10266 C CA  . SER E 320 ? 0.5689 0.3986 0.4345 0.2140  -0.0453 -0.0187 320 SER E CA  
10267 C C   . SER E 320 ? 0.6819 0.4262 0.4547 0.2692  -0.0302 -0.0079 320 SER E C   
10268 O O   . SER E 320 ? 0.6764 0.4704 0.4680 0.3170  -0.0315 -0.0003 320 SER E O   
10269 C CB  . SER E 320 ? 0.5429 0.4192 0.4344 0.2207  -0.0589 -0.0135 320 SER E CB  
10270 O OG  . SER E 320 ? 0.4583 0.3975 0.4203 0.1744  -0.0704 -0.0236 320 SER E OG  
10271 N N   . PRO E 321 ? 0.7981 0.4093 0.4599 0.2625  -0.0138 -0.0080 321 PRO E N   
10272 C CA  . PRO E 321 ? 0.9364 0.4339 0.4799 0.3211  0.0038  0.0035  321 PRO E CA  
10273 C C   . PRO E 321 ? 0.9923 0.4766 0.4925 0.3762  -0.0003 0.0189  321 PRO E C   
10274 O O   . PRO E 321 ? 0.9465 0.5385 0.5033 0.4298  -0.0138 0.0292  321 PRO E O   
10275 C CB  . PRO E 321 ? 1.0439 0.3919 0.4763 0.2692  0.0262  -0.0072 321 PRO E CB  
10276 C CG  . PRO E 321 ? 0.9787 0.3674 0.4582 0.1989  0.0166  -0.0190 321 PRO E CG  
10277 C CD  . PRO E 321 ? 0.8162 0.3711 0.4467 0.1929  -0.0076 -0.0215 321 PRO E CD  
10278 N N   . GLY F 1   ? 0.3223 0.2553 0.2943 -0.0627 -0.0632 -0.0205 1   GLY F N   
10279 C CA  . GLY F 1   ? 0.2736 0.2521 0.2870 -0.0414 -0.0401 -0.0289 1   GLY F CA  
10280 C C   . GLY F 1   ? 0.2551 0.2941 0.2792 -0.0515 -0.0272 -0.0282 1   GLY F C   
10281 O O   . GLY F 1   ? 0.2692 0.3282 0.2782 -0.0753 -0.0321 -0.0224 1   GLY F O   
10282 N N   . LEU F 2   ? 0.2287 0.2981 0.2749 -0.0312 -0.0120 -0.0352 2   LEU F N   
10283 C CA  . LEU F 2   ? 0.2177 0.3499 0.2700 -0.0293 -0.0017 -0.0384 2   LEU F CA  
10284 C C   . LEU F 2   ? 0.2155 0.3701 0.2696 -0.0271 0.0026  -0.0431 2   LEU F C   
10285 O O   . LEU F 2   ? 0.2173 0.4317 0.2674 -0.0361 0.0052  -0.0439 2   LEU F O   
10286 C CB  . LEU F 2   ? 0.2019 0.3448 0.2684 0.0009  0.0098  -0.0471 2   LEU F CB  
10287 C CG  . LEU F 2   ? 0.2011 0.3511 0.2672 -0.0013 0.0085  -0.0434 2   LEU F CG  
10288 C CD1 . LEU F 2   ? 0.1918 0.3453 0.2669 0.0310  0.0185  -0.0525 2   LEU F CD1 
10289 C CD2 . LEU F 2   ? 0.2101 0.4192 0.2647 -0.0280 0.0044  -0.0366 2   LEU F CD2 
10290 N N   . PHE F 3   ? 0.2133 0.3277 0.2724 -0.0162 0.0034  -0.0469 3   PHE F N   
10291 C CA  . PHE F 3   ? 0.2133 0.3415 0.2725 -0.0109 0.0082  -0.0528 3   PHE F CA  
10292 C C   . PHE F 3   ? 0.2255 0.3453 0.2746 -0.0360 -0.0016 -0.0456 3   PHE F C   
10293 O O   . PHE F 3   ? 0.2265 0.3620 0.2743 -0.0362 0.0014  -0.0493 3   PHE F O   
10294 C CB  . PHE F 3   ? 0.2108 0.3043 0.2743 0.0131  0.0154  -0.0616 3   PHE F CB  
10295 C CG  . PHE F 3   ? 0.2128 0.3097 0.2737 0.0375  0.0225  -0.0688 3   PHE F CG  
10296 C CD1 . PHE F 3   ? 0.2250 0.3501 0.2742 0.0590  0.0271  -0.0786 3   PHE F CD1 
10297 C CD2 . PHE F 3   ? 0.2077 0.2824 0.2739 0.0417  0.0226  -0.0666 3   PHE F CD2 
10298 C CE1 . PHE F 3   ? 0.2375 0.3598 0.2761 0.0866  0.0298  -0.0861 3   PHE F CE1 
10299 C CE2 . PHE F 3   ? 0.2150 0.2892 0.2742 0.0634  0.0271  -0.0723 3   PHE F CE2 
10300 C CZ  . PHE F 3   ? 0.2323 0.3270 0.2758 0.0869  0.0298  -0.0819 3   PHE F CZ  
10301 N N   . GLY F 4   ? 0.2430 0.3322 0.2782 -0.0558 -0.0157 -0.0357 4   GLY F N   
10302 C CA  . GLY F 4   ? 0.2708 0.3470 0.2818 -0.0848 -0.0304 -0.0264 4   GLY F CA  
10303 C C   . GLY F 4   ? 0.2770 0.3165 0.2874 -0.0785 -0.0363 -0.0281 4   GLY F C   
10304 O O   . GLY F 4   ? 0.3035 0.3299 0.2907 -0.1007 -0.0492 -0.0208 4   GLY F O   
10305 N N   . ALA F 5   ? 0.2577 0.2832 0.2895 -0.0520 -0.0282 -0.0371 5   ALA F N   
10306 C CA  . ALA F 5   ? 0.2605 0.2664 0.2949 -0.0460 -0.0320 -0.0401 5   ALA F CA  
10307 C C   . ALA F 5   ? 0.2792 0.2456 0.3046 -0.0358 -0.0476 -0.0399 5   ALA F C   
10308 O O   . ALA F 5   ? 0.3094 0.2480 0.3117 -0.0421 -0.0652 -0.0356 5   ALA F O   
10309 C CB  . ALA F 5   ? 0.2383 0.2574 0.2924 -0.0298 -0.0160 -0.0498 5   ALA F CB  
10310 N N   . ILE F 6   ? 0.2674 0.2315 0.3065 -0.0175 -0.0427 -0.0457 6   ILE F N   
10311 C CA  . ILE F 6   ? 0.2860 0.2242 0.3173 0.0003  -0.0568 -0.0497 6   ILE F CA  
10312 C C   . ILE F 6   ? 0.3313 0.2247 0.3240 -0.0075 -0.0784 -0.0421 6   ILE F C   
10313 O O   . ILE F 6   ? 0.3351 0.2271 0.3198 -0.0212 -0.0763 -0.0362 6   ILE F O   
10314 C CB  . ILE F 6   ? 0.2626 0.2177 0.3161 0.0179  -0.0453 -0.0577 6   ILE F CB  
10315 C CG1 . ILE F 6   ? 0.2379 0.2243 0.3138 0.0200  -0.0302 -0.0643 6   ILE F CG1 
10316 C CG2 . ILE F 6   ? 0.2852 0.2211 0.3271 0.0398  -0.0611 -0.0638 6   ILE F CG2 
10317 C CD1 . ILE F 6   ? 0.2217 0.2250 0.3122 0.0273  -0.0186 -0.0702 6   ILE F CD1 
10318 N N   . ALA F 7   ? 0.3750 0.2282 0.3370 0.0008  -0.1013 -0.0425 7   ALA F N   
10319 C CA  . ALA F 7   ? 0.4412 0.2292 0.3464 -0.0102 -0.1286 -0.0342 7   ALA F CA  
10320 C C   . ALA F 7   ? 0.4538 0.2445 0.3389 -0.0547 -0.1278 -0.0193 7   ALA F C   
10321 O O   . ALA F 7   ? 0.4957 0.2513 0.3406 -0.0768 -0.1415 -0.0101 7   ALA F O   
10322 C CB  . ALA F 7   ? 0.4594 0.2202 0.3513 0.0071  -0.1359 -0.0385 7   ALA F CB  
10323 N N   . GLY F 8   ? 0.4213 0.2587 0.3313 -0.0693 -0.1123 -0.0176 8   GLY F N   
10324 C CA  . GLY F 8   ? 0.4246 0.2916 0.3238 -0.1085 -0.1075 -0.0069 8   GLY F CA  
10325 C C   . GLY F 8   ? 0.4442 0.3081 0.3267 -0.1264 -0.1154 -0.0019 8   GLY F C   
10326 O O   . GLY F 8   ? 0.5057 0.3080 0.3375 -0.1383 -0.1420 0.0054  8   GLY F O   
10327 N N   . PHE F 9   ? 0.4009 0.3240 0.3189 -0.1271 -0.0946 -0.0065 9   PHE F N   
10328 C CA  . PHE F 9   ? 0.4144 0.3393 0.3214 -0.1414 -0.0998 -0.0034 9   PHE F CA  
10329 C C   . PHE F 9   ? 0.4114 0.3098 0.3304 -0.1108 -0.1045 -0.0116 9   PHE F C   
10330 O O   . PHE F 9   ? 0.4354 0.3173 0.3366 -0.1186 -0.1160 -0.0084 9   PHE F O   
10331 C CB  . PHE F 9   ? 0.3789 0.3773 0.3106 -0.1540 -0.0787 -0.0061 9   PHE F CB  
10332 C CG  . PHE F 9   ? 0.3297 0.3601 0.3055 -0.1216 -0.0559 -0.0203 9   PHE F CG  
10333 C CD1 . PHE F 9   ? 0.3207 0.3479 0.3072 -0.1119 -0.0527 -0.0257 9   PHE F CD1 
10334 C CD2 . PHE F 9   ? 0.3012 0.3607 0.2997 -0.1042 -0.0398 -0.0276 9   PHE F CD2 
10335 C CE1 . PHE F 9   ? 0.2907 0.3360 0.3038 -0.0895 -0.0351 -0.0372 9   PHE F CE1 
10336 C CE2 . PHE F 9   ? 0.2741 0.3463 0.2972 -0.0782 -0.0234 -0.0394 9   PHE F CE2 
10337 C CZ  . PHE F 9   ? 0.2720 0.3340 0.2993 -0.0732 -0.0215 -0.0438 9   PHE F CZ  
10338 N N   . ILE F 10  ? 0.3850 0.2868 0.3326 -0.0783 -0.0959 -0.0220 10  ILE F N   
10339 C CA  . ILE F 10  ? 0.3884 0.2758 0.3430 -0.0493 -0.1034 -0.0307 10  ILE F CA  
10340 C C   . ILE F 10  ? 0.4302 0.2681 0.3558 -0.0293 -0.1251 -0.0324 10  ILE F C   
10341 O O   . ILE F 10  ? 0.4115 0.2593 0.3549 -0.0116 -0.1174 -0.0389 10  ILE F O   
10342 C CB  . ILE F 10  ? 0.3371 0.2709 0.3376 -0.0314 -0.0800 -0.0420 10  ILE F CB  
10343 C CG1 . ILE F 10  ? 0.3101 0.2787 0.3272 -0.0478 -0.0611 -0.0418 10  ILE F CG1 
10344 C CG2 . ILE F 10  ? 0.3402 0.2801 0.3477 -0.0081 -0.0876 -0.0509 10  ILE F CG2 
10345 C CD1 . ILE F 10  ? 0.2778 0.2731 0.3223 -0.0371 -0.0409 -0.0507 10  ILE F CD1 
10346 N N   . GLU F 11  ? 0.4957 0.2743 0.3696 -0.0312 -0.1544 -0.0270 11  GLU F N   
10347 C CA  . GLU F 11  ? 0.5601 0.2701 0.3846 -0.0138 -0.1821 -0.0278 11  GLU F CA  
10348 C C   . GLU F 11  ? 0.5475 0.2715 0.3934 0.0338  -0.1817 -0.0446 11  GLU F C   
10349 O O   . GLU F 11  ? 0.5765 0.2651 0.3991 0.0467  -0.1924 -0.0470 11  GLU F O   
10350 C CB  . GLU F 11  ? 0.6444 0.2786 0.4012 -0.0142 -0.2181 -0.0224 11  GLU F CB  
10351 C CG  . GLU F 11  ? 0.6984 0.2854 0.3993 -0.0671 -0.2328 -0.0029 11  GLU F CG  
10352 C CD  . GLU F 11  ? 0.8041 0.2910 0.4194 -0.0647 -0.2756 0.0024  11  GLU F CD  
10353 O OE1 . GLU F 11  ? 0.8079 0.2983 0.4272 -0.0425 -0.2827 -0.0035 11  GLU F OE1 
10354 O OE2 . GLU F 11  ? 0.8906 0.2905 0.4286 -0.0847 -0.3042 0.0125  11  GLU F OE2 
10355 N N   . GLY F 12  ? 0.5096 0.2889 0.3957 0.0575  -0.1705 -0.0563 12  GLY F N   
10356 C CA  . GLY F 12  ? 0.5012 0.3116 0.4057 0.1009  -0.1714 -0.0737 12  GLY F CA  
10357 C C   . GLY F 12  ? 0.4378 0.3362 0.4000 0.1051  -0.1460 -0.0828 12  GLY F C   
10358 O O   . GLY F 12  ? 0.4100 0.3343 0.3915 0.0811  -0.1325 -0.0773 12  GLY F O   
10359 N N   . GLY F 13  ? 0.4214 0.3653 0.4055 0.1328  -0.1408 -0.0969 13  GLY F N   
10360 C CA  . GLY F 13  ? 0.3731 0.4032 0.4023 0.1315  -0.1197 -0.1056 13  GLY F CA  
10361 C C   . GLY F 13  ? 0.3893 0.4607 0.4170 0.1561  -0.1331 -0.1168 13  GLY F C   
10362 O O   . GLY F 13  ? 0.4419 0.4683 0.4314 0.1811  -0.1606 -0.1191 13  GLY F O   
10363 N N   . TRP F 14  ? 0.3514 0.5073 0.4147 0.1473  -0.1153 -0.1237 14  TRP F N   
10364 C CA  . TRP F 14  ? 0.3583 0.5754 0.4268 0.1642  -0.1239 -0.1343 14  TRP F CA  
10365 C C   . TRP F 14  ? 0.3488 0.6619 0.4366 0.1921  -0.1229 -0.1535 14  TRP F C   
10366 O O   . TRP F 14  ? 0.3112 0.6899 0.4274 0.1643  -0.1005 -0.1542 14  TRP F O   
10367 C CB  . TRP F 14  ? 0.3281 0.5736 0.4162 0.1211  -0.1050 -0.1252 14  TRP F CB  
10368 C CG  . TRP F 14  ? 0.3396 0.5124 0.4098 0.0982  -0.1074 -0.1099 14  TRP F CG  
10369 C CD1 . TRP F 14  ? 0.3824 0.4824 0.4172 0.1116  -0.1299 -0.1043 14  TRP F CD1 
10370 C CD2 . TRP F 14  ? 0.3164 0.4846 0.3964 0.0566  -0.0884 -0.0992 14  TRP F CD2 
10371 N NE1 . TRP F 14  ? 0.3796 0.4430 0.4077 0.0778  -0.1238 -0.0903 14  TRP F NE1 
10372 C CE2 . TRP F 14  ? 0.3385 0.4440 0.3956 0.0481  -0.0983 -0.0884 14  TRP F CE2 
10373 C CE3 . TRP F 14  ? 0.2890 0.4949 0.3868 0.0251  -0.0663 -0.0980 14  TRP F CE3 
10374 C CZ2 . TRP F 14  ? 0.3247 0.4165 0.3833 0.0149  -0.0849 -0.0789 14  TRP F CZ2 
10375 C CZ3 . TRP F 14  ? 0.2844 0.4606 0.3764 -0.0051 -0.0556 -0.0886 14  TRP F CZ3 
10376 C CH2 . TRP F 14  ? 0.2983 0.4241 0.3745 -0.0072 -0.0640 -0.0803 14  TRP F CH2 
10377 N N   . GLN F 15  ? 0.3912 0.7118 0.4564 0.2474  -0.1495 -0.1698 15  GLN F N   
10378 C CA  . GLN F 15  ? 0.3885 0.8223 0.4701 0.2834  -0.1526 -0.1927 15  GLN F CA  
10379 C C   . GLN F 15  ? 0.3545 0.8974 0.4673 0.2563  -0.1380 -0.1952 15  GLN F C   
10380 O O   . GLN F 15  ? 0.3314 0.9893 0.4697 0.2527  -0.1263 -0.2074 15  GLN F O   
10381 C CB  . GLN F 15  ? 0.4549 0.8704 0.4963 0.3561  -0.1896 -0.2118 15  GLN F CB  
10382 C CG  . GLN F 15  ? 0.5085 0.8108 0.5035 0.3866  -0.2108 -0.2119 15  GLN F CG  
10383 C CD  . GLN F 15  ? 0.5073 0.8601 0.5103 0.4184  -0.2088 -0.2296 15  GLN F CD  
10384 O OE1 . GLN F 15  ? 0.5098 0.7972 0.5031 0.4061  -0.2042 -0.2215 15  GLN F OE1 
10385 N NE2 . GLN F 15  ? 0.5055 0.9827 0.5256 0.4593  -0.2125 -0.2546 15  GLN F NE2 
10386 N N   . GLY F 16  ? 0.3552 0.8641 0.4621 0.2336  -0.1394 -0.1833 16  GLY F N   
10387 C CA  . GLY F 16  ? 0.3316 0.9307 0.4601 0.2050  -0.1283 -0.1841 16  GLY F CA  
10388 C C   . GLY F 16  ? 0.2901 0.9204 0.4408 0.1375  -0.0976 -0.1717 16  GLY F C   
10389 O O   . GLY F 16  ? 0.2784 0.9899 0.4408 0.1084  -0.0891 -0.1730 16  GLY F O   
10390 N N   . MET F 17  ? 0.2763 0.8385 0.4257 0.1119  -0.0833 -0.1597 17  MET F N   
10391 C CA  . MET F 17  ? 0.2534 0.8273 0.4100 0.0529  -0.0586 -0.1489 17  MET F CA  
10392 C C   . MET F 17  ? 0.2428 0.8738 0.4094 0.0481  -0.0488 -0.1561 17  MET F C   
10393 O O   . MET F 17  ? 0.2405 0.8155 0.4042 0.0582  -0.0465 -0.1532 17  MET F O   
10394 C CB  . MET F 17  ? 0.2513 0.7118 0.3945 0.0276  -0.0499 -0.1312 17  MET F CB  
10395 C CG  . MET F 17  ? 0.2462 0.6985 0.3818 -0.0274 -0.0301 -0.1211 17  MET F CG  
10396 S SD  . MET F 17  ? 0.2500 0.5831 0.3671 -0.0442 -0.0231 -0.1054 17  MET F SD  
10397 C CE  . MET F 17  ? 0.2434 0.5304 0.3657 -0.0108 -0.0270 -0.1058 17  MET F CE  
10398 N N   . VAL F 18  ? 0.2379 0.9859 0.4143 0.0283  -0.0430 -0.1649 18  VAL F N   
10399 C CA  . VAL F 18  ? 0.2311 1.0590 0.4167 0.0241  -0.0357 -0.1744 18  VAL F CA  
10400 C C   . VAL F 18  ? 0.2321 1.0648 0.4042 -0.0473 -0.0162 -0.1614 18  VAL F C   
10401 O O   . VAL F 18  ? 0.2303 1.0981 0.4030 -0.0588 -0.0089 -0.1643 18  VAL F O   
10402 C CB  . VAL F 18  ? 0.2326 1.2119 0.4346 0.0561  -0.0455 -0.1972 18  VAL F CB  
10403 C CG1 . VAL F 18  ? 0.2494 1.2095 0.4501 0.1313  -0.0703 -0.2111 18  VAL F CG1 
10404 C CG2 . VAL F 18  ? 0.2324 1.3104 0.4352 0.0056  -0.0381 -0.1955 18  VAL F CG2 
10405 N N   . ASP F 19  ? 0.2437 1.0333 0.3961 -0.0949 -0.0099 -0.1473 19  ASP F N   
10406 C CA  . ASP F 19  ? 0.2657 1.0471 0.3876 -0.1656 0.0029  -0.1351 19  ASP F CA  
10407 C C   . ASP F 19  ? 0.2790 0.9208 0.3742 -0.1806 0.0093  -0.1200 19  ASP F C   
10408 O O   . ASP F 19  ? 0.3131 0.9133 0.3683 -0.2347 0.0156  -0.1088 19  ASP F O   
10409 C CB  . ASP F 19  ? 0.2861 1.1030 0.3891 -0.2125 0.0034  -0.1300 19  ASP F CB  
10410 C CG  . ASP F 19  ? 0.2848 1.0220 0.3871 -0.1941 -0.0022 -0.1244 19  ASP F CG  
10411 O OD1 . ASP F 19  ? 0.2687 0.9354 0.3860 -0.1453 -0.0078 -0.1251 19  ASP F OD1 
10412 O OD2 . ASP F 19  ? 0.3039 1.0511 0.3870 -0.2324 -0.0018 -0.1190 19  ASP F OD2 
10413 N N   . GLY F 20  ? 0.2601 0.8298 0.3706 -0.1332 0.0056  -0.1203 20  GLY F N   
10414 C CA  . GLY F 20  ? 0.2702 0.7254 0.3595 -0.1402 0.0111  -0.1087 20  GLY F CA  
10415 C C   . GLY F 20  ? 0.2481 0.6512 0.3573 -0.0900 0.0063  -0.1104 20  GLY F C   
10416 O O   . GLY F 20  ? 0.2331 0.6670 0.3648 -0.0492 -0.0039 -0.1194 20  GLY F O   
10417 N N   . TRP F 21  ? 0.2546 0.5756 0.3483 -0.0939 0.0116  -0.1020 21  TRP F N   
10418 C CA  . TRP F 21  ? 0.2385 0.5092 0.3451 -0.0562 0.0078  -0.1014 21  TRP F CA  
10419 C C   . TRP F 21  ? 0.2375 0.4519 0.3411 -0.0455 0.0033  -0.0958 21  TRP F C   
10420 O O   . TRP F 21  ? 0.2286 0.4271 0.3432 -0.0158 -0.0057 -0.0970 21  TRP F O   
10421 C CB  . TRP F 21  ? 0.2453 0.4685 0.3384 -0.0635 0.0152  -0.0960 21  TRP F CB  
10422 C CG  . TRP F 21  ? 0.2350 0.5017 0.3422 -0.0512 0.0157  -0.1027 21  TRP F CG  
10423 C CD1 . TRP F 21  ? 0.2198 0.5395 0.3507 -0.0173 0.0075  -0.1139 21  TRP F CD1 
10424 C CD2 . TRP F 21  ? 0.2461 0.5010 0.3387 -0.0693 0.0229  -0.0995 21  TRP F CD2 
10425 N NE1 . TRP F 21  ? 0.2164 0.5653 0.3520 -0.0135 0.0108  -0.1187 21  TRP F NE1 
10426 C CE2 . TRP F 21  ? 0.2299 0.5413 0.3441 -0.0476 0.0209  -0.1090 21  TRP F CE2 
10427 C CE3 . TRP F 21  ? 0.2764 0.4727 0.3332 -0.0992 0.0285  -0.0903 21  TRP F CE3 
10428 C CZ2 . TRP F 21  ? 0.2354 0.5537 0.3424 -0.0596 0.0267  -0.1085 21  TRP F CZ2 
10429 C CZ3 . TRP F 21  ? 0.2874 0.4827 0.3322 -0.1107 0.0323  -0.0890 21  TRP F CZ3 
10430 C CH2 . TRP F 21  ? 0.2632 0.5228 0.3360 -0.0932 0.0326  -0.0974 21  TRP F CH2 
10431 N N   . TYR F 22  ? 0.2543 0.4355 0.3359 -0.0719 0.0083  -0.0898 22  TYR F N   
10432 C CA  . TYR F 22  ? 0.2552 0.3938 0.3322 -0.0655 0.0055  -0.0856 22  TYR F CA  
10433 C C   . TYR F 22  ? 0.2697 0.4250 0.3348 -0.0892 0.0051  -0.0853 22  TYR F C   
10434 O O   . TYR F 22  ? 0.2900 0.4627 0.3359 -0.1203 0.0092  -0.0852 22  TYR F O   
10435 C CB  . TYR F 22  ? 0.2679 0.3410 0.3240 -0.0669 0.0115  -0.0805 22  TYR F CB  
10436 C CG  . TYR F 22  ? 0.2662 0.3242 0.3210 -0.0593 0.0155  -0.0802 22  TYR F CG  
10437 C CD1 . TYR F 22  ? 0.2437 0.3086 0.3206 -0.0348 0.0119  -0.0808 22  TYR F CD1 
10438 C CD2 . TYR F 22  ? 0.2960 0.3254 0.3196 -0.0788 0.0206  -0.0787 22  TYR F CD2 
10439 C CE1 . TYR F 22  ? 0.2419 0.2951 0.3180 -0.0286 0.0157  -0.0805 22  TYR F CE1 
10440 C CE2 . TYR F 22  ? 0.2971 0.3114 0.3176 -0.0719 0.0233  -0.0781 22  TYR F CE2 
10441 C CZ  . TYR F 22  ? 0.2655 0.2965 0.3162 -0.0462 0.0220  -0.0792 22  TYR F CZ  
10442 O OH  . TYR F 22  ? 0.2664 0.2845 0.3144 -0.0400 0.0249  -0.0785 22  TYR F OH  
10443 N N   . GLY F 23  ? 0.2645 0.4129 0.3359 -0.0791 -0.0009 -0.0843 23  GLY F N   
10444 C CA  . GLY F 23  ? 0.2779 0.4402 0.3384 -0.1004 -0.0017 -0.0838 23  GLY F CA  
10445 C C   . GLY F 23  ? 0.2725 0.4221 0.3393 -0.0873 -0.0093 -0.0819 23  GLY F C   
10446 O O   . GLY F 23  ? 0.2654 0.3820 0.3359 -0.0694 -0.0124 -0.0789 23  GLY F O   
10447 N N   . TYR F 24  ? 0.2795 0.4597 0.3444 -0.1006 -0.0128 -0.0830 24  TYR F N   
10448 C CA  . TYR F 24  ? 0.2813 0.4476 0.3455 -0.0960 -0.0198 -0.0802 24  TYR F CA  
10449 C C   . TYR F 24  ? 0.2768 0.4948 0.3563 -0.0802 -0.0335 -0.0845 24  TYR F C   
10450 O O   . TYR F 24  ? 0.2742 0.5547 0.3629 -0.0815 -0.0346 -0.0910 24  TYR F O   
10451 C CB  . TYR F 24  ? 0.3024 0.4479 0.3420 -0.1255 -0.0132 -0.0780 24  TYR F CB  
10452 C CG  . TYR F 24  ? 0.3259 0.4197 0.3362 -0.1395 -0.0032 -0.0771 24  TYR F CG  
10453 C CD1 . TYR F 24  ? 0.3460 0.4431 0.3377 -0.1612 0.0012  -0.0779 24  TYR F CD1 
10454 C CD2 . TYR F 24  ? 0.3356 0.3789 0.3306 -0.1303 -0.0002 -0.0764 24  TYR F CD2 
10455 C CE1 . TYR F 24  ? 0.3826 0.4169 0.3346 -0.1716 0.0058  -0.0772 24  TYR F CE1 
10456 C CE2 . TYR F 24  ? 0.3672 0.3594 0.3278 -0.1339 0.0053  -0.0784 24  TYR F CE2 
10457 C CZ  . TYR F 24  ? 0.3943 0.3736 0.3302 -0.1536 0.0070  -0.0784 24  TYR F CZ  
10458 O OH  . TYR F 24  ? 0.4402 0.3539 0.3297 -0.1550 0.0082  -0.0804 24  TYR F OH  
10459 N N   . HIS F 25  ? 0.2820 0.4763 0.3593 -0.0651 -0.0454 -0.0813 25  HIS F N   
10460 C CA  . HIS F 25  ? 0.2911 0.5203 0.3715 -0.0495 -0.0616 -0.0851 25  HIS F CA  
10461 C C   . HIS F 25  ? 0.3018 0.5069 0.3697 -0.0653 -0.0642 -0.0787 25  HIS F C   
10462 O O   . HIS F 25  ? 0.3082 0.4623 0.3645 -0.0675 -0.0660 -0.0716 25  HIS F O   
10463 C CB  . HIS F 25  ? 0.3047 0.5176 0.3813 -0.0107 -0.0815 -0.0879 25  HIS F CB  
10464 C CG  . HIS F 25  ? 0.3252 0.5704 0.3968 0.0148  -0.1022 -0.0947 25  HIS F CG  
10465 N ND1 . HIS F 25  ? 0.3518 0.5559 0.4015 0.0193  -0.1191 -0.0888 25  HIS F ND1 
10466 C CD2 . HIS F 25  ? 0.3271 0.6476 0.4097 0.0385  -0.1100 -0.1078 25  HIS F CD2 
10467 C CE1 . HIS F 25  ? 0.3725 0.6151 0.4174 0.0486  -0.1381 -0.0980 25  HIS F CE1 
10468 N NE2 . HIS F 25  ? 0.3563 0.6759 0.4229 0.0629  -0.1326 -0.1107 25  HIS F NE2 
10469 N N   . HIS F 26  ? 0.3054 0.5551 0.3748 -0.0790 -0.0644 -0.0815 26  HIS F N   
10470 C CA  . HIS F 26  ? 0.3160 0.5498 0.3736 -0.0956 -0.0667 -0.0763 26  HIS F CA  
10471 C C   . HIS F 26  ? 0.3307 0.5886 0.3873 -0.0724 -0.0881 -0.0787 26  HIS F C   
10472 O O   . HIS F 26  ? 0.3326 0.6410 0.3988 -0.0469 -0.0984 -0.0876 26  HIS F O   
10473 C CB  . HIS F 26  ? 0.3185 0.5747 0.3690 -0.1322 -0.0528 -0.0769 26  HIS F CB  
10474 C CG  . HIS F 26  ? 0.3186 0.6556 0.3783 -0.1384 -0.0564 -0.0833 26  HIS F CG  
10475 N ND1 . HIS F 26  ? 0.3132 0.7013 0.3805 -0.1453 -0.0502 -0.0889 26  HIS F ND1 
10476 C CD2 . HIS F 26  ? 0.3246 0.7102 0.3864 -0.1406 -0.0656 -0.0855 26  HIS F CD2 
10477 C CE1 . HIS F 26  ? 0.3149 0.7885 0.3896 -0.1526 -0.0550 -0.0947 26  HIS F CE1 
10478 N NE2 . HIS F 26  ? 0.3213 0.7946 0.3935 -0.1479 -0.0646 -0.0931 26  HIS F NE2 
10479 N N   . SER F 27  ? 0.3465 0.5692 0.3877 -0.0788 -0.0963 -0.0718 27  SER F N   
10480 C CA  . SER F 27  ? 0.3697 0.6087 0.4018 -0.0611 -0.1179 -0.0732 27  SER F CA  
10481 C C   . SER F 27  ? 0.3768 0.6014 0.3976 -0.0895 -0.1153 -0.0661 27  SER F C   
10482 O O   . SER F 27  ? 0.3790 0.5542 0.3875 -0.1074 -0.1094 -0.0581 27  SER F O   
10483 C CB  . SER F 27  ? 0.4031 0.5917 0.4124 -0.0269 -0.1433 -0.0716 27  SER F CB  
10484 O OG  . SER F 27  ? 0.4177 0.5370 0.4047 -0.0456 -0.1449 -0.0593 27  SER F OG  
10485 N N   . ASN F 28  ? 0.3809 0.6582 0.4060 -0.0936 -0.1194 -0.0701 28  ASN F N   
10486 C CA  . ASN F 28  ? 0.3891 0.6599 0.4033 -0.1204 -0.1177 -0.0645 28  ASN F CA  
10487 C C   . ASN F 28  ? 0.4055 0.7288 0.4191 -0.1051 -0.1358 -0.0691 28  ASN F C   
10488 O O   . ASN F 28  ? 0.4162 0.7725 0.4334 -0.0670 -0.1527 -0.0772 28  ASN F O   
10489 C CB  . ASN F 28  ? 0.3746 0.6519 0.3906 -0.1597 -0.0932 -0.0644 28  ASN F CB  
10490 C CG  . ASN F 28  ? 0.3658 0.7101 0.3934 -0.1714 -0.0851 -0.0717 28  ASN F CG  
10491 O OD1 . ASN F 28  ? 0.3641 0.7736 0.4052 -0.1510 -0.0964 -0.0784 28  ASN F OD1 
10492 N ND2 . ASN F 28  ? 0.3679 0.6973 0.3838 -0.2048 -0.0673 -0.0711 28  ASN F ND2 
10493 N N   . GLU F 29  ? 0.4118 0.7451 0.4186 -0.1307 -0.1338 -0.0654 29  GLU F N   
10494 C CA  . GLU F 29  ? 0.4287 0.8153 0.4340 -0.1165 -0.1515 -0.0695 29  GLU F CA  
10495 C C   . GLU F 29  ? 0.4153 0.9045 0.4428 -0.1068 -0.1498 -0.0819 29  GLU F C   
10496 O O   . GLU F 29  ? 0.4306 0.9740 0.4595 -0.0704 -0.1704 -0.0905 29  GLU F O   
10497 C CB  . GLU F 29  ? 0.4349 0.8181 0.4300 -0.1525 -0.1461 -0.0632 29  GLU F CB  
10498 C CG  . GLU F 29  ? 0.4536 0.7568 0.4248 -0.1614 -0.1518 -0.0522 29  GLU F CG  
10499 C CD  . GLU F 29  ? 0.4651 0.7749 0.4245 -0.1874 -0.1530 -0.0477 29  GLU F CD  
10500 O OE1 . GLU F 29  ? 0.4571 0.8251 0.4258 -0.2059 -0.1452 -0.0522 29  GLU F OE1 
10501 O OE2 . GLU F 29  ? 0.4857 0.7438 0.4231 -0.1934 -0.1623 -0.0390 29  GLU F OE2 
10502 N N   . GLN F 30  ? 0.3933 0.9107 0.4325 -0.1394 -0.1271 -0.0833 30  GLN F N   
10503 C CA  . GLN F 30  ? 0.3828 1.0070 0.4391 -0.1445 -0.1227 -0.0934 30  GLN F CA  
10504 C C   . GLN F 30  ? 0.3760 1.0385 0.4478 -0.0989 -0.1314 -0.1044 30  GLN F C   
10505 O O   . GLN F 30  ? 0.3733 1.1435 0.4599 -0.0833 -0.1372 -0.1166 30  GLN F O   
10506 C CB  . GLN F 30  ? 0.3779 1.0023 0.4265 -0.2020 -0.0987 -0.0891 30  GLN F CB  
10507 C CG  . GLN F 30  ? 0.3940 0.9975 0.4208 -0.2475 -0.0921 -0.0819 30  GLN F CG  
10508 C CD  . GLN F 30  ? 0.4058 0.9142 0.4065 -0.2806 -0.0754 -0.0747 30  GLN F CD  
10509 O OE1 . GLN F 30  ? 0.4058 0.8352 0.4005 -0.2661 -0.0752 -0.0703 30  GLN F OE1 
10510 N NE2 . GLN F 30  ? 0.4242 0.9405 0.4027 -0.3254 -0.0633 -0.0741 30  GLN F NE2 
10511 N N   . GLY F 31  ? 0.3750 0.9567 0.4421 -0.0780 -0.1324 -0.1011 31  GLY F N   
10512 C CA  . GLY F 31  ? 0.3744 0.9778 0.4506 -0.0330 -0.1418 -0.1116 31  GLY F CA  
10513 C C   . GLY F 31  ? 0.3647 0.8868 0.4381 -0.0356 -0.1314 -0.1054 31  GLY F C   
10514 O O   . GLY F 31  ? 0.3630 0.8052 0.4247 -0.0615 -0.1219 -0.0935 31  GLY F O   
10515 N N   . SER F 32  ? 0.3591 0.9101 0.4429 -0.0065 -0.1337 -0.1148 32  SER F N   
10516 C CA  . SER F 32  ? 0.3492 0.8351 0.4322 -0.0072 -0.1241 -0.1103 32  SER F CA  
10517 C C   . SER F 32  ? 0.3298 0.8864 0.4322 -0.0078 -0.1124 -0.1197 32  SER F C   
10518 O O   . SER F 32  ? 0.3283 0.9892 0.4437 0.0051  -0.1171 -0.1323 32  SER F O   
10519 C CB  . SER F 32  ? 0.3790 0.7910 0.4407 0.0374  -0.1473 -0.1100 32  SER F CB  
10520 O OG  . SER F 32  ? 0.4052 0.8660 0.4614 0.0905  -0.1716 -0.1251 32  SER F OG  
10521 N N   . GLY F 33  ? 0.3165 0.8240 0.4198 -0.0234 -0.0976 -0.1141 33  GLY F N   
10522 C CA  . GLY F 33  ? 0.3017 0.8679 0.4192 -0.0283 -0.0865 -0.1213 33  GLY F CA  
10523 C C   . GLY F 33  ? 0.2915 0.7916 0.4054 -0.0457 -0.0711 -0.1138 33  GLY F C   
10524 O O   . GLY F 33  ? 0.2929 0.7101 0.3938 -0.0637 -0.0642 -0.1028 33  GLY F O   
10525 N N   . TYR F 34  ? 0.2827 0.8289 0.4076 -0.0386 -0.0663 -0.1213 34  TYR F N   
10526 C CA  . TYR F 34  ? 0.2752 0.7701 0.3966 -0.0528 -0.0529 -0.1157 34  TYR F CA  
10527 C C   . TYR F 34  ? 0.2789 0.7968 0.3891 -0.1069 -0.0356 -0.1112 34  TYR F C   
10528 O O   . TYR F 34  ? 0.2822 0.8925 0.3957 -0.1272 -0.0340 -0.1171 34  TYR F O   
10529 C CB  . TYR F 34  ? 0.2700 0.7936 0.4041 -0.0135 -0.0595 -0.1261 34  TYR F CB  
10530 C CG  . TYR F 34  ? 0.2853 0.7690 0.4143 0.0401  -0.0814 -0.1309 34  TYR F CG  
10531 C CD1 . TYR F 34  ? 0.2924 0.6761 0.4076 0.0480  -0.0846 -0.1216 34  TYR F CD1 
10532 C CD2 . TYR F 34  ? 0.3024 0.8468 0.4323 0.0826  -0.1016 -0.1451 34  TYR F CD2 
10533 C CE1 . TYR F 34  ? 0.3221 0.6566 0.4181 0.0889  -0.1081 -0.1239 34  TYR F CE1 
10534 C CE2 . TYR F 34  ? 0.3357 0.8235 0.4443 0.1323  -0.1269 -0.1494 34  TYR F CE2 
10535 C CZ  . TYR F 34  ? 0.3485 0.7258 0.4370 0.1313  -0.1305 -0.1375 34  TYR F CZ  
10536 O OH  . TYR F 34  ? 0.3966 0.7056 0.4503 0.1724  -0.1587 -0.1398 34  TYR F OH  
10537 N N   . ALA F 35  ? 0.2870 0.7202 0.3774 -0.1306 -0.0248 -0.1012 35  ALA F N   
10538 C CA  . ALA F 35  ? 0.3088 0.7332 0.3718 -0.1794 -0.0127 -0.0962 35  ALA F CA  
10539 C C   . ALA F 35  ? 0.3102 0.6686 0.3646 -0.1733 -0.0061 -0.0927 35  ALA F C   
10540 O O   . ALA F 35  ? 0.3079 0.5900 0.3583 -0.1558 -0.0055 -0.0884 35  ALA F O   
10541 C CB  . ALA F 35  ? 0.3371 0.7101 0.3671 -0.2148 -0.0099 -0.0888 35  ALA F CB  
10542 N N   . ALA F 36  ? 0.3150 0.7112 0.3662 -0.1887 -0.0014 -0.0949 36  ALA F N   
10543 C CA  . ALA F 36  ? 0.3203 0.6576 0.3602 -0.1858 0.0043  -0.0915 36  ALA F CA  
10544 C C   . ALA F 36  ? 0.3647 0.6104 0.3541 -0.2193 0.0087  -0.0827 36  ALA F C   
10545 O O   . ALA F 36  ? 0.4030 0.6487 0.3559 -0.2630 0.0086  -0.0792 36  ALA F O   
10546 C CB  . ALA F 36  ? 0.3179 0.7253 0.3641 -0.1969 0.0072  -0.0962 36  ALA F CB  
10547 N N   . ASP F 37  ? 0.3667 0.5343 0.3487 -0.1971 0.0107  -0.0802 37  ASP F N   
10548 C CA  . ASP F 37  ? 0.4176 0.4933 0.3455 -0.2156 0.0119  -0.0754 37  ASP F CA  
10549 C C   . ASP F 37  ? 0.4509 0.5125 0.3471 -0.2410 0.0134  -0.0727 37  ASP F C   
10550 O O   . ASP F 37  ? 0.4298 0.4904 0.3448 -0.2183 0.0160  -0.0738 37  ASP F O   
10551 C CB  . ASP F 37  ? 0.4054 0.4219 0.3402 -0.1766 0.0126  -0.0761 37  ASP F CB  
10552 C CG  . ASP F 37  ? 0.4637 0.3891 0.3394 -0.1832 0.0110  -0.0754 37  ASP F CG  
10553 O OD1 . ASP F 37  ? 0.4888 0.3862 0.3403 -0.1902 0.0083  -0.0763 37  ASP F OD1 
10554 O OD2 . ASP F 37  ? 0.4897 0.3690 0.3392 -0.1780 0.0109  -0.0750 37  ASP F OD2 
10555 N N   . LYS F 38  ? 0.5088 0.5572 0.3515 -0.2924 0.0104  -0.0682 38  LYS F N   
10556 C CA  . LYS F 38  ? 0.5520 0.5915 0.3543 -0.3296 0.0095  -0.0637 38  LYS F CA  
10557 C C   . LYS F 38  ? 0.5913 0.5256 0.3525 -0.3139 0.0067  -0.0613 38  LYS F C   
10558 O O   . LYS F 38  ? 0.5850 0.5303 0.3518 -0.3125 0.0089  -0.0604 38  LYS F O   
10559 C CB  . LYS F 38  ? 0.6224 0.6575 0.3600 -0.3979 0.0037  -0.0573 38  LYS F CB  
10560 C CG  . LYS F 38  ? 0.5898 0.7627 0.3641 -0.4261 0.0069  -0.0597 38  LYS F CG  
10561 C CD  . LYS F 38  ? 0.6678 0.8451 0.3697 -0.5068 0.0010  -0.0513 38  LYS F CD  
10562 C CE  . LYS F 38  ? 0.7109 0.8403 0.3717 -0.5311 -0.0052 -0.0480 38  LYS F CE  
10563 N NZ  . LYS F 38  ? 0.8119 0.9049 0.3774 -0.6157 -0.0149 -0.0372 38  LYS F NZ  
10564 N N   . GLU F 39  ? 0.6346 0.4720 0.3529 -0.2992 0.0010  -0.0618 39  GLU F N   
10565 C CA  . GLU F 39  ? 0.6859 0.4202 0.3541 -0.2786 -0.0048 -0.0620 39  GLU F CA  
10566 C C   . GLU F 39  ? 0.6222 0.3823 0.3477 -0.2295 0.0022  -0.0658 39  GLU F C   
10567 O O   . GLU F 39  ? 0.6434 0.3757 0.3484 -0.2304 0.0005  -0.0635 39  GLU F O   
10568 C CB  . GLU F 39  ? 0.7412 0.3832 0.3581 -0.2594 -0.0130 -0.0664 39  GLU F CB  
10569 C CG  . GLU F 39  ? 0.7641 0.3339 0.3598 -0.2090 -0.0171 -0.0727 39  GLU F CG  
10570 C CD  . GLU F 39  ? 0.8596 0.3175 0.3686 -0.1972 -0.0314 -0.0788 39  GLU F CD  
10571 O OE1 . GLU F 39  ? 0.8736 0.3275 0.3704 -0.2081 -0.0332 -0.0808 39  GLU F OE1 
10572 O OE2 . GLU F 39  ? 0.9273 0.2984 0.3757 -0.1741 -0.0424 -0.0827 39  GLU F OE2 
10573 N N   . SER F 40  ? 0.5516 0.3596 0.3416 -0.1906 0.0086  -0.0705 40  SER F N   
10574 C CA  . SER F 40  ? 0.4984 0.3285 0.3362 -0.1495 0.0137  -0.0731 40  SER F CA  
10575 C C   . SER F 40  ? 0.4605 0.3557 0.3350 -0.1582 0.0181  -0.0714 40  SER F C   
10576 O O   . SER F 40  ? 0.4500 0.3365 0.3332 -0.1403 0.0199  -0.0714 40  SER F O   
10577 C CB  . SER F 40  ? 0.4438 0.3092 0.3320 -0.1168 0.0168  -0.0765 40  SER F CB  
10578 O OG  . SER F 40  ? 0.4072 0.3389 0.3328 -0.1281 0.0178  -0.0761 40  SER F OG  
10579 N N   . THR F 41  ? 0.4423 0.4080 0.3368 -0.1836 0.0194  -0.0714 41  THR F N   
10580 C CA  . THR F 41  ? 0.4106 0.4528 0.3377 -0.1891 0.0227  -0.0732 41  THR F CA  
10581 C C   . THR F 41  ? 0.4568 0.4721 0.3390 -0.2215 0.0221  -0.0685 41  THR F C   
10582 O O   . THR F 41  ? 0.4360 0.4699 0.3374 -0.2081 0.0251  -0.0697 41  THR F O   
10583 C CB  . THR F 41  ? 0.3904 0.5259 0.3423 -0.2072 0.0226  -0.0769 41  THR F CB  
10584 O OG1 . THR F 41  ? 0.3542 0.5063 0.3420 -0.1761 0.0204  -0.0806 41  THR F OG1 
10585 C CG2 . THR F 41  ? 0.3605 0.5878 0.3457 -0.2043 0.0250  -0.0829 41  THR F CG2 
10586 N N   . GLN F 42  ? 0.5270 0.4925 0.3423 -0.2670 0.0166  -0.0626 42  GLN F N   
10587 C CA  . GLN F 42  ? 0.5894 0.5172 0.3453 -0.3078 0.0122  -0.0559 42  GLN F CA  
10588 C C   . GLN F 42  ? 0.6111 0.4514 0.3436 -0.2770 0.0091  -0.0549 42  GLN F C   
10589 O O   . GLN F 42  ? 0.6247 0.4640 0.3441 -0.2889 0.0090  -0.0518 42  GLN F O   
10590 C CB  . GLN F 42  ? 0.6802 0.5480 0.3511 -0.3657 0.0021  -0.0485 42  GLN F CB  
10591 C CG  . GLN F 42  ? 0.7602 0.5882 0.3559 -0.4219 -0.0056 -0.0393 42  GLN F CG  
10592 C CD  . GLN F 42  ? 0.7167 0.6723 0.3555 -0.4480 0.0030  -0.0400 42  GLN F CD  
10593 O OE1 . GLN F 42  ? 0.7175 0.6718 0.3546 -0.4464 0.0043  -0.0385 42  GLN F OE1 
10594 N NE2 . GLN F 42  ? 0.6793 0.7522 0.3568 -0.4687 0.0086  -0.0439 42  GLN F NE2 
10595 N N   . LYS F 43  ? 0.6149 0.3903 0.3420 -0.2370 0.0063  -0.0582 43  LYS F N   
10596 C CA  . LYS F 43  ? 0.6297 0.3375 0.3411 -0.1979 0.0032  -0.0600 43  LYS F CA  
10597 C C   . LYS F 43  ? 0.5538 0.3278 0.3346 -0.1682 0.0126  -0.0623 43  LYS F C   
10598 O O   . LYS F 43  ? 0.5700 0.3122 0.3346 -0.1588 0.0108  -0.0608 43  LYS F O   
10599 C CB  . LYS F 43  ? 0.6353 0.2970 0.3414 -0.1573 0.0002  -0.0662 43  LYS F CB  
10600 C CG  . LYS F 43  ? 0.7163 0.2691 0.3482 -0.1347 -0.0121 -0.0690 43  LYS F CG  
10601 C CD  . LYS F 43  ? 0.7739 0.2637 0.3542 -0.1284 -0.0213 -0.0742 43  LYS F CD  
10602 C CE  . LYS F 43  ? 0.8318 0.2406 0.3610 -0.0778 -0.0325 -0.0839 43  LYS F CE  
10603 N NZ  . LYS F 43  ? 0.8456 0.2404 0.3634 -0.0552 -0.0352 -0.0931 43  LYS F NZ  
10604 N N   . ALA F 44  ? 0.4791 0.3375 0.3301 -0.1530 0.0203  -0.0662 44  ALA F N   
10605 C CA  . ALA F 44  ? 0.4166 0.3326 0.3260 -0.1263 0.0263  -0.0691 44  ALA F CA  
10606 C C   . ALA F 44  ? 0.4182 0.3790 0.3278 -0.1525 0.0286  -0.0681 44  ALA F C   
10607 O O   . ALA F 44  ? 0.4026 0.3676 0.3260 -0.1374 0.0308  -0.0684 44  ALA F O   
10608 C CB  . ALA F 44  ? 0.3584 0.3371 0.3245 -0.1051 0.0286  -0.0738 44  ALA F CB  
10609 N N   . ILE F 45  ? 0.4378 0.4404 0.3316 -0.1940 0.0281  -0.0670 45  ILE F N   
10610 C CA  . ILE F 45  ? 0.4444 0.5064 0.3342 -0.2263 0.0304  -0.0667 45  ILE F CA  
10611 C C   . ILE F 45  ? 0.5040 0.4900 0.3345 -0.2487 0.0262  -0.0587 45  ILE F C   
10612 O O   . ILE F 45  ? 0.4914 0.5095 0.3341 -0.2497 0.0294  -0.0593 45  ILE F O   
10613 C CB  . ILE F 45  ? 0.4617 0.5931 0.3389 -0.2738 0.0301  -0.0667 45  ILE F CB  
10614 C CG1 . ILE F 45  ? 0.3960 0.6315 0.3407 -0.2437 0.0335  -0.0779 45  ILE F CG1 
10615 C CG2 . ILE F 45  ? 0.4965 0.6717 0.3422 -0.3250 0.0305  -0.0631 45  ILE F CG2 
10616 C CD1 . ILE F 45  ? 0.4079 0.7114 0.3457 -0.2797 0.0324  -0.0793 45  ILE F CD1 
10617 N N   . ASP F 46  ? 0.5753 0.4563 0.3367 -0.2637 0.0169  -0.0522 46  ASP F N   
10618 C CA  . ASP F 46  ? 0.6500 0.4379 0.3397 -0.2802 0.0077  -0.0450 46  ASP F CA  
10619 C C   . ASP F 46  ? 0.6170 0.3826 0.3355 -0.2289 0.0102  -0.0481 46  ASP F C   
10620 O O   . ASP F 46  ? 0.6339 0.3908 0.3361 -0.2388 0.0091  -0.0446 46  ASP F O   
10621 C CB  . ASP F 46  ? 0.7453 0.4116 0.3458 -0.2947 -0.0071 -0.0404 46  ASP F CB  
10622 C CG  . ASP F 46  ? 0.7963 0.4710 0.3505 -0.3573 -0.0122 -0.0348 46  ASP F CG  
10623 O OD1 . ASP F 46  ? 0.7662 0.5450 0.3497 -0.3961 -0.0047 -0.0336 46  ASP F OD1 
10624 O OD2 . ASP F 46  ? 0.8702 0.4515 0.3559 -0.3672 -0.0245 -0.0327 46  ASP F OD2 
10625 N N   . GLY F 47  ? 0.5715 0.3339 0.3312 -0.1783 0.0134  -0.0542 47  GLY F N   
10626 C CA  . GLY F 47  ? 0.5414 0.2911 0.3275 -0.1323 0.0155  -0.0571 47  GLY F CA  
10627 C C   . GLY F 47  ? 0.4817 0.3068 0.3236 -0.1263 0.0242  -0.0586 47  GLY F C   
10628 O O   . GLY F 47  ? 0.4892 0.2923 0.3229 -0.1154 0.0233  -0.0569 47  GLY F O   
10629 N N   . VAL F 48  ? 0.4282 0.3402 0.3222 -0.1302 0.0309  -0.0630 48  VAL F N   
10630 C CA  . VAL F 48  ? 0.3777 0.3631 0.3207 -0.1187 0.0368  -0.0678 48  VAL F CA  
10631 C C   . VAL F 48  ? 0.4057 0.4173 0.3237 -0.1570 0.0377  -0.0653 48  VAL F C   
10632 O O   . VAL F 48  ? 0.3869 0.4216 0.3227 -0.1464 0.0407  -0.0671 48  VAL F O   
10633 C CB  . VAL F 48  ? 0.3267 0.3904 0.3218 -0.1037 0.0392  -0.0760 48  VAL F CB  
10634 C CG1 . VAL F 48  ? 0.2928 0.4332 0.3241 -0.0926 0.0419  -0.0840 48  VAL F CG1 
10635 C CG2 . VAL F 48  ? 0.2990 0.3373 0.3185 -0.0670 0.0373  -0.0771 48  VAL F CG2 
10636 N N   . THR F 49  ? 0.4550 0.4640 0.3278 -0.2054 0.0345  -0.0605 49  THR F N   
10637 C CA  . THR F 49  ? 0.4938 0.5271 0.3312 -0.2533 0.0339  -0.0561 49  THR F CA  
10638 C C   . THR F 49  ? 0.5419 0.4852 0.3316 -0.2539 0.0280  -0.0482 49  THR F C   
10639 O O   . THR F 49  ? 0.5307 0.5071 0.3309 -0.2574 0.0314  -0.0487 49  THR F O   
10640 C CB  . THR F 49  ? 0.5539 0.5879 0.3358 -0.3152 0.0287  -0.0497 49  THR F CB  
10641 O OG1 . THR F 49  ? 0.5067 0.6407 0.3366 -0.3135 0.0344  -0.0582 49  THR F OG1 
10642 C CG2 . THR F 49  ? 0.6050 0.6622 0.3392 -0.3751 0.0265  -0.0428 49  THR F CG2 
10643 N N   . ASN F 50  ? 0.5992 0.4302 0.3344 -0.2463 0.0179  -0.0426 50  ASN F N   
10644 C CA  . ASN F 50  ? 0.6571 0.3917 0.3375 -0.2380 0.0083  -0.0368 50  ASN F CA  
10645 C C   . ASN F 50  ? 0.5952 0.3599 0.3330 -0.1910 0.0157  -0.0417 50  ASN F C   
10646 O O   . ASN F 50  ? 0.6183 0.3614 0.3339 -0.1970 0.0130  -0.0377 50  ASN F O   
10647 C CB  . ASN F 50  ? 0.7207 0.3409 0.3421 -0.2169 -0.0048 -0.0356 50  ASN F CB  
10648 C CG  . ASN F 50  ? 0.8116 0.3684 0.3495 -0.2681 -0.0175 -0.0289 50  ASN F CG  
10649 O OD1 . ASN F 50  ? 0.8789 0.4124 0.3545 -0.3248 -0.0253 -0.0198 50  ASN F OD1 
10650 N ND2 . ASN F 50  ? 0.8204 0.3473 0.3509 -0.2524 -0.0207 -0.0329 50  ASN F ND2 
10651 N N   . LYS F 51  ? 0.5237 0.3343 0.3292 -0.1480 0.0236  -0.0495 51  LYS F N   
10652 C CA  . LYS F 51  ? 0.4668 0.3083 0.3254 -0.1070 0.0297  -0.0539 51  LYS F CA  
10653 C C   . LYS F 51  ? 0.4368 0.3484 0.3251 -0.1195 0.0362  -0.0560 51  LYS F C   
10654 O O   . LYS F 51  ? 0.4317 0.3336 0.3234 -0.1060 0.0367  -0.0550 51  LYS F O   
10655 C CB  . LYS F 51  ? 0.4068 0.2882 0.3220 -0.0737 0.0345  -0.0603 51  LYS F CB  
10656 C CG  . LYS F 51  ? 0.3526 0.2698 0.3182 -0.0400 0.0388  -0.0642 51  LYS F CG  
10657 C CD  . LYS F 51  ? 0.3124 0.2557 0.3167 -0.0174 0.0396  -0.0684 51  LYS F CD  
10658 C CE  . LYS F 51  ? 0.2985 0.2219 0.3133 0.0126  0.0383  -0.0673 51  LYS F CE  
10659 N NZ  . LYS F 51  ? 0.2838 0.2116 0.3123 0.0243  0.0369  -0.0686 51  LYS F NZ  
10660 N N   . VAL F 52  ? 0.4180 0.4069 0.3279 -0.1424 0.0409  -0.0607 52  VAL F N   
10661 C CA  . VAL F 52  ? 0.3927 0.4636 0.3298 -0.1508 0.0466  -0.0664 52  VAL F CA  
10662 C C   . VAL F 52  ? 0.4481 0.4926 0.3327 -0.1916 0.0439  -0.0580 52  VAL F C   
10663 O O   . VAL F 52  ? 0.4340 0.4997 0.3318 -0.1838 0.0468  -0.0598 52  VAL F O   
10664 C CB  . VAL F 52  ? 0.3676 0.5386 0.3335 -0.1636 0.0503  -0.0758 52  VAL F CB  
10665 C CG1 . VAL F 52  ? 0.3538 0.6202 0.3366 -0.1759 0.0552  -0.0839 52  VAL F CG1 
10666 C CG2 . VAL F 52  ? 0.3176 0.5101 0.3330 -0.1175 0.0502  -0.0847 52  VAL F CG2 
10667 N N   . ASN F 53  ? 0.5198 0.5099 0.3379 -0.2367 0.0363  -0.0484 53  ASN F N   
10668 C CA  . ASN F 53  ? 0.5939 0.5376 0.3428 -0.2831 0.0291  -0.0377 53  ASN F CA  
10669 C C   . ASN F 53  ? 0.6219 0.4697 0.3437 -0.2532 0.0219  -0.0325 53  ASN F C   
10670 O O   . ASN F 53  ? 0.6427 0.4855 0.3443 -0.2683 0.0205  -0.0284 53  ASN F O   
10671 C CB  . ASN F 53  ? 0.6817 0.5666 0.3487 -0.3403 0.0177  -0.0274 53  ASN F CB  
10672 C CG  . ASN F 53  ? 0.6612 0.6508 0.3499 -0.3768 0.0242  -0.0318 53  ASN F CG  
10673 O OD1 . ASN F 53  ? 0.5950 0.7098 0.3485 -0.3679 0.0358  -0.0427 53  ASN F OD1 
10674 N ND2 . ASN F 53  ? 0.7242 0.6630 0.3542 -0.4157 0.0151  -0.0245 53  ASN F ND2 
10675 N N   . SER F 54  ? 0.6242 0.4040 0.3452 -0.2102 0.0172  -0.0337 54  SER F N   
10676 C CA  . SER F 54  ? 0.6445 0.3510 0.3473 -0.1718 0.0105  -0.0319 54  SER F CA  
10677 C C   . SER F 54  ? 0.5775 0.3493 0.3435 -0.1453 0.0209  -0.0367 54  SER F C   
10678 O O   . SER F 54  ? 0.6029 0.3427 0.3448 -0.1439 0.0168  -0.0325 54  SER F O   
10679 C CB  . SER F 54  ? 0.6399 0.3001 0.3473 -0.1255 0.0065  -0.0363 54  SER F CB  
10680 O OG  . SER F 54  ? 0.7307 0.2946 0.3557 -0.1407 -0.0087 -0.0319 54  SER F OG  
10681 N N   . ILE F 55  ? 0.5013 0.3573 0.3412 -0.1242 0.0323  -0.0457 55  ILE F N   
10682 C CA  . ILE F 55  ? 0.4442 0.3588 0.3394 -0.0990 0.0401  -0.0517 55  ILE F CA  
10683 C C   . ILE F 55  ? 0.4575 0.4135 0.3433 -0.1305 0.0430  -0.0510 55  ILE F C   
10684 O O   . ILE F 55  ? 0.4537 0.4026 0.3425 -0.1192 0.0434  -0.0499 55  ILE F O   
10685 C CB  . ILE F 55  ? 0.3791 0.3631 0.3372 -0.0744 0.0466  -0.0619 55  ILE F CB  
10686 C CG1 . ILE F 55  ? 0.3609 0.3088 0.3345 -0.0383 0.0442  -0.0617 55  ILE F CG1 
10687 C CG2 . ILE F 55  ? 0.3374 0.3861 0.3365 -0.0597 0.0516  -0.0701 55  ILE F CG2 
10688 C CD1 . ILE F 55  ? 0.3184 0.3092 0.3340 -0.0215 0.0461  -0.0687 55  ILE F CD1 
10689 N N   . ILE F 56  ? 0.4754 0.4822 0.3492 -0.1719 0.0450  -0.0520 56  ILE F N   
10690 C CA  . ILE F 56  ? 0.4898 0.5544 0.3530 -0.2081 0.0482  -0.0523 56  ILE F CA  
10691 C C   . ILE F 56  ? 0.5613 0.5416 0.3571 -0.2347 0.0392  -0.0391 56  ILE F C   
10692 O O   . ILE F 56  ? 0.5537 0.5522 0.3563 -0.2327 0.0417  -0.0394 56  ILE F O   
10693 C CB  . ILE F 56  ? 0.5043 0.6455 0.3572 -0.2558 0.0506  -0.0548 56  ILE F CB  
10694 C CG1 . ILE F 56  ? 0.4359 0.6765 0.3574 -0.2225 0.0581  -0.0712 56  ILE F CG1 
10695 C CG2 . ILE F 56  ? 0.5345 0.7326 0.3598 -0.3061 0.0523  -0.0525 56  ILE F CG2 
10696 C CD1 . ILE F 56  ? 0.4475 0.7574 0.3616 -0.2597 0.0591  -0.0740 56  ILE F CD1 
10697 N N   . ASP F 57  ? 0.6392 0.5212 0.3643 -0.2571 0.0267  -0.0281 57  ASP F N   
10698 C CA  . ASP F 57  ? 0.7313 0.5132 0.3718 -0.2836 0.0122  -0.0151 57  ASP F CA  
10699 C C   . ASP F 57  ? 0.7218 0.4575 0.3721 -0.2364 0.0097  -0.0151 57  ASP F C   
10700 O O   . ASP F 57  ? 0.7633 0.4699 0.3749 -0.2550 0.0039  -0.0083 57  ASP F O   
10701 C CB  . ASP F 57  ? 0.8250 0.4919 0.3795 -0.3034 -0.0051 -0.0061 57  ASP F CB  
10702 C CG  . ASP F 57  ? 0.8827 0.5676 0.3849 -0.3779 -0.0091 0.0009  57  ASP F CG  
10703 O OD1 . ASP F 57  ? 0.9223 0.6324 0.3883 -0.4323 -0.0110 0.0080  57  ASP F OD1 
10704 O OD2 . ASP F 57  ? 0.8921 0.5700 0.3867 -0.3861 -0.0108 -0.0001 57  ASP F OD2 
10705 N N   . LYS F 58  ? 0.6717 0.4053 0.3709 -0.1788 0.0135  -0.0223 58  LYS F N   
10706 C CA  . LYS F 58  ? 0.6580 0.3652 0.3715 -0.1347 0.0119  -0.0231 58  LYS F CA  
10707 C C   . LYS F 58  ? 0.6076 0.3906 0.3699 -0.1343 0.0228  -0.0267 58  LYS F C   
10708 O O   . LYS F 58  ? 0.6241 0.3778 0.3708 -0.1237 0.0187  -0.0229 58  LYS F O   
10709 C CB  . LYS F 58  ? 0.6129 0.3194 0.3680 -0.0812 0.0140  -0.0299 58  LYS F CB  
10710 C CG  . LYS F 58  ? 0.6766 0.2875 0.3743 -0.0521 -0.0013 -0.0276 58  LYS F CG  
10711 C CD  . LYS F 58  ? 0.7808 0.2978 0.3838 -0.0865 -0.0179 -0.0203 58  LYS F CD  
10712 C CE  . LYS F 58  ? 0.8683 0.2753 0.3938 -0.0542 -0.0389 -0.0189 58  LYS F CE  
10713 N NZ  . LYS F 58  ? 0.9865 0.2832 0.4053 -0.0878 -0.0595 -0.0121 58  LYS F NZ  
10714 N N   . MET F 59  ? 0.5539 0.4329 0.3705 -0.1430 0.0351  -0.0352 59  MET F N   
10715 C CA  . MET F 59  ? 0.5115 0.4656 0.3706 -0.1391 0.0442  -0.0421 59  MET F CA  
10716 C C   . MET F 59  ? 0.5545 0.5352 0.3759 -0.1912 0.0440  -0.0377 59  MET F C   
10717 O O   . MET F 59  ? 0.5383 0.5573 0.3747 -0.1908 0.0484  -0.0406 59  MET F O   
10718 C CB  . MET F 59  ? 0.4446 0.4859 0.3694 -0.1168 0.0536  -0.0562 59  MET F CB  
10719 C CG  . MET F 59  ? 0.4111 0.4284 0.3670 -0.0749 0.0525  -0.0590 59  MET F CG  
10720 S SD  . MET F 59  ? 0.3999 0.3729 0.3649 -0.0378 0.0498  -0.0553 59  MET F SD  
10721 C CE  . MET F 59  ? 0.3513 0.3930 0.3630 -0.0202 0.0554  -0.0666 59  MET F CE  
10722 N N   . ASN F 60  ? 0.6148 0.5756 0.3829 -0.2396 0.0381  -0.0304 60  ASN F N   
10723 C CA  . ASN F 60  ? 0.6673 0.6574 0.3884 -0.3028 0.0364  -0.0242 60  ASN F CA  
10724 C C   . ASN F 60  ? 0.7024 0.6526 0.3903 -0.3114 0.0313  -0.0164 60  ASN F C   
10725 O O   . ASN F 60  ? 0.6945 0.7212 0.3901 -0.3398 0.0377  -0.0193 60  ASN F O   
10726 C CB  . ASN F 60  ? 0.7528 0.6826 0.3946 -0.3583 0.0243  -0.0120 60  ASN F CB  
10727 C CG  . ASN F 60  ? 0.8460 0.7374 0.4008 -0.4268 0.0131  0.0023  60  ASN F CG  
10728 O OD1 . ASN F 60  ? 0.8982 0.6961 0.4037 -0.4219 0.0013  0.0118  60  ASN F OD1 
10729 N ND2 . ASN F 60  ? 0.8736 0.8383 0.4040 -0.4934 0.0151  0.0045  60  ASN F ND2 
10730 N N   . THR F 61  ? 0.7442 0.5807 0.3936 -0.2855 0.0190  -0.0078 61  THR F N   
10731 C CA  . THR F 61  ? 0.7778 0.5712 0.3958 -0.2863 0.0126  -0.0007 61  THR F CA  
10732 C C   . THR F 61  ? 0.7021 0.5206 0.3899 -0.2229 0.0210  -0.0097 61  THR F C   
10733 O O   . THR F 61  ? 0.6895 0.4618 0.3903 -0.1768 0.0173  -0.0113 61  THR F O   
10734 C CB  . THR F 61  ? 0.8951 0.5429 0.4052 -0.3042 -0.0112 0.0149  61  THR F CB  
10735 O OG1 . THR F 61  ? 0.9013 0.4982 0.4067 -0.2632 -0.0176 0.0167  61  THR F OG1 
10736 C CG2 . THR F 61  ? 0.9381 0.5036 0.4105 -0.2892 -0.0229 0.0164  61  THR F CG2 
10737 N N   . GLN F 62  ? 0.6570 0.5544 0.3856 -0.2245 0.0316  -0.0161 62  GLN F N   
10738 C CA  . GLN F 62  ? 0.5838 0.5217 0.3798 -0.1738 0.0404  -0.0261 62  GLN F CA  
10739 C C   . GLN F 62  ? 0.5695 0.5638 0.3768 -0.1876 0.0465  -0.0294 62  GLN F C   
10740 O O   . GLN F 62  ? 0.5995 0.6349 0.3805 -0.2354 0.0480  -0.0279 62  GLN F O   
10741 C CB  . GLN F 62  ? 0.5179 0.5227 0.3784 -0.1462 0.0502  -0.0399 62  GLN F CB  
10742 C CG  . GLN F 62  ? 0.4587 0.5489 0.3778 -0.1224 0.0600  -0.0548 62  GLN F CG  
10743 C CD  . GLN F 62  ? 0.4138 0.5509 0.3798 -0.0943 0.0642  -0.0679 62  GLN F CD  
10744 O OE1 . GLN F 62  ? 0.4188 0.5277 0.3816 -0.0914 0.0616  -0.0650 62  GLN F OE1 
10745 N NE2 . GLN F 62  ? 0.3779 0.5813 0.3819 -0.0712 0.0686  -0.0831 62  GLN F NE2 
10746 N N   . PHE F 63  ? 0.5264 0.5274 0.3705 -0.1489 0.0496  -0.0340 63  PHE F N   
10747 C CA  . PHE F 63  ? 0.5157 0.5565 0.3669 -0.1561 0.0538  -0.0367 63  PHE F CA  
10748 C C   . PHE F 63  ? 0.4916 0.6403 0.3664 -0.1784 0.0640  -0.0501 63  PHE F C   
10749 O O   . PHE F 63  ? 0.4526 0.6626 0.3677 -0.1607 0.0700  -0.0640 63  PHE F O   
10750 C CB  . PHE F 63  ? 0.4695 0.5092 0.3622 -0.1091 0.0559  -0.0419 63  PHE F CB  
10751 C CG  . PHE F 63  ? 0.4676 0.5319 0.3608 -0.1143 0.0583  -0.0432 63  PHE F CG  
10752 C CD1 . PHE F 63  ? 0.5137 0.5197 0.3614 -0.1289 0.0502  -0.0295 63  PHE F CD1 
10753 C CD2 . PHE F 63  ? 0.4268 0.5687 0.3601 -0.1018 0.0666  -0.0591 63  PHE F CD2 
10754 C CE1 . PHE F 63  ? 0.5123 0.5422 0.3601 -0.1355 0.0526  -0.0303 63  PHE F CE1 
10755 C CE2 . PHE F 63  ? 0.4276 0.5924 0.3594 -0.1061 0.0687  -0.0613 63  PHE F CE2 
10756 C CZ  . PHE F 63  ? 0.4664 0.5781 0.3582 -0.1254 0.0628  -0.0462 63  PHE F CZ  
10757 N N   . GLU F 64  ? 0.5182 0.6929 0.3647 -0.2154 0.0647  -0.0467 64  GLU F N   
10758 C CA  . GLU F 64  ? 0.4982 0.7912 0.3650 -0.2352 0.0744  -0.0614 64  GLU F CA  
10759 C C   . GLU F 64  ? 0.4821 0.8037 0.3614 -0.2239 0.0779  -0.0671 64  GLU F C   
10760 O O   . GLU F 64  ? 0.5213 0.7870 0.3604 -0.2464 0.0722  -0.0526 64  GLU F O   
10761 C CB  . GLU F 64  ? 0.5564 0.8741 0.3691 -0.3057 0.0722  -0.0520 64  GLU F CB  
10762 C CG  . GLU F 64  ? 0.5858 0.8662 0.3717 -0.3276 0.0667  -0.0441 64  GLU F CG  
10763 C CD  . GLU F 64  ? 0.6563 0.9569 0.3764 -0.4077 0.0622  -0.0329 64  GLU F CD  
10764 O OE1 . GLU F 64  ? 0.6794 1.0335 0.3778 -0.4478 0.0642  -0.0317 64  GLU F OE1 
10765 O OE2 . GLU F 64  ? 0.6942 0.9565 0.3796 -0.4347 0.0556  -0.0246 64  GLU F OE2 
10766 N N   . ALA F 65  ? 0.4312 0.8344 0.3598 -0.1873 0.0852  -0.0887 65  ALA F N   
10767 C CA  . ALA F 65  ? 0.4167 0.8494 0.3569 -0.1723 0.0881  -0.0971 65  ALA F CA  
10768 C C   . ALA F 65  ? 0.4439 0.9503 0.3566 -0.2235 0.0925  -0.0973 65  ALA F C   
10769 O O   . ALA F 65  ? 0.4576 1.0389 0.3596 -0.2605 0.0960  -0.1011 65  ALA F O   
10770 C CB  . ALA F 65  ? 0.3740 0.8625 0.3606 -0.1168 0.0905  -0.1221 65  ALA F CB  
10771 N N   . VAL F 66  ? 0.4524 0.9414 0.3519 -0.2289 0.0919  -0.0926 66  VAL F N   
10772 C CA  . VAL F 66  ? 0.4801 1.0383 0.3517 -0.2784 0.0957  -0.0924 66  VAL F CA  
10773 C C   . VAL F 66  ? 0.4497 1.0608 0.3498 -0.2449 0.1008  -0.1099 66  VAL F C   
10774 O O   . VAL F 66  ? 0.4314 0.9756 0.3469 -0.2036 0.0973  -0.1089 66  VAL F O   
10775 C CB  . VAL F 66  ? 0.5461 1.0087 0.3502 -0.3322 0.0859  -0.0637 66  VAL F CB  
10776 C CG1 . VAL F 66  ? 0.5845 1.1189 0.3526 -0.3922 0.0885  -0.0616 66  VAL F CG1 
10777 C CG2 . VAL F 66  ? 0.5877 0.9788 0.3518 -0.3608 0.0771  -0.0472 66  VAL F CG2 
10778 N N   . GLY F 67  ? 0.4477 1.1839 0.3515 -0.2643 0.1084  -0.1267 67  GLY F N   
10779 C CA  . GLY F 67  ? 0.4269 1.2235 0.3514 -0.2335 0.1127  -0.1465 67  GLY F CA  
10780 C C   . GLY F 67  ? 0.4539 1.2023 0.3447 -0.2672 0.1107  -0.1289 67  GLY F C   
10781 O O   . GLY F 67  ? 0.4962 1.2618 0.3444 -0.3324 0.1106  -0.1141 67  GLY F O   
10782 N N   . ARG F 68  ? 0.4348 1.1202 0.3391 -0.2258 0.1075  -0.1297 68  ARG F N   
10783 C CA  . ARG F 68  ? 0.4567 1.0951 0.3331 -0.2486 0.1048  -0.1146 68  ARG F CA  
10784 C C   . ARG F 68  ? 0.4319 1.1157 0.3337 -0.2071 0.1082  -0.1365 68  ARG F C   
10785 O O   . ARG F 68  ? 0.4045 1.0716 0.3357 -0.1503 0.1057  -0.1519 68  ARG F O   
10786 C CB  . ARG F 68  ? 0.4684 0.9666 0.3274 -0.2415 0.0947  -0.0894 68  ARG F CB  
10787 C CG  . ARG F 68  ? 0.5201 0.9512 0.3266 -0.2925 0.0866  -0.0637 68  ARG F CG  
10788 C CD  . ARG F 68  ? 0.5312 0.8339 0.3233 -0.2694 0.0752  -0.0447 68  ARG F CD  
10789 N NE  . ARG F 68  ? 0.5592 0.8068 0.3246 -0.2849 0.0681  -0.0327 68  ARG F NE  
10790 C CZ  . ARG F 68  ? 0.5270 0.7618 0.3239 -0.2512 0.0691  -0.0385 68  ARG F CZ  
10791 N NH1 . ARG F 68  ? 0.4693 0.7322 0.3217 -0.2001 0.0750  -0.0546 68  ARG F NH1 
10792 N NH2 . ARG F 68  ? 0.5621 0.7455 0.3261 -0.2711 0.0620  -0.0270 68  ARG F NH2 
10793 N N   . GLU F 69  ? 0.4495 1.1833 0.3322 -0.2379 0.1119  -0.1372 69  GLU F N   
10794 C CA  . GLU F 69  ? 0.4343 1.2227 0.3343 -0.2027 0.1150  -0.1604 69  GLU F CA  
10795 C C   . GLU F 69  ? 0.4427 1.1454 0.3260 -0.2056 0.1101  -0.1436 69  GLU F C   
10796 O O   . GLU F 69  ? 0.4728 1.1264 0.3213 -0.2531 0.1070  -0.1181 69  GLU F O   
10797 C CB  . GLU F 69  ? 0.4474 1.3813 0.3411 -0.2334 0.1241  -0.1782 69  GLU F CB  
10798 C CG  . GLU F 69  ? 0.4361 1.4849 0.3495 -0.2255 0.1293  -0.2003 69  GLU F CG  
10799 C CD  . GLU F 69  ? 0.4163 1.5489 0.3607 -0.1532 0.1299  -0.2407 69  GLU F CD  
10800 O OE1 . GLU F 69  ? 0.4089 1.4584 0.3636 -0.0955 0.1219  -0.2478 69  GLU F OE1 
10801 O OE2 . GLU F 69  ? 0.4172 1.6999 0.3692 -0.1545 0.1365  -0.2659 69  GLU F OE2 
10802 N N   . PHE F 70  ? 0.4230 1.1046 0.3246 -0.1550 0.1073  -0.1582 70  PHE F N   
10803 C CA  . PHE F 70  ? 0.4290 1.0407 0.3179 -0.1542 0.1027  -0.1450 70  PHE F CA  
10804 C C   . PHE F 70  ? 0.4270 1.0928 0.3216 -0.1239 0.1043  -0.1709 70  PHE F C   
10805 O O   . PHE F 70  ? 0.4193 1.1302 0.3293 -0.0790 0.1033  -0.1992 70  PHE F O   
10806 C CB  . PHE F 70  ? 0.4162 0.9186 0.3132 -0.1256 0.0940  -0.1309 70  PHE F CB  
10807 C CG  . PHE F 70  ? 0.4170 0.8673 0.3096 -0.1422 0.0912  -0.1109 70  PHE F CG  
10808 C CD1 . PHE F 70  ? 0.3994 0.8627 0.3120 -0.1218 0.0917  -0.1207 70  PHE F CD1 
10809 C CD2 . PHE F 70  ? 0.4421 0.8264 0.3050 -0.1748 0.0859  -0.0835 70  PHE F CD2 
10810 C CE1 . PHE F 70  ? 0.4031 0.8171 0.3092 -0.1363 0.0888  -0.1032 70  PHE F CE1 
10811 C CE2 . PHE F 70  ? 0.4531 0.7828 0.3040 -0.1849 0.0809  -0.0674 70  PHE F CE2 
10812 C CZ  . PHE F 70  ? 0.4314 0.7775 0.3055 -0.1670 0.0832  -0.0771 70  PHE F CZ  
10813 N N   . ASN F 71  ? 0.4402 1.0964 0.3170 -0.1452 0.1047  -0.1622 71  ASN F N   
10814 C CA  . ASN F 71  ? 0.4446 1.1476 0.3211 -0.1182 0.1054  -0.1865 71  ASN F CA  
10815 C C   . ASN F 71  ? 0.4425 1.0600 0.3210 -0.0717 0.0951  -0.1908 71  ASN F C   
10816 O O   . ASN F 71  ? 0.4323 0.9696 0.3171 -0.0602 0.0886  -0.1767 71  ASN F O   
10817 C CB  . ASN F 71  ? 0.4638 1.2029 0.3181 -0.1637 0.1104  -0.1773 71  ASN F CB  
10818 C CG  . ASN F 71  ? 0.4732 1.1098 0.3100 -0.1825 0.1039  -0.1476 71  ASN F CG  
10819 O OD1 . ASN F 71  ? 0.4658 1.0329 0.3085 -0.1500 0.0969  -0.1460 71  ASN F OD1 
10820 N ND2 . ASN F 71  ? 0.4973 1.1258 0.3061 -0.2367 0.1043  -0.1242 71  ASN F ND2 
10821 N N   . ASN F 72  ? 0.4574 1.0940 0.3252 -0.0486 0.0926  -0.2102 72  ASN F N   
10822 C CA  . ASN F 72  ? 0.4713 1.0319 0.3281 -0.0063 0.0800  -0.2191 72  ASN F CA  
10823 C C   . ASN F 72  ? 0.4689 0.9319 0.3180 -0.0255 0.0743  -0.1893 72  ASN F C   
10824 O O   . ASN F 72  ? 0.4799 0.8710 0.3192 -0.0017 0.0629  -0.1893 72  ASN F O   
10825 C CB  . ASN F 72  ? 0.5002 1.1083 0.3382 0.0238  0.0771  -0.2506 72  ASN F CB  
10826 C CG  . ASN F 72  ? 0.5348 1.0648 0.3471 0.0744  0.0595  -0.2677 72  ASN F CG  
10827 O OD1 . ASN F 72  ? 0.5414 1.0333 0.3525 0.1044  0.0504  -0.2748 72  ASN F OD1 
10828 N ND2 . ASN F 72  ? 0.5649 1.0643 0.3495 0.0812  0.0528  -0.2738 72  ASN F ND2 
10829 N N   . LEU F 73  ? 0.4613 0.9243 0.3091 -0.0690 0.0803  -0.1645 73  LEU F N   
10830 C CA  . LEU F 73  ? 0.4595 0.8452 0.3009 -0.0844 0.0745  -0.1368 73  LEU F CA  
10831 C C   . LEU F 73  ? 0.4462 0.7980 0.2949 -0.1050 0.0749  -0.1113 73  LEU F C   
10832 O O   . LEU F 73  ? 0.4521 0.7647 0.2902 -0.1256 0.0716  -0.0876 73  LEU F O   
10833 C CB  . LEU F 73  ? 0.4739 0.8721 0.2982 -0.1093 0.0765  -0.1295 73  LEU F CB  
10834 C CG  . LEU F 73  ? 0.4929 0.9004 0.3035 -0.0860 0.0727  -0.1517 73  LEU F CG  
10835 C CD1 . LEU F 73  ? 0.5055 0.9495 0.3016 -0.1139 0.0777  -0.1484 73  LEU F CD1 
10836 C CD2 . LEU F 73  ? 0.5014 0.8289 0.3027 -0.0679 0.0605  -0.1456 73  LEU F CD2 
10837 N N   . GLU F 74  ? 0.4336 0.7998 0.2966 -0.0953 0.0770  -0.1179 74  GLU F N   
10838 C CA  . GLU F 74  ? 0.4252 0.7526 0.2925 -0.1070 0.0755  -0.0977 74  GLU F CA  
10839 C C   . GLU F 74  ? 0.4085 0.7116 0.2942 -0.0748 0.0716  -0.1059 74  GLU F C   
10840 O O   . GLU F 74  ? 0.3994 0.7061 0.2942 -0.0769 0.0737  -0.1035 74  GLU F O   
10841 C CB  . GLU F 74  ? 0.4346 0.8071 0.2931 -0.1400 0.0821  -0.0949 74  GLU F CB  
10842 C CG  . GLU F 74  ? 0.4625 0.8438 0.2913 -0.1813 0.0829  -0.0812 74  GLU F CG  
10843 C CD  . GLU F 74  ? 0.4853 0.8994 0.2928 -0.2240 0.0860  -0.0746 74  GLU F CD  
10844 O OE1 . GLU F 74  ? 0.4740 0.9637 0.2962 -0.2237 0.0936  -0.0934 74  GLU F OE1 
10845 O OE2 . GLU F 74  ? 0.5218 0.8842 0.2916 -0.2582 0.0789  -0.0509 74  GLU F OE2 
10846 N N   . ARG F 75  ? 0.4117 0.6857 0.2963 -0.0486 0.0645  -0.1148 75  ARG F N   
10847 C CA  . ARG F 75  ? 0.4089 0.6555 0.3002 -0.0196 0.0579  -0.1246 75  ARG F CA  
10848 C C   . ARG F 75  ? 0.3937 0.5928 0.2944 -0.0247 0.0545  -0.1033 75  ARG F C   
10849 O O   . ARG F 75  ? 0.3853 0.5745 0.2961 -0.0107 0.0526  -0.1073 75  ARG F O   
10850 C CB  . ARG F 75  ? 0.4356 0.6503 0.3060 0.0036  0.0469  -0.1390 75  ARG F CB  
10851 C CG  . ARG F 75  ? 0.4590 0.7188 0.3158 0.0259  0.0467  -0.1689 75  ARG F CG  
10852 C CD  . ARG F 75  ? 0.4648 0.7484 0.3254 0.0592  0.0437  -0.1921 75  ARG F CD  
10853 N NE  . ARG F 75  ? 0.4867 0.8363 0.3366 0.0859  0.0442  -0.2239 75  ARG F NE  
10854 C CZ  . ARG F 75  ? 0.4710 0.9182 0.3396 0.0831  0.0559  -0.2371 75  ARG F CZ  
10855 N NH1 . ARG F 75  ? 0.4386 0.9176 0.3322 0.0501  0.0672  -0.2195 75  ARG F NH1 
10856 N NH2 . ARG F 75  ? 0.4941 1.0110 0.3509 0.1129  0.0549  -0.2692 75  ARG F NH2 
10857 N N   . ARG F 76  ? 0.3925 0.5670 0.2887 -0.0416 0.0530  -0.0821 76  ARG F N   
10858 C CA  . ARG F 76  ? 0.3814 0.5227 0.2849 -0.0417 0.0491  -0.0639 76  ARG F CA  
10859 C C   . ARG F 76  ? 0.3738 0.5188 0.2847 -0.0465 0.0535  -0.0587 76  ARG F C   
10860 O O   . ARG F 76  ? 0.3622 0.4915 0.2843 -0.0352 0.0515  -0.0573 76  ARG F O   
10861 C CB  . ARG F 76  ? 0.3874 0.5144 0.2812 -0.0530 0.0454  -0.0453 76  ARG F CB  
10862 C CG  . ARG F 76  ? 0.3955 0.5145 0.2807 -0.0524 0.0392  -0.0459 76  ARG F CG  
10863 C CD  . ARG F 76  ? 0.4016 0.5219 0.2780 -0.0636 0.0365  -0.0291 76  ARG F CD  
10864 N NE  . ARG F 76  ? 0.4141 0.5471 0.2787 -0.0769 0.0412  -0.0288 76  ARG F NE  
10865 C CZ  . ARG F 76  ? 0.4281 0.5546 0.2782 -0.0861 0.0381  -0.0137 76  ARG F CZ  
10866 N NH1 . ARG F 76  ? 0.4295 0.5442 0.2777 -0.0767 0.0304  0.0004  76  ARG F NH1 
10867 N NH2 . ARG F 76  ? 0.4466 0.5815 0.2796 -0.1041 0.0413  -0.0137 76  ARG F NH2 
10868 N N   . ILE F 77  ? 0.3865 0.5496 0.2853 -0.0674 0.0582  -0.0552 77  ILE F N   
10869 C CA  . ILE F 77  ? 0.3934 0.5528 0.2864 -0.0803 0.0601  -0.0490 77  ILE F CA  
10870 C C   . ILE F 77  ? 0.3801 0.5801 0.2897 -0.0744 0.0662  -0.0669 77  ILE F C   
10871 O O   . ILE F 77  ? 0.3785 0.5695 0.2901 -0.0773 0.0665  -0.0631 77  ILE F O   
10872 C CB  . ILE F 77  ? 0.4274 0.5828 0.2873 -0.1134 0.0595  -0.0369 77  ILE F CB  
10873 C CG1 . ILE F 77  ? 0.4330 0.6477 0.2889 -0.1325 0.0669  -0.0498 77  ILE F CG1 
10874 C CG2 . ILE F 77  ? 0.4476 0.5548 0.2862 -0.1118 0.0501  -0.0187 77  ILE F CG2 
10875 C CD1 . ILE F 77  ? 0.4737 0.6898 0.2905 -0.1757 0.0659  -0.0377 77  ILE F CD1 
10876 N N   . GLU F 78  ? 0.3755 0.6207 0.2936 -0.0628 0.0696  -0.0877 78  GLU F N   
10877 C CA  . GLU F 78  ? 0.3664 0.6541 0.2994 -0.0450 0.0724  -0.1086 78  GLU F CA  
10878 C C   . GLU F 78  ? 0.3546 0.5988 0.2999 -0.0184 0.0658  -0.1089 78  GLU F C   
10879 O O   . GLU F 78  ? 0.3463 0.6034 0.3025 -0.0115 0.0671  -0.1145 78  GLU F O   
10880 C CB  . GLU F 78  ? 0.3745 0.7127 0.3060 -0.0266 0.0733  -0.1339 78  GLU F CB  
10881 C CG  . GLU F 78  ? 0.3728 0.7681 0.3148 -0.0007 0.0743  -0.1600 78  GLU F CG  
10882 C CD  . GLU F 78  ? 0.3896 0.8469 0.3237 0.0205  0.0744  -0.1877 78  GLU F CD  
10883 O OE1 . GLU F 78  ? 0.4075 0.8238 0.3262 0.0418  0.0660  -0.1942 78  GLU F OE1 
10884 O OE2 . GLU F 78  ? 0.3892 0.9403 0.3289 0.0150  0.0821  -0.2037 78  GLU F OE2 
10885 N N   . ASN F 79  ? 0.3574 0.5538 0.2980 -0.0078 0.0583  -0.1022 79  ASN F N   
10886 C CA  . ASN F 79  ? 0.3534 0.5080 0.2986 0.0093  0.0505  -0.0999 79  ASN F CA  
10887 C C   . ASN F 79  ? 0.3390 0.4723 0.2937 -0.0001 0.0519  -0.0814 79  ASN F C   
10888 O O   . ASN F 79  ? 0.3305 0.4517 0.2945 0.0106  0.0496  -0.0830 79  ASN F O   
10889 C CB  . ASN F 79  ? 0.3683 0.4854 0.2981 0.0125  0.0413  -0.0960 79  ASN F CB  
10890 C CG  . ASN F 79  ? 0.3753 0.4513 0.2998 0.0232  0.0310  -0.0945 79  ASN F CG  
10891 O OD1 . ASN F 79  ? 0.3863 0.4546 0.3066 0.0420  0.0259  -0.1092 79  ASN F OD1 
10892 N ND2 . ASN F 79  ? 0.3737 0.4277 0.2949 0.0105  0.0266  -0.0773 79  ASN F ND2 
10893 N N   . LEU F 80  ? 0.3431 0.4679 0.2901 -0.0175 0.0536  -0.0648 80  LEU F N   
10894 C CA  . LEU F 80  ? 0.3429 0.4425 0.2881 -0.0213 0.0522  -0.0492 80  LEU F CA  
10895 C C   . LEU F 80  ? 0.3433 0.4555 0.2908 -0.0279 0.0568  -0.0541 80  LEU F C   
10896 O O   . LEU F 80  ? 0.3359 0.4314 0.2907 -0.0198 0.0552  -0.0512 80  LEU F O   
10897 C CB  . LEU F 80  ? 0.3643 0.4468 0.2870 -0.0349 0.0496  -0.0340 80  LEU F CB  
10898 C CG  . LEU F 80  ? 0.3794 0.4244 0.2873 -0.0284 0.0425  -0.0187 80  LEU F CG  
10899 C CD1 . LEU F 80  ? 0.4094 0.4348 0.2886 -0.0342 0.0360  -0.0068 80  LEU F CD1 
10900 C CD2 . LEU F 80  ? 0.3955 0.4214 0.2901 -0.0364 0.0426  -0.0169 80  LEU F CD2 
10901 N N   . ASN F 81  ? 0.3538 0.5029 0.2940 -0.0453 0.0624  -0.0619 81  ASN F N   
10902 C CA  . ASN F 81  ? 0.3578 0.5355 0.2973 -0.0591 0.0672  -0.0673 81  ASN F CA  
10903 C C   . ASN F 81  ? 0.3367 0.5337 0.3011 -0.0347 0.0679  -0.0825 81  ASN F C   
10904 O O   . ASN F 81  ? 0.3344 0.5274 0.3016 -0.0385 0.0686  -0.0800 81  ASN F O   
10905 C CB  . ASN F 81  ? 0.3708 0.6072 0.2997 -0.0836 0.0734  -0.0760 81  ASN F CB  
10906 C CG  . ASN F 81  ? 0.3778 0.6594 0.3027 -0.1061 0.0783  -0.0810 81  ASN F CG  
10907 O OD1 . ASN F 81  ? 0.4011 0.6470 0.3021 -0.1308 0.0752  -0.0658 81  ASN F OD1 
10908 N ND2 . ASN F 81  ? 0.3643 0.7256 0.3073 -0.0966 0.0842  -0.1034 81  ASN F ND2 
10909 N N   . LYS F 82  ? 0.3302 0.5405 0.3055 -0.0094 0.0656  -0.0981 82  LYS F N   
10910 C CA  . LYS F 82  ? 0.3236 0.5406 0.3117 0.0178  0.0619  -0.1137 82  LYS F CA  
10911 C C   . LYS F 82  ? 0.3148 0.4797 0.3085 0.0246  0.0567  -0.1011 82  LYS F C   
10912 O O   . LYS F 82  ? 0.3072 0.4769 0.3104 0.0312  0.0568  -0.1048 82  LYS F O   
10913 C CB  . LYS F 82  ? 0.3381 0.5563 0.3189 0.0457  0.0546  -0.1324 82  LYS F CB  
10914 C CG  . LYS F 82  ? 0.3471 0.5481 0.3271 0.0775  0.0449  -0.1469 82  LYS F CG  
10915 C CD  . LYS F 82  ? 0.3799 0.5857 0.3391 0.1109  0.0346  -0.1721 82  LYS F CD  
10916 C CE  . LYS F 82  ? 0.4104 0.5384 0.3404 0.1179  0.0199  -0.1674 82  LYS F CE  
10917 N NZ  . LYS F 82  ? 0.4576 0.5751 0.3534 0.1512  0.0064  -0.1926 82  LYS F NZ  
10918 N N   . LYS F 83  ? 0.7293 0.6859 0.2727 -0.0454 -0.0567 -0.0202 83  LYS F N   
10919 C CA  . LYS F 83  ? 0.6987 0.6519 0.2749 -0.0699 -0.0677 -0.0075 83  LYS F CA  
10920 C C   . LYS F 83  ? 0.6192 0.6254 0.2683 -0.0629 -0.0512 0.0147  83  LYS F C   
10921 O O   . LYS F 83  ? 0.5887 0.5874 0.2683 -0.0650 -0.0506 0.0175  83  LYS F O   
10922 C CB  . LYS F 83  ? 0.7255 0.6870 0.2811 -0.1080 -0.0909 0.0021  83  LYS F CB  
10923 C CG  . LYS F 83  ? 0.8091 0.6939 0.2933 -0.1339 -0.1157 -0.0166 83  LYS F CG  
10924 C CD  . LYS F 83  ? 0.8833 0.6903 0.2978 -0.1044 -0.1147 -0.0472 83  LYS F CD  
10925 C CE  . LYS F 83  ? 0.9838 0.6860 0.3131 -0.1272 -0.1418 -0.0662 83  LYS F CE  
10926 N NZ  . LYS F 83  ? 1.0732 0.7354 0.3224 -0.1509 -0.1630 -0.0768 83  LYS F NZ  
10927 N N   . MET F 84  ? 0.5964 0.6475 0.2645 -0.0550 -0.0392 0.0302  84  MET F N   
10928 C CA  . MET F 84  ? 0.5430 0.6254 0.2620 -0.0475 -0.0252 0.0505  84  MET F CA  
10929 C C   . MET F 84  ? 0.5218 0.5929 0.2598 -0.0318 -0.0089 0.0407  84  MET F C   
10930 O O   . MET F 84  ? 0.4851 0.5547 0.2592 -0.0319 -0.0061 0.0474  84  MET F O   
10931 C CB  . MET F 84  ? 0.5468 0.6603 0.2618 -0.0440 -0.0173 0.0681  84  MET F CB  
10932 C CG  . MET F 84  ? 0.5163 0.6442 0.2644 -0.0402 -0.0118 0.0931  84  MET F CG  
10933 S SD  . MET F 84  ? 0.5294 0.6640 0.2664 -0.0373 0.0069  0.1070  84  MET F SD  
10934 C CE  . MET F 84  ? 0.5079 0.6393 0.2637 -0.0335 0.0233  0.0886  84  MET F CE  
10935 N N   . GLU F 85  ? 0.5470 0.6179 0.2595 -0.0164 0.0013  0.0242  85  GLU F N   
10936 C CA  . GLU F 85  ? 0.5294 0.6094 0.2595 0.0007  0.0171  0.0151  85  GLU F CA  
10937 C C   . GLU F 85  ? 0.5308 0.5684 0.2610 0.0082  0.0086  -0.0008 85  GLU F C   
10938 O O   . GLU F 85  ? 0.4940 0.5382 0.2602 0.0113  0.0162  0.0029  85  GLU F O   
10939 C CB  . GLU F 85  ? 0.5607 0.6705 0.2618 0.0203  0.0301  0.0011  85  GLU F CB  
10940 C CG  . GLU F 85  ? 0.5640 0.7175 0.2616 0.0079  0.0394  0.0196  85  GLU F CG  
10941 C CD  . GLU F 85  ? 0.5623 0.7766 0.2648 0.0143  0.0608  0.0206  85  GLU F CD  
10942 O OE1 . GLU F 85  ? 0.5944 0.8349 0.2677 0.0385  0.0671  -0.0003 85  GLU F OE1 
10943 O OE2 . GLU F 85  ? 0.5379 0.7758 0.2673 -0.0059 0.0703  0.0430  85  GLU F OE2 
10944 N N   . ASP F 86  ? 0.5816 0.5690 0.2646 0.0078  -0.0088 -0.0177 86  ASP F N   
10945 C CA  . ASP F 86  ? 0.6007 0.5318 0.2691 0.0082  -0.0215 -0.0302 86  ASP F CA  
10946 C C   . ASP F 86  ? 0.5542 0.4910 0.2666 -0.0175 -0.0277 -0.0116 86  ASP F C   
10947 O O   . ASP F 86  ? 0.5402 0.4570 0.2678 -0.0139 -0.0280 -0.0148 86  ASP F O   
10948 C CB  . ASP F 86  ? 0.6852 0.5459 0.2777 0.0022  -0.0438 -0.0486 86  ASP F CB  
10949 C CG  . ASP F 86  ? 0.7511 0.5711 0.2854 0.0429  -0.0422 -0.0772 86  ASP F CG  
10950 O OD1 . ASP F 86  ? 0.7418 0.5598 0.2881 0.0711  -0.0335 -0.0860 86  ASP F OD1 
10951 O OD2 . ASP F 86  ? 0.8179 0.6092 0.2906 0.0500  -0.0505 -0.0916 86  ASP F OD2 
10952 N N   . GLY F 87  ? 0.5349 0.5032 0.2642 -0.0400 -0.0334 0.0073  87  GLY F N   
10953 C CA  . GLY F 87  ? 0.4959 0.4855 0.2641 -0.0588 -0.0395 0.0249  87  GLY F CA  
10954 C C   . GLY F 87  ? 0.4399 0.4524 0.2600 -0.0449 -0.0233 0.0348  87  GLY F C   
10955 O O   . GLY F 87  ? 0.4185 0.4259 0.2610 -0.0505 -0.0263 0.0374  87  GLY F O   
10956 N N   . PHE F 88  ? 0.4234 0.4590 0.2567 -0.0308 -0.0070 0.0407  88  PHE F N   
10957 C CA  . PHE F 88  ? 0.3844 0.4332 0.2554 -0.0232 0.0069  0.0501  88  PHE F CA  
10958 C C   . PHE F 88  ? 0.3776 0.4111 0.2555 -0.0124 0.0137  0.0343  88  PHE F C   
10959 O O   . PHE F 88  ? 0.3471 0.3810 0.2552 -0.0122 0.0178  0.0391  88  PHE F O   
10960 C CB  . PHE F 88  ? 0.3854 0.4562 0.2555 -0.0209 0.0198  0.0626  88  PHE F CB  
10961 C CG  . PHE F 88  ? 0.3896 0.4690 0.2581 -0.0250 0.0139  0.0837  88  PHE F CG  
10962 C CD1 . PHE F 88  ? 0.3713 0.4486 0.2614 -0.0212 0.0097  0.0969  88  PHE F CD1 
10963 C CD2 . PHE F 88  ? 0.4178 0.5087 0.2589 -0.0275 0.0119  0.0898  88  PHE F CD2 
10964 C CE1 . PHE F 88  ? 0.3854 0.4710 0.2671 -0.0143 0.0029  0.1153  88  PHE F CE1 
10965 C CE2 . PHE F 88  ? 0.4289 0.5269 0.2636 -0.0254 0.0049  0.1098  88  PHE F CE2 
10966 C CZ  . PHE F 88  ? 0.4149 0.5097 0.2686 -0.0161 0.0000  0.1224  88  PHE F CZ  
10967 N N   . LEU F 89  ? 0.4117 0.4319 0.2575 0.0009  0.0140  0.0148  89  LEU F N   
10968 C CA  . LEU F 89  ? 0.4161 0.4219 0.2607 0.0194  0.0176  -0.0016 89  LEU F CA  
10969 C C   . LEU F 89  ? 0.4170 0.3805 0.2626 0.0110  0.0037  -0.0039 89  LEU F C   
10970 O O   . LEU F 89  ? 0.3946 0.3573 0.2625 0.0185  0.0083  -0.0058 89  LEU F O   
10971 C CB  . LEU F 89  ? 0.4698 0.4619 0.2657 0.0450  0.0168  -0.0244 89  LEU F CB  
10972 C CG  . LEU F 89  ? 0.4734 0.5220 0.2661 0.0575  0.0330  -0.0252 89  LEU F CG  
10973 C CD1 . LEU F 89  ? 0.5346 0.5684 0.2731 0.0933  0.0307  -0.0520 89  LEU F CD1 
10974 C CD2 . LEU F 89  ? 0.4280 0.5369 0.2657 0.0547  0.0516  -0.0139 89  LEU F CD2 
10975 N N   . ASP F 90  ? 0.4471 0.3799 0.2655 -0.0084 -0.0139 -0.0027 90  ASP F N   
10976 C CA  . ASP F 90  ? 0.4567 0.3549 0.2696 -0.0267 -0.0290 -0.0016 90  ASP F CA  
10977 C C   . ASP F 90  ? 0.3966 0.3353 0.2656 -0.0376 -0.0233 0.0169  90  ASP F C   
10978 O O   . ASP F 90  ? 0.3859 0.3108 0.2670 -0.0407 -0.0258 0.0166  90  ASP F O   
10979 C CB  . ASP F 90  ? 0.5081 0.3768 0.2756 -0.0557 -0.0503 -0.0015 90  ASP F CB  
10980 C CG  . ASP F 90  ? 0.5891 0.3937 0.2834 -0.0446 -0.0606 -0.0232 90  ASP F CG  
10981 O OD1 . ASP F 90  ? 0.6111 0.3874 0.2862 -0.0102 -0.0540 -0.0403 90  ASP F OD1 
10982 O OD2 . ASP F 90  ? 0.6365 0.4213 0.2885 -0.0680 -0.0762 -0.0237 90  ASP F OD2 
10983 N N   . VAL F 91  ? 0.3666 0.3506 0.2626 -0.0400 -0.0168 0.0326  91  VAL F N   
10984 C CA  . VAL F 91  ? 0.3226 0.3394 0.2615 -0.0404 -0.0116 0.0488  91  VAL F CA  
10985 C C   . VAL F 91  ? 0.2959 0.3082 0.2597 -0.0256 0.0026  0.0457  91  VAL F C   
10986 O O   . VAL F 91  ? 0.2741 0.2871 0.2600 -0.0269 0.0023  0.0485  91  VAL F O   
10987 C CB  . VAL F 91  ? 0.3144 0.3658 0.2620 -0.0365 -0.0087 0.0651  91  VAL F CB  
10988 C CG1 . VAL F 91  ? 0.2856 0.3535 0.2639 -0.0251 -0.0022 0.0784  91  VAL F CG1 
10989 C CG2 . VAL F 91  ? 0.3341 0.4083 0.2653 -0.0528 -0.0245 0.0711  91  VAL F CG2 
10990 N N   . TRP F 92  ? 0.3001 0.3154 0.2591 -0.0143 0.0146  0.0404  92  TRP F N   
10991 C CA  . TRP F 92  ? 0.2789 0.3021 0.2596 -0.0065 0.0276  0.0390  92  TRP F CA  
10992 C C   . TRP F 92  ? 0.2824 0.2891 0.2607 0.0036  0.0259  0.0230  92  TRP F C   
10993 O O   . TRP F 92  ? 0.2592 0.2722 0.2611 0.0061  0.0318  0.0236  92  TRP F O   
10994 C CB  . TRP F 92  ? 0.2861 0.3338 0.2610 -0.0050 0.0405  0.0417  92  TRP F CB  
10995 C CG  . TRP F 92  ? 0.2880 0.3380 0.2636 -0.0151 0.0426  0.0613  92  TRP F CG  
10996 C CD1 . TRP F 92  ? 0.3105 0.3658 0.2647 -0.0187 0.0413  0.0699  92  TRP F CD1 
10997 C CD2 . TRP F 92  ? 0.2789 0.3156 0.2675 -0.0190 0.0442  0.0744  92  TRP F CD2 
10998 N NE1 . TRP F 92  ? 0.3197 0.3620 0.2702 -0.0230 0.0414  0.0885  92  TRP F NE1 
10999 C CE2 . TRP F 92  ? 0.3045 0.3312 0.2726 -0.0220 0.0428  0.0907  92  TRP F CE2 
11000 C CE3 . TRP F 92  ? 0.2601 0.2867 0.2688 -0.0182 0.0458  0.0733  92  TRP F CE3 
11001 C CZ2 . TRP F 92  ? 0.3213 0.3181 0.2808 -0.0207 0.0415  0.1050  92  TRP F CZ2 
11002 C CZ3 . TRP F 92  ? 0.2713 0.2739 0.2755 -0.0193 0.0456  0.0865  92  TRP F CZ3 
11003 C CH2 . TRP F 92  ? 0.3062 0.2893 0.2823 -0.0188 0.0428  0.1017  92  TRP F CH2 
11004 N N   . THR F 93  ? 0.3211 0.2993 0.2634 0.0109  0.0162  0.0086  93  THR F N   
11005 C CA  . THR F 93  ? 0.3429 0.2882 0.2680 0.0251  0.0103  -0.0062 93  THR F CA  
11006 C C   . THR F 93  ? 0.3301 0.2544 0.2685 0.0077  0.0007  0.0014  93  THR F C   
11007 O O   . THR F 93  ? 0.3174 0.2374 0.2700 0.0153  0.0029  -0.0013 93  THR F O   
11008 C CB  . THR F 93  ? 0.4103 0.3064 0.2740 0.0382  -0.0022 -0.0237 93  THR F CB  
11009 O OG1 . THR F 93  ? 0.4235 0.3502 0.2749 0.0604  0.0085  -0.0327 93  THR F OG1 
11010 C CG2 . THR F 93  ? 0.4501 0.2936 0.2818 0.0566  -0.0121 -0.0380 93  THR F CG2 
11011 N N   . TYR F 94  ? 0.3354 0.2566 0.2689 -0.0162 -0.0100 0.0118  94  TYR F N   
11012 C CA  . TYR F 94  ? 0.3254 0.2450 0.2708 -0.0368 -0.0192 0.0212  94  TYR F CA  
11013 C C   . TYR F 94  ? 0.2726 0.2288 0.2676 -0.0304 -0.0067 0.0307  94  TYR F C   
11014 O O   . TYR F 94  ? 0.2634 0.2111 0.2681 -0.0328 -0.0086 0.0304  94  TYR F O   
11015 C CB  . TYR F 94  ? 0.3363 0.2749 0.2727 -0.0632 -0.0310 0.0326  94  TYR F CB  
11016 C CG  . TYR F 94  ? 0.3138 0.2872 0.2741 -0.0835 -0.0367 0.0467  94  TYR F CG  
11017 C CD1 . TYR F 94  ? 0.2673 0.2966 0.2710 -0.0725 -0.0266 0.0593  94  TYR F CD1 
11018 C CD2 . TYR F 94  ? 0.3492 0.2988 0.2809 -0.1134 -0.0531 0.0477  94  TYR F CD2 
11019 C CE1 . TYR F 94  ? 0.2497 0.3233 0.2738 -0.0839 -0.0309 0.0708  94  TYR F CE1 
11020 C CE2 . TYR F 94  ? 0.3287 0.3274 0.2833 -0.1343 -0.0573 0.0618  94  TYR F CE2 
11021 C CZ  . TYR F 94  ? 0.2752 0.3427 0.2791 -0.1161 -0.0452 0.0724  94  TYR F CZ  
11022 O OH  . TYR F 94  ? 0.2578 0.3857 0.2831 -0.1298 -0.0484 0.0849  94  TYR F OH  
11023 N N   . ASN F 95  ? 0.2488 0.2368 0.2663 -0.0230 0.0045  0.0390  95  ASN F N   
11024 C CA  . ASN F 95  ? 0.2172 0.2232 0.2664 -0.0161 0.0147  0.0467  95  ASN F CA  
11025 C C   . ASN F 95  ? 0.2083 0.2047 0.2677 -0.0079 0.0220  0.0376  95  ASN F C   
11026 O O   . ASN F 95  ? 0.1905 0.1888 0.2684 -0.0082 0.0230  0.0400  95  ASN F O   
11027 C CB  . ASN F 95  ? 0.2169 0.2351 0.2675 -0.0107 0.0232  0.0558  95  ASN F CB  
11028 C CG  . ASN F 95  ? 0.2246 0.2600 0.2698 -0.0115 0.0161  0.0679  95  ASN F CG  
11029 O OD1 . ASN F 95  ? 0.2252 0.2774 0.2711 -0.0196 0.0055  0.0702  95  ASN F OD1 
11030 N ND2 . ASN F 95  ? 0.2367 0.2716 0.2727 -0.0050 0.0207  0.0772  95  ASN F ND2 
11031 N N   . ALA F 96  ? 0.2232 0.2178 0.2695 0.0014  0.0268  0.0269  96  ALA F N   
11032 C CA  . ALA F 96  ? 0.2167 0.2194 0.2720 0.0127  0.0336  0.0179  96  ALA F CA  
11033 C C   . ALA F 96  ? 0.2255 0.2002 0.2736 0.0177  0.0239  0.0106  96  ALA F C   
11034 O O   . ALA F 96  ? 0.2059 0.1875 0.2741 0.0186  0.0269  0.0114  96  ALA F O   
11035 C CB  . ALA F 96  ? 0.2369 0.2587 0.2753 0.0278  0.0396  0.0071  96  ALA F CB  
11036 N N   . GLU F 97  ? 0.2646 0.2010 0.2765 0.0181  0.0107  0.0042  97  GLU F N   
11037 C CA  . GLU F 97  ? 0.2943 0.1869 0.2818 0.0200  -0.0017 -0.0018 97  GLU F CA  
11038 C C   . GLU F 97  ? 0.2719 0.1675 0.2794 -0.0031 -0.0065 0.0107  97  GLU F C   
11039 O O   . GLU F 97  ? 0.2764 0.1553 0.2824 -0.0015 -0.0105 0.0093  97  GLU F O   
11040 C CB  . GLU F 97  ? 0.3628 0.1963 0.2895 0.0201  -0.0181 -0.0108 97  GLU F CB  
11041 C CG  . GLU F 97  ? 0.3976 0.2252 0.2948 0.0534  -0.0144 -0.0273 97  GLU F CG  
11042 C CD  . GLU F 97  ? 0.4844 0.2338 0.3057 0.0587  -0.0333 -0.0394 97  GLU F CD  
11043 O OE1 . GLU F 97  ? 0.5175 0.2198 0.3097 0.0257  -0.0498 -0.0323 97  GLU F OE1 
11044 O OE2 . GLU F 97  ? 0.5282 0.2645 0.3135 0.0952  -0.0324 -0.0563 97  GLU F OE2 
11045 N N   . LEU F 98  ? 0.2514 0.1745 0.2754 -0.0216 -0.0063 0.0232  98  LEU F N   
11046 C CA  . LEU F 98  ? 0.2297 0.1753 0.2738 -0.0386 -0.0094 0.0351  98  LEU F CA  
11047 C C   . LEU F 98  ? 0.1892 0.1598 0.2704 -0.0254 0.0034  0.0370  98  LEU F C   
11048 O O   . LEU F 98  ? 0.1813 0.1523 0.2707 -0.0294 0.0014  0.0386  98  LEU F O   
11049 C CB  . LEU F 98  ? 0.2226 0.2055 0.2733 -0.0528 -0.0124 0.0471  98  LEU F CB  
11050 C CG  . LEU F 98  ? 0.2055 0.2314 0.2746 -0.0671 -0.0161 0.0595  98  LEU F CG  
11051 C CD1 . LEU F 98  ? 0.2412 0.2454 0.2802 -0.0983 -0.0319 0.0616  98  LEU F CD1 
11052 C CD2 . LEU F 98  ? 0.1953 0.2760 0.2762 -0.0675 -0.0164 0.0708  98  LEU F CD2 
11053 N N   . LEU F 99  ? 0.1720 0.1585 0.2686 -0.0135 0.0151  0.0373  99  LEU F N   
11054 C CA  . LEU F 99  ? 0.1494 0.1474 0.2687 -0.0064 0.0250  0.0390  99  LEU F CA  
11055 C C   . LEU F 99  ? 0.1457 0.1351 0.2691 -0.0016 0.0260  0.0301  99  LEU F C   
11056 O O   . LEU F 99  ? 0.1316 0.1258 0.2692 -0.0020 0.0277  0.0317  99  LEU F O   
11057 C CB  . LEU F 99  ? 0.1515 0.1542 0.2706 -0.0030 0.0345  0.0411  99  LEU F CB  
11058 C CG  . LEU F 99  ? 0.1479 0.1473 0.2748 -0.0033 0.0418  0.0445  99  LEU F CG  
11059 C CD1 . LEU F 99  ? 0.1481 0.1438 0.2770 0.0036  0.0388  0.0517  99  LEU F CD1 
11060 C CD2 . LEU F 99  ? 0.1663 0.1614 0.2797 -0.0100 0.0483  0.0491  99  LEU F CD2 
11061 N N   . VAL F 100 ? 0.1632 0.1420 0.2704 0.0071  0.0243  0.0201  100 VAL F N   
11062 C CA  . VAL F 100 ? 0.1672 0.1422 0.2730 0.0194  0.0234  0.0112  100 VAL F CA  
11063 C C   . VAL F 100 ? 0.1781 0.1250 0.2734 0.0129  0.0121  0.0133  100 VAL F C   
11064 O O   . VAL F 100 ? 0.1633 0.1181 0.2735 0.0140  0.0138  0.0137  100 VAL F O   
11065 C CB  . VAL F 100 ? 0.1957 0.1684 0.2778 0.0409  0.0226  -0.0013 100 VAL F CB  
11066 C CG1 . VAL F 100 ? 0.2161 0.1762 0.2840 0.0623  0.0167  -0.0109 100 VAL F CG1 
11067 C CG2 . VAL F 100 ? 0.1789 0.2005 0.2782 0.0425  0.0363  -0.0015 100 VAL F CG2 
11068 N N   . LEU F 101 ? 0.2091 0.1242 0.2748 0.0013  -0.0001 0.0158  101 LEU F N   
11069 C CA  . LEU F 101 ? 0.2299 0.1194 0.2777 -0.0162 -0.0127 0.0217  101 LEU F CA  
11070 C C   . LEU F 101 ? 0.1906 0.1206 0.2736 -0.0283 -0.0070 0.0322  101 LEU F C   
11071 O O   . LEU F 101 ? 0.1922 0.1161 0.2750 -0.0313 -0.0101 0.0337  101 LEU F O   
11072 C CB  . LEU F 101 ? 0.2723 0.1325 0.2818 -0.0400 -0.0271 0.0266  101 LEU F CB  
11073 C CG  . LEU F 101 ? 0.3501 0.1310 0.2929 -0.0415 -0.0454 0.0194  101 LEU F CG  
11074 C CD1 . LEU F 101 ? 0.3732 0.1269 0.2973 0.0000  -0.0426 0.0024  101 LEU F CD1 
11075 C CD2 . LEU F 101 ? 0.3930 0.1494 0.2974 -0.0687 -0.0582 0.0232  101 LEU F CD2 
11076 N N   . MET F 102 ? 0.1628 0.1316 0.2697 -0.0313 0.0003  0.0391  102 MET F N   
11077 C CA  . MET F 102 ? 0.1371 0.1448 0.2684 -0.0339 0.0049  0.0473  102 MET F CA  
11078 C C   . MET F 102 ? 0.1164 0.1265 0.2672 -0.0186 0.0146  0.0421  102 MET F C   
11079 O O   . MET F 102 ? 0.1082 0.1312 0.2672 -0.0203 0.0147  0.0444  102 MET F O   
11080 C CB  . MET F 102 ? 0.1268 0.1696 0.2686 -0.0302 0.0087  0.0546  102 MET F CB  
11081 C CG  . MET F 102 ? 0.1463 0.2042 0.2718 -0.0506 -0.0020 0.0620  102 MET F CG  
11082 S SD  . MET F 102 ? 0.1348 0.2548 0.2750 -0.0404 0.0007  0.0727  102 MET F SD  
11083 C CE  . MET F 102 ? 0.1327 0.2189 0.2730 -0.0150 0.0114  0.0666  102 MET F CE  
11084 N N   . GLU F 103 ? 0.1120 0.1135 0.2670 -0.0077 0.0223  0.0357  103 GLU F N   
11085 C CA  . GLU F 103 ? 0.1005 0.1049 0.2680 -0.0014 0.0300  0.0318  103 GLU F CA  
11086 C C   . GLU F 103 ? 0.1008 0.1004 0.2688 0.0009  0.0274  0.0249  103 GLU F C   
11087 O O   . GLU F 103 ? 0.0920 0.0983 0.2697 0.0012  0.0302  0.0233  103 GLU F O   
11088 C CB  . GLU F 103 ? 0.1049 0.1079 0.2708 -0.0004 0.0376  0.0306  103 GLU F CB  
11089 C CG  . GLU F 103 ? 0.1150 0.1128 0.2733 0.0020  0.0395  0.0383  103 GLU F CG  
11090 C CD  . GLU F 103 ? 0.1210 0.1143 0.2772 0.0108  0.0400  0.0411  103 GLU F CD  
11091 O OE1 . GLU F 103 ? 0.1183 0.1068 0.2780 0.0093  0.0413  0.0365  103 GLU F OE1 
11092 O OE2 . GLU F 103 ? 0.1333 0.1308 0.2811 0.0230  0.0385  0.0473  103 GLU F OE2 
11093 N N   . ASN F 104 ? 0.1189 0.1027 0.2702 0.0058  0.0206  0.0201  104 ASN F N   
11094 C CA  . ASN F 104 ? 0.1321 0.1038 0.2734 0.0149  0.0144  0.0145  104 ASN F CA  
11095 C C   . ASN F 104 ? 0.1336 0.0970 0.2727 0.0036  0.0082  0.0212  104 ASN F C   
11096 O O   . ASN F 104 ? 0.1283 0.0973 0.2735 0.0081  0.0082  0.0191  104 ASN F O   
11097 C CB  . ASN F 104 ? 0.1732 0.1095 0.2783 0.0276  0.0041  0.0084  104 ASN F CB  
11098 C CG  . ASN F 104 ? 0.1764 0.1339 0.2816 0.0491  0.0103  -0.0015 104 ASN F CG  
11099 O OD1 . ASN F 104 ? 0.1472 0.1504 0.2806 0.0482  0.0216  -0.0024 104 ASN F OD1 
11100 N ND2 . ASN F 104 ? 0.2204 0.1447 0.2876 0.0670  0.0018  -0.0091 104 ASN F ND2 
11101 N N   . GLU F 105 ? 0.1421 0.1005 0.2717 -0.0132 0.0027  0.0300  105 GLU F N   
11102 C CA  . GLU F 105 ? 0.1455 0.1111 0.2722 -0.0291 -0.0025 0.0387  105 GLU F CA  
11103 C C   . GLU F 105 ? 0.1110 0.1148 0.2676 -0.0233 0.0081  0.0392  105 GLU F C   
11104 O O   . GLU F 105 ? 0.1095 0.1196 0.2676 -0.0258 0.0069  0.0406  105 GLU F O   
11105 C CB  . GLU F 105 ? 0.1627 0.1363 0.2748 -0.0533 -0.0101 0.0496  105 GLU F CB  
11106 C CG  . GLU F 105 ? 0.1857 0.1618 0.2799 -0.0788 -0.0200 0.0603  105 GLU F CG  
11107 C CD  . GLU F 105 ? 0.2182 0.1984 0.2861 -0.1129 -0.0318 0.0720  105 GLU F CD  
11108 O OE1 . GLU F 105 ? 0.1961 0.2265 0.2848 -0.1144 -0.0263 0.0760  105 GLU F OE1 
11109 O OE2 . GLU F 105 ? 0.2749 0.2050 0.2952 -0.1392 -0.0481 0.0778  105 GLU F OE2 
11110 N N   . ARG F 106 ? 0.0930 0.1142 0.2651 -0.0145 0.0173  0.0379  106 ARG F N   
11111 C CA  . ARG F 106 ? 0.0805 0.1177 0.2650 -0.0048 0.0253  0.0361  106 ARG F CA  
11112 C C   . ARG F 106 ? 0.0757 0.1004 0.2640 -0.0010 0.0282  0.0277  106 ARG F C   
11113 O O   . ARG F 106 ? 0.0745 0.1052 0.2650 0.0015  0.0303  0.0258  106 ARG F O   
11114 C CB  . ARG F 106 ? 0.0846 0.1238 0.2688 0.0057  0.0312  0.0370  106 ARG F CB  
11115 C CG  . ARG F 106 ? 0.0878 0.1585 0.2712 0.0073  0.0288  0.0458  106 ARG F CG  
11116 C CD  . ARG F 106 ? 0.1011 0.1769 0.2780 0.0308  0.0339  0.0461  106 ARG F CD  
11117 N NE  . ARG F 106 ? 0.1055 0.2143 0.2821 0.0463  0.0354  0.0467  106 ARG F NE  
11118 C CZ  . ARG F 106 ? 0.1316 0.2239 0.2903 0.0738  0.0390  0.0415  106 ARG F CZ  
11119 N NH1 . ARG F 106 ? 0.1606 0.1947 0.2961 0.0818  0.0402  0.0371  106 ARG F NH1 
11120 N NH2 . ARG F 106 ? 0.1388 0.2690 0.2948 0.0930  0.0404  0.0407  106 ARG F NH2 
11121 N N   . THR F 107 ? 0.0751 0.0903 0.2626 -0.0001 0.0280  0.0225  107 THR F N   
11122 C CA  . THR F 107 ? 0.0707 0.0929 0.2636 0.0012  0.0300  0.0155  107 THR F CA  
11123 C C   . THR F 107 ? 0.0707 0.0943 0.2618 0.0038  0.0236  0.0147  107 THR F C   
11124 O O   . THR F 107 ? 0.0662 0.1002 0.2628 0.0020  0.0252  0.0116  107 THR F O   
11125 C CB  . THR F 107 ? 0.0738 0.1070 0.2670 0.0054  0.0315  0.0106  107 THR F CB  
11126 O OG1 . THR F 107 ? 0.0758 0.1088 0.2682 -0.0019 0.0379  0.0127  107 THR F OG1 
11127 C CG2 . THR F 107 ? 0.0717 0.1336 0.2727 0.0062  0.0324  0.0046  107 THR F CG2 
11128 N N   . LEU F 108 ? 0.0836 0.0896 0.2593 0.0056  0.0146  0.0183  108 LEU F N   
11129 C CA  . LEU F 108 ? 0.0965 0.0924 0.2600 0.0065  0.0062  0.0200  108 LEU F CA  
11130 C C   . LEU F 108 ? 0.0846 0.0962 0.2554 -0.0047 0.0086  0.0256  108 LEU F C   
11131 O O   . LEU F 108 ? 0.0839 0.1029 0.2562 -0.0030 0.0074  0.0239  108 LEU F O   
11132 C CB  . LEU F 108 ? 0.1354 0.0897 0.2639 0.0054  -0.0069 0.0244  108 LEU F CB  
11133 C CG  . LEU F 108 ? 0.1605 0.0923 0.2697 0.0256  -0.0112 0.0164  108 LEU F CG  
11134 C CD1 . LEU F 108 ? 0.2223 0.0895 0.2778 0.0258  -0.0286 0.0199  108 LEU F CD1 
11135 C CD2 . LEU F 108 ? 0.1519 0.1142 0.2743 0.0497  -0.0073 0.0065  108 LEU F CD2 
11136 N N   . ASP F 109 ? 0.0769 0.1010 0.2510 -0.0131 0.0118  0.0318  109 ASP F N   
11137 C CA  . ASP F 109 ? 0.0686 0.1213 0.2482 -0.0165 0.0154  0.0360  109 ASP F CA  
11138 C C   . ASP F 109 ? 0.0585 0.1172 0.2474 -0.0039 0.0239  0.0269  109 ASP F C   
11139 O O   . ASP F 109 ? 0.0603 0.1338 0.2475 -0.0016 0.0254  0.0260  109 ASP F O   
11140 C CB  . ASP F 109 ? 0.0672 0.1471 0.2481 -0.0219 0.0168  0.0442  109 ASP F CB  
11141 C CG  . ASP F 109 ? 0.0882 0.1642 0.2507 -0.0461 0.0057  0.0557  109 ASP F CG  
11142 O OD1 . ASP F 109 ? 0.1105 0.1643 0.2533 -0.0595 -0.0033 0.0600  109 ASP F OD1 
11143 O OD2 . ASP F 109 ? 0.0903 0.1820 0.2518 -0.0538 0.0046  0.0612  109 ASP F OD2 
11144 N N   . PHE F 110 ? 0.0563 0.0995 0.2476 0.0010  0.0283  0.0206  110 PHE F N   
11145 C CA  . PHE F 110 ? 0.0652 0.0965 0.2506 0.0043  0.0330  0.0125  110 PHE F CA  
11146 C C   . PHE F 110 ? 0.0640 0.1004 0.2514 -0.0014 0.0300  0.0075  110 PHE F C   
11147 O O   . PHE F 110 ? 0.0759 0.1090 0.2538 -0.0005 0.0309  0.0027  110 PHE F O   
11148 C CB  . PHE F 110 ? 0.0731 0.0857 0.2543 0.0003  0.0359  0.0104  110 PHE F CB  
11149 C CG  . PHE F 110 ? 0.1005 0.0879 0.2626 -0.0072 0.0375  0.0041  110 PHE F CG  
11150 C CD1 . PHE F 110 ? 0.1324 0.0907 0.2678 0.0032  0.0380  0.0007  110 PHE F CD1 
11151 C CD2 . PHE F 110 ? 0.1047 0.0970 0.2678 -0.0257 0.0373  0.0017  110 PHE F CD2 
11152 C CE1 . PHE F 110 ? 0.1773 0.0923 0.2789 -0.0081 0.0361  -0.0051 110 PHE F CE1 
11153 C CE2 . PHE F 110 ? 0.1418 0.1072 0.2784 -0.0442 0.0363  -0.0019 110 PHE F CE2 
11154 C CZ  . PHE F 110 ? 0.1830 0.0996 0.2844 -0.0372 0.0346  -0.0055 110 PHE F CZ  
11155 N N   . HIS F 111 ? 0.0552 0.0999 0.2504 -0.0036 0.0255  0.0079  111 HIS F N   
11156 C CA  . HIS F 111 ? 0.0554 0.1141 0.2525 -0.0041 0.0209  0.0043  111 HIS F CA  
11157 C C   . HIS F 111 ? 0.0580 0.1183 0.2487 -0.0031 0.0170  0.0084  111 HIS F C   
11158 O O   . HIS F 111 ? 0.0619 0.1315 0.2506 -0.0050 0.0159  0.0044  111 HIS F O   
11159 C CB  . HIS F 111 ? 0.0563 0.1242 0.2555 0.0051  0.0154  0.0039  111 HIS F CB  
11160 C CG  . HIS F 111 ? 0.0528 0.1415 0.2605 0.0029  0.0199  -0.0008 111 HIS F CG  
11161 N ND1 . HIS F 111 ? 0.0539 0.1701 0.2669 -0.0112 0.0226  -0.0054 111 HIS F ND1 
11162 C CD2 . HIS F 111 ? 0.0530 0.1437 0.2611 0.0094  0.0216  -0.0008 111 HIS F CD2 
11163 C CE1 . HIS F 111 ? 0.0535 0.1943 0.2718 -0.0161 0.0263  -0.0066 111 HIS F CE1 
11164 N NE2 . HIS F 111 ? 0.0509 0.1775 0.2676 -0.0006 0.0265  -0.0045 111 HIS F NE2 
11165 N N   . ASP F 112 ? 0.0596 0.1143 0.2442 -0.0044 0.0142  0.0173  112 ASP F N   
11166 C CA  . ASP F 112 ? 0.0666 0.1303 0.2418 -0.0103 0.0104  0.0246  112 ASP F CA  
11167 C C   . ASP F 112 ? 0.0628 0.1476 0.2403 -0.0066 0.0183  0.0204  112 ASP F C   
11168 O O   . ASP F 112 ? 0.0685 0.1654 0.2403 -0.0074 0.0171  0.0198  112 ASP F O   
11169 C CB  . ASP F 112 ? 0.0772 0.1363 0.2407 -0.0222 0.0052  0.0369  112 ASP F CB  
11170 C CG  . ASP F 112 ? 0.0968 0.1618 0.2417 -0.0377 -0.0021 0.0482  112 ASP F CG  
11171 O OD1 . ASP F 112 ? 0.1006 0.1688 0.2422 -0.0344 -0.0038 0.0461  112 ASP F OD1 
11172 O OD2 . ASP F 112 ? 0.1125 0.1809 0.2429 -0.0573 -0.0072 0.0604  112 ASP F OD2 
11173 N N   . SER F 113 ? 0.0611 0.1454 0.2404 0.0014  0.0253  0.0168  113 SER F N   
11174 C CA  . SER F 113 ? 0.0741 0.1646 0.2427 0.0155  0.0314  0.0100  113 SER F CA  
11175 C C   . SER F 113 ? 0.0918 0.1580 0.2476 0.0153  0.0309  -0.0018 113 SER F C   
11176 O O   . SER F 113 ? 0.1084 0.1800 0.2493 0.0235  0.0322  -0.0073 113 SER F O   
11177 C CB  . SER F 113 ? 0.0825 0.1623 0.2454 0.0292  0.0361  0.0085  113 SER F CB  
11178 O OG  . SER F 113 ? 0.1144 0.1770 0.2519 0.0501  0.0396  -0.0011 113 SER F OG  
11179 N N   . ASN F 114 ? 0.0921 0.1374 0.2509 0.0040  0.0288  -0.0057 114 ASN F N   
11180 C CA  . ASN F 114 ? 0.1135 0.1426 0.2580 -0.0062 0.0264  -0.0153 114 ASN F CA  
11181 C C   . ASN F 114 ? 0.1077 0.1608 0.2566 -0.0101 0.0217  -0.0159 114 ASN F C   
11182 O O   . ASN F 114 ? 0.1320 0.1749 0.2612 -0.0133 0.0203  -0.0242 114 ASN F O   
11183 C CB  . ASN F 114 ? 0.1119 0.1379 0.2631 -0.0231 0.0248  -0.0161 114 ASN F CB  
11184 C CG  . ASN F 114 ? 0.1308 0.1237 0.2674 -0.0244 0.0283  -0.0159 114 ASN F CG  
11185 O OD1 . ASN F 114 ? 0.1632 0.1193 0.2714 -0.0129 0.0299  -0.0192 114 ASN F OD1 
11186 N ND2 . ASN F 114 ? 0.1171 0.1229 0.2681 -0.0346 0.0290  -0.0122 114 ASN F ND2 
11187 N N   . VAL F 115 ? 0.0854 0.1620 0.2519 -0.0094 0.0178  -0.0072 115 VAL F N   
11188 C CA  . VAL F 115 ? 0.0862 0.1810 0.2517 -0.0105 0.0117  -0.0050 115 VAL F CA  
11189 C C   . VAL F 115 ? 0.0961 0.1992 0.2489 -0.0061 0.0145  -0.0038 115 VAL F C   
11190 O O   . VAL F 115 ? 0.1080 0.2189 0.2505 -0.0075 0.0123  -0.0086 115 VAL F O   
11191 C CB  . VAL F 115 ? 0.0798 0.1777 0.2503 -0.0071 0.0042  0.0054  115 VAL F CB  
11192 C CG1 . VAL F 115 ? 0.0919 0.1983 0.2513 -0.0067 -0.0038 0.0104  115 VAL F CG1 
11193 C CG2 . VAL F 115 ? 0.0750 0.1771 0.2554 -0.0026 0.0013  0.0021  115 VAL F CG2 
11194 N N   . LYS F 116 ? 0.0925 0.2034 0.2460 -0.0007 0.0192  0.0027  116 LYS F N   
11195 C CA  . LYS F 116 ? 0.1013 0.2411 0.2448 0.0060  0.0235  0.0051  116 LYS F CA  
11196 C C   . LYS F 116 ? 0.1278 0.2554 0.2500 0.0222  0.0284  -0.0103 116 LYS F C   
11197 O O   . LYS F 116 ? 0.1420 0.2873 0.2503 0.0276  0.0291  -0.0140 116 LYS F O   
11198 C CB  . LYS F 116 ? 0.0933 0.2576 0.2431 0.0089  0.0277  0.0145  116 LYS F CB  
11199 C CG  . LYS F 116 ? 0.0940 0.3070 0.2415 -0.0029 0.0266  0.0289  116 LYS F CG  
11200 C CD  . LYS F 116 ? 0.1072 0.3616 0.2431 0.0125  0.0333  0.0233  116 LYS F CD  
11201 C CE  . LYS F 116 ? 0.1104 0.4191 0.2423 -0.0088 0.0310  0.0401  116 LYS F CE  
11202 N NZ  . LYS F 116 ? 0.1051 0.4700 0.2439 -0.0182 0.0336  0.0536  116 LYS F NZ  
11203 N N   . ASN F 117 ? 0.1445 0.2341 0.2559 0.0299  0.0305  -0.0193 117 ASN F N   
11204 C CA  . ASN F 117 ? 0.1922 0.2448 0.2653 0.0460  0.0319  -0.0347 117 ASN F CA  
11205 C C   . ASN F 117 ? 0.2146 0.2449 0.2706 0.0298  0.0256  -0.0442 117 ASN F C   
11206 O O   . ASN F 117 ? 0.2562 0.2684 0.2766 0.0418  0.0250  -0.0559 117 ASN F O   
11207 C CB  . ASN F 117 ? 0.2178 0.2204 0.2727 0.0525  0.0324  -0.0392 117 ASN F CB  
11208 C CG  . ASN F 117 ? 0.2064 0.2344 0.2705 0.0753  0.0382  -0.0320 117 ASN F CG  
11209 O OD1 . ASN F 117 ? 0.1904 0.2761 0.2664 0.0889  0.0424  -0.0260 117 ASN F OD1 
11210 N ND2 . ASN F 117 ? 0.2173 0.2095 0.2748 0.0768  0.0380  -0.0312 117 ASN F ND2 
11211 N N   . LEU F 118 ? 0.1916 0.2283 0.2701 0.0049  0.0202  -0.0396 118 LEU F N   
11212 C CA  . LEU F 118 ? 0.2063 0.2425 0.2756 -0.0135 0.0131  -0.0460 118 LEU F CA  
11213 C C   . LEU F 118 ? 0.1974 0.2700 0.2706 -0.0078 0.0118  -0.0431 118 LEU F C   
11214 O O   . LEU F 118 ? 0.2270 0.2923 0.2757 -0.0119 0.0080  -0.0526 118 LEU F O   
11215 C CB  . LEU F 118 ? 0.1805 0.2373 0.2771 -0.0343 0.0081  -0.0404 118 LEU F CB  
11216 C CG  . LEU F 118 ? 0.1908 0.2683 0.2841 -0.0550 -0.0002 -0.0451 118 LEU F CG  
11217 C CD1 . LEU F 118 ? 0.2490 0.2808 0.2960 -0.0727 -0.0039 -0.0586 118 LEU F CD1 
11218 C CD2 . LEU F 118 ? 0.1661 0.2811 0.2875 -0.0671 -0.0035 -0.0394 118 LEU F CD2 
11219 N N   . TYR F 119 ? 0.1652 0.2725 0.2626 -0.0020 0.0136  -0.0291 119 TYR F N   
11220 C CA  . TYR F 119 ? 0.1634 0.3032 0.2589 -0.0012 0.0118  -0.0226 119 TYR F CA  
11221 C C   . TYR F 119 ? 0.1909 0.3390 0.2604 0.0155  0.0184  -0.0311 119 TYR F C   
11222 O O   . TYR F 119 ? 0.2088 0.3676 0.2615 0.0152  0.0161  -0.0361 119 TYR F O   
11223 C CB  . TYR F 119 ? 0.1403 0.3025 0.2530 -0.0056 0.0103  -0.0039 119 TYR F CB  
11224 C CG  . TYR F 119 ? 0.1482 0.3403 0.2506 -0.0111 0.0075  0.0063  119 TYR F CG  
11225 C CD1 . TYR F 119 ? 0.1559 0.3465 0.2527 -0.0185 -0.0024 0.0105  119 TYR F CD1 
11226 C CD2 . TYR F 119 ? 0.1518 0.3812 0.2480 -0.0088 0.0145  0.0131  119 TYR F CD2 
11227 C CE1 . TYR F 119 ? 0.1707 0.3829 0.2517 -0.0262 -0.0062 0.0219  119 TYR F CE1 
11228 C CE2 . TYR F 119 ? 0.1634 0.4262 0.2470 -0.0200 0.0120  0.0249  119 TYR F CE2 
11229 C CZ  . TYR F 119 ? 0.1746 0.4219 0.2486 -0.0300 0.0013  0.0296  119 TYR F CZ  
11230 O OH  . TYR F 119 ? 0.1933 0.4671 0.2487 -0.0435 -0.0024 0.0430  119 TYR F OH  
11231 N N   . ASP F 120 ? 0.1981 0.3460 0.2619 0.0343  0.0262  -0.0331 120 ASP F N   
11232 C CA  . ASP F 120 ? 0.2307 0.3949 0.2659 0.0618  0.0330  -0.0426 120 ASP F CA  
11233 C C   . ASP F 120 ? 0.2877 0.3935 0.2768 0.0720  0.0295  -0.0642 120 ASP F C   
11234 O O   . ASP F 120 ? 0.3207 0.4363 0.2799 0.0889  0.0311  -0.0741 120 ASP F O   
11235 C CB  . ASP F 120 ? 0.2302 0.4120 0.2675 0.0860  0.0407  -0.0402 120 ASP F CB  
11236 C CG  . ASP F 120 ? 0.1875 0.4355 0.2599 0.0715  0.0432  -0.0187 120 ASP F CG  
11237 O OD1 . ASP F 120 ? 0.1750 0.4650 0.2553 0.0528  0.0413  -0.0067 120 ASP F OD1 
11238 O OD2 . ASP F 120 ? 0.1744 0.4283 0.2601 0.0758  0.0457  -0.0129 120 ASP F OD2 
11239 N N   . LYS F 121 ? 0.3069 0.3511 0.2845 0.0583  0.0238  -0.0710 121 LYS F N   
11240 C CA  . LYS F 121 ? 0.3755 0.3496 0.2986 0.0546  0.0166  -0.0896 121 LYS F CA  
11241 C C   . LYS F 121 ? 0.3836 0.3752 0.2988 0.0390  0.0109  -0.0942 121 LYS F C   
11242 O O   . LYS F 121 ? 0.4444 0.4025 0.3080 0.0520  0.0082  -0.1102 121 LYS F O   
11243 C CB  . LYS F 121 ? 0.3843 0.3096 0.3057 0.0244  0.0098  -0.0892 121 LYS F CB  
11244 C CG  . LYS F 121 ? 0.4702 0.3098 0.3237 0.0090  -0.0002 -0.1057 121 LYS F CG  
11245 C CD  . LYS F 121 ? 0.4719 0.2851 0.3307 -0.0300 -0.0062 -0.1001 121 LYS F CD  
11246 C CE  . LYS F 121 ? 0.5771 0.2835 0.3527 -0.0471 -0.0170 -0.1131 121 LYS F CE  
11247 N NZ  . LYS F 121 ? 0.6266 0.3120 0.3646 -0.0860 -0.0295 -0.1223 121 LYS F NZ  
11248 N N   . VAL F 122 ? 0.3302 0.3709 0.2910 0.0148  0.0078  -0.0804 122 VAL F N   
11249 C CA  . VAL F 122 ? 0.3317 0.3994 0.2905 0.0016  0.0017  -0.0812 122 VAL F CA  
11250 C C   . VAL F 122 ? 0.3343 0.4428 0.2856 0.0244  0.0082  -0.0795 122 VAL F C   
11251 O O   . VAL F 122 ? 0.3742 0.4762 0.2901 0.0294  0.0058  -0.0917 122 VAL F O   
11252 C CB  . VAL F 122 ? 0.2807 0.3895 0.2851 -0.0203 -0.0043 -0.0656 122 VAL F CB  
11253 C CG1 . VAL F 122 ? 0.2797 0.4245 0.2832 -0.0268 -0.0109 -0.0625 122 VAL F CG1 
11254 C CG2 . VAL F 122 ? 0.2863 0.3738 0.2939 -0.0443 -0.0109 -0.0695 122 VAL F CG2 
11255 N N   . ARG F 123 ? 0.2975 0.4514 0.2783 0.0348  0.0159  -0.0641 123 ARG F N   
11256 C CA  . ARG F 123 ? 0.2987 0.5092 0.2747 0.0497  0.0228  -0.0585 123 ARG F CA  
11257 C C   . ARG F 123 ? 0.3565 0.5537 0.2840 0.0838  0.0284  -0.0794 123 ARG F C   
11258 O O   . ARG F 123 ? 0.3778 0.6055 0.2842 0.0922  0.0299  -0.0841 123 ARG F O   
11259 C CB  . ARG F 123 ? 0.2616 0.5198 0.2684 0.0508  0.0297  -0.0397 123 ARG F CB  
11260 C CG  . ARG F 123 ? 0.2580 0.5921 0.2646 0.0515  0.0353  -0.0270 123 ARG F CG  
11261 C CD  . ARG F 123 ? 0.2302 0.6133 0.2617 0.0432  0.0400  -0.0073 123 ARG F CD  
11262 N NE  . ARG F 123 ? 0.2316 0.6057 0.2655 0.0691  0.0467  -0.0163 123 ARG F NE  
11263 C CZ  . ARG F 123 ? 0.2597 0.6625 0.2717 0.1089  0.0558  -0.0297 123 ARG F CZ  
11264 N NH1 . ARG F 123 ? 0.2877 0.7353 0.2744 0.1289  0.0610  -0.0375 123 ARG F NH1 
11265 N NH2 . ARG F 123 ? 0.2661 0.6520 0.2767 0.1338  0.0594  -0.0360 123 ARG F NH2 
11266 N N   . LEU F 124 ? 0.3909 0.5377 0.2942 0.1063  0.0305  -0.0923 124 LEU F N   
11267 C CA  . LEU F 124 ? 0.4645 0.5814 0.3075 0.1500  0.0339  -0.1141 124 LEU F CA  
11268 C C   . LEU F 124 ? 0.5349 0.5829 0.3196 0.1452  0.0240  -0.1352 124 LEU F C   
11269 O O   . LEU F 124 ? 0.5987 0.6336 0.3284 0.1815  0.0259  -0.1532 124 LEU F O   
11270 C CB  . LEU F 124 ? 0.4944 0.5594 0.3167 0.1767  0.0354  -0.1209 124 LEU F CB  
11271 C CG  . LEU F 124 ? 0.4426 0.5820 0.3097 0.1917  0.0457  -0.1040 124 LEU F CG  
11272 C CD1 . LEU F 124 ? 0.4609 0.5402 0.3172 0.2042  0.0440  -0.1065 124 LEU F CD1 
11273 C CD2 . LEU F 124 ? 0.4573 0.6809 0.3120 0.2360  0.0564  -0.1066 124 LEU F CD2 
11274 N N   . GLN F 125 ? 0.5296 0.5380 0.3226 0.1014  0.0128  -0.1334 125 GLN F N   
11275 C CA  . GLN F 125 ? 0.5926 0.5474 0.3345 0.0840  0.0011  -0.1502 125 GLN F CA  
11276 C C   . GLN F 125 ? 0.5728 0.5938 0.3271 0.0798  0.0020  -0.1464 125 GLN F C   
11277 O O   . GLN F 125 ? 0.6350 0.6353 0.3346 0.0969  0.0000  -0.1641 125 GLN F O   
11278 C CB  . GLN F 125 ? 0.5853 0.5055 0.3397 0.0337  -0.0109 -0.1461 125 GLN F CB  
11279 C CG  . GLN F 125 ? 0.6274 0.4673 0.3527 0.0266  -0.0152 -0.1514 125 GLN F CG  
11280 C CD  . GLN F 125 ? 0.6204 0.4489 0.3593 -0.0283 -0.0266 -0.1458 125 GLN F CD  
11281 O OE1 . GLN F 125 ? 0.6733 0.4716 0.3719 -0.0591 -0.0390 -0.1560 125 GLN F OE1 
11282 N NE2 . GLN F 125 ? 0.5586 0.4190 0.3527 -0.0416 -0.0229 -0.1298 125 GLN F NE2 
11283 N N   . LEU F 126 ? 0.4962 0.5891 0.3149 0.0580  0.0038  -0.1234 126 LEU F N   
11284 C CA  . LEU F 126 ? 0.4802 0.6301 0.3095 0.0477  0.0019  -0.1157 126 LEU F CA  
11285 C C   . LEU F 126 ? 0.4938 0.6979 0.3077 0.0803  0.0135  -0.1165 126 LEU F C   
11286 O O   . LEU F 126 ? 0.5211 0.7450 0.3088 0.0827  0.0118  -0.1229 126 LEU F O   
11287 C CB  . LEU F 126 ? 0.4108 0.6074 0.2992 0.0206  -0.0016 -0.0900 126 LEU F CB  
11288 C CG  . LEU F 126 ? 0.3936 0.5621 0.3031 -0.0069 -0.0122 -0.0877 126 LEU F CG  
11289 C CD1 . LEU F 126 ? 0.3461 0.5597 0.2967 -0.0220 -0.0186 -0.0660 126 LEU F CD1 
11290 C CD2 . LEU F 126 ? 0.4469 0.5732 0.3153 -0.0246 -0.0231 -0.1070 126 LEU F CD2 
11291 N N   . ARG F 127 ? 0.4782 0.7158 0.3077 0.1047  0.0252  -0.1097 127 ARG F N   
11292 C CA  . ARG F 127 ? 0.4896 0.8026 0.3082 0.1360  0.0375  -0.1088 127 ARG F CA  
11293 C C   . ARG F 127 ? 0.4612 0.8467 0.3011 0.1092  0.0370  -0.0891 127 ARG F C   
11294 O O   . ARG F 127 ? 0.4136 0.8126 0.2939 0.0743  0.0316  -0.0657 127 ARG F O   
11295 C CB  . ARG F 127 ? 0.5743 0.8472 0.3216 0.1828  0.0397  -0.1396 127 ARG F CB  
11296 C CG  . ARG F 127 ? 0.6131 0.8265 0.3328 0.2190  0.0417  -0.1538 127 ARG F CG  
11297 C CD  . ARG F 127 ? 0.7165 0.8090 0.3513 0.2408  0.0314  -0.1850 127 ARG F CD  
11298 N NE  . ARG F 127 ? 0.8002 0.8808 0.3624 0.2812  0.0318  -0.2094 127 ARG F NE  
11299 C CZ  . ARG F 127 ? 0.8075 0.9801 0.3622 0.3256  0.0448  -0.2121 127 ARG F CZ  
11300 N NH1 . ARG F 127 ? 0.7356 1.0320 0.3519 0.3318  0.0590  -0.1898 127 ARG F NH1 
11301 N NH2 . ARG F 127 ? 0.8964 1.0392 0.3745 0.3635  0.0428  -0.2382 127 ARG F NH2 
11302 N N   . ASP F 128 ? 0.4988 0.9233 0.3047 0.1265  0.0411  -0.0981 128 ASP F N   
11303 C CA  . ASP F 128 ? 0.4802 0.9734 0.2991 0.1000  0.0403  -0.0776 128 ASP F CA  
11304 C C   . ASP F 128 ? 0.4941 0.9442 0.2993 0.0752  0.0261  -0.0815 128 ASP F C   
11305 O O   . ASP F 128 ? 0.4964 0.9927 0.2960 0.0606  0.0242  -0.0699 128 ASP F O   
11306 C CB  . ASP F 128 ? 0.5079 1.0909 0.3016 0.1294  0.0539  -0.0811 128 ASP F CB  
11307 C CG  . ASP F 128 ? 0.5802 1.1269 0.3116 0.1708  0.0547  -0.1154 128 ASP F CG  
11308 O OD1 . ASP F 128 ? 0.6156 1.0597 0.3190 0.1725  0.0439  -0.1362 128 ASP F OD1 
11309 O OD2 . ASP F 128 ? 0.6103 1.2317 0.3150 0.2000  0.0653  -0.1214 128 ASP F OD2 
11310 N N   . ASN F 129 ? 0.5071 0.8761 0.3049 0.0680  0.0155  -0.0965 129 ASN F N   
11311 C CA  . ASN F 129 ? 0.5170 0.8578 0.3071 0.0411  0.0004  -0.0989 129 ASN F CA  
11312 C C   . ASN F 129 ? 0.4641 0.8153 0.3010 0.0093  -0.0094 -0.0732 129 ASN F C   
11313 O O   . ASN F 129 ? 0.4684 0.8097 0.3038 -0.0093 -0.0227 -0.0729 129 ASN F O   
11314 C CB  . ASN F 129 ? 0.5678 0.8254 0.3201 0.0410  -0.0084 -0.1261 129 ASN F CB  
11315 C CG  . ASN F 129 ? 0.6493 0.8770 0.3310 0.0687  -0.0067 -0.1544 129 ASN F CG  
11316 O OD1 . ASN F 129 ? 0.6643 0.9419 0.3294 0.0990  0.0048  -0.1565 129 ASN F OD1 
11317 N ND2 . ASN F 129 ? 0.7112 0.8577 0.3447 0.0570  -0.0193 -0.1766 129 ASN F ND2 
11318 N N   . ALA F 130 ? 0.4219 0.7929 0.2941 0.0057  -0.0042 -0.0525 130 ALA F N   
11319 C CA  . ALA F 130 ? 0.3873 0.7577 0.2907 -0.0166 -0.0145 -0.0286 130 ALA F CA  
11320 C C   . ALA F 130 ? 0.3672 0.7707 0.2851 -0.0243 -0.0090 -0.0030 130 ALA F C   
11321 O O   . ALA F 130 ? 0.3637 0.7946 0.2836 -0.0130 0.0039  -0.0046 130 ALA F O   
11322 C CB  . ALA F 130 ? 0.3683 0.6936 0.2944 -0.0203 -0.0202 -0.0350 130 ALA F CB  
11323 N N   . LYS F 131 ? 0.3638 0.7633 0.2851 -0.0438 -0.0207 0.0208  131 LYS F N   
11324 C CA  . LYS F 131 ? 0.3612 0.7739 0.2837 -0.0619 -0.0206 0.0479  131 LYS F CA  
11325 C C   . LYS F 131 ? 0.3361 0.7111 0.2838 -0.0617 -0.0216 0.0508  131 LYS F C   
11326 O O   . LYS F 131 ? 0.3286 0.6609 0.2866 -0.0570 -0.0319 0.0478  131 LYS F O   
11327 C CB  . LYS F 131 ? 0.3910 0.7894 0.2886 -0.0820 -0.0369 0.0723  131 LYS F CB  
11328 C CG  . LYS F 131 ? 0.4202 0.8557 0.2893 -0.0867 -0.0381 0.0744  131 LYS F CG  
11329 C CD  . LYS F 131 ? 0.4555 0.8566 0.2970 -0.0983 -0.0586 0.0949  131 LYS F CD  
11330 C CE  . LYS F 131 ? 0.4944 0.9325 0.2982 -0.1161 -0.0606 0.1106  131 LYS F CE  
11331 N NZ  . LYS F 131 ? 0.5125 0.9831 0.2989 -0.1472 -0.0543 0.1351  131 LYS F NZ  
11332 N N   . GLU F 132 ? 0.3238 0.7239 0.2810 -0.0658 -0.0111 0.0569  132 GLU F N   
11333 C CA  . GLU F 132 ? 0.3047 0.6716 0.2814 -0.0695 -0.0127 0.0627  132 GLU F CA  
11334 C C   . GLU F 132 ? 0.3309 0.6665 0.2862 -0.0974 -0.0277 0.0909  132 GLU F C   
11335 O O   . GLU F 132 ? 0.3521 0.7173 0.2882 -0.1246 -0.0274 0.1117  132 GLU F O   
11336 C CB  . GLU F 132 ? 0.2877 0.6980 0.2789 -0.0629 0.0025  0.0589  132 GLU F CB  
11337 C CG  . GLU F 132 ? 0.2673 0.6453 0.2791 -0.0652 0.0016  0.0622  132 GLU F CG  
11338 C CD  . GLU F 132 ? 0.2503 0.6708 0.2777 -0.0489 0.0163  0.0537  132 GLU F CD  
11339 O OE1 . GLU F 132 ? 0.2584 0.7486 0.2782 -0.0408 0.0268  0.0526  132 GLU F OE1 
11340 O OE2 . GLU F 132 ? 0.2320 0.6205 0.2774 -0.0406 0.0173  0.0478  132 GLU F OE2 
11341 N N   . LEU F 133 ? 0.3390 0.6143 0.2907 -0.0904 -0.0419 0.0918  133 LEU F N   
11342 C CA  . LEU F 133 ? 0.3866 0.6088 0.2997 -0.1075 -0.0607 0.1161  133 LEU F CA  
11343 C C   . LEU F 133 ? 0.4036 0.5948 0.3042 -0.1296 -0.0642 0.1323  133 LEU F C   
11344 O O   . LEU F 133 ? 0.4619 0.6102 0.3133 -0.1565 -0.0793 0.1564  133 LEU F O   
11345 C CB  . LEU F 133 ? 0.3971 0.5713 0.3060 -0.0815 -0.0754 0.1094  133 LEU F CB  
11346 C CG  . LEU F 133 ? 0.4234 0.6037 0.3100 -0.0738 -0.0860 0.1114  133 LEU F CG  
11347 C CD1 . LEU F 133 ? 0.4086 0.6520 0.3019 -0.0827 -0.0734 0.1040  133 LEU F CD1 
11348 C CD2 . LEU F 133 ? 0.4093 0.5844 0.3147 -0.0421 -0.0932 0.0953  133 LEU F CD2 
11349 N N   . GLY F 134 ? 0.3626 0.5688 0.2995 -0.1208 -0.0521 0.1198  134 GLY F N   
11350 C CA  . GLY F 134 ? 0.3761 0.5587 0.3039 -0.1421 -0.0550 0.1329  134 GLY F CA  
11351 C C   . GLY F 134 ? 0.3832 0.4937 0.3099 -0.1240 -0.0650 0.1274  134 GLY F C   
11352 O O   . GLY F 134 ? 0.3987 0.4797 0.3137 -0.1398 -0.0689 0.1360  134 GLY F O   
11353 N N   . ASN F 135 ? 0.3736 0.4649 0.3119 -0.0912 -0.0689 0.1125  135 ASN F N   
11354 C CA  . ASN F 135 ? 0.3849 0.4208 0.3193 -0.0673 -0.0789 0.1068  135 ASN F CA  
11355 C C   . ASN F 135 ? 0.3246 0.3928 0.3104 -0.0403 -0.0670 0.0828  135 ASN F C   
11356 O O   . ASN F 135 ? 0.3288 0.3731 0.3169 -0.0165 -0.0736 0.0760  135 ASN F O   
11357 C CB  . ASN F 135 ? 0.4475 0.4318 0.3355 -0.0510 -0.0996 0.1151  135 ASN F CB  
11358 C CG  . ASN F 135 ? 0.4318 0.4620 0.3355 -0.0360 -0.0980 0.1062  135 ASN F CG  
11359 O OD1 . ASN F 135 ? 0.3798 0.4711 0.3255 -0.0378 -0.0821 0.0917  135 ASN F OD1 
11360 N ND2 . ASN F 135 ? 0.4895 0.4844 0.3516 -0.0203 -0.1163 0.1149  135 ASN F ND2 
11361 N N   . GLY F 136 ? 0.2779 0.3990 0.2975 -0.0438 -0.0506 0.0705  136 GLY F N   
11362 C CA  . GLY F 136 ? 0.2371 0.3796 0.2923 -0.0272 -0.0416 0.0495  136 GLY F CA  
11363 C C   . GLY F 136 ? 0.2330 0.4032 0.2913 -0.0209 -0.0429 0.0386  136 GLY F C   
11364 O O   . GLY F 136 ? 0.2119 0.3989 0.2902 -0.0170 -0.0367 0.0220  136 GLY F O   
11365 N N   . CYS F 137 ? 0.2597 0.4314 0.2924 -0.0241 -0.0522 0.0489  137 CYS F N   
11366 C CA  . CYS F 137 ? 0.2620 0.4618 0.2937 -0.0195 -0.0557 0.0399  137 CYS F CA  
11367 C C   . CYS F 137 ? 0.2658 0.4924 0.2876 -0.0313 -0.0473 0.0373  137 CYS F C   
11368 O O   . CYS F 137 ? 0.2754 0.5066 0.2839 -0.0433 -0.0428 0.0496  137 CYS F O   
11369 C CB  . CYS F 137 ? 0.2962 0.4822 0.3024 -0.0073 -0.0740 0.0516  137 CYS F CB  
11370 S SG  . CYS F 137 ? 0.3037 0.4662 0.3128 0.0209  -0.0853 0.0515  137 CYS F SG  
11371 N N   . PHE F 138 ? 0.2636 0.5124 0.2883 -0.0291 -0.0459 0.0211  138 PHE F N   
11372 C CA  . PHE F 138 ? 0.2770 0.5492 0.2845 -0.0339 -0.0399 0.0148  138 PHE F CA  
11373 C C   . PHE F 138 ? 0.2977 0.5854 0.2903 -0.0345 -0.0521 0.0147  138 PHE F C   
11374 O O   . PHE F 138 ? 0.2945 0.5887 0.2966 -0.0325 -0.0589 0.0042  138 PHE F O   
11375 C CB  . PHE F 138 ? 0.2732 0.5424 0.2832 -0.0300 -0.0288 -0.0080 138 PHE F CB  
11376 C CG  . PHE F 138 ? 0.2578 0.5161 0.2790 -0.0241 -0.0170 -0.0088 138 PHE F CG  
11377 C CD1 . PHE F 138 ? 0.2626 0.5461 0.2741 -0.0187 -0.0065 -0.0049 138 PHE F CD1 
11378 C CD2 . PHE F 138 ? 0.2394 0.4726 0.2807 -0.0231 -0.0165 -0.0127 138 PHE F CD2 
11379 C CE1 . PHE F 138 ? 0.2496 0.5342 0.2719 -0.0104 0.0033  -0.0052 138 PHE F CE1 
11380 C CE2 . PHE F 138 ? 0.2275 0.4516 0.2775 -0.0165 -0.0066 -0.0128 138 PHE F CE2 
11381 C CZ  . PHE F 138 ? 0.2325 0.4827 0.2733 -0.0092 0.0028  -0.0091 138 PHE F CZ  
11382 N N   . GLU F 139 ? 0.3216 0.6227 0.2896 -0.0400 -0.0550 0.0275  139 GLU F N   
11383 C CA  . GLU F 139 ? 0.3459 0.6630 0.2952 -0.0397 -0.0673 0.0296  139 GLU F CA  
11384 C C   . GLU F 139 ? 0.3586 0.7020 0.2930 -0.0437 -0.0597 0.0131  139 GLU F C   
11385 O O   . GLU F 139 ? 0.3661 0.7251 0.2868 -0.0462 -0.0489 0.0154  139 GLU F O   
11386 C CB  . GLU F 139 ? 0.3774 0.6814 0.2979 -0.0446 -0.0781 0.0565  139 GLU F CB  
11387 C CG  . GLU F 139 ? 0.4091 0.7256 0.3045 -0.0411 -0.0928 0.0624  139 GLU F CG  
11388 C CD  . GLU F 139 ? 0.4562 0.7458 0.3094 -0.0501 -0.1041 0.0911  139 GLU F CD  
11389 O OE1 . GLU F 139 ? 0.4779 0.7178 0.3165 -0.0462 -0.1140 0.1066  139 GLU F OE1 
11390 O OE2 . GLU F 139 ? 0.4804 0.7931 0.3078 -0.0630 -0.1039 0.0983  139 GLU F OE2 
11391 N N   . PHE F 140 ? 0.3677 0.7200 0.3003 -0.0445 -0.0662 -0.0035 140 PHE F N   
11392 C CA  . PHE F 140 ? 0.3929 0.7532 0.3013 -0.0480 -0.0611 -0.0242 140 PHE F CA  
11393 C C   . PHE F 140 ? 0.4214 0.8099 0.3011 -0.0499 -0.0650 -0.0167 140 PHE F C   
11394 O O   . PHE F 140 ? 0.4275 0.8284 0.3040 -0.0517 -0.0779 0.0007  140 PHE F O   
11395 C CB  . PHE F 140 ? 0.4022 0.7574 0.3103 -0.0585 -0.0696 -0.0435 140 PHE F CB  
11396 C CG  . PHE F 140 ? 0.3860 0.7129 0.3130 -0.0620 -0.0649 -0.0530 140 PHE F CG  
11397 C CD1 . PHE F 140 ? 0.3559 0.6929 0.3164 -0.0618 -0.0706 -0.0425 140 PHE F CD1 
11398 C CD2 . PHE F 140 ? 0.4098 0.6968 0.3141 -0.0622 -0.0557 -0.0725 140 PHE F CD2 
11399 C CE1 . PHE F 140 ? 0.3425 0.6582 0.3192 -0.0675 -0.0659 -0.0500 140 PHE F CE1 
11400 C CE2 . PHE F 140 ? 0.4031 0.6576 0.3181 -0.0676 -0.0527 -0.0792 140 PHE F CE2 
11401 C CZ  . PHE F 140 ? 0.3660 0.6388 0.3200 -0.0732 -0.0571 -0.0673 140 PHE F CZ  
11402 N N   . TYR F 141 ? 0.4470 0.8439 0.3003 -0.0456 -0.0544 -0.0304 141 TYR F N   
11403 C CA  . TYR F 141 ? 0.4794 0.9081 0.3016 -0.0477 -0.0570 -0.0273 141 TYR F CA  
11404 C C   . TYR F 141 ? 0.5064 0.9341 0.3111 -0.0555 -0.0705 -0.0432 141 TYR F C   
11405 O O   . TYR F 141 ? 0.5231 0.9770 0.3134 -0.0609 -0.0811 -0.0333 141 TYR F O   
11406 C CB  . TYR F 141 ? 0.5004 0.9488 0.2972 -0.0344 -0.0403 -0.0384 141 TYR F CB  
11407 C CG  . TYR F 141 ? 0.4787 0.9527 0.2917 -0.0324 -0.0280 -0.0191 141 TYR F CG  
11408 C CD1 . TYR F 141 ? 0.4759 0.9755 0.2900 -0.0505 -0.0326 0.0122  141 TYR F CD1 
11409 C CD2 . TYR F 141 ? 0.4699 0.9397 0.2909 -0.0150 -0.0138 -0.0310 141 TYR F CD2 
11410 C CE1 . TYR F 141 ? 0.4639 0.9888 0.2872 -0.0589 -0.0234 0.0315  141 TYR F CE1 
11411 C CE2 . TYR F 141 ? 0.4499 0.9562 0.2872 -0.0169 -0.0035 -0.0125 141 TYR F CE2 
11412 C CZ  . TYR F 141 ? 0.4466 0.9827 0.2855 -0.0427 -0.0084 0.0189  141 TYR F CZ  
11413 O OH  . TYR F 141 ? 0.4353 1.0095 0.2846 -0.0544 -0.0001 0.0388  141 TYR F OH  
11414 N N   . HIS F 142 ? 0.5186 0.9148 0.3196 -0.0596 -0.0714 -0.0668 142 HIS F N   
11415 C CA  . HIS F 142 ? 0.5486 0.9447 0.3316 -0.0773 -0.0861 -0.0818 142 HIS F CA  
11416 C C   . HIS F 142 ? 0.5191 0.9340 0.3400 -0.0887 -0.0990 -0.0711 142 HIS F C   
11417 O O   . HIS F 142 ? 0.4828 0.8895 0.3378 -0.0818 -0.0946 -0.0605 142 HIS F O   
11418 C CB  . HIS F 142 ? 0.5966 0.9398 0.3397 -0.0831 -0.0834 -0.1124 142 HIS F CB  
11419 C CG  . HIS F 142 ? 0.5835 0.8829 0.3417 -0.0802 -0.0757 -0.1177 142 HIS F CG  
11420 N ND1 . HIS F 142 ? 0.5824 0.8639 0.3522 -0.1045 -0.0847 -0.1224 142 HIS F ND1 
11421 C CD2 . HIS F 142 ? 0.5730 0.8502 0.3358 -0.0568 -0.0600 -0.1177 142 HIS F CD2 
11422 C CE1 . HIS F 142 ? 0.5732 0.8140 0.3514 -0.0961 -0.0750 -0.1252 142 HIS F CE1 
11423 N NE2 . HIS F 142 ? 0.5664 0.8036 0.3413 -0.0655 -0.0604 -0.1228 142 HIS F NE2 
11424 N N   . LYS F 143 ? 0.5381 0.9862 0.3513 -0.1044 -0.1151 -0.0743 143 LYS F N   
11425 C CA  . LYS F 143 ? 0.5169 1.0027 0.3628 -0.1133 -0.1279 -0.0677 143 LYS F CA  
11426 C C   . LYS F 143 ? 0.5215 0.9775 0.3709 -0.1348 -0.1245 -0.0843 143 LYS F C   
11427 O O   . LYS F 143 ? 0.5687 0.9854 0.3771 -0.1562 -0.1248 -0.1056 143 LYS F O   
11428 C CB  . LYS F 143 ? 0.5411 1.0825 0.3738 -0.1270 -0.1462 -0.0688 143 LYS F CB  
11429 C CG  . LYS F 143 ? 0.5175 1.1261 0.3861 -0.1238 -0.1605 -0.0567 143 LYS F CG  
11430 C CD  . LYS F 143 ? 0.5450 1.2202 0.3986 -0.1374 -0.1793 -0.0585 143 LYS F CD  
11431 C CE  . LYS F 143 ? 0.5300 1.2893 0.4159 -0.1452 -0.1931 -0.0553 143 LYS F CE  
11432 N NZ  . LYS F 143 ? 0.5414 1.3004 0.4260 -0.1913 -0.1923 -0.0732 143 LYS F NZ  
11433 N N   . CYS F 144 ? 0.4836 0.9502 0.3732 -0.1289 -0.1225 -0.0745 144 CYS F N   
11434 C CA  . CYS F 144 ? 0.4873 0.9236 0.3804 -0.1497 -0.1181 -0.0863 144 CYS F CA  
11435 C C   . CYS F 144 ? 0.4725 0.9767 0.3945 -0.1693 -0.1304 -0.0821 144 CYS F C   
11436 O O   . CYS F 144 ? 0.4315 0.9747 0.3943 -0.1471 -0.1303 -0.0673 144 CYS F O   
11437 C CB  . CYS F 144 ? 0.4562 0.8496 0.3703 -0.1264 -0.1022 -0.0794 144 CYS F CB  
11438 S SG  . CYS F 144 ? 0.4711 0.8071 0.3779 -0.1465 -0.0948 -0.0936 144 CYS F SG  
11439 N N   . ASP F 145 ? 0.5136 1.0348 0.4091 -0.2115 -0.1419 -0.0955 145 ASP F N   
11440 C CA  . ASP F 145 ? 0.5049 1.1117 0.4255 -0.2389 -0.1542 -0.0916 145 ASP F CA  
11441 C C   . ASP F 145 ? 0.4923 1.0814 0.4298 -0.2550 -0.1467 -0.0922 145 ASP F C   
11442 O O   . ASP F 145 ? 0.4883 0.9955 0.4189 -0.2409 -0.1328 -0.0952 145 ASP F O   
11443 C CB  . ASP F 145 ? 0.5611 1.1965 0.4417 -0.2891 -0.1710 -0.1040 145 ASP F CB  
11444 C CG  . ASP F 145 ? 0.6330 1.1658 0.4486 -0.3324 -0.1708 -0.1246 145 ASP F CG  
11445 O OD1 . ASP F 145 ? 0.6363 1.0840 0.4412 -0.3212 -0.1576 -0.1292 145 ASP F OD1 
11446 O OD2 . ASP F 145 ? 0.6960 1.2286 0.4635 -0.3771 -0.1858 -0.1366 145 ASP F OD2 
11447 N N   . ASN F 146 ? 0.4873 1.1621 0.4467 -0.2844 -0.1560 -0.0885 146 ASN F N   
11448 C CA  . ASN F 146 ? 0.4752 1.1486 0.4522 -0.3023 -0.1494 -0.0866 146 ASN F CA  
11449 C C   . ASN F 146 ? 0.5373 1.1034 0.4587 -0.3483 -0.1471 -0.1009 146 ASN F C   
11450 O O   . ASN F 146 ? 0.5296 1.0518 0.4565 -0.3490 -0.1373 -0.0995 146 ASN F O   
11451 C CB  . ASN F 146 ? 0.4593 1.2700 0.4706 -0.3255 -0.1601 -0.0784 146 ASN F CB  
11452 C CG  . ASN F 146 ? 0.4054 1.3126 0.4677 -0.2646 -0.1618 -0.0642 146 ASN F CG  
11453 O OD1 . ASN F 146 ? 0.3797 1.2372 0.4514 -0.2096 -0.1543 -0.0582 146 ASN F OD1 
11454 N ND2 . ASN F 146 ? 0.3974 1.4434 0.4863 -0.2744 -0.1731 -0.0583 146 ASN F ND2 
11455 N N   . GLU F 147 ? 0.6094 1.1256 0.4693 -0.3840 -0.1575 -0.1150 147 GLU F N   
11456 C CA  . GLU F 147 ? 0.6927 1.0788 0.4787 -0.4175 -0.1580 -0.1310 147 GLU F CA  
11457 C C   . GLU F 147 ? 0.6870 0.9717 0.4605 -0.3622 -0.1415 -0.1369 147 GLU F C   
11458 O O   . GLU F 147 ? 0.7157 0.9122 0.4622 -0.3609 -0.1341 -0.1420 147 GLU F O   
11459 C CB  . GLU F 147 ? 0.7856 1.1373 0.4966 -0.4682 -0.1763 -0.1463 147 GLU F CB  
11460 C CG  . GLU F 147 ? 0.8039 1.2647 0.5196 -0.5335 -0.1950 -0.1404 147 GLU F CG  
11461 C CD  . GLU F 147 ? 0.7532 1.3437 0.5166 -0.5122 -0.2017 -0.1322 147 GLU F CD  
11462 O OE1 . GLU F 147 ? 0.6664 1.3458 0.5046 -0.4609 -0.1928 -0.1169 147 GLU F OE1 
11463 O OE2 . GLU F 147 ? 0.8091 1.4051 0.5279 -0.5447 -0.2172 -0.1414 147 GLU F OE2 
11464 N N   . CYS F 148 ? 0.6553 0.9600 0.4461 -0.3179 -0.1364 -0.1348 148 CYS F N   
11465 C CA  . CYS F 148 ? 0.6398 0.8822 0.4288 -0.2658 -0.1202 -0.1365 148 CYS F CA  
11466 C C   . CYS F 148 ? 0.5784 0.8271 0.4201 -0.2380 -0.1062 -0.1229 148 CYS F C   
11467 O O   . CYS F 148 ? 0.5902 0.7666 0.4149 -0.2172 -0.0948 -0.1279 148 CYS F O   
11468 C CB  . CYS F 148 ? 0.6112 0.8977 0.4152 -0.2327 -0.1190 -0.1310 148 CYS F CB  
11469 S SG  . CYS F 148 ? 0.5724 0.8287 0.3927 -0.1742 -0.0991 -0.1239 148 CYS F SG  
11470 N N   . MET F 149 ? 0.5206 0.8568 0.4215 -0.2348 -0.1080 -0.1068 149 MET F N   
11471 C CA  . MET F 149 ? 0.4695 0.8124 0.4154 -0.2114 -0.0969 -0.0950 149 MET F CA  
11472 C C   . MET F 149 ? 0.5041 0.7974 0.4301 -0.2424 -0.0948 -0.1013 149 MET F C   
11473 O O   . MET F 149 ? 0.4870 0.7351 0.4223 -0.2218 -0.0831 -0.0987 149 MET F O   
11474 C CB  . MET F 149 ? 0.4154 0.8599 0.4156 -0.1982 -0.1021 -0.0794 149 MET F CB  
11475 C CG  . MET F 149 ? 0.3919 0.8747 0.4064 -0.1624 -0.1061 -0.0695 149 MET F CG  
11476 S SD  . MET F 149 ? 0.3669 0.7869 0.3845 -0.1183 -0.0924 -0.0602 149 MET F SD  
11477 C CE  . MET F 149 ? 0.3561 0.8292 0.3831 -0.0876 -0.1038 -0.0438 149 MET F CE  
11478 N N   . GLU F 150 ? 0.5618 0.8637 0.4560 -0.2956 -0.1076 -0.1081 150 GLU F N   
11479 C CA  . GLU F 150 ? 0.6135 0.8625 0.4758 -0.3359 -0.1090 -0.1119 150 GLU F CA  
11480 C C   . GLU F 150 ? 0.6841 0.7949 0.4806 -0.3257 -0.1042 -0.1259 150 GLU F C   
11481 O O   . GLU F 150 ? 0.7033 0.7573 0.4856 -0.3307 -0.0994 -0.1251 150 GLU F O   
11482 C CB  . GLU F 150 ? 0.6702 0.9595 0.5013 -0.4059 -0.1269 -0.1145 150 GLU F CB  
11483 C CG  . GLU F 150 ? 0.7328 0.9690 0.5208 -0.4615 -0.1318 -0.1152 150 GLU F CG  
11484 C CD  . GLU F 150 ? 0.6710 0.9570 0.5166 -0.4484 -0.1201 -0.1011 150 GLU F CD  
11485 O OE1 . GLU F 150 ? 0.5903 0.9927 0.5096 -0.4179 -0.1147 -0.0898 150 GLU F OE1 
11486 O OE2 . GLU F 150 ? 0.7127 0.9161 0.5236 -0.4655 -0.1171 -0.1018 150 GLU F OE2 
11487 N N   . SER F 151 ? 0.7307 0.7910 0.4839 -0.3073 -0.1059 -0.1388 151 SER F N   
11488 C CA  . SER F 151 ? 0.8065 0.7430 0.4912 -0.2844 -0.1017 -0.1543 151 SER F CA  
11489 C C   . SER F 151 ? 0.7540 0.6844 0.4792 -0.2275 -0.0830 -0.1472 151 SER F C   
11490 O O   . SER F 151 ? 0.8013 0.6449 0.4847 -0.2107 -0.0785 -0.1547 151 SER F O   
11491 C CB  . SER F 151 ? 0.8625 0.7635 0.4928 -0.2721 -0.1073 -0.1706 151 SER F CB  
11492 O OG  . SER F 151 ? 0.7869 0.7644 0.4726 -0.2304 -0.0974 -0.1624 151 SER F OG  
11493 N N   . VAL F 152 ? 0.6680 0.6876 0.4677 -0.1989 -0.0740 -0.1322 152 VAL F N   
11494 C CA  . VAL F 152 ? 0.6147 0.6410 0.4554 -0.1553 -0.0584 -0.1223 152 VAL F CA  
11495 C C   . VAL F 152 ? 0.6038 0.6225 0.4673 -0.1679 -0.0553 -0.1143 152 VAL F C   
11496 O O   . VAL F 152 ? 0.6064 0.5787 0.4636 -0.1447 -0.0462 -0.1146 152 VAL F O   
11497 C CB  . VAL F 152 ? 0.5362 0.6467 0.4372 -0.1314 -0.0538 -0.1063 152 VAL F CB  
11498 C CG1 . VAL F 152 ? 0.4886 0.6010 0.4228 -0.0966 -0.0401 -0.0952 152 VAL F CG1 
11499 C CG2 . VAL F 152 ? 0.5562 0.6794 0.4336 -0.1223 -0.0571 -0.1121 152 VAL F CG2 
11500 N N   . ARG F 153 ? 0.5966 0.6708 0.4863 -0.2034 -0.0631 -0.1071 153 ARG F N   
11501 C CA  . ARG F 153 ? 0.5960 0.6722 0.5024 -0.2224 -0.0611 -0.0999 153 ARG F CA  
11502 C C   . ARG F 153 ? 0.7022 0.6766 0.5359 -0.2534 -0.0667 -0.1107 153 ARG F C   
11503 O O   . ARG F 153 ? 0.7052 0.6387 0.5357 -0.2486 -0.0608 -0.1072 153 ARG F O   
11504 C CB  . ARG F 153 ? 0.5567 0.7352 0.5052 -0.2514 -0.0684 -0.0902 153 ARG F CB  
11505 C CG  . ARG F 153 ? 0.4716 0.7313 0.4869 -0.2114 -0.0627 -0.0771 153 ARG F CG  
11506 C CD  . ARG F 153 ? 0.4426 0.8095 0.4954 -0.2275 -0.0697 -0.0689 153 ARG F CD  
11507 N NE  . ARG F 153 ? 0.4276 0.8630 0.4957 -0.2137 -0.0782 -0.0664 153 ARG F NE  
11508 C CZ  . ARG F 153 ? 0.4568 0.9416 0.5090 -0.2479 -0.0908 -0.0707 153 ARG F CZ  
11509 N NH1 . ARG F 153 ? 0.5093 0.9804 0.5248 -0.3059 -0.0978 -0.0774 153 ARG F NH1 
11510 N NH2 . ARG F 153 ? 0.4416 0.9877 0.5089 -0.2267 -0.0983 -0.0670 153 ARG F NH2 
11511 N N   . ASN F 154 ? 0.8084 0.7352 0.5763 -0.2859 -0.0800 -0.1236 154 ASN F N   
11512 C CA  . ASN F 154 ? 0.9434 0.7443 0.6161 -0.3145 -0.0898 -0.1360 154 ASN F CA  
11513 C C   . ASN F 154 ? 0.9653 0.6676 0.6005 -0.2632 -0.0808 -0.1437 154 ASN F C   
11514 O O   . ASN F 154 ? 1.0357 0.6466 0.6151 -0.2761 -0.0850 -0.1459 154 ASN F O   
11515 C CB  . ASN F 154 ? 1.0631 0.8147 0.6615 -0.3415 -0.1055 -0.1520 154 ASN F CB  
11516 C CG  . ASN F 154 ? 1.1515 0.9359 0.7276 -0.4207 -0.1232 -0.1487 154 ASN F CG  
11517 O OD1 . ASN F 154 ? 1.1312 0.9726 0.7407 -0.4579 -0.1238 -0.1348 154 ASN F OD1 
11518 N ND2 . ASN F 154 ? 1.2848 1.0393 0.8008 -0.4488 -0.1382 -0.1617 154 ASN F ND2 
11519 N N   . GLY F 155 ? 0.9069 0.6334 0.5693 -0.2060 -0.0693 -0.1467 155 GLY F N   
11520 C CA  . GLY F 155 ? 0.9430 0.5891 0.5570 -0.1529 -0.0628 -0.1585 155 GLY F CA  
11521 C C   . GLY F 155 ? 1.0343 0.6055 0.5607 -0.1464 -0.0730 -0.1800 155 GLY F C   
11522 O O   . GLY F 155 ? 1.1059 0.5957 0.5680 -0.1012 -0.0713 -0.1944 155 GLY F O   
11523 N N   . THR F 156 ? 1.0343 0.6384 0.5564 -0.1872 -0.0839 -0.1826 156 THR F N   
11524 C CA  . THR F 156 ? 1.1388 0.6629 0.5665 -0.1968 -0.0980 -0.2038 156 THR F CA  
11525 C C   . THR F 156 ? 1.0889 0.6870 0.5457 -0.1689 -0.0926 -0.2079 156 THR F C   
11526 O O   . THR F 156 ? 1.1707 0.7199 0.5574 -0.1769 -0.1039 -0.2252 156 THR F O   
11527 C CB  . THR F 156 ? 1.2052 0.7020 0.5888 -0.2789 -0.1190 -0.2041 156 THR F CB  
11528 O OG1 . THR F 156 ? 1.2648 0.6804 0.6056 -0.3092 -0.1254 -0.2000 156 THR F OG1 
11529 C CG2 . THR F 156 ? 1.3311 0.7397 0.6093 -0.2988 -0.1371 -0.2262 156 THR F CG2 
11530 N N   . TYR F 157 ? 0.9637 0.6721 0.5154 -0.1383 -0.0766 -0.1916 157 TYR F N   
11531 C CA  . TYR F 157 ? 0.9161 0.6996 0.4969 -0.1178 -0.0720 -0.1907 157 TYR F CA  
11532 C C   . TYR F 157 ? 1.0009 0.7209 0.5029 -0.0778 -0.0714 -0.2132 157 TYR F C   
11533 O O   . TYR F 157 ? 1.0173 0.7082 0.5006 -0.0267 -0.0603 -0.2190 157 TYR F O   
11534 C CB  . TYR F 157 ? 0.7972 0.6795 0.4701 -0.0872 -0.0557 -0.1695 157 TYR F CB  
11535 C CG  . TYR F 157 ? 0.7588 0.7121 0.4540 -0.0694 -0.0518 -0.1653 157 TYR F CG  
11536 C CD1 . TYR F 157 ? 0.7262 0.7416 0.4504 -0.0988 -0.0611 -0.1567 157 TYR F CD1 
11537 C CD2 . TYR F 157 ? 0.7598 0.7246 0.4440 -0.0232 -0.0393 -0.1690 157 TYR F CD2 
11538 C CE1 . TYR F 157 ? 0.7009 0.7739 0.4385 -0.0840 -0.0589 -0.1512 157 TYR F CE1 
11539 C CE2 . TYR F 157 ? 0.7325 0.7643 0.4325 -0.0127 -0.0360 -0.1630 157 TYR F CE2 
11540 C CZ  . TYR F 157 ? 0.7045 0.7830 0.4291 -0.0439 -0.0462 -0.1538 157 TYR F CZ  
11541 O OH  . TYR F 157 ? 0.6848 0.8229 0.4188 -0.0345 -0.0442 -0.1462 157 TYR F OH  
11542 N N   . ASP F 158 ? 1.0572 0.7633 0.5117 -0.0983 -0.0835 -0.2262 158 ASP F N   
11543 C CA  . ASP F 158 ? 1.1550 0.7932 0.5217 -0.0605 -0.0850 -0.2510 158 ASP F CA  
11544 C C   . ASP F 158 ? 1.0906 0.8260 0.5023 -0.0150 -0.0692 -0.2456 158 ASP F C   
11545 O O   . ASP F 158 ? 1.0709 0.8648 0.4976 -0.0310 -0.0729 -0.2430 158 ASP F O   
11546 C CB  . ASP F 158 ? 1.2599 0.8287 0.5423 -0.1061 -0.1070 -0.2691 158 ASP F CB  
11547 C CG  . ASP F 158 ? 1.4041 0.8493 0.5619 -0.0679 -0.1135 -0.3003 158 ASP F CG  
11548 O OD1 . ASP F 158 ? 1.4753 0.8229 0.5746 -0.0342 -0.1126 -0.3108 158 ASP F OD1 
11549 O OD2 . ASP F 158 ? 1.4543 0.8964 0.5667 -0.0679 -0.1205 -0.3151 158 ASP F OD2 
11550 N N   . TYR F 159 ? 1.0623 0.8192 0.4928 0.0388  -0.0523 -0.2425 159 TYR F N   
11551 C CA  . TYR F 159 ? 1.0078 0.8620 0.4749 0.0792  -0.0363 -0.2355 159 TYR F CA  
11552 C C   . TYR F 159 ? 1.0856 0.9259 0.4826 0.0993  -0.0400 -0.2572 159 TYR F C   
11553 O O   . TYR F 159 ? 1.0387 0.9642 0.4708 0.0915  -0.0367 -0.2470 159 TYR F O   
11554 C CB  . TYR F 159 ? 0.9864 0.8625 0.4693 0.1323  -0.0196 -0.2318 159 TYR F CB  
11555 C CG  . TYR F 159 ? 0.9497 0.9297 0.4558 0.1728  -0.0034 -0.2261 159 TYR F CG  
11556 C CD1 . TYR F 159 ? 0.8421 0.9336 0.4352 0.1558  0.0062  -0.1965 159 TYR F CD1 
11557 C CD2 . TYR F 159 ? 1.0326 0.9982 0.4658 0.2273  0.0010  -0.2500 159 TYR F CD2 
11558 C CE1 . TYR F 159 ? 0.8162 1.0072 0.4257 0.1822  0.0199  -0.1881 159 TYR F CE1 
11559 C CE2 . TYR F 159 ? 0.9999 1.0790 0.4555 0.2611  0.0168  -0.2433 159 TYR F CE2 
11560 C CZ  . TYR F 159 ? 0.8913 1.0856 0.4365 0.2336  0.0262  -0.2109 159 TYR F CZ  
11561 O OH  . TYR F 159 ? 0.8679 1.1785 0.4300 0.2573  0.0408  -0.2014 159 TYR F OH  
11562 N N   . PRO F 160 ? 1.2153 0.9402 0.5048 0.1256  -0.0485 -0.2874 160 PRO F N   
11563 C CA  . PRO F 160 ? 1.3028 1.0048 0.5141 0.1492  -0.0530 -0.3115 160 PRO F CA  
11564 C C   . PRO F 160 ? 1.3014 1.0234 0.5145 0.0935  -0.0670 -0.3100 160 PRO F C   
11565 O O   . PRO F 160 ? 1.3288 1.0840 0.5132 0.1120  -0.0653 -0.3204 160 PRO F O   
11566 C CB  . PRO F 160 ? 1.4586 0.9984 0.5419 0.1764  -0.0661 -0.3435 160 PRO F CB  
11567 C CG  . PRO F 160 ? 1.4375 0.9529 0.5428 0.1986  -0.0590 -0.3346 160 PRO F CG  
11568 C CD  . PRO F 160 ? 1.2981 0.9020 0.5231 0.1422  -0.0547 -0.3012 160 PRO F CD  
11569 N N   . GLN F 161 ? 1.2744 0.9847 0.5189 0.0282  -0.0807 -0.2975 161 GLN F N   
11570 C CA  . GLN F 161 ? 1.2692 1.0145 0.5214 -0.0249 -0.0951 -0.2940 161 GLN F CA  
11571 C C   . GLN F 161 ? 1.1525 1.0391 0.4991 -0.0229 -0.0839 -0.2682 161 GLN F C   
11572 O O   . GLN F 161 ? 1.1636 1.0890 0.4963 -0.0292 -0.0886 -0.2713 161 GLN F O   
11573 C CB  . GLN F 161 ? 1.2697 0.9847 0.5328 -0.0936 -0.1124 -0.2860 161 GLN F CB  
11574 C CG  . GLN F 161 ? 1.2579 1.0282 0.5351 -0.1492 -0.1284 -0.2804 161 GLN F CG  
11575 C CD  . GLN F 161 ? 1.2341 1.0189 0.5445 -0.2138 -0.1419 -0.2667 161 GLN F CD  
11576 O OE1 . GLN F 161 ? 1.2174 0.9739 0.5471 -0.2189 -0.1380 -0.2592 161 GLN F OE1 
11577 N NE2 . GLN F 161 ? 1.2324 1.0726 0.5503 -0.2628 -0.1577 -0.2627 161 GLN F NE2 
11578 N N   . TYR F 162 ? 1.0517 1.0057 0.4856 -0.0159 -0.0710 -0.2425 162 TYR F N   
11579 C CA  . TYR F 162 ? 0.9546 1.0230 0.4684 -0.0189 -0.0637 -0.2148 162 TYR F CA  
11580 C C   . TYR F 162 ? 0.9349 1.0628 0.4596 0.0276  -0.0447 -0.2088 162 TYR F C   
11581 O O   . TYR F 162 ? 0.8655 1.0780 0.4472 0.0236  -0.0386 -0.1833 162 TYR F O   
11582 C CB  . TYR F 162 ? 0.8663 0.9701 0.4597 -0.0415 -0.0632 -0.1894 162 TYR F CB  
11583 C CG  . TYR F 162 ? 0.8795 0.9542 0.4718 -0.0895 -0.0805 -0.1916 162 TYR F CG  
11584 C CD1 . TYR F 162 ? 0.8691 0.9931 0.4742 -0.1235 -0.0950 -0.1854 162 TYR F CD1 
11585 C CD2 . TYR F 162 ? 0.9051 0.9118 0.4819 -0.1023 -0.0828 -0.1986 162 TYR F CD2 
11586 C CE1 . TYR F 162 ? 0.8815 1.0013 0.4879 -0.1699 -0.1106 -0.1861 162 TYR F CE1 
11587 C CE2 . TYR F 162 ? 0.9203 0.9140 0.4949 -0.1530 -0.0984 -0.1984 162 TYR F CE2 
11588 C CZ  . TYR F 162 ? 0.9070 0.9642 0.4984 -0.1874 -0.1119 -0.1921 162 TYR F CZ  
11589 O OH  . TYR F 162 ? 0.9212 0.9868 0.5127 -0.2401 -0.1272 -0.1907 162 TYR F OH  
11590 N N   . SER F 163 ? 1.0074 1.0925 0.4711 0.0717  -0.0366 -0.2316 163 SER F N   
11591 C CA  . SER F 163 ? 0.9946 1.1545 0.4643 0.1172  -0.0181 -0.2275 163 SER F CA  
11592 C C   . SER F 163 ? 1.0287 1.2281 0.4618 0.1217  -0.0196 -0.2353 163 SER F C   
11593 O O   . SER F 163 ? 1.0384 1.3009 0.4580 0.1598  -0.0054 -0.2374 163 SER F O   
11594 C CB  . SER F 163 ? 1.0603 1.1695 0.4772 0.1725  -0.0091 -0.2498 163 SER F CB  
11595 O OG  . SER F 163 ? 1.0319 1.2396 0.4717 0.2147  0.0104  -0.2407 163 SER F OG  
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   
;NAG B1164 HAS THE WRONG CHIRALITY AT ATOM C1 NAG D1164 HAS THE WRONG CHIRALITY AT ATOM C1 NAG F1164 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  1322 1322 NAG NAG A . 
H  3 NAG 1  1323 1323 NAG NAG A . 
I  4 SIA 1  1324 1324 SIA SIA A . 
J  5 GLA 2  1325 1325 GLA GLA A . 
K  3 NAG 3  1326 1326 NAG NAG A . 
L  6 FUC 4  1327 1327 FUC FUC A . 
M  3 NAG 1  1164 1164 NAG NAG B . 
N  7 EPE 1  1165 1165 EPE EPE B . 
O  3 NAG 1  1322 1322 NAG NAG C . 
P  3 NAG 1  1323 1323 NAG NAG C . 
Q  4 SIA 1  1324 1324 SIA SIA C . 
R  5 GLA 2  1325 1325 GLA GLA C . 
S  3 NAG 3  1326 1326 NAG NAG C . 
T  6 FUC 4  1327 1327 FUC FUC C . 
U  3 NAG 1  1164 1164 NAG NAG D . 
V  7 EPE 1  1165 1165 EPE EPE D . 
W  3 NAG 1  1322 1322 NAG NAG E . 
X  3 NAG 1  1323 1323 NAG NAG E . 
Y  4 SIA 1  1324 1324 SIA SIA E . 
Z  5 GLA 2  1325 1325 GLA GLA E . 
AA 3 NAG 3  1326 1326 NAG NAG E . 
BA 6 FUC 4  1327 1327 FUC FUC E . 
CA 3 NAG 1  1164 1164 NAG NAG F . 
DA 7 EPE 1  1165 1165 EPE EPE F . 
EA 8 HOH 1  2001 2001 HOH HOH A . 
EA 8 HOH 2  2002 2002 HOH HOH A . 
EA 8 HOH 3  2003 2003 HOH HOH A . 
EA 8 HOH 4  2004 2004 HOH HOH A . 
EA 8 HOH 5  2005 2005 HOH HOH A . 
EA 8 HOH 6  2006 2006 HOH HOH A . 
EA 8 HOH 7  2007 2007 HOH HOH A . 
EA 8 HOH 8  2008 2008 HOH HOH A . 
EA 8 HOH 9  2009 2009 HOH HOH A . 
EA 8 HOH 10 2010 2010 HOH HOH A . 
EA 8 HOH 11 2011 2011 HOH HOH A . 
EA 8 HOH 12 2012 2012 HOH HOH A . 
EA 8 HOH 13 2013 2013 HOH HOH A . 
EA 8 HOH 14 2014 2014 HOH HOH A . 
EA 8 HOH 15 2015 2015 HOH HOH A . 
EA 8 HOH 16 2016 2016 HOH HOH A . 
EA 8 HOH 17 2017 2017 HOH HOH A . 
EA 8 HOH 18 2018 2018 HOH HOH A . 
EA 8 HOH 19 2019 2019 HOH HOH A . 
EA 8 HOH 20 2020 2020 HOH HOH A . 
EA 8 HOH 21 2021 2021 HOH HOH A . 
EA 8 HOH 22 2022 2022 HOH HOH A . 
EA 8 HOH 23 2023 2023 HOH HOH A . 
EA 8 HOH 24 2024 2024 HOH HOH A . 
EA 8 HOH 25 2025 2025 HOH HOH A . 
EA 8 HOH 26 2026 2026 HOH HOH A . 
EA 8 HOH 27 2027 2027 HOH HOH A . 
EA 8 HOH 28 2028 2028 HOH HOH A . 
EA 8 HOH 29 2029 2029 HOH HOH A . 
EA 8 HOH 30 2030 2030 HOH HOH A . 
EA 8 HOH 31 2031 2031 HOH HOH A . 
EA 8 HOH 32 2032 2032 HOH HOH A . 
EA 8 HOH 33 2033 2033 HOH HOH A . 
EA 8 HOH 34 2034 2034 HOH HOH A . 
EA 8 HOH 35 2035 2035 HOH HOH A . 
EA 8 HOH 36 2036 2036 HOH HOH A . 
EA 8 HOH 37 2037 2037 HOH HOH A . 
EA 8 HOH 38 2038 2038 HOH HOH A . 
EA 8 HOH 39 2039 2039 HOH HOH A . 
EA 8 HOH 40 2040 2040 HOH HOH A . 
EA 8 HOH 41 2041 2041 HOH HOH A . 
EA 8 HOH 42 2042 2042 HOH HOH A . 
EA 8 HOH 43 2043 2043 HOH HOH A . 
EA 8 HOH 44 2044 2044 HOH HOH A . 
EA 8 HOH 45 2045 2045 HOH HOH A . 
EA 8 HOH 46 2046 2046 HOH HOH A . 
EA 8 HOH 47 2047 2047 HOH HOH A . 
EA 8 HOH 48 2048 2048 HOH HOH A . 
EA 8 HOH 49 2049 2049 HOH HOH A . 
EA 8 HOH 50 2050 2050 HOH HOH A . 
EA 8 HOH 51 2051 2051 HOH HOH A . 
EA 8 HOH 52 2052 2052 HOH HOH A . 
EA 8 HOH 53 2053 2053 HOH HOH A . 
EA 8 HOH 54 2054 2054 HOH HOH A . 
EA 8 HOH 55 2055 2055 HOH HOH A . 
EA 8 HOH 56 2056 2056 HOH HOH A . 
EA 8 HOH 57 2057 2057 HOH HOH A . 
EA 8 HOH 58 2058 2058 HOH HOH A . 
EA 8 HOH 59 2059 2059 HOH HOH A . 
EA 8 HOH 60 2060 2060 HOH HOH A . 
EA 8 HOH 61 2061 2061 HOH HOH A . 
EA 8 HOH 62 2062 2062 HOH HOH A . 
EA 8 HOH 63 2063 2063 HOH HOH A . 
EA 8 HOH 64 2064 2064 HOH HOH A . 
FA 8 HOH 1  2001 2001 HOH HOH B . 
FA 8 HOH 2  2002 2002 HOH HOH B . 
FA 8 HOH 3  2003 2003 HOH HOH B . 
FA 8 HOH 4  2004 2004 HOH HOH B . 
FA 8 HOH 5  2005 2005 HOH HOH B . 
FA 8 HOH 6  2006 2006 HOH HOH B . 
FA 8 HOH 7  2007 2007 HOH HOH B . 
FA 8 HOH 8  2008 2008 HOH HOH B . 
FA 8 HOH 9  2009 2009 HOH HOH B . 
FA 8 HOH 10 2010 2010 HOH HOH B . 
FA 8 HOH 11 2011 2011 HOH HOH B . 
FA 8 HOH 12 2012 2012 HOH HOH B . 
FA 8 HOH 13 2013 2013 HOH HOH B . 
FA 8 HOH 14 2014 2014 HOH HOH B . 
FA 8 HOH 15 2015 2015 HOH HOH B . 
FA 8 HOH 16 2016 2016 HOH HOH B . 
FA 8 HOH 17 2017 2017 HOH HOH B . 
FA 8 HOH 18 2018 2018 HOH HOH B . 
FA 8 HOH 19 2019 2019 HOH HOH B . 
FA 8 HOH 20 2020 2020 HOH HOH B . 
FA 8 HOH 21 2021 2021 HOH HOH B . 
FA 8 HOH 22 2022 2022 HOH HOH B . 
FA 8 HOH 23 2023 2023 HOH HOH B . 
FA 8 HOH 24 2024 2024 HOH HOH B . 
FA 8 HOH 25 2025 2025 HOH HOH B . 
FA 8 HOH 26 2026 2026 HOH HOH B . 
FA 8 HOH 27 2027 2027 HOH HOH B . 
FA 8 HOH 28 2028 2028 HOH HOH B . 
FA 8 HOH 29 2029 2029 HOH HOH B . 
FA 8 HOH 30 2030 2030 HOH HOH B . 
FA 8 HOH 31 2031 2031 HOH HOH B . 
FA 8 HOH 32 2032 2032 HOH HOH B . 
FA 8 HOH 33 2033 2033 HOH HOH B . 
FA 8 HOH 34 2034 2034 HOH HOH B . 
FA 8 HOH 35 2035 2035 HOH HOH B . 
FA 8 HOH 36 2036 2036 HOH HOH B . 
FA 8 HOH 37 2037 2037 HOH HOH B . 
FA 8 HOH 38 2038 2038 HOH HOH B . 
FA 8 HOH 39 2039 2039 HOH HOH B . 
FA 8 HOH 40 2040 2040 HOH HOH B . 
FA 8 HOH 41 2041 2041 HOH HOH B . 
FA 8 HOH 42 2042 2042 HOH HOH B . 
FA 8 HOH 43 2043 2043 HOH HOH B . 
FA 8 HOH 44 2044 2044 HOH HOH B . 
FA 8 HOH 45 2045 2045 HOH HOH B . 
FA 8 HOH 46 2046 2046 HOH HOH B . 
FA 8 HOH 47 2047 2047 HOH HOH B . 
FA 8 HOH 48 2048 2048 HOH HOH B . 
GA 8 HOH 1  2001 2001 HOH HOH C . 
GA 8 HOH 2  2002 2002 HOH HOH C . 
GA 8 HOH 3  2003 2003 HOH HOH C . 
GA 8 HOH 4  2004 2004 HOH HOH C . 
GA 8 HOH 5  2005 2005 HOH HOH C . 
GA 8 HOH 6  2006 2006 HOH HOH C . 
GA 8 HOH 7  2007 2007 HOH HOH C . 
GA 8 HOH 8  2008 2008 HOH HOH C . 
GA 8 HOH 9  2009 2009 HOH HOH C . 
GA 8 HOH 10 2010 2010 HOH HOH C . 
GA 8 HOH 11 2011 2011 HOH HOH C . 
GA 8 HOH 12 2012 2012 HOH HOH C . 
GA 8 HOH 13 2013 2013 HOH HOH C . 
GA 8 HOH 14 2014 2014 HOH HOH C . 
GA 8 HOH 15 2015 2015 HOH HOH C . 
GA 8 HOH 16 2016 2016 HOH HOH C . 
GA 8 HOH 17 2017 2017 HOH HOH C . 
GA 8 HOH 18 2018 2018 HOH HOH C . 
GA 8 HOH 19 2019 2019 HOH HOH C . 
GA 8 HOH 20 2020 2020 HOH HOH C . 
GA 8 HOH 21 2021 2021 HOH HOH C . 
GA 8 HOH 22 2022 2022 HOH HOH C . 
GA 8 HOH 23 2023 2023 HOH HOH C . 
GA 8 HOH 24 2024 2024 HOH HOH C . 
GA 8 HOH 25 2025 2025 HOH HOH C . 
GA 8 HOH 26 2026 2026 HOH HOH C . 
GA 8 HOH 27 2027 2027 HOH HOH C . 
GA 8 HOH 28 2028 2028 HOH HOH C . 
GA 8 HOH 29 2029 2029 HOH HOH C . 
GA 8 HOH 30 2030 2030 HOH HOH C . 
GA 8 HOH 31 2031 2031 HOH HOH C . 
GA 8 HOH 32 2032 2032 HOH HOH C . 
GA 8 HOH 33 2033 2033 HOH HOH C . 
GA 8 HOH 34 2034 2034 HOH HOH C . 
GA 8 HOH 35 2035 2035 HOH HOH C . 
GA 8 HOH 36 2036 2036 HOH HOH C . 
GA 8 HOH 37 2037 2037 HOH HOH C . 
GA 8 HOH 38 2038 2038 HOH HOH C . 
GA 8 HOH 39 2039 2039 HOH HOH C . 
GA 8 HOH 40 2040 2040 HOH HOH C . 
GA 8 HOH 41 2041 2041 HOH HOH C . 
GA 8 HOH 42 2042 2042 HOH HOH C . 
GA 8 HOH 43 2043 2043 HOH HOH C . 
GA 8 HOH 44 2044 2044 HOH HOH C . 
GA 8 HOH 45 2045 2045 HOH HOH C . 
GA 8 HOH 46 2046 2046 HOH HOH C . 
GA 8 HOH 47 2047 2047 HOH HOH C . 
GA 8 HOH 48 2048 2048 HOH HOH C . 
GA 8 HOH 49 2049 2049 HOH HOH C . 
GA 8 HOH 50 2050 2050 HOH HOH C . 
GA 8 HOH 51 2051 2051 HOH HOH C . 
GA 8 HOH 52 2052 2052 HOH HOH C . 
GA 8 HOH 53 2053 2053 HOH HOH C . 
GA 8 HOH 54 2054 2054 HOH HOH C . 
GA 8 HOH 55 2055 2055 HOH HOH C . 
GA 8 HOH 56 2056 2056 HOH HOH C . 
GA 8 HOH 57 2057 2057 HOH HOH C . 
GA 8 HOH 58 2058 2058 HOH HOH C . 
GA 8 HOH 59 2059 2059 HOH HOH C . 
GA 8 HOH 60 2060 2060 HOH HOH C . 
HA 8 HOH 1  2001 2001 HOH HOH D . 
HA 8 HOH 2  2002 2002 HOH HOH D . 
HA 8 HOH 3  2003 2003 HOH HOH D . 
HA 8 HOH 4  2004 2004 HOH HOH D . 
HA 8 HOH 5  2005 2005 HOH HOH D . 
HA 8 HOH 6  2006 2006 HOH HOH D . 
HA 8 HOH 7  2007 2007 HOH HOH D . 
HA 8 HOH 8  2008 2008 HOH HOH D . 
HA 8 HOH 9  2009 2009 HOH HOH D . 
HA 8 HOH 10 2010 2010 HOH HOH D . 
HA 8 HOH 11 2011 2011 HOH HOH D . 
HA 8 HOH 12 2012 2012 HOH HOH D . 
HA 8 HOH 13 2013 2013 HOH HOH D . 
HA 8 HOH 14 2014 2014 HOH HOH D . 
HA 8 HOH 15 2015 2015 HOH HOH D . 
HA 8 HOH 16 2016 2016 HOH HOH D . 
HA 8 HOH 17 2017 2017 HOH HOH D . 
HA 8 HOH 18 2018 2018 HOH HOH D . 
HA 8 HOH 19 2019 2019 HOH HOH D . 
HA 8 HOH 20 2020 2020 HOH HOH D . 
HA 8 HOH 21 2021 2021 HOH HOH D . 
HA 8 HOH 22 2022 2022 HOH HOH D . 
HA 8 HOH 23 2023 2023 HOH HOH D . 
HA 8 HOH 24 2024 2024 HOH HOH D . 
HA 8 HOH 25 2025 2025 HOH HOH D . 
HA 8 HOH 26 2026 2026 HOH HOH D . 
HA 8 HOH 27 2027 2027 HOH HOH D . 
HA 8 HOH 28 2028 2028 HOH HOH D . 
HA 8 HOH 29 2029 2029 HOH HOH D . 
HA 8 HOH 30 2030 2030 HOH HOH D . 
HA 8 HOH 31 2031 2031 HOH HOH D . 
HA 8 HOH 32 2032 2032 HOH HOH D . 
HA 8 HOH 33 2033 2033 HOH HOH D . 
HA 8 HOH 34 2034 2034 HOH HOH D . 
HA 8 HOH 35 2035 2035 HOH HOH D . 
HA 8 HOH 36 2036 2036 HOH HOH D . 
HA 8 HOH 37 2037 2037 HOH HOH D . 
HA 8 HOH 38 2038 2038 HOH HOH D . 
HA 8 HOH 39 2039 2039 HOH HOH D . 
HA 8 HOH 40 2040 2040 HOH HOH D . 
HA 8 HOH 41 2041 2041 HOH HOH D . 
IA 8 HOH 1  2001 2001 HOH HOH E . 
IA 8 HOH 2  2002 2002 HOH HOH E . 
IA 8 HOH 3  2003 2003 HOH HOH E . 
IA 8 HOH 4  2004 2004 HOH HOH E . 
IA 8 HOH 5  2005 2005 HOH HOH E . 
IA 8 HOH 6  2006 2006 HOH HOH E . 
IA 8 HOH 7  2007 2007 HOH HOH E . 
IA 8 HOH 8  2008 2008 HOH HOH E . 
IA 8 HOH 9  2009 2009 HOH HOH E . 
IA 8 HOH 10 2010 2010 HOH HOH E . 
IA 8 HOH 11 2011 2011 HOH HOH E . 
IA 8 HOH 12 2012 2012 HOH HOH E . 
IA 8 HOH 13 2013 2013 HOH HOH E . 
IA 8 HOH 14 2014 2014 HOH HOH E . 
IA 8 HOH 15 2015 2015 HOH HOH E . 
IA 8 HOH 16 2016 2016 HOH HOH E . 
IA 8 HOH 17 2017 2017 HOH HOH E . 
IA 8 HOH 18 2018 2018 HOH HOH E . 
IA 8 HOH 19 2019 2019 HOH HOH E . 
IA 8 HOH 20 2020 2020 HOH HOH E . 
IA 8 HOH 21 2021 2021 HOH HOH E . 
IA 8 HOH 22 2022 2022 HOH HOH E . 
IA 8 HOH 23 2023 2023 HOH HOH E . 
IA 8 HOH 24 2024 2024 HOH HOH E . 
IA 8 HOH 25 2025 2025 HOH HOH E . 
IA 8 HOH 26 2026 2026 HOH HOH E . 
IA 8 HOH 27 2027 2027 HOH HOH E . 
IA 8 HOH 28 2028 2028 HOH HOH E . 
IA 8 HOH 29 2029 2029 HOH HOH E . 
IA 8 HOH 30 2030 2030 HOH HOH E . 
IA 8 HOH 31 2031 2031 HOH HOH E . 
IA 8 HOH 32 2032 2032 HOH HOH E . 
IA 8 HOH 33 2033 2033 HOH HOH E . 
IA 8 HOH 34 2034 2034 HOH HOH E . 
IA 8 HOH 35 2035 2035 HOH HOH E . 
IA 8 HOH 36 2036 2036 HOH HOH E . 
IA 8 HOH 37 2037 2037 HOH HOH E . 
IA 8 HOH 38 2038 2038 HOH HOH E . 
IA 8 HOH 39 2039 2039 HOH HOH E . 
IA 8 HOH 40 2040 2040 HOH HOH E . 
IA 8 HOH 41 2041 2041 HOH HOH E . 
IA 8 HOH 42 2042 2042 HOH HOH E . 
IA 8 HOH 43 2043 2043 HOH HOH E . 
IA 8 HOH 44 2044 2044 HOH HOH E . 
IA 8 HOH 45 2045 2045 HOH HOH E . 
IA 8 HOH 46 2046 2046 HOH HOH E . 
IA 8 HOH 47 2047 2047 HOH HOH E . 
IA 8 HOH 48 2048 2048 HOH HOH E . 
IA 8 HOH 49 2049 2049 HOH HOH E . 
IA 8 HOH 50 2050 2050 HOH HOH E . 
IA 8 HOH 51 2051 2051 HOH HOH E . 
JA 8 HOH 1  2001 2001 HOH HOH F . 
JA 8 HOH 2  2002 2002 HOH HOH F . 
JA 8 HOH 3  2003 2003 HOH HOH F . 
JA 8 HOH 4  2004 2004 HOH HOH F . 
JA 8 HOH 5  2005 2005 HOH HOH F . 
JA 8 HOH 6  2006 2006 HOH HOH F . 
JA 8 HOH 7  2007 2007 HOH HOH F . 
JA 8 HOH 8  2008 2008 HOH HOH F . 
JA 8 HOH 9  2009 2009 HOH HOH F . 
JA 8 HOH 10 2010 2010 HOH HOH F . 
JA 8 HOH 11 2011 2011 HOH HOH F . 
JA 8 HOH 12 2012 2012 HOH HOH F . 
JA 8 HOH 13 2013 2013 HOH HOH F . 
JA 8 HOH 14 2014 2014 HOH HOH F . 
JA 8 HOH 15 2015 2015 HOH HOH F . 
JA 8 HOH 16 2016 2016 HOH HOH F . 
JA 8 HOH 17 2017 2017 HOH HOH F . 
JA 8 HOH 18 2018 2018 HOH HOH F . 
JA 8 HOH 19 2019 2019 HOH HOH F . 
JA 8 HOH 20 2020 2020 HOH HOH F . 
JA 8 HOH 21 2021 2021 HOH HOH F . 
JA 8 HOH 22 2022 2022 HOH HOH F . 
JA 8 HOH 23 2023 2023 HOH HOH F . 
JA 8 HOH 24 2024 2024 HOH HOH F . 
JA 8 HOH 25 2025 2025 HOH HOH F . 
JA 8 HOH 26 2026 2026 HOH HOH F . 
JA 8 HOH 27 2027 2027 HOH HOH F . 
JA 8 HOH 28 2028 2028 HOH HOH F . 
JA 8 HOH 29 2029 2029 HOH HOH F . 
JA 8 HOH 30 2030 2030 HOH HOH F . 
JA 8 HOH 31 2031 2031 HOH HOH F . 
JA 8 HOH 32 2032 2032 HOH HOH F . 
JA 8 HOH 33 2033 2033 HOH HOH F . 
JA 8 HOH 34 2034 2034 HOH HOH F . 
JA 8 HOH 35 2035 2035 HOH HOH F . 
JA 8 HOH 36 2036 2036 HOH HOH F . 
JA 8 HOH 37 2037 2037 HOH HOH F . 
JA 8 HOH 38 2038 2038 HOH HOH F . 
JA 8 HOH 39 2039 2039 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)' 34390 ? 
1 MORE         -70.6 ? 
1 'SSA (A^2)'  60540 ? 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    F 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     2017 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   JA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 
3 'Structure model' 1 2 2015-01-21 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'     
2 3 'Structure model' 'Atomic model'            
3 3 'Structure model' 'Derived calculations'    
4 3 'Structure model' 'Non-polymer description' 
5 3 'Structure model' Other                     
6 3 'Structure model' 'Refinement description'  
# 
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 35.8531 28.7213 52.2625 0.5820 0.4015 0.3443 0.1510  0.0504  0.1138  0.2987 0.4519 6.8026  
-0.1078 0.9569  -0.4844 0.0630  -0.1673 -0.1557 0.1810  -0.0345 -0.0636 1.2834  0.3840  -0.0284 
'X-RAY DIFFRACTION' 2  ? refined 43.4169 35.4244 81.1968 0.5180 0.5734 0.3617 0.1889  -0.0288 0.1757  1.9900 4.0864 4.9221  
-1.0449 2.0965  -0.6350 -0.0055 -0.1073 -0.1086 0.4288  -0.2552 -0.4132 0.8252  0.8016  0.2607  
'X-RAY DIFFRACTION' 3  ? refined 40.1976 35.9215 93.0471 0.7443 0.7778 0.3278 0.1336  -0.0248 0.1505  2.1991 2.2115 2.0804  0.6800 
0.9391  0.8762  0.1092  -0.5725 -0.0947 0.6881  -0.2829 0.0050  0.6914  0.3302  0.1736  
'X-RAY DIFFRACTION' 4  ? refined 35.4742 31.5131 48.5969 0.5040 0.2771 0.4108 0.0711  0.0108  0.1042  0.7137 0.4072 11.5261 
-0.3883 0.5347  -1.1444 -0.0490 -0.2910 -0.3214 0.0705  0.1468  -0.0091 0.7094  0.3752  -0.0978 
'X-RAY DIFFRACTION' 5  ? refined 33.4482 40.4412 34.0859 0.2348 0.2190 0.2414 0.0411  0.0336  0.0652  0.8011 0.4863 8.4083  
-0.3825 -1.3189 1.6003  -0.2077 -0.1883 -0.1326 0.1724  0.0003  0.0053  0.6367  0.7502  0.2074  
'X-RAY DIFFRACTION' 6  ? refined 37.4408 41.9681 1.6881  0.2680 0.2513 0.2596 0.0683  0.0722  0.0355  2.4665 3.3652 10.0799 
-0.6864 0.4629  0.7402  0.2146  0.7045  0.0473  -0.9256 -0.2774 -0.4086 -0.4194 0.7932  0.0628  
'X-RAY DIFFRACTION' 7  ? refined 44.5114 67.6505 56.0890 0.4694 0.4011 0.3483 -0.1485 -0.1164 -0.0239 0.3492 0.3105 6.0277  0.0473 
-0.5070 0.3576  0.0076  -0.2481 0.1617  0.1757  0.0164  -0.1156 -0.9983 0.9751  -0.0240 
'X-RAY DIFFRACTION' 8  ? refined 38.2067 68.9088 92.7750 0.8441 0.6560 0.3477 -0.0869 -0.1246 -0.0973 2.6884 1.7020 2.3645  
-0.0677 -0.9141 0.0462  -0.1333 -0.9034 0.1588  0.4162  -0.0704 -0.1324 -0.5940 0.4885  0.2037  
'X-RAY DIFFRACTION' 9  ? refined 31.0345 73.5533 83.7345 1.1500 0.5434 0.3722 0.0477  -0.2042 -0.1863 3.1253 1.3729 3.1616  
-0.8210 -2.9624 0.6424  0.1527  -0.1936 0.2251  0.1851  -0.0885 0.1479  -0.7723 0.0230  -0.0642 
'X-RAY DIFFRACTION' 10 ? refined 43.8993 66.4323 47.4468 0.3095 0.4052 0.3808 -0.1598 -0.0962 -0.0438 0.4701 1.3864 13.3573 0.0954 
1.4220  0.9256  -0.0197 -0.1844 0.2638  0.3346  0.0917  -0.1783 -0.7297 0.4527  -0.0720 
'X-RAY DIFFRACTION' 11 ? refined 36.6458 60.4940 34.0929 0.2150 0.2088 0.2473 -0.0369 -0.0797 0.0069  0.2019 1.0719 9.1391  0.1298 
-0.5726 -2.0152 -0.0629 -0.1018 0.0731  0.2376  -0.1440 -0.0992 -0.9358 0.1925  0.2069  
'X-RAY DIFFRACTION' 12 ? refined 33.3153 63.1866 1.6930  0.3009 0.2056 0.2573 -0.0450 -0.0703 0.0327  2.4556 2.9961 10.3836 0.8175 
-0.9476 -0.1189 -0.2865 0.6392  0.3459  -0.8839 0.1701  0.2164  -0.5218 -0.7095 0.1164  
'X-RAY DIFFRACTION' 13 ? refined 7.5687  56.4734 56.0670 0.2938 0.6238 0.3582 0.0094  0.0900  -0.0980 0.3622 0.2105 5.6670  
-0.0878 -0.1321 -0.5826 -0.0330 -0.1507 -0.0156 0.1840  0.0631  0.1725  -0.4065 -1.3400 -0.0300 
'X-RAY DIFFRACTION' 14 ? refined 9.2994  50.6683 93.3255 0.6554 0.9405 0.3804 -0.0375 0.1650  -0.0522 1.5696 1.8076 2.0829  
-0.4496 0.5384  -0.7444 -0.3191 -0.4654 0.0241  0.7264  0.1227  0.1531  -0.0965 -0.7545 0.1964  
'X-RAY DIFFRACTION' 15 ? refined 10.3433 42.7988 83.8854 0.4589 0.8858 0.3325 -0.2305 0.1803  -0.0648 0.7838 3.4512 4.3170  
-0.3129 -0.0798 -2.3890 -0.1285 -0.2401 -0.2457 0.3146  0.0877  0.2138  0.7040  -1.0684 0.0408  
'X-RAY DIFFRACTION' 16 ? refined 8.9226  56.5503 47.4227 0.2092 0.4601 0.3566 0.0860  0.0647  -0.0600 1.1327 0.6401 13.1781 0.1801 
-1.9442 0.8354  0.0953  -0.2824 0.0407  0.2830  -0.0367 0.3153  0.0345  -0.7150 -0.0586 
'X-RAY DIFFRACTION' 17 ? refined 15.8577 52.5601 31.0476 0.1795 0.3223 0.2724 -0.0021 0.0432  -0.0939 1.3123 0.4597 9.8632  0.6286 
2.5770  0.7948  -0.0188 -0.3641 0.0613  0.0467  -0.1593 0.1199  0.5260  -1.3461 0.1782  
'X-RAY DIFFRACTION' 18 ? refined 18.9354 50.8261 13.4716 0.0529 0.1232 0.2133 -0.0064 0.0206  -0.0087 2.0421 1.1024 11.2148 0.0451 
1.7845  -0.4785 -0.0529 0.4080  -0.1067 -0.1824 -0.0655 0.0932  0.4484  0.0152  0.1184  
# 
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  ? ? 1.85 
2 1 O  B HOH 2036 ? ? O   D HOH 2028 ? ? 1.99 
# 
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  ? ? 61.47   -113.14 
2  1 ASP A 88  ? ? -101.83 -119.39 
3  1 GLN A 192 ? ? 71.91   -51.88  
4  1 GLU A 270 ? ? -99.91  -113.76 
5  1 ALA B 5   ? ? -95.33  -63.10  
6  1 ARG B 127 ? ? 54.03   -129.55 
7  1 ARG C 53  ? ? 61.47   -113.00 
8  1 ASP C 88  ? ? -101.90 -119.42 
9  1 GLN C 192 ? ? 71.78   -51.68  
10 1 GLU C 270 ? ? -99.91  -113.70 
11 1 ALA D 5   ? ? -95.23  -63.14  
12 1 ARG D 127 ? ? 54.09   -129.57 
13 1 ARG E 53  ? ? 61.46   -113.02 
14 1 ASP E 88  ? ? -101.93 -119.38 
15 1 GLN E 192 ? ? 71.92   -51.84  
16 1 GLU E 270 ? ? -99.91  -113.89 
17 1 ALA F 5   ? ? -95.33  -62.83  
18 1 ARG F 127 ? ? 54.11   -129.63 
# 
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 1164 ? 'WRONG HAND' . 
2 1 C1 ? D NAG 1164 ? 'WRONG HAND' . 
3 1 C1 ? F NAG 1164 ? '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 ? A HOH 2062 ? 6.34 . 
2 1 O ? C HOH 2057 ? 6.10 . 
3 1 O ? C HOH 2058 ? 5.92 . 
4 1 O ? E HOH 2050 ? 6.32 . 
# 
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 ALPHA-L-FUCOSE                                        FUC 
7 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
8 water                                                 HOH 
# 
